HEADER DNA BINDING PROTEIN 23-FEB-20 XXXX TITLE CRYSTAL STRUCTURE OF STREPTOCOCCUS THERMOPHILUS CAS9 IN COMPLEX WITH TITLE 2 AGGA PAM KEYWDS CAS9, CRISPR, DNA BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR Y.ZHANG,H.ZHANG,X.XU,Y.WANG,W.CHEN,Y.WANG,Z.WU,N.TANG,Y.WANG,S.ZHAO, AUTHOR 2 J.GAN,Q.JI JRNL AUTH Y.ZHANG,H.ZHANG,X.XU,Y.WANG,W.CHEN,Y.WANG,Z.WU,N.TANG, JRNL AUTH 2 Y.WANG,S.ZHAO,J.GAN,Q.JI JRNL TITL CATALYTIC-STATE STRUCTURE AND ENGINEERING OF STREPTOCOCCUS JRNL TITL 2 THERMOPHILUS CAS9 JRNL REF NAT CATAL 2020 JRNL REFN ESSN 2520-1158 JRNL DOI 10.1038/S41929-020-00506-9 SEQRES 1 A 1122 MET GLY SER ASP LEU VAL LEU GLY LEU ASP ILE GLY ILE SEQRES 2 A 1122 GLY SER VAL GLY VAL GLY ILE LEU ASN LYS VAL THR GLY SEQRES 3 A 1122 GLU ILE ILE HIS LYS ASN SER ARG ILE PHE PRO ALA ALA SEQRES 4 A 1122 GLN ALA GLU ASN ASN LEU VAL ARG ARG THR ASN ARG GLN SEQRES 5 A 1122 GLY ARG ARG LEU ALA ARG ARG LYS LYS HIS ARG ARG VAL SEQRES 6 A 1122 ARG LEU ASN ARG LEU PHE GLU GLU SER GLY LEU ILE THR SEQRES 7 A 1122 ASP PHE THR LYS ILE SER ILE ASN LEU ASN PRO TYR GLN SEQRES 8 A 1122 LEU ARG VAL LYS GLY LEU THR ASP GLU LEU SER ASN GLU SEQRES 9 A 1122 GLU LEU PHE ILE ALA LEU LYS ASN MET VAL LYS HIS ARG SEQRES 10 A 1122 GLY ILE SER TYR LEU ASP ASP ALA SER ASP ASP GLY ASN SEQRES 11 A 1122 SER SER VAL GLY ASP TYR ALA GLN ILE VAL LYS GLU ASN SEQRES 12 A 1122 SER LYS GLN LEU GLU THR LYS THR PRO GLY GLN ILE GLN SEQRES 13 A 1122 LEU GLU ARG TYR GLN THR TYR GLY GLN LEU ARG GLY ASP SEQRES 14 A 1122 PHE THR VAL GLU LYS ASP GLY LYS LYS HIS ARG LEU ILE SEQRES 15 A 1122 ASN VAL PHE PRO THR SER ALA TYR ARG SER GLU ALA LEU SEQRES 16 A 1122 ARG ILE LEU GLN THR GLN GLN GLU PHE ASN PRO GLN ILE SEQRES 17 A 1122 THR ASP GLU PHE ILE ASN ARG TYR LEU GLU ILE LEU THR SEQRES 18 A 1122 GLY LYS ARG LYS TYR TYR HIS GLY PRO GLY ASN GLU LYS SEQRES 19 A 1122 SER ARG THR ASP TYR GLY ARG TYR ARG THR SER GLY GLU SEQRES 20 A 1122 THR LEU ASP ASN ILE PHE GLY ILE LEU ILE GLY LYS CYS SEQRES 21 A 1122 THR PHE TYR PRO ASP GLU PHE ARG ALA ALA LYS ALA SER SEQRES 22 A 1122 TYR THR ALA GLN GLU PHE ASN LEU LEU ASN ASP LEU ASN SEQRES 23 A 1122 ASN LEU THR VAL PRO THR GLU THR LYS LYS LEU SER LYS SEQRES 24 A 1122 GLU GLN LYS ASN GLN ILE ILE ASN TYR VAL LYS ASN GLU SEQRES 25 A 1122 LYS ALA MET GLY PRO ALA LYS LEU PHE LYS TYR ILE ALA SEQRES 26 A 1122 LYS LEU LEU SER CYS ASP VAL ALA ASP ILE LYS GLY TYR SEQRES 27 A 1122 ARG ILE ASP LYS SER GLY LYS ALA GLU ILE HIS THR PHE SEQRES 28 A 1122 GLU ALA TYR ARG LYS MET LYS THR LEU GLU THR LEU ASP SEQRES 29 A 1122 ILE GLU GLN MET ASP ARG GLU THR LEU ASP LYS LEU ALA SEQRES 30 A 1122 TYR VAL LEU THR LEU ASN THR GLU ARG GLU GLY ILE GLN SEQRES 31 A 1122 GLU ALA LEU GLU HIS GLU PHE ALA ASP GLY SER PHE SER SEQRES 32 A 1122 GLN LYS GLN VAL ASP GLU LEU VAL GLN PHE ARG LYS ALA SEQRES 33 A 1122 ASN SER SER ILE PHE GLY LYS GLY TRP HIS ASN PHE SER SEQRES 34 A 1122 VAL LYS LEU MET MET GLU LEU ILE PRO GLU LEU TYR GLU SEQRES 35 A 1122 THR SER GLU GLU GLN MET THR ILE LEU THR ARG LEU GLY SEQRES 36 A 1122 LYS GLN LYS THR THR SER SER SER ASN LYS THR LYS TYR SEQRES 37 A 1122 ILE ASP GLU LYS LEU LEU THR GLU GLU ILE TYR ASN PRO SEQRES 38 A 1122 VAL VAL ALA LYS SER VAL ARG GLN ALA ILE LYS ILE VAL SEQRES 39 A 1122 ASN ALA ALA ILE LYS GLU TYR GLY ASP PHE ASP ASN ILE SEQRES 40 A 1122 VAL ILE GLU MET ALA ARG GLU THR ASN GLU ASP ASP GLU SEQRES 41 A 1122 LYS LYS ALA ILE GLN LYS ILE GLN LYS ALA ASN LYS ASP SEQRES 42 A 1122 GLU LYS ASP ALA ALA MET LEU LYS ALA ALA ASN GLN TYR SEQRES 43 A 1122 ASN GLY LYS ALA GLU LEU PRO HIS SER VAL PHE HIS GLY SEQRES 44 A 1122 HIS LYS GLN LEU ALA THR LYS ILE ARG LEU TRP HIS GLN SEQRES 45 A 1122 GLN GLY GLU ARG CYS LEU TYR THR GLY LYS THR ILE SER SEQRES 46 A 1122 ILE HIS ASP LEU ILE ASN ASN SER ASN GLN PHE GLU VAL SEQRES 47 A 1122 ASP ALA ILE LEU PRO LEU SER ILE THR PHE ASP ASP SER SEQRES 48 A 1122 LEU ALA ASN LYS VAL LEU VAL TYR ALA THR ALA ASN GLN SEQRES 49 A 1122 GLU LYS GLY GLN ARG THR PRO TYR GLN ALA LEU ASP SER SEQRES 50 A 1122 MET ASP ASP ALA TRP SER PHE ARG GLU LEU LYS ALA PHE SEQRES 51 A 1122 VAL ARG GLU SER LYS THR LEU SER ASN LYS LYS LYS GLU SEQRES 52 A 1122 TYR LEU LEU THR GLU GLU ASP ILE SER LYS PHE ASP VAL SEQRES 53 A 1122 ARG LYS LYS PHE ILE GLU ARG ASN LEU VAL ASP THR ARG SEQRES 54 A 1122 TYR ALA SER ARG VAL VAL LEU ASN ALA LEU GLN GLU HIS SEQRES 55 A 1122 PHE ARG ALA HIS LYS ILE ASP THR LYS VAL SER VAL VAL SEQRES 56 A 1122 ARG GLY GLN PHE THR SER GLN LEU ARG ARG HIS TRP GLY SEQRES 57 A 1122 ILE GLU LYS THR ARG ASP THR TYR HIS HIS HIS ALA VAL SEQRES 58 A 1122 ASP ALA LEU ILE ILE ALA ALA SER SER GLN LEU ASN LEU SEQRES 59 A 1122 TRP LYS LYS GLN LYS ASN THR LEU VAL SER TYR SER GLU SEQRES 60 A 1122 ASP GLN LEU LEU ASP ILE GLU THR GLY GLU LEU ILE SER SEQRES 61 A 1122 ASP ASP GLU TYR LYS GLU SER VAL PHE LYS ALA PRO TYR SEQRES 62 A 1122 GLN HIS PHE VAL ASP THR LEU LYS SER LYS GLU PHE GLU SEQRES 63 A 1122 ASP SER ILE LEU PHE SER TYR GLN VAL ASP SER LYS PHE SEQRES 64 A 1122 ASN ARG LYS ILE SER ASP ALA THR ILE TYR ALA THR ARG SEQRES 65 A 1122 GLN ALA LYS VAL GLY LYS ASP LYS ALA ASP GLU THR TYR SEQRES 66 A 1122 VAL LEU GLY LYS ILE LYS ASP ILE TYR THR GLN ASP GLY SEQRES 67 A 1122 TYR ASP ALA PHE MET LYS ILE TYR LYS LYS ASP LYS SER SEQRES 68 A 1122 LYS PHE LEU MET TYR ARG HIS ASP PRO GLN THR PHE GLU SEQRES 69 A 1122 LYS VAL ILE GLU PRO ILE LEU GLU ASN TYR PRO ASN LYS SEQRES 70 A 1122 GLN ILE ASN GLU LYS GLY LYS GLU VAL PRO CYS ASN PRO SEQRES 71 A 1122 PHE LEU LYS TYR LYS GLU GLU HIS GLY TYR ILE ARG LYS SEQRES 72 A 1122 TYR SER LYS LYS GLY ASN GLY PRO GLU ILE LYS SER LEU SEQRES 73 A 1122 LYS TYR TYR ASP SER LYS LEU GLY ASN HIS ILE ASP ILE SEQRES 74 A 1122 THR PRO LYS ASP SER ASN ASN LYS VAL VAL LEU GLN SER SEQRES 75 A 1122 VAL SER PRO TRP ARG ALA ASP VAL TYR PHE ASN LYS THR SEQRES 76 A 1122 THR GLY LYS TYR GLU ILE LEU GLY LEU LYS TYR ALA ASP SEQRES 77 A 1122 LEU GLN PHE GLU LYS GLY THR GLY THR TYR LYS ILE SER SEQRES 78 A 1122 GLN GLU LYS TYR ASN ASP ILE LYS LYS LYS GLU GLY VAL SEQRES 79 A 1122 ASP SER ASP SER GLU PHE LYS PHE THR LEU TYR LYS ASN SEQRES 80 A 1122 ASP LEU LEU LEU VAL LYS ASP THR GLU THR LYS GLU GLN SEQRES 81 A 1122 GLN LEU PHE ARG PHE LEU SER ARG THR MET PRO LYS GLN SEQRES 82 A 1122 LYS HIS TYR VAL GLU LEU LYS PRO TYR ASP LYS GLN LYS SEQRES 83 A 1122 PHE GLU GLY GLY GLU ALA LEU ILE LYS VAL LEU GLY ASN SEQRES 84 A 1122 VAL ALA ASN SER GLY GLN CYS LYS LYS GLY LEU GLY LYS SEQRES 85 A 1122 SER ASN ILE SER ILE TYR LYS VAL ARG THR ASP VAL LEU SEQRES 86 A 1122 GLY ASN GLN HIS ILE ILE LYS ASN GLU GLY ASP LYS PRO SEQRES 87 A 1122 LYS LEU ASP PHE SEQRES 1 B 71 G G U G C U A A G A U U A SEQRES 2 B 71 A U C A G G A U G U U U U SEQRES 3 B 71 U G U A C U C G A A A G A SEQRES 4 B 71 A G C U A C A A A G A U A SEQRES 5 B 71 A G G C U U C A U G C C G SEQRES 6 B 71 A A A U C A SEQRES 1 C 28 DG DC DT DC DC DT DT DT DA DT DC DC DT SEQRES 2 C 28 DG DA DT DT DA DA DT DC DT DT DA DG DC SEQRES 3 C 28 DA DC SEQRES 1 D 8 DA DA DA DG DG DA DG DC HETNAM BA BARIUM ION HETNAM MG MAGNESIUM ION FORMUL 5 BA 14(BA 2+) FORMUL 11 MG 2(MG 2+) FORMUL 21 HOH *51(H2 O) HELIX 1 AA1 ALA A 37 ASN A 42 1 6 HELIX 2 AA2 ASN A 42 SER A 73 1 32 HELIX 3 AA3 ASN A 87 GLY A 95 1 9 HELIX 4 AA4 SER A 101 LYS A 114 1 14 HELIX 5 AA5 THR A 150 GLY A 163 1 14 HELIX 6 AA6 PRO A 185 ASN A 204 1 20 HELIX 7 AA7 THR A 208 GLY A 221 1 14 HELIX 8 AA8 PHE A 252 ILE A 256 5 5 HELIX 9 AA9 SER A 272 ASN A 286 1 15 HELIX 10 AB1 SER A 297 GLU A 311 1 15 HELIX 11 AB2 GLY A 315 LEU A 326 1 12 HELIX 12 AB3 ASP A 330 ILE A 334 5 5 HELIX 13 AB4 PHE A 350 THR A 358 1 9 HELIX 14 AB5 ASP A 363 MET A 367 5 5 HELIX 15 AB6 ASP A 368 ASN A 382 1 15 HELIX 16 AB7 GLU A 384 PHE A 396 1 13 HELIX 17 AB8 SER A 402 ASN A 416 1 15 HELIX 18 AB9 ASN A 416 GLY A 421 1 6 HELIX 19 AC1 SER A 428 GLU A 434 1 7 HELIX 20 AC2 LEU A 435 THR A 442 1 8 HELIX 21 AC3 GLU A 445 GLY A 454 1 10 HELIX 22 AC4 ASP A 469 THR A 474 1 6 HELIX 23 AC5 ASN A 479 GLY A 501 1 23 HELIX 24 AC6 GLU A 516 ASN A 546 1 31 HELIX 25 AC7 PRO A 552 HIS A 557 5 6 HELIX 26 AC8 GLN A 561 GLN A 572 1 12 HELIX 27 AC9 SER A 584 ASN A 591 1 8 HELIX 28 AD1 SER A 610 ALA A 612 5 3 HELIX 29 AD2 ALA A 619 GLY A 626 1 8 HELIX 30 AD3 THR A 629 LEU A 634 1 6 HELIX 31 AD4 SER A 642 SER A 653 1 12 HELIX 32 AD5 SER A 657 THR A 666 1 10 HELIX 33 AD6 GLU A 681 HIS A 705 1 25 HELIX 34 AD7 GLY A 716 TRP A 726 1 11 HELIX 35 AD8 TYR A 735 GLN A 750 1 16 HELIX 36 AD9 TYR A 792 SER A 801 1 10 HELIX 37 AE1 PHE A 804 ILE A 808 5 5 HELIX 38 AE2 THR A 854 LYS A 869 1 16 HELIX 39 AE3 PHE A 872 ASP A 878 1 7 HELIX 40 AE4 ASP A 878 VAL A 885 1 8 HELIX 41 AE5 VAL A 885 TYR A 893 1 9 HELIX 42 AE6 ASN A 908 GLY A 918 1 11 HELIX 43 AE7 ALA A 986 LEU A 988 5 3 HELIX 44 AE8 SER A 1000 GLU A 1011 1 12 SHEET 1 AA1 6 LYS A 710 ARG A 715 0 SHEET 2 AA1 6 ASN A 505 MET A 510 1 N MET A 510 O VAL A 714 SHEET 3 AA1 6 VAL A 5 ILE A 10 1 N LEU A 6 O VAL A 507 SHEET 4 AA1 6 SER A 14 LEU A 20 -1 O GLY A 18 N GLY A 7 SHEET 5 AA1 6 ILE A 27 ILE A 34 -1 O HIS A 29 N ILE A 19 SHEET 6 AA1 6 LEU A 809 TYR A 812 1 O SER A 811 N ILE A 34 SHEET 1 AA2 2 ASP A 168 LYS A 173 0 SHEET 2 AA2 2 LYS A 176 ILE A 181 -1 O LYS A 176 N LYS A 173 SHEET 1 AA3 2 PHE A 595 ALA A 599 0 SHEET 2 AA3 2 LYS A 614 TYR A 618 -1 O VAL A 617 N GLU A 596 SHEET 1 AA4 5 LEU A 935 LYS A 941 0 SHEET 2 AA4 5 GLU A 842 ILE A 849 -1 N VAL A 845 O SER A 940 SHEET 3 AA4 5 TYR A 828 ALA A 833 -1 N ARG A 831 O TYR A 844 SHEET 4 AA4 5 VAL A 957 LEU A 959 -1 O VAL A 958 N TYR A 828 SHEET 5 AA4 5 ILE A 946 ASP A 947 -1 N ILE A 946 O LEU A 959 SHEET 1 AA5 2 LYS A 896 ILE A 898 0 SHEET 2 AA5 2 GLU A 904 PRO A 906 -1 O VAL A 905 N GLN A 897 SHEET 1 AA6 3 LYS A 977 LYS A 984 0 SHEET 2 AA6 3 PRO A 964 ASN A 972 -1 N ARG A 966 O LEU A 983 SHEET 3 AA6 3 GLU A1018 TYR A1024 -1 O PHE A1021 N VAL A 969 SHEET 1 AA7 2 GLN A 989 PHE A 990 0 SHEET 2 AA7 2 TYR A 997 LYS A 998 -1 O LYS A 998 N GLN A 989 SHEET 1 AA8 6 CYS A1085 GLY A1088 0 SHEET 2 AA8 6 TYR A1055 LYS A1059 -1 N VAL A1056 O LYS A1087 SHEET 3 AA8 6 GLN A1039 ARG A1047 -1 N ARG A1043 O LYS A1059 SHEET 4 AA8 6 LEU A1028 ASP A1033 -1 N LEU A1029 O PHE A1042 SHEET 5 AA8 6 ILE A1094 THR A1101 -1 O SER A1095 N LYS A1032 SHEET 6 AA8 6 GLN A1107 ILE A1110 -1 O ILE A1110 N LYS A1098 LINK O ASP A 168 BA BA A1205 1555 1555 3.01 LINK O LYS A 357 BA BA A1206 1555 1555 2.88 LINK O LEU A 359 BA BA A1206 1555 1555 2.96 LINK OD1 ASP A 363 BA BA A1206 1555 1555 3.42 LINK OD2 ASP A 398 MG MG A1208 1555 1554 2.17 LINK O GLY A 421 BA BA A1201 1555 1555 2.91 LINK O THR A 514 BA BA A1203 1555 1555 3.12 LINK OD1 ASP A 598 MG MG A1207 1555 1555 2.07 LINK OD1 ASN A 622 MG MG A1207 1555 1555 2.52 LINK OD1 ASP A 824 BA BA A1204 1555 1555 2.87 LINK O LYS A 848 BA BA A1202 1555 1555 2.99 LINK OG SER A 961 BA BA A1204 1555 1555 3.11 LINK O SER A1082 MG MG A1208 1555 1555 2.24 LINK BA BA A1201 OP2 DT C 17 1555 1555 2.68 LINK BA BA A1201 O HOH C 204 1555 1555 3.01 LINK BA BA A1204 O HOH A1316 1555 1555 2.68 LINK BA BA A1204 O HOH D 201 1555 1555 3.01 LINK BA BA A1205 O HOH A1301 1555 1555 3.09 LINK MG MG A1207 O HOH A1309 1555 1555 2.15 LINK MG MG A1207 O HOH A1312 1555 1555 2.07 LINK MG MG A1207 O3' DC C 11 1555 1555 2.53 LINK MG MG A1207 OP1 DC C 12 1555 1555 2.22 LINK MG MG A1208 O HOH A1322 1555 1556 2.86 LINK O HOH A1320 BA BA B 104 1555 1555 2.77 LINK O4 U B 2 BA BA B 103 1555 1555 2.68 LINK O6 G B 33 BA BA B 105 1555 1555 2.69 LINK O6 G B 40 BA BA B 102 1555 1555 2.84 LINK OP1 U B 50 BA BA B 101 1555 1555 2.72 LINK O6 G B 53 BA BA B 101 1555 1555 3.12 LINK BA BA B 102 O HOH B 208 1555 1555 2.65 LINK BA BA B 102 O HOH B 221 1555 1555 2.73 LINK BA BA B 105 O HOH B 218 1555 1555 3.24 LINK BA BA B 106 O HOH B 222 1555 1555 2.80 LINK O6 DG C 1 BA BA C 101 1555 1555 3.01 LINK O HOH C 201 BA BA D 101 1555 1555 2.58 LINK BA BA D 101 O HOH D 203 1555 1555 2.61 SITE 1 AC1 3 GLY A 421 DT C 17 HOH C 204 SITE 1 AC2 1 LYS A 848 SITE 1 AC3 1 THR A 514 SITE 1 AC4 4 ASP A 824 SER A 961 HOH A1316 HOH D 201 SITE 1 AC5 2 ASP A 168 HOH A1301 SITE 1 AC6 3 LYS A 357 LEU A 359 ASP A 363 SITE 1 AC7 6 ASP A 598 ASN A 622 HOH A1309 HOH A1312 SITE 2 AC7 6 DC C 11 DC C 12 SITE 1 AC8 4 ASP A 398 SER A1082 GLY A1083 HOH A1322 SITE 1 AC9 3 U B 50 G B 53 HOH B 213 SITE 1 AD1 3 G B 40 HOH B 208 HOH B 221 SITE 1 AD2 1 U B 2 SITE 1 AD3 1 HOH A1320 SITE 1 AD4 1 G B 33 SITE 1 AD5 1 HOH B 222 SITE 1 AD6 1 DG C 1 SITE 1 AD7 2 HOH C 201 HOH D 203 CRYST1 322.165 75.250 70.008 90.00 93.28 90.00 C 1 2 1 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.003104 0.000000 0.000178 0.00000 SCALE2 0.000000 0.013289 0.000000 0.00000 SCALE3 0.000000 0.000000 0.014308 0.00000 MODEL 1 ATOM 1 N LEU A 4 7.976 -22.269 151.662 1.00 93.16 N ANISOU 1 N LEU A 4 10093 14428 10874 -6981 -596 1196 N ATOM 2 CA LEU A 4 8.933 -21.433 152.382 1.00 90.31 C ANISOU 2 CA LEU A 4 9732 14010 10574 -6740 -512 1212 C ATOM 3 C LEU A 4 9.067 -20.058 151.739 1.00 87.87 C ANISOU 3 C LEU A 4 9218 13893 10274 -6482 -475 1112 C ATOM 4 O LEU A 4 9.060 -19.934 150.518 1.00 87.47 O ANISOU 4 O LEU A 4 9170 13812 10251 -6457 -537 1002 O ATOM 5 CB LEU A 4 10.297 -22.120 152.452 1.00 89.06 C ANISOU 5 CB LEU A 4 9921 13367 10549 -6715 -546 1205 C ATOM 6 CG LEU A 4 10.492 -23.047 153.653 1.00 90.50 C ANISOU 6 CG LEU A 4 10275 13381 10728 -6853 -536 1339 C ATOM 7 CD1 LEU A 4 11.741 -23.898 153.497 1.00 89.79 C ANISOU 7 CD1 LEU A 4 10549 12796 10772 -6842 -594 1318 C ATOM 8 CD2 LEU A 4 10.556 -22.233 154.930 1.00 89.42 C ANISOU 8 CD2 LEU A 4 9979 13453 10544 -6721 -425 1431 C ATOM 9 N VAL A 5 9.192 -19.024 152.565 1.00 87.71 N ANISOU 9 N VAL A 5 9026 14072 10229 -6288 -377 1150 N ATOM 10 CA VAL A 5 9.208 -17.642 152.103 1.00 86.54 C ANISOU 10 CA VAL A 5 8657 14150 10075 -6033 -334 1068 C ATOM 11 C VAL A 5 10.491 -16.967 152.567 1.00 83.33 C ANISOU 11 C VAL A 5 8340 13560 9761 -5808 -273 1060 C ATOM 12 O VAL A 5 10.898 -17.113 153.725 1.00 83.53 O ANISOU 12 O VAL A 5 8436 13512 9791 -5803 -214 1152 O ATOM 13 CB VAL A 5 7.967 -16.879 152.607 1.00 86.97 C ANISOU 13 CB VAL A 5 8370 14684 9991 -5983 -269 1108 C ATOM 14 CG1 VAL A 5 8.252 -15.384 152.713 1.00 84.58 C ANISOU 14 CG1 VAL A 5 7872 14574 9691 -5667 -192 1061 C ATOM 15 CG2 VAL A 5 6.792 -17.131 151.671 1.00 89.56 C ANISOU 15 CG2 VAL A 5 8561 15229 10238 -6121 -339 1067 C ATOM 16 N LEU A 6 11.116 -16.212 151.665 1.00 79.06 N ANISOU 16 N LEU A 6 7795 12959 9287 -5625 -288 952 N ATOM 17 CA LEU A 6 12.387 -15.551 151.922 1.00 76.19 C ANISOU 17 CA LEU A 6 7524 12410 9015 -5416 -239 931 C ATOM 18 C LEU A 6 12.200 -14.042 151.884 1.00 74.66 C ANISOU 18 C LEU A 6 7055 12530 8782 -5157 -171 888 C ATOM 19 O LEU A 6 11.701 -13.495 150.896 1.00 74.66 O ANISOU 19 O LEU A 6 6906 12708 8754 -5089 -208 804 O ATOM 20 CB LEU A 6 13.434 -15.980 150.889 1.00 74.90 C ANISOU 20 CB LEU A 6 7622 11867 8968 -5416 -318 835 C ATOM 21 CG LEU A 6 14.889 -15.562 151.076 1.00 72.17 C ANISOU 21 CG LEU A 6 7452 11241 8729 -5207 -284 806 C ATOM 22 CD1 LEU A 6 15.543 -16.300 152.236 1.00 72.33 C ANISOU 22 CD1 LEU A 6 7669 11024 8791 -5299 -256 916 C ATOM 23 CD2 LEU A 6 15.668 -15.787 149.784 1.00 71.13 C ANISOU 23 CD2 LEU A 6 7533 10810 8684 -5117 -362 672 C ATOM 24 N GLY A 7 12.620 -13.370 152.948 1.00 79.44 N ANISOU 24 N GLY A 7 7603 13198 9384 -5004 -75 943 N ATOM 25 CA GLY A 7 12.582 -11.923 153.017 1.00 77.72 C ANISOU 25 CA GLY A 7 7175 13220 9136 -4697 -6 896 C ATOM 26 C GLY A 7 13.985 -11.363 152.896 1.00 75.76 C ANISOU 26 C GLY A 7 7146 12645 8994 -4384 11 827 C ATOM 27 O GLY A 7 14.956 -12.009 153.292 1.00 76.68 O ANISOU 27 O GLY A 7 7516 12431 9187 -4420 7 858 O ATOM 28 N LEU A 8 14.090 -10.150 152.351 1.00 68.87 N ANISOU 28 N LEU A 8 6175 11869 8121 -4077 28 737 N ATOM 29 CA LEU A 8 15.383 -9.510 152.133 1.00 65.43 C ANISOU 29 CA LEU A 8 5928 11153 7778 -3780 42 666 C ATOM 30 C LEU A 8 15.281 -8.020 152.410 1.00 63.77 C ANISOU 30 C LEU A 8 5545 11156 7527 -3455 111 632 C ATOM 31 O LEU A 8 14.424 -7.338 151.841 1.00 64.39 O ANISOU 31 O LEU A 8 5412 11509 7543 -3377 97 590 O ATOM 32 CB LEU A 8 15.881 -9.731 150.704 1.00 64.17 C ANISOU 32 CB LEU A 8 5925 10769 7688 -3756 -46 561 C ATOM 33 CG LEU A 8 16.303 -11.140 150.295 1.00 64.91 C ANISOU 33 CG LEU A 8 6259 10558 7846 -4012 -121 563 C ATOM 34 CD1 LEU A 8 16.534 -11.202 148.778 1.00 64.49 C ANISOU 34 CD1 LEU A 8 6296 10378 7830 -3978 -205 444 C ATOM 35 CD2 LEU A 8 17.556 -11.574 151.063 1.00 63.69 C ANISOU 35 CD2 LEU A 8 6359 10064 7777 -3962 -91 601 C ATOM 36 N ASP A 9 16.167 -7.516 153.267 1.00 64.66 N ANISOU 36 N ASP A 9 5757 11136 7676 -3262 178 647 N ATOM 37 CA ASP A 9 16.282 -6.089 153.563 1.00 64.48 C ANISOU 37 CA ASP A 9 5626 11246 7628 -2936 240 606 C ATOM 38 C ASP A 9 17.653 -5.646 153.065 1.00 62.09 C ANISOU 38 C ASP A 9 5552 10613 7427 -2713 226 534 C ATOM 39 O ASP A 9 18.636 -5.688 153.804 1.00 61.07 O ANISOU 39 O ASP A 9 5581 10276 7348 -2644 264 559 O ATOM 40 CB ASP A 9 16.092 -5.813 155.052 1.00 67.94 C ANISOU 40 CB ASP A 9 5967 11844 8004 -2908 335 684 C ATOM 41 CG ASP A 9 16.029 -4.332 155.371 1.00 69.83 C ANISOU 41 CG ASP A 9 6075 12255 8202 -2581 396 635 C ATOM 42 OD1 ASP A 9 15.946 -3.513 154.438 1.00 70.36 O ANISOU 42 OD1 ASP A 9 6095 12358 8279 -2394 363 552 O ATOM 43 OD2 ASP A 9 16.035 -3.984 156.566 1.00 73.94 O ANISOU 43 OD2 ASP A 9 6542 12877 8675 -2514 476 679 O ATOM 44 N ILE A 10 17.711 -5.219 151.809 1.00 58.02 N ANISOU 44 N ILE A 10 5046 10065 6936 -2607 169 447 N ATOM 45 CA ILE A 10 18.966 -4.899 151.142 1.00 55.81 C ANISOU 45 CA ILE A 10 4978 9482 6745 -2431 146 375 C ATOM 46 C ILE A 10 19.340 -3.458 151.454 1.00 54.36 C ANISOU 46 C ILE A 10 4752 9349 6552 -2112 200 342 C ATOM 47 O ILE A 10 18.518 -2.550 151.295 1.00 54.88 O ANISOU 47 O ILE A 10 4625 9675 6552 -1984 209 322 O ATOM 48 CB ILE A 10 18.845 -5.124 149.627 1.00 55.97 C ANISOU 48 CB ILE A 10 5033 9451 6782 -2477 59 299 C ATOM 49 CG1 ILE A 10 18.238 -6.496 149.352 1.00 57.82 C ANISOU 49 CG1 ILE A 10 5278 9686 7007 -2808 2 329 C ATOM 50 CG2 ILE A 10 20.188 -5.016 148.947 1.00 54.08 C ANISOU 50 CG2 ILE A 10 5025 8890 6631 -2340 37 231 C ATOM 51 CD1 ILE A 10 17.932 -6.740 147.897 1.00 58.34 C ANISOU 51 CD1 ILE A 10 5350 9749 7069 -2878 -86 253 C ATOM 52 N GLY A 11 20.584 -3.249 151.896 1.00 52.96 N ANISOU 52 N GLY A 11 4757 8923 6441 -1983 232 336 N ATOM 53 CA GLY A 11 21.075 -1.930 152.240 1.00 51.27 C ANISOU 53 CA GLY A 11 4538 8716 6226 -1698 280 305 C ATOM 54 C GLY A 11 22.488 -1.719 151.719 1.00 49.33 C ANISOU 54 C GLY A 11 4514 8159 6068 -1567 262 252 C ATOM 55 O GLY A 11 23.065 -2.589 151.067 1.00 50.73 O ANISOU 55 O GLY A 11 4841 8128 6306 -1683 216 234 O ATOM 56 N ILE A 12 23.031 -0.537 152.027 1.00 48.07 N ANISOU 56 N ILE A 12 4374 7980 5912 -1324 301 225 N ATOM 57 CA ILE A 12 24.338 -0.178 151.487 1.00 46.32 C ANISOU 57 CA ILE A 12 4339 7497 5762 -1190 286 174 C ATOM 58 C ILE A 12 25.478 -0.900 152.191 1.00 45.51 C ANISOU 58 C ILE A 12 4414 7152 5725 -1250 308 206 C ATOM 59 O ILE A 12 26.556 -1.058 151.609 1.00 44.39 O ANISOU 59 O ILE A 12 4435 6781 5650 -1211 284 167 O ATOM 60 CB ILE A 12 24.569 1.339 151.551 1.00 45.37 C ANISOU 60 CB ILE A 12 4194 7422 5621 -922 312 137 C ATOM 61 CG1 ILE A 12 24.673 1.809 152.996 1.00 45.24 C ANISOU 61 CG1 ILE A 12 4149 7464 5578 -840 384 175 C ATOM 62 CG2 ILE A 12 23.462 2.077 150.817 1.00 46.27 C ANISOU 62 CG2 ILE A 12 4141 7767 5671 -841 282 107 C ATOM 63 CD1 ILE A 12 25.160 3.219 153.110 1.00 44.21 C ANISOU 63 CD1 ILE A 12 4048 7307 5441 -586 405 133 C ATOM 64 N GLY A 13 25.275 -1.349 153.423 1.00 46.15 N ANISOU 64 N GLY A 13 4463 7287 5783 -1340 351 277 N ATOM 65 CA GLY A 13 26.294 -2.115 154.102 1.00 45.60 C ANISOU 65 CA GLY A 13 4560 6996 5772 -1406 362 317 C ATOM 66 C GLY A 13 25.758 -3.335 154.813 1.00 47.07 C ANISOU 66 C GLY A 13 4730 7215 5940 -1646 364 402 C ATOM 67 O GLY A 13 26.434 -3.916 155.666 1.00 46.92 O ANISOU 67 O GLY A 13 4822 7055 5949 -1698 380 457 O ATOM 68 N SER A 14 24.542 -3.736 154.468 1.00 51.05 N ANISOU 68 N SER A 14 5096 7909 6393 -1800 342 417 N ATOM 69 CA SER A 14 23.915 -4.866 155.131 1.00 53.73 C ANISOU 69 CA SER A 14 5407 8305 6703 -2052 342 505 C ATOM 70 C SER A 14 22.803 -5.406 154.248 1.00 57.94 C ANISOU 70 C SER A 14 5832 8979 7203 -2233 289 494 C ATOM 71 O SER A 14 22.187 -4.667 153.480 1.00 61.07 O ANISOU 71 O SER A 14 6097 9543 7565 -2141 275 436 O ATOM 72 CB SER A 14 23.358 -4.463 156.497 1.00 54.76 C ANISOU 72 CB SER A 14 5399 8657 6751 -2040 416 576 C ATOM 73 OG SER A 14 22.577 -3.286 156.389 1.00 55.00 O ANISOU 73 OG SER A 14 5236 8951 6713 -1881 447 534 O ATOM 74 N VAL A 15 22.568 -6.708 154.365 1.00 53.14 N ANISOU 74 N VAL A 15 5289 8296 6606 -2494 255 552 N ATOM 75 CA VAL A 15 21.382 -7.359 153.825 1.00 55.04 C ANISOU 75 CA VAL A 15 5412 8702 6798 -2723 211 565 C ATOM 76 C VAL A 15 20.826 -8.248 154.924 1.00 56.75 C ANISOU 76 C VAL A 15 5595 9000 6968 -2966 233 683 C ATOM 77 O VAL A 15 21.530 -9.125 155.431 1.00 56.79 O ANISOU 77 O VAL A 15 5785 8768 7023 -3068 222 738 O ATOM 78 CB VAL A 15 21.691 -8.185 152.564 1.00 55.16 C ANISOU 78 CB VAL A 15 5579 8502 6879 -2834 124 503 C ATOM 79 CG1 VAL A 15 20.644 -9.265 152.362 1.00 57.44 C ANISOU 79 CG1 VAL A 15 5809 8889 7126 -3149 74 547 C ATOM 80 CG2 VAL A 15 21.785 -7.285 151.345 1.00 54.09 C ANISOU 80 CG2 VAL A 15 5405 8397 6751 -2643 98 394 C ATOM 81 N GLY A 16 19.564 -8.012 155.301 1.00 67.04 N ANISOU 81 N GLY A 16 6658 10644 8169 -3053 264 726 N ATOM 82 CA GLY A 16 18.897 -8.839 156.284 1.00 67.30 C ANISOU 82 CA GLY A 16 6632 10799 8140 -3309 287 843 C ATOM 83 C GLY A 16 18.199 -10.000 155.609 1.00 68.42 C ANISOU 83 C GLY A 16 6785 10935 8278 -3621 210 864 C ATOM 84 O GLY A 16 17.528 -9.824 154.590 1.00 66.95 O ANISOU 84 O GLY A 16 6486 10882 8071 -3643 166 799 O ATOM 85 N VAL A 17 18.358 -11.186 156.183 1.00 63.22 N ANISOU 85 N VAL A 17 6269 10116 7634 -3864 190 957 N ATOM 86 CA VAL A 17 17.811 -12.413 155.623 1.00 65.15 C ANISOU 86 CA VAL A 17 6572 10299 7882 -4185 110 983 C ATOM 87 C VAL A 17 16.906 -13.067 156.654 1.00 67.46 C ANISOU 87 C VAL A 17 6756 10793 8083 -4469 139 1122 C ATOM 88 O VAL A 17 17.127 -12.949 157.863 1.00 67.38 O ANISOU 88 O VAL A 17 6742 10820 8040 -4439 207 1209 O ATOM 89 CB VAL A 17 18.932 -13.382 155.198 1.00 64.59 C ANISOU 89 CB VAL A 17 6827 9787 7928 -4233 40 961 C ATOM 90 CG1 VAL A 17 18.399 -14.429 154.239 1.00 66.33 C ANISOU 90 CG1 VAL A 17 7113 9931 8159 -4507 -57 938 C ATOM 91 CG2 VAL A 17 20.091 -12.620 154.595 1.00 62.04 C ANISOU 91 CG2 VAL A 17 6619 9265 7690 -3912 42 849 C ATOM 92 N GLY A 18 15.891 -13.779 156.171 1.00 69.63 N ANISOU 92 N GLY A 18 6944 11203 8310 -4757 85 1144 N ATOM 93 CA GLY A 18 14.989 -14.492 157.057 1.00 72.11 C ANISOU 93 CA GLY A 18 7169 11698 8531 -5040 102 1273 C ATOM 94 C GLY A 18 13.970 -15.355 156.340 1.00 74.52 C ANISOU 94 C GLY A 18 7461 12058 8796 -5261 19 1258 C ATOM 95 O GLY A 18 13.369 -14.918 155.356 1.00 74.65 O ANISOU 95 O GLY A 18 7325 12248 8790 -5229 -11 1172 O ATOM 96 N ILE A 19 13.757 -16.578 156.821 1.00 76.57 N ANISOU 96 N ILE A 19 7878 12174 9041 -5485 -20 1345 N ATOM 97 CA ILE A 19 12.898 -17.536 156.139 1.00 79.00 C ANISOU 97 CA ILE A 19 8217 12483 9317 -5716 -106 1334 C ATOM 98 C ILE A 19 11.808 -18.019 157.083 1.00 81.75 C ANISOU 98 C ILE A 19 8451 13069 9540 -5892 -81 1446 C ATOM 99 O ILE A 19 11.982 -18.056 158.306 1.00 81.94 O ANISOU 99 O ILE A 19 8490 13114 9529 -5886 -20 1545 O ATOM 100 CB ILE A 19 13.701 -18.727 155.582 1.00 79.21 C ANISOU 100 CB ILE A 19 8584 12058 9454 -5841 -203 1314 C ATOM 101 CG1 ILE A 19 15.043 -18.242 155.047 1.00 76.32 C ANISOU 101 CG1 ILE A 19 8364 11422 9211 -5643 -208 1229 C ATOM 102 CG2 ILE A 19 12.924 -19.420 154.476 1.00 81.13 C ANISOU 102 CG2 ILE A 19 8840 12308 9679 -6021 -296 1252 C ATOM 103 CD1 ILE A 19 15.849 -19.313 154.386 1.00 76.48 C ANISOU 103 CD1 ILE A 19 8711 11008 9339 -5723 -303 1184 C ATOM 104 N LEU A 20 10.642 -18.315 156.527 1.00 84.01 N ANISOU 104 N LEU A 20 8631 13533 9755 -6059 -132 1429 N ATOM 105 CA LEU A 20 9.532 -18.744 157.360 1.00 86.72 C ANISOU 105 CA LEU A 20 8793 14197 9957 -6208 -103 1515 C ATOM 106 C LEU A 20 8.566 -19.660 156.635 1.00 89.44 C ANISOU 106 C LEU A 20 9206 14506 10273 -6481 -199 1516 C ATOM 107 O LEU A 20 8.111 -19.369 155.529 1.00 89.35 O ANISOU 107 O LEU A 20 9164 14502 10284 -6483 -259 1417 O ATOM 108 CB LEU A 20 8.781 -17.528 157.911 1.00 86.38 C ANISOU 108 CB LEU A 20 8403 14598 9819 -6027 -30 1474 C ATOM 109 CG LEU A 20 7.363 -17.310 157.381 1.00 88.51 C ANISOU 109 CG LEU A 20 8404 15295 9930 -6058 35 1538 C ATOM 110 CD1 LEU A 20 6.334 -17.610 158.460 1.00 87.37 C ANISOU 110 CD1 LEU A 20 7967 15490 9739 -5791 92 1453 C ATOM 111 CD2 LEU A 20 7.197 -15.893 156.856 1.00 91.93 C ANISOU 111 CD2 LEU A 20 8800 15859 10271 -6349 -26 1584 C ATOM 112 N ASN A 21 8.260 -20.774 157.283 1.00104.37 N ANISOU 112 N ASN A 21 11188 16360 12107 -6712 -217 1627 N ATOM 113 CA ASN A 21 7.330 -21.758 156.742 1.00109.87 C ANISOU 113 CA ASN A 21 11908 17090 12748 -6985 -299 1638 C ATOM 114 C ASN A 21 5.945 -21.135 156.761 1.00111.52 C ANISOU 114 C ASN A 21 11774 17790 12810 -7003 -260 1639 C ATOM 115 O ASN A 21 5.332 -20.980 157.821 1.00113.11 O ANISOU 115 O ASN A 21 11823 18253 12901 -7037 -195 1729 O ATOM 116 CB ASN A 21 7.355 -23.072 157.515 1.00115.75 C ANISOU 116 CB ASN A 21 12872 17628 13479 -7232 -336 1758 C ATOM 117 CG ASN A 21 6.316 -24.063 157.003 1.00122.08 C ANISOU 117 CG ASN A 21 13683 18492 14210 -7526 -418 1775 C ATOM 118 OD1 ASN A 21 5.823 -24.897 157.757 1.00126.52 O ANISOU 118 OD1 ASN A 21 14295 19077 14698 -7746 -430 1887 O ATOM 119 ND2 ASN A 21 5.971 -23.964 155.719 1.00122.20 N ANISOU 119 ND2 ASN A 21 13647 18543 14241 -7535 -477 1664 N ATOM 120 N LYS A 22 5.439 -20.777 155.599 1.00114.56 N ANISOU 120 N LYS A 22 12040 18296 13192 -6970 -304 1536 N ATOM 121 CA LYS A 22 4.208 -20.030 155.546 1.00115.35 C ANISOU 121 CA LYS A 22 11809 18856 13163 -6946 -277 1515 C ATOM 122 C LYS A 22 3.032 -20.686 156.251 1.00119.78 C ANISOU 122 C LYS A 22 12257 19675 13578 -7178 -263 1627 C ATOM 123 O LYS A 22 2.197 -20.006 156.835 1.00113.46 O ANISOU 123 O LYS A 22 11190 19256 12664 -7090 -187 1657 O ATOM 124 CB LYS A 22 3.894 -19.610 154.103 1.00113.62 C ANISOU 124 CB LYS A 22 11575 18628 12967 -6982 -365 1406 C ATOM 125 CG LYS A 22 3.155 -20.629 153.264 1.00110.62 C ANISOU 125 CG LYS A 22 10994 18433 12602 -6694 -335 1301 C ATOM 126 CD LYS A 22 3.554 -20.547 151.805 1.00111.79 C ANISOU 126 CD LYS A 22 10835 19026 12613 -6615 -251 1351 C ATOM 127 CE LYS A 22 3.366 -21.894 151.137 1.00106.90 C ANISOU 127 CE LYS A 22 9972 18670 11975 -6315 -203 1274 C ATOM 128 NZ LYS A 22 3.456 -21.847 149.654 1.00108.74 N ANISOU 128 NZ LYS A 22 10010 19227 12079 -6335 -131 1354 N ATOM 129 N VAL A 23 2.945 -21.998 156.210 1.00103.69 N ANISOU 129 N VAL A 23 10421 17438 11540 -7469 -336 1688 N ATOM 130 CA VAL A 23 1.798 -22.613 156.861 1.00107.26 C ANISOU 130 CA VAL A 23 10764 18144 11846 -7720 -335 1791 C ATOM 131 C VAL A 23 1.942 -22.534 158.379 1.00108.10 C ANISOU 131 C VAL A 23 10853 18324 11898 -7700 -250 1906 C ATOM 132 O VAL A 23 1.067 -22.009 159.078 1.00109.40 O ANISOU 132 O VAL A 23 10758 18882 11927 -7680 -181 1950 O ATOM 133 CB VAL A 23 1.620 -24.053 156.345 1.00109.77 C ANISOU 133 CB VAL A 23 11314 18214 12181 -8039 -445 1818 C ATOM 134 CG1 VAL A 23 1.625 -24.032 154.842 1.00109.19 C ANISOU 134 CG1 VAL A 23 11269 18050 12170 -8021 -524 1691 C ATOM 135 CG2 VAL A 23 2.729 -24.966 156.814 1.00109.20 C ANISOU 135 CG2 VAL A 23 11593 17681 12218 -8108 -476 1874 C ATOM 136 N THR A 24 3.084 -22.980 158.897 1.00105.99 N ANISOU 136 N THR A 24 10854 17683 11734 -7680 -251 1949 N ATOM 137 CA THR A 24 3.289 -23.043 160.334 1.00106.33 C ANISOU 137 CA THR A 24 10917 17756 11728 -7685 -182 2065 C ATOM 138 C THR A 24 3.511 -21.662 160.923 1.00103.99 C ANISOU 138 C THR A 24 10411 17690 11409 -7378 -70 2036 C ATOM 139 O THR A 24 3.083 -21.389 162.049 1.00105.02 O ANISOU 139 O THR A 24 10400 18072 11429 -7371 5 2113 O ATOM 140 CB THR A 24 4.484 -23.948 160.632 1.00105.55 C ANISOU 140 CB THR A 24 11181 17173 11751 -7743 -226 2116 C ATOM 141 OG1 THR A 24 4.300 -25.206 159.977 1.00107.74 O ANISOU 141 OG1 THR A 24 11663 17216 12056 -8007 -336 2126 O ATOM 142 CG2 THR A 24 4.632 -24.176 162.118 1.00106.38 C ANISOU 142 CG2 THR A 24 11323 17301 11794 -7788 -169 2250 C ATOM 143 N GLY A 25 4.153 -20.778 160.173 1.00100.98 N ANISOU 143 N GLY A 25 10008 17235 11127 -7123 -58 1922 N ATOM 144 CA GLY A 25 4.646 -19.555 160.753 1.00101.42 C ANISOU 144 CA GLY A 25 9936 17409 11190 -6824 41 1894 C ATOM 145 C GLY A 25 5.917 -19.724 161.548 1.00100.70 C ANISOU 145 C GLY A 25 10078 16995 11189 -6750 69 1948 C ATOM 146 O GLY A 25 6.320 -18.795 162.253 1.00 94.87 O ANISOU 146 O GLY A 25 9245 16359 10441 -6526 157 1945 O ATOM 147 N GLU A 26 6.561 -20.881 161.464 1.00104.00 N ANISOU 147 N GLU A 26 10799 17025 11691 -6922 -6 1995 N ATOM 148 CA GLU A 26 7.791 -21.104 162.200 1.00101.84 C ANISOU 148 CA GLU A 26 10760 16431 11504 -6851 12 2051 C ATOM 149 C GLU A 26 8.964 -20.469 161.468 1.00 99.29 C ANISOU 149 C GLU A 26 10540 15859 11328 -6611 9 1946 C ATOM 150 O GLU A 26 9.009 -20.447 160.235 1.00 96.63 O ANISOU 150 O GLU A 26 10227 15430 11059 -6595 -50 1844 O ATOM 151 CB GLU A 26 8.031 -22.598 162.393 1.00104.77 C ANISOU 151 CB GLU A 26 11424 16476 11909 -7112 -73 2141 C ATOM 152 CG GLU A 26 9.205 -22.914 163.290 1.00105.10 C ANISOU 152 CG GLU A 26 11702 16209 12021 -7051 -59 2218 C ATOM 153 CD GLU A 26 9.923 -24.165 162.858 1.00106.24 C ANISOU 153 CD GLU A 26 12194 15892 12279 -7187 -164 2234 C ATOM 154 OE1 GLU A 26 9.645 -24.643 161.739 1.00106.93 O ANISOU 154 OE1 GLU A 26 12341 15879 12407 -7291 -244 2161 O ATOM 155 OE2 GLU A 26 10.766 -24.667 163.629 1.00106.16 O ANISOU 155 OE2 GLU A 26 12400 15621 12316 -7182 -170 2315 O ATOM 156 N ILE A 27 9.904 -19.933 162.239 1.00 93.73 N ANISOU 156 N ILE A 27 9890 15059 10664 -6426 74 1971 N ATOM 157 CA ILE A 27 11.100 -19.300 161.702 1.00 86.61 C ANISOU 157 CA ILE A 27 9089 13924 9894 -6195 81 1884 C ATOM 158 C ILE A 27 12.159 -20.366 161.485 1.00 86.28 C ANISOU 158 C ILE A 27 9404 13400 9980 -6280 -1 1906 C ATOM 159 O ILE A 27 12.502 -21.113 162.409 1.00 87.28 O ANISOU 159 O ILE A 27 9697 13364 10101 -6377 -7 2016 O ATOM 160 CB ILE A 27 11.611 -18.208 162.652 1.00 84.65 C ANISOU 160 CB ILE A 27 8732 13808 9623 -5956 189 1901 C ATOM 161 CG1 ILE A 27 10.518 -17.174 162.902 1.00 85.26 C ANISOU 161 CG1 ILE A 27 8461 14365 9569 -5855 269 1872 C ATOM 162 CG2 ILE A 27 12.864 -17.560 162.094 1.00 81.39 C ANISOU 162 CG2 ILE A 27 8427 13156 9343 -5731 194 1816 C ATOM 163 CD1 ILE A 27 10.933 -16.087 163.855 1.00 83.61 C ANISOU 163 CD1 ILE A 27 8138 14305 9324 -5615 377 1878 C ATOM 164 N ILE A 28 12.696 -20.429 160.273 1.00 84.96 N ANISOU 164 N ILE A 28 9355 13002 9924 -6230 -65 1800 N ATOM 165 CA ILE A 28 13.649 -21.480 159.944 1.00 84.89 C ANISOU 165 CA ILE A 28 9688 12532 10035 -6299 -151 1802 C ATOM 166 C ILE A 28 15.070 -20.926 159.978 1.00 81.83 C ANISOU 166 C ILE A 28 9434 11896 9762 -6062 -126 1763 C ATOM 167 O ILE A 28 16.013 -21.635 160.352 1.00 81.66 O ANISOU 167 O ILE A 28 9679 11531 9817 -6065 -161 1811 O ATOM 168 CB ILE A 28 13.318 -22.116 158.580 1.00 85.89 C ANISOU 168 CB ILE A 28 9895 12534 10205 -6425 -251 1708 C ATOM 169 CG1 ILE A 28 12.300 -23.252 158.741 1.00 89.43 C ANISOU 169 CG1 ILE A 28 10374 13034 10572 -6719 -308 1783 C ATOM 170 CG2 ILE A 28 14.558 -22.655 157.917 1.00 84.58 C ANISOU 170 CG2 ILE A 28 10037 11911 10187 -6361 -322 1643 C ATOM 171 CD1 ILE A 28 10.931 -22.810 159.196 1.00 91.18 C ANISOU 171 CD1 ILE A 28 10282 13723 10637 -6806 -252 1831 C ATOM 172 N HIS A 29 15.233 -19.650 159.625 1.00 79.53 N ANISOU 172 N HIS A 29 8959 11782 9478 -5851 -65 1681 N ATOM 173 CA HIS A 29 16.559 -19.052 159.594 1.00 76.67 C ANISOU 173 CA HIS A 29 8708 11204 9217 -5630 -40 1640 C ATOM 174 C HIS A 29 16.438 -17.538 159.714 1.00 74.77 C ANISOU 174 C HIS A 29 8195 11284 8931 -5416 57 1594 C ATOM 175 O HIS A 29 15.594 -16.927 159.061 1.00 74.96 O ANISOU 175 O HIS A 29 7993 11586 8903 -5393 67 1523 O ATOM 176 CB HIS A 29 17.301 -19.451 158.312 1.00 76.91 C ANISOU 176 CB HIS A 29 8948 10900 9373 -5609 -129 1528 C ATOM 177 CG HIS A 29 18.793 -19.266 158.374 1.00 72.95 C ANISOU 177 CG HIS A 29 8583 10155 8979 -5394 -113 1483 C ATOM 178 ND1 HIS A 29 19.667 -20.332 158.488 1.00 72.50 N ANISOU 178 ND1 HIS A 29 8830 9676 9040 -5377 -190 1443 N ATOM 179 CD2 HIS A 29 19.558 -18.148 158.302 1.00 70.63 C ANISOU 179 CD2 HIS A 29 8166 9983 8687 -5172 -32 1463 C ATOM 180 CE1 HIS A 29 20.903 -19.870 158.509 1.00 70.02 C ANISOU 180 CE1 HIS A 29 8571 9239 8794 -5134 -156 1399 C ATOM 181 NE2 HIS A 29 20.864 -18.551 158.401 1.00 68.85 N ANISOU 181 NE2 HIS A 29 8178 9403 8577 -4956 -61 1396 N ATOM 182 N LYS A 30 17.262 -16.953 160.589 1.00 73.12 N ANISOU 182 N LYS A 30 8008 11039 8734 -5255 128 1638 N ATOM 183 CA LYS A 30 17.446 -15.514 160.698 1.00 71.03 C ANISOU 183 CA LYS A 30 7537 11002 8448 -5019 218 1588 C ATOM 184 C LYS A 30 18.925 -15.208 160.514 1.00 68.48 C ANISOU 184 C LYS A 30 7436 10338 8245 -4743 206 1517 C ATOM 185 O LYS A 30 19.786 -16.041 160.807 1.00 68.48 O ANISOU 185 O LYS A 30 7695 10009 8316 -4798 163 1571 O ATOM 186 CB LYS A 30 16.953 -14.981 162.045 1.00 71.65 C ANISOU 186 CB LYS A 30 7437 11383 8405 -4968 319 1672 C ATOM 187 N ASN A 31 19.246 -14.098 159.889 1.00 67.88 N ANISOU 187 N ASN A 31 7260 10342 8189 -4432 243 1397 N ATOM 188 CA ASN A 31 20.632 -13.866 159.593 1.00 64.66 C ANISOU 188 CA ASN A 31 7054 9614 7901 -4184 212 1298 C ATOM 189 C ASN A 31 20.890 -12.421 159.273 1.00 62.41 C ANISOU 189 C ASN A 31 6620 9488 7604 -3851 275 1198 C ATOM 190 O ASN A 31 20.006 -11.721 158.859 1.00 65.54 O ANISOU 190 O ASN A 31 6775 10202 7925 -3815 309 1162 O ATOM 191 CB ASN A 31 20.905 -14.753 158.384 1.00 65.25 C ANISOU 191 CB ASN A 31 7263 9474 8055 -4279 114 1214 C ATOM 192 CG ASN A 31 22.079 -14.340 157.595 1.00 63.34 C ANISOU 192 CG ASN A 31 7284 8844 7937 -4107 70 1144 C ATOM 193 OD1 ASN A 31 22.918 -13.633 158.081 1.00 61.70 O ANISOU 193 OD1 ASN A 31 7193 8487 7765 -3968 99 1181 O ATOM 194 ND2 ASN A 31 22.133 -14.757 156.347 1.00 64.89 N ANISOU 194 ND2 ASN A 31 7572 8887 8195 -4118 -1 1039 N ATOM 195 N SER A 32 22.106 -11.964 159.471 1.00 61.05 N ANISOU 195 N SER A 32 6597 9093 7506 -3609 287 1155 N ATOM 196 CA SER A 32 22.455 -10.600 159.149 1.00 58.09 C ANISOU 196 CA SER A 32 6138 8793 7142 -3292 328 1048 C ATOM 197 C SER A 32 23.748 -10.639 158.407 1.00 56.28 C ANISOU 197 C SER A 32 6135 8218 7031 -3126 285 971 C ATOM 198 O SER A 32 24.677 -11.171 158.907 1.00 55.66 O ANISOU 198 O SER A 32 6221 7929 6998 -3076 289 1014 O ATOM 199 CB SER A 32 22.625 -9.812 160.408 1.00 57.62 C ANISOU 199 CB SER A 32 5956 8930 7007 -3142 421 1088 C ATOM 200 OG SER A 32 21.577 -8.897 160.553 1.00 58.70 O ANISOU 200 OG SER A 32 5824 9443 7035 -3163 469 1089 O ATOM 201 N ARG A 33 23.815 -10.060 157.222 1.00 55.59 N ANISOU 201 N ARG A 33 6048 8086 6986 -3048 243 859 N ATOM 202 CA ARG A 33 25.036 -10.047 156.431 1.00 53.95 C ANISOU 202 CA ARG A 33 6024 7594 6880 -2883 205 768 C ATOM 203 C ARG A 33 25.537 -8.627 156.460 1.00 52.00 C ANISOU 203 C ARG A 33 5704 7424 6630 -2583 257 697 C ATOM 204 O ARG A 33 24.800 -7.724 156.172 1.00 52.00 O ANISOU 204 O ARG A 33 5512 7679 6567 -2507 286 663 O ATOM 205 CB ARG A 33 24.732 -10.505 155.020 1.00 54.48 C ANISOU 205 CB ARG A 33 6133 7586 6981 -2981 130 687 C ATOM 206 CG ARG A 33 25.878 -10.491 154.048 1.00 52.82 C ANISOU 206 CG ARG A 33 6078 7132 6858 -2792 99 577 C ATOM 207 CD ARG A 33 27.040 -11.310 154.523 1.00 52.72 C ANISOU 207 CD ARG A 33 6305 6799 6926 -2814 71 604 C ATOM 208 NE ARG A 33 28.070 -11.410 153.519 1.00 51.63 N ANISOU 208 NE ARG A 33 6324 6422 6869 -2681 32 498 N ATOM 209 CZ ARG A 33 29.111 -12.203 153.629 1.00 51.32 C ANISOU 209 CZ ARG A 33 6493 6098 6908 -2636 8 497 C ATOM 210 NH1 ARG A 33 29.235 -12.952 154.688 1.00 52.01 N ANISOU 210 NH1 ARG A 33 6674 6082 7008 -2716 11 605 N ATOM 211 NH2 ARG A 33 30.014 -12.268 152.690 1.00 50.43 N ANISOU 211 NH2 ARG A 33 6498 5805 6857 -2507 -22 389 N ATOM 212 N ILE A 34 26.789 -8.438 156.850 1.00 50.48 N ANISOU 212 N ILE A 34 5662 7016 6503 -2415 266 677 N ATOM 213 CA ILE A 34 27.383 -7.123 157.013 1.00 48.85 C ANISOU 213 CA ILE A 34 5397 6882 6283 -2158 322 637 C ATOM 214 C ILE A 34 28.617 -6.869 156.205 1.00 47.16 C ANISOU 214 C ILE A 34 5335 6430 6155 -1980 299 553 C ATOM 215 O ILE A 34 29.503 -7.690 156.169 1.00 47.03 O ANISOU 215 O ILE A 34 5497 6164 6207 -2011 266 563 O ATOM 216 CB ILE A 34 27.797 -6.922 158.470 1.00 48.95 C ANISOU 216 CB ILE A 34 5392 6957 6251 -2141 381 728 C ATOM 217 CG1 ILE A 34 26.658 -7.269 159.408 1.00 50.87 C ANISOU 217 CG1 ILE A 34 5478 7448 6400 -2342 404 813 C ATOM 218 CG2 ILE A 34 28.275 -5.511 158.712 1.00 47.45 C ANISOU 218 CG2 ILE A 34 5140 6850 6037 -1883 438 682 C ATOM 219 CD1 ILE A 34 25.629 -6.188 159.534 1.00 51.22 C ANISOU 219 CD1 ILE A 34 5457 7630 6375 -2333 468 891 C ATOM 220 N PHE A 35 28.660 -5.704 155.567 1.00 48.71 N ANISOU 220 N PHE A 35 5459 6707 6341 -1790 316 473 N ATOM 221 CA PHE A 35 29.787 -5.277 154.759 1.00 49.23 C ANISOU 221 CA PHE A 35 5639 6594 6473 -1623 298 388 C ATOM 222 C PHE A 35 29.809 -3.755 154.757 1.00 52.81 C ANISOU 222 C PHE A 35 5992 7184 6889 -1410 340 343 C ATOM 223 O PHE A 35 29.106 -3.131 153.960 1.00 53.61 O ANISOU 223 O PHE A 35 5987 7426 6956 -1367 330 294 O ATOM 224 CB PHE A 35 29.692 -5.847 153.338 1.00 47.76 C ANISOU 224 CB PHE A 35 5507 6317 6322 -1696 236 316 C ATOM 225 CG PHE A 35 28.332 -5.702 152.699 1.00 47.97 C ANISOU 225 CG PHE A 35 5375 6564 6288 -1789 218 300 C ATOM 226 CD1 PHE A 35 27.294 -6.562 153.027 1.00 48.07 C ANISOU 226 CD1 PHE A 35 5320 6682 6262 -2014 202 364 C ATOM 227 CD2 PHE A 35 28.099 -4.726 151.744 1.00 47.76 C ANISOU 227 CD2 PHE A 35 5267 6642 6238 -1658 211 225 C ATOM 228 CE1 PHE A 35 26.051 -6.430 152.443 1.00 48.68 C ANISOU 228 CE1 PHE A 35 5237 6980 6278 -2102 183 350 C ATOM 229 CE2 PHE A 35 26.857 -4.591 151.157 1.00 48.57 C ANISOU 229 CE2 PHE A 35 5216 6956 6281 -1734 188 213 C ATOM 230 CZ PHE A 35 25.834 -5.447 151.503 1.00 48.91 C ANISOU 230 CZ PHE A 35 5180 7117 6286 -1956 175 272 C ATOM 231 N PRO A 36 30.585 -3.125 155.643 1.00 61.20 N ANISOU 231 N PRO A 36 7090 8210 7953 -1275 382 360 N ATOM 232 CA PRO A 36 30.516 -1.665 155.791 1.00 62.73 C ANISOU 232 CA PRO A 36 7195 8535 8103 -1083 422 323 C ATOM 233 C PRO A 36 30.652 -0.922 154.472 1.00 65.24 C ANISOU 233 C PRO A 36 7513 8836 8438 -967 394 235 C ATOM 234 O PRO A 36 31.620 -1.118 153.733 1.00 66.82 O ANISOU 234 O PRO A 36 7837 8851 8699 -933 365 191 O ATOM 235 CB PRO A 36 31.688 -1.364 156.727 1.00 63.45 C ANISOU 235 CB PRO A 36 7386 8504 8217 -979 451 343 C ATOM 236 CG PRO A 36 31.846 -2.618 157.517 1.00 63.17 C ANISOU 236 CG PRO A 36 7420 8381 8199 -1137 445 425 C ATOM 237 CD PRO A 36 31.577 -3.722 156.551 1.00 62.41 C ANISOU 237 CD PRO A 36 7373 8193 8146 -1290 390 414 C ATOM 238 N ALA A 37 29.664 -0.080 154.164 1.00 63.82 N ANISOU 238 N ALA A 37 7192 8859 8199 -905 401 212 N ATOM 239 CA ALA A 37 29.660 0.652 152.903 1.00 64.16 C ANISOU 239 CA ALA A 37 7228 8906 8246 -800 369 140 C ATOM 240 C ALA A 37 30.771 1.687 152.825 1.00 63.86 C ANISOU 240 C ALA A 37 7283 8751 8232 -612 382 99 C ATOM 241 O ALA A 37 31.069 2.170 151.727 1.00 66.15 O ANISOU 241 O ALA A 37 7609 8990 8535 -538 352 45 O ATOM 242 CB ALA A 37 28.311 1.338 152.696 1.00 67.18 C ANISOU 242 CB ALA A 37 7430 9543 8553 -763 369 133 C ATOM 243 N ALA A 38 31.383 2.038 153.959 1.00 56.14 N ANISOU 243 N ALA A 38 6343 7733 7254 -544 424 127 N ATOM 244 CA ALA A 38 32.453 3.028 153.963 1.00 53.29 C ANISOU 244 CA ALA A 38 6071 7265 6913 -383 435 92 C ATOM 245 C ALA A 38 33.621 2.611 153.087 1.00 48.95 C ANISOU 245 C ALA A 38 5656 6512 6431 -392 404 57 C ATOM 246 O ALA A 38 34.370 3.474 152.618 1.00 45.56 O ANISOU 246 O ALA A 38 5286 6014 6012 -273 401 17 O ATOM 247 CB ALA A 38 32.941 3.270 155.395 1.00 52.34 C ANISOU 247 CB ALA A 38 5974 7133 6779 -340 480 130 C ATOM 248 N GLN A 39 33.788 1.310 152.852 1.00 55.73 N ANISOU 248 N GLN A 39 6568 7275 7332 -531 381 71 N ATOM 249 CA GLN A 39 34.923 0.835 152.072 1.00 56.93 C ANISOU 249 CA GLN A 39 6847 7239 7546 -531 356 31 C ATOM 250 C GLN A 39 34.817 1.286 150.622 1.00 56.45 C ANISOU 250 C GLN A 39 6782 7189 7476 -489 325 -35 C ATOM 251 O GLN A 39 35.762 1.861 150.070 1.00 58.69 O ANISOU 251 O GLN A 39 7135 7387 7777 -394 324 -75 O ATOM 252 CB GLN A 39 35.012 -0.686 152.169 1.00 58.88 C ANISOU 252 CB GLN A 39 7156 7379 7836 -684 334 56 C ATOM 253 CG GLN A 39 36.411 -1.213 152.391 1.00 58.52 C ANISOU 253 CG GLN A 39 7244 7137 7852 -656 332 53 C ATOM 254 CD GLN A 39 36.417 -2.661 152.824 1.00 60.05 C ANISOU 254 CD GLN A 39 7506 7228 8085 -795 311 97 C ATOM 255 OE1 GLN A 39 36.962 -3.006 153.871 1.00 60.46 O ANISOU 255 OE1 GLN A 39 7606 7213 8154 -796 324 152 O ATOM 256 NE2 GLN A 39 35.806 -3.519 152.022 1.00 61.34 N ANISOU 256 NE2 GLN A 39 7678 7370 8256 -916 272 74 N ATOM 257 N ALA A 40 33.663 1.048 149.991 1.00 61.09 N ANISOU 257 N ALA A 40 7284 7896 8032 -565 298 -43 N ATOM 258 CA ALA A 40 33.474 1.434 148.597 1.00 61.02 C ANISOU 258 CA ALA A 40 7267 7914 8005 -534 262 -100 C ATOM 259 C ALA A 40 33.135 2.911 148.453 1.00 60.37 C ANISOU 259 C ALA A 40 7119 7946 7872 -385 270 -108 C ATOM 260 O ALA A 40 33.402 3.502 147.400 1.00 60.50 O ANISOU 260 O ALA A 40 7166 7944 7877 -318 246 -149 O ATOM 261 CB ALA A 40 32.381 0.578 147.950 1.00 64.30 C ANISOU 261 CB ALA A 40 7617 8413 8401 -681 222 -107 C ATOM 262 N GLU A 41 32.555 3.527 149.487 1.00 53.90 N ANISOU 262 N GLU A 41 6216 7244 7018 -329 301 -69 N ATOM 263 CA GLU A 41 32.361 4.968 149.441 1.00 54.12 C ANISOU 263 CA GLU A 41 6208 7350 7004 -167 307 -80 C ATOM 264 C GLU A 41 33.689 5.710 149.377 1.00 50.41 C ANISOU 264 C GLU A 41 5863 6730 6562 -60 318 -101 C ATOM 265 O GLU A 41 33.726 6.861 148.930 1.00 48.64 O ANISOU 265 O GLU A 41 5650 6522 6309 61 306 -119 O ATOM 266 CB GLU A 41 31.542 5.433 150.645 1.00 56.58 C ANISOU 266 CB GLU A 41 6414 7812 7271 -119 343 -45 C ATOM 267 CG GLU A 41 30.086 4.980 150.637 1.00 58.49 C ANISOU 267 CG GLU A 41 6501 8254 7467 -204 333 -25 C ATOM 268 CD GLU A 41 29.266 5.644 151.731 1.00 58.88 C ANISOU 268 CD GLU A 41 6433 8480 7459 -123 373 -1 C ATOM 269 OE1 GLU A 41 28.315 6.379 151.398 1.00 58.78 O ANISOU 269 OE1 GLU A 41 6310 8630 7394 -34 358 -16 O ATOM 270 OE2 GLU A 41 29.580 5.447 152.927 1.00 59.36 O ANISOU 270 OE2 GLU A 41 6512 8521 7523 -141 418 30 O ATOM 271 N ASN A 42 34.782 5.066 149.792 1.00 50.34 N ANISOU 271 N ASN A 42 5948 6575 6604 -106 336 -95 N ATOM 272 CA ASN A 42 36.107 5.646 149.665 1.00 48.55 C ANISOU 272 CA ASN A 42 5830 6216 6402 -27 344 -115 C ATOM 273 C ASN A 42 36.561 5.789 148.223 1.00 46.81 C ANISOU 273 C ASN A 42 5663 5938 6184 -18 313 -159 C ATOM 274 O ASN A 42 37.628 6.363 147.997 1.00 50.74 O ANISOU 274 O ASN A 42 6242 6346 6693 43 319 -175 O ATOM 275 CB ASN A 42 37.134 4.805 150.419 1.00 48.86 C ANISOU 275 CB ASN A 42 5942 6129 6493 -81 365 -98 C ATOM 276 CG ASN A 42 37.170 5.117 151.894 1.00 47.71 C ANISOU 276 CG ASN A 42 5780 6012 6336 -46 401 -57 C ATOM 277 OD1 ASN A 42 36.775 6.201 152.322 1.00 48.60 O ANISOU 277 OD1 ASN A 42 5855 6206 6405 48 414 -55 O ATOM 278 ND2 ASN A 42 37.650 4.169 152.682 1.00 46.95 N ANISOU 278 ND2 ASN A 42 5718 5847 6274 -116 413 -25 N ATOM 279 N ASN A 43 35.800 5.281 147.247 1.00 47.42 N ANISOU 279 N ASN A 43 5697 6075 6247 -84 279 -180 N ATOM 280 CA ASN A 43 36.209 5.443 145.857 1.00 40.03 C ANISOU 280 CA ASN A 43 4811 5098 5299 -75 249 -223 C ATOM 281 C ASN A 43 36.355 6.909 145.495 1.00 34.80 C ANISOU 281 C ASN A 43 4167 4460 4597 52 243 -221 C ATOM 282 O ASN A 43 37.191 7.260 144.661 1.00 33.29 O ANISOU 282 O ASN A 43 4050 4198 4401 77 235 -245 O ATOM 283 CB ASN A 43 35.217 4.764 144.923 1.00 41.36 C ANISOU 283 CB ASN A 43 4920 5351 5445 -164 209 -244 C ATOM 284 CG ASN A 43 35.662 4.812 143.487 1.00 39.11 C ANISOU 284 CG ASN A 43 4692 5028 5142 -165 179 -293 C ATOM 285 OD1 ASN A 43 36.596 4.120 143.105 1.00 40.41 O ANISOU 285 OD1 ASN A 43 4937 5078 5338 -208 186 -329 O ATOM 286 ND2 ASN A 43 35.010 5.639 142.684 1.00 37.93 N ANISOU 286 ND2 ASN A 43 4499 4978 4934 -112 146 -294 N ATOM 287 N LEU A 44 35.565 7.775 146.129 1.00 34.56 N ANISOU 287 N LEU A 44 4073 4525 4533 134 245 -194 N ATOM 288 CA LEU A 44 35.755 9.211 145.980 1.00 33.93 C ANISOU 288 CA LEU A 44 4032 4440 4419 263 237 -188 C ATOM 289 C LEU A 44 37.178 9.622 146.327 1.00 33.97 C ANISOU 289 C LEU A 44 4148 4306 4452 292 263 -190 C ATOM 290 O LEU A 44 37.771 10.462 145.643 1.00 36.55 O ANISOU 290 O LEU A 44 4547 4581 4759 343 248 -195 O ATOM 291 CB LEU A 44 34.762 9.962 146.859 1.00 34.47 C ANISOU 291 CB LEU A 44 4022 4619 4454 356 243 -166 C ATOM 292 CG LEU A 44 35.039 11.458 146.962 1.00 34.17 C ANISOU 292 CG LEU A 44 4049 4545 4389 500 236 -162 C ATOM 293 CD1 LEU A 44 34.883 12.135 145.606 1.00 34.47 C ANISOU 293 CD1 LEU A 44 4118 4589 4389 547 185 -167 C ATOM 294 CD2 LEU A 44 34.116 12.074 147.979 1.00 34.80 C ANISOU 294 CD2 LEU A 44 4054 4730 4438 598 249 -152 C ATOM 295 N VAL A 45 37.741 9.043 147.390 1.00 32.95 N ANISOU 295 N VAL A 45 4033 4122 4364 254 300 -180 N ATOM 296 CA VAL A 45 39.117 9.339 147.772 1.00 31.71 C ANISOU 296 CA VAL A 45 3969 3849 4233 272 322 -181 C ATOM 297 C VAL A 45 40.082 8.806 146.727 1.00 31.40 C ANISOU 297 C VAL A 45 3987 3731 4213 217 316 -210 C ATOM 298 O VAL A 45 41.067 9.462 146.375 1.00 31.88 O ANISOU 298 O VAL A 45 4118 3730 4267 246 318 -217 O ATOM 299 CB VAL A 45 39.416 8.747 149.164 1.00 31.52 C ANISOU 299 CB VAL A 45 3935 3799 4241 244 357 -160 C ATOM 300 CG1 VAL A 45 40.897 8.915 149.523 1.00 30.82 C ANISOU 300 CG1 VAL A 45 3931 3599 4179 252 375 -163 C ATOM 301 CG2 VAL A 45 38.520 9.370 150.217 1.00 31.90 C ANISOU 301 CG2 VAL A 45 3927 3938 4257 307 370 -138 C ATOM 302 N ARG A 46 39.815 7.604 146.224 1.00 31.71 N ANISOU 302 N ARG A 46 3999 3776 4273 132 307 -230 N ATOM 303 CA ARG A 46 40.679 6.999 145.216 1.00 31.58 C ANISOU 303 CA ARG A 46 4035 3693 4270 87 303 -270 C ATOM 304 C ARG A 46 40.721 7.829 143.941 1.00 31.67 C ANISOU 304 C ARG A 46 4071 3732 4230 119 280 -287 C ATOM 305 O ARG A 46 41.797 8.079 143.387 1.00 31.35 O ANISOU 305 O ARG A 46 4091 3638 4183 125 290 -304 O ATOM 306 CB ARG A 46 40.205 5.587 144.916 1.00 32.11 C ANISOU 306 CB ARG A 46 4077 3760 4364 -8 291 -295 C ATOM 307 CG ARG A 46 41.020 4.899 143.882 1.00 32.15 C ANISOU 307 CG ARG A 46 4137 3700 4380 -45 287 -349 C ATOM 308 CD ARG A 46 40.581 3.483 143.770 1.00 32.79 C ANISOU 308 CD ARG A 46 4211 3755 4491 -138 272 -375 C ATOM 309 NE ARG A 46 41.427 2.752 142.844 1.00 32.94 N ANISOU 309 NE ARG A 46 4293 3701 4522 -161 270 -439 N ATOM 310 CZ ARG A 46 41.091 2.439 141.596 1.00 33.49 C ANISOU 310 CZ ARG A 46 4368 3800 4557 -201 244 -491 C ATOM 311 NH1 ARG A 46 41.957 1.784 140.841 1.00 33.69 N ANISOU 311 NH1 ARG A 46 4452 3758 4589 -209 249 -557 N ATOM 312 NH2 ARG A 46 39.904 2.775 141.101 1.00 33.94 N ANISOU 312 NH2 ARG A 46 4367 3962 4567 -228 211 -482 N ATOM 313 N ARG A 47 39.553 8.252 143.446 1.00 32.21 N ANISOU 313 N ARG A 47 4089 3894 4255 137 247 -278 N ATOM 314 CA ARG A 47 39.537 9.066 142.240 1.00 32.42 C ANISOU 314 CA ARG A 47 4144 3948 4225 170 217 -283 C ATOM 315 C ARG A 47 40.200 10.407 142.482 1.00 33.96 C ANISOU 315 C ARG A 47 4405 4099 4400 250 223 -253 C ATOM 316 O ARG A 47 40.974 10.882 141.645 1.00 38.06 O ANISOU 316 O ARG A 47 4988 4585 4890 249 219 -258 O ATOM 317 CB ARG A 47 38.109 9.275 141.739 1.00 34.28 C ANISOU 317 CB ARG A 47 4306 4302 4416 186 173 -274 C ATOM 318 CG ARG A 47 38.057 9.906 140.344 1.00 35.22 C ANISOU 318 CG ARG A 47 4456 4455 4472 205 134 -278 C ATOM 319 CD ARG A 47 36.723 10.555 140.010 1.00 34.95 C ANISOU 319 CD ARG A 47 4355 4537 4386 265 84 -252 C ATOM 320 NE ARG A 47 35.579 9.723 140.355 1.00 35.60 N ANISOU 320 NE ARG A 47 4327 4719 4479 218 74 -261 N ATOM 321 CZ ARG A 47 34.607 10.116 141.171 1.00 38.19 C ANISOU 321 CZ ARG A 47 4574 5133 4803 280 70 -232 C ATOM 322 NH1 ARG A 47 34.627 11.340 141.695 1.00 37.19 N ANISOU 322 NH1 ARG A 47 4476 4992 4663 405 71 -202 N ATOM 323 NH2 ARG A 47 33.594 9.299 141.458 1.00 41.84 N ANISOU 323 NH2 ARG A 47 4927 5700 5270 217 63 -237 N ATOM 324 N THR A 48 39.894 11.043 143.614 1.00 31.94 N ANISOU 324 N THR A 48 4137 3844 4153 314 233 -223 N ATOM 325 CA THR A 48 40.490 12.337 143.914 1.00 31.72 C ANISOU 325 CA THR A 48 4185 3760 4106 385 233 -199 C ATOM 326 C THR A 48 42.005 12.257 143.915 1.00 31.13 C ANISOU 326 C THR A 48 4181 3595 4051 341 262 -208 C ATOM 327 O THR A 48 42.678 13.130 143.362 1.00 31.12 O ANISOU 327 O THR A 48 4252 3555 4017 352 252 -195 O ATOM 328 CB THR A 48 39.986 12.848 145.256 1.00 35.41 C ANISOU 328 CB THR A 48 4631 4240 4583 456 244 -180 C ATOM 329 OG1 THR A 48 38.558 12.818 145.259 1.00 35.36 O ANISOU 329 OG1 THR A 48 4537 4343 4555 497 222 -176 O ATOM 330 CG2 THR A 48 40.446 14.274 145.485 1.00 31.76 C ANISOU 330 CG2 THR A 48 4260 3714 4093 534 233 -161 C ATOM 331 N ASN A 49 42.558 11.198 144.504 1.00 30.75 N ANISOU 331 N ASN A 49 4111 3518 4055 288 295 -226 N ATOM 332 CA ASN A 49 44.002 11.066 144.613 1.00 30.30 C ANISOU 332 CA ASN A 49 4102 3391 4017 256 322 -236 C ATOM 333 C ASN A 49 44.636 10.666 143.294 1.00 30.42 C ANISOU 333 C ASN A 49 4137 3408 4013 208 323 -268 C ATOM 334 O ASN A 49 45.728 11.137 142.974 1.00 31.18 O ANISOU 334 O ASN A 49 4280 3476 4092 196 336 -267 O ATOM 335 CB ASN A 49 44.346 10.066 145.717 1.00 30.00 C ANISOU 335 CB ASN A 49 4036 3323 4038 231 351 -241 C ATOM 336 CG ASN A 49 44.231 10.679 147.102 1.00 29.82 C ANISOU 336 CG ASN A 49 4016 3291 4022 277 360 -210 C ATOM 337 OD1 ASN A 49 43.439 10.232 147.915 1.00 34.83 O ANISOU 337 OD1 ASN A 49 4603 3958 4674 281 365 -198 O ATOM 338 ND2 ASN A 49 45.042 11.690 147.380 1.00 29.61 N ANISOU 338 ND2 ASN A 49 4049 3224 3978 302 363 -198 N ATOM 339 N ARG A 50 43.968 9.812 142.508 1.00 30.78 N ANISOU 339 N ARG A 50 4145 3495 4056 174 309 -298 N ATOM 340 CA ARG A 50 44.455 9.499 141.165 1.00 31.05 C ANISOU 340 CA ARG A 50 4198 3544 4056 135 307 -335 C ATOM 341 C ARG A 50 44.550 10.748 140.305 1.00 31.27 C ANISOU 341 C ARG A 50 4272 3597 4013 155 286 -307 C ATOM 342 O ARG A 50 45.544 10.954 139.602 1.00 31.32 O ANISOU 342 O ARG A 50 4316 3597 3986 128 302 -318 O ATOM 343 CB ARG A 50 43.544 8.474 140.488 1.00 31.73 C ANISOU 343 CB ARG A 50 4242 3673 4141 93 285 -374 C ATOM 344 CG ARG A 50 43.971 8.105 139.065 1.00 31.96 C ANISOU 344 CG ARG A 50 4293 3725 4124 54 282 -424 C ATOM 345 CD ARG A 50 43.107 7.024 138.448 1.00 32.54 C ANISOU 345 CD ARG A 50 4334 3833 4197 3 257 -471 C ATOM 346 NE ARG A 50 41.704 7.383 138.310 1.00 32.94 N ANISOU 346 NE ARG A 50 4338 3959 4218 7 213 -442 N ATOM 347 CZ ARG A 50 40.723 6.932 139.083 1.00 33.08 C ANISOU 347 CZ ARG A 50 4300 3998 4272 -7 200 -427 C ATOM 348 NH1 ARG A 50 40.975 6.092 140.090 1.00 32.83 N ANISOU 348 NH1 ARG A 50 4263 3903 4309 -32 226 -432 N ATOM 349 NH2 ARG A 50 39.475 7.339 138.855 1.00 33.58 N ANISOU 349 NH2 ARG A 50 4308 4154 4298 5 160 -402 N ATOM 350 N GLN A 51 43.517 11.590 140.348 1.00 32.55 N ANISOU 350 N GLN A 51 4431 3790 4146 203 249 -269 N ATOM 351 CA GLN A 51 43.509 12.812 139.556 1.00 36.62 C ANISOU 351 CA GLN A 51 5004 4315 4593 229 219 -233 C ATOM 352 C GLN A 51 44.545 13.809 140.049 1.00 37.12 C ANISOU 352 C GLN A 51 5143 4310 4652 239 235 -199 C ATOM 353 O GLN A 51 45.214 14.463 139.240 1.00 41.52 O ANISOU 353 O GLN A 51 5759 4860 5155 211 229 -180 O ATOM 354 CB GLN A 51 42.120 13.428 139.582 1.00 41.54 C ANISOU 354 CB GLN A 51 5605 4987 5193 299 172 -202 C ATOM 355 CG GLN A 51 41.074 12.562 138.917 1.00 46.60 C ANISOU 355 CG GLN A 51 6170 5715 5822 275 147 -230 C ATOM 356 CD GLN A 51 39.682 13.051 139.187 1.00 50.36 C ANISOU 356 CD GLN A 51 6594 6258 6283 349 105 -203 C ATOM 357 OE1 GLN A 51 39.453 13.787 140.140 1.00 54.83 O ANISOU 357 OE1 GLN A 51 7169 6800 6864 424 106 -175 O ATOM 358 NE2 GLN A 51 38.737 12.635 138.364 1.00 52.25 N ANISOU 358 NE2 GLN A 51 6774 6591 6488 332 68 -215 N ATOM 359 N GLY A 52 44.688 13.947 141.373 1.00 32.14 N ANISOU 359 N GLY A 52 4510 3633 4070 269 252 -190 N ATOM 360 CA GLY A 52 45.730 14.806 141.907 1.00 31.02 C ANISOU 360 CA GLY A 52 4437 3426 3924 264 265 -165 C ATOM 361 C GLY A 52 47.114 14.368 141.477 1.00 30.85 C ANISOU 361 C GLY A 52 4421 3401 3899 188 301 -186 C ATOM 362 O GLY A 52 47.945 15.193 141.107 1.00 31.05 O ANISOU 362 O GLY A 52 4508 3407 3883 154 301 -160 O ATOM 363 N ARG A 53 47.376 13.061 141.508 1.00 30.60 N ANISOU 363 N ARG A 53 4326 3391 3910 161 331 -232 N ATOM 364 CA ARG A 53 48.671 12.556 141.071 1.00 30.58 C ANISOU 364 CA ARG A 53 4317 3400 3904 109 367 -262 C ATOM 365 C ARG A 53 48.919 12.850 139.599 1.00 31.11 C ANISOU 365 C ARG A 53 4408 3517 3896 69 362 -265 C ATOM 366 O ARG A 53 50.047 13.168 139.210 1.00 35.21 O ANISOU 366 O ARG A 53 4944 4053 4379 24 386 -262 O ATOM 367 CB ARG A 53 48.777 11.052 141.328 1.00 30.41 C ANISOU 367 CB ARG A 53 4234 3380 3941 105 392 -315 C ATOM 368 CG ARG A 53 48.714 10.650 142.779 1.00 29.98 C ANISOU 368 CG ARG A 53 4157 3281 3954 132 400 -306 C ATOM 369 CD ARG A 53 49.085 9.191 142.987 1.00 29.96 C ANISOU 369 CD ARG A 53 4114 3264 4007 124 422 -351 C ATOM 370 NE ARG A 53 48.304 8.280 142.157 1.00 30.55 N ANISOU 370 NE ARG A 53 4171 3357 4082 109 410 -392 N ATOM 371 CZ ARG A 53 47.297 7.531 142.594 1.00 31.60 C ANISOU 371 CZ ARG A 53 4278 3475 4252 106 394 -395 C ATOM 372 NH1 ARG A 53 46.647 6.740 141.759 1.00 30.83 N ANISOU 372 NH1 ARG A 53 4170 3397 4149 76 378 -436 N ATOM 373 NH2 ARG A 53 46.942 7.570 143.867 1.00 35.87 N ANISOU 373 NH2 ARG A 53 4807 3992 4832 124 393 -357 N ATOM 374 N ARG A 54 47.884 12.752 138.757 1.00 31.46 N ANISOU 374 N ARG A 54 4448 3599 3908 79 331 -270 N ATOM 375 CA ARG A 54 48.078 13.060 137.339 1.00 32.06 C ANISOU 375 CA ARG A 54 4550 3731 3901 39 323 -269 C ATOM 376 C ARG A 54 48.420 14.531 137.131 1.00 32.37 C ANISOU 376 C ARG A 54 4669 3750 3880 26 303 -199 C ATOM 377 O ARG A 54 49.271 14.855 136.295 1.00 32.79 O ANISOU 377 O ARG A 54 4750 3840 3870 -34 318 -189 O ATOM 378 CB ARG A 54 46.848 12.668 136.519 1.00 32.46 C ANISOU 378 CB ARG A 54 4578 3831 3924 52 286 -287 C ATOM 379 CG ARG A 54 46.683 11.164 136.302 1.00 32.47 C ANISOU 379 CG ARG A 54 4519 3857 3961 34 304 -365 C ATOM 380 CD ARG A 54 45.909 10.860 135.016 1.00 33.14 C ANISOU 380 CD ARG A 54 4595 4015 3982 12 272 -391 C ATOM 381 NE ARG A 54 45.546 9.454 134.861 1.00 33.29 N ANISOU 381 NE ARG A 54 4568 4044 4036 -10 276 -467 N ATOM 382 CZ ARG A 54 44.325 8.981 135.075 1.00 33.42 C ANISOU 382 CZ ARG A 54 4546 4072 4078 -6 241 -473 C ATOM 383 NH1 ARG A 54 43.359 9.797 135.456 1.00 33.41 N ANISOU 383 NH1 ARG A 54 4534 4088 4072 34 203 -412 N ATOM 384 NH2 ARG A 54 44.069 7.700 134.913 1.00 33.68 N ANISOU 384 NH2 ARG A 54 4553 4103 4141 -42 242 -541 N ATOM 385 N LEU A 55 47.795 15.435 137.891 1.00 32.29 N ANISOU 385 N LEU A 55 4702 3680 3885 78 268 -150 N ATOM 386 CA LEU A 55 48.120 16.855 137.750 1.00 32.72 C ANISOU 386 CA LEU A 55 4855 3690 3887 65 241 -83 C ATOM 387 C LEU A 55 49.556 17.137 138.162 1.00 32.60 C ANISOU 387 C LEU A 55 4862 3651 3873 -4 278 -76 C ATOM 388 O LEU A 55 50.260 17.904 137.496 1.00 33.15 O ANISOU 388 O LEU A 55 4994 3727 3876 -72 275 -35 O ATOM 389 CB LEU A 55 47.163 17.719 138.569 1.00 32.77 C ANISOU 389 CB LEU A 55 4908 3629 3915 151 196 -47 C ATOM 390 CG LEU A 55 45.711 17.786 138.113 1.00 33.17 C ANISOU 390 CG LEU A 55 4942 3714 3947 227 147 -38 C ATOM 391 CD1 LEU A 55 45.003 18.890 138.847 1.00 33.47 C ANISOU 391 CD1 LEU A 55 5043 3684 3990 321 103 2 C ATOM 392 CD2 LEU A 55 45.634 18.016 136.628 1.00 33.88 C ANISOU 392 CD2 LEU A 55 5062 3856 3954 190 119 -13 C ATOM 393 N ALA A 56 50.006 16.521 139.256 1.00 31.98 N ANISOU 393 N ALA A 56 4732 3553 3864 6 312 -110 N ATOM 394 CA ALA A 56 51.368 16.729 139.731 1.00 31.91 C ANISOU 394 CA ALA A 56 4729 3537 3858 -57 344 -105 C ATOM 395 C ALA A 56 52.380 16.025 138.842 1.00 32.16 C ANISOU 395 C ALA A 56 4704 3657 3856 -122 389 -140 C ATOM 396 O ALA A 56 53.469 16.551 138.600 1.00 32.56 O ANISOU 396 O ALA A 56 4772 3736 3861 -198 407 -117 O ATOM 397 CB ALA A 56 51.494 16.243 141.174 1.00 31.27 C ANISOU 397 CB ALA A 56 4606 3417 3856 -18 361 -129 C ATOM 398 N ARG A 57 52.047 14.826 138.365 1.00 32.03 N ANISOU 398 N ARG A 57 4620 3691 3860 -95 408 -199 N ATOM 399 CA ARG A 57 52.892 14.149 137.390 1.00 32.44 C ANISOU 399 CA ARG A 57 4623 3833 3871 -140 450 -245 C ATOM 400 C ARG A 57 53.153 15.021 136.173 1.00 33.22 C ANISOU 400 C ARG A 57 4772 3986 3863 -209 442 -203 C ATOM 401 O ARG A 57 54.286 15.106 135.691 1.00 33.69 O ANISOU 401 O ARG A 57 4812 4119 3872 -276 480 -206 O ATOM 402 CB ARG A 57 52.240 12.841 136.958 1.00 32.37 C ANISOU 402 CB ARG A 57 4560 3848 3890 -97 456 -316 C ATOM 403 CG ARG A 57 52.911 12.184 135.778 1.00 32.97 C ANISOU 403 CG ARG A 57 4600 4019 3909 -130 493 -373 C ATOM 404 CD ARG A 57 51.923 11.336 135.026 1.00 33.16 C ANISOU 404 CD ARG A 57 4612 4060 3928 -105 475 -426 C ATOM 405 NE ARG A 57 51.309 10.316 135.864 1.00 32.67 N ANISOU 405 NE ARG A 57 4519 3934 3960 -52 468 -466 N ATOM 406 CZ ARG A 57 50.291 9.556 135.481 1.00 32.80 C ANISOU 406 CZ ARG A 57 4527 3948 3989 -38 443 -506 C ATOM 407 NH1 ARG A 57 49.765 9.717 134.280 1.00 33.37 N ANISOU 407 NH1 ARG A 57 4615 4081 3983 -64 422 -515 N ATOM 408 NH2 ARG A 57 49.799 8.643 136.292 1.00 32.47 N ANISOU 408 NH2 ARG A 57 4461 3847 4030 -7 436 -534 N ATOM 409 N ARG A 58 52.117 15.689 135.666 1.00 33.46 N ANISOU 409 N ARG A 58 4868 3991 3856 -194 392 -159 N ATOM 410 CA ARG A 58 52.284 16.470 134.449 1.00 34.32 C ANISOU 410 CA ARG A 58 5032 4150 3857 -260 378 -111 C ATOM 411 C ARG A 58 52.915 17.823 134.731 1.00 34.70 C ANISOU 411 C ARG A 58 5167 4149 3868 -324 362 -28 C ATOM 412 O ARG A 58 53.628 18.357 133.875 1.00 35.48 O ANISOU 412 O ARG A 58 5298 4306 3877 -416 373 10 O ATOM 413 CB ARG A 58 50.937 16.611 133.728 1.00 34.59 C ANISOU 413 CB ARG A 58 5101 4183 3859 -214 324 -94 C ATOM 414 CG ARG A 58 50.441 15.287 133.155 1.00 34.52 C ANISOU 414 CG ARG A 58 5012 4242 3860 -186 339 -177 C ATOM 415 CD ARG A 58 48.940 15.255 132.926 1.00 34.58 C ANISOU 415 CD ARG A 58 5027 4239 3871 -124 281 -169 C ATOM 416 NE ARG A 58 48.520 13.943 132.447 1.00 34.58 N ANISOU 416 NE ARG A 58 4957 4298 3884 -115 293 -254 N ATOM 417 CZ ARG A 58 47.269 13.508 132.436 1.00 34.56 C ANISOU 417 CZ ARG A 58 4926 4299 3905 -71 253 -272 C ATOM 418 NH1 ARG A 58 46.291 14.274 132.878 1.00 34.53 N ANISOU 418 NH1 ARG A 58 4948 4256 3915 -16 201 -213 N ATOM 419 NH2 ARG A 58 47.005 12.293 131.995 1.00 34.68 N ANISOU 419 NH2 ARG A 58 4888 4359 3929 -81 264 -353 N ATOM 420 N LYS A 59 52.708 18.384 135.922 1.00 34.27 N ANISOU 420 N LYS A 59 5156 3990 3875 -287 336 -1 N ATOM 421 CA LYS A 59 53.429 19.606 136.265 1.00 34.72 C ANISOU 421 CA LYS A 59 5302 3991 3900 -360 321 67 C ATOM 422 C LYS A 59 54.925 19.344 136.340 1.00 34.88 C ANISOU 422 C LYS A 59 5259 4089 3903 -456 378 49 C ATOM 423 O LYS A 59 55.729 20.139 135.844 1.00 35.68 O ANISOU 423 O LYS A 59 5409 4220 3929 -567 381 103 O ATOM 424 CB LYS A 59 52.919 20.183 137.577 1.00 34.30 C ANISOU 424 CB LYS A 59 5305 3814 3914 -294 284 83 C ATOM 425 CG LYS A 59 53.651 21.445 137.965 1.00 34.88 C ANISOU 425 CG LYS A 59 5485 3813 3954 -376 261 146 C ATOM 426 CD LYS A 59 53.333 21.880 139.373 1.00 34.48 C ANISOU 426 CD LYS A 59 5479 3652 3970 -313 235 141 C ATOM 427 CE LYS A 59 51.936 22.407 139.494 1.00 34.58 C ANISOU 427 CE LYS A 59 5566 3577 3995 -196 177 159 C ATOM 428 NZ LYS A 59 51.969 23.857 139.738 1.00 35.40 N ANISOU 428 NZ LYS A 59 5829 3556 4064 -217 121 220 N ATOM 429 N LYS A 60 55.312 18.205 136.919 1.00 34.24 N ANISOU 429 N LYS A 60 5068 4052 3889 -416 424 -24 N ATOM 430 CA LYS A 60 56.718 17.832 136.973 1.00 34.47 C ANISOU 430 CA LYS A 60 5017 4176 3905 -486 479 -50 C ATOM 431 C LYS A 60 57.235 17.468 135.595 1.00 35.22 C ANISOU 431 C LYS A 60 5064 4405 3912 -542 519 -70 C ATOM 432 O LYS A 60 58.387 17.763 135.262 1.00 36.42 O ANISOU 432 O LYS A 60 5186 4650 4001 -640 553 -53 O ATOM 433 CB LYS A 60 56.926 16.671 137.949 1.00 35.32 C ANISOU 433 CB LYS A 60 5027 4287 4107 -409 509 -121 C ATOM 434 CG LYS A 60 58.222 15.901 137.724 1.00 38.29 C ANISOU 434 CG LYS A 60 5292 4788 4469 -440 569 -171 C ATOM 435 CD LYS A 60 58.173 14.520 138.334 1.00 39.56 C ANISOU 435 CD LYS A 60 5367 4947 4718 -339 592 -248 C ATOM 436 CE LYS A 60 58.023 14.611 139.853 1.00 41.34 C ANISOU 436 CE LYS A 60 5604 5077 5027 -298 567 -231 C ATOM 437 NZ LYS A 60 57.941 13.274 140.543 1.00 43.65 N ANISOU 437 NZ LYS A 60 5826 5353 5405 -204 582 -292 N ATOM 438 N HIS A 61 56.407 16.807 134.788 1.00 35.17 N ANISOU 438 N HIS A 61 5044 4423 3895 -485 516 -109 N ATOM 439 CA HIS A 61 56.825 16.498 133.427 1.00 35.98 C ANISOU 439 CA HIS A 61 5111 4658 3902 -536 552 -132 C ATOM 440 C HIS A 61 57.022 17.755 132.597 1.00 36.93 C ANISOU 440 C HIS A 61 5320 4803 3909 -647 530 -39 C ATOM 441 O HIS A 61 57.803 17.732 131.646 1.00 37.81 O ANISOU 441 O HIS A 61 5395 5045 3925 -728 572 -41 O ATOM 442 CB HIS A 61 55.821 15.570 132.733 1.00 35.83 C ANISOU 442 CB HIS A 61 5072 4653 3888 -459 544 -195 C ATOM 443 CG HIS A 61 56.357 14.921 131.495 1.00 36.62 C ANISOU 443 CG HIS A 61 5114 4897 3902 -491 593 -253 C ATOM 444 ND1 HIS A 61 57.531 14.202 131.481 1.00 36.92 N ANISOU 444 ND1 HIS A 61 5056 5037 3937 -497 659 -320 N ATOM 445 CD2 HIS A 61 55.876 14.877 130.231 1.00 37.27 C ANISOU 445 CD2 HIS A 61 5219 5048 3895 -510 584 -260 C ATOM 446 CE1 HIS A 61 57.753 13.747 130.262 1.00 37.74 C ANISOU 446 CE1 HIS A 61 5126 5265 3950 -517 694 -371 C ATOM 447 NE2 HIS A 61 56.762 14.141 129.485 1.00 37.95 N ANISOU 447 NE2 HIS A 61 5225 5273 3921 -531 649 -335 N ATOM 448 N ARG A 62 56.353 18.853 132.943 1.00 36.91 N ANISOU 448 N ARG A 62 5435 4677 3911 -652 466 43 N ATOM 449 CA ARG A 62 56.529 20.070 132.166 1.00 37.96 C ANISOU 449 CA ARG A 62 5673 4813 3937 -760 436 142 C ATOM 450 C ARG A 62 57.942 20.612 132.304 1.00 38.63 C ANISOU 450 C ARG A 62 5746 4960 3974 -896 472 179 C ATOM 451 O ARG A 62 58.520 21.100 131.325 1.00 39.73 O ANISOU 451 O ARG A 62 5905 5191 3999 -1014 487 230 O ATOM 452 CB ARG A 62 55.498 21.128 132.570 1.00 37.92 C ANISOU 452 CB ARG A 62 5808 4646 3954 -717 353 217 C ATOM 453 CG ARG A 62 54.097 20.848 132.043 1.00 37.74 C ANISOU 453 CG ARG A 62 5804 4600 3936 -611 308 206 C ATOM 454 CD ARG A 62 53.202 22.069 131.954 1.00 38.28 C ANISOU 454 CD ARG A 62 6019 4547 3977 -584 224 298 C ATOM 455 NE ARG A 62 52.806 22.622 133.239 1.00 37.78 N ANISOU 455 NE ARG A 62 6016 4339 4001 -514 186 310 N ATOM 456 CZ ARG A 62 51.874 22.107 134.035 1.00 36.92 C ANISOU 456 CZ ARG A 62 5862 4183 3982 -384 173 257 C ATOM 457 NH1 ARG A 62 51.246 20.997 133.700 1.00 36.43 N ANISOU 457 NH1 ARG A 62 5698 4199 3944 -320 191 191 N ATOM 458 NH2 ARG A 62 51.578 22.695 135.181 1.00 36.64 N ANISOU 458 NH2 ARG A 62 5886 4026 4010 -326 142 269 N ATOM 459 N ARG A 63 58.526 20.526 133.497 1.00 38.10 N ANISOU 459 N ARG A 63 5638 4855 3984 -891 486 157 N ATOM 460 CA ARG A 63 59.882 21.023 133.673 1.00 38.83 C ANISOU 460 CA ARG A 63 5705 5020 4028 -1028 517 190 C ATOM 461 C ARG A 63 60.925 20.018 133.224 1.00 39.13 C ANISOU 461 C ARG A 63 5581 5251 4035 -1049 600 117 C ATOM 462 O ARG A 63 62.049 20.416 132.906 1.00 42.36 O ANISOU 462 O ARG A 63 5952 5779 4365 -1181 635 150 O ATOM 463 CB ARG A 63 60.123 21.422 135.126 1.00 38.42 C ANISOU 463 CB ARG A 63 5678 4858 4059 -1023 492 199 C ATOM 464 CG ARG A 63 60.141 20.288 136.138 1.00 37.21 C ANISOU 464 CG ARG A 63 5412 4709 4018 -904 520 108 C ATOM 465 CD ARG A 63 59.612 20.794 137.468 1.00 36.54 C ANISOU 465 CD ARG A 63 5407 4462 4016 -852 468 125 C ATOM 466 NE ARG A 63 59.689 19.791 138.523 1.00 35.61 N ANISOU 466 NE ARG A 63 5190 4346 3995 -754 491 53 N ATOM 467 CZ ARG A 63 58.826 19.712 139.531 1.00 34.78 C ANISOU 467 CZ ARG A 63 5122 4121 3973 -653 457 38 C ATOM 468 NH1 ARG A 63 57.803 20.557 139.618 1.00 34.76 N ANISOU 468 NH1 ARG A 63 5246 3992 3970 -622 401 81 N ATOM 469 NH2 ARG A 63 58.966 18.768 140.440 1.00 34.07 N ANISOU 469 NH2 ARG A 63 4942 4042 3961 -577 479 -18 N ATOM 470 N VAL A 64 60.579 18.734 133.178 1.00 38.45 N ANISOU 470 N VAL A 64 5401 5203 4005 -922 632 19 N ATOM 471 CA VAL A 64 61.460 17.747 132.562 1.00 38.94 C ANISOU 471 CA VAL A 64 5322 5446 4027 -920 708 -60 C ATOM 472 C VAL A 64 61.498 17.947 131.055 1.00 40.01 C ANISOU 472 C VAL A 64 5471 5702 4029 -994 729 -40 C ATOM 473 O VAL A 64 62.565 17.943 130.430 1.00 41.06 O ANISOU 473 O VAL A 64 5525 6006 4068 -1084 787 -45 O ATOM 474 CB VAL A 64 60.997 16.328 132.928 1.00 38.04 C ANISOU 474 CB VAL A 64 5132 5309 4012 -761 725 -170 C ATOM 475 CG1 VAL A 64 61.561 15.309 131.955 1.00 38.73 C ANISOU 475 CG1 VAL A 64 5110 5562 4042 -735 792 -261 C ATOM 476 CG2 VAL A 64 61.409 16.008 134.346 1.00 37.33 C ANISOU 476 CG2 VAL A 64 4992 5161 4029 -709 724 -192 C ATOM 477 N ARG A 65 60.325 18.121 130.452 1.00 39.86 N ANISOU 477 N ARG A 65 5545 5608 3992 -957 683 -18 N ATOM 478 CA ARG A 65 60.236 18.444 129.035 1.00 40.93 C ANISOU 478 CA ARG A 65 5715 5844 3992 -1033 689 17 C ATOM 479 C ARG A 65 60.995 19.724 128.719 1.00 42.07 C ANISOU 479 C ARG A 65 5924 6030 4032 -1207 684 133 C ATOM 480 O ARG A 65 61.624 19.834 127.662 1.00 43.27 O ANISOU 480 O ARG A 65 6042 6344 4054 -1307 727 150 O ATOM 481 CB ARG A 65 58.762 18.566 128.663 1.00 41.19 C ANISOU 481 CB ARG A 65 5849 5765 4036 -959 621 38 C ATOM 482 CG ARG A 65 58.404 18.062 127.301 1.00 43.27 C ANISOU 482 CG ARG A 65 6095 6144 4202 -954 637 0 C ATOM 483 CD ARG A 65 57.150 17.214 127.357 1.00 44.78 C ANISOU 483 CD ARG A 65 6285 6261 4469 -818 602 -71 C ATOM 484 NE ARG A 65 56.104 17.793 128.191 1.00 43.24 N ANISOU 484 NE ARG A 65 6179 5889 4361 -758 525 -13 N ATOM 485 CZ ARG A 65 55.111 18.556 127.741 1.00 43.95 C ANISOU 485 CZ ARG A 65 6374 5915 4411 -753 453 64 C ATOM 486 NH1 ARG A 65 55.022 18.860 126.451 1.00 46.73 N ANISOU 486 NH1 ARG A 65 6762 6360 4633 -816 444 102 N ATOM 487 NH2 ARG A 65 54.208 19.028 128.589 1.00 43.20 N ANISOU 487 NH2 ARG A 65 6345 5669 4400 -680 389 103 N ATOM 488 N LEU A 66 60.978 20.690 129.640 1.00 41.84 N ANISOU 488 N LEU A 66 5987 5859 4051 -1251 633 212 N ATOM 489 CA LEU A 66 61.737 21.921 129.446 1.00 43.03 C ANISOU 489 CA LEU A 66 6211 6029 4109 -1432 621 324 C ATOM 490 C LEU A 66 63.236 21.678 129.536 1.00 43.72 C ANISOU 490 C LEU A 66 6160 6299 4154 -1535 698 298 C ATOM 491 O LEU A 66 64.013 22.347 128.848 1.00 45.10 O ANISOU 491 O LEU A 66 6342 6589 4205 -1702 720 370 O ATOM 492 CB LEU A 66 61.310 22.966 130.470 1.00 42.67 C ANISOU 492 CB LEU A 66 6309 5770 4132 -1442 542 400 C ATOM 493 CG LEU A 66 62.107 24.266 130.461 1.00 43.93 C ANISOU 493 CG LEU A 66 6566 5915 4212 -1637 519 515 C ATOM 494 CD1 LEU A 66 61.797 25.059 129.207 1.00 45.19 C ANISOU 494 CD1 LEU A 66 6845 6084 4241 -1735 486 616 C ATOM 495 CD2 LEU A 66 61.812 25.092 131.701 1.00 43.49 C ANISOU 495 CD2 LEU A 66 6633 5648 4243 -1626 448 554 C ATOM 496 N ASN A 67 63.663 20.737 130.377 1.00 43.24 N ANISOU 496 N ASN A 67 5968 6272 4187 -1440 738 201 N ATOM 497 CA ASN A 67 65.077 20.389 130.428 1.00 47.29 C ANISOU 497 CA ASN A 67 6327 6982 4660 -1513 812 165 C ATOM 498 C ASN A 67 65.537 19.786 129.110 1.00 48.01 C ANISOU 498 C ASN A 67 6314 7294 4632 -1533 887 117 C ATOM 499 O ASN A 67 66.592 20.151 128.583 1.00 48.58 O ANISOU 499 O ASN A 67 6319 7549 4590 -1678 936 152 O ATOM 500 CB ASN A 67 65.342 19.422 131.579 1.00 46.49 C ANISOU 500 CB ASN A 67 6113 6865 4688 -1379 832 69 C ATOM 501 CG ASN A 67 65.435 20.117 132.915 1.00 43.66 C ANISOU 501 CG ASN A 67 5815 6363 4409 -1412 779 119 C ATOM 502 OD1 ASN A 67 65.096 21.291 133.044 1.00 45.12 O ANISOU 502 OD1 ASN A 67 6148 6424 4572 -1509 719 216 O ATOM 503 ND2 ASN A 67 65.893 19.393 133.923 1.00 41.50 N ANISOU 503 ND2 ASN A 67 5436 6105 4227 -1328 797 52 N ATOM 504 N ARG A 68 64.760 18.857 128.557 1.00 53.87 N ANISOU 504 N ARG A 68 7041 8033 5393 -1395 897 33 N ATOM 505 CA ARG A 68 65.179 18.238 127.310 1.00 55.05 C ANISOU 505 CA ARG A 68 7097 8393 5426 -1403 968 -27 C ATOM 506 C ARG A 68 65.109 19.221 126.149 1.00 52.25 C ANISOU 506 C ARG A 68 6834 8105 4915 -1561 957 79 C ATOM 507 O ARG A 68 65.864 19.083 125.182 1.00 51.49 O ANISOU 507 O ARG A 68 6652 8227 4685 -1639 1026 64 O ATOM 508 CB ARG A 68 64.338 17.002 127.029 1.00 59.60 C ANISOU 508 CB ARG A 68 7650 8936 6061 -1225 973 -147 C ATOM 509 CG ARG A 68 65.126 15.904 126.342 1.00 64.44 C ANISOU 509 CG ARG A 68 8109 9762 6613 -1170 1064 -271 C ATOM 510 CD ARG A 68 64.384 14.593 126.413 1.00 66.82 C ANISOU 510 CD ARG A 68 8392 9989 7008 -984 1060 -400 C ATOM 511 NE ARG A 68 63.685 14.459 127.687 1.00 66.04 N ANISOU 511 NE ARG A 68 8348 9673 7073 -894 998 -393 N ATOM 512 CZ ARG A 68 63.129 13.334 128.115 1.00 67.35 C ANISOU 512 CZ ARG A 68 8496 9747 7347 -742 989 -492 C ATOM 513 NH1 ARG A 68 63.203 12.237 127.381 1.00 67.50 N ANISOU 513 NH1 ARG A 68 8453 9858 7336 -658 1034 -612 N ATOM 514 NH2 ARG A 68 62.507 13.302 129.280 1.00 68.74 N ANISOU 514 NH2 ARG A 68 8720 9739 7657 -678 935 -472 N ATOM 515 N LEU A 69 64.233 20.229 126.235 1.00 46.24 N ANISOU 515 N LEU A 69 6246 7160 4161 -1606 872 190 N ATOM 516 CA LEU A 69 64.211 21.273 125.214 1.00 47.58 C ANISOU 516 CA LEU A 69 6522 7372 4182 -1766 850 312 C ATOM 517 C LEU A 69 65.460 22.131 125.288 1.00 48.87 C ANISOU 517 C LEU A 69 6662 7644 4261 -1970 879 399 C ATOM 518 O LEU A 69 66.027 22.502 124.256 1.00 50.41 O ANISOU 518 O LEU A 69 6842 8011 4298 -2115 918 454 O ATOM 519 CB LEU A 69 62.959 22.144 125.351 1.00 47.08 C ANISOU 519 CB LEU A 69 6658 7074 4158 -1745 743 408 C ATOM 520 CG LEU A 69 62.913 23.458 124.565 1.00 48.49 C ANISOU 520 CG LEU A 69 6989 7234 4203 -1915 695 563 C ATOM 521 CD1 LEU A 69 62.702 23.207 123.073 1.00 49.52 C ANISOU 521 CD1 LEU A 69 7109 7522 4186 -1942 721 565 C ATOM 522 CD2 LEU A 69 61.784 24.323 125.095 1.00 47.91 C ANISOU 522 CD2 LEU A 69 7104 6894 4204 -1862 583 646 C ATOM 523 N PHE A 70 65.893 22.477 126.500 1.00 48.36 N ANISOU 523 N PHE A 70 6597 7488 4291 -1994 858 417 N ATOM 524 CA PHE A 70 67.132 23.230 126.645 1.00 49.65 C ANISOU 524 CA PHE A 70 6723 7765 4378 -2197 884 492 C ATOM 525 C PHE A 70 68.340 22.391 126.260 1.00 50.51 C ANISOU 525 C PHE A 70 6606 8168 4416 -2216 995 405 C ATOM 526 O PHE A 70 69.296 22.917 125.687 1.00 52.14 O ANISOU 526 O PHE A 70 6764 8561 4488 -2405 1038 469 O ATOM 527 CB PHE A 70 67.271 23.764 128.078 1.00 48.93 C ANISOU 527 CB PHE A 70 6685 7502 4404 -2212 830 521 C ATOM 528 CG PHE A 70 66.690 25.136 128.276 1.00 49.22 C ANISOU 528 CG PHE A 70 6950 7316 4435 -2314 732 655 C ATOM 529 CD1 PHE A 70 65.328 25.314 128.403 1.00 48.23 C ANISOU 529 CD1 PHE A 70 6977 6966 4382 -2182 655 668 C ATOM 530 CD2 PHE A 70 67.508 26.247 128.329 1.00 50.63 C ANISOU 530 CD2 PHE A 70 7193 7512 4533 -2543 714 767 C ATOM 531 CE1 PHE A 70 64.799 26.574 128.583 1.00 48.65 C ANISOU 531 CE1 PHE A 70 7244 6811 4430 -2256 562 785 C ATOM 532 CE2 PHE A 70 66.976 27.506 128.513 1.00 51.05 C ANISOU 532 CE2 PHE A 70 7475 7340 4582 -2631 618 887 C ATOM 533 CZ PHE A 70 65.622 27.666 128.639 1.00 50.06 C ANISOU 533 CZ PHE A 70 7502 6988 4532 -2476 542 893 C ATOM 534 N GLU A 71 68.316 21.093 126.555 1.00 56.49 N ANISOU 534 N GLU A 71 7228 8974 5261 -2024 1040 260 N ATOM 535 CA GLU A 71 69.392 20.220 126.100 1.00 64.90 C ANISOU 535 CA GLU A 71 8082 10320 6257 -2009 1144 164 C ATOM 536 C GLU A 71 69.460 20.179 124.579 1.00 66.07 C ANISOU 536 C GLU A 71 8212 10658 6235 -2076 1197 168 C ATOM 537 O GLU A 71 70.526 20.392 123.988 1.00 68.21 O ANISOU 537 O GLU A 71 8372 11175 6368 -2218 1267 191 O ATOM 538 CB GLU A 71 69.201 18.810 126.653 1.00 72.37 C ANISOU 538 CB GLU A 71 8920 11244 7333 -1771 1169 8 C ATOM 539 CG GLU A 71 69.863 18.572 127.982 1.00 78.28 C ANISOU 539 CG GLU A 71 9577 11970 8196 -1726 1168 -24 C ATOM 540 CD GLU A 71 69.956 17.099 128.319 1.00 83.48 C ANISOU 540 CD GLU A 71 10102 12667 8948 -1506 1209 -178 C ATOM 541 OE1 GLU A 71 69.040 16.580 128.996 1.00 82.91 O ANISOU 541 OE1 GLU A 71 10101 12390 9013 -1356 1160 -220 O ATOM 542 OE2 GLU A 71 70.944 16.458 127.896 1.00 91.04 O ANISOU 542 OE2 GLU A 71 10888 13863 9840 -1482 1291 -255 O ATOM 543 N GLU A 72 68.328 19.894 123.927 1.00 62.70 N ANISOU 543 N GLU A 72 7885 10132 5806 -1980 1165 146 N ATOM 544 CA GLU A 72 68.323 19.760 122.475 1.00 63.58 C ANISOU 544 CA GLU A 72 7981 10425 5752 -2028 1213 138 C ATOM 545 C GLU A 72 68.690 21.069 121.804 1.00 62.10 C ANISOU 545 C GLU A 72 7880 10309 5408 -2275 1201 302 C ATOM 546 O GLU A 72 69.467 21.084 120.846 1.00 61.84 O ANISOU 546 O GLU A 72 7754 10533 5210 -2388 1277 308 O ATOM 547 CB GLU A 72 66.958 19.280 121.992 1.00 66.44 C ANISOU 547 CB GLU A 72 8446 10649 6148 -1886 1164 93 C ATOM 548 CG GLU A 72 66.658 17.853 122.372 1.00 67.85 C ANISOU 548 CG GLU A 72 8533 10800 6447 -1662 1189 -78 C ATOM 549 CD GLU A 72 65.190 17.513 122.238 1.00 69.93 C ANISOU 549 CD GLU A 72 8917 10874 6781 -1535 1118 -105 C ATOM 550 OE1 GLU A 72 64.369 18.444 122.092 1.00 72.45 O ANISOU 550 OE1 GLU A 72 9391 11054 7084 -1600 1039 13 O ATOM 551 OE2 GLU A 72 64.856 16.312 122.277 1.00 71.36 O ANISOU 551 OE2 GLU A 72 9037 11044 7031 -1371 1137 -244 O ATOM 552 N SER A 73 68.146 22.179 122.295 1.00 56.96 N ANISOU 552 N SER A 73 7410 9432 4800 -2361 1105 436 N ATOM 553 CA SER A 73 68.531 23.477 121.769 1.00 57.09 C ANISOU 553 CA SER A 73 7531 9485 4677 -2606 1082 603 C ATOM 554 C SER A 73 70.013 23.759 121.960 1.00 57.10 C ANISOU 554 C SER A 73 7391 9700 4603 -2784 1152 630 C ATOM 555 O SER A 73 70.563 24.594 121.237 1.00 60.03 O ANISOU 555 O SER A 73 7795 10199 4815 -3007 1167 748 O ATOM 556 CB SER A 73 67.682 24.563 122.418 1.00 54.71 C ANISOU 556 CB SER A 73 7457 8873 4459 -2638 961 726 C ATOM 557 OG SER A 73 66.318 24.380 122.095 1.00 53.77 O ANISOU 557 OG SER A 73 7458 8591 4383 -2489 897 714 O ATOM 558 N GLY A 74 70.678 23.050 122.869 1.00 67.55 N ANISOU 558 N GLY A 74 8552 11085 6028 -2694 1197 524 N ATOM 559 CA GLY A 74 72.092 23.252 123.105 1.00 69.65 C ANISOU 559 CA GLY A 74 8662 11575 6228 -2849 1262 541 C ATOM 560 C GLY A 74 72.403 24.462 123.948 1.00 72.50 C ANISOU 560 C GLY A 74 9133 11796 6617 -3036 1191 674 C ATOM 561 O GLY A 74 73.545 24.928 123.953 1.00 74.82 O ANISOU 561 O GLY A 74 9330 12279 6818 -3234 1232 729 O ATOM 562 N LEU A 75 71.412 24.985 124.666 1.00 70.87 N ANISOU 562 N LEU A 75 9127 11268 6534 -2979 1086 723 N ATOM 563 CA LEU A 75 71.579 26.198 125.456 1.00 71.29 C ANISOU 563 CA LEU A 75 9323 11150 6616 -3148 1007 846 C ATOM 564 C LEU A 75 72.111 25.919 126.854 1.00 70.93 C ANISOU 564 C LEU A 75 9180 11068 6704 -3094 1002 780 C ATOM 565 O LEU A 75 72.938 26.688 127.355 1.00 72.69 O ANISOU 565 O LEU A 75 9403 11321 6896 -3288 987 854 O ATOM 566 CB LEU A 75 70.255 26.970 125.537 1.00 71.16 C ANISOU 566 CB LEU A 75 9576 10805 6655 -3107 892 930 C ATOM 567 CG LEU A 75 69.820 27.853 124.360 1.00 73.11 C ANISOU 567 CG LEU A 75 9996 11024 6759 -3248 854 1066 C ATOM 568 CD1 LEU A 75 69.941 27.178 122.998 1.00 75.72 C ANISOU 568 CD1 LEU A 75 10210 11610 6949 -3236 938 1028 C ATOM 569 CD2 LEU A 75 68.403 28.393 124.598 1.00 71.24 C ANISOU 569 CD2 LEU A 75 10000 10456 6610 -3132 738 1117 C ATOM 570 N ILE A 76 71.635 24.855 127.505 1.00 60.45 N ANISOU 570 N ILE A 76 7778 9672 5520 -2842 1009 647 N ATOM 571 CA ILE A 76 72.153 24.414 128.798 1.00 59.25 C ANISOU 571 CA ILE A 76 7513 9510 5490 -2766 1012 575 C ATOM 572 C ILE A 76 72.300 22.901 128.756 1.00 59.94 C ANISOU 572 C ILE A 76 7398 9745 5629 -2543 1089 416 C ATOM 573 O ILE A 76 71.324 22.191 128.494 1.00 60.08 O ANISOU 573 O ILE A 76 7458 9662 5708 -2355 1082 347 O ATOM 574 CB ILE A 76 71.241 24.814 129.969 1.00 52.78 C ANISOU 574 CB ILE A 76 6866 8367 4822 -2678 911 591 C ATOM 575 CG1 ILE A 76 71.185 26.328 130.116 1.00 52.56 C ANISOU 575 CG1 ILE A 76 7046 8178 4747 -2892 830 738 C ATOM 576 CG2 ILE A 76 71.727 24.191 131.247 1.00 50.77 C ANISOU 576 CG2 ILE A 76 6482 8121 4687 -2577 919 505 C ATOM 577 CD1 ILE A 76 70.229 26.779 131.169 1.00 51.23 C ANISOU 577 CD1 ILE A 76 7059 7694 4712 -2797 732 750 C ATOM 578 N THR A 77 73.508 22.408 129.014 1.00 70.12 N ANISOU 578 N THR A 77 8473 11274 6896 -2563 1157 359 N ATOM 579 CA THR A 77 73.759 20.980 129.156 1.00 69.87 C ANISOU 579 CA THR A 77 8254 11367 6928 -2341 1222 207 C ATOM 580 C THR A 77 73.888 20.551 130.609 1.00 71.31 C ANISOU 580 C THR A 77 8387 11443 7266 -2219 1187 153 C ATOM 581 O THR A 77 73.337 19.517 131.000 1.00 72.09 O ANISOU 581 O THR A 77 8462 11450 7480 -1992 1185 50 O ATOM 582 CB THR A 77 75.030 20.588 128.401 1.00 74.52 C ANISOU 582 CB THR A 77 8615 12319 7380 -2408 1327 165 C ATOM 583 OG1 THR A 77 74.805 20.711 126.991 1.00 75.08 O ANISOU 583 OG1 THR A 77 8719 12500 7308 -2473 1370 187 O ATOM 584 CG2 THR A 77 75.435 19.159 128.729 1.00 76.58 C ANISOU 584 CG2 THR A 77 8680 12701 7716 -2171 1386 6 C ATOM 585 N ASP A 78 74.590 21.338 131.420 1.00 69.08 N ANISOU 585 N ASP A 78 8096 11169 6983 -2376 1154 224 N ATOM 586 CA ASP A 78 74.821 21.033 132.825 1.00 64.90 C ANISOU 586 CA ASP A 78 7516 10562 6583 -2287 1118 184 C ATOM 587 C ASP A 78 73.792 21.786 133.661 1.00 60.64 C ANISOU 587 C ASP A 78 7206 9693 6141 -2292 1015 248 C ATOM 588 O ASP A 78 73.847 23.015 133.767 1.00 60.99 O ANISOU 588 O ASP A 78 7383 9654 6137 -2493 964 357 O ATOM 589 CB ASP A 78 76.243 21.420 133.223 1.00 64.56 C ANISOU 589 CB ASP A 78 7312 10745 6472 -2457 1141 216 C ATOM 590 CG ASP A 78 76.708 20.726 134.482 1.00 63.43 C ANISOU 590 CG ASP A 78 7042 10616 6443 -2322 1129 143 C ATOM 591 OD1 ASP A 78 75.870 20.473 135.372 1.00 62.81 O ANISOU 591 OD1 ASP A 78 7071 10294 6499 -2178 1069 118 O ATOM 592 OD2 ASP A 78 77.917 20.427 134.571 1.00 63.52 O ANISOU 592 OD2 ASP A 78 6838 10895 6402 -2360 1179 114 O ATOM 593 N PHE A 79 72.859 21.048 134.259 1.00 55.87 N ANISOU 593 N PHE A 79 6653 8905 5672 -2073 986 177 N ATOM 594 CA PHE A 79 71.834 21.629 135.112 1.00 54.01 C ANISOU 594 CA PHE A 79 6614 8373 5533 -2043 896 219 C ATOM 595 C PHE A 79 72.201 21.576 136.588 1.00 54.77 C ANISOU 595 C PHE A 79 6673 8410 5726 -2012 858 201 C ATOM 596 O PHE A 79 71.340 21.805 137.439 1.00 52.46 O ANISOU 596 O PHE A 79 6517 7886 5528 -1940 792 208 O ATOM 597 CB PHE A 79 70.494 20.927 134.885 1.00 50.09 C ANISOU 597 CB PHE A 79 6202 7712 5118 -1838 883 164 C ATOM 598 CG PHE A 79 69.907 21.159 133.516 1.00 48.41 C ANISOU 598 CG PHE A 79 6070 7509 4813 -1874 897 196 C ATOM 599 CD1 PHE A 79 69.077 22.239 133.276 1.00 48.94 C ANISOU 599 CD1 PHE A 79 6345 7396 4856 -1959 830 292 C ATOM 600 CD2 PHE A 79 70.182 20.291 132.471 1.00 46.98 C ANISOU 600 CD2 PHE A 79 5763 7521 4567 -1816 974 127 C ATOM 601 CE1 PHE A 79 68.536 22.452 132.026 1.00 48.81 C ANISOU 601 CE1 PHE A 79 6403 7393 4750 -1989 837 328 C ATOM 602 CE2 PHE A 79 69.645 20.503 131.216 1.00 46.83 C ANISOU 602 CE2 PHE A 79 5819 7521 4454 -1853 984 156 C ATOM 603 CZ PHE A 79 68.823 21.583 130.994 1.00 46.79 C ANISOU 603 CZ PHE A 79 6015 7338 4424 -1942 914 261 C ATOM 604 N THR A 80 73.456 21.279 136.914 1.00 61.35 N ANISOU 604 N THR A 80 7319 9460 6531 -2061 897 175 N ATOM 605 CA THR A 80 73.848 21.208 138.315 1.00 63.25 C ANISOU 605 CA THR A 80 7515 9661 6854 -2033 857 159 C ATOM 606 C THR A 80 74.097 22.593 138.897 1.00 65.27 C ANISOU 606 C THR A 80 7898 9828 7075 -2253 790 256 C ATOM 607 O THR A 80 73.674 22.884 140.020 1.00 66.78 O ANISOU 607 O THR A 80 8190 9835 7349 -2220 723 261 O ATOM 608 CB THR A 80 75.090 20.338 138.465 1.00 65.92 C ANISOU 608 CB THR A 80 7599 10272 7176 -1987 917 93 C ATOM 609 OG1 THR A 80 76.154 20.890 137.677 1.00 69.14 O ANISOU 609 OG1 THR A 80 7903 10925 7443 -2191 963 141 O ATOM 610 CG2 THR A 80 74.796 18.925 137.992 1.00 66.68 C ANISOU 610 CG2 THR A 80 7595 10422 7320 -1748 973 -13 C ATOM 611 N LYS A 81 74.772 23.461 138.154 1.00 69.33 N ANISOU 611 N LYS A 81 8414 10466 7462 -2484 804 333 N ATOM 612 CA LYS A 81 75.076 24.809 138.626 1.00 70.88 C ANISOU 612 CA LYS A 81 8742 10576 7614 -2719 737 428 C ATOM 613 C LYS A 81 73.960 25.799 138.333 1.00 68.69 C ANISOU 613 C LYS A 81 8739 10024 7335 -2769 672 502 C ATOM 614 O LYS A 81 74.232 26.960 138.020 1.00 74.79 O ANISOU 614 O LYS A 81 9632 10764 8019 -2998 637 600 O ATOM 615 CB LYS A 81 76.390 25.270 138.009 1.00 77.43 C ANISOU 615 CB LYS A 81 9438 11678 8302 -2962 781 483 C ATOM 616 CG LYS A 81 76.553 24.877 136.550 1.00 80.40 C ANISOU 616 CG LYS A 81 9722 12250 8578 -2968 865 481 C ATOM 617 CD LYS A 81 77.997 25.027 136.093 1.00 83.28 C ANISOU 617 CD LYS A 81 9883 12951 8809 -3168 926 508 C ATOM 618 CE LYS A 81 78.939 24.207 136.967 1.00 84.30 C ANISOU 618 CE LYS A 81 9771 13273 8985 -3077 952 426 C ATOM 619 NZ LYS A 81 78.545 22.769 137.012 1.00 83.52 N ANISOU 619 NZ LYS A 81 9562 13190 8984 -2763 997 303 N ATOM 620 N ILE A 82 72.700 25.389 138.427 1.00 54.85 N ANISOU 620 N ILE A 82 7094 8071 5675 -2562 651 462 N ATOM 621 CA ILE A 82 71.569 26.268 138.159 1.00 50.42 C ANISOU 621 CA ILE A 82 6784 7256 5117 -2575 586 526 C ATOM 622 C ILE A 82 71.068 26.812 139.484 1.00 47.49 C ANISOU 622 C ILE A 82 6558 6650 4836 -2541 504 525 C ATOM 623 O ILE A 82 70.608 26.051 140.340 1.00 45.54 O ANISOU 623 O ILE A 82 6266 6340 4696 -2350 500 448 O ATOM 624 CB ILE A 82 70.444 25.539 137.407 1.00 46.78 C ANISOU 624 CB ILE A 82 6348 6733 4693 -2376 610 484 C ATOM 625 CG1 ILE A 82 70.936 25.063 136.046 1.00 47.42 C ANISOU 625 CG1 ILE A 82 6300 7047 4670 -2418 691 481 C ATOM 626 CG2 ILE A 82 69.252 26.466 137.205 1.00 46.29 C ANISOU 626 CG2 ILE A 82 6539 6413 4638 -2373 536 550 C ATOM 627 CD1 ILE A 82 71.184 26.181 135.076 1.00 49.49 C ANISOU 627 CD1 ILE A 82 6673 7334 4798 -2647 678 596 C ATOM 628 N SER A 83 71.129 28.128 139.643 1.00 47.96 N ANISOU 628 N SER A 83 6801 6575 4849 -2724 436 609 N ATOM 629 CA SER A 83 70.780 28.741 140.914 1.00 47.57 C ANISOU 629 CA SER A 83 6894 6314 4868 -2712 357 603 C ATOM 630 C SER A 83 69.294 28.627 141.198 1.00 46.10 C ANISOU 630 C SER A 83 6850 5890 4775 -2492 319 570 C ATOM 631 O SER A 83 68.455 28.681 140.299 1.00 45.89 O ANISOU 631 O SER A 83 6909 5793 4734 -2426 319 596 O ATOM 632 CB SER A 83 71.166 30.215 140.939 1.00 49.24 C ANISOU 632 CB SER A 83 7291 6416 5000 -2965 288 700 C ATOM 633 OG SER A 83 70.549 30.851 142.047 1.00 48.82 O ANISOU 633 OG SER A 83 7420 6114 5015 -2917 206 685 O ATOM 634 N ILE A 84 68.970 28.503 142.481 1.00 45.19 N ANISOU 634 N ILE A 84 6760 5662 4749 -2384 283 515 N ATOM 635 CA ILE A 84 67.587 28.464 142.917 1.00 43.94 C ANISOU 635 CA ILE A 84 6732 5289 4675 -2185 245 482 C ATOM 636 C ILE A 84 67.234 29.647 143.805 1.00 44.42 C ANISOU 636 C ILE A 84 7011 5121 4746 -2236 157 505 C ATOM 637 O ILE A 84 66.151 29.677 144.373 1.00 43.52 O ANISOU 637 O ILE A 84 6998 4837 4701 -2069 123 470 O ATOM 638 CB ILE A 84 67.263 27.132 143.615 1.00 42.35 C ANISOU 638 CB ILE A 84 6373 5146 4572 -1969 286 388 C ATOM 639 CG1 ILE A 84 68.045 27.007 144.918 1.00 42.36 C ANISOU 639 CG1 ILE A 84 6296 5196 4604 -2003 273 351 C ATOM 640 CG2 ILE A 84 67.606 25.967 142.705 1.00 42.05 C ANISOU 640 CG2 ILE A 84 6138 5316 4523 -1912 368 357 C ATOM 641 CD1 ILE A 84 67.656 25.795 145.746 1.00 40.90 C ANISOU 641 CD1 ILE A 84 5989 5035 4516 -1794 299 270 C ATOM 642 N ASN A 85 68.111 30.651 143.900 1.00 45.96 N ANISOU 642 N ASN A 85 7287 5309 4869 -2467 117 563 N ATOM 643 CA ASN A 85 67.894 31.768 144.814 1.00 46.61 C ANISOU 643 CA ASN A 85 7581 5172 4957 -2526 30 573 C ATOM 644 C ASN A 85 67.915 33.118 144.109 1.00 48.30 C ANISOU 644 C ASN A 85 8021 5243 5088 -2712 -32 672 C ATOM 645 O ASN A 85 68.233 34.136 144.737 1.00 49.46 O ANISOU 645 O ASN A 85 8327 5256 5208 -2853 -102 694 O ATOM 646 CB ASN A 85 68.927 31.748 145.941 1.00 46.99 C ANISOU 646 CB ASN A 85 7539 5308 5005 -2633 20 538 C ATOM 647 CG ASN A 85 68.825 30.516 146.794 1.00 45.43 C ANISOU 647 CG ASN A 85 7156 5212 4893 -2441 64 447 C ATOM 648 OD1 ASN A 85 69.780 29.753 146.912 1.00 45.41 O ANISOU 648 OD1 ASN A 85 6941 5431 4884 -2479 113 425 O ATOM 649 ND2 ASN A 85 67.657 30.303 147.387 1.00 44.22 N ANISOU 649 ND2 ASN A 85 7081 4903 4818 -2231 46 396 N ATOM 650 N LEU A 86 67.600 33.151 142.821 1.00 48.59 N ANISOU 650 N LEU A 86 8082 5302 5077 -2721 -11 733 N ATOM 651 CA LEU A 86 67.329 34.392 142.110 1.00 50.08 C ANISOU 651 CA LEU A 86 8515 5318 5196 -2849 -78 833 C ATOM 652 C LEU A 86 65.822 34.578 141.995 1.00 49.34 C ANISOU 652 C LEU A 86 8583 5006 5158 -2623 -121 822 C ATOM 653 O LEU A 86 65.056 33.624 142.093 1.00 48.59 O ANISOU 653 O LEU A 86 8374 4951 5136 -2396 -80 753 O ATOM 654 CB LEU A 86 67.966 34.391 140.717 1.00 51.13 C ANISOU 654 CB LEU A 86 8580 5625 5224 -3019 -32 920 C ATOM 655 CG LEU A 86 69.385 33.849 140.575 1.00 51.67 C ANISOU 655 CG LEU A 86 8409 5990 5233 -3193 41 918 C ATOM 656 CD1 LEU A 86 69.687 33.546 139.107 1.00 52.28 C ANISOU 656 CD1 LEU A 86 8389 6258 5218 -3271 105 979 C ATOM 657 CD2 LEU A 86 70.418 34.828 141.151 1.00 53.39 C ANISOU 657 CD2 LEU A 86 8706 6187 5392 -3464 -11 965 C ATOM 658 N ASN A 87 65.400 35.815 141.776 1.00 50.66 N ANISOU 658 N ASN A 87 9016 4944 5287 -2686 -207 894 N ATOM 659 CA ASN A 87 63.975 36.100 141.691 1.00 50.21 C ANISOU 659 CA ASN A 87 9120 4679 5278 -2467 -258 887 C ATOM 660 C ASN A 87 63.468 35.838 140.274 1.00 50.19 C ANISOU 660 C ASN A 87 9097 4741 5232 -2422 -233 950 C ATOM 661 O ASN A 87 63.709 36.631 139.360 1.00 51.74 O ANISOU 661 O ASN A 87 9428 4892 5338 -2583 -269 1058 O ATOM 662 CB ASN A 87 63.690 37.540 142.079 1.00 51.77 C ANISOU 662 CB ASN A 87 9626 4587 5457 -2527 -369 930 C ATOM 663 CG ASN A 87 62.219 37.821 142.232 1.00 51.34 C ANISOU 663 CG ASN A 87 9724 4323 5462 -2268 -423 902 C ATOM 664 OD1 ASN A 87 61.391 37.097 141.708 1.00 50.20 O ANISOU 664 OD1 ASN A 87 9479 4246 5348 -2084 -386 884 O ATOM 665 ND2 ASN A 87 61.884 38.874 142.958 1.00 52.38 N ANISOU 665 ND2 ASN A 87 10096 4201 5604 -2250 -513 893 N ATOM 666 N PRO A 88 62.728 34.745 140.052 1.00 48.56 N ANISOU 666 N PRO A 88 8733 4637 5083 -2210 -177 888 N ATOM 667 CA PRO A 88 62.283 34.461 138.672 1.00 48.63 C ANISOU 667 CA PRO A 88 8713 4723 5039 -2177 -154 944 C ATOM 668 C PRO A 88 61.260 35.467 138.174 1.00 49.58 C ANISOU 668 C PRO A 88 9084 4618 5137 -2110 -246 1017 C ATOM 669 O PRO A 88 61.253 35.786 136.985 1.00 50.56 O ANISOU 669 O PRO A 88 9268 4767 5177 -2195 -257 1111 O ATOM 670 CB PRO A 88 61.692 33.049 138.783 1.00 46.67 C ANISOU 670 CB PRO A 88 8248 4612 4870 -1960 -83 843 C ATOM 671 CG PRO A 88 61.258 32.951 140.204 1.00 45.72 C ANISOU 671 CG PRO A 88 8141 4382 4850 -1818 -104 756 C ATOM 672 CD PRO A 88 62.175 33.760 141.031 1.00 46.72 C ANISOU 672 CD PRO A 88 8358 4438 4958 -1990 -140 769 C ATOM 673 N TYR A 89 60.449 36.034 139.064 1.00 49.52 N ANISOU 673 N TYR A 89 9231 4390 5195 -1966 -315 981 N ATOM 674 CA TYR A 89 59.459 37.018 138.658 1.00 50.58 C ANISOU 674 CA TYR A 89 9608 4299 5311 -1877 -409 1045 C ATOM 675 C TYR A 89 60.093 38.291 138.145 1.00 52.78 C ANISOU 675 C TYR A 89 10114 4447 5494 -2110 -480 1169 C ATOM 676 O TYR A 89 59.524 38.947 137.270 1.00 53.90 O ANISOU 676 O TYR A 89 10421 4475 5583 -2093 -542 1260 O ATOM 677 CB TYR A 89 58.542 37.345 139.819 1.00 50.18 C ANISOU 677 CB TYR A 89 9664 4056 5348 -1670 -463 966 C ATOM 678 CG TYR A 89 57.832 36.139 140.312 1.00 48.19 C ANISOU 678 CG TYR A 89 9201 3924 5183 -1448 -399 857 C ATOM 679 CD1 TYR A 89 58.417 35.299 141.254 1.00 46.95 C ANISOU 679 CD1 TYR A 89 8861 3897 5080 -1458 -331 767 C ATOM 680 CD2 TYR A 89 56.589 35.807 139.808 1.00 47.63 C ANISOU 680 CD2 TYR A 89 9111 3849 5136 -1237 -408 849 C ATOM 681 CE1 TYR A 89 57.764 34.169 141.682 1.00 45.23 C ANISOU 681 CE1 TYR A 89 8461 3785 4939 -1267 -275 677 C ATOM 682 CE2 TYR A 89 55.934 34.700 140.235 1.00 45.94 C ANISOU 682 CE2 TYR A 89 8708 3748 4998 -1054 -351 756 C ATOM 683 CZ TYR A 89 56.511 33.885 141.170 1.00 44.75 C ANISOU 683 CZ TYR A 89 8392 3710 4901 -1071 -285 672 C ATOM 684 OH TYR A 89 55.818 32.780 141.574 1.00 43.19 O ANISOU 684 OH TYR A 89 8020 3615 4776 -895 -234 588 O ATOM 685 N GLN A 90 61.244 38.675 138.681 1.00 53.56 N ANISOU 685 N GLN A 90 10230 4554 5565 -2331 -479 1177 N ATOM 686 CA GLN A 90 61.875 39.892 138.200 1.00 56.44 C ANISOU 686 CA GLN A 90 10818 4793 5835 -2579 -549 1300 C ATOM 687 C GLN A 90 62.591 39.661 136.879 1.00 56.50 C ANISOU 687 C GLN A 90 10727 5006 5733 -2776 -496 1401 C ATOM 688 O GLN A 90 62.637 40.568 136.046 1.00 58.30 O ANISOU 688 O GLN A 90 11150 5128 5872 -2913 -558 1527 O ATOM 689 CB GLN A 90 62.827 40.441 139.263 1.00 56.88 C ANISOU 689 CB GLN A 90 10936 4782 5893 -2760 -574 1274 C ATOM 690 CG GLN A 90 63.700 41.569 138.784 1.00 60.09 C ANISOU 690 CG GLN A 90 11537 5102 6193 -3070 -634 1401 C ATOM 691 CD GLN A 90 65.154 41.179 138.741 1.00 61.45 C ANISOU 691 CD GLN A 90 11513 5529 6305 -3340 -560 1415 C ATOM 692 OE1 GLN A 90 65.531 40.116 139.226 1.00 60.47 O ANISOU 692 OE1 GLN A 90 11125 5622 6229 -3281 -473 1319 O ATOM 693 NE2 GLN A 90 65.982 42.028 138.146 1.00 64.64 N ANISOU 693 NE2 GLN A 90 12016 5939 6606 -3611 -595 1521 N ATOM 694 N LEU A 91 63.130 38.457 136.660 1.00 55.20 N ANISOU 694 N LEU A 91 10270 5132 5569 -2785 -385 1346 N ATOM 695 CA LEU A 91 63.733 38.148 135.368 1.00 55.82 C ANISOU 695 CA LEU A 91 10239 5430 5541 -2943 -326 1426 C ATOM 696 C LEU A 91 62.665 37.966 134.299 1.00 55.60 C ANISOU 696 C LEU A 91 10247 5388 5491 -2783 -338 1466 C ATOM 697 O LEU A 91 62.939 38.122 133.107 1.00 56.69 O ANISOU 697 O LEU A 91 10398 5625 5518 -2918 -327 1566 O ATOM 698 CB LEU A 91 64.609 36.901 135.476 1.00 54.62 C ANISOU 698 CB LEU A 91 9768 5589 5398 -2976 -206 1343 C ATOM 699 CG LEU A 91 65.611 36.957 136.623 1.00 54.69 C ANISOU 699 CG LEU A 91 9711 5632 5437 -3103 -194 1291 C ATOM 700 CD1 LEU A 91 66.155 35.558 136.932 1.00 53.12 C ANISOU 700 CD1 LEU A 91 9192 5707 5283 -3030 -84 1182 C ATOM 701 CD2 LEU A 91 66.740 37.956 136.314 1.00 56.95 C ANISOU 701 CD2 LEU A 91 10102 5928 5608 -3440 -224 1405 C ATOM 702 N ARG A 92 61.452 37.627 134.714 1.00 54.28 N ANISOU 702 N ARG A 92 10089 5114 5421 -2502 -362 1390 N ATOM 703 CA ARG A 92 60.303 37.628 133.834 1.00 54.27 C ANISOU 703 CA ARG A 92 10155 5060 5404 -2337 -398 1430 C ATOM 704 C ARG A 92 59.869 39.026 133.433 1.00 56.79 C ANISOU 704 C ARG A 92 10789 5122 5666 -2383 -518 1556 C ATOM 705 O ARG A 92 59.128 39.179 132.452 1.00 58.01 O ANISOU 705 O ARG A 92 11015 5254 5771 -2307 -555 1626 O ATOM 706 CB ARG A 92 59.164 36.925 134.535 1.00 52.45 C ANISOU 706 CB ARG A 92 9843 4791 5296 -2036 -392 1311 C ATOM 707 CG ARG A 92 59.331 35.441 134.552 1.00 50.62 C ANISOU 707 CG ARG A 92 9315 4812 5106 -1962 -281 1207 C ATOM 708 CD ARG A 92 58.106 34.813 134.055 1.00 49.67 C ANISOU 708 CD ARG A 92 9137 4720 5018 -1737 -281 1173 C ATOM 709 NE ARG A 92 56.883 35.330 134.631 1.00 49.59 N ANISOU 709 NE ARG A 92 9271 4495 5076 -1528 -363 1155 N ATOM 710 CZ ARG A 92 56.355 34.785 135.704 1.00 48.20 C ANISOU 710 CZ ARG A 92 9009 4298 5008 -1353 -345 1044 C ATOM 711 NH1 ARG A 92 56.989 33.767 136.270 1.00 46.88 N ANISOU 711 NH1 ARG A 92 8633 4291 4888 -1377 -257 956 N ATOM 712 NH2 ARG A 92 55.205 35.231 136.200 1.00 48.22 N ANISOU 712 NH2 ARG A 92 9127 4129 5066 -1153 -414 1023 N ATOM 713 N VAL A 93 60.299 40.040 134.169 1.00 57.46 N ANISOU 713 N VAL A 93 11068 5009 5756 -2502 -585 1585 N ATOM 714 CA VAL A 93 60.069 41.418 133.789 1.00 59.66 C ANISOU 714 CA VAL A 93 11666 5031 5972 -2583 -704 1712 C ATOM 715 C VAL A 93 61.269 41.994 133.051 1.00 61.54 C ANISOU 715 C VAL A 93 11968 5335 6080 -2929 -702 1844 C ATOM 716 O VAL A 93 61.105 42.669 132.035 1.00 63.18 O ANISOU 716 O VAL A 93 12305 5497 6203 -2988 -757 1955 O ATOM 717 CB VAL A 93 59.709 42.248 135.038 1.00 60.09 C ANISOU 717 CB VAL A 93 11928 4796 6107 -2491 -791 1660 C ATOM 718 CG1 VAL A 93 59.342 43.657 134.655 1.00 62.45 C ANISOU 718 CG1 VAL A 93 12516 4847 6363 -2501 -917 1751 C ATOM 719 CG2 VAL A 93 58.557 41.581 135.786 1.00 58.21 C ANISOU 719 CG2 VAL A 93 11590 4538 5990 -2155 -778 1525 C ATOM 720 N LYS A 94 62.482 41.700 133.525 1.00 61.40 N ANISOU 720 N LYS A 94 11805 5474 6049 -3133 -633 1809 N ATOM 721 CA LYS A 94 63.681 42.137 132.817 1.00 63.19 C ANISOU 721 CA LYS A 94 12004 5846 6158 -3437 -615 1898 C ATOM 722 C LYS A 94 63.723 41.562 131.406 1.00 63.58 C ANISOU 722 C LYS A 94 11938 6118 6102 -3494 -550 1979 C ATOM 723 O LYS A 94 63.991 42.282 130.436 1.00 67.16 O ANISOU 723 O LYS A 94 12467 6593 6459 -3624 -589 2075 O ATOM 724 CB LYS A 94 64.930 41.731 133.599 1.00 63.69 C ANISOU 724 CB LYS A 94 11889 6080 6229 -3619 -543 1835 C ATOM 725 CG LYS A 94 66.217 42.400 133.122 1.00 66.97 C ANISOU 725 CG LYS A 94 12274 6632 6539 -3913 -545 1899 C ATOM 726 CD LYS A 94 67.438 41.563 133.490 1.00 68.43 C ANISOU 726 CD LYS A 94 12189 7105 6705 -4077 -436 1847 C ATOM 727 CE LYS A 94 68.742 42.233 133.081 1.00 71.27 C ANISOU 727 CE LYS A 94 12506 7616 6959 -4366 -441 1904 C ATOM 728 NZ LYS A 94 69.307 43.104 134.153 1.00 72.55 N ANISOU 728 NZ LYS A 94 12774 7640 7151 -4470 -517 1868 N ATOM 729 N GLY A 95 63.451 40.263 131.271 1.00 61.23 N ANISOU 729 N GLY A 95 11391 6031 5842 -3336 -453 1888 N ATOM 730 CA GLY A 95 63.463 39.626 129.967 1.00 61.22 C ANISOU 730 CA GLY A 95 11249 6266 5746 -3355 -386 1930 C ATOM 731 C GLY A 95 62.456 40.205 129.002 1.00 62.19 C ANISOU 731 C GLY A 95 11571 6245 5813 -3270 -470 2037 C ATOM 732 O GLY A 95 62.594 40.022 127.790 1.00 62.91 O ANISOU 732 O GLY A 95 11614 6504 5787 -3358 -437 2115 O ATOM 733 N LEU A 96 61.449 40.909 129.519 1.00 62.33 N ANISOU 733 N LEU A 96 11812 5964 5906 -3096 -579 2043 N ATOM 734 CA LEU A 96 60.448 41.546 128.675 1.00 63.43 C ANISOU 734 CA LEU A 96 12159 5945 5996 -2995 -675 2149 C ATOM 735 C LEU A 96 61.057 42.637 127.797 1.00 66.10 C ANISOU 735 C LEU A 96 12622 6267 6225 -3212 -730 2271 C ATOM 736 O LEU A 96 60.550 42.907 126.704 1.00 67.14 O ANISOU 736 O LEU A 96 12824 6404 6280 -3182 -771 2361 O ATOM 737 CB LEU A 96 59.348 42.117 129.568 1.00 63.19 C ANISOU 737 CB LEU A 96 12319 5608 6083 -2748 -779 2104 C ATOM 738 CG LEU A 96 57.878 41.988 129.205 1.00 62.68 C ANISOU 738 CG LEU A 96 12297 5462 6058 -2446 -836 2093 C ATOM 739 CD1 LEU A 96 57.540 40.548 128.899 1.00 60.57 C ANISOU 739 CD1 LEU A 96 11721 5472 5821 -2300 -730 1984 C ATOM 740 CD2 LEU A 96 57.039 42.491 130.367 1.00 62.41 C ANISOU 740 CD2 LEU A 96 12408 5158 6146 -2221 -916 2018 C ATOM 741 N THR A 97 62.140 43.274 128.252 1.00 67.34 N ANISOU 741 N THR A 97 12793 6418 6374 -3423 -735 2266 N ATOM 742 CA THR A 97 62.751 44.372 127.512 1.00 70.07 C ANISOU 742 CA THR A 97 13255 6744 6625 -3627 -794 2368 C ATOM 743 C THR A 97 64.262 44.224 127.372 1.00 70.84 C ANISOU 743 C THR A 97 13183 7089 6642 -3924 -712 2375 C ATOM 744 O THR A 97 64.840 44.706 126.396 1.00 72.81 O ANISOU 744 O THR A 97 13444 7443 6779 -4111 -718 2467 O ATOM 745 CB THR A 97 62.457 45.717 128.178 1.00 71.70 C ANISOU 745 CB THR A 97 13723 6630 6890 -3586 -926 2371 C ATOM 746 OG1 THR A 97 63.193 45.808 129.402 1.00 71.36 O ANISOU 746 OG1 THR A 97 13647 6556 6909 -3670 -911 2284 O ATOM 747 CG2 THR A 97 60.972 45.887 128.464 1.00 71.02 C ANISOU 747 CG2 THR A 97 13789 6303 6893 -3268 -1007 2345 C ATOM 748 N ASP A 98 64.923 43.593 128.334 1.00 69.46 N ANISOU 748 N ASP A 98 12851 7018 6523 -3969 -638 2279 N ATOM 749 CA ASP A 98 66.375 43.501 128.309 1.00 70.33 C ANISOU 749 CA ASP A 98 12793 7366 6563 -4237 -569 2277 C ATOM 750 C ASP A 98 66.821 42.048 128.283 1.00 68.36 C ANISOU 750 C ASP A 98 12244 7426 6304 -4237 -422 2209 C ATOM 751 O ASP A 98 66.043 41.129 128.548 1.00 66.18 O ANISOU 751 O ASP A 98 11905 7147 6093 -4036 -378 2150 O ATOM 752 CB ASP A 98 67.019 44.216 129.511 1.00 71.06 C ANISOU 752 CB ASP A 98 12961 7325 6713 -4337 -622 2227 C ATOM 753 CG ASP A 98 66.617 45.679 129.612 1.00 73.18 C ANISOU 753 CG ASP A 98 13534 7283 6990 -4336 -767 2281 C ATOM 754 OD1 ASP A 98 65.479 45.963 130.038 1.00 72.58 O ANISOU 754 OD1 ASP A 98 13627 6949 6999 -4104 -840 2255 O ATOM 755 OD2 ASP A 98 67.447 46.553 129.285 1.00 75.58 O ANISOU 755 OD2 ASP A 98 13904 7603 7210 -4565 -808 2347 O ATOM 756 N GLU A 99 68.102 41.855 127.979 1.00 69.29 N ANISOU 756 N GLU A 99 12175 7816 6337 -4463 -347 2214 N ATOM 757 CA GLU A 99 68.618 40.512 127.766 1.00 67.86 C ANISOU 757 CA GLU A 99 11695 7963 6124 -4470 -203 2152 C ATOM 758 C GLU A 99 68.874 39.802 129.092 1.00 65.99 C ANISOU 758 C GLU A 99 11329 7746 5997 -4408 -152 2036 C ATOM 759 O GLU A 99 69.241 40.422 130.096 1.00 66.43 O ANISOU 759 O GLU A 99 11464 7663 6113 -4467 -211 2009 O ATOM 760 CB GLU A 99 69.897 40.543 126.920 1.00 69.70 C ANISOU 760 CB GLU A 99 11757 8503 6222 -4715 -139 2191 C ATOM 761 CG GLU A 99 70.641 39.201 126.814 1.00 68.53 C ANISOU 761 CG GLU A 99 11276 8720 6042 -4729 13 2108 C ATOM 762 CD GLU A 99 71.933 39.309 126.019 1.00 70.60 C ANISOU 762 CD GLU A 99 11368 9287 6170 -4960 69 2139 C ATOM 763 OE1 GLU A 99 72.506 38.270 125.638 1.00 70.08 O ANISOU 763 OE1 GLU A 99 11033 9540 6053 -4960 193 2078 O ATOM 764 OE2 GLU A 99 72.380 40.444 125.771 1.00 72.89 O ANISOU 764 OE2 GLU A 99 11794 9498 6403 -5140 -13 2222 O ATOM 765 N LEU A 100 68.657 38.489 129.074 1.00 63.98 N ANISOU 765 N LEU A 100 10880 7667 5761 -4285 -43 1968 N ATOM 766 CA LEU A 100 68.851 37.547 130.158 1.00 62.04 C ANISOU 766 CA LEU A 100 10429 7504 5641 -4137 15 1813 C ATOM 767 C LEU A 100 69.923 36.541 129.775 1.00 61.95 C ANISOU 767 C LEU A 100 10095 7877 5565 -4217 148 1755 C ATOM 768 O LEU A 100 70.161 36.271 128.598 1.00 62.74 O ANISOU 768 O LEU A 100 10108 8184 5545 -4291 209 1802 O ATOM 769 CB LEU A 100 67.561 36.780 130.469 1.00 59.78 C ANISOU 769 CB LEU A 100 10119 7107 5487 -3781 8 1700 C ATOM 770 CG LEU A 100 66.246 37.516 130.681 1.00 59.61 C ANISOU 770 CG LEU A 100 10371 6746 5532 -3617 -108 1734 C ATOM 771 CD1 LEU A 100 65.118 36.539 131.044 1.00 57.30 C ANISOU 771 CD1 LEU A 100 9982 6422 5368 -3277 -91 1604 C ATOM 772 CD2 LEU A 100 66.426 38.583 131.756 1.00 60.43 C ANISOU 772 CD2 LEU A 100 10684 6594 5682 -3713 -201 1761 C ATOM 773 N SER A 101 70.551 35.969 130.792 1.00 64.41 N ANISOU 773 N SER A 101 10228 8286 5957 -4187 191 1647 N ATOM 774 CA SER A 101 71.379 34.796 130.597 1.00 63.38 C ANISOU 774 CA SER A 101 9774 8503 5803 -4168 316 1555 C ATOM 775 C SER A 101 70.497 33.590 130.292 1.00 61.50 C ANISOU 775 C SER A 101 9414 8314 5639 -3861 367 1443 C ATOM 776 O SER A 101 69.309 33.556 130.621 1.00 58.42 O ANISOU 776 O SER A 101 9153 7692 5351 -3646 308 1409 O ATOM 777 CB SER A 101 72.228 34.537 131.846 1.00 65.14 C ANISOU 777 CB SER A 101 9854 8797 6100 -4202 333 1474 C ATOM 778 OG SER A 101 72.832 33.250 131.836 1.00 65.13 O ANISOU 778 OG SER A 101 9541 9093 6112 -4099 444 1360 O ATOM 779 N ASN A 102 71.091 32.584 129.649 1.00 58.49 N ANISOU 779 N ASN A 102 8780 8244 5200 -3842 478 1380 N ATOM 780 CA ASN A 102 70.346 31.353 129.409 1.00 56.71 C ANISOU 780 CA ASN A 102 8430 8072 5046 -3560 529 1260 C ATOM 781 C ASN A 102 69.889 30.726 130.715 1.00 54.70 C ANISOU 781 C ASN A 102 8131 7684 4967 -3335 510 1139 C ATOM 782 O ASN A 102 68.793 30.159 130.786 1.00 53.15 O ANISOU 782 O ASN A 102 7964 7369 4863 -3098 495 1074 O ATOM 783 CB ASN A 102 71.189 30.360 128.609 1.00 57.16 C ANISOU 783 CB ASN A 102 8219 8487 5013 -3577 653 1198 C ATOM 784 CG ASN A 102 71.412 30.798 127.171 1.00 58.98 C ANISOU 784 CG ASN A 102 8485 8862 5062 -3754 681 1305 C ATOM 785 OD1 ASN A 102 72.086 30.106 126.409 1.00 59.64 O ANISOU 785 OD1 ASN A 102 8367 9244 5049 -3782 781 1263 O ATOM 786 ND2 ASN A 102 70.852 31.948 126.793 1.00 59.91 N ANISOU 786 ND2 ASN A 102 8862 8774 5128 -3868 590 1443 N ATOM 787 N GLU A 103 70.703 30.842 131.765 1.00 58.09 N ANISOU 787 N GLU A 103 8494 8137 5442 -3415 508 1114 N ATOM 788 CA GLU A 103 70.288 30.375 133.080 1.00 55.06 C ANISOU 788 CA GLU A 103 8089 7615 5215 -3223 481 1014 C ATOM 789 C GLU A 103 69.171 31.243 133.641 1.00 52.56 C ANISOU 789 C GLU A 103 8041 6957 4973 -3153 372 1055 C ATOM 790 O GLU A 103 68.211 30.726 134.222 1.00 50.90 O ANISOU 790 O GLU A 103 7848 6610 4880 -2919 352 977 O ATOM 791 CB GLU A 103 71.487 30.356 134.024 1.00 58.63 C ANISOU 791 CB GLU A 103 8407 8191 5680 -3343 501 986 C ATOM 792 CG GLU A 103 71.159 29.960 135.458 1.00 58.56 C ANISOU 792 CG GLU A 103 8384 8046 5821 -3171 468 894 C ATOM 793 CD GLU A 103 72.397 29.867 136.328 1.00 60.94 C ANISOU 793 CD GLU A 103 8531 8501 6122 -3288 487 865 C ATOM 794 OE1 GLU A 103 72.291 30.085 137.555 1.00 61.94 O ANISOU 794 OE1 GLU A 103 8716 8482 6335 -3250 432 835 O ATOM 795 OE2 GLU A 103 73.482 29.585 135.778 1.00 63.36 O ANISOU 795 OE2 GLU A 103 8651 9087 6336 -3418 558 873 O ATOM 796 N GLU A 104 69.271 32.564 133.480 1.00 58.18 N ANISOU 796 N GLU A 104 8966 7525 5613 -3353 298 1177 N ATOM 797 CA GLU A 104 68.180 33.430 133.912 1.00 58.08 C ANISOU 797 CA GLU A 104 9222 7183 5662 -3272 191 1215 C ATOM 798 C GLU A 104 66.914 33.174 133.109 1.00 56.28 C ANISOU 798 C GLU A 104 9067 6871 5445 -3080 176 1219 C ATOM 799 O GLU A 104 65.807 33.265 133.655 1.00 55.00 O ANISOU 799 O GLU A 104 9023 6494 5380 -2887 117 1184 O ATOM 800 CB GLU A 104 68.575 34.893 133.781 1.00 64.15 C ANISOU 800 CB GLU A 104 10219 7811 6342 -3532 112 1350 C ATOM 801 CG GLU A 104 69.765 35.305 134.615 1.00 68.25 C ANISOU 801 CG GLU A 104 10697 8387 6845 -3745 107 1355 C ATOM 802 CD GLU A 104 70.113 36.764 134.407 1.00 71.27 C ANISOU 802 CD GLU A 104 11328 8617 7135 -4018 23 1494 C ATOM 803 OE1 GLU A 104 70.511 37.428 135.387 1.00 72.21 O ANISOU 803 OE1 GLU A 104 11545 8610 7283 -4130 -36 1494 O ATOM 804 OE2 GLU A 104 69.974 37.249 133.260 1.00 73.10 O ANISOU 804 OE2 GLU A 104 11665 8847 7262 -4124 11 1605 O ATOM 805 N LEU A 105 67.056 32.853 131.819 1.00 53.78 N ANISOU 805 N LEU A 105 8675 6734 5023 -3132 230 1257 N ATOM 806 CA LEU A 105 65.888 32.551 130.999 1.00 53.17 C ANISOU 806 CA LEU A 105 8651 6604 4946 -2958 217 1258 C ATOM 807 C LEU A 105 65.253 31.230 131.410 1.00 51.06 C ANISOU 807 C LEU A 105 8217 6387 4797 -2691 264 1114 C ATOM 808 O LEU A 105 64.025 31.121 131.500 1.00 50.09 O ANISOU 808 O LEU A 105 8178 6108 4744 -2495 218 1089 O ATOM 809 CB LEU A 105 66.278 32.516 129.521 1.00 54.48 C ANISOU 809 CB LEU A 105 8771 6971 4958 -3094 265 1332 C ATOM 810 CG LEU A 105 65.136 32.085 128.610 1.00 53.90 C ANISOU 810 CG LEU A 105 8724 6882 4873 -2919 257 1323 C ATOM 811 CD1 LEU A 105 64.238 33.276 128.328 1.00 54.80 C ANISOU 811 CD1 LEU A 105 9122 6738 4962 -2927 140 1445 C ATOM 812 CD2 LEU A 105 65.669 31.485 127.325 1.00 54.66 C ANISOU 812 CD2 LEU A 105 8670 7262 4836 -3000 345 1328 C ATOM 813 N PHE A 106 66.080 30.217 131.667 1.00 50.47 N ANISOU 813 N PHE A 106 7905 6529 4742 -2681 355 1021 N ATOM 814 CA PHE A 106 65.575 28.921 132.099 1.00 48.62 C ANISOU 814 CA PHE A 106 7517 6338 4619 -2443 399 886 C ATOM 815 C PHE A 106 64.880 29.013 133.451 1.00 47.35 C ANISOU 815 C PHE A 106 7434 5960 4598 -2297 340 838 C ATOM 816 O PHE A 106 63.887 28.318 133.688 1.00 45.96 O ANISOU 816 O PHE A 106 7235 5717 4511 -2085 336 766 O ATOM 817 CB PHE A 106 66.715 27.905 132.142 1.00 48.54 C ANISOU 817 CB PHE A 106 7252 6595 4596 -2470 501 804 C ATOM 818 CG PHE A 106 66.333 26.601 132.777 1.00 46.79 C ANISOU 818 CG PHE A 106 6885 6395 4497 -2241 538 669 C ATOM 819 CD1 PHE A 106 65.590 25.677 132.082 1.00 46.02 C ANISOU 819 CD1 PHE A 106 6729 6344 4412 -2081 569 606 C ATOM 820 CD2 PHE A 106 66.721 26.294 134.068 1.00 46.01 C ANISOU 820 CD2 PHE A 106 6714 6272 4497 -2192 539 609 C ATOM 821 CE1 PHE A 106 65.235 24.473 132.650 1.00 44.56 C ANISOU 821 CE1 PHE A 106 6425 6169 4338 -1885 599 489 C ATOM 822 CE2 PHE A 106 66.359 25.078 134.639 1.00 44.52 C ANISOU 822 CE2 PHE A 106 6401 6096 4417 -1987 570 495 C ATOM 823 CZ PHE A 106 65.615 24.177 133.919 1.00 43.82 C ANISOU 823 CZ PHE A 106 6266 6043 4341 -1837 600 437 C ATOM 824 N ILE A 107 65.393 29.853 134.355 1.00 47.91 N ANISOU 824 N ILE A 107 7593 5925 4684 -2414 295 874 N ATOM 825 CA ILE A 107 64.708 30.089 135.624 1.00 46.93 C ANISOU 825 CA ILE A 107 7568 5587 4678 -2284 234 833 C ATOM 826 C ILE A 107 63.379 30.794 135.394 1.00 46.94 C ANISOU 826 C ILE A 107 7783 5358 4694 -2177 151 881 C ATOM 827 O ILE A 107 62.365 30.456 136.014 1.00 45.70 O ANISOU 827 O ILE A 107 7644 5084 4635 -1972 127 818 O ATOM 828 CB ILE A 107 65.610 30.891 136.583 1.00 47.77 C ANISOU 828 CB ILE A 107 7731 5638 4780 -2452 200 860 C ATOM 829 CG1 ILE A 107 66.784 30.039 137.066 1.00 47.49 C ANISOU 829 CG1 ILE A 107 7459 5830 4757 -2501 276 792 C ATOM 830 CG2 ILE A 107 64.820 31.423 137.761 1.00 47.17 C ANISOU 830 CG2 ILE A 107 7812 5310 4799 -2337 122 834 C ATOM 831 CD1 ILE A 107 67.900 30.844 137.648 1.00 48.78 C ANISOU 831 CD1 ILE A 107 7650 6010 4875 -2727 252 837 C ATOM 832 N ALA A 108 63.356 31.783 134.500 1.00 48.45 N ANISOU 832 N ALA A 108 8137 5487 4785 -2311 104 995 N ATOM 833 CA ALA A 108 62.121 32.520 134.245 1.00 48.70 C ANISOU 833 CA ALA A 108 8381 5298 4825 -2203 17 1049 C ATOM 834 C ALA A 108 61.055 31.637 133.603 1.00 47.61 C ANISOU 834 C ALA A 108 8161 5214 4713 -1999 39 1001 C ATOM 835 O ALA A 108 59.867 31.766 133.920 1.00 47.00 O ANISOU 835 O ALA A 108 8175 4981 4703 -1816 -17 982 O ATOM 836 CB ALA A 108 62.408 33.733 133.365 1.00 50.73 C ANISOU 836 CB ALA A 108 8831 5485 4960 -2403 -40 1193 C ATOM 837 N LEU A 109 61.454 30.734 132.701 1.00 47.44 N ANISOU 837 N LEU A 109 7967 5422 4637 -2026 119 977 N ATOM 838 CA LEU A 109 60.471 29.903 132.010 1.00 46.59 C ANISOU 838 CA LEU A 109 7790 5371 4542 -1853 135 932 C ATOM 839 C LEU A 109 60.026 28.720 132.858 1.00 44.76 C ANISOU 839 C LEU A 109 7403 5166 4436 -1660 176 800 C ATOM 840 O LEU A 109 58.862 28.310 132.785 1.00 47.35 O ANISOU 840 O LEU A 109 7736 5440 4817 -1483 152 762 O ATOM 841 CB LEU A 109 61.019 29.411 130.668 1.00 47.29 C ANISOU 841 CB LEU A 109 7769 5686 4513 -1954 201 951 C ATOM 842 CG LEU A 109 61.507 30.471 129.687 1.00 49.24 C ANISOU 842 CG LEU A 109 8150 5944 4615 -2165 172 1091 C ATOM 843 CD1 LEU A 109 62.314 29.832 128.554 1.00 49.90 C ANISOU 843 CD1 LEU A 109 8077 6302 4580 -2278 262 1086 C ATOM 844 CD2 LEU A 109 60.334 31.286 129.159 1.00 49.84 C ANISOU 844 CD2 LEU A 109 8434 5838 4665 -2093 74 1179 C ATOM 845 N LYS A 110 60.941 28.155 133.653 1.00 44.49 N ANISOU 845 N LYS A 110 7231 5223 4448 -1696 233 733 N ATOM 846 CA LYS A 110 60.581 27.061 134.550 1.00 43.70 C ANISOU 846 CA LYS A 110 6999 5137 4468 -1524 266 617 C ATOM 847 C LYS A 110 59.603 27.524 135.614 1.00 41.95 C ANISOU 847 C LYS A 110 6896 4702 4339 -1393 197 607 C ATOM 848 O LYS A 110 58.668 26.800 135.975 1.00 40.79 O ANISOU 848 O LYS A 110 6697 4527 4273 -1216 198 539 O ATOM 849 CB LYS A 110 61.834 26.482 135.196 1.00 42.39 C ANISOU 849 CB LYS A 110 6676 5108 4323 -1597 331 563 C ATOM 850 CG LYS A 110 61.537 25.498 136.293 1.00 40.90 C ANISOU 850 CG LYS A 110 6378 4905 4257 -1435 353 460 C ATOM 851 CD LYS A 110 62.814 25.032 136.948 1.00 41.41 C ANISOU 851 CD LYS A 110 6298 5100 4335 -1507 405 418 C ATOM 852 CE LYS A 110 62.681 23.610 137.467 1.00 39.67 C ANISOU 852 CE LYS A 110 5917 4950 4208 -1347 454 311 C ATOM 853 NZ LYS A 110 64.005 22.945 137.626 1.00 39.91 N ANISOU 853 NZ LYS A 110 5773 5167 4225 -1407 518 269 N ATOM 854 N ASN A 111 59.816 28.722 136.140 1.00 42.79 N ANISOU 854 N ASN A 111 7164 4661 4433 -1482 136 669 N ATOM 855 CA ASN A 111 58.858 29.287 137.075 1.00 42.44 C ANISOU 855 CA ASN A 111 7253 4411 4462 -1352 67 659 C ATOM 856 C ASN A 111 57.491 29.445 136.429 1.00 42.43 C ANISOU 856 C ASN A 111 7337 4327 4459 -1206 18 682 C ATOM 857 O ASN A 111 56.460 29.221 137.070 1.00 41.60 O ANISOU 857 O ASN A 111 7236 4139 4432 -1028 -6 630 O ATOM 858 CB ASN A 111 59.373 30.631 137.583 1.00 43.68 C ANISOU 858 CB ASN A 111 7593 4416 4587 -1489 4 725 C ATOM 859 CG ASN A 111 58.320 31.418 138.300 1.00 43.75 C ANISOU 859 CG ASN A 111 7779 4197 4648 -1353 -78 725 C ATOM 860 OD1 ASN A 111 57.845 32.432 137.806 1.00 44.90 O ANISOU 860 OD1 ASN A 111 8114 4199 4747 -1364 -151 802 O ATOM 861 ND2 ASN A 111 57.920 30.934 139.466 1.00 42.61 N ANISOU 861 ND2 ASN A 111 7571 4021 4597 -1215 -67 636 N ATOM 862 N MET A 112 57.464 29.814 135.148 1.00 45.69 N ANISOU 862 N MET A 112 7810 4776 4776 -1282 2 761 N ATOM 863 CA MET A 112 56.200 30.048 134.455 1.00 44.72 C ANISOU 863 CA MET A 112 7774 4582 4638 -1153 -54 795 C ATOM 864 C MET A 112 55.446 28.743 134.233 1.00 44.41 C ANISOU 864 C MET A 112 7563 4664 4647 -999 -9 709 C ATOM 865 O MET A 112 54.224 28.684 134.402 1.00 42.99 O ANISOU 865 O MET A 112 7408 4411 4514 -829 -50 688 O ATOM 866 CB MET A 112 56.483 30.753 133.131 1.00 47.27 C ANISOU 866 CB MET A 112 8201 4926 4832 -1294 -82 909 C ATOM 867 CG MET A 112 55.417 31.711 132.648 1.00 47.80 C ANISOU 867 CG MET A 112 8462 4831 4867 -1210 -182 992 C ATOM 868 SD MET A 112 56.153 33.158 131.879 1.00 48.43 S ANISOU 868 SD MET A 112 8766 4816 4818 -1436 -244 1150 S ATOM 869 CE MET A 112 57.708 32.515 131.294 1.00 48.58 C ANISOU 869 CE MET A 112 8614 5089 4754 -1673 -135 1150 C ATOM 870 N VAL A 113 56.169 27.678 133.892 1.00 41.81 N ANISOU 870 N VAL A 113 7058 4522 4307 -1055 76 655 N ATOM 871 CA VAL A 113 55.572 26.382 133.605 1.00 40.76 C ANISOU 871 CA VAL A 113 6769 4504 4212 -932 120 570 C ATOM 872 C VAL A 113 54.953 25.727 134.839 1.00 39.42 C ANISOU 872 C VAL A 113 6529 4280 4167 -779 127 482 C ATOM 873 O VAL A 113 54.058 24.877 134.707 1.00 38.68 O ANISOU 873 O VAL A 113 6353 4227 4114 -654 135 426 O ATOM 874 CB VAL A 113 56.657 25.494 132.961 1.00 40.77 C ANISOU 874 CB VAL A 113 6618 4708 4164 -1038 208 532 C ATOM 875 CG1 VAL A 113 56.856 24.194 133.724 1.00 39.47 C ANISOU 875 CG1 VAL A 113 6284 4619 4095 -954 272 417 C ATOM 876 CG2 VAL A 113 56.340 25.236 131.516 1.00 41.37 C ANISOU 876 CG2 VAL A 113 6680 4892 4146 -1053 214 554 C ATOM 877 N LYS A 114 55.392 26.102 136.043 1.00 39.77 N ANISOU 877 N LYS A 114 6604 4238 4267 -794 122 470 N ATOM 878 CA LYS A 114 54.862 25.504 137.256 1.00 39.13 C ANISOU 878 CA LYS A 114 6457 4116 4293 -661 131 393 C ATOM 879 C LYS A 114 53.597 26.177 137.755 1.00 38.08 C ANISOU 879 C LYS A 114 6438 3833 4196 -522 60 406 C ATOM 880 O LYS A 114 52.976 25.672 138.693 1.00 37.20 O ANISOU 880 O LYS A 114 6269 3700 4165 -401 67 344 O ATOM 881 CB LYS A 114 55.915 25.539 138.366 1.00 45.09 C ANISOU 881 CB LYS A 114 7183 4864 5085 -735 158 368 C ATOM 882 CG LYS A 114 57.223 24.880 137.971 1.00 50.30 C ANISOU 882 CG LYS A 114 7715 5687 5711 -860 228 351 C ATOM 883 CD LYS A 114 58.332 25.183 138.952 1.00 52.03 C ANISOU 883 CD LYS A 114 7924 5901 5945 -958 239 347 C ATOM 884 CE LYS A 114 58.257 24.283 140.166 1.00 54.17 C ANISOU 884 CE LYS A 114 8087 6180 6313 -853 266 266 C ATOM 885 NZ LYS A 114 57.086 24.574 141.043 1.00 55.23 N ANISOU 885 NZ LYS A 114 8304 6170 6511 -716 219 251 N ATOM 886 N HIS A 115 53.212 27.310 137.172 1.00 39.20 N ANISOU 886 N HIS A 115 6742 3874 4278 -534 -8 486 N ATOM 887 CA HIS A 115 51.986 27.997 137.523 1.00 39.49 C ANISOU 887 CA HIS A 115 6890 3776 4340 -385 -80 499 C ATOM 888 C HIS A 115 51.458 28.633 136.244 1.00 40.61 C ANISOU 888 C HIS A 115 7134 3896 4399 -385 -137 582 C ATOM 889 O HIS A 115 51.544 29.839 136.046 1.00 41.84 O ANISOU 889 O HIS A 115 7470 3922 4506 -428 -202 661 O ATOM 890 CB HIS A 115 52.220 29.037 138.617 1.00 40.01 C ANISOU 890 CB HIS A 115 7097 3676 4429 -390 -122 509 C ATOM 891 CG HIS A 115 53.273 28.643 139.599 1.00 39.33 C ANISOU 891 CG HIS A 115 6936 3626 4383 -478 -68 459 C ATOM 892 ND1 HIS A 115 53.017 27.816 140.670 1.00 38.17 N ANISOU 892 ND1 HIS A 115 6670 3516 4318 -381 -29 375 N ATOM 893 CD2 HIS A 115 54.592 28.939 139.658 1.00 39.78 C ANISOU 893 CD2 HIS A 115 7010 3701 4404 -657 -48 486 C ATOM 894 CE1 HIS A 115 54.130 27.633 141.356 1.00 37.92 C ANISOU 894 CE1 HIS A 115 6591 3516 4299 -488 8 352 C ATOM 895 NE2 HIS A 115 55.102 28.299 140.759 1.00 39.24 N ANISOU 895 NE2 HIS A 115 6834 3679 4398 -656 -2 416 N ATOM 896 N ARG A 116 50.914 27.794 135.358 1.00 40.26 N ANISOU 896 N ARG A 116 6981 3980 4337 -340 -117 565 N ATOM 897 CA ARG A 116 50.493 28.215 134.031 1.00 41.30 C ANISOU 897 CA ARG A 116 7183 4130 4378 -353 -165 642 C ATOM 898 C ARG A 116 49.025 28.620 133.971 1.00 41.69 C ANISOU 898 C ARG A 116 7291 4107 4440 -171 -242 658 C ATOM 899 O ARG A 116 48.496 28.827 132.878 1.00 42.48 O ANISOU 899 O ARG A 116 7430 4241 4470 -154 -286 715 O ATOM 900 CB ARG A 116 50.799 27.113 133.006 1.00 40.92 C ANISOU 900 CB ARG A 116 6988 4274 4285 -419 -103 613 C ATOM 901 CG ARG A 116 50.309 25.706 133.354 1.00 39.58 C ANISOU 901 CG ARG A 116 6635 4212 4192 -324 -49 505 C ATOM 902 CD ARG A 116 48.964 25.402 132.726 1.00 39.68 C ANISOU 902 CD ARG A 116 6617 4266 4195 -200 -92 500 C ATOM 903 NE ARG A 116 48.580 23.997 132.837 1.00 38.62 N ANISOU 903 NE ARG A 116 6312 4247 4116 -147 -41 403 N ATOM 904 CZ ARG A 116 48.849 23.070 131.924 1.00 38.53 C ANISOU 904 CZ ARG A 116 6205 4372 4061 -206 2 366 C ATOM 905 NH1 ARG A 116 48.449 21.819 132.104 1.00 37.68 N ANISOU 905 NH1 ARG A 116 5963 4343 4010 -156 40 276 N ATOM 906 NH2 ARG A 116 49.515 23.396 130.830 1.00 41.23 N ANISOU 906 NH2 ARG A 116 6593 4773 4300 -320 7 418 N ATOM 907 N GLY A 117 48.358 28.737 135.104 1.00 41.25 N ANISOU 907 N GLY A 117 7240 3968 4466 -33 -260 609 N ATOM 908 CA GLY A 117 47.092 29.434 135.157 1.00 42.00 C ANISOU 908 CA GLY A 117 7421 3972 4564 141 -342 634 C ATOM 909 C GLY A 117 45.914 28.645 134.633 1.00 41.68 C ANISOU 909 C GLY A 117 7249 4057 4529 264 -349 603 C ATOM 910 O GLY A 117 46.025 27.523 134.158 1.00 40.89 O ANISOU 910 O GLY A 117 7000 4108 4428 212 -293 560 O ATOM 911 N ILE A 118 44.746 29.269 134.737 1.00 42.44 N ANISOU 911 N ILE A 118 7407 4089 4629 434 -424 622 N ATOM 912 CA ILE A 118 43.518 28.643 134.280 1.00 42.36 C ANISOU 912 CA ILE A 118 7275 4202 4620 559 -443 598 C ATOM 913 C ILE A 118 43.354 28.857 132.778 1.00 43.36 C ANISOU 913 C ILE A 118 7445 4384 4647 517 -493 679 C ATOM 914 O ILE A 118 43.898 29.792 132.183 1.00 44.44 O ANISOU 914 O ILE A 118 7745 4427 4714 440 -537 769 O ATOM 915 CB ILE A 118 42.299 29.176 135.051 1.00 42.87 C ANISOU 915 CB ILE A 118 7359 4203 4725 773 -499 578 C ATOM 916 CG1 ILE A 118 42.259 30.702 135.010 1.00 44.42 C ANISOU 916 CG1 ILE A 118 7784 4210 4884 835 -589 657 C ATOM 917 CG2 ILE A 118 42.297 28.657 136.484 1.00 41.76 C ANISOU 917 CG2 ILE A 118 7125 4065 4676 817 -437 484 C ATOM 918 CD1 ILE A 118 40.958 31.283 135.510 1.00 45.28 C ANISOU 918 CD1 ILE A 118 7917 4272 5015 1072 -656 643 C ATOM 919 N SER A 119 42.599 27.960 132.156 1.00 43.93 N ANISOU 919 N SER A 119 7373 4613 4706 557 -488 647 N ATOM 920 CA SER A 119 42.261 28.112 130.753 1.00 48.49 C ANISOU 920 CA SER A 119 7978 5261 5184 538 -543 717 C ATOM 921 C SER A 119 40.796 27.839 130.459 1.00 51.46 C ANISOU 921 C SER A 119 8260 5735 5557 698 -600 703 C ATOM 922 O SER A 119 40.405 27.915 129.296 1.00 56.24 O ANISOU 922 O SER A 119 8876 6415 6077 694 -653 758 O ATOM 923 CB SER A 119 43.130 27.194 129.882 1.00 45.11 C ANISOU 923 CB SER A 119 7468 4966 4706 361 -475 698 C ATOM 924 OG SER A 119 42.853 25.837 130.155 1.00 42.46 O ANISOU 924 OG SER A 119 6945 4761 4429 368 -411 593 O ATOM 925 N TYR A 120 39.977 27.538 131.460 1.00 61.31 N ANISOU 925 N TYR A 120 9411 6997 6887 834 -592 634 N ATOM 926 CA TYR A 120 38.563 27.280 131.228 1.00 65.91 C ANISOU 926 CA TYR A 120 9886 7693 7463 982 -645 620 C ATOM 927 C TYR A 120 37.829 28.572 130.882 1.00 69.37 C ANISOU 927 C TYR A 120 10463 8044 7851 1135 -758 708 C ATOM 928 O TYR A 120 36.716 28.544 130.350 1.00 70.21 O ANISOU 928 O TYR A 120 10502 8253 7922 1251 -823 724 O ATOM 929 CB TYR A 120 37.924 26.616 132.448 1.00 69.34 C ANISOU 929 CB TYR A 120 10175 8179 7994 1074 -600 526 C ATOM 930 CG TYR A 120 37.796 27.514 133.657 1.00 72.16 C ANISOU 930 CG TYR A 120 10621 8393 8405 1202 -613 520 C ATOM 931 CD1 TYR A 120 38.841 27.653 134.560 1.00 71.93 C ANISOU 931 CD1 TYR A 120 10659 8245 8425 1122 -554 494 C ATOM 932 CD2 TYR A 120 36.621 28.212 133.904 1.00 74.24 C ANISOU 932 CD2 TYR A 120 10894 8648 8665 1408 -687 533 C ATOM 933 CE1 TYR A 120 38.722 28.474 135.668 1.00 72.69 C ANISOU 933 CE1 TYR A 120 10843 8211 8563 1235 -569 480 C ATOM 934 CE2 TYR A 120 36.495 29.032 135.012 1.00 74.71 C ANISOU 934 CE2 TYR A 120 11040 8577 8768 1535 -698 515 C ATOM 935 CZ TYR A 120 37.545 29.158 135.888 1.00 74.29 C ANISOU 935 CZ TYR A 120 11064 8401 8761 1444 -639 487 C ATOM 936 OH TYR A 120 37.415 29.974 136.987 1.00 76.00 O ANISOU 936 OH TYR A 120 11373 8490 9015 1568 -652 462 O ATOM 937 N LYS A 149 49.911 44.838 131.380 1.00 66.89 N ANISOU 937 N LYS A 149 13590 4813 7012 -631 -1409 1902 N ATOM 938 CA LYS A 149 50.677 44.265 132.485 1.00 64.78 C ANISOU 938 CA LYS A 149 13229 4580 6805 -731 -1322 1802 C ATOM 939 C LYS A 149 50.648 42.744 132.454 1.00 60.76 C ANISOU 939 C LYS A 149 12377 4380 6329 -702 -1194 1708 C ATOM 940 O LYS A 149 49.601 42.129 132.629 1.00 60.53 O ANISOU 940 O LYS A 149 12204 4435 6359 -455 -1181 1626 O ATOM 941 CB LYS A 149 50.149 44.771 133.827 1.00 66.19 C ANISOU 941 CB LYS A 149 13472 4589 7088 -527 -1357 1672 C ATOM 942 CG LYS A 149 51.122 45.676 134.564 1.00 67.30 C ANISOU 942 CG LYS A 149 13733 4600 7239 -709 -1370 1640 C ATOM 943 CD LYS A 149 50.429 46.468 135.667 1.00 68.49 C ANISOU 943 CD LYS A 149 13995 4561 7466 -485 -1432 1529 C ATOM 944 CE LYS A 149 51.381 47.482 136.293 1.00 70.81 C ANISOU 944 CE LYS A 149 14436 4717 7750 -674 -1462 1509 C ATOM 945 NZ LYS A 149 50.678 48.651 136.899 1.00 73.59 N ANISOU 945 NZ LYS A 149 14970 4856 8136 -481 -1556 1449 N ATOM 946 N THR A 150 51.807 42.141 132.221 1.00 60.93 N ANISOU 946 N THR A 150 12255 4583 6313 -955 -1098 1713 N ATOM 947 CA THR A 150 51.890 40.695 132.173 1.00 59.61 C ANISOU 947 CA THR A 150 11763 4707 6178 -939 -974 1616 C ATOM 948 C THR A 150 51.731 40.118 133.577 1.00 59.69 C ANISOU 948 C THR A 150 11638 4730 6310 -808 -918 1458 C ATOM 949 O THR A 150 52.004 40.801 134.567 1.00 61.71 O ANISOU 949 O THR A 150 12035 4805 6607 -821 -952 1427 O ATOM 950 CB THR A 150 53.224 40.250 131.589 1.00 59.46 C ANISOU 950 CB THR A 150 11633 4877 6083 -1234 -887 1659 C ATOM 951 OG1 THR A 150 54.264 40.451 132.555 1.00 58.75 O ANISOU 951 OG1 THR A 150 11559 4737 6025 -1395 -854 1617 O ATOM 952 CG2 THR A 150 53.540 41.035 130.335 1.00 61.21 C ANISOU 952 CG2 THR A 150 12030 5057 6172 -1406 -948 1829 C ATOM 953 N PRO A 151 51.280 38.864 133.689 1.00 60.16 N ANISOU 953 N PRO A 151 11435 4999 6425 -684 -835 1358 N ATOM 954 CA PRO A 151 51.195 38.231 135.018 1.00 56.94 C ANISOU 954 CA PRO A 151 10888 4623 6125 -580 -775 1215 C ATOM 955 C PRO A 151 52.442 38.412 135.866 1.00 57.05 C ANISOU 955 C PRO A 151 10924 4601 6153 -776 -737 1187 C ATOM 956 O PRO A 151 52.328 38.742 137.047 1.00 55.65 O ANISOU 956 O PRO A 151 10808 4295 6041 -697 -755 1115 O ATOM 957 CB PRO A 151 50.945 36.760 134.670 1.00 56.59 C ANISOU 957 CB PRO A 151 10552 4843 6104 -527 -680 1146 C ATOM 958 CG PRO A 151 50.188 36.824 133.390 1.00 58.25 C ANISOU 958 CG PRO A 151 10787 5098 6246 -461 -728 1227 C ATOM 959 CD PRO A 151 50.736 37.994 132.631 1.00 59.89 C ANISOU 959 CD PRO A 151 11233 5169 6355 -624 -802 1370 C ATOM 960 N GLY A 152 53.629 38.240 135.283 1.00 52.36 N ANISOU 960 N GLY A 152 10280 4124 5492 -1030 -687 1244 N ATOM 961 CA GLY A 152 54.856 38.414 136.044 1.00 52.42 C ANISOU 961 CA GLY A 152 10294 4119 5504 -1229 -654 1222 C ATOM 962 C GLY A 152 54.974 39.786 136.678 1.00 54.10 C ANISOU 962 C GLY A 152 10790 4052 5712 -1272 -752 1259 C ATOM 963 O GLY A 152 55.392 39.910 137.831 1.00 53.82 O ANISOU 963 O GLY A 152 10768 3954 5728 -1297 -744 1185 O ATOM 964 N GLN A 153 54.600 40.833 135.940 1.00 55.96 N ANISOU 964 N GLN A 153 11266 4112 5885 -1279 -852 1374 N ATOM 965 CA GLN A 153 54.668 42.185 136.483 1.00 57.81 C ANISOU 965 CA GLN A 153 11801 4052 6112 -1314 -957 1411 C ATOM 966 C GLN A 153 53.643 42.395 137.584 1.00 57.48 C ANISOU 966 C GLN A 153 11822 3854 6164 -1035 -999 1302 C ATOM 967 O GLN A 153 53.886 43.164 138.520 1.00 58.35 O ANISOU 967 O GLN A 153 12103 3769 6297 -1058 -1049 1266 O ATOM 968 CB GLN A 153 54.473 43.219 135.376 1.00 60.01 C ANISOU 968 CB GLN A 153 12329 4173 6298 -1378 -1059 1568 C ATOM 969 CG GLN A 153 55.547 43.214 134.310 1.00 60.78 C ANISOU 969 CG GLN A 153 12404 4404 6284 -1682 -1026 1690 C ATOM 970 CD GLN A 153 55.201 44.117 133.130 1.00 62.88 C ANISOU 970 CD GLN A 153 12852 4575 6463 -1703 -1117 1827 C ATOM 971 OE1 GLN A 153 55.958 45.028 132.783 1.00 64.81 O ANISOU 971 OE1 GLN A 153 13200 4777 6647 -1906 -1155 1892 O ATOM 972 NE2 GLN A 153 54.052 43.867 132.512 1.00 62.61 N ANISOU 972 NE2 GLN A 153 12823 4538 6426 -1484 -1151 1856 N ATOM 973 N ILE A 154 52.479 41.753 137.472 1.00 56.40 N ANISOU 973 N ILE A 154 11553 3803 6074 -774 -983 1248 N ATOM 974 CA ILE A 154 51.500 41.823 138.549 1.00 56.00 C ANISOU 974 CA ILE A 154 11518 3653 6108 -505 -1006 1134 C ATOM 975 C ILE A 154 52.004 41.057 139.754 1.00 54.96 C ANISOU 975 C ILE A 154 11206 3634 6043 -531 -917 1007 C ATOM 976 O ILE A 154 51.861 41.498 140.899 1.00 55.55 O ANISOU 976 O ILE A 154 11373 3570 6163 -446 -943 926 O ATOM 977 CB ILE A 154 50.135 41.294 138.079 1.00 55.38 C ANISOU 977 CB ILE A 154 11322 3666 6053 -237 -1010 1115 C ATOM 978 CG1 ILE A 154 49.596 42.162 136.936 1.00 57.30 C ANISOU 978 CG1 ILE A 154 11767 3780 6226 -194 -1115 1246 C ATOM 979 CG2 ILE A 154 49.151 41.256 139.235 1.00 54.91 C ANISOU 979 CG2 ILE A 154 11239 3549 6076 35 -1018 990 C ATOM 980 CD1 ILE A 154 49.152 41.378 135.728 1.00 57.78 C ANISOU 980 CD1 ILE A 154 11657 4050 6246 -166 -1085 1298 C ATOM 981 N GLN A 155 52.613 39.899 139.513 1.00 52.72 N ANISOU 981 N GLN A 155 10666 3603 5763 -646 -812 988 N ATOM 982 CA GLN A 155 53.144 39.108 140.610 1.00 51.19 C ANISOU 982 CA GLN A 155 10295 3527 5630 -675 -729 878 C ATOM 983 C GLN A 155 54.295 39.838 141.286 1.00 52.14 C ANISOU 983 C GLN A 155 10551 3532 5728 -888 -751 884 C ATOM 984 O GLN A 155 54.278 40.043 142.502 1.00 52.03 O ANISOU 984 O GLN A 155 10578 3431 5761 -828 -760 795 O ATOM 985 CB GLN A 155 53.563 37.733 140.091 1.00 49.50 C ANISOU 985 CB GLN A 155 9794 3596 5418 -746 -621 863 C ATOM 986 CG GLN A 155 52.369 36.911 139.592 1.00 48.48 C ANISOU 986 CG GLN A 155 9517 3585 5319 -531 -598 836 C ATOM 987 CD GLN A 155 52.759 35.636 138.867 1.00 47.15 C ANISOU 987 CD GLN A 155 9103 3672 5140 -608 -505 831 C ATOM 988 OE1 GLN A 155 53.695 35.613 138.076 1.00 47.56 O ANISOU 988 OE1 GLN A 155 9141 3804 5126 -810 -481 899 O ATOM 989 NE2 GLN A 155 52.037 34.568 139.142 1.00 45.67 N ANISOU 989 NE2 GLN A 155 8722 3614 5014 -449 -452 749 N ATOM 990 N LEU A 156 55.275 40.299 140.506 1.00 53.26 N ANISOU 990 N LEU A 156 10776 3669 5791 -1143 -766 990 N ATOM 991 CA LEU A 156 56.416 40.995 141.091 1.00 54.32 C ANISOU 991 CA LEU A 156 11033 3709 5896 -1375 -790 1003 C ATOM 992 C LEU A 156 55.980 42.199 141.916 1.00 55.81 C ANISOU 992 C LEU A 156 11505 3598 6101 -1290 -894 976 C ATOM 993 O LEU A 156 56.515 42.441 143.007 1.00 55.94 O ANISOU 993 O LEU A 156 11562 3553 6140 -1357 -898 906 O ATOM 994 CB LEU A 156 57.386 41.431 140.001 1.00 55.65 C ANISOU 994 CB LEU A 156 11271 3908 5965 -1659 -802 1138 C ATOM 995 CG LEU A 156 58.640 42.124 140.529 1.00 56.89 C ANISOU 995 CG LEU A 156 11539 3994 6082 -1935 -826 1161 C ATOM 996 CD1 LEU A 156 59.263 41.365 141.720 1.00 55.45 C ANISOU 996 CD1 LEU A 156 11158 3953 5958 -1957 -752 1041 C ATOM 997 CD2 LEU A 156 59.649 42.308 139.408 1.00 57.99 C ANISOU 997 CD2 LEU A 156 11678 4240 6117 -2227 -812 1292 C ATOM 998 N GLU A 157 55.016 42.971 141.414 1.00 59.35 N ANISOU 998 N GLU A 157 12155 3859 6537 -1137 -982 1027 N ATOM 999 CA GLU A 157 54.534 44.111 142.184 1.00 61.70 C ANISOU 999 CA GLU A 157 12692 3898 6852 -1016 -1077 980 C ATOM 1000 C GLU A 157 53.933 43.679 143.516 1.00 58.96 C ANISOU 1000 C GLU A 157 12283 3533 6586 -802 -1049 834 C ATOM 1001 O GLU A 157 54.030 44.413 144.499 1.00 59.52 O ANISOU 1001 O GLU A 157 12453 3493 6669 -777 -1088 753 O ATOM 1002 CB GLU A 157 53.532 44.912 141.363 1.00 60.88 C ANISOU 1002 CB GLU A 157 12729 3678 6725 -845 -1162 1040 C ATOM 1003 CG GLU A 157 54.211 45.816 140.357 1.00 78.13 C ANISOU 1003 CG GLU A 157 15045 5816 8824 -1067 -1218 1166 C ATOM 1004 CD GLU A 157 53.228 46.434 139.371 1.00 75.95 C ANISOU 1004 CD GLU A 157 14885 5452 8520 -907 -1297 1242 C ATOM 1005 OE1 GLU A 157 52.001 46.291 139.560 1.00 73.74 O ANISOU 1005 OE1 GLU A 157 14593 5135 8289 -612 -1316 1188 O ATOM 1006 OE2 GLU A 157 53.688 47.063 138.401 1.00 76.27 O ANISOU 1006 OE2 GLU A 157 15023 5471 8486 -1077 -1339 1357 O ATOM 1007 N ARG A 158 53.324 42.496 143.576 1.00 55.41 N ANISOU 1007 N ARG A 158 11563 3302 6187 -635 -964 770 N ATOM 1008 CA ARG A 158 52.845 41.987 144.855 1.00 54.23 C ANISOU 1008 CA ARG A 158 11296 3201 6107 -455 -920 628 C ATOM 1009 C ARG A 158 54.003 41.554 145.734 1.00 53.42 C ANISOU 1009 C ARG A 158 11083 3199 6013 -648 -860 573 C ATOM 1010 O ARG A 158 53.949 41.681 146.962 1.00 53.35 O ANISOU 1010 O ARG A 158 11102 3133 6035 -579 -861 470 O ATOM 1011 CB ARG A 158 51.919 40.806 144.632 1.00 52.42 C ANISOU 1011 CB ARG A 158 10807 3187 5925 -254 -846 587 C ATOM 1012 CG ARG A 158 50.564 41.171 144.137 1.00 53.14 C ANISOU 1012 CG ARG A 158 10977 3194 6020 0 -905 603 C ATOM 1013 CD ARG A 158 50.038 40.039 143.343 1.00 51.65 C ANISOU 1013 CD ARG A 158 10542 3239 5845 71 -839 621 C ATOM 1014 NE ARG A 158 48.655 40.220 142.948 1.00 52.16 N ANISOU 1014 NE ARG A 158 10631 3271 5918 331 -887 625 N ATOM 1015 CZ ARG A 158 47.834 39.213 142.667 1.00 50.87 C ANISOU 1015 CZ ARG A 158 10241 3303 5783 472 -834 596 C ATOM 1016 NH1 ARG A 158 48.260 37.941 142.732 1.00 48.98 N ANISOU 1016 NH1 ARG A 158 9748 3291 5571 380 -731 560 N ATOM 1017 NH2 ARG A 158 46.570 39.464 142.317 1.00 51.56 N ANISOU 1017 NH2 ARG A 158 10355 3364 5871 708 -886 601 N ATOM 1018 N TYR A 159 55.034 40.990 145.114 1.00 52.81 N ANISOU 1018 N TYR A 159 10867 3293 5906 -879 -803 636 N ATOM 1019 CA TYR A 159 56.246 40.649 145.836 1.00 52.31 C ANISOU 1019 CA TYR A 159 10703 3333 5841 -1082 -755 599 C ATOM 1020 C TYR A 159 56.851 41.879 146.491 1.00 54.17 C ANISOU 1020 C TYR A 159 11199 3343 6042 -1226 -839 598 C ATOM 1021 O TYR A 159 57.279 41.831 147.645 1.00 53.95 O ANISOU 1021 O TYR A 159 11148 3317 6032 -1258 -828 511 O ATOM 1022 CB TYR A 159 57.230 40.015 144.863 1.00 51.82 C ANISOU 1022 CB TYR A 159 10476 3478 5737 -1304 -693 682 C ATOM 1023 CG TYR A 159 58.250 39.130 145.488 1.00 50.64 C ANISOU 1023 CG TYR A 159 10103 3534 5603 -1434 -611 630 C ATOM 1024 CD1 TYR A 159 58.327 38.994 146.861 1.00 50.14 C ANISOU 1024 CD1 TYR A 159 10010 3457 5583 -1378 -603 525 C ATOM 1025 CD2 TYR A 159 59.148 38.430 144.705 1.00 50.14 C ANISOU 1025 CD2 TYR A 159 9858 3688 5505 -1607 -544 684 C ATOM 1026 CE1 TYR A 159 59.270 38.189 147.436 1.00 49.16 C ANISOU 1026 CE1 TYR A 159 9685 3524 5471 -1490 -536 484 C ATOM 1027 CE2 TYR A 159 60.096 37.620 145.276 1.00 49.20 C ANISOU 1027 CE2 TYR A 159 9532 3760 5400 -1711 -474 636 C ATOM 1028 CZ TYR A 159 60.155 37.507 146.643 1.00 48.71 C ANISOU 1028 CZ TYR A 159 9449 3675 5385 -1652 -473 540 C ATOM 1029 OH TYR A 159 61.102 36.698 147.217 1.00 47.87 O ANISOU 1029 OH TYR A 159 9137 3762 5290 -1748 -411 498 O ATOM 1030 N GLN A 160 56.888 42.994 145.770 1.00 56.13 N ANISOU 1030 N GLN A 160 11704 3389 6234 -1317 -929 694 N ATOM 1031 CA GLN A 160 57.567 44.174 146.272 1.00 58.12 C ANISOU 1031 CA GLN A 160 12157 3479 6444 -1475 -1005 693 C ATOM 1032 C GLN A 160 56.726 44.905 147.306 1.00 58.96 C ANISOU 1032 C GLN A 160 12397 3420 6584 -1244 -1063 581 C ATOM 1033 O GLN A 160 57.228 45.271 148.373 1.00 59.49 O ANISOU 1033 O GLN A 160 12508 3447 6649 -1308 -1078 503 O ATOM 1034 CB GLN A 160 57.918 45.100 145.113 1.00 60.07 C ANISOU 1034 CB GLN A 160 12536 3673 6617 -1631 -1066 820 C ATOM 1035 CG GLN A 160 58.793 44.458 144.067 1.00 59.51 C ANISOU 1035 CG GLN A 160 12330 3785 6497 -1871 -1006 930 C ATOM 1036 CD GLN A 160 58.805 45.243 142.780 1.00 61.28 C ANISOU 1036 CD GLN A 160 12673 3962 6648 -1958 -1061 1057 C ATOM 1037 OE1 GLN A 160 57.822 45.891 142.430 1.00 62.26 O ANISOU 1037 OE1 GLN A 160 12939 3939 6776 -1770 -1129 1072 O ATOM 1038 NE2 GLN A 160 59.924 45.202 142.072 1.00 61.83 N ANISOU 1038 NE2 GLN A 160 12679 4167 6645 -2245 -1033 1149 N ATOM 1039 N THR A 161 55.445 45.119 147.024 1.00 59.18 N ANISOU 1039 N THR A 161 12483 3364 6637 -971 -1094 569 N ATOM 1040 CA THR A 161 54.659 45.995 147.881 1.00 60.47 C ANISOU 1040 CA THR A 161 12788 3372 6816 -759 -1155 473 C ATOM 1041 C THR A 161 54.001 45.272 149.051 1.00 58.96 C ANISOU 1041 C THR A 161 12482 3234 6686 -542 -1102 336 C ATOM 1042 O THR A 161 53.632 45.932 150.028 1.00 59.99 O ANISOU 1042 O THR A 161 12708 3264 6820 -416 -1139 238 O ATOM 1043 CB THR A 161 53.594 46.738 147.062 1.00 61.88 C ANISOU 1043 CB THR A 161 13093 3434 6984 -565 -1225 522 C ATOM 1044 OG1 THR A 161 52.511 45.857 146.771 1.00 60.32 O ANISOU 1044 OG1 THR A 161 12759 3325 6833 -325 -1181 507 O ATOM 1045 CG2 THR A 161 54.182 47.251 145.753 1.00 63.14 C ANISOU 1045 CG2 THR A 161 13339 3570 7081 -775 -1267 670 C ATOM 1046 N TYR A 162 53.847 43.945 148.988 1.00 56.68 N ANISOU 1046 N TYR A 162 11995 3102 6439 -498 -1017 327 N ATOM 1047 CA TYR A 162 53.286 43.165 150.087 1.00 55.23 C ANISOU 1047 CA TYR A 162 11681 2995 6307 -311 -958 202 C ATOM 1048 C TYR A 162 54.151 41.999 150.534 1.00 53.34 C ANISOU 1048 C TYR A 162 11167 3014 6087 -458 -858 175 C ATOM 1049 O TYR A 162 53.721 41.249 151.412 1.00 52.08 O ANISOU 1049 O TYR A 162 10840 2981 5966 -314 -797 79 O ATOM 1050 CB TYR A 162 51.899 42.602 149.721 1.00 54.35 C ANISOU 1050 CB TYR A 162 11440 2975 6235 -18 -928 185 C ATOM 1051 CG TYR A 162 51.055 43.525 148.886 1.00 56.00 C ANISOU 1051 CG TYR A 162 11828 3025 6424 123 -1014 244 C ATOM 1052 CD1 TYR A 162 50.689 44.761 149.357 1.00 58.07 C ANISOU 1052 CD1 TYR A 162 12261 3137 6665 222 -1089 196 C ATOM 1053 CD2 TYR A 162 50.636 43.162 147.614 1.00 55.60 C ANISOU 1053 CD2 TYR A 162 11728 3029 6370 155 -1013 345 C ATOM 1054 CE1 TYR A 162 49.927 45.624 148.596 1.00 59.93 C ANISOU 1054 CE1 TYR A 162 12621 3270 6881 353 -1163 248 C ATOM 1055 CE2 TYR A 162 49.860 44.027 146.842 1.00 57.25 C ANISOU 1055 CE2 TYR A 162 12063 3134 6554 286 -1091 400 C ATOM 1056 CZ TYR A 162 49.509 45.258 147.339 1.00 59.33 C ANISOU 1056 CZ TYR A 162 12495 3246 6801 386 -1166 351 C ATOM 1057 OH TYR A 162 48.742 46.141 146.601 1.00 61.31 O ANISOU 1057 OH TYR A 162 12873 3394 7029 520 -1246 403 O ATOM 1058 N GLY A 163 55.324 41.797 149.945 1.00 53.20 N ANISOU 1058 N GLY A 163 11089 3086 6038 -731 -838 258 N ATOM 1059 CA GLY A 163 56.218 40.750 150.389 1.00 51.66 C ANISOU 1059 CA GLY A 163 10644 3127 5857 -866 -751 232 C ATOM 1060 C GLY A 163 55.806 39.323 150.092 1.00 49.52 C ANISOU 1060 C GLY A 163 10073 3110 5634 -751 -651 222 C ATOM 1061 O GLY A 163 56.538 38.406 150.467 1.00 48.30 O ANISOU 1061 O GLY A 163 9711 3146 5494 -847 -581 200 O ATOM 1062 N GLN A 164 54.696 39.101 149.427 1.00 49.13 N ANISOU 1062 N GLN A 164 9990 3069 5607 -552 -646 239 N ATOM 1063 CA GLN A 164 54.311 37.745 149.110 1.00 47.21 C ANISOU 1063 CA GLN A 164 9471 3061 5408 -460 -556 230 C ATOM 1064 C GLN A 164 53.464 37.627 147.859 1.00 47.30 C ANISOU 1064 C GLN A 164 9484 3077 5412 -365 -569 302 C ATOM 1065 O GLN A 164 52.738 38.520 147.559 1.00 48.72 O ANISOU 1065 O GLN A 164 9871 3073 5568 -285 -648 337 O ATOM 1066 CB GLN A 164 53.578 37.162 150.286 1.00 46.18 C ANISOU 1066 CB GLN A 164 9221 2997 5328 -250 -514 120 C ATOM 1067 CG GLN A 164 52.322 37.892 150.608 1.00 47.27 C ANISOU 1067 CG GLN A 164 9534 2960 5468 -29 -575 68 C ATOM 1068 CD GLN A 164 51.555 37.206 151.673 1.00 46.23 C ANISOU 1068 CD GLN A 164 9247 2939 5378 188 -522 -26 C ATOM 1069 OE1 GLN A 164 51.498 35.994 151.715 1.00 44.63 O ANISOU 1069 OE1 GLN A 164 8808 2939 5211 206 -445 -30 O ATOM 1070 NE2 GLN A 164 50.968 37.964 152.544 1.00 47.23 N ANISOU 1070 NE2 GLN A 164 9510 2935 5499 354 -563 -104 N ATOM 1071 N LEU A 165 53.549 36.512 147.138 1.00 45.84 N ANISOU 1071 N LEU A 165 9066 3103 5246 -367 -494 321 N ATOM 1072 CA LEU A 165 52.758 36.291 145.926 1.00 45.70 C ANISOU 1072 CA LEU A 165 9005 3140 5219 -293 -494 384 C ATOM 1073 C LEU A 165 51.852 35.108 145.929 1.00 44.17 C ANISOU 1073 C LEU A 165 8595 3107 5081 -105 -432 324 C ATOM 1074 O LEU A 165 50.800 35.148 145.388 1.00 44.36 O ANISOU 1074 O LEU A 165 8632 3112 5112 76 -458 328 O ATOM 1075 CB LEU A 165 53.659 36.033 144.743 1.00 45.52 C ANISOU 1075 CB LEU A 165 8900 3241 5154 -505 -459 467 C ATOM 1076 CG LEU A 165 55.108 35.957 145.050 1.00 46.56 C ANISOU 1076 CG LEU A 165 9142 3314 5234 -760 -481 517 C ATOM 1077 CD1 LEU A 165 55.751 34.812 144.347 1.00 46.09 C ANISOU 1077 CD1 LEU A 165 8928 3445 5138 -948 -420 574 C ATOM 1078 CD2 LEU A 165 55.661 37.246 144.544 1.00 52.60 C ANISOU 1078 CD2 LEU A 165 10177 3858 5951 -767 -580 590 C ATOM 1079 N ARG A 166 52.292 34.039 146.544 1.00 42.75 N ANISOU 1079 N ARG A 166 8214 3093 4936 -156 -352 275 N ATOM 1080 CA ARG A 166 51.578 32.792 146.539 1.00 41.29 C ANISOU 1080 CA ARG A 166 7807 3087 4796 -48 -286 243 C ATOM 1081 C ARG A 166 50.302 32.671 147.298 1.00 41.11 C ANISOU 1081 C ARG A 166 7766 3044 4811 186 -292 174 C ATOM 1082 O ARG A 166 50.083 33.339 148.252 1.00 41.84 O ANISOU 1082 O ARG A 166 7981 3013 4904 262 -329 128 O ATOM 1083 CB ARG A 166 52.517 31.684 146.956 1.00 40.03 C ANISOU 1083 CB ARG A 166 7459 3087 4664 -160 -207 209 C ATOM 1084 CG ARG A 166 53.874 31.725 146.313 1.00 40.36 C ANISOU 1084 CG ARG A 166 7503 3169 4662 -391 -196 267 C ATOM 1085 CD ARG A 166 53.861 31.269 144.876 1.00 40.32 C ANISOU 1085 CD ARG A 166 7440 3255 4624 -444 -179 332 C ATOM 1086 NE ARG A 166 53.074 30.080 144.671 1.00 39.19 N ANISOU 1086 NE ARG A 166 7136 3233 4523 -302 -136 299 N ATOM 1087 CZ ARG A 166 53.570 28.862 144.665 1.00 37.99 C ANISOU 1087 CZ ARG A 166 6787 3243 4406 -319 -63 261 C ATOM 1088 NH1 ARG A 166 52.780 27.840 144.479 1.00 37.15 N ANISOU 1088 NH1 ARG A 166 6555 3227 4333 -199 -33 233 N ATOM 1089 NH2 ARG A 166 54.842 28.664 144.846 1.00 37.75 N ANISOU 1089 NH2 ARG A 166 6686 3282 4374 -456 -25 250 N ATOM 1090 N GLY A 167 49.467 31.773 146.825 1.00 40.27 N ANISOU 1090 N GLY A 167 7504 3066 4731 298 -257 166 N ATOM 1091 CA GLY A 167 48.191 31.430 147.399 1.00 39.89 C ANISOU 1091 CA GLY A 167 7377 3061 4720 496 -242 97 C ATOM 1092 C GLY A 167 47.207 32.537 147.484 1.00 41.24 C ANISOU 1092 C GLY A 167 7705 3092 4872 675 -314 88 C ATOM 1093 O GLY A 167 47.123 33.306 146.591 1.00 42.32 O ANISOU 1093 O GLY A 167 7978 3129 4973 689 -378 149 O ATOM 1094 N ASP A 168 46.449 32.595 148.558 1.00 44.82 N ANISOU 1094 N ASP A 168 8143 3541 5346 815 -304 10 N ATOM 1095 CA ASP A 168 45.514 33.654 148.732 1.00 49.00 C ANISOU 1095 CA ASP A 168 8747 4005 5867 1042 -351 -23 C ATOM 1096 C ASP A 168 45.836 34.254 150.047 1.00 53.87 C ANISOU 1096 C ASP A 168 9501 4494 6474 1096 -372 -96 C ATOM 1097 O ASP A 168 46.023 33.555 150.995 1.00 62.42 O ANISOU 1097 O ASP A 168 10476 5665 7576 1138 -319 -168 O ATOM 1098 CB ASP A 168 44.078 33.184 148.678 1.00 50.68 C ANISOU 1098 CB ASP A 168 8740 4407 6109 1175 -300 -56 C ATOM 1099 CG ASP A 168 43.836 32.006 149.470 1.00 52.56 C ANISOU 1099 CG ASP A 168 8998 4632 6340 1417 -325 -114 C ATOM 1100 OD1 ASP A 168 44.741 31.200 149.550 1.00 48.25 O ANISOU 1100 OD1 ASP A 168 8277 4241 5816 1503 -270 -165 O ATOM 1101 OD2 ASP A 168 42.744 31.872 150.009 1.00 58.53 O ANISOU 1101 OD2 ASP A 168 9941 5229 7067 1525 -400 -110 O ATOM 1102 N PHE A 169 45.913 35.564 150.091 1.00 56.36 N ANISOU 1102 N PHE A 169 10061 4598 6756 1086 -452 -77 N ATOM 1103 CA PHE A 169 46.226 36.260 151.306 1.00 53.57 C ANISOU 1103 CA PHE A 169 9867 4100 6385 1096 -480 -145 C ATOM 1104 C PHE A 169 45.572 37.610 151.387 1.00 54.94 C ANISOU 1104 C PHE A 169 10271 4072 6531 1275 -570 -162 C ATOM 1105 O PHE A 169 45.048 38.100 150.414 1.00 58.74 O ANISOU 1105 O PHE A 169 10807 4509 7002 1366 -620 -103 O ATOM 1106 CB PHE A 169 47.692 36.454 151.376 1.00 51.58 C ANISOU 1106 CB PHE A 169 9711 3769 6117 838 -489 -111 C ATOM 1107 CG PHE A 169 48.259 37.090 150.183 1.00 49.75 C ANISOU 1107 CG PHE A 169 9623 3424 5856 702 -548 -6 C ATOM 1108 CD1 PHE A 169 48.676 36.343 149.141 1.00 48.68 C ANISOU 1108 CD1 PHE A 169 9353 3419 5724 571 -511 73 C ATOM 1109 CD2 PHE A 169 48.416 38.429 150.127 1.00 50.24 C ANISOU 1109 CD2 PHE A 169 9961 3246 5881 694 -640 13 C ATOM 1110 CE1 PHE A 169 49.243 36.920 148.046 1.00 47.74 C ANISOU 1110 CE1 PHE A 169 9363 3211 5566 435 -561 173 C ATOM 1111 CE2 PHE A 169 48.980 39.023 149.035 1.00 49.39 C ANISOU 1111 CE2 PHE A 169 9991 3035 5739 550 -695 120 C ATOM 1112 CZ PHE A 169 49.390 38.265 147.986 1.00 48.18 C ANISOU 1112 CZ PHE A 169 9690 3032 5583 419 -653 202 C ATOM 1113 N THR A 170 45.602 38.226 152.554 1.00 50.83 N ANISOU 1113 N THR A 170 9895 3425 5994 1327 -595 -246 N ATOM 1114 CA THR A 170 44.986 39.520 152.707 1.00 52.47 C ANISOU 1114 CA THR A 170 10339 3424 6175 1513 -682 -284 C ATOM 1115 C THR A 170 45.926 40.681 152.460 1.00 52.09 C ANISOU 1115 C THR A 170 10576 3120 6094 1347 -766 -242 C ATOM 1116 O THR A 170 47.109 40.588 152.679 1.00 51.54 O ANISOU 1116 O THR A 170 10515 3047 6019 1106 -747 -225 O ATOM 1117 CB THR A 170 44.384 39.692 154.092 1.00 51.10 C ANISOU 1117 CB THR A 170 10149 3273 5995 1698 -656 -418 C ATOM 1118 OG1 THR A 170 43.482 38.629 154.360 1.00 49.71 O ANISOU 1118 OG1 THR A 170 9688 3356 5843 1802 -567 -449 O ATOM 1119 CG2 THR A 170 43.632 40.993 154.167 1.00 53.32 C ANISOU 1119 CG2 THR A 170 10643 3367 6249 1949 -739 -470 C ATOM 1120 N VAL A 171 45.376 41.777 151.971 1.00 54.04 N ANISOU 1120 N VAL A 171 11058 3155 6319 1478 -863 -223 N ATOM 1121 CA VAL A 171 46.164 42.982 151.750 1.00 56.28 C ANISOU 1121 CA VAL A 171 11577 3241 6567 1316 -945 -177 C ATOM 1122 C VAL A 171 45.319 44.183 152.168 1.00 61.50 C ANISOU 1122 C VAL A 171 12366 3798 7205 1521 -1011 -240 C ATOM 1123 O VAL A 171 44.088 44.146 152.101 1.00 62.46 O ANISOU 1123 O VAL A 171 12410 3987 7334 1778 -1011 -273 O ATOM 1124 CB VAL A 171 46.630 43.067 150.271 1.00 55.84 C ANISOU 1124 CB VAL A 171 11581 3138 6498 1154 -984 -27 C ATOM 1125 CG1 VAL A 171 46.857 44.499 149.819 1.00 58.21 C ANISOU 1125 CG1 VAL A 171 12112 3251 6755 1090 -1085 27 C ATOM 1126 CG2 VAL A 171 47.906 42.254 150.072 1.00 54.89 C ANISOU 1126 CG2 VAL A 171 11369 3105 6381 863 -926 27 C ATOM 1127 N GLU A 172 45.984 45.236 152.651 1.00 71.36 N ANISOU 1127 N GLU A 172 13804 4889 8421 1407 -1066 -262 N ATOM 1128 CA GLU A 172 45.293 46.453 153.061 1.00 78.00 C ANISOU 1128 CA GLU A 172 14795 5606 9236 1585 -1135 -323 C ATOM 1129 C GLU A 172 45.005 47.341 151.861 1.00 81.39 C ANISOU 1129 C GLU A 172 15372 5907 9645 1606 -1224 -220 C ATOM 1130 O GLU A 172 45.853 47.516 150.982 1.00 82.25 O ANISOU 1130 O GLU A 172 15566 5945 9739 1382 -1257 -108 O ATOM 1131 CB GLU A 172 46.125 47.228 154.079 1.00 80.56 C ANISOU 1131 CB GLU A 172 15274 5806 9529 1454 -1163 -392 C ATOM 1132 N LYS A 173 43.795 47.919 151.832 1.00 89.92 N ANISOU 1132 N LYS A 173 16479 6966 10721 1879 -1265 -258 N ATOM 1133 CA LYS A 173 43.341 48.741 150.714 1.00 89.78 C ANISOU 1133 CA LYS A 173 16592 6837 10684 1942 -1353 -166 C ATOM 1134 C LYS A 173 42.629 49.981 151.263 1.00 93.26 C ANISOU 1134 C LYS A 173 17193 7143 11100 2145 -1423 -245 C ATOM 1135 O LYS A 173 41.407 50.110 151.183 1.00 90.82 O ANISOU 1135 O LYS A 173 16826 6887 10794 2417 -1436 -280 O ATOM 1136 CB LYS A 173 42.430 47.950 149.773 1.00 90.50 C ANISOU 1136 CB LYS A 173 16511 7079 10797 2090 -1330 -107 C ATOM 1137 N ASP A 174 43.415 50.896 151.827 1.00 89.62 N ANISOU 1137 N ASP A 174 16932 6510 10611 2009 -1469 -274 N ATOM 1138 CA ASP A 174 42.937 52.203 152.268 1.00 92.64 C ANISOU 1138 CA ASP A 174 17513 6722 10964 2161 -1550 -338 C ATOM 1139 C ASP A 174 41.737 52.067 153.202 1.00 89.07 C ANISOU 1139 C ASP A 174 16943 6380 10519 2473 -1511 -474 C ATOM 1140 O ASP A 174 40.623 52.497 152.901 1.00 90.86 O ANISOU 1140 O ASP A 174 17176 6605 10741 2724 -1549 -487 O ATOM 1141 CB ASP A 174 42.598 53.085 151.065 1.00 94.96 C ANISOU 1141 CB ASP A 174 17968 6874 11238 2202 -1649 -231 C ATOM 1142 CG ASP A 174 43.767 53.250 150.117 1.00 95.37 C ANISOU 1142 CG ASP A 174 18135 6830 11273 1887 -1686 -91 C ATOM 1143 OD1 ASP A 174 44.894 53.471 150.607 1.00 96.62 O ANISOU 1143 OD1 ASP A 174 18385 6912 11413 1648 -1686 -99 O ATOM 1144 OD2 ASP A 174 43.563 53.152 148.885 1.00 95.99 O ANISOU 1144 OD2 ASP A 174 18204 6920 11349 1874 -1715 27 O ATOM 1145 N GLY A 175 41.985 51.447 154.353 1.00 89.80 N ANISOU 1145 N GLY A 175 16920 6580 10618 2452 -1432 -577 N ATOM 1146 CA GLY A 175 40.970 51.226 155.354 1.00 89.62 C ANISOU 1146 CA GLY A 175 16768 6688 10595 2715 -1381 -710 C ATOM 1147 C GLY A 175 40.243 49.902 155.228 1.00 89.86 C ANISOU 1147 C GLY A 175 16508 6977 10657 2834 -1289 -713 C ATOM 1148 O GLY A 175 39.718 49.397 156.226 1.00 91.09 O ANISOU 1148 O GLY A 175 16515 7285 10812 2970 -1218 -822 O ATOM 1149 N LYS A 176 40.210 49.326 154.030 1.00 87.19 N ANISOU 1149 N LYS A 176 16087 6698 10344 2778 -1288 -595 N ATOM 1150 CA LYS A 176 39.512 48.078 153.772 1.00 84.90 C ANISOU 1150 CA LYS A 176 15529 6645 10084 2883 -1210 -587 C ATOM 1151 C LYS A 176 40.514 46.956 153.533 1.00 82.51 C ANISOU 1151 C LYS A 176 15121 6419 9809 2634 -1145 -526 C ATOM 1152 O LYS A 176 41.618 47.182 153.030 1.00 83.34 O ANISOU 1152 O LYS A 176 15357 6396 9911 2386 -1179 -443 O ATOM 1153 CB LYS A 176 38.573 48.214 152.565 1.00 85.68 C ANISOU 1153 CB LYS A 176 15597 6771 10186 3039 -1259 -504 C ATOM 1154 CG LYS A 176 37.741 46.969 152.290 1.00 83.28 C ANISOU 1154 CG LYS A 176 15013 6722 9908 3164 -1186 -499 C ATOM 1155 CD LYS A 176 36.478 47.265 151.504 1.00 83.30 C ANISOU 1155 CD LYS A 176 14966 6782 9900 3405 -1235 -467 C ATOM 1156 CE LYS A 176 35.382 46.276 151.877 1.00 81.55 C ANISOU 1156 CE LYS A 176 14459 6836 9689 3603 -1156 -531 C ATOM 1157 NZ LYS A 176 34.173 46.395 151.020 1.00 82.42 N ANISOU 1157 NZ LYS A 176 14486 7039 9791 3819 -1200 -490 N ATOM 1158 N LYS A 177 40.123 45.743 153.920 1.00 82.94 N ANISOU 1158 N LYS A 177 14936 6690 9888 2700 -1051 -568 N ATOM 1159 CA LYS A 177 40.904 44.544 153.657 1.00 79.41 C ANISOU 1159 CA LYS A 177 14364 6338 9472 2503 -985 -514 C ATOM 1160 C LYS A 177 40.419 43.890 152.372 1.00 74.09 C ANISOU 1160 C LYS A 177 13573 5757 8819 2540 -985 -411 C ATOM 1161 O LYS A 177 39.225 43.608 152.227 1.00 75.83 O ANISOU 1161 O LYS A 177 13652 6117 9044 2768 -972 -433 O ATOM 1162 CB LYS A 177 40.783 43.553 154.815 1.00 80.37 C ANISOU 1162 CB LYS A 177 14296 6637 9604 2547 -883 -617 C ATOM 1163 CG LYS A 177 41.325 44.040 156.144 1.00 80.65 C ANISOU 1163 CG LYS A 177 14427 6604 9613 2495 -875 -722 C ATOM 1164 CD LYS A 177 42.827 43.838 156.240 1.00 79.23 C ANISOU 1164 CD LYS A 177 14329 6337 9437 2192 -869 -684 C ATOM 1165 CE LYS A 177 43.592 45.119 155.936 1.00 82.76 C ANISOU 1165 CE LYS A 177 15037 6551 9858 2045 -965 -640 C ATOM 1166 NZ LYS A 177 45.053 44.977 156.197 1.00 82.64 N ANISOU 1166 NZ LYS A 177 15089 6473 9839 1747 -958 -617 N ATOM 1167 N HIS A 178 41.345 43.645 151.446 1.00 61.87 N ANISOU 1167 N HIS A 178 12081 4146 7279 2313 -1001 -298 N ATOM 1168 CA HIS A 178 41.052 42.960 150.199 1.00 59.21 C ANISOU 1168 CA HIS A 178 11645 3895 6958 2314 -1001 -194 C ATOM 1169 C HIS A 178 41.833 41.654 150.119 1.00 55.35 C ANISOU 1169 C HIS A 178 11022 3510 6497 2132 -920 -165 C ATOM 1170 O HIS A 178 42.857 41.472 150.781 1.00 54.51 O ANISOU 1170 O HIS A 178 10940 3375 6395 1944 -883 -193 O ATOM 1171 CB HIS A 178 41.381 43.842 148.986 1.00 62.67 C ANISOU 1171 CB HIS A 178 12271 4172 7368 2214 -1095 -71 C ATOM 1172 N ARG A 179 41.344 40.753 149.271 1.00 54.12 N ANISOU 1172 N ARG A 179 10663 3545 6357 2151 -885 -105 N ATOM 1173 CA ARG A 179 41.868 39.401 149.134 1.00 51.84 C ANISOU 1173 CA ARG A 179 10119 3485 6094 1960 -785 -82 C ATOM 1174 C ARG A 179 42.452 39.184 147.743 1.00 51.39 C ANISOU 1174 C ARG A 179 10062 3438 6025 1771 -803 48 C ATOM 1175 O ARG A 179 41.813 39.508 146.739 1.00 52.26 O ANISOU 1175 O ARG A 179 10215 3525 6115 1868 -864 117 O ATOM 1176 CB ARG A 179 40.767 38.382 149.410 1.00 50.87 C ANISOU 1176 CB ARG A 179 9718 3616 5994 2125 -715 -136 C ATOM 1177 CG ARG A 179 40.682 38.018 150.878 1.00 50.35 C ANISOU 1177 CG ARG A 179 9559 3631 5942 2180 -645 -254 C ATOM 1178 CD ARG A 179 41.470 36.750 151.152 1.00 48.22 C ANISOU 1178 CD ARG A 179 9087 3534 5700 1965 -548 -250 C ATOM 1179 NE ARG A 179 42.241 36.747 152.391 1.00 47.87 N ANISOU 1179 NE ARG A 179 9076 3456 5657 1874 -510 -322 N ATOM 1180 CZ ARG A 179 42.950 35.706 152.853 1.00 46.21 C ANISOU 1180 CZ ARG A 179 8704 3385 5469 1707 -430 -329 C ATOM 1181 NH1 ARG A 179 43.616 35.840 154.011 1.00 46.17 N ANISOU 1181 NH1 ARG A 179 8749 3338 5454 1640 -409 -395 N ATOM 1182 NH2 ARG A 179 43.004 34.523 152.209 1.00 44.68 N ANISOU 1182 NH2 ARG A 179 8303 3370 5305 1612 -374 -275 N ATOM 1183 N LEU A 180 43.648 38.609 147.682 1.00 50.10 N ANISOU 1183 N LEU A 180 9840 3326 5868 1508 -750 79 N ATOM 1184 CA LEU A 180 44.294 38.302 146.417 1.00 49.60 C ANISOU 1184 CA LEU A 180 9755 3305 5788 1315 -751 191 C ATOM 1185 C LEU A 180 44.577 36.811 146.326 1.00 47.47 C ANISOU 1185 C LEU A 180 9203 3287 5548 1203 -647 182 C ATOM 1186 O LEU A 180 44.625 36.108 147.337 1.00 46.38 O ANISOU 1186 O LEU A 180 8924 3255 5445 1212 -577 101 O ATOM 1187 CB LEU A 180 45.599 39.078 146.252 1.00 50.35 C ANISOU 1187 CB LEU A 180 10060 3222 5850 1081 -792 250 C ATOM 1188 CG LEU A 180 45.514 40.586 146.443 1.00 52.59 C ANISOU 1188 CG LEU A 180 10659 3221 6104 1152 -900 256 C ATOM 1189 CD1 LEU A 180 46.849 41.222 146.141 1.00 53.29 C ANISOU 1189 CD1 LEU A 180 10931 3162 6155 878 -936 331 C ATOM 1190 CD2 LEU A 180 44.454 41.141 145.546 1.00 53.92 C ANISOU 1190 CD2 LEU A 180 10915 3322 6251 1347 -980 314 C ATOM 1191 N ILE A 181 44.773 36.334 145.098 1.00 46.99 N ANISOU 1191 N ILE A 181 9069 3316 5470 1096 -640 267 N ATOM 1192 CA ILE A 181 45.099 34.935 144.854 1.00 45.16 C ANISOU 1192 CA ILE A 181 8590 3305 5263 984 -548 262 C ATOM 1193 C ILE A 181 45.947 34.851 143.594 1.00 45.12 C ANISOU 1193 C ILE A 181 8607 3318 5217 783 -553 361 C ATOM 1194 O ILE A 181 45.806 35.662 142.677 1.00 46.40 O ANISOU 1194 O ILE A 181 8923 3375 5332 785 -627 442 O ATOM 1195 CB ILE A 181 43.822 34.070 144.753 1.00 44.51 C ANISOU 1195 CB ILE A 181 8305 3399 5206 1162 -518 226 C ATOM 1196 CG1 ILE A 181 44.161 32.594 144.898 1.00 42.65 C ANISOU 1196 CG1 ILE A 181 7829 3368 5009 1058 -420 194 C ATOM 1197 CG2 ILE A 181 43.118 34.310 143.448 1.00 45.31 C ANISOU 1197 CG2 ILE A 181 8432 3513 5271 1232 -577 302 C ATOM 1198 CD1 ILE A 181 43.044 31.785 145.530 1.00 42.02 C ANISOU 1198 CD1 ILE A 181 7562 3436 4965 1220 -377 123 C ATOM 1199 N ASN A 182 46.853 33.874 143.556 1.00 43.75 N ANISOU 1199 N ASN A 182 8285 3281 5059 610 -474 355 N ATOM 1200 CA ASN A 182 47.823 33.784 142.460 1.00 43.77 C ANISOU 1200 CA ASN A 182 8300 3317 5016 403 -467 438 C ATOM 1201 C ASN A 182 47.244 33.052 141.240 1.00 43.37 C ANISOU 1201 C ASN A 182 8121 3414 4945 432 -454 477 C ATOM 1202 O ASN A 182 47.864 32.152 140.677 1.00 42.46 O ANISOU 1202 O ASN A 182 7870 3441 4822 301 -394 486 O ATOM 1203 CB ASN A 182 49.099 33.116 142.965 1.00 42.71 C ANISOU 1203 CB ASN A 182 8065 3265 4899 215 -392 409 C ATOM 1204 CG ASN A 182 50.288 33.347 142.049 1.00 43.17 C ANISOU 1204 CG ASN A 182 8177 3328 4898 -14 -391 491 C ATOM 1205 OD1 ASN A 182 50.487 34.456 141.538 1.00 44.64 O ANISOU 1205 OD1 ASN A 182 8563 3369 5029 -76 -462 567 O ATOM 1206 ND2 ASN A 182 51.117 32.317 141.875 1.00 42.06 N ANISOU 1206 ND2 ASN A 182 7863 3354 4765 -144 -312 477 N ATOM 1207 N VAL A 183 46.044 33.442 140.813 1.00 44.18 N ANISOU 1207 N VAL A 183 8266 3485 5034 610 -515 496 N ATOM 1208 CA VAL A 183 45.336 32.792 139.712 1.00 43.95 C ANISOU 1208 CA VAL A 183 8117 3598 4983 658 -514 527 C ATOM 1209 C VAL A 183 45.269 33.746 138.527 1.00 45.49 C ANISOU 1209 C VAL A 183 8486 3698 5102 636 -599 637 C ATOM 1210 O VAL A 183 44.693 34.835 138.624 1.00 46.92 O ANISOU 1210 O VAL A 183 8842 3718 5267 763 -685 666 O ATOM 1211 CB VAL A 183 43.924 32.355 140.119 1.00 43.69 C ANISOU 1211 CB VAL A 183 7960 3649 4991 882 -516 464 C ATOM 1212 CG1 VAL A 183 43.158 31.869 138.884 1.00 43.80 C ANISOU 1212 CG1 VAL A 183 7879 3795 4970 926 -536 506 C ATOM 1213 CG2 VAL A 183 43.996 31.290 141.185 1.00 42.18 C ANISOU 1213 CG2 VAL A 183 7587 3572 4867 882 -428 369 C ATOM 1214 N PHE A 184 45.833 33.328 137.409 1.00 45.32 N ANISOU 1214 N PHE A 184 8419 3774 5028 483 -578 696 N ATOM 1215 CA PHE A 184 45.866 34.118 136.190 1.00 46.77 C ANISOU 1215 CA PHE A 184 8753 3892 5125 431 -651 811 C ATOM 1216 C PHE A 184 45.470 33.258 134.999 1.00 46.38 C ANISOU 1216 C PHE A 184 8557 4031 5034 421 -632 834 C ATOM 1217 O PHE A 184 45.607 32.035 135.042 1.00 44.95 O ANISOU 1217 O PHE A 184 8174 4022 4885 380 -549 766 O ATOM 1218 CB PHE A 184 47.262 34.714 135.970 1.00 47.37 C ANISOU 1218 CB PHE A 184 8967 3881 5151 195 -648 878 C ATOM 1219 CG PHE A 184 47.675 35.676 137.042 1.00 48.05 C ANISOU 1219 CG PHE A 184 9226 3764 5265 186 -682 864 C ATOM 1220 CD1 PHE A 184 48.249 35.226 138.212 1.00 46.93 C ANISOU 1220 CD1 PHE A 184 8999 3645 5187 143 -615 774 C ATOM 1221 CD2 PHE A 184 47.489 37.033 136.878 1.00 49.92 C ANISOU 1221 CD2 PHE A 184 9722 3783 5463 220 -786 940 C ATOM 1222 CE1 PHE A 184 48.623 36.107 139.200 1.00 47.63 C ANISOU 1222 CE1 PHE A 184 9249 3553 5294 130 -649 754 C ATOM 1223 CE2 PHE A 184 47.861 37.915 137.863 1.00 50.66 C ANISOU 1223 CE2 PHE A 184 9988 3682 5580 208 -821 918 C ATOM 1224 CZ PHE A 184 48.431 37.447 139.028 1.00 49.50 C ANISOU 1224 CZ PHE A 184 9745 3569 5492 160 -751 821 C ATOM 1225 N PRO A 185 44.928 33.857 133.942 1.00 47.71 N ANISOU 1225 N PRO A 185 8828 4170 5130 466 -713 925 N ATOM 1226 CA PRO A 185 44.693 33.100 132.704 1.00 47.52 C ANISOU 1226 CA PRO A 185 8681 4327 5046 424 -698 953 C ATOM 1227 C PRO A 185 45.980 32.547 132.109 1.00 46.97 C ANISOU 1227 C PRO A 185 8556 4361 4930 183 -622 970 C ATOM 1228 O PRO A 185 47.035 33.178 132.172 1.00 47.51 O ANISOU 1228 O PRO A 185 8748 4335 4967 26 -619 1021 O ATOM 1229 CB PRO A 185 44.060 34.142 131.778 1.00 49.39 C ANISOU 1229 CB PRO A 185 9093 4470 5205 500 -814 1068 C ATOM 1230 CG PRO A 185 43.385 35.067 132.680 1.00 50.22 C ANISOU 1230 CG PRO A 185 9330 4393 5359 686 -883 1056 C ATOM 1231 CD PRO A 185 44.266 35.172 133.932 1.00 49.48 C ANISOU 1231 CD PRO A 185 9268 4201 5331 605 -827 991 C ATOM 1232 N THR A 186 45.877 31.332 131.552 1.00 45.97 N ANISOU 1232 N THR A 186 8235 4436 4797 155 -560 921 N ATOM 1233 CA THR A 186 46.957 30.780 130.730 1.00 45.74 C ANISOU 1233 CA THR A 186 8145 4532 4702 -48 -494 937 C ATOM 1234 C THR A 186 47.195 31.627 129.489 1.00 47.37 C ANISOU 1234 C THR A 186 8504 4711 4785 -146 -555 1067 C ATOM 1235 O THR A 186 48.301 31.646 128.942 1.00 47.68 O ANISOU 1235 O THR A 186 8561 4801 4754 -340 -513 1109 O ATOM 1236 CB THR A 186 46.626 29.345 130.302 1.00 44.61 C ANISOU 1236 CB THR A 186 7784 4596 4570 -30 -430 854 C ATOM 1237 OG1 THR A 186 46.227 28.599 131.455 1.00 43.27 O ANISOU 1237 OG1 THR A 186 7486 4442 4514 74 -386 746 O ATOM 1238 CG2 THR A 186 47.828 28.662 129.662 1.00 44.27 C ANISOU 1238 CG2 THR A 186 7660 4687 4473 -222 -346 842 C ATOM 1239 N SER A 187 46.149 32.273 128.987 1.00 48.51 N ANISOU 1239 N SER A 187 8746 4795 4892 -12 -654 1133 N ATOM 1240 CA SER A 187 46.329 33.177 127.861 1.00 50.26 C ANISOU 1240 CA SER A 187 9136 4967 4992 -98 -725 1271 C ATOM 1241 C SER A 187 47.318 34.287 128.208 1.00 51.23 C ANISOU 1241 C SER A 187 9463 4909 5095 -237 -747 1349 C ATOM 1242 O SER A 187 48.248 34.558 127.441 1.00 53.21 O ANISOU 1242 O SER A 187 9777 5191 5248 -437 -732 1431 O ATOM 1243 CB SER A 187 44.977 33.746 127.430 1.00 51.41 C ANISOU 1243 CB SER A 187 9362 5059 5114 100 -839 1328 C ATOM 1244 OG SER A 187 44.134 34.011 128.532 1.00 51.17 O ANISOU 1244 OG SER A 187 9340 4916 5184 305 -875 1268 O ATOM 1245 N ALA A 188 47.173 34.902 129.382 1.00 51.23 N ANISOU 1245 N ALA A 188 9558 4728 5179 -145 -777 1319 N ATOM 1246 CA ALA A 188 48.095 35.968 129.756 1.00 52.27 C ANISOU 1246 CA ALA A 188 9893 4675 5292 -285 -805 1387 C ATOM 1247 C ALA A 188 49.502 35.436 130.008 1.00 51.39 C ANISOU 1247 C ALA A 188 9684 4661 5179 -512 -699 1350 C ATOM 1248 O ALA A 188 50.486 36.094 129.654 1.00 52.47 O ANISOU 1248 O ALA A 188 9947 4748 5243 -715 -706 1439 O ATOM 1249 CB ALA A 188 47.574 36.707 130.980 1.00 52.52 C ANISOU 1249 CB ALA A 188 10048 4495 5413 -123 -862 1347 C ATOM 1250 N TYR A 189 49.625 34.254 130.618 1.00 49.55 N ANISOU 1250 N TYR A 189 9229 4573 5024 -483 -603 1224 N ATOM 1251 CA TYR A 189 50.946 33.658 130.787 1.00 48.78 C ANISOU 1251 CA TYR A 189 9019 4594 4922 -680 -503 1187 C ATOM 1252 C TYR A 189 51.600 33.397 129.443 1.00 49.40 C ANISOU 1252 C TYR A 189 9056 4833 4880 -852 -468 1254 C ATOM 1253 O TYR A 189 52.782 33.692 129.245 1.00 50.02 O ANISOU 1253 O TYR A 189 9169 4938 4898 -1063 -435 1304 O ATOM 1254 CB TYR A 189 50.861 32.355 131.579 1.00 46.82 C ANISOU 1254 CB TYR A 189 8541 4474 4774 -597 -414 1045 C ATOM 1255 CG TYR A 189 50.774 32.504 133.077 1.00 46.11 C ANISOU 1255 CG TYR A 189 8465 4263 4792 -509 -413 971 C ATOM 1256 CD1 TYR A 189 51.804 33.081 133.807 1.00 46.42 C ANISOU 1256 CD1 TYR A 189 8589 4209 4840 -644 -404 981 C ATOM 1257 CD2 TYR A 189 49.670 32.043 133.757 1.00 45.21 C ANISOU 1257 CD2 TYR A 189 8271 4144 4763 -299 -420 889 C ATOM 1258 CE1 TYR A 189 51.718 33.203 135.193 1.00 45.82 C ANISOU 1258 CE1 TYR A 189 8526 4030 4855 -563 -405 907 C ATOM 1259 CE2 TYR A 189 49.570 32.157 135.106 1.00 44.64 C ANISOU 1259 CE2 TYR A 189 8207 3978 4778 -218 -415 821 C ATOM 1260 CZ TYR A 189 50.589 32.732 135.831 1.00 44.93 C ANISOU 1260 CZ TYR A 189 8334 3916 4821 -345 -408 827 C ATOM 1261 OH TYR A 189 50.441 32.821 137.185 1.00 44.40 O ANISOU 1261 OH TYR A 189 8273 3763 4834 -258 -405 753 O ATOM 1262 N ARG A 190 50.842 32.825 128.504 1.00 49.31 N ANISOU 1262 N ARG A 190 8963 4947 4827 -770 -474 1254 N ATOM 1263 CA ARG A 190 51.354 32.642 127.151 1.00 50.11 C ANISOU 1263 CA ARG A 190 9039 5203 4797 -921 -449 1320 C ATOM 1264 C ARG A 190 51.696 33.979 126.506 1.00 52.16 C ANISOU 1264 C ARG A 190 9532 5337 4947 -1052 -528 1480 C ATOM 1265 O ARG A 190 52.750 34.128 125.876 1.00 52.96 O ANISOU 1265 O ARG A 190 9646 5525 4950 -1268 -487 1543 O ATOM 1266 CB ARG A 190 50.336 31.894 126.302 1.00 49.82 C ANISOU 1266 CB ARG A 190 8897 5302 4733 -795 -459 1291 C ATOM 1267 CG ARG A 190 50.919 31.398 125.009 1.00 52.05 C ANISOU 1267 CG ARG A 190 9104 5785 4887 -943 -408 1319 C ATOM 1268 CD ARG A 190 49.897 31.393 123.910 1.00 57.48 C ANISOU 1268 CD ARG A 190 9813 6532 5495 -855 -475 1369 C ATOM 1269 NE ARG A 190 50.485 30.929 122.663 1.00 60.81 N ANISOU 1269 NE ARG A 190 10168 7155 5782 -1002 -423 1391 N ATOM 1270 CZ ARG A 190 49.942 31.131 121.476 1.00 64.06 C ANISOU 1270 CZ ARG A 190 10632 7634 6076 -999 -480 1470 C ATOM 1271 NH1 ARG A 190 50.539 30.676 120.386 1.00 68.54 N ANISOU 1271 NH1 ARG A 190 11132 8396 6514 -1139 -424 1480 N ATOM 1272 NH2 ARG A 190 48.801 31.795 121.388 1.00 64.91 N ANISOU 1272 NH2 ARG A 190 10856 7619 6189 -850 -595 1537 N ATOM 1273 N SER A 191 50.817 34.966 126.658 1.00 53.15 N ANISOU 1273 N SER A 191 9846 5261 5087 -924 -641 1548 N ATOM 1274 CA SER A 191 51.106 36.293 126.134 1.00 55.24 C ANISOU 1274 CA SER A 191 10363 5370 5257 -1041 -729 1705 C ATOM 1275 C SER A 191 52.421 36.821 126.696 1.00 55.67 C ANISOU 1275 C SER A 191 10495 5351 5306 -1260 -695 1732 C ATOM 1276 O SER A 191 53.288 37.285 125.949 1.00 57.00 O ANISOU 1276 O SER A 191 10743 5555 5358 -1484 -691 1839 O ATOM 1277 CB SER A 191 49.941 37.230 126.455 1.00 56.17 C ANISOU 1277 CB SER A 191 10670 5258 5416 -832 -857 1750 C ATOM 1278 OG SER A 191 50.192 38.537 125.994 1.00 58.34 O ANISOU 1278 OG SER A 191 11211 5350 5604 -936 -953 1904 O ATOM 1279 N GLU A 192 52.604 36.710 128.014 1.00 54.59 N ANISOU 1279 N GLU A 192 10323 5132 5287 -1209 -667 1633 N ATOM 1280 CA GLU A 192 53.839 37.158 128.650 1.00 54.94 C ANISOU 1280 CA GLU A 192 10425 5118 5333 -1413 -637 1646 C ATOM 1281 C GLU A 192 55.055 36.409 128.116 1.00 54.60 C ANISOU 1281 C GLU A 192 10204 5323 5220 -1632 -525 1635 C ATOM 1282 O GLU A 192 56.033 37.023 127.676 1.00 55.99 O ANISOU 1282 O GLU A 192 10470 5507 5299 -1868 -524 1734 O ATOM 1283 CB GLU A 192 53.723 36.984 130.159 1.00 54.65 C ANISOU 1283 CB GLU A 192 10346 4985 5434 -1295 -621 1524 C ATOM 1284 CG GLU A 192 55.048 37.005 130.902 1.00 53.49 C ANISOU 1284 CG GLU A 192 10163 4857 5301 -1495 -561 1495 C ATOM 1285 CD GLU A 192 54.823 36.882 132.386 1.00 52.35 C ANISOU 1285 CD GLU A 192 9994 4611 5286 -1363 -556 1380 C ATOM 1286 OE1 GLU A 192 55.780 37.026 133.162 1.00 52.49 O ANISOU 1286 OE1 GLU A 192 10008 4611 5324 -1500 -526 1353 O ATOM 1287 OE2 GLU A 192 53.668 36.650 132.779 1.00 51.59 O ANISOU 1287 OE2 GLU A 192 9878 4461 5265 -1122 -584 1317 O ATOM 1288 N ALA A 193 55.013 35.078 128.142 1.00 52.89 N ANISOU 1288 N ALA A 193 9736 5314 5047 -1556 -430 1516 N ATOM 1289 CA ALA A 193 56.174 34.300 127.725 1.00 52.58 C ANISOU 1289 CA ALA A 193 9514 5514 4949 -1734 -319 1486 C ATOM 1290 C ALA A 193 56.555 34.577 126.279 1.00 54.13 C ANISOU 1290 C ALA A 193 9753 5830 4983 -1899 -318 1603 C ATOM 1291 O ALA A 193 57.745 34.583 125.941 1.00 54.82 O ANISOU 1291 O ALA A 193 9791 6052 4988 -2120 -256 1637 O ATOM 1292 CB ALA A 193 55.906 32.810 127.924 1.00 50.64 C ANISOU 1292 CB ALA A 193 9014 5448 4779 -1595 -230 1337 C ATOM 1293 N LEU A 194 55.564 34.809 125.414 1.00 54.78 N ANISOU 1293 N LEU A 194 9923 5880 5012 -1798 -387 1667 N ATOM 1294 CA LEU A 194 55.857 35.089 124.012 1.00 56.36 C ANISOU 1294 CA LEU A 194 10173 6195 5046 -1951 -393 1785 C ATOM 1295 C LEU A 194 56.663 36.369 123.863 1.00 58.36 C ANISOU 1295 C LEU A 194 10638 6327 5210 -2181 -443 1937 C ATOM 1296 O LEU A 194 57.664 36.407 123.140 1.00 63.09 O ANISOU 1296 O LEU A 194 11202 7085 5684 -2410 -388 2001 O ATOM 1297 CB LEU A 194 54.557 35.185 123.219 1.00 56.78 C ANISOU 1297 CB LEU A 194 10297 6213 5063 -1783 -476 1831 C ATOM 1298 CG LEU A 194 54.720 35.571 121.759 1.00 58.58 C ANISOU 1298 CG LEU A 194 10603 6542 5112 -1925 -500 1967 C ATOM 1299 CD1 LEU A 194 55.471 34.481 121.021 1.00 58.13 C ANISOU 1299 CD1 LEU A 194 10322 6793 4972 -2038 -375 1900 C ATOM 1300 CD2 LEU A 194 53.362 35.834 121.133 1.00 59.14 C ANISOU 1300 CD2 LEU A 194 10772 6540 5158 -1742 -606 2022 C ATOM 1301 N ARG A 195 56.246 37.428 124.550 1.00 59.05 N ANISOU 1301 N ARG A 195 10947 6133 5355 -2128 -548 1993 N ATOM 1302 CA ARG A 195 56.991 38.674 124.489 1.00 61.06 C ANISOU 1302 CA ARG A 195 11427 6241 5533 -2353 -606 2135 C ATOM 1303 C ARG A 195 58.397 38.526 125.043 1.00 60.92 C ANISOU 1303 C ARG A 195 11309 6326 5514 -2578 -517 2101 C ATOM 1304 O ARG A 195 59.319 39.177 124.554 1.00 62.65 O ANISOU 1304 O ARG A 195 11616 6571 5616 -2841 -517 2218 O ATOM 1305 CB ARG A 195 56.238 39.757 125.240 1.00 61.76 C ANISOU 1305 CB ARG A 195 11772 5993 5699 -2224 -735 2176 C ATOM 1306 CG ARG A 195 54.846 40.005 124.692 1.00 62.18 C ANISOU 1306 CG ARG A 195 11931 5944 5748 -1995 -833 2220 C ATOM 1307 CD ARG A 195 54.168 41.070 125.486 1.00 62.99 C ANISOU 1307 CD ARG A 195 12282 5721 5929 -1856 -956 2248 C ATOM 1308 NE ARG A 195 55.129 42.027 126.022 1.00 64.29 N ANISOU 1308 NE ARG A 195 12631 5715 6080 -2071 -985 2312 N ATOM 1309 CZ ARG A 195 54.855 42.891 126.995 1.00 64.86 C ANISOU 1309 CZ ARG A 195 12905 5505 6234 -1990 -1069 2302 C ATOM 1310 NH1 ARG A 195 55.797 43.731 127.427 1.00 66.16 N ANISOU 1310 NH1 ARG A 195 13160 5574 6403 -2182 -1083 2312 N ATOM 1311 NH2 ARG A 195 53.640 42.928 127.557 1.00 64.26 N ANISOU 1311 NH2 ARG A 195 12865 5291 6259 -1685 -1130 2230 N ATOM 1312 N ILE A 196 58.590 37.675 126.049 1.00 59.02 N ANISOU 1312 N ILE A 196 10878 6153 5394 -2486 -442 1946 N ATOM 1313 CA ILE A 196 59.928 37.489 126.602 1.00 58.91 C ANISOU 1313 CA ILE A 196 10750 6254 5380 -2687 -360 1909 C ATOM 1314 C ILE A 196 60.850 36.876 125.557 1.00 59.40 C ANISOU 1314 C ILE A 196 10635 6624 5310 -2869 -258 1931 C ATOM 1315 O ILE A 196 61.903 37.434 125.227 1.00 60.97 O ANISOU 1315 O ILE A 196 10876 6889 5403 -3136 -241 2025 O ATOM 1316 CB ILE A 196 59.872 36.629 127.877 1.00 56.77 C ANISOU 1316 CB ILE A 196 10307 5999 5264 -2528 -305 1740 C ATOM 1317 CG1 ILE A 196 59.191 37.397 129.003 1.00 56.65 C ANISOU 1317 CG1 ILE A 196 10480 5685 5360 -2395 -402 1725 C ATOM 1318 CG2 ILE A 196 61.260 36.195 128.293 1.00 56.57 C ANISOU 1318 CG2 ILE A 196 10110 6157 5228 -2714 -208 1691 C ATOM 1319 CD1 ILE A 196 58.836 36.549 130.174 1.00 54.57 C ANISOU 1319 CD1 ILE A 196 10062 5428 5243 -2198 -359 1566 C ATOM 1320 N LEU A 197 60.456 35.724 125.009 1.00 58.18 N ANISOU 1320 N LEU A 197 10282 6668 5156 -2731 -188 1841 N ATOM 1321 CA LEU A 197 61.341 34.989 124.112 1.00 58.50 C ANISOU 1321 CA LEU A 197 10128 7020 5081 -2873 -77 1827 C ATOM 1322 C LEU A 197 61.583 35.749 122.816 1.00 60.72 C ANISOU 1322 C LEU A 197 10539 7354 5178 -3069 -107 1993 C ATOM 1323 O LEU A 197 62.698 35.733 122.283 1.00 61.85 O ANISOU 1323 O LEU A 197 10597 7702 5200 -3297 -34 2036 O ATOM 1324 CB LEU A 197 60.762 33.604 123.835 1.00 56.81 C ANISOU 1324 CB LEU A 197 9699 6973 4911 -2665 -9 1687 C ATOM 1325 CG LEU A 197 60.639 32.804 125.124 1.00 54.74 C ANISOU 1325 CG LEU A 197 9301 6676 4823 -2496 28 1531 C ATOM 1326 CD1 LEU A 197 59.875 31.509 124.902 1.00 53.16 C ANISOU 1326 CD1 LEU A 197 8931 6590 4678 -2281 74 1401 C ATOM 1327 CD2 LEU A 197 62.036 32.533 125.684 1.00 54.75 C ANISOU 1327 CD2 LEU A 197 9157 6819 4824 -2656 115 1486 C ATOM 1328 N GLN A 198 60.553 36.409 122.286 1.00 61.55 N ANISOU 1328 N GLN A 198 10844 7288 5252 -2983 -214 2090 N ATOM 1329 CA GLN A 198 60.755 37.238 121.103 1.00 63.84 C ANISOU 1329 CA GLN A 198 11290 7600 5365 -3175 -257 2267 C ATOM 1330 C GLN A 198 61.719 38.377 121.397 1.00 65.63 C ANISOU 1330 C GLN A 198 11682 7717 5538 -3447 -292 2393 C ATOM 1331 O GLN A 198 62.537 38.744 120.547 1.00 67.44 O ANISOU 1331 O GLN A 198 11916 8091 5617 -3688 -264 2496 O ATOM 1332 CB GLN A 198 59.417 37.774 120.606 1.00 69.14 C ANISOU 1332 CB GLN A 198 12159 8083 6029 -3008 -381 2348 C ATOM 1333 CG GLN A 198 58.734 36.865 119.612 1.00 68.76 C ANISOU 1333 CG GLN A 198 11973 8229 5923 -2873 -348 2300 C ATOM 1334 CD GLN A 198 57.394 37.409 119.197 1.00 69.89 C ANISOU 1334 CD GLN A 198 12301 8191 6064 -2697 -477 2379 C ATOM 1335 OE1 GLN A 198 56.823 38.251 119.889 1.00 71.80 O ANISOU 1335 OE1 GLN A 198 12736 8151 6392 -2603 -583 2423 O ATOM 1336 NE2 GLN A 198 56.884 36.945 118.059 1.00 69.88 N ANISOU 1336 NE2 GLN A 198 12239 8352 5958 -2648 -473 2395 N ATOM 1337 N THR A 199 61.651 38.937 122.602 1.00 65.19 N ANISOU 1337 N THR A 199 11746 7416 5609 -3408 -352 2371 N ATOM 1338 CA THR A 199 62.610 39.964 122.984 1.00 66.88 C ANISOU 1338 CA THR A 199 12075 7532 5802 -3644 -386 2444 C ATOM 1339 C THR A 199 64.010 39.385 123.129 1.00 66.79 C ANISOU 1339 C THR A 199 11826 7800 5750 -3847 -259 2386 C ATOM 1340 O THR A 199 64.999 40.046 122.793 1.00 68.72 O ANISOU 1340 O THR A 199 12062 8122 5928 -4065 -261 2436 O ATOM 1341 CB THR A 199 62.153 40.632 124.273 1.00 66.46 C ANISOU 1341 CB THR A 199 12196 7157 5897 -3529 -479 2410 C ATOM 1342 OG1 THR A 199 60.863 41.218 124.053 1.00 66.84 O ANISOU 1342 OG1 THR A 199 12455 6964 5976 -3327 -599 2462 O ATOM 1343 CG2 THR A 199 63.125 41.705 124.693 1.00 68.72 C ANISOU 1343 CG2 THR A 199 12566 7355 6190 -3732 -523 2436 C ATOM 1344 N GLN A 200 64.109 38.144 123.601 1.00 64.69 N ANISOU 1344 N GLN A 200 11324 7707 5550 -3731 -155 2244 N ATOM 1345 CA GLN A 200 65.401 37.480 123.703 1.00 69.10 C ANISOU 1345 CA GLN A 200 11633 8555 6069 -3890 -30 2179 C ATOM 1346 C GLN A 200 65.968 37.148 122.333 1.00 70.17 C ANISOU 1346 C GLN A 200 11647 8992 6021 -4044 52 2237 C ATOM 1347 O GLN A 200 67.190 37.150 122.141 1.00 72.47 O ANISOU 1347 O GLN A 200 11790 9501 6244 -4241 119 2233 O ATOM 1348 CB GLN A 200 65.253 36.217 124.546 1.00 62.11 C ANISOU 1348 CB GLN A 200 10507 7759 5332 -3658 45 1980 C ATOM 1349 CG GLN A 200 66.275 36.172 125.651 1.00 61.84 C ANISOU 1349 CG GLN A 200 10371 7763 5362 -3765 84 1920 C ATOM 1350 CD GLN A 200 66.072 37.331 126.562 1.00 62.42 C ANISOU 1350 CD GLN A 200 10696 7518 5501 -3814 -30 1984 C ATOM 1351 OE1 GLN A 200 64.931 37.698 126.892 1.00 61.83 O ANISOU 1351 OE1 GLN A 200 10799 7180 5513 -3624 -123 1984 O ATOM 1352 NE2 GLN A 200 67.149 38.003 126.873 1.00 63.87 N ANISOU 1352 NE2 GLN A 200 10916 7721 5630 -4080 -33 2050 N ATOM 1353 N GLN A 201 65.089 36.833 121.385 1.00 70.30 N ANISOU 1353 N GLN A 201 11682 9040 5987 -3908 39 2250 N ATOM 1354 CA GLN A 201 65.526 36.430 120.058 1.00 71.58 C ANISOU 1354 CA GLN A 201 11725 9500 5973 -4026 119 2288 C ATOM 1355 C GLN A 201 66.405 37.491 119.418 1.00 72.96 C ANISOU 1355 C GLN A 201 11952 9712 6058 -4261 83 2390 C ATOM 1356 O GLN A 201 67.341 37.159 118.684 1.00 72.14 O ANISOU 1356 O GLN A 201 11664 9903 5844 -4399 173 2375 O ATOM 1357 CB GLN A 201 64.301 36.143 119.186 1.00 71.24 C ANISOU 1357 CB GLN A 201 11739 9428 5902 -3831 76 2294 C ATOM 1358 CG GLN A 201 64.486 35.017 118.181 1.00 69.82 C ANISOU 1358 CG GLN A 201 11328 9581 5620 -3797 189 2210 C ATOM 1359 CD GLN A 201 63.171 34.576 117.548 1.00 68.69 C ANISOU 1359 CD GLN A 201 11219 9395 5486 -3565 142 2178 C ATOM 1360 OE1 GLN A 201 62.258 35.380 117.358 1.00 68.71 O ANISOU 1360 OE1 GLN A 201 11447 9172 5487 -3511 20 2289 O ATOM 1361 NE2 GLN A 201 63.066 33.290 117.233 1.00 68.99 N ANISOU 1361 NE2 GLN A 201 11033 9647 5533 -3424 233 2024 N ATOM 1362 N GLU A 202 66.130 38.767 119.688 1.00 76.03 N ANISOU 1362 N GLU A 202 12586 9808 6492 -4302 -49 2487 N ATOM 1363 CA GLU A 202 66.929 39.825 119.082 1.00 81.14 C ANISOU 1363 CA GLU A 202 13301 10475 7051 -4530 -93 2587 C ATOM 1364 C GLU A 202 68.292 39.956 119.745 1.00 82.97 C ANISOU 1364 C GLU A 202 13402 10826 7296 -4724 -43 2543 C ATOM 1365 O GLU A 202 69.237 40.440 119.116 1.00 81.71 O ANISOU 1365 O GLU A 202 13195 10819 7033 -4938 -31 2598 O ATOM 1366 CB GLU A 202 66.180 41.155 119.132 1.00 86.51 C ANISOU 1366 CB GLU A 202 14295 10803 7772 -4504 -253 2697 C ATOM 1367 CG GLU A 202 65.200 41.341 117.991 1.00 91.21 C ANISOU 1367 CG GLU A 202 15011 11356 8289 -4407 -310 2786 C ATOM 1368 CD GLU A 202 63.780 41.554 118.469 1.00 93.18 C ANISOU 1368 CD GLU A 202 15458 11300 8645 -4154 -415 2794 C ATOM 1369 OE1 GLU A 202 63.603 42.022 119.612 1.00 93.45 O ANISOU 1369 OE1 GLU A 202 15610 11090 8807 -4093 -477 2763 O ATOM 1370 OE2 GLU A 202 62.840 41.247 117.704 1.00 95.49 O ANISOU 1370 OE2 GLU A 202 15783 11610 8890 -4012 -437 2826 O ATOM 1371 N PHE A 203 68.435 39.403 120.935 1.00 74.93 N ANISOU 1371 N PHE A 203 12320 9752 6399 -4656 -17 2447 N ATOM 1372 CA PHE A 203 69.727 39.383 121.582 1.00 85.57 C ANISOU 1372 CA PHE A 203 13516 11243 7754 -4829 34 2398 C ATOM 1373 C PHE A 203 70.409 38.059 121.383 1.00 95.51 C ANISOU 1373 C PHE A 203 14450 12898 8940 -4864 187 2310 C ATOM 1374 O PHE A 203 71.608 37.991 121.345 1.00 96.26 O ANISOU 1374 O PHE A 203 14376 13151 9049 -4970 243 2249 O ATOM 1375 CB PHE A 203 69.619 39.565 123.087 1.00 76.26 C ANISOU 1375 CB PHE A 203 12399 9847 6729 -4747 -5 2332 C ATOM 1376 CG PHE A 203 69.047 40.862 123.510 1.00 72.39 C ANISOU 1376 CG PHE A 203 12215 8987 6302 -4743 -156 2404 C ATOM 1377 CD1 PHE A 203 69.817 41.975 123.546 1.00 74.91 C ANISOU 1377 CD1 PHE A 203 12643 9249 6569 -4959 -228 2478 C ATOM 1378 CD2 PHE A 203 67.749 40.946 123.919 1.00 70.95 C ANISOU 1378 CD2 PHE A 203 12212 8520 6226 -4516 -229 2393 C ATOM 1379 CE1 PHE A 203 69.297 43.168 123.960 1.00 75.98 C ANISOU 1379 CE1 PHE A 203 13066 9044 6758 -4946 -367 2535 C ATOM 1380 CE2 PHE A 203 67.220 42.133 124.331 1.00 72.01 C ANISOU 1380 CE2 PHE A 203 12623 8320 6418 -4490 -367 2446 C ATOM 1381 CZ PHE A 203 67.996 43.249 124.346 1.00 74.54 C ANISOU 1381 CZ PHE A 203 13055 8580 6685 -4704 -435 2515 C ATOM 1382 N ASN A 204 69.634 36.993 121.293 1.00127.19 N ANISOU 1382 N ASN A 204 18376 17075 12876 -4765 252 2296 N ATOM 1383 CA ASN A 204 70.197 35.654 121.183 1.00132.86 C ANISOU 1383 CA ASN A 204 18817 18181 13485 -4808 386 2229 C ATOM 1384 C ASN A 204 69.716 34.817 120.011 1.00127.06 C ANISOU 1384 C ASN A 204 17818 17650 12808 -4720 508 2079 C ATOM 1385 O ASN A 204 68.520 34.713 119.763 1.00129.73 O ANISOU 1385 O ASN A 204 17921 18292 13077 -4817 601 2024 O ATOM 1386 CB ASN A 204 69.914 34.931 122.479 1.00140.67 C ANISOU 1386 CB ASN A 204 19753 19337 14359 -5064 386 2297 C ATOM 1387 CG ASN A 204 70.490 33.553 122.514 1.00144.49 C ANISOU 1387 CG ASN A 204 20162 20053 14685 -5110 434 2332 C ATOM 1388 OD1 ASN A 204 69.845 32.581 122.165 1.00147.03 O ANISOU 1388 OD1 ASN A 204 20630 20267 14969 -5032 387 2396 O ATOM 1389 ND2 ASN A 204 71.717 33.461 122.952 1.00146.57 N ANISOU 1389 ND2 ASN A 204 20193 20644 14853 -5231 528 2289 N ATOM 1390 N PRO A 205 70.666 34.253 119.268 1.00 94.02 N ANISOU 1390 N PRO A 205 13653 13326 8744 -4532 515 2007 N ATOM 1391 CA PRO A 205 70.359 33.439 118.082 1.00 86.53 C ANISOU 1391 CA PRO A 205 12440 12618 7821 -4418 647 1860 C ATOM 1392 C PRO A 205 70.103 31.948 118.323 1.00 81.88 C ANISOU 1392 C PRO A 205 11775 12153 7182 -4236 702 1791 C ATOM 1393 O PRO A 205 69.642 31.275 117.401 1.00 81.30 O ANISOU 1393 O PRO A 205 11870 11994 7029 -4242 645 1888 O ATOM 1394 CB PRO A 205 71.608 33.615 117.214 1.00 77.07 C ANISOU 1394 CB PRO A 205 11287 11171 6825 -4248 595 1778 C ATOM 1395 CG PRO A 205 72.703 33.882 118.189 1.00 77.13 C ANISOU 1395 CG PRO A 205 11618 10816 6872 -4283 452 1906 C ATOM 1396 CD PRO A 205 72.077 34.677 119.301 1.00 87.53 C ANISOU 1396 CD PRO A 205 13061 12157 8040 -4438 411 2043 C ATOM 1397 N GLN A 206 70.390 31.436 119.516 1.00 90.08 N ANISOU 1397 N GLN A 206 12564 13383 8278 -4057 799 1615 N ATOM 1398 CA GLN A 206 70.168 30.027 119.783 1.00 84.02 C ANISOU 1398 CA GLN A 206 11708 12740 7474 -3872 849 1521 C ATOM 1399 C GLN A 206 68.666 29.830 120.016 1.00 77.62 C ANISOU 1399 C GLN A 206 11029 11655 6809 -3611 763 1470 C ATOM 1400 O GLN A 206 68.164 28.733 119.973 1.00 70.15 O ANISOU 1400 O GLN A 206 9959 10766 5927 -3390 805 1325 O ATOM 1401 CB GLN A 206 71.031 29.532 120.941 1.00 85.55 C ANISOU 1401 CB GLN A 206 11600 13230 7673 -3777 980 1349 C ATOM 1402 CG GLN A 206 72.206 28.621 120.562 1.00 91.50 C ANISOU 1402 CG GLN A 206 12200 14303 8261 -4028 1074 1396 C ATOM 1403 CD GLN A 206 73.325 28.569 121.624 1.00 96.05 C ANISOU 1403 CD GLN A 206 12920 14900 8675 -4249 1029 1563 C ATOM 1404 OE1 GLN A 206 73.149 28.034 122.712 1.00 97.18 O ANISOU 1404 OE1 GLN A 206 13170 14930 8825 -4429 952 1674 O ATOM 1405 NE2 GLN A 206 74.482 29.117 121.292 1.00 98.13 N ANISOU 1405 NE2 GLN A 206 13183 15277 8824 -4198 1054 1556 N ATOM 1406 N ILE A 207 67.954 30.914 120.255 1.00 75.19 N ANISOU 1406 N ILE A 207 10971 11047 6551 -3634 641 1588 N ATOM 1407 CA ILE A 207 66.536 30.835 120.466 1.00 60.55 C ANISOU 1407 CA ILE A 207 9252 8948 4805 -3404 553 1564 C ATOM 1408 C ILE A 207 65.813 30.887 119.138 1.00 61.51 C ANISOU 1408 C ILE A 207 9434 9154 4782 -3406 542 1624 C ATOM 1409 O ILE A 207 65.415 31.928 118.682 1.00 62.97 O ANISOU 1409 O ILE A 207 9823 9235 4869 -3536 464 1788 O ATOM 1410 CB ILE A 207 66.055 31.972 121.375 1.00 60.43 C ANISOU 1410 CB ILE A 207 9481 8591 4887 -3414 426 1662 C ATOM 1411 CG1 ILE A 207 66.444 31.690 122.814 1.00 59.44 C ANISOU 1411 CG1 ILE A 207 9281 8400 4901 -3405 440 1587 C ATOM 1412 CG2 ILE A 207 64.553 32.136 121.354 1.00 59.20 C ANISOU 1412 CG2 ILE A 207 9455 8212 4827 -3172 336 1643 C ATOM 1413 CD1 ILE A 207 66.542 32.926 123.665 1.00 60.32 C ANISOU 1413 CD1 ILE A 207 9606 8275 5036 -3554 346 1707 C ATOM 1414 N THR A 208 65.611 29.732 118.543 1.00 60.84 N ANISOU 1414 N THR A 208 9177 9264 4676 -3268 619 1493 N ATOM 1415 CA THR A 208 64.921 29.609 117.273 1.00 61.68 C ANISOU 1415 CA THR A 208 9327 9462 4645 -3253 610 1531 C ATOM 1416 C THR A 208 63.422 29.714 117.375 1.00 60.58 C ANISOU 1416 C THR A 208 9346 9070 4603 -3054 496 1541 C ATOM 1417 O THR A 208 62.888 29.703 118.433 1.00 59.05 O ANISOU 1417 O THR A 208 9196 8655 4585 -2907 440 1494 O ATOM 1418 CB THR A 208 65.226 28.262 116.659 1.00 61.50 C ANISOU 1418 CB THR A 208 9070 9737 4560 -3177 731 1375 C ATOM 1419 OG1 THR A 208 64.553 27.262 117.396 1.00 59.36 O ANISOU 1419 OG1 THR A 208 8703 9390 4463 -2922 739 1205 O ATOM 1420 CG2 THR A 208 66.673 27.987 116.736 1.00 62.52 C ANISOU 1420 CG2 THR A 208 9017 10126 4611 -3341 848 1347 C ATOM 1421 N ASP A 209 62.745 29.844 116.258 1.00 61.50 N ANISOU 1421 N ASP A 209 9540 9235 4593 -3052 460 1604 N ATOM 1422 CA ASP A 209 61.289 29.865 116.222 1.00 61.25 C ANISOU 1422 CA ASP A 209 9628 9009 4634 -2855 356 1606 C ATOM 1423 C ASP A 209 60.712 28.553 116.723 1.00 58.55 C ANISOU 1423 C ASP A 209 9129 8681 4438 -2614 393 1410 C ATOM 1424 O ASP A 209 59.654 28.535 117.360 1.00 57.28 O ANISOU 1424 O ASP A 209 9036 8314 4415 -2436 314 1382 O ATOM 1425 CB ASP A 209 60.813 30.147 114.800 1.00 63.28 C ANISOU 1425 CB ASP A 209 9973 9362 4708 -2909 319 1705 C ATOM 1426 CG ASP A 209 61.329 31.457 114.272 1.00 64.55 C ANISOU 1426 CG ASP A 209 10310 9497 4720 -3154 274 1914 C ATOM 1427 OD1 ASP A 209 62.454 31.481 113.730 1.00 68.71 O ANISOU 1427 OD1 ASP A 209 10752 10252 5104 -3360 364 1946 O ATOM 1428 OD2 ASP A 209 60.608 32.464 114.402 1.00 64.90 O ANISOU 1428 OD2 ASP A 209 10577 9294 4787 -3139 148 2047 O ATOM 1429 N GLU A 210 61.386 27.441 116.431 1.00 58.32 N ANISOU 1429 N GLU A 210 8889 8895 4374 -2605 511 1271 N ATOM 1430 CA GLU A 210 60.904 26.153 116.907 1.00 59.48 C ANISOU 1430 CA GLU A 210 8894 9049 4657 -2389 546 1085 C ATOM 1431 C GLU A 210 60.996 26.071 118.419 1.00 58.44 C ANISOU 1431 C GLU A 210 8738 8743 4722 -2303 537 1029 C ATOM 1432 O GLU A 210 60.063 25.599 119.074 1.00 54.48 O ANISOU 1432 O GLU A 210 8239 8095 4367 -2116 494 952 O ATOM 1433 CB GLU A 210 61.682 25.010 116.255 1.00 66.04 C ANISOU 1433 CB GLU A 210 9520 10171 5401 -2396 673 948 C ATOM 1434 CG GLU A 210 61.326 23.623 116.796 1.00 68.78 C ANISOU 1434 CG GLU A 210 9724 10518 5892 -2185 713 751 C ATOM 1435 CD GLU A 210 59.908 23.186 116.460 1.00 70.16 C ANISOU 1435 CD GLU A 210 9955 10598 6104 -2023 640 708 C ATOM 1436 OE1 GLU A 210 59.211 23.900 115.707 1.00 73.68 O ANISOU 1436 OE1 GLU A 210 10537 11005 6454 -2062 562 823 O ATOM 1437 OE2 GLU A 210 59.489 22.116 116.947 1.00 70.55 O ANISOU 1437 OE2 GLU A 210 9912 10616 6277 -1858 657 560 O ATOM 1438 N PHE A 211 62.107 26.540 118.992 1.00 57.12 N ANISOU 1438 N PHE A 211 8546 8600 4558 -2447 577 1070 N ATOM 1439 CA PHE A 211 62.216 26.594 120.441 1.00 54.03 C ANISOU 1439 CA PHE A 211 8149 8040 4341 -2383 559 1031 C ATOM 1440 C PHE A 211 61.040 27.343 121.050 1.00 53.35 C ANISOU 1440 C PHE A 211 8253 7658 4358 -2283 435 1101 C ATOM 1441 O PHE A 211 60.461 26.895 122.044 1.00 51.73 O ANISOU 1441 O PHE A 211 8024 7319 4314 -2115 414 1015 O ATOM 1442 CB PHE A 211 63.534 27.245 120.854 1.00 55.01 C ANISOU 1442 CB PHE A 211 8253 8224 4425 -2587 599 1097 C ATOM 1443 CG PHE A 211 63.634 27.512 122.335 1.00 53.89 C ANISOU 1443 CG PHE A 211 8138 7892 4446 -2546 564 1081 C ATOM 1444 CD1 PHE A 211 64.089 26.536 123.198 1.00 52.63 C ANISOU 1444 CD1 PHE A 211 7803 7794 4400 -2445 630 941 C ATOM 1445 CD2 PHE A 211 63.250 28.733 122.861 1.00 54.20 C ANISOU 1445 CD2 PHE A 211 8387 7686 4521 -2602 462 1203 C ATOM 1446 CE1 PHE A 211 64.167 26.778 124.557 1.00 51.67 C ANISOU 1446 CE1 PHE A 211 7706 7506 4418 -2409 596 927 C ATOM 1447 CE2 PHE A 211 63.321 28.978 124.218 1.00 53.25 C ANISOU 1447 CE2 PHE A 211 8296 7396 4541 -2561 429 1179 C ATOM 1448 CZ PHE A 211 63.783 28.000 125.066 1.00 51.97 C ANISOU 1448 CZ PHE A 211 7950 7310 4485 -2469 498 1042 C ATOM 1449 N ILE A 212 60.675 28.489 120.475 1.00 54.67 N ANISOU 1449 N ILE A 212 8613 7726 4432 -2379 352 1258 N ATOM 1450 CA ILE A 212 59.533 29.234 120.992 1.00 54.24 C ANISOU 1450 CA ILE A 212 8745 7397 4469 -2265 230 1323 C ATOM 1451 C ILE A 212 58.260 28.418 120.844 1.00 53.04 C ANISOU 1451 C ILE A 212 8548 7222 4384 -2039 202 1231 C ATOM 1452 O ILE A 212 57.398 28.419 121.728 1.00 51.86 O ANISOU 1452 O ILE A 212 8440 6890 4374 -1877 144 1195 O ATOM 1453 CB ILE A 212 59.414 30.596 120.287 1.00 56.16 C ANISOU 1453 CB ILE A 212 9210 7543 4585 -2409 143 1514 C ATOM 1454 CG1 ILE A 212 60.697 31.396 120.467 1.00 57.46 C ANISOU 1454 CG1 ILE A 212 9419 7732 4682 -2656 170 1608 C ATOM 1455 CG2 ILE A 212 58.217 31.371 120.801 1.00 55.90 C ANISOU 1455 CG2 ILE A 212 9370 7225 4643 -2268 13 1576 C ATOM 1456 CD1 ILE A 212 60.608 32.799 119.943 1.00 59.42 C ANISOU 1456 CD1 ILE A 212 9913 7842 4822 -2808 74 1803 C ATOM 1457 N ASN A 213 58.124 27.704 119.727 1.00 53.43 N ANISOU 1457 N ASN A 213 8509 7464 4328 -2030 243 1189 N ATOM 1458 CA ASN A 213 56.934 26.893 119.500 1.00 52.47 C ANISOU 1458 CA ASN A 213 8341 7339 4257 -1837 214 1100 C ATOM 1459 C ASN A 213 56.816 25.797 120.543 1.00 50.57 C ANISOU 1459 C ASN A 213 7954 7077 4184 -1688 263 937 C ATOM 1460 O ASN A 213 55.757 25.613 121.150 1.00 49.48 O ANISOU 1460 O ASN A 213 7837 6799 4164 -1524 204 898 O ATOM 1461 CB ASN A 213 56.976 26.278 118.099 1.00 53.38 C ANISOU 1461 CB ASN A 213 8381 7685 4216 -1878 259 1072 C ATOM 1462 CG ASN A 213 56.626 27.266 117.010 1.00 55.15 C ANISOU 1462 CG ASN A 213 8765 7908 4280 -1973 183 1233 C ATOM 1463 OD1 ASN A 213 55.728 28.091 117.165 1.00 55.34 O ANISOU 1463 OD1 ASN A 213 8948 7743 4336 -1909 71 1332 O ATOM 1464 ND2 ASN A 213 57.326 27.175 115.889 1.00 58.87 N ANISOU 1464 ND2 ASN A 213 9195 8597 4575 -2119 243 1260 N ATOM 1465 N ARG A 214 57.900 25.053 120.756 1.00 50.28 N ANISOU 1465 N ARG A 214 7763 7186 4154 -1741 369 843 N ATOM 1466 CA ARG A 214 57.841 23.871 121.607 1.00 50.55 C ANISOU 1466 CA ARG A 214 7652 7222 4332 -1600 419 686 C ATOM 1467 C ARG A 214 57.560 24.223 123.059 1.00 48.79 C ANISOU 1467 C ARG A 214 7478 6787 4272 -1522 374 690 C ATOM 1468 O ARG A 214 56.846 23.486 123.751 1.00 49.57 O ANISOU 1468 O ARG A 214 7523 6813 4498 -1365 364 596 O ATOM 1469 CB ARG A 214 59.141 23.092 121.505 1.00 48.86 C ANISOU 1469 CB ARG A 214 7273 7212 4082 -1671 536 595 C ATOM 1470 CG ARG A 214 59.502 22.769 120.107 1.00 50.34 C ANISOU 1470 CG ARG A 214 7407 7623 4098 -1749 590 584 C ATOM 1471 CD ARG A 214 59.728 21.324 119.971 1.00 51.80 C ANISOU 1471 CD ARG A 214 7423 7950 4309 -1649 672 411 C ATOM 1472 NE ARG A 214 60.521 20.782 121.053 1.00 53.32 N ANISOU 1472 NE ARG A 214 7502 8139 4619 -1611 731 327 N ATOM 1473 CZ ARG A 214 61.776 20.377 120.894 1.00 55.90 C ANISOU 1473 CZ ARG A 214 7695 8658 4887 -1680 828 272 C ATOM 1474 NH1 ARG A 214 62.385 20.467 119.692 1.00 59.73 N ANISOU 1474 NH1 ARG A 214 8143 9360 5193 -1796 884 291 N ATOM 1475 NH2 ARG A 214 62.432 19.868 121.939 1.00 55.95 N ANISOU 1475 NH2 ARG A 214 7598 8653 5009 -1627 871 197 N ATOM 1476 N TYR A 215 58.133 25.329 123.542 1.00 48.08 N ANISOU 1476 N TYR A 215 7492 6602 4175 -1639 347 795 N ATOM 1477 CA TYR A 215 57.921 25.741 124.923 1.00 47.89 C ANISOU 1477 CA TYR A 215 7525 6379 4292 -1575 304 798 C ATOM 1478 C TYR A 215 56.470 26.127 125.157 1.00 50.08 C ANISOU 1478 C TYR A 215 7922 6472 4635 -1425 203 828 C ATOM 1479 O TYR A 215 55.852 25.688 126.128 1.00 52.57 O ANISOU 1479 O TYR A 215 8201 6689 5084 -1279 190 753 O ATOM 1480 CB TYR A 215 58.867 26.893 125.301 1.00 48.11 C ANISOU 1480 CB TYR A 215 7653 6345 4282 -1751 291 905 C ATOM 1481 CG TYR A 215 58.462 27.558 126.608 1.00 47.43 C ANISOU 1481 CG TYR A 215 7676 6024 4322 -1684 222 924 C ATOM 1482 CD1 TYR A 215 58.952 27.098 127.814 1.00 46.34 C ANISOU 1482 CD1 TYR A 215 7443 5867 4298 -1648 262 840 C ATOM 1483 CD2 TYR A 215 57.573 28.623 126.642 1.00 47.97 C ANISOU 1483 CD2 TYR A 215 7943 5892 4392 -1645 116 1022 C ATOM 1484 CE1 TYR A 215 58.564 27.661 129.015 1.00 45.76 C ANISOU 1484 CE1 TYR A 215 7466 5591 4331 -1582 204 847 C ATOM 1485 CE2 TYR A 215 57.178 29.197 127.854 1.00 47.43 C ANISOU 1485 CE2 TYR A 215 7973 5613 4435 -1567 58 1024 C ATOM 1486 CZ TYR A 215 57.685 28.707 129.039 1.00 46.31 C ANISOU 1486 CZ TYR A 215 7730 5466 4400 -1541 104 934 C ATOM 1487 OH TYR A 215 57.334 29.248 130.266 1.00 45.83 O ANISOU 1487 OH TYR A 215 7761 5211 4441 -1467 51 928 O ATOM 1488 N LEU A 216 55.905 26.945 124.273 1.00 47.84 N ANISOU 1488 N LEU A 216 7778 6148 4253 -1455 131 939 N ATOM 1489 CA LEU A 216 54.516 27.357 124.432 1.00 47.64 C ANISOU 1489 CA LEU A 216 7860 5962 4278 -1301 31 971 C ATOM 1490 C LEU A 216 53.544 26.189 124.416 1.00 46.46 C ANISOU 1490 C LEU A 216 7584 5872 4197 -1131 41 854 C ATOM 1491 O LEU A 216 52.451 26.306 124.977 1.00 45.88 O ANISOU 1491 O LEU A 216 7550 5673 4210 -981 -24 844 O ATOM 1492 CB LEU A 216 54.127 28.357 123.343 1.00 49.30 C ANISOU 1492 CB LEU A 216 8233 6144 4356 -1362 -49 1114 C ATOM 1493 CG LEU A 216 54.711 29.759 123.479 1.00 50.64 C ANISOU 1493 CG LEU A 216 8590 6176 4475 -1504 -100 1255 C ATOM 1494 CD1 LEU A 216 54.061 30.707 122.473 1.00 52.27 C ANISOU 1494 CD1 LEU A 216 8974 6319 4566 -1520 -199 1398 C ATOM 1495 CD2 LEU A 216 54.552 30.270 124.912 1.00 49.91 C ANISOU 1495 CD2 LEU A 216 8572 5870 4522 -1428 -139 1240 C ATOM 1496 N GLU A 217 53.909 25.072 123.790 1.00 46.22 N ANISOU 1496 N GLU A 217 7406 6031 4126 -1152 119 762 N ATOM 1497 CA GLU A 217 53.104 23.865 123.915 1.00 45.26 C ANISOU 1497 CA GLU A 217 7162 5954 4081 -1008 134 638 C ATOM 1498 C GLU A 217 53.333 23.191 125.260 1.00 43.63 C ANISOU 1498 C GLU A 217 6861 5689 4026 -936 179 538 C ATOM 1499 O GLU A 217 52.393 22.646 125.848 1.00 42.65 O ANISOU 1499 O GLU A 217 6696 5504 4003 -798 155 475 O ATOM 1500 CB GLU A 217 53.415 22.898 122.773 1.00 46.12 C ANISOU 1500 CB GLU A 217 7162 6271 4089 -1052 197 566 C ATOM 1501 CG GLU A 217 52.701 21.545 122.855 1.00 47.19 C ANISOU 1501 CG GLU A 217 7175 6457 4300 -925 217 426 C ATOM 1502 CD GLU A 217 51.178 21.630 122.719 1.00 50.16 C ANISOU 1502 CD GLU A 217 7594 6763 4699 -804 124 444 C ATOM 1503 OE1 GLU A 217 50.666 22.666 122.241 1.00 50.02 O ANISOU 1503 OE1 GLU A 217 7699 6693 4611 -814 44 563 O ATOM 1504 OE2 GLU A 217 50.494 20.649 123.093 1.00 48.56 O ANISOU 1504 OE2 GLU A 217 7303 6562 4584 -701 127 342 O ATOM 1505 N ILE A 218 54.574 23.207 125.756 1.00 43.55 N ANISOU 1505 N ILE A 218 6811 5709 4029 -1032 244 526 N ATOM 1506 CA ILE A 218 54.840 22.721 127.110 1.00 42.30 C ANISOU 1506 CA ILE A 218 6580 5482 4008 -969 277 450 C ATOM 1507 C ILE A 218 54.024 23.519 128.116 1.00 41.85 C ANISOU 1507 C ILE A 218 6633 5226 4042 -883 199 499 C ATOM 1508 O ILE A 218 53.302 22.960 128.946 1.00 40.76 O ANISOU 1508 O ILE A 218 6446 5026 4015 -753 189 432 O ATOM 1509 CB ILE A 218 56.342 22.805 127.430 1.00 42.57 C ANISOU 1509 CB ILE A 218 6564 5588 4024 -1099 347 449 C ATOM 1510 CG1 ILE A 218 57.144 21.846 126.545 1.00 42.98 C ANISOU 1510 CG1 ILE A 218 6480 5853 3998 -1152 435 375 C ATOM 1511 CG2 ILE A 218 56.568 22.544 128.896 1.00 41.43 C ANISOU 1511 CG2 ILE A 218 6374 5352 4016 -1039 361 395 C ATOM 1512 CD1 ILE A 218 58.632 22.093 126.589 1.00 43.70 C ANISOU 1512 CD1 ILE A 218 6519 6053 4033 -1298 500 394 C ATOM 1513 N LEU A 219 54.090 24.844 128.005 1.00 42.84 N ANISOU 1513 N LEU A 219 6914 5251 4113 -953 140 617 N ATOM 1514 CA LEU A 219 53.385 25.737 128.913 1.00 42.71 C ANISOU 1514 CA LEU A 219 7021 5037 4168 -870 62 665 C ATOM 1515 C LEU A 219 51.871 25.605 128.774 1.00 42.45 C ANISOU 1515 C LEU A 219 7005 4957 4168 -704 -3 654 C ATOM 1516 O LEU A 219 51.165 25.396 129.763 1.00 41.56 O ANISOU 1516 O LEU A 219 6868 4761 4161 -574 -21 603 O ATOM 1517 CB LEU A 219 53.840 27.175 128.653 1.00 44.12 C ANISOU 1517 CB LEU A 219 7381 5118 4266 -994 9 796 C ATOM 1518 CG LEU A 219 53.288 28.235 129.598 1.00 44.28 C ANISOU 1518 CG LEU A 219 7556 4917 4350 -921 -73 845 C ATOM 1519 CD1 LEU A 219 54.227 28.404 130.798 1.00 43.83 C ANISOU 1519 CD1 LEU A 219 7492 4800 4360 -989 -39 816 C ATOM 1520 CD2 LEU A 219 53.095 29.552 128.881 1.00 45.94 C ANISOU 1520 CD2 LEU A 219 7970 5021 4464 -981 -160 983 C ATOM 1521 N THR A 220 51.349 25.720 127.554 1.00 44.36 N ANISOU 1521 N THR A 220 7280 5264 4311 -708 -40 702 N ATOM 1522 CA THR A 220 49.904 25.810 127.369 1.00 44.63 C ANISOU 1522 CA THR A 220 7342 5253 4360 -557 -117 713 C ATOM 1523 C THR A 220 49.230 24.463 127.160 1.00 44.33 C ANISOU 1523 C THR A 220 7145 5339 4359 -472 -86 604 C ATOM 1524 O THR A 220 48.017 24.360 127.370 1.00 44.04 O ANISOU 1524 O THR A 220 7095 5270 4369 -335 -139 588 O ATOM 1525 CB THR A 220 49.571 26.726 126.183 1.00 46.82 C ANISOU 1525 CB THR A 220 7753 5526 4510 -594 -193 833 C ATOM 1526 OG1 THR A 220 50.165 26.200 124.994 1.00 48.64 O ANISOU 1526 OG1 THR A 220 7922 5931 4627 -714 -143 830 O ATOM 1527 CG2 THR A 220 50.109 28.128 126.417 1.00 48.05 C ANISOU 1527 CG2 THR A 220 8096 5528 4634 -675 -240 950 C ATOM 1528 N GLY A 221 49.978 23.433 126.773 1.00 42.15 N ANISOU 1528 N GLY A 221 6749 5204 4062 -548 -2 526 N ATOM 1529 CA GLY A 221 49.408 22.136 126.459 1.00 41.55 C ANISOU 1529 CA GLY A 221 6540 5238 4008 -486 25 421 C ATOM 1530 C GLY A 221 48.502 21.504 127.499 1.00 40.42 C ANISOU 1530 C GLY A 221 6325 5037 3996 -352 14 347 C ATOM 1531 O GLY A 221 48.867 21.366 128.672 1.00 39.55 O ANISOU 1531 O GLY A 221 6188 4854 3985 -331 47 312 O ATOM 1532 N LYS A 222 47.310 21.106 127.062 1.00 40.53 N ANISOU 1532 N LYS A 222 6301 5095 4004 -269 -33 326 N ATOM 1533 CA LYS A 222 46.358 20.362 127.870 1.00 39.65 C ANISOU 1533 CA LYS A 222 6102 4966 3999 -158 -41 254 C ATOM 1534 C LYS A 222 45.857 19.168 127.077 1.00 39.68 C ANISOU 1534 C LYS A 222 6004 5099 3975 -161 -31 172 C ATOM 1535 O LYS A 222 45.930 19.139 125.849 1.00 41.39 O ANISOU 1535 O LYS A 222 6235 5412 4081 -218 -41 185 O ATOM 1536 CB LYS A 222 45.154 21.210 128.277 1.00 42.31 C ANISOU 1536 CB LYS A 222 6495 5219 4360 -37 -128 315 C ATOM 1537 CG LYS A 222 45.434 22.253 129.299 1.00 46.04 C ANISOU 1537 CG LYS A 222 7066 5545 4884 -5 -143 371 C ATOM 1538 CD LYS A 222 44.146 22.924 129.714 1.00 48.54 C ANISOU 1538 CD LYS A 222 7419 5794 5228 143 -224 409 C ATOM 1539 CE LYS A 222 43.136 21.903 130.180 1.00 49.52 C ANISOU 1539 CE LYS A 222 7402 5989 5424 230 -217 326 C ATOM 1540 NZ LYS A 222 41.874 22.527 130.663 1.00 51.04 N ANISOU 1540 NZ LYS A 222 7608 6141 5644 383 -290 355 N ATOM 1541 N ARG A 223 45.309 18.196 127.783 1.00 38.86 N ANISOU 1541 N ARG A 223 5803 4996 3966 -104 -14 89 N ATOM 1542 CA ARG A 223 44.666 17.062 127.148 1.00 38.96 C ANISOU 1542 CA ARG A 223 5728 5112 3964 -105 -17 8 C ATOM 1543 C ARG A 223 43.177 17.338 127.022 1.00 39.41 C ANISOU 1543 C ARG A 223 5773 5189 4014 -18 -103 42 C ATOM 1544 O ARG A 223 42.587 17.991 127.886 1.00 39.22 O ANISOU 1544 O ARG A 223 5767 5087 4048 69 -139 87 O ATOM 1545 CB ARG A 223 44.904 15.774 127.933 1.00 38.01 C ANISOU 1545 CB ARG A 223 5514 4982 3945 -105 45 -99 C ATOM 1546 CG ARG A 223 46.347 15.310 127.867 1.00 37.78 C ANISOU 1546 CG ARG A 223 5477 4966 3911 -180 127 -147 C ATOM 1547 CD ARG A 223 46.692 14.223 128.860 1.00 36.86 C ANISOU 1547 CD ARG A 223 5290 4809 3908 -164 182 -233 C ATOM 1548 NE ARG A 223 47.989 13.672 128.502 1.00 36.96 N ANISOU 1548 NE ARG A 223 5282 4867 3893 -224 254 -291 N ATOM 1549 CZ ARG A 223 48.155 12.560 127.799 1.00 37.29 C ANISOU 1549 CZ ARG A 223 5279 4982 3909 -247 283 -388 C ATOM 1550 NH1 ARG A 223 47.103 11.860 127.411 1.00 37.51 N ANISOU 1550 NH1 ARG A 223 5280 5037 3937 -229 244 -436 N ATOM 1551 NH2 ARG A 223 49.370 12.142 127.489 1.00 37.51 N ANISOU 1551 NH2 ARG A 223 5286 5060 3908 -286 350 -441 N ATOM 1552 N LYS A 224 42.592 16.870 125.918 1.00 40.15 N ANISOU 1552 N LYS A 224 5833 5395 4027 -40 -137 17 N ATOM 1553 CA LYS A 224 41.149 16.905 125.745 1.00 40.66 C ANISOU 1553 CA LYS A 224 5855 5511 4083 35 -217 33 C ATOM 1554 C LYS A 224 40.470 16.045 126.794 1.00 39.88 C ANISOU 1554 C LYS A 224 5654 5397 4100 80 -203 -37 C ATOM 1555 O LYS A 224 40.894 14.924 127.060 1.00 39.27 O ANISOU 1555 O LYS A 224 5522 5324 4075 26 -144 -127 O ATOM 1556 CB LYS A 224 40.768 16.390 124.352 1.00 41.61 C ANISOU 1556 CB LYS A 224 5949 5769 4092 -20 -250 3 C ATOM 1557 CG LYS A 224 41.341 17.177 123.223 1.00 42.56 C ANISOU 1557 CG LYS A 224 6164 5928 4080 -72 -267 75 C ATOM 1558 CD LYS A 224 40.630 18.487 123.135 1.00 43.34 C ANISOU 1558 CD LYS A 224 6336 5990 4139 11 -357 199 C ATOM 1559 CE LYS A 224 41.576 19.604 122.783 1.00 43.84 C ANISOU 1559 CE LYS A 224 6533 5993 4132 -34 -353 298 C ATOM 1560 NZ LYS A 224 40.816 20.880 122.646 1.00 45.87 N ANISOU 1560 NZ LYS A 224 6880 6199 4348 58 -453 421 N ATOM 1561 N TYR A 225 39.369 16.548 127.347 1.00 40.06 N ANISOU 1561 N TYR A 225 5651 5412 4157 180 -262 6 N ATOM 1562 CA TYR A 225 38.649 15.785 128.360 1.00 39.47 C ANISOU 1562 CA TYR A 225 5474 5341 4182 217 -249 -49 C ATOM 1563 C TYR A 225 38.092 14.470 127.824 1.00 39.71 C ANISOU 1563 C TYR A 225 5408 5477 4201 150 -253 -134 C ATOM 1564 O TYR A 225 37.842 13.558 128.618 1.00 39.15 O ANISOU 1564 O TYR A 225 5263 5397 4214 134 -222 -195 O ATOM 1565 CB TYR A 225 37.508 16.620 128.954 1.00 39.87 C ANISOU 1565 CB TYR A 225 5504 5392 4253 345 -312 11 C ATOM 1566 CG TYR A 225 36.256 16.706 128.091 1.00 41.04 C ANISOU 1566 CG TYR A 225 5596 5670 4326 387 -399 33 C ATOM 1567 CD1 TYR A 225 35.236 15.772 128.214 1.00 41.22 C ANISOU 1567 CD1 TYR A 225 5487 5800 4373 377 -417 -23 C ATOM 1568 CD2 TYR A 225 36.091 17.728 127.167 1.00 42.07 C ANISOU 1568 CD2 TYR A 225 5805 5820 4359 431 -468 115 C ATOM 1569 CE1 TYR A 225 34.093 15.848 127.434 1.00 42.38 C ANISOU 1569 CE1 TYR A 225 5571 6083 4448 410 -500 -3 C ATOM 1570 CE2 TYR A 225 34.947 17.811 126.388 1.00 43.22 C ANISOU 1570 CE2 TYR A 225 5895 6095 4433 476 -554 138 C ATOM 1571 CZ TYR A 225 33.956 16.867 126.525 1.00 43.36 C ANISOU 1571 CZ TYR A 225 5769 6230 4476 466 -569 76 C ATOM 1572 OH TYR A 225 32.821 16.936 125.750 1.00 44.60 O ANISOU 1572 OH TYR A 225 5858 6531 4558 504 -657 98 O ATOM 1573 N TYR A 226 37.873 14.357 126.512 1.00 40.62 N ANISOU 1573 N TYR A 226 5531 5692 4212 105 -295 -139 N ATOM 1574 CA TYR A 226 37.355 13.140 125.887 1.00 41.04 C ANISOU 1574 CA TYR A 226 5507 5846 4242 30 -307 -226 C ATOM 1575 C TYR A 226 38.457 12.231 125.348 1.00 40.83 C ANISOU 1575 C TYR A 226 5511 5808 4195 -72 -241 -313 C ATOM 1576 O TYR A 226 38.157 11.223 124.704 1.00 41.33 O ANISOU 1576 O TYR A 226 5533 5942 4226 -140 -251 -394 O ATOM 1577 CB TYR A 226 36.361 13.486 124.759 1.00 42.34 C ANISOU 1577 CB TYR A 226 5651 6143 4294 44 -399 -190 C ATOM 1578 CG TYR A 226 36.844 14.548 123.809 1.00 43.01 C ANISOU 1578 CG TYR A 226 5837 6236 4268 55 -427 -109 C ATOM 1579 CD1 TYR A 226 37.597 14.224 122.703 1.00 43.43 C ANISOU 1579 CD1 TYR A 226 5938 6338 4226 -38 -405 -144 C ATOM 1580 CD2 TYR A 226 36.554 15.880 124.031 1.00 43.33 C ANISOU 1580 CD2 TYR A 226 5933 6235 4295 158 -477 2 C ATOM 1581 CE1 TYR A 226 38.052 15.196 121.851 1.00 44.13 C ANISOU 1581 CE1 TYR A 226 6121 6442 4207 -41 -428 -62 C ATOM 1582 CE2 TYR A 226 37.003 16.854 123.189 1.00 44.05 C ANISOU 1582 CE2 TYR A 226 6131 6321 4285 158 -507 85 C ATOM 1583 CZ TYR A 226 37.747 16.506 122.100 1.00 44.44 C ANISOU 1583 CZ TYR A 226 6221 6428 4238 52 -482 58 C ATOM 1584 OH TYR A 226 38.197 17.480 121.259 1.00 45.27 O ANISOU 1584 OH TYR A 226 6433 6535 4233 39 -511 150 O ATOM 1585 N HIS A 227 39.705 12.538 125.665 1.00 40.24 N ANISOU 1585 N HIS A 227 5505 5650 4134 -82 -176 -300 N ATOM 1586 CA HIS A 227 40.829 11.698 125.309 1.00 40.01 C ANISOU 1586 CA HIS A 227 5492 5609 4102 -157 -103 -388 C ATOM 1587 C HIS A 227 41.402 11.035 126.535 1.00 38.95 C ANISOU 1587 C HIS A 227 5334 5370 4096 -150 -38 -436 C ATOM 1588 O HIS A 227 41.521 9.847 126.577 1.00 38.88 O ANISOU 1588 O HIS A 227 5293 5354 4126 -192 -8 -534 O ATOM 1589 CB HIS A 227 41.901 12.500 124.646 1.00 40.29 C ANISOU 1589 CB HIS A 227 5607 5651 4049 -184 -73 -342 C ATOM 1590 CG HIS A 227 41.561 12.881 123.262 1.00 41.48 C ANISOU 1590 CG HIS A 227 5790 5915 4055 -214 -126 -308 C ATOM 1591 ND1 HIS A 227 42.316 13.752 122.528 1.00 42.26 N ANISOU 1591 ND1 HIS A 227 5842 6110 4104 -219 -195 -334 N ATOM 1592 CD2 HIS A 227 40.543 12.504 122.468 1.00 42.13 C ANISOU 1592 CD2 HIS A 227 5945 6037 4025 -248 -123 -247 C ATOM 1593 CE1 HIS A 227 41.767 13.910 121.347 1.00 43.29 C ANISOU 1593 CE1 HIS A 227 6019 6333 4098 -246 -233 -291 C ATOM 1594 NE2 HIS A 227 40.689 13.166 121.288 1.00 43.24 N ANISOU 1594 NE2 HIS A 227 6087 6293 4050 -266 -189 -235 N ATOM 1595 N GLY A 228 41.750 11.827 127.536 1.00 38.23 N ANISOU 1595 N GLY A 228 5266 5191 4068 -97 -19 -369 N ATOM 1596 CA GLY A 228 42.222 11.320 128.794 1.00 37.27 C ANISOU 1596 CA GLY A 228 5122 4975 4062 -83 35 -399 C ATOM 1597 C GLY A 228 43.703 10.993 128.749 1.00 36.96 C ANISOU 1597 C GLY A 228 5114 4902 4027 -123 110 -442 C ATOM 1598 O GLY A 228 44.474 11.573 127.983 1.00 37.35 O ANISOU 1598 O GLY A 228 5211 4987 3993 -152 126 -418 O ATOM 1599 N PRO A 229 44.126 10.044 129.580 1.00 36.36 N ANISOU 1599 N PRO A 229 5007 4764 4044 -124 156 -505 N ATOM 1600 CA PRO A 229 45.555 9.724 129.662 1.00 36.12 C ANISOU 1600 CA PRO A 229 4993 4706 4025 -144 226 -546 C ATOM 1601 C PRO A 229 46.025 8.868 128.507 1.00 36.86 C ANISOU 1601 C PRO A 229 5086 4870 4051 -189 250 -640 C ATOM 1602 O PRO A 229 45.257 8.198 127.828 1.00 37.45 O ANISOU 1602 O PRO A 229 5147 4990 4094 -212 216 -694 O ATOM 1603 CB PRO A 229 45.691 8.942 130.983 1.00 35.36 C ANISOU 1603 CB PRO A 229 4864 4517 4053 -117 254 -577 C ATOM 1604 CG PRO A 229 44.331 8.797 131.497 1.00 35.26 C ANISOU 1604 CG PRO A 229 4819 4494 4086 -99 204 -557 C ATOM 1605 CD PRO A 229 43.436 9.760 130.867 1.00 35.73 C ANISOU 1605 CD PRO A 229 4887 4619 4071 -86 146 -493 C ATOM 1606 N GLY A 230 47.326 8.926 128.288 1.00 37.06 N ANISOU 1606 N GLY A 230 5122 4911 4046 -202 310 -660 N ATOM 1607 CA GLY A 230 48.028 7.973 127.460 1.00 38.21 C ANISOU 1607 CA GLY A 230 5259 5112 4146 -224 352 -768 C ATOM 1608 C GLY A 230 48.625 8.623 126.224 1.00 40.62 C ANISOU 1608 C GLY A 230 5587 5534 4312 -268 370 -753 C ATOM 1609 O GLY A 230 48.426 9.803 125.933 1.00 40.15 O ANISOU 1609 O GLY A 230 5560 5506 4189 -289 341 -653 O ATOM 1610 N ASN A 231 49.311 7.793 125.469 1.00 39.11 N ANISOU 1610 N ASN A 231 5382 5405 4072 -279 420 -857 N ATOM 1611 CA ASN A 231 49.901 8.127 124.193 1.00 40.13 C ANISOU 1611 CA ASN A 231 5524 5671 4054 -326 444 -870 C ATOM 1612 C ASN A 231 49.986 6.839 123.402 1.00 41.23 C ANISOU 1612 C ASN A 231 5654 5857 4153 -324 457 -1016 C ATOM 1613 O ASN A 231 49.630 5.819 123.901 1.00 40.81 O ANISOU 1613 O ASN A 231 5597 5719 4189 -294 437 -1091 O ATOM 1614 CB ASN A 231 51.174 8.945 124.283 1.00 42.50 C ANISOU 1614 CB ASN A 231 5808 6017 4324 -341 514 -836 C ATOM 1615 CG ASN A 231 52.327 8.177 124.783 1.00 45.37 C ANISOU 1615 CG ASN A 231 6123 6352 4764 -291 579 -932 C ATOM 1616 OD1 ASN A 231 53.278 8.705 125.287 1.00 49.55 O ANISOU 1616 OD1 ASN A 231 6639 6893 5295 -260 598 -1056 O ATOM 1617 ND2 ASN A 231 52.229 6.912 124.655 1.00 46.91 N ANISOU 1617 ND2 ASN A 231 6296 6505 5023 -279 609 -876 N ATOM 1618 N GLU A 232 50.435 6.877 122.168 1.00 44.31 N ANISOU 1618 N GLU A 232 6047 6382 4406 -359 490 -1061 N ATOM 1619 CA GLU A 232 50.379 5.681 121.326 1.00 48.35 C ANISOU 1619 CA GLU A 232 6562 6941 4868 -354 501 -1212 C ATOM 1620 C GLU A 232 51.154 4.520 121.940 1.00 44.65 C ANISOU 1620 C GLU A 232 6071 6399 4496 -285 555 -1330 C ATOM 1621 O GLU A 232 50.830 3.351 121.697 1.00 45.91 O ANISOU 1621 O GLU A 232 6249 6519 4676 -264 542 -1454 O ATOM 1622 CB GLU A 232 50.906 5.980 119.914 1.00 54.80 C ANISOU 1622 CB GLU A 232 7383 7934 5505 -402 534 -1238 C ATOM 1623 CG GLU A 232 50.135 7.072 119.183 1.00 60.20 C ANISOU 1623 CG GLU A 232 8101 8694 6079 -468 472 -1122 C ATOM 1624 CD GLU A 232 50.820 8.434 119.270 1.00 62.90 C ANISOU 1624 CD GLU A 232 8449 9080 6370 -506 496 -980 C ATOM 1625 OE1 GLU A 232 51.368 8.895 118.247 1.00 66.33 O ANISOU 1625 OE1 GLU A 232 8891 9659 6654 -563 526 -963 O ATOM 1626 OE2 GLU A 232 50.820 9.042 120.366 1.00 63.90 O ANISOU 1626 OE2 GLU A 232 8577 9099 6604 -486 485 -886 O ATOM 1627 N LYS A 233 52.167 4.818 122.742 1.00 46.43 N ANISOU 1627 N LYS A 233 6260 6601 4780 -250 609 -1292 N ATOM 1628 CA LYS A 233 52.954 3.795 123.409 1.00 44.93 C ANISOU 1628 CA LYS A 233 6045 6341 4685 -171 655 -1389 C ATOM 1629 C LYS A 233 52.559 3.565 124.855 1.00 47.54 C ANISOU 1629 C LYS A 233 6379 6505 5180 -133 624 -1342 C ATOM 1630 O LYS A 233 52.911 2.521 125.418 1.00 53.96 O ANISOU 1630 O LYS A 233 7190 7230 6082 -67 640 -1426 O ATOM 1631 CB LYS A 233 54.433 4.163 123.352 1.00 44.26 C ANISOU 1631 CB LYS A 233 5904 6362 4552 -152 738 -1389 C ATOM 1632 CG LYS A 233 55.103 3.685 122.095 1.00 45.40 C ANISOU 1632 CG LYS A 233 6030 6657 4562 -145 793 -1508 C ATOM 1633 CD LYS A 233 55.930 4.801 121.528 1.00 45.38 C ANISOU 1633 CD LYS A 233 5987 6823 4433 -210 843 -1428 C ATOM 1634 CE LYS A 233 56.690 4.333 120.326 1.00 46.27 C ANISOU 1634 CE LYS A 233 6069 7110 4404 -200 910 -1548 C ATOM 1635 NZ LYS A 233 57.772 5.282 120.022 1.00 46.76 N ANISOU 1635 NZ LYS A 233 6068 7339 4361 -257 975 -1476 N ATOM 1636 N SER A 234 51.844 4.497 125.469 1.00 43.86 N ANISOU 1636 N SER A 234 5921 5992 4751 -168 578 -1213 N ATOM 1637 CA SER A 234 51.488 4.405 126.873 1.00 40.63 C ANISOU 1637 CA SER A 234 5509 5444 4485 -136 553 -1159 C ATOM 1638 C SER A 234 50.010 4.049 126.936 1.00 39.08 C ANISOU 1638 C SER A 234 5341 5182 4324 -162 480 -1156 C ATOM 1639 O SER A 234 49.145 4.907 127.123 1.00 39.12 O ANISOU 1639 O SER A 234 5351 5188 4325 -191 433 -1057 O ATOM 1640 CB SER A 234 51.810 5.708 127.600 1.00 38.33 C ANISOU 1640 CB SER A 234 5203 5152 4208 -150 559 -1026 C ATOM 1641 OG SER A 234 53.114 6.165 127.271 1.00 38.73 O ANISOU 1641 OG SER A 234 5224 5300 4192 -157 622 -1022 O ATOM 1642 N ARG A 235 49.734 2.758 126.788 1.00 42.05 N ANISOU 1642 N ARG A 235 5739 5504 4736 -149 469 -1268 N ATOM 1643 CA ARG A 235 48.371 2.254 126.811 1.00 41.22 C ANISOU 1643 CA ARG A 235 5654 5345 4661 -189 400 -1278 C ATOM 1644 C ARG A 235 47.806 2.327 128.216 1.00 41.17 C ANISOU 1644 C ARG A 235 5634 5229 4779 -178 374 -1196 C ATOM 1645 O ARG A 235 48.467 1.926 129.176 1.00 44.39 O ANISOU 1645 O ARG A 235 6038 5550 5278 -131 405 -1200 O ATOM 1646 CB ARG A 235 48.351 0.812 126.317 1.00 43.10 C ANISOU 1646 CB ARG A 235 5932 5539 4905 -187 396 -1424 C ATOM 1647 CG ARG A 235 48.708 0.696 124.836 1.00 46.58 C ANISOU 1647 CG ARG A 235 6389 6103 5207 -203 415 -1517 C ATOM 1648 CD ARG A 235 47.550 1.126 124.000 1.00 48.60 C ANISOU 1648 CD ARG A 235 6650 6441 5373 -280 352 -1488 C ATOM 1649 NE ARG A 235 47.872 1.864 122.786 1.00 49.69 N ANISOU 1649 NE ARG A 235 6783 6736 5360 -304 370 -1482 N ATOM 1650 CZ ARG A 235 46.953 2.285 121.914 1.00 50.93 C ANISOU 1650 CZ ARG A 235 6947 6986 5419 -365 313 -1455 C ATOM 1651 NH1 ARG A 235 47.334 2.962 120.820 1.00 52.25 N ANISOU 1651 NH1 ARG A 235 7115 7297 5441 -389 331 -1443 N ATOM 1652 NH2 ARG A 235 45.643 2.057 122.122 1.00 53.78 N ANISOU 1652 NH2 ARG A 235 7307 7308 5818 -408 237 -1435 N ATOM 1653 N THR A 236 46.580 2.829 128.339 1.00 43.79 N ANISOU 1653 N THR A 236 5954 5575 5109 -218 316 -1124 N ATOM 1654 CA THR A 236 45.892 2.828 129.621 1.00 40.03 C ANISOU 1654 CA THR A 236 5459 5013 4739 -213 290 -1055 C ATOM 1655 C THR A 236 44.397 2.908 129.368 1.00 39.42 C ANISOU 1655 C THR A 236 5362 4977 4638 -266 220 -1027 C ATOM 1656 O THR A 236 43.939 3.759 128.603 1.00 38.72 O ANISOU 1656 O THR A 236 5263 4988 4460 -280 192 -985 O ATOM 1657 CB THR A 236 46.370 3.985 130.526 1.00 36.60 C ANISOU 1657 CB THR A 236 5003 4568 4334 -169 315 -946 C ATOM 1658 OG1 THR A 236 45.449 4.168 131.603 1.00 36.09 O ANISOU 1658 OG1 THR A 236 4915 4453 4344 -167 282 -875 O ATOM 1659 CG2 THR A 236 46.498 5.278 129.756 1.00 37.03 C ANISOU 1659 CG2 THR A 236 5060 4722 4286 -176 313 -883 C ATOM 1660 N ASP A 237 43.645 2.017 130.001 1.00 37.98 N ANISOU 1660 N ASP A 237 5174 4726 4532 -298 191 -1047 N ATOM 1661 CA ASP A 237 42.206 1.958 129.809 1.00 38.42 C ANISOU 1661 CA ASP A 237 5196 4834 4568 -359 125 -1027 C ATOM 1662 C ASP A 237 41.463 3.017 130.603 1.00 37.72 C ANISOU 1662 C ASP A 237 5052 4781 4500 -331 104 -908 C ATOM 1663 O ASP A 237 40.242 2.937 130.733 1.00 38.05 O ANISOU 1663 O ASP A 237 5045 4868 4543 -371 53 -882 O ATOM 1664 CB ASP A 237 41.687 0.563 130.157 1.00 38.99 C ANISOU 1664 CB ASP A 237 5285 4823 4705 -423 100 -1093 C ATOM 1665 CG ASP A 237 42.192 -0.504 129.190 1.00 40.06 C ANISOU 1665 CG ASP A 237 5488 4928 4806 -451 105 -1226 C ATOM 1666 OD1 ASP A 237 42.671 -0.146 128.090 1.00 41.50 O ANISOU 1666 OD1 ASP A 237 5685 5192 4892 -436 118 -1268 O ATOM 1667 OD2 ASP A 237 42.103 -1.703 129.529 1.00 43.76 O ANISOU 1667 OD2 ASP A 237 5998 5290 5338 -490 93 -1289 O ATOM 1668 N TYR A 238 42.174 3.996 131.148 1.00 36.89 N ANISOU 1668 N TYR A 238 4949 4659 4408 -264 141 -839 N ATOM 1669 CA TYR A 238 41.541 5.202 131.653 1.00 36.43 C ANISOU 1669 CA TYR A 238 4854 4643 4345 -222 118 -734 C ATOM 1670 C TYR A 238 41.317 6.218 130.550 1.00 36.87 C ANISOU 1670 C TYR A 238 4917 4799 4291 -211 87 -699 C ATOM 1671 O TYR A 238 40.571 7.178 130.747 1.00 36.81 O ANISOU 1671 O TYR A 238 4884 4836 4265 -173 50 -620 O ATOM 1672 CB TYR A 238 42.398 5.847 132.747 1.00 35.46 C ANISOU 1672 CB TYR A 238 4745 4448 4281 -160 165 -677 C ATOM 1673 CG TYR A 238 42.388 5.153 134.096 1.00 34.97 C ANISOU 1673 CG TYR A 238 4665 4297 4324 -157 185 -675 C ATOM 1674 CD1 TYR A 238 41.243 5.123 134.868 1.00 34.95 C ANISOU 1674 CD1 TYR A 238 4610 4309 4359 -165 155 -632 C ATOM 1675 CD2 TYR A 238 43.543 4.564 134.610 1.00 34.62 C ANISOU 1675 CD2 TYR A 238 4652 4165 4336 -143 234 -709 C ATOM 1676 CE1 TYR A 238 41.238 4.500 136.096 1.00 34.59 C ANISOU 1676 CE1 TYR A 238 4552 4191 4399 -170 174 -622 C ATOM 1677 CE2 TYR A 238 43.543 3.947 135.829 1.00 34.26 C ANISOU 1677 CE2 TYR A 238 4597 4039 4380 -140 247 -698 C ATOM 1678 CZ TYR A 238 42.395 3.918 136.570 1.00 34.23 C ANISOU 1678 CZ TYR A 238 4550 4049 4408 -159 218 -652 C ATOM 1679 OH TYR A 238 42.388 3.299 137.786 1.00 33.97 O ANISOU 1679 OH TYR A 238 4510 3943 4455 -165 231 -634 O ATOM 1680 N GLY A 239 41.956 6.037 129.408 1.00 37.40 N ANISOU 1680 N GLY A 239 5023 4906 4282 -238 99 -755 N ATOM 1681 CA GLY A 239 41.927 7.028 128.362 1.00 37.87 C ANISOU 1681 CA GLY A 239 5102 5056 4229 -232 75 -713 C ATOM 1682 C GLY A 239 41.685 6.419 126.990 1.00 38.93 C ANISOU 1682 C GLY A 239 5246 5278 4269 -292 48 -790 C ATOM 1683 O GLY A 239 41.044 5.375 126.832 1.00 39.44 O ANISOU 1683 O GLY A 239 5290 5347 4349 -341 21 -863 O ATOM 1684 N ARG A 240 42.240 7.100 125.999 1.00 39.36 N ANISOU 1684 N ARG A 240 5337 5401 4217 -295 56 -773 N ATOM 1685 CA ARG A 240 41.922 6.878 124.598 1.00 40.48 C ANISOU 1685 CA ARG A 240 5489 5652 4237 -345 21 -821 C ATOM 1686 C ARG A 240 42.635 5.660 124.023 1.00 41.01 C ANISOU 1686 C ARG A 240 5580 5715 4286 -386 64 -958 C ATOM 1687 O ARG A 240 42.048 4.905 123.241 1.00 41.92 O ANISOU 1687 O ARG A 240 5694 5884 4349 -438 26 -1037 O ATOM 1688 CB ARG A 240 42.281 8.146 123.830 1.00 40.79 C ANISOU 1688 CB ARG A 240 5566 5766 4166 -333 14 -736 C ATOM 1689 CG ARG A 240 42.326 8.008 122.377 1.00 41.93 C ANISOU 1689 CG ARG A 240 5733 6028 4171 -384 -3 -782 C ATOM 1690 CD ARG A 240 42.378 9.363 121.721 1.00 42.34 C ANISOU 1690 CD ARG A 240 5823 6150 4115 -375 -31 -668 C ATOM 1691 NE ARG A 240 43.553 10.135 122.097 1.00 41.83 N ANISOU 1691 NE ARG A 240 5798 6036 4059 -360 31 -609 N ATOM 1692 CZ ARG A 240 44.001 11.157 121.376 1.00 44.18 C ANISOU 1692 CZ ARG A 240 6147 6392 4247 -380 28 -527 C ATOM 1693 NH1 ARG A 240 43.368 11.490 120.258 1.00 45.96 N ANISOU 1693 NH1 ARG A 240 6391 6725 4348 -405 -34 -497 N ATOM 1694 NH2 ARG A 240 45.081 11.828 121.743 1.00 44.89 N ANISOU 1694 NH2 ARG A 240 6271 6439 4345 -384 82 -474 N ATOM 1695 N TYR A 241 43.894 5.453 124.390 1.00 40.57 N ANISOU 1695 N TYR A 241 5545 5600 4270 -360 139 -991 N ATOM 1696 CA TYR A 241 44.718 4.392 123.815 1.00 41.21 C ANISOU 1696 CA TYR A 241 5651 5681 4326 -374 187 -1124 C ATOM 1697 C TYR A 241 44.524 3.129 124.640 1.00 41.03 C ANISOU 1697 C TYR A 241 5628 5538 4425 -371 188 -1202 C ATOM 1698 O TYR A 241 45.207 2.901 125.638 1.00 40.31 O ANISOU 1698 O TYR A 241 5535 5350 4433 -327 232 -1197 O ATOM 1699 CB TYR A 241 46.175 4.827 123.778 1.00 41.01 C ANISOU 1699 CB TYR A 241 5636 5672 4275 -341 266 -1118 C ATOM 1700 CG TYR A 241 46.391 6.194 123.168 1.00 41.14 C ANISOU 1700 CG TYR A 241 5662 5786 4184 -356 264 -1014 C ATOM 1701 CD1 TYR A 241 46.335 7.330 123.947 1.00 40.31 C ANISOU 1701 CD1 TYR A 241 5556 5640 4120 -332 253 -884 C ATOM 1702 CD2 TYR A 241 46.657 6.345 121.813 1.00 42.22 C ANISOU 1702 CD2 TYR A 241 5818 6052 4172 -396 270 -1046 C ATOM 1703 CE1 TYR A 241 46.537 8.583 123.407 1.00 40.57 C ANISOU 1703 CE1 TYR A 241 5616 5741 4056 -351 244 -784 C ATOM 1704 CE2 TYR A 241 46.861 7.601 121.259 1.00 42.46 C ANISOU 1704 CE2 TYR A 241 5868 6166 4099 -419 264 -939 C ATOM 1705 CZ TYR A 241 46.799 8.718 122.069 1.00 41.64 C ANISOU 1705 CZ TYR A 241 5773 6003 4047 -398 248 -806 C ATOM 1706 OH TYR A 241 46.999 9.981 121.552 1.00 42.00 O ANISOU 1706 OH TYR A 241 5856 6108 3994 -425 235 -693 O ATOM 1707 N ARG A 242 43.585 2.290 124.216 1.00 41.80 N ANISOU 1707 N ARG A 242 5731 5641 4510 -426 134 -1270 N ATOM 1708 CA ARG A 242 43.189 1.139 125.011 1.00 41.78 C ANISOU 1708 CA ARG A 242 5736 5518 4619 -445 119 -1326 C ATOM 1709 C ARG A 242 44.241 0.044 124.961 1.00 42.21 C ANISOU 1709 C ARG A 242 5844 5489 4706 -417 172 -1450 C ATOM 1710 O ARG A 242 44.940 -0.126 123.960 1.00 42.99 O ANISOU 1710 O ARG A 242 5971 5651 4714 -406 203 -1535 O ATOM 1711 CB ARG A 242 41.861 0.591 124.518 1.00 42.66 C ANISOU 1711 CB ARG A 242 5839 5670 4698 -531 40 -1361 C ATOM 1712 CG ARG A 242 40.926 1.669 124.061 1.00 42.71 C ANISOU 1712 CG ARG A 242 5796 5808 4626 -548 -15 -1265 C ATOM 1713 CD ARG A 242 40.477 2.491 125.221 1.00 41.65 C ANISOU 1713 CD ARG A 242 5607 5646 4571 -506 -23 -1136 C ATOM 1714 NE ARG A 242 39.716 1.679 126.150 1.00 41.57 N ANISOU 1714 NE ARG A 242 5571 5561 4662 -546 -48 -1144 N ATOM 1715 CZ ARG A 242 39.135 2.155 127.239 1.00 40.84 C ANISOU 1715 CZ ARG A 242 5423 5451 4643 -522 -58 -1049 C ATOM 1716 NH1 ARG A 242 38.459 1.340 128.032 1.00 40.94 N ANISOU 1716 NH1 ARG A 242 5411 5407 4736 -574 -78 -1058 N ATOM 1717 NH2 ARG A 242 39.241 3.445 127.530 1.00 40.13 N ANISOU 1717 NH2 ARG A 242 5309 5398 4539 -448 -48 -946 N ATOM 1718 N THR A 243 44.336 -0.717 126.058 1.00 41.82 N ANISOU 1718 N THR A 243 5809 5300 4783 -399 180 -1461 N ATOM 1719 CA THR A 243 45.315 -1.799 126.128 1.00 42.47 C ANISOU 1719 CA THR A 243 5947 5283 4908 -354 222 -1575 C ATOM 1720 C THR A 243 45.046 -2.864 125.074 1.00 43.81 C ANISOU 1720 C THR A 243 6179 5450 5016 -401 193 -1720 C ATOM 1721 O THR A 243 45.973 -3.555 124.642 1.00 44.57 O ANISOU 1721 O THR A 243 6324 5515 5095 -348 233 -1836 O ATOM 1722 CB THR A 243 45.339 -2.427 127.531 1.00 42.23 C ANISOU 1722 CB THR A 243 5929 5095 5023 -332 223 -1546 C ATOM 1723 OG1 THR A 243 44.023 -2.844 127.915 1.00 42.71 O ANISOU 1723 OG1 THR A 243 5988 5115 5126 -421 156 -1518 O ATOM 1724 CG2 THR A 243 45.870 -1.441 128.558 1.00 40.41 C ANISOU 1724 CG2 THR A 243 5645 4865 4845 -272 263 -1425 C ATOM 1725 N SER A 244 43.795 -3.000 124.630 1.00 44.36 N ANISOU 1725 N SER A 244 6246 5561 5047 -498 121 -1721 N ATOM 1726 CA SER A 244 43.496 -3.919 123.538 1.00 46.13 C ANISOU 1726 CA SER A 244 6533 5798 5196 -557 86 -1860 C ATOM 1727 C SER A 244 44.154 -3.508 122.232 1.00 47.17 C ANISOU 1727 C SER A 244 6670 6069 5184 -528 121 -1924 C ATOM 1728 O SER A 244 44.223 -4.325 121.311 1.00 51.09 O ANISOU 1728 O SER A 244 7229 6573 5612 -552 110 -2065 O ATOM 1729 CB SER A 244 41.986 -4.027 123.322 1.00 46.37 C ANISOU 1729 CB SER A 244 6542 5873 5203 -678 -2 -1835 C ATOM 1730 OG SER A 244 41.454 -2.808 122.833 1.00 46.00 O ANISOU 1730 OG SER A 244 6421 5991 5066 -692 -24 -1738 O ATOM 1731 N GLY A 245 44.639 -2.280 122.128 1.00 48.48 N ANISOU 1731 N GLY A 245 6778 6345 5296 -484 161 -1828 N ATOM 1732 CA GLY A 245 45.236 -1.775 120.917 1.00 48.24 C ANISOU 1732 CA GLY A 245 6746 6463 5119 -471 195 -1865 C ATOM 1733 C GLY A 245 44.357 -0.810 120.153 1.00 51.11 C ANISOU 1733 C GLY A 245 7073 6976 5369 -536 141 -1782 C ATOM 1734 O GLY A 245 44.862 -0.073 119.299 1.00 55.10 O ANISOU 1734 O GLY A 245 7570 7615 5752 -527 171 -1764 O ATOM 1735 N GLU A 246 43.061 -0.802 120.438 1.00 48.33 N ANISOU 1735 N GLU A 246 6699 6613 5050 -601 62 -1727 N ATOM 1736 CA GLU A 246 42.148 0.123 119.799 1.00 46.64 C ANISOU 1736 CA GLU A 246 6443 6540 4737 -648 1 -1639 C ATOM 1737 C GLU A 246 42.386 1.534 120.314 1.00 45.47 C ANISOU 1737 C GLU A 246 6250 6425 4600 -592 23 -1479 C ATOM 1738 O GLU A 246 42.757 1.739 121.468 1.00 44.34 O ANISOU 1738 O GLU A 246 6091 6182 4574 -541 59 -1418 O ATOM 1739 CB GLU A 246 40.707 -0.309 120.057 1.00 52.22 C ANISOU 1739 CB GLU A 246 7124 7234 5485 -726 -88 -1627 C ATOM 1740 CG GLU A 246 39.690 0.811 120.003 1.00 51.31 C ANISOU 1740 CG GLU A 246 6938 7232 5326 -739 -151 -1490 C ATOM 1741 CD GLU A 246 38.261 0.289 120.025 1.00 52.37 C ANISOU 1741 CD GLU A 246 7031 7396 5470 -828 -242 -1499 C ATOM 1742 OE1 GLU A 246 37.399 0.850 119.326 1.00 53.99 O ANISOU 1742 OE1 GLU A 246 7193 7743 5579 -860 -310 -1452 O ATOM 1743 OE2 GLU A 246 37.998 -0.691 120.741 1.00 56.71 O ANISOU 1743 OE2 GLU A 246 7592 7833 6123 -870 -247 -1551 O ATOM 1744 N THR A 247 42.204 2.514 119.437 1.00 45.85 N ANISOU 1744 N THR A 247 6287 6611 4521 -604 -1 -1412 N ATOM 1745 CA THR A 247 42.254 3.920 119.811 1.00 45.00 C ANISOU 1745 CA THR A 247 6154 6532 4412 -561 0 -1255 C ATOM 1746 C THR A 247 40.870 4.514 119.603 1.00 45.29 C ANISOU 1746 C THR A 247 6152 6646 4410 -585 -95 -1168 C ATOM 1747 O THR A 247 40.334 4.464 118.497 1.00 46.41 O ANISOU 1747 O THR A 247 6298 6906 4430 -635 -148 -1197 O ATOM 1748 CB THR A 247 43.300 4.679 118.991 1.00 45.33 C ANISOU 1748 CB THR A 247 6224 6666 4334 -549 52 -1230 C ATOM 1749 OG1 THR A 247 44.589 4.084 119.182 1.00 45.21 O ANISOU 1749 OG1 THR A 247 6227 6600 4351 -519 142 -1319 O ATOM 1750 CG2 THR A 247 43.368 6.131 119.422 1.00 44.57 C ANISOU 1750 CG2 THR A 247 6120 6573 4240 -513 47 -1066 C ATOM 1751 N LEU A 248 40.290 5.061 120.662 1.00 44.38 N ANISOU 1751 N LEU A 248 5996 6474 4393 -546 -119 -1065 N ATOM 1752 CA LEU A 248 38.964 5.652 120.600 1.00 44.69 C ANISOU 1752 CA LEU A 248 5984 6589 4406 -547 -208 -980 C ATOM 1753 C LEU A 248 39.035 7.095 120.121 1.00 44.79 C ANISOU 1753 C LEU A 248 6014 6675 4327 -501 -230 -855 C ATOM 1754 O LEU A 248 40.059 7.766 120.240 1.00 44.28 O ANISOU 1754 O LEU A 248 5994 6572 4256 -466 -173 -808 O ATOM 1755 CB LEU A 248 38.283 5.607 121.965 1.00 43.83 C ANISOU 1755 CB LEU A 248 5819 6398 4436 -516 -222 -930 C ATOM 1756 CG LEU A 248 38.181 4.258 122.663 1.00 43.68 C ANISOU 1756 CG LEU A 248 5789 6284 4524 -564 -203 -1026 C ATOM 1757 CD1 LEU A 248 37.387 4.388 123.949 1.00 42.99 C ANISOU 1757 CD1 LEU A 248 5636 6150 4549 -539 -222 -955 C ATOM 1758 CD2 LEU A 248 37.548 3.249 121.727 1.00 44.98 C ANISOU 1758 CD2 LEU A 248 5954 6516 4621 -660 -255 -1133 C ATOM 1759 N ASP A 249 37.919 7.567 119.565 1.00 45.58 N ANISOU 1759 N ASP A 249 6081 6885 4353 -503 -320 -799 N ATOM 1760 CA ASP A 249 37.798 8.985 119.253 1.00 48.19 C ANISOU 1760 CA ASP A 249 6433 7266 4611 -445 -358 -663 C ATOM 1761 C ASP A 249 37.370 9.777 120.476 1.00 44.87 C ANISOU 1761 C ASP A 249 5984 6766 4299 -356 -370 -559 C ATOM 1762 O ASP A 249 37.798 10.918 120.666 1.00 44.55 O ANISOU 1762 O ASP A 249 5993 6686 4250 -296 -362 -457 O ATOM 1763 CB ASP A 249 36.794 9.197 118.122 1.00 53.97 C ANISOU 1763 CB ASP A 249 7143 8153 5210 -470 -455 -641 C ATOM 1764 CG ASP A 249 37.262 8.612 116.823 1.00 57.25 C ANISOU 1764 CG ASP A 249 7599 8660 5492 -554 -445 -733 C ATOM 1765 OD1 ASP A 249 38.482 8.657 116.579 1.00 61.44 O ANISOU 1765 OD1 ASP A 249 8192 9159 5993 -566 -366 -758 O ATOM 1766 OD2 ASP A 249 36.415 8.106 116.050 1.00 58.06 O ANISOU 1766 OD2 ASP A 249 7667 8876 5516 -608 -515 -784 O ATOM 1767 N ASN A 250 36.526 9.183 121.307 1.00 44.58 N ANISOU 1767 N ASN A 250 5870 6707 4359 -351 -391 -586 N ATOM 1768 CA ASN A 250 35.948 9.852 122.460 1.00 43.93 C ANISOU 1768 CA ASN A 250 5745 6575 4371 -264 -407 -500 C ATOM 1769 C ASN A 250 35.697 8.781 123.505 1.00 43.31 C ANISOU 1769 C ASN A 250 5606 6432 4417 -296 -374 -570 C ATOM 1770 O ASN A 250 34.915 7.859 123.266 1.00 43.96 O ANISOU 1770 O ASN A 250 5630 6580 4494 -366 -412 -636 O ATOM 1771 CB ASN A 250 34.654 10.573 122.075 1.00 44.89 C ANISOU 1771 CB ASN A 250 5810 6817 4428 -210 -508 -421 C ATOM 1772 CG ASN A 250 34.053 11.348 123.223 1.00 44.40 C ANISOU 1772 CG ASN A 250 5705 6715 4451 -100 -524 -337 C ATOM 1773 OD1 ASN A 250 33.925 10.841 124.334 1.00 43.65 O ANISOU 1773 OD1 ASN A 250 5560 6559 4467 -98 -486 -366 O ATOM 1774 ND2 ASN A 250 33.679 12.588 122.960 1.00 44.94 N ANISOU 1774 ND2 ASN A 250 5797 6816 4461 -3 -582 -232 N ATOM 1775 N ILE A 251 36.358 8.900 124.658 1.00 42.15 N ANISOU 1775 N ILE A 251 5479 6160 4377 -254 -309 -553 N ATOM 1776 CA ILE A 251 36.324 7.838 125.659 1.00 41.57 C ANISOU 1776 CA ILE A 251 5367 6009 4419 -291 -270 -616 C ATOM 1777 C ILE A 251 34.977 7.712 126.344 1.00 41.82 C ANISOU 1777 C ILE A 251 5296 6096 4496 -282 -320 -587 C ATOM 1778 O ILE A 251 34.749 6.736 127.060 1.00 41.62 O ANISOU 1778 O ILE A 251 5233 6030 4551 -337 -301 -637 O ATOM 1779 CB ILE A 251 37.419 8.045 126.721 1.00 40.34 C ANISOU 1779 CB ILE A 251 5257 5714 4356 -246 -190 -598 C ATOM 1780 CG1 ILE A 251 37.153 9.309 127.524 1.00 39.85 C ANISOU 1780 CG1 ILE A 251 5187 5631 4324 -144 -201 -488 C ATOM 1781 CG2 ILE A 251 38.764 8.157 126.070 1.00 40.21 C ANISOU 1781 CG2 ILE A 251 5324 5664 4291 -260 -136 -626 C ATOM 1782 CD1 ILE A 251 38.017 9.421 128.776 1.00 38.69 C ANISOU 1782 CD1 ILE A 251 5068 5355 4279 -107 -131 -474 C ATOM 1783 N PHE A 252 34.074 8.661 126.137 1.00 42.37 N ANISOU 1783 N PHE A 252 5319 6266 4514 -214 -385 -508 N ATOM 1784 CA PHE A 252 32.741 8.576 126.711 1.00 42.83 C ANISOU 1784 CA PHE A 252 5260 6411 4601 -199 -434 -483 C ATOM 1785 C PHE A 252 31.746 7.871 125.803 1.00 45.25 C ANISOU 1785 C PHE A 252 5494 6863 4835 -290 -507 -530 C ATOM 1786 O PHE A 252 30.645 7.539 126.255 1.00 47.90 O ANISOU 1786 O PHE A 252 5718 7286 5194 -311 -544 -525 O ATOM 1787 CB PHE A 252 32.246 9.977 127.060 1.00 43.68 C ANISOU 1787 CB PHE A 252 5346 6554 4695 -57 -469 -376 C ATOM 1788 CG PHE A 252 33.098 10.658 128.086 1.00 43.08 C ANISOU 1788 CG PHE A 252 5336 6337 4695 25 -404 -333 C ATOM 1789 CD1 PHE A 252 32.882 10.441 129.432 1.00 42.08 C ANISOU 1789 CD1 PHE A 252 5157 6165 4668 49 -366 -330 C ATOM 1790 CD2 PHE A 252 34.140 11.479 127.704 1.00 43.25 C ANISOU 1790 CD2 PHE A 252 5472 6278 4682 62 -381 -296 C ATOM 1791 CE1 PHE A 252 33.666 11.045 130.368 1.00 41.45 C ANISOU 1791 CE1 PHE A 252 5138 5960 4650 118 -310 -296 C ATOM 1792 CE2 PHE A 252 34.933 12.082 128.650 1.00 42.58 C ANISOU 1792 CE2 PHE A 252 5448 6067 4664 122 -326 -260 C ATOM 1793 CZ PHE A 252 34.695 11.865 129.981 1.00 41.53 C ANISOU 1793 CZ PHE A 252 5263 5887 4628 153 -292 -263 C ATOM 1794 N GLY A 253 32.111 7.619 124.547 1.00 44.74 N ANISOU 1794 N GLY A 253 5487 6834 4677 -351 -527 -578 N ATOM 1795 CA GLY A 253 31.236 6.852 123.684 1.00 46.02 C ANISOU 1795 CA GLY A 253 5591 7128 4768 -453 -596 -637 C ATOM 1796 C GLY A 253 30.967 5.463 124.223 1.00 46.09 C ANISOU 1796 C GLY A 253 5564 7098 4852 -574 -578 -724 C ATOM 1797 O GLY A 253 29.846 4.961 124.137 1.00 47.08 O ANISOU 1797 O GLY A 253 5591 7338 4959 -647 -640 -740 O ATOM 1798 N ILE A 254 31.989 4.827 124.796 1.00 45.17 N ANISOU 1798 N ILE A 254 5524 6819 4818 -600 -498 -777 N ATOM 1799 CA ILE A 254 31.824 3.485 125.337 1.00 45.30 C ANISOU 1799 CA ILE A 254 5531 6771 4911 -713 -483 -855 C ATOM 1800 C ILE A 254 30.965 3.455 126.586 1.00 45.10 C ANISOU 1800 C ILE A 254 5403 6765 4970 -710 -487 -797 C ATOM 1801 O ILE A 254 30.615 2.366 127.050 1.00 45.45 O ANISOU 1801 O ILE A 254 5427 6775 5068 -821 -487 -845 O ATOM 1802 CB ILE A 254 33.189 2.845 125.649 1.00 44.46 C ANISOU 1802 CB ILE A 254 5538 6482 4871 -721 -400 -921 C ATOM 1803 CG1 ILE A 254 33.927 3.662 126.708 1.00 43.06 C ANISOU 1803 CG1 ILE A 254 5379 6209 4772 -604 -333 -843 C ATOM 1804 CG2 ILE A 254 34.025 2.752 124.400 1.00 44.85 C ANISOU 1804 CG2 ILE A 254 5678 6532 4830 -732 -391 -993 C ATOM 1805 CD1 ILE A 254 35.306 3.137 127.043 1.00 42.26 C ANISOU 1805 CD1 ILE A 254 5376 5949 4734 -596 -254 -899 C ATOM 1806 N LEU A 255 30.614 4.615 127.140 1.00 44.68 N ANISOU 1806 N LEU A 255 5289 6764 4923 -587 -490 -697 N ATOM 1807 CA LEU A 255 29.776 4.689 128.329 1.00 44.59 C ANISOU 1807 CA LEU A 255 5170 6795 4979 -568 -488 -642 C ATOM 1808 C LEU A 255 28.316 4.944 128.007 1.00 45.88 C ANISOU 1808 C LEU A 255 5190 7166 5076 -576 -572 -607 C ATOM 1809 O LEU A 255 27.486 4.937 128.924 1.00 46.09 O ANISOU 1809 O LEU A 255 5104 7264 5144 -571 -574 -567 O ATOM 1810 CB LEU A 255 30.275 5.788 129.272 1.00 43.44 C ANISOU 1810 CB LEU A 255 5042 6576 4885 -417 -437 -562 C ATOM 1811 CG LEU A 255 31.668 5.622 129.873 1.00 42.13 C ANISOU 1811 CG LEU A 255 4993 6220 4796 -399 -352 -582 C ATOM 1812 CD1 LEU A 255 32.114 6.928 130.473 1.00 41.27 C ANISOU 1812 CD1 LEU A 255 4911 6065 4705 -250 -321 -503 C ATOM 1813 CD2 LEU A 255 31.665 4.521 130.916 1.00 41.86 C ANISOU 1813 CD2 LEU A 255 4943 6106 4857 -485 -312 -613 C ATOM 1814 N ILE A 256 27.996 5.190 126.734 1.00 46.83 N ANISOU 1814 N ILE A 256 5307 7397 5089 -586 -640 -618 N ATOM 1815 CA ILE A 256 26.611 5.305 126.303 1.00 48.26 C ANISOU 1815 CA ILE A 256 5347 7793 5198 -607 -729 -595 C ATOM 1816 C ILE A 256 25.864 4.039 126.687 1.00 49.04 C ANISOU 1816 C ILE A 256 5361 7940 5330 -778 -744 -647 C ATOM 1817 O ILE A 256 26.416 2.934 126.656 1.00 48.89 O ANISOU 1817 O ILE A 256 5428 7799 5350 -907 -714 -728 O ATOM 1818 CB ILE A 256 26.562 5.568 124.787 1.00 49.20 C ANISOU 1818 CB ILE A 256 5498 8004 5190 -616 -799 -613 C ATOM 1819 CG1 ILE A 256 27.315 6.857 124.460 1.00 48.52 C ANISOU 1819 CG1 ILE A 256 5504 7862 5070 -458 -784 -546 C ATOM 1820 CG2 ILE A 256 25.131 5.668 124.290 1.00 50.81 C ANISOU 1820 CG2 ILE A 256 5550 8444 5313 -639 -900 -589 C ATOM 1821 CD1 ILE A 256 27.580 7.075 123.010 1.00 49.25 C ANISOU 1821 CD1 ILE A 256 5665 8009 5039 -475 -833 -563 C ATOM 1822 N GLY A 257 24.608 4.199 127.078 1.00 53.46 N ANISOU 1822 N GLY A 257 5756 8680 5877 -777 -790 -601 N ATOM 1823 CA GLY A 257 23.827 3.073 127.541 1.00 53.59 C ANISOU 1823 CA GLY A 257 5680 8759 5922 -950 -804 -635 C ATOM 1824 C GLY A 257 23.559 2.044 126.460 1.00 53.37 C ANISOU 1824 C GLY A 257 5674 8775 5828 -1135 -868 -723 C ATOM 1825 O GLY A 257 23.745 2.266 125.263 1.00 53.69 O ANISOU 1825 O GLY A 257 5767 8851 5780 -1124 -915 -754 O ATOM 1826 N LYS A 258 23.124 0.875 126.909 1.00 52.74 N ANISOU 1826 N LYS A 258 5562 8689 5790 -1317 -871 -764 N ATOM 1827 CA LYS A 258 22.678 -0.185 126.023 1.00 54.21 C ANISOU 1827 CA LYS A 258 5756 8927 5916 -1517 -940 -849 C ATOM 1828 C LYS A 258 21.160 -0.173 125.909 1.00 55.92 C ANISOU 1828 C LYS A 258 5766 9416 6065 -1596 -1025 -814 C ATOM 1829 O LYS A 258 20.455 0.426 126.725 1.00 55.98 O ANISOU 1829 O LYS A 258 5622 9556 6090 -1516 -1016 -731 O ATOM 1830 CB LYS A 258 23.152 -1.554 126.512 1.00 54.15 C ANISOU 1830 CB LYS A 258 5859 8726 5991 -1687 -902 -921 C ATOM 1831 CG LYS A 258 24.643 -1.743 126.426 1.00 52.82 C ANISOU 1831 CG LYS A 258 5891 8304 5874 -1625 -831 -977 C ATOM 1832 CD LYS A 258 25.202 -1.141 125.159 1.00 52.72 C ANISOU 1832 CD LYS A 258 5952 8309 5770 -1533 -852 -1013 C ATOM 1833 CE LYS A 258 26.670 -1.463 125.014 1.00 51.66 C ANISOU 1833 CE LYS A 258 6005 7946 5679 -1492 -782 -1082 C ATOM 1834 NZ LYS A 258 26.916 -2.884 124.649 1.00 52.54 N ANISOU 1834 NZ LYS A 258 6228 7934 5801 -1660 -796 -1204 N ATOM 1835 N CYS A 259 20.667 -0.852 124.875 1.00 57.43 N ANISOU 1835 N CYS A 259 5949 9699 6172 -1755 -1107 -885 N ATOM 1836 CA CYS A 259 19.237 -0.903 124.617 1.00 59.27 C ANISOU 1836 CA CYS A 259 5983 10211 6327 -1849 -1199 -860 C ATOM 1837 C CYS A 259 18.514 -1.674 125.711 1.00 59.92 C ANISOU 1837 C CYS A 259 5957 10337 6472 -2005 -1183 -838 C ATOM 1838 O CYS A 259 19.035 -2.638 126.274 1.00 59.53 O ANISOU 1838 O CYS A 259 6022 10091 6504 -2131 -1135 -879 O ATOM 1839 CB CYS A 259 18.950 -1.552 123.257 1.00 60.81 C ANISOU 1839 CB CYS A 259 6211 10479 6414 -2007 -1293 -951 C ATOM 1840 SG CYS A 259 17.189 -1.607 122.809 1.00 63.29 S ANISOU 1840 SG CYS A 259 6269 11163 6616 -2133 -1420 -924 S ATOM 1841 N THR A 260 17.284 -1.241 125.988 1.00 61.07 N ANISOU 1841 N THR A 260 5876 10754 6573 -1995 -1228 -769 N ATOM 1842 CA THR A 260 16.451 -1.901 126.987 1.00 61.98 C ANISOU 1842 CA THR A 260 5854 10967 6728 -2151 -1218 -737 C ATOM 1843 C THR A 260 16.180 -3.361 126.638 1.00 65.51 C ANISOU 1843 C THR A 260 6354 11374 7163 -2458 -1268 -818 C ATOM 1844 O THR A 260 15.996 -4.183 127.541 1.00 66.97 O ANISOU 1844 O THR A 260 6531 11502 7411 -2617 -1235 -807 O ATOM 1845 CB THR A 260 15.137 -1.135 127.140 1.00 63.26 C ANISOU 1845 CB THR A 260 5746 11469 6821 -2077 -1268 -659 C ATOM 1846 OG1 THR A 260 15.421 0.262 127.285 1.00 62.12 O ANISOU 1846 OG1 THR A 260 5582 11342 6678 -1780 -1237 -594 O ATOM 1847 CG2 THR A 260 14.356 -1.615 128.349 1.00 64.02 C ANISOU 1847 CG2 THR A 260 5686 11680 6958 -2200 -1235 -610 C ATOM 1848 N PHE A 261 16.153 -3.717 125.349 1.00 64.37 N ANISOU 1848 N PHE A 261 6272 11251 6934 -2550 -1349 -900 N ATOM 1849 CA PHE A 261 15.920 -5.104 124.965 1.00 67.45 C ANISOU 1849 CA PHE A 261 6734 11586 7309 -2843 -1404 -989 C ATOM 1850 C PHE A 261 17.043 -5.740 124.165 1.00 74.65 C ANISOU 1850 C PHE A 261 7907 12230 8229 -2881 -1398 -1106 C ATOM 1851 O PHE A 261 17.092 -6.970 124.090 1.00 73.30 O ANISOU 1851 O PHE A 261 7847 11928 8077 -3105 -1422 -1185 O ATOM 1852 CB PHE A 261 14.620 -5.243 124.159 1.00 68.18 C ANISOU 1852 CB PHE A 261 6642 11987 7277 -2992 -1525 -1000 C ATOM 1853 CG PHE A 261 13.388 -4.909 124.939 1.00 69.23 C ANISOU 1853 CG PHE A 261 6502 12407 7394 -3012 -1539 -901 C ATOM 1854 CD1 PHE A 261 12.915 -3.611 124.984 1.00 69.01 C ANISOU 1854 CD1 PHE A 261 6295 12602 7323 -2774 -1544 -816 C ATOM 1855 CD2 PHE A 261 12.706 -5.889 125.634 1.00 70.55 C ANISOU 1855 CD2 PHE A 261 6594 12625 7587 -3267 -1546 -891 C ATOM 1856 CE1 PHE A 261 11.790 -3.294 125.705 1.00 70.09 C ANISOU 1856 CE1 PHE A 261 6173 13017 7442 -2775 -1552 -733 C ATOM 1857 CE2 PHE A 261 11.579 -5.578 126.359 1.00 71.63 C ANISOU 1857 CE2 PHE A 261 6465 13049 7701 -3287 -1552 -801 C ATOM 1858 CZ PHE A 261 11.120 -4.277 126.394 1.00 71.39 C ANISOU 1858 CZ PHE A 261 6248 13251 7627 -3033 -1553 -726 C ATOM 1859 N TYR A 262 17.934 -4.955 123.563 1.00 89.67 N ANISOU 1859 N TYR A 262 9911 14048 10112 -2672 -1370 -1121 N ATOM 1860 CA TYR A 262 19.109 -5.478 122.871 1.00 93.49 C ANISOU 1860 CA TYR A 262 10636 14283 10603 -2678 -1348 -1231 C ATOM 1861 C TYR A 262 20.345 -5.134 123.691 1.00 91.76 C ANISOU 1861 C TYR A 262 10545 13822 10497 -2501 -1230 -1203 C ATOM 1862 O TYR A 262 20.974 -4.091 123.465 1.00 93.27 O ANISOU 1862 O TYR A 262 10760 14004 10676 -2286 -1192 -1167 O ATOM 1863 CB TYR A 262 19.216 -4.897 121.462 1.00 95.29 C ANISOU 1863 CB TYR A 262 10883 14618 10705 -2596 -1407 -1275 C ATOM 1864 N PRO A 263 20.727 -5.970 124.664 1.00 90.15 N ANISOU 1864 N PRO A 263 10428 13421 10404 -2589 -1174 -1211 N ATOM 1865 CA PRO A 263 21.850 -5.618 125.559 1.00 87.64 C ANISOU 1865 CA PRO A 263 10211 12894 10195 -2421 -1065 -1173 C ATOM 1866 C PRO A 263 23.189 -5.414 124.862 1.00 86.49 C ANISOU 1866 C PRO A 263 10248 12570 10045 -2287 -1022 -1244 C ATOM 1867 O PRO A 263 24.093 -4.835 125.478 1.00 83.58 O ANISOU 1867 O PRO A 263 9934 12078 9746 -2118 -938 -1201 O ATOM 1868 CB PRO A 263 21.936 -6.810 126.522 1.00 88.70 C ANISOU 1868 CB PRO A 263 10422 12850 10428 -2587 -1038 -1187 C ATOM 1869 CG PRO A 263 20.729 -7.620 126.316 1.00 91.88 C ANISOU 1869 CG PRO A 263 10733 13396 10780 -2837 -1126 -1205 C ATOM 1870 CD PRO A 263 19.988 -7.172 125.104 1.00 93.20 C ANISOU 1870 CD PRO A 263 10793 13803 10816 -2850 -1215 -1232 C ATOM 1871 N ASP A 264 23.366 -5.886 123.629 1.00 87.31 N ANISOU 1871 N ASP A 264 10445 12661 10066 -2360 -1075 -1355 N ATOM 1872 CA ASP A 264 24.619 -5.694 122.916 1.00 84.11 C ANISOU 1872 CA ASP A 264 10200 12115 9642 -2236 -1031 -1426 C ATOM 1873 C ASP A 264 24.524 -4.597 121.877 1.00 76.87 C ANISOU 1873 C ASP A 264 9224 11378 8606 -2114 -1065 -1403 C ATOM 1874 O ASP A 264 25.405 -4.489 121.020 1.00 80.55 O ANISOU 1874 O ASP A 264 9809 11776 9019 -2047 -1046 -1473 O ATOM 1875 CB ASP A 264 25.073 -6.998 122.264 1.00 87.14 C ANISOU 1875 CB ASP A 264 10760 12336 10016 -2381 -1054 -1578 C ATOM 1876 CG ASP A 264 25.068 -8.167 123.240 1.00 90.93 C ANISOU 1876 CG ASP A 264 11312 12630 10608 -2523 -1039 -1598 C ATOM 1877 OD1 ASP A 264 24.725 -7.965 124.423 1.00 92.74 O ANISOU 1877 OD1 ASP A 264 11449 12869 10918 -2513 -1006 -1491 O ATOM 1878 OD2 ASP A 264 25.405 -9.293 122.825 1.00 94.04 O ANISOU 1878 OD2 ASP A 264 11862 12863 11004 -2642 -1061 -1721 O ATOM 1879 N GLU A 265 23.483 -3.779 121.945 1.00 71.62 N ANISOU 1879 N GLU A 265 8375 10944 7892 -2079 -1114 -1305 N ATOM 1880 CA GLU A 265 23.281 -2.661 121.041 1.00 68.70 C ANISOU 1880 CA GLU A 265 7940 10752 7410 -1953 -1156 -1261 C ATOM 1881 C GLU A 265 23.290 -1.381 121.857 1.00 56.89 C ANISOU 1881 C GLU A 265 6354 9301 5962 -1751 -1109 -1126 C ATOM 1882 O GLU A 265 22.574 -1.277 122.855 1.00 56.88 O ANISOU 1882 O GLU A 265 6224 9367 6020 -1756 -1103 -1053 O ATOM 1883 CB GLU A 265 21.953 -2.800 120.283 1.00 65.92 C ANISOU 1883 CB GLU A 265 7449 10654 6944 -2081 -1275 -1269 C ATOM 1884 CG GLU A 265 21.973 -3.796 119.130 1.00 62.60 C ANISOU 1884 CG GLU A 265 7128 10222 6434 -2255 -1338 -1408 C ATOM 1885 CD GLU A 265 22.706 -3.253 117.932 1.00 61.57 C ANISOU 1885 CD GLU A 265 7096 10099 6197 -2151 -1341 -1449 C ATOM 1886 OE1 GLU A 265 23.605 -3.945 117.416 1.00 63.38 O ANISOU 1886 OE1 GLU A 265 7496 10167 6418 -2194 -1310 -1567 O ATOM 1887 OE2 GLU A 265 22.386 -2.124 117.511 1.00 63.88 O ANISOU 1887 OE2 GLU A 265 7298 10562 6414 -2021 -1375 -1361 O ATOM 1888 N PHE A 266 24.112 -0.420 121.449 1.00 55.87 N ANISOU 1888 N PHE A 266 6294 9131 5802 -1579 -1073 -1096 N ATOM 1889 CA PHE A 266 24.052 0.906 122.038 1.00 54.88 C ANISOU 1889 CA PHE A 266 6093 9059 5701 -1384 -1047 -970 C ATOM 1890 C PHE A 266 22.744 1.587 121.666 1.00 56.17 C ANISOU 1890 C PHE A 266 6079 9488 5774 -1352 -1143 -899 C ATOM 1891 O PHE A 266 22.046 1.190 120.735 1.00 57.73 O ANISOU 1891 O PHE A 266 6226 9835 5871 -1465 -1231 -944 O ATOM 1892 CB PHE A 266 25.239 1.761 121.590 1.00 53.72 C ANISOU 1892 CB PHE A 266 6075 8807 5531 -1230 -996 -953 C ATOM 1893 CG PHE A 266 26.533 1.369 122.236 1.00 52.26 C ANISOU 1893 CG PHE A 266 6030 8378 5450 -1210 -891 -993 C ATOM 1894 CD1 PHE A 266 26.903 1.909 123.471 1.00 50.86 C ANISOU 1894 CD1 PHE A 266 5843 8103 5379 -1097 -819 -917 C ATOM 1895 CD2 PHE A 266 27.359 0.427 121.652 1.00 52.40 C ANISOU 1895 CD2 PHE A 266 6184 8270 5457 -1301 -867 -1111 C ATOM 1896 CE1 PHE A 266 28.085 1.532 124.085 1.00 49.61 C ANISOU 1896 CE1 PHE A 266 5804 7733 5313 -1080 -729 -951 C ATOM 1897 CE2 PHE A 266 28.545 0.044 122.273 1.00 51.19 C ANISOU 1897 CE2 PHE A 266 6148 7901 5399 -1271 -773 -1148 C ATOM 1898 CZ PHE A 266 28.903 0.603 123.488 1.00 49.78 C ANISOU 1898 CZ PHE A 266 5953 7636 5326 -1163 -706 -1063 C ATOM 1899 N ARG A 267 22.409 2.619 122.412 1.00 55.61 N ANISOU 1899 N ARG A 267 5914 9479 5738 -1192 -1128 -791 N ATOM 1900 CA ARG A 267 21.190 3.350 122.153 1.00 56.86 C ANISOU 1900 CA ARG A 267 5898 9890 5818 -1126 -1216 -718 C ATOM 1901 C ARG A 267 21.408 4.456 121.140 1.00 57.03 C ANISOU 1901 C ARG A 267 5962 9969 5736 -977 -1262 -670 C ATOM 1902 O ARG A 267 22.535 4.848 120.834 1.00 55.95 O ANISOU 1902 O ARG A 267 5983 9675 5601 -903 -1212 -673 O ATOM 1903 CB ARG A 267 20.653 3.966 123.427 1.00 56.44 C ANISOU 1903 CB ARG A 267 5716 9887 5841 -1007 -1182 -628 C ATOM 1904 CG ARG A 267 20.876 3.172 124.674 1.00 55.64 C ANISOU 1904 CG ARG A 267 5621 9656 5862 -1096 -1100 -650 C ATOM 1905 CD ARG A 267 20.588 4.034 125.857 1.00 55.01 C ANISOU 1905 CD ARG A 267 5447 9609 5845 -933 -1056 -559 C ATOM 1906 NE ARG A 267 20.521 3.309 127.116 1.00 54.59 N ANISOU 1906 NE ARG A 267 5358 9491 5892 -1024 -989 -564 N ATOM 1907 CZ ARG A 267 20.268 3.889 128.296 1.00 54.33 C ANISOU 1907 CZ ARG A 267 5241 9486 5917 -906 -940 -496 C ATOM 1908 NH1 ARG A 267 20.022 5.210 128.390 1.00 56.55 N ANISOU 1908 NH1 ARG A 267 5464 9851 6170 -684 -952 -425 N ATOM 1909 NH2 ARG A 267 20.241 3.149 129.411 1.00 53.80 N ANISOU 1909 NH2 ARG A 267 5149 9360 5931 -1008 -879 -500 N ATOM 1910 N ALA A 268 20.291 4.973 120.648 1.00 63.30 N ANISOU 1910 N ALA A 268 6609 11003 6439 -934 -1362 -618 N ATOM 1911 CA ALA A 268 20.256 6.043 119.675 1.00 63.78 C ANISOU 1911 CA ALA A 268 6690 11155 6390 -794 -1428 -556 C ATOM 1912 C ALA A 268 20.280 7.396 120.362 1.00 63.23 C ANISOU 1912 C ALA A 268 6601 11062 6362 -553 -1406 -441 C ATOM 1913 O ALA A 268 19.804 7.554 121.489 1.00 63.82 O ANISOU 1913 O ALA A 268 6569 11159 6519 -491 -1374 -404 O ATOM 1914 CB ALA A 268 18.997 5.935 118.827 1.00 66.97 C ANISOU 1914 CB ALA A 268 6938 11836 6672 -856 -1556 -553 C ATOM 1915 N ALA A 269 20.826 8.378 119.659 1.00 58.17 N ANISOU 1915 N ALA A 269 6068 10377 5655 -421 -1426 -385 N ATOM 1916 CA ALA A 269 20.729 9.749 120.115 1.00 57.92 C ANISOU 1916 CA ALA A 269 6028 10336 5640 -188 -1431 -272 C ATOM 1917 C ALA A 269 19.279 10.210 120.090 1.00 59.63 C ANISOU 1917 C ALA A 269 6043 10811 5802 -96 -1534 -212 C ATOM 1918 O ALA A 269 18.490 9.801 119.238 1.00 61.19 O ANISOU 1918 O ALA A 269 6142 11208 5900 -188 -1627 -234 O ATOM 1919 CB ALA A 269 21.584 10.664 119.246 1.00 57.66 C ANISOU 1919 CB ALA A 269 6165 10209 5535 -92 -1444 -219 C ATOM 1920 N LYS A 270 18.925 11.058 121.054 1.00 59.42 N ANISOU 1920 N LYS A 270 5951 10788 5838 89 -1517 -141 N ATOM 1921 CA LYS A 270 17.616 11.696 121.032 1.00 61.13 C ANISOU 1921 CA LYS A 270 5981 11248 5999 227 -1613 -76 C ATOM 1922 C LYS A 270 17.386 12.413 119.712 1.00 62.47 C ANISOU 1922 C LYS A 270 6183 11522 6031 309 -1728 -18 C ATOM 1923 O LYS A 270 16.273 12.413 119.176 1.00 64.31 O ANISOU 1923 O LYS A 270 6252 12007 6174 318 -1835 1 O ATOM 1924 CB LYS A 270 17.495 12.691 122.184 1.00 60.65 C ANISOU 1924 CB LYS A 270 5894 11133 6019 453 -1572 -9 C ATOM 1925 CG LYS A 270 17.681 12.095 123.571 1.00 59.43 C ANISOU 1925 CG LYS A 270 5700 10888 5992 391 -1459 -54 C ATOM 1926 CD LYS A 270 16.370 12.111 124.351 1.00 60.67 C ANISOU 1926 CD LYS A 270 5613 11281 6160 456 -1483 -38 C ATOM 1927 CE LYS A 270 16.592 12.466 125.824 1.00 59.58 C ANISOU 1927 CE LYS A 270 5473 11032 6133 570 -1383 -27 C ATOM 1928 NZ LYS A 270 16.762 11.303 126.732 1.00 58.70 N ANISOU 1928 NZ LYS A 270 5323 10873 6107 375 -1290 -91 N ATOM 1929 N ALA A 271 18.430 13.036 119.180 1.00 61.67 N ANISOU 1929 N ALA A 271 6289 11237 5905 365 -1711 17 N ATOM 1930 CA ALA A 271 18.342 13.844 117.980 1.00 62.87 C ANISOU 1930 CA ALA A 271 6503 11458 5926 455 -1814 91 C ATOM 1931 C ALA A 271 18.458 13.023 116.705 1.00 63.58 C ANISOU 1931 C ALA A 271 6622 11633 5902 257 -1862 28 C ATOM 1932 O ALA A 271 18.478 13.601 115.616 1.00 66.00 O ANISOU 1932 O ALA A 271 6994 11997 6085 305 -1944 85 O ATOM 1933 CB ALA A 271 19.424 14.923 118.003 1.00 61.83 C ANISOU 1933 CB ALA A 271 6587 11093 5814 593 -1773 165 C ATOM 1934 N SER A 272 18.538 11.701 116.807 1.00 63.18 N ANISOU 1934 N SER A 272 6535 11588 5884 37 -1814 -87 N ATOM 1935 CA SER A 272 18.577 10.873 115.616 1.00 64.04 C ANISOU 1935 CA SER A 272 6669 11784 5881 -153 -1863 -161 C ATOM 1936 C SER A 272 17.203 10.838 114.948 1.00 66.29 C ANISOU 1936 C SER A 272 6764 12373 6051 -162 -2003 -141 C ATOM 1937 O SER A 272 16.173 11.089 115.576 1.00 67.09 O ANISOU 1937 O SER A 272 6682 12628 6183 -72 -2044 -99 O ATOM 1938 CB SER A 272 19.036 9.462 115.970 1.00 63.13 C ANISOU 1938 CB SER A 272 6579 11569 5839 -378 -1778 -294 C ATOM 1939 OG SER A 272 18.121 8.846 116.850 1.00 63.50 O ANISOU 1939 OG SER A 272 6447 11722 5959 -439 -1777 -323 O ATOM 1940 N TYR A 273 17.192 10.523 113.652 1.00 67.42 N ANISOU 1940 N TYR A 273 6946 12617 6054 -273 -2078 -172 N ATOM 1941 CA TYR A 273 15.920 10.425 112.944 1.00 69.66 C ANISOU 1941 CA TYR A 273 7051 13201 6218 -301 -2218 -159 C ATOM 1942 C TYR A 273 15.084 9.277 113.492 1.00 70.22 C ANISOU 1942 C TYR A 273 6940 13404 6338 -478 -2219 -248 C ATOM 1943 O TYR A 273 13.889 9.441 113.758 1.00 71.61 O ANISOU 1943 O TYR A 273 6903 13809 6498 -425 -2295 -207 O ATOM 1944 CB TYR A 273 16.154 10.262 111.439 1.00 70.75 C ANISOU 1944 CB TYR A 273 7281 13414 6188 -400 -2294 -184 C ATOM 1945 CG TYR A 273 14.881 10.309 110.615 1.00 73.20 C ANISOU 1945 CG TYR A 273 7415 14041 6356 -411 -2452 -155 C ATOM 1946 CD1 TYR A 273 14.127 9.165 110.403 1.00 74.37 C ANISOU 1946 CD1 TYR A 273 7424 14366 6468 -625 -2500 -257 C ATOM 1947 CD2 TYR A 273 14.430 11.498 110.058 1.00 74.46 C ANISOU 1947 CD2 TYR A 273 7550 14323 6417 -208 -2558 -24 C ATOM 1948 CE1 TYR A 273 12.966 9.201 109.671 1.00 76.68 C ANISOU 1948 CE1 TYR A 273 7545 14962 6629 -643 -2647 -232 C ATOM 1949 CE2 TYR A 273 13.263 11.538 109.313 1.00 76.79 C ANISOU 1949 CE2 TYR A 273 7676 14922 6580 -210 -2708 5 C ATOM 1950 CZ TYR A 273 12.539 10.383 109.125 1.00 77.88 C ANISOU 1950 CZ TYR A 273 7664 15244 6682 -431 -2751 -101 C ATOM 1951 OH TYR A 273 11.379 10.397 108.391 1.00 80.28 O ANISOU 1951 OH TYR A 273 7789 15864 6851 -446 -2903 -76 O ATOM 1952 N THR A 274 15.706 8.111 113.690 1.00 69.25 N ANISOU 1952 N THR A 274 6900 13138 6275 -687 -2136 -368 N ATOM 1953 CA THR A 274 14.972 6.941 114.163 1.00 69.90 C ANISOU 1953 CA THR A 274 6836 13323 6399 -887 -2140 -453 C ATOM 1954 C THR A 274 14.264 7.214 115.478 1.00 69.71 C ANISOU 1954 C THR A 274 6640 13361 6486 -788 -2108 -396 C ATOM 1955 O THR A 274 13.129 6.778 115.683 1.00 71.17 O ANISOU 1955 O THR A 274 6616 13774 6652 -874 -2169 -405 O ATOM 1956 CB THR A 274 15.910 5.760 114.343 1.00 68.67 C ANISOU 1956 CB THR A 274 6834 12943 6316 -1088 -2041 -580 C ATOM 1957 OG1 THR A 274 16.679 5.563 113.159 1.00 68.78 O ANISOU 1957 OG1 THR A 274 7018 12889 6227 -1157 -2054 -639 O ATOM 1958 CG2 THR A 274 15.124 4.520 114.656 1.00 69.68 C ANISOU 1958 CG2 THR A 274 6832 13177 6466 -1320 -2064 -666 C ATOM 1959 N ALA A 275 14.928 7.912 116.394 1.00 68.01 N ANISOU 1959 N ALA A 275 6506 12951 6381 -618 -2012 -341 N ATOM 1960 CA ALA A 275 14.344 8.141 117.707 1.00 67.76 C ANISOU 1960 CA ALA A 275 6325 12965 6455 -524 -1968 -297 C ATOM 1961 C ALA A 275 13.268 9.209 117.664 1.00 69.29 C ANISOU 1961 C ALA A 275 6340 13400 6586 -309 -2064 -194 C ATOM 1962 O ALA A 275 12.331 9.168 118.465 1.00 70.05 O ANISOU 1962 O ALA A 275 6232 13665 6720 -280 -2070 -176 O ATOM 1963 CB ALA A 275 15.431 8.528 118.709 1.00 65.50 C ANISOU 1963 CB ALA A 275 6193 12392 6303 -415 -1836 -280 C ATOM 1964 N GLN A 276 13.389 10.168 116.744 1.00 69.86 N ANISOU 1964 N GLN A 276 6487 13496 6562 -153 -2140 -125 N ATOM 1965 CA GLN A 276 12.349 11.178 116.594 1.00 71.57 C ANISOU 1965 CA GLN A 276 6542 13944 6710 64 -2247 -26 C ATOM 1966 C GLN A 276 11.095 10.589 115.970 1.00 73.88 C ANISOU 1966 C GLN A 276 6608 14571 6893 -63 -2367 -50 C ATOM 1967 O GLN A 276 9.977 10.958 116.345 1.00 75.35 O ANISOU 1967 O GLN A 276 6568 14999 7063 53 -2427 -2 O ATOM 1968 CB GLN A 276 12.851 12.342 115.748 1.00 71.68 C ANISOU 1968 CB GLN A 276 6717 13875 6645 255 -2303 63 C ATOM 1969 CG GLN A 276 13.977 13.120 116.370 1.00 69.73 C ANISOU 1969 CG GLN A 276 6675 13323 6494 404 -2201 106 C ATOM 1970 CD GLN A 276 14.513 14.176 115.436 1.00 69.99 C ANISOU 1970 CD GLN A 276 6883 13272 6438 547 -2260 195 C ATOM 1971 OE1 GLN A 276 14.024 15.302 115.410 1.00 71.02 O ANISOU 1971 OE1 GLN A 276 6983 13466 6536 785 -2334 299 O ATOM 1972 NE2 GLN A 276 15.524 13.818 114.660 1.00 69.19 N ANISOU 1972 NE2 GLN A 276 6970 13027 6292 406 -2228 157 N ATOM 1973 N GLU A 277 11.258 9.682 115.008 1.00 75.92 N ANISOU 1973 N GLU A 277 6920 14857 7069 -298 -2406 -129 N ATOM 1974 CA GLU A 277 10.089 9.066 114.395 1.00 82.88 C ANISOU 1974 CA GLU A 277 7592 16056 7842 -446 -2525 -160 C ATOM 1975 C GLU A 277 9.366 8.176 115.395 1.00 81.25 C ANISOU 1975 C GLU A 277 7192 15965 7715 -600 -2484 -213 C ATOM 1976 O GLU A 277 8.139 8.248 115.525 1.00 82.58 O ANISOU 1976 O GLU A 277 7105 16436 7837 -577 -2564 -181 O ATOM 1977 CB GLU A 277 10.495 8.279 113.147 1.00 84.11 C ANISOU 1977 CB GLU A 277 7873 16197 7890 -669 -2572 -244 C ATOM 1978 CG GLU A 277 9.328 7.905 112.238 1.00 86.52 C ANISOU 1978 CG GLU A 277 7986 16842 8046 -788 -2724 -259 C ATOM 1979 CD GLU A 277 9.766 7.162 110.989 1.00 86.89 C ANISOU 1979 CD GLU A 277 8172 16867 7977 -1001 -2771 -350 C ATOM 1980 OE1 GLU A 277 10.865 6.582 111.002 1.00 84.86 O ANISOU 1980 OE1 GLU A 277 8126 16343 7775 -1117 -2671 -433 O ATOM 1981 OE2 GLU A 277 9.010 7.158 109.986 1.00 90.48 O ANISOU 1981 OE2 GLU A 277 8522 17578 8279 -1049 -2909 -343 O ATOM 1982 N PHE A 278 10.112 7.346 116.125 1.00 75.25 N ANISOU 1982 N PHE A 278 6547 14974 7073 -755 -2361 -288 N ATOM 1983 CA PHE A 278 9.504 6.514 117.156 1.00 75.50 C ANISOU 1983 CA PHE A 278 6414 15087 7184 -907 -2313 -327 C ATOM 1984 C PHE A 278 8.800 7.363 118.206 1.00 75.77 C ANISOU 1984 C PHE A 278 6260 15256 7273 -681 -2293 -239 C ATOM 1985 O PHE A 278 7.712 7.010 118.671 1.00 77.26 O ANISOU 1985 O PHE A 278 6202 15703 7451 -753 -2323 -236 O ATOM 1986 CB PHE A 278 10.574 5.635 117.804 1.00 73.46 C ANISOU 1986 CB PHE A 278 6347 14515 7050 -1067 -2180 -406 C ATOM 1987 CG PHE A 278 10.106 4.897 119.030 1.00 73.44 C ANISOU 1987 CG PHE A 278 6210 14548 7145 -1198 -2113 -427 C ATOM 1988 CD1 PHE A 278 9.486 3.665 118.915 1.00 74.78 C ANISOU 1988 CD1 PHE A 278 6283 14843 7287 -1494 -2152 -499 C ATOM 1989 CD2 PHE A 278 10.302 5.426 120.293 1.00 72.16 C ANISOU 1989 CD2 PHE A 278 6029 14291 7097 -1035 -2013 -373 C ATOM 1990 CE1 PHE A 278 9.060 2.981 120.031 1.00 74.89 C ANISOU 1990 CE1 PHE A 278 6180 14890 7383 -1630 -2092 -508 C ATOM 1991 CE2 PHE A 278 9.876 4.748 121.418 1.00 72.22 C ANISOU 1991 CE2 PHE A 278 5915 14342 7184 -1162 -1950 -387 C ATOM 1992 CZ PHE A 278 9.255 3.523 121.286 1.00 73.60 C ANISOU 1992 CZ PHE A 278 5992 14643 7328 -1462 -1989 -449 C ATOM 1993 N ASN A 279 9.401 8.492 118.583 1.00 74.48 N ANISOU 1993 N ASN A 279 6209 14928 7162 -408 -2242 -169 N ATOM 1994 CA ASN A 279 8.870 9.297 119.678 1.00 74.58 C ANISOU 1994 CA ASN A 279 6075 15024 7237 -180 -2207 -99 C ATOM 1995 C ASN A 279 7.512 9.890 119.335 1.00 77.10 C ANISOU 1995 C ASN A 279 6131 15711 7451 -39 -2333 -38 C ATOM 1996 O ASN A 279 6.591 9.869 120.159 1.00 78.13 O ANISOU 1996 O ASN A 279 6026 16056 7602 -2 -2324 -23 O ATOM 1997 CB ASN A 279 9.853 10.407 120.041 1.00 72.80 C ANISOU 1997 CB ASN A 279 6055 14526 7081 77 -2138 -43 C ATOM 1998 CG ASN A 279 10.896 9.960 121.043 1.00 70.46 C ANISOU 1998 CG ASN A 279 5918 13931 6924 0 -1988 -88 C ATOM 1999 OD1 ASN A 279 10.688 9.007 121.788 1.00 70.28 O ANISOU 1999 OD1 ASN A 279 5809 13931 6961 -184 -1927 -140 O ATOM 2000 ND2 ASN A 279 12.019 10.657 121.070 1.00 68.77 N ANISOU 2000 ND2 ASN A 279 5934 13439 6757 136 -1931 -61 N ATOM 2001 N LEU A 280 7.372 10.439 118.127 1.00 78.22 N ANISOU 2001 N LEU A 280 6306 15940 7474 49 -2452 2 N ATOM 2002 CA LEU A 280 6.103 11.045 117.746 1.00 80.74 C ANISOU 2002 CA LEU A 280 6378 16611 7688 204 -2583 65 C ATOM 2003 C LEU A 280 5.062 9.989 117.404 1.00 82.72 C ANISOU 2003 C LEU A 280 6391 17180 7860 -58 -2659 11 C ATOM 2004 O LEU A 280 3.884 10.152 117.733 1.00 84.64 O ANISOU 2004 O LEU A 280 6389 17683 8086 12 -2686 42 O ATOM 2005 CB LEU A 280 6.309 11.998 116.573 1.00 81.38 C ANISOU 2005 CB LEU A 280 6582 16676 7663 385 -2692 136 C ATOM 2006 CG LEU A 280 5.134 12.924 116.279 1.00 83.85 C ANISOU 2006 CG LEU A 280 6675 17303 7881 636 -2825 224 C ATOM 2007 CD1 LEU A 280 4.591 13.480 117.581 1.00 84.00 C ANISOU 2007 CD1 LEU A 280 6540 17383 7995 850 -2758 255 C ATOM 2008 CD2 LEU A 280 5.567 14.051 115.362 1.00 84.06 C ANISOU 2008 CD2 LEU A 280 6884 17223 7834 862 -2908 313 C ATOM 2009 N LEU A 281 5.479 8.899 116.753 1.00 82.41 N ANISOU 2009 N LEU A 281 6461 17061 7791 -362 -2664 -74 N ATOM 2010 CA LEU A 281 4.558 7.808 116.441 1.00 84.30 C ANISOU 2010 CA LEU A 281 6515 17548 7967 -646 -2723 -134 C ATOM 2011 C LEU A 281 3.852 7.297 117.689 1.00 84.70 C ANISOU 2011 C LEU A 281 6376 17696 8111 -729 -2634 -145 C ATOM 2012 O LEU A 281 2.626 7.147 117.704 1.00 86.98 O ANISOU 2012 O LEU A 281 6465 18213 8372 -760 -2651 -126 O ATOM 2013 CB LEU A 281 5.303 6.658 115.763 1.00 83.57 C ANISOU 2013 CB LEU A 281 6607 17294 7851 -961 -2721 -240 C ATOM 2014 CG LEU A 281 4.957 6.484 114.291 1.00 85.35 C ANISOU 2014 CG LEU A 281 6858 17637 7936 -1055 -2839 -259 C ATOM 2015 CD1 LEU A 281 5.291 7.763 113.617 1.00 85.22 C ANISOU 2015 CD1 LEU A 281 6931 17601 7849 -765 -2903 -171 C ATOM 2016 CD2 LEU A 281 5.731 5.344 113.669 1.00 84.67 C ANISOU 2016 CD2 LEU A 281 6956 17395 7820 -1357 -2837 -379 C ATOM 2017 N ASN A 282 4.619 6.999 118.743 1.00 82.59 N ANISOU 2017 N ASN A 282 6193 17229 7960 -773 -2521 -173 N ATOM 2018 CA ASN A 282 4.019 6.519 119.985 1.00 82.91 C ANISOU 2018 CA ASN A 282 6044 17384 8074 -860 -2444 -178 C ATOM 2019 C ASN A 282 3.234 7.622 120.674 1.00 83.85 C ANISOU 2019 C ASN A 282 5991 17657 8212 -543 -2419 -93 C ATOM 2020 O ASN A 282 2.236 7.342 121.344 1.00 85.36 O ANISOU 2020 O ASN A 282 5986 18028 8419 -591 -2372 -83 O ATOM 2021 CB ASN A 282 5.099 5.952 120.914 1.00 80.85 C ANISOU 2021 CB ASN A 282 5990 16774 7955 -966 -2293 -222 C ATOM 2022 CG ASN A 282 4.547 5.489 122.256 1.00 82.38 C ANISOU 2022 CG ASN A 282 6003 17075 8222 -1053 -2209 -218 C ATOM 2023 OD1 ASN A 282 4.277 6.289 123.154 1.00 80.56 O ANISOU 2023 OD1 ASN A 282 5662 16913 8033 -818 -2156 -161 O ATOM 2024 ND2 ASN A 282 4.351 4.186 122.380 1.00 83.32 N ANISOU 2024 ND2 ASN A 282 6092 17217 8349 -1396 -2199 -279 N ATOM 2025 N ASP A 283 3.656 8.875 120.506 1.00 83.15 N ANISOU 2025 N ASP A 283 5983 17496 8113 -219 -2448 -32 N ATOM 2026 CA ASP A 283 2.868 9.991 121.013 1.00 84.37 C ANISOU 2026 CA ASP A 283 5998 17783 8276 104 -2437 43 C ATOM 2027 C ASP A 283 1.487 10.003 120.383 1.00 87.42 C ANISOU 2027 C ASP A 283 6196 18446 8575 99 -2505 65 C ATOM 2028 O ASP A 283 0.475 10.163 121.076 1.00 89.02 O ANISOU 2028 O ASP A 283 6198 18837 8789 177 -2461 85 O ATOM 2029 CB ASP A 283 3.584 11.311 120.738 1.00 87.10 C ANISOU 2029 CB ASP A 283 6505 17973 8617 436 -2476 106 C ATOM 2030 CG ASP A 283 4.406 11.790 121.914 1.00 83.06 C ANISOU 2030 CG ASP A 283 6118 17211 8229 592 -2351 113 C ATOM 2031 OD1 ASP A 283 4.619 11.009 122.868 1.00 83.36 O ANISOU 2031 OD1 ASP A 283 6145 17174 8355 416 -2237 64 O ATOM 2032 OD2 ASP A 283 4.843 12.958 121.880 1.00 81.44 O ANISOU 2032 OD2 ASP A 283 6052 16851 8038 884 -2357 170 O ATOM 2033 N LEU A 284 1.429 9.817 119.061 1.00 88.37 N ANISOU 2033 N LEU A 284 6376 18599 8599 3 -2611 59 N ATOM 2034 CA LEU A 284 0.168 9.944 118.345 1.00 91.34 C ANISOU 2034 CA LEU A 284 6586 19236 8885 25 -2691 86 C ATOM 2035 C LEU A 284 -0.789 8.814 118.696 1.00 92.99 C ANISOU 2035 C LEU A 284 6602 19642 9088 -259 -2653 40 C ATOM 2036 O LEU A 284 -1.979 9.057 118.918 1.00 95.32 O ANISOU 2036 O LEU A 284 6684 20181 9352 -176 -2655 72 O ATOM 2037 CB LEU A 284 0.422 9.999 116.838 1.00 91.88 C ANISOU 2037 CB LEU A 284 6782 19279 8849 -19 -2812 90 C ATOM 2038 CG LEU A 284 1.294 11.175 116.398 1.00 90.61 C ANISOU 2038 CG LEU A 284 6818 18936 8675 263 -2857 152 C ATOM 2039 CD1 LEU A 284 1.709 11.048 114.924 1.00 90.90 C ANISOU 2039 CD1 LEU A 284 7008 18927 8602 164 -2964 146 C ATOM 2040 CD2 LEU A 284 0.605 12.519 116.687 1.00 91.99 C ANISOU 2040 CD2 LEU A 284 6899 19200 8854 640 -2876 242 C ATOM 2041 N ASN A 285 -0.294 7.576 118.754 1.00 91.96 N ANISOU 2041 N ASN A 285 6549 19407 8984 -597 -2620 -35 N ATOM 2042 CA ASN A 285 -1.180 6.457 119.051 1.00 93.65 C ANISOU 2042 CA ASN A 285 6607 19786 9189 -888 -2590 -73 C ATOM 2043 C ASN A 285 -1.740 6.540 120.463 1.00 96.26 C ANISOU 2043 C ASN A 285 6768 20220 9588 -823 -2479 -48 C ATOM 2044 O ASN A 285 -2.848 6.059 120.719 1.00 96.17 O ANISOU 2044 O ASN A 285 6562 20437 9542 -948 -2464 -45 O ATOM 2045 CB ASN A 285 -0.450 5.139 118.835 1.00 92.47 C ANISOU 2045 CB ASN A 285 6614 19458 9062 -1252 -2577 -160 C ATOM 2046 CG ASN A 285 0.031 4.984 117.420 1.00 92.48 C ANISOU 2046 CG ASN A 285 6779 19377 8981 -1332 -2681 -197 C ATOM 2047 OD1 ASN A 285 0.195 5.972 116.692 1.00 92.52 O ANISOU 2047 OD1 ASN A 285 6834 19388 8931 -1092 -2752 -150 O ATOM 2048 ND2 ASN A 285 0.248 3.741 117.004 1.00 92.59 N ANISOU 2048 ND2 ASN A 285 6888 19309 8983 -1671 -2692 -281 N ATOM 2049 N ASN A 286 -1.007 7.155 121.387 1.00 97.86 N ANISOU 2049 N ASN A 286 7040 20266 9878 -628 -2401 -29 N ATOM 2050 CA ASN A 286 -1.537 7.309 122.733 1.00 99.69 C ANISOU 2050 CA ASN A 286 7115 20598 10165 -545 -2293 -6 C ATOM 2051 C ASN A 286 -2.600 8.393 122.816 1.00104.67 C ANISOU 2051 C ASN A 286 7564 21461 10745 -234 -2311 53 C ATOM 2052 O ASN A 286 -3.240 8.527 123.864 1.00111.36 O ANISOU 2052 O ASN A 286 8255 22442 11614 -163 -2225 67 O ATOM 2053 CB ASN A 286 -0.399 7.589 123.710 1.00 96.82 C ANISOU 2053 CB ASN A 286 6889 19988 9909 -442 -2202 -10 C ATOM 2054 CG ASN A 286 0.480 6.380 123.922 1.00 94.64 C ANISOU 2054 CG ASN A 286 6752 19514 9692 -774 -2161 -72 C ATOM 2055 OD1 ASN A 286 0.026 5.245 123.801 1.00 96.22 O ANISOU 2055 OD1 ASN A 286 6905 19784 9871 -1090 -2161 -107 O ATOM 2056 ND2 ASN A 286 1.744 6.612 124.235 1.00 90.87 N ANISOU 2056 ND2 ASN A 286 6456 18781 9288 -704 -2127 -85 N ATOM 2057 N LEU A 287 -2.807 9.159 121.747 1.00 97.21 N ANISOU 2057 N LEU A 287 6641 20566 9730 -50 -2419 85 N ATOM 2058 CA LEU A 287 -3.975 10.017 121.692 1.00 98.03 C ANISOU 2058 CA LEU A 287 6556 20916 9773 199 -2450 134 C ATOM 2059 C LEU A 287 -5.225 9.161 121.496 1.00100.86 C ANISOU 2059 C LEU A 287 6697 21569 10055 -41 -2466 119 C ATOM 2060 O LEU A 287 -5.156 7.964 121.200 1.00100.84 O ANISOU 2060 O LEU A 287 6717 21558 10040 -392 -2474 74 O ATOM 2061 CB LEU A 287 -3.850 11.045 120.564 1.00 98.51 C ANISOU 2061 CB LEU A 287 6712 20940 9778 451 -2569 180 C ATOM 2062 CG LEU A 287 -2.573 11.876 120.421 1.00 95.97 C ANISOU 2062 CG LEU A 287 6639 20318 9506 662 -2584 203 C ATOM 2063 CD1 LEU A 287 -2.365 12.274 118.951 1.00 96.51 C ANISOU 2063 CD1 LEU A 287 6830 20348 9490 714 -2720 235 C ATOM 2064 CD2 LEU A 287 -2.607 13.120 121.318 1.00 95.79 C ANISOU 2064 CD2 LEU A 287 6609 20248 9538 1040 -2529 246 C ATOM 2065 N THR A 288 -6.382 9.784 121.683 1.00103.44 N ANISOU 2065 N THR A 288 6818 22154 10329 152 -2471 155 N ATOM 2066 CA THR A 288 -7.661 9.165 121.362 1.00106.55 C ANISOU 2066 CA THR A 288 6991 22861 10632 -28 -2504 152 C ATOM 2067 C THR A 288 -8.507 10.185 120.619 1.00109.05 C ANISOU 2067 C THR A 288 7198 23371 10866 254 -2600 200 C ATOM 2068 O THR A 288 -8.665 11.319 121.082 1.00109.34 O ANISOU 2068 O THR A 288 7204 23418 10921 602 -2578 234 O ATOM 2069 CB THR A 288 -8.385 8.665 122.615 1.00107.60 C ANISOU 2069 CB THR A 288 6936 23168 10777 -135 -2387 143 C ATOM 2070 OG1 THR A 288 -8.387 9.693 123.613 1.00107.18 O ANISOU 2070 OG1 THR A 288 6849 23104 10770 197 -2309 166 O ATOM 2071 CG2 THR A 288 -7.694 7.423 123.166 1.00105.68 C ANISOU 2071 CG2 THR A 288 6795 22758 10599 -487 -2313 99 C ATOM 2072 N VAL A 289 -9.035 9.787 119.468 1.00110.93 N ANISOU 2072 N VAL A 289 7385 23751 11013 105 -2707 199 N ATOM 2073 CA VAL A 289 -9.678 10.732 118.562 1.00113.14 C ANISOU 2073 CA VAL A 289 7598 24176 11212 360 -2819 248 C ATOM 2074 C VAL A 289 -11.062 10.228 118.170 1.00116.72 C ANISOU 2074 C VAL A 289 7800 24987 11560 212 -2865 248 C ATOM 2075 O VAL A 289 -11.308 9.013 118.187 1.00117.21 O ANISOU 2075 O VAL A 289 7805 25129 11601 -147 -2844 207 O ATOM 2076 CB VAL A 289 -8.794 10.976 117.330 1.00111.81 C ANISOU 2076 CB VAL A 289 7658 23798 11027 379 -2928 259 C ATOM 2077 CG1 VAL A 289 -7.683 11.947 117.676 1.00109.13 C ANISOU 2077 CG1 VAL A 289 7530 23164 10770 656 -2901 285 C ATOM 2078 CG2 VAL A 289 -8.204 9.670 116.858 1.00110.56 C ANISOU 2078 CG2 VAL A 289 7615 23528 10865 -20 -2938 198 C ATOM 2079 N PRO A 290 -11.997 11.124 117.830 1.00119.40 N ANISOU 2079 N PRO A 290 7988 25547 11831 478 -2928 294 N ATOM 2080 CA PRO A 290 -13.335 10.662 117.415 1.00123.00 C ANISOU 2080 CA PRO A 290 8194 26363 12178 341 -2978 296 C ATOM 2081 C PRO A 290 -13.316 9.797 116.171 1.00123.63 C ANISOU 2081 C PRO A 290 8324 26461 12187 38 -3082 275 C ATOM 2082 O PRO A 290 -14.005 8.772 116.117 1.00125.37 O ANISOU 2082 O PRO A 290 8405 26875 12353 -268 -3079 245 O ATOM 2083 CB PRO A 290 -14.097 11.976 117.180 1.00125.37 C ANISOU 2083 CB PRO A 290 8376 26830 12428 740 -3039 353 C ATOM 2084 CG PRO A 290 -13.035 13.011 116.972 1.00122.99 C ANISOU 2084 CG PRO A 290 8322 26215 12194 1028 -3069 384 C ATOM 2085 CD PRO A 290 -11.903 12.593 117.857 1.00119.45 C ANISOU 2085 CD PRO A 290 8044 25484 11856 916 -2956 346 C ATOM 2086 N THR A 291 -12.542 10.180 115.166 1.00122.36 N ANISOU 2086 N THR A 291 8367 26103 12022 112 -3176 288 N ATOM 2087 CA THR A 291 -12.470 9.412 113.936 1.00122.96 C ANISOU 2087 CA THR A 291 8511 26185 12024 -158 -3278 261 C ATOM 2088 C THR A 291 -11.313 8.418 114.001 1.00119.97 C ANISOU 2088 C THR A 291 8352 25522 11708 -457 -3231 197 C ATOM 2089 O THR A 291 -11.193 7.651 114.958 1.00118.99 O ANISOU 2089 O THR A 291 8206 25358 11646 -652 -3125 158 O ATOM 2090 CB THR A 291 -12.298 10.332 112.708 1.00123.52 C ANISOU 2090 CB THR A 291 8685 26214 12035 69 -3413 311 C ATOM 2091 OG1 THR A 291 -13.129 11.491 112.853 1.00125.70 O ANISOU 2091 OG1 THR A 291 8806 26673 12283 427 -3442 377 O ATOM 2092 CG2 THR A 291 -12.686 9.599 111.436 1.00125.39 C ANISOU 2092 CG2 THR A 291 8903 26580 12161 -188 -3527 288 C ATOM 2093 N LYS A 295 -8.646 6.404 117.527 1.00111.17 N ANISOU 2093 N LYS A 295 7583 23706 10948 -941 -2827 63 N ATOM 2094 CA LYS A 295 -7.268 6.232 117.087 1.00108.24 C ANISOU 2094 CA LYS A 295 7491 23009 10627 -1003 -2844 27 C ATOM 2095 C LYS A 295 -7.075 6.663 115.637 1.00108.75 C ANISOU 2095 C LYS A 295 7658 23051 10609 -925 -2977 37 C ATOM 2096 O LYS A 295 -7.849 6.292 114.756 1.00111.19 O ANISOU 2096 O LYS A 295 7875 23550 10821 -1056 -3062 30 O ATOM 2097 CB LYS A 295 -6.830 4.778 117.256 1.00107.31 C ANISOU 2097 CB LYS A 295 7472 22758 10543 -1411 -2801 -47 C ATOM 2098 N LEU A 296 -6.028 7.448 115.401 1.00106.49 N ANISOU 2098 N LEU A 296 7570 22534 10358 -714 -2993 56 N ATOM 2099 CA LEU A 296 -5.682 7.873 114.054 1.00106.70 C ANISOU 2099 CA LEU A 296 7730 22505 10305 -641 -3113 71 C ATOM 2100 C LEU A 296 -5.258 6.678 113.204 1.00106.46 C ANISOU 2100 C LEU A 296 7832 22387 10231 -1000 -3155 -10 C ATOM 2101 O LEU A 296 -4.735 5.683 113.710 1.00105.02 O ANISOU 2101 O LEU A 296 7731 22063 10110 -1257 -3084 -78 O ATOM 2102 CB LEU A 296 -4.559 8.906 114.101 1.00104.20 C ANISOU 2102 CB LEU A 296 7616 21937 10038 -362 -3108 111 C ATOM 2103 CG LEU A 296 -4.890 10.180 114.873 1.00104.44 C ANISOU 2103 CG LEU A 296 7556 22014 10113 20 -3074 187 C ATOM 2104 CD1 LEU A 296 -3.686 10.638 115.667 1.00101.29 C ANISOU 2104 CD1 LEU A 296 7337 21331 9818 161 -2993 192 C ATOM 2105 CD2 LEU A 296 -5.341 11.271 113.934 1.00106.28 C ANISOU 2105 CD2 LEU A 296 7777 22341 10263 292 -3190 262 C ATOM 2106 N SER A 297 -5.493 6.783 111.899 1.00108.01 N ANISOU 2106 N SER A 297 8057 22662 10318 -1013 -3273 -5 N ATOM 2107 CA SER A 297 -5.154 5.704 110.984 1.00108.12 C ANISOU 2107 CA SER A 297 8201 22604 10276 -1336 -3322 -88 C ATOM 2108 C SER A 297 -3.676 5.754 110.617 1.00105.25 C ANISOU 2108 C SER A 297 8128 21928 9935 -1335 -3316 -123 C ATOM 2109 O SER A 297 -2.968 6.721 110.913 1.00103.41 O ANISOU 2109 O SER A 297 7992 21554 9746 -1071 -3294 -70 O ATOM 2110 CB SER A 297 -5.982 5.796 109.711 1.00111.01 C ANISOU 2110 CB SER A 297 8487 23186 10508 -1353 -3451 -71 C ATOM 2111 OG SER A 297 -5.715 7.013 109.051 1.00110.90 O ANISOU 2111 OG SER A 297 8546 23145 10447 -1047 -3524 4 O ATOM 2112 N LYS A 298 -3.215 4.695 109.940 1.00105.03 N ANISOU 2112 N LYS A 298 8245 21792 9870 -1634 -3338 -217 N ATOM 2113 CA LYS A 298 -1.849 4.692 109.432 1.00102.67 C ANISOU 2113 CA LYS A 298 8222 21220 9568 -1647 -3340 -260 C ATOM 2114 C LYS A 298 -1.602 5.923 108.591 1.00102.75 C ANISOU 2114 C LYS A 298 8304 21236 9502 -1360 -3421 -179 C ATOM 2115 O LYS A 298 -0.702 6.718 108.877 1.00100.61 O ANISOU 2115 O LYS A 298 8165 20790 9273 -1151 -3390 -136 O ATOM 2116 CB LYS A 298 -1.553 3.445 108.603 1.00103.10 C ANISOU 2116 CB LYS A 298 8414 21191 9567 -1987 -3370 -377 C ATOM 2117 CG LYS A 298 -0.415 3.680 107.604 1.00101.73 C ANISOU 2117 CG LYS A 298 8498 20827 9328 -1952 -3411 -408 C ATOM 2118 CD LYS A 298 0.411 2.443 107.400 1.00100.66 C ANISOU 2118 CD LYS A 298 8563 20478 9207 -2253 -3373 -543 C ATOM 2119 CE LYS A 298 -0.478 1.234 107.240 1.00102.94 C ANISOU 2119 CE LYS A 298 8755 20883 9473 -2559 -3395 -617 C ATOM 2120 NZ LYS A 298 0.322 -0.015 107.261 1.00101.87 N ANISOU 2120 NZ LYS A 298 8822 20505 9377 -2845 -3345 -751 N ATOM 2121 N GLU A 299 -2.401 6.094 107.541 1.00105.34 N ANISOU 2121 N GLU A 299 8550 21762 9713 -1350 -3530 -153 N ATOM 2122 CA GLU A 299 -2.267 7.294 106.739 1.00105.74 C ANISOU 2122 CA GLU A 299 8664 21827 9687 -1073 -3615 -62 C ATOM 2123 C GLU A 299 -2.297 8.514 107.638 1.00104.92 C ANISOU 2123 C GLU A 299 8496 21708 9661 -727 -3576 42 C ATOM 2124 O GLU A 299 -1.374 9.328 107.608 1.00103.10 O ANISOU 2124 O GLU A 299 8439 21290 9446 -531 -3570 90 O ATOM 2125 CB GLU A 299 -3.356 7.350 105.660 1.00109.04 C ANISOU 2125 CB GLU A 299 8950 22504 9977 -1092 -3736 -36 C ATOM 2126 CG GLU A 299 -2.886 6.656 104.370 1.00109.43 C ANISOU 2126 CG GLU A 299 9171 22491 9915 -1318 -3802 -114 C ATOM 2127 CD GLU A 299 -3.828 6.796 103.167 1.00112.62 C ANISOU 2127 CD GLU A 299 9477 23135 10180 -1323 -3933 -84 C ATOM 2128 OE1 GLU A 299 -3.628 6.059 102.175 1.00113.34 O ANISOU 2128 OE1 GLU A 299 9676 23210 10179 -1545 -3983 -162 O ATOM 2129 OE2 GLU A 299 -4.748 7.638 103.197 1.00114.48 O ANISOU 2129 OE2 GLU A 299 9534 23570 10395 -1103 -3987 14 O ATOM 2130 N GLN A 300 -3.275 8.586 108.546 1.00106.10 N ANISOU 2130 N GLN A 300 8412 22032 9868 -664 -3535 68 N ATOM 2131 CA GLN A 300 -3.430 9.810 109.328 1.00105.78 C ANISOU 2131 CA GLN A 300 8304 21995 9891 -311 -3506 163 C ATOM 2132 C GLN A 300 -2.144 10.300 109.999 1.00102.55 C ANISOU 2132 C GLN A 300 8094 21296 9573 -173 -3429 175 C ATOM 2133 O GLN A 300 -1.990 11.511 110.193 1.00102.22 O ANISOU 2133 O GLN A 300 8092 21195 9553 149 -3440 263 O ATOM 2134 CB GLN A 300 -4.556 9.648 110.341 1.00107.27 C ANISOU 2134 CB GLN A 300 8226 22400 10133 -300 -3446 167 C ATOM 2135 CG GLN A 300 -5.870 9.955 109.708 1.00110.73 C ANISOU 2135 CG GLN A 300 8460 23135 10476 -226 -3541 213 C ATOM 2136 CD GLN A 300 -7.053 9.694 110.603 1.00112.59 C ANISOU 2136 CD GLN A 300 8420 23619 10740 -249 -3484 211 C ATOM 2137 OE1 GLN A 300 -7.514 8.560 110.720 1.00113.48 O ANISOU 2137 OE1 GLN A 300 8433 23843 10841 -554 -3458 146 O ATOM 2138 NE2 GLN A 300 -7.602 10.755 111.185 1.00113.48 N ANISOU 2138 NE2 GLN A 300 8410 23827 10880 75 -3470 282 N ATOM 2139 N LYS A 301 -1.198 9.401 110.299 1.00100.28 N ANISOU 2139 N LYS A 301 7947 20820 9336 -407 -3357 89 N ATOM 2140 CA LYS A 301 0.072 9.805 110.914 1.00 97.70 C ANISOU 2140 CA LYS A 301 7810 20222 9090 -295 -3285 96 C ATOM 2141 C LYS A 301 1.053 10.363 109.900 1.00 96.62 C ANISOU 2141 C LYS A 301 7916 19919 8877 -210 -3349 126 C ATOM 2142 O LYS A 301 1.721 11.366 110.174 1.00 94.89 O ANISOU 2142 O LYS A 301 7816 19549 8690 41 -3335 196 O ATOM 2143 CB LYS A 301 0.700 8.638 111.686 1.00 95.30 C ANISOU 2143 CB LYS A 301 7558 19781 8871 -571 -3182 -6 C ATOM 2144 CG LYS A 301 -0.335 7.871 112.487 1.00 96.67 C ANISOU 2144 CG LYS A 301 7501 20134 9093 -730 -3129 -39 C ATOM 2145 CD LYS A 301 0.083 6.441 112.709 1.00 95.74 C ANISOU 2145 CD LYS A 301 7453 19911 9014 -1095 -3073 -150 C ATOM 2146 CE LYS A 301 -0.908 5.692 113.602 1.00 97.08 C ANISOU 2146 CE LYS A 301 7409 20244 9234 -1259 -3012 -170 C ATOM 2147 NZ LYS A 301 -0.715 4.242 113.328 1.00 97.16 N ANISOU 2147 NZ LYS A 301 7501 20177 9238 -1644 -3004 -276 N ATOM 2148 N ASN A 302 1.202 9.696 108.755 1.00 97.01 N ANISOU 2148 N ASN A 302 8053 19981 8824 -427 -3412 69 N ATOM 2149 CA ASN A 302 2.134 10.195 107.752 1.00 96.25 C ANISOU 2149 CA ASN A 302 8190 19740 8640 -361 -3466 97 C ATOM 2150 C ASN A 302 1.757 11.585 107.289 1.00 97.58 C ANISOU 2150 C ASN A 302 8351 19970 8754 -36 -3552 232 C ATOM 2151 O ASN A 302 2.631 12.350 106.878 1.00 96.50 O ANISOU 2151 O ASN A 302 8414 19669 8582 110 -3572 292 O ATOM 2152 CB ASN A 302 2.225 9.271 106.522 1.00 97.24 C ANISOU 2152 CB ASN A 302 8399 19896 8650 -638 -3524 11 C ATOM 2153 CG ASN A 302 2.295 7.804 106.884 1.00 96.74 C ANISOU 2153 CG ASN A 302 8319 19803 8634 -977 -3458 -127 C ATOM 2154 OD1 ASN A 302 1.317 7.220 107.342 1.00 98.14 O ANISOU 2154 OD1 ASN A 302 8299 20140 8848 -1093 -3447 -153 O ATOM 2155 ND2 ASN A 302 3.448 7.192 106.653 1.00 94.91 N ANISOU 2155 ND2 ASN A 302 8303 19362 8397 -1142 -3415 -216 N ATOM 2156 N GLN A 303 0.477 11.934 107.354 1.00100.01 N ANISOU 2156 N GLN A 303 8439 20506 9054 80 -3601 283 N ATOM 2157 CA GLN A 303 0.113 13.327 107.138 1.00101.23 C ANISOU 2157 CA GLN A 303 8587 20692 9184 424 -3672 412 C ATOM 2158 C GLN A 303 0.853 14.223 108.107 1.00 99.11 C ANISOU 2158 C GLN A 303 8424 20214 9018 674 -3600 470 C ATOM 2159 O GLN A 303 1.551 15.153 107.698 1.00 98.46 O ANISOU 2159 O GLN A 303 8536 19971 8905 859 -3638 551 O ATOM 2160 CB GLN A 303 -1.392 13.568 107.295 1.00109.85 C ANISOU 2160 CB GLN A 303 9407 22062 10271 531 -3716 449 C ATOM 2161 CG GLN A 303 -2.230 13.180 106.104 1.00112.07 C ANISOU 2161 CG GLN A 303 9596 22564 10423 397 -3827 440 C ATOM 2162 CD GLN A 303 -2.391 11.707 105.968 1.00111.51 C ANISOU 2162 CD GLN A 303 9460 22574 10334 21 -3798 317 C ATOM 2163 OE1 GLN A 303 -1.517 11.013 105.448 1.00109.62 O ANISOU 2163 OE1 GLN A 303 9398 22193 10058 -195 -3788 245 O ATOM 2164 NE2 GLN A 303 -3.517 11.214 106.394 1.00113.40 N ANISOU 2164 NE2 GLN A 303 9455 23042 10591 -65 -3787 289 N ATOM 2165 N ILE A 304 0.706 13.959 109.404 1.00 98.10 N ANISOU 2165 N ILE A 304 8179 20084 9011 677 -3496 431 N ATOM 2166 CA ILE A 304 1.235 14.869 110.410 1.00 96.44 C ANISOU 2166 CA ILE A 304 8042 19700 8903 939 -3429 486 C ATOM 2167 C ILE A 304 2.756 14.853 110.385 1.00 93.59 C ANISOU 2167 C ILE A 304 7946 19059 8554 889 -3386 473 C ATOM 2168 O ILE A 304 3.408 15.893 110.529 1.00 92.62 O ANISOU 2168 O ILE A 304 7984 18755 8452 1129 -3387 553 O ATOM 2169 CB ILE A 304 0.665 14.485 111.785 1.00 96.23 C ANISOU 2169 CB ILE A 304 7813 19760 8990 926 -3324 439 C ATOM 2170 CG1 ILE A 304 -0.792 14.050 111.615 1.00 99.14 C ANISOU 2170 CG1 ILE A 304 7914 20437 9316 845 -3362 422 C ATOM 2171 CG2 ILE A 304 0.797 15.647 112.749 1.00 95.56 C ANISOU 2171 CG2 ILE A 304 7753 19559 8995 1265 -3276 508 C ATOM 2172 CD1 ILE A 304 -1.541 13.776 112.888 1.00 99.53 C ANISOU 2172 CD1 ILE A 304 7744 20617 9455 850 -3266 391 C ATOM 2173 N ILE A 305 3.342 13.677 110.162 1.00 92.36 N ANISOU 2173 N ILE A 305 7852 18860 8382 574 -3351 370 N ATOM 2174 CA ILE A 305 4.794 13.562 110.091 1.00 89.79 C ANISOU 2174 CA ILE A 305 7773 18287 8056 503 -3307 344 C ATOM 2175 C ILE A 305 5.340 14.412 108.962 1.00 90.13 C ANISOU 2175 C ILE A 305 8019 18240 7987 629 -3391 430 C ATOM 2176 O ILE A 305 6.249 15.227 109.159 1.00 88.64 O ANISOU 2176 O ILE A 305 8012 17851 7816 801 -3370 496 O ATOM 2177 CB ILE A 305 5.200 12.094 109.923 1.00 88.92 C ANISOU 2177 CB ILE A 305 7688 18162 7935 133 -3263 207 C ATOM 2178 CG1 ILE A 305 4.875 11.352 111.205 1.00 88.20 C ANISOU 2178 CG1 ILE A 305 7439 18104 7970 21 -3166 139 C ATOM 2179 CG2 ILE A 305 6.672 11.990 109.554 1.00 86.73 C ANISOU 2179 CG2 ILE A 305 7677 17654 7623 55 -3233 176 C ATOM 2180 CD1 ILE A 305 5.575 10.086 111.312 1.00 86.75 C ANISOU 2180 CD1 ILE A 305 7338 17815 7808 -294 -3105 14 C ATOM 2181 N ASN A 306 4.814 14.204 107.752 1.00 92.16 N ANISOU 2181 N ASN A 306 8255 18640 8123 533 -3487 431 N ATOM 2182 CA ASN A 306 5.197 15.039 106.625 1.00 93.16 C ANISOU 2182 CA ASN A 306 8559 18705 8133 653 -3575 524 C ATOM 2183 C ASN A 306 4.930 16.507 106.920 1.00 93.59 C ANISOU 2183 C ASN A 306 8631 18708 8220 1016 -3615 666 C ATOM 2184 O ASN A 306 5.783 17.360 106.663 1.00 92.73 O ANISOU 2184 O ASN A 306 8740 18411 8083 1159 -3627 751 O ATOM 2185 CB ASN A 306 4.455 14.591 105.364 1.00 95.34 C ANISOU 2185 CB ASN A 306 8768 19179 8279 506 -3676 503 C ATOM 2186 CG ASN A 306 5.227 13.552 104.575 1.00 94.55 C ANISOU 2186 CG ASN A 306 8805 19025 8095 202 -3660 395 C ATOM 2187 OD1 ASN A 306 5.835 13.861 103.550 1.00 94.72 O ANISOU 2187 OD1 ASN A 306 9009 18979 8001 197 -3707 430 O ATOM 2188 ND2 ASN A 306 5.221 12.315 105.058 1.00 93.77 N ANISOU 2188 ND2 ASN A 306 8630 18947 8053 -54 -3589 261 N ATOM 2189 N TYR A 307 3.764 16.826 107.481 1.00 95.23 N ANISOU 2189 N TYR A 307 8622 19073 8488 1168 -3631 693 N ATOM 2190 CA TYR A 307 3.450 18.229 107.729 1.00107.33 C ANISOU 2190 CA TYR A 307 10179 20549 10052 1522 -3672 818 C ATOM 2191 C TYR A 307 4.486 18.873 108.642 1.00101.57 C ANISOU 2191 C TYR A 307 9623 19551 9418 1681 -3589 852 C ATOM 2192 O TYR A 307 5.014 19.948 108.339 1.00100.32 O ANISOU 2192 O TYR A 307 9663 19218 9236 1882 -3630 959 O ATOM 2193 CB TYR A 307 2.053 18.373 108.324 1.00107.43 C ANISOU 2193 CB TYR A 307 9919 20779 10121 1650 -3681 819 C ATOM 2194 CG TYR A 307 1.834 19.733 108.941 1.00105.49 C ANISOU 2194 CG TYR A 307 9702 20436 9945 2018 -3687 918 C ATOM 2195 CD1 TYR A 307 1.901 20.890 108.171 1.00104.79 C ANISOU 2195 CD1 TYR A 307 9769 20254 9793 2240 -3789 1040 C ATOM 2196 CD2 TYR A 307 1.583 19.862 110.298 1.00104.15 C ANISOU 2196 CD2 TYR A 307 9417 20253 9902 2141 -3589 887 C ATOM 2197 CE1 TYR A 307 1.710 22.134 108.738 1.00105.37 C ANISOU 2197 CE1 TYR A 307 9889 20213 9935 2573 -3797 1124 C ATOM 2198 CE2 TYR A 307 1.391 21.093 110.871 1.00104.57 C ANISOU 2198 CE2 TYR A 307 9509 20203 10018 2477 -3590 963 C ATOM 2199 CZ TYR A 307 1.456 22.227 110.093 1.00105.72 C ANISOU 2199 CZ TYR A 307 9818 20244 10107 2693 -3695 1080 C ATOM 2200 OH TYR A 307 1.262 23.456 110.680 1.00106.73 O ANISOU 2200 OH TYR A 307 10001 20249 10304 3025 -3697 1149 O ATOM 2201 N VAL A 308 4.812 18.215 109.754 1.00105.40 N ANISOU 2201 N VAL A 308 10047 19992 10010 1583 -3473 765 N ATOM 2202 CA VAL A 308 5.740 18.822 110.701 1.00104.60 C ANISOU 2202 CA VAL A 308 10095 19645 10004 1741 -3393 794 C ATOM 2203 C VAL A 308 7.164 18.755 110.182 1.00105.89 C ANISOU 2203 C VAL A 308 10527 19598 10109 1631 -3379 801 C ATOM 2204 O VAL A 308 7.977 19.643 110.463 1.00106.23 O ANISOU 2204 O VAL A 308 10765 19416 10180 1809 -3358 876 O ATOM 2205 CB VAL A 308 5.593 18.146 112.072 1.00107.22 C ANISOU 2205 CB VAL A 308 10267 20009 10464 1673 -3276 702 C ATOM 2206 CG1 VAL A 308 4.148 18.187 112.469 1.00110.85 C ANISOU 2206 CG1 VAL A 308 10457 20704 10956 1761 -3288 696 C ATOM 2207 CG2 VAL A 308 6.092 16.705 112.028 1.00107.50 C ANISOU 2207 CG2 VAL A 308 10286 20071 10489 1314 -3220 580 C ATOM 2208 N LYS A 309 7.490 17.728 109.402 1.00 96.78 N ANISOU 2208 N LYS A 309 9396 18507 8869 1338 -3386 723 N ATOM 2209 CA LYS A 309 8.857 17.588 108.928 1.00 85.49 C ANISOU 2209 CA LYS A 309 8244 16823 7417 1204 -3322 707 C ATOM 2210 C LYS A 309 9.223 18.707 107.964 1.00 86.41 C ANISOU 2210 C LYS A 309 8553 16862 7416 1371 -3419 843 C ATOM 2211 O LYS A 309 10.351 19.213 107.996 1.00 84.89 O ANISOU 2211 O LYS A 309 8618 16373 7263 1402 -3342 882 O ATOM 2212 CB LYS A 309 9.044 16.225 108.269 1.00 85.28 C ANISOU 2212 CB LYS A 309 8203 16876 7325 858 -3304 579 C ATOM 2213 CG LYS A 309 10.485 15.780 108.219 1.00 82.94 C ANISOU 2213 CG LYS A 309 8166 16270 7079 687 -3167 512 C ATOM 2214 CD LYS A 309 10.813 15.030 106.941 1.00 83.51 C ANISOU 2214 CD LYS A 309 8318 16409 7004 447 -3210 446 C ATOM 2215 CE LYS A 309 9.998 13.765 106.813 1.00 84.52 C ANISOU 2215 CE LYS A 309 8238 16777 7097 209 -3246 323 C ATOM 2216 NZ LYS A 309 10.018 12.946 108.036 1.00 83.04 N ANISOU 2216 NZ LYS A 309 7969 16505 7078 99 -3122 223 N ATOM 2217 N ASN A 310 8.278 19.116 107.113 1.00 88.99 N ANISOU 2217 N ASN A 310 8789 17381 7640 1459 -3552 913 N ATOM 2218 CA ASN A 310 8.533 20.096 106.066 1.00 98.75 C ANISOU 2218 CA ASN A 310 10216 18539 8766 1582 -3645 1042 C ATOM 2219 C ASN A 310 8.154 21.517 106.463 1.00 97.62 C ANISOU 2219 C ASN A 310 10116 18292 8682 1928 -3691 1177 C ATOM 2220 O ASN A 310 8.467 22.451 105.716 1.00 97.33 O ANISOU 2220 O ASN A 310 10270 18143 8569 2046 -3764 1299 O ATOM 2221 CB ASN A 310 7.793 19.719 104.770 1.00 92.57 C ANISOU 2221 CB ASN A 310 9357 17968 7849 1454 -3750 1035 C ATOM 2222 CG ASN A 310 8.078 18.291 104.315 1.00 91.86 C ANISOU 2222 CG ASN A 310 9230 17975 7699 1108 -3709 889 C ATOM 2223 OD1 ASN A 310 7.327 17.364 104.618 1.00 92.32 O ANISOU 2223 OD1 ASN A 310 9078 18201 7797 966 -3693 784 O ATOM 2224 ND2 ASN A 310 9.164 18.114 103.570 1.00 90.90 N ANISOU 2224 ND2 ASN A 310 9321 17741 7476 968 -3691 880 N ATOM 2225 N GLU A 311 7.498 21.708 107.607 1.00114.01 N ANISOU 2225 N GLU A 311 12031 20395 10891 2086 -3649 1156 N ATOM 2226 CA GLU A 311 7.224 23.045 108.114 1.00114.01 C ANISOU 2226 CA GLU A 311 12092 20264 10964 2419 -3676 1265 C ATOM 2227 C GLU A 311 8.352 23.462 109.043 1.00109.55 C ANISOU 2227 C GLU A 311 11714 19420 10489 2503 -3580 1278 C ATOM 2228 O GLU A 311 8.864 22.649 109.814 1.00104.52 O ANISOU 2228 O GLU A 311 11032 18764 9916 2361 -3474 1178 O ATOM 2229 CB GLU A 311 5.885 23.097 108.852 1.00117.07 C ANISOU 2229 CB GLU A 311 12208 20833 11438 2562 -3677 1231 C ATOM 2230 CG GLU A 311 5.340 24.506 109.013 1.00121.87 C ANISOU 2230 CG GLU A 311 12865 21354 12085 2906 -3740 1343 C ATOM 2231 CD GLU A 311 4.357 24.875 107.923 1.00126.26 C ANISOU 2231 CD GLU A 311 13348 22085 12540 2971 -3879 1413 C ATOM 2232 OE1 GLU A 311 3.978 23.980 107.141 1.00127.87 O ANISOU 2232 OE1 GLU A 311 13430 22504 12651 2748 -3918 1362 O ATOM 2233 OE2 GLU A 311 3.962 26.058 107.848 1.00127.78 O ANISOU 2233 OE2 GLU A 311 13611 22196 12746 3242 -3950 1515 O ATOM 2234 N LYS A 312 8.750 24.729 108.950 1.00 91.06 N ANISOU 2234 N LYS A 312 9592 16856 8150 2727 -3619 1403 N ATOM 2235 CA LYS A 312 9.907 25.213 109.689 1.00 87.99 C ANISOU 2235 CA LYS A 312 9422 16179 7831 2800 -3537 1430 C ATOM 2236 C LYS A 312 9.600 25.328 111.179 1.00 87.16 C ANISOU 2236 C LYS A 312 9200 16030 7889 2955 -3448 1369 C ATOM 2237 O LYS A 312 10.133 24.561 111.988 1.00 84.96 O ANISOU 2237 O LYS A 312 8898 15673 7709 2796 -3309 1262 O ATOM 2238 CB LYS A 312 10.370 26.557 109.123 1.00 88.99 C ANISOU 2238 CB LYS A 312 9828 16069 7913 2978 -3610 1585 C ATOM 2239 N ALA A 313 8.742 26.271 111.552 1.00 89.03 N ANISOU 2239 N ALA A 313 9387 16251 8188 3224 -3489 1420 N ATOM 2240 CA ALA A 313 8.358 26.444 112.945 1.00 88.58 C ANISOU 2240 CA ALA A 313 9214 16166 8275 3385 -3403 1359 C ATOM 2241 C ALA A 313 7.303 25.422 113.349 1.00 89.11 C ANISOU 2241 C ALA A 313 8942 16546 8368 3276 -3369 1246 C ATOM 2242 O ALA A 313 6.387 25.112 112.582 1.00 91.08 O ANISOU 2242 O ALA A 313 9031 17033 8542 3216 -3447 1246 O ATOM 2243 CB ALA A 313 7.833 27.858 113.180 1.00 90.58 C ANISOU 2243 CB ALA A 313 9551 16284 8580 3714 -3456 1445 C ATOM 2244 N MET A 314 7.435 24.898 114.565 1.00 87.43 N ANISOU 2244 N MET A 314 8626 16333 8261 3242 -3251 1153 N ATOM 2245 CA MET A 314 6.529 23.867 115.038 1.00 87.79 C ANISOU 2245 CA MET A 314 8362 16659 8334 3106 -3204 1047 C ATOM 2246 C MET A 314 6.590 23.787 116.550 1.00 86.45 C ANISOU 2246 C MET A 314 8115 16433 8297 3181 -3078 977 C ATOM 2247 O MET A 314 7.660 23.862 117.152 1.00 84.20 O ANISOU 2247 O MET A 314 7997 15925 8070 3180 -3007 968 O ATOM 2248 CB MET A 314 6.852 22.500 114.418 1.00 86.72 C ANISOU 2248 CB MET A 314 8160 16663 8125 2751 -3199 977 C ATOM 2249 CG MET A 314 5.974 21.384 114.934 1.00 87.08 C ANISOU 2249 CG MET A 314 7907 16974 8203 2577 -3147 869 C ATOM 2250 SD MET A 314 4.239 21.760 114.660 1.00 90.66 S ANISOU 2250 SD MET A 314 8111 17708 8628 2726 -3224 893 S ATOM 2251 CE MET A 314 4.189 21.725 112.886 1.00 92.18 C ANISOU 2251 CE MET A 314 8388 17975 8661 2613 -3368 956 C ATOM 2252 N GLY A 315 5.420 23.656 117.151 1.00 97.18 N ANISOU 2252 N GLY A 315 9223 18004 9699 3249 -3051 929 N ATOM 2253 CA GLY A 315 5.283 23.498 118.587 1.00 97.09 C ANISOU 2253 CA GLY A 315 9097 17993 9800 3305 -2929 855 C ATOM 2254 C GLY A 315 4.132 22.570 118.890 1.00100.17 C ANISOU 2254 C GLY A 315 9163 18709 10186 3163 -2896 778 C ATOM 2255 O GLY A 315 3.587 21.944 117.971 1.00103.25 O ANISOU 2255 O GLY A 315 9437 19304 10491 2989 -2966 775 O ATOM 2256 N PRO A 316 3.746 22.455 120.161 1.00100.53 N ANISOU 2256 N PRO A 316 9066 18810 10319 3221 -2789 716 N ATOM 2257 CA PRO A 316 2.662 21.553 120.503 1.00100.39 C ANISOU 2257 CA PRO A 316 8746 19104 10293 3068 -2749 649 C ATOM 2258 C PRO A 316 1.281 22.086 120.139 1.00103.56 C ANISOU 2258 C PRO A 316 8976 19733 10640 3235 -2816 677 C ATOM 2259 O PRO A 316 0.428 21.332 119.631 1.00101.87 O ANISOU 2259 O PRO A 316 8558 19789 10361 3058 -2852 655 O ATOM 2260 CB PRO A 316 2.823 21.369 122.001 1.00100.52 C ANISOU 2260 CB PRO A 316 8701 19078 10414 3091 -2608 584 C ATOM 2261 CG PRO A 316 3.663 22.540 122.491 1.00101.16 C ANISOU 2261 CG PRO A 316 9033 18843 10559 3363 -2587 623 C ATOM 2262 CD PRO A 316 4.189 23.263 121.268 1.00 99.83 C ANISOU 2262 CD PRO A 316 9096 18509 10328 3448 -2709 714 C ATOM 2263 N ALA A 317 1.031 23.371 120.400 1.00 94.85 N ANISOU 2263 N ALA A 317 7955 18524 9561 3570 -2835 723 N ATOM 2264 CA ALA A 317 -0.223 23.995 120.000 1.00 97.22 C ANISOU 2264 CA ALA A 317 8114 19019 9806 3759 -2910 756 C ATOM 2265 C ALA A 317 -0.367 24.019 118.487 1.00 98.51 C ANISOU 2265 C ALA A 317 8322 19241 9865 3695 -3054 825 C ATOM 2266 O ALA A 317 -1.374 23.554 117.946 1.00100.60 O ANISOU 2266 O ALA A 317 8375 19789 10058 3602 -3105 817 O ATOM 2267 CB ALA A 317 -0.286 25.412 120.569 1.00 98.18 C ANISOU 2267 CB ALA A 317 8364 18961 9979 4132 -2904 788 C ATOM 2268 N LYS A 318 0.632 24.564 117.787 1.00 97.38 N ANISOU 2268 N LYS A 318 8458 18837 9706 3738 -3119 896 N ATOM 2269 CA LYS A 318 0.495 24.780 116.350 1.00 98.85 C ANISOU 2269 CA LYS A 318 8712 19061 9787 3716 -3261 975 C ATOM 2270 C LYS A 318 0.359 23.468 115.585 1.00 98.64 C ANISOU 2270 C LYS A 318 8552 19246 9680 3369 -3288 933 C ATOM 2271 O LYS A 318 -0.278 23.434 114.526 1.00100.71 O ANISOU 2271 O LYS A 318 8746 19672 9846 3333 -3396 971 O ATOM 2272 CB LYS A 318 1.681 25.591 115.830 1.00 97.57 C ANISOU 2272 CB LYS A 318 8890 18564 9619 3807 -3312 1061 C ATOM 2273 CG LYS A 318 1.539 26.054 114.390 1.00 99.36 C ANISOU 2273 CG LYS A 318 9218 18801 9735 3834 -3462 1160 C ATOM 2274 CD LYS A 318 2.305 25.156 113.448 1.00 97.85 C ANISOU 2274 CD LYS A 318 9109 18610 9460 3527 -3493 1158 C ATOM 2275 CE LYS A 318 2.825 25.931 112.256 1.00 98.53 C ANISOU 2275 CE LYS A 318 9444 18534 9458 3591 -3611 1276 C ATOM 2276 NZ LYS A 318 3.092 25.026 111.110 1.00 98.24 N ANISOU 2276 NZ LYS A 318 9410 18612 9304 3301 -3666 1267 N ATOM 2277 N LEU A 319 0.940 22.383 116.095 1.00 96.30 N ANISOU 2277 N LEU A 319 8223 18945 9421 3109 -3194 853 N ATOM 2278 CA LEU A 319 0.671 21.070 115.519 1.00 96.37 C ANISOU 2278 CA LEU A 319 8085 19166 9365 2770 -3208 794 C ATOM 2279 C LEU A 319 -0.759 20.645 115.814 1.00 98.77 C ANISOU 2279 C LEU A 319 8076 19797 9657 2740 -3196 751 C ATOM 2280 O LEU A 319 -1.513 20.265 114.909 1.00100.77 O ANISOU 2280 O LEU A 319 8205 20265 9818 2628 -3280 757 O ATOM 2281 CB LEU A 319 1.668 20.048 116.069 1.00 93.36 C ANISOU 2281 CB LEU A 319 7760 18677 9037 2508 -3108 717 C ATOM 2282 CG LEU A 319 1.549 18.582 115.661 1.00 93.09 C ANISOU 2282 CG LEU A 319 7604 18810 8955 2128 -3102 638 C ATOM 2283 CD1 LEU A 319 2.932 17.960 115.668 1.00 90.12 C ANISOU 2283 CD1 LEU A 319 7420 18223 8598 1926 -3056 598 C ATOM 2284 CD2 LEU A 319 0.650 17.816 116.612 1.00 93.78 C ANISOU 2284 CD2 LEU A 319 7424 19114 9094 2013 -3016 564 C ATOM 2285 N PHE A 320 -1.141 20.693 117.088 1.00 98.68 N ANISOU 2285 N PHE A 320 7935 19831 9730 2833 -3089 707 N ATOM 2286 CA PHE A 320 -2.516 20.395 117.461 1.00101.14 C ANISOU 2286 CA PHE A 320 7951 20456 10022 2829 -3068 672 C ATOM 2287 C PHE A 320 -3.485 21.357 116.788 1.00104.32 C ANISOU 2287 C PHE A 320 8291 20987 10357 3084 -3177 739 C ATOM 2288 O PHE A 320 -4.578 20.959 116.370 1.00106.75 O ANISOU 2288 O PHE A 320 8379 21586 10595 3005 -3223 730 O ATOM 2289 CB PHE A 320 -2.663 20.442 118.983 1.00100.49 C ANISOU 2289 CB PHE A 320 7772 20373 10035 2919 -2929 619 C ATOM 2290 CG PHE A 320 -2.259 19.167 119.668 1.00 98.44 C ANISOU 2290 CG PHE A 320 7447 20134 9822 2602 -2823 541 C ATOM 2291 CD1 PHE A 320 -2.749 17.951 119.227 1.00 99.13 C ANISOU 2291 CD1 PHE A 320 7375 20437 9854 2276 -2837 498 C ATOM 2292 CD2 PHE A 320 -1.389 19.179 120.744 1.00 95.95 C ANISOU 2292 CD2 PHE A 320 7238 19614 9605 2625 -2713 510 C ATOM 2293 CE1 PHE A 320 -2.386 16.773 119.850 1.00 97.42 C ANISOU 2293 CE1 PHE A 320 7114 20221 9682 1976 -2744 429 C ATOM 2294 CE2 PHE A 320 -1.024 18.003 121.366 1.00 94.21 C ANISOU 2294 CE2 PHE A 320 6960 19408 9427 2332 -2621 443 C ATOM 2295 CZ PHE A 320 -1.524 16.800 120.918 1.00 94.96 C ANISOU 2295 CZ PHE A 320 6904 19708 9469 2006 -2637 403 C ATOM 2296 N LYS A 321 -3.096 22.628 116.658 1.00114.87 N ANISOU 2296 N LYS A 321 9827 22105 11713 3386 -3225 811 N ATOM 2297 CA LYS A 321 -3.913 23.572 115.906 1.00118.51 C ANISOU 2297 CA LYS A 321 10264 22655 12109 3626 -3345 885 C ATOM 2298 C LYS A 321 -4.084 23.137 114.463 1.00122.34 C ANISOU 2298 C LYS A 321 10743 23261 12481 3448 -3471 924 C ATOM 2299 O LYS A 321 -5.047 23.551 113.815 1.00124.85 O ANISOU 2299 O LYS A 321 10948 23761 12728 3567 -3569 967 O ATOM 2300 CB LYS A 321 -3.304 24.974 115.950 1.00118.54 C ANISOU 2300 CB LYS A 321 10531 22354 12155 3947 -3380 961 C ATOM 2301 N TYR A 322 -3.173 22.314 113.949 1.00116.35 N ANISOU 2301 N TYR A 322 10104 22405 11699 3168 -3472 905 N ATOM 2302 CA TYR A 322 -3.299 21.775 112.603 1.00117.77 C ANISOU 2302 CA TYR A 322 10280 22703 11765 2964 -3581 924 C ATOM 2303 C TYR A 322 -4.153 20.516 112.577 1.00119.65 C ANISOU 2303 C TYR A 322 10248 23250 11962 2679 -3558 843 C ATOM 2304 O TYR A 322 -5.013 20.372 111.705 1.00126.27 O ANISOU 2304 O TYR A 322 10958 24312 12707 2633 -3654 861 O ATOM 2305 CB TYR A 322 -1.909 21.498 112.021 1.00114.78 C ANISOU 2305 CB TYR A 322 10168 22076 11367 2798 -3592 935 C ATOM 2306 CG TYR A 322 -1.881 20.523 110.866 1.00115.41 C ANISOU 2306 CG TYR A 322 10232 22280 11338 2489 -3660 909 C ATOM 2307 CD1 TYR A 322 -2.023 20.962 109.556 1.00115.81 C ANISOU 2307 CD1 TYR A 322 10367 22359 11277 2530 -3796 985 C ATOM 2308 CD2 TYR A 322 -1.691 19.165 111.083 1.00115.36 C ANISOU 2308 CD2 TYR A 322 10140 22351 11339 2153 -3589 806 C ATOM 2309 CE1 TYR A 322 -1.991 20.073 108.498 1.00116.00 C ANISOU 2309 CE1 TYR A 322 10385 22494 11196 2248 -3855 953 C ATOM 2310 CE2 TYR A 322 -1.658 18.272 110.034 1.00115.61 C ANISOU 2310 CE2 TYR A 322 10173 22480 11272 1870 -3649 771 C ATOM 2311 CZ TYR A 322 -1.807 18.730 108.745 1.00116.17 C ANISOU 2311 CZ TYR A 322 10325 22585 11229 1920 -3780 841 C ATOM 2312 OH TYR A 322 -1.773 17.838 107.700 1.00116.97 O ANISOU 2312 OH TYR A 322 10433 22782 11227 1638 -3836 797 O ATOM 2313 N ILE A 323 -3.938 19.598 113.520 1.00117.63 N ANISOU 2313 N ILE A 323 9910 23009 11775 2481 -3435 756 N ATOM 2314 CA ILE A 323 -4.767 18.398 113.575 1.00117.63 C ANISOU 2314 CA ILE A 323 9663 23289 11741 2198 -3408 682 C ATOM 2315 C ILE A 323 -6.221 18.769 113.825 1.00120.40 C ANISOU 2315 C ILE A 323 9753 23930 12065 2362 -3425 695 C ATOM 2316 O ILE A 323 -7.138 18.194 113.229 1.00122.15 O ANISOU 2316 O ILE A 323 9789 24417 12203 2210 -3481 681 O ATOM 2317 CB ILE A 323 -4.243 17.433 114.653 1.00110.26 C ANISOU 2317 CB ILE A 323 8707 22291 10895 1975 -3268 596 C ATOM 2318 CG1 ILE A 323 -2.737 17.255 114.529 1.00104.82 C ANISOU 2318 CG1 ILE A 323 8290 21295 10242 1875 -3246 587 C ATOM 2319 CG2 ILE A 323 -4.925 16.083 114.535 1.00110.16 C ANISOU 2319 CG2 ILE A 323 8494 22521 10839 1627 -3253 525 C ATOM 2320 CD1 ILE A 323 -2.195 16.205 115.466 1.00101.07 C ANISOU 2320 CD1 ILE A 323 7798 20757 9846 1625 -3122 501 C ATOM 2321 N ALA A 324 -6.454 19.736 114.708 1.00128.77 N ANISOU 2321 N ALA A 324 10793 24944 13188 2673 -3376 719 N ATOM 2322 CA ALA A 324 -7.807 20.169 115.025 1.00137.80 C ANISOU 2322 CA ALA A 324 11694 26360 14305 2858 -3383 727 C ATOM 2323 C ALA A 324 -8.388 21.006 113.896 1.00146.36 C ANISOU 2323 C ALA A 324 12786 27523 15301 3056 -3535 808 C ATOM 2324 O ALA A 324 -9.273 20.549 113.166 1.00147.91 O ANISOU 2324 O ALA A 324 12807 27988 15406 2933 -3609 808 O ATOM 2325 CB ALA A 324 -7.819 20.964 116.329 1.00125.49 C ANISOU 2325 CB ALA A 324 10134 24709 12837 3137 -3281 717 C ATOM 2326 N LYS A 325 -7.885 22.228 113.739 1.00167.28 N ANISOU 2326 N LYS A 325 15646 29936 17978 3356 -3584 879 N ATOM 2327 CA LYS A 325 -8.402 23.162 112.744 1.00167.14 C ANISOU 2327 CA LYS A 325 15659 29961 17885 3580 -3730 968 C ATOM 2328 C LYS A 325 -8.101 22.743 111.316 1.00162.78 C ANISOU 2328 C LYS A 325 15201 29414 17235 3378 -3851 1007 C ATOM 2329 O LYS A 325 -8.290 23.571 110.415 1.00166.38 O ANISOU 2329 O LYS A 325 15741 29845 17630 3558 -3978 1094 O ATOM 2330 CB LYS A 325 -7.849 24.564 113.002 1.00168.31 C ANISOU 2330 CB LYS A 325 16041 29814 18094 3935 -3747 1036 C ATOM 2331 N LEU A 326 -7.637 21.512 111.063 1.00149.47 N ANISOU 2331 N LEU A 326 13513 27751 15528 3016 -3818 946 N ATOM 2332 CA LEU A 326 -7.532 21.043 109.686 1.00143.39 C ANISOU 2332 CA LEU A 326 12799 27036 14649 2813 -3933 969 C ATOM 2333 C LEU A 326 -7.767 19.539 109.565 1.00138.73 C ANISOU 2333 C LEU A 326 12054 26636 14020 2416 -3894 875 C ATOM 2334 O LEU A 326 -7.356 18.946 108.561 1.00134.54 O ANISOU 2334 O LEU A 326 11618 26086 13414 2189 -3958 866 O ATOM 2335 CB LEU A 326 -6.168 21.406 109.085 1.00138.68 C ANISOU 2335 CB LEU A 326 12534 26112 14048 2812 -3969 1019 C ATOM 2336 N LEU A 327 -8.410 18.910 110.545 1.00134.50 N ANISOU 2336 N LEU A 327 11295 26277 13531 2322 -3792 804 N ATOM 2337 CA LEU A 327 -8.802 17.508 110.439 1.00119.01 C ANISOU 2337 CA LEU A 327 9173 24515 11531 1946 -3763 721 C ATOM 2338 C LEU A 327 -9.831 17.156 111.510 1.00120.42 C ANISOU 2338 C LEU A 327 9072 24940 11743 1933 -3670 675 C ATOM 2339 O LEU A 327 -10.715 16.322 111.296 1.00122.37 O ANISOU 2339 O LEU A 327 9110 25458 11927 1715 -3683 637 O ATOM 2340 CB LEU A 327 -7.585 16.591 110.553 1.00115.65 C ANISOU 2340 CB LEU A 327 8927 23865 11148 1660 -3694 657 C ATOM 2341 N ASP A 330 -11.599 21.103 116.225 1.00123.62 N ANISOU 2341 N ASP A 330 9163 25393 12413 3327 -3357 711 N ATOM 2342 CA ASP A 330 -11.880 21.091 117.654 1.00123.41 C ANISOU 2342 CA ASP A 330 9018 25426 12446 3397 -3213 655 C ATOM 2343 C ASP A 330 -10.728 20.449 118.432 1.00119.61 C ANISOU 2343 C ASP A 330 8683 24703 12058 3201 -3096 607 C ATOM 2344 O ASP A 330 -10.637 19.225 118.517 1.00118.58 O ANISOU 2344 O ASP A 330 8478 24656 11922 2852 -3048 562 O ATOM 2345 CB ASP A 330 -13.191 20.351 117.934 1.00126.13 C ANISOU 2345 CB ASP A 330 9027 26179 12717 3247 -3179 614 C ATOM 2346 CG ASP A 330 -14.407 21.064 117.345 1.00130.15 C ANISOU 2346 CG ASP A 330 9365 26951 13136 3480 -3282 656 C ATOM 2347 OD1 ASP A 330 -14.340 22.297 117.155 1.00130.97 O ANISOU 2347 OD1 ASP A 330 9589 26920 13254 3830 -3344 705 O ATOM 2348 OD2 ASP A 330 -15.434 20.397 117.078 1.00132.62 O ANISOU 2348 OD2 ASP A 330 9425 27603 13362 3313 -3303 642 O ATOM 2349 N VAL A 331 -9.848 21.281 118.997 1.00117.63 N ANISOU 2349 N VAL A 331 8651 24149 11895 3425 -3053 618 N ATOM 2350 CA VAL A 331 -8.711 20.747 119.742 1.00114.06 C ANISOU 2350 CA VAL A 331 8346 23459 11533 3263 -2946 577 C ATOM 2351 C VAL A 331 -9.176 20.133 121.053 1.00114.07 C ANISOU 2351 C VAL A 331 8154 23623 11565 3161 -2801 507 C ATOM 2352 O VAL A 331 -8.554 19.198 121.566 1.00111.72 O ANISOU 2352 O VAL A 331 7885 23250 11315 2895 -2716 464 O ATOM 2353 CB VAL A 331 -7.650 21.841 119.965 1.00112.13 C ANISOU 2353 CB VAL A 331 8391 22845 11367 3532 -2945 611 C ATOM 2354 CG1 VAL A 331 -8.175 22.923 120.895 1.00113.65 C ANISOU 2354 CG1 VAL A 331 8545 23045 11592 3890 -2893 603 C ATOM 2355 CG2 VAL A 331 -6.373 21.232 120.511 1.00108.39 C ANISOU 2355 CG2 VAL A 331 8085 22122 10977 3338 -2855 575 C ATOM 2356 N ALA A 332 -10.285 20.625 121.603 1.00116.83 N ANISOU 2356 N ALA A 332 8306 24206 11880 3362 -2773 497 N ATOM 2357 CA ALA A 332 -10.852 20.022 122.799 1.00117.28 C ANISOU 2357 CA ALA A 332 8159 24460 11942 3254 -2640 437 C ATOM 2358 C ALA A 332 -11.249 18.568 122.581 1.00118.00 C ANISOU 2358 C ALA A 332 8077 24776 11984 2836 -2625 410 C ATOM 2359 O ALA A 332 -11.376 17.821 123.556 1.00117.02 O ANISOU 2359 O ALA A 332 7843 24741 11878 2654 -2508 365 O ATOM 2360 CB ALA A 332 -12.064 20.829 123.264 1.00123.02 C ANISOU 2360 CB ALA A 332 8694 25433 12617 3549 -2630 432 C ATOM 2361 N ASP A 333 -11.446 18.147 121.328 1.00118.45 N ANISOU 2361 N ASP A 333 8116 24917 11974 2674 -2742 439 N ATOM 2362 CA ASP A 333 -11.848 16.774 121.046 1.00118.95 C ANISOU 2362 CA ASP A 333 8030 25182 11985 2270 -2738 411 C ATOM 2363 C ASP A 333 -10.699 15.781 121.180 1.00115.55 C ANISOU 2363 C ASP A 333 7764 24518 11622 1953 -2687 378 C ATOM 2364 O ASP A 333 -10.953 14.585 121.362 1.00115.65 O ANISOU 2364 O ASP A 333 7666 24660 11615 1612 -2644 342 O ATOM 2365 CB ASP A 333 -12.453 16.677 119.643 1.00121.22 C ANISOU 2365 CB ASP A 333 8249 25637 12172 2207 -2885 446 C ATOM 2366 N ILE A 334 -9.453 16.239 121.102 1.00112.69 N ANISOU 2366 N ILE A 334 7667 23815 11336 2055 -2693 390 N ATOM 2367 CA ILE A 334 -8.294 15.358 121.180 1.00109.49 C ANISOU 2367 CA ILE A 334 7431 23177 10993 1776 -2651 358 C ATOM 2368 C ILE A 334 -7.870 15.219 122.634 1.00107.66 C ANISOU 2368 C ILE A 334 7211 22845 10852 1778 -2503 321 C ATOM 2369 O ILE A 334 -7.740 16.216 123.354 1.00107.39 O ANISOU 2369 O ILE A 334 7224 22716 10864 2087 -2455 332 O ATOM 2370 CB ILE A 334 -7.138 15.891 120.321 1.00107.43 C ANISOU 2370 CB ILE A 334 7449 22614 10756 1870 -2734 392 C ATOM 2371 CG1 ILE A 334 -7.635 16.254 118.924 1.00109.57 C ANISOU 2371 CG1 ILE A 334 7709 22993 10930 1931 -2884 439 C ATOM 2372 CG2 ILE A 334 -6.026 14.861 120.243 1.00104.51 C ANISOU 2372 CG2 ILE A 334 7234 22044 10431 1551 -2704 352 C ATOM 2373 CD1 ILE A 334 -6.598 16.937 118.074 1.00107.98 C ANISOU 2373 CD1 ILE A 334 7779 22511 10735 2061 -2970 486 C ATOM 2374 N LYS A 335 -7.644 13.982 123.066 1.00106.50 N ANISOU 2374 N LYS A 335 7031 22705 10728 1430 -2432 278 N ATOM 2375 CA LYS A 335 -7.281 13.700 124.444 1.00104.90 C ANISOU 2375 CA LYS A 335 6828 22425 10604 1386 -2291 246 C ATOM 2376 C LYS A 335 -6.204 12.624 124.463 1.00102.09 C ANISOU 2376 C LYS A 335 6623 21857 10308 1059 -2260 213 C ATOM 2377 O LYS A 335 -5.925 11.977 123.452 1.00101.78 O ANISOU 2377 O LYS A 335 6656 21779 10239 836 -2341 205 O ATOM 2378 CB LYS A 335 -8.503 13.266 125.262 1.00107.35 C ANISOU 2378 CB LYS A 335 6869 23053 10866 1303 -2214 229 C ATOM 2379 N GLY A 336 -5.594 12.440 125.630 1.00116.33 N ANISOU 2379 N GLY A 336 8481 23522 12196 1033 -2143 189 N ATOM 2380 CA GLY A 336 -4.552 11.442 125.784 1.00113.96 C ANISOU 2380 CA GLY A 336 8325 23013 11962 738 -2104 156 C ATOM 2381 C GLY A 336 -3.156 11.908 125.430 1.00114.81 C ANISOU 2381 C GLY A 336 8698 22793 12134 846 -2135 160 C ATOM 2382 O GLY A 336 -2.388 11.151 124.819 1.00115.29 O ANISOU 2382 O GLY A 336 8892 22709 12204 604 -2173 137 O ATOM 2383 N TYR A 337 -2.800 13.134 125.800 1.00105.26 N ANISOU 2383 N TYR A 337 7576 21456 10962 1200 -2120 187 N ATOM 2384 CA TYR A 337 -1.495 13.703 125.510 1.00100.41 C ANISOU 2384 CA TYR A 337 7217 20532 10402 1331 -2149 200 C ATOM 2385 C TYR A 337 -0.793 14.067 126.808 1.00 96.10 C ANISOU 2385 C TYR A 337 6750 19810 9954 1465 -2032 187 C ATOM 2386 O TYR A 337 -1.424 14.490 127.782 1.00 95.72 O ANISOU 2386 O TYR A 337 6581 19871 9917 1624 -1954 183 O ATOM 2387 CB TYR A 337 -1.613 14.946 124.625 1.00101.63 C ANISOU 2387 CB TYR A 337 7452 20652 10510 1647 -2256 254 C ATOM 2388 CG TYR A 337 -2.783 15.834 124.988 1.00104.62 C ANISOU 2388 CG TYR A 337 7668 21230 10854 1928 -2249 276 C ATOM 2389 CD1 TYR A 337 -2.646 16.851 125.922 1.00104.90 C ANISOU 2389 CD1 TYR A 337 7754 21159 10944 2238 -2183 281 C ATOM 2390 CD2 TYR A 337 -4.029 15.654 124.396 1.00107.58 C ANISOU 2390 CD2 TYR A 337 7840 21899 11136 1883 -2311 286 C ATOM 2391 CE1 TYR A 337 -3.715 17.662 126.256 1.00108.37 C ANISOU 2391 CE1 TYR A 337 8052 21778 11346 2499 -2177 291 C ATOM 2392 CE2 TYR A 337 -5.101 16.461 124.726 1.00110.96 C ANISOU 2392 CE2 TYR A 337 8114 22520 11527 2144 -2306 302 C ATOM 2393 CZ TYR A 337 -4.940 17.463 125.655 1.00111.42 C ANISOU 2393 CZ TYR A 337 8230 22465 11639 2453 -2239 302 C ATOM 2394 OH TYR A 337 -6.007 18.265 125.985 1.00114.83 O ANISOU 2394 OH TYR A 337 8515 23087 12029 2716 -2235 308 O ATOM 2395 N ARG A 338 0.523 13.911 126.816 1.00102.13 N ANISOU 2395 N ARG A 338 7719 20304 10781 1403 -2022 176 N ATOM 2396 CA ARG A 338 1.255 14.178 128.040 1.00 99.65 C ANISOU 2396 CA ARG A 338 7485 19816 10560 1507 -1912 162 C ATOM 2397 C ARG A 338 1.344 15.670 128.312 1.00 97.96 C ANISOU 2397 C ARG A 338 7364 19490 10364 1920 -1914 195 C ATOM 2398 O ARG A 338 1.401 16.503 127.401 1.00 99.01 O ANISOU 2398 O ARG A 338 7602 19560 10459 2111 -2014 237 O ATOM 2399 CB ARG A 338 2.641 13.562 127.994 1.00 97.52 C ANISOU 2399 CB ARG A 338 7402 19299 10351 1319 -1899 139 C ATOM 2400 CG ARG A 338 2.731 12.342 127.109 1.00 97.51 C ANISOU 2400 CG ARG A 338 7383 19350 10315 936 -1945 108 C ATOM 2401 CD ARG A 338 3.979 12.409 126.392 1.00 95.66 C ANISOU 2401 CD ARG A 338 7424 18801 10122 853 -1954 94 C ATOM 2402 NE ARG A 338 4.371 13.798 126.268 1.00 94.98 N ANISOU 2402 NE ARG A 338 7513 18547 10029 1168 -2002 142 N ATOM 2403 CZ ARG A 338 5.515 14.175 125.728 1.00 91.68 C ANISOU 2403 CZ ARG A 338 7408 17773 9655 1160 -1982 143 C ATOM 2404 NH1 ARG A 338 6.345 13.251 125.258 1.00 89.09 N ANISOU 2404 NH1 ARG A 338 7237 17234 9380 870 -1916 92 N ATOM 2405 NH2 ARG A 338 5.841 15.467 125.654 1.00 93.04 N ANISOU 2405 NH2 ARG A 338 7739 17797 9815 1441 -2029 197 N ATOM 2406 N ILE A 339 1.344 15.998 129.591 1.00 84.57 N ANISOU 2406 N ILE A 339 5641 17765 8725 2051 -1803 175 N ATOM 2407 CA ILE A 339 1.038 17.337 130.056 1.00 85.59 C ANISOU 2407 CA ILE A 339 5804 17854 8860 2431 -1788 190 C ATOM 2408 C ILE A 339 2.277 17.952 130.690 1.00 83.14 C ANISOU 2408 C ILE A 339 5723 17228 8639 2590 -1737 186 C ATOM 2409 O ILE A 339 3.164 17.251 131.194 1.00 80.89 O ANISOU 2409 O ILE A 339 5501 16817 8416 2405 -1673 162 O ATOM 2410 CB ILE A 339 -0.155 17.274 131.035 1.00 87.71 C ANISOU 2410 CB ILE A 339 5840 18385 9102 2468 -1700 161 C ATOM 2411 CG1 ILE A 339 -0.549 18.659 131.523 1.00 89.08 C ANISOU 2411 CG1 ILE A 339 6045 18527 9272 2863 -1685 163 C ATOM 2412 CG2 ILE A 339 0.129 16.355 132.166 1.00 86.38 C ANISOU 2412 CG2 ILE A 339 5612 18224 8984 2245 -1574 122 C ATOM 2413 CD1 ILE A 339 -1.026 19.495 130.398 1.00 90.91 C ANISOU 2413 CD1 ILE A 339 6307 18789 9444 3064 -1813 207 C ATOM 2414 N ASP A 340 2.347 19.278 130.633 1.00 83.70 N ANISOU 2414 N ASP A 340 5929 17160 8714 2931 -1771 212 N ATOM 2415 CA ASP A 340 3.440 20.022 131.235 1.00 81.75 C ANISOU 2415 CA ASP A 340 5914 16604 8545 3114 -1727 211 C ATOM 2416 C ASP A 340 3.406 19.901 132.756 1.00 81.28 C ANISOU 2416 C ASP A 340 5786 16557 8539 3132 -1583 156 C ATOM 2417 O ASP A 340 2.388 19.553 133.363 1.00 82.94 O ANISOU 2417 O ASP A 340 5778 17020 8716 3084 -1522 127 O ATOM 2418 CB ASP A 340 3.347 21.496 130.837 1.00 86.21 C ANISOU 2418 CB ASP A 340 6636 17026 9094 3469 -1800 250 C ATOM 2419 CG ASP A 340 4.607 22.261 131.107 1.00 81.85 C ANISOU 2419 CG ASP A 340 6373 16114 8611 3625 -1788 264 C ATOM 2420 OD1 ASP A 340 4.906 22.512 132.294 1.00 83.20 O ANISOU 2420 OD1 ASP A 340 6586 16184 8844 3715 -1683 221 O ATOM 2421 OD2 ASP A 340 5.288 22.631 130.129 1.00 80.28 O ANISOU 2421 OD2 ASP A 340 6368 15737 8399 3656 -1884 319 O ATOM 2422 N LYS A 341 4.557 20.186 133.371 1.00 85.81 N ANISOU 2422 N LYS A 341 6555 16856 9192 3195 -1529 146 N ATOM 2423 CA LYS A 341 4.593 20.445 134.804 1.00 86.05 C ANISOU 2423 CA LYS A 341 6577 16847 9270 3299 -1402 98 C ATOM 2424 C LYS A 341 3.575 21.511 135.181 1.00 87.77 C ANISOU 2424 C LYS A 341 6741 17162 9446 3597 -1396 82 C ATOM 2425 O LYS A 341 2.886 21.398 136.202 1.00 88.93 O ANISOU 2425 O LYS A 341 6735 17476 9577 3613 -1301 37 O ATOM 2426 CB LYS A 341 5.997 20.891 135.211 1.00 85.51 C ANISOU 2426 CB LYS A 341 6771 16432 9286 3386 -1370 96 C ATOM 2427 CG LYS A 341 6.612 20.096 136.343 1.00 83.60 C ANISOU 2427 CG LYS A 341 6539 16111 9113 3185 -1231 52 C ATOM 2428 CD LYS A 341 6.712 18.646 135.948 1.00 82.80 C ANISOU 2428 CD LYS A 341 6370 16076 9016 2781 -1213 54 C ATOM 2429 CE LYS A 341 7.408 17.845 137.002 1.00 80.85 C ANISOU 2429 CE LYS A 341 6167 15714 8839 2562 -1074 18 C ATOM 2430 NZ LYS A 341 7.310 16.400 136.698 1.00 80.65 N ANISOU 2430 NZ LYS A 341 5996 15847 8800 2196 -1060 15 N ATOM 2431 N SER A 342 3.565 22.572 134.388 1.00 87.78 N ANISOU 2431 N SER A 342 6867 17065 9421 3829 -1500 120 N ATOM 2432 CA SER A 342 2.646 23.689 134.528 1.00 90.75 C ANISOU 2432 CA SER A 342 7232 17488 9761 4140 -1510 106 C ATOM 2433 C SER A 342 1.189 23.405 134.143 1.00 95.02 C ANISOU 2433 C SER A 342 7540 18355 10210 4144 -1572 120 C ATOM 2434 O SER A 342 0.262 23.933 134.757 1.00 91.65 O ANISOU 2434 O SER A 342 7052 18027 9743 4386 -1571 100 O ATOM 2435 CB SER A 342 3.160 24.896 133.737 1.00 89.85 C ANISOU 2435 CB SER A 342 7413 17052 9675 4402 -1589 143 C ATOM 2436 OG SER A 342 3.249 26.045 134.562 1.00 90.53 O ANISOU 2436 OG SER A 342 7582 17041 9775 4681 -1539 100 O ATOM 2437 N GLY A 343 0.999 22.598 133.098 1.00 87.81 N ANISOU 2437 N GLY A 343 6498 17608 9259 3886 -1628 151 N ATOM 2438 CA GLY A 343 -0.320 22.358 132.545 1.00 90.57 C ANISOU 2438 CA GLY A 343 6610 18286 9519 3853 -1679 161 C ATOM 2439 C GLY A 343 -0.474 22.624 131.062 1.00 91.53 C ANISOU 2439 C GLY A 343 6777 18410 9591 3881 -1827 224 C ATOM 2440 O GLY A 343 -1.598 22.537 130.556 1.00 94.06 O ANISOU 2440 O GLY A 343 6905 18999 9833 3883 -1879 235 O ATOM 2441 N LYS A 344 0.598 22.939 130.344 1.00 89.73 N ANISOU 2441 N LYS A 344 6794 17903 9397 3899 -1898 269 N ATOM 2442 CA LYS A 344 0.523 23.041 128.896 1.00 90.49 C ANISOU 2442 CA LYS A 344 6936 18009 9436 3877 -2037 333 C ATOM 2443 C LYS A 344 0.673 21.664 128.264 1.00 89.45 C ANISOU 2443 C LYS A 344 6700 18009 9276 3504 -2059 333 C ATOM 2444 O LYS A 344 1.376 20.789 128.776 1.00 87.23 O ANISOU 2444 O LYS A 344 6430 17669 9045 3279 -1984 300 O ATOM 2445 CB LYS A 344 1.603 23.982 128.358 1.00 89.20 C ANISOU 2445 CB LYS A 344 7092 17493 9306 4045 -2107 387 C ATOM 2446 N ALA A 345 0.016 21.436 127.148 1.00 91.19 N ANISOU 2446 N ALA A 345 6823 18410 9417 3435 -2163 367 N ATOM 2447 CA ALA A 345 0.165 20.156 126.514 1.00 90.39 C ANISOU 2447 CA ALA A 345 6652 18411 9280 3083 -2197 363 C ATOM 2448 C ALA A 345 1.483 20.159 125.776 1.00 87.89 C ANISOU 2448 C ALA A 345 6594 17816 8986 3006 -2250 394 C ATOM 2449 O ALA A 345 1.971 21.195 125.375 1.00 87.61 O ANISOU 2449 O ALA A 345 6772 17558 8957 3232 -2307 445 O ATOM 2450 CB ALA A 345 -0.986 19.874 125.578 1.00 93.09 C ANISOU 2450 CB ALA A 345 6826 19022 9523 3032 -2298 388 C ATOM 2451 N GLU A 346 2.060 18.985 125.609 1.00 86.43 N ANISOU 2451 N GLU A 346 6394 17638 8808 2679 -2229 363 N ATOM 2452 CA GLU A 346 3.325 18.852 124.921 1.00 88.42 C ANISOU 2452 CA GLU A 346 6872 17657 9065 2572 -2275 382 C ATOM 2453 C GLU A 346 3.375 17.592 124.083 1.00 84.04 C ANISOU 2453 C GLU A 346 6240 17237 8453 2213 -2321 355 C ATOM 2454 O GLU A 346 2.690 16.624 124.356 1.00 84.97 O ANISOU 2454 O GLU A 346 6149 17577 8561 2002 -2282 311 O ATOM 2455 CB GLU A 346 4.476 18.850 125.938 1.00 87.17 C ANISOU 2455 CB GLU A 346 6857 17258 9005 2574 -2175 354 C ATOM 2456 CG GLU A 346 4.412 17.749 126.984 1.00 87.21 C ANISOU 2456 CG GLU A 346 6700 17367 9069 2366 -2053 286 C ATOM 2457 CD GLU A 346 5.407 17.947 128.105 1.00 85.03 C ANISOU 2457 CD GLU A 346 6638 16762 8909 2373 -1921 259 C ATOM 2458 OE1 GLU A 346 6.270 18.836 127.978 1.00 85.25 O ANISOU 2458 OE1 GLU A 346 6934 16487 8972 2540 -1925 291 O ATOM 2459 OE2 GLU A 346 5.323 17.212 129.110 1.00 83.99 O ANISOU 2459 OE2 GLU A 346 6421 16656 8833 2197 -1808 209 O ATOM 2460 N ILE A 347 4.195 17.609 123.051 1.00 82.77 N ANISOU 2460 N ILE A 347 6265 16936 8249 2141 -2404 382 N ATOM 2461 CA ILE A 347 4.329 16.453 122.206 1.00 82.64 C ANISOU 2461 CA ILE A 347 6220 17010 8168 1807 -2455 349 C ATOM 2462 C ILE A 347 5.621 16.533 121.432 1.00 80.66 C ANISOU 2462 C ILE A 347 6295 16429 7925 1741 -2458 361 C ATOM 2463 O ILE A 347 6.243 17.569 121.376 1.00 80.72 O ANISOU 2463 O ILE A 347 6507 16207 7955 1973 -2462 417 O ATOM 2464 CB ILE A 347 3.128 16.345 121.254 1.00 85.50 C ANISOU 2464 CB ILE A 347 6435 17620 8431 1784 -2551 371 C ATOM 2465 CG1 ILE A 347 2.987 14.927 120.730 1.00 85.65 C ANISOU 2465 CG1 ILE A 347 6376 17769 8397 1402 -2576 312 C ATOM 2466 CG2 ILE A 347 3.225 17.357 120.127 1.00 86.30 C ANISOU 2466 CG2 ILE A 347 6696 17630 8464 2007 -2666 452 C ATOM 2467 CD1 ILE A 347 2.047 14.819 119.569 1.00 88.36 C ANISOU 2467 CD1 ILE A 347 6591 18345 8639 1360 -2676 331 C ATOM 2468 N HIS A 348 6.037 15.430 120.848 1.00 79.77 N ANISOU 2468 N HIS A 348 6251 16257 7800 1412 -2440 305 N ATOM 2469 CA HIS A 348 7.234 15.426 120.043 1.00 78.29 C ANISOU 2469 CA HIS A 348 6364 15780 7602 1337 -2442 312 C ATOM 2470 C HIS A 348 6.990 16.165 118.736 1.00 80.02 C ANISOU 2470 C HIS A 348 6604 16111 7690 1483 -2598 389 C ATOM 2471 O HIS A 348 5.937 16.052 118.157 1.00 82.39 O ANISOU 2471 O HIS A 348 6672 16733 7901 1586 -2711 423 O ATOM 2472 CB HIS A 348 7.645 14.000 119.768 1.00 77.16 C ANISOU 2472 CB HIS A 348 6285 15563 7471 965 -2390 223 C ATOM 2473 CG HIS A 348 8.344 13.360 120.915 1.00 75.14 C ANISOU 2473 CG HIS A 348 6089 15110 7350 834 -2234 160 C ATOM 2474 ND1 HIS A 348 9.643 13.657 121.250 1.00 72.79 N ANISOU 2474 ND1 HIS A 348 6060 14452 7144 855 -2131 153 N ATOM 2475 CD2 HIS A 348 7.918 12.458 121.822 1.00 75.22 C ANISOU 2475 CD2 HIS A 348 5923 15243 7417 685 -2167 108 C ATOM 2476 CE1 HIS A 348 9.993 12.946 122.300 1.00 71.50 C ANISOU 2476 CE1 HIS A 348 5884 14196 7087 727 -2011 98 C ATOM 2477 NE2 HIS A 348 8.965 12.211 122.665 1.00 72.93 N ANISOU 2477 NE2 HIS A 348 5803 14659 7248 621 -2029 72 N ATOM 2478 N THR A 349 7.963 16.931 118.282 1.00 78.92 N ANISOU 2478 N THR A 349 6743 15710 7532 1491 -2603 421 N ATOM 2479 CA THR A 349 7.816 17.670 117.047 1.00 80.31 C ANISOU 2479 CA THR A 349 6995 15908 7612 1729 -2730 525 C ATOM 2480 C THR A 349 8.990 17.648 116.064 1.00 79.22 C ANISOU 2480 C THR A 349 7142 15532 7424 1617 -2737 542 C ATOM 2481 O THR A 349 9.236 18.632 115.396 1.00 80.72 O ANISOU 2481 O THR A 349 7437 15713 7523 1769 -2841 633 O ATOM 2482 CB THR A 349 7.385 19.117 117.300 1.00 80.47 C ANISOU 2482 CB THR A 349 7031 15840 7702 2077 -2711 588 C ATOM 2483 OG1 THR A 349 8.530 19.940 117.452 1.00 82.55 O ANISOU 2483 OG1 THR A 349 6984 16439 7943 2219 -2766 591 O ATOM 2484 CG2 THR A 349 6.530 19.227 118.516 1.00 81.00 C ANISOU 2484 CG2 THR A 349 7308 15748 7723 2331 -2794 698 C ATOM 2485 N PHE A 350 9.757 16.568 116.021 1.00 77.30 N ANISOU 2485 N PHE A 350 7020 15119 7232 1343 -2632 455 N ATOM 2486 CA PHE A 350 10.871 16.456 115.085 1.00 76.29 C ANISOU 2486 CA PHE A 350 7144 14792 7052 1205 -2624 452 C ATOM 2487 C PHE A 350 11.761 17.668 115.166 1.00 75.28 C ANISOU 2487 C PHE A 350 7273 14373 6956 1401 -2595 538 C ATOM 2488 O PHE A 350 12.251 18.148 114.176 1.00 75.54 O ANISOU 2488 O PHE A 350 7479 14328 6897 1407 -2651 595 O ATOM 2489 CB PHE A 350 10.347 16.304 113.671 1.00 78.22 C ANISOU 2489 CB PHE A 350 7337 15258 7126 1124 -2768 472 C ATOM 2490 CG PHE A 350 10.322 14.906 113.197 1.00 78.26 C ANISOU 2490 CG PHE A 350 7263 15379 7092 798 -2758 356 C ATOM 2491 CD1 PHE A 350 9.244 14.118 113.428 1.00 79.67 C ANISOU 2491 CD1 PHE A 350 7168 15848 7253 698 -2804 306 C ATOM 2492 CD2 PHE A 350 11.379 14.386 112.525 1.00 77.03 C ANISOU 2492 CD2 PHE A 350 7310 15047 6912 590 -2706 294 C ATOM 2493 CE1 PHE A 350 9.219 12.822 113.002 1.00 79.84 C ANISOU 2493 CE1 PHE A 350 7134 15961 7240 389 -2802 199 C ATOM 2494 CE2 PHE A 350 11.365 13.092 112.099 1.00 77.21 C ANISOU 2494 CE2 PHE A 350 7276 15161 6899 299 -2702 179 C ATOM 2495 CZ PHE A 350 10.279 12.307 112.330 1.00 78.61 C ANISOU 2495 CZ PHE A 350 7197 15609 7065 194 -2752 132 C ATOM 2496 N GLU A 351 11.992 18.155 116.360 1.00 79.41 N ANISOU 2496 N GLU A 351 7829 14736 7607 1552 -2505 547 N ATOM 2497 CA GLU A 351 12.754 19.362 116.534 1.00 80.81 C ANISOU 2497 CA GLU A 351 8233 14658 7814 1764 -2494 636 C ATOM 2498 C GLU A 351 14.157 19.274 116.011 1.00 80.04 C ANISOU 2498 C GLU A 351 8404 14300 7707 1609 -2432 632 C ATOM 2499 O GLU A 351 14.663 20.227 115.455 1.00 80.56 O ANISOU 2499 O GLU A 351 8662 14228 7718 1723 -2480 726 O ATOM 2500 CB GLU A 351 12.731 19.770 117.991 1.00 80.56 C ANISOU 2500 CB GLU A 351 8185 14501 7923 1916 -2397 623 C ATOM 2501 CG GLU A 351 13.394 21.095 118.261 1.00 79.95 C ANISOU 2501 CG GLU A 351 8343 14150 7884 2133 -2386 707 C ATOM 2502 CD GLU A 351 13.449 21.418 119.727 1.00 78.73 C ANISOU 2502 CD GLU A 351 8153 13906 7856 2297 -2303 686 C ATOM 2503 OE1 GLU A 351 12.901 20.667 120.536 1.00 78.51 O ANISOU 2503 OE1 GLU A 351 7920 14026 7884 2223 -2244 608 O ATOM 2504 OE2 GLU A 351 14.035 22.441 120.066 1.00 80.49 O ANISOU 2504 OE2 GLU A 351 8555 13913 8116 2492 -2299 749 O ATOM 2505 N ALA A 352 14.794 18.138 116.191 1.00 79.71 N ANISOU 2505 N ALA A 352 8381 14192 7714 1349 -2329 525 N ATOM 2506 CA ALA A 352 16.149 17.996 115.722 1.00 76.38 C ANISOU 2506 CA ALA A 352 8198 13538 7285 1206 -2259 509 C ATOM 2507 C ALA A 352 16.258 18.132 114.220 1.00 76.27 C ANISOU 2507 C ALA A 352 8256 13617 7108 1142 -2362 552 C ATOM 2508 O ALA A 352 17.123 18.808 113.719 1.00 74.12 O ANISOU 2508 O ALA A 352 8194 13182 6787 1179 -2365 622 O ATOM 2509 CB ALA A 352 16.691 16.666 116.165 1.00 75.14 C ANISOU 2509 CB ALA A 352 8029 13309 7213 956 -2134 378 C ATOM 2510 N TYR A 353 15.348 17.502 113.514 1.00 77.49 N ANISOU 2510 N TYR A 353 8235 14039 7166 1039 -2450 513 N ATOM 2511 CA TYR A 353 15.331 17.512 112.055 1.00 77.42 C ANISOU 2511 CA TYR A 353 8282 14145 6989 966 -2554 546 C ATOM 2512 C TYR A 353 15.116 18.920 111.516 1.00 75.67 C ANISOU 2512 C TYR A 353 8145 13925 6682 1209 -2668 700 C ATOM 2513 O TYR A 353 15.833 19.370 110.617 1.00 74.61 O ANISOU 2513 O TYR A 353 8200 13696 6453 1190 -2693 762 O ATOM 2514 CB TYR A 353 14.243 16.566 111.544 1.00 81.36 C ANISOU 2514 CB TYR A 353 8555 14951 7405 825 -2638 477 C ATOM 2515 CG TYR A 353 14.244 16.346 110.050 1.00 83.82 C ANISOU 2515 CG TYR A 353 8915 15394 7538 705 -2736 482 C ATOM 2516 CD1 TYR A 353 13.641 17.258 109.195 1.00 86.61 C ANISOU 2516 CD1 TYR A 353 9255 15897 7757 865 -2885 603 C ATOM 2517 CD2 TYR A 353 14.832 15.219 109.496 1.00 84.41 C ANISOU 2517 CD2 TYR A 353 9051 15447 7574 438 -2684 364 C ATOM 2518 CE1 TYR A 353 13.631 17.062 107.825 1.00 88.55 C ANISOU 2518 CE1 TYR A 353 9543 16274 7827 753 -2977 610 C ATOM 2519 CE2 TYR A 353 14.828 15.012 108.129 1.00 86.82 C ANISOU 2519 CE2 TYR A 353 9400 15881 7706 328 -2772 360 C ATOM 2520 CZ TYR A 353 14.221 15.936 107.298 1.00 89.08 C ANISOU 2520 CZ TYR A 353 9667 16324 7853 481 -2918 486 C ATOM 2521 OH TYR A 353 14.211 15.737 105.938 1.00 91.69 O ANISOU 2521 OH TYR A 353 10042 16794 8001 370 -3008 485 O ATOM 2522 N ARG A 354 14.181 19.619 112.093 1.00 75.68 N ANISOU 2522 N ARG A 354 8008 14037 6710 1442 -2739 765 N ATOM 2523 CA ARG A 354 13.905 20.920 111.603 1.00 77.28 C ANISOU 2523 CA ARG A 354 8295 14234 6835 1694 -2859 914 C ATOM 2524 C ARG A 354 15.115 21.796 111.683 1.00 76.05 C ANISOU 2524 C ARG A 354 8427 13750 6717 1763 -2797 988 C ATOM 2525 O ARG A 354 15.376 22.550 110.791 1.00 77.11 O ANISOU 2525 O ARG A 354 8719 13835 6746 1845 -2883 1104 O ATOM 2526 CB ARG A 354 12.701 21.503 112.338 1.00 78.62 C ANISOU 2526 CB ARG A 354 8278 14540 7052 1956 -2923 956 C ATOM 2527 CG ARG A 354 11.425 20.770 111.989 1.00 80.95 C ANISOU 2527 CG ARG A 354 8323 15195 7240 1980 -3060 961 C ATOM 2528 CD ARG A 354 10.433 20.732 113.119 1.00 81.35 C ANISOU 2528 CD ARG A 354 8119 15410 7380 2077 -3040 911 C ATOM 2529 NE ARG A 354 10.499 21.930 113.929 1.00 80.66 N ANISOU 2529 NE ARG A 354 8097 15133 7418 2316 -2978 945 N ATOM 2530 CZ ARG A 354 10.321 21.930 115.236 1.00 79.74 C ANISOU 2530 CZ ARG A 354 7843 15030 7425 2315 -2876 865 C ATOM 2531 NH1 ARG A 354 10.407 23.057 115.907 1.00 79.40 N ANISOU 2531 NH1 ARG A 354 7612 15163 7395 2077 -2830 759 N ATOM 2532 NH2 ARG A 354 10.056 20.799 115.862 1.00 79.18 N ANISOU 2532 NH2 ARG A 354 7831 14791 7461 2533 -2818 887 N ATOM 2533 N LYS A 355 15.866 21.702 112.753 1.00 78.30 N ANISOU 2533 N LYS A 355 8787 13813 7150 1726 -2651 928 N ATOM 2534 CA LYS A 355 17.070 22.510 112.888 1.00 76.69 C ANISOU 2534 CA LYS A 355 8852 13304 6984 1769 -2589 993 C ATOM 2535 C LYS A 355 18.153 22.037 111.929 1.00 74.09 C ANISOU 2535 C LYS A 355 8685 12896 6571 1536 -2545 974 C ATOM 2536 O LYS A 355 18.897 22.852 111.371 1.00 76.04 O ANISOU 2536 O LYS A 355 9145 12993 6756 1568 -2565 1073 O ATOM 2537 CB LYS A 355 17.566 22.474 114.329 1.00 74.50 C ANISOU 2537 CB LYS A 355 8596 12828 6883 1799 -2452 933 C ATOM 2538 CG LYS A 355 18.509 23.606 114.673 1.00 72.52 C ANISOU 2538 CG LYS A 355 8595 12280 6678 1920 -2417 1020 C ATOM 2539 CD LYS A 355 17.775 24.898 114.945 1.00 74.03 C ANISOU 2539 CD LYS A 355 8801 12459 6869 2228 -2523 1130 C ATOM 2540 CE LYS A 355 16.889 24.769 116.165 1.00 74.50 C ANISOU 2540 CE LYS A 355 8658 12611 7040 2370 -2495 1065 C ATOM 2541 NZ LYS A 355 16.332 26.083 116.576 1.00 77.19 N ANISOU 2541 NZ LYS A 355 9040 12893 7395 2691 -2579 1158 N ATOM 2542 N MET A 356 18.251 20.724 111.713 1.00 74.13 N ANISOU 2542 N MET A 356 8594 13005 6568 1299 -2488 846 N ATOM 2543 CA MET A 356 19.227 20.205 110.763 1.00 71.67 C ANISOU 2543 CA MET A 356 8419 12645 6166 1085 -2446 811 C ATOM 2544 C MET A 356 18.834 20.481 109.315 1.00 73.31 C ANISOU 2544 C MET A 356 8647 13030 6178 1076 -2584 887 C ATOM 2545 O MET A 356 19.689 20.394 108.427 1.00 72.70 O ANISOU 2545 O MET A 356 8720 12903 6000 943 -2564 895 O ATOM 2546 CB MET A 356 19.428 18.702 110.978 1.00 72.34 C ANISOU 2546 CB MET A 356 8407 12777 6302 847 -2348 643 C ATOM 2547 CG MET A 356 19.858 18.329 112.388 1.00 71.40 C ANISOU 2547 CG MET A 356 8271 12488 6370 837 -2211 567 C ATOM 2548 SD MET A 356 20.404 16.620 112.575 1.00 69.69 S ANISOU 2548 SD MET A 356 8011 12256 6212 553 -2089 383 S ATOM 2549 CE MET A 356 21.984 16.712 111.755 1.00 69.09 C ANISOU 2549 CE MET A 356 8184 12000 6065 437 -2016 384 C ATOM 2550 N LYS A 357 17.567 20.800 109.050 1.00 74.78 N ANISOU 2550 N LYS A 357 8679 13435 6300 1213 -2724 944 N ATOM 2551 CA LYS A 357 17.193 21.231 107.708 1.00 76.90 C ANISOU 2551 CA LYS A 357 8980 13861 6378 1235 -2868 1039 C ATOM 2552 C LYS A 357 17.640 22.655 107.421 1.00 77.59 C ANISOU 2552 C LYS A 357 9282 13781 6419 1413 -2922 1210 C ATOM 2553 O LYS A 357 17.727 23.037 106.253 1.00 79.02 O ANISOU 2553 O LYS A 357 9560 14028 6436 1393 -3014 1299 O ATOM 2554 CB LYS A 357 15.678 21.116 107.497 1.00 78.97 C ANISOU 2554 CB LYS A 357 8997 14428 6580 1329 -3008 1048 C ATOM 2555 N THR A 358 17.928 23.441 108.457 1.00 78.48 N ANISOU 2555 N THR A 358 9478 13675 6667 1578 -2870 1257 N ATOM 2556 CA THR A 358 18.366 24.820 108.291 1.00 78.22 C ANISOU 2556 CA THR A 358 9667 13451 6604 1745 -2922 1418 C ATOM 2557 C THR A 358 19.799 24.931 107.797 1.00 78.19 C ANISOU 2557 C THR A 358 9904 13250 6554 1578 -2837 1444 C ATOM 2558 O THR A 358 20.213 26.027 107.409 1.00 79.37 O ANISOU 2558 O THR A 358 10255 13259 6642 1669 -2892 1589 O ATOM 2559 CB THR A 358 18.243 25.570 109.617 1.00 77.48 C ANISOU 2559 CB THR A 358 9589 13178 6673 1964 -2887 1441 C ATOM 2560 OG1 THR A 358 19.072 24.928 110.590 1.00 74.29 O ANISOU 2560 OG1 THR A 358 9200 12613 6415 1832 -2716 1323 O ATOM 2561 CG2 THR A 358 16.803 25.571 110.113 1.00 79.45 C ANISOU 2561 CG2 THR A 358 9593 13637 6959 2156 -2972 1424 C ATOM 2562 N LEU A 359 20.567 23.846 107.828 1.00 76.83 N ANISOU 2562 N LEU A 359 9720 13062 6410 1340 -2706 1310 N ATOM 2563 CA LEU A 359 21.953 23.896 107.386 1.00 76.40 C ANISOU 2563 CA LEU A 359 9874 12845 6311 1179 -2615 1324 C ATOM 2564 C LEU A 359 22.031 24.317 105.926 1.00 78.65 C ANISOU 2564 C LEU A 359 10268 13233 6384 1134 -2720 1434 C ATOM 2565 O LEU A 359 21.249 23.862 105.091 1.00 78.72 O ANISOU 2565 O LEU A 359 10155 13484 6269 1097 -2816 1417 O ATOM 2566 CB LEU A 359 22.616 22.532 107.571 1.00 73.77 C ANISOU 2566 CB LEU A 359 9478 12521 6030 944 -2472 1146 C ATOM 2567 CG LEU A 359 22.792 22.020 109.000 1.00 70.86 C ANISOU 2567 CG LEU A 359 9032 12027 5866 949 -2347 1035 C ATOM 2568 CD1 LEU A 359 22.989 20.520 109.000 1.00 70.16 C ANISOU 2568 CD1 LEU A 359 8831 12025 5802 734 -2255 858 C ATOM 2569 CD2 LEU A 359 23.972 22.700 109.675 1.00 70.31 C ANISOU 2569 CD2 LEU A 359 9152 11675 5889 970 -2245 1081 C ATOM 2570 N GLU A 360 22.987 25.186 105.616 1.00 77.94 N ANISOU 2570 N GLU A 360 10409 12961 6245 1125 -2703 1551 N ATOM 2571 CA GLU A 360 23.109 25.721 104.269 1.00 80.55 C ANISOU 2571 CA GLU A 360 10865 13372 6368 1088 -2804 1680 C ATOM 2572 C GLU A 360 24.117 24.976 103.409 1.00 77.51 C ANISOU 2572 C GLU A 360 10544 13038 5866 827 -2712 1610 C ATOM 2573 O GLU A 360 23.907 24.864 102.197 1.00 78.80 O ANISOU 2573 O GLU A 360 10714 13385 5841 753 -2794 1648 O ATOM 2574 CB GLU A 360 23.486 27.204 104.324 1.00 85.75 C ANISOU 2574 CB GLU A 360 11751 13813 7016 1232 -2859 1872 C ATOM 2575 CG GLU A 360 22.484 28.068 105.071 1.00 90.35 C ANISOU 2575 CG GLU A 360 12296 14339 7694 1518 -2965 1951 C ATOM 2576 CD GLU A 360 21.246 28.376 104.258 1.00 95.93 C ANISOU 2576 CD GLU A 360 12912 15268 8267 1660 -3151 2041 C ATOM 2577 OE1 GLU A 360 21.047 29.560 103.914 1.00 99.63 O ANISOU 2577 OE1 GLU A 360 13532 15654 8670 1824 -3274 2216 O ATOM 2578 OE2 GLU A 360 20.473 27.442 103.956 1.00 99.10 O ANISOU 2578 OE2 GLU A 360 13097 15926 8629 1606 -3180 1938 O ATOM 2579 N THR A 361 25.200 24.466 103.993 1.00 77.03 N ANISOU 2579 N THR A 361 10528 12834 5908 694 -2547 1507 N ATOM 2580 CA THR A 361 26.208 23.730 103.241 1.00 75.83 C ANISOU 2580 CA THR A 361 10429 12731 5651 461 -2448 1426 C ATOM 2581 C THR A 361 25.895 22.250 103.123 1.00 75.39 C ANISOU 2581 C THR A 361 10192 12852 5602 327 -2401 1227 C ATOM 2582 O THR A 361 26.701 21.505 102.560 1.00 73.41 O ANISOU 2582 O THR A 361 9972 12647 5276 142 -2312 1130 O ATOM 2583 CB THR A 361 27.579 23.888 103.885 1.00 75.23 C ANISOU 2583 CB THR A 361 10487 12425 5673 383 -2295 1411 C ATOM 2584 OG1 THR A 361 27.587 23.200 105.141 1.00 75.38 O ANISOU 2584 OG1 THR A 361 10391 12353 5896 398 -2193 1271 O ATOM 2585 CG2 THR A 361 27.888 25.351 104.105 1.00 75.38 C ANISOU 2585 CG2 THR A 361 10695 12246 5700 505 -2342 1603 C ATOM 2586 N LEU A 362 24.761 21.805 103.650 1.00 74.43 N ANISOU 2586 N LEU A 362 9886 12830 5566 413 -2457 1161 N ATOM 2587 CA LEU A 362 24.348 20.417 103.544 1.00 76.05 C ANISOU 2587 CA LEU A 362 9921 13199 5775 280 -2430 980 C ATOM 2588 C LEU A 362 22.831 20.368 103.568 1.00 78.03 C ANISOU 2588 C LEU A 362 9988 13640 6019 395 -2570 992 C ATOM 2589 O LEU A 362 22.176 21.266 104.101 1.00 79.58 O ANISOU 2589 O LEU A 362 10163 13797 6278 598 -2647 1105 O ATOM 2590 CB LEU A 362 24.925 19.560 104.678 1.00 71.85 C ANISOU 2590 CB LEU A 362 9342 12524 5434 209 -2273 827 C ATOM 2591 CG LEU A 362 26.413 19.210 104.612 1.00 69.86 C ANISOU 2591 CG LEU A 362 9223 12136 5185 59 -2122 761 C ATOM 2592 CD1 LEU A 362 26.874 18.569 105.907 1.00 67.65 C ANISOU 2592 CD1 LEU A 362 8898 11694 5113 39 -1987 642 C ATOM 2593 CD2 LEU A 362 26.688 18.291 103.437 1.00 70.64 C ANISOU 2593 CD2 LEU A 362 9318 12402 5120 -127 -2111 655 C ATOM 2594 N ASP A 363 22.277 19.311 102.990 1.00 87.78 N ANISOU 2594 N ASP A 363 11088 15087 7176 265 -2603 872 N ATOM 2595 CA ASP A 363 20.832 19.135 102.928 1.00 93.82 C ANISOU 2595 CA ASP A 363 11656 16072 7919 341 -2737 870 C ATOM 2596 C ASP A 363 20.474 17.830 103.621 1.00 92.17 C ANISOU 2596 C ASP A 363 11277 15913 7829 225 -2669 686 C ATOM 2597 O ASP A 363 20.779 16.748 103.106 1.00 94.39 O ANISOU 2597 O ASP A 363 11547 16265 8053 25 -2623 547 O ATOM 2598 CB ASP A 363 20.341 19.141 101.486 1.00102.75 C ANISOU 2598 CB ASP A 363 12778 17443 8818 285 -2872 914 C ATOM 2599 CG ASP A 363 18.842 19.313 101.389 1.00106.52 C ANISOU 2599 CG ASP A 363 13066 18147 9259 410 -3035 963 C ATOM 2600 OD1 ASP A 363 18.357 20.432 101.655 1.00108.67 O ANISOU 2600 OD1 ASP A 363 13350 18388 9551 633 -3122 1116 O ATOM 2601 OD2 ASP A 363 18.149 18.333 101.043 1.00107.45 O ANISOU 2601 OD2 ASP A 363 13025 18477 9325 288 -3079 847 O ATOM 2602 N ILE A 364 19.821 17.935 104.783 1.00 83.87 N ANISOU 2602 N ILE A 364 10100 14827 6940 351 -2664 686 N ATOM 2603 CA ILE A 364 19.421 16.756 105.542 1.00 81.92 C ANISOU 2603 CA ILE A 364 9689 14622 6813 244 -2603 530 C ATOM 2604 C ILE A 364 18.477 15.863 104.748 1.00 81.06 C ANISOU 2604 C ILE A 364 9423 14791 6585 112 -2703 446 C ATOM 2605 O ILE A 364 18.420 14.653 104.991 1.00 78.19 O ANISOU 2605 O ILE A 364 8978 14459 6272 -59 -2646 292 O ATOM 2606 CB ILE A 364 18.782 17.176 106.882 1.00 83.19 C ANISOU 2606 CB ILE A 364 9734 14728 7145 421 -2595 566 C ATOM 2607 N GLU A 365 17.733 16.425 103.795 1.00 78.26 N ANISOU 2607 N GLU A 365 9029 14638 6067 184 -2856 545 N ATOM 2608 CA GLU A 365 16.849 15.604 102.975 1.00 79.99 C ANISOU 2608 CA GLU A 365 9101 15134 6157 48 -2960 467 C ATOM 2609 C GLU A 365 17.620 14.735 101.992 1.00 82.84 C ANISOU 2609 C GLU A 365 9572 15507 6395 -184 -2915 350 C ATOM 2610 O GLU A 365 17.075 13.743 101.501 1.00 81.18 O ANISOU 2610 O GLU A 365 9255 15478 6112 -348 -2963 232 O ATOM 2611 CB GLU A 365 15.852 16.487 102.227 1.00 82.42 C ANISOU 2611 CB GLU A 365 9336 15661 6319 202 -3143 613 C ATOM 2612 N GLN A 366 18.876 15.079 101.704 1.00 98.27 N ANISOU 2612 N GLN A 366 11737 17278 8323 -203 -2824 375 N ATOM 2613 CA GLN A 366 19.702 14.292 100.799 1.00 99.18 C ANISOU 2613 CA GLN A 366 11963 17402 8319 -407 -2767 259 C ATOM 2614 C GLN A 366 20.345 13.090 101.473 1.00 96.58 C ANISOU 2614 C GLN A 366 11640 16929 8126 -561 -2619 73 C ATOM 2615 O GLN A 366 20.881 12.224 100.774 1.00 95.97 O ANISOU 2615 O GLN A 366 11628 16879 7959 -736 -2576 -59 O ATOM 2616 CB GLN A 366 20.794 15.170 100.185 1.00101.48 C ANISOU 2616 CB GLN A 366 12467 17578 8513 -368 -2728 367 C ATOM 2617 N MET A 367 20.313 13.015 102.799 1.00 88.29 N ANISOU 2617 N MET A 367 10532 15731 7284 -495 -2542 57 N ATOM 2618 CA MET A 367 20.917 11.910 103.525 1.00 83.62 C ANISOU 2618 CA MET A 367 9953 14989 6831 -627 -2406 -105 C ATOM 2619 C MET A 367 19.862 10.869 103.865 1.00 80.78 C ANISOU 2619 C MET A 367 9408 14764 6520 -733 -2454 -218 C ATOM 2620 O MET A 367 18.720 11.209 104.182 1.00 80.90 O ANISOU 2620 O MET A 367 9262 14923 6555 -644 -2553 -147 O ATOM 2621 CB MET A 367 21.587 12.408 104.802 1.00 80.59 C ANISOU 2621 CB MET A 367 9625 14355 6642 -508 -2288 -56 C ATOM 2622 CG MET A 367 22.283 13.746 104.636 1.00 79.12 C ANISOU 2622 CG MET A 367 9587 14058 6419 -361 -2278 104 C ATOM 2623 SD MET A 367 23.450 14.057 105.965 1.00 74.95 S ANISOU 2623 SD MET A 367 9166 13216 6097 -292 -2111 114 S ATOM 2624 CE MET A 367 22.643 13.197 107.293 1.00 73.78 C ANISOU 2624 CE MET A 367 8836 13058 6141 -303 -2082 15 C ATOM 2625 N ASP A 368 20.252 9.598 103.793 1.00 77.11 N ANISOU 2625 N ASP A 368 8971 14256 6073 -926 -2386 -394 N ATOM 2626 CA ASP A 368 19.375 8.513 104.209 1.00 77.85 C ANISOU 2626 CA ASP A 368 8912 14438 6228 -1057 -2417 -509 C ATOM 2627 C ASP A 368 19.256 8.481 105.726 1.00 75.15 C ANISOU 2627 C ASP A 368 8496 13953 6105 -987 -2339 -494 C ATOM 2628 O ASP A 368 19.634 9.438 106.406 1.00 71.80 O ANISOU 2628 O ASP A 368 8112 13398 5770 -812 -2289 -380 O ATOM 2629 CB ASP A 368 19.894 7.172 103.697 1.00 75.39 C ANISOU 2629 CB ASP A 368 8681 14089 5874 -1279 -2368 -704 C ATOM 2630 CG ASP A 368 21.355 6.969 104.008 1.00 72.89 C ANISOU 2630 CG ASP A 368 8542 13514 5637 -1284 -2209 -766 C ATOM 2631 OD1 ASP A 368 22.149 7.889 103.717 1.00 72.37 O ANISOU 2631 OD1 ASP A 368 8591 13380 5525 -1173 -2170 -670 O ATOM 2632 OD2 ASP A 368 21.714 5.905 104.563 1.00 72.04 O ANISOU 2632 OD2 ASP A 368 8460 13272 5638 -1398 -2126 -905 O ATOM 2633 N ARG A 369 18.752 7.376 106.268 1.00 74.67 N ANISOU 2633 N ARG A 369 8334 13910 6127 -1131 -2329 -610 N ATOM 2634 CA ARG A 369 18.476 7.323 107.697 1.00 73.06 C ANISOU 2634 CA ARG A 369 8036 13610 6113 -1074 -2268 -589 C ATOM 2635 C ARG A 369 19.733 7.030 108.511 1.00 71.87 C ANISOU 2635 C ARG A 369 8031 13165 6109 -1077 -2107 -643 C ATOM 2636 O ARG A 369 20.130 7.832 109.358 1.00 73.02 O ANISOU 2636 O ARG A 369 8206 13176 6364 -917 -2041 -549 O ATOM 2637 CB ARG A 369 17.405 6.280 107.990 1.00 74.36 C ANISOU 2637 CB ARG A 369 8030 13918 6304 -1238 -2323 -677 C ATOM 2638 CG ARG A 369 17.443 5.833 109.421 1.00 72.80 C ANISOU 2638 CG ARG A 369 7786 13573 6302 -1250 -2226 -702 C ATOM 2639 CD ARG A 369 16.349 4.869 109.719 1.00 73.39 C ANISOU 2639 CD ARG A 369 7688 13801 6395 -1421 -2285 -771 C ATOM 2640 NE ARG A 369 15.220 5.518 110.373 1.00 73.99 N ANISOU 2640 NE ARG A 369 7551 14059 6505 -1298 -2345 -659 N ATOM 2641 CZ ARG A 369 14.038 5.695 109.803 1.00 75.47 C ANISOU 2641 CZ ARG A 369 7561 14537 6576 -1307 -2482 -620 C ATOM 2642 NH1 ARG A 369 13.054 6.273 110.467 1.00 77.63 N ANISOU 2642 NH1 ARG A 369 7633 14975 6887 -1180 -2527 -525 N ATOM 2643 NH2 ARG A 369 13.834 5.255 108.576 1.00 76.94 N ANISOU 2643 NH2 ARG A 369 7767 14861 6606 -1444 -2575 -684 N ATOM 2644 N GLU A 370 20.370 5.882 108.269 1.00 69.27 N ANISOU 2644 N GLU A 370 7800 12736 5784 -1253 -2046 -796 N ATOM 2645 CA GLU A 370 21.525 5.502 109.068 1.00 67.30 C ANISOU 2645 CA GLU A 370 7675 12219 5675 -1256 -1899 -855 C ATOM 2646 C GLU A 370 22.642 6.529 108.988 1.00 66.10 C ANISOU 2646 C GLU A 370 7663 11932 5518 -1105 -1826 -767 C ATOM 2647 O GLU A 370 23.544 6.510 109.826 1.00 64.36 O ANISOU 2647 O GLU A 370 7524 11502 5429 -1064 -1708 -777 O ATOM 2648 CB GLU A 370 22.051 4.138 108.636 1.00 67.54 C ANISOU 2648 CB GLU A 370 7803 12174 5686 -1453 -1858 -1038 C ATOM 2649 CG GLU A 370 22.930 4.170 107.417 1.00 68.74 C ANISOU 2649 CG GLU A 370 8104 12324 5689 -1478 -1844 -1092 C ATOM 2650 CD GLU A 370 23.593 2.834 107.148 1.00 72.46 C ANISOU 2650 CD GLU A 370 8687 12681 6163 -1641 -1784 -1284 C ATOM 2651 OE1 GLU A 370 23.843 2.514 105.962 1.00 74.68 O ANISOU 2651 OE1 GLU A 370 9045 13044 6286 -1721 -1815 -1370 O ATOM 2652 OE2 GLU A 370 23.870 2.107 108.127 1.00 72.24 O ANISOU 2652 OE2 GLU A 370 8676 12481 6292 -1683 -1708 -1349 O ATOM 2653 N THR A 371 22.605 7.421 108.004 1.00 67.08 N ANISOU 2653 N THR A 371 7820 12174 5491 -1031 -1896 -678 N ATOM 2654 CA THR A 371 23.561 8.516 107.932 1.00 66.17 C ANISOU 2654 CA THR A 371 7832 11944 5364 -892 -1840 -571 C ATOM 2655 C THR A 371 23.136 9.681 108.805 1.00 65.60 C ANISOU 2655 C THR A 371 7699 11845 5383 -699 -1859 -413 C ATOM 2656 O THR A 371 23.984 10.395 109.347 1.00 64.26 O ANISOU 2656 O THR A 371 7627 11501 5286 -593 -1778 -344 O ATOM 2657 CB THR A 371 23.718 8.967 106.478 1.00 67.62 C ANISOU 2657 CB THR A 371 8091 12264 5338 -905 -1910 -536 C ATOM 2658 OG1 THR A 371 24.412 7.956 105.751 1.00 67.88 O ANISOU 2658 OG1 THR A 371 8215 12281 5295 -1065 -1860 -692 O ATOM 2659 CG2 THR A 371 24.490 10.260 106.382 1.00 67.05 C ANISOU 2659 CG2 THR A 371 8135 12101 5238 -761 -1878 -391 C ATOM 2660 N LEU A 372 21.839 9.890 108.947 1.00 68.47 N ANISOU 2660 N LEU A 372 7900 12380 5737 -649 -1967 -358 N ATOM 2661 CA LEU A 372 21.349 10.958 109.797 1.00 67.05 C ANISOU 2661 CA LEU A 372 7652 12184 5640 -451 -1989 -222 C ATOM 2662 C LEU A 372 21.310 10.543 111.256 1.00 65.37 C ANISOU 2662 C LEU A 372 7372 11847 5620 -442 -1900 -261 C ATOM 2663 O LEU A 372 21.522 11.385 112.135 1.00 63.95 O ANISOU 2663 O LEU A 372 7212 11547 5538 -285 -1857 -173 O ATOM 2664 CB LEU A 372 19.966 11.405 109.319 1.00 72.25 C ANISOU 2664 CB LEU A 372 8153 13100 6198 -381 -2143 -144 C ATOM 2665 CG LEU A 372 19.421 12.713 109.885 1.00 74.40 C ANISOU 2665 CG LEU A 372 8371 13386 6510 -139 -2194 11 C ATOM 2666 CD1 LEU A 372 20.486 13.788 109.912 1.00 74.45 C ANISOU 2666 CD1 LEU A 372 8570 13189 6527 -11 -2138 110 C ATOM 2667 CD2 LEU A 372 18.248 13.176 109.063 1.00 79.07 C ANISOU 2667 CD2 LEU A 372 8840 14241 6961 -70 -2356 88 C ATOM 2668 N ASP A 373 21.061 9.260 111.529 1.00 64.91 N ANISOU 2668 N ASP A 373 7245 11808 5611 -613 -1875 -391 N ATOM 2669 CA ASP A 373 21.252 8.745 112.878 1.00 63.43 C ANISOU 2669 CA ASP A 373 7027 11472 5600 -632 -1775 -436 C ATOM 2670 C ASP A 373 22.713 8.813 113.292 1.00 61.53 C ANISOU 2670 C ASP A 373 6964 10972 5443 -612 -1642 -456 C ATOM 2671 O ASP A 373 23.022 9.181 114.430 1.00 60.17 O ANISOU 2671 O ASP A 373 6798 10659 5404 -516 -1568 -413 O ATOM 2672 CB ASP A 373 20.747 7.309 112.985 1.00 63.96 C ANISOU 2672 CB ASP A 373 7010 11600 5692 -840 -1780 -568 C ATOM 2673 CG ASP A 373 19.268 7.193 112.719 1.00 65.86 C ANISOU 2673 CG ASP A 373 7052 12110 5862 -876 -1907 -550 C ATOM 2674 OD1 ASP A 373 18.567 8.223 112.760 1.00 66.55 O ANISOU 2674 OD1 ASP A 373 7042 12327 5918 -709 -1978 -430 O ATOM 2675 OD2 ASP A 373 18.798 6.058 112.523 1.00 66.73 O ANISOU 2675 OD2 ASP A 373 7102 12300 5955 -1069 -1937 -655 O ATOM 2676 N LYS A 374 23.625 8.456 112.386 1.00 61.52 N ANISOU 2676 N LYS A 374 7101 10916 5359 -702 -1611 -524 N ATOM 2677 CA LYS A 374 25.042 8.525 112.717 1.00 59.89 C ANISOU 2677 CA LYS A 374 7050 10486 5219 -684 -1486 -544 C ATOM 2678 C LYS A 374 25.490 9.968 112.907 1.00 59.29 C ANISOU 2678 C LYS A 374 7044 10337 5146 -504 -1474 -397 C ATOM 2679 O LYS A 374 26.300 10.262 113.792 1.00 57.75 O ANISOU 2679 O LYS A 374 6917 9960 5066 -442 -1378 -376 O ATOM 2680 CB LYS A 374 25.874 7.840 111.637 1.00 60.28 C ANISOU 2680 CB LYS A 374 7217 10523 5162 -812 -1458 -653 C ATOM 2681 CG LYS A 374 27.290 7.540 112.080 1.00 59.36 C ANISOU 2681 CG LYS A 374 7232 10192 5130 -824 -1321 -712 C ATOM 2682 CD LYS A 374 28.200 7.271 110.895 1.00 61.84 C ANISOU 2682 CD LYS A 374 7668 10518 5310 -899 -1293 -786 C ATOM 2683 CE LYS A 374 27.743 6.070 110.087 1.00 64.74 C ANISOU 2683 CE LYS A 374 8014 10994 5591 -1058 -1343 -932 C ATOM 2684 NZ LYS A 374 28.062 4.787 110.765 1.00 66.64 N ANISOU 2684 NZ LYS A 374 8270 11096 5953 -1156 -1272 -1074 N ATOM 2685 N LEU A 375 24.963 10.885 112.100 1.00 60.59 N ANISOU 2685 N LEU A 375 7197 10638 5184 -421 -1576 -294 N ATOM 2686 CA LEU A 375 25.283 12.293 112.292 1.00 60.26 C ANISOU 2686 CA LEU A 375 7231 10519 5145 -249 -1580 -146 C ATOM 2687 C LEU A 375 24.862 12.769 113.678 1.00 59.38 C ANISOU 2687 C LEU A 375 7046 10329 5187 -114 -1558 -89 C ATOM 2688 O LEU A 375 25.601 13.504 114.340 1.00 58.23 O ANISOU 2688 O LEU A 375 6994 10012 5118 -18 -1492 -28 O ATOM 2689 CB LEU A 375 24.610 13.127 111.207 1.00 62.08 C ANISOU 2689 CB LEU A 375 7453 10921 5214 -179 -1711 -42 C ATOM 2690 CG LEU A 375 25.110 14.558 111.072 1.00 62.08 C ANISOU 2690 CG LEU A 375 7580 10830 5178 -30 -1724 110 C ATOM 2691 CD1 LEU A 375 26.612 14.559 111.007 1.00 60.85 C ANISOU 2691 CD1 LEU A 375 7591 10498 5032 -95 -1607 86 C ATOM 2692 CD2 LEU A 375 24.537 15.219 109.836 1.00 64.05 C ANISOU 2692 CD2 LEU A 375 7840 11251 5247 12 -1857 205 C ATOM 2693 N ALA A 376 23.679 12.358 114.135 1.00 63.63 N ANISOU 2693 N ALA A 376 7412 11000 5765 -112 -1612 -111 N ATOM 2694 CA ALA A 376 23.221 12.766 115.456 1.00 63.01 C ANISOU 2694 CA ALA A 376 7250 10872 5821 15 -1588 -65 C ATOM 2695 C ALA A 376 24.026 12.094 116.559 1.00 62.69 C ANISOU 2695 C ALA A 376 7249 10640 5930 -50 -1455 -142 C ATOM 2696 O ALA A 376 24.140 12.640 117.659 1.00 63.67 O ANISOU 2696 O ALA A 376 7372 10655 6164 67 -1406 -95 O ATOM 2697 CB ALA A 376 21.738 12.457 115.616 1.00 64.84 C ANISOU 2697 CB ALA A 376 7270 11323 6042 22 -1677 -71 C ATOM 2698 N TYR A 377 24.581 10.914 116.290 1.00 61.62 N ANISOU 2698 N TYR A 377 7151 10462 5798 -228 -1400 -263 N ATOM 2699 CA TYR A 377 25.501 10.299 117.238 1.00 57.75 C ANISOU 2699 CA TYR A 377 6724 9778 5442 -282 -1276 -331 C ATOM 2700 C TYR A 377 26.711 11.192 117.466 1.00 54.36 C ANISOU 2700 C TYR A 377 6447 9166 5042 -186 -1203 -269 C ATOM 2701 O TYR A 377 27.038 11.532 118.604 1.00 52.97 O ANISOU 2701 O TYR A 377 6283 8858 4985 -107 -1138 -238 O ATOM 2702 CB TYR A 377 25.928 8.921 116.730 1.00 55.43 C ANISOU 2702 CB TYR A 377 6466 9467 5128 -476 -1242 -472 C ATOM 2703 CG TYR A 377 27.103 8.308 117.462 1.00 53.83 C ANISOU 2703 CG TYR A 377 6361 9053 5040 -525 -1117 -544 C ATOM 2704 CD1 TYR A 377 28.407 8.526 117.035 1.00 54.54 C ANISOU 2704 CD1 TYR A 377 6598 9024 5102 -520 -1050 -556 C ATOM 2705 CD2 TYR A 377 26.911 7.499 118.567 1.00 53.15 C ANISOU 2705 CD2 TYR A 377 6214 8897 5084 -578 -1069 -596 C ATOM 2706 CE1 TYR A 377 29.477 7.969 117.697 1.00 53.16 C ANISOU 2706 CE1 TYR A 377 6499 8671 5027 -554 -940 -621 C ATOM 2707 CE2 TYR A 377 27.981 6.941 119.232 1.00 52.39 C ANISOU 2707 CE2 TYR A 377 6207 8610 5088 -613 -963 -655 C ATOM 2708 CZ TYR A 377 29.258 7.177 118.790 1.00 51.53 C ANISOU 2708 CZ TYR A 377 6237 8391 4952 -595 -901 -670 C ATOM 2709 OH TYR A 377 30.320 6.610 119.449 1.00 50.48 O ANISOU 2709 OH TYR A 377 6181 8083 4918 -621 -799 -730 O ATOM 2710 N VAL A 378 27.377 11.593 116.386 1.00 54.57 N ANISOU 2710 N VAL A 378 6589 9193 4954 -200 -1215 -247 N ATOM 2711 CA VAL A 378 28.592 12.392 116.490 1.00 53.61 C ANISOU 2711 CA VAL A 378 6614 8911 4845 -140 -1146 -189 C ATOM 2712 C VAL A 378 28.310 13.726 117.162 1.00 53.47 C ANISOU 2712 C VAL A 378 6606 8840 4871 39 -1175 -56 C ATOM 2713 O VAL A 378 29.082 14.188 118.005 1.00 52.25 O ANISOU 2713 O VAL A 378 6526 8520 4808 96 -1100 -27 O ATOM 2714 CB VAL A 378 29.207 12.584 115.094 1.00 54.44 C ANISOU 2714 CB VAL A 378 6825 9067 4793 -199 -1166 -182 C ATOM 2715 CG1 VAL A 378 30.293 13.637 115.119 1.00 53.82 C ANISOU 2715 CG1 VAL A 378 6889 8855 4705 -133 -1116 -91 C ATOM 2716 CG2 VAL A 378 29.744 11.270 114.572 1.00 54.39 C ANISOU 2716 CG2 VAL A 378 6836 9072 4758 -363 -1113 -331 C ATOM 2717 N LEU A 379 27.210 14.370 116.805 1.00 54.82 N ANISOU 2717 N LEU A 379 6705 9150 4974 136 -1286 22 N ATOM 2718 CA LEU A 379 26.941 15.703 117.323 1.00 54.97 C ANISOU 2718 CA LEU A 379 6752 9114 5020 324 -1324 147 C ATOM 2719 C LEU A 379 26.353 15.686 118.721 1.00 54.31 C ANISOU 2719 C LEU A 379 6562 9000 5076 414 -1297 138 C ATOM 2720 O LEU A 379 26.340 16.728 119.378 1.00 54.15 O ANISOU 2720 O LEU A 379 6584 8889 5103 571 -1302 221 O ATOM 2721 CB LEU A 379 25.990 16.451 116.391 1.00 56.85 C ANISOU 2721 CB LEU A 379 6958 9514 5129 417 -1461 240 C ATOM 2722 CG LEU A 379 26.440 16.649 114.949 1.00 57.82 C ANISOU 2722 CG LEU A 379 7186 9691 5091 346 -1506 273 C ATOM 2723 CD1 LEU A 379 25.304 17.241 114.157 1.00 59.78 C ANISOU 2723 CD1 LEU A 379 7370 10122 5221 441 -1652 359 C ATOM 2724 CD2 LEU A 379 27.653 17.545 114.891 1.00 57.19 C ANISOU 2724 CD2 LEU A 379 7298 9430 5002 374 -1454 351 C ATOM 2725 N THR A 380 25.838 14.548 119.180 1.00 54.09 N ANISOU 2725 N THR A 380 6399 9046 5106 318 -1272 42 N ATOM 2726 CA THR A 380 25.369 14.472 120.558 1.00 53.44 C ANISOU 2726 CA THR A 380 6217 8936 5151 386 -1233 32 C ATOM 2727 C THR A 380 26.528 14.245 121.514 1.00 55.10 C ANISOU 2727 C THR A 380 6523 8933 5478 351 -1108 -6 C ATOM 2728 O THR A 380 26.616 14.900 122.556 1.00 57.24 O ANISOU 2728 O THR A 380 6808 9107 5834 470 -1073 37 O ATOM 2729 CB THR A 380 24.340 13.353 120.712 1.00 55.21 C ANISOU 2729 CB THR A 380 6260 9329 5388 283 -1257 -45 C ATOM 2730 OG1 THR A 380 23.220 13.608 119.856 1.00 58.96 O ANISOU 2730 OG1 THR A 380 6631 10021 5751 322 -1379 -6 O ATOM 2731 CG2 THR A 380 23.859 13.265 122.146 1.00 54.46 C ANISOU 2731 CG2 THR A 380 6057 9220 5414 344 -1211 -51 C ATOM 2732 N LEU A 381 27.439 13.348 121.148 1.00 52.19 N ANISOU 2732 N LEU A 381 6224 8496 5109 195 -1045 -88 N ATOM 2733 CA LEU A 381 28.515 12.938 122.035 1.00 49.28 C ANISOU 2733 CA LEU A 381 5926 7946 4850 149 -930 -136 C ATOM 2734 C LEU A 381 29.664 13.933 122.066 1.00 48.54 C ANISOU 2734 C LEU A 381 5991 7694 4758 217 -887 -71 C ATOM 2735 O LEU A 381 30.310 14.077 123.098 1.00 47.34 O ANISOU 2735 O LEU A 381 5881 7400 4706 249 -811 -71 O ATOM 2736 CB LEU A 381 29.025 11.564 121.610 1.00 49.01 C ANISOU 2736 CB LEU A 381 5904 7903 4814 -31 -884 -254 C ATOM 2737 CG LEU A 381 30.256 10.975 122.289 1.00 47.53 C ANISOU 2737 CG LEU A 381 5799 7538 4722 -92 -770 -317 C ATOM 2738 CD1 LEU A 381 29.958 10.578 123.725 1.00 46.71 C ANISOU 2738 CD1 LEU A 381 5619 7376 4752 -76 -724 -332 C ATOM 2739 CD2 LEU A 381 30.729 9.781 121.476 1.00 47.76 C ANISOU 2739 CD2 LEU A 381 5860 7578 4708 -245 -749 -430 C ATOM 2740 N ASN A 382 29.948 14.621 120.971 1.00 50.78 N ANISOU 2740 N ASN A 382 6364 8003 4926 232 -934 -14 N ATOM 2741 CA ASN A 382 31.119 15.481 120.903 1.00 49.59 C ANISOU 2741 CA ASN A 382 6369 7708 4764 260 -891 47 C ATOM 2742 C ASN A 382 30.729 16.942 121.055 1.00 52.28 C ANISOU 2742 C ASN A 382 6762 8017 5085 425 -957 174 C ATOM 2743 O ASN A 382 29.757 17.402 120.452 1.00 52.25 O ANISOU 2743 O ASN A 382 6715 8135 5002 499 -1059 230 O ATOM 2744 CB ASN A 382 31.869 15.278 119.591 1.00 50.93 C ANISOU 2744 CB ASN A 382 6624 7914 4812 150 -887 29 C ATOM 2745 CG ASN A 382 32.528 13.928 119.509 1.00 52.04 C ANISOU 2745 CG ASN A 382 6749 8044 4979 5 -807 -102 C ATOM 2746 OD1 ASN A 382 33.684 13.762 119.905 1.00 53.23 O ANISOU 2746 OD1 ASN A 382 6970 8072 5184 -34 -714 -134 O ATOM 2747 ND2 ASN A 382 31.795 12.943 119.003 1.00 53.69 N ANISOU 2747 ND2 ASN A 382 6868 8382 5152 -75 -845 -183 N ATOM 2748 N THR A 383 31.506 17.669 121.855 1.00 48.82 N ANISOU 2748 N THR A 383 6424 7410 4717 482 -904 217 N ATOM 2749 CA THR A 383 31.251 19.072 122.131 1.00 49.53 C ANISOU 2749 CA THR A 383 6591 7428 4802 641 -961 330 C ATOM 2750 C THR A 383 32.325 20.008 121.601 1.00 49.94 C ANISOU 2750 C THR A 383 6826 7358 4791 623 -955 412 C ATOM 2751 O THR A 383 32.132 21.227 121.639 1.00 51.61 O ANISOU 2751 O THR A 383 7129 7499 4980 746 -1017 516 O ATOM 2752 CB THR A 383 31.112 19.299 123.642 1.00 48.20 C ANISOU 2752 CB THR A 383 6390 7158 4765 741 -917 318 C ATOM 2753 OG1 THR A 383 32.386 19.114 124.258 1.00 46.80 O ANISOU 2753 OG1 THR A 383 6295 6828 4658 661 -814 285 O ATOM 2754 CG2 THR A 383 30.136 18.307 124.238 1.00 48.06 C ANISOU 2754 CG2 THR A 383 6188 7262 4809 735 -910 239 C ATOM 2755 N GLU A 384 33.446 19.488 121.126 1.00 53.83 N ANISOU 2755 N GLU A 384 7375 7824 5253 474 -883 371 N ATOM 2756 CA GLU A 384 34.564 20.295 120.671 1.00 56.50 C ANISOU 2756 CA GLU A 384 7875 8060 5531 429 -863 445 C ATOM 2757 C GLU A 384 34.762 20.125 119.172 1.00 55.52 C ANISOU 2757 C GLU A 384 7785 8057 5255 329 -895 461 C ATOM 2758 O GLU A 384 34.399 19.101 118.597 1.00 53.51 O ANISOU 2758 O GLU A 384 7431 7939 4960 256 -896 376 O ATOM 2759 CB GLU A 384 35.851 19.900 121.399 1.00 63.06 C ANISOU 2759 CB GLU A 384 8741 8772 6445 339 -743 386 C ATOM 2760 CG GLU A 384 35.994 20.464 122.780 1.00 68.46 C ANISOU 2760 CG GLU A 384 9455 9306 7252 429 -714 405 C ATOM 2761 CD GLU A 384 37.238 21.305 122.895 1.00 73.60 C ANISOU 2761 CD GLU A 384 10257 9814 7893 384 -674 469 C ATOM 2762 OE1 GLU A 384 37.778 21.433 124.015 1.00 73.24 O ANISOU 2762 OE1 GLU A 384 10232 9646 7948 399 -615 450 O ATOM 2763 OE2 GLU A 384 37.674 21.834 121.847 1.00 79.29 O ANISOU 2763 OE2 GLU A 384 11075 10555 8498 325 -702 540 O ATOM 2764 N ARG A 385 35.382 21.137 118.558 1.00 53.41 N ANISOU 2764 N ARG A 385 7664 7731 4897 315 -919 569 N ATOM 2765 CA ARG A 385 35.672 21.084 117.131 1.00 56.34 C ANISOU 2765 CA ARG A 385 8082 8217 5108 214 -944 597 C ATOM 2766 C ARG A 385 36.454 19.830 116.768 1.00 53.64 C ANISOU 2766 C ARG A 385 7681 7949 4749 61 -846 468 C ATOM 2767 O ARG A 385 36.074 19.088 115.857 1.00 54.82 O ANISOU 2767 O ARG A 385 7768 8252 4810 1 -869 409 O ATOM 2768 CB ARG A 385 36.449 22.325 116.696 1.00 58.12 C ANISOU 2768 CB ARG A 385 8485 8347 5251 194 -963 734 C ATOM 2769 CG ARG A 385 37.006 22.210 115.271 1.00 59.88 C ANISOU 2769 CG ARG A 385 8760 8691 5302 60 -962 757 C ATOM 2770 CD ARG A 385 38.021 23.301 114.950 1.00 61.96 C ANISOU 2770 CD ARG A 385 9197 8855 5491 -2 -952 883 C ATOM 2771 NE ARG A 385 39.073 23.380 115.964 1.00 63.28 N ANISOU 2771 NE ARG A 385 9398 8876 5769 -44 -852 856 N ATOM 2772 CZ ARG A 385 39.256 24.423 116.772 1.00 66.66 C ANISOU 2772 CZ ARG A 385 9934 9125 6267 22 -871 944 C ATOM 2773 NH1 ARG A 385 38.468 25.486 116.671 1.00 69.33 N ANISOU 2773 NH1 ARG A 385 10366 9399 6578 143 -987 1065 N ATOM 2774 NH2 ARG A 385 40.230 24.410 117.675 1.00 67.04 N ANISOU 2774 NH2 ARG A 385 10002 9059 6409 -29 -779 908 N ATOM 2775 N GLU A 386 37.555 19.577 117.470 1.00 58.30 N ANISOU 2775 N GLU A 386 8294 8435 5421 3 -738 419 N ATOM 2776 CA GLU A 386 38.427 18.485 117.064 1.00 61.01 C ANISOU 2776 CA GLU A 386 8599 8843 5739 -128 -644 302 C ATOM 2777 C GLU A 386 37.749 17.138 117.257 1.00 55.80 C ANISOU 2777 C GLU A 386 7803 8260 5139 -137 -635 164 C ATOM 2778 O GLU A 386 37.875 16.248 116.410 1.00 56.10 O ANISOU 2778 O GLU A 386 7805 8412 5099 -226 -616 74 O ATOM 2779 CB GLU A 386 39.738 18.560 117.837 1.00 65.80 C ANISOU 2779 CB GLU A 386 9253 9326 6424 -174 -538 286 C ATOM 2780 CG GLU A 386 40.312 19.961 117.868 1.00 70.34 C ANISOU 2780 CG GLU A 386 9966 9799 6961 -167 -556 429 C ATOM 2781 CD GLU A 386 41.729 19.990 118.378 1.00 72.77 C ANISOU 2781 CD GLU A 386 10314 10026 7311 -248 -451 412 C ATOM 2782 OE1 GLU A 386 42.414 18.955 118.252 1.00 76.22 O ANISOU 2782 OE1 GLU A 386 10682 10525 7752 -325 -365 298 O ATOM 2783 OE2 GLU A 386 42.156 21.039 118.910 1.00 74.75 O ANISOU 2783 OE2 GLU A 386 10663 10149 7589 -231 -457 509 O ATOM 2784 N GLY A 387 37.006 16.980 118.349 1.00 53.97 N ANISOU 2784 N GLY A 387 7498 7971 5039 -51 -649 144 N ATOM 2785 CA GLY A 387 36.295 15.732 118.566 1.00 52.77 C ANISOU 2785 CA GLY A 387 7220 7888 4942 -72 -647 26 C ATOM 2786 C GLY A 387 35.274 15.443 117.481 1.00 54.34 C ANISOU 2786 C GLY A 387 7364 8255 5025 -90 -739 16 C ATOM 2787 O GLY A 387 35.147 14.307 117.023 1.00 55.93 O ANISOU 2787 O GLY A 387 7505 8543 5202 -177 -725 -97 O ATOM 2788 N ILE A 388 34.527 16.468 117.064 1.00 53.26 N ANISOU 2788 N ILE A 388 7252 8166 4817 -6 -838 133 N ATOM 2789 CA ILE A 388 33.582 16.306 115.960 1.00 55.06 C ANISOU 2789 CA ILE A 388 7433 8569 4920 -20 -936 138 C ATOM 2790 C ILE A 388 34.329 16.006 114.670 1.00 52.40 C ANISOU 2790 C ILE A 388 7159 8315 4435 -141 -915 107 C ATOM 2791 O ILE A 388 34.022 15.039 113.963 1.00 52.98 O ANISOU 2791 O ILE A 388 7172 8513 4443 -225 -928 8 O ATOM 2792 CB ILE A 388 32.682 17.550 115.822 1.00 52.77 C ANISOU 2792 CB ILE A 388 7163 8303 4584 117 -1051 281 C ATOM 2793 CG1 ILE A 388 31.712 17.640 116.990 1.00 52.35 C ANISOU 2793 CG1 ILE A 388 7010 8222 4660 241 -1079 284 C ATOM 2794 CG2 ILE A 388 31.883 17.478 114.527 1.00 54.46 C ANISOU 2794 CG2 ILE A 388 7343 8706 4642 95 -1156 300 C ATOM 2795 CD1 ILE A 388 31.108 18.994 117.196 1.00 53.16 C ANISOU 2795 CD1 ILE A 388 7158 8287 4754 408 -1166 420 C ATOM 2796 N GLN A 389 35.332 16.824 114.358 1.00 52.47 N ANISOU 2796 N GLN A 389 7292 8259 4385 -159 -881 188 N ATOM 2797 CA GLN A 389 36.077 16.641 113.124 1.00 53.31 C ANISOU 2797 CA GLN A 389 7459 8459 4336 -273 -856 169 C ATOM 2798 C GLN A 389 36.666 15.244 113.027 1.00 52.73 C ANISOU 2798 C GLN A 389 7333 8422 4282 -379 -763 -3 C ATOM 2799 O GLN A 389 36.593 14.611 111.971 1.00 53.71 O ANISOU 2799 O GLN A 389 7442 8683 4282 -459 -777 -75 O ATOM 2800 CB GLN A 389 37.169 17.700 113.004 1.00 61.74 C ANISOU 2800 CB GLN A 389 8662 9441 5356 -290 -817 282 C ATOM 2801 CG GLN A 389 37.616 17.907 111.568 1.00 63.53 C ANISOU 2801 CG GLN A 389 8958 9798 5383 -385 -830 319 C ATOM 2802 CD GLN A 389 38.266 19.256 111.330 1.00 64.96 C ANISOU 2802 CD GLN A 389 9281 9910 5492 -388 -842 484 C ATOM 2803 OE1 GLN A 389 39.310 19.346 110.691 1.00 70.23 O ANISOU 2803 OE1 GLN A 389 10012 10618 6055 -496 -779 494 O ATOM 2804 NE2 GLN A 389 37.640 20.315 111.829 1.00 66.98 N ANISOU 2804 NE2 GLN A 389 9589 10065 5796 -272 -926 613 N ATOM 2805 N GLU A 390 37.249 14.744 114.117 1.00 51.27 N ANISOU 2805 N GLU A 390 7124 8111 4246 -375 -672 -74 N ATOM 2806 CA GLU A 390 37.840 13.410 114.108 1.00 50.79 C ANISOU 2806 CA GLU A 390 7022 8060 4215 -458 -586 -238 C ATOM 2807 C GLU A 390 36.775 12.335 113.963 1.00 51.19 C ANISOU 2807 C GLU A 390 6978 8192 4279 -482 -638 -345 C ATOM 2808 O GLU A 390 36.982 11.329 113.280 1.00 51.71 O ANISOU 2808 O GLU A 390 7032 8331 4283 -567 -614 -471 O ATOM 2809 CB GLU A 390 38.657 13.196 115.386 1.00 55.90 C ANISOU 2809 CB GLU A 390 7667 8548 5024 -436 -488 -272 C ATOM 2810 CG GLU A 390 39.209 11.784 115.556 1.00 54.53 C ANISOU 2810 CG GLU A 390 7454 8359 4906 -497 -406 -440 C ATOM 2811 CD GLU A 390 39.752 11.525 116.976 1.00 54.47 C ANISOU 2811 CD GLU A 390 7428 8193 5074 -458 -331 -466 C ATOM 2812 OE1 GLU A 390 40.724 10.755 117.118 1.00 56.16 O ANISOU 2812 OE1 GLU A 390 7646 8370 5321 -495 -243 -566 O ATOM 2813 OE2 GLU A 390 39.218 12.092 117.959 1.00 55.23 O ANISOU 2813 OE2 GLU A 390 7506 8207 5272 -383 -360 -388 O ATOM 2814 N ALA A 391 35.633 12.521 114.614 1.00 51.06 N ANISOU 2814 N ALA A 391 6891 8166 4341 -411 -710 -300 N ATOM 2815 CA ALA A 391 34.572 11.530 114.529 1.00 51.54 C ANISOU 2815 CA ALA A 391 6854 8315 4416 -448 -765 -392 C ATOM 2816 C ALA A 391 33.960 11.492 113.137 1.00 56.36 C ANISOU 2816 C ALA A 391 7457 9105 4851 -499 -853 -395 C ATOM 2817 O ALA A 391 33.594 10.417 112.649 1.00 58.24 O ANISOU 2817 O ALA A 391 7650 9426 5051 -586 -870 -516 O ATOM 2818 CB ALA A 391 33.499 11.822 115.575 1.00 51.13 C ANISOU 2818 CB ALA A 391 6715 8233 4480 -357 -817 -334 C ATOM 2819 N LEU A 392 33.847 12.651 112.489 1.00 56.27 N ANISOU 2819 N LEU A 392 7499 9153 4728 -449 -915 -261 N ATOM 2820 CA LEU A 392 33.331 12.695 111.127 1.00 55.77 C ANISOU 2820 CA LEU A 392 7439 9269 4484 -496 -1002 -251 C ATOM 2821 C LEU A 392 34.286 12.014 110.160 1.00 56.24 C ANISOU 2821 C LEU A 392 7558 9383 4427 -613 -936 -357 C ATOM 2822 O LEU A 392 33.853 11.272 109.274 1.00 57.37 O ANISOU 2822 O LEU A 392 7671 9662 4465 -692 -979 -448 O ATOM 2823 CB LEU A 392 33.082 14.141 110.713 1.00 56.61 C ANISOU 2823 CB LEU A 392 7605 9404 4500 -408 -1081 -70 C ATOM 2824 CG LEU A 392 31.967 14.847 111.479 1.00 56.61 C ANISOU 2824 CG LEU A 392 7540 9383 4585 -272 -1168 30 C ATOM 2825 CD1 LEU A 392 31.872 16.293 111.071 1.00 57.51 C ANISOU 2825 CD1 LEU A 392 7744 9494 4614 -177 -1243 207 C ATOM 2826 CD2 LEU A 392 30.636 14.147 111.272 1.00 57.49 C ANISOU 2826 CD2 LEU A 392 7515 9648 4681 -285 -1258 -29 C ATOM 2827 N GLU A 393 35.588 12.236 110.331 1.00 55.48 N ANISOU 2827 N GLU A 393 7542 9192 4346 -626 -830 -354 N ATOM 2828 CA GLU A 393 36.575 11.619 109.456 1.00 58.26 C ANISOU 2828 CA GLU A 393 7943 9607 4587 -724 -755 -458 C ATOM 2829 C GLU A 393 36.636 10.110 109.631 1.00 57.03 C ANISOU 2829 C GLU A 393 7739 9436 4495 -786 -706 -654 C ATOM 2830 O GLU A 393 36.863 9.386 108.657 1.00 58.17 O ANISOU 2830 O GLU A 393 7899 9684 4516 -866 -694 -768 O ATOM 2831 CB GLU A 393 37.948 12.242 109.707 1.00 61.01 C ANISOU 2831 CB GLU A 393 8370 9864 4945 -720 -653 -403 C ATOM 2832 CG GLU A 393 37.964 13.722 109.393 1.00 65.37 C ANISOU 2832 CG GLU A 393 8997 10426 5414 -681 -705 -210 C ATOM 2833 CD GLU A 393 39.350 14.319 109.331 1.00 69.21 C ANISOU 2833 CD GLU A 393 9567 10867 5861 -718 -610 -156 C ATOM 2834 OE1 GLU A 393 39.489 15.516 109.658 1.00 70.48 O ANISOU 2834 OE1 GLU A 393 9794 10948 6036 -673 -634 1 O ATOM 2835 OE2 GLU A 393 40.296 13.600 108.948 1.00 72.35 O ANISOU 2835 OE2 GLU A 393 9967 11312 6211 -791 -515 -271 O ATOM 2836 N HIS A 394 36.433 9.612 110.846 1.00 61.19 N ANISOU 2836 N HIS A 394 8214 9830 5204 -751 -679 -697 N ATOM 2837 CA HIS A 394 36.677 8.210 111.144 1.00 62.51 C ANISOU 2837 CA HIS A 394 8360 9943 5450 -806 -621 -873 C ATOM 2838 C HIS A 394 35.427 7.349 111.090 1.00 63.74 C ANISOU 2838 C HIS A 394 8442 10155 5622 -854 -707 -950 C ATOM 2839 O HIS A 394 35.542 6.121 111.072 1.00 67.77 O ANISOU 2839 O HIS A 394 8952 10635 6161 -920 -678 -1106 O ATOM 2840 CB HIS A 394 37.328 8.071 112.524 1.00 64.90 C ANISOU 2840 CB HIS A 394 8659 10061 5940 -754 -534 -878 C ATOM 2841 CG HIS A 394 38.697 8.666 112.600 1.00 65.19 C ANISOU 2841 CG HIS A 394 8761 10043 5966 -730 -437 -836 C ATOM 2842 ND1 HIS A 394 39.379 8.817 113.786 1.00 64.70 N ANISOU 2842 ND1 HIS A 394 8701 9830 6052 -678 -363 -811 N ATOM 2843 CD2 HIS A 394 39.510 9.148 111.632 1.00 63.98 C ANISOU 2843 CD2 HIS A 394 8667 9979 5664 -761 -404 -812 C ATOM 2844 CE1 HIS A 394 40.557 9.366 113.544 1.00 63.97 C ANISOU 2844 CE1 HIS A 394 8663 9738 5905 -680 -291 -775 C ATOM 2845 NE2 HIS A 394 40.661 9.577 112.244 1.00 64.26 N ANISOU 2845 NE2 HIS A 394 8735 9921 5761 -732 -311 -773 N ATOM 2846 N GLU A 395 34.242 7.950 111.066 1.00 62.61 N ANISOU 2846 N GLU A 395 8237 10094 5459 -822 -814 -848 N ATOM 2847 CA GLU A 395 33.010 7.183 111.025 1.00 63.64 C ANISOU 2847 CA GLU A 395 8282 10301 5599 -878 -900 -912 C ATOM 2848 C GLU A 395 32.286 7.273 109.690 1.00 62.41 C ANISOU 2848 C GLU A 395 8112 10345 5254 -932 -1004 -911 C ATOM 2849 O GLU A 395 31.485 6.386 109.376 1.00 59.59 O ANISOU 2849 O GLU A 395 7702 10070 4872 -1019 -1066 -1008 O ATOM 2850 CB GLU A 395 32.074 7.639 112.152 1.00 66.30 C ANISOU 2850 CB GLU A 395 8525 10597 6067 -800 -946 -813 C ATOM 2851 CG GLU A 395 32.686 7.477 113.538 1.00 66.12 C ANISOU 2851 CG GLU A 395 8510 10384 6230 -754 -850 -819 C ATOM 2852 CD GLU A 395 32.816 6.024 113.957 1.00 66.82 C ANISOU 2852 CD GLU A 395 8591 10392 6408 -845 -804 -975 C ATOM 2853 OE1 GLU A 395 31.931 5.543 114.690 1.00 69.34 O ANISOU 2853 OE1 GLU A 395 8826 10700 6820 -867 -840 -987 O ATOM 2854 OE2 GLU A 395 33.792 5.360 113.550 1.00 68.63 O ANISOU 2854 OE2 GLU A 395 8897 10569 6608 -893 -734 -1085 O ATOM 2855 N PHE A 396 32.564 8.294 108.892 1.00 58.48 N ANISOU 2855 N PHE A 396 7667 9931 4622 -894 -1027 -804 N ATOM 2856 CA PHE A 396 31.976 8.436 107.574 1.00 60.29 C ANISOU 2856 CA PHE A 396 7894 10357 4657 -943 -1125 -793 C ATOM 2857 C PHE A 396 33.023 8.163 106.507 1.00 61.00 C ANISOU 2857 C PHE A 396 8080 10499 4597 -1015 -1062 -874 C ATOM 2858 O PHE A 396 34.219 8.383 106.719 1.00 60.14 O ANISOU 2858 O PHE A 396 8043 10294 4515 -993 -954 -871 O ATOM 2859 CB PHE A 396 31.388 9.835 107.391 1.00 60.79 C ANISOU 2859 CB PHE A 396 7946 10493 4659 -843 -1216 -597 C ATOM 2860 CG PHE A 396 30.214 10.108 108.277 1.00 60.52 C ANISOU 2860 CG PHE A 396 7800 10453 4740 -764 -1291 -526 C ATOM 2861 CD1 PHE A 396 30.401 10.488 109.600 1.00 58.95 C ANISOU 2861 CD1 PHE A 396 7587 10090 4719 -671 -1235 -470 C ATOM 2862 CD2 PHE A 396 28.925 9.963 107.799 1.00 61.92 C ANISOU 2862 CD2 PHE A 396 7878 10803 4845 -783 -1417 -519 C ATOM 2863 CE1 PHE A 396 29.324 10.729 110.426 1.00 58.80 C ANISOU 2863 CE1 PHE A 396 7459 10082 4799 -593 -1297 -411 C ATOM 2864 CE2 PHE A 396 27.838 10.206 108.620 1.00 61.80 C ANISOU 2864 CE2 PHE A 396 7744 10807 4931 -706 -1482 -457 C ATOM 2865 CZ PHE A 396 28.041 10.592 109.939 1.00 60.24 C ANISOU 2865 CZ PHE A 396 7535 10446 4907 -607 -1419 -404 C ATOM 2866 N ALA A 397 32.553 7.676 105.356 1.00 62.67 N ANISOU 2866 N ALA A 397 8288 10878 4645 -1102 -1131 -950 N ATOM 2867 CA ALA A 397 33.430 7.409 104.227 1.00 66.80 C ANISOU 2867 CA ALA A 397 8896 11487 4999 -1171 -1081 -1034 C ATOM 2868 C ALA A 397 34.186 8.669 103.829 1.00 69.37 C ANISOU 2868 C ALA A 397 9293 11837 5227 -1119 -1051 -879 C ATOM 2869 O ALA A 397 33.686 9.787 103.961 1.00 65.88 O ANISOU 2869 O ALA A 397 8841 11409 4780 -1045 -1122 -701 O ATOM 2870 CB ALA A 397 32.627 6.881 103.042 1.00 65.62 C ANISOU 2870 CB ALA A 397 8726 11533 4673 -1266 -1183 -1114 C ATOM 2871 N ASP A 398 35.395 8.465 103.300 1.00 89.47 N ANISOU 2871 N ASP A 398 11914 14394 7687 -1161 -947 -950 N ATOM 2872 CA ASP A 398 36.378 9.542 103.209 1.00 90.82 C ANISOU 2872 CA ASP A 398 12155 14545 7808 -1125 -883 -816 C ATOM 2873 C ASP A 398 35.842 10.760 102.464 1.00 92.13 C ANISOU 2873 C ASP A 398 12349 14833 7824 -1107 -988 -627 C ATOM 2874 O ASP A 398 36.202 11.898 102.786 1.00 95.25 O ANISOU 2874 O ASP A 398 12791 15160 8240 -1050 -979 -459 O ATOM 2875 CB ASP A 398 37.650 9.020 102.542 1.00 90.18 C ANISOU 2875 CB ASP A 398 12131 14515 7618 -1189 -764 -940 C ATOM 2876 CG ASP A 398 38.388 8.024 103.410 1.00 90.75 C ANISOU 2876 CG ASP A 398 12188 14449 7846 -1184 -657 -1114 C ATOM 2877 OD1 ASP A 398 38.993 8.447 104.418 1.00 91.93 O ANISOU 2877 OD1 ASP A 398 12319 14427 8182 -1119 -610 -1066 O ATOM 2878 OD2 ASP A 398 38.352 6.818 103.088 1.00 90.57 O ANISOU 2878 OD2 ASP A 398 12176 14484 7754 -1242 -625 -1300 O ATOM 2879 N GLY A 399 34.985 10.551 101.473 1.00 86.59 N ANISOU 2879 N GLY A 399 11626 14306 6968 -1156 -1094 -648 N ATOM 2880 CA GLY A 399 34.513 11.677 100.693 1.00 85.83 C ANISOU 2880 CA GLY A 399 11564 14334 6715 -1135 -1199 -467 C ATOM 2881 C GLY A 399 33.187 12.239 101.160 1.00 78.84 C ANISOU 2881 C GLY A 399 10609 13441 5905 -1045 -1334 -345 C ATOM 2882 O GLY A 399 32.499 12.926 100.399 1.00 80.50 O ANISOU 2882 O GLY A 399 10827 13785 5974 -1028 -1453 -224 O ATOM 2883 N SER A 400 32.817 11.973 102.414 1.00 74.74 N ANISOU 2883 N SER A 400 10020 12774 5603 -981 -1320 -371 N ATOM 2884 CA SER A 400 31.479 12.325 102.874 1.00 71.58 C ANISOU 2884 CA SER A 400 9529 12394 5274 -897 -1444 -286 C ATOM 2885 C SER A 400 31.338 13.789 103.261 1.00 74.26 C ANISOU 2885 C SER A 400 9910 12662 5643 -766 -1493 -69 C ATOM 2886 O SER A 400 30.215 14.300 103.274 1.00 75.96 O ANISOU 2886 O SER A 400 10064 12945 5851 -683 -1618 28 O ATOM 2887 CB SER A 400 31.076 11.462 104.066 1.00 67.36 C ANISOU 2887 CB SER A 400 8899 11747 4950 -885 -1410 -396 C ATOM 2888 OG SER A 400 31.115 10.085 103.749 1.00 65.47 O ANISOU 2888 OG SER A 400 8631 11553 4691 -1004 -1379 -596 O ATOM 2889 N PHE A 401 32.429 14.473 103.581 1.00 72.48 N ANISOU 2889 N PHE A 401 9786 12302 5450 -743 -1402 7 N ATOM 2890 CA PHE A 401 32.341 15.830 104.094 1.00 71.48 C ANISOU 2890 CA PHE A 401 9716 12068 5375 -620 -1444 202 C ATOM 2891 C PHE A 401 33.475 16.670 103.532 1.00 69.46 C ANISOU 2891 C PHE A 401 9604 11783 5004 -660 -1392 309 C ATOM 2892 O PHE A 401 34.585 16.178 103.314 1.00 68.36 O ANISOU 2892 O PHE A 401 9505 11638 4832 -759 -1274 218 O ATOM 2893 CB PHE A 401 32.401 15.873 105.640 1.00 66.28 C ANISOU 2893 CB PHE A 401 9019 11208 4956 -531 -1384 194 C ATOM 2894 CG PHE A 401 31.240 15.195 106.318 1.00 64.09 C ANISOU 2894 CG PHE A 401 8598 10956 4799 -486 -1437 117 C ATOM 2895 CD1 PHE A 401 30.035 15.850 106.476 1.00 64.10 C ANISOU 2895 CD1 PHE A 401 8536 11010 4809 -368 -1563 225 C ATOM 2896 CD2 PHE A 401 31.359 13.906 106.803 1.00 63.87 C ANISOU 2896 CD2 PHE A 401 8497 10900 4870 -563 -1361 -60 C ATOM 2897 CE1 PHE A 401 28.971 15.229 107.090 1.00 65.72 C ANISOU 2897 CE1 PHE A 401 8594 11262 5114 -337 -1608 156 C ATOM 2898 CE2 PHE A 401 30.296 13.284 107.423 1.00 63.50 C ANISOU 2898 CE2 PHE A 401 8319 10882 4927 -542 -1410 -123 C ATOM 2899 CZ PHE A 401 29.104 13.946 107.566 1.00 65.57 C ANISOU 2899 CZ PHE A 401 8506 11217 5191 -434 -1530 -14 C ATOM 2900 N SER A 402 33.188 17.950 103.322 1.00 72.95 N ANISOU 2900 N SER A 402 10124 12208 5386 -579 -1482 505 N ATOM 2901 CA SER A 402 34.204 18.938 102.997 1.00 72.41 C ANISOU 2901 CA SER A 402 10204 12076 5234 -610 -1442 640 C ATOM 2902 C SER A 402 34.510 19.789 104.221 1.00 73.39 C ANISOU 2902 C SER A 402 10382 11969 5532 -510 -1412 738 C ATOM 2903 O SER A 402 33.742 19.831 105.184 1.00 72.78 O ANISOU 2903 O SER A 402 10236 11804 5614 -390 -1451 734 O ATOM 2904 CB SER A 402 33.751 19.838 101.849 1.00 75.68 C ANISOU 2904 CB SER A 402 10699 12614 5443 -601 -1570 805 C ATOM 2905 OG SER A 402 33.116 21.001 102.351 1.00 76.46 O ANISOU 2905 OG SER A 402 10847 12597 5606 -452 -1673 979 O ATOM 2906 N GLN A 403 35.648 20.486 104.162 1.00 69.52 N ANISOU 2906 N GLN A 403 10019 11392 5005 -567 -1342 826 N ATOM 2907 CA GLN A 403 36.062 21.337 105.274 1.00 69.23 C ANISOU 2907 CA GLN A 403 10053 11132 5119 -492 -1310 918 C ATOM 2908 C GLN A 403 34.999 22.376 105.614 1.00 70.77 C ANISOU 2908 C GLN A 403 10285 11249 5357 -327 -1451 1069 C ATOM 2909 O GLN A 403 34.732 22.640 106.791 1.00 71.26 O ANISOU 2909 O GLN A 403 10326 11153 5595 -214 -1448 1073 O ATOM 2910 CB GLN A 403 37.386 22.021 104.941 1.00 69.94 C ANISOU 2910 CB GLN A 403 10282 11171 5121 -600 -1235 1010 C ATOM 2911 CG GLN A 403 37.903 22.940 106.037 1.00 70.05 C ANISOU 2911 CG GLN A 403 10385 10953 5277 -545 -1205 1107 C ATOM 2912 CD GLN A 403 38.683 22.204 107.108 1.00 68.09 C ANISOU 2912 CD GLN A 403 10067 10607 5199 -573 -1065 965 C ATOM 2913 OE1 GLN A 403 38.888 20.993 107.027 1.00 66.33 O ANISOU 2913 OE1 GLN A 403 9734 10480 4989 -631 -987 794 O ATOM 2914 NE2 GLN A 403 39.129 22.937 108.117 1.00 69.29 N ANISOU 2914 NE2 GLN A 403 10288 10563 5477 -529 -1038 1034 N ATOM 2915 N LYS A 404 34.376 22.973 104.597 1.00 78.37 N ANISOU 2915 N LYS A 404 11300 12322 6155 -303 -1577 1191 N ATOM 2916 CA LYS A 404 33.366 24.000 104.841 1.00 81.27 C ANISOU 2916 CA LYS A 404 11708 12620 6550 -129 -1719 1340 C ATOM 2917 C LYS A 404 32.116 23.406 105.472 1.00 81.64 C ANISOU 2917 C LYS A 404 11584 12717 6718 -2 -1775 1246 C ATOM 2918 O LYS A 404 31.426 24.069 106.255 1.00 83.07 O ANISOU 2918 O LYS A 404 11763 12791 7010 166 -1843 1315 O ATOM 2919 CB LYS A 404 33.024 24.709 103.531 1.00 86.87 C ANISOU 2919 CB LYS A 404 12513 13454 7041 -139 -1844 1493 C ATOM 2920 CG LYS A 404 31.646 25.360 103.495 1.00 89.68 C ANISOU 2920 CG LYS A 404 12849 13834 7393 51 -2016 1600 C ATOM 2921 CD LYS A 404 31.232 25.683 102.081 1.00 91.69 C ANISOU 2921 CD LYS A 404 13154 14270 7416 21 -2136 1709 C ATOM 2922 CE LYS A 404 32.370 26.325 101.315 1.00 91.99 C ANISOU 2922 CE LYS A 404 13378 14274 7301 -121 -2097 1830 C ATOM 2923 NZ LYS A 404 32.697 27.674 101.823 1.00 92.13 N ANISOU 2923 NZ LYS A 404 13578 14055 7373 -39 -2132 2010 N ATOM 2924 N GLN A 405 31.796 22.165 105.122 1.00 76.01 N ANISOU 2924 N GLN A 405 10729 12173 5979 -82 -1751 1087 N ATOM 2925 CA GLN A 405 30.636 21.513 105.707 1.00 72.69 C ANISOU 2925 CA GLN A 405 10137 11815 5667 8 -1798 993 C ATOM 2926 C GLN A 405 30.909 21.031 107.122 1.00 72.21 C ANISOU 2926 C GLN A 405 10011 11600 5825 35 -1689 887 C ATOM 2927 O GLN A 405 30.004 21.062 107.962 1.00 69.36 O ANISOU 2927 O GLN A 405 9553 11215 5587 163 -1734 879 O ATOM 2928 CB GLN A 405 30.185 20.349 104.829 1.00 72.83 C ANISOU 2928 CB GLN A 405 10038 12060 5575 -104 -1818 862 C ATOM 2929 CG GLN A 405 30.238 20.659 103.352 1.00 72.95 C ANISOU 2929 CG GLN A 405 10130 12234 5352 -176 -1892 941 C ATOM 2930 CD GLN A 405 29.633 19.556 102.526 1.00 70.99 C ANISOU 2930 CD GLN A 405 9762 12215 4995 -272 -1930 810 C ATOM 2931 OE1 GLN A 405 29.924 18.380 102.737 1.00 70.22 O ANISOU 2931 OE1 GLN A 405 9589 12137 4954 -374 -1837 630 O ATOM 2932 NE2 GLN A 405 28.785 19.924 101.574 1.00 72.23 N ANISOU 2932 NE2 GLN A 405 9909 12543 4993 -239 -2074 898 N ATOM 2933 N VAL A 406 32.136 20.592 107.415 1.00 70.42 N ANISOU 2933 N VAL A 406 9831 11281 5646 -80 -1548 808 N ATOM 2934 CA VAL A 406 32.463 20.330 108.811 1.00 69.18 C ANISOU 2934 CA VAL A 406 9635 10957 5694 -41 -1453 737 C ATOM 2935 C VAL A 406 32.609 21.643 109.559 1.00 67.29 C ANISOU 2935 C VAL A 406 9506 10528 5531 84 -1476 883 C ATOM 2936 O VAL A 406 32.301 21.718 110.750 1.00 67.57 O ANISOU 2936 O VAL A 406 9494 10450 5730 187 -1459 862 O ATOM 2937 CB VAL A 406 33.722 19.450 108.956 1.00 67.29 C ANISOU 2937 CB VAL A 406 9404 10676 5489 -187 -1300 606 C ATOM 2938 CG1 VAL A 406 33.670 18.273 108.005 1.00 68.22 C ANISOU 2938 CG1 VAL A 406 9450 10976 5496 -312 -1285 470 C ATOM 2939 CG2 VAL A 406 35.002 20.250 108.773 1.00 67.81 C ANISOU 2939 CG2 VAL A 406 9623 10641 5501 -246 -1235 699 C ATOM 2940 N ASP A 407 33.053 22.701 108.878 1.00 74.31 N ANISOU 2940 N ASP A 407 10553 11381 6301 76 -1520 1033 N ATOM 2941 CA ASP A 407 33.088 24.014 109.508 1.00 75.14 C ANISOU 2941 CA ASP A 407 10785 11299 6468 201 -1564 1179 C ATOM 2942 C ASP A 407 31.699 24.436 109.963 1.00 75.12 C ANISOU 2942 C ASP A 407 10711 11303 6527 403 -1684 1224 C ATOM 2943 O ASP A 407 31.538 24.978 111.061 1.00 73.90 O ANISOU 2943 O ASP A 407 10576 10991 6511 531 -1682 1249 O ATOM 2944 CB ASP A 407 33.673 25.048 108.546 1.00 77.75 C ANISOU 2944 CB ASP A 407 11300 11606 6636 147 -1610 1343 C ATOM 2945 CG ASP A 407 35.186 25.034 108.526 1.00 79.30 C ANISOU 2945 CG ASP A 407 11591 11725 6814 -19 -1481 1333 C ATOM 2946 OD1 ASP A 407 35.784 24.057 109.025 1.00 80.16 O ANISOU 2946 OD1 ASP A 407 11610 11839 7009 -100 -1357 1183 O ATOM 2947 OD2 ASP A 407 35.777 26.001 108.001 1.00 80.24 O ANISOU 2947 OD2 ASP A 407 11875 11783 6828 -69 -1506 1479 O ATOM 2948 N GLU A 408 30.679 24.180 109.140 1.00 74.42 N ANISOU 2948 N GLU A 408 10534 11408 6333 436 -1790 1229 N ATOM 2949 CA GLU A 408 29.328 24.595 109.499 1.00 77.18 C ANISOU 2949 CA GLU A 408 10801 11796 6727 635 -1911 1276 C ATOM 2950 C GLU A 408 28.752 23.698 110.583 1.00 73.86 C ANISOU 2950 C GLU A 408 10194 11400 6468 676 -1858 1131 C ATOM 2951 O GLU A 408 28.048 24.175 111.479 1.00 74.59 O ANISOU 2951 O GLU A 408 10243 11429 6669 849 -1898 1157 O ATOM 2952 CB GLU A 408 28.422 24.593 108.267 1.00 80.41 C ANISOU 2952 CB GLU A 408 11162 12424 6965 652 -2046 1329 C ATOM 2953 CG GLU A 408 27.091 25.300 108.491 1.00 80.30 C ANISOU 2953 CG GLU A 408 11091 12451 6970 880 -2190 1416 C ATOM 2954 CD GLU A 408 26.117 25.102 107.350 1.00 80.40 C ANISOU 2954 CD GLU A 408 11014 12712 6822 890 -2322 1445 C ATOM 2955 OE1 GLU A 408 25.610 23.975 107.188 1.00 81.63 O ANISOU 2955 OE1 GLU A 408 10993 13052 6972 808 -2310 1314 O ATOM 2956 OE2 GLU A 408 25.856 26.074 106.611 1.00 81.46 O ANISOU 2956 OE2 GLU A 408 11260 12856 6834 977 -2443 1603 O ATOM 2957 N LEU A 409 29.037 22.396 110.518 1.00 77.16 N ANISOU 2957 N LEU A 409 10505 11909 6902 521 -1769 977 N ATOM 2958 CA LEU A 409 28.578 21.492 111.565 1.00 73.94 C ANISOU 2958 CA LEU A 409 9934 11512 6648 535 -1712 844 C ATOM 2959 C LEU A 409 29.160 21.868 112.919 1.00 71.38 C ANISOU 2959 C LEU A 409 9662 10969 6491 599 -1623 842 C ATOM 2960 O LEU A 409 28.478 21.742 113.941 1.00 69.99 O ANISOU 2960 O LEU A 409 9378 10777 6440 704 -1621 803 O ATOM 2961 CB LEU A 409 28.937 20.051 111.208 1.00 74.80 C ANISOU 2961 CB LEU A 409 9959 11725 6739 346 -1631 684 C ATOM 2962 CG LEU A 409 28.066 19.461 110.098 1.00 75.33 C ANISOU 2962 CG LEU A 409 9926 12031 6666 290 -1725 650 C ATOM 2963 CD1 LEU A 409 28.590 18.113 109.635 1.00 73.62 C ANISOU 2963 CD1 LEU A 409 9669 11889 6414 95 -1644 491 C ATOM 2964 CD2 LEU A 409 26.642 19.330 110.582 1.00 75.51 C ANISOU 2964 CD2 LEU A 409 9778 12167 6746 406 -1813 640 C ATOM 2965 N VAL A 410 30.407 22.344 112.950 1.00 67.10 N ANISOU 2965 N VAL A 410 9280 10269 5947 534 -1549 885 N ATOM 2966 CA VAL A 410 31.003 22.763 114.215 1.00 64.17 C ANISOU 2966 CA VAL A 410 8967 9688 5725 588 -1471 887 C ATOM 2967 C VAL A 410 30.223 23.932 114.809 1.00 63.32 C ANISOU 2967 C VAL A 410 8900 9494 5666 802 -1563 996 C ATOM 2968 O VAL A 410 29.761 23.875 115.954 1.00 63.24 O ANISOU 2968 O VAL A 410 8808 9431 5789 908 -1543 950 O ATOM 2969 CB VAL A 410 32.487 23.122 114.025 1.00 61.17 C ANISOU 2969 CB VAL A 410 8752 9176 5314 466 -1386 924 C ATOM 2970 CG1 VAL A 410 33.024 23.767 115.292 1.00 56.47 C ANISOU 2970 CG1 VAL A 410 8234 8363 4859 535 -1330 948 C ATOM 2971 CG2 VAL A 410 33.295 21.877 113.677 1.00 56.63 C ANISOU 2971 CG2 VAL A 410 8120 8678 4720 280 -1276 790 C ATOM 2972 N GLN A 411 30.058 25.011 114.035 1.00 68.58 N ANISOU 2972 N GLN A 411 9694 10144 6218 873 -1669 1141 N ATOM 2973 CA GLN A 411 29.324 26.172 114.530 1.00 70.51 C ANISOU 2973 CA GLN A 411 9996 10295 6501 1094 -1767 1245 C ATOM 2974 C GLN A 411 27.882 25.818 114.841 1.00 68.76 C ANISOU 2974 C GLN A 411 9577 10233 6317 1241 -1838 1198 C ATOM 2975 O GLN A 411 27.268 26.416 115.729 1.00 69.04 O ANISOU 2975 O GLN A 411 9594 10197 6441 1429 -1873 1220 O ATOM 2976 CB GLN A 411 29.377 27.288 113.499 1.00 77.15 C ANISOU 2976 CB GLN A 411 11014 11104 7197 1133 -1879 1412 C ATOM 2977 CG GLN A 411 30.745 27.458 112.893 1.00 80.19 C ANISOU 2977 CG GLN A 411 11563 11404 7502 942 -1812 1458 C ATOM 2978 CD GLN A 411 31.675 28.231 113.793 1.00 80.37 C ANISOU 2978 CD GLN A 411 11744 11172 7620 948 -1749 1500 C ATOM 2979 OE1 GLN A 411 32.409 27.656 114.601 1.00 78.77 O ANISOU 2979 OE1 GLN A 411 11502 10901 7525 860 -1624 1397 O ATOM 2980 NE2 GLN A 411 31.649 29.552 113.661 1.00 81.92 N ANISOU 2980 NE2 GLN A 411 12129 11221 7777 1050 -1842 1653 N ATOM 2981 N PHE A 412 27.337 24.837 114.129 1.00 65.77 N ANISOU 2981 N PHE A 412 9046 10076 5866 1152 -1859 1128 N ATOM 2982 CA PHE A 412 25.955 24.431 114.343 1.00 65.44 C ANISOU 2982 CA PHE A 412 8800 10218 5847 1264 -1929 1083 C ATOM 2983 C PHE A 412 25.799 23.714 115.675 1.00 64.46 C ANISOU 2983 C PHE A 412 8537 10067 5886 1270 -1832 960 C ATOM 2984 O PHE A 412 24.867 23.993 116.435 1.00 66.86 O ANISOU 2984 O PHE A 412 8737 10406 6260 1441 -1872 961 O ATOM 2985 CB PHE A 412 25.500 23.542 113.191 1.00 66.35 C ANISOU 2985 CB PHE A 412 8802 10573 5835 1137 -1976 1037 C ATOM 2986 CG PHE A 412 24.078 23.095 113.298 1.00 65.03 C ANISOU 2986 CG PHE A 412 8415 10621 5672 1225 -2056 994 C ATOM 2987 CD1 PHE A 412 23.047 23.960 112.992 1.00 66.85 C ANISOU 2987 CD1 PHE A 412 8617 10943 5841 1423 -2198 1101 C ATOM 2988 CD2 PHE A 412 23.765 21.807 113.674 1.00 64.02 C ANISOU 2988 CD2 PHE A 412 8108 10611 5605 1107 -1994 851 C ATOM 2989 CE1 PHE A 412 21.730 23.546 113.071 1.00 67.85 C ANISOU 2989 CE1 PHE A 412 8523 11294 5964 1501 -2273 1062 C ATOM 2990 CE2 PHE A 412 22.445 21.397 113.756 1.00 65.02 C ANISOU 2990 CE2 PHE A 412 8025 10952 5729 1170 -2069 817 C ATOM 2991 CZ PHE A 412 21.438 22.267 113.455 1.00 66.93 C ANISOU 2991 CZ PHE A 412 8223 11301 5905 1365 -2206 921 C ATOM 2992 N ARG A 413 26.705 22.781 115.969 1.00 59.83 N ANISOU 2992 N ARG A 413 7947 9427 5357 1089 -1704 855 N ATOM 2993 CA ARG A 413 26.609 22.016 117.207 1.00 58.33 C ANISOU 2993 CA ARG A 413 7634 9213 5316 1076 -1611 741 C ATOM 2994 C ARG A 413 26.711 22.929 118.421 1.00 57.82 C ANISOU 2994 C ARG A 413 7636 8967 5367 1239 -1587 784 C ATOM 2995 O ARG A 413 25.952 22.785 119.386 1.00 57.64 O ANISOU 2995 O ARG A 413 7482 8983 5434 1343 -1580 741 O ATOM 2996 CB ARG A 413 27.705 20.948 117.235 1.00 56.72 C ANISOU 2996 CB ARG A 413 7448 8958 5146 863 -1484 634 C ATOM 2997 CG ARG A 413 27.422 19.759 118.126 1.00 55.56 C ANISOU 2997 CG ARG A 413 7141 8856 5112 797 -1408 503 C ATOM 2998 CD ARG A 413 27.718 20.062 119.579 1.00 54.28 C ANISOU 2998 CD ARG A 413 6995 8531 5099 881 -1332 493 C ATOM 2999 NE ARG A 413 27.284 18.989 120.464 1.00 53.42 N ANISOU 2999 NE ARG A 413 6726 8481 5091 832 -1274 384 N ATOM 3000 CZ ARG A 413 27.120 19.125 121.776 1.00 52.65 C ANISOU 3000 CZ ARG A 413 6584 8307 5112 920 -1226 369 C ATOM 3001 NH1 ARG A 413 27.349 20.297 122.352 1.00 52.63 N ANISOU 3001 NH1 ARG A 413 6688 8163 5146 1069 -1233 445 N ATOM 3002 NH2 ARG A 413 26.725 18.092 122.510 1.00 52.00 N ANISOU 3002 NH2 ARG A 413 6358 8290 5109 855 -1175 277 N ATOM 3003 N LYS A 414 27.643 23.880 118.383 1.00 66.40 N ANISOU 3003 N LYS A 414 8926 9860 6442 1256 -1574 868 N ATOM 3004 CA LYS A 414 27.794 24.815 119.489 1.00 66.08 C ANISOU 3004 CA LYS A 414 8975 9631 6501 1405 -1559 908 C ATOM 3005 C LYS A 414 26.541 25.658 119.675 1.00 67.70 C ANISOU 3005 C LYS A 414 9134 9891 6699 1650 -1676 973 C ATOM 3006 O LYS A 414 26.105 25.891 120.808 1.00 67.18 O ANISOU 3006 O LYS A 414 9011 9778 6734 1789 -1657 942 O ATOM 3007 CB LYS A 414 29.018 25.697 119.256 1.00 67.91 C ANISOU 3007 CB LYS A 414 9445 9653 6703 1355 -1538 994 C ATOM 3008 CG LYS A 414 30.268 24.884 118.969 1.00 69.99 C ANISOU 3008 CG LYS A 414 9742 9892 6958 1121 -1426 931 C ATOM 3009 CD LYS A 414 31.544 25.707 118.995 1.00 70.97 C ANISOU 3009 CD LYS A 414 10079 9812 7074 1059 -1385 1004 C ATOM 3010 CE LYS A 414 32.706 24.848 119.494 1.00 70.84 C ANISOU 3010 CE LYS A 414 10045 9741 7128 887 -1242 904 C ATOM 3011 NZ LYS A 414 34.029 25.533 119.417 1.00 71.95 N ANISOU 3011 NZ LYS A 414 10371 9719 7246 792 -1196 969 N ATOM 3012 N ALA A 415 25.934 26.110 118.576 1.00 61.05 N ANISOU 3012 N ALA A 415 8307 9156 5731 1712 -1799 1061 N ATOM 3013 CA ALA A 415 24.750 26.952 118.680 1.00 63.79 C ANISOU 3013 CA ALA A 415 8613 9561 6063 1964 -1920 1129 C ATOM 3014 C ALA A 415 23.512 26.183 119.115 1.00 62.83 C ANISOU 3014 C ALA A 415 8225 9670 5979 2030 -1933 1043 C ATOM 3015 O ALA A 415 22.484 26.810 119.384 1.00 64.26 O ANISOU 3015 O ALA A 415 8336 9919 6161 2254 -2020 1081 O ATOM 3016 CB ALA A 415 24.477 27.645 117.346 1.00 64.59 C ANISOU 3016 CB ALA A 415 8812 9717 6012 2010 -2055 1257 C ATOM 3017 N ASN A 416 23.584 24.857 119.191 1.00 65.89 N ANISOU 3017 N ASN A 416 8463 10180 6394 1842 -1851 929 N ATOM 3018 CA ASN A 416 22.457 24.007 119.561 1.00 66.18 C ANISOU 3018 CA ASN A 416 8243 10444 6460 1858 -1858 845 C ATOM 3019 C ASN A 416 22.871 22.982 120.604 1.00 65.39 C ANISOU 3019 C ASN A 416 8058 10307 6481 1722 -1719 723 C ATOM 3020 O ASN A 416 22.409 21.837 120.601 1.00 64.15 O ANISOU 3020 O ASN A 416 7726 10318 6331 1597 -1694 636 O ATOM 3021 CB ASN A 416 21.864 23.314 118.339 1.00 67.06 C ANISOU 3021 CB ASN A 416 8238 10793 6448 1749 -1934 837 C ATOM 3022 CG ASN A 416 21.016 24.243 117.500 1.00 68.81 C ANISOU 3022 CG ASN A 416 8467 11122 6555 1928 -2091 952 C ATOM 3023 OD1 ASN A 416 19.865 24.517 117.835 1.00 69.17 O ANISOU 3023 OD1 ASN A 416 8363 11311 6608 2108 -2163 964 O ATOM 3024 ND2 ASN A 416 21.582 24.736 116.404 1.00 70.56 N ANISOU 3024 ND2 ASN A 416 8861 11283 6666 1882 -2145 1041 N ATOM 3025 N SER A 417 23.757 23.381 121.515 1.00 65.47 N ANISOU 3025 N SER A 417 8198 10091 6586 1741 -1632 718 N ATOM 3026 CA SER A 417 24.071 22.525 122.650 1.00 61.71 C ANISOU 3026 CA SER A 417 7641 9575 6229 1648 -1509 614 C ATOM 3027 C SER A 417 22.814 22.145 123.416 1.00 60.70 C ANISOU 3027 C SER A 417 7285 9631 6147 1744 -1521 564 C ATOM 3028 O SER A 417 22.732 21.042 123.968 1.00 61.49 O ANISOU 3028 O SER A 417 7255 9803 6308 1613 -1446 472 O ATOM 3029 CB SER A 417 25.064 23.232 123.568 1.00 59.58 C ANISOU 3029 CB SER A 417 7542 9048 6046 1696 -1435 630 C ATOM 3030 OG SER A 417 24.582 24.516 123.927 1.00 59.52 O ANISOU 3030 OG SER A 417 7602 8972 6040 1937 -1506 705 O ATOM 3031 N SER A 418 21.821 23.032 123.441 1.00 59.12 N ANISOU 3031 N SER A 418 7033 9516 5914 1971 -1618 625 N ATOM 3032 CA SER A 418 20.590 22.764 124.169 1.00 59.89 C ANISOU 3032 CA SER A 418 6900 9812 6044 2079 -1630 582 C ATOM 3033 C SER A 418 19.829 21.577 123.603 1.00 60.39 C ANISOU 3033 C SER A 418 6752 10136 6057 1924 -1655 527 C ATOM 3034 O SER A 418 18.978 21.014 124.297 1.00 60.66 O ANISOU 3034 O SER A 418 6579 10339 6128 1932 -1634 472 O ATOM 3035 CB SER A 418 19.709 24.011 124.161 1.00 61.85 C ANISOU 3035 CB SER A 418 7143 10106 6253 2371 -1740 661 C ATOM 3036 OG SER A 418 19.855 24.724 122.943 1.00 63.00 O ANISOU 3036 OG SER A 418 7429 10214 6295 2415 -1846 759 O ATOM 3037 N ILE A 419 20.111 21.185 122.367 1.00 66.70 N ANISOU 3037 N ILE A 419 7600 10978 6767 1777 -1699 540 N ATOM 3038 CA ILE A 419 19.430 20.067 121.731 1.00 67.18 C ANISOU 3038 CA ILE A 419 7482 11276 6769 1616 -1731 485 C ATOM 3039 C ILE A 419 20.303 18.822 121.714 1.00 64.20 C ANISOU 3039 C ILE A 419 7138 10824 6430 1346 -1630 392 C ATOM 3040 O ILE A 419 19.840 17.725 122.022 1.00 66.00 O ANISOU 3040 O ILE A 419 7208 11182 6688 1210 -1597 311 O ATOM 3041 CB ILE A 419 18.984 20.458 120.306 1.00 70.90 C ANISOU 3041 CB ILE A 419 7965 11880 7095 1648 -1866 557 C ATOM 3042 CG1 ILE A 419 18.283 21.816 120.327 1.00 73.93 C ANISOU 3042 CG1 ILE A 419 8359 12287 7445 1940 -1970 660 C ATOM 3043 CG2 ILE A 419 18.072 19.397 119.741 1.00 73.24 C ANISOU 3043 CG2 ILE A 419 8051 12450 7327 1507 -1916 499 C ATOM 3044 CD1 ILE A 419 17.838 22.300 118.969 1.00 75.34 C ANISOU 3044 CD1 ILE A 419 8560 12588 7478 1995 -2112 746 C ATOM 3045 N PHE A 420 21.572 18.972 121.346 1.00 58.43 N ANISOU 3045 N PHE A 420 6615 9888 5697 1266 -1580 403 N ATOM 3046 CA PHE A 420 22.485 17.840 121.351 1.00 56.90 C ANISOU 3046 CA PHE A 420 6466 9611 5544 1035 -1481 312 C ATOM 3047 C PHE A 420 23.047 17.536 122.734 1.00 55.21 C ANISOU 3047 C PHE A 420 6263 9245 5470 1017 -1359 260 C ATOM 3048 O PHE A 420 23.755 16.538 122.891 1.00 53.98 O ANISOU 3048 O PHE A 420 6131 9019 5360 840 -1275 181 O ATOM 3049 CB PHE A 420 23.630 18.085 120.373 1.00 56.52 C ANISOU 3049 CB PHE A 420 6618 9432 5427 954 -1473 341 C ATOM 3050 CG PHE A 420 23.193 18.188 118.953 1.00 58.11 C ANISOU 3050 CG PHE A 420 6813 9787 5479 931 -1583 382 C ATOM 3051 CD1 PHE A 420 22.723 17.075 118.278 1.00 58.67 C ANISOU 3051 CD1 PHE A 420 6767 10035 5489 769 -1609 304 C ATOM 3052 CD2 PHE A 420 23.255 19.395 118.281 1.00 59.15 C ANISOU 3052 CD2 PHE A 420 7067 9883 5525 1063 -1664 498 C ATOM 3053 CE1 PHE A 420 22.319 17.166 116.955 1.00 60.21 C ANISOU 3053 CE1 PHE A 420 6958 10382 5538 743 -1714 339 C ATOM 3054 CE2 PHE A 420 22.850 19.489 116.955 1.00 60.71 C ANISOU 3054 CE2 PHE A 420 7261 10230 5575 1039 -1770 542 C ATOM 3055 CZ PHE A 420 22.388 18.373 116.298 1.00 61.21 C ANISOU 3055 CZ PHE A 420 7199 10481 5576 880 -1794 460 C ATOM 3056 N GLY A 421 22.758 18.363 123.729 1.00 55.21 N ANISOU 3056 N GLY A 421 6252 9193 5534 1200 -1351 299 N ATOM 3057 CA GLY A 421 23.048 18.026 125.102 1.00 53.88 C ANISOU 3057 CA GLY A 421 6057 8928 5488 1190 -1246 248 C ATOM 3058 C GLY A 421 21.942 17.290 125.821 1.00 54.36 C ANISOU 3058 C GLY A 421 5891 9178 5585 1174 -1239 196 C ATOM 3059 O GLY A 421 22.044 17.071 127.029 1.00 53.46 O ANISOU 3059 O GLY A 421 5741 9007 5566 1182 -1158 162 O ATOM 3060 N LYS A 422 20.884 16.893 125.128 1.00 55.82 N ANISOU 3060 N LYS A 422 5919 9598 5694 1144 -1322 192 N ATOM 3061 CA LYS A 422 19.764 16.254 125.802 1.00 56.53 C ANISOU 3061 CA LYS A 422 5779 9891 5807 1125 -1321 152 C ATOM 3062 C LYS A 422 19.962 14.757 125.975 1.00 55.71 C ANISOU 3062 C LYS A 422 5619 9804 5745 868 -1256 63 C ATOM 3063 O LYS A 422 19.132 14.110 126.616 1.00 56.20 O ANISOU 3063 O LYS A 422 5500 10020 5833 814 -1242 29 O ATOM 3064 CB LYS A 422 18.456 16.536 125.044 1.00 58.69 C ANISOU 3064 CB LYS A 422 5889 10433 5978 1213 -1447 190 C ATOM 3065 N GLY A 423 21.021 14.191 125.417 1.00 54.64 N ANISOU 3065 N GLY A 423 5632 9519 5611 711 -1217 25 N ATOM 3066 CA GLY A 423 21.370 12.827 125.746 1.00 53.76 C ANISOU 3066 CA GLY A 423 5503 9368 5557 491 -1145 -61 C ATOM 3067 C GLY A 423 20.939 11.771 124.754 1.00 54.69 C ANISOU 3067 C GLY A 423 5552 9626 5602 298 -1200 -118 C ATOM 3068 O GLY A 423 21.073 11.946 123.539 1.00 55.32 O ANISOU 3068 O GLY A 423 5696 9738 5587 279 -1265 -109 O ATOM 3069 N TRP A 424 20.418 10.660 125.269 1.00 54.88 N ANISOU 3069 N TRP A 424 5452 9734 5666 144 -1176 -177 N ATOM 3070 CA TRP A 424 20.239 9.453 124.484 1.00 55.52 C ANISOU 3070 CA TRP A 424 5506 9888 5700 -79 -1208 -252 C ATOM 3071 C TRP A 424 18.890 8.823 124.797 1.00 56.95 C ANISOU 3071 C TRP A 424 5463 10309 5867 -167 -1254 -266 C ATOM 3072 O TRP A 424 18.351 8.970 125.896 1.00 56.98 O ANISOU 3072 O TRP A 424 5347 10374 5929 -104 -1219 -240 O ATOM 3073 CB TRP A 424 21.386 8.460 124.732 1.00 54.07 C ANISOU 3073 CB TRP A 424 5467 9485 5592 -239 -1116 -330 C ATOM 3074 CG TRP A 424 22.722 9.107 124.503 1.00 52.73 C ANISOU 3074 CG TRP A 424 5498 9102 5436 -153 -1065 -314 C ATOM 3075 CD1 TRP A 424 23.422 9.851 125.408 1.00 51.44 C ANISOU 3075 CD1 TRP A 424 5414 8779 5351 -20 -993 -269 C ATOM 3076 CD2 TRP A 424 23.496 9.122 123.290 1.00 52.71 C ANISOU 3076 CD2 TRP A 424 5635 9037 5357 -196 -1084 -338 C ATOM 3077 NE1 TRP A 424 24.585 10.311 124.847 1.00 50.62 N ANISOU 3077 NE1 TRP A 424 5486 8519 5228 12 -967 -261 N ATOM 3078 CE2 TRP A 424 24.654 9.879 123.550 1.00 51.38 C ANISOU 3078 CE2 TRP A 424 5619 8675 5228 -92 -1018 -302 C ATOM 3079 CE3 TRP A 424 23.333 8.554 122.024 1.00 53.76 C ANISOU 3079 CE3 TRP A 424 5777 9264 5386 -319 -1148 -390 C ATOM 3080 CZ2 TRP A 424 25.635 10.086 122.593 1.00 51.10 C ANISOU 3080 CZ2 TRP A 424 5735 8552 5131 -109 -1011 -310 C ATOM 3081 CZ3 TRP A 424 24.303 8.767 121.076 1.00 53.46 C ANISOU 3081 CZ3 TRP A 424 5893 9136 5284 -326 -1140 -403 C ATOM 3082 CH2 TRP A 424 25.438 9.527 121.360 1.00 52.16 C ANISOU 3082 CH2 TRP A 424 5869 8791 5159 -223 -1071 -360 C ATOM 3083 N HIS A 425 18.339 8.145 123.794 1.00 58.27 N ANISOU 3083 N HIS A 425 5570 10625 5947 -316 -1334 -308 N ATOM 3084 CA HIS A 425 17.058 7.467 123.909 1.00 59.88 C ANISOU 3084 CA HIS A 425 5559 11075 6119 -437 -1389 -326 C ATOM 3085 C HIS A 425 17.248 6.127 124.608 1.00 59.38 C ANISOU 3085 C HIS A 425 5502 10922 6137 -663 -1321 -398 C ATOM 3086 O HIS A 425 18.301 5.502 124.511 1.00 58.21 O ANISOU 3086 O HIS A 425 5531 10551 6034 -764 -1263 -457 O ATOM 3087 CB HIS A 425 16.445 7.263 122.517 1.00 61.58 C ANISOU 3087 CB HIS A 425 5720 11476 6201 -522 -1509 -346 C ATOM 3088 CG HIS A 425 14.960 7.081 122.524 1.00 63.60 C ANISOU 3088 CG HIS A 425 5721 12046 6397 -564 -1593 -329 C ATOM 3089 ND1 HIS A 425 14.356 5.890 122.863 1.00 64.38 N ANISOU 3089 ND1 HIS A 425 5705 12245 6513 -797 -1592 -385 N ATOM 3090 CD2 HIS A 425 13.956 7.942 122.232 1.00 65.13 C ANISOU 3090 CD2 HIS A 425 5750 12484 6511 -405 -1684 -260 C ATOM 3091 CE1 HIS A 425 13.044 6.028 122.790 1.00 66.29 C ANISOU 3091 CE1 HIS A 425 5710 12792 6686 -788 -1675 -352 C ATOM 3092 NE2 HIS A 425 12.775 7.261 122.404 1.00 66.78 N ANISOU 3092 NE2 HIS A 425 5734 12951 6689 -543 -1732 -278 N ATOM 3093 N ASN A 426 16.214 5.676 125.306 1.00 60.41 N ANISOU 3093 N ASN A 426 5439 11233 6281 -742 -1329 -391 N ATOM 3094 CA ASN A 426 16.364 4.418 126.019 1.00 60.07 C ANISOU 3094 CA ASN A 426 5412 11099 6314 -962 -1269 -446 C ATOM 3095 C ASN A 426 16.435 3.212 125.097 1.00 60.82 C ANISOU 3095 C ASN A 426 5573 11171 6366 -1214 -1317 -536 C ATOM 3096 O ASN A 426 16.801 2.127 125.563 1.00 63.56 O ANISOU 3096 O ASN A 426 5993 11377 6780 -1396 -1267 -590 O ATOM 3097 CB ASN A 426 15.221 4.235 127.013 1.00 61.15 C ANISOU 3097 CB ASN A 426 5319 11448 6467 -999 -1263 -409 C ATOM 3098 CG ASN A 426 15.612 4.626 128.416 1.00 59.78 C ANISOU 3098 CG ASN A 426 5169 11143 6401 -909 -1152 -375 C ATOM 3099 OD1 ASN A 426 16.529 5.419 128.618 1.00 61.03 O ANISOU 3099 OD1 ASN A 426 5382 11175 6633 -1070 -1089 -405 O ATOM 3100 ND2 ASN A 426 14.905 4.087 129.395 1.00 59.32 N ANISOU 3100 ND2 ASN A 426 5083 11108 6350 -649 -1133 -313 N ATOM 3101 N PHE A 427 16.098 3.371 123.819 1.00 61.98 N ANISOU 3101 N PHE A 427 5704 11447 6399 -1227 -1414 -553 N ATOM 3102 CA PHE A 427 16.085 2.281 122.858 1.00 62.95 C ANISOU 3102 CA PHE A 427 5885 11569 6462 -1460 -1471 -647 C ATOM 3103 C PHE A 427 17.241 2.411 121.879 1.00 62.04 C ANISOU 3103 C PHE A 427 5991 11266 6314 -1421 -1463 -696 C ATOM 3104 O PHE A 427 17.716 3.512 121.596 1.00 61.28 O ANISOU 3104 O PHE A 427 5955 11134 6196 -1215 -1455 -640 O ATOM 3105 CB PHE A 427 14.771 2.263 122.077 1.00 65.23 C ANISOU 3105 CB PHE A 427 5978 12178 6628 -1532 -1597 -639 C ATOM 3106 CG PHE A 427 13.656 1.551 122.776 1.00 66.60 C ANISOU 3106 CG PHE A 427 5951 12540 6815 -1701 -1616 -634 C ATOM 3107 CD1 PHE A 427 13.925 0.611 123.756 1.00 66.00 C ANISOU 3107 CD1 PHE A 427 5922 12315 6842 -1858 -1538 -664 C ATOM 3108 CD2 PHE A 427 12.337 1.817 122.450 1.00 68.63 C ANISOU 3108 CD2 PHE A 427 5968 13132 6976 -1706 -1715 -595 C ATOM 3109 CE1 PHE A 427 12.898 -0.051 124.401 1.00 67.40 C ANISOU 3109 CE1 PHE A 427 5915 12671 7024 -2031 -1555 -651 C ATOM 3110 CE2 PHE A 427 11.308 1.159 123.088 1.00 70.04 C ANISOU 3110 CE2 PHE A 427 5948 13504 7159 -1875 -1731 -589 C ATOM 3111 CZ PHE A 427 11.590 0.219 124.064 1.00 69.43 C ANISOU 3111 CZ PHE A 427 5925 13272 7182 -2046 -1649 -615 C ATOM 3112 N SER A 428 17.686 1.272 121.357 1.00 62.26 N ANISOU 3112 N SER A 428 6143 11177 6335 -1622 -1465 -801 N ATOM 3113 CA SER A 428 18.536 1.283 120.179 1.00 62.04 C ANISOU 3113 CA SER A 428 6288 11049 6237 -1616 -1480 -863 C ATOM 3114 C SER A 428 17.707 1.600 118.935 1.00 63.84 C ANISOU 3114 C SER A 428 6421 11526 6311 -1630 -1604 -859 C ATOM 3115 O SER A 428 16.476 1.652 118.972 1.00 65.34 O ANISOU 3115 O SER A 428 6412 11962 6453 -1670 -1683 -821 O ATOM 3116 CB SER A 428 19.241 -0.058 120.011 1.00 61.92 C ANISOU 3116 CB SER A 428 6434 10836 6258 -1815 -1445 -990 C ATOM 3117 OG SER A 428 18.304 -1.101 119.849 1.00 63.67 O ANISOU 3117 OG SER A 428 6568 11178 6446 -2047 -1517 -1048 O ATOM 3118 N VAL A 429 18.398 1.822 117.816 1.00 63.78 N ANISOU 3118 N VAL A 429 6552 11466 6217 -1598 -1624 -897 N ATOM 3119 CA VAL A 429 17.699 2.037 116.552 1.00 65.56 C ANISOU 3119 CA VAL A 429 6709 11918 6283 -1626 -1745 -900 C ATOM 3120 C VAL A 429 17.172 0.717 116.009 1.00 67.18 C ANISOU 3120 C VAL A 429 6896 12196 6434 -1896 -1810 -1017 C ATOM 3121 O VAL A 429 16.086 0.658 115.419 1.00 69.06 O ANISOU 3121 O VAL A 429 6985 12687 6568 -1974 -1923 -1012 O ATOM 3122 CB VAL A 429 18.628 2.735 115.542 1.00 65.05 C ANISOU 3122 CB VAL A 429 6802 11781 6134 -1508 -1741 -895 C ATOM 3123 CG1 VAL A 429 18.082 2.610 114.111 1.00 66.98 C ANISOU 3123 CG1 VAL A 429 7020 12227 6204 -1595 -1862 -934 C ATOM 3124 CG2 VAL A 429 18.807 4.189 115.910 1.00 64.10 C ANISOU 3124 CG2 VAL A 429 6666 11655 6034 -1249 -1718 -759 C ATOM 3125 N LYS A 430 17.937 -0.360 116.197 1.00 66.59 N ANISOU 3125 N LYS A 430 6976 11898 6427 -2039 -1745 -1126 N ATOM 3126 CA LYS A 430 17.514 -1.677 115.743 1.00 68.16 C ANISOU 3126 CA LYS A 430 7190 12123 6585 -2303 -1804 -1248 C ATOM 3127 C LYS A 430 16.123 -2.013 116.254 1.00 69.65 C ANISOU 3127 C LYS A 430 7160 12529 6776 -2435 -1874 -1210 C ATOM 3128 O LYS A 430 15.263 -2.485 115.503 1.00 72.21 O ANISOU 3128 O LYS A 430 7397 13046 6992 -2598 -1983 -1256 O ATOM 3129 CB LYS A 430 18.515 -2.732 116.208 1.00 67.19 C ANISOU 3129 CB LYS A 430 7260 11700 6569 -2405 -1712 -1351 C ATOM 3130 CG LYS A 430 18.056 -4.155 115.957 1.00 69.18 C ANISOU 3130 CG LYS A 430 7542 11939 6803 -2685 -1770 -1473 C ATOM 3131 CD LYS A 430 18.606 -5.096 117.006 1.00 69.05 C ANISOU 3131 CD LYS A 430 7637 11663 6936 -2775 -1684 -1517 C ATOM 3132 CE LYS A 430 18.404 -6.537 116.597 1.00 69.93 C ANISOU 3132 CE LYS A 430 7845 11701 7025 -3044 -1739 -1657 C ATOM 3133 NZ LYS A 430 19.127 -6.839 115.331 1.00 70.16 N ANISOU 3133 NZ LYS A 430 8049 11655 6955 -3055 -1759 -1789 N ATOM 3134 N LEU A 431 15.884 -1.763 117.534 1.00 70.62 N ANISOU 3134 N LEU A 431 7182 12636 7013 -2369 -1813 -1125 N ATOM 3135 CA LEU A 431 14.590 -2.094 118.110 1.00 73.28 C ANISOU 3135 CA LEU A 431 7299 13191 7354 -2499 -1867 -1086 C ATOM 3136 C LEU A 431 13.493 -1.202 117.551 1.00 72.62 C ANISOU 3136 C LEU A 431 6998 13443 7150 -2404 -1972 -1007 C ATOM 3137 O LEU A 431 12.386 -1.671 117.276 1.00 73.84 O ANISOU 3137 O LEU A 431 6989 13835 7232 -2573 -2067 -1021 O ATOM 3138 CB LEU A 431 14.658 -1.979 119.627 1.00 73.63 C ANISOU 3138 CB LEU A 431 7291 13143 7540 -2434 -1767 -1013 C ATOM 3139 CG LEU A 431 13.387 -2.377 120.365 1.00 75.91 C ANISOU 3139 CG LEU A 431 7352 13651 7839 -2578 -1803 -970 C ATOM 3140 CD1 LEU A 431 13.765 -3.123 121.607 1.00 75.75 C ANISOU 3140 CD1 LEU A 431 7397 13428 7955 -2677 -1707 -974 C ATOM 3141 CD2 LEU A 431 12.589 -1.154 120.733 1.00 76.28 C ANISOU 3141 CD2 LEU A 431 7174 13951 7859 -2366 -1821 -849 C ATOM 3142 N MET A 432 13.776 0.089 117.386 1.00 75.95 N ANISOU 3142 N MET A 432 7416 13891 7550 -2136 -1961 -921 N ATOM 3143 CA MET A 432 12.760 1.002 116.877 1.00 78.72 C ANISOU 3143 CA MET A 432 7569 14550 7791 -2014 -2065 -838 C ATOM 3144 C MET A 432 12.335 0.626 115.461 1.00 80.50 C ANISOU 3144 C MET A 432 7789 14940 7859 -2154 -2190 -903 C ATOM 3145 O MET A 432 11.157 0.752 115.103 1.00 80.55 O ANISOU 3145 O MET A 432 7586 15250 7770 -2193 -2300 -870 O ATOM 3146 CB MET A 432 13.289 2.429 116.927 1.00 80.67 C ANISOU 3146 CB MET A 432 7862 14741 8046 -1702 -2030 -738 C ATOM 3147 CG MET A 432 13.402 2.975 118.321 1.00 79.36 C ANISOU 3147 CG MET A 432 7648 14492 8013 -1545 -1932 -660 C ATOM 3148 SD MET A 432 14.422 4.447 118.340 1.00 78.54 S ANISOU 3148 SD MET A 432 7695 14212 7936 -1224 -1873 -574 S ATOM 3149 CE MET A 432 13.791 5.251 119.777 1.00 80.21 C ANISOU 3149 CE MET A 432 7730 14507 8241 -1030 -1826 -471 C ATOM 3150 N MET A 433 13.278 0.150 114.644 1.00 80.66 N ANISOU 3150 N MET A 433 8030 14775 7842 -2230 -2175 -1000 N ATOM 3151 CA MET A 433 12.934 -0.270 113.291 1.00 82.42 C ANISOU 3151 CA MET A 433 8265 15144 7909 -2373 -2290 -1076 C ATOM 3152 C MET A 433 12.124 -1.557 113.265 1.00 82.12 C ANISOU 3152 C MET A 433 8146 15207 7849 -2680 -2354 -1169 C ATOM 3153 O MET A 433 11.438 -1.818 112.276 1.00 85.70 O ANISOU 3153 O MET A 433 8529 15871 8163 -2806 -2475 -1211 O ATOM 3154 CB MET A 433 14.200 -0.418 112.446 1.00 81.02 C ANISOU 3154 CB MET A 433 8348 14745 7692 -2363 -2248 -1162 C ATOM 3155 CG MET A 433 15.033 0.827 112.445 1.00 81.04 C ANISOU 3155 CG MET A 433 8438 14645 7710 -2088 -2186 -1068 C ATOM 3156 SD MET A 433 13.893 2.201 112.481 1.00 82.39 S ANISOU 3156 SD MET A 433 8369 15117 7817 -1874 -2279 -902 S ATOM 3157 CE MET A 433 13.936 2.665 110.776 1.00 85.76 C ANISOU 3157 CE MET A 433 8858 15687 8038 -1845 -2390 -906 C ATOM 3158 N GLU A 434 12.196 -2.369 114.310 1.00 78.99 N ANISOU 3158 N GLU A 434 7764 14665 7582 -2811 -2282 -1199 N ATOM 3159 CA GLU A 434 11.256 -3.460 114.489 1.00 81.04 C ANISOU 3159 CA GLU A 434 7912 15050 7831 -3098 -2345 -1253 C ATOM 3160 C GLU A 434 9.973 -2.998 115.154 1.00 81.90 C ANISOU 3160 C GLU A 434 7720 15463 7937 -3072 -2390 -1141 C ATOM 3161 O GLU A 434 9.114 -3.830 115.461 1.00 82.14 O ANISOU 3161 O GLU A 434 7622 15624 7963 -3311 -2436 -1165 O ATOM 3162 CB GLU A 434 11.894 -4.569 115.319 1.00 83.66 C ANISOU 3162 CB GLU A 434 8403 15085 8298 -3261 -2252 -1328 C ATOM 3163 CG GLU A 434 13.198 -5.078 114.750 1.00 85.71 C ANISOU 3163 CG GLU A 434 8956 15039 8570 -3273 -2200 -1447 C ATOM 3164 CD GLU A 434 13.615 -6.391 115.363 1.00 88.97 C ANISOU 3164 CD GLU A 434 9521 15193 9089 -3483 -2147 -1541 C ATOM 3165 OE1 GLU A 434 12.995 -6.793 116.369 1.00 92.82 O ANISOU 3165 OE1 GLU A 434 9895 15717 9657 -3598 -2134 -1493 O ATOM 3166 OE2 GLU A 434 14.555 -7.024 114.840 1.00 89.09 O ANISOU 3166 OE2 GLU A 434 9770 14975 9105 -3531 -2120 -1662 O ATOM 3167 N LEU A 435 9.828 -1.710 115.383 1.00 79.06 N ANISOU 3167 N LEU A 435 7246 15217 7575 -2790 -2378 -1022 N ATOM 3168 CA LEU A 435 8.655 -1.169 116.056 1.00 80.08 C ANISOU 3168 CA LEU A 435 7085 15640 7703 -2719 -2411 -916 C ATOM 3169 C LEU A 435 7.988 -0.043 115.283 1.00 81.23 C ANISOU 3169 C LEU A 435 7073 16069 7722 -2518 -2515 -835 C ATOM 3170 O LEU A 435 6.760 0.040 115.283 1.00 83.22 O ANISOU 3170 O LEU A 435 7065 16651 7905 -2560 -2604 -792 O ATOM 3171 CB LEU A 435 9.035 -0.680 117.471 1.00 78.16 C ANISOU 3171 CB LEU A 435 6834 15253 7611 -2546 -2279 -837 C ATOM 3172 CG LEU A 435 8.727 -1.616 118.648 1.00 78.27 C ANISOU 3172 CG LEU A 435 6785 15228 7728 -2749 -2216 -849 C ATOM 3173 CD1 LEU A 435 9.498 -2.929 118.571 1.00 77.84 C ANISOU 3173 CD1 LEU A 435 6965 14885 7726 -3002 -2179 -967 C ATOM 3174 CD2 LEU A 435 8.998 -0.918 119.957 1.00 76.58 C ANISOU 3174 CD2 LEU A 435 6534 14929 7634 -2538 -2099 -760 C ATOM 3175 N ILE A 436 8.762 0.830 114.632 1.00 80.14 N ANISOU 3175 N ILE A 436 7084 15818 7548 -2300 -2509 -809 N ATOM 3176 CA ILE A 436 8.163 1.950 113.902 1.00 82.71 C ANISOU 3176 CA ILE A 436 7279 16394 7752 -2092 -2613 -721 C ATOM 3177 C ILE A 436 7.187 1.476 112.832 1.00 85.23 C ANISOU 3177 C ILE A 436 7460 17012 7911 -2277 -2767 -763 C ATOM 3178 O ILE A 436 6.091 2.048 112.735 1.00 86.04 O ANISOU 3178 O ILE A 436 7356 17364 7970 -2163 -2825 -676 O ATOM 3179 CB ILE A 436 9.254 2.875 113.354 1.00 82.12 C ANISOU 3179 CB ILE A 436 7421 16118 7664 -1863 -2578 -686 C ATOM 3180 CG1 ILE A 436 9.942 3.632 114.493 1.00 77.47 C ANISOU 3180 CG1 ILE A 436 6900 15314 7221 -1635 -2448 -613 C ATOM 3181 CG2 ILE A 436 8.675 3.830 112.301 1.00 81.28 C ANISOU 3181 CG2 ILE A 436 7222 16259 7402 -1704 -2710 -610 C ATOM 3182 CD1 ILE A 436 11.082 4.504 114.036 1.00 75.91 C ANISOU 3182 CD1 ILE A 436 6925 14900 7018 -1435 -2405 -578 C ATOM 3183 N PRO A 437 7.505 0.469 111.984 1.00 84.57 N ANISOU 3183 N PRO A 437 7529 16834 7769 -2520 -2795 -884 N ATOM 3184 CA PRO A 437 6.486 -0.072 111.072 1.00 87.30 C ANISOU 3184 CA PRO A 437 7795 17349 8025 -2672 -2877 -910 C ATOM 3185 C PRO A 437 5.178 -0.377 111.780 1.00 89.02 C ANISOU 3185 C PRO A 437 7771 17761 8292 -2750 -2875 -859 C ATOM 3186 O PRO A 437 4.139 0.184 111.420 1.00 90.90 O ANISOU 3186 O PRO A 437 7825 18250 8464 -2645 -2940 -781 O ATOM 3187 CB PRO A 437 7.129 -1.357 110.532 1.00 87.34 C ANISOU 3187 CB PRO A 437 8021 17145 8020 -2948 -2864 -1065 C ATOM 3188 CG PRO A 437 8.517 -1.418 111.128 1.00 84.60 C ANISOU 3188 CG PRO A 437 7868 16523 7754 -2922 -2775 -1118 C ATOM 3189 CD PRO A 437 8.834 -0.076 111.675 1.00 82.96 C ANISOU 3189 CD PRO A 437 7622 16302 7597 -2596 -2721 -988 C ATOM 3190 N GLU A 438 5.218 -1.234 112.808 1.00 92.57 N ANISOU 3190 N GLU A 438 8219 18099 8855 -2925 -2797 -898 N ATOM 3191 CA GLU A 438 3.983 -1.679 113.447 1.00 94.20 C ANISOU 3191 CA GLU A 438 8210 18485 9095 -3042 -2788 -857 C ATOM 3192 C GLU A 438 3.287 -0.568 114.226 1.00 95.57 C ANISOU 3192 C GLU A 438 8147 18870 9295 -2782 -2769 -725 C ATOM 3193 O GLU A 438 2.099 -0.708 114.537 1.00 98.34 O ANISOU 3193 O GLU A 438 8289 19440 9638 -2831 -2777 -679 O ATOM 3194 CB GLU A 438 4.250 -2.900 114.336 1.00 94.17 C ANISOU 3194 CB GLU A 438 8290 18288 9201 -3303 -2709 -925 C ATOM 3195 CG GLU A 438 5.006 -3.991 113.587 1.00 94.05 C ANISOU 3195 CG GLU A 438 8536 18032 9168 -3535 -2724 -1065 C ATOM 3196 CD GLU A 438 4.384 -5.388 113.752 1.00 95.52 C ANISOU 3196 CD GLU A 438 8731 18179 9381 -3860 -2723 -1125 C ATOM 3197 OE1 GLU A 438 3.215 -5.502 114.160 1.00 95.30 O ANISOU 3197 OE1 GLU A 438 8493 18365 9350 -3924 -2731 -1058 O ATOM 3198 OE2 GLU A 438 5.056 -6.382 113.435 1.00 96.61 O ANISOU 3198 OE2 GLU A 438 9097 18073 9539 -4050 -2715 -1241 O ATOM 3199 N LEU A 439 3.977 0.542 114.512 1.00 88.46 N ANISOU 3199 N LEU A 439 7278 17913 8418 -2501 -2746 -666 N ATOM 3200 CA LEU A 439 3.298 1.722 115.043 1.00 88.82 C ANISOU 3200 CA LEU A 439 7119 18159 8471 -2212 -2744 -545 C ATOM 3201 C LEU A 439 2.595 2.510 113.942 1.00 90.73 C ANISOU 3201 C LEU A 439 7275 18609 8590 -2049 -2850 -489 C ATOM 3202 O LEU A 439 1.561 3.140 114.194 1.00 92.29 O ANISOU 3202 O LEU A 439 7259 19036 8773 -1893 -2868 -406 O ATOM 3203 CB LEU A 439 4.287 2.616 115.796 1.00 86.16 C ANISOU 3203 CB LEU A 439 6859 17670 8209 -1967 -2681 -501 C ATOM 3204 CG LEU A 439 4.771 2.044 117.132 1.00 84.49 C ANISOU 3204 CG LEU A 439 6669 17303 8129 -2074 -2569 -528 C ATOM 3205 CD1 LEU A 439 6.247 2.336 117.370 1.00 81.63 C ANISOU 3205 CD1 LEU A 439 6574 16592 7851 -1959 -2481 -547 C ATOM 3206 CD2 LEU A 439 3.918 2.572 118.284 1.00 85.04 C ANISOU 3206 CD2 LEU A 439 6507 17545 8259 -1921 -2512 -440 C ATOM 3207 N TYR A 440 3.154 2.509 112.731 1.00 90.70 N ANISOU 3207 N TYR A 440 7439 18527 8494 -2076 -2920 -532 N ATOM 3208 CA TYR A 440 2.412 2.989 111.570 1.00 92.91 C ANISOU 3208 CA TYR A 440 7648 19007 8648 -1994 -3029 -492 C ATOM 3209 C TYR A 440 1.238 2.068 111.260 1.00 95.66 C ANISOU 3209 C TYR A 440 7850 19544 8952 -2236 -3070 -529 C ATOM 3210 O TYR A 440 0.090 2.514 111.172 1.00 97.81 O ANISOU 3210 O TYR A 440 7910 20072 9179 -2138 -3116 -458 O ATOM 3211 CB TYR A 440 3.338 3.077 110.358 1.00 92.27 C ANISOU 3211 CB TYR A 440 7796 18789 8473 -1999 -3085 -538 C ATOM 3212 CG TYR A 440 4.095 4.371 110.185 1.00 90.75 C ANISOU 3212 CG TYR A 440 7703 18521 8259 -1693 -3096 -456 C ATOM 3213 CD1 TYR A 440 3.476 5.601 110.357 1.00 91.48 C ANISOU 3213 CD1 TYR A 440 7652 18765 8341 -1393 -3131 -329 C ATOM 3214 CD2 TYR A 440 5.428 4.356 109.813 1.00 88.78 C ANISOU 3214 CD2 TYR A 440 7699 18042 7990 -1707 -3074 -507 C ATOM 3215 CE1 TYR A 440 4.178 6.779 110.176 1.00 90.25 C ANISOU 3215 CE1 TYR A 440 7611 18517 8164 -1118 -3146 -249 C ATOM 3216 CE2 TYR A 440 6.131 5.519 109.634 1.00 87.53 C ANISOU 3216 CE2 TYR A 440 7643 17812 7802 -1443 -3085 -426 C ATOM 3217 CZ TYR A 440 5.508 6.726 109.816 1.00 88.27 C ANISOU 3217 CZ TYR A 440 7605 18041 7891 -1152 -3123 -293 C ATOM 3218 OH TYR A 440 6.242 7.870 109.628 1.00 87.11 O ANISOU 3218 OH TYR A 440 7588 17796 7716 -898 -3136 -208 O ATOM 3219 N GLU A 441 1.517 0.770 111.105 1.00 95.73 N ANISOU 3219 N GLU A 441 7978 19422 8973 -2552 -3052 -641 N ATOM 3220 CA GLU A 441 0.517 -0.174 110.616 1.00103.85 C ANISOU 3220 CA GLU A 441 8914 20601 9943 -2807 -3103 -687 C ATOM 3221 C GLU A 441 -0.643 -0.325 111.590 1.00 99.93 C ANISOU 3221 C GLU A 441 8166 20308 9497 -2844 -3065 -628 C ATOM 3222 O GLU A 441 -1.806 -0.329 111.175 1.00104.38 O ANISOU 3222 O GLU A 441 8548 21129 9984 -2876 -3128 -596 O ATOM 3223 CB GLU A 441 1.169 -1.531 110.352 1.00101.94 C ANISOU 3223 CB GLU A 441 8885 20130 9719 -3123 -3084 -823 C ATOM 3224 CG GLU A 441 2.411 -1.465 109.466 1.00 99.95 C ANISOU 3224 CG GLU A 441 8896 19661 9419 -3096 -3103 -896 C ATOM 3225 CD GLU A 441 3.252 -2.730 109.530 1.00101.15 C ANISOU 3225 CD GLU A 441 9276 19533 9624 -3360 -3053 -1033 C ATOM 3226 OE1 GLU A 441 2.972 -3.676 108.765 1.00103.13 O ANISOU 3226 OE1 GLU A 441 9595 19774 9815 -3589 -3102 -1123 O ATOM 3227 OE2 GLU A 441 4.187 -2.784 110.359 1.00100.51 O ANISOU 3227 OE2 GLU A 441 9309 19236 9645 -3334 -2967 -1052 O ATOM 3228 N THR A 442 -0.354 -0.471 112.876 1.00 98.36 N ANISOU 3228 N THR A 442 7951 20005 9416 -2849 -2962 -615 N ATOM 3229 CA THR A 442 -1.380 -0.618 113.894 1.00 99.66 C ANISOU 3229 CA THR A 442 7887 20355 9626 -2884 -2910 -560 C ATOM 3230 C THR A 442 -1.351 0.586 114.823 1.00 98.38 C ANISOU 3230 C THR A 442 7608 20249 9523 -2557 -2852 -463 C ATOM 3231 O THR A 442 -0.392 1.359 114.841 1.00 96.15 O ANISOU 3231 O THR A 442 7451 19812 9270 -2346 -2838 -447 O ATOM 3232 CB THR A 442 -1.192 -1.910 114.697 1.00 99.29 C ANISOU 3232 CB THR A 442 7913 20149 9665 -3191 -2833 -622 C ATOM 3233 OG1 THR A 442 -0.108 -1.751 115.622 1.00 96.36 O ANISOU 3233 OG1 THR A 442 7667 19538 9406 -3111 -2741 -626 O ATOM 3234 CG2 THR A 442 -0.884 -3.069 113.759 1.00100.04 C ANISOU 3234 CG2 THR A 442 8199 20097 9716 -3487 -2886 -736 C ATOM 3235 N SER A 443 -2.415 0.738 115.602 1.00 99.93 N ANISOU 3235 N SER A 443 7566 20671 9731 -2516 -2815 -401 N ATOM 3236 CA SER A 443 -2.574 1.886 116.481 1.00 99.22 C ANISOU 3236 CA SER A 443 7345 20668 9688 -2195 -2760 -313 C ATOM 3237 C SER A 443 -2.069 1.635 117.898 1.00 97.28 C ANISOU 3237 C SER A 443 7122 20277 9565 -2224 -2635 -313 C ATOM 3238 O SER A 443 -2.334 2.450 118.786 1.00 97.00 O ANISOU 3238 O SER A 443 6957 20329 9569 -1987 -2575 -247 O ATOM 3239 CB SER A 443 -4.045 2.306 116.525 1.00102.19 C ANISOU 3239 CB SER A 443 7442 21389 9996 -2096 -2788 -247 C ATOM 3240 OG SER A 443 -4.876 1.206 116.854 1.00104.13 O ANISOU 3240 OG SER A 443 7572 21764 10229 -2397 -2763 -273 O ATOM 3241 N GLU A 444 -1.352 0.540 118.132 1.00 96.05 N ANISOU 3241 N GLU A 444 7133 19896 9468 -2499 -2593 -386 N ATOM 3242 CA GLU A 444 -0.890 0.212 119.472 1.00 94.38 C ANISOU 3242 CA GLU A 444 6946 19543 9370 -2552 -2477 -383 C ATOM 3243 C GLU A 444 0.399 0.949 119.811 1.00 92.27 C ANISOU 3243 C GLU A 444 6836 19045 9176 -2335 -2436 -380 C ATOM 3244 O GLU A 444 1.230 1.229 118.943 1.00 90.11 O ANISOU 3244 O GLU A 444 6734 18629 8874 -2272 -2493 -414 O ATOM 3245 CB GLU A 444 -0.649 -1.285 119.605 1.00 94.48 C ANISOU 3245 CB GLU A 444 7089 19391 9420 -2936 -2451 -458 C ATOM 3246 CG GLU A 444 -1.884 -2.124 119.589 1.00 97.47 C ANISOU 3246 CG GLU A 444 7376 19942 9718 -3191 -2510 -479 C ATOM 3247 CD GLU A 444 -1.571 -3.490 119.064 1.00 97.32 C ANISOU 3247 CD GLU A 444 7579 19682 9715 -3520 -2527 -577 C ATOM 3248 OE1 GLU A 444 -2.408 -4.407 119.189 1.00 98.76 O ANISOU 3248 OE1 GLU A 444 7742 19870 9912 -3796 -2502 -592 O ATOM 3249 OE2 GLU A 444 -0.443 -3.654 118.552 1.00 95.75 O ANISOU 3249 OE2 GLU A 444 7591 19274 9516 -3494 -2563 -642 O ATOM 3250 N GLU A 445 0.570 1.243 121.096 1.00 94.01 N ANISOU 3250 N GLU A 445 7001 19233 9486 -2230 -2336 -340 N ATOM 3251 CA GLU A 445 1.782 1.883 121.577 1.00 90.03 C ANISOU 3251 CA GLU A 445 6637 18511 9060 -2041 -2287 -336 C ATOM 3252 C GLU A 445 2.852 0.828 121.861 1.00 88.21 C ANISOU 3252 C GLU A 445 6619 17991 8907 -2299 -2241 -413 C ATOM 3253 O GLU A 445 2.605 -0.377 121.789 1.00 88.60 O ANISOU 3253 O GLU A 445 6706 18000 8958 -2612 -2239 -464 O ATOM 3254 CB GLU A 445 1.472 2.738 122.803 1.00 91.69 C ANISOU 3254 CB GLU A 445 6693 18819 9326 -1790 -2202 -262 C ATOM 3255 CG GLU A 445 0.531 2.093 123.801 1.00 95.59 C ANISOU 3255 CG GLU A 445 7021 19453 9846 -1954 -2122 -243 C ATOM 3256 CD GLU A 445 1.267 1.249 124.807 1.00 96.46 C ANISOU 3256 CD GLU A 445 7259 19337 10053 -2188 -2037 -280 C ATOM 3257 OE1 GLU A 445 2.222 1.770 125.415 1.00 95.19 O ANISOU 3257 OE1 GLU A 445 7271 18937 9961 -2116 -2012 -304 O ATOM 3258 OE2 GLU A 445 0.905 0.069 124.975 1.00 98.59 O ANISOU 3258 OE2 GLU A 445 7466 19665 10329 -2447 -1997 -283 O ATOM 3259 N GLN A 446 4.057 1.298 122.198 1.00 82.72 N ANISOU 3259 N GLN A 446 6071 17084 8277 -2161 -2203 -422 N ATOM 3260 CA GLN A 446 5.219 0.416 122.284 1.00 80.91 C ANISOU 3260 CA GLN A 446 6110 16507 8126 -2351 -2147 -498 C ATOM 3261 C GLN A 446 4.991 -0.739 123.249 1.00 81.29 C ANISOU 3261 C GLN A 446 6117 16528 8240 -2640 -2086 -519 C ATOM 3262 O GLN A 446 5.401 -1.872 122.974 1.00 81.28 O ANISOU 3262 O GLN A 446 6282 16343 8258 -2916 -2091 -597 O ATOM 3263 CB GLN A 446 6.457 1.217 122.694 1.00 78.17 C ANISOU 3263 CB GLN A 446 5989 15834 7879 -2081 -2041 -476 C ATOM 3264 CG GLN A 446 6.252 2.161 123.872 1.00 77.53 C ANISOU 3264 CG GLN A 446 5779 15819 7860 -1822 -1959 -390 C ATOM 3265 CD GLN A 446 6.580 1.536 125.216 1.00 76.46 C ANISOU 3265 CD GLN A 446 5680 15528 7841 -1935 -1834 -391 C ATOM 3266 OE1 GLN A 446 7.304 0.545 125.303 1.00 75.69 O ANISOU 3266 OE1 GLN A 446 5777 15176 7806 -2149 -1790 -450 O ATOM 3267 NE2 GLN A 446 6.048 2.123 126.273 1.00 76.80 N ANISOU 3267 NE2 GLN A 446 5540 15727 7911 -1782 -1778 -325 N ATOM 3268 N MET A 447 4.346 -0.476 124.385 1.00 85.66 N ANISOU 3268 N MET A 447 6479 17237 8832 -2571 -2017 -448 N ATOM 3269 CA MET A 447 4.132 -1.537 125.364 1.00 89.93 C ANISOU 3269 CA MET A 447 7013 17718 9439 -2828 -1938 -449 C ATOM 3270 C MET A 447 3.308 -2.662 124.762 1.00 86.28 C ANISOU 3270 C MET A 447 6542 17323 8918 -3133 -1990 -483 C ATOM 3271 O MET A 447 3.681 -3.838 124.835 1.00 86.26 O ANISOU 3271 O MET A 447 6699 17117 8957 -3414 -1977 -538 O ATOM 3272 CB MET A 447 3.443 -0.975 126.607 1.00 92.71 C ANISOU 3272 CB MET A 447 7153 18254 9819 -2676 -1851 -362 C ATOM 3273 CG MET A 447 3.492 -1.891 127.811 1.00 93.48 C ANISOU 3273 CG MET A 447 7271 18253 9996 -2894 -1753 -349 C ATOM 3274 SD MET A 447 5.191 -2.413 128.083 1.00 91.21 S ANISOU 3274 SD MET A 447 7307 17519 9829 -2975 -1698 -410 S ATOM 3275 CE MET A 447 4.998 -4.055 128.807 1.00 95.80 C ANISOU 3275 CE MET A 447 7947 17996 10457 -3397 -1659 -422 C ATOM 3276 N THR A 448 2.197 -2.303 124.130 1.00 86.81 N ANISOU 3276 N THR A 448 6433 17667 8886 -3072 -2054 -452 N ATOM 3277 CA THR A 448 1.314 -3.278 123.507 1.00 89.41 C ANISOU 3277 CA THR A 448 6729 18097 9145 -3345 -2111 -480 C ATOM 3278 C THR A 448 2.035 -4.108 122.452 1.00 89.11 C ANISOU 3278 C THR A 448 6936 17826 9094 -3547 -2179 -583 C ATOM 3279 O THR A 448 1.844 -5.326 122.374 1.00 90.33 O ANISOU 3279 O THR A 448 7179 17889 9254 -3850 -2187 -628 O ATOM 3280 CB THR A 448 0.147 -2.525 122.902 1.00 91.61 C ANISOU 3280 CB THR A 448 6782 18709 9315 -3188 -2176 -431 C ATOM 3281 OG1 THR A 448 -0.489 -1.793 123.954 1.00 90.29 O ANISOU 3281 OG1 THR A 448 6643 18538 9124 -2882 -2222 -423 O ATOM 3282 CG2 THR A 448 -0.851 -3.496 122.310 1.00 92.81 C ANISOU 3282 CG2 THR A 448 6688 19108 9468 -3088 -2104 -346 C ATOM 3283 N ILE A 449 2.871 -3.472 121.635 1.00 87.60 N ANISOU 3283 N ILE A 449 6868 17533 8881 -3381 -2228 -622 N ATOM 3284 CA ILE A 449 3.510 -4.188 120.536 1.00 87.53 C ANISOU 3284 CA ILE A 449 7087 17329 8839 -3549 -2293 -727 C ATOM 3285 C ILE A 449 4.515 -5.201 121.066 1.00 86.05 C ANISOU 3285 C ILE A 449 7135 16807 8754 -3752 -2232 -797 C ATOM 3286 O ILE A 449 4.491 -6.377 120.685 1.00 87.20 O ANISOU 3286 O ILE A 449 7417 16818 8895 -4023 -2257 -870 O ATOM 3287 CB ILE A 449 4.158 -3.190 119.564 1.00 86.34 C ANISOU 3287 CB ILE A 449 7009 17169 8628 -3307 -2355 -743 C ATOM 3288 CG1 ILE A 449 3.174 -2.060 119.287 1.00 87.68 C ANISOU 3288 CG1 ILE A 449 6941 17657 8718 -3061 -2402 -651 C ATOM 3289 CG2 ILE A 449 4.548 -3.875 118.273 1.00 86.94 C ANISOU 3289 CG2 ILE A 449 7280 17117 8635 -3472 -2431 -849 C ATOM 3290 CD1 ILE A 449 3.607 -1.123 118.222 1.00 87.12 C ANISOU 3290 CD1 ILE A 449 6933 17602 8567 -2842 -2478 -652 C ATOM 3291 N LEU A 450 5.396 -4.766 121.973 1.00 83.63 N ANISOU 3291 N LEU A 450 6882 16355 8540 -3619 -2153 -775 N ATOM 3292 CA LEU A 450 6.450 -5.643 122.478 1.00 82.12 C ANISOU 3292 CA LEU A 450 6924 15829 8448 -3783 -2095 -841 C ATOM 3293 C LEU A 450 5.885 -6.901 123.117 1.00 83.69 C ANISOU 3293 C LEU A 450 7135 15970 8692 -4077 -2061 -837 C ATOM 3294 O LEU A 450 6.499 -7.970 123.028 1.00 83.55 O ANISOU 3294 O LEU A 450 7347 15676 8723 -4286 -2055 -917 O ATOM 3295 CB LEU A 450 7.322 -4.885 123.473 1.00 79.52 C ANISOU 3295 CB LEU A 450 6660 15324 8230 -3527 -1974 -785 C ATOM 3296 CG LEU A 450 8.295 -3.885 122.853 1.00 77.58 C ANISOU 3296 CG LEU A 450 6574 14916 7988 -3219 -1952 -793 C ATOM 3297 CD1 LEU A 450 8.645 -2.813 123.860 1.00 75.77 C ANISOU 3297 CD1 LEU A 450 6305 14643 7839 -2919 -1847 -701 C ATOM 3298 CD2 LEU A 450 9.550 -4.594 122.360 1.00 76.32 C ANISOU 3298 CD2 LEU A 450 6741 14381 7876 -3298 -1923 -895 C ATOM 3299 N THR A 451 4.726 -6.795 123.766 1.00 85.30 N ANISOU 3299 N THR A 451 7104 16426 8879 -4090 -2037 -745 N ATOM 3300 CA THR A 451 4.020 -7.986 124.219 1.00 87.31 C ANISOU 3300 CA THR A 451 7356 16669 9147 -4383 -2021 -733 C ATOM 3301 C THR A 451 3.851 -8.987 123.084 1.00 89.10 C ANISOU 3301 C THR A 451 7728 16809 9316 -4617 -2108 -825 C ATOM 3302 O THR A 451 4.190 -10.166 123.224 1.00 89.49 O ANISOU 3302 O THR A 451 7976 16610 9418 -4858 -2099 -878 O ATOM 3303 CB THR A 451 2.654 -7.602 124.781 1.00 89.24 C ANISOU 3303 CB THR A 451 7302 17265 9339 -4344 -2001 -629 C ATOM 3304 OG1 THR A 451 2.830 -6.979 126.060 1.00 90.86 O ANISOU 3304 OG1 THR A 451 7360 17732 9430 -4249 -2089 -629 O ATOM 3305 CG2 THR A 451 1.792 -8.824 124.953 1.00 87.61 C ANISOU 3305 CG2 THR A 451 6956 17149 9183 -4090 -1914 -547 C ATOM 3306 N ARG A 452 3.241 -8.525 121.998 1.00 90.27 N ANISOU 3306 N ARG A 452 7791 17152 9357 -4541 -2196 -847 N ATOM 3307 CA ARG A 452 2.933 -9.363 120.841 1.00 92.48 C ANISOU 3307 CA ARG A 452 8161 17412 9564 -4766 -2282 -924 C ATOM 3308 C ARG A 452 4.084 -10.196 120.285 1.00 91.41 C ANISOU 3308 C ARG A 452 8351 16908 9472 -4881 -2296 -1049 C ATOM 3309 O ARG A 452 3.937 -11.397 120.062 1.00 92.91 O ANISOU 3309 O ARG A 452 8690 16941 9672 -5141 -2319 -1111 O ATOM 3310 CB ARG A 452 2.330 -8.509 119.720 1.00 93.71 C ANISOU 3310 CB ARG A 452 8168 17841 9595 -4628 -2372 -920 C ATOM 3311 CG ARG A 452 2.237 -9.220 118.380 1.00 95.94 C ANISOU 3311 CG ARG A 452 8553 18108 9792 -4841 -2470 -1011 C ATOM 3312 CD ARG A 452 1.022 -8.756 117.592 1.00 96.24 C ANISOU 3312 CD ARG A 452 8532 18316 9719 -4661 -2555 -1027 C ATOM 3313 NE ARG A 452 1.320 -7.593 116.762 1.00 95.95 N ANISOU 3313 NE ARG A 452 8239 18562 9656 -4388 -2541 -915 N ATOM 3314 CZ ARG A 452 0.934 -6.354 117.046 1.00 95.38 C ANISOU 3314 CZ ARG A 452 8110 18616 9516 -4132 -2591 -895 C ATOM 3315 NH1 ARG A 452 1.251 -5.356 116.232 1.00 94.99 N ANISOU 3315 NH1 ARG A 452 8233 18453 9406 -4113 -2656 -977 N ATOM 3316 NH2 ARG A 452 0.231 -6.111 118.144 1.00 95.27 N ANISOU 3316 NH2 ARG A 452 7871 18837 9491 -3879 -2573 -790 N ATOM 3317 N LEU A 453 5.225 -9.557 120.064 1.00 90.97 N ANISOU 3317 N LEU A 453 8413 16715 9436 -4683 -2284 -1092 N ATOM 3318 CA LEU A 453 6.371 -10.240 119.488 1.00 91.53 C ANISOU 3318 CA LEU A 453 8791 16452 9535 -4764 -2294 -1220 C ATOM 3319 C LEU A 453 7.060 -11.141 120.501 1.00 91.89 C ANISOU 3319 C LEU A 453 9018 16185 9709 -4904 -2216 -1238 C ATOM 3320 O LEU A 453 7.858 -11.997 120.108 1.00 92.20 O ANISOU 3320 O LEU A 453 9324 15926 9780 -5017 -2222 -1349 O ATOM 3321 CB LEU A 453 7.360 -9.226 118.902 1.00 90.31 C ANISOU 3321 CB LEU A 453 8706 16257 9351 -4511 -2300 -1257 C ATOM 3322 CG LEU A 453 6.892 -8.342 117.730 1.00 92.03 C ANISOU 3322 CG LEU A 453 8802 16731 9433 -4358 -2386 -1248 C ATOM 3323 CD1 LEU A 453 5.897 -7.255 118.137 1.00 92.60 C ANISOU 3323 CD1 LEU A 453 8564 17147 9471 -4175 -2390 -1113 C ATOM 3324 CD2 LEU A 453 8.083 -7.715 117.008 1.00 89.47 C ANISOU 3324 CD2 LEU A 453 8642 16276 9075 -4179 -2394 -1315 C ATOM 3325 N GLY A 454 6.760 -10.973 121.786 1.00 98.86 N ANISOU 3325 N GLY A 454 9768 17130 10664 -4890 -2142 -1132 N ATOM 3326 CA GLY A 454 7.293 -11.836 122.821 1.00 99.20 C ANISOU 3326 CA GLY A 454 9968 16897 10825 -5029 -2069 -1129 C ATOM 3327 C GLY A 454 8.772 -11.649 123.072 1.00 96.66 C ANISOU 3327 C GLY A 454 9857 16282 10589 -4908 -2015 -1186 C ATOM 3328 O GLY A 454 9.426 -12.539 123.614 1.00 95.75 O ANISOU 3328 O GLY A 454 9950 15865 10566 -5032 -1972 -1220 O ATOM 3329 N TYR A 467 22.098 -20.572 138.128 1.00103.23 N ANISOU 3329 N TYR A 467 13693 12336 13194 -4809 -1051 -709 N ATOM 3330 CA TYR A 467 21.635 -19.513 139.023 1.00102.26 C ANISOU 3330 CA TYR A 467 13307 12505 13044 -4721 -969 -576 C ATOM 3331 C TYR A 467 22.212 -18.187 138.622 1.00 93.11 C ANISOU 3331 C TYR A 467 12029 11472 11875 -4392 -901 -620 C ATOM 3332 O TYR A 467 23.117 -18.134 137.797 1.00 94.21 O ANISOU 3332 O TYR A 467 12307 11451 12040 -4225 -905 -739 O ATOM 3333 CB TYR A 467 22.014 -19.842 140.449 1.00109.11 C ANISOU 3333 CB TYR A 467 14245 13233 13978 -4730 -919 -444 C ATOM 3334 CG TYR A 467 21.550 -21.228 140.745 1.00117.06 C ANISOU 3334 CG TYR A 467 15411 14068 14997 -5060 -997 -406 C ATOM 3335 CD1 TYR A 467 20.258 -21.611 140.425 1.00122.37 C ANISOU 3335 CD1 TYR A 467 15968 14936 15590 -5364 -1063 -390 C ATOM 3336 CD2 TYR A 467 22.424 -22.183 141.216 1.00118.33 C ANISOU 3336 CD2 TYR A 467 15852 13861 15247 -5068 -1015 -398 C ATOM 3337 CE1 TYR A 467 19.820 -22.893 140.651 1.00125.84 C ANISOU 3337 CE1 TYR A 467 16550 15224 16038 -5569 -1118 -348 C ATOM 3338 CE2 TYR A 467 22.000 -23.488 141.431 1.00124.37 C ANISOU 3338 CE2 TYR A 467 16776 14456 16024 -5316 -1084 -361 C ATOM 3339 CZ TYR A 467 20.690 -23.839 141.155 1.00127.39 C ANISOU 3339 CZ TYR A 467 17026 15051 16326 -5536 -1127 -333 C ATOM 3340 OH TYR A 467 20.255 -25.135 141.387 1.00131.46 O ANISOU 3340 OH TYR A 467 17688 15413 16849 -5717 -1180 -288 O ATOM 3341 N ILE A 468 21.688 -17.123 139.230 1.00 76.67 N ANISOU 3341 N ILE A 468 9697 9679 9753 -4301 -837 -523 N ATOM 3342 CA ILE A 468 22.084 -15.781 138.846 1.00 72.48 C ANISOU 3342 CA ILE A 468 9042 9295 9204 -4006 -780 -555 C ATOM 3343 C ILE A 468 23.592 -15.660 138.948 1.00 61.68 C ANISOU 3343 C ILE A 468 7861 7654 7920 -3761 -729 -599 C ATOM 3344 O ILE A 468 24.198 -16.036 139.958 1.00 61.31 O ANISOU 3344 O ILE A 468 7921 7429 7943 -3737 -692 -533 O ATOM 3345 CB ILE A 468 21.375 -14.741 139.722 1.00 62.80 C ANISOU 3345 CB ILE A 468 7549 8376 7936 -3938 -715 -434 C ATOM 3346 CG1 ILE A 468 19.882 -15.066 139.846 1.00 64.95 C ANISOU 3346 CG1 ILE A 468 7637 8911 8129 -4215 -761 -373 C ATOM 3347 CG2 ILE A 468 21.569 -13.374 139.117 1.00 61.07 C ANISOU 3347 CG2 ILE A 468 7198 8324 7680 -3669 -679 -476 C ATOM 3348 CD1 ILE A 468 19.490 -15.774 141.153 1.00 66.10 C ANISOU 3348 CD1 ILE A 468 7784 9038 8294 -4417 -742 -246 C ATOM 3349 N ASP A 469 24.210 -15.173 137.881 1.00 67.84 N ANISOU 3349 N ASP A 469 8682 8406 8687 -3584 -732 -712 N ATOM 3350 CA ASP A 469 25.629 -14.837 137.897 1.00 66.78 C ANISOU 3350 CA ASP A 469 8681 8074 8618 -3327 -675 -756 C ATOM 3351 C ASP A 469 25.729 -13.420 138.434 1.00 63.86 C ANISOU 3351 C ASP A 469 8130 7899 8235 -3108 -594 -680 C ATOM 3352 O ASP A 469 25.481 -12.452 137.711 1.00 62.81 O ANISOU 3352 O ASP A 469 7868 7957 8042 -2996 -590 -712 O ATOM 3353 CB ASP A 469 26.231 -14.955 136.504 1.00 70.60 C ANISOU 3353 CB ASP A 469 9285 8457 9083 -3249 -711 -909 C ATOM 3354 CG ASP A 469 27.738 -14.868 136.516 1.00 72.59 C ANISOU 3354 CG ASP A 469 9696 8482 9403 -3018 -659 -962 C ATOM 3355 OD1 ASP A 469 28.309 -14.478 137.554 1.00 73.19 O ANISOU 3355 OD1 ASP A 469 9759 8514 9535 -2890 -593 -877 O ATOM 3356 OD2 ASP A 469 28.356 -15.184 135.485 1.00 74.73 O ANISOU 3356 OD2 ASP A 469 10098 8631 9667 -2964 -684 -1092 O ATOM 3357 N GLU A 470 26.094 -13.298 139.713 1.00 58.69 N ANISOU 3357 N GLU A 470 7474 7189 7634 -3048 -534 -580 N ATOM 3358 CA GLU A 470 26.123 -11.990 140.355 1.00 57.36 C ANISOU 3358 CA GLU A 470 7140 7201 7452 -2856 -459 -505 C ATOM 3359 C GLU A 470 27.126 -11.061 139.685 1.00 52.65 C ANISOU 3359 C GLU A 470 6575 6569 6862 -2597 -423 -576 C ATOM 3360 O GLU A 470 26.949 -9.838 139.705 1.00 51.56 O ANISOU 3360 O GLU A 470 6288 6617 6685 -2447 -386 -547 O ATOM 3361 CB GLU A 470 26.437 -12.144 141.848 1.00 54.03 C ANISOU 3361 CB GLU A 470 6742 6702 7086 -2848 -404 -394 C ATOM 3362 CG GLU A 470 27.847 -12.614 142.158 1.00 53.21 C ANISOU 3362 CG GLU A 470 6850 6297 7070 -2734 -382 -419 C ATOM 3363 CD GLU A 470 27.983 -14.111 142.203 1.00 54.84 C ANISOU 3363 CD GLU A 470 7254 6258 7323 -2921 -440 -436 C ATOM 3364 OE1 GLU A 470 26.961 -14.814 142.044 1.00 56.65 O ANISOU 3364 OE1 GLU A 470 7461 6547 7518 -3163 -497 -422 O ATOM 3365 OE2 GLU A 470 29.124 -14.581 142.394 1.00 54.40 O ANISOU 3365 OE2 GLU A 470 7379 5951 7339 -2823 -431 -463 O ATOM 3366 N LYS A 471 28.154 -11.618 139.051 1.00 52.49 N ANISOU 3366 N LYS A 471 6745 6316 6883 -2544 -438 -672 N ATOM 3367 CA LYS A 471 29.194 -10.795 138.446 1.00 53.99 C ANISOU 3367 CA LYS A 471 6970 6469 7076 -2310 -399 -736 C ATOM 3368 C LYS A 471 28.759 -10.250 137.091 1.00 54.78 C ANISOU 3368 C LYS A 471 6996 6726 7093 -2292 -436 -813 C ATOM 3369 O LYS A 471 28.870 -9.047 136.833 1.00 53.59 O ANISOU 3369 O LYS A 471 6744 6714 6905 -2129 -404 -801 O ATOM 3370 CB LYS A 471 30.478 -11.611 138.334 1.00 54.54 C ANISOU 3370 CB LYS A 471 7259 6249 7217 -2252 -395 -808 C ATOM 3371 CG LYS A 471 30.650 -12.513 139.532 1.00 56.25 C ANISOU 3371 CG LYS A 471 7570 6296 7506 -2339 -390 -735 C ATOM 3372 CD LYS A 471 32.034 -13.087 139.654 1.00 57.74 C ANISOU 3372 CD LYS A 471 7951 6215 7771 -2222 -374 -785 C ATOM 3373 CE LYS A 471 32.213 -13.696 141.037 1.00 61.23 C ANISOU 3373 CE LYS A 471 8458 6527 8281 -2272 -361 -680 C ATOM 3374 NZ LYS A 471 33.388 -14.605 141.117 1.00 64.57 N ANISOU 3374 NZ LYS A 471 9093 6660 8779 -2203 -371 -732 N ATOM 3375 N LEU A 472 28.257 -11.114 136.211 1.00 65.95 N ANISOU 3375 N LEU A 472 8468 8117 8472 -2461 -509 -892 N ATOM 3376 CA LEU A 472 27.659 -10.622 134.973 1.00 67.28 C ANISOU 3376 CA LEU A 472 8547 8468 8548 -2469 -554 -954 C ATOM 3377 C LEU A 472 26.480 -9.710 135.280 1.00 62.71 C ANISOU 3377 C LEU A 472 7735 8183 7910 -2482 -555 -861 C ATOM 3378 O LEU A 472 26.240 -8.723 134.574 1.00 60.67 O ANISOU 3378 O LEU A 472 7369 8098 7585 -2373 -561 -872 O ATOM 3379 CB LEU A 472 27.233 -11.800 134.101 1.00 73.84 C ANISOU 3379 CB LEU A 472 9480 9227 9350 -2677 -638 -1052 C ATOM 3380 CG LEU A 472 27.348 -11.629 132.585 1.00 78.23 C ANISOU 3380 CG LEU A 472 10065 9831 9827 -2642 -679 -1173 C ATOM 3381 CD1 LEU A 472 27.145 -12.981 131.897 1.00 82.07 C ANISOU 3381 CD1 LEU A 472 10702 10178 10302 -2845 -758 -1283 C ATOM 3382 CD2 LEU A 472 26.371 -10.583 132.023 1.00 79.25 C ANISOU 3382 CD2 LEU A 472 9985 10267 9858 -2624 -704 -1139 C ATOM 3383 N LEU A 473 25.747 -10.020 136.349 1.00 55.42 N ANISOU 3383 N LEU A 473 6729 7320 7006 -2607 -549 -766 N ATOM 3384 CA LEU A 473 24.663 -9.156 136.791 1.00 53.88 C ANISOU 3384 CA LEU A 473 6302 7411 6757 -2600 -540 -676 C ATOM 3385 C LEU A 473 25.159 -7.746 137.084 1.00 52.00 C ANISOU 3385 C LEU A 473 5990 7248 6521 -2336 -473 -635 C ATOM 3386 O LEU A 473 24.460 -6.765 136.803 1.00 51.95 O ANISOU 3386 O LEU A 473 5817 7472 6448 -2257 -481 -609 O ATOM 3387 CB LEU A 473 24.001 -9.761 138.023 1.00 54.80 C ANISOU 3387 CB LEU A 473 6362 7559 6899 -2766 -528 -580 C ATOM 3388 CG LEU A 473 22.827 -9.014 138.640 1.00 55.18 C ANISOU 3388 CG LEU A 473 6162 7913 6891 -2776 -512 -485 C ATOM 3389 CD1 LEU A 473 21.760 -8.709 137.596 1.00 58.67 C ANISOU 3389 CD1 LEU A 473 6451 8604 7238 -2839 -581 -521 C ATOM 3390 CD2 LEU A 473 22.248 -9.834 139.783 1.00 56.71 C ANISOU 3390 CD2 LEU A 473 6326 8116 7104 -2979 -503 -398 C ATOM 3391 N THR A 474 26.364 -7.622 137.644 1.00 50.56 N ANISOU 3391 N THR A 474 5931 6870 6411 -2197 -411 -630 N ATOM 3392 CA THR A 474 26.935 -6.331 138.003 1.00 48.84 C ANISOU 3392 CA THR A 474 5665 6693 6198 -1961 -348 -591 C ATOM 3393 C THR A 474 28.184 -6.012 137.193 1.00 47.70 C ANISOU 3393 C THR A 474 5656 6400 6068 -1809 -333 -668 C ATOM 3394 O THR A 474 29.045 -5.262 137.646 1.00 46.24 O ANISOU 3394 O THR A 474 5498 6156 5916 -1637 -274 -643 O ATOM 3395 CB THR A 474 27.272 -6.264 139.495 1.00 48.09 C ANISOU 3395 CB THR A 474 5570 6535 6165 -1917 -282 -504 C ATOM 3396 OG1 THR A 474 28.050 -7.404 139.866 1.00 48.26 O ANISOU 3396 OG1 THR A 474 5765 6310 6259 -1998 -279 -522 O ATOM 3397 CG2 THR A 474 26.018 -6.195 140.342 1.00 49.03 C ANISOU 3397 CG2 THR A 474 5514 6863 6251 -2019 -281 -416 C ATOM 3398 N GLU A 475 28.306 -6.576 135.998 1.00 51.93 N ANISOU 3398 N GLU A 475 6275 6882 6573 -1876 -383 -765 N ATOM 3399 CA GLU A 475 29.486 -6.313 135.182 1.00 56.28 C ANISOU 3399 CA GLU A 475 6947 7312 7125 -1740 -365 -843 C ATOM 3400 C GLU A 475 29.557 -4.851 134.752 1.00 56.12 C ANISOU 3400 C GLU A 475 6835 7437 7049 -1563 -345 -818 C ATOM 3401 O GLU A 475 30.617 -4.226 134.807 1.00 55.10 O ANISOU 3401 O GLU A 475 6767 7225 6943 -1406 -295 -819 O ATOM 3402 CB GLU A 475 29.475 -7.222 133.960 1.00 61.55 C ANISOU 3402 CB GLU A 475 7714 7918 7756 -1856 -426 -959 C ATOM 3403 CG GLU A 475 30.693 -7.105 133.081 1.00 63.39 C ANISOU 3403 CG GLU A 475 8073 8031 7981 -1731 -405 -1050 C ATOM 3404 CD GLU A 475 31.292 -8.454 132.785 1.00 66.43 C ANISOU 3404 CD GLU A 475 8636 8200 8406 -1817 -424 -1151 C ATOM 3405 OE1 GLU A 475 30.528 -9.441 132.763 1.00 67.69 O ANISOU 3405 OE1 GLU A 475 8819 8335 8565 -2006 -482 -1173 O ATOM 3406 OE2 GLU A 475 32.524 -8.528 132.596 1.00 69.94 O ANISOU 3406 OE2 GLU A 475 9196 8499 8881 -1697 -383 -1209 O ATOM 3407 N GLU A 476 28.448 -4.293 134.303 1.00 64.14 N ANISOU 3407 N GLU A 476 7709 8672 7990 -1588 -390 -793 N ATOM 3408 CA GLU A 476 28.450 -2.995 133.647 1.00 66.74 C ANISOU 3408 CA GLU A 476 7973 9130 8254 -1433 -392 -779 C ATOM 3409 C GLU A 476 27.867 -1.909 134.536 1.00 66.99 C ANISOU 3409 C GLU A 476 7862 9308 8284 -1324 -366 -677 C ATOM 3410 O GLU A 476 27.409 -0.875 134.049 1.00 63.73 O ANISOU 3410 O GLU A 476 7360 9049 7807 -1223 -389 -651 O ATOM 3411 CB GLU A 476 27.670 -3.070 132.342 1.00 75.68 C ANISOU 3411 CB GLU A 476 9056 10408 9291 -1512 -471 -831 C ATOM 3412 CG GLU A 476 28.501 -3.237 131.083 1.00 82.19 C ANISOU 3412 CG GLU A 476 10010 11145 10075 -1489 -485 -928 C ATOM 3413 CD GLU A 476 27.661 -3.746 129.937 1.00 88.75 C ANISOU 3413 CD GLU A 476 10811 12093 10818 -1628 -570 -993 C ATOM 3414 OE1 GLU A 476 28.190 -4.424 129.037 1.00 91.64 O ANISOU 3414 OE1 GLU A 476 11298 12362 11159 -1683 -589 -1096 O ATOM 3415 OE2 GLU A 476 26.446 -3.488 129.966 1.00 93.20 O ANISOU 3415 OE2 GLU A 476 11222 12855 11334 -1684 -619 -944 O ATOM 3416 N ILE A 477 27.861 -2.133 135.834 1.00 62.30 N ANISOU 3416 N ILE A 477 7250 8668 7755 -1340 -320 -620 N ATOM 3417 CA ILE A 477 27.340 -1.149 136.771 1.00 60.07 C ANISOU 3417 CA ILE A 477 6838 8519 7469 -1232 -289 -533 C ATOM 3418 C ILE A 477 28.519 -0.404 137.385 1.00 52.51 C ANISOU 3418 C ILE A 477 5966 7425 6562 -1062 -221 -510 C ATOM 3419 O ILE A 477 29.462 -1.018 137.899 1.00 52.53 O ANISOU 3419 O ILE A 477 6085 7243 6632 -1082 -181 -523 O ATOM 3420 CB ILE A 477 26.468 -1.821 137.841 1.00 57.50 C ANISOU 3420 CB ILE A 477 6417 8267 7165 -1368 -282 -480 C ATOM 3421 CG1 ILE A 477 26.059 -0.832 138.930 1.00 55.99 C ANISOU 3421 CG1 ILE A 477 6102 8201 6971 -1241 -237 -399 C ATOM 3422 CG2 ILE A 477 27.203 -2.951 138.453 1.00 55.66 C ANISOU 3422 CG2 ILE A 477 6319 7822 7009 -1472 -254 -493 C ATOM 3423 CD1 ILE A 477 25.306 -1.492 140.011 1.00 56.96 C ANISOU 3423 CD1 ILE A 477 6136 8399 7108 -1374 -220 -345 C ATOM 3424 N TYR A 478 28.493 0.921 137.289 1.00 51.29 N ANISOU 3424 N TYR A 478 5760 7356 6371 -895 -213 -476 N ATOM 3425 CA TYR A 478 29.642 1.704 137.720 1.00 49.63 C ANISOU 3425 CA TYR A 478 5640 7019 6199 -744 -157 -460 C ATOM 3426 C TYR A 478 29.322 2.456 139.008 1.00 53.73 C ANISOU 3426 C TYR A 478 6078 7601 6736 -648 -115 -388 C ATOM 3427 O TYR A 478 29.384 3.687 139.078 1.00 55.52 O ANISOU 3427 O TYR A 478 6286 7871 6939 -492 -106 -358 O ATOM 3428 CB TYR A 478 30.090 2.622 136.591 1.00 50.35 C ANISOU 3428 CB TYR A 478 5777 7116 6236 -633 -178 -482 C ATOM 3429 CG TYR A 478 30.446 1.821 135.367 1.00 53.31 C ANISOU 3429 CG TYR A 478 6233 7435 6586 -730 -212 -561 C ATOM 3430 CD1 TYR A 478 31.474 0.892 135.405 1.00 54.35 C ANISOU 3430 CD1 TYR A 478 6490 7387 6773 -788 -182 -615 C ATOM 3431 CD2 TYR A 478 29.742 1.971 134.178 1.00 54.74 C ANISOU 3431 CD2 TYR A 478 6366 7747 6684 -759 -278 -586 C ATOM 3432 CE1 TYR A 478 31.798 0.147 134.290 1.00 55.17 C ANISOU 3432 CE1 TYR A 478 6673 7440 6850 -867 -211 -699 C ATOM 3433 CE2 TYR A 478 30.062 1.234 133.063 1.00 55.12 C ANISOU 3433 CE2 TYR A 478 6493 7751 6701 -848 -309 -666 C ATOM 3434 CZ TYR A 478 31.088 0.323 133.123 1.00 55.06 C ANISOU 3434 CZ TYR A 478 6613 7560 6749 -900 -273 -726 C ATOM 3435 OH TYR A 478 31.406 -0.415 132.008 1.00 56.96 O ANISOU 3435 OH TYR A 478 6934 7756 6952 -978 -301 -818 O ATOM 3436 N ASN A 479 28.945 1.695 140.030 1.00 50.19 N ANISOU 3436 N ASN A 479 5587 7158 6324 -746 -92 -360 N ATOM 3437 CA ASN A 479 28.666 2.237 141.355 1.00 41.34 C ANISOU 3437 CA ASN A 479 4393 6098 5218 -673 -46 -298 C ATOM 3438 C ASN A 479 29.055 1.146 142.323 1.00 41.27 C ANISOU 3438 C ASN A 479 4439 5971 5271 -792 -10 -282 C ATOM 3439 O ASN A 479 28.267 0.237 142.606 1.00 42.34 O ANISOU 3439 O ASN A 479 4512 6173 5403 -947 -26 -266 O ATOM 3440 CB ASN A 479 27.199 2.631 141.514 1.00 42.52 C ANISOU 3440 CB ASN A 479 4358 6492 5305 -671 -71 -263 C ATOM 3441 CG ASN A 479 26.898 3.237 142.861 1.00 42.38 C ANISOU 3441 CG ASN A 479 4261 6550 5290 -581 -19 -208 C ATOM 3442 OD1 ASN A 479 27.433 2.805 143.875 1.00 41.87 O ANISOU 3442 OD1 ASN A 479 4250 6385 5274 -616 31 -186 O ATOM 3443 ND2 ASN A 479 26.027 4.240 142.883 1.00 42.94 N ANISOU 3443 ND2 ASN A 479 4205 6806 5305 -458 -31 -188 N ATOM 3444 N PRO A 480 30.282 1.191 142.848 1.00 40.12 N ANISOU 3444 N PRO A 480 4413 5649 5180 -728 34 -282 N ATOM 3445 CA PRO A 480 30.789 0.048 143.617 1.00 40.12 C ANISOU 3445 CA PRO A 480 4492 5510 5243 -838 57 -270 C ATOM 3446 C PRO A 480 29.961 -0.281 144.839 1.00 44.95 C ANISOU 3446 C PRO A 480 5007 6221 5850 -916 79 -204 C ATOM 3447 O PRO A 480 29.941 -1.445 145.254 1.00 51.12 O ANISOU 3447 O PRO A 480 5830 6928 6665 -1064 75 -188 O ATOM 3448 CB PRO A 480 32.204 0.492 143.989 1.00 38.75 C ANISOU 3448 CB PRO A 480 4434 5174 5115 -714 100 -275 C ATOM 3449 CG PRO A 480 32.133 1.965 143.985 1.00 38.15 C ANISOU 3449 CG PRO A 480 4306 5190 4999 -553 113 -260 C ATOM 3450 CD PRO A 480 31.239 2.308 142.845 1.00 38.89 C ANISOU 3450 CD PRO A 480 4324 5420 5031 -556 62 -285 C ATOM 3451 N VAL A 481 29.253 0.688 145.418 1.00 43.24 N ANISOU 3451 N VAL A 481 4664 6174 5590 -823 100 -164 N ATOM 3452 CA VAL A 481 28.421 0.388 146.579 1.00 43.57 C ANISOU 3452 CA VAL A 481 4600 6340 5615 -899 127 -102 C ATOM 3453 C VAL A 481 27.174 -0.370 146.157 1.00 44.90 C ANISOU 3453 C VAL A 481 4657 6660 5743 -1072 84 -96 C ATOM 3454 O VAL A 481 26.814 -1.388 146.758 1.00 48.51 O ANISOU 3454 O VAL A 481 5104 7118 6211 -1241 87 -58 O ATOM 3455 CB VAL A 481 28.057 1.672 147.343 1.00 41.45 C ANISOU 3455 CB VAL A 481 4230 6213 5305 -733 167 -72 C ATOM 3456 CG1 VAL A 481 27.249 1.322 148.585 1.00 42.37 C ANISOU 3456 CG1 VAL A 481 4234 6469 5395 -813 203 -10 C ATOM 3457 CG2 VAL A 481 29.301 2.439 147.725 1.00 39.99 C ANISOU 3457 CG2 VAL A 481 4163 5875 5156 -578 203 -80 C ATOM 3458 N VAL A 482 26.482 0.123 145.130 1.00 52.25 N ANISOU 3458 N VAL A 482 5503 7727 6624 -1039 39 -129 N ATOM 3459 CA VAL A 482 25.331 -0.610 144.615 1.00 51.00 C ANISOU 3459 CA VAL A 482 5237 7718 6422 -1213 -11 -131 C ATOM 3460 C VAL A 482 25.767 -1.961 144.074 1.00 51.50 C ANISOU 3460 C VAL A 482 5434 7603 6529 -1397 -48 -166 C ATOM 3461 O VAL A 482 25.130 -2.986 144.338 1.00 54.21 O ANISOU 3461 O VAL A 482 5745 7983 6868 -1598 -66 -141 O ATOM 3462 CB VAL A 482 24.594 0.213 143.544 1.00 51.94 C ANISOU 3462 CB VAL A 482 5247 8012 6476 -1127 -60 -162 C ATOM 3463 CG1 VAL A 482 23.621 -0.659 142.806 1.00 56.77 C ANISOU 3463 CG1 VAL A 482 5779 8743 7048 -1323 -123 -178 C ATOM 3464 CG2 VAL A 482 23.844 1.333 144.183 1.00 51.62 C ANISOU 3464 CG2 VAL A 482 5047 8180 6385 -976 -32 -123 C ATOM 3465 N ALA A 483 26.869 -1.989 143.326 1.00 48.25 N ANISOU 3465 N ALA A 483 5180 6997 6158 -1334 -58 -224 N ATOM 3466 CA ALA A 483 27.334 -3.244 142.751 1.00 48.39 C ANISOU 3466 CA ALA A 483 5336 6835 6214 -1483 -94 -273 C ATOM 3467 C ALA A 483 27.651 -4.263 143.834 1.00 47.40 C ANISOU 3467 C ALA A 483 5290 6574 6146 -1601 -68 -227 C ATOM 3468 O ALA A 483 27.399 -5.462 143.661 1.00 49.76 O ANISOU 3468 O ALA A 483 5647 6801 6460 -1791 -107 -238 O ATOM 3469 CB ALA A 483 28.555 -2.999 141.867 1.00 45.32 C ANISOU 3469 CB ALA A 483 5093 6275 5853 -1366 -96 -344 C ATOM 3470 N LYS A 484 28.183 -3.804 144.969 1.00 46.83 N ANISOU 3470 N LYS A 484 5227 6464 6102 -1496 -8 -173 N ATOM 3471 CA LYS A 484 28.527 -4.730 146.040 1.00 45.94 C ANISOU 3471 CA LYS A 484 5194 6224 6038 -1598 14 -119 C ATOM 3472 C LYS A 484 27.277 -5.301 146.696 1.00 46.31 C ANISOU 3472 C LYS A 484 5121 6430 6045 -1784 6 -51 C ATOM 3473 O LYS A 484 27.106 -6.521 146.757 1.00 47.44 O ANISOU 3473 O LYS A 484 5335 6481 6210 -1978 -27 -37 O ATOM 3474 CB LYS A 484 29.413 -4.039 147.077 1.00 44.75 C ANISOU 3474 CB LYS A 484 5077 6008 5916 -1437 77 -80 C ATOM 3475 CG LYS A 484 29.740 -4.910 148.272 1.00 43.72 C ANISOU 3475 CG LYS A 484 5020 5765 5827 -1530 99 -12 C ATOM 3476 CD LYS A 484 30.646 -4.197 149.258 1.00 42.43 C ANISOU 3476 CD LYS A 484 4889 5547 5685 -1369 156 21 C ATOM 3477 CE LYS A 484 32.027 -3.990 148.684 1.00 41.17 C ANISOU 3477 CE LYS A 484 4866 5199 5579 -1235 155 -42 C ATOM 3478 NZ LYS A 484 32.972 -3.485 149.700 1.00 40.11 N ANISOU 3478 NZ LYS A 484 4774 4996 5468 -1110 203 -6 N ATOM 3479 N SER A 485 26.384 -4.439 147.186 1.00 50.06 N ANISOU 3479 N SER A 485 5414 7149 6459 -1731 35 -8 N ATOM 3480 CA SER A 485 25.223 -4.944 147.913 1.00 54.18 C ANISOU 3480 CA SER A 485 5803 7849 6933 -1906 39 64 C ATOM 3481 C SER A 485 24.382 -5.861 147.041 1.00 59.77 C ANISOU 3481 C SER A 485 6484 8608 7617 -2123 -30 40 C ATOM 3482 O SER A 485 23.844 -6.863 147.526 1.00 61.17 O ANISOU 3482 O SER A 485 6655 8798 7788 -2341 -44 93 O ATOM 3483 CB SER A 485 24.375 -3.794 148.448 1.00 55.46 C ANISOU 3483 CB SER A 485 5760 8288 7024 -1787 81 97 C ATOM 3484 OG SER A 485 24.230 -2.778 147.486 1.00 57.65 O ANISOU 3484 OG SER A 485 5976 8655 7273 -1626 60 37 O ATOM 3485 N VAL A 486 24.259 -5.539 145.752 1.00 55.50 N ANISOU 3485 N VAL A 486 5931 8100 7058 -2076 -78 -37 N ATOM 3486 CA VAL A 486 23.593 -6.453 144.833 1.00 51.14 C ANISOU 3486 CA VAL A 486 5378 7569 6483 -2284 -152 -74 C ATOM 3487 C VAL A 486 24.307 -7.794 144.828 1.00 51.50 C ANISOU 3487 C VAL A 486 5636 7334 6596 -2437 -180 -90 C ATOM 3488 O VAL A 486 23.688 -8.846 145.011 1.00 53.11 O ANISOU 3488 O VAL A 486 5848 7538 6793 -2675 -215 -58 O ATOM 3489 CB VAL A 486 23.517 -5.849 143.419 1.00 50.87 C ANISOU 3489 CB VAL A 486 5318 7593 6415 -2188 -199 -160 C ATOM 3490 CG1 VAL A 486 23.111 -6.920 142.416 1.00 52.30 C ANISOU 3490 CG1 VAL A 486 5554 7735 6584 -2402 -280 -216 C ATOM 3491 CG2 VAL A 486 22.516 -4.699 143.379 1.00 51.13 C ANISOU 3491 CG2 VAL A 486 5126 7932 6371 -2078 -192 -137 C ATOM 3492 N ARG A 487 25.626 -7.775 144.641 1.00 50.12 N ANISOU 3492 N ARG A 487 5638 6916 6488 -2300 -165 -137 N ATOM 3493 CA ARG A 487 26.390 -9.017 144.649 1.00 50.49 C ANISOU 3493 CA ARG A 487 5897 6684 6604 -2409 -191 -157 C ATOM 3494 C ARG A 487 26.194 -9.791 145.946 1.00 52.10 C ANISOU 3494 C ARG A 487 6125 6843 6829 -2556 -173 -55 C ATOM 3495 O ARG A 487 26.182 -11.026 145.935 1.00 52.94 O ANISOU 3495 O ARG A 487 6359 6791 6965 -2745 -219 -51 O ATOM 3496 CB ARG A 487 27.868 -8.710 144.420 1.00 49.66 C ANISOU 3496 CB ARG A 487 5944 6364 6560 -2205 -165 -213 C ATOM 3497 CG ARG A 487 28.480 -9.468 143.266 1.00 50.06 C ANISOU 3497 CG ARG A 487 6160 6219 6640 -2237 -217 -320 C ATOM 3498 CD ARG A 487 29.936 -9.105 143.025 1.00 48.39 C ANISOU 3498 CD ARG A 487 6076 5832 6480 -2029 -185 -376 C ATOM 3499 NE ARG A 487 30.074 -7.792 142.415 1.00 47.70 N ANISOU 3499 NE ARG A 487 5894 5879 6350 -1849 -160 -409 N ATOM 3500 CZ ARG A 487 30.448 -6.704 143.072 1.00 47.12 C ANISOU 3500 CZ ARG A 487 5755 5871 6278 -1681 -102 -361 C ATOM 3501 NH1 ARG A 487 30.727 -6.775 144.360 1.00 48.31 N ANISOU 3501 NH1 ARG A 487 5915 5974 6464 -1666 -60 -283 N ATOM 3502 NH2 ARG A 487 30.546 -5.545 142.445 1.00 46.90 N ANISOU 3502 NH2 ARG A 487 5660 5950 6210 -1531 -89 -390 N ATOM 3503 N GLN A 488 26.024 -9.087 147.069 1.00 54.35 N ANISOU 3503 N GLN A 488 6296 7263 7094 -2475 -109 28 N ATOM 3504 CA GLN A 488 25.798 -9.764 148.340 1.00 56.01 C ANISOU 3504 CA GLN A 488 6517 7457 7309 -2617 -87 134 C ATOM 3505 C GLN A 488 24.392 -10.343 148.412 1.00 54.77 C ANISOU 3505 C GLN A 488 6230 7494 7086 -2873 -119 185 C ATOM 3506 O GLN A 488 24.197 -11.447 148.929 1.00 55.34 O ANISOU 3506 O GLN A 488 6383 7472 7172 -3086 -143 247 O ATOM 3507 CB GLN A 488 26.026 -8.800 149.505 1.00 59.05 C ANISOU 3507 CB GLN A 488 6814 7946 7679 -2452 -7 200 C ATOM 3508 CG GLN A 488 27.342 -8.043 149.479 1.00 59.73 C ANISOU 3508 CG GLN A 488 6997 7884 7816 -2198 27 155 C ATOM 3509 CD GLN A 488 28.541 -8.911 149.807 1.00 62.64 C ANISOU 3509 CD GLN A 488 7582 7953 8266 -2202 17 161 C ATOM 3510 OE1 GLN A 488 28.553 -9.625 150.808 1.00 64.39 O ANISOU 3510 OE1 GLN A 488 7856 8110 8500 -2312 25 246 O ATOM 3511 NE2 GLN A 488 29.565 -8.847 148.964 1.00 65.27 N ANISOU 3511 NE2 GLN A 488 8039 8110 8649 -2075 0 72 N ATOM 3512 N ALA A 489 23.399 -9.608 147.913 1.00 54.09 N ANISOU 3512 N ALA A 489 5940 7684 6927 -2857 -122 165 N ATOM 3513 CA ALA A 489 22.020 -10.081 147.988 1.00 56.15 C ANISOU 3513 CA ALA A 489 6045 8172 7117 -3097 -150 214 C ATOM 3514 C ALA A 489 21.791 -11.325 147.137 1.00 57.68 C ANISOU 3514 C ALA A 489 6360 8231 7327 -3341 -238 172 C ATOM 3515 O ALA A 489 20.962 -12.169 147.491 1.00 59.60 O ANISOU 3515 O ALA A 489 6564 8545 7536 -3604 -265 236 O ATOM 3516 CB ALA A 489 21.057 -8.973 147.565 1.00 56.23 C ANISOU 3516 CB ALA A 489 5807 8512 7046 -2998 -140 192 C ATOM 3517 N ILE A 490 22.513 -11.464 146.030 1.00 57.00 N ANISOU 3517 N ILE A 490 6422 7951 7285 -3266 -283 66 N ATOM 3518 CA ILE A 490 22.330 -12.618 145.159 1.00 58.52 C ANISOU 3518 CA ILE A 490 6742 8004 7487 -3483 -369 9 C ATOM 3519 C ILE A 490 23.129 -13.819 145.653 1.00 58.97 C ANISOU 3519 C ILE A 490 7050 7733 7624 -3588 -388 32 C ATOM 3520 O ILE A 490 22.657 -14.956 145.570 1.00 60.89 O ANISOU 3520 O ILE A 490 7376 7895 7865 -3850 -449 47 O ATOM 3521 CB ILE A 490 22.679 -12.256 143.696 1.00 57.82 C ANISOU 3521 CB ILE A 490 6697 7875 7398 -3361 -411 -123 C ATOM 3522 CG1 ILE A 490 21.435 -11.804 142.932 1.00 58.84 C ANISOU 3522 CG1 ILE A 490 6611 8312 7434 -3434 -451 -146 C ATOM 3523 CG2 ILE A 490 23.261 -13.444 142.959 1.00 58.61 C ANISOU 3523 CG2 ILE A 490 7039 7681 7548 -3479 -480 -206 C ATOM 3524 CD1 ILE A 490 20.704 -10.664 143.545 1.00 58.46 C ANISOU 3524 CD1 ILE A 490 6309 8577 7325 -3321 -394 -76 C ATOM 3525 N LYS A 491 24.338 -13.604 146.181 1.00 57.38 N ANISOU 3525 N LYS A 491 6976 7335 7490 -3392 -340 38 N ATOM 3526 CA LYS A 491 25.074 -14.719 146.769 1.00 57.93 C ANISOU 3526 CA LYS A 491 7275 7105 7633 -3477 -359 74 C ATOM 3527 C LYS A 491 24.274 -15.376 147.884 1.00 59.59 C ANISOU 3527 C LYS A 491 7442 7387 7814 -3717 -357 210 C ATOM 3528 O LYS A 491 24.389 -16.588 148.102 1.00 61.05 O ANISOU 3528 O LYS A 491 7807 7355 8035 -3904 -408 242 O ATOM 3529 CB LYS A 491 26.434 -14.251 147.295 1.00 56.44 C ANISOU 3529 CB LYS A 491 7188 6748 7510 -3217 -302 74 C ATOM 3530 CG LYS A 491 27.485 -14.048 146.212 1.00 55.36 C ANISOU 3530 CG LYS A 491 7174 6442 7420 -3025 -317 -58 C ATOM 3531 CD LYS A 491 28.888 -13.923 146.787 1.00 54.65 C ANISOU 3531 CD LYS A 491 7217 6145 7401 -2819 -275 -52 C ATOM 3532 CE LYS A 491 29.933 -13.853 145.677 1.00 54.90 C ANISOU 3532 CE LYS A 491 7373 6014 7474 -2650 -290 -186 C ATOM 3533 NZ LYS A 491 31.331 -13.953 146.183 1.00 54.18 N ANISOU 3533 NZ LYS A 491 7425 5705 7456 -2474 -261 -185 N ATOM 3534 N ILE A 492 23.435 -14.599 148.571 1.00 59.56 N ANISOU 3534 N ILE A 492 7202 7690 7737 -3719 -301 289 N ATOM 3535 CA ILE A 492 22.632 -15.132 149.667 1.00 61.19 C ANISOU 3535 CA ILE A 492 7340 8011 7899 -3946 -289 423 C ATOM 3536 C ILE A 492 21.508 -16.019 149.138 1.00 63.61 C ANISOU 3536 C ILE A 492 7613 8398 8158 -4267 -363 428 C ATOM 3537 O ILE A 492 21.312 -17.146 149.611 1.00 65.37 O ANISOU 3537 O ILE A 492 7958 8491 8391 -4516 -403 503 O ATOM 3538 CB ILE A 492 22.088 -13.980 150.529 1.00 60.49 C ANISOU 3538 CB ILE A 492 6999 8245 7740 -3830 -201 492 C ATOM 3539 CG1 ILE A 492 23.213 -13.382 151.378 1.00 58.56 C ANISOU 3539 CG1 ILE A 492 6827 7881 7542 -3582 -132 517 C ATOM 3540 CG2 ILE A 492 20.918 -14.455 151.380 1.00 62.58 C ANISOU 3540 CG2 ILE A 492 7126 8726 7926 -4099 -191 614 C ATOM 3541 CD1 ILE A 492 22.806 -12.183 152.186 1.00 57.77 C ANISOU 3541 CD1 ILE A 492 6505 8070 7375 -3435 -47 564 C ATOM 3542 N VAL A 493 20.748 -15.526 148.153 1.00 67.17 N ANISOU 3542 N VAL A 493 7902 9067 8554 -4273 -388 353 N ATOM 3543 CA VAL A 493 19.591 -16.287 147.685 1.00 67.95 C ANISOU 3543 CA VAL A 493 7936 9289 8594 -4587 -459 361 C ATOM 3544 C VAL A 493 20.030 -17.576 147.009 1.00 69.23 C ANISOU 3544 C VAL A 493 8374 9114 8817 -4756 -552 300 C ATOM 3545 O VAL A 493 19.297 -18.568 147.029 1.00 72.13 O ANISOU 3545 O VAL A 493 8776 9473 9156 -5070 -613 343 O ATOM 3546 CB VAL A 493 18.697 -15.444 146.753 1.00 67.40 C ANISOU 3546 CB VAL A 493 7624 9536 8447 -4541 -473 292 C ATOM 3547 CG1 VAL A 493 18.372 -14.101 147.385 1.00 65.34 C ANISOU 3547 CG1 VAL A 493 7114 9580 8134 -4327 -383 337 C ATOM 3548 CG2 VAL A 493 19.358 -15.254 145.400 1.00 67.29 C ANISOU 3548 CG2 VAL A 493 7728 9367 8472 -4387 -519 145 C ATOM 3549 N ASN A 494 21.226 -17.597 146.418 1.00 70.45 N ANISOU 3549 N ASN A 494 8731 8985 9051 -4556 -564 200 N ATOM 3550 CA ASN A 494 21.741 -18.830 145.841 1.00 67.81 C ANISOU 3550 CA ASN A 494 8678 8308 8778 -4684 -648 134 C ATOM 3551 C ASN A 494 22.061 -19.842 146.928 1.00 68.90 C ANISOU 3551 C ASN A 494 9000 8214 8964 -4831 -657 246 C ATOM 3552 O ASN A 494 21.706 -21.020 146.817 1.00 71.87 O ANISOU 3552 O ASN A 494 9525 8437 9346 -5105 -735 261 O ATOM 3553 CB ASN A 494 22.964 -18.527 144.980 1.00 66.02 C ANISOU 3553 CB ASN A 494 8600 7868 8617 -4409 -648 -3 C ATOM 3554 CG ASN A 494 22.627 -17.633 143.804 1.00 65.72 C ANISOU 3554 CG ASN A 494 8406 8041 8524 -4294 -653 -111 C ATOM 3555 OD1 ASN A 494 21.583 -16.961 143.785 1.00 65.51 O ANISOU 3555 OD1 ASN A 494 8129 8345 8417 -4343 -639 -75 O ATOM 3556 ND2 ASN A 494 23.508 -17.620 142.806 1.00 64.36 N ANISOU 3556 ND2 ASN A 494 8378 7685 8391 -4134 -675 -244 N ATOM 3557 N ALA A 495 22.708 -19.391 148.002 1.00 68.31 N ANISOU 3557 N ALA A 495 8921 8114 8919 -4658 -581 329 N ATOM 3558 CA ALA A 495 22.977 -20.262 149.136 1.00 69.45 C ANISOU 3558 CA ALA A 495 9222 8069 9098 -4788 -586 455 C ATOM 3559 C ALA A 495 21.697 -20.639 149.871 1.00 71.45 C ANISOU 3559 C ALA A 495 9334 8546 9268 -5104 -588 591 C ATOM 3560 O ALA A 495 21.591 -21.751 150.400 1.00 73.36 O ANISOU 3560 O ALA A 495 9739 8611 9523 -5329 -635 677 O ATOM 3561 CB ALA A 495 23.964 -19.583 150.087 1.00 68.43 C ANISOU 3561 CB ALA A 495 9099 7894 9008 -4517 -503 508 C ATOM 3562 N ALA A 496 20.718 -19.735 149.919 1.00 69.79 N ANISOU 3562 N ALA A 496 8823 8728 8968 -5110 -538 612 N ATOM 3563 CA ALA A 496 19.437 -20.088 150.518 1.00 71.99 C ANISOU 3563 CA ALA A 496 8941 9258 9156 -5420 -540 732 C ATOM 3564 C ALA A 496 18.705 -21.122 149.672 1.00 74.44 C ANISOU 3564 C ALA A 496 9330 9510 9443 -5621 -633 680 C ATOM 3565 O ALA A 496 18.062 -22.032 150.206 1.00 76.78 O ANISOU 3565 O ALA A 496 9668 9803 9701 -5806 -655 769 O ATOM 3566 CB ALA A 496 18.582 -18.837 150.703 1.00 71.30 C ANISOU 3566 CB ALA A 496 8503 9614 8974 -5320 -463 748 C ATOM 3567 N ILE A 497 18.797 -21.001 148.349 1.00 74.03 N ANISOU 3567 N ILE A 497 9305 9415 9409 -5587 -689 535 N ATOM 3568 CA ILE A 497 18.140 -21.966 147.478 1.00 76.37 C ANISOU 3568 CA ILE A 497 9683 9651 9681 -5767 -779 475 C ATOM 3569 C ILE A 497 18.847 -23.318 147.555 1.00 77.64 C ANISOU 3569 C ILE A 497 10189 9388 9924 -5822 -841 471 C ATOM 3570 O ILE A 497 18.195 -24.365 147.546 1.00 80.55 O ANISOU 3570 O ILE A 497 10638 9704 10264 -6022 -896 504 O ATOM 3571 CB ILE A 497 18.059 -21.414 146.041 1.00 75.58 C ANISOU 3571 CB ILE A 497 9511 9637 9568 -5704 -821 318 C ATOM 3572 CG1 ILE A 497 16.913 -20.406 145.922 1.00 75.57 C ANISOU 3572 CG1 ILE A 497 9153 10100 9461 -5718 -785 338 C ATOM 3573 CG2 ILE A 497 17.795 -22.509 145.061 1.00 77.68 C ANISOU 3573 CG2 ILE A 497 9950 9729 9838 -5848 -920 230 C ATOM 3574 CD1 ILE A 497 16.892 -19.638 144.624 1.00 74.48 C ANISOU 3574 CD1 ILE A 497 8912 10084 9303 -5619 -817 199 C ATOM 3575 N LYS A 498 20.184 -23.321 147.680 1.00 75.97 N ANISOU 3575 N LYS A 498 10183 8872 9810 -5641 -832 437 N ATOM 3576 CA LYS A 498 20.906 -24.591 147.809 1.00 81.94 C ANISOU 3576 CA LYS A 498 11263 9225 10646 -5658 -889 435 C ATOM 3577 C LYS A 498 20.486 -25.345 149.056 1.00 85.79 C ANISOU 3577 C LYS A 498 11787 9701 11109 -5807 -880 601 C ATOM 3578 O LYS A 498 20.321 -26.568 149.024 1.00 86.48 O ANISOU 3578 O LYS A 498 12062 9588 11210 -5947 -947 616 O ATOM 3579 CB LYS A 498 22.428 -24.392 147.868 1.00 85.86 C ANISOU 3579 CB LYS A 498 11951 9426 11245 -5412 -873 382 C ATOM 3580 CG LYS A 498 23.066 -23.930 146.620 1.00 89.17 C ANISOU 3580 CG LYS A 498 12419 9763 11700 -5260 -895 207 C ATOM 3581 CD LYS A 498 22.277 -24.408 145.461 1.00 94.20 C ANISOU 3581 CD LYS A 498 13047 10455 12292 -5403 -967 104 C ATOM 3582 CE LYS A 498 21.773 -23.252 144.783 1.00 95.40 C ANISOU 3582 CE LYS A 498 12949 10922 12378 -5375 -941 42 C ATOM 3583 NZ LYS A 498 20.813 -23.621 143.772 1.00 99.21 N ANISOU 3583 NZ LYS A 498 13373 11528 12796 -5533 -1007 -34 N ATOM 3584 N GLU A 499 20.354 -24.643 150.170 1.00103.77 N ANISOU 3584 N GLU A 499 13896 12182 13348 -5774 -797 726 N ATOM 3585 CA GLU A 499 20.115 -25.307 151.436 1.00106.57 C ANISOU 3585 CA GLU A 499 14301 12513 13678 -5890 -782 886 C ATOM 3586 C GLU A 499 18.645 -25.632 151.637 1.00104.36 C ANISOU 3586 C GLU A 499 13849 12517 13286 -6142 -790 962 C ATOM 3587 O GLU A 499 18.317 -26.506 152.447 1.00105.64 O ANISOU 3587 O GLU A 499 14098 12621 13421 -6295 -806 1078 O ATOM 3588 CB GLU A 499 20.639 -24.423 152.567 1.00108.89 C ANISOU 3588 CB GLU A 499 14495 12906 13972 -5740 -689 984 C ATOM 3589 CG GLU A 499 20.743 -25.103 153.907 1.00113.25 C ANISOU 3589 CG GLU A 499 15150 13366 14515 -5808 -675 1142 C ATOM 3590 CD GLU A 499 21.968 -25.986 154.013 1.00115.77 C ANISOU 3590 CD GLU A 499 15800 13245 14943 -5708 -729 1132 C ATOM 3591 OE1 GLU A 499 21.963 -26.899 154.863 1.00118.46 O ANISOU 3591 OE1 GLU A 499 16278 13452 15280 -5805 -753 1246 O ATOM 3592 OE2 GLU A 499 22.934 -25.770 153.250 1.00116.71 O ANISOU 3592 OE2 GLU A 499 16038 13158 15149 -5525 -749 1010 O ATOM 3593 N TYR A 500 17.756 -24.973 150.893 1.00100.32 N ANISOU 3593 N TYR A 500 13100 12312 12704 -6187 -783 898 N ATOM 3594 CA TYR A 500 16.330 -25.093 151.137 1.00 99.12 C ANISOU 3594 CA TYR A 500 12740 12487 12433 -6400 -778 972 C ATOM 3595 C TYR A 500 15.494 -25.371 149.898 1.00 98.92 C ANISOU 3595 C TYR A 500 12660 12558 12366 -6535 -849 870 C ATOM 3596 O TYR A 500 14.282 -25.561 150.030 1.00 97.66 O ANISOU 3596 O TYR A 500 12339 12664 12105 -6724 -854 927 O ATOM 3597 CB TYR A 500 15.798 -23.816 151.802 1.00 96.94 C ANISOU 3597 CB TYR A 500 12136 12620 12076 -6318 -676 1034 C ATOM 3598 CG TYR A 500 16.494 -23.457 153.088 1.00 94.89 C ANISOU 3598 CG TYR A 500 11897 12322 11837 -6196 -598 1141 C ATOM 3599 CD1 TYR A 500 17.686 -22.753 153.081 1.00 90.32 C ANISOU 3599 CD1 TYR A 500 11383 11591 11342 -5960 -563 1094 C ATOM 3600 CD2 TYR A 500 15.958 -23.823 154.307 1.00 96.96 C ANISOU 3600 CD2 TYR A 500 12111 12702 12026 -6322 -563 1289 C ATOM 3601 CE1 TYR A 500 18.325 -22.423 154.251 1.00 88.27 C ANISOU 3601 CE1 TYR A 500 11142 11299 11097 -5851 -494 1192 C ATOM 3602 CE2 TYR A 500 16.589 -23.503 155.480 1.00 94.83 C ANISOU 3602 CE2 TYR A 500 11860 12404 11768 -6211 -494 1386 C ATOM 3603 CZ TYR A 500 17.773 -22.799 155.454 1.00 91.40 C ANISOU 3603 CZ TYR A 500 11491 11818 11420 -5974 -460 1337 C ATOM 3604 OH TYR A 500 18.412 -22.470 156.630 1.00 90.84 O ANISOU 3604 OH TYR A 500 11439 11722 11355 -5864 -394 1435 O ATOM 3605 N GLY A 501 16.088 -25.403 148.712 1.00 85.98 N ANISOU 3605 N GLY A 501 11150 10725 10795 -6444 -903 721 N ATOM 3606 CA GLY A 501 15.305 -25.460 147.493 1.00 86.14 C ANISOU 3606 CA GLY A 501 11084 10879 10764 -6545 -964 616 C ATOM 3607 C GLY A 501 14.655 -24.116 147.224 1.00 84.74 C ANISOU 3607 C GLY A 501 10568 11119 10512 -6460 -909 594 C ATOM 3608 O GLY A 501 14.843 -23.141 147.947 1.00 82.88 O ANISOU 3608 O GLY A 501 10172 11053 10267 -6317 -824 651 O ATOM 3609 N ASP A 502 13.868 -24.071 146.156 1.00 85.79 N ANISOU 3609 N ASP A 502 10592 11419 10587 -6544 -962 509 N ATOM 3610 CA ASP A 502 13.232 -22.816 145.795 1.00 84.67 C ANISOU 3610 CA ASP A 502 10129 11670 10371 -6449 -922 480 C ATOM 3611 C ASP A 502 12.137 -22.464 146.796 1.00 85.83 C ANISOU 3611 C ASP A 502 10008 12191 10414 -6532 -857 615 C ATOM 3612 O ASP A 502 11.684 -23.294 147.590 1.00 87.95 O ANISOU 3612 O ASP A 502 10331 12437 10648 -6712 -858 722 O ATOM 3613 CB ASP A 502 12.667 -22.889 144.379 1.00 86.53 C ANISOU 3613 CB ASP A 502 10320 11992 10565 -6514 -1001 357 C ATOM 3614 CG ASP A 502 13.725 -23.230 143.351 1.00 87.30 C ANISOU 3614 CG ASP A 502 10679 11737 10753 -6425 -1063 212 C ATOM 3615 OD1 ASP A 502 14.394 -22.302 142.850 1.00 85.19 O ANISOU 3615 OD1 ASP A 502 10370 11480 10517 -6220 -1042 127 O ATOM 3616 OD2 ASP A 502 13.891 -24.431 143.051 1.00 89.77 O ANISOU 3616 OD2 ASP A 502 11241 11764 11101 -6557 -1133 180 O ATOM 3617 N PHE A 503 11.715 -21.208 146.751 1.00 84.53 N ANISOU 3617 N PHE A 503 9551 12374 10192 -6390 -801 606 N ATOM 3618 CA PHE A 503 10.760 -20.664 147.699 1.00 85.31 C ANISOU 3618 CA PHE A 503 9373 12852 10190 -6406 -726 717 C ATOM 3619 C PHE A 503 9.461 -20.318 146.990 1.00 86.91 C ANISOU 3619 C PHE A 503 9314 13427 10282 -6473 -754 684 C ATOM 3620 O PHE A 503 9.443 -20.044 145.788 1.00 86.47 O ANISOU 3620 O PHE A 503 9236 13388 10231 -6423 -811 571 O ATOM 3621 CB PHE A 503 11.322 -19.416 148.384 1.00 82.61 C ANISOU 3621 CB PHE A 503 8891 12631 9868 -6153 -627 740 C ATOM 3622 CG PHE A 503 12.668 -19.625 149.014 1.00 80.83 C ANISOU 3622 CG PHE A 503 8910 12051 9751 -6062 -599 765 C ATOM 3623 CD1 PHE A 503 13.818 -19.590 148.247 1.00 78.93 C ANISOU 3623 CD1 PHE A 503 8870 11504 9615 -5942 -636 659 C ATOM 3624 CD2 PHE A 503 12.782 -19.857 150.372 1.00 81.16 C ANISOU 3624 CD2 PHE A 503 8981 12074 9784 -6091 -536 893 C ATOM 3625 CE1 PHE A 503 15.054 -19.782 148.822 1.00 77.41 C ANISOU 3625 CE1 PHE A 503 8902 10992 9519 -5849 -612 682 C ATOM 3626 CE2 PHE A 503 14.016 -20.050 150.952 1.00 79.62 C ANISOU 3626 CE2 PHE A 503 9010 11559 9685 -6001 -515 920 C ATOM 3627 CZ PHE A 503 15.155 -20.013 150.176 1.00 77.75 C ANISOU 3627 CZ PHE A 503 8970 11017 9555 -5877 -553 815 C ATOM 3628 N ASP A 504 8.368 -20.343 147.748 1.00 90.01 N ANISOU 3628 N ASP A 504 9509 14124 10567 -6584 -716 786 N ATOM 3629 CA ASP A 504 7.099 -19.879 147.205 1.00 96.46 C ANISOU 3629 CA ASP A 504 10043 15339 11269 -6616 -731 765 C ATOM 3630 C ASP A 504 7.163 -18.393 146.870 1.00 93.44 C ANISOU 3630 C ASP A 504 9425 15201 10876 -6332 -684 704 C ATOM 3631 O ASP A 504 6.601 -17.951 145.862 1.00 93.19 O ANISOU 3631 O ASP A 504 9248 15361 10798 -6292 -729 628 O ATOM 3632 CB ASP A 504 5.973 -20.175 148.198 1.00 97.35 C ANISOU 3632 CB ASP A 504 9993 15732 11265 -6777 -690 889 C ATOM 3633 CG ASP A 504 4.661 -19.521 147.812 1.00 97.17 C ANISOU 3633 CG ASP A 504 9643 16164 11114 -6766 -687 878 C ATOM 3634 OD1 ASP A 504 3.922 -20.094 146.978 1.00 99.42 O ANISOU 3634 OD1 ASP A 504 9916 16510 11348 -6943 -766 843 O ATOM 3635 OD2 ASP A 504 4.366 -18.437 148.359 1.00 94.72 O ANISOU 3635 OD2 ASP A 504 9087 16150 10752 -6573 -606 902 O ATOM 3636 N ASN A 505 7.876 -17.614 147.679 1.00 96.51 N ANISOU 3636 N ASN A 505 9785 15577 11308 -6129 -598 735 N ATOM 3637 CA ASN A 505 7.918 -16.168 147.534 1.00 95.93 C ANISOU 3637 CA ASN A 505 9482 15747 11219 -5849 -545 690 C ATOM 3638 C ASN A 505 9.235 -15.676 148.108 1.00 92.72 C ANISOU 3638 C ASN A 505 9201 15116 10914 -5663 -483 692 C ATOM 3639 O ASN A 505 9.690 -16.167 149.143 1.00 90.43 O ANISOU 3639 O ASN A 505 9044 14662 10654 -5722 -439 777 O ATOM 3640 CB ASN A 505 6.731 -15.514 148.258 1.00101.44 C ANISOU 3640 CB ASN A 505 9863 16889 11791 -5801 -477 760 C ATOM 3641 CG ASN A 505 6.651 -13.996 148.063 1.00103.19 C ANISOU 3641 CG ASN A 505 9837 17381 11989 -5492 -429 708 C ATOM 3642 OD1 ASN A 505 5.880 -13.326 148.761 1.00105.27 O ANISOU 3642 OD1 ASN A 505 9860 17976 12162 -5391 -361 756 O ATOM 3643 ND2 ASN A 505 7.403 -13.454 147.100 1.00103.97 N ANISOU 3643 ND2 ASN A 505 9996 17348 12161 -5338 -468 609 N ATOM 3644 N ILE A 506 9.851 -14.725 147.415 1.00 78.76 N ANISOU 3644 N ILE A 506 7394 13339 9193 -5444 -485 602 N ATOM 3645 CA ILE A 506 10.999 -13.986 147.920 1.00 76.01 C ANISOU 3645 CA ILE A 506 7101 12855 8923 -5233 -418 599 C ATOM 3646 C ILE A 506 10.616 -12.514 147.942 1.00 74.98 C ANISOU 3646 C ILE A 506 6676 13075 8738 -4972 -361 577 C ATOM 3647 O ILE A 506 10.308 -11.933 146.894 1.00 74.79 O ANISOU 3647 O ILE A 506 6535 13191 8691 -4877 -410 494 O ATOM 3648 CB ILE A 506 12.252 -14.219 147.070 1.00 74.18 C ANISOU 3648 CB ILE A 506 7129 12252 8806 -5201 -475 505 C ATOM 3649 CG1 ILE A 506 12.477 -15.713 146.875 1.00 75.64 C ANISOU 3649 CG1 ILE A 506 7603 12103 9035 -5445 -547 508 C ATOM 3650 CG2 ILE A 506 13.453 -13.612 147.758 1.00 71.63 C ANISOU 3650 CG2 ILE A 506 6941 11717 8560 -4908 -394 511 C ATOM 3651 CD1 ILE A 506 13.683 -16.046 146.047 1.00 74.16 C ANISOU 3651 CD1 ILE A 506 7689 11537 8953 -5411 -604 406 C ATOM 3652 N VAL A 507 10.637 -11.912 149.128 1.00 74.43 N ANISOU 3652 N VAL A 507 6493 13141 8644 -4845 -260 650 N ATOM 3653 CA VAL A 507 10.074 -10.586 149.362 1.00 74.05 C ANISOU 3653 CA VAL A 507 6155 13454 8526 -4596 -197 642 C ATOM 3654 C VAL A 507 11.203 -9.592 149.592 1.00 71.21 C ANISOU 3654 C VAL A 507 5907 12911 8239 -4236 -137 598 C ATOM 3655 O VAL A 507 12.103 -9.841 150.403 1.00 70.08 O ANISOU 3655 O VAL A 507 5953 12518 8157 -4205 -88 639 O ATOM 3656 CB VAL A 507 9.114 -10.596 150.562 1.00 75.90 C ANISOU 3656 CB VAL A 507 6223 13960 8657 -4631 -123 738 C ATOM 3657 CG1 VAL A 507 8.245 -9.368 150.538 1.00 76.27 C ANISOU 3657 CG1 VAL A 507 5964 14401 8612 -4393 -84 710 C ATOM 3658 CG2 VAL A 507 8.273 -11.856 150.551 1.00 78.68 C ANISOU 3658 CG2 VAL A 507 6626 14316 8954 -4941 -176 790 C ATOM 3659 N ILE A 508 11.137 -8.456 148.902 1.00 70.20 N ANISOU 3659 N ILE A 508 5672 12901 8099 -3951 -144 519 N ATOM 3660 CA ILE A 508 12.159 -7.418 148.976 1.00 67.63 C ANISOU 3660 CA ILE A 508 5460 12400 7836 -3592 -97 469 C ATOM 3661 C ILE A 508 11.501 -6.126 149.426 1.00 67.73 C ANISOU 3661 C ILE A 508 5210 12752 7771 -3339 -34 470 C ATOM 3662 O ILE A 508 10.600 -5.616 148.751 1.00 68.77 O ANISOU 3662 O ILE A 508 5130 13163 7837 -3286 -73 437 O ATOM 3663 CB ILE A 508 12.865 -7.213 147.630 1.00 66.21 C ANISOU 3663 CB ILE A 508 5446 11989 7721 -3464 -170 365 C ATOM 3664 CG1 ILE A 508 13.601 -8.482 147.220 1.00 66.12 C ANISOU 3664 CG1 ILE A 508 5711 11623 7788 -3686 -227 350 C ATOM 3665 CG2 ILE A 508 13.822 -6.037 147.711 1.00 63.77 C ANISOU 3665 CG2 ILE A 508 5225 11543 7463 -3099 -120 320 C ATOM 3666 CD1 ILE A 508 14.171 -8.416 145.839 1.00 65.14 C ANISOU 3666 CD1 ILE A 508 5733 11308 7710 -3601 -301 245 C ATOM 3667 N GLU A 509 11.952 -5.589 150.554 1.00 70.59 N ANISOU 3667 N GLU A 509 5589 13091 8141 -3174 59 505 N ATOM 3668 CA GLU A 509 11.478 -4.280 150.972 1.00 71.50 C ANISOU 3668 CA GLU A 509 5493 13482 8192 -2891 118 490 C ATOM 3669 C GLU A 509 12.006 -3.226 150.013 1.00 70.15 C ANISOU 3669 C GLU A 509 5392 13199 8065 -2584 82 397 C ATOM 3670 O GLU A 509 13.160 -3.281 149.581 1.00 67.03 O ANISOU 3670 O GLU A 509 5249 12456 7762 -2513 60 357 O ATOM 3671 CB GLU A 509 11.914 -3.973 152.402 1.00 76.49 C ANISOU 3671 CB GLU A 509 6153 14092 8820 -2790 223 541 C ATOM 3672 CG GLU A 509 11.819 -2.506 152.786 1.00 80.05 C ANISOU 3672 CG GLU A 509 6477 14708 9232 -2433 283 499 C ATOM 3673 CD GLU A 509 11.647 -2.311 154.288 1.00 81.60 C ANISOU 3673 CD GLU A 509 6580 15057 9366 -2405 389 558 C ATOM 3674 OE1 GLU A 509 11.839 -1.181 154.766 1.00 83.39 O ANISOU 3674 OE1 GLU A 509 6772 15337 9577 -2110 445 521 O ATOM 3675 OE2 GLU A 509 11.301 -3.281 154.991 1.00 82.52 O ANISOU 3675 OE2 GLU A 509 6662 15248 9446 -2681 415 643 O ATOM 3676 N MET A 510 11.144 -2.285 149.647 1.00 65.77 N ANISOU 3676 N MET A 510 4608 12944 7439 -2408 71 365 N ATOM 3677 CA MET A 510 11.502 -1.226 148.721 1.00 65.51 C ANISOU 3677 CA MET A 510 4620 12838 7431 -2120 30 288 C ATOM 3678 C MET A 510 11.298 0.126 149.386 1.00 64.25 C ANISOU 3678 C MET A 510 4332 12850 7229 -1795 96 275 C ATOM 3679 O MET A 510 10.425 0.292 150.240 1.00 65.78 O ANISOU 3679 O MET A 510 4303 13350 7341 -1797 153 311 O ATOM 3680 CB MET A 510 10.673 -1.314 147.442 1.00 65.97 C ANISOU 3680 CB MET A 510 4548 13073 7444 -2191 -68 253 C ATOM 3681 CG MET A 510 10.767 -2.652 146.723 1.00 67.52 C ANISOU 3681 CG MET A 510 4864 13119 7672 -2520 -142 254 C ATOM 3682 SD MET A 510 12.289 -2.909 145.794 1.00 65.95 S ANISOU 3682 SD MET A 510 5028 12439 7592 -2478 -189 189 S ATOM 3683 CE MET A 510 12.241 -1.543 144.655 1.00 66.02 C ANISOU 3683 CE MET A 510 4984 12521 7578 -2156 -241 118 C ATOM 3684 N ALA A 511 11.942 1.137 148.865 1.00 62.42 N ANISOU 3684 N ALA A 511 4247 12418 7050 -1518 88 220 N ATOM 3685 CA ALA A 511 11.754 2.434 149.427 1.00 62.06 C ANISOU 3685 CA ALA A 511 4130 12475 6976 -1189 141 197 C ATOM 3686 C ALA A 511 11.182 3.316 148.373 1.00 62.87 C ANISOU 3686 C ALA A 511 4088 12770 7031 -997 72 153 C ATOM 3687 O ALA A 511 11.834 4.155 147.813 1.00 61.60 O ANISOU 3687 O ALA A 511 4059 12436 6910 -790 32 108 O ATOM 3688 CB ALA A 511 13.074 2.989 149.908 1.00 59.66 C ANISOU 3688 CB ALA A 511 4090 11818 6758 -1018 178 174 C ATOM 3689 N ARG A 512 9.921 3.058 148.125 1.00 66.70 N ANISOU 3689 N ARG A 512 4293 13628 7423 -1075 56 171 N ATOM 3690 CA ARG A 512 9.113 3.826 147.219 1.00 68.30 C ANISOU 3690 CA ARG A 512 4322 14064 7567 -900 -13 138 C ATOM 3691 C ARG A 512 7.946 4.361 148.019 1.00 72.35 C ANISOU 3691 C ARG A 512 4524 14992 7974 -781 33 149 C ATOM 3692 O ARG A 512 7.459 3.742 148.931 1.00 78.07 O ANISOU 3692 O ARG A 512 5125 15884 8653 -927 108 191 O ATOM 3693 CB ARG A 512 8.597 2.968 146.083 1.00 68.66 C ANISOU 3693 CB ARG A 512 4314 14178 7595 -1133 -113 138 C ATOM 3694 CG ARG A 512 9.622 2.068 145.442 1.00 67.43 C ANISOU 3694 CG ARG A 512 4444 13644 7531 -1290 -155 123 C ATOM 3695 CD ARG A 512 9.059 1.456 144.189 1.00 68.58 C ANISOU 3695 CD ARG A 512 4537 13869 7651 -1547 -246 120 C ATOM 3696 NE ARG A 512 10.088 1.240 143.207 1.00 67.66 N ANISOU 3696 NE ARG A 512 4628 13493 7588 -1494 -320 71 N ATOM 3697 CZ ARG A 512 10.146 0.199 142.396 1.00 67.27 C ANISOU 3697 CZ ARG A 512 4641 13376 7542 -1727 -400 51 C ATOM 3698 NH1 ARG A 512 11.144 0.088 141.555 1.00 67.52 N ANISOU 3698 NH1 ARG A 512 4865 13174 7615 -1655 -459 2 N ATOM 3699 NH2 ARG A 512 9.219 -0.722 142.419 1.00 67.69 N ANISOU 3699 NH2 ARG A 512 4573 13591 7555 -2043 -422 79 N ATOM 3700 N GLU A 513 7.493 5.537 147.687 1.00 77.35 N ANISOU 3700 N GLU A 513 5028 15801 8562 -520 -17 113 N ATOM 3701 CA GLU A 513 6.379 6.089 148.398 1.00 84.77 C ANISOU 3701 CA GLU A 513 5690 17115 9405 -320 26 106 C ATOM 3702 C GLU A 513 5.046 5.544 147.939 1.00 95.05 C ANISOU 3702 C GLU A 513 6735 18771 10609 -501 -16 132 C ATOM 3703 O GLU A 513 4.939 4.870 146.938 1.00 74.23 O ANISOU 3703 O GLU A 513 4086 16142 7975 -678 -108 137 O ATOM 3704 CB GLU A 513 6.328 7.600 148.231 1.00 74.84 C ANISOU 3704 CB GLU A 513 4463 15825 8147 87 -9 53 C ATOM 3705 CG GLU A 513 7.572 8.254 147.717 1.00 68.27 C ANISOU 3705 CG GLU A 513 3949 14579 7409 254 23 27 C ATOM 3706 CD GLU A 513 7.844 9.529 148.435 1.00 68.47 C ANISOU 3706 CD GLU A 513 3959 14646 7411 653 47 -18 C ATOM 3707 OE1 GLU A 513 8.265 9.446 149.596 1.00 68.30 O ANISOU 3707 OE1 GLU A 513 4010 14541 7400 744 139 -30 O ATOM 3708 OE2 GLU A 513 7.632 10.603 147.858 1.00 69.38 O ANISOU 3708 OE2 GLU A 513 3997 14870 7493 875 -29 -42 O ATOM 3709 N THR A 514 4.038 5.826 148.736 1.00103.95 N ANISOU 3709 N THR A 514 7731 20121 11644 -463 54 145 N ATOM 3710 CA THR A 514 2.664 5.575 148.412 1.00112.10 C ANISOU 3710 CA THR A 514 8568 21462 12561 -528 25 159 C ATOM 3711 C THR A 514 2.091 6.865 148.936 1.00114.44 C ANISOU 3711 C THR A 514 8757 21945 12780 -181 69 122 C ATOM 3712 O THR A 514 2.163 7.143 150.129 1.00118.96 O ANISOU 3712 O THR A 514 9278 22626 13297 -174 161 132 O ATOM 3713 CB THR A 514 2.073 4.350 149.087 1.00116.89 C ANISOU 3713 CB THR A 514 9116 22180 13116 -888 71 221 C ATOM 3714 OG1 THR A 514 2.530 3.166 148.429 1.00116.84 O ANISOU 3714 OG1 THR A 514 9195 22065 13135 -917 177 243 O ATOM 3715 CG2 THR A 514 0.568 4.421 149.026 1.00117.83 C ANISOU 3715 CG2 THR A 514 9309 22180 13281 -1252 -2 253 C ATOM 3716 N ASN A 515 1.541 7.661 148.045 1.00110.44 N ANISOU 3716 N ASN A 515 8227 21472 12264 106 0 79 N ATOM 3717 CA ASN A 515 0.999 8.927 148.442 1.00105.41 C ANISOU 3717 CA ASN A 515 7501 20999 11552 448 32 37 C ATOM 3718 C ASN A 515 -0.437 9.119 148.017 1.00104.45 C ANISOU 3718 C ASN A 515 7163 21210 11312 421 -16 46 C ATOM 3719 O ASN A 515 -0.835 8.725 146.935 1.00104.91 O ANISOU 3719 O ASN A 515 7147 21368 11348 130 -66 84 O ATOM 3720 CB ASN A 515 1.811 10.062 147.835 1.00 96.95 C ANISOU 3720 CB ASN A 515 6564 19732 10542 819 -8 -15 C ATOM 3721 CG ASN A 515 3.094 10.321 148.563 1.00 89.72 C ANISOU 3721 CG ASN A 515 5866 18472 9751 804 9 -18 C ATOM 3722 OD1 ASN A 515 4.157 10.003 148.073 1.00 85.62 O ANISOU 3722 OD1 ASN A 515 5414 17820 9298 581 -41 8 O ATOM 3723 ND2 ASN A 515 3.001 10.922 149.731 1.00 89.33 N ANISOU 3723 ND2 ASN A 515 5928 18282 9730 1038 78 -54 N ATOM 3724 N GLU A 516 -1.221 9.740 148.875 1.00123.90 N ANISOU 3724 N GLU A 516 9529 23850 13698 716 1 8 N ATOM 3725 CA GLU A 516 -2.584 10.028 148.516 1.00128.46 C ANISOU 3725 CA GLU A 516 9904 24739 14165 756 -50 7 C ATOM 3726 C GLU A 516 -2.512 11.304 147.709 1.00127.59 C ANISOU 3726 C GLU A 516 9821 24607 14052 1172 -103 -46 C ATOM 3727 O GLU A 516 -1.495 11.979 147.675 1.00124.03 O ANISOU 3727 O GLU A 516 9495 23991 13640 1448 -63 -90 O ATOM 3728 CB GLU A 516 -3.506 10.141 149.723 1.00135.38 C ANISOU 3728 CB GLU A 516 10596 25925 14917 697 30 16 C ATOM 3729 CG GLU A 516 -4.340 8.890 149.977 1.00139.15 C ANISOU 3729 CG GLU A 516 10973 26551 15348 286 44 79 C ATOM 3730 CD GLU A 516 -4.294 8.447 151.431 1.00140.91 C ANISOU 3730 CD GLU A 516 11168 26851 15521 187 160 97 C ATOM 3731 OE1 GLU A 516 -3.626 9.129 152.233 1.00142.52 O ANISOU 3731 OE1 GLU A 516 11301 27197 15652 440 220 57 O ATOM 3732 OE2 GLU A 516 -4.917 7.422 151.778 1.00140.00 O ANISOU 3732 OE2 GLU A 516 11123 26626 15444 -140 189 150 O ATOM 3733 N ASP A 517 -3.612 11.623 147.066 1.00111.80 N ANISOU 3733 N ASP A 517 7701 22783 11996 1222 -192 -43 N ATOM 3734 CA ASP A 517 -3.725 12.748 146.175 1.00111.68 C ANISOU 3734 CA ASP A 517 7748 22683 12000 1553 -279 -76 C ATOM 3735 C ASP A 517 -3.478 14.152 146.698 1.00111.95 C ANISOU 3735 C ASP A 517 7837 22680 12019 1948 -238 -132 C ATOM 3736 O ASP A 517 -2.989 14.979 145.955 1.00109.89 O ANISOU 3736 O ASP A 517 7688 22268 11795 2225 -305 -156 O ATOM 3737 CB ASP A 517 -5.030 12.640 145.428 1.00114.32 C ANISOU 3737 CB ASP A 517 7905 23281 12249 1540 -368 -61 C ATOM 3738 CG ASP A 517 -5.122 11.359 144.650 1.00114.78 C ANISOU 3738 CG ASP A 517 7892 23419 12301 1135 -410 -11 C ATOM 3739 OD1 ASP A 517 -4.295 11.172 143.745 1.00114.68 O ANISOU 3739 OD1 ASP A 517 7973 23250 12349 1049 -500 4 O ATOM 3740 OD2 ASP A 517 -6.003 10.524 144.938 1.00117.43 O ANISOU 3740 OD2 ASP A 517 8075 23981 12561 896 -358 14 O ATOM 3741 N ASP A 518 -3.819 14.452 147.942 1.00116.03 N ANISOU 3741 N ASP A 518 8282 23330 12476 1977 -135 -154 N ATOM 3742 CA ASP A 518 -3.575 15.795 148.451 1.00116.70 C ANISOU 3742 CA ASP A 518 8489 23277 12576 2304 -83 -213 C ATOM 3743 C ASP A 518 -2.095 15.988 148.370 1.00114.55 C ANISOU 3743 C ASP A 518 8479 22607 12437 2344 -84 -219 C ATOM 3744 O ASP A 518 -1.609 17.051 148.009 1.00117.53 O ANISOU 3744 O ASP A 518 9013 22785 12857 2655 -114 -260 O ATOM 3745 CB ASP A 518 -3.944 15.907 149.913 1.00118.72 C ANISOU 3745 CB ASP A 518 8639 23719 12751 2244 33 -227 C ATOM 3746 CG ASP A 518 -4.878 17.018 150.178 1.00122.16 C ANISOU 3746 CG ASP A 518 8804 24560 13050 2131 37 -209 C ATOM 3747 OD1 ASP A 518 -5.893 17.122 149.459 1.00122.00 O ANISOU 3747 OD1 ASP A 518 8682 24661 13012 1779 34 -150 O ATOM 3748 OD2 ASP A 518 -4.589 17.796 151.109 1.00124.41 O ANISOU 3748 OD2 ASP A 518 8984 25041 13247 2395 38 -254 O ATOM 3749 N GLU A 519 -1.391 14.934 148.753 1.00107.81 N ANISOU 3749 N GLU A 519 7682 21630 11651 2029 -56 -176 N ATOM 3750 CA GLU A 519 0.050 14.897 148.727 1.00101.38 C ANISOU 3750 CA GLU A 519 7101 20458 10962 2035 -56 -177 C ATOM 3751 C GLU A 519 0.610 14.892 147.314 1.00 97.19 C ANISOU 3751 C GLU A 519 6661 19762 10504 1990 -169 -152 C ATOM 3752 O GLU A 519 1.557 15.606 147.024 1.00 92.70 O ANISOU 3752 O GLU A 519 6295 18896 10030 2092 -185 -163 O ATOM 3753 CB GLU A 519 0.544 13.686 149.506 1.00100.81 C ANISOU 3753 CB GLU A 519 7059 20319 10927 1732 35 -147 C ATOM 3754 N LYS A 520 -0.003 14.101 146.435 1.00 90.75 N ANISOU 3754 N LYS A 520 5708 19126 9645 1837 -248 -119 N ATOM 3755 CA LYS A 520 0.477 13.994 145.069 1.00 87.61 C ANISOU 3755 CA LYS A 520 5405 18577 9306 1824 -364 -100 C ATOM 3756 C LYS A 520 0.399 15.322 144.434 1.00 84.90 C ANISOU 3756 C LYS A 520 5155 18138 8965 2196 -438 -127 C ATOM 3757 O LYS A 520 1.311 15.739 143.778 1.00 81.60 O ANISOU 3757 O LYS A 520 4921 17457 8625 2281 -496 -123 O ATOM 3758 CB LYS A 520 -0.331 13.003 144.276 1.00 84.68 C ANISOU 3758 CB LYS A 520 4881 18413 8881 1597 -445 -65 C ATOM 3759 CG LYS A 520 0.106 11.589 144.528 1.00 85.77 C ANISOU 3759 CG LYS A 520 4896 18704 8988 1231 -394 -34 C ATOM 3760 CD LYS A 520 -0.304 10.678 143.399 1.00 82.56 C ANISOU 3760 CD LYS A 520 4636 18057 8678 1010 -335 -20 C ATOM 3761 CE LYS A 520 0.168 9.265 143.668 1.00 84.14 C ANISOU 3761 CE LYS A 520 4715 18430 8824 772 -256 3 C ATOM 3762 NZ LYS A 520 0.631 8.560 142.442 1.00 86.71 N ANISOU 3762 NZ LYS A 520 4853 19036 9059 586 -321 29 N ATOM 3763 N LYS A 521 -0.687 16.027 144.658 1.00 86.33 N ANISOU 3763 N LYS A 521 5192 18558 9053 2365 -463 -140 N ATOM 3764 CA LYS A 521 -0.823 17.354 144.111 1.00 87.04 C ANISOU 3764 CA LYS A 521 5378 18553 9139 2743 -524 -167 C ATOM 3765 C LYS A 521 0.254 18.124 144.824 1.00 91.58 C ANISOU 3765 C LYS A 521 6164 18850 9780 2957 -464 -207 C ATOM 3766 O LYS A 521 0.782 19.093 144.317 1.00 90.78 O ANISOU 3766 O LYS A 521 6250 18516 9726 3199 -525 -216 O ATOM 3767 CB LYS A 521 -2.193 17.943 144.408 1.00 90.49 C ANISOU 3767 CB LYS A 521 5619 19303 9461 2906 -530 -186 C ATOM 3768 CG LYS A 521 -3.262 17.611 143.397 1.00 92.32 C ANISOU 3768 CG LYS A 521 5612 19852 9615 2631 -554 -150 C ATOM 3769 CD LYS A 521 -4.637 17.802 144.005 1.00 95.80 C ANISOU 3769 CD LYS A 521 5844 20622 9934 2783 -536 -173 C ATOM 3770 CE LYS A 521 -5.577 18.518 143.053 1.00 97.31 C ANISOU 3770 CE LYS A 521 6073 20797 10103 3138 -628 -190 C ATOM 3771 NZ LYS A 521 -5.590 19.995 143.249 1.00100.92 N ANISOU 3771 NZ LYS A 521 6281 21627 10436 3197 -646 -194 N ATOM 3772 N ALA A 522 0.567 17.664 146.029 1.00 97.84 N ANISOU 3772 N ALA A 522 6947 19649 10579 2850 -347 -226 N ATOM 3773 CA ALA A 522 1.577 18.328 146.844 1.00 95.22 C ANISOU 3773 CA ALA A 522 6824 19042 10312 3017 -287 -264 C ATOM 3774 C ALA A 522 2.980 18.189 146.271 1.00 89.65 C ANISOU 3774 C ALA A 522 6332 18009 9722 2952 -325 -241 C ATOM 3775 O ALA A 522 3.864 18.951 146.666 1.00 88.21 O ANISOU 3775 O ALA A 522 6355 17563 9596 3137 -304 -271 O ATOM 3776 CB ALA A 522 1.550 17.826 148.283 1.00 96.04 C ANISOU 3776 CB ALA A 522 6864 19235 10390 2895 -157 -284 C ATOM 3777 N ILE A 523 3.207 17.262 145.348 1.00 83.68 N ANISOU 3777 N ILE A 523 5538 17261 8995 2696 -382 -193 N ATOM 3778 CA ILE A 523 4.529 17.113 144.757 1.00 79.76 C ANISOU 3778 CA ILE A 523 5234 16471 8599 2634 -423 -173 C ATOM 3779 C ILE A 523 4.679 17.965 143.500 1.00 77.03 C ANISOU 3779 C ILE A 523 5006 15997 8264 2840 -551 -159 C ATOM 3780 O ILE A 523 5.713 18.610 143.306 1.00 74.49 O ANISOU 3780 O ILE A 523 4907 15387 8009 2987 -577 -163 O ATOM 3781 CB ILE A 523 4.793 15.620 144.481 1.00 75.01 C ANISOU 3781 CB ILE A 523 4549 15926 8024 2234 -416 -134 C ATOM 3782 CG1 ILE A 523 4.871 14.853 145.803 1.00 74.66 C ANISOU 3782 CG1 ILE A 523 4443 15941 7981 2042 -287 -139 C ATOM 3783 CG2 ILE A 523 6.055 15.439 143.664 1.00 72.49 C ANISOU 3783 CG2 ILE A 523 4421 15325 7795 2162 -476 -115 C ATOM 3784 CD1 ILE A 523 4.972 13.353 145.650 1.00 74.03 C ANISOU 3784 CD1 ILE A 523 4281 15929 7919 1632 -275 -98 C ATOM 3785 N GLN A 524 3.654 18.004 142.642 1.00 84.51 N ANISOU 3785 N GLN A 524 5814 17154 9140 2853 -633 -140 N ATOM 3786 CA GLN A 524 3.776 18.711 141.369 1.00 85.90 C ANISOU 3786 CA GLN A 524 6099 17221 9320 3016 -762 -115 C ATOM 3787 C GLN A 524 3.770 20.220 141.557 1.00 86.01 C ANISOU 3787 C GLN A 524 6265 17085 9330 3402 -781 -142 C ATOM 3788 O GLN A 524 4.436 20.937 140.801 1.00 85.70 O ANISOU 3788 O GLN A 524 6424 16810 9328 3554 -864 -121 O ATOM 3789 CB GLN A 524 2.664 18.277 140.409 1.00 87.38 C ANISOU 3789 CB GLN A 524 6089 17683 9427 2906 -844 -86 C ATOM 3790 CG GLN A 524 1.314 18.030 141.061 1.00 91.67 C ANISOU 3790 CG GLN A 524 6416 18539 9876 2981 -804 -107 C ATOM 3791 CD GLN A 524 0.545 16.912 140.380 1.00 96.52 C ANISOU 3791 CD GLN A 524 6797 19453 10424 2697 -830 -80 C ATOM 3792 OE1 GLN A 524 -0.455 16.413 140.902 1.00 99.62 O ANISOU 3792 OE1 GLN A 524 6989 20126 10736 2675 -786 -92 O ATOM 3793 NE2 GLN A 524 1.011 16.511 139.202 1.00 98.62 N ANISOU 3793 NE2 GLN A 524 7095 19660 10717 2471 -905 -46 N ATOM 3794 N LYS A 525 3.119 20.680 142.600 1.00 92.44 N ANISOU 3794 N LYS A 525 7001 18026 10096 3558 -708 -187 N ATOM 3795 CA LYS A 525 3.112 22.080 142.892 1.00 94.18 C ANISOU 3795 CA LYS A 525 7389 18076 10318 3914 -719 -223 C ATOM 3796 C LYS A 525 4.526 22.514 143.180 1.00 93.24 C ANISOU 3796 C LYS A 525 7546 17589 10293 3977 -693 -235 C ATOM 3797 O LYS A 525 4.928 23.587 142.788 1.00 92.38 O ANISOU 3797 O LYS A 525 7653 17240 10208 4222 -753 -238 O ATOM 3798 CB LYS A 525 2.267 22.342 144.124 1.00 99.58 C ANISOU 3798 CB LYS A 525 7941 18963 10931 4041 -633 -281 C ATOM 3799 CG LYS A 525 2.463 23.729 144.724 1.00100.52 C ANISOU 3799 CG LYS A 525 8030 19096 11068 3880 -501 -311 C ATOM 3800 CD LYS A 525 1.339 24.137 145.665 1.00104.78 C ANISOU 3800 CD LYS A 525 8316 19986 11512 3812 -425 -335 C ATOM 3801 CE LYS A 525 1.733 25.353 146.486 1.00109.13 C ANISOU 3801 CE LYS A 525 8815 20669 11980 4116 -427 -387 C ATOM 3802 NZ LYS A 525 1.037 25.373 147.800 1.00112.07 N ANISOU 3802 NZ LYS A 525 8912 21419 12250 3992 -355 -399 N ATOM 3803 N ILE A 526 5.272 21.675 143.894 1.00 86.47 N ANISOU 3803 N ILE A 526 6691 16679 9486 3756 -606 -240 N ATOM 3804 CA ILE A 526 6.648 21.978 144.265 1.00 81.12 C ANISOU 3804 CA ILE A 526 6263 15663 8895 3797 -575 -251 C ATOM 3805 C ILE A 526 7.564 21.835 143.059 1.00 76.64 C ANISOU 3805 C ILE A 526 5839 14896 8384 3728 -673 -197 C ATOM 3806 O ILE A 526 8.366 22.726 142.759 1.00 75.45 O ANISOU 3806 O ILE A 526 5937 14455 8277 3905 -721 -191 O ATOM 3807 CB ILE A 526 7.111 21.078 145.431 1.00 78.13 C ANISOU 3807 CB ILE A 526 5830 15309 8546 3587 -446 -273 C ATOM 3808 CG1 ILE A 526 6.080 21.080 146.571 1.00 78.80 C ANISOU 3808 CG1 ILE A 526 5741 15645 8552 3619 -355 -318 C ATOM 3809 CG2 ILE A 526 8.461 21.542 145.954 1.00 75.90 C ANISOU 3809 CG2 ILE A 526 5808 14686 8344 3669 -407 -295 C ATOM 3810 CD1 ILE A 526 6.600 20.566 147.913 1.00 77.42 C ANISOU 3810 CD1 ILE A 526 5574 15442 8400 3494 -225 -346 C ATOM 3811 N GLN A 527 7.458 20.708 142.347 1.00 72.38 N ANISOU 3811 N GLN A 527 5155 14508 7840 3458 -706 -156 N ATOM 3812 CA GLN A 527 8.257 20.515 141.140 1.00 70.88 C ANISOU 3812 CA GLN A 527 5163 14080 7690 3320 -788 -108 C ATOM 3813 C GLN A 527 8.000 21.615 140.121 1.00 72.14 C ANISOU 3813 C GLN A 527 5394 14202 7814 3596 -920 -78 C ATOM 3814 O GLN A 527 8.899 21.974 139.354 1.00 70.86 O ANISOU 3814 O GLN A 527 5497 13736 7690 3585 -974 -44 O ATOM 3815 CB GLN A 527 7.961 19.147 140.528 1.00 70.71 C ANISOU 3815 CB GLN A 527 4990 14226 7651 2968 -801 -80 C ATOM 3816 CG GLN A 527 8.327 17.981 141.422 1.00 69.39 C ANISOU 3816 CG GLN A 527 4793 14047 7524 2665 -683 -96 C ATOM 3817 CD GLN A 527 8.099 16.643 140.754 1.00 69.28 C ANISOU 3817 CD GLN A 527 4668 14157 7498 2313 -707 -71 C ATOM 3818 OE1 GLN A 527 7.339 16.543 139.795 1.00 70.73 O ANISOU 3818 OE1 GLN A 527 4706 14546 7621 2302 -804 -49 O ATOM 3819 NE2 GLN A 527 8.767 15.606 141.250 1.00 67.65 N ANISOU 3819 NE2 GLN A 527 4539 13818 7347 2023 -625 -74 N ATOM 3820 N LYS A 528 6.787 22.163 140.103 1.00 79.57 N ANISOU 3820 N LYS A 528 6183 15367 8683 3778 -950 -89 N ATOM 3821 CA LYS A 528 6.493 23.273 139.206 1.00 80.07 C ANISOU 3821 CA LYS A 528 6362 15345 8714 4023 -1063 -60 C ATOM 3822 C LYS A 528 7.058 24.583 139.744 1.00 82.87 C ANISOU 3822 C LYS A 528 6978 15403 9106 4305 -1050 -85 C ATOM 3823 O LYS A 528 7.519 25.429 138.970 1.00 83.11 O ANISOU 3823 O LYS A 528 7223 15208 9148 4455 -1143 -46 O ATOM 3824 CB LYS A 528 4.982 23.360 138.980 1.00 82.81 C ANISOU 3824 CB LYS A 528 6480 16013 8973 4085 -1091 -64 C ATOM 3825 CG LYS A 528 4.441 24.744 138.652 1.00 85.74 C ANISOU 3825 CG LYS A 528 6950 16320 9307 4416 -1164 -63 C ATOM 3826 CD LYS A 528 2.922 24.726 138.649 1.00 88.41 C ANISOU 3826 CD LYS A 528 7028 17007 9555 4469 -1169 -78 C ATOM 3827 CE LYS A 528 2.370 26.136 138.602 1.00 89.65 C ANISOU 3827 CE LYS A 528 7281 17103 9681 4819 -1220 -93 C ATOM 3828 NZ LYS A 528 3.378 27.076 138.080 1.00 87.23 N ANISOU 3828 NZ LYS A 528 7293 16422 9430 4974 -1294 -59 N ATOM 3829 N ALA A 529 7.054 24.761 141.065 1.00 76.10 N ANISOU 3829 N ALA A 529 6119 14534 8264 4367 -938 -150 N ATOM 3830 CA ALA A 529 7.683 25.941 141.645 1.00 75.88 C ANISOU 3830 CA ALA A 529 6355 14205 8273 4603 -922 -183 C ATOM 3831 C ALA A 529 9.185 25.934 141.414 1.00 73.16 C ANISOU 3831 C ALA A 529 6264 13526 8009 4536 -935 -154 C ATOM 3832 O ALA A 529 9.804 26.999 141.317 1.00 73.03 O ANISOU 3832 O ALA A 529 6516 13211 8020 4717 -976 -149 O ATOM 3833 CB ALA A 529 7.374 26.020 143.138 1.00 76.46 C ANISOU 3833 CB ALA A 529 6360 14356 8334 4653 -797 -263 C ATOM 3834 N ASN A 530 9.783 24.747 141.327 1.00 71.68 N ANISOU 3834 N ASN A 530 6004 13376 7857 4266 -901 -134 N ATOM 3835 CA ASN A 530 11.204 24.649 141.027 1.00 69.16 C ANISOU 3835 CA ASN A 530 5995 12671 7612 4082 -887 -106 C ATOM 3836 C ASN A 530 11.499 25.139 139.616 1.00 71.90 C ANISOU 3836 C ASN A 530 6507 12863 7947 4118 -1015 -36 C ATOM 3837 O ASN A 530 12.390 25.970 139.411 1.00 69.85 O ANISOU 3837 O ASN A 530 6536 12280 7722 4207 -1046 -16 O ATOM 3838 CB ASN A 530 11.673 23.209 141.211 1.00 73.31 C ANISOU 3838 CB ASN A 530 6465 13214 8174 3696 -801 -105 C ATOM 3839 CG ASN A 530 11.970 22.877 142.657 1.00 69.72 C ANISOU 3839 CG ASN A 530 5991 12744 7754 3635 -668 -161 C ATOM 3840 OD1 ASN A 530 12.479 23.713 143.398 1.00 69.15 O ANISOU 3840 OD1 ASN A 530 6085 12480 7708 3808 -632 -196 O ATOM 3841 ND2 ASN A 530 11.654 21.654 143.065 1.00 68.08 N ANISOU 3841 ND2 ASN A 530 5589 12736 7542 3383 -596 -168 N ATOM 3842 N LYS A 531 10.748 24.642 138.629 1.00 71.51 N ANISOU 3842 N LYS A 531 6279 13050 7843 4043 -1093 4 N ATOM 3843 CA LYS A 531 10.958 25.070 137.252 1.00 70.23 C ANISOU 3843 CA LYS A 531 6257 12772 7655 4072 -1219 74 C ATOM 3844 C LYS A 531 10.606 26.538 137.062 1.00 72.35 C ANISOU 3844 C LYS A 531 6625 12972 7891 4455 -1315 94 C ATOM 3845 O LYS A 531 11.132 27.187 136.151 1.00 73.28 O ANISOU 3845 O LYS A 531 6968 12870 8005 4510 -1406 156 O ATOM 3846 CB LYS A 531 10.137 24.198 136.303 1.00 71.57 C ANISOU 3846 CB LYS A 531 6190 13241 7762 3911 -1283 105 C ATOM 3847 CG LYS A 531 10.402 24.459 134.836 1.00 72.38 C ANISOU 3847 CG LYS A 531 6431 13240 7830 3890 -1407 179 C ATOM 3848 CD LYS A 531 9.604 23.510 133.949 1.00 73.86 C ANISOU 3848 CD LYS A 531 6382 13732 7951 3706 -1466 198 C ATOM 3849 CE LYS A 531 9.790 23.840 132.470 1.00 73.85 C ANISOU 3849 CE LYS A 531 6509 13652 7898 3707 -1597 272 C ATOM 3850 NZ LYS A 531 11.229 23.849 132.087 1.00 71.55 N ANISOU 3850 NZ LYS A 531 6538 12988 7660 3550 -1570 295 N ATOM 3851 N ASP A 532 9.728 27.078 137.911 1.00 73.70 N ANISOU 3851 N ASP A 532 6678 13285 8042 4669 -1279 39 N ATOM 3852 CA ASP A 532 9.290 28.461 137.750 1.00 75.83 C ANISOU 3852 CA ASP A 532 7095 13431 8287 4949 -1341 43 C ATOM 3853 C ASP A 532 10.403 29.447 138.079 1.00 74.84 C ANISOU 3853 C ASP A 532 7315 12903 8219 5072 -1340 43 C ATOM 3854 O ASP A 532 10.557 30.467 137.396 1.00 75.80 O ANISOU 3854 O ASP A 532 7650 12821 8331 5223 -1434 91 O ATOM 3855 CB ASP A 532 8.071 28.731 138.626 1.00 78.15 C ANISOU 3855 CB ASP A 532 7198 13954 8540 5087 -1279 -29 C ATOM 3856 CG ASP A 532 6.777 28.344 137.956 1.00 80.26 C ANISOU 3856 CG ASP A 532 7195 14568 8731 5067 -1331 -9 C ATOM 3857 OD1 ASP A 532 6.632 28.611 136.745 1.00 81.02 O ANISOU 3857 OD1 ASP A 532 7337 14650 8797 5100 -1449 60 O ATOM 3858 OD2 ASP A 532 5.903 27.776 138.641 1.00 81.25 O ANISOU 3858 OD2 ASP A 532 7066 14984 8821 5012 -1256 -59 O ATOM 3859 N GLU A 533 11.184 29.174 139.127 1.00 78.15 N ANISOU 3859 N GLU A 533 7798 13199 8695 5001 -1235 -10 N ATOM 3860 CA GLU A 533 12.201 30.137 139.523 1.00 79.58 C ANISOU 3860 CA GLU A 533 8308 13003 8927 5108 -1230 -18 C ATOM 3861 C GLU A 533 13.446 30.054 138.657 1.00 75.45 C ANISOU 3861 C GLU A 533 8016 12214 8436 4976 -1287 60 C ATOM 3862 O GLU A 533 14.191 31.036 138.572 1.00 74.70 O ANISOU 3862 O GLU A 533 8215 11801 8365 5084 -1329 83 O ATOM 3863 CB GLU A 533 12.561 29.975 141.003 1.00 82.27 C ANISOU 3863 CB GLU A 533 8649 13302 9309 5087 -1096 -107 C ATOM 3864 CG GLU A 533 12.956 28.586 141.453 1.00 81.74 C ANISOU 3864 CG GLU A 533 8417 13368 9272 4821 -999 -123 C ATOM 3865 CD GLU A 533 13.429 28.574 142.903 1.00 80.30 C ANISOU 3865 CD GLU A 533 8283 13098 9129 4812 -874 -202 C ATOM 3866 OE1 GLU A 533 14.219 29.468 143.276 1.00 78.64 O ANISOU 3866 OE1 GLU A 533 8343 12584 8954 4925 -876 -221 O ATOM 3867 OE2 GLU A 533 13.002 27.683 143.671 1.00 82.28 O ANISOU 3867 OE2 GLU A 533 8304 13587 9370 4689 -778 -245 O ATOM 3868 N LYS A 534 13.684 28.922 137.997 1.00 71.80 N ANISOU 3868 N LYS A 534 7467 11838 7977 4663 -1269 95 N ATOM 3869 CA LYS A 534 14.762 28.880 137.020 1.00 71.44 C ANISOU 3869 CA LYS A 534 7660 11534 7950 4470 -1309 166 C ATOM 3870 C LYS A 534 14.446 29.804 135.850 1.00 75.90 C ANISOU 3870 C LYS A 534 8331 12052 8458 4660 -1460 249 C ATOM 3871 O LYS A 534 15.248 30.674 135.497 1.00 76.83 O ANISOU 3871 O LYS A 534 8740 11865 8588 4716 -1510 297 O ATOM 3872 CB LYS A 534 14.988 27.447 136.540 1.00 69.50 C ANISOU 3872 CB LYS A 534 7286 11410 7710 4116 -1262 175 C ATOM 3873 CG LYS A 534 14.872 26.414 137.634 1.00 68.81 C ANISOU 3873 CG LYS A 534 7013 11472 7660 3954 -1132 102 C ATOM 3874 CD LYS A 534 14.689 25.022 137.070 1.00 67.59 C ANISOU 3874 CD LYS A 534 6680 11507 7493 3653 -1114 110 C ATOM 3875 CE LYS A 534 16.016 24.389 136.717 1.00 63.35 C ANISOU 3875 CE LYS A 534 6335 10726 7008 3367 -1068 126 C ATOM 3876 NZ LYS A 534 15.813 23.126 135.961 1.00 61.93 N ANISOU 3876 NZ LYS A 534 6011 10712 6806 3098 -1074 135 N ATOM 3877 N ASP A 535 13.257 29.649 135.254 1.00 82.46 N ANISOU 3877 N ASP A 535 8925 13187 9219 4761 -1539 269 N ATOM 3878 CA ASP A 535 12.795 30.603 134.251 1.00 83.66 C ANISOU 3878 CA ASP A 535 9155 13323 9308 4992 -1691 347 C ATOM 3879 C ASP A 535 12.820 32.026 134.792 1.00 84.54 C ANISOU 3879 C ASP A 535 9495 13183 9445 5236 -1697 327 C ATOM 3880 O ASP A 535 13.262 32.954 134.104 1.00 82.65 O ANISOU 3880 O ASP A 535 9516 12692 9196 5314 -1784 398 O ATOM 3881 CB ASP A 535 11.383 30.242 133.793 1.00 86.65 C ANISOU 3881 CB ASP A 535 9233 14071 9620 5026 -1734 345 C ATOM 3882 CG ASP A 535 11.306 28.869 133.158 1.00 87.50 C ANISOU 3882 CG ASP A 535 9131 14417 9696 4750 -1736 363 C ATOM 3883 OD1 ASP A 535 12.291 28.457 132.514 1.00 86.62 O ANISOU 3883 OD1 ASP A 535 9192 14116 9603 4498 -1726 401 O ATOM 3884 OD2 ASP A 535 10.258 28.204 133.297 1.00 89.36 O ANISOU 3884 OD2 ASP A 535 9059 14998 9896 4722 -1722 328 O ATOM 3885 N ALA A 536 12.348 32.216 136.029 1.00 80.42 N ANISOU 3885 N ALA A 536 8886 12721 8949 5340 -1602 229 N ATOM 3886 CA ALA A 536 12.329 33.550 136.619 1.00 76.62 C ANISOU 3886 CA ALA A 536 8617 12009 8487 5558 -1603 194 C ATOM 3887 C ALA A 536 13.736 34.108 136.753 1.00 75.03 C ANISOU 3887 C ALA A 536 8760 11408 8339 5516 -1602 218 C ATOM 3888 O ALA A 536 13.956 35.310 136.569 1.00 76.30 O ANISOU 3888 O ALA A 536 9178 11309 8503 5652 -1664 245 O ATOM 3889 CB ALA A 536 11.632 33.513 137.975 1.00 77.44 C ANISOU 3889 CB ALA A 536 8553 12274 8597 5648 -1494 78 C ATOM 3890 N ALA A 537 14.704 33.244 137.065 1.00 73.61 N ANISOU 3890 N ALA A 537 8592 11176 8201 5320 -1535 212 N ATOM 3891 CA ALA A 537 16.089 33.680 137.192 1.00 72.35 C ANISOU 3891 CA ALA A 537 8751 10650 8089 5254 -1528 238 C ATOM 3892 C ALA A 537 16.708 33.965 135.834 1.00 70.87 C ANISOU 3892 C ALA A 537 8763 10290 7873 5183 -1641 360 C ATOM 3893 O ALA A 537 17.454 34.937 135.680 1.00 70.81 O ANISOU 3893 O ALA A 537 9063 9962 7880 5221 -1684 401 O ATOM 3894 CB ALA A 537 16.901 32.621 137.928 1.00 68.12 C ANISOU 3894 CB ALA A 537 8165 10108 7611 4982 -1394 186 C ATOM 3895 N MET A 538 16.423 33.116 134.841 1.00 80.03 N ANISOU 3895 N MET A 538 9763 11652 8993 5009 -1669 411 N ATOM 3896 CA MET A 538 16.938 33.341 133.493 1.00 82.30 C ANISOU 3896 CA MET A 538 10225 11805 9239 4904 -1765 524 C ATOM 3897 C MET A 538 16.328 34.595 132.879 1.00 85.06 C ANISOU 3897 C MET A 538 10696 12088 9536 5199 -1910 593 C ATOM 3898 O MET A 538 17.039 35.428 132.305 1.00 82.08 O ANISOU 3898 O MET A 538 10609 11426 9149 5197 -1977 674 O ATOM 3899 CB MET A 538 16.653 32.128 132.607 1.00 87.94 C ANISOU 3899 CB MET A 538 10723 12776 9914 4664 -1763 548 C ATOM 3900 CG MET A 538 17.122 30.803 133.161 1.00 89.28 C ANISOU 3900 CG MET A 538 10757 13029 10136 4362 -1621 477 C ATOM 3901 SD MET A 538 18.853 30.816 133.623 1.00 92.12 S ANISOU 3901 SD MET A 538 11405 13024 10574 4138 -1523 468 S ATOM 3902 CE MET A 538 19.608 31.140 132.035 1.00 92.03 C ANISOU 3902 CE MET A 538 11616 12846 10504 4010 -1621 590 C ATOM 3903 N LEU A 539 15.002 34.733 132.977 1.00 77.52 N ANISOU 3903 N LEU A 539 9524 11374 8555 5353 -1924 553 N ATOM 3904 CA LEU A 539 14.332 35.933 132.487 1.00 77.80 C ANISOU 3904 CA LEU A 539 9666 11335 8559 5556 -2019 593 C ATOM 3905 C LEU A 539 14.960 37.182 133.078 1.00 78.38 C ANISOU 3905 C LEU A 539 10056 11043 8680 5663 -2013 578 C ATOM 3906 O LEU A 539 15.209 38.166 132.372 1.00 79.69 O ANISOU 3906 O LEU A 539 10464 10985 8828 5722 -2107 660 O ATOM 3907 CB LEU A 539 12.844 35.874 132.839 1.00 79.93 C ANISOU 3907 CB LEU A 539 9646 11919 8804 5716 -2006 524 C ATOM 3908 CG LEU A 539 11.778 36.540 131.957 1.00 82.89 C ANISOU 3908 CG LEU A 539 9972 12405 9118 5886 -2120 578 C ATOM 3909 CD1 LEU A 539 10.416 36.298 132.573 1.00 84.62 C ANISOU 3909 CD1 LEU A 539 9880 12954 9317 6015 -2075 488 C ATOM 3910 CD2 LEU A 539 12.007 38.025 131.756 1.00 84.73 C ANISOU 3910 CD2 LEU A 539 10518 12316 9360 6057 -2196 623 C ATOM 3911 N LYS A 540 15.239 37.147 134.376 1.00 77.47 N ANISOU 3911 N LYS A 540 9946 10867 8623 5674 -1903 474 N ATOM 3912 CA LYS A 540 15.803 38.306 135.043 1.00 78.11 C ANISOU 3912 CA LYS A 540 10315 10618 8745 5765 -1893 443 C ATOM 3913 C LYS A 540 17.251 38.528 134.641 1.00 76.45 C ANISOU 3913 C LYS A 540 10410 10080 8557 5595 -1915 521 C ATOM 3914 O LYS A 540 17.665 39.663 134.402 1.00 77.67 O ANISOU 3914 O LYS A 540 10847 9949 8715 5647 -1977 567 O ATOM 3915 CB LYS A 540 15.683 38.122 136.541 1.00 77.60 C ANISOU 3915 CB LYS A 540 10152 10609 8722 5808 -1769 307 C ATOM 3916 CG LYS A 540 16.211 39.259 137.322 1.00 78.32 C ANISOU 3916 CG LYS A 540 10520 10389 8850 5895 -1754 259 C ATOM 3917 CD LYS A 540 15.767 39.091 138.727 1.00 78.42 C ANISOU 3917 CD LYS A 540 10386 10531 8880 5973 -1644 123 C ATOM 3918 CE LYS A 540 16.377 40.131 139.580 1.00 78.96 C ANISOU 3918 CE LYS A 540 10725 10295 8980 6034 -1625 66 C ATOM 3919 NZ LYS A 540 16.838 39.506 140.845 1.00 77.08 N ANISOU 3919 NZ LYS A 540 10420 10090 8779 5938 -1496 -32 N ATOM 3920 N ALA A 541 18.044 37.462 134.566 1.00 73.79 N ANISOU 3920 N ALA A 541 10025 9780 8233 5383 -1865 538 N ATOM 3921 CA ALA A 541 19.400 37.619 134.057 1.00 72.35 C ANISOU 3921 CA ALA A 541 10120 9312 8057 5209 -1890 624 C ATOM 3922 C ALA A 541 19.375 38.196 132.651 1.00 73.74 C ANISOU 3922 C ALA A 541 10438 9410 8170 5209 -2020 757 C ATOM 3923 O ALA A 541 20.215 39.030 132.295 1.00 74.03 O ANISOU 3923 O ALA A 541 10775 9146 8206 5153 -2066 829 O ATOM 3924 CB ALA A 541 20.133 36.280 134.079 1.00 69.50 C ANISOU 3924 CB ALA A 541 9645 9048 7713 4943 -1804 615 C ATOM 3925 N ALA A 542 18.392 37.785 131.851 1.00 74.78 N ANISOU 3925 N ALA A 542 10352 9817 8242 5264 -2081 793 N ATOM 3926 CA ALA A 542 18.299 38.250 130.473 1.00 76.17 C ANISOU 3926 CA ALA A 542 10638 9953 8348 5261 -2207 922 C ATOM 3927 C ALA A 542 18.041 39.751 130.403 1.00 78.82 C ANISOU 3927 C ALA A 542 11197 10062 8691 5437 -2279 952 C ATOM 3928 O ALA A 542 18.718 40.471 129.661 1.00 79.37 O ANISOU 3928 O ALA A 542 11534 9888 8736 5373 -2352 1058 O ATOM 3929 CB ALA A 542 17.203 37.478 129.745 1.00 76.88 C ANISOU 3929 CB ALA A 542 10423 10412 8374 5288 -2253 938 C ATOM 3930 N ASN A 543 17.062 40.245 131.167 1.00 80.64 N ANISOU 3930 N ASN A 543 11321 10372 8946 5657 -2260 859 N ATOM 3931 CA ASN A 543 16.736 41.664 131.093 1.00 83.43 C ANISOU 3931 CA ASN A 543 11876 10523 9300 5843 -2336 881 C ATOM 3932 C ASN A 543 17.833 42.506 131.714 1.00 83.03 C ANISOU 3932 C ASN A 543 12148 10099 9301 5789 -2308 868 C ATOM 3933 O ASN A 543 18.126 43.604 131.232 1.00 84.71 O ANISOU 3933 O ASN A 543 12625 10058 9504 5824 -2391 944 O ATOM 3934 CB ASN A 543 15.403 41.963 131.772 1.00 85.61 C ANISOU 3934 CB ASN A 543 11954 10993 9580 6097 -2321 779 C ATOM 3935 CG ASN A 543 14.335 40.944 131.448 1.00 85.68 C ANISOU 3935 CG ASN A 543 11597 11411 9546 6118 -2317 762 C ATOM 3936 OD1 ASN A 543 13.512 40.617 132.303 1.00 86.11 O ANISOU 3936 OD1 ASN A 543 11420 11687 9612 6225 -2246 652 O ATOM 3937 ND2 ASN A 543 14.334 40.441 130.215 1.00 85.37 N ANISOU 3937 ND2 ASN A 543 11503 11484 9451 6007 -2392 870 N ATOM 3938 N GLN A 544 18.439 42.018 132.792 1.00 80.95 N ANISOU 3938 N GLN A 544 11867 9799 9090 5698 -2194 773 N ATOM 3939 CA GLN A 544 19.544 42.740 133.407 1.00 80.44 C ANISOU 3939 CA GLN A 544 12099 9393 9072 5618 -2164 757 C ATOM 3940 C GLN A 544 20.734 42.828 132.468 1.00 85.94 C ANISOU 3940 C GLN A 544 13034 9871 9748 5395 -2213 889 C ATOM 3941 O GLN A 544 21.450 43.834 132.462 1.00 86.50 O ANISOU 3941 O GLN A 544 13400 9636 9832 5354 -2248 928 O ATOM 3942 CB GLN A 544 19.935 42.056 134.714 1.00 78.31 C ANISOU 3942 CB GLN A 544 11732 9165 8857 5551 -2030 632 C ATOM 3943 CG GLN A 544 18.801 42.007 135.729 1.00 79.43 C ANISOU 3943 CG GLN A 544 11647 9523 9011 5758 -1972 499 C ATOM 3944 CD GLN A 544 19.176 42.636 137.035 1.00 79.61 C ANISOU 3944 CD GLN A 544 11808 9362 9078 5805 -1905 389 C ATOM 3945 OE1 GLN A 544 20.354 42.658 137.423 1.00 77.96 O ANISOU 3945 OE1 GLN A 544 11784 8932 8905 5637 -1862 387 O ATOM 3946 NE2 GLN A 544 18.175 43.147 137.741 1.00 81.70 N ANISOU 3946 NE2 GLN A 544 11981 9727 9334 6030 -1893 293 N ATOM 3947 N TYR A 545 20.946 41.799 131.658 1.00 93.50 N ANISOU 3947 N TYR A 545 13869 10992 10667 5242 -2218 960 N ATOM 3948 CA TYR A 545 22.094 41.756 130.752 1.00 96.54 C ANISOU 3948 CA TYR A 545 14461 11205 11016 5013 -2255 1085 C ATOM 3949 C TYR A 545 21.712 42.324 129.390 1.00 99.91 C ANISOU 3949 C TYR A 545 14966 11627 11368 5048 -2384 1221 C ATOM 3950 O TYR A 545 22.118 43.433 129.034 1.00102.95 O ANISOU 3950 O TYR A 545 15620 11752 11746 5042 -2449 1295 O ATOM 3951 CB TYR A 545 22.608 40.321 130.645 1.00 98.36 C ANISOU 3951 CB TYR A 545 14530 11608 11233 4823 -2189 1083 C ATOM 3952 CG TYR A 545 23.915 40.187 129.908 1.00100.72 C ANISOU 3952 CG TYR A 545 15041 11734 11495 4569 -2203 1193 C ATOM 3953 CD1 TYR A 545 24.995 41.001 130.217 1.00101.99 C ANISOU 3953 CD1 TYR A 545 15496 11570 11687 4457 -2188 1215 C ATOM 3954 CD2 TYR A 545 24.076 39.235 128.913 1.00100.52 C ANISOU 3954 CD2 TYR A 545 14895 11893 11407 4383 -2204 1254 C ATOM 3955 CE1 TYR A 545 26.194 40.879 129.548 1.00101.76 C ANISOU 3955 CE1 TYR A 545 15650 11400 11616 4209 -2194 1317 C ATOM 3956 CE2 TYR A 545 25.271 39.104 128.240 1.00100.34 C ANISOU 3956 CE2 TYR A 545 15026 11743 11355 4087 -2177 1330 C ATOM 3957 CZ TYR A 545 26.326 39.928 128.563 1.00101.39 C ANISOU 3957 CZ TYR A 545 15456 11556 11511 4009 -2175 1366 C ATOM 3958 OH TYR A 545 27.522 39.808 127.899 1.00101.74 O ANISOU 3958 OH TYR A 545 15641 11495 11520 3711 -2145 1443 O ATOM 3959 N ASN A 546 20.917 41.570 128.626 1.00 95.22 N ANISOU 3959 N ASN A 546 14135 11328 10716 5080 -2424 1254 N ATOM 3960 CA ASN A 546 20.561 41.940 127.262 1.00 92.26 C ANISOU 3960 CA ASN A 546 13809 10988 10259 5092 -2546 1388 C ATOM 3961 C ASN A 546 19.487 43.011 127.189 1.00 92.87 C ANISOU 3961 C ASN A 546 13898 11051 10338 5349 -2627 1389 C ATOM 3962 O ASN A 546 19.384 43.702 126.169 1.00 91.91 O ANISOU 3962 O ASN A 546 13912 10847 10161 5368 -2735 1510 O ATOM 3963 CB ASN A 546 20.065 40.709 126.505 1.00 89.29 C ANISOU 3963 CB ASN A 546 13160 10952 9813 5027 -2561 1411 C ATOM 3964 CG ASN A 546 21.040 40.243 125.467 1.00 86.02 C ANISOU 3964 CG ASN A 546 12863 10500 9321 4779 -2589 1527 C ATOM 3965 OD1 ASN A 546 22.120 40.810 125.320 1.00 84.74 O ANISOU 3965 OD1 ASN A 546 12979 10060 9159 4642 -2590 1594 O ATOM 3966 ND2 ASN A 546 20.668 39.205 124.730 1.00 84.90 N ANISOU 3966 ND2 ASN A 546 12507 10647 9104 4707 -2611 1548 N ATOM 3967 N GLY A 547 18.681 43.160 128.233 1.00 89.37 N ANISOU 3967 N GLY A 547 13315 10691 9949 5549 -2578 1260 N ATOM 3968 CA GLY A 547 17.426 43.858 128.115 1.00 91.10 C ANISOU 3968 CA GLY A 547 13453 11006 10155 5808 -2650 1248 C ATOM 3969 C GLY A 547 16.336 43.046 127.460 1.00 88.72 C ANISOU 3969 C GLY A 547 12836 11077 9797 5866 -2687 1261 C ATOM 3970 O GLY A 547 15.156 43.372 127.627 1.00 90.23 O ANISOU 3970 O GLY A 547 12877 11423 9984 6090 -2716 1214 O ATOM 3971 N LYS A 548 16.691 41.996 126.724 1.00 86.12 N ANISOU 3971 N LYS A 548 12401 10904 9418 5668 -2686 1319 N ATOM 3972 CA LYS A 548 15.711 41.103 126.132 1.00 86.37 C ANISOU 3972 CA LYS A 548 12119 11307 9391 5687 -2716 1321 C ATOM 3973 C LYS A 548 15.271 40.074 127.170 1.00 84.82 C ANISOU 3973 C LYS A 548 11628 11363 9236 5692 -2600 1179 C ATOM 3974 O LYS A 548 15.712 40.086 128.320 1.00 83.61 O ANISOU 3974 O LYS A 548 11520 11094 9155 5692 -2501 1084 O ATOM 3975 CB LYS A 548 16.282 40.438 124.880 1.00 85.19 C ANISOU 3975 CB LYS A 548 11992 11220 9157 5466 -2771 1440 C ATOM 3976 N ALA A 549 14.382 39.170 126.764 1.00 92.78 N ANISOU 3976 N ALA A 549 12328 12727 10197 5685 -2613 1165 N ATOM 3977 CA ALA A 549 13.815 38.179 127.666 1.00 92.05 C ANISOU 3977 CA ALA A 549 11928 12913 10134 5682 -2511 1040 C ATOM 3978 C ALA A 549 14.486 36.818 127.534 1.00 89.73 C ANISOU 3978 C ALA A 549 11520 12747 9826 5429 -2454 1035 C ATOM 3979 O ALA A 549 13.919 35.810 127.968 1.00 89.03 O ANISOU 3979 O ALA A 549 11137 12948 9740 5386 -2391 955 O ATOM 3980 CB ALA A 549 12.310 38.053 127.431 1.00 93.99 C ANISOU 3980 CB ALA A 549 11884 13489 10338 5834 -2553 1014 C ATOM 3981 N GLU A 550 15.682 36.770 126.952 1.00 90.27 N ANISOU 3981 N GLU A 550 11816 12609 9872 5255 -2476 1118 N ATOM 3982 CA GLU A 550 16.382 35.518 126.718 1.00 90.69 C ANISOU 3982 CA GLU A 550 11787 12772 9898 5017 -2433 1120 C ATOM 3983 C GLU A 550 17.875 35.797 126.637 1.00 88.76 C ANISOU 3983 C GLU A 550 11857 12190 9676 4833 -2398 1169 C ATOM 3984 O GLU A 550 18.299 36.846 126.147 1.00 89.12 O ANISOU 3984 O GLU A 550 12180 11986 9695 4901 -2482 1267 O ATOM 3985 CB GLU A 550 15.883 34.839 125.438 1.00 96.06 C ANISOU 3985 CB GLU A 550 12305 13720 10472 4921 -2520 1187 C ATOM 3986 CG GLU A 550 16.693 33.644 124.980 1.00 96.69 C ANISOU 3986 CG GLU A 550 12343 13845 10550 4533 -2427 1167 C ATOM 3987 CD GLU A 550 15.852 32.645 124.211 1.00 99.03 C ANISOU 3987 CD GLU A 550 12355 14498 10772 4431 -2461 1157 C ATOM 3988 OE1 GLU A 550 14.871 32.131 124.789 1.00100.28 O ANISOU 3988 OE1 GLU A 550 12234 14919 10950 4514 -2437 1077 O ATOM 3989 OE2 GLU A 550 16.159 32.386 123.027 1.00101.67 O ANISOU 3989 OE2 GLU A 550 12746 14858 11025 4264 -2515 1229 O ATOM 3990 N LEU A 551 18.665 34.857 127.137 1.00 84.14 N ANISOU 3990 N LEU A 551 11223 11593 9153 4556 -2253 1091 N ATOM 3991 CA LEU A 551 20.096 35.090 127.011 1.00 80.61 C ANISOU 3991 CA LEU A 551 11054 10847 8728 4346 -2206 1133 C ATOM 3992 C LEU A 551 20.629 34.463 125.725 1.00 79.06 C ANISOU 3992 C LEU A 551 10873 10709 8457 4075 -2220 1204 C ATOM 3993 O LEU A 551 20.203 33.370 125.343 1.00 81.52 O ANISOU 3993 O LEU A 551 10946 11286 8742 3941 -2191 1164 O ATOM 3994 CB LEU A 551 20.844 34.516 128.211 1.00 77.02 C ANISOU 3994 CB LEU A 551 10578 10310 8377 4192 -2046 1021 C ATOM 3995 CG LEU A 551 20.814 35.404 129.454 1.00 75.89 C ANISOU 3995 CG LEU A 551 10548 9986 8303 4417 -2028 967 C ATOM 3996 CD1 LEU A 551 21.517 34.741 130.610 1.00 74.26 C ANISOU 3996 CD1 LEU A 551 10298 9731 8187 4251 -1872 858 C ATOM 3997 CD2 LEU A 551 21.450 36.746 129.155 1.00 75.06 C ANISOU 3997 CD2 LEU A 551 10794 9547 8179 4509 -2117 1064 C ATOM 3998 N PRO A 552 21.558 35.141 125.056 1.00 70.55 N ANISOU 3998 N PRO A 552 10075 9391 7339 3987 -2264 1308 N ATOM 3999 CA PRO A 552 22.139 34.581 123.833 1.00 72.80 C ANISOU 3999 CA PRO A 552 10386 9731 7542 3727 -2270 1373 C ATOM 4000 C PRO A 552 22.880 33.291 124.125 1.00 71.56 C ANISOU 4000 C PRO A 552 10108 9646 7436 3429 -2118 1275 C ATOM 4001 O PRO A 552 23.561 33.167 125.142 1.00 65.74 O ANISOU 4001 O PRO A 552 9414 8772 6792 3362 -2009 1202 O ATOM 4002 CB PRO A 552 23.097 35.680 123.366 1.00 70.58 C ANISOU 4002 CB PRO A 552 10451 9142 7225 3698 -2327 1495 C ATOM 4003 CG PRO A 552 23.447 36.416 124.608 1.00 70.39 C ANISOU 4003 CG PRO A 552 10571 8873 7298 3822 -2284 1450 C ATOM 4004 CD PRO A 552 22.194 36.414 125.429 1.00 71.29 C ANISOU 4004 CD PRO A 552 10481 9146 7458 4097 -2300 1365 C ATOM 4005 N HIS A 553 22.758 32.326 123.214 1.00 73.65 N ANISOU 4005 N HIS A 553 10227 10122 7634 3250 -2115 1272 N ATOM 4006 CA HIS A 553 23.439 31.055 123.413 1.00 72.75 C ANISOU 4006 CA HIS A 553 10003 10075 7563 2974 -1979 1177 C ATOM 4007 C HIS A 553 24.954 31.204 123.431 1.00 70.26 C ANISOU 4007 C HIS A 553 9911 9516 7270 2775 -1900 1198 C ATOM 4008 O HIS A 553 25.646 30.272 123.855 1.00 69.38 O ANISOU 4008 O HIS A 553 9734 9411 7216 2576 -1777 1111 O ATOM 4009 CB HIS A 553 23.020 30.059 122.332 1.00 79.52 C ANISOU 4009 CB HIS A 553 10689 11192 8334 2827 -2005 1171 C ATOM 4010 CG HIS A 553 22.989 28.641 122.806 1.00 84.47 C ANISOU 4010 CG HIS A 553 11097 11979 9020 2651 -1890 1042 C ATOM 4011 ND1 HIS A 553 22.329 28.258 123.954 1.00 87.96 N ANISOU 4011 ND1 HIS A 553 11359 12513 9551 2742 -1836 950 N ATOM 4012 CD2 HIS A 553 23.540 27.515 122.295 1.00 86.35 C ANISOU 4012 CD2 HIS A 553 11275 12296 9238 2390 -1821 991 C ATOM 4013 CE1 HIS A 553 22.474 26.957 124.129 1.00 87.15 C ANISOU 4013 CE1 HIS A 553 11101 12530 9482 2536 -1742 856 C ATOM 4014 NE2 HIS A 553 23.204 26.482 123.135 1.00 86.88 N ANISOU 4014 NE2 HIS A 553 11140 12485 9386 2327 -1733 874 N ATOM 4015 N SER A 554 25.480 32.353 122.999 1.00 72.07 N ANISOU 4015 N SER A 554 10400 9532 7453 2823 -1971 1312 N ATOM 4016 CA SER A 554 26.921 32.574 123.014 1.00 70.46 C ANISOU 4016 CA SER A 554 10405 9104 7260 2629 -1902 1340 C ATOM 4017 C SER A 554 27.485 32.545 124.430 1.00 69.26 C ANISOU 4017 C SER A 554 10275 8804 7236 2622 -1791 1249 C ATOM 4018 O SER A 554 28.660 32.215 124.623 1.00 69.53 O ANISOU 4018 O SER A 554 10384 8735 7301 2414 -1694 1224 O ATOM 4019 CB SER A 554 27.252 33.912 122.350 1.00 73.78 C ANISOU 4019 CB SER A 554 11106 9321 7605 2697 -2012 1490 C ATOM 4020 OG SER A 554 26.914 33.917 120.972 1.00 76.24 O ANISOU 4020 OG SER A 554 11420 9763 7787 2667 -2109 1585 O ATOM 4021 N VAL A 555 26.673 32.886 125.434 1.00 64.90 N ANISOU 4021 N VAL A 555 9655 8250 6753 2849 -1804 1197 N ATOM 4022 CA VAL A 555 27.208 33.035 126.786 1.00 62.11 C ANISOU 4022 CA VAL A 555 9353 7737 6508 2861 -1713 1120 C ATOM 4023 C VAL A 555 27.341 31.716 127.528 1.00 58.81 C ANISOU 4023 C VAL A 555 8719 7460 6165 2718 -1579 992 C ATOM 4024 O VAL A 555 28.037 31.666 128.548 1.00 57.53 O ANISOU 4024 O VAL A 555 8604 7170 6086 2664 -1488 932 O ATOM 4025 CB VAL A 555 26.352 34.001 127.628 1.00 62.40 C ANISOU 4025 CB VAL A 555 9425 7700 6583 3170 -1776 1109 C ATOM 4026 CG1 VAL A 555 26.218 35.345 126.928 1.00 64.65 C ANISOU 4026 CG1 VAL A 555 9948 7818 6798 3327 -1918 1238 C ATOM 4027 CG2 VAL A 555 24.992 33.407 127.915 1.00 62.89 C ANISOU 4027 CG2 VAL A 555 9204 8034 6655 3327 -1785 1038 C ATOM 4028 N PHE A 556 26.718 30.643 127.050 1.00 58.49 N ANISOU 4028 N PHE A 556 8453 7674 6099 2648 -1567 952 N ATOM 4029 CA PHE A 556 26.779 29.352 127.721 1.00 56.71 C ANISOU 4029 CA PHE A 556 8027 7579 5942 2510 -1449 837 C ATOM 4030 C PHE A 556 27.917 28.469 127.223 1.00 55.08 C ANISOU 4030 C PHE A 556 7844 7355 5727 2225 -1367 819 C ATOM 4031 O PHE A 556 27.989 27.305 127.620 1.00 53.70 O ANISOU 4031 O PHE A 556 7512 7290 5602 2096 -1278 729 O ATOM 4032 CB PHE A 556 25.459 28.593 127.552 1.00 57.35 C ANISOU 4032 CB PHE A 556 7843 7947 6002 2576 -1479 793 C ATOM 4033 CG PHE A 556 24.334 29.113 128.397 1.00 58.57 C ANISOU 4033 CG PHE A 556 7898 8169 6187 2840 -1517 767 C ATOM 4034 CD1 PHE A 556 23.514 30.128 127.940 1.00 60.74 C ANISOU 4034 CD1 PHE A 556 8218 8458 6401 3077 -1644 841 C ATOM 4035 CD2 PHE A 556 24.079 28.568 129.640 1.00 57.66 C ANISOU 4035 CD2 PHE A 556 7638 8116 6156 2857 -1425 668 C ATOM 4036 CE1 PHE A 556 22.477 30.599 128.721 1.00 61.99 C ANISOU 4036 CE1 PHE A 556 8276 8693 6585 3336 -1675 809 C ATOM 4037 CE2 PHE A 556 23.037 29.037 130.419 1.00 58.90 C ANISOU 4037 CE2 PHE A 556 7691 8358 6331 3102 -1453 638 C ATOM 4038 CZ PHE A 556 22.241 30.051 129.962 1.00 61.07 C ANISOU 4038 CZ PHE A 556 8007 8649 6547 3347 -1576 704 C ATOM 4039 N HIS A 557 28.793 28.974 126.358 1.00 61.15 N ANISOU 4039 N HIS A 557 8803 7999 6432 2124 -1395 902 N ATOM 4040 CA HIS A 557 29.831 28.129 125.780 1.00 63.10 C ANISOU 4040 CA HIS A 557 9058 8261 6658 1866 -1319 882 C ATOM 4041 C HIS A 557 31.019 28.038 126.724 1.00 61.74 C ANISOU 4041 C HIS A 557 8968 7919 6570 1755 -1209 835 C ATOM 4042 O HIS A 557 31.610 29.056 127.092 1.00 59.43 O ANISOU 4042 O HIS A 557 8864 7423 6292 1798 -1221 887 O ATOM 4043 CB HIS A 557 30.281 28.661 124.420 1.00 72.13 C ANISOU 4043 CB HIS A 557 10354 9370 7682 1791 -1389 992 C ATOM 4044 CG HIS A 557 31.224 27.744 123.701 1.00 77.86 C ANISOU 4044 CG HIS A 557 11063 10154 8366 1542 -1315 964 C ATOM 4045 ND1 HIS A 557 32.561 28.033 123.529 1.00 80.01 N ANISOU 4045 ND1 HIS A 557 11499 10280 8623 1391 -1263 1000 N ATOM 4046 CD2 HIS A 557 31.023 26.538 123.118 1.00 80.64 C ANISOU 4046 CD2 HIS A 557 11255 10698 8687 1419 -1285 897 C ATOM 4047 CE1 HIS A 557 33.142 27.048 122.868 1.00 80.49 C ANISOU 4047 CE1 HIS A 557 11493 10448 8642 1200 -1200 954 C ATOM 4048 NE2 HIS A 557 32.231 26.128 122.608 1.00 80.15 N ANISOU 4048 NE2 HIS A 557 11263 10601 8591 1215 -1213 888 N ATOM 4049 N GLY A 558 31.383 26.813 127.093 1.00 53.81 N ANISOU 4049 N GLY A 558 7828 6997 5620 1608 -1106 738 N ATOM 4050 CA GLY A 558 32.370 26.619 128.133 1.00 52.20 C ANISOU 4050 CA GLY A 558 7666 6661 5505 1524 -1003 683 C ATOM 4051 C GLY A 558 31.899 27.062 129.496 1.00 49.24 C ANISOU 4051 C GLY A 558 7275 6218 5217 1688 -991 646 C ATOM 4052 O GLY A 558 32.722 27.369 130.363 1.00 48.45 O ANISOU 4052 O GLY A 558 7271 5962 5176 1659 -934 628 O ATOM 4053 N HIS A 559 30.584 27.110 129.700 1.00 54.73 N ANISOU 4053 N HIS A 559 7844 7039 5913 1861 -1045 632 N ATOM 4054 CA HIS A 559 29.982 27.626 130.916 1.00 55.04 C ANISOU 4054 CA HIS A 559 7860 7037 6015 2049 -1044 598 C ATOM 4055 C HIS A 559 28.543 27.141 131.013 1.00 57.98 C ANISOU 4055 C HIS A 559 8010 7638 6383 2173 -1075 559 C ATOM 4056 O HIS A 559 27.620 27.941 131.177 1.00 60.88 O ANISOU 4056 O HIS A 559 8371 8029 6732 2393 -1150 583 O ATOM 4057 CB HIS A 559 30.046 29.152 130.935 1.00 58.19 C ANISOU 4057 CB HIS A 559 8474 7245 6390 2211 -1125 675 C ATOM 4058 CG HIS A 559 29.754 29.752 132.274 1.00 59.21 C ANISOU 4058 CG HIS A 559 8628 7284 6587 2383 -1109 628 C ATOM 4059 ND1 HIS A 559 29.992 31.078 132.562 1.00 60.87 N ANISOU 4059 ND1 HIS A 559 9054 7278 6794 2514 -1164 674 N ATOM 4060 CD2 HIS A 559 29.246 29.207 133.403 1.00 57.80 C ANISOU 4060 CD2 HIS A 559 8287 7200 6473 2442 -1043 536 C ATOM 4061 CE1 HIS A 559 29.636 31.324 133.808 1.00 61.04 C ANISOU 4061 CE1 HIS A 559 9047 7270 6876 2656 -1133 605 C ATOM 4062 NE2 HIS A 559 29.181 30.205 134.341 1.00 59.34 N ANISOU 4062 NE2 HIS A 559 8599 7248 6700 2614 -1057 523 N ATOM 4063 N LYS A 560 28.345 25.829 130.904 1.00 54.07 N ANISOU 4063 N LYS A 560 7331 7314 5900 2032 -1021 498 N ATOM 4064 CA LYS A 560 27.010 25.261 130.994 1.00 55.65 C ANISOU 4064 CA LYS A 560 7305 7749 6091 2112 -1046 461 C ATOM 4065 C LYS A 560 26.414 25.396 132.392 1.00 55.20 C ANISOU 4065 C LYS A 560 7154 7718 6100 2257 -1006 404 C ATOM 4066 O LYS A 560 25.196 25.291 132.555 1.00 57.80 O ANISOU 4066 O LYS A 560 7311 8237 6414 2382 -1041 387 O ATOM 4067 CB LYS A 560 27.058 23.796 130.555 1.00 54.54 C ANISOU 4067 CB LYS A 560 7017 7757 5948 1898 -997 408 C ATOM 4068 CG LYS A 560 25.812 22.992 130.877 1.00 54.45 C ANISOU 4068 CG LYS A 560 6759 7986 5944 1925 -999 355 C ATOM 4069 CD LYS A 560 25.998 21.522 130.584 1.00 51.78 C ANISOU 4069 CD LYS A 560 6308 7750 5616 1695 -943 295 C ATOM 4070 CE LYS A 560 25.942 21.226 129.102 1.00 50.28 C ANISOU 4070 CE LYS A 560 6124 7645 5336 1599 -1010 325 C ATOM 4071 NZ LYS A 560 25.280 19.914 128.911 1.00 50.31 N ANISOU 4071 NZ LYS A 560 5934 7847 5333 1464 -999 262 N ATOM 4072 N GLN A 561 27.227 25.657 133.405 1.00 59.78 N ANISOU 4072 N GLN A 561 7841 8127 6748 2246 -934 376 N ATOM 4073 CA GLN A 561 26.676 25.787 134.746 1.00 58.77 C ANISOU 4073 CA GLN A 561 7626 8031 6672 2381 -892 318 C ATOM 4074 C GLN A 561 26.007 27.130 134.984 1.00 61.70 C ANISOU 4074 C GLN A 561 8072 8352 7019 2655 -970 348 C ATOM 4075 O GLN A 561 25.510 27.359 136.089 1.00 60.22 O ANISOU 4075 O GLN A 561 7820 8195 6864 2795 -939 296 O ATOM 4076 CB GLN A 561 27.766 25.557 135.797 1.00 59.11 C ANISOU 4076 CB GLN A 561 7751 7919 6790 2272 -789 272 C ATOM 4077 CG GLN A 561 28.392 24.177 135.746 1.00 59.13 C ANISOU 4077 CG GLN A 561 7670 7970 6827 2026 -707 233 C ATOM 4078 CD GLN A 561 27.377 23.069 135.940 1.00 60.44 C ANISOU 4078 CD GLN A 561 7591 8374 6997 1990 -684 186 C ATOM 4079 OE1 GLN A 561 26.375 23.240 136.632 1.00 63.54 O ANISOU 4079 OE1 GLN A 561 7861 8889 7392 2134 -690 162 O ATOM 4080 NE2 GLN A 561 27.628 21.924 135.317 1.00 60.12 N ANISOU 4080 NE2 GLN A 561 7482 8405 6955 1792 -660 170 N ATOM 4081 N LEU A 562 25.965 28.007 133.979 1.00 58.41 N ANISOU 4081 N LEU A 562 7791 7862 6541 2739 -1072 429 N ATOM 4082 CA LEU A 562 25.391 29.335 134.172 1.00 56.96 C ANISOU 4082 CA LEU A 562 7709 7598 6335 3011 -1156 460 C ATOM 4083 C LEU A 562 23.934 29.261 134.611 1.00 56.38 C ANISOU 4083 C LEU A 562 7413 7759 6250 3216 -1180 417 C ATOM 4084 O LEU A 562 23.495 30.050 135.454 1.00 57.39 O ANISOU 4084 O LEU A 562 7569 7844 6394 3437 -1191 387 O ATOM 4085 CB LEU A 562 25.511 30.152 132.887 1.00 56.26 C ANISOU 4085 CB LEU A 562 7788 7416 6173 3051 -1271 566 C ATOM 4086 CG LEU A 562 26.363 31.420 132.957 1.00 56.73 C ANISOU 4086 CG LEU A 562 8147 7173 6234 3108 -1310 622 C ATOM 4087 CD1 LEU A 562 26.124 32.294 131.734 1.00 58.49 C ANISOU 4087 CD1 LEU A 562 8509 7342 6373 3202 -1442 735 C ATOM 4088 CD2 LEU A 562 26.109 32.189 134.244 1.00 57.34 C ANISOU 4088 CD2 LEU A 562 8279 7146 6361 3316 -1296 565 C ATOM 4089 N ALA A 563 23.167 28.325 134.046 1.00 61.70 N ANISOU 4089 N ALA A 563 7865 8689 6891 3145 -1190 411 N ATOM 4090 CA ALA A 563 21.751 28.224 134.390 1.00 65.63 C ANISOU 4090 CA ALA A 563 8127 9441 7367 3325 -1216 376 C ATOM 4091 C ALA A 563 21.559 28.056 135.889 1.00 66.02 C ANISOU 4091 C ALA A 563 8082 9526 7475 3387 -1120 288 C ATOM 4092 O ALA A 563 20.625 28.613 136.474 1.00 69.30 O ANISOU 4092 O ALA A 563 8408 10044 7878 3629 -1144 259 O ATOM 4093 CB ALA A 563 21.107 27.061 133.634 1.00 66.34 C ANISOU 4093 CB ALA A 563 7989 9798 7418 3175 -1226 374 C ATOM 4094 N THR A 564 22.441 27.296 136.526 1.00 63.99 N ANISOU 4094 N THR A 564 7843 9191 7279 3177 -1012 244 N ATOM 4095 CA THR A 564 22.368 27.081 137.963 1.00 62.90 C ANISOU 4095 CA THR A 564 7628 9080 7192 3210 -916 166 C ATOM 4096 C THR A 564 22.983 28.244 138.732 1.00 63.89 C ANISOU 4096 C THR A 564 7976 8954 7345 3357 -911 153 C ATOM 4097 O THR A 564 22.400 28.720 139.711 1.00 67.26 O ANISOU 4097 O THR A 564 8353 9426 7776 3552 -893 100 O ATOM 4098 CB THR A 564 23.062 25.767 138.304 1.00 61.22 C ANISOU 4098 CB THR A 564 7349 8884 7029 2925 -812 131 C ATOM 4099 OG1 THR A 564 24.260 25.667 137.527 1.00 60.75 O ANISOU 4099 OG1 THR A 564 7470 8632 6979 2746 -816 174 O ATOM 4100 CG2 THR A 564 22.161 24.597 137.956 1.00 61.91 C ANISOU 4100 CG2 THR A 564 7175 9255 7092 2815 -806 117 C ATOM 4101 N LYS A 565 24.148 28.721 138.293 1.00 64.91 N ANISOU 4101 N LYS A 565 8352 8824 7487 3265 -929 199 N ATOM 4102 CA LYS A 565 24.750 29.896 138.910 1.00 66.23 C ANISOU 4102 CA LYS A 565 8754 8736 7673 3392 -940 194 C ATOM 4103 C LYS A 565 23.773 31.058 138.980 1.00 65.40 C ANISOU 4103 C LYS A 565 8679 8640 7530 3715 -1030 197 C ATOM 4104 O LYS A 565 23.741 31.779 139.978 1.00 63.82 O ANISOU 4104 O LYS A 565 8559 8340 7348 3879 -1013 143 O ATOM 4105 CB LYS A 565 25.993 30.310 138.139 1.00 54.11 C ANISOU 4105 CB LYS A 565 7469 6953 6138 3248 -971 264 C ATOM 4106 CG LYS A 565 27.045 29.226 138.070 1.00 51.94 C ANISOU 4106 CG LYS A 565 7176 6659 5899 2948 -883 256 C ATOM 4107 CD LYS A 565 28.413 29.858 138.043 1.00 51.25 C ANISOU 4107 CD LYS A 565 7349 6296 5829 2845 -879 290 C ATOM 4108 CE LYS A 565 29.480 28.824 137.747 1.00 49.33 C ANISOU 4108 CE LYS A 565 7089 6043 5611 2559 -804 292 C ATOM 4109 NZ LYS A 565 30.598 29.417 136.977 1.00 49.19 N ANISOU 4109 NZ LYS A 565 7294 5825 5569 2447 -838 364 N ATOM 4110 N ILE A 566 22.974 31.262 137.925 1.00 69.75 N ANISOU 4110 N ILE A 566 9171 9308 8024 3818 -1129 256 N ATOM 4111 CA ILE A 566 21.996 32.346 137.921 1.00 69.32 C ANISOU 4111 CA ILE A 566 9136 9273 7929 4145 -1224 263 C ATOM 4112 C ILE A 566 20.887 32.058 138.918 1.00 68.29 C ANISOU 4112 C ILE A 566 8757 9392 7800 4309 -1174 173 C ATOM 4113 O ILE A 566 20.342 32.968 139.551 1.00 67.43 O ANISOU 4113 O ILE A 566 8685 9253 7681 4586 -1203 132 O ATOM 4114 CB ILE A 566 21.438 32.550 136.502 1.00 70.68 C ANISOU 4114 CB ILE A 566 9293 9527 8034 4199 -1345 356 C ATOM 4115 CG1 ILE A 566 22.515 33.106 135.580 1.00 70.77 C ANISOU 4115 CG1 ILE A 566 9587 9270 8032 4079 -1403 451 C ATOM 4116 CG2 ILE A 566 20.240 33.479 136.519 1.00 74.37 C ANISOU 4116 CG2 ILE A 566 9719 10081 8459 4552 -1443 357 C ATOM 4117 CD1 ILE A 566 22.120 33.099 134.123 1.00 71.08 C ANISOU 4117 CD1 ILE A 566 9606 9402 7998 4068 -1509 547 C ATOM 4118 N ARG A 567 20.545 30.786 139.085 1.00 60.78 N ANISOU 4118 N ARG A 567 7550 8687 6856 4140 -1097 139 N ATOM 4119 CA ARG A 567 19.429 30.439 139.949 1.00 61.70 C ANISOU 4119 CA ARG A 567 7404 9079 6961 4272 -1050 65 C ATOM 4120 C ARG A 567 19.743 30.740 141.403 1.00 61.36 C ANISOU 4120 C ARG A 567 7418 8941 6956 4344 -961 -21 C ATOM 4121 O ARG A 567 18.938 31.364 142.105 1.00 63.05 O ANISOU 4121 O ARG A 567 7567 9243 7147 4609 -967 -77 O ATOM 4122 CB ARG A 567 19.080 28.972 139.779 1.00 60.68 C ANISOU 4122 CB ARG A 567 7012 9213 6830 4035 -990 57 C ATOM 4123 CG ARG A 567 17.812 28.624 140.461 1.00 61.97 C ANISOU 4123 CG ARG A 567 6886 9696 6964 4161 -958 -1 C ATOM 4124 CD ARG A 567 17.695 27.173 140.684 1.00 60.72 C ANISOU 4124 CD ARG A 567 6511 9740 6820 3895 -871 -22 C ATOM 4125 NE ARG A 567 16.470 26.883 141.407 1.00 62.13 N ANISOU 4125 NE ARG A 567 6407 10236 6962 4009 -836 -75 N ATOM 4126 CZ ARG A 567 15.936 25.670 141.513 1.00 61.85 C ANISOU 4126 CZ ARG A 567 6123 10460 6917 3820 -784 -87 C ATOM 4127 NH1 ARG A 567 16.532 24.607 140.950 1.00 60.18 N ANISOU 4127 NH1 ARG A 567 5921 10212 6733 3513 -763 -56 N ATOM 4128 NH2 ARG A 567 14.791 25.506 142.187 1.00 63.38 N ANISOU 4128 NH2 ARG A 567 6057 10957 7069 3935 -753 -131 N ATOM 4129 N LEU A 568 20.894 30.257 141.889 1.00 60.26 N ANISOU 4129 N LEU A 568 7386 8640 6871 4112 -876 -36 N ATOM 4130 CA LEU A 568 21.342 30.627 143.228 1.00 59.92 C ANISOU 4130 CA LEU A 568 7434 8473 6860 4169 -800 -111 C ATOM 4131 C LEU A 568 21.597 32.122 143.300 1.00 61.46 C ANISOU 4131 C LEU A 568 7897 8407 7048 4401 -876 -112 C ATOM 4132 O LEU A 568 21.299 32.767 144.308 1.00 63.79 O ANISOU 4132 O LEU A 568 8220 8680 7338 4604 -855 -187 O ATOM 4133 CB LEU A 568 22.610 29.853 143.609 1.00 59.53 C ANISOU 4133 CB LEU A 568 7464 8288 6867 3870 -709 -115 C ATOM 4134 CG LEU A 568 22.672 28.334 143.447 1.00 54.88 C ANISOU 4134 CG LEU A 568 6678 7878 6297 3595 -639 -106 C ATOM 4135 CD1 LEU A 568 24.121 27.866 143.426 1.00 52.72 C ANISOU 4135 CD1 LEU A 568 6560 7395 6076 3333 -589 -86 C ATOM 4136 CD2 LEU A 568 21.892 27.623 144.547 1.00 55.08 C ANISOU 4136 CD2 LEU A 568 6458 8153 6316 3609 -551 -174 C ATOM 4137 N TRP A 569 22.155 32.684 142.234 1.00 60.73 N ANISOU 4137 N TRP A 569 8010 8113 6950 4370 -966 -27 N ATOM 4138 CA TRP A 569 22.359 34.123 142.159 1.00 61.84 C ANISOU 4138 CA TRP A 569 8424 7993 7080 4582 -1056 -11 C ATOM 4139 C TRP A 569 21.062 34.894 142.397 1.00 64.44 C ANISOU 4139 C TRP A 569 8671 8448 7366 4945 -1118 -52 C ATOM 4140 O TRP A 569 21.056 35.918 143.089 1.00 66.84 O ANISOU 4140 O TRP A 569 9133 8591 7670 5103 -1126 -107 O ATOM 4141 CB TRP A 569 22.931 34.461 140.793 1.00 61.99 C ANISOU 4141 CB TRP A 569 8625 7845 7083 4483 -1150 104 C ATOM 4142 CG TRP A 569 23.065 35.878 140.559 1.00 63.53 C ANISOU 4142 CG TRP A 569 9097 7780 7260 4685 -1256 140 C ATOM 4143 CD1 TRP A 569 24.057 36.675 141.013 1.00 63.35 C ANISOU 4143 CD1 TRP A 569 9358 7447 7265 4659 -1258 132 C ATOM 4144 CD2 TRP A 569 22.179 36.703 139.809 1.00 65.89 C ANISOU 4144 CD2 TRP A 569 9430 8096 7508 4945 -1385 192 C ATOM 4145 NE1 TRP A 569 23.853 37.960 140.593 1.00 65.49 N ANISOU 4145 NE1 TRP A 569 9845 7529 7507 4849 -1371 174 N ATOM 4146 CE2 TRP A 569 22.702 38.001 139.849 1.00 67.08 C ANISOU 4146 CE2 TRP A 569 9892 7931 7664 4992 -1438 209 C ATOM 4147 CE3 TRP A 569 20.991 36.468 139.104 1.00 67.24 C ANISOU 4147 CE3 TRP A 569 9386 8531 7631 5070 -1443 221 C ATOM 4148 CZ2 TRP A 569 22.088 39.062 139.216 1.00 69.54 C ANISOU 4148 CZ2 TRP A 569 10307 8176 7939 5142 -1539 252 C ATOM 4149 CZ3 TRP A 569 20.380 37.521 138.480 1.00 69.63 C ANISOU 4149 CZ3 TRP A 569 9788 8771 7896 5222 -1542 263 C ATOM 4150 CH2 TRP A 569 20.918 38.804 138.549 1.00 70.79 C ANISOU 4150 CH2 TRP A 569 10249 8595 8054 5265 -1589 278 C ATOM 4151 N HIS A 570 19.953 34.423 141.828 1.00 66.80 N ANISOU 4151 N HIS A 570 8719 9040 7624 5019 -1151 -32 N ATOM 4152 CA HIS A 570 18.671 35.088 142.024 1.00 70.15 C ANISOU 4152 CA HIS A 570 9034 9615 8003 5269 -1185 -76 C ATOM 4153 C HIS A 570 18.138 34.865 143.431 1.00 69.76 C ANISOU 4153 C HIS A 570 8818 9733 7955 5326 -1073 -195 C ATOM 4154 O HIS A 570 17.452 35.736 143.975 1.00 73.07 O ANISOU 4154 O HIS A 570 9260 10158 8346 5507 -1077 -257 O ATOM 4155 CB HIS A 570 17.681 34.586 140.982 1.00 73.93 C ANISOU 4155 CB HIS A 570 9282 10373 8434 5297 -1250 -16 C ATOM 4156 CG HIS A 570 16.286 35.097 141.165 1.00 78.00 C ANISOU 4156 CG HIS A 570 9642 11094 8901 5503 -1269 -62 C ATOM 4157 ND1 HIS A 570 15.888 36.351 140.753 1.00 79.86 N ANISOU 4157 ND1 HIS A 570 10042 11191 9110 5687 -1360 -42 N ATOM 4158 CD2 HIS A 570 15.181 34.505 141.681 1.00 79.29 C ANISOU 4158 CD2 HIS A 570 9496 11599 9033 5548 -1210 -124 C ATOM 4159 CE1 HIS A 570 14.605 36.516 141.023 1.00 81.65 C ANISOU 4159 CE1 HIS A 570 10068 11664 9292 5852 -1356 -94 C ATOM 4160 NE2 HIS A 570 14.152 35.411 141.585 1.00 81.16 N ANISOU 4160 NE2 HIS A 570 9714 11899 9223 5766 -1264 -143 N ATOM 4161 N GLN A 571 18.484 33.730 144.029 1.00 66.61 N ANISOU 4161 N GLN A 571 8252 9477 7581 5175 -973 -227 N ATOM 4162 CA GLN A 571 18.032 33.402 145.378 1.00 67.75 C ANISOU 4162 CA GLN A 571 8242 9782 7717 5205 -861 -333 C ATOM 4163 C GLN A 571 18.765 34.188 146.467 1.00 66.68 C ANISOU 4163 C GLN A 571 8358 9373 7603 5250 -826 -401 C ATOM 4164 O GLN A 571 18.250 34.347 147.574 1.00 68.03 O ANISOU 4164 O GLN A 571 8474 9629 7744 5365 -775 -489 O ATOM 4165 CB GLN A 571 18.172 31.900 145.635 1.00 68.44 C ANISOU 4165 CB GLN A 571 8110 10065 7828 4985 -761 -340 C ATOM 4166 CG GLN A 571 17.098 31.053 144.972 1.00 69.00 C ANISOU 4166 CG GLN A 571 7916 10426 7875 4855 -777 -285 C ATOM 4167 CD GLN A 571 17.416 29.571 145.016 1.00 66.34 C ANISOU 4167 CD GLN A 571 7391 10256 7560 4562 -661 -301 C ATOM 4168 OE1 GLN A 571 18.449 29.161 145.545 1.00 67.96 O ANISOU 4168 OE1 GLN A 571 7534 10519 7768 4561 -565 -371 O ATOM 4169 NE2 GLN A 571 16.525 28.758 144.459 1.00 64.82 N ANISOU 4169 NE2 GLN A 571 7119 10132 7379 4313 -671 -236 N ATOM 4170 N GLN A 572 19.963 34.676 146.157 1.00 65.35 N ANISOU 4170 N GLN A 572 8466 8885 7480 5151 -854 -361 N ATOM 4171 CA GLN A 572 20.744 35.428 147.128 1.00 65.27 C ANISOU 4171 CA GLN A 572 8691 8618 7490 5153 -819 -425 C ATOM 4172 C GLN A 572 20.617 36.928 146.951 1.00 67.49 C ANISOU 4172 C GLN A 572 9216 8675 7750 5314 -909 -429 C ATOM 4173 O GLN A 572 21.536 37.669 147.325 1.00 67.31 O ANISOU 4173 O GLN A 572 9463 8363 7751 5274 -919 -445 O ATOM 4174 CB GLN A 572 22.204 34.993 147.060 1.00 62.79 C ANISOU 4174 CB GLN A 572 8543 8082 7231 4944 -796 -387 C ATOM 4175 CG GLN A 572 22.341 33.510 147.246 1.00 60.74 C ANISOU 4175 CG GLN A 572 8049 8036 6993 4690 -694 -381 C ATOM 4176 CD GLN A 572 23.590 32.953 146.630 1.00 58.53 C ANISOU 4176 CD GLN A 572 7888 7590 6758 4371 -683 -306 C ATOM 4177 OE1 GLN A 572 23.655 31.771 146.330 1.00 57.08 O ANISOU 4177 OE1 GLN A 572 7534 7563 6591 4150 -632 -275 O ATOM 4178 NE2 GLN A 572 24.598 33.795 146.450 1.00 58.36 N ANISOU 4178 NE2 GLN A 572 8162 7254 6756 4343 -731 -279 N ATOM 4179 N GLY A 573 19.495 37.394 146.403 1.00 69.69 N ANISOU 4179 N GLY A 573 9406 9088 7985 5489 -975 -415 N ATOM 4180 CA GLY A 573 19.276 38.805 146.157 1.00 72.07 C ANISOU 4180 CA GLY A 573 9927 9190 8265 5657 -1067 -414 C ATOM 4181 C GLY A 573 20.392 39.423 145.342 1.00 71.48 C ANISOU 4181 C GLY A 573 10167 8771 8222 5555 -1150 -325 C ATOM 4182 O GLY A 573 20.741 40.588 145.538 1.00 72.82 O ANISOU 4182 O GLY A 573 10595 8682 8391 5618 -1198 -341 O ATOM 4183 N GLU A 574 20.971 38.636 144.434 1.00 69.57 N ANISOU 4183 N GLU A 574 9904 8528 8002 5386 -1167 -230 N ATOM 4184 CA GLU A 574 22.082 39.054 143.580 1.00 68.83 C ANISOU 4184 CA GLU A 574 10087 8136 7930 5253 -1238 -131 C ATOM 4185 C GLU A 574 23.263 39.552 144.383 1.00 68.03 C ANISOU 4185 C GLU A 574 10236 7750 7864 5143 -1202 -171 C ATOM 4186 O GLU A 574 24.063 40.352 143.890 1.00 68.35 O ANISOU 4186 O GLU A 574 10554 7507 7911 5072 -1270 -109 O ATOM 4187 CB GLU A 574 21.651 40.133 142.593 1.00 78.15 C ANISOU 4187 CB GLU A 574 11416 9200 9076 5382 -1364 -59 C ATOM 4188 CG GLU A 574 20.441 39.744 141.828 1.00 78.05 C ANISOU 4188 CG GLU A 574 11160 9471 9023 5501 -1407 -24 C ATOM 4189 CD GLU A 574 19.687 40.955 141.339 1.00 80.23 C ANISOU 4189 CD GLU A 574 11544 9677 9264 5706 -1509 -2 C ATOM 4190 OE1 GLU A 574 20.327 41.926 140.881 1.00 81.40 O ANISOU 4190 OE1 GLU A 574 11984 9528 9415 5686 -1586 57 O ATOM 4191 OE2 GLU A 574 18.454 40.947 141.447 1.00 82.60 O ANISOU 4191 OE2 GLU A 574 11636 10220 9528 5884 -1512 -45 O ATOM 4192 N ARG A 575 23.361 39.108 145.627 1.00 68.71 N ANISOU 4192 N ARG A 575 10224 7916 7965 5120 -1097 -273 N ATOM 4193 CA ARG A 575 24.433 39.491 146.519 1.00 67.33 C ANISOU 4193 CA ARG A 575 10255 7507 7818 5011 -1055 -324 C ATOM 4194 C ARG A 575 25.198 38.239 146.907 1.00 65.85 C ANISOU 4194 C ARG A 575 9960 7391 7668 4816 -959 -330 C ATOM 4195 O ARG A 575 24.611 37.163 147.054 1.00 66.82 O ANISOU 4195 O ARG A 575 9806 7792 7789 4822 -896 -350 O ATOM 4196 CB ARG A 575 23.881 40.194 147.759 1.00 69.27 C ANISOU 4196 CB ARG A 575 10505 7774 8040 5171 -1020 -447 C ATOM 4197 CG ARG A 575 24.931 40.840 148.633 1.00 69.21 C ANISOU 4197 CG ARG A 575 10742 7503 8049 5078 -1000 -500 C ATOM 4198 CD ARG A 575 24.317 41.300 149.931 1.00 71.06 C ANISOU 4198 CD ARG A 575 10931 7816 8252 5234 -952 -629 C ATOM 4199 NE ARG A 575 22.986 41.860 149.722 1.00 74.58 N ANISOU 4199 NE ARG A 575 11282 8402 8653 5480 -1000 -652 N ATOM 4200 CZ ARG A 575 22.758 43.102 149.311 1.00 77.13 C ANISOU 4200 CZ ARG A 575 11804 8545 8957 5613 -1099 -638 C ATOM 4201 NH1 ARG A 575 23.776 43.915 149.058 1.00 76.22 N ANISOU 4201 NH1 ARG A 575 11992 8105 8862 5510 -1161 -597 N ATOM 4202 NH2 ARG A 575 21.515 43.532 149.150 1.00 80.96 N ANISOU 4202 NH2 ARG A 575 12182 9179 9399 5845 -1137 -662 N ATOM 4203 N CYS A 576 26.512 38.378 147.029 1.00 63.62 N ANISOU 4203 N CYS A 576 9894 6860 7417 4637 -952 -309 N ATOM 4204 CA CYS A 576 27.331 37.338 147.623 1.00 61.37 C ANISOU 4204 CA CYS A 576 9541 6608 7170 4462 -856 -334 C ATOM 4205 C CYS A 576 27.164 37.358 149.135 1.00 61.48 C ANISOU 4205 C CYS A 576 9491 6692 7178 4513 -768 -459 C ATOM 4206 O CYS A 576 27.396 38.386 149.777 1.00 61.75 O ANISOU 4206 O CYS A 576 9710 6552 7199 4556 -787 -513 O ATOM 4207 CB CYS A 576 28.790 37.546 147.254 1.00 60.68 C ANISOU 4207 CB CYS A 576 9693 6253 7110 4208 -873 -268 C ATOM 4208 SG CYS A 576 29.892 36.779 148.426 1.00 60.57 S ANISOU 4208 SG CYS A 576 9646 6235 7133 3953 -748 -331 S ATOM 4209 N LEU A 577 26.772 36.223 149.705 1.00 59.03 N ANISOU 4209 N LEU A 577 8916 6642 6872 4486 -671 -503 N ATOM 4210 CA LEU A 577 26.373 36.191 151.105 1.00 59.52 C ANISOU 4210 CA LEU A 577 8879 6825 6911 4569 -589 -619 C ATOM 4211 C LEU A 577 27.549 36.154 152.078 1.00 59.64 C ANISOU 4211 C LEU A 577 9037 6675 6948 4420 -529 -668 C ATOM 4212 O LEU A 577 27.325 36.178 153.293 1.00 58.68 O ANISOU 4212 O LEU A 577 8855 6640 6802 4466 -462 -762 O ATOM 4213 CB LEU A 577 25.455 34.998 151.361 1.00 59.01 C ANISOU 4213 CB LEU A 577 8470 7120 6833 4586 -507 -640 C ATOM 4214 CG LEU A 577 24.223 34.911 150.472 1.00 60.29 C ANISOU 4214 CG LEU A 577 8449 7492 6966 4734 -560 -599 C ATOM 4215 CD1 LEU A 577 23.300 33.818 150.958 1.00 60.08 C ANISOU 4215 CD1 LEU A 577 8082 7830 6917 4729 -471 -634 C ATOM 4216 CD2 LEU A 577 23.507 36.238 150.436 1.00 62.92 C ANISOU 4216 CD2 LEU A 577 8894 7755 7259 4936 -636 -627 C ATOM 4217 N TYR A 578 28.786 36.100 151.591 1.00 61.54 N ANISOU 4217 N TYR A 578 9445 6711 7228 4185 -548 -598 N ATOM 4218 CA TYR A 578 29.953 36.215 152.456 1.00 60.63 C ANISOU 4218 CA TYR A 578 9482 6426 7128 4027 -507 -638 C ATOM 4219 C TYR A 578 30.601 37.590 152.367 1.00 61.23 C ANISOU 4219 C TYR A 578 9890 6174 7198 4070 -597 -639 C ATOM 4220 O TYR A 578 31.052 38.122 153.382 1.00 62.82 O ANISOU 4220 O TYR A 578 10210 6271 7388 4047 -577 -714 O ATOM 4221 CB TYR A 578 30.981 35.123 152.125 1.00 58.53 C ANISOU 4221 CB TYR A 578 9148 6185 6906 3691 -452 -565 C ATOM 4222 CG TYR A 578 30.425 33.708 152.199 1.00 58.15 C ANISOU 4222 CG TYR A 578 8786 6442 6867 3602 -366 -556 C ATOM 4223 CD1 TYR A 578 29.330 33.412 152.994 1.00 58.98 C ANISOU 4223 CD1 TYR A 578 8692 6779 6939 3765 -312 -629 C ATOM 4224 CD2 TYR A 578 30.989 32.674 151.468 1.00 57.32 C ANISOU 4224 CD2 TYR A 578 8588 6392 6798 3353 -339 -475 C ATOM 4225 CE1 TYR A 578 28.813 32.136 153.056 1.00 57.04 C ANISOU 4225 CE1 TYR A 578 8170 6804 6697 3667 -239 -614 C ATOM 4226 CE2 TYR A 578 30.474 31.393 151.526 1.00 55.88 C ANISOU 4226 CE2 TYR A 578 8140 6468 6624 3267 -269 -468 C ATOM 4227 CZ TYR A 578 29.387 31.134 152.323 1.00 55.80 C ANISOU 4227 CZ TYR A 578 7943 6677 6582 3417 -221 -533 C ATOM 4228 OH TYR A 578 28.866 29.868 152.400 1.00 55.68 O ANISOU 4228 OH TYR A 578 7672 6914 6571 3316 -154 -520 O ATOM 4229 N THR A 579 30.628 38.193 151.177 1.00 57.92 N ANISOU 4229 N THR A 579 9604 5621 6782 4077 -694 -549 N ATOM 4230 CA THR A 579 31.160 39.544 151.028 1.00 59.41 C ANISOU 4230 CA THR A 579 10082 5531 6959 4057 -780 -533 C ATOM 4231 C THR A 579 30.140 40.598 151.427 1.00 62.02 C ANISOU 4231 C THR A 579 10441 5875 7249 4289 -823 -600 C ATOM 4232 O THR A 579 30.506 41.647 151.966 1.00 63.38 O ANISOU 4232 O THR A 579 10819 5856 7405 4297 -859 -645 O ATOM 4233 CB THR A 579 31.588 39.794 149.583 1.00 59.35 C ANISOU 4233 CB THR A 579 10211 5378 6962 3965 -867 -402 C ATOM 4234 OG1 THR A 579 30.427 39.806 148.741 1.00 60.44 O ANISOU 4234 OG1 THR A 579 10225 5660 7079 4140 -916 -361 O ATOM 4235 CG2 THR A 579 32.551 38.726 149.113 1.00 56.92 C ANISOU 4235 CG2 THR A 579 9855 5083 6687 3724 -822 -333 C ATOM 4236 N GLY A 580 28.863 40.343 151.159 1.00 62.88 N ANISOU 4236 N GLY A 580 10345 6210 7337 4477 -822 -608 N ATOM 4237 CA GLY A 580 27.878 41.400 151.196 1.00 65.59 C ANISOU 4237 CA GLY A 580 10731 6551 7640 4702 -883 -646 C ATOM 4238 C GLY A 580 27.903 42.305 149.986 1.00 66.97 C ANISOU 4238 C GLY A 580 11097 6539 7811 4729 -1003 -550 C ATOM 4239 O GLY A 580 27.357 43.408 150.044 1.00 69.43 O ANISOU 4239 O GLY A 580 11522 6765 8092 4894 -1068 -580 O ATOM 4240 N LYS A 581 28.526 41.874 148.891 1.00 65.59 N ANISOU 4240 N LYS A 581 10962 6297 7660 4572 -1035 -435 N ATOM 4241 CA LYS A 581 28.659 42.676 147.687 1.00 66.79 C ANISOU 4241 CA LYS A 581 11302 6271 7803 4566 -1147 -329 C ATOM 4242 C LYS A 581 27.705 42.186 146.609 1.00 67.01 C ANISOU 4242 C LYS A 581 11148 6494 7817 4673 -1183 -257 C ATOM 4243 O LYS A 581 27.397 40.995 146.520 1.00 65.93 O ANISOU 4243 O LYS A 581 10769 6589 7691 4651 -1122 -253 O ATOM 4244 CB LYS A 581 30.084 42.632 147.142 1.00 66.02 C ANISOU 4244 CB LYS A 581 11399 5955 7730 4299 -1166 -240 C ATOM 4245 CG LYS A 581 31.107 43.323 148.014 1.00 67.73 C ANISOU 4245 CG LYS A 581 11835 5947 7954 4173 -1157 -291 C ATOM 4246 CD LYS A 581 32.487 43.213 147.384 1.00 67.29 C ANISOU 4246 CD LYS A 581 11943 5707 7915 3895 -1174 -193 C ATOM 4247 CE LYS A 581 33.586 43.269 148.440 1.00 66.52 C ANISOU 4247 CE LYS A 581 11952 5489 7834 3724 -1121 -257 C ATOM 4248 NZ LYS A 581 34.879 43.761 147.887 1.00 67.22 N ANISOU 4248 NZ LYS A 581 12277 5341 7923 3477 -1169 -169 N ATOM 4249 N THR A 582 27.257 43.120 145.777 1.00 74.69 N ANISOU 4249 N THR A 582 12245 7371 8764 4783 -1287 -198 N ATOM 4250 CA THR A 582 26.354 42.779 144.690 1.00 73.99 C ANISOU 4250 CA THR A 582 12003 7457 8655 4887 -1336 -123 C ATOM 4251 C THR A 582 27.100 42.055 143.580 1.00 73.95 C ANISOU 4251 C THR A 582 12011 7427 8661 4686 -1355 2 C ATOM 4252 O THR A 582 28.255 42.364 143.271 1.00 74.35 O ANISOU 4252 O THR A 582 12283 7245 8722 4495 -1379 64 O ATOM 4253 CB THR A 582 25.681 44.033 144.133 1.00 77.93 C ANISOU 4253 CB THR A 582 12642 7849 9120 5067 -1446 -93 C ATOM 4254 OG1 THR A 582 26.627 45.106 144.093 1.00 80.04 O ANISOU 4254 OG1 THR A 582 13232 7789 9390 4966 -1504 -63 O ATOM 4255 CG2 THR A 582 24.501 44.431 145.000 1.00 80.86 C ANISOU 4255 CG2 THR A 582 12891 8366 9467 5323 -1427 -211 C ATOM 4256 N ILE A 583 26.429 41.080 142.985 1.00 66.93 N ANISOU 4256 N ILE A 583 10877 6790 7761 4723 -1344 37 N ATOM 4257 CA ILE A 583 26.963 40.318 141.868 1.00 65.33 C ANISOU 4257 CA ILE A 583 10659 6607 7556 4560 -1368 153 C ATOM 4258 C ILE A 583 26.213 40.751 140.615 1.00 67.05 C ANISOU 4258 C ILE A 583 10879 6869 7729 4670 -1477 249 C ATOM 4259 O ILE A 583 25.026 40.442 140.454 1.00 67.91 O ANISOU 4259 O ILE A 583 10763 7225 7815 4836 -1487 228 O ATOM 4260 CB ILE A 583 26.830 38.809 142.102 1.00 63.13 C ANISOU 4260 CB ILE A 583 10102 6588 7297 4503 -1279 125 C ATOM 4261 CG1 ILE A 583 27.546 38.412 143.393 1.00 61.60 C ANISOU 4261 CG1 ILE A 583 9900 6359 7146 4386 -1165 28 C ATOM 4262 CG2 ILE A 583 27.378 38.045 140.917 1.00 61.67 C ANISOU 4262 CG2 ILE A 583 9870 6458 7102 4245 -1281 232 C ATOM 4263 CD1 ILE A 583 27.293 36.986 143.822 1.00 59.77 C ANISOU 4263 CD1 ILE A 583 9349 6425 6936 4251 -1045 -22 C ATOM 4264 N SER A 584 26.892 41.497 139.757 1.00 67.69 N ANISOU 4264 N SER A 584 11210 6720 7791 4569 -1560 356 N ATOM 4265 CA SER A 584 26.288 41.952 138.527 1.00 69.15 C ANISOU 4265 CA SER A 584 11405 6942 7926 4639 -1666 465 C ATOM 4266 C SER A 584 26.256 40.814 137.550 1.00 69.85 C ANISOU 4266 C SER A 584 11364 7186 7992 4503 -1667 555 C ATOM 4267 O SER A 584 27.194 40.058 137.459 1.00 65.08 O ANISOU 4267 O SER A 584 10752 6566 7409 4302 -1599 559 O ATOM 4268 CB SER A 584 27.020 43.153 137.959 1.00 70.81 C ANISOU 4268 CB SER A 584 11937 6850 8117 4582 -1756 549 C ATOM 4269 OG SER A 584 28.215 42.808 137.338 1.00 69.24 O ANISOU 4269 OG SER A 584 11912 6472 7923 4314 -1741 619 O ATOM 4270 N ILE A 585 25.174 40.693 136.808 1.00 75.21 N ANISOU 4270 N ILE A 585 11929 8026 8620 4601 -1743 624 N ATOM 4271 CA ILE A 585 25.060 39.614 135.862 1.00 72.55 C ANISOU 4271 CA ILE A 585 11458 7859 8248 4456 -1746 704 C ATOM 4272 C ILE A 585 26.163 39.763 134.871 1.00 72.86 C ANISOU 4272 C ILE A 585 11732 7694 8257 4215 -1783 824 C ATOM 4273 O ILE A 585 26.656 38.794 134.351 1.00 72.19 O ANISOU 4273 O ILE A 585 11565 7692 8173 3928 -1709 843 O ATOM 4274 CB ILE A 585 23.719 39.569 135.151 1.00 76.09 C ANISOU 4274 CB ILE A 585 11698 8569 8642 4631 -1821 739 C ATOM 4275 CG1 ILE A 585 23.388 38.156 134.689 1.00 78.09 C ANISOU 4275 CG1 ILE A 585 11672 9076 8923 4812 -1760 614 C ATOM 4276 CG2 ILE A 585 23.793 40.398 133.895 1.00 75.81 C ANISOU 4276 CG2 ILE A 585 11509 8722 8573 4378 -1796 799 C ATOM 4277 CD1 ILE A 585 23.022 37.150 135.763 1.00 81.46 C ANISOU 4277 CD1 ILE A 585 12169 9426 9356 5022 -1791 561 C ATOM 4278 N HIS A 586 26.537 40.990 134.590 1.00 76.14 N ANISOU 4278 N HIS A 586 12418 7864 8649 4284 -1880 895 N ATOM 4279 CA HIS A 586 27.600 41.223 133.644 1.00 68.29 C ANISOU 4279 CA HIS A 586 11676 6653 7617 4064 -1922 1017 C ATOM 4280 C HIS A 586 28.882 40.641 134.126 1.00 66.03 C ANISOU 4280 C HIS A 586 11431 6282 7374 3794 -1810 978 C ATOM 4281 O HIS A 586 29.609 40.022 133.379 1.00 64.76 O ANISOU 4281 O HIS A 586 11280 6138 7187 3516 -1775 1044 O ATOM 4282 CB HIS A 586 27.746 42.717 133.411 1.00 70.84 C ANISOU 4282 CB HIS A 586 12252 6729 7936 4123 -2000 1054 C ATOM 4283 CG HIS A 586 26.486 43.338 132.922 1.00 73.31 C ANISOU 4283 CG HIS A 586 12490 7144 8221 4374 -2087 1067 C ATOM 4284 ND1 HIS A 586 26.358 43.865 131.660 1.00 73.90 N ANISOU 4284 ND1 HIS A 586 12339 7416 8323 4612 -2061 954 N ATOM 4285 CD2 HIS A 586 25.266 43.429 133.494 1.00 75.41 C ANISOU 4285 CD2 HIS A 586 12868 7354 8431 4416 -2198 1182 C ATOM 4286 CE1 HIS A 586 25.121 44.277 131.484 1.00 76.27 C ANISOU 4286 CE1 HIS A 586 12617 7774 8586 4793 -2153 997 C ATOM 4287 NE2 HIS A 586 24.439 44.029 132.584 1.00 77.21 N ANISOU 4287 NE2 HIS A 586 12941 7738 8657 4684 -2239 1135 N ATOM 4288 N ASP A 587 29.166 40.847 135.389 1.00 67.38 N ANISOU 4288 N ASP A 587 11587 6403 7613 3850 -1736 857 N ATOM 4289 CA ASP A 587 30.377 40.316 135.950 1.00 64.16 C ANISOU 4289 CA ASP A 587 11132 5993 7254 3581 -1606 796 C ATOM 4290 C ASP A 587 30.323 38.811 135.975 1.00 64.34 C ANISOU 4290 C ASP A 587 10821 6332 7294 3454 -1500 744 C ATOM 4291 O ASP A 587 31.260 38.136 135.610 1.00 64.97 O ANISOU 4291 O ASP A 587 10853 6462 7370 3181 -1436 773 O ATOM 4292 CB ASP A 587 30.548 40.824 137.364 1.00 64.39 C ANISOU 4292 CB ASP A 587 11242 5883 7340 3687 -1566 682 C ATOM 4293 CG ASP A 587 31.564 41.910 137.473 1.00 66.36 C ANISOU 4293 CG ASP A 587 11823 5807 7583 3659 -1632 719 C ATOM 4294 OD1 ASP A 587 32.358 42.135 136.541 1.00 66.46 O ANISOU 4294 OD1 ASP A 587 12013 5682 7555 3482 -1682 839 O ATOM 4295 OD2 ASP A 587 31.567 42.544 138.526 1.00 67.45 O ANISOU 4295 OD2 ASP A 587 12011 5863 7754 3770 -1616 618 O ATOM 4296 N LEU A 588 29.197 38.272 136.390 1.00 61.24 N ANISOU 4296 N LEU A 588 10197 6158 6915 3652 -1484 668 N ATOM 4297 CA LEU A 588 29.162 36.853 136.476 1.00 59.46 C ANISOU 4297 CA LEU A 588 9661 6221 6710 3533 -1384 610 C ATOM 4298 C LEU A 588 29.432 36.236 135.139 1.00 58.95 C ANISOU 4298 C LEU A 588 9503 6300 6594 3367 -1403 694 C ATOM 4299 O LEU A 588 30.489 35.643 134.963 1.00 57.15 O ANISOU 4299 O LEU A 588 9089 6241 6386 3175 -1312 658 O ATOM 4300 CB LEU A 588 27.786 36.482 136.948 1.00 60.22 C ANISOU 4300 CB LEU A 588 9535 6526 6818 3784 -1376 523 C ATOM 4301 CG LEU A 588 27.374 35.041 137.097 1.00 58.86 C ANISOU 4301 CG LEU A 588 9031 6672 6660 3696 -1290 467 C ATOM 4302 CD1 LEU A 588 28.291 34.337 138.063 1.00 56.63 C ANISOU 4302 CD1 LEU A 588 8680 6398 6438 3481 -1156 392 C ATOM 4303 CD2 LEU A 588 25.967 35.033 137.629 1.00 60.25 C ANISOU 4303 CD2 LEU A 588 9013 7053 6828 3972 -1309 405 C ATOM 4304 N ILE A 589 28.563 36.434 134.160 1.00 60.56 N ANISOU 4304 N ILE A 589 9840 6439 6731 3437 -1520 804 N ATOM 4305 CA ILE A 589 28.769 35.881 132.819 1.00 60.30 C ANISOU 4305 CA ILE A 589 9730 6546 6635 3287 -1546 885 C ATOM 4306 C ILE A 589 30.015 36.341 132.085 1.00 59.86 C ANISOU 4306 C ILE A 589 9890 6310 6545 3045 -1550 977 C ATOM 4307 O ILE A 589 30.702 35.558 131.471 1.00 58.43 O ANISOU 4307 O ILE A 589 9619 6236 6347 2808 -1488 986 O ATOM 4308 CB ILE A 589 27.630 36.351 131.898 1.00 62.45 C ANISOU 4308 CB ILE A 589 9969 6920 6840 3517 -1675 951 C ATOM 4309 CG1 ILE A 589 26.279 36.049 132.515 1.00 62.27 C ANISOU 4309 CG1 ILE A 589 9622 7210 6826 3620 -1645 873 C ATOM 4310 CG2 ILE A 589 27.724 35.723 130.526 1.00 62.94 C ANISOU 4310 CG2 ILE A 589 10123 6977 6815 3380 -1746 1079 C ATOM 4311 CD1 ILE A 589 25.115 36.187 131.575 1.00 64.32 C ANISOU 4311 CD1 ILE A 589 9808 7610 7022 3841 -1764 926 C ATOM 4312 N ASN A 590 30.269 37.623 132.108 1.00 61.19 N ANISOU 4312 N ASN A 590 10346 6205 6699 3097 -1622 1043 N ATOM 4313 CA ASN A 590 31.404 38.175 131.404 1.00 61.24 C ANISOU 4313 CA ASN A 590 10555 6055 6658 2861 -1634 1145 C ATOM 4314 C ASN A 590 32.787 37.940 131.932 1.00 63.79 C ANISOU 4314 C ASN A 590 10919 6282 7038 2636 -1520 1088 C ATOM 4315 O ASN A 590 33.740 37.823 131.203 1.00 66.21 O ANISOU 4315 O ASN A 590 11274 6573 7311 2382 -1482 1141 O ATOM 4316 CB ASN A 590 31.120 39.609 130.963 1.00 63.68 C ANISOU 4316 CB ASN A 590 11171 6106 6918 2984 -1770 1257 C ATOM 4317 CG ASN A 590 30.057 39.657 129.883 1.00 65.80 C ANISOU 4317 CG ASN A 590 11411 6452 7138 3259 -1894 1308 C ATOM 4318 OD1 ASN A 590 29.038 40.296 130.026 1.00 67.80 O ANISOU 4318 OD1 ASN A 590 11813 6547 7400 3509 -1984 1314 O ATOM 4319 ND2 ASN A 590 30.276 38.920 128.825 1.00 66.30 N ANISOU 4319 ND2 ASN A 590 11283 6761 7145 3221 -1904 1340 N ATOM 4320 N ASN A 591 32.802 37.758 133.249 1.00 72.83 N ANISOU 4320 N ASN A 591 12038 7374 8261 2727 -1466 981 N ATOM 4321 CA ASN A 591 33.967 37.435 134.049 1.00 75.94 C ANISOU 4321 CA ASN A 591 12473 7670 8710 2545 -1367 920 C ATOM 4322 C ASN A 591 33.656 36.359 135.090 1.00 76.99 C ANISOU 4322 C ASN A 591 12352 7986 8916 2572 -1258 786 C ATOM 4323 O ASN A 591 33.693 36.593 136.276 1.00 76.07 O ANISOU 4323 O ASN A 591 12263 7783 8856 2603 -1209 705 O ATOM 4324 CB ASN A 591 34.496 38.701 134.667 1.00 79.63 C ANISOU 4324 CB ASN A 591 13224 7840 9191 2618 -1423 931 C ATOM 4325 CG ASN A 591 34.937 39.678 133.620 1.00 81.97 C ANISOU 4325 CG ASN A 591 13796 7933 9416 2550 -1528 1074 C ATOM 4326 OD1 ASN A 591 34.882 39.381 132.424 1.00 83.65 O ANISOU 4326 OD1 ASN A 591 13987 8235 9561 2450 -1558 1169 O ATOM 4327 ND2 ASN A 591 35.387 40.834 134.044 1.00 82.91 N ANISOU 4327 ND2 ASN A 591 14186 7774 9543 2597 -1587 1090 N ATOM 4328 N SER A 592 33.412 35.162 134.591 1.00 70.88 N ANISOU 4328 N SER A 592 11329 7468 8135 2554 -1222 764 N ATOM 4329 CA SER A 592 33.027 33.987 135.337 1.00 71.05 C ANISOU 4329 CA SER A 592 11100 7678 8217 2571 -1126 650 C ATOM 4330 C SER A 592 34.001 33.495 136.388 1.00 68.77 C ANISOU 4330 C SER A 592 10791 7355 7983 2359 -1012 591 C ATOM 4331 O SER A 592 33.593 32.876 137.346 1.00 65.53 O ANISOU 4331 O SER A 592 10208 7062 7627 2373 -931 498 O ATOM 4332 CB SER A 592 32.765 32.852 134.356 1.00 71.71 C ANISOU 4332 CB SER A 592 10945 8027 8273 2546 -1117 651 C ATOM 4333 OG SER A 592 33.627 32.898 133.247 1.00 74.33 O ANISOU 4333 OG SER A 592 11284 8388 8570 2308 -1093 703 O ATOM 4334 N ASN A 593 35.280 33.738 136.188 1.00 76.10 N ANISOU 4334 N ASN A 593 11880 8140 8893 2161 -1004 649 N ATOM 4335 CA ASN A 593 36.308 33.276 137.097 1.00 75.08 C ANISOU 4335 CA ASN A 593 11784 7931 8811 1988 -917 602 C ATOM 4336 C ASN A 593 36.368 33.905 138.470 1.00 70.23 C ANISOU 4336 C ASN A 593 11187 7243 8256 2126 -892 512 C ATOM 4337 O ASN A 593 37.041 33.415 139.348 1.00 66.81 O ANISOU 4337 O ASN A 593 10615 6895 7875 2066 -800 431 O ATOM 4338 CB ASN A 593 37.643 33.450 136.447 1.00 82.11 C ANISOU 4338 CB ASN A 593 12910 8631 9657 1825 -954 695 C ATOM 4339 CG ASN A 593 37.974 34.876 136.259 1.00 85.88 C ANISOU 4339 CG ASN A 593 13476 8979 10174 1672 -891 658 C ATOM 4340 OD1 ASN A 593 38.739 35.446 137.016 1.00 90.30 O ANISOU 4340 OD1 ASN A 593 13960 9555 10796 1710 -830 565 O ATOM 4341 ND2 ASN A 593 37.381 35.480 135.266 1.00 88.03 N ANISOU 4341 ND2 ASN A 593 13915 9129 10403 1489 -909 739 N ATOM 4342 N GLN A 594 35.686 35.008 138.648 1.00 68.18 N ANISOU 4342 N GLN A 594 11096 6828 7982 2323 -977 524 N ATOM 4343 CA GLN A 594 35.693 35.728 139.895 1.00 64.56 C ANISOU 4343 CA GLN A 594 10720 6247 7565 2432 -962 443 C ATOM 4344 C GLN A 594 34.780 35.095 140.886 1.00 58.94 C ANISOU 4344 C GLN A 594 9787 5715 6891 2587 -902 336 C ATOM 4345 O GLN A 594 34.665 35.542 141.982 1.00 58.54 O ANISOU 4345 O GLN A 594 9790 5589 6865 2714 -893 261 O ATOM 4346 CB GLN A 594 35.166 37.124 139.645 1.00 67.84 C ANISOU 4346 CB GLN A 594 11395 6433 7949 2613 -1077 482 C ATOM 4347 CG GLN A 594 36.189 38.206 139.389 1.00 68.42 C ANISOU 4347 CG GLN A 594 11710 6311 7974 2466 -1148 601 C ATOM 4348 CD GLN A 594 35.526 39.519 139.023 1.00 69.61 C ANISOU 4348 CD GLN A 594 12127 6227 8096 2659 -1272 644 C ATOM 4349 OE1 GLN A 594 34.459 39.845 139.518 1.00 69.63 O ANISOU 4349 OE1 GLN A 594 12122 6222 8113 2924 -1306 578 O ATOM 4350 NE2 GLN A 594 36.158 40.272 138.153 1.00 70.77 N ANISOU 4350 NE2 GLN A 594 12511 6183 8196 2530 -1343 755 N ATOM 4351 N PHE A 595 34.098 34.054 140.486 1.00 50.56 N ANISOU 4351 N PHE A 595 8481 4897 5834 2568 -861 326 N ATOM 4352 CA PHE A 595 33.096 33.430 141.337 1.00 50.35 C ANISOU 4352 CA PHE A 595 8237 5060 5834 2707 -810 237 C ATOM 4353 C PHE A 595 33.255 31.921 141.342 1.00 48.48 C ANISOU 4353 C PHE A 595 7767 5027 5626 2528 -715 210 C ATOM 4354 O PHE A 595 33.797 31.324 140.407 1.00 47.65 O ANISOU 4354 O PHE A 595 7636 4959 5509 2348 -706 262 O ATOM 4355 CB PHE A 595 31.667 33.775 140.909 1.00 52.01 C ANISOU 4355 CB PHE A 595 8368 5384 6008 2956 -885 247 C ATOM 4356 CG PHE A 595 31.482 35.215 140.536 1.00 54.05 C ANISOU 4356 CG PHE A 595 8868 5440 6231 3131 -1001 299 C ATOM 4357 CD1 PHE A 595 31.139 36.161 141.486 1.00 55.38 C ANISOU 4357 CD1 PHE A 595 9152 5483 6406 3343 -1028 238 C ATOM 4358 CD2 PHE A 595 31.651 35.626 139.232 1.00 54.79 C ANISOU 4358 CD2 PHE A 595 9079 5462 6276 3085 -1085 409 C ATOM 4359 CE1 PHE A 595 30.985 37.484 141.135 1.00 57.40 C ANISOU 4359 CE1 PHE A 595 9649 5531 6630 3508 -1141 286 C ATOM 4360 CE2 PHE A 595 31.496 36.948 138.889 1.00 56.79 C ANISOU 4360 CE2 PHE A 595 9569 5513 6495 3241 -1198 466 C ATOM 4361 CZ PHE A 595 31.161 37.869 139.837 1.00 58.10 C ANISOU 4361 CZ PHE A 595 9858 5543 6676 3454 -1228 404 C ATOM 4362 N GLU A 596 32.803 31.322 142.443 1.00 47.94 N ANISOU 4362 N GLU A 596 7540 5083 5592 2579 -644 125 N ATOM 4363 CA GLU A 596 32.809 29.885 142.639 1.00 46.42 C ANISOU 4363 CA GLU A 596 7127 5081 5431 2433 -555 92 C ATOM 4364 C GLU A 596 31.559 29.506 143.412 1.00 46.88 C ANISOU 4364 C GLU A 596 6988 5333 5492 2592 -527 27 C ATOM 4365 O GLU A 596 30.980 30.322 144.130 1.00 48.10 O ANISOU 4365 O GLU A 596 7185 5455 5636 2795 -550 -14 O ATOM 4366 CB GLU A 596 34.065 29.418 143.379 1.00 44.83 C ANISOU 4366 CB GLU A 596 6965 4796 5272 2243 -475 63 C ATOM 4367 CG GLU A 596 35.360 29.897 142.754 1.00 55.47 C ANISOU 4367 CG GLU A 596 8508 5956 6611 2088 -498 123 C ATOM 4368 CD GLU A 596 36.581 29.344 143.460 1.00 51.58 C ANISOU 4368 CD GLU A 596 8024 5416 6160 1901 -419 94 C ATOM 4369 OE1 GLU A 596 36.463 28.922 144.627 1.00 51.70 O ANISOU 4369 OE1 GLU A 596 7952 5485 6208 1924 -358 26 O ATOM 4370 OE2 GLU A 596 37.665 29.326 142.852 1.00 51.31 O ANISOU 4370 OE2 GLU A 596 8078 5299 6119 1730 -416 140 O ATOM 4371 N VAL A 597 31.130 28.262 143.239 1.00 48.45 N ANISOU 4371 N VAL A 597 6970 5739 5702 2497 -480 17 N ATOM 4372 CA VAL A 597 29.976 27.740 143.959 1.00 49.57 C ANISOU 4372 CA VAL A 597 6898 6094 5843 2605 -443 -39 C ATOM 4373 C VAL A 597 30.486 27.063 145.224 1.00 49.23 C ANISOU 4373 C VAL A 597 6800 6063 5842 2502 -344 -97 C ATOM 4374 O VAL A 597 31.061 25.971 145.181 1.00 48.28 O ANISOU 4374 O VAL A 597 6607 5983 5752 2301 -287 -93 O ATOM 4375 CB VAL A 597 29.149 26.779 143.098 1.00 49.22 C ANISOU 4375 CB VAL A 597 6650 6271 5780 2552 -454 -16 C ATOM 4376 CG1 VAL A 597 28.043 26.156 143.931 1.00 49.37 C ANISOU 4376 CG1 VAL A 597 6440 6522 5798 2625 -406 -71 C ATOM 4377 CG2 VAL A 597 28.547 27.524 141.935 1.00 51.02 C ANISOU 4377 CG2 VAL A 597 6927 6502 5957 2680 -559 41 C ATOM 4378 N ASP A 598 30.288 27.726 146.352 1.00 47.49 N ANISOU 4378 N ASP A 598 6622 5804 5618 2648 -327 -153 N ATOM 4379 CA ASP A 598 30.711 27.181 147.624 1.00 46.24 C ANISOU 4379 CA ASP A 598 6417 5664 5488 2569 -238 -207 C ATOM 4380 C ASP A 598 29.699 26.168 148.130 1.00 45.05 C ANISOU 4380 C ASP A 598 6012 5774 5332 2573 -181 -237 C ATOM 4381 O ASP A 598 28.489 26.391 148.064 1.00 46.41 O ANISOU 4381 O ASP A 598 6065 6102 5467 2741 -207 -252 O ATOM 4382 CB ASP A 598 30.880 28.297 148.652 1.00 49.63 C ANISOU 4382 CB ASP A 598 6995 5957 5905 2721 -242 -261 C ATOM 4383 CG ASP A 598 30.836 27.781 150.075 1.00 51.62 C ANISOU 4383 CG ASP A 598 7163 6283 6168 2686 -153 -325 C ATOM 4384 OD1 ASP A 598 31.837 27.183 150.524 1.00 52.79 O ANISOU 4384 OD1 ASP A 598 7374 6336 6348 2512 -110 -322 O ATOM 4385 OD2 ASP A 598 29.800 27.971 150.744 1.00 53.48 O ANISOU 4385 OD2 ASP A 598 7263 6684 6374 2833 -127 -375 O ATOM 4386 N ALA A 599 30.200 25.050 148.638 1.00 43.68 N ANISOU 4386 N ALA A 599 5754 5651 5192 2387 -106 -244 N ATOM 4387 CA ALA A 599 29.391 24.181 149.479 1.00 43.79 C ANISOU 4387 CA ALA A 599 5558 5882 5198 2379 -41 -278 C ATOM 4388 C ALA A 599 29.348 24.788 150.878 1.00 44.34 C ANISOU 4388 C ALA A 599 5665 5934 5249 2504 0 -341 C ATOM 4389 O ALA A 599 30.389 24.931 151.526 1.00 43.51 O ANISOU 4389 O ALA A 599 5689 5676 5165 2430 29 -356 O ATOM 4390 CB ALA A 599 29.968 22.771 149.497 1.00 42.27 C ANISOU 4390 CB ALA A 599 5284 5728 5047 2135 16 -256 C ATOM 4391 N ILE A 600 28.150 25.181 151.322 1.00 45.87 N ANISOU 4391 N ILE A 600 5744 6288 5395 2699 0 -381 N ATOM 4392 CA ILE A 600 28.008 25.930 152.571 1.00 46.74 C ANISOU 4392 CA ILE A 600 5901 6384 5473 2857 30 -453 C ATOM 4393 C ILE A 600 28.615 25.143 153.721 1.00 45.63 C ANISOU 4393 C ILE A 600 5725 6265 5347 2704 118 -473 C ATOM 4394 O ILE A 600 29.588 25.572 154.350 1.00 45.09 O ANISOU 4394 O ILE A 600 5819 6022 5291 2674 131 -497 O ATOM 4395 CB ILE A 600 26.530 26.270 152.833 1.00 48.64 C ANISOU 4395 CB ILE A 600 5977 6848 5654 3084 27 -495 C ATOM 4396 CG1 ILE A 600 25.907 26.923 151.585 1.00 49.75 C ANISOU 4396 CG1 ILE A 600 6137 6984 5782 3226 -69 -462 C ATOM 4397 CG2 ILE A 600 26.404 27.165 154.036 1.00 49.73 C ANISOU 4397 CG2 ILE A 600 6186 6956 5752 3272 53 -580 C ATOM 4398 CD1 ILE A 600 24.396 27.126 151.615 1.00 51.68 C ANISOU 4398 CD1 ILE A 600 6185 7484 5969 3441 -82 -492 C ATOM 4399 N LEU A 601 28.059 23.967 153.998 1.00 59.07 N ANISOU 4399 N LEU A 601 7218 8181 7045 2595 176 -459 N ATOM 4400 CA LEU A 601 28.699 23.006 154.888 1.00 57.16 C ANISOU 4400 CA LEU A 601 6942 7952 6823 2411 250 -454 C ATOM 4401 C LEU A 601 29.613 22.131 154.036 1.00 54.22 C ANISOU 4401 C LEU A 601 6611 7474 6514 2185 238 -391 C ATOM 4402 O LEU A 601 29.111 21.357 153.189 1.00 55.00 O ANISOU 4402 O LEU A 601 6590 7682 6625 2102 224 -351 O ATOM 4403 CB LEU A 601 27.667 22.143 155.595 1.00 55.00 C ANISOU 4403 CB LEU A 601 6434 7952 6510 2390 315 -462 C ATOM 4404 CG LEU A 601 26.417 22.791 156.211 1.00 57.15 C ANISOU 4404 CG LEU A 601 6586 8420 6707 2617 330 -521 C ATOM 4405 CD1 LEU A 601 25.733 21.798 157.125 1.00 57.68 C ANISOU 4405 CD1 LEU A 601 6441 8741 6735 2532 412 -520 C ATOM 4406 CD2 LEU A 601 26.742 24.069 156.945 1.00 58.73 C ANISOU 4406 CD2 LEU A 601 6952 8484 6878 2806 323 -592 C ATOM 4407 N PRO A 602 30.916 22.213 154.198 1.00 45.76 N ANISOU 4407 N PRO A 602 5701 6205 5481 2084 242 -383 N ATOM 4408 CA PRO A 602 31.839 21.627 153.231 1.00 45.86 C ANISOU 4408 CA PRO A 602 5776 6101 5548 1908 220 -331 C ATOM 4409 C PRO A 602 31.560 20.151 152.989 1.00 40.59 C ANISOU 4409 C PRO A 602 4948 5569 4904 1741 254 -296 C ATOM 4410 O PRO A 602 31.133 19.418 153.889 1.00 39.62 O ANISOU 4410 O PRO A 602 4701 5582 4769 1696 309 -302 O ATOM 4411 CB PRO A 602 33.204 21.836 153.893 1.00 39.16 C ANISOU 4411 CB PRO A 602 5083 5073 4724 1830 240 -340 C ATOM 4412 CG PRO A 602 33.006 23.089 154.690 1.00 40.23 C ANISOU 4412 CG PRO A 602 5312 5158 4815 2011 230 -397 C ATOM 4413 CD PRO A 602 31.577 23.037 155.190 1.00 41.50 C ANISOU 4413 CD PRO A 602 5305 5537 4926 2150 255 -429 C ATOM 4414 N LEU A 603 31.776 19.720 151.745 1.00 49.17 N ANISOU 4414 N LEU A 603 6042 6620 6020 1647 216 -258 N ATOM 4415 CA LEU A 603 31.397 18.360 151.365 1.00 51.74 C ANISOU 4415 CA LEU A 603 6225 7070 6365 1497 235 -231 C ATOM 4416 C LEU A 603 32.334 17.320 151.944 1.00 51.01 C ANISOU 4416 C LEU A 603 6148 6915 6317 1323 285 -218 C ATOM 4417 O LEU A 603 31.966 16.147 152.004 1.00 50.68 O ANISOU 4417 O LEU A 603 5991 6977 6288 1202 310 -200 O ATOM 4418 CB LEU A 603 31.355 18.237 149.853 1.00 55.16 C ANISOU 4418 CB LEU A 603 6669 7482 6807 1455 178 -204 C ATOM 4419 CG LEU A 603 30.105 17.484 149.410 1.00 58.48 C ANISOU 4419 CG LEU A 603 6904 8111 7205 1428 168 -194 C ATOM 4420 CD1 LEU A 603 28.931 18.290 149.872 1.00 62.42 C ANISOU 4420 CD1 LEU A 603 7313 8755 7649 1618 160 -217 C ATOM 4421 CD2 LEU A 603 30.088 17.310 147.919 1.00 59.78 C ANISOU 4421 CD2 LEU A 603 7082 8261 7372 1376 110 -171 C ATOM 4422 N SER A 604 33.536 17.731 152.358 1.00 46.89 N ANISOU 4422 N SER A 604 5772 6227 5818 1307 294 -225 N ATOM 4423 CA SER A 604 34.444 16.835 153.057 1.00 44.38 C ANISOU 4423 CA SER A 604 5470 5856 5538 1167 339 -213 C ATOM 4424 C SER A 604 33.805 16.258 154.306 1.00 44.12 C ANISOU 4424 C SER A 604 5321 5961 5481 1156 392 -216 C ATOM 4425 O SER A 604 34.161 15.159 154.739 1.00 44.55 O ANISOU 4425 O SER A 604 5339 6023 5564 1021 425 -192 O ATOM 4426 CB SER A 604 35.704 17.596 153.438 1.00 42.05 C ANISOU 4426 CB SER A 604 5337 5388 5254 1180 336 -225 C ATOM 4427 OG SER A 604 36.071 18.465 152.398 1.00 41.33 O ANISOU 4427 OG SER A 604 5355 5189 5162 1224 285 -222 O ATOM 4428 N ILE A 605 32.875 16.986 154.897 1.00 42.76 N ANISOU 4428 N ILE A 605 5094 5899 5254 1299 401 -245 N ATOM 4429 CA ILE A 605 32.264 16.624 156.160 1.00 43.56 C ANISOU 4429 CA ILE A 605 5088 6145 5316 1305 457 -253 C ATOM 4430 C ILE A 605 30.844 16.119 155.962 1.00 47.08 C ANISOU 4430 C ILE A 605 5347 6813 5728 1311 464 -243 C ATOM 4431 O ILE A 605 30.455 15.098 156.526 1.00 51.98 O ANISOU 4431 O ILE A 605 5855 7555 6341 1198 505 -215 O ATOM 4432 CB ILE A 605 32.295 17.822 157.134 1.00 40.61 C ANISOU 4432 CB ILE A 605 4785 5750 4894 1466 469 -304 C ATOM 4433 CG1 ILE A 605 33.729 18.312 157.291 1.00 40.08 C ANISOU 4433 CG1 ILE A 605 4903 5467 4858 1437 455 -312 C ATOM 4434 CG2 ILE A 605 31.655 17.460 158.461 1.00 39.18 C ANISOU 4434 CG2 ILE A 605 4490 5739 4659 1474 532 -315 C ATOM 4435 CD1 ILE A 605 33.837 19.674 157.880 1.00 38.16 C ANISOU 4435 CD1 ILE A 605 4772 5155 4573 1597 444 -368 C ATOM 4436 N THR A 606 30.056 16.822 155.156 1.00 53.54 N ANISOU 4436 N THR A 606 6130 7691 6522 1437 422 -260 N ATOM 4437 CA THR A 606 28.628 16.559 155.091 1.00 55.35 C ANISOU 4437 CA THR A 606 6167 8160 6705 1476 428 -259 C ATOM 4438 C THR A 606 28.224 15.660 153.937 1.00 58.54 C ANISOU 4438 C THR A 606 6486 8623 7134 1349 394 -221 C ATOM 4439 O THR A 606 27.288 14.873 154.090 1.00 61.40 O ANISOU 4439 O THR A 606 6680 9179 7470 1274 414 -203 O ATOM 4440 CB THR A 606 27.859 17.879 155.005 1.00 57.37 C ANISOU 4440 CB THR A 606 6413 8478 6908 1716 399 -304 C ATOM 4441 OG1 THR A 606 28.257 18.587 153.828 1.00 55.70 O ANISOU 4441 OG1 THR A 606 6326 8114 6723 1778 328 -301 O ATOM 4442 CG2 THR A 606 28.171 18.728 156.216 1.00 59.05 C ANISOU 4442 CG2 THR A 606 6707 8642 7086 1842 435 -353 C ATOM 4443 N PHE A 607 28.907 15.747 152.797 1.00 56.14 N ANISOU 4443 N PHE A 607 6294 8164 6874 1313 343 -210 N ATOM 4444 CA PHE A 607 28.550 14.987 151.600 1.00 57.31 C ANISOU 4444 CA PHE A 607 6377 8360 7039 1203 303 -184 C ATOM 4445 C PHE A 607 27.153 15.357 151.093 1.00 59.10 C ANISOU 4445 C PHE A 607 6455 8792 7210 1312 268 -191 C ATOM 4446 O PHE A 607 26.463 14.542 150.482 1.00 60.74 O ANISOU 4446 O PHE A 607 6539 9128 7411 1207 249 -172 O ATOM 4447 CB PHE A 607 28.670 13.477 151.851 1.00 54.26 C ANISOU 4447 CB PHE A 607 5928 8005 6684 986 337 -155 C ATOM 4448 CG PHE A 607 30.051 13.044 152.292 1.00 51.36 C ANISOU 4448 CG PHE A 607 5700 7443 6371 886 365 -146 C ATOM 4449 CD1 PHE A 607 30.402 13.035 153.636 1.00 51.79 C ANISOU 4449 CD1 PHE A 607 5772 7486 6420 890 419 -145 C ATOM 4450 CD2 PHE A 607 31.000 12.656 151.360 1.00 50.59 C ANISOU 4450 CD2 PHE A 607 5709 7186 6325 796 337 -140 C ATOM 4451 CE1 PHE A 607 31.671 12.646 154.038 1.00 51.69 C ANISOU 4451 CE1 PHE A 607 5879 7306 6454 806 438 -134 C ATOM 4452 CE2 PHE A 607 32.272 12.261 151.755 1.00 49.60 C ANISOU 4452 CE2 PHE A 607 5699 6899 6249 717 361 -133 C ATOM 4453 CZ PHE A 607 32.607 12.258 153.094 1.00 50.66 C ANISOU 4453 CZ PHE A 607 5847 7023 6379 723 408 -128 C ATOM 4454 N ASP A 608 26.744 16.600 151.341 1.00 64.36 N ANISOU 4454 N ASP A 608 7133 9485 7834 1526 253 -220 N ATOM 4455 CA ASP A 608 25.441 17.132 150.947 1.00 65.65 C ANISOU 4455 CA ASP A 608 7159 9844 7940 1676 217 -231 C ATOM 4456 C ASP A 608 25.636 17.980 149.693 1.00 64.57 C ANISOU 4456 C ASP A 608 7134 9592 7808 1777 135 -225 C ATOM 4457 O ASP A 608 25.979 19.162 149.778 1.00 64.08 O ANISOU 4457 O ASP A 608 7206 9403 7739 1943 111 -244 O ATOM 4458 CB ASP A 608 24.844 17.948 152.090 1.00 69.15 C ANISOU 4458 CB ASP A 608 7548 10395 8331 1866 254 -273 C ATOM 4459 CG ASP A 608 23.385 18.314 151.857 1.00 73.29 C ANISOU 4459 CG ASP A 608 7885 11172 8790 2017 228 -286 C ATOM 4460 OD1 ASP A 608 22.508 17.441 151.994 1.00 75.75 O ANISOU 4460 OD1 ASP A 608 7996 11714 9073 1917 253 -270 O ATOM 4461 OD2 ASP A 608 23.100 19.482 151.540 1.00 75.16 O ANISOU 4461 OD2 ASP A 608 8173 11384 9001 2237 180 -312 O ATOM 4462 N ASP A 609 25.412 17.376 148.525 1.00 62.88 N ANISOU 4462 N ASP A 609 6872 9418 7600 1671 88 -196 N ATOM 4463 CA ASP A 609 25.666 18.035 147.252 1.00 61.01 C ANISOU 4463 CA ASP A 609 6743 9075 7361 1733 11 -180 C ATOM 4464 C ASP A 609 24.410 18.671 146.653 1.00 59.64 C ANISOU 4464 C ASP A 609 6453 9080 7129 1902 -53 -178 C ATOM 4465 O ASP A 609 24.369 18.912 145.445 1.00 57.79 O ANISOU 4465 O ASP A 609 6259 8817 6882 1916 -125 -154 O ATOM 4466 CB ASP A 609 26.282 17.042 146.259 1.00 61.30 C ANISOU 4466 CB ASP A 609 6818 9039 7434 1521 -6 -155 C ATOM 4467 CG ASP A 609 27.156 17.720 145.231 1.00 60.00 C ANISOU 4467 CG ASP A 609 6836 8682 7279 1547 -59 -138 C ATOM 4468 OD1 ASP A 609 27.334 18.948 145.337 1.00 60.68 O ANISOU 4468 OD1 ASP A 609 7032 8672 7350 1715 -85 -140 O ATOM 4469 OD2 ASP A 609 27.678 17.036 144.334 1.00 60.50 O ANISOU 4469 OD2 ASP A 609 6938 8689 7362 1398 -75 -125 O ATOM 4470 N SER A 610 23.387 18.935 147.464 1.00 54.83 N ANISOU 4470 N SER A 610 5693 8663 6476 2034 -29 -203 N ATOM 4471 CA SER A 610 22.131 19.483 146.970 1.00 53.95 C ANISOU 4471 CA SER A 610 5443 8752 6305 2207 -88 -204 C ATOM 4472 C SER A 610 22.247 20.989 146.736 1.00 50.93 C ANISOU 4472 C SER A 610 5210 8236 5904 2460 -147 -214 C ATOM 4473 O SER A 610 23.228 21.627 147.112 1.00 50.22 O ANISOU 4473 O SER A 610 5321 7915 5845 2500 -134 -225 O ATOM 4474 CB SER A 610 20.999 19.183 147.952 1.00 52.55 C ANISOU 4474 CB SER A 610 5036 8851 6081 2255 -35 -231 C ATOM 4475 OG SER A 610 21.245 19.763 149.217 1.00 52.54 O ANISOU 4475 OG SER A 610 5088 8799 6075 2374 26 -272 O ATOM 4476 N LEU A 611 21.225 21.554 146.085 1.00 57.36 N ANISOU 4476 N LEU A 611 5928 9198 6667 2631 -218 -206 N ATOM 4477 CA LEU A 611 21.209 22.995 145.844 1.00 59.76 C ANISOU 4477 CA LEU A 611 6376 9381 6951 2889 -284 -211 C ATOM 4478 C LEU A 611 21.207 23.772 147.150 1.00 57.87 C ANISOU 4478 C LEU A 611 6182 9103 6704 3070 -234 -270 C ATOM 4479 O LEU A 611 21.839 24.829 147.258 1.00 57.52 O ANISOU 4479 O LEU A 611 6353 8832 6671 3201 -262 -282 O ATOM 4480 CB LEU A 611 19.985 23.392 145.021 1.00 68.70 C ANISOU 4480 CB LEU A 611 7366 10714 8023 3056 -370 -194 C ATOM 4481 CG LEU A 611 19.955 23.244 143.505 1.00 72.79 C ANISOU 4481 CG LEU A 611 7905 11224 8528 2985 -461 -134 C ATOM 4482 CD1 LEU A 611 19.173 21.989 143.059 1.00 73.91 C ANISOU 4482 CD1 LEU A 611 7804 11632 8648 2804 -458 -121 C ATOM 4483 CD2 LEU A 611 19.369 24.521 142.901 1.00 76.31 C ANISOU 4483 CD2 LEU A 611 8403 11665 8928 3267 -563 -117 C ATOM 4484 N ALA A 612 20.479 23.271 148.146 1.00 56.10 N ANISOU 4484 N ALA A 612 5760 9105 6453 3074 -162 -309 N ATOM 4485 CA ALA A 612 20.343 23.967 149.414 1.00 56.37 C ANISOU 4485 CA ALA A 612 5811 9144 6463 3255 -110 -374 C ATOM 4486 C ALA A 612 21.648 24.025 150.200 1.00 52.43 C ANISOU 4486 C ALA A 612 5516 8392 6012 3156 -54 -392 C ATOM 4487 O ALA A 612 21.704 24.727 151.214 1.00 53.17 O ANISOU 4487 O ALA A 612 5672 8444 6087 3306 -19 -451 O ATOM 4488 CB ALA A 612 19.248 23.304 150.242 1.00 55.14 C ANISOU 4488 CB ALA A 612 5374 9320 6256 3253 -40 -404 C ATOM 4489 N ASN A 613 22.689 23.320 149.762 1.00 50.56 N ANISOU 4489 N ASN A 613 5384 7994 5833 2914 -46 -348 N ATOM 4490 CA ASN A 613 24.020 23.438 150.343 1.00 49.06 C ANISOU 4490 CA ASN A 613 5398 7554 5690 2821 -8 -358 C ATOM 4491 C ASN A 613 24.982 24.115 149.377 1.00 48.37 C ANISOU 4491 C ASN A 613 5547 7197 5636 2813 -79 -323 C ATOM 4492 O ASN A 613 26.157 23.763 149.292 1.00 46.80 O ANISOU 4492 O ASN A 613 5478 6819 5484 2637 -61 -301 O ATOM 4493 CB ASN A 613 24.564 22.075 150.756 1.00 47.54 C ANISOU 4493 CB ASN A 613 5141 7387 5534 2550 65 -338 C ATOM 4494 CG ASN A 613 25.717 22.192 151.719 1.00 46.38 C ANISOU 4494 CG ASN A 613 5153 7052 5419 2489 118 -361 C ATOM 4495 OD1 ASN A 613 25.813 23.169 152.456 1.00 47.01 O ANISOU 4495 OD1 ASN A 613 5328 7057 5476 2655 124 -409 O ATOM 4496 ND2 ASN A 613 26.597 21.205 151.720 1.00 44.81 N ANISOU 4496 ND2 ASN A 613 4984 6773 5269 2257 153 -329 N ATOM 4497 N LYS A 614 24.488 25.095 148.635 1.00 49.67 N ANISOU 4497 N LYS A 614 5764 7336 5771 3005 -163 -313 N ATOM 4498 CA LYS A 614 25.285 25.813 147.655 1.00 49.33 C ANISOU 4498 CA LYS A 614 5943 7053 5746 3006 -239 -269 C ATOM 4499 C LYS A 614 24.889 27.276 147.677 1.00 51.04 C ANISOU 4499 C LYS A 614 6283 7181 5928 3288 -307 -291 C ATOM 4500 O LYS A 614 23.707 27.604 147.796 1.00 52.72 O ANISOU 4500 O LYS A 614 6360 7576 6097 3491 -329 -318 O ATOM 4501 CB LYS A 614 25.078 25.289 146.219 1.00 49.17 C ANISOU 4501 CB LYS A 614 5864 7096 5722 2901 -298 -204 C ATOM 4502 CG LYS A 614 25.139 23.776 146.051 1.00 47.96 C ANISOU 4502 CG LYS A 614 5555 7075 5592 2649 -245 -189 C ATOM 4503 CD LYS A 614 25.954 23.376 144.832 1.00 46.86 C ANISOU 4503 CD LYS A 614 5514 6815 5476 2471 -281 -135 C ATOM 4504 CE LYS A 614 25.537 21.999 144.335 1.00 46.44 C ANISOU 4504 CE LYS A 614 5278 6943 5426 2284 -263 -122 C ATOM 4505 NZ LYS A 614 26.215 20.895 145.062 1.00 44.99 N ANISOU 4505 NZ LYS A 614 5067 6736 5290 2079 -176 -140 N ATOM 4506 N VAL A 615 25.880 28.142 147.528 1.00 50.72 N ANISOU 4506 N VAL A 615 6501 6863 5907 3298 -345 -278 N ATOM 4507 CA VAL A 615 25.660 29.567 147.354 1.00 52.36 C ANISOU 4507 CA VAL A 615 6879 6929 6088 3543 -428 -284 C ATOM 4508 C VAL A 615 26.689 30.087 146.367 1.00 51.81 C ANISOU 4508 C VAL A 615 7047 6601 6036 3447 -495 -214 C ATOM 4509 O VAL A 615 27.833 29.625 146.341 1.00 50.14 O ANISOU 4509 O VAL A 615 6921 6268 5862 3221 -456 -192 O ATOM 4510 CB VAL A 615 25.753 30.340 148.682 1.00 53.06 C ANISOU 4510 CB VAL A 615 7063 6929 6168 3698 -393 -369 C ATOM 4511 CG1 VAL A 615 24.501 30.124 149.516 1.00 54.30 C ANISOU 4511 CG1 VAL A 615 6988 7360 6285 3866 -345 -438 C ATOM 4512 CG2 VAL A 615 27.009 29.931 149.446 1.00 51.27 C ANISOU 4512 CG2 VAL A 615 6936 6563 5983 3486 -319 -386 C ATOM 4513 N LEU A 616 26.276 31.042 145.545 1.00 53.32 N ANISOU 4513 N LEU A 616 7343 6719 6196 3618 -597 -174 N ATOM 4514 CA LEU A 616 27.177 31.718 144.625 1.00 53.68 C ANISOU 4514 CA LEU A 616 7635 6516 6246 3550 -670 -101 C ATOM 4515 C LEU A 616 27.870 32.845 145.377 1.00 55.55 C ANISOU 4515 C LEU A 616 8126 6489 6491 3634 -684 -136 C ATOM 4516 O LEU A 616 27.207 33.723 145.934 1.00 62.95 O ANISOU 4516 O LEU A 616 9110 7402 7406 3888 -718 -189 O ATOM 4517 CB LEU A 616 26.413 32.259 143.418 1.00 56.43 C ANISOU 4517 CB LEU A 616 7993 6898 6549 3695 -782 -34 C ATOM 4518 CG LEU A 616 27.217 33.119 142.446 1.00 55.05 C ANISOU 4518 CG LEU A 616 8087 6466 6364 3654 -870 52 C ATOM 4519 CD1 LEU A 616 28.229 32.270 141.682 1.00 53.18 C ANISOU 4519 CD1 LEU A 616 7858 6204 6143 3346 -837 111 C ATOM 4520 CD2 LEU A 616 26.288 33.848 141.488 1.00 57.08 C ANISOU 4520 CD2 LEU A 616 8365 6754 6569 3866 -989 110 C ATOM 4521 N VAL A 617 29.199 32.811 145.411 1.00 52.34 N ANISOU 4521 N VAL A 617 7880 5892 6115 3423 -660 -113 N ATOM 4522 CA VAL A 617 29.980 33.796 146.144 1.00 52.72 C ANISOU 4522 CA VAL A 617 8171 5687 6172 3457 -670 -147 C ATOM 4523 C VAL A 617 31.187 34.180 145.305 1.00 52.17 C ANISOU 4523 C VAL A 617 8323 5391 6109 3272 -716 -63 C ATOM 4524 O VAL A 617 31.573 33.480 144.369 1.00 51.10 O ANISOU 4524 O VAL A 617 8127 5311 5977 3088 -710 6 O ATOM 4525 CB VAL A 617 30.448 33.283 147.529 1.00 51.58 C ANISOU 4525 CB VAL A 617 7969 5574 6056 3371 -566 -231 C ATOM 4526 CG1 VAL A 617 29.291 32.669 148.318 1.00 51.93 C ANISOU 4526 CG1 VAL A 617 7759 5886 6087 3503 -504 -304 C ATOM 4527 CG2 VAL A 617 31.577 32.284 147.367 1.00 49.42 C ANISOU 4527 CG2 VAL A 617 7662 5295 5819 3066 -502 -195 C ATOM 4528 N TYR A 618 31.778 35.318 145.650 1.00 53.06 N ANISOU 4528 N TYR A 618 8695 5249 6218 3321 -762 -71 N ATOM 4529 CA TYR A 618 33.059 35.696 145.072 1.00 52.56 C ANISOU 4529 CA TYR A 618 8844 4969 6158 3117 -793 2 C ATOM 4530 C TYR A 618 34.113 34.639 145.386 1.00 50.35 C ANISOU 4530 C TYR A 618 8473 4744 5914 2840 -694 -5 C ATOM 4531 O TYR A 618 34.108 34.023 146.454 1.00 49.64 O ANISOU 4531 O TYR A 618 8257 4755 5849 2822 -611 -83 O ATOM 4532 CB TYR A 618 33.503 37.062 145.599 1.00 53.99 C ANISOU 4532 CB TYR A 618 9316 4868 6328 3206 -854 -19 C ATOM 4533 CG TYR A 618 32.786 38.228 144.946 1.00 56.28 C ANISOU 4533 CG TYR A 618 9772 5030 6582 3435 -976 24 C ATOM 4534 CD1 TYR A 618 31.416 38.381 145.063 1.00 59.32 C ANISOU 4534 CD1 TYR A 618 10039 5551 6949 3720 -1005 -19 C ATOM 4535 CD2 TYR A 618 33.481 39.168 144.203 1.00 57.20 C ANISOU 4535 CD2 TYR A 618 10162 4895 6678 3366 -1066 112 C ATOM 4536 CE1 TYR A 618 30.762 39.437 144.467 1.00 59.86 C ANISOU 4536 CE1 TYR A 618 10259 5503 6984 3945 -1123 22 C ATOM 4537 CE2 TYR A 618 32.828 40.228 143.604 1.00 59.42 C ANISOU 4537 CE2 TYR A 618 10608 5046 6924 3578 -1185 160 C ATOM 4538 CZ TYR A 618 31.471 40.357 143.738 1.00 60.74 C ANISOU 4538 CZ TYR A 618 10641 5361 7078 3854 -1209 111 C ATOM 4539 OH TYR A 618 30.819 41.410 143.133 1.00 63.08 O ANISOU 4539 OH TYR A 618 11041 5587 7339 3993 -1306 151 O ATOM 4540 N ALA A 619 35.029 34.435 144.434 1.00 49.56 N ANISOU 4540 N ALA A 619 8436 4583 5810 2626 -705 78 N ATOM 4541 CA ALA A 619 35.962 33.313 144.523 1.00 47.54 C ANISOU 4541 CA ALA A 619 8068 4410 5587 2375 -615 77 C ATOM 4542 C ALA A 619 36.885 33.444 145.728 1.00 46.93 C ANISOU 4542 C ALA A 619 8070 4226 5536 2289 -564 18 C ATOM 4543 O ALA A 619 37.088 32.478 146.468 1.00 45.59 O ANISOU 4543 O ALA A 619 7745 4180 5398 2206 -477 -33 O ATOM 4544 CB ALA A 619 36.778 33.199 143.235 1.00 47.11 C ANISOU 4544 CB ALA A 619 8080 4309 5512 2182 -641 174 C ATOM 4545 N THR A 620 37.457 34.635 145.940 1.00 48.00 N ANISOU 4545 N THR A 620 8454 4127 5655 2302 -621 26 N ATOM 4546 CA THR A 620 38.373 34.821 147.060 1.00 47.56 C ANISOU 4546 CA THR A 620 8485 3967 5617 2209 -581 -31 C ATOM 4547 C THR A 620 37.678 34.594 148.392 1.00 47.58 C ANISOU 4547 C THR A 620 8378 4067 5634 2361 -529 -139 C ATOM 4548 O THR A 620 38.307 34.121 149.345 1.00 46.58 O ANISOU 4548 O THR A 620 8204 3967 5526 2256 -461 -189 O ATOM 4549 CB THR A 620 38.986 36.220 147.046 1.00 49.01 C ANISOU 4549 CB THR A 620 8971 3876 5776 2206 -663 -7 C ATOM 4550 OG1 THR A 620 37.947 37.203 147.110 1.00 50.94 O ANISOU 4550 OG1 THR A 620 9324 4032 5996 2471 -740 -30 O ATOM 4551 CG2 THR A 620 39.828 36.434 145.809 1.00 49.00 C ANISOU 4551 CG2 THR A 620 9082 3784 5753 2017 -706 106 C ATOM 4552 N ALA A 621 36.393 34.932 148.482 1.00 48.83 N ANISOU 4552 N ALA A 621 8490 4289 5774 2611 -560 -173 N ATOM 4553 CA ALA A 621 35.663 34.714 149.723 1.00 49.02 C ANISOU 4553 CA ALA A 621 8395 4433 5799 2762 -505 -277 C ATOM 4554 C ALA A 621 35.404 33.237 149.962 1.00 47.41 C ANISOU 4554 C ALA A 621 7908 4486 5619 2670 -410 -289 C ATOM 4555 O ALA A 621 35.239 32.816 151.109 1.00 47.05 O ANISOU 4555 O ALA A 621 7761 4539 5578 2695 -342 -363 O ATOM 4556 CB ALA A 621 34.347 35.493 149.708 1.00 50.99 C ANISOU 4556 CB ALA A 621 8660 4697 6017 3064 -565 -311 C ATOM 4557 N ASN A 622 35.362 32.435 148.903 1.00 51.41 N ANISOU 4557 N ASN A 622 8293 5102 6138 2559 -405 -218 N ATOM 4558 CA ASN A 622 35.187 30.999 149.074 1.00 50.58 C ANISOU 4558 CA ASN A 622 7942 5218 6059 2451 -321 -226 C ATOM 4559 C ASN A 622 36.501 30.317 149.426 1.00 49.99 C ANISOU 4559 C ASN A 622 7873 5103 6017 2212 -261 -220 C ATOM 4560 O ASN A 622 36.511 29.344 150.186 1.00 46.75 O ANISOU 4560 O ASN A 622 7310 4825 5628 2147 -185 -255 O ATOM 4561 CB ASN A 622 34.577 30.400 147.804 1.00 50.31 C ANISOU 4561 CB ASN A 622 7779 5316 6020 2434 -345 -164 C ATOM 4562 CG ASN A 622 34.592 28.891 147.800 1.00 49.58 C ANISOU 4562 CG ASN A 622 7468 5412 5957 2279 -268 -162 C ATOM 4563 OD1 ASN A 622 34.013 28.251 148.673 1.00 49.36 O ANISOU 4563 OD1 ASN A 622 7283 5534 5936 2317 -209 -214 O ATOM 4564 ND2 ASN A 622 35.236 28.312 146.799 1.00 48.77 N ANISOU 4564 ND2 ASN A 622 7359 5305 5867 2105 -269 -104 N ATOM 4565 N GLN A 623 37.615 30.825 148.905 1.00 49.34 N ANISOU 4565 N GLN A 623 7965 4846 5935 2080 -296 -172 N ATOM 4566 CA GLN A 623 38.906 30.251 149.246 1.00 50.61 C ANISOU 4566 CA GLN A 623 8130 4976 6123 1863 -243 -168 C ATOM 4567 C GLN A 623 39.293 30.579 150.684 1.00 50.61 C ANISOU 4567 C GLN A 623 8190 4915 6123 1881 -214 -239 C ATOM 4568 O GLN A 623 39.853 29.731 151.390 1.00 51.56 O ANISOU 4568 O GLN A 623 8214 5109 6268 1764 -147 -262 O ATOM 4569 CB GLN A 623 39.963 30.745 148.264 1.00 52.00 C ANISOU 4569 CB GLN A 623 8464 5004 6289 1715 -288 -95 C ATOM 4570 CG GLN A 623 39.783 30.206 146.860 1.00 52.80 C ANISOU 4570 CG GLN A 623 8488 5189 6385 1653 -303 -25 C ATOM 4571 CD GLN A 623 39.813 28.700 146.803 1.00 52.23 C ANISOU 4571 CD GLN A 623 8198 5301 6346 1547 -227 -35 C ATOM 4572 OE1 GLN A 623 38.770 28.045 146.700 1.00 54.66 O ANISOU 4572 OE1 GLN A 623 8347 5762 6658 1631 -213 -50 O ATOM 4573 NE2 GLN A 623 41.015 28.135 146.835 1.00 52.12 N ANISOU 4573 NE2 GLN A 623 8178 5274 6353 1358 -183 -24 N ATOM 4574 N GLU A 624 38.992 31.794 151.147 1.00 55.20 N ANISOU 4574 N GLU A 624 8935 5362 6676 2033 -265 -279 N ATOM 4575 CA GLU A 624 39.315 32.120 152.529 1.00 56.02 C ANISOU 4575 CA GLU A 624 9100 5414 6771 2055 -239 -357 C ATOM 4576 C GLU A 624 38.415 31.370 153.500 1.00 50.95 C ANISOU 4576 C GLU A 624 8261 4971 6128 2161 -170 -423 C ATOM 4577 O GLU A 624 38.864 30.978 154.580 1.00 51.66 O ANISOU 4577 O GLU A 624 8311 5097 6218 2097 -115 -468 O ATOM 4578 CB GLU A 624 39.223 33.625 152.764 1.00 60.62 C ANISOU 4578 CB GLU A 624 9924 5788 7319 2193 -316 -391 C ATOM 4579 CG GLU A 624 39.953 34.065 154.016 1.00 63.63 C ANISOU 4579 CG GLU A 624 10421 6068 7688 2151 -302 -462 C ATOM 4580 CD GLU A 624 39.622 35.486 154.424 1.00 68.64 C ANISOU 4580 CD GLU A 624 11282 6513 8284 2327 -373 -521 C ATOM 4581 OE1 GLU A 624 38.853 36.145 153.696 1.00 71.87 O ANISOU 4581 OE1 GLU A 624 11764 6861 8681 2487 -437 -499 O ATOM 4582 OE2 GLU A 624 40.126 35.940 155.477 1.00 70.51 O ANISOU 4582 OE2 GLU A 624 11629 6661 8502 2311 -369 -592 O ATOM 4583 N LYS A 625 37.157 31.144 153.126 1.00 47.95 N ANISOU 4583 N LYS A 625 7748 4731 5739 2314 -172 -423 N ATOM 4584 CA LYS A 625 36.254 30.369 153.969 1.00 45.84 C ANISOU 4584 CA LYS A 625 7275 4679 5464 2396 -103 -476 C ATOM 4585 C LYS A 625 36.820 28.987 154.266 1.00 46.03 C ANISOU 4585 C LYS A 625 7143 4826 5522 2196 -26 -453 C ATOM 4586 O LYS A 625 36.640 28.463 155.370 1.00 47.04 O ANISOU 4586 O LYS A 625 7169 5066 5640 2200 36 -500 O ATOM 4587 CB LYS A 625 34.885 30.255 153.300 1.00 47.49 C ANISOU 4587 CB LYS A 625 7350 5036 5659 2556 -123 -463 C ATOM 4588 CG LYS A 625 33.857 29.450 154.073 1.00 47.18 C ANISOU 4588 CG LYS A 625 7080 5242 5603 2633 -53 -509 C ATOM 4589 CD LYS A 625 32.597 29.297 153.259 1.00 46.34 C ANISOU 4589 CD LYS A 625 6832 5292 5483 2761 -80 -486 C ATOM 4590 CE LYS A 625 31.491 28.605 154.018 1.00 46.27 C ANISOU 4590 CE LYS A 625 6591 5542 5448 2843 -15 -530 C ATOM 4591 NZ LYS A 625 31.415 27.154 153.698 1.00 44.98 N ANISOU 4591 NZ LYS A 625 6229 5547 5313 2658 36 -480 N ATOM 4592 N GLY A 626 37.508 28.385 153.300 1.00 41.00 N ANISOU 4592 N GLY A 626 6489 4169 4920 2024 -31 -383 N ATOM 4593 CA GLY A 626 38.111 27.078 153.459 1.00 39.47 C ANISOU 4593 CA GLY A 626 6165 4069 4762 1841 32 -360 C ATOM 4594 C GLY A 626 37.106 26.017 153.864 1.00 39.25 C ANISOU 4594 C GLY A 626 5918 4260 4736 1875 89 -374 C ATOM 4595 O GLY A 626 35.910 26.096 153.565 1.00 40.10 O ANISOU 4595 O GLY A 626 5936 4477 4823 2010 76 -382 O ATOM 4596 N GLN A 627 37.603 25.001 154.570 1.00 44.37 N ANISOU 4596 N GLN A 627 6476 4977 5407 1745 150 -375 N ATOM 4597 CA GLN A 627 36.779 23.881 155.023 1.00 43.99 C ANISOU 4597 CA GLN A 627 6227 5128 5360 1737 207 -379 C ATOM 4598 C GLN A 627 36.061 24.262 156.319 1.00 45.20 C ANISOU 4598 C GLN A 627 6344 5364 5464 1875 239 -442 C ATOM 4599 O GLN A 627 36.282 23.701 157.393 1.00 44.77 O ANISOU 4599 O GLN A 627 6236 5373 5402 1818 292 -459 O ATOM 4600 CB GLN A 627 37.642 22.642 155.201 1.00 45.43 C ANISOU 4600 CB GLN A 627 6346 5332 5585 1544 252 -346 C ATOM 4601 CG GLN A 627 36.880 21.349 155.443 1.00 48.07 C ANISOU 4601 CG GLN A 627 6487 5849 5928 1496 301 -332 C ATOM 4602 CD GLN A 627 37.793 20.249 155.932 1.00 48.41 C ANISOU 4602 CD GLN A 627 6498 5887 6007 1330 343 -307 C ATOM 4603 OE1 GLN A 627 38.752 20.487 156.663 1.00 49.38 O ANISOU 4603 OE1 GLN A 627 6501 6105 6156 1240 369 -278 O ATOM 4604 NE2 GLN A 627 37.490 19.025 155.532 1.00 49.20 N ANISOU 4604 NE2 GLN A 627 6712 5874 6110 1289 344 -319 N ATOM 4605 N ARG A 628 35.179 25.248 156.207 1.00 44.39 N ANISOU 4605 N ARG A 628 6276 5267 5323 2067 203 -478 N ATOM 4606 CA ARG A 628 34.472 25.755 157.370 1.00 44.57 C ANISOU 4606 CA ARG A 628 6276 5367 5290 2226 230 -551 C ATOM 4607 C ARG A 628 33.056 26.125 156.977 1.00 45.11 C ANISOU 4607 C ARG A 628 6249 5566 5325 2419 210 -570 C ATOM 4608 O ARG A 628 32.766 26.382 155.810 1.00 46.10 O ANISOU 4608 O ARG A 628 6391 5659 5466 2456 154 -533 O ATOM 4609 CB ARG A 628 35.171 26.979 157.979 1.00 43.87 C ANISOU 4609 CB ARG A 628 6402 5088 5178 2294 199 -605 C ATOM 4610 CG ARG A 628 36.491 26.668 158.674 1.00 41.89 C ANISOU 4610 CG ARG A 628 6227 4746 4944 2121 225 -601 C ATOM 4611 CD ARG A 628 37.128 27.908 159.265 1.00 41.85 C ANISOU 4611 CD ARG A 628 6434 4558 4909 2180 188 -660 C ATOM 4612 NE ARG A 628 37.485 28.889 158.252 1.00 42.21 N ANISOU 4612 NE ARG A 628 6657 4411 4970 2204 109 -638 N ATOM 4613 CZ ARG A 628 38.061 30.055 158.515 1.00 43.32 C ANISOU 4613 CZ ARG A 628 7012 4357 5089 2241 59 -677 C ATOM 4614 NH1 ARG A 628 38.351 30.383 159.762 1.00 43.47 N ANISOU 4614 NH1 ARG A 628 7093 4355 5070 2262 80 -749 N ATOM 4615 NH2 ARG A 628 38.346 30.896 157.531 1.00 45.70 N ANISOU 4615 NH2 ARG A 628 7475 4487 5404 2250 -16 -643 N ATOM 4616 N THR A 629 32.176 26.147 157.970 1.00 45.93 N ANISOU 4616 N THR A 629 6245 5831 5375 2544 256 -628 N ATOM 4617 CA THR A 629 30.844 26.704 157.811 1.00 46.90 C ANISOU 4617 CA THR A 629 6284 6082 5453 2768 238 -665 C ATOM 4618 C THR A 629 30.915 28.223 157.924 1.00 48.56 C ANISOU 4618 C THR A 629 6700 6115 5635 2967 179 -728 C ATOM 4619 O THR A 629 31.873 28.763 158.485 1.00 50.07 O ANISOU 4619 O THR A 629 7070 6126 5827 2929 172 -758 O ATOM 4620 CB THR A 629 29.911 26.151 158.880 1.00 48.76 C ANISOU 4620 CB THR A 629 6320 6573 5632 2822 316 -707 C ATOM 4621 OG1 THR A 629 30.241 26.739 160.139 1.00 52.59 O ANISOU 4621 OG1 THR A 629 6901 7010 6073 2893 347 -784 O ATOM 4622 CG2 THR A 629 30.042 24.653 158.984 1.00 48.45 C ANISOU 4622 CG2 THR A 629 6119 6669 5621 2596 374 -645 C ATOM 4623 N PRO A 630 29.918 28.943 157.402 1.00 48.36 N ANISOU 4623 N PRO A 630 6659 6131 5583 3183 130 -748 N ATOM 4624 CA PRO A 630 29.953 30.404 157.545 1.00 51.32 C ANISOU 4624 CA PRO A 630 7248 6321 5931 3388 68 -811 C ATOM 4625 C PRO A 630 30.050 30.845 158.992 1.00 52.68 C ANISOU 4625 C PRO A 630 7475 6489 6052 3474 115 -912 C ATOM 4626 O PRO A 630 30.814 31.768 159.307 1.00 56.27 O ANISOU 4626 O PRO A 630 8163 6714 6503 3500 76 -953 O ATOM 4627 CB PRO A 630 28.644 30.857 156.892 1.00 52.56 C ANISOU 4627 CB PRO A 630 7314 6596 6059 3621 22 -818 C ATOM 4628 CG PRO A 630 28.221 29.719 156.049 1.00 50.56 C ANISOU 4628 CG PRO A 630 6851 6526 5833 3488 37 -736 C ATOM 4629 CD PRO A 630 28.699 28.491 156.725 1.00 48.99 C ANISOU 4629 CD PRO A 630 6532 6432 5651 3259 125 -719 C ATOM 4630 N TYR A 631 29.306 30.192 159.887 1.00 57.45 N ANISOU 4630 N TYR A 631 7872 7347 6609 3507 197 -952 N ATOM 4631 CA TYR A 631 29.387 30.524 161.304 1.00 58.39 C ANISOU 4631 CA TYR A 631 8029 7490 6667 3579 250 -1049 C ATOM 4632 C TYR A 631 30.820 30.433 161.806 1.00 58.99 C ANISOU 4632 C TYR A 631 8267 7378 6770 3375 257 -1040 C ATOM 4633 O TYR A 631 31.349 31.391 162.380 1.00 59.35 O ANISOU 4633 O TYR A 631 8515 7245 6789 3445 230 -1111 O ATOM 4634 CB TYR A 631 28.482 29.604 162.115 1.00 60.45 C ANISOU 4634 CB TYR A 631 8020 8074 6873 3583 346 -1067 C ATOM 4635 CG TYR A 631 28.706 29.739 163.599 1.00 61.54 C ANISOU 4635 CG TYR A 631 8185 8252 6943 3605 410 -1153 C ATOM 4636 CD1 TYR A 631 28.399 30.920 164.261 1.00 63.37 C ANISOU 4636 CD1 TYR A 631 8539 8428 7111 3847 396 -1272 C ATOM 4637 CD2 TYR A 631 29.236 28.692 164.339 1.00 59.77 C ANISOU 4637 CD2 TYR A 631 7875 8119 6716 3387 481 -1118 C ATOM 4638 CE1 TYR A 631 28.606 31.054 165.624 1.00 63.44 C ANISOU 4638 CE1 TYR A 631 8577 8481 7048 3866 454 -1358 C ATOM 4639 CE2 TYR A 631 29.444 28.814 165.698 1.00 59.65 C ANISOU 4639 CE2 TYR A 631 7885 8149 6629 3403 537 -1193 C ATOM 4640 CZ TYR A 631 29.128 29.998 166.335 1.00 62.13 C ANISOU 4640 CZ TYR A 631 8316 8417 6875 3640 525 -1315 C ATOM 4641 OH TYR A 631 29.332 30.124 167.687 1.00 63.25 O ANISOU 4641 OH TYR A 631 8485 8612 6936 3656 581 -1397 O ATOM 4642 N GLN A 632 31.469 29.289 161.579 1.00 52.60 N ANISOU 4642 N GLN A 632 7373 6601 6009 3123 289 -954 N ATOM 4643 CA GLN A 632 32.845 29.120 162.026 1.00 53.05 C ANISOU 4643 CA GLN A 632 7561 6503 6093 2928 295 -938 C ATOM 4644 C GLN A 632 33.792 30.092 161.342 1.00 51.81 C ANISOU 4644 C GLN A 632 7658 6055 5973 2905 209 -927 C ATOM 4645 O GLN A 632 34.813 30.465 161.928 1.00 53.38 O ANISOU 4645 O GLN A 632 8012 6102 6167 2820 200 -954 O ATOM 4646 CB GLN A 632 33.321 27.691 161.768 1.00 51.99 C ANISOU 4646 CB GLN A 632 7287 6457 6010 2681 337 -845 C ATOM 4647 CG GLN A 632 32.481 26.596 162.394 1.00 53.02 C ANISOU 4647 CG GLN A 632 7174 6864 6108 2655 419 -835 C ATOM 4648 CD GLN A 632 32.753 25.241 161.767 1.00 54.04 C ANISOU 4648 CD GLN A 632 7177 7057 6298 2438 438 -735 C ATOM 4649 OE1 GLN A 632 33.257 25.155 160.648 1.00 58.01 O ANISOU 4649 OE1 GLN A 632 7739 7437 6864 2353 390 -678 O ATOM 4650 NE2 GLN A 632 32.426 24.175 162.486 1.00 54.15 N ANISOU 4650 NE2 GLN A 632 7023 7261 6290 2346 508 -714 N ATOM 4651 N ALA A 633 33.480 30.522 160.118 1.00 62.36 N ANISOU 4651 N ALA A 633 9040 7315 7341 2972 143 -885 N ATOM 4652 CA ALA A 633 34.469 31.179 159.270 1.00 62.23 C ANISOU 4652 CA ALA A 633 9238 7040 7365 2886 66 -840 C ATOM 4653 C ALA A 633 34.277 32.680 159.081 1.00 63.24 C ANISOU 4653 C ALA A 633 9587 6972 7467 3082 -16 -891 C ATOM 4654 O ALA A 633 35.276 33.391 158.955 1.00 65.68 O ANISOU 4654 O ALA A 633 10118 7048 7789 3001 -69 -885 O ATOM 4655 CB ALA A 633 34.498 30.510 157.890 1.00 61.16 C ANISOU 4655 CB ALA A 633 9021 6932 7286 2769 44 -735 C ATOM 4656 N LEU A 634 33.038 33.184 159.061 1.00 52.95 N ANISOU 4656 N LEU A 634 8236 5757 6128 3335 -31 -941 N ATOM 4657 CA LEU A 634 32.801 34.542 158.572 1.00 53.29 C ANISOU 4657 CA LEU A 634 8491 5600 6157 3527 -126 -967 C ATOM 4658 C LEU A 634 33.541 35.584 159.398 1.00 53.05 C ANISOU 4658 C LEU A 634 8717 5340 6099 3554 -157 -1048 C ATOM 4659 O LEU A 634 34.362 36.341 158.871 1.00 53.22 O ANISOU 4659 O LEU A 634 8973 5106 6143 3482 -233 -1014 O ATOM 4660 CB LEU A 634 31.303 34.845 158.527 1.00 53.90 C ANISOU 4660 CB LEU A 634 8447 5838 6193 3816 -132 -1016 C ATOM 4661 CG LEU A 634 30.712 34.671 157.122 1.00 53.91 C ANISOU 4661 CG LEU A 634 8368 5890 6224 3848 -184 -923 C ATOM 4662 CD1 LEU A 634 29.228 34.999 157.084 1.00 55.80 C ANISOU 4662 CD1 LEU A 634 8478 6304 6420 4144 -196 -972 C ATOM 4663 CD2 LEU A 634 31.469 35.489 156.073 1.00 54.02 C ANISOU 4663 CD2 LEU A 634 8636 5618 6272 3794 -287 -854 C ATOM 4664 N ASP A 635 33.245 35.647 160.695 1.00 59.01 N ANISOU 4664 N ASP A 635 9435 6188 6799 3652 -101 -1155 N ATOM 4665 CA ASP A 635 33.835 36.676 161.543 1.00 62.11 C ANISOU 4665 CA ASP A 635 10066 6379 7155 3688 -134 -1245 C ATOM 4666 C ASP A 635 35.358 36.693 161.455 1.00 60.05 C ANISOU 4666 C ASP A 635 9975 5911 6929 3424 -160 -1197 C ATOM 4667 O ASP A 635 35.973 37.763 161.543 1.00 62.68 O ANISOU 4667 O ASP A 635 10561 6000 7253 3412 -231 -1226 O ATOM 4668 CB ASP A 635 33.378 36.481 162.992 1.00 63.95 C ANISOU 4668 CB ASP A 635 10183 6796 7319 3767 -53 -1352 C ATOM 4669 CG ASP A 635 31.886 36.728 163.177 1.00 67.37 C ANISOU 4669 CG ASP A 635 10455 7435 7707 3997 -37 -1397 C ATOM 4670 OD1 ASP A 635 31.306 37.529 162.409 1.00 70.03 O ANISOU 4670 OD1 ASP A 635 10854 7698 8055 4120 -113 -1374 O ATOM 4671 OD2 ASP A 635 31.295 36.135 164.101 1.00 69.00 O ANISOU 4671 OD2 ASP A 635 10473 7883 7861 4051 50 -1454 O ATOM 4672 N SER A 636 35.977 35.530 161.261 1.00 64.02 N ANISOU 4672 N SER A 636 10325 6525 7473 3182 -108 -1113 N ATOM 4673 CA SER A 636 37.426 35.440 161.132 1.00 61.06 C ANISOU 4673 CA SER A 636 10071 5998 7132 2919 -127 -1058 C ATOM 4674 C SER A 636 37.935 35.868 159.761 1.00 62.75 C ANISOU 4674 C SER A 636 10421 6028 7393 2830 -207 -961 C ATOM 4675 O SER A 636 39.135 36.124 159.617 1.00 59.38 O ANISOU 4675 O SER A 636 10141 5437 6983 2637 -241 -925 O ATOM 4676 CB SER A 636 37.888 34.009 161.407 1.00 59.64 C ANISOU 4676 CB SER A 636 9674 6009 6978 2711 -44 -1003 C ATOM 4677 OG SER A 636 36.863 33.255 162.033 1.00 61.12 O ANISOU 4677 OG SER A 636 9636 6451 7136 2818 34 -1039 O ATOM 4678 N MET A 637 37.066 35.940 158.754 1.00 61.23 N ANISOU 4678 N MET A 637 10176 5871 7216 2958 -239 -914 N ATOM 4679 CA MET A 637 37.496 36.288 157.407 1.00 61.30 C ANISOU 4679 CA MET A 637 10302 5728 7261 2871 -313 -814 C ATOM 4680 C MET A 637 37.742 37.785 157.291 1.00 60.13 C ANISOU 4680 C MET A 637 10464 5292 7090 2960 -413 -841 C ATOM 4681 O MET A 637 36.940 38.597 157.754 1.00 65.50 O ANISOU 4681 O MET A 637 11227 5925 7733 3202 -443 -926 O ATOM 4682 CB MET A 637 36.450 35.860 156.384 1.00 60.56 C ANISOU 4682 CB MET A 637 10048 5780 7184 2980 -318 -754 C ATOM 4683 CG MET A 637 36.545 34.418 155.964 1.00 55.66 C ANISOU 4683 CG MET A 637 9181 5367 6600 2808 -249 -684 C ATOM 4684 SD MET A 637 35.295 34.063 154.721 1.00 56.27 S ANISOU 4684 SD MET A 637 9095 5597 6686 2938 -272 -621 S ATOM 4685 CE MET A 637 34.098 33.165 155.672 1.00 58.15 C ANISOU 4685 CE MET A 637 9050 6144 6902 3064 -180 -691 C ATOM 4686 N ASP A 638 38.856 38.145 156.653 1.00 54.66 N ANISOU 4686 N ASP A 638 9940 4411 6417 2759 -465 -767 N ATOM 4687 CA ASP A 638 39.239 39.552 156.569 1.00 56.90 C ANISOU 4687 CA ASP A 638 10541 4399 6679 2797 -565 -784 C ATOM 4688 C ASP A 638 38.333 40.329 155.622 1.00 59.02 C ANISOU 4688 C ASP A 638 10857 4625 6941 2957 -641 -735 C ATOM 4689 O ASP A 638 37.919 41.453 155.930 1.00 60.20 O ANISOU 4689 O ASP A 638 11131 4682 7059 3075 -697 -781 O ATOM 4690 CB ASP A 638 40.693 39.666 156.123 1.00 56.38 C ANISOU 4690 CB ASP A 638 10609 4184 6629 2500 -594 -704 C ATOM 4691 CG ASP A 638 41.659 39.210 157.179 1.00 54.89 C ANISOU 4691 CG ASP A 638 10381 4039 6435 2317 -536 -752 C ATOM 4692 OD1 ASP A 638 41.302 39.255 158.374 1.00 56.37 O ANISOU 4692 OD1 ASP A 638 10545 4281 6593 2434 -500 -863 O ATOM 4693 OD2 ASP A 638 42.778 38.805 156.812 1.00 52.85 O ANISOU 4693 OD2 ASP A 638 10110 3773 6197 2060 -525 -678 O ATOM 4694 N ASP A 639 38.047 39.774 154.469 1.00 61.87 N ANISOU 4694 N ASP A 639 11129 5049 7329 2963 -649 -643 N ATOM 4695 CA ASP A 639 37.198 40.463 153.572 1.00 63.14 C ANISOU 4695 CA ASP A 639 11319 5191 7480 3115 -723 -589 C ATOM 4696 C ASP A 639 35.889 39.790 153.664 1.00 62.66 C ANISOU 4696 C ASP A 639 11004 5386 7417 3334 -672 -628 C ATOM 4697 O ASP A 639 35.626 38.861 152.933 1.00 64.06 O ANISOU 4697 O ASP A 639 11008 5716 7617 3308 -644 -565 O ATOM 4698 CB ASP A 639 37.749 40.343 152.167 1.00 63.57 C ANISOU 4698 CB ASP A 639 11459 5143 7553 2964 -775 -454 C ATOM 4699 CG ASP A 639 36.785 40.803 151.117 1.00 65.22 C ANISOU 4699 CG ASP A 639 11680 5353 7747 3123 -851 -391 C ATOM 4700 OD1 ASP A 639 35.709 41.307 151.442 1.00 66.36 O ANISOU 4700 OD1 ASP A 639 11845 5502 7866 3324 -886 -448 O ATOM 4701 OD2 ASP A 639 37.115 40.660 149.938 1.00 65.50 O ANISOU 4701 OD2 ASP A 639 11705 5389 7793 3048 -877 -283 O ATOM 4702 N ALA A 640 35.048 40.252 154.565 1.00 59.49 N ANISOU 4702 N ALA A 640 10558 5063 6983 3520 -658 -730 N ATOM 4703 CA ALA A 640 33.737 39.671 154.682 1.00 60.59 C ANISOU 4703 CA ALA A 640 10447 5465 7108 3724 -608 -774 C ATOM 4704 C ALA A 640 32.827 40.482 155.563 1.00 61.27 C ANISOU 4704 C ALA A 640 10558 5572 7148 3925 -620 -876 C ATOM 4705 O ALA A 640 33.296 41.242 156.388 1.00 61.55 O ANISOU 4705 O ALA A 640 10759 5463 7163 3885 -631 -939 O ATOM 4706 CB ALA A 640 33.864 38.259 155.196 1.00 59.64 C ANISOU 4706 CB ALA A 640 10108 5550 7003 3659 -495 -807 C ATOM 4707 N TRP A 641 31.526 40.302 155.409 1.00 64.44 N ANISOU 4707 N TRP A 641 10795 6161 7528 4139 -619 -894 N ATOM 4708 CA TRP A 641 30.609 40.980 156.289 1.00 66.55 C ANISOU 4708 CA TRP A 641 11038 6502 7745 4338 -610 -1002 C ATOM 4709 C TRP A 641 30.508 40.124 157.523 1.00 65.84 C ANISOU 4709 C TRP A 641 10737 6643 7634 4343 -494 -1087 C ATOM 4710 O TRP A 641 30.876 38.980 157.489 1.00 65.21 O ANISOU 4710 O TRP A 641 10480 6718 7578 4245 -424 -1055 O ATOM 4711 CB TRP A 641 29.274 41.381 155.662 1.00 68.19 C ANISOU 4711 CB TRP A 641 11162 6816 7929 4570 -661 -990 C ATOM 4712 CG TRP A 641 28.342 40.339 155.258 1.00 66.42 C ANISOU 4712 CG TRP A 641 10642 6886 7708 4641 -614 -957 C ATOM 4713 CD1 TRP A 641 28.527 39.022 155.305 1.00 64.13 C ANISOU 4713 CD1 TRP A 641 10155 6769 7443 4520 -531 -932 C ATOM 4714 CD2 TRP A 641 27.059 40.548 154.710 1.00 65.76 C ANISOU 4714 CD2 TRP A 641 10427 6960 7598 4847 -651 -944 C ATOM 4715 NE1 TRP A 641 27.434 38.372 154.835 1.00 64.02 N ANISOU 4715 NE1 TRP A 641 9894 7012 7421 4628 -515 -905 N ATOM 4716 CE2 TRP A 641 26.511 39.295 154.454 1.00 64.34 C ANISOU 4716 CE2 TRP A 641 9965 7053 7428 4828 -588 -912 C ATOM 4717 CE3 TRP A 641 26.314 41.684 154.404 1.00 68.69 C ANISOU 4717 CE3 TRP A 641 10892 7269 7937 5047 -734 -958 C ATOM 4718 CZ2 TRP A 641 25.249 39.132 153.905 1.00 65.46 C ANISOU 4718 CZ2 TRP A 641 9908 7417 7546 4989 -606 -892 C ATOM 4719 CZ3 TRP A 641 25.064 41.527 153.870 1.00 69.78 C ANISOU 4719 CZ3 TRP A 641 10836 7626 8053 5219 -751 -939 C ATOM 4720 CH2 TRP A 641 24.540 40.261 153.628 1.00 68.09 C ANISOU 4720 CH2 TRP A 641 10334 7692 7846 5184 -688 -906 C ATOM 4721 N SER A 642 30.053 40.690 158.615 1.00 67.40 N ANISOU 4721 N SER A 642 10966 6860 7783 4455 -475 -1196 N ATOM 4722 CA SER A 642 29.945 39.980 159.855 1.00 66.64 C ANISOU 4722 CA SER A 642 10700 6966 7654 4447 -367 -1279 C ATOM 4723 C SER A 642 28.902 38.904 159.825 1.00 64.75 C ANISOU 4723 C SER A 642 10142 7053 7406 4525 -295 -1264 C ATOM 4724 O SER A 642 27.950 38.988 159.096 1.00 66.30 O ANISOU 4724 O SER A 642 10244 7346 7603 4655 -332 -1224 O ATOM 4725 CB SER A 642 29.559 40.965 160.941 1.00 68.90 C ANISOU 4725 CB SER A 642 11063 7239 7878 4592 -367 -1398 C ATOM 4726 OG SER A 642 28.190 41.297 160.851 1.00 70.19 O ANISOU 4726 OG SER A 642 11095 7573 8003 4828 -375 -1431 O ATOM 4727 N PHE A 643 29.086 37.878 160.636 1.00 62.19 N ANISOU 4727 N PHE A 643 9653 6906 7070 4437 -192 -1295 N ATOM 4728 CA PHE A 643 28.084 36.819 160.689 1.00 62.03 C ANISOU 4728 CA PHE A 643 9320 7217 7031 4495 -114 -1289 C ATOM 4729 C PHE A 643 26.725 37.358 161.120 1.00 65.50 C ANISOU 4729 C PHE A 643 9642 7840 7405 4725 -111 -1357 C ATOM 4730 O PHE A 643 25.688 36.803 160.743 1.00 67.50 O ANISOU 4730 O PHE A 643 9661 8343 7645 4807 -87 -1332 O ATOM 4731 CB PHE A 643 28.549 35.711 161.635 1.00 60.85 C ANISOU 4731 CB PHE A 643 9041 7210 6868 4356 -4 -1316 C ATOM 4732 CG PHE A 643 27.582 34.574 161.759 1.00 58.44 C ANISOU 4732 CG PHE A 643 8414 7251 6539 4385 82 -1305 C ATOM 4733 CD1 PHE A 643 27.441 33.656 160.738 1.00 57.35 C ANISOU 4733 CD1 PHE A 643 8132 7210 6448 4317 87 -1215 C ATOM 4734 CD2 PHE A 643 26.808 34.426 162.889 1.00 59.58 C ANISOU 4734 CD2 PHE A 643 8398 7631 6608 4470 157 -1383 C ATOM 4735 CE1 PHE A 643 26.544 32.609 160.847 1.00 56.91 C ANISOU 4735 CE1 PHE A 643 7776 7480 6368 4317 162 -1199 C ATOM 4736 CE2 PHE A 643 25.916 33.382 163.007 1.00 59.40 C ANISOU 4736 CE2 PHE A 643 8076 7937 6556 4472 236 -1365 C ATOM 4737 CZ PHE A 643 25.785 32.473 161.989 1.00 58.07 C ANISOU 4737 CZ PHE A 643 7765 7862 6439 4394 238 -1274 C ATOM 4738 N ARG A 644 26.689 38.432 161.882 1.00 67.11 N ANISOU 4738 N ARG A 644 10003 7929 7565 4829 -138 -1445 N ATOM 4739 CA ARG A 644 25.423 39.012 162.276 1.00 70.84 C ANISOU 4739 CA ARG A 644 10384 8558 7973 5062 -142 -1514 C ATOM 4740 C ARG A 644 24.673 39.569 161.083 1.00 72.49 C ANISOU 4740 C ARG A 644 10611 8731 8199 5203 -235 -1459 C ATOM 4741 O ARG A 644 23.498 39.341 160.908 1.00 69.97 O ANISOU 4741 O ARG A 644 10088 8656 7843 5354 -221 -1467 O ATOM 4742 CB ARG A 644 25.660 40.072 163.325 1.00 74.51 C ANISOU 4742 CB ARG A 644 11043 8877 8391 5139 -159 -1622 C ATOM 4743 CG ARG A 644 24.819 41.314 163.207 1.00 78.05 C ANISOU 4743 CG ARG A 644 11542 9320 8795 5389 -221 -1679 C ATOM 4744 CD ARG A 644 25.348 42.333 164.192 1.00 80.03 C ANISOU 4744 CD ARG A 644 12054 9336 9016 5436 -263 -1771 C ATOM 4745 NE ARG A 644 26.531 43.019 163.702 1.00 80.23 N ANISOU 4745 NE ARG A 644 12369 9013 9101 5311 -353 -1716 N ATOM 4746 CZ ARG A 644 26.505 43.886 162.710 1.00 83.06 C ANISOU 4746 CZ ARG A 644 12894 9182 9484 5395 -460 -1672 C ATOM 4747 NH1 ARG A 644 25.356 44.152 162.124 1.00 85.97 N ANISOU 4747 NH1 ARG A 644 13168 9673 9825 5617 -492 -1679 N ATOM 4748 NH2 ARG A 644 27.617 44.483 162.313 1.00 82.34 N ANISOU 4748 NH2 ARG A 644 13061 8786 9440 5253 -535 -1617 N ATOM 4749 N GLU A 645 25.392 40.226 160.199 1.00 68.52 N ANISOU 4749 N GLU A 645 10351 7936 7748 5149 -331 -1398 N ATOM 4750 CA GLU A 645 24.789 40.759 159.002 1.00 70.74 C ANISOU 4750 CA GLU A 645 10661 8175 8044 5270 -422 -1333 C ATOM 4751 C GLU A 645 24.218 39.651 158.142 1.00 69.04 C ANISOU 4751 C GLU A 645 10192 8189 7850 5236 -396 -1250 C ATOM 4752 O GLU A 645 23.118 39.764 157.619 1.00 71.45 O ANISOU 4752 O GLU A 645 10381 8630 8135 5390 -433 -1229 O ATOM 4753 CB GLU A 645 25.814 41.523 158.229 1.00 69.82 C ANISOU 4753 CB GLU A 645 10852 7703 7973 5180 -524 -1271 C ATOM 4754 CG GLU A 645 26.676 42.371 159.108 1.00 71.04 C ANISOU 4754 CG GLU A 645 11264 7621 8105 5195 -557 -1350 C ATOM 4755 CD GLU A 645 27.184 43.551 158.365 1.00 72.10 C ANISOU 4755 CD GLU A 645 11698 7423 8274 5132 -669 -1286 C ATOM 4756 OE1 GLU A 645 26.458 44.043 157.505 1.00 73.88 O ANISOU 4756 OE1 GLU A 645 11953 7612 8508 5230 -746 -1221 O ATOM 4757 OE2 GLU A 645 28.306 43.987 158.630 1.00 71.55 O ANISOU 4757 OE2 GLU A 645 11832 7135 8218 4977 -682 -1299 O ATOM 4758 N LEU A 646 24.943 38.549 158.027 1.00 71.68 N ANISOU 4758 N LEU A 646 10438 8573 8223 5036 -333 -1204 N ATOM 4759 CA LEU A 646 24.463 37.425 157.271 1.00 71.54 C ANISOU 4759 CA LEU A 646 10159 8801 8222 4996 -297 -1137 C ATOM 4760 C LEU A 646 23.219 36.878 157.896 1.00 74.03 C ANISOU 4760 C LEU A 646 10183 9470 8476 5107 -217 -1196 C ATOM 4761 O LEU A 646 22.277 36.588 157.205 1.00 74.10 O ANISOU 4761 O LEU A 646 9993 9691 8469 5192 -229 -1160 O ATOM 4762 CB LEU A 646 25.492 36.315 157.185 1.00 70.52 C ANISOU 4762 CB LEU A 646 10010 8638 8146 4761 -244 -1083 C ATOM 4763 CG LEU A 646 24.896 35.149 156.415 1.00 70.11 C ANISOU 4763 CG LEU A 646 9676 8853 8109 4702 -195 -1023 C ATOM 4764 CD1 LEU A 646 25.188 35.310 154.947 1.00 68.99 C ANISOU 4764 CD1 LEU A 646 9557 8654 8003 4715 -285 -923 C ATOM 4765 CD2 LEU A 646 25.360 33.805 156.909 1.00 68.16 C ANISOU 4765 CD2 LEU A 646 9368 8634 7894 4496 -109 -1009 C ATOM 4766 N LYS A 647 23.163 36.793 159.216 1.00 66.82 N ANISOU 4766 N LYS A 647 9236 8634 7520 5100 -138 -1284 N ATOM 4767 CA LYS A 647 21.968 36.290 159.867 1.00 68.43 C ANISOU 4767 CA LYS A 647 9174 9173 7651 5204 -62 -1342 C ATOM 4768 C LYS A 647 20.795 37.169 159.557 1.00 69.87 C ANISOU 4768 C LYS A 647 9320 9438 7790 5441 -125 -1367 C ATOM 4769 O LYS A 647 19.722 36.684 159.231 1.00 70.78 O ANISOU 4769 O LYS A 647 9173 9856 7862 5516 -93 -1363 O ATOM 4770 CB LYS A 647 22.106 36.347 161.373 1.00 67.43 C ANISOU 4770 CB LYS A 647 9077 9069 7474 5190 14 -1440 C ATOM 4771 CG LYS A 647 23.354 35.767 161.974 1.00 65.06 C ANISOU 4771 CG LYS A 647 8700 8829 7190 4976 107 -1424 C ATOM 4772 CD LYS A 647 23.063 35.445 163.419 1.00 65.86 C ANISOU 4772 CD LYS A 647 8668 9146 7210 4998 205 -1510 C ATOM 4773 CE LYS A 647 21.689 34.831 163.561 1.00 67.39 C ANISOU 4773 CE LYS A 647 8566 9699 7341 5108 248 -1517 C ATOM 4774 NZ LYS A 647 21.319 34.687 164.984 1.00 68.06 N ANISOU 4774 NZ LYS A 647 8500 10017 7340 5097 352 -1586 N ATOM 4775 N ALA A 648 21.011 38.475 159.612 1.00 80.25 N ANISOU 4775 N ALA A 648 10895 10488 9109 5557 -216 -1391 N ATOM 4776 CA ALA A 648 19.942 39.395 159.360 1.00 83.20 C ANISOU 4776 CA ALA A 648 11265 10905 9443 5794 -286 -1412 C ATOM 4777 C ALA A 648 19.414 39.209 157.982 1.00 83.57 C ANISOU 4777 C ALA A 648 11167 11070 9515 5802 -332 -1314 C ATOM 4778 O ALA A 648 18.236 38.977 157.819 1.00 84.84 O ANISOU 4778 O ALA A 648 11043 11555 9638 5847 -286 -1310 O ATOM 4779 CB ALA A 648 20.456 40.806 159.505 1.00 86.84 C ANISOU 4779 CB ALA A 648 12059 11021 9914 5886 -384 -1441 C ATOM 4780 N PHE A 649 20.303 39.126 157.017 1.00 79.08 N ANISOU 4780 N PHE A 649 10790 10250 9008 5739 -419 -1230 N ATOM 4781 CA PHE A 649 19.884 38.989 155.644 1.00 78.80 C ANISOU 4781 CA PHE A 649 10680 10266 8994 5764 -488 -1133 C ATOM 4782 C PHE A 649 19.115 37.723 155.448 1.00 77.97 C ANISOU 4782 C PHE A 649 10231 10518 8877 5700 -417 -1101 C ATOM 4783 O PHE A 649 18.033 37.750 154.913 1.00 77.64 O ANISOU 4783 O PHE A 649 10020 10678 8803 5821 -449 -1079 O ATOM 4784 CB PHE A 649 21.124 38.970 154.773 1.00 76.27 C ANISOU 4784 CB PHE A 649 10597 9638 8745 5614 -559 -1039 C ATOM 4785 CG PHE A 649 20.856 39.024 153.307 1.00 76.11 C ANISOU 4785 CG PHE A 649 10517 9654 8746 5618 -635 -930 C ATOM 4786 CD1 PHE A 649 20.101 38.069 152.692 1.00 78.10 C ANISOU 4786 CD1 PHE A 649 10583 10137 8957 5787 -666 -922 C ATOM 4787 CD2 PHE A 649 21.417 40.005 152.542 1.00 74.70 C ANISOU 4787 CD2 PHE A 649 10479 9278 8626 5447 -677 -834 C ATOM 4788 CE1 PHE A 649 19.875 38.114 151.342 1.00 77.09 C ANISOU 4788 CE1 PHE A 649 10398 10049 8843 5782 -739 -820 C ATOM 4789 CE2 PHE A 649 21.192 40.058 151.189 1.00 74.54 C ANISOU 4789 CE2 PHE A 649 10408 9296 8619 5448 -750 -732 C ATOM 4790 CZ PHE A 649 20.415 39.107 150.587 1.00 75.83 C ANISOU 4790 CZ PHE A 649 10380 9694 8740 5613 -781 -726 C ATOM 4791 N VAL A 650 19.605 36.637 156.007 1.00 69.84 N ANISOU 4791 N VAL A 650 9090 9579 7867 5511 -323 -1099 N ATOM 4792 CA VAL A 650 18.926 35.383 155.796 1.00 70.17 C ANISOU 4792 CA VAL A 650 8822 9932 7905 5415 -265 -1052 C ATOM 4793 C VAL A 650 17.539 35.366 156.366 1.00 70.96 C ANISOU 4793 C VAL A 650 8659 10377 7926 5559 -228 -1101 C ATOM 4794 O VAL A 650 16.621 34.935 155.675 1.00 71.69 O ANISOU 4794 O VAL A 650 8561 10676 8002 5602 -258 -1054 O ATOM 4795 CB VAL A 650 19.748 34.191 156.295 1.00 66.24 C ANISOU 4795 CB VAL A 650 8262 9466 7439 5191 -166 -1047 C ATOM 4796 CG1 VAL A 650 19.005 32.897 156.066 1.00 65.32 C ANISOU 4796 CG1 VAL A 650 7834 9664 7321 5082 -114 -993 C ATOM 4797 CG2 VAL A 650 21.038 34.143 155.537 1.00 64.21 C ANISOU 4797 CG2 VAL A 650 8259 8881 7258 5049 -206 -995 C ATOM 4798 N ARG A 651 17.359 35.836 157.599 1.00 74.26 N ANISOU 4798 N ARG A 651 9056 10871 8288 5631 -165 -1197 N ATOM 4799 CA ARG A 651 15.989 35.791 158.132 1.00 80.55 C ANISOU 4799 CA ARG A 651 9603 12000 9000 5767 -127 -1246 C ATOM 4800 C ARG A 651 15.081 36.790 157.495 1.00 85.66 C ANISOU 4800 C ARG A 651 10339 12600 9606 6031 -215 -1285 C ATOM 4801 O ARG A 651 13.893 36.564 157.386 1.00 89.51 O ANISOU 4801 O ARG A 651 10623 13366 10021 6167 -196 -1324 O ATOM 4802 CB ARG A 651 15.817 35.716 159.651 1.00 82.21 C ANISOU 4802 CB ARG A 651 9718 12362 9154 5731 -15 -1328 C ATOM 4803 CG ARG A 651 16.802 36.439 160.534 1.00 84.59 C ANISOU 4803 CG ARG A 651 10280 12417 9446 5808 -19 -1416 C ATOM 4804 CD ARG A 651 16.993 35.659 161.828 1.00 85.43 C ANISOU 4804 CD ARG A 651 10288 12661 9509 5699 99 -1472 C ATOM 4805 NE ARG A 651 17.741 36.435 162.804 1.00 87.59 N ANISOU 4805 NE ARG A 651 10778 12748 9756 5786 100 -1569 N ATOM 4806 CZ ARG A 651 17.749 36.184 164.101 1.00 87.51 C ANISOU 4806 CZ ARG A 651 10764 12771 9715 5689 187 -1622 C ATOM 4807 NH1 ARG A 651 17.048 35.172 164.574 1.00 85.24 N ANISOU 4807 NH1 ARG A 651 10273 12692 9423 5502 279 -1582 N ATOM 4808 NH2 ARG A 651 18.455 36.949 164.920 1.00 89.82 N ANISOU 4808 NH2 ARG A 651 11258 12889 9979 5774 178 -1713 N ATOM 4809 N GLU A 652 15.648 37.932 157.132 1.00 97.98 N ANISOU 4809 N GLU A 652 12197 13821 11209 6103 -310 -1274 N ATOM 4810 CA GLU A 652 14.892 39.036 156.556 1.00103.07 C ANISOU 4810 CA GLU A 652 12918 14422 11822 6345 -405 -1290 C ATOM 4811 C GLU A 652 14.213 38.762 155.220 1.00101.22 C ANISOU 4811 C GLU A 652 12529 14334 11594 6366 -465 -1199 C ATOM 4812 O GLU A 652 13.094 39.221 154.988 1.00104.54 O ANISOU 4812 O GLU A 652 12872 14883 11965 6567 -515 -1215 O ATOM 4813 CB GLU A 652 15.786 40.275 156.431 1.00109.97 C ANISOU 4813 CB GLU A 652 14163 14884 12736 6399 -494 -1296 C ATOM 4814 CG GLU A 652 15.108 41.465 155.772 1.00114.66 C ANISOU 4814 CG GLU A 652 14934 15306 13328 6355 -445 -1381 C ATOM 4815 CD GLU A 652 15.847 42.766 156.016 1.00119.88 C ANISOU 4815 CD GLU A 652 15927 15626 13995 6481 -536 -1419 C ATOM 4816 OE1 GLU A 652 15.306 43.834 155.662 1.00121.23 O ANISOU 4816 OE1 GLU A 652 16318 15519 14225 6409 -618 -1344 O ATOM 4817 OE2 GLU A 652 16.970 42.720 156.561 1.00122.79 O ANISOU 4817 OE2 GLU A 652 16341 16005 14307 6643 -525 -1523 O ATOM 4818 N SER A 653 14.876 38.022 154.340 1.00 90.75 N ANISOU 4818 N SER A 653 11140 13016 10324 6164 -458 -1109 N ATOM 4819 CA SER A 653 14.310 37.802 153.006 1.00 92.09 C ANISOU 4819 CA SER A 653 11268 13207 10515 6174 -545 -1013 C ATOM 4820 C SER A 653 13.283 36.676 152.822 1.00 86.21 C ANISOU 4820 C SER A 653 10169 12852 9737 6121 -506 -978 C ATOM 4821 O SER A 653 12.988 35.904 153.735 1.00 82.91 O ANISOU 4821 O SER A 653 9539 12665 9298 5999 -403 -1003 O ATOM 4822 CB SER A 653 15.440 37.630 151.984 1.00 75.76 C ANISOU 4822 CB SER A 653 9399 10857 8528 5997 -586 -929 C ATOM 4823 OG SER A 653 16.507 38.523 152.248 1.00 76.02 O ANISOU 4823 OG SER A 653 9742 10560 8580 6036 -612 -972 O ATOM 4824 N LYS A 654 12.759 36.623 151.600 1.00 99.37 N ANISOU 4824 N LYS A 654 11777 14587 11393 6209 -594 -917 N ATOM 4825 CA LYS A 654 11.771 35.661 151.130 1.00101.33 C ANISOU 4825 CA LYS A 654 11704 15193 11604 6172 -584 -876 C ATOM 4826 C LYS A 654 12.222 35.049 149.811 1.00 98.93 C ANISOU 4826 C LYS A 654 11341 14892 11357 5952 -600 -775 C ATOM 4827 O LYS A 654 11.436 34.919 148.873 1.00 99.99 O ANISOU 4827 O LYS A 654 11200 15327 11464 5870 -585 -739 O ATOM 4828 CB LYS A 654 10.407 36.332 150.961 1.00106.54 C ANISOU 4828 CB LYS A 654 12327 15938 12213 6403 -677 -869 C ATOM 4829 CG LYS A 654 9.415 36.009 152.067 1.00111.19 C ANISOU 4829 CG LYS A 654 12771 16759 12717 6595 -635 -965 C ATOM 4830 CD LYS A 654 8.054 36.624 151.784 1.00111.67 C ANISOU 4830 CD LYS A 654 13009 16650 12772 6660 -580 -1064 C ATOM 4831 CE LYS A 654 8.132 38.141 151.735 1.00114.14 C ANISOU 4831 CE LYS A 654 13102 17273 12994 6770 -501 -1157 C ATOM 4832 NZ LYS A 654 6.875 38.745 151.214 1.00114.17 N ANISOU 4832 NZ LYS A 654 13219 17170 12991 6750 -420 -1245 N ATOM 4833 N THR A 655 13.496 34.674 149.747 1.00 92.58 N ANISOU 4833 N THR A 655 10786 13768 10623 5848 -631 -731 N ATOM 4834 CA THR A 655 14.057 34.083 148.538 1.00 88.32 C ANISOU 4834 CA THR A 655 10241 13186 10131 5688 -679 -629 C ATOM 4835 C THR A 655 14.758 32.755 148.809 1.00 83.37 C ANISOU 4835 C THR A 655 9467 12673 9539 5443 -586 -615 C ATOM 4836 O THR A 655 14.672 31.828 148.003 1.00 79.67 O ANISOU 4836 O THR A 655 8806 12393 9073 5317 -596 -554 O ATOM 4837 CB THR A 655 15.048 35.042 147.852 1.00 87.52 C ANISOU 4837 CB THR A 655 10488 12685 10081 5697 -765 -580 C ATOM 4838 OG1 THR A 655 15.926 35.608 148.832 1.00 84.10 O ANISOU 4838 OG1 THR A 655 10202 12051 9702 5538 -702 -595 O ATOM 4839 CG2 THR A 655 14.302 36.159 147.139 1.00 91.73 C ANISOU 4839 CG2 THR A 655 11228 13039 10588 5927 -826 -626 C ATOM 4840 N LEU A 656 15.451 32.663 149.940 1.00 74.21 N ANISOU 4840 N LEU A 656 8398 11396 8401 5370 -500 -671 N ATOM 4841 CA LEU A 656 16.162 31.440 150.279 1.00 69.27 C ANISOU 4841 CA LEU A 656 7680 10823 7816 5140 -415 -657 C ATOM 4842 C LEU A 656 15.196 30.361 150.752 1.00 69.32 C ANISOU 4842 C LEU A 656 7336 11227 7777 5056 -332 -673 C ATOM 4843 O LEU A 656 14.189 30.642 151.403 1.00 75.87 O ANISOU 4843 O LEU A 656 8031 12257 8539 5174 -301 -730 O ATOM 4844 CB LEU A 656 17.193 31.715 151.374 1.00 66.65 C ANISOU 4844 CB LEU A 656 7547 10263 7513 5098 -348 -716 C ATOM 4845 CG LEU A 656 18.319 32.739 151.181 1.00 65.51 C ANISOU 4845 CG LEU A 656 7767 9709 7415 5128 -410 -709 C ATOM 4846 CD1 LEU A 656 18.463 33.667 152.389 1.00 63.96 C ANISOU 4846 CD1 LEU A 656 7681 9348 7273 5021 -485 -608 C ATOM 4847 CD2 LEU A 656 19.648 32.081 150.810 1.00 68.00 C ANISOU 4847 CD2 LEU A 656 8248 9896 7693 5354 -478 -753 C ATOM 4848 N SER A 657 15.517 29.110 150.433 1.00 65.71 N ANISOU 4848 N SER A 657 6732 10883 7352 4843 -296 -622 N ATOM 4849 CA SER A 657 14.658 28.016 150.852 1.00 66.05 C ANISOU 4849 CA SER A 657 6449 11295 7353 4721 -218 -627 C ATOM 4850 C SER A 657 14.783 27.791 152.358 1.00 65.88 C ANISOU 4850 C SER A 657 6392 11332 7309 4676 -97 -698 C ATOM 4851 O SER A 657 15.681 28.311 153.024 1.00 66.76 O ANISOU 4851 O SER A 657 6726 11193 7448 4707 -70 -739 O ATOM 4852 CB SER A 657 14.991 26.741 150.080 1.00 64.23 C ANISOU 4852 CB SER A 657 6110 11131 7164 4439 -218 -548 C ATOM 4853 OG SER A 657 16.212 26.171 150.508 1.00 61.88 O ANISOU 4853 OG SER A 657 5973 10611 6927 4182 -154 -534 O ATOM 4854 N ASN A 658 13.847 27.006 152.893 1.00 76.32 N ANISOU 4854 N ASN A 658 7431 12996 8573 4592 -26 -708 N ATOM 4855 CA ASN A 658 13.844 26.708 154.322 1.00 76.57 C ANISOU 4855 CA ASN A 658 7400 13126 8567 4536 89 -765 C ATOM 4856 C ASN A 658 15.113 25.981 154.733 1.00 74.94 C ANISOU 4856 C ASN A 658 7286 12762 8424 4344 157 -751 C ATOM 4857 O ASN A 658 15.761 26.341 155.722 1.00 73.30 O ANISOU 4857 O ASN A 658 7228 12404 8217 4369 211 -805 O ATOM 4858 CB ASN A 658 12.617 25.871 154.678 1.00 81.05 C ANISOU 4858 CB ASN A 658 7639 14099 9059 4441 147 -758 C ATOM 4859 CG ASN A 658 11.568 26.664 155.414 1.00 86.37 C ANISOU 4859 CG ASN A 658 8249 14929 9639 4639 160 -828 C ATOM 4860 OD1 ASN A 658 11.636 27.890 155.486 1.00 89.01 O ANISOU 4860 OD1 ASN A 658 8776 15077 9968 4866 111 -880 O ATOM 4861 ND2 ASN A 658 10.590 25.966 155.977 1.00 87.66 N ANISOU 4861 ND2 ASN A 658 8145 15436 9726 4549 227 -829 N ATOM 4862 N LYS A 659 15.482 24.944 153.982 1.00 68.49 N ANISOU 4862 N LYS A 659 6428 11935 7659 4077 144 -668 N ATOM 4863 CA LYS A 659 16.666 24.168 154.323 1.00 64.39 C ANISOU 4863 CA LYS A 659 6049 11212 7202 3787 197 -634 C ATOM 4864 C LYS A 659 17.947 24.943 154.042 1.00 58.84 C ANISOU 4864 C LYS A 659 5683 10106 6567 3816 147 -635 C ATOM 4865 O LYS A 659 18.949 24.757 154.737 1.00 57.38 O ANISOU 4865 O LYS A 659 5645 9741 6416 3687 200 -644 O ATOM 4866 CB LYS A 659 16.652 22.841 153.567 1.00 60.56 C ANISOU 4866 CB LYS A 659 5446 10813 6751 3479 191 -549 C ATOM 4867 CG LYS A 659 18.024 22.216 153.372 1.00 56.66 C ANISOU 4867 CG LYS A 659 5158 10029 6343 3214 199 -501 C ATOM 4868 CD LYS A 659 17.905 20.872 152.681 1.00 57.77 C ANISOU 4868 CD LYS A 659 5172 10270 6508 2926 194 -430 C ATOM 4869 CE LYS A 659 19.261 20.176 152.586 1.00 57.23 C ANISOU 4869 CE LYS A 659 5294 9931 6521 2673 211 -391 C ATOM 4870 NZ LYS A 659 19.111 18.700 152.530 1.00 58.66 N ANISOU 4870 NZ LYS A 659 5334 10240 6713 2383 246 -341 N ATOM 4871 N LYS A 660 17.934 25.828 153.051 1.00 63.42 N ANISOU 4871 N LYS A 660 6388 10547 7162 3981 45 -622 N ATOM 4872 CA LYS A 660 19.111 26.652 152.810 1.00 62.47 C ANISOU 4872 CA LYS A 660 6588 10052 7096 4012 -4 -621 C ATOM 4873 C LYS A 660 19.360 27.615 153.960 1.00 64.35 C ANISOU 4873 C LYS A 660 6964 10179 7309 4209 31 -712 C ATOM 4874 O LYS A 660 20.508 27.993 154.215 1.00 62.33 O ANISOU 4874 O LYS A 660 6953 9634 7094 4149 31 -720 O ATOM 4875 CB LYS A 660 18.956 27.418 151.495 1.00 64.89 C ANISOU 4875 CB LYS A 660 6996 10246 7412 4150 -125 -581 C ATOM 4876 CG LYS A 660 19.968 28.526 151.301 1.00 65.01 C ANISOU 4876 CG LYS A 660 7342 9895 7465 4240 -185 -585 C ATOM 4877 CD LYS A 660 20.316 28.699 149.851 1.00 65.38 C ANISOU 4877 CD LYS A 660 7508 9789 7543 4184 -286 -502 C ATOM 4878 CE LYS A 660 20.974 27.450 149.317 1.00 63.99 C ANISOU 4878 CE LYS A 660 7293 9606 7414 3846 -256 -435 C ATOM 4879 NZ LYS A 660 21.327 27.595 147.886 1.00 64.43 N ANISOU 4879 NZ LYS A 660 7462 9528 7490 3785 -350 -357 N ATOM 4880 N LYS A 661 18.307 28.008 154.678 1.00 67.35 N ANISOU 4880 N LYS A 661 7183 10794 7614 4440 64 -786 N ATOM 4881 CA LYS A 661 18.478 28.961 155.768 1.00 69.52 C ANISOU 4881 CA LYS A 661 7601 10959 7855 4616 92 -879 C ATOM 4882 C LYS A 661 19.134 28.309 156.982 1.00 67.43 C ANISOU 4882 C LYS A 661 7328 10705 7587 4458 204 -912 C ATOM 4883 O LYS A 661 20.001 28.916 157.621 1.00 67.71 O ANISOU 4883 O LYS A 661 7588 10504 7634 4486 213 -960 O ATOM 4884 CB LYS A 661 17.133 29.587 156.140 1.00 71.69 C ANISOU 4884 CB LYS A 661 7748 11444 8045 4800 84 -930 C ATOM 4885 CG LYS A 661 16.602 30.559 155.094 1.00 70.79 C ANISOU 4885 CG LYS A 661 7719 11248 7930 4985 -36 -910 C ATOM 4886 CD LYS A 661 15.610 31.555 155.678 1.00 71.51 C ANISOU 4886 CD LYS A 661 7798 11431 7944 5210 -48 -986 C ATOM 4887 CE LYS A 661 14.224 31.381 155.087 1.00 73.65 C ANISOU 4887 CE LYS A 661 7817 12007 8160 5293 -80 -962 C ATOM 4888 NZ LYS A 661 13.362 32.576 155.313 1.00 77.55 N ANISOU 4888 NZ LYS A 661 8356 12519 8591 5552 -125 -1026 N ATOM 4889 N GLU A 662 18.743 27.074 157.313 1.00 68.56 N ANISOU 4889 N GLU A 662 7232 11106 7710 4254 281 -876 N ATOM 4890 CA GLU A 662 19.382 26.377 158.426 1.00 68.48 C ANISOU 4890 CA GLU A 662 7228 11095 7697 4057 379 -885 C ATOM 4891 C GLU A 662 20.871 26.191 158.176 1.00 65.93 C ANISOU 4891 C GLU A 662 7155 10435 7460 3843 357 -837 C ATOM 4892 O GLU A 662 21.692 26.427 159.067 1.00 64.00 O ANISOU 4892 O GLU A 662 7061 10039 7216 3814 396 -877 O ATOM 4893 CB GLU A 662 18.731 25.016 158.652 1.00 72.83 C ANISOU 4893 CB GLU A 662 7495 11958 8219 3847 451 -834 C ATOM 4894 CG GLU A 662 17.238 24.981 158.473 1.00 79.73 C ANISOU 4894 CG GLU A 662 8085 13189 9020 3995 454 -849 C ATOM 4895 CD GLU A 662 16.702 23.569 158.548 1.00 83.26 C ANISOU 4895 CD GLU A 662 8274 13913 9447 3735 513 -782 C ATOM 4896 OE1 GLU A 662 15.777 23.243 157.775 1.00 85.50 O ANISOU 4896 OE1 GLU A 662 8361 14413 9714 3736 477 -746 O ATOM 4897 OE2 GLU A 662 17.216 22.781 159.373 1.00 83.32 O ANISOU 4897 OE2 GLU A 662 8283 13919 9456 3523 590 -762 O ATOM 4898 N TYR A 663 21.236 25.768 156.967 1.00 62.84 N ANISOU 4898 N TYR A 663 6804 9937 7136 3693 295 -753 N ATOM 4899 CA TYR A 663 22.627 25.446 156.679 1.00 53.38 C ANISOU 4899 CA TYR A 663 5807 8458 6016 3471 282 -702 C ATOM 4900 C TYR A 663 23.510 26.681 156.691 1.00 53.29 C ANISOU 4900 C TYR A 663 6087 8135 6027 3598 229 -741 C ATOM 4901 O TYR A 663 24.703 26.581 156.979 1.00 51.81 O ANISOU 4901 O TYR A 663 6067 7737 5881 3448 243 -730 O ATOM 4902 CB TYR A 663 22.736 24.738 155.331 1.00 62.27 C ANISOU 4902 CB TYR A 663 6901 9563 7198 3299 228 -613 C ATOM 4903 CG TYR A 663 22.310 23.290 155.353 1.00 61.03 C ANISOU 4903 CG TYR A 663 6518 9630 7040 3074 282 -563 C ATOM 4904 CD1 TYR A 663 21.075 22.915 155.858 1.00 61.88 C ANISOU 4904 CD1 TYR A 663 6370 10063 7080 3129 330 -583 C ATOM 4905 CD2 TYR A 663 23.139 22.297 154.854 1.00 59.06 C ANISOU 4905 CD2 TYR A 663 6314 9270 6855 2804 284 -497 C ATOM 4906 CE1 TYR A 663 20.681 21.597 155.874 1.00 61.96 C ANISOU 4906 CE1 TYR A 663 6186 10270 7087 2906 373 -532 C ATOM 4907 CE2 TYR A 663 22.756 20.972 154.869 1.00 59.36 C ANISOU 4907 CE2 TYR A 663 6168 9491 6894 2596 326 -452 C ATOM 4908 CZ TYR A 663 21.524 20.629 155.378 1.00 62.86 C ANISOU 4908 CZ TYR A 663 6368 10245 7269 2639 368 -467 C ATOM 4909 OH TYR A 663 21.130 19.313 155.393 1.00 65.61 O ANISOU 4909 OH TYR A 663 6542 10769 7616 2415 405 -417 O ATOM 4910 N LEU A 664 22.965 27.845 156.372 1.00 62.57 N ANISOU 4910 N LEU A 664 7329 9270 7173 3869 164 -784 N ATOM 4911 CA LEU A 664 23.802 29.033 156.353 1.00 62.97 C ANISOU 4911 CA LEU A 664 7675 9007 7245 3976 106 -816 C ATOM 4912 C LEU A 664 24.078 29.579 157.743 1.00 64.06 C ANISOU 4912 C LEU A 664 7904 9095 7341 4072 161 -914 C ATOM 4913 O LEU A 664 24.971 30.420 157.889 1.00 67.31 O ANISOU 4913 O LEU A 664 8574 9229 7772 4100 122 -941 O ATOM 4914 CB LEU A 664 23.162 30.120 155.486 1.00 65.08 C ANISOU 4914 CB LEU A 664 8013 9218 7498 4235 5 -822 C ATOM 4915 CG LEU A 664 23.502 30.055 153.994 1.00 62.93 C ANISOU 4915 CG LEU A 664 7818 8816 7278 4133 -82 -723 C ATOM 4916 CD1 LEU A 664 22.346 30.598 153.178 1.00 64.70 C ANISOU 4916 CD1 LEU A 664 7953 9163 7467 4369 -159 -715 C ATOM 4917 CD2 LEU A 664 24.781 30.827 153.681 1.00 60.84 C ANISOU 4917 CD2 LEU A 664 7872 8188 7058 4078 -139 -703 C ATOM 4918 N LEU A 665 23.357 29.110 158.766 1.00 63.05 N ANISOU 4918 N LEU A 665 7574 9232 7151 4109 249 -965 N ATOM 4919 CA LEU A 665 23.459 29.693 160.095 1.00 64.16 C ANISOU 4919 CA LEU A 665 7786 9359 7233 4235 300 -1070 C ATOM 4920 C LEU A 665 23.635 28.668 161.207 1.00 63.85 C ANISOU 4920 C LEU A 665 7611 9486 7164 4047 410 -1072 C ATOM 4921 O LEU A 665 23.580 29.052 162.379 1.00 65.76 O ANISOU 4921 O LEU A 665 7874 9773 7340 4150 463 -1162 O ATOM 4922 CB LEU A 665 22.224 30.552 160.401 1.00 66.11 C ANISOU 4922 CB LEU A 665 7954 9760 7404 4520 286 -1149 C ATOM 4923 CG LEU A 665 21.909 31.735 159.484 1.00 64.43 C ANISOU 4923 CG LEU A 665 7894 9379 7207 4692 168 -1143 C ATOM 4924 CD1 LEU A 665 20.819 32.594 160.084 1.00 67.54 C ANISOU 4924 CD1 LEU A 665 8241 9899 7524 4897 159 -1219 C ATOM 4925 CD2 LEU A 665 23.136 32.568 159.224 1.00 61.13 C ANISOU 4925 CD2 LEU A 665 7809 8575 6843 4669 99 -1142 C ATOM 4926 N THR A 666 23.829 27.387 160.893 1.00 61.50 N ANISOU 4926 N THR A 666 7182 9280 6906 3780 442 -979 N ATOM 4927 CA THR A 666 24.051 26.411 161.954 1.00 59.96 C ANISOU 4927 CA THR A 666 6879 9219 6682 3595 538 -970 C ATOM 4928 C THR A 666 25.283 26.794 162.740 1.00 57.91 C ANISOU 4928 C THR A 666 6846 8724 6434 3535 548 -1006 C ATOM 4929 O THR A 666 26.384 26.860 162.192 1.00 56.30 O ANISOU 4929 O THR A 666 6826 8262 6303 3406 497 -961 O ATOM 4930 CB THR A 666 24.219 25.000 161.402 1.00 58.07 C ANISOU 4930 CB THR A 666 6511 9055 6498 3310 555 -859 C ATOM 4931 OG1 THR A 666 24.864 25.051 160.122 1.00 57.78 O ANISOU 4931 OG1 THR A 666 6605 8801 6548 3227 474 -796 O ATOM 4932 CG2 THR A 666 22.873 24.293 161.310 1.00 58.87 C ANISOU 4932 CG2 THR A 666 6317 9500 6549 3317 594 -838 C ATOM 4933 N GLU A 667 25.091 27.064 164.021 1.00 65.88 N ANISOU 4933 N GLU A 667 7837 9834 7361 3628 611 -1089 N ATOM 4934 CA GLU A 667 26.202 27.273 164.931 1.00 66.57 C ANISOU 4934 CA GLU A 667 8106 9746 7443 3546 631 -1124 C ATOM 4935 C GLU A 667 26.746 25.968 165.473 1.00 65.76 C ANISOU 4935 C GLU A 667 7914 9722 7351 3268 695 -1050 C ATOM 4936 O GLU A 667 27.449 25.960 166.487 1.00 65.25 O ANISOU 4936 O GLU A 667 7935 9603 7255 3202 731 -1080 O ATOM 4937 CB GLU A 667 25.773 28.206 166.058 1.00 71.94 C ANISOU 4937 CB GLU A 667 8824 10490 8022 3781 665 -1256 C ATOM 4938 CG GLU A 667 25.486 29.599 165.551 1.00 75.60 C ANISOU 4938 CG GLU A 667 9443 10797 8484 4057 585 -1334 C ATOM 4939 CD GLU A 667 24.358 30.268 166.280 1.00 78.40 C ANISOU 4939 CD GLU A 667 9707 11337 8743 4285 609 -1430 C ATOM 4940 OE1 GLU A 667 23.492 30.863 165.601 1.00 80.35 O ANISOU 4940 OE1 GLU A 667 9920 11613 8995 4434 548 -1428 O ATOM 4941 OE2 GLU A 667 24.338 30.199 167.526 1.00 78.69 O ANISOU 4941 OE2 GLU A 667 9712 11484 8702 4273 678 -1489 O ATOM 4942 N GLU A 668 26.418 24.871 164.802 1.00 54.62 N ANISOU 4942 N GLU A 668 6336 8434 5982 3107 705 -953 N ATOM 4943 CA GLU A 668 26.904 23.550 165.157 1.00 56.17 C ANISOU 4943 CA GLU A 668 6454 8687 6200 2838 754 -870 C ATOM 4944 C GLU A 668 28.325 23.400 164.646 1.00 51.69 C ANISOU 4944 C GLU A 668 6081 7831 5726 2669 704 -817 C ATOM 4945 O GLU A 668 28.581 23.580 163.453 1.00 50.94 O ANISOU 4945 O GLU A 668 6059 7593 5705 2657 636 -781 O ATOM 4946 CB GLU A 668 25.989 22.497 164.548 1.00 59.40 C ANISOU 4946 CB GLU A 668 6630 9318 6619 2736 773 -794 C ATOM 4947 CG GLU A 668 26.261 21.074 164.940 1.00 60.72 C ANISOU 4947 CG GLU A 668 6699 9573 6800 2470 825 -707 C ATOM 4948 CD GLU A 668 25.078 20.186 164.609 1.00 65.46 C ANISOU 4948 CD GLU A 668 7047 10448 7376 2404 853 -655 C ATOM 4949 OE1 GLU A 668 23.931 20.680 164.715 1.00 73.45 O ANISOU 4949 OE1 GLU A 668 7919 11673 8316 2585 871 -708 O ATOM 4950 OE2 GLU A 668 25.287 19.013 164.224 1.00 66.43 O ANISOU 4950 OE2 GLU A 668 7115 10575 7550 2176 854 -565 O ATOM 4951 N ASP A 669 29.256 23.093 165.546 1.00 61.43 N ANISOU 4951 N ASP A 669 7395 8991 6953 2543 735 -812 N ATOM 4952 CA ASP A 669 30.651 22.898 165.158 1.00 65.58 C ANISOU 4952 CA ASP A 669 8088 9269 7561 2379 692 -763 C ATOM 4953 C ASP A 669 30.805 21.489 164.590 1.00 66.15 C ANISOU 4953 C ASP A 669 8049 9389 7698 2156 703 -656 C ATOM 4954 O ASP A 669 31.382 20.586 165.201 1.00 65.71 O ANISOU 4954 O ASP A 669 7973 9347 7648 1987 738 -608 O ATOM 4955 CB ASP A 669 31.588 23.137 166.331 1.00 70.03 C ANISOU 4955 CB ASP A 669 8777 9744 8089 2338 714 -801 C ATOM 4956 CG ASP A 669 33.033 23.243 165.900 1.00 73.09 C ANISOU 4956 CG ASP A 669 9349 9870 8553 2211 660 -768 C ATOM 4957 OD1 ASP A 669 33.626 22.207 165.534 1.00 73.41 O ANISOU 4957 OD1 ASP A 669 9353 9883 8655 2019 661 -683 O ATOM 4958 OD2 ASP A 669 33.578 24.363 165.926 1.00 76.82 O ANISOU 4958 OD2 ASP A 669 10004 10165 9020 2302 614 -829 O ATOM 4959 N ILE A 670 30.255 21.310 163.388 1.00 61.13 N ANISOU 4959 N ILE A 670 7344 8777 7106 2163 667 -620 N ATOM 4960 CA ILE A 670 30.353 20.022 162.728 1.00 59.30 C ANISOU 4960 CA ILE A 670 7020 8578 6936 1961 668 -529 C ATOM 4961 C ILE A 670 31.821 19.696 162.487 1.00 58.63 C ANISOU 4961 C ILE A 670 7087 8266 6925 1805 641 -488 C ATOM 4962 O ILE A 670 32.675 20.586 162.391 1.00 62.23 O ANISOU 4962 O ILE A 670 7717 8530 7397 1856 602 -522 O ATOM 4963 CB ILE A 670 29.551 20.010 161.416 1.00 56.85 C ANISOU 4963 CB ILE A 670 6625 8320 6653 2005 625 -508 C ATOM 4964 CG1 ILE A 670 29.943 21.188 160.519 1.00 55.80 C ANISOU 4964 CG1 ILE A 670 6659 7989 6552 2135 550 -539 C ATOM 4965 CG2 ILE A 670 28.070 20.042 161.709 1.00 58.18 C ANISOU 4965 CG2 ILE A 670 6596 8761 6747 2124 659 -534 C ATOM 4966 CD1 ILE A 670 30.958 20.847 159.469 1.00 53.49 C ANISOU 4966 CD1 ILE A 670 6475 7504 6344 1989 503 -483 C ATOM 4967 N SER A 671 32.119 18.406 162.399 1.00 56.08 N ANISOU 4967 N SER A 671 6697 7968 6642 1611 660 -415 N ATOM 4968 CA SER A 671 33.490 17.971 162.219 1.00 51.53 C ANISOU 4968 CA SER A 671 6243 7204 6134 1467 639 -376 C ATOM 4969 C SER A 671 33.495 16.661 161.456 1.00 47.53 C ANISOU 4969 C SER A 671 5655 6716 5687 1298 635 -302 C ATOM 4970 O SER A 671 32.503 15.928 161.431 1.00 46.97 O ANISOU 4970 O SER A 671 5432 6817 5598 1257 660 -275 O ATOM 4971 CB SER A 671 34.207 17.811 163.562 1.00 47.93 C ANISOU 4971 CB SER A 671 5834 6733 5644 1414 676 -380 C ATOM 4972 OG SER A 671 35.383 17.049 163.404 1.00 44.02 O ANISOU 4972 OG SER A 671 5405 6108 5214 1255 662 -326 O ATOM 4973 N LYS A 672 34.617 16.359 160.851 1.00 49.49 N ANISOU 4973 N LYS A 672 6008 6789 6006 1199 603 -274 N ATOM 4974 CA LYS A 672 34.758 15.149 160.069 1.00 51.21 C ANISOU 4974 CA LYS A 672 6176 6995 6285 1048 593 -216 C ATOM 4975 C LYS A 672 34.741 13.881 160.874 1.00 53.85 C ANISOU 4975 C LYS A 672 6426 7419 6615 913 636 -165 C ATOM 4976 O LYS A 672 34.513 12.824 160.334 1.00 53.16 O ANISOU 4976 O LYS A 672 6264 7373 6560 799 633 -121 O ATOM 4977 CB LYS A 672 36.059 15.223 159.283 1.00 52.26 C ANISOU 4977 CB LYS A 672 6440 6930 6487 980 555 -204 C ATOM 4978 CG LYS A 672 36.311 16.603 158.717 1.00 53.60 C ANISOU 4978 CG LYS A 672 6731 6977 6658 1088 511 -245 C ATOM 4979 CD LYS A 672 37.101 17.517 159.639 1.00 53.96 C ANISOU 4979 CD LYS A 672 6892 6939 6672 1149 515 -282 C ATOM 4980 CE LYS A 672 38.385 17.959 158.968 1.00 55.21 C ANISOU 4980 CE LYS A 672 7201 6919 6859 1160 467 -295 C ATOM 4981 NZ LYS A 672 39.089 18.984 159.752 1.00 57.06 N ANISOU 4981 NZ LYS A 672 7554 7066 7061 1203 464 -333 N ATOM 4982 N PHE A 673 34.966 13.991 162.174 1.00 50.43 N ANISOU 4982 N PHE A 673 6012 7013 6137 919 671 -169 N ATOM 4983 CA PHE A 673 35.056 12.819 163.031 1.00 48.01 C ANISOU 4983 CA PHE A 673 5652 6766 5822 785 706 -109 C ATOM 4984 C PHE A 673 33.919 12.736 164.040 1.00 51.19 C ANISOU 4984 C PHE A 673 5927 7386 6136 810 759 -107 C ATOM 4985 O PHE A 673 33.991 11.929 164.969 1.00 50.79 O ANISOU 4985 O PHE A 673 5843 7395 6059 709 792 -57 O ATOM 4986 CB PHE A 673 36.419 12.796 163.731 1.00 40.20 C ANISOU 4986 CB PHE A 673 4783 5642 4850 744 701 -99 C ATOM 4987 CG PHE A 673 37.579 12.815 162.773 1.00 36.46 C ANISOU 4987 CG PHE A 673 4418 4977 4457 710 654 -99 C ATOM 4988 CD1 PHE A 673 37.983 11.660 162.132 1.00 34.10 C ANISOU 4988 CD1 PHE A 673 4112 4616 4227 586 638 -48 C ATOM 4989 CD2 PHE A 673 38.248 13.990 162.496 1.00 34.36 C ANISOU 4989 CD2 PHE A 673 4262 4599 4193 800 626 -151 C ATOM 4990 CE1 PHE A 673 39.038 11.673 161.232 1.00 33.18 C ANISOU 4990 CE1 PHE A 673 4086 4346 4177 562 601 -54 C ATOM 4991 CE2 PHE A 673 39.306 14.010 161.602 1.00 33.44 C ANISOU 4991 CE2 PHE A 673 4235 4330 4143 758 588 -147 C ATOM 4992 CZ PHE A 673 39.695 12.849 160.968 1.00 32.86 C ANISOU 4992 CZ PHE A 673 4139 4213 4132 644 578 -100 C ATOM 4993 N ASP A 674 32.868 13.535 163.872 1.00 55.89 N ANISOU 4993 N ASP A 674 6447 8109 6681 944 768 -158 N ATOM 4994 CA ASP A 674 31.717 13.447 164.759 1.00 62.74 C ANISOU 4994 CA ASP A 674 7169 9212 7456 973 824 -160 C ATOM 4995 C ASP A 674 31.077 12.070 164.665 1.00 66.06 C ANISOU 4995 C ASP A 674 7460 9755 7883 799 842 -80 C ATOM 4996 O ASP A 674 30.922 11.510 163.578 1.00 67.24 O ANISOU 4996 O ASP A 674 7587 9866 8096 723 807 -52 O ATOM 4997 CB ASP A 674 30.688 14.524 164.411 1.00 64.23 C ANISOU 4997 CB ASP A 674 7290 9517 7596 1161 822 -231 C ATOM 4998 CG ASP A 674 31.145 15.916 164.799 1.00 65.03 C ANISOU 4998 CG ASP A 674 7519 9521 7667 1341 812 -315 C ATOM 4999 OD1 ASP A 674 32.081 16.035 165.624 1.00 64.49 O ANISOU 4999 OD1 ASP A 674 7559 9356 7590 1315 821 -321 O ATOM 5000 OD2 ASP A 674 30.557 16.893 164.285 1.00 66.00 O ANISOU 5000 OD2 ASP A 674 7638 9666 7774 1509 790 -374 O ATOM 5001 N VAL A 675 30.708 11.523 165.817 1.00 75.19 N ANISOU 5001 N VAL A 675 8540 11060 8970 728 896 -42 N ATOM 5002 CA VAL A 675 30.096 10.206 165.871 1.00 77.91 C ANISOU 5002 CA VAL A 675 8772 11522 9310 544 914 43 C ATOM 5003 C VAL A 675 28.704 10.260 165.254 1.00 79.38 C ANISOU 5003 C VAL A 675 8788 11910 9463 572 921 29 C ATOM 5004 O VAL A 675 28.369 9.458 164.383 1.00 80.90 O ANISOU 5004 O VAL A 675 8931 12101 9704 451 892 71 O ATOM 5005 CB VAL A 675 30.040 9.675 167.318 1.00 79.19 C ANISOU 5005 CB VAL A 675 8896 11801 9391 459 971 94 C ATOM 5006 N ILE A 680 23.164 10.656 154.798 1.00 51.53 N ANISOU 5006 N ILE A 680 4661 8831 6089 696 501 -68 N ATOM 5007 CA ILE A 680 23.452 11.339 153.539 1.00 50.75 C ANISOU 5007 CA ILE A 680 4651 8610 6022 803 431 -97 C ATOM 5008 C ILE A 680 22.573 10.775 152.429 1.00 52.08 C ANISOU 5008 C ILE A 680 4693 8919 6178 708 376 -82 C ATOM 5009 O ILE A 680 22.107 9.640 152.512 1.00 57.54 O ANISOU 5009 O ILE A 680 5284 9716 6863 507 387 -47 O ATOM 5010 CB ILE A 680 24.931 11.230 153.166 1.00 46.81 C ANISOU 5010 CB ILE A 680 4377 7806 5604 751 414 -96 C ATOM 5011 CG1 ILE A 680 25.210 9.880 152.511 1.00 44.63 C ANISOU 5011 CG1 ILE A 680 4120 7459 5377 516 392 -63 C ATOM 5012 CG2 ILE A 680 25.780 11.382 154.402 1.00 46.67 C ANISOU 5012 CG2 ILE A 680 4460 7677 5597 770 472 -97 C ATOM 5013 CD1 ILE A 680 26.681 9.588 152.293 1.00 42.65 C ANISOU 5013 CD1 ILE A 680 4070 6932 5202 453 386 -63 C ATOM 5014 N GLU A 681 22.358 11.576 151.382 1.00 53.52 N ANISOU 5014 N GLU A 681 4887 9095 6352 847 313 -107 N ATOM 5015 CA GLU A 681 21.393 11.195 150.356 1.00 55.33 C ANISOU 5015 CA GLU A 681 4975 9494 6553 785 256 -98 C ATOM 5016 C GLU A 681 21.931 10.099 149.453 1.00 53.87 C ANISOU 5016 C GLU A 681 4872 9175 6423 563 219 -80 C ATOM 5017 O GLU A 681 21.150 9.317 148.903 1.00 52.92 O ANISOU 5017 O GLU A 681 4625 9202 6279 421 188 -65 O ATOM 5018 CB GLU A 681 20.985 12.416 149.536 1.00 59.51 C ANISOU 5018 CB GLU A 681 5496 10063 7051 1014 194 -125 C ATOM 5019 CG GLU A 681 19.993 13.311 150.246 1.00 63.94 C ANISOU 5019 CG GLU A 681 5908 10846 7540 1225 216 -148 C ATOM 5020 CD GLU A 681 18.706 12.589 150.588 1.00 68.94 C ANISOU 5020 CD GLU A 681 6283 11801 8111 1125 238 -130 C ATOM 5021 OE1 GLU A 681 17.798 12.549 149.735 1.00 72.63 O ANISOU 5021 OE1 GLU A 681 6608 12448 8540 1131 180 -125 O ATOM 5022 OE2 GLU A 681 18.603 12.058 151.711 1.00 73.01 O ANISOU 5022 OE2 GLU A 681 6732 12398 8610 1032 312 -117 O ATOM 5023 N ARG A 682 23.226 9.958 149.363 1.00 49.02 N ANISOU 5023 N ARG A 682 4462 8287 5875 532 221 -85 N ATOM 5024 CA ARG A 682 23.780 8.921 148.557 1.00 49.61 C ANISOU 5024 CA ARG A 682 4620 8228 6001 328 195 -76 C ATOM 5025 C ARG A 682 23.273 7.597 149.088 1.00 51.44 C ANISOU 5025 C ARG A 682 4758 8555 6232 104 223 -45 C ATOM 5026 O ARG A 682 23.071 6.663 148.350 1.00 52.07 O ANISOU 5026 O ARG A 682 4831 8627 6326 -71 185 -41 O ATOM 5027 CB ARG A 682 25.294 8.976 148.643 1.00 47.16 C ANISOU 5027 CB ARG A 682 4528 7632 5758 336 211 -86 C ATOM 5028 CG ARG A 682 25.982 8.031 147.710 1.00 47.34 C ANISOU 5028 CG ARG A 682 4653 7503 5831 172 179 -92 C ATOM 5029 CD ARG A 682 27.332 7.601 148.221 1.00 46.36 C ANISOU 5029 CD ARG A 682 4640 7208 5768 51 224 -79 C ATOM 5030 NE ARG A 682 27.848 6.527 147.387 1.00 45.77 N ANISOU 5030 NE ARG A 682 4663 6988 5738 -90 193 -94 N ATOM 5031 CZ ARG A 682 29.092 6.427 146.975 1.00 46.07 C ANISOU 5031 CZ ARG A 682 4859 6827 5820 -61 188 -117 C ATOM 5032 NH1 ARG A 682 29.967 7.328 147.321 1.00 47.87 N ANISOU 5032 NH1 ARG A 682 5167 6967 6054 88 209 -121 N ATOM 5033 NH2 ARG A 682 29.449 5.426 146.210 1.00 45.29 N ANISOU 5033 NH2 ARG A 682 4835 6620 5754 -183 162 -140 N ATOM 5034 N ASN A 683 23.091 7.498 150.389 1.00 62.37 N ANISOU 5034 N ASN A 683 6071 10032 7593 100 287 -21 N ATOM 5035 CA ASN A 683 22.632 6.248 150.985 1.00 62.33 C ANISOU 5035 CA ASN A 683 5982 10121 7581 -122 314 22 C ATOM 5036 C ASN A 683 21.257 5.864 150.470 1.00 59.43 C ANISOU 5036 C ASN A 683 5412 10016 7154 -214 279 31 C ATOM 5037 O ASN A 683 20.981 4.680 150.250 1.00 58.25 O ANISOU 5037 O ASN A 683 5233 9886 7013 -443 261 57 O ATOM 5038 CB ASN A 683 22.601 6.365 152.509 1.00 66.84 C ANISOU 5038 CB ASN A 683 6514 10759 8125 -94 392 48 C ATOM 5039 CG ASN A 683 23.974 6.515 153.112 1.00 68.09 C ANISOU 5039 CG ASN A 683 6866 10664 8340 -50 424 46 C ATOM 5040 OD1 ASN A 683 24.975 6.563 152.404 1.00 68.13 O ANISOU 5040 OD1 ASN A 683 7031 10447 8407 -35 392 25 O ATOM 5041 ND2 ASN A 683 24.029 6.592 154.436 1.00 70.09 N ANISOU 5041 ND2 ASN A 683 7100 10964 8566 -31 488 69 N ATOM 5042 N LEU A 684 20.377 6.846 150.288 1.00 55.23 N ANISOU 5042 N LEU A 684 4738 9689 6560 -37 265 11 N ATOM 5043 CA LEU A 684 19.022 6.550 149.845 1.00 53.15 C ANISOU 5043 CA LEU A 684 4255 9709 6229 -111 231 21 C ATOM 5044 C LEU A 684 18.980 6.215 148.362 1.00 50.64 C ANISOU 5044 C LEU A 684 3969 9342 5928 -190 145 3 C ATOM 5045 O LEU A 684 18.304 5.263 147.965 1.00 51.71 O ANISOU 5045 O LEU A 684 4006 9599 6044 -395 113 19 O ATOM 5046 CB LEU A 684 18.100 7.726 150.161 1.00 51.82 C ANISOU 5046 CB LEU A 684 3919 9784 5985 126 243 2 C ATOM 5047 CG LEU A 684 16.627 7.587 149.775 1.00 53.91 C ANISOU 5047 CG LEU A 684 3925 10388 6170 90 210 10 C ATOM 5048 CD1 LEU A 684 16.037 6.299 150.317 1.00 54.99 C ANISOU 5048 CD1 LEU A 684 3936 10677 6281 -193 240 58 C ATOM 5049 CD2 LEU A 684 15.830 8.782 150.268 1.00 55.09 C ANISOU 5049 CD2 LEU A 684 3919 10766 6247 356 232 -15 C ATOM 5050 N VAL A 685 19.701 6.967 147.532 1.00 49.53 N ANISOU 5050 N VAL A 685 3973 9027 5820 -41 105 -31 N ATOM 5051 CA VAL A 685 19.729 6.672 146.102 1.00 49.52 C ANISOU 5051 CA VAL A 685 4014 8977 5826 -112 24 -51 C ATOM 5052 C VAL A 685 20.240 5.258 145.863 1.00 49.11 C ANISOU 5052 C VAL A 685 4059 8777 5824 -378 18 -45 C ATOM 5053 O VAL A 685 19.642 4.478 145.114 1.00 50.86 O ANISOU 5053 O VAL A 685 4210 9089 6023 -546 -34 -49 O ATOM 5054 CB VAL A 685 20.589 7.706 145.357 1.00 48.32 C ANISOU 5054 CB VAL A 685 4024 8637 5698 80 -7 -79 C ATOM 5055 CG1 VAL A 685 20.699 7.338 143.893 1.00 48.30 C ANISOU 5055 CG1 VAL A 685 4076 8581 5697 -6 -85 -99 C ATOM 5056 CG2 VAL A 685 20.014 9.097 145.521 1.00 48.98 C ANISOU 5056 CG2 VAL A 685 4024 8856 5732 346 -14 -85 C ATOM 5057 N ASP A 686 21.349 4.904 146.507 1.00 49.54 N ANISOU 5057 N ASP A 686 4278 8600 5944 -417 67 -39 N ATOM 5058 CA ASP A 686 22.002 3.630 146.242 1.00 49.77 C ANISOU 5058 CA ASP A 686 4434 8447 6030 -634 57 -41 C ATOM 5059 C ASP A 686 21.261 2.449 146.850 1.00 49.85 C ANISOU 5059 C ASP A 686 4341 8575 6023 -868 70 -1 C ATOM 5060 O ASP A 686 21.337 1.339 146.313 1.00 49.75 O ANISOU 5060 O ASP A 686 4388 8481 6036 -1071 33 -7 O ATOM 5061 CB ASP A 686 23.438 3.662 146.757 1.00 50.42 C ANISOU 5061 CB ASP A 686 4718 8255 6185 -584 102 -45 C ATOM 5062 CG ASP A 686 24.291 4.680 146.038 1.00 50.90 C ANISOU 5062 CG ASP A 686 4902 8174 6264 -399 83 -82 C ATOM 5063 OD1 ASP A 686 23.888 5.157 144.955 1.00 52.29 O ANISOU 5063 OD1 ASP A 686 5041 8423 6404 -338 27 -106 O ATOM 5064 OD2 ASP A 686 25.370 5.006 146.563 1.00 49.38 O ANISOU 5064 OD2 ASP A 686 4844 7803 6117 -319 123 -83 O ATOM 5065 N THR A 687 20.560 2.647 147.963 1.00 49.43 N ANISOU 5065 N THR A 687 4143 8711 5927 -851 122 40 N ATOM 5066 CA THR A 687 19.724 1.571 148.479 1.00 50.93 C ANISOU 5066 CA THR A 687 4215 9052 6086 -1088 131 88 C ATOM 5067 C THR A 687 18.584 1.265 147.519 1.00 52.54 C ANISOU 5067 C THR A 687 4261 9469 6233 -1200 63 76 C ATOM 5068 O THR A 687 18.292 0.097 147.237 1.00 53.44 O ANISOU 5068 O THR A 687 4377 9578 6351 -1450 29 90 O ATOM 5069 CB THR A 687 19.165 1.942 149.851 1.00 51.63 C ANISOU 5069 CB THR A 687 4163 9333 6123 -1034 206 132 C ATOM 5070 OG1 THR A 687 20.216 2.503 150.661 1.00 50.12 O ANISOU 5070 OG1 THR A 687 4111 8958 5972 -882 262 131 O ATOM 5071 CG2 THR A 687 18.586 0.711 150.534 1.00 52.99 C ANISOU 5071 CG2 THR A 687 4260 9603 6272 -1308 225 195 C ATOM 5072 N ARG A 688 17.913 2.312 147.031 1.00 53.05 N ANISOU 5072 N ARG A 688 4188 9726 6241 -1015 37 52 N ATOM 5073 CA ARG A 688 16.893 2.137 146.006 1.00 54.53 C ANISOU 5073 CA ARG A 688 4228 10119 6372 -1095 -38 37 C ATOM 5074 C ARG A 688 17.460 1.428 144.788 1.00 54.03 C ANISOU 5074 C ARG A 688 4322 9855 6351 -1226 -108 -2 C ATOM 5075 O ARG A 688 16.834 0.510 144.251 1.00 55.31 O ANISOU 5075 O ARG A 688 4423 10105 6488 -1448 -160 -2 O ATOM 5076 CB ARG A 688 16.311 3.492 145.613 1.00 54.93 C ANISOU 5076 CB ARG A 688 4149 10356 6366 -829 -61 16 C ATOM 5077 CG ARG A 688 15.533 4.145 146.732 1.00 55.91 C ANISOU 5077 CG ARG A 688 4083 10729 6431 -700 2 42 C ATOM 5078 CD ARG A 688 15.251 5.600 146.446 1.00 56.01 C ANISOU 5078 CD ARG A 688 4031 10843 6406 -387 -16 14 C ATOM 5079 NE ARG A 688 14.149 6.096 147.260 1.00 57.64 N ANISOU 5079 NE ARG A 688 3996 11371 6534 -284 24 29 N ATOM 5080 CZ ARG A 688 13.793 7.372 147.329 1.00 58.05 C ANISOU 5080 CZ ARG A 688 3972 11539 6546 8 23 5 C ATOM 5081 NH1 ARG A 688 14.457 8.284 146.635 1.00 56.93 N ANISOU 5081 NH1 ARG A 688 3986 11206 6437 211 -19 -26 N ATOM 5082 NH2 ARG A 688 12.775 7.736 148.092 1.00 59.71 N ANISOU 5082 NH2 ARG A 688 3953 12054 6679 98 64 12 N ATOM 5083 N TYR A 689 18.654 1.833 144.352 1.00 52.26 N ANISOU 5083 N TYR A 689 4304 9366 6187 -1099 -109 -38 N ATOM 5084 CA TYR A 689 19.265 1.228 143.175 1.00 51.78 C ANISOU 5084 CA TYR A 689 4397 9118 6160 -1199 -169 -84 C ATOM 5085 C TYR A 689 19.550 -0.248 143.418 1.00 52.06 C ANISOU 5085 C TYR A 689 4530 9010 6239 -1467 -167 -77 C ATOM 5086 O TYR A 689 19.178 -1.106 142.608 1.00 53.05 O ANISOU 5086 O TYR A 689 4657 9150 6350 -1656 -230 -102 O ATOM 5087 CB TYR A 689 20.534 2.007 142.797 1.00 49.89 C ANISOU 5087 CB TYR A 689 4348 8639 5970 -1003 -158 -118 C ATOM 5088 CG TYR A 689 21.195 1.628 141.465 1.00 49.40 C ANISOU 5088 CG TYR A 689 4436 8408 5926 -1057 -216 -175 C ATOM 5089 CD1 TYR A 689 20.803 0.512 140.754 1.00 50.46 C ANISOU 5089 CD1 TYR A 689 4568 8559 6048 -1281 -272 -202 C ATOM 5090 CD2 TYR A 689 22.222 2.392 140.928 1.00 47.98 C ANISOU 5090 CD2 TYR A 689 4402 8057 5771 -889 -214 -204 C ATOM 5091 CE1 TYR A 689 21.405 0.163 139.569 1.00 50.12 C ANISOU 5091 CE1 TYR A 689 4662 8369 6013 -1324 -321 -262 C ATOM 5092 CE2 TYR A 689 22.830 2.039 139.728 1.00 47.64 C ANISOU 5092 CE2 TYR A 689 4488 7879 5735 -939 -260 -258 C ATOM 5093 CZ TYR A 689 22.411 0.920 139.055 1.00 48.72 C ANISOU 5093 CZ TYR A 689 4617 8038 5855 -1151 -312 -291 C ATOM 5094 OH TYR A 689 22.983 0.531 137.861 1.00 48.54 O ANISOU 5094 OH TYR A 689 4721 7891 5829 -1201 -357 -354 O ATOM 5095 N ALA A 690 20.187 -0.565 144.541 1.00 51.32 N ANISOU 5095 N ALA A 690 4524 8777 6197 -1488 -100 -42 N ATOM 5096 CA ALA A 690 20.571 -1.946 144.799 1.00 51.57 C ANISOU 5096 CA ALA A 690 4678 8636 6278 -1723 -102 -30 C ATOM 5097 C ALA A 690 19.351 -2.853 144.909 1.00 53.66 C ANISOU 5097 C ALA A 690 4795 9101 6491 -1976 -133 6 C ATOM 5098 O ALA A 690 19.293 -3.908 144.270 1.00 54.45 O ANISOU 5098 O ALA A 690 4969 9115 6604 -2185 -189 -18 O ATOM 5099 CB ALA A 690 21.422 -2.020 146.066 1.00 50.51 C ANISOU 5099 CB ALA A 690 4649 8342 6200 -1681 -27 14 C ATOM 5100 N SER A 691 18.365 -2.458 145.723 1.00 58.94 N ANISOU 5100 N SER A 691 5254 10044 7098 -1965 -97 60 N ATOM 5101 CA SER A 691 17.177 -3.285 145.928 1.00 60.88 C ANISOU 5101 CA SER A 691 5338 10511 7285 -2217 -118 104 C ATOM 5102 C SER A 691 16.467 -3.544 144.616 1.00 63.73 C ANISOU 5102 C SER A 691 5625 10988 7601 -2323 -210 57 C ATOM 5103 O SER A 691 16.022 -4.660 144.334 1.00 66.79 O ANISOU 5103 O SER A 691 6017 11383 7979 -2595 -259 63 O ATOM 5104 CB SER A 691 16.218 -2.591 146.885 1.00 63.06 C ANISOU 5104 CB SER A 691 5371 11104 7485 -2137 -62 158 C ATOM 5105 OG SER A 691 16.784 -2.458 148.158 1.00 62.70 O ANISOU 5105 OG SER A 691 5385 10971 7468 -2071 22 203 O ATOM 5106 N ARG A 692 16.343 -2.507 143.812 1.00 57.60 N ANISOU 5106 N ARG A 692 4786 10305 6795 -2113 -239 12 N ATOM 5107 CA ARG A 692 15.689 -2.626 142.526 1.00 58.70 C ANISOU 5107 CA ARG A 692 4851 10570 6884 -2185 -331 -33 C ATOM 5108 C ARG A 692 16.366 -3.663 141.639 1.00 58.48 C ANISOU 5108 C ARG A 692 5037 10279 6903 -2360 -388 -89 C ATOM 5109 O ARG A 692 15.714 -4.581 141.137 1.00 60.09 O ANISOU 5109 O ARG A 692 5201 10555 7074 -2605 -451 -100 O ATOM 5110 CB ARG A 692 15.703 -1.271 141.859 1.00 57.98 C ANISOU 5110 CB ARG A 692 4708 10560 6763 -1897 -349 -66 C ATOM 5111 CG ARG A 692 15.366 -1.352 140.431 1.00 58.69 C ANISOU 5111 CG ARG A 692 4784 10706 6811 -1943 -445 -119 C ATOM 5112 CD ARG A 692 14.168 -0.563 140.175 1.00 60.09 C ANISOU 5112 CD ARG A 692 4706 11230 6897 -1841 -480 -103 C ATOM 5113 NE ARG A 692 13.650 -0.723 138.835 1.00 61.17 N ANISOU 5113 NE ARG A 692 4795 11472 6976 -1916 -582 -146 N ATOM 5114 CZ ARG A 692 13.192 0.302 138.122 1.00 61.52 C ANISOU 5114 CZ ARG A 692 4728 11688 6960 -1717 -631 -156 C ATOM 5115 NH1 ARG A 692 12.711 0.093 136.893 1.00 62.62 N ANISOU 5115 NH1 ARG A 692 4823 11930 7039 -1802 -729 -192 N ATOM 5116 NH2 ARG A 692 13.241 1.558 138.611 1.00 60.84 N ANISOU 5116 NH2 ARG A 692 4586 11659 6870 -1426 -587 -131 N ATOM 5117 N VAL A 693 17.680 -3.542 141.439 1.00 56.61 N ANISOU 5117 N VAL A 693 5028 9741 6741 -2238 -367 -128 N ATOM 5118 CA VAL A 693 18.387 -4.449 140.536 1.00 56.41 C ANISOU 5118 CA VAL A 693 5209 9469 6758 -2367 -419 -195 C ATOM 5119 C VAL A 693 18.183 -5.891 140.955 1.00 57.68 C ANISOU 5119 C VAL A 693 5430 9545 6941 -2666 -434 -174 C ATOM 5120 O VAL A 693 17.960 -6.777 140.121 1.00 58.81 O ANISOU 5120 O VAL A 693 5632 9642 7071 -2862 -506 -223 O ATOM 5121 CB VAL A 693 19.876 -4.079 140.486 1.00 54.26 C ANISOU 5121 CB VAL A 693 5153 8902 6561 -2180 -377 -230 C ATOM 5122 CG1 VAL A 693 20.687 -5.187 139.842 1.00 54.17 C ANISOU 5122 CG1 VAL A 693 5364 8618 6601 -2320 -413 -296 C ATOM 5123 CG2 VAL A 693 20.020 -2.830 139.714 1.00 53.41 C ANISOU 5123 CG2 VAL A 693 5010 8863 6419 -1942 -391 -261 C ATOM 5124 N VAL A 694 18.240 -6.143 142.258 1.00 62.54 N ANISOU 5124 N VAL A 694 6039 10138 7586 -2710 -369 -99 N ATOM 5125 CA VAL A 694 17.996 -7.482 142.769 1.00 62.81 C ANISOU 5125 CA VAL A 694 6131 10097 7638 -3000 -382 -60 C ATOM 5126 C VAL A 694 16.591 -7.939 142.417 1.00 64.19 C ANISOU 5126 C VAL A 694 6115 10548 7728 -3233 -444 -45 C ATOM 5127 O VAL A 694 16.386 -9.078 141.987 1.00 64.63 O ANISOU 5127 O VAL A 694 6256 10516 7786 -3492 -507 -65 O ATOM 5128 CB VAL A 694 18.246 -7.503 144.284 1.00 62.79 C ANISOU 5128 CB VAL A 694 6131 10062 7665 -2985 -298 30 C ATOM 5129 CG1 VAL A 694 17.985 -8.882 144.848 1.00 64.31 C ANISOU 5129 CG1 VAL A 694 6392 10172 7871 -3292 -315 85 C ATOM 5130 CG2 VAL A 694 19.668 -7.057 144.567 1.00 62.06 C ANISOU 5130 CG2 VAL A 694 6226 9700 7653 -2760 -246 9 C ATOM 5131 N LEU A 695 15.604 -7.062 142.593 1.00 61.98 N ANISOU 5131 N LEU A 695 5574 10607 7370 -3145 -429 -10 N ATOM 5132 CA LEU A 695 14.228 -7.426 142.283 1.00 64.33 C ANISOU 5132 CA LEU A 695 5657 11208 7578 -3358 -486 8 C ATOM 5133 C LEU A 695 14.092 -7.839 140.821 1.00 65.04 C ANISOU 5133 C LEU A 695 5805 11262 7646 -3461 -589 -79 C ATOM 5134 O LEU A 695 13.745 -8.984 140.519 1.00 66.62 O ANISOU 5134 O LEU A 695 6058 11417 7837 -3753 -650 -89 O ATOM 5135 CB LEU A 695 13.295 -6.261 142.619 1.00 64.78 C ANISOU 5135 CB LEU A 695 5424 11634 7555 -3182 -453 45 C ATOM 5136 CG LEU A 695 11.867 -6.312 142.071 1.00 67.10 C ANISOU 5136 CG LEU A 695 5456 12295 7744 -3324 -519 50 C ATOM 5137 CD1 LEU A 695 11.185 -7.609 142.418 1.00 69.23 C ANISOU 5137 CD1 LEU A 695 5688 12628 7987 -3701 -546 97 C ATOM 5138 CD2 LEU A 695 11.069 -5.160 142.619 1.00 67.49 C ANISOU 5138 CD2 LEU A 695 5231 12688 7724 -3116 -471 90 C ATOM 5139 N ASN A 696 14.400 -6.917 139.902 1.00 63.94 N ANISOU 5139 N ASN A 696 5670 11129 7495 -3227 -612 -142 N ATOM 5140 CA ASN A 696 14.310 -7.197 138.471 1.00 64.55 C ANISOU 5140 CA ASN A 696 5800 11186 7540 -3298 -709 -228 C ATOM 5141 C ASN A 696 15.052 -8.468 138.095 1.00 64.64 C ANISOU 5141 C ASN A 696 6077 10872 7612 -3499 -745 -284 C ATOM 5142 O ASN A 696 14.535 -9.297 137.341 1.00 66.31 O ANISOU 5142 O ASN A 696 6299 11111 7784 -3733 -829 -329 O ATOM 5143 CB ASN A 696 14.862 -6.018 137.675 1.00 62.97 C ANISOU 5143 CB ASN A 696 5627 10963 7334 -2994 -712 -278 C ATOM 5144 CG ASN A 696 14.052 -4.764 137.865 1.00 63.19 C ANISOU 5144 CG ASN A 696 5403 11310 7295 -2790 -697 -233 C ATOM 5145 OD1 ASN A 696 14.295 -3.752 137.213 1.00 64.41 O ANISOU 5145 OD1 ASN A 696 5352 11713 7410 -2855 -673 -167 O ATOM 5146 ND2 ASN A 696 13.073 -4.822 138.758 1.00 62.11 N ANISOU 5146 ND2 ASN A 696 5283 11171 7144 -2538 -712 -267 N ATOM 5147 N ALA A 697 16.264 -8.644 138.616 1.00 63.48 N ANISOU 5147 N ALA A 697 6147 10415 7559 -3408 -685 -287 N ATOM 5148 CA ALA A 697 17.038 -9.834 138.288 1.00 68.06 C ANISOU 5148 CA ALA A 697 6989 10669 8200 -3566 -718 -346 C ATOM 5149 C ALA A 697 16.350 -11.100 138.772 1.00 68.07 C ANISOU 5149 C ALA A 697 6994 10674 8195 -3906 -753 -303 C ATOM 5150 O ALA A 697 16.486 -12.155 138.145 1.00 68.92 O ANISOU 5150 O ALA A 697 7265 10605 8315 -4103 -821 -367 O ATOM 5151 CB ALA A 697 18.441 -9.732 138.883 1.00 61.54 C ANISOU 5151 CB ALA A 697 6370 9539 7474 -3388 -644 -346 C ATOM 5152 N LEU A 698 15.599 -11.016 139.867 1.00 65.99 N ANISOU 5152 N LEU A 698 6555 10612 7906 -3983 -709 -197 N ATOM 5153 CA LEU A 698 14.914 -12.200 140.368 1.00 68.14 C ANISOU 5153 CA LEU A 698 6824 10902 8164 -4324 -741 -142 C ATOM 5154 C LEU A 698 13.711 -12.550 139.501 1.00 72.76 C ANISOU 5154 C LEU A 698 7255 11734 8655 -4552 -835 -171 C ATOM 5155 O LEU A 698 13.533 -13.711 139.117 1.00 75.00 O ANISOU 5155 O LEU A 698 7663 11894 8940 -4834 -908 -202 O ATOM 5156 CB LEU A 698 14.490 -11.987 141.820 1.00 68.78 C ANISOU 5156 CB LEU A 698 6757 11141 8233 -4340 -659 -15 C ATOM 5157 CG LEU A 698 15.607 -11.953 142.867 1.00 68.28 C ANISOU 5157 CG LEU A 698 6863 10820 8259 -4199 -574 31 C ATOM 5158 CD1 LEU A 698 15.053 -11.617 144.237 1.00 66.97 C ANISOU 5158 CD1 LEU A 698 6516 10870 8058 -4206 -494 150 C ATOM 5159 CD2 LEU A 698 16.381 -13.263 142.911 1.00 66.96 C ANISOU 5159 CD2 LEU A 698 6992 10279 8171 -4377 -609 15 C ATOM 5160 N GLN A 699 12.873 -11.559 139.189 1.00 70.67 N ANISOU 5160 N GLN A 699 6723 11819 8308 -4433 -839 -164 N ATOM 5161 CA GLN A 699 11.708 -11.813 138.352 1.00 72.88 C ANISOU 5161 CA GLN A 699 6833 12368 8492 -4635 -933 -190 C ATOM 5162 C GLN A 699 12.123 -12.438 137.028 1.00 73.17 C ANISOU 5162 C GLN A 699 7071 12197 8535 -4723 -1027 -310 C ATOM 5163 O GLN A 699 11.655 -13.523 136.664 1.00 75.19 O ANISOU 5163 O GLN A 699 7382 12422 8765 -5036 -1105 -335 O ATOM 5164 CB GLN A 699 10.942 -10.512 138.114 1.00 72.81 C ANISOU 5164 CB GLN A 699 6530 12734 8401 -4418 -925 -175 C ATOM 5165 CG GLN A 699 11.083 -9.513 139.230 1.00 71.43 C ANISOU 5165 CG GLN A 699 6240 12658 8244 -4165 -816 -98 C ATOM 5166 CD GLN A 699 10.024 -8.452 139.214 1.00 72.20 C ANISOU 5166 CD GLN A 699 6012 13173 8248 -4021 -813 -67 C ATOM 5167 OE1 GLN A 699 8.976 -8.592 139.848 1.00 74.00 O ANISOU 5167 OE1 GLN A 699 6008 13698 8410 -4166 -801 3 O ATOM 5168 NE2 GLN A 699 10.294 -7.364 138.511 1.00 70.93 N ANISOU 5168 NE2 GLN A 699 5830 13044 8077 -3727 -824 -115 N ATOM 5169 N GLU A 700 13.040 -11.778 136.316 1.00 71.35 N ANISOU 5169 N GLU A 700 6962 11812 8336 -4454 -1018 -388 N ATOM 5170 CA GLU A 700 13.476 -12.246 135.007 1.00 71.55 C ANISOU 5170 CA GLU A 700 7169 11662 8355 -4502 -1099 -511 C ATOM 5171 C GLU A 700 14.141 -13.612 135.089 1.00 74.95 C ANISOU 5171 C GLU A 700 7888 11731 8857 -4711 -1122 -554 C ATOM 5172 O GLU A 700 14.082 -14.388 134.130 1.00 77.35 O ANISOU 5172 O GLU A 700 8314 11939 9136 -4885 -1210 -648 O ATOM 5173 CB GLU A 700 14.414 -11.217 134.378 1.00 77.05 C ANISOU 5173 CB GLU A 700 7939 12265 9071 -4161 -1068 -569 C ATOM 5174 CG GLU A 700 15.514 -11.801 133.521 1.00 77.09 C ANISOU 5174 CG GLU A 700 8235 11934 9122 -4148 -1097 -686 C ATOM 5175 CD GLU A 700 16.176 -10.724 132.686 1.00 75.67 C ANISOU 5175 CD GLU A 700 8075 11751 8924 -3850 -1083 -742 C ATOM 5176 OE1 GLU A 700 15.738 -9.563 132.776 1.00 74.10 O ANISOU 5176 OE1 GLU A 700 7675 11797 8682 -3666 -1060 -687 O ATOM 5177 OE2 GLU A 700 17.126 -11.026 131.940 1.00 77.15 O ANISOU 5177 OE2 GLU A 700 8479 11696 9138 -3799 -1095 -840 O ATOM 5178 N HIS A 701 14.774 -13.929 136.217 1.00 74.02 N ANISOU 5178 N HIS A 701 7890 11409 8827 -4696 -1049 -489 N ATOM 5179 CA HIS A 701 15.380 -15.248 136.354 1.00 75.98 C ANISOU 5179 CA HIS A 701 8418 11307 9145 -4888 -1076 -521 C ATOM 5180 C HIS A 701 14.331 -16.337 136.536 1.00 80.53 C ANISOU 5180 C HIS A 701 8953 11967 9677 -5279 -1147 -482 C ATOM 5181 O HIS A 701 14.536 -17.467 136.080 1.00 85.12 O ANISOU 5181 O HIS A 701 9753 12307 10280 -5487 -1219 -550 O ATOM 5182 CB HIS A 701 16.366 -15.280 137.526 1.00 75.74 C ANISOU 5182 CB HIS A 701 8527 11035 9217 -4756 -984 -455 C ATOM 5183 CG HIS A 701 17.107 -16.572 137.649 1.00 75.34 C ANISOU 5183 CG HIS A 701 8781 10601 9245 -4906 -1013 -490 C ATOM 5184 ND1 HIS A 701 16.798 -17.522 138.598 1.00 75.07 N ANISOU 5184 ND1 HIS A 701 8807 10481 9236 -5155 -1019 -399 N ATOM 5185 CD2 HIS A 701 18.134 -17.080 136.928 1.00 73.13 C ANISOU 5185 CD2 HIS A 701 8766 10002 9019 -4839 -1042 -606 C ATOM 5186 CE1 HIS A 701 17.606 -18.557 138.461 1.00 74.42 C ANISOU 5186 CE1 HIS A 701 9024 10028 9226 -5228 -1055 -456 C ATOM 5187 NE2 HIS A 701 18.426 -18.314 137.455 1.00 73.79 N ANISOU 5187 NE2 HIS A 701 9068 9804 9165 -5033 -1068 -587 N ATOM 5188 N PHE A 702 13.208 -16.020 137.177 1.00 82.13 N ANISOU 5188 N PHE A 702 8881 12510 9814 -5386 -1131 -377 N ATOM 5189 CA PHE A 702 12.175 -17.011 137.457 1.00 84.97 C ANISOU 5189 CA PHE A 702 9215 12940 10130 -5658 -1165 -313 C ATOM 5190 C PHE A 702 11.205 -17.210 136.301 1.00 85.20 C ANISOU 5190 C PHE A 702 9153 13156 10064 -5763 -1253 -376 C ATOM 5191 O PHE A 702 10.344 -18.094 136.380 1.00 86.70 O ANISOU 5191 O PHE A 702 9344 13385 10213 -5979 -1287 -335 O ATOM 5192 CB PHE A 702 11.403 -16.623 138.718 1.00 86.63 C ANISOU 5192 CB PHE A 702 9191 13418 10305 -5664 -1086 -165 C ATOM 5193 CG PHE A 702 12.215 -16.728 139.969 1.00 85.18 C ANISOU 5193 CG PHE A 702 9123 13035 10207 -5621 -1005 -86 C ATOM 5194 CD1 PHE A 702 13.134 -17.752 140.128 1.00 85.07 C ANISOU 5194 CD1 PHE A 702 9431 12607 10283 -5702 -1021 -107 C ATOM 5195 CD2 PHE A 702 12.083 -15.791 140.979 1.00 83.68 C ANISOU 5195 CD2 PHE A 702 8723 13066 10003 -5483 -914 7 C ATOM 5196 CE1 PHE A 702 13.895 -17.850 141.278 1.00 83.93 C ANISOU 5196 CE1 PHE A 702 9397 12278 10214 -5655 -951 -28 C ATOM 5197 CE2 PHE A 702 12.842 -15.880 142.130 1.00 82.41 C ANISOU 5197 CE2 PHE A 702 8670 12726 9915 -5444 -839 82 C ATOM 5198 CZ PHE A 702 13.748 -16.913 142.280 1.00 82.69 C ANISOU 5198 CZ PHE A 702 9027 12351 10039 -5534 -860 68 C ATOM 5199 N ARG A 703 11.309 -16.415 135.240 1.00 81.31 N ANISOU 5199 N ARG A 703 8580 12785 9530 -5622 -1294 -470 N ATOM 5200 CA ARG A 703 10.538 -16.655 134.031 1.00 82.61 C ANISOU 5200 CA ARG A 703 8696 13086 9607 -5716 -1385 -542 C ATOM 5201 C ARG A 703 11.353 -17.372 132.969 1.00 82.42 C ANISOU 5201 C ARG A 703 8963 12737 9615 -5756 -1454 -685 C ATOM 5202 O ARG A 703 10.921 -18.402 132.443 1.00 83.71 O ANISOU 5202 O ARG A 703 9244 12808 9754 -5949 -1520 -726 O ATOM 5203 CB ARG A 703 10.022 -15.347 133.446 1.00 81.91 C ANISOU 5203 CB ARG A 703 8328 13361 9434 -5533 -1397 -553 C ATOM 5204 CG ARG A 703 9.238 -14.469 134.379 1.00 81.99 C ANISOU 5204 CG ARG A 703 8033 13714 9404 -5435 -1328 -431 C ATOM 5205 CD ARG A 703 8.563 -13.351 133.591 1.00 82.34 C ANISOU 5205 CD ARG A 703 7819 14113 9353 -5269 -1365 -451 C ATOM 5206 NE ARG A 703 9.514 -12.537 132.836 1.00 80.08 N ANISOU 5206 NE ARG A 703 7592 13749 9084 -5060 -1386 -541 N ATOM 5207 CZ ARG A 703 9.892 -12.775 131.585 1.00 80.27 C ANISOU 5207 CZ ARG A 703 7763 13649 9084 -5079 -1466 -658 C ATOM 5208 NH1 ARG A 703 9.407 -13.815 130.927 1.00 83.94 N ANISOU 5208 NH1 ARG A 703 8333 14045 9513 -5295 -1535 -705 N ATOM 5209 NH2 ARG A 703 10.765 -11.976 130.991 1.00 78.42 N ANISOU 5209 NH2 ARG A 703 7625 13302 8870 -4790 -1445 -715 N ATOM 5210 N ALA A 704 12.524 -16.830 132.638 1.00 79.07 N ANISOU 5210 N ALA A 704 8658 12147 9240 -5571 -1438 -767 N ATOM 5211 CA ALA A 704 13.406 -17.482 131.683 1.00 78.99 C ANISOU 5211 CA ALA A 704 8935 11819 9259 -5580 -1491 -911 C ATOM 5212 C ALA A 704 13.766 -18.894 132.116 1.00 80.27 C ANISOU 5212 C ALA A 704 9377 11622 9501 -5743 -1497 -913 C ATOM 5213 O ALA A 704 14.211 -19.692 131.284 1.00 81.10 O ANISOU 5213 O ALA A 704 9717 11481 9618 -5792 -1554 -1032 O ATOM 5214 CB ALA A 704 14.672 -16.652 131.483 1.00 76.17 C ANISOU 5214 CB ALA A 704 8674 11314 8952 -5270 -1432 -969 C ATOM 5215 N HIS A 705 13.579 -19.224 133.393 1.00 83.43 N ANISOU 5215 N HIS A 705 9759 11991 9951 -5819 -1441 -784 N ATOM 5216 CA HIS A 705 13.760 -20.581 133.872 1.00 82.60 C ANISOU 5216 CA HIS A 705 9899 11575 9911 -5985 -1454 -763 C ATOM 5217 C HIS A 705 12.476 -21.219 134.374 1.00 86.87 C ANISOU 5217 C HIS A 705 10320 12288 10397 -6217 -1471 -654 C ATOM 5218 O HIS A 705 12.480 -22.422 134.657 1.00 88.37 O ANISOU 5218 O HIS A 705 10710 12238 10626 -6382 -1498 -637 O ATOM 5219 CB HIS A 705 14.822 -20.618 134.980 1.00 80.82 C ANISOU 5219 CB HIS A 705 9820 11092 9795 -5883 -1378 -705 C ATOM 5220 CG HIS A 705 16.195 -20.258 134.502 1.00 79.08 C ANISOU 5220 CG HIS A 705 9778 10633 9635 -5679 -1365 -822 C ATOM 5221 ND1 HIS A 705 17.154 -21.204 134.213 1.00 79.00 N ANISOU 5221 ND1 HIS A 705 10092 10225 9699 -5668 -1391 -915 N ATOM 5222 CD2 HIS A 705 16.760 -19.057 134.240 1.00 76.15 C ANISOU 5222 CD2 HIS A 705 9310 10367 9258 -5432 -1319 -857 C ATOM 5223 CE1 HIS A 705 18.255 -20.601 133.804 1.00 76.64 C ANISOU 5223 CE1 HIS A 705 9881 9807 9431 -5464 -1366 -1010 C ATOM 5224 NE2 HIS A 705 18.043 -19.297 133.811 1.00 74.96 N ANISOU 5224 NE2 HIS A 705 9419 9887 9176 -5255 -1305 -963 N ATOM 5225 N LYS A 706 11.384 -20.463 134.473 1.00 85.34 N ANISOU 5225 N LYS A 706 9811 12501 10113 -6229 -1459 -581 N ATOM 5226 CA LYS A 706 10.073 -20.987 134.853 1.00 88.08 C ANISOU 5226 CA LYS A 706 10017 13062 10389 -6447 -1475 -485 C ATOM 5227 C LYS A 706 10.147 -21.751 136.173 1.00 88.81 C ANISOU 5227 C LYS A 706 10215 12993 10537 -6565 -1426 -364 C ATOM 5228 O LYS A 706 9.823 -22.935 136.263 1.00 91.20 O ANISOU 5228 O LYS A 706 10668 13142 10841 -6780 -1469 -346 O ATOM 5229 CB LYS A 706 9.494 -21.864 133.741 1.00 90.68 C ANISOU 5229 CB LYS A 706 10435 13358 10661 -6633 -1577 -572 C ATOM 5230 N ILE A 707 10.603 -21.043 137.207 1.00 95.01 N ANISOU 5230 N ILE A 707 10922 13813 11365 -6419 -1335 -281 N ATOM 5231 CA ILE A 707 10.642 -21.609 138.550 1.00 97.29 C ANISOU 5231 CA ILE A 707 11277 13995 11694 -6510 -1280 -152 C ATOM 5232 C ILE A 707 9.351 -21.346 139.318 1.00100.93 C ANISOU 5232 C ILE A 707 11451 14838 12058 -6611 -1240 -22 C ATOM 5233 O ILE A 707 9.025 -22.102 140.245 1.00104.06 O ANISOU 5233 O ILE A 707 11901 15186 12452 -6773 -1221 84 O ATOM 5234 CB ILE A 707 11.847 -21.056 139.332 1.00 93.78 C ANISOU 5234 CB ILE A 707 10915 13373 11345 -6306 -1202 -127 C ATOM 5235 CG1 ILE A 707 13.127 -21.186 138.503 1.00 91.84 C ANISOU 5235 CG1 ILE A 707 10928 12783 11182 -6179 -1238 -268 C ATOM 5236 CG2 ILE A 707 12.015 -21.782 140.658 1.00 94.02 C ANISOU 5236 CG2 ILE A 707 11063 13239 11420 -6402 -1157 -1 C ATOM 5237 CD1 ILE A 707 13.509 -22.615 138.186 1.00 93.76 C ANISOU 5237 CD1 ILE A 707 11494 12651 11479 -6322 -1305 -322 C ATOM 5238 N ASP A 708 8.602 -20.308 138.947 1.00108.18 N ANISOU 5238 N ASP A 708 12072 16139 12891 -6515 -1230 -27 N ATOM 5239 CA ASP A 708 7.342 -19.955 139.598 1.00111.15 C ANISOU 5239 CA ASP A 708 12154 16913 13166 -6578 -1189 83 C ATOM 5240 C ASP A 708 7.533 -19.693 141.087 1.00107.35 C ANISOU 5240 C ASP A 708 11619 16461 12708 -6521 -1087 208 C ATOM 5241 O ASP A 708 6.637 -19.942 141.896 1.00109.44 O ANISOU 5241 O ASP A 708 11751 16928 12902 -6651 -1054 316 O ATOM 5242 CB ASP A 708 6.268 -21.021 139.363 1.00120.27 C ANISOU 5242 CB ASP A 708 13317 18135 14244 -6868 -1254 110 C ATOM 5243 CG ASP A 708 5.711 -20.984 137.945 1.00126.26 C ANISOU 5243 CG ASP A 708 14013 19019 14939 -6908 -1344 3 C ATOM 5244 OD1 ASP A 708 6.460 -20.603 137.017 1.00125.39 O ANISOU 5244 OD1 ASP A 708 13994 18777 14871 -6762 -1379 -113 O ATOM 5245 OD2 ASP A 708 4.523 -21.328 137.758 1.00130.42 O ANISOU 5245 OD2 ASP A 708 14400 19787 15366 -7087 -1381 37 O ATOM 5246 N THR A 709 8.718 -19.210 141.449 1.00 92.80 N ANISOU 5246 N THR A 709 9884 14417 10960 -6331 -1037 193 N ATOM 5247 CA THR A 709 8.928 -18.556 142.732 1.00 88.36 C ANISOU 5247 CA THR A 709 9210 13954 10410 -6204 -932 294 C ATOM 5248 C THR A 709 8.383 -17.142 142.609 1.00 84.23 C ANISOU 5248 C THR A 709 8360 13827 9818 -5997 -890 288 C ATOM 5249 O THR A 709 8.913 -16.333 141.844 1.00 82.31 O ANISOU 5249 O THR A 709 8091 13582 9602 -5808 -905 198 O ATOM 5250 CB THR A 709 10.410 -18.545 143.100 1.00 82.71 C ANISOU 5250 CB THR A 709 8731 12877 9818 -6076 -899 275 C ATOM 5251 OG1 THR A 709 10.828 -19.866 143.469 1.00 83.91 O ANISOU 5251 OG1 THR A 709 9171 12682 10027 -6253 -929 307 O ATOM 5252 CG2 THR A 709 10.672 -17.591 144.261 1.00 80.94 C ANISOU 5252 CG2 THR A 709 8357 12796 9600 -5897 -790 360 C ATOM 5253 N LYS A 710 7.305 -16.849 143.327 1.00 85.72 N ANISOU 5253 N LYS A 710 8299 14358 9911 -6024 -840 380 N ATOM 5254 CA LYS A 710 6.763 -15.500 143.303 1.00 84.98 C ANISOU 5254 CA LYS A 710 7896 14640 9751 -5800 -796 377 C ATOM 5255 C LYS A 710 7.778 -14.524 143.883 1.00 81.98 C ANISOU 5255 C LYS A 710 7513 14192 9443 -5541 -717 378 C ATOM 5256 O LYS A 710 8.666 -14.899 144.652 1.00 80.88 O ANISOU 5256 O LYS A 710 7560 13787 9382 -5557 -675 418 O ATOM 5257 CB LYS A 710 5.454 -15.431 144.085 1.00 87.29 C ANISOU 5257 CB LYS A 710 7941 15300 9927 -5873 -750 475 C ATOM 5258 N VAL A 711 7.660 -13.260 143.482 1.00 80.73 N ANISOU 5258 N VAL A 711 7147 14269 9257 -5294 -702 334 N ATOM 5259 CA VAL A 711 8.570 -12.205 143.915 1.00 77.97 C ANISOU 5259 CA VAL A 711 6772 13886 8967 -5029 -632 325 C ATOM 5260 C VAL A 711 7.723 -10.975 144.209 1.00 78.18 C ANISOU 5260 C VAL A 711 6473 14325 8907 -4808 -580 350 C ATOM 5261 O VAL A 711 7.257 -10.307 143.282 1.00 78.36 O ANISOU 5261 O VAL A 711 6349 14543 8882 -4687 -629 289 O ATOM 5262 CB VAL A 711 9.645 -11.878 142.866 1.00 75.81 C ANISOU 5262 CB VAL A 711 6646 13386 8771 -4914 -686 214 C ATOM 5263 CG1 VAL A 711 10.633 -10.883 143.425 1.00 73.11 C ANISOU 5263 CG1 VAL A 711 6366 12919 8494 -4568 -596 213 C ATOM 5264 CG2 VAL A 711 10.378 -13.131 142.425 1.00 75.97 C ANISOU 5264 CG2 VAL A 711 6992 13007 8867 -5122 -749 170 C ATOM 5265 N SER A 712 7.534 -10.666 145.486 1.00 78.86 N ANISOU 5265 N SER A 712 6455 14538 8968 -4743 -482 434 N ATOM 5266 CA SER A 712 6.654 -9.584 145.899 1.00 79.57 C ANISOU 5266 CA SER A 712 6248 15017 8966 -4533 -425 458 C ATOM 5267 C SER A 712 7.454 -8.441 146.513 1.00 76.36 C ANISOU 5267 C SER A 712 5800 14606 8609 -4236 -342 453 C ATOM 5268 O SER A 712 8.650 -8.554 146.784 1.00 75.48 O ANISOU 5268 O SER A 712 5880 14204 8595 -4220 -318 449 O ATOM 5269 CB SER A 712 5.595 -10.102 146.877 1.00 83.03 C ANISOU 5269 CB SER A 712 6572 15665 9309 -4688 -378 553 C ATOM 5270 OG SER A 712 6.191 -10.923 147.861 1.00 83.22 O ANISOU 5270 OG SER A 712 6786 15452 9383 -4846 -333 624 O ATOM 5271 N VAL A 713 6.766 -7.325 146.732 1.00 77.14 N ANISOU 5271 N VAL A 713 5649 15029 8634 -3992 -300 452 N ATOM 5272 CA VAL A 713 7.385 -6.065 147.117 1.00 75.73 C ANISOU 5272 CA VAL A 713 5403 14884 8487 -3666 -234 430 C ATOM 5273 C VAL A 713 6.632 -5.477 148.302 1.00 78.59 C ANISOU 5273 C VAL A 713 5571 15526 8763 -3528 -136 486 C ATOM 5274 O VAL A 713 5.396 -5.481 148.331 1.00 83.73 O ANISOU 5274 O VAL A 713 6042 16465 9308 -3559 -144 505 O ATOM 5275 CB VAL A 713 7.402 -5.080 145.930 1.00 74.01 C ANISOU 5275 CB VAL A 713 5135 14716 8268 -3406 -297 343 C ATOM 5276 CG1 VAL A 713 7.402 -3.664 146.372 1.00 72.84 C ANISOU 5276 CG1 VAL A 713 4868 14707 8100 -3023 -231 329 C ATOM 5277 CG2 VAL A 713 8.564 -5.331 145.076 1.00 73.02 C ANISOU 5277 CG2 VAL A 713 5323 14179 8244 -3373 -349 279 C ATOM 5278 N VAL A 714 7.384 -4.971 149.276 1.00 80.49 N ANISOU 5278 N VAL A 714 5852 15686 9044 -3375 -45 507 N ATOM 5279 CA VAL A 714 6.845 -4.286 150.442 1.00 81.74 C ANISOU 5279 CA VAL A 714 5849 16083 9125 -3202 54 544 C ATOM 5280 C VAL A 714 7.543 -2.940 150.563 1.00 80.39 C ANISOU 5280 C VAL A 714 5666 15885 8994 -2828 101 490 C ATOM 5281 O VAL A 714 8.727 -2.819 150.235 1.00 77.44 O ANISOU 5281 O VAL A 714 5567 15132 8723 -2712 86 451 O ATOM 5282 CB VAL A 714 7.044 -5.121 151.720 1.00 84.90 C ANISOU 5282 CB VAL A 714 6351 16387 9520 -3399 126 633 C ATOM 5283 CG1 VAL A 714 6.409 -4.433 152.922 1.00 87.72 C ANISOU 5283 CG1 VAL A 714 6537 17014 9780 -3229 225 664 C ATOM 5284 CG2 VAL A 714 6.468 -6.508 151.519 1.00 87.57 C ANISOU 5284 CG2 VAL A 714 6759 16684 9830 -3763 66 684 C ATOM 5285 N ARG A 715 6.812 -1.930 151.024 1.00 77.24 N ANISOU 5285 N ARG A 715 5056 15780 8512 -2580 151 478 N ATOM 5286 CA ARG A 715 7.373 -0.600 151.190 1.00 77.03 C ANISOU 5286 CA ARG A 715 5046 15709 8514 -2196 193 422 C ATOM 5287 C ARG A 715 7.742 -0.340 152.637 1.00 78.84 C ANISOU 5287 C ARG A 715 5301 15924 8731 -2108 309 457 C ATOM 5288 O ARG A 715 7.112 -0.853 153.566 1.00 80.74 O ANISOU 5288 O ARG A 715 5445 16336 8895 -2265 364 519 O ATOM 5289 CB ARG A 715 6.401 0.470 150.708 1.00 75.83 C ANISOU 5289 CB ARG A 715 4653 15876 8282 -1938 166 374 C ATOM 5290 CG ARG A 715 6.322 0.527 149.186 1.00 73.82 C ANISOU 5290 CG ARG A 715 4407 15589 8054 -1934 48 326 C ATOM 5291 CD ARG A 715 4.963 0.974 148.706 1.00 75.55 C ANISOU 5291 CD ARG A 715 4409 16132 8164 -1834 2 309 C ATOM 5292 NE ARG A 715 5.045 1.751 147.480 1.00 74.71 N ANISOU 5292 NE ARG A 715 4285 16022 8077 -1628 -87 250 N ATOM 5293 CZ ARG A 715 5.383 1.228 146.305 1.00 74.14 C ANISOU 5293 CZ ARG A 715 4299 15818 8051 -1783 -185 230 C ATOM 5294 NH1 ARG A 715 5.686 -0.080 146.198 1.00 74.34 N ANISOU 5294 NH1 ARG A 715 4453 15679 8115 -2141 -205 258 N ATOM 5295 NH2 ARG A 715 5.414 2.008 145.218 1.00 73.73 N ANISOU 5295 NH2 ARG A 715 4262 15749 8003 -1568 -266 179 N ATOM 5296 N GLY A 716 8.754 0.510 152.813 1.00 88.44 N ANISOU 5296 N GLY A 716 6708 16882 10014 -1826 337 410 N ATOM 5297 CA GLY A 716 9.346 0.690 154.126 1.00 89.42 C ANISOU 5297 CA GLY A 716 6917 16916 10141 -1753 437 437 C ATOM 5298 C GLY A 716 8.407 1.335 155.125 1.00 93.14 C ANISOU 5298 C GLY A 716 7116 17780 10494 -1624 523 445 C ATOM 5299 O GLY A 716 8.395 0.964 156.301 1.00 95.00 O ANISOU 5299 O GLY A 716 7325 18086 10685 -1732 607 502 O ATOM 5300 N GLN A 717 7.614 2.310 154.678 1.00 96.24 N ANISOU 5300 N GLN A 717 7302 18438 10827 -1385 504 388 N ATOM 5301 CA GLN A 717 6.721 2.995 155.606 1.00 97.66 C ANISOU 5301 CA GLN A 717 7333 18880 10892 -1200 569 375 C ATOM 5302 C GLN A 717 5.673 2.048 156.170 1.00 96.78 C ANISOU 5302 C GLN A 717 7113 18978 10679 -1472 584 443 C ATOM 5303 O GLN A 717 5.195 2.250 157.291 1.00 96.40 O ANISOU 5303 O GLN A 717 6991 19096 10541 -1417 660 457 O ATOM 5304 CB GLN A 717 6.053 4.183 154.919 1.00101.90 C ANISOU 5304 CB GLN A 717 7746 19582 11390 -877 523 298 C ATOM 5305 CG GLN A 717 7.032 5.148 154.280 1.00102.86 C ANISOU 5305 CG GLN A 717 7981 19497 11606 -601 495 233 C ATOM 5306 CD GLN A 717 6.717 5.403 152.823 1.00105.82 C ANISOU 5306 CD GLN A 717 8309 19896 12000 -539 382 200 C ATOM 5307 OE1 GLN A 717 5.580 5.228 152.384 1.00109.77 O ANISOU 5307 OE1 GLN A 717 8661 20623 12424 -599 333 207 O ATOM 5308 NE2 GLN A 717 7.726 5.813 152.062 1.00103.23 N ANISOU 5308 NE2 GLN A 717 8228 19224 11772 -413 326 163 N ATOM 5309 N PHE A 718 5.315 1.007 155.419 1.00 85.10 N ANISOU 5309 N PHE A 718 5633 17492 9209 -1770 511 485 N ATOM 5310 CA PHE A 718 4.374 0.025 155.940 1.00 83.52 C ANISOU 5310 CA PHE A 718 5350 17468 8915 -2053 521 556 C ATOM 5311 C PHE A 718 5.040 -0.881 156.965 1.00 81.32 C ANISOU 5311 C PHE A 718 5221 17016 8660 -2286 581 636 C ATOM 5312 O PHE A 718 4.442 -1.207 157.997 1.00 80.58 O ANISOU 5312 O PHE A 718 5059 17087 8470 -2382 637 688 O ATOM 5313 CB PHE A 718 3.782 -0.796 154.796 1.00 82.65 C ANISOU 5313 CB PHE A 718 5208 17390 8804 -2296 420 571 C ATOM 5314 CG PHE A 718 2.822 -1.850 155.251 1.00 84.02 C ANISOU 5314 CG PHE A 718 5310 17733 8882 -2602 421 646 C ATOM 5315 CD1 PHE A 718 1.545 -1.509 155.667 1.00 87.66 C ANISOU 5315 CD1 PHE A 718 5553 18550 9204 -2532 446 647 C ATOM 5316 CD2 PHE A 718 3.195 -3.182 155.267 1.00 82.49 C ANISOU 5316 CD2 PHE A 718 5273 17336 8733 -2958 394 716 C ATOM 5317 CE1 PHE A 718 0.658 -2.479 156.093 1.00 90.40 C ANISOU 5317 CE1 PHE A 718 5828 19066 9455 -2821 447 719 C ATOM 5318 CE2 PHE A 718 2.311 -4.159 155.693 1.00 85.30 C ANISOU 5318 CE2 PHE A 718 5574 17839 8997 -3243 391 790 C ATOM 5319 CZ PHE A 718 1.041 -3.806 156.105 1.00 89.11 C ANISOU 5319 CZ PHE A 718 5827 18694 9338 -3179 419 792 C ATOM 5320 N THR A 719 6.280 -1.296 156.702 1.00 77.27 N ANISOU 5320 N THR A 719 4914 16174 8271 -2378 566 649 N ATOM 5321 CA THR A 719 7.002 -2.108 157.675 1.00 77.04 C ANISOU 5321 CA THR A 719 5046 15956 8270 -2576 619 727 C ATOM 5322 C THR A 719 7.277 -1.334 158.959 1.00 76.88 C ANISOU 5322 C THR A 719 5008 15998 8204 -2359 725 723 C ATOM 5323 O THR A 719 7.313 -1.926 160.044 1.00 77.95 O ANISOU 5323 O THR A 719 5193 16130 8295 -2511 780 797 O ATOM 5324 CB THR A 719 8.310 -2.610 157.067 1.00 72.78 C ANISOU 5324 CB THR A 719 4733 15047 7874 -2687 578 732 C ATOM 5325 OG1 THR A 719 8.917 -1.561 156.303 1.00 70.82 O ANISOU 5325 OG1 THR A 719 4505 14710 7695 -2397 557 641 O ATOM 5326 CG2 THR A 719 8.058 -3.794 156.164 1.00 73.67 C ANISOU 5326 CG2 THR A 719 4915 15057 8017 -3004 481 762 C ATOM 5327 N SER A 720 7.454 -0.016 158.859 1.00 82.55 N ANISOU 5327 N SER A 720 5666 16771 8926 -2003 751 636 N ATOM 5328 CA SER A 720 7.739 0.782 160.045 1.00 81.99 C ANISOU 5328 CA SER A 720 5594 16746 8811 -1779 848 617 C ATOM 5329 C SER A 720 6.546 0.829 160.991 1.00 86.57 C ANISOU 5329 C SER A 720 6006 17644 9241 -1782 896 636 C ATOM 5330 O SER A 720 6.713 0.698 162.209 1.00 86.34 O ANISOU 5330 O SER A 720 6011 17634 9160 -1813 971 677 O ATOM 5331 CB SER A 720 8.164 2.190 159.635 1.00 82.01 C ANISOU 5331 CB SER A 720 5590 16716 8853 -1391 852 512 C ATOM 5332 OG SER A 720 9.406 2.156 158.949 1.00 80.91 O ANISOU 5332 OG SER A 720 5652 16243 8848 -1379 815 496 O ATOM 5333 N GLN A 721 5.334 1.013 160.457 1.00 92.93 N ANISOU 5333 N GLN A 721 6627 18712 9971 -1751 852 609 N ATOM 5334 CA GLN A 721 4.161 1.037 161.324 1.00 95.16 C ANISOU 5334 CA GLN A 721 6736 19317 10103 -1762 896 627 C ATOM 5335 C GLN A 721 3.777 -0.364 161.772 1.00 93.46 C ANISOU 5335 C GLN A 721 6535 19135 9841 -2156 893 739 C ATOM 5336 O GLN A 721 3.258 -0.538 162.879 1.00 91.37 O ANISOU 5336 O GLN A 721 6200 19051 9466 -2214 953 780 O ATOM 5337 CB GLN A 721 2.977 1.712 160.630 1.00 97.93 C ANISOU 5337 CB GLN A 721 6881 19947 10380 -1592 852 564 C ATOM 5338 CG GLN A 721 1.658 1.542 161.391 1.00102.03 C ANISOU 5338 CG GLN A 721 7206 20825 10738 -1660 886 592 C ATOM 5339 CD GLN A 721 0.457 1.914 160.569 1.00106.32 C ANISOU 5339 CD GLN A 721 7549 21638 11209 -1573 828 550 C ATOM 5340 OE1 GLN A 721 -0.567 1.215 160.583 1.00109.77 O ANISOU 5340 OE1 GLN A 721 7853 22305 11550 -1790 810 600 O ATOM 5341 NE2 GLN A 721 0.554 3.034 159.860 1.00107.63 N ANISOU 5341 NE2 GLN A 721 7695 21783 11415 -1250 797 460 N ATOM 5342 N LEU A 722 4.005 -1.370 160.927 1.00 89.43 N ANISOU 5342 N LEU A 722 6121 18453 9406 -2428 819 786 N ATOM 5343 CA LEU A 722 3.789 -2.745 161.363 1.00 88.65 C ANISOU 5343 CA LEU A 722 6084 18323 9276 -2806 809 895 C ATOM 5344 C LEU A 722 4.666 -3.060 162.564 1.00 87.83 C ANISOU 5344 C LEU A 722 6135 18048 9188 -2868 880 957 C ATOM 5345 O LEU A 722 4.194 -3.613 163.565 1.00 89.61 O ANISOU 5345 O LEU A 722 6329 18402 9316 -3028 920 1031 O ATOM 5346 CB LEU A 722 4.064 -3.719 160.211 1.00 86.02 C ANISOU 5346 CB LEU A 722 5872 17771 9039 -3063 712 922 C ATOM 5347 CG LEU A 722 3.557 -5.172 160.305 1.00 87.33 C ANISOU 5347 CG LEU A 722 6087 17929 9167 -3464 670 1021 C ATOM 5348 CD1 LEU A 722 3.861 -5.938 159.014 1.00 86.04 C ANISOU 5348 CD1 LEU A 722 6050 17537 9106 -3658 566 1017 C ATOM 5349 CD2 LEU A 722 4.052 -5.995 161.526 1.00 87.31 C ANISOU 5349 CD2 LEU A 722 6232 17788 9153 -3661 720 1124 C ATOM 5350 N ARG A 723 5.954 -2.715 162.479 1.00 83.58 N ANISOU 5350 N ARG A 723 5766 17225 8767 -2744 895 931 N ATOM 5351 CA ARG A 723 6.856 -2.945 163.603 1.00 85.38 C ANISOU 5351 CA ARG A 723 6146 17286 9009 -2781 962 988 C ATOM 5352 C ARG A 723 6.362 -2.232 164.852 1.00 87.45 C ANISOU 5352 C ARG A 723 6283 17802 9143 -2605 1052 973 C ATOM 5353 O ARG A 723 6.466 -2.764 165.962 1.00 90.10 O ANISOU 5353 O ARG A 723 6673 18139 9421 -2744 1100 1051 O ATOM 5354 CB ARG A 723 8.270 -2.484 163.252 1.00 82.45 C ANISOU 5354 CB ARG A 723 5949 16606 8773 -2629 967 947 C ATOM 5355 N ARG A 724 5.817 -1.025 164.687 1.00 89.43 N ANISOU 5355 N ARG A 724 6371 18264 9344 -2295 1071 872 N ATOM 5356 CA ARG A 724 5.219 -0.322 165.815 1.00 90.49 C ANISOU 5356 CA ARG A 724 6376 18660 9346 -2119 1149 843 C ATOM 5357 C ARG A 724 3.949 -1.018 166.286 1.00 92.46 C ANISOU 5357 C ARG A 724 6470 19204 9459 -2337 1149 908 C ATOM 5358 O ARG A 724 3.720 -1.150 167.495 1.00 94.71 O ANISOU 5358 O ARG A 724 6725 19619 9642 -2382 1213 950 O ATOM 5359 CB ARG A 724 4.926 1.128 165.433 1.00 92.38 C ANISOU 5359 CB ARG A 724 6498 19029 9572 -1728 1156 714 C ATOM 5360 N HIS A 725 3.113 -1.469 165.348 1.00 94.51 N ANISOU 5360 N HIS A 725 6626 19577 9706 -2477 1077 917 N ATOM 5361 CA HIS A 725 1.880 -2.157 165.718 1.00 97.88 C ANISOU 5361 CA HIS A 725 6899 20291 9998 -2697 1073 980 C ATOM 5362 C HIS A 725 2.181 -3.439 166.482 1.00 96.41 C ANISOU 5362 C HIS A 725 6849 19982 9801 -3043 1082 1108 C ATOM 5363 O HIS A 725 1.614 -3.685 167.552 1.00 98.21 O ANISOU 5363 O HIS A 725 6999 20415 9903 -3131 1132 1160 O ATOM 5364 CB HIS A 725 1.045 -2.455 164.473 1.00 95.42 C ANISOU 5364 CB HIS A 725 6479 20090 9687 -2798 986 967 C ATOM 5365 N TRP A 726 3.071 -4.269 165.949 1.00 98.30 N ANISOU 5365 N TRP A 726 7298 19885 10168 -3239 1030 1160 N ATOM 5366 CA TRP A 726 3.521 -5.430 166.694 1.00 98.66 C ANISOU 5366 CA TRP A 726 7512 19759 10218 -3535 1035 1281 C ATOM 5367 C TRP A 726 4.418 -4.991 167.857 1.00 97.30 C ANISOU 5367 C TRP A 726 7441 19484 10045 -3392 1118 1290 C ATOM 5368 O TRP A 726 4.797 -3.823 167.985 1.00 95.82 O ANISOU 5368 O TRP A 726 7217 19318 9871 -3073 1167 1197 O ATOM 5369 CB TRP A 726 4.252 -6.404 165.771 1.00 97.84 C ANISOU 5369 CB TRP A 726 7618 19303 10254 -3762 951 1324 C ATOM 5370 N GLY A 727 4.748 -5.946 168.721 1.00101.78 N ANISOU 5370 N GLY A 727 8142 19937 10591 -3633 1130 1403 N ATOM 5371 CA GLY A 727 5.581 -5.653 169.873 1.00 99.30 C ANISOU 5371 CA GLY A 727 7932 19530 10266 -3531 1204 1426 C ATOM 5372 C GLY A 727 7.059 -5.766 169.568 1.00 97.12 C ANISOU 5372 C GLY A 727 7902 18852 10146 -3506 1188 1433 C ATOM 5373 O GLY A 727 7.765 -6.576 170.175 1.00 93.35 O ANISOU 5373 O GLY A 727 7613 18161 9696 -3684 1186 1532 O ATOM 5374 N ILE A 728 7.540 -4.956 168.629 1.00 83.86 N ANISOU 5374 N ILE A 728 6226 17070 8566 -3282 1173 1332 N ATOM 5375 CA ILE A 728 8.914 -5.027 168.151 1.00 78.84 C ANISOU 5375 CA ILE A 728 5808 16064 8081 -3255 1151 1329 C ATOM 5376 C ILE A 728 9.726 -3.925 168.814 1.00 78.08 C ANISOU 5376 C ILE A 728 5741 15938 7987 -2957 1230 1267 C ATOM 5377 O ILE A 728 9.349 -2.747 168.768 1.00 77.16 O ANISOU 5377 O ILE A 728 5475 16016 7827 -2670 1268 1160 O ATOM 5378 CB ILE A 728 8.974 -4.910 166.620 1.00 77.67 C ANISOU 5378 CB ILE A 728 5657 15809 8043 -3224 1076 1261 C ATOM 5379 N GLU A 729 10.838 -4.308 169.432 1.00 84.48 N ANISOU 5379 N GLU A 729 6753 16498 8846 -3020 1250 1333 N ATOM 5380 CA GLU A 729 11.757 -3.384 170.077 1.00 86.40 C ANISOU 5380 CA GLU A 729 7059 16673 9095 -2768 1321 1284 C ATOM 5381 C GLU A 729 13.127 -3.507 169.424 1.00 85.38 C ANISOU 5381 C GLU A 729 7138 16185 9118 -2761 1290 1288 C ATOM 5382 O GLU A 729 13.601 -4.618 169.166 1.00 88.44 O ANISOU 5382 O GLU A 729 7692 16331 9581 -3013 1232 1380 O ATOM 5383 CB GLU A 729 11.858 -3.666 171.580 1.00 89.20 C ANISOU 5383 CB GLU A 729 7459 17087 9345 -2838 1381 1364 C ATOM 5384 N LYS A 730 13.757 -2.367 169.151 1.00 81.62 N ANISOU 5384 N LYS A 730 6659 15668 8685 -2470 1323 1184 N ATOM 5385 CA LYS A 730 15.071 -2.331 168.521 1.00 81.03 C ANISOU 5385 CA LYS A 730 6853 15168 8767 -2373 1256 1147 C ATOM 5386 C LYS A 730 16.137 -2.147 169.592 1.00 79.77 C ANISOU 5386 C LYS A 730 6876 14829 8606 -2279 1295 1169 C ATOM 5387 O LYS A 730 16.105 -1.168 170.346 1.00 83.72 O ANISOU 5387 O LYS A 730 7300 15487 9024 -2059 1368 1109 O ATOM 5388 CB LYS A 730 15.152 -1.207 167.490 1.00 82.64 C ANISOU 5388 CB LYS A 730 7035 15323 9041 -2072 1221 1001 C ATOM 5389 N THR A 731 17.074 -3.086 169.661 1.00 80.71 N ANISOU 5389 N THR A 731 7235 14621 8810 -2441 1242 1252 N ATOM 5390 CA THR A 731 18.202 -2.931 170.565 1.00 79.19 C ANISOU 5390 CA THR A 731 7231 14227 8630 -2345 1262 1271 C ATOM 5391 C THR A 731 19.110 -1.809 170.080 1.00 76.25 C ANISOU 5391 C THR A 731 6974 13649 8350 -2020 1240 1136 C ATOM 5392 O THR A 731 19.400 -1.692 168.888 1.00 74.53 O ANISOU 5392 O THR A 731 6827 13245 8248 -1952 1170 1069 O ATOM 5393 CB THR A 731 18.984 -4.238 170.680 1.00 76.69 C ANISOU 5393 CB THR A 731 7144 13605 8389 -2586 1200 1393 C ATOM 5394 OG1 THR A 731 19.065 -4.863 169.395 1.00 74.21 O ANISOU 5394 OG1 THR A 731 6915 13083 8200 -2690 1109 1380 O ATOM 5395 CG2 THR A 731 18.296 -5.175 171.647 1.00 80.75 C ANISOU 5395 CG2 THR A 731 7579 14322 8782 -2879 1242 1543 C ATOM 5396 N ARG A 732 19.551 -0.981 171.019 1.00 79.93 N ANISOU 5396 N ARG A 732 7460 14154 8755 -1828 1299 1096 N ATOM 5397 CA ARG A 732 20.351 0.195 170.704 1.00 79.77 C ANISOU 5397 CA ARG A 732 7537 13971 8801 -1521 1286 968 C ATOM 5398 C ARG A 732 21.672 -0.191 170.051 1.00 77.21 C ANISOU 5398 C ARG A 732 7473 13229 8634 -1522 1200 969 C ATOM 5399 O ARG A 732 22.465 -0.939 170.629 1.00 77.35 O ANISOU 5399 O ARG A 732 7649 13065 8676 -1643 1184 1056 O ATOM 5400 CB ARG A 732 20.591 0.989 171.989 1.00 83.92 C ANISOU 5400 CB ARG A 732 8052 14615 9220 -1362 1364 939 C ATOM 5401 CG ARG A 732 21.768 1.948 171.967 1.00 85.91 C ANISOU 5401 CG ARG A 732 8479 14622 9542 -1108 1342 842 C ATOM 5402 CD ARG A 732 21.693 2.910 173.140 1.00 89.36 C ANISOU 5402 CD ARG A 732 8857 15245 9851 -930 1424 786 C ATOM 5403 NE ARG A 732 20.592 3.855 172.984 1.00 92.64 N ANISOU 5403 NE ARG A 732 9059 15956 10184 -759 1473 688 N ATOM 5404 CZ ARG A 732 20.746 5.111 172.585 1.00 93.96 C ANISOU 5404 CZ ARG A 732 9243 16081 10377 -477 1466 553 C ATOM 5405 NH1 ARG A 732 21.957 5.578 172.313 1.00 93.25 N ANISOU 5405 NH1 ARG A 732 9366 15675 10389 -352 1414 502 N ATOM 5406 NH2 ARG A 732 19.691 5.902 172.459 1.00 95.58 N ANISOU 5406 NH2 ARG A 732 9250 16562 10504 -320 1507 470 N ATOM 5407 N ASP A 733 21.896 0.309 168.834 1.00 73.11 N ANISOU 5407 N ASP A 733 6993 12570 8217 -1386 1145 876 N ATOM 5408 CA ASP A 733 23.188 0.212 168.150 1.00 68.68 C ANISOU 5408 CA ASP A 733 6662 11638 7797 -1330 1073 848 C ATOM 5409 C ASP A 733 23.626 -1.239 167.946 1.00 65.99 C ANISOU 5409 C ASP A 733 6459 11084 7530 -1583 1016 954 C ATOM 5410 O ASP A 733 24.753 -1.620 168.259 1.00 63.11 O ANISOU 5410 O ASP A 733 6284 10469 7225 -1593 989 989 O ATOM 5411 CB ASP A 733 24.259 0.998 168.912 1.00 67.54 C ANISOU 5411 CB ASP A 733 6644 11365 7651 -1140 1095 807 C ATOM 5412 CG ASP A 733 23.862 2.436 169.161 1.00 69.71 C ANISOU 5412 CG ASP A 733 6808 11825 7853 -885 1147 698 C ATOM 5413 OD1 ASP A 733 22.649 2.729 169.112 1.00 72.76 O ANISOU 5413 OD1 ASP A 733 6990 12498 8156 -870 1186 676 O ATOM 5414 OD2 ASP A 733 24.760 3.270 169.404 1.00 70.14 O ANISOU 5414 OD2 ASP A 733 6980 11739 7931 -700 1147 633 O ATOM 5415 N THR A 734 22.737 -2.054 167.399 1.00 63.78 N ANISOU 5415 N THR A 734 6088 10901 7244 -1788 993 1001 N ATOM 5416 CA THR A 734 23.047 -3.461 167.214 1.00 61.17 C ANISOU 5416 CA THR A 734 5893 10371 6977 -2039 935 1100 C ATOM 5417 C THR A 734 22.579 -3.925 165.844 1.00 61.87 C ANISOU 5417 C THR A 734 5961 10410 7135 -2139 869 1068 C ATOM 5418 O THR A 734 21.572 -3.446 165.314 1.00 67.65 O ANISOU 5418 O THR A 734 6506 11375 7821 -2109 882 1017 O ATOM 5419 CB THR A 734 22.403 -4.308 168.305 1.00 61.45 C ANISOU 5419 CB THR A 734 5861 10580 6906 -2278 976 1234 C ATOM 5420 OG1 THR A 734 22.920 -3.893 169.578 1.00 58.63 O ANISOU 5420 OG1 THR A 734 5539 10257 6481 -2183 1033 1262 O ATOM 5421 CG2 THR A 734 22.724 -5.769 168.113 1.00 63.01 C ANISOU 5421 CG2 THR A 734 6221 10548 7172 -2539 907 1339 C ATOM 5422 N TYR A 735 23.332 -4.872 165.281 1.00 54.56 N ANISOU 5422 N TYR A 735 5231 9181 6316 -2252 796 1096 N ATOM 5423 CA TYR A 735 23.070 -5.496 163.990 1.00 54.73 C ANISOU 5423 CA TYR A 735 5281 9102 6412 -2369 723 1068 C ATOM 5424 C TYR A 735 21.892 -6.452 164.013 1.00 56.99 C ANISOU 5424 C TYR A 735 5453 9565 6636 -2661 714 1153 C ATOM 5425 O TYR A 735 21.622 -7.082 162.988 1.00 57.39 O ANISOU 5425 O TYR A 735 5532 9535 6740 -2792 649 1135 O ATOM 5426 CB TYR A 735 24.315 -6.249 163.535 1.00 53.61 C ANISOU 5426 CB TYR A 735 5397 8575 6396 -2391 653 1071 C ATOM 5427 CG TYR A 735 25.433 -5.355 163.067 1.00 51.40 C ANISOU 5427 CG TYR A 735 5222 8115 6194 -2123 643 969 C ATOM 5428 CD1 TYR A 735 25.173 -4.150 162.453 1.00 50.56 C ANISOU 5428 CD1 TYR A 735 5003 8132 6077 -1922 661 864 C ATOM 5429 CD2 TYR A 735 26.754 -5.733 163.214 1.00 50.29 C ANISOU 5429 CD2 TYR A 735 5292 7680 6137 -2076 612 981 C ATOM 5430 CE1 TYR A 735 26.204 -3.334 162.012 1.00 48.67 C ANISOU 5430 CE1 TYR A 735 4866 7723 5904 -1696 649 778 C ATOM 5431 CE2 TYR A 735 27.783 -4.930 162.762 1.00 48.40 C ANISOU 5431 CE2 TYR A 735 5139 7289 5964 -1849 603 890 C ATOM 5432 CZ TYR A 735 27.508 -3.731 162.167 1.00 47.60 C ANISOU 5432 CZ TYR A 735 4929 7309 5847 -1668 622 791 C ATOM 5433 OH TYR A 735 28.552 -2.943 161.729 1.00 45.84 O ANISOU 5433 OH TYR A 735 4801 6931 5685 -1461 612 710 O ATOM 5434 N HIS A 736 21.200 -6.596 165.142 1.00 62.65 N ANISOU 5434 N HIS A 736 6045 10523 7236 -2778 777 1244 N ATOM 5435 CA HIS A 736 20.078 -7.523 165.191 1.00 66.14 C ANISOU 5435 CA HIS A 736 6374 11146 7611 -3080 769 1334 C ATOM 5436 C HIS A 736 18.922 -7.060 164.316 1.00 66.27 C ANISOU 5436 C HIS A 736 6163 11431 7587 -3074 767 1262 C ATOM 5437 O HIS A 736 18.216 -7.891 163.736 1.00 65.05 O ANISOU 5437 O HIS A 736 5967 11320 7430 -3315 720 1298 O ATOM 5438 CB HIS A 736 19.610 -7.701 166.635 1.00 71.69 C ANISOU 5438 CB HIS A 736 6981 12074 8185 -3198 846 1448 C ATOM 5439 CG HIS A 736 20.511 -8.564 167.460 1.00 75.03 C ANISOU 5439 CG HIS A 736 7626 12246 8635 -3310 828 1559 C ATOM 5440 ND1 HIS A 736 20.961 -9.792 167.029 1.00 76.41 N ANISOU 5440 ND1 HIS A 736 8009 12123 8901 -3508 742 1620 N ATOM 5441 CD2 HIS A 736 21.036 -8.385 168.695 1.00 75.99 C ANISOU 5441 CD2 HIS A 736 7798 12373 8701 -3249 880 1619 C ATOM 5442 CE1 HIS A 736 21.733 -10.328 167.958 1.00 76.74 C ANISOU 5442 CE1 HIS A 736 8219 11993 8947 -3554 740 1718 C ATOM 5443 NE2 HIS A 736 21.801 -9.490 168.976 1.00 76.36 N ANISOU 5443 NE2 HIS A 736 8078 12128 8809 -3403 822 1721 N ATOM 5444 N HIS A 737 18.727 -5.748 164.194 1.00 66.69 N ANISOU 5444 N HIS A 737 6075 11657 7608 -2803 812 1162 N ATOM 5445 CA HIS A 737 17.509 -5.235 163.584 1.00 68.73 C ANISOU 5445 CA HIS A 737 6082 12230 7801 -2782 820 1108 C ATOM 5446 C HIS A 737 17.465 -5.459 162.080 1.00 64.97 C ANISOU 5446 C HIS A 737 5649 11622 7413 -2810 730 1040 C ATOM 5447 O HIS A 737 16.380 -5.422 161.498 1.00 66.06 O ANISOU 5447 O HIS A 737 5592 12008 7500 -2884 716 1021 O ATOM 5448 CB HIS A 737 17.348 -3.750 163.906 1.00 69.84 C ANISOU 5448 CB HIS A 737 6080 12573 7884 -2464 888 1019 C ATOM 5449 CG HIS A 737 18.299 -2.864 163.169 1.00 67.79 C ANISOU 5449 CG HIS A 737 5958 12076 7725 -2184 854 907 C ATOM 5450 ND1 HIS A 737 19.645 -3.137 163.069 1.00 65.30 N ANISOU 5450 ND1 HIS A 737 5904 11390 7518 -2147 817 905 N ATOM 5451 CD2 HIS A 737 18.099 -1.703 162.502 1.00 68.57 C ANISOU 5451 CD2 HIS A 737 5967 12258 7826 -1931 851 799 C ATOM 5452 CE1 HIS A 737 20.233 -2.184 162.367 1.00 65.70 C ANISOU 5452 CE1 HIS A 737 6015 11316 7632 -1896 795 800 C ATOM 5453 NE2 HIS A 737 19.317 -1.303 162.010 1.00 65.90 N ANISOU 5453 NE2 HIS A 737 5840 11602 7596 -1763 813 737 N ATOM 5454 N HIS A 738 18.608 -5.688 161.435 1.00 60.71 N ANISOU 5454 N HIS A 738 5351 10716 6999 -2750 670 1000 N ATOM 5455 CA HIS A 738 18.580 -6.045 160.021 1.00 60.96 C ANISOU 5455 CA HIS A 738 5438 10617 7106 -2806 583 940 C ATOM 5456 C HIS A 738 17.917 -7.403 159.814 1.00 62.81 C ANISOU 5456 C HIS A 738 5672 10865 7327 -3160 534 1019 C ATOM 5457 O HIS A 738 17.183 -7.604 158.841 1.00 63.24 O ANISOU 5457 O HIS A 738 5633 11020 7375 -3261 482 983 O ATOM 5458 CB HIS A 738 19.994 -6.040 159.444 1.00 61.14 C ANISOU 5458 CB HIS A 738 5722 10253 7258 -2669 537 881 C ATOM 5459 CG HIS A 738 20.649 -4.696 159.455 1.00 59.74 C ANISOU 5459 CG HIS A 738 5552 10047 7098 -2339 572 797 C ATOM 5460 ND1 HIS A 738 21.917 -4.492 159.948 1.00 57.52 N ANISOU 5460 ND1 HIS A 738 5456 9523 6876 -2204 587 793 N ATOM 5461 CD2 HIS A 738 20.215 -3.488 159.026 1.00 59.49 C ANISOU 5461 CD2 HIS A 738 5375 10195 7032 -2122 590 715 C ATOM 5462 CE1 HIS A 738 22.237 -3.217 159.826 1.00 56.96 C ANISOU 5462 CE1 HIS A 738 5355 9482 6806 -1931 613 712 C ATOM 5463 NE2 HIS A 738 21.221 -2.586 159.267 1.00 56.54 N ANISOU 5463 NE2 HIS A 738 5110 9674 6698 -1873 614 664 N ATOM 5464 N ALA A 739 18.147 -8.340 160.729 1.00 62.28 N ANISOU 5464 N ALA A 739 5712 10701 7250 -3360 544 1131 N ATOM 5465 CA ALA A 739 17.578 -9.674 160.583 1.00 64.29 C ANISOU 5465 CA ALA A 739 5998 10934 7494 -3713 491 1216 C ATOM 5466 C ALA A 739 16.073 -9.658 160.788 1.00 68.77 C ANISOU 5466 C ALA A 739 6275 11920 7932 -3883 524 1260 C ATOM 5467 O ALA A 739 15.320 -10.176 159.959 1.00 71.94 O ANISOU 5467 O ALA A 739 6607 12403 8326 -4073 465 1250 O ATOM 5468 CB ALA A 739 18.231 -10.632 161.574 1.00 64.70 C ANISOU 5468 CB ALA A 739 6248 10772 7564 -3870 493 1334 C ATOM 5469 N VAL A 740 15.612 -9.077 161.898 1.00 80.58 N ANISOU 5469 N VAL A 740 7596 13700 9320 -3821 618 1307 N ATOM 5470 CA VAL A 740 14.188 -9.147 162.203 1.00 84.23 C ANISOU 5470 CA VAL A 740 7774 14582 9649 -4000 656 1360 C ATOM 5471 C VAL A 740 13.390 -8.279 161.245 1.00 84.97 C ANISOU 5471 C VAL A 740 7642 14927 9716 -3850 645 1251 C ATOM 5472 O VAL A 740 12.212 -8.556 160.987 1.00 88.61 O ANISOU 5472 O VAL A 740 7931 15639 10099 -3993 624 1262 O ATOM 5473 CB VAL A 740 13.915 -8.775 163.675 1.00 86.03 C ANISOU 5473 CB VAL A 740 7881 15048 9758 -3958 762 1432 C ATOM 5474 CG1 VAL A 740 14.865 -9.530 164.594 1.00 86.84 C ANISOU 5474 CG1 VAL A 740 8223 14879 9893 -4071 768 1538 C ATOM 5475 CG2 VAL A 740 14.005 -7.268 163.892 1.00 86.79 C ANISOU 5475 CG2 VAL A 740 7839 15316 9822 -3590 835 1332 C ATOM 5476 N ASP A 741 14.000 -7.224 160.697 1.00 87.84 N ANISOU 5476 N ASP A 741 8048 15184 10142 -3517 642 1134 N ATOM 5477 CA ASP A 741 13.326 -6.471 159.649 1.00 67.67 C ANISOU 5477 CA ASP A 741 5317 12819 7575 -3377 612 1035 C ATOM 5478 C ASP A 741 13.000 -7.377 158.476 1.00 68.49 C ANISOU 5478 C ASP A 741 5464 12835 7724 -3615 510 1027 C ATOM 5479 O ASP A 741 11.892 -7.328 157.938 1.00 70.10 O ANISOU 5479 O ASP A 741 5445 13330 7860 -3702 487 1013 O ATOM 5480 CB ASP A 741 14.181 -5.284 159.209 1.00 65.21 C ANISOU 5480 CB ASP A 741 5096 12344 7335 -3003 613 921 C ATOM 5481 CG ASP A 741 13.878 -4.029 160.004 1.00 65.13 C ANISOU 5481 CG ASP A 741 4912 12592 7241 -2733 703 889 C ATOM 5482 OD1 ASP A 741 12.729 -3.895 160.476 1.00 67.13 O ANISOU 5482 OD1 ASP A 741 4904 13226 7375 -2795 752 920 O ATOM 5483 OD2 ASP A 741 14.772 -3.165 160.138 1.00 63.19 O ANISOU 5483 OD2 ASP A 741 4787 12175 7046 -2459 724 827 O ATOM 5484 N ALA A 742 13.942 -8.246 158.103 1.00 67.58 N ANISOU 5484 N ALA A 742 5633 12328 7716 -3727 447 1037 N ATOM 5485 CA ALA A 742 13.720 -9.187 157.013 1.00 68.42 C ANISOU 5485 CA ALA A 742 5816 12314 7867 -3961 347 1022 C ATOM 5486 C ALA A 742 12.598 -10.163 157.326 1.00 71.28 C ANISOU 5486 C ALA A 742 6040 12902 8140 -4334 335 1123 C ATOM 5487 O ALA A 742 11.879 -10.592 156.418 1.00 72.59 O ANISOU 5487 O ALA A 742 6156 13135 8291 -4473 261 1091 O ATOM 5488 CB ALA A 742 15.006 -9.953 156.708 1.00 67.03 C ANISOU 5488 CB ALA A 742 5983 11667 7820 -3994 290 1014 C ATOM 5489 N LEU A 743 12.435 -10.536 158.594 1.00 72.37 N ANISOU 5489 N LEU A 743 6186 13096 8214 -4423 393 1225 N ATOM 5490 CA LEU A 743 11.342 -11.431 158.940 1.00 75.25 C ANISOU 5490 CA LEU A 743 6505 13599 8487 -4659 367 1296 C ATOM 5491 C LEU A 743 10.013 -10.699 158.963 1.00 76.82 C ANISOU 5491 C LEU A 743 6396 14235 8558 -4567 401 1265 C ATOM 5492 O LEU A 743 8.972 -11.298 158.672 1.00 79.17 O ANISOU 5492 O LEU A 743 6615 14680 8787 -4750 354 1283 O ATOM 5493 CB LEU A 743 11.623 -12.103 160.277 1.00 76.03 C ANISOU 5493 CB LEU A 743 6732 13599 8555 -4778 409 1415 C ATOM 5494 CG LEU A 743 12.641 -13.224 160.110 1.00 75.49 C ANISOU 5494 CG LEU A 743 6990 13089 8602 -4945 340 1458 C ATOM 5495 CD1 LEU A 743 12.804 -13.988 161.397 1.00 76.66 C ANISOU 5495 CD1 LEU A 743 7266 13149 8711 -5079 366 1586 C ATOM 5496 CD2 LEU A 743 12.196 -14.151 159.001 1.00 76.85 C ANISOU 5496 CD2 LEU A 743 7246 13149 8806 -5154 231 1426 C ATOM 5497 N ILE A 744 10.023 -9.411 159.302 1.00 75.70 N ANISOU 5497 N ILE A 744 6081 14300 8380 -4279 480 1216 N ATOM 5498 CA ILE A 744 8.829 -8.603 159.102 1.00 77.02 C ANISOU 5498 CA ILE A 744 5965 14857 8443 -4143 499 1163 C ATOM 5499 C ILE A 744 8.506 -8.516 157.618 1.00 76.96 C ANISOU 5499 C ILE A 744 5907 14860 8474 -4142 411 1079 C ATOM 5500 O ILE A 744 7.332 -8.479 157.228 1.00 78.96 O ANISOU 5500 O ILE A 744 5979 15382 8639 -4180 382 1062 O ATOM 5501 CB ILE A 744 9.027 -7.217 159.745 1.00 75.75 C ANISOU 5501 CB ILE A 744 5666 14868 8246 -3805 596 1116 C ATOM 5502 CG1 ILE A 744 9.044 -7.354 161.267 1.00 76.51 C ANISOU 5502 CG1 ILE A 744 5775 15027 8266 -3830 680 1200 C ATOM 5503 CG2 ILE A 744 7.951 -6.244 159.306 1.00 76.77 C ANISOU 5503 CG2 ILE A 744 5529 15350 8292 -3605 600 1038 C ATOM 5504 CD1 ILE A 744 9.106 -6.039 162.000 1.00 75.70 C ANISOU 5504 CD1 ILE A 744 5538 15115 8110 -3508 776 1149 C ATOM 5505 N ILE A 745 9.535 -8.529 156.767 1.00 74.81 N ANISOU 5505 N ILE A 745 5798 14298 8328 -4112 363 1028 N ATOM 5506 CA ILE A 745 9.326 -8.501 155.322 1.00 74.77 C ANISOU 5506 CA ILE A 745 5770 14279 8361 -4123 271 947 C ATOM 5507 C ILE A 745 8.701 -9.806 154.847 1.00 78.11 C ANISOU 5507 C ILE A 745 6273 14640 8766 -4447 186 982 C ATOM 5508 O ILE A 745 7.705 -9.806 154.114 1.00 82.00 O ANISOU 5508 O ILE A 745 6619 15340 9195 -4492 134 948 O ATOM 5509 CB ILE A 745 10.652 -8.226 154.595 1.00 72.03 C ANISOU 5509 CB ILE A 745 5603 13617 8148 -4008 242 881 C ATOM 5510 CG1 ILE A 745 11.220 -6.873 154.998 1.00 69.92 C ANISOU 5510 CG1 ILE A 745 5323 13351 7894 -3608 313 826 C ATOM 5511 CG2 ILE A 745 10.447 -8.255 153.103 1.00 71.95 C ANISOU 5511 CG2 ILE A 745 5596 13572 8170 -4018 141 793 C ATOM 5512 CD1 ILE A 745 12.606 -6.665 154.498 1.00 67.31 C ANISOU 5512 CD1 ILE A 745 5281 12603 7689 -3419 284 759 C ATOM 5513 N ALA A 746 9.242 -10.931 155.257 1.00 83.39 N ANISOU 5513 N ALA A 746 7183 15014 9487 -4671 165 1050 N ATOM 5514 CA ALA A 746 8.655 -12.179 154.832 1.00 85.57 C ANISOU 5514 CA ALA A 746 7568 15195 9751 -4977 80 1082 C ATOM 5515 C ALA A 746 7.234 -12.280 155.338 1.00 89.94 C ANISOU 5515 C ALA A 746 7924 16089 10161 -5101 97 1141 C ATOM 5516 O ALA A 746 6.343 -12.699 154.645 1.00 90.91 O ANISOU 5516 O ALA A 746 8039 16259 10245 -5308 23 1141 O ATOM 5517 CB ALA A 746 9.464 -13.343 155.336 1.00 87.17 C ANISOU 5517 CB ALA A 746 8078 15007 10035 -5160 59 1149 C ATOM 5518 N ALA A 747 7.030 -11.891 156.570 1.00 84.80 N ANISOU 5518 N ALA A 747 7114 15682 9424 -4980 191 1187 N ATOM 5519 CA ALA A 747 5.712 -11.938 157.162 1.00 87.37 C ANISOU 5519 CA ALA A 747 7235 16359 9602 -5077 215 1239 C ATOM 5520 C ALA A 747 4.710 -11.017 156.489 1.00 87.34 C ANISOU 5520 C ALA A 747 6939 16730 9516 -4875 226 1164 C ATOM 5521 O ALA A 747 3.535 -11.309 156.468 1.00 89.87 O ANISOU 5521 O ALA A 747 7080 17356 9712 -4967 228 1193 O ATOM 5522 CB ALA A 747 5.769 -11.666 158.652 1.00 87.08 C ANISOU 5522 CB ALA A 747 7183 16403 9500 -5064 308 1328 C ATOM 5523 N SER A 748 5.155 -9.893 155.965 1.00 83.83 N ANISOU 5523 N SER A 748 6445 16275 9133 -4600 231 1072 N ATOM 5524 CA SER A 748 4.237 -8.962 155.338 1.00 84.53 C ANISOU 5524 CA SER A 748 6276 16694 9149 -4402 226 1000 C ATOM 5525 C SER A 748 3.547 -9.651 154.185 1.00 86.20 C ANISOU 5525 C SER A 748 6456 16958 9339 -4586 124 974 C ATOM 5526 O SER A 748 2.376 -9.465 153.945 1.00 88.50 O ANISOU 5526 O SER A 748 6532 17578 9515 -4595 115 972 O ATOM 5527 CB SER A 748 5.016 -7.787 154.797 1.00 81.79 C ANISOU 5527 CB SER A 748 5908 16291 8877 -4067 246 912 C ATOM 5528 OG SER A 748 6.071 -8.264 153.998 1.00 79.67 O ANISOU 5528 OG SER A 748 5874 15651 8744 -4131 195 887 O ATOM 5529 N SER A 749 4.296 -10.441 153.460 1.00 85.15 N ANISOU 5529 N SER A 749 6535 16505 9312 -4726 44 948 N ATOM 5530 CA SER A 749 3.759 -11.128 152.328 1.00 86.97 C ANISOU 5530 CA SER A 749 6777 16747 9519 -4950 -56 931 C ATOM 5531 C SER A 749 2.682 -12.141 152.649 1.00 90.00 C ANISOU 5531 C SER A 749 7152 17234 9810 -5248 -61 1023 C ATOM 5532 O SER A 749 1.742 -12.288 151.894 1.00 92.29 O ANISOU 5532 O SER A 749 7357 17678 10029 -5412 -125 1018 O ATOM 5533 CB SER A 749 4.877 -11.723 151.487 1.00 85.36 C ANISOU 5533 CB SER A 749 6842 16144 9448 -5056 -136 885 C ATOM 5534 OG SER A 749 4.995 -13.112 151.654 1.00 85.51 O ANISOU 5534 OG SER A 749 7106 15865 9518 -5278 -136 957 O ATOM 5535 N GLN A 750 2.774 -12.851 153.764 1.00 90.16 N ANISOU 5535 N GLN A 750 7258 17179 9821 -5324 4 1110 N ATOM 5536 CA GLN A 750 1.736 -13.848 154.056 1.00 93.06 C ANISOU 5536 CA GLN A 750 7641 17617 10101 -5620 -2 1208 C ATOM 5537 C GLN A 750 0.601 -13.362 154.944 1.00 95.75 C ANISOU 5537 C GLN A 750 7685 18418 10277 -5612 34 1233 C ATOM 5538 O GLN A 750 -0.074 -14.141 155.596 1.00 98.57 O ANISOU 5538 O GLN A 750 8025 18879 10547 -5879 11 1304 O ATOM 5539 CB GLN A 750 2.333 -15.145 154.603 1.00 92.53 C ANISOU 5539 CB GLN A 750 7740 17358 10059 -5682 60 1301 C ATOM 5540 N LEU A 751 0.414 -12.059 154.967 1.00 95.07 N ANISOU 5540 N LEU A 751 7372 18605 10147 -5309 87 1175 N ATOM 5541 CA LEU A 751 -0.635 -11.418 155.736 1.00 97.23 C ANISOU 5541 CA LEU A 751 7392 19281 10269 -5244 155 1209 C ATOM 5542 C LEU A 751 -2.061 -11.688 155.280 1.00100.25 C ANISOU 5542 C LEU A 751 7567 19991 10531 -5357 106 1201 C ATOM 5543 O LEU A 751 -2.971 -11.734 156.085 1.00102.69 O ANISOU 5543 O LEU A 751 7685 20633 10702 -5387 152 1246 O ATOM 5544 CB LEU A 751 -0.382 -9.930 155.849 1.00 95.40 C ANISOU 5544 CB LEU A 751 7018 19192 10037 -4851 235 1147 C ATOM 5545 CG LEU A 751 -0.286 -9.399 157.267 1.00 96.31 C ANISOU 5545 CG LEU A 751 7034 19506 10055 -4781 338 1202 C ATOM 5546 CD1 LEU A 751 0.468 -10.366 158.143 1.00 96.61 C ANISOU 5546 CD1 LEU A 751 7277 19317 10113 -5045 351 1305 C ATOM 5547 CD2 LEU A 751 0.358 -8.030 157.274 1.00 93.85 C ANISOU 5547 CD2 LEU A 751 6686 19187 9787 -4411 410 1138 C ATOM 5548 N ASN A 752 -2.275 -11.797 153.977 1.00100.26 N ANISOU 5548 N ASN A 752 7600 19918 10576 -5425 12 1146 N ATOM 5549 CA ASN A 752 -3.611 -12.077 153.478 1.00103.29 C ANISOU 5549 CA ASN A 752 7794 20608 10841 -5556 -41 1143 C ATOM 5550 C ASN A 752 -4.003 -13.441 153.978 1.00106.34 C ANISOU 5550 C ASN A 752 8219 21042 11141 -5926 -56 1244 C ATOM 5551 O ASN A 752 -5.112 -13.654 154.405 1.00109.36 O ANISOU 5551 O ASN A 752 8391 21776 11383 -6022 -60 1270 O ATOM 5552 CB ASN A 752 -3.644 -12.063 151.962 1.00102.62 C ANISOU 5552 CB ASN A 752 7767 20400 10826 -5571 -143 1064 C ATOM 5553 N LEU A 753 -3.070 -14.373 153.929 1.00108.67 N ANISOU 5553 N LEU A 753 8781 20995 11515 -6134 -67 1304 N ATOM 5554 CA LEU A 753 -3.340 -15.697 154.411 1.00113.82 C ANISOU 5554 CA LEU A 753 9497 21661 12089 -6486 -85 1408 C ATOM 5555 C LEU A 753 -3.610 -15.606 155.891 1.00113.47 C ANISOU 5555 C LEU A 753 9251 21960 11901 -6459 7 1479 C ATOM 5556 O LEU A 753 -4.523 -16.218 156.413 1.00111.79 O ANISOU 5556 O LEU A 753 8997 21781 11699 -6221 93 1475 O ATOM 5557 CB LEU A 753 -2.127 -16.569 154.188 1.00112.38 C ANISOU 5557 CB LEU A 753 9659 21013 12027 -6670 -114 1458 C ATOM 5558 CG LEU A 753 -1.911 -17.190 152.815 1.00110.93 C ANISOU 5558 CG LEU A 753 9607 20652 11889 -6597 -35 1520 C ATOM 5559 CD1 LEU A 753 -1.702 -18.684 152.970 1.00109.15 C ANISOU 5559 CD1 LEU A 753 9720 19935 11818 -6688 -85 1522 C ATOM 5560 CD2 LEU A 753 -3.037 -16.895 151.849 1.00113.72 C ANISOU 5560 CD2 LEU A 753 9919 21169 12120 -6800 8 1640 C ATOM 5561 N PRO A 791 -1.187 -19.578 163.733 1.00117.40 N ANISOU 5561 N PRO A 791 10882 21316 12407 -7369 207 2173 N ATOM 5562 CA PRO A 791 0.155 -19.549 163.140 1.00113.39 C ANISOU 5562 CA PRO A 791 10623 20373 12088 -7238 175 2116 C ATOM 5563 C PRO A 791 0.685 -18.127 162.983 1.00110.19 C ANISOU 5563 C PRO A 791 10093 20035 11738 -6857 245 2010 C ATOM 5564 O PRO A 791 1.892 -17.906 163.049 1.00107.24 O ANISOU 5564 O PRO A 791 9898 19358 11491 -6707 259 1989 O ATOM 5565 CB PRO A 791 -0.045 -20.218 161.776 1.00113.61 C ANISOU 5565 CB PRO A 791 10746 20244 12178 -7401 66 2065 C ATOM 5566 CG PRO A 791 -1.500 -20.080 161.490 1.00116.70 C ANISOU 5566 CG PRO A 791 10856 21066 12418 -7499 60 2056 C ATOM 5567 CD PRO A 791 -2.181 -20.163 162.820 1.00119.90 C ANISOU 5567 CD PRO A 791 11127 21762 12669 -7592 127 2161 C ATOM 5568 N TYR A 792 -0.224 -17.175 162.773 1.00111.28 N ANISOU 5568 N TYR A 792 9930 20572 11781 -6700 286 1944 N ATOM 5569 CA TYR A 792 0.164 -15.769 162.744 1.00108.70 C ANISOU 5569 CA TYR A 792 9467 20348 11487 -6328 357 1848 C ATOM 5570 C TYR A 792 0.619 -15.301 164.121 1.00108.16 C ANISOU 5570 C TYR A 792 9392 20322 11381 -6189 455 1895 C ATOM 5571 O TYR A 792 1.643 -14.621 164.247 1.00105.66 O ANISOU 5571 O TYR A 792 9158 19828 11161 -5953 496 1850 O ATOM 5572 CB TYR A 792 -1.006 -14.928 162.228 1.00109.56 C ANISOU 5572 CB TYR A 792 9259 20879 11491 -6199 370 1772 C ATOM 5573 CG TYR A 792 -1.007 -13.473 162.649 1.00108.71 C ANISOU 5573 CG TYR A 792 8949 21008 11348 -5832 463 1699 C ATOM 5574 CD1 TYR A 792 -1.645 -13.070 163.816 1.00110.78 C ANISOU 5574 CD1 TYR A 792 9030 21593 11466 -5773 546 1737 C ATOM 5575 CD2 TYR A 792 -0.401 -12.500 161.867 1.00106.58 C ANISOU 5575 CD2 TYR A 792 8669 20645 11182 -5543 463 1588 C ATOM 5576 CE1 TYR A 792 -1.659 -11.746 164.204 1.00110.32 C ANISOU 5576 CE1 TYR A 792 8801 21742 11374 -5428 628 1662 C ATOM 5577 CE2 TYR A 792 -0.414 -11.169 162.248 1.00106.17 C ANISOU 5577 CE2 TYR A 792 8445 20798 11097 -5201 543 1519 C ATOM 5578 CZ TYR A 792 -1.045 -10.800 163.417 1.00108.17 C ANISOU 5578 CZ TYR A 792 8532 21357 11210 -5141 625 1553 C ATOM 5579 OH TYR A 792 -1.065 -9.481 163.807 1.00107.70 O ANISOU 5579 OH TYR A 792 8315 21489 11116 -4793 701 1476 O ATOM 5580 N GLN A 793 -0.146 -15.585 165.148 1.00114.50 N ANISOU 5580 N GLN A 793 10098 21368 12040 -6336 493 1986 N ATOM 5581 CA GLN A 793 0.260 -15.161 166.469 1.00114.34 C ANISOU 5581 CA GLN A 793 10097 21370 11977 -6241 580 2041 C ATOM 5582 C GLN A 793 1.515 -15.935 166.869 1.00112.99 C ANISOU 5582 C GLN A 793 10253 20761 11916 -6372 550 2123 C ATOM 5583 O GLN A 793 2.331 -15.449 167.629 1.00112.75 O ANISOU 5583 O GLN A 793 10304 20613 11924 -6209 611 2133 O ATOM 5584 CB GLN A 793 -0.863 -15.335 167.486 1.00118.90 C ANISOU 5584 CB GLN A 793 10482 22332 12361 -6380 623 2117 C ATOM 5585 N HIS A 794 1.655 -17.160 166.380 1.00110.25 N ANISOU 5585 N HIS A 794 10101 20169 11619 -6661 456 2181 N ATOM 5586 CA HIS A 794 2.805 -17.959 166.744 1.00108.05 C ANISOU 5586 CA HIS A 794 10154 19442 11459 -6769 414 2249 C ATOM 5587 C HIS A 794 4.078 -17.313 166.309 1.00100.21 C ANISOU 5587 C HIS A 794 9285 18172 10620 -6496 434 2170 C ATOM 5588 O HIS A 794 5.036 -17.201 167.071 1.00 98.80 O ANISOU 5588 O HIS A 794 9255 17798 10485 -6422 470 2217 O ATOM 5589 CB HIS A 794 2.739 -19.271 166.002 1.00107.17 C ANISOU 5589 CB HIS A 794 10224 19098 11398 -7066 299 2280 C ATOM 5590 CG HIS A 794 3.916 -20.156 166.241 1.00104.49 C ANISOU 5590 CG HIS A 794 10235 18268 11199 -7150 239 2325 C ATOM 5591 ND1 HIS A 794 4.317 -21.120 165.344 1.00103.28 N ANISOU 5591 ND1 HIS A 794 10233 17925 11082 -7081 276 2388 N ATOM 5592 CD2 HIS A 794 4.767 -20.238 167.284 1.00104.36 C ANISOU 5592 CD2 HIS A 794 10444 17914 11293 -7282 142 2308 C ATOM 5593 CE1 HIS A 794 5.363 -21.761 165.825 1.00102.50 C ANISOU 5593 CE1 HIS A 794 10437 17396 11112 -7165 203 2411 C ATOM 5594 NE2 HIS A 794 5.656 -21.243 167.000 1.00103.14 N ANISOU 5594 NE2 HIS A 794 10571 17378 11240 -7284 122 2361 N ATOM 5595 N PHE A 795 4.080 -16.851 165.075 1.00 99.29 N ANISOU 5595 N PHE A 795 9092 18059 10575 -6336 414 2050 N ATOM 5596 CA PHE A 795 5.270 -16.269 164.548 1.00 95.79 C ANISOU 5596 CA PHE A 795 8787 17324 10284 -6114 416 1975 C ATOM 5597 C PHE A 795 5.603 -15.077 165.396 1.00 93.86 C ANISOU 5597 C PHE A 795 8408 17240 10013 -5807 523 1937 C ATOM 5598 O PHE A 795 6.731 -14.928 165.822 1.00 90.77 O ANISOU 5598 O PHE A 795 8176 16596 9716 -5672 548 1936 O ATOM 5599 CB PHE A 795 5.041 -15.893 163.096 1.00 94.07 C ANISOU 5599 CB PHE A 795 8537 17061 10143 -6063 351 1863 C ATOM 5600 CG PHE A 795 5.987 -14.870 162.578 1.00 90.70 C ANISOU 5600 CG PHE A 795 8096 16547 9818 -5751 384 1757 C ATOM 5601 CD1 PHE A 795 7.282 -15.200 162.292 1.00 88.25 C ANISOU 5601 CD1 PHE A 795 8042 15832 9657 -5705 355 1743 C ATOM 5602 CD2 PHE A 795 5.578 -13.572 162.380 1.00 90.13 C ANISOU 5602 CD2 PHE A 795 7758 16796 9691 -5502 438 1669 C ATOM 5603 CE1 PHE A 795 8.158 -14.252 161.813 1.00 85.32 C ANISOU 5603 CE1 PHE A 795 7656 15389 9373 -5434 383 1649 C ATOM 5604 CE2 PHE A 795 6.448 -12.617 161.900 1.00 87.17 C ANISOU 5604 CE2 PHE A 795 7377 16335 9408 -5220 463 1574 C ATOM 5605 CZ PHE A 795 7.738 -12.960 161.616 1.00 84.79 C ANISOU 5605 CZ PHE A 795 7326 15639 9249 -5197 436 1566 C ATOM 5606 N VAL A 796 4.614 -14.258 165.701 1.00 94.33 N ANISOU 5606 N VAL A 796 8179 17718 9944 -5687 585 1901 N ATOM 5607 CA VAL A 796 4.882 -13.083 166.498 1.00 92.77 C ANISOU 5607 CA VAL A 796 7849 17684 9713 -5378 685 1851 C ATOM 5608 C VAL A 796 5.381 -13.350 167.900 1.00 95.10 C ANISOU 5608 C VAL A 796 8234 17944 9956 -5416 745 1950 C ATOM 5609 O VAL A 796 6.225 -12.631 168.403 1.00 90.89 O ANISOU 5609 O VAL A 796 7775 17287 9472 -5217 800 1933 O ATOM 5610 CB VAL A 796 3.696 -12.144 166.538 1.00 94.21 C ANISOU 5610 CB VAL A 796 7708 18319 9770 -5228 728 1780 C ATOM 5611 CG1 VAL A 796 4.049 -10.897 167.318 1.00 93.62 C ANISOU 5611 CG1 VAL A 796 7503 18447 9620 -4964 834 1753 C ATOM 5612 CG2 VAL A 796 3.340 -11.756 165.135 1.00 92.89 C ANISOU 5612 CG2 VAL A 796 7459 18159 9675 -5075 685 1663 C ATOM 5613 N ASP A 797 4.829 -14.353 168.548 1.00109.91 N ANISOU 5613 N ASP A 797 10106 19932 11724 -5674 734 2058 N ATOM 5614 CA ASP A 797 5.242 -14.656 169.895 1.00109.41 C ANISOU 5614 CA ASP A 797 10122 19850 11601 -5709 788 2154 C ATOM 5615 C ASP A 797 6.689 -15.106 169.858 1.00108.08 C ANISOU 5615 C ASP A 797 10278 19223 11566 -5780 747 2218 C ATOM 5616 O ASP A 797 7.544 -14.709 170.681 1.00107.65 O ANISOU 5616 O ASP A 797 10308 19089 11504 -5696 800 2264 O ATOM 5617 CB ASP A 797 4.310 -15.707 170.498 1.00116.26 C ANISOU 5617 CB ASP A 797 10895 20968 12311 -5970 785 2255 C ATOM 5618 CG ASP A 797 3.100 -15.082 171.193 1.00120.90 C ANISOU 5618 CG ASP A 797 11157 22042 12738 -5836 860 2204 C ATOM 5619 OD1 ASP A 797 2.917 -13.857 171.082 1.00120.04 O ANISOU 5619 OD1 ASP A 797 10901 22062 12646 -5537 907 2086 O ATOM 5620 OD2 ASP A 797 2.332 -15.810 171.854 1.00124.75 O ANISOU 5620 OD2 ASP A 797 11538 22781 13081 -6026 870 2281 O ATOM 5621 N THR A 798 6.977 -15.911 168.851 1.00 97.51 N ANISOU 5621 N THR A 798 9126 17576 10348 -5923 653 2217 N ATOM 5622 CA THR A 798 8.305 -16.432 168.708 1.00 94.22 C ANISOU 5622 CA THR A 798 9008 16714 10078 -5911 615 2243 C ATOM 5623 C THR A 798 9.221 -15.226 168.556 1.00 88.73 C ANISOU 5623 C THR A 798 8303 15935 9475 -5593 665 2142 C ATOM 5624 O THR A 798 10.255 -15.136 169.178 1.00 86.91 O ANISOU 5624 O THR A 798 8266 15432 9324 -5517 674 2173 O ATOM 5625 CB THR A 798 8.348 -17.349 167.475 1.00 92.55 C ANISOU 5625 CB THR A 798 8995 16197 9973 -6116 500 2246 C ATOM 5626 OG1 THR A 798 7.869 -18.644 167.832 1.00 92.84 O ANISOU 5626 OG1 THR A 798 8858 16414 10005 -6097 473 2147 O ATOM 5627 CG2 THR A 798 9.756 -17.503 166.927 1.00 95.60 C ANISOU 5627 CG2 THR A 798 9510 16512 10301 -6439 442 2375 C ATOM 5628 N LEU A 799 8.786 -14.276 167.757 1.00 95.03 N ANISOU 5628 N LEU A 799 8882 16965 10261 -5404 693 2025 N ATOM 5629 CA LEU A 799 9.539 -13.066 167.500 1.00 90.77 C ANISOU 5629 CA LEU A 799 8338 16336 9814 -5110 730 1924 C ATOM 5630 C LEU A 799 9.811 -12.174 168.709 1.00 90.87 C ANISOU 5630 C LEU A 799 8290 16472 9765 -4899 834 1930 C ATOM 5631 O LEU A 799 10.895 -11.628 168.833 1.00 88.15 O ANISOU 5631 O LEU A 799 8085 15903 9506 -4752 856 1917 O ATOM 5632 CB LEU A 799 8.826 -12.245 166.433 1.00 90.49 C ANISOU 5632 CB LEU A 799 8086 16519 9775 -4966 725 1800 C ATOM 5633 CG LEU A 799 9.605 -11.137 165.734 1.00 87.72 C ANISOU 5633 CG LEU A 799 7793 15974 9560 -4757 710 1696 C ATOM 5634 CD1 LEU A 799 10.106 -11.637 164.395 1.00 85.95 C ANISOU 5634 CD1 LEU A 799 7774 15425 9459 -4943 602 1695 C ATOM 5635 CD2 LEU A 799 8.730 -9.914 165.547 1.00 88.65 C ANISOU 5635 CD2 LEU A 799 7648 16399 9635 -4520 742 1579 C ATOM 5636 N LYS A 800 8.760 -11.996 169.506 1.00 91.83 N ANISOU 5636 N LYS A 800 8203 16954 9732 -4879 896 1945 N ATOM 5637 CA LYS A 800 8.745 -11.207 170.733 1.00 92.67 C ANISOU 5637 CA LYS A 800 8239 17210 9762 -4677 995 1940 C ATOM 5638 C LYS A 800 9.593 -11.817 171.840 1.00 93.58 C ANISOU 5638 C LYS A 800 8542 17159 9854 -4816 1005 2068 C ATOM 5639 O LYS A 800 10.226 -11.106 172.620 1.00 91.24 O ANISOU 5639 O LYS A 800 8198 16988 9479 -4678 1084 2075 O ATOM 5640 CB LYS A 800 7.308 -11.014 171.223 1.00 95.86 C ANISOU 5640 CB LYS A 800 8348 18070 10005 -4591 1055 1897 C ATOM 5641 N SER A 801 9.790 -13.111 171.744 1.00 95.38 N ANISOU 5641 N SER A 801 8988 17106 10146 -5077 923 2165 N ATOM 5642 CA SER A 801 10.532 -13.787 172.746 1.00 99.27 C ANISOU 5642 CA SER A 801 9671 17430 10618 -5213 921 2294 C ATOM 5643 C SER A 801 11.795 -13.017 173.018 1.00 98.76 C ANISOU 5643 C SER A 801 9750 17147 10628 -5006 960 2283 C ATOM 5644 O SER A 801 12.488 -12.593 172.122 1.00 97.79 O ANISOU 5644 O SER A 801 9655 16889 10613 -4820 961 2191 O ATOM 5645 CB SER A 801 10.886 -15.170 172.220 1.00 99.03 C ANISOU 5645 CB SER A 801 9869 17099 10660 -5506 813 2387 C ATOM 5646 OG SER A 801 12.033 -15.699 172.844 1.00 95.53 O ANISOU 5646 OG SER A 801 9660 16254 10384 -5453 758 2365 O ATOM 5647 N LYS A 802 12.061 -12.823 174.299 1.00104.07 N ANISOU 5647 N LYS A 802 10511 17796 11234 -5045 991 2380 N ATOM 5648 CA LYS A 802 13.249 -12.143 174.775 1.00104.23 C ANISOU 5648 CA LYS A 802 10690 17598 11315 -4881 1019 2390 C ATOM 5649 C LYS A 802 14.410 -12.988 174.353 1.00103.76 C ANISOU 5649 C LYS A 802 10938 17085 11402 -4997 927 2459 C ATOM 5650 O LYS A 802 15.469 -12.480 174.043 1.00104.00 O ANISOU 5650 O LYS A 802 11113 16896 11505 -4854 936 2457 O ATOM 5651 CB LYS A 802 13.241 -11.995 176.296 1.00106.97 C ANISOU 5651 CB LYS A 802 11009 18111 11525 -4868 1086 2465 C ATOM 5652 N GLU A 803 14.196 -14.291 174.371 1.00108.66 N ANISOU 5652 N GLU A 803 11665 17560 12063 -5244 837 2515 N ATOM 5653 CA GLU A 803 15.188 -15.271 174.005 1.00105.51 C ANISOU 5653 CA GLU A 803 11563 16720 11804 -5350 739 2567 C ATOM 5654 C GLU A 803 15.541 -15.323 172.514 1.00103.87 C ANISOU 5654 C GLU A 803 11393 16338 11736 -5298 685 2459 C ATOM 5655 O GLU A 803 16.475 -16.004 172.134 1.00101.19 O ANISOU 5655 O GLU A 803 11273 15671 11503 -5430 589 2485 O ATOM 5656 CB GLU A 803 14.703 -16.641 174.446 1.00109.53 C ANISOU 5656 CB GLU A 803 12198 17143 12276 -5649 665 2691 C ATOM 5657 N PHE A 804 14.763 -14.668 171.668 1.00 95.15 N ANISOU 5657 N PHE A 804 10084 15437 10630 -5101 742 2335 N ATOM 5658 CA PHE A 804 15.005 -14.707 170.235 1.00 92.68 C ANISOU 5658 CA PHE A 804 9766 15020 10429 -5059 694 2227 C ATOM 5659 C PHE A 804 16.301 -14.107 169.671 1.00 86.45 C ANISOU 5659 C PHE A 804 9075 14016 9755 -4834 708 2160 C ATOM 5660 O PHE A 804 16.977 -14.733 168.879 1.00 84.55 O ANISOU 5660 O PHE A 804 9057 13422 9646 -4873 631 2157 O ATOM 5661 CB PHE A 804 13.807 -14.059 169.545 1.00 91.80 C ANISOU 5661 CB PHE A 804 9353 15292 10234 -5009 733 2137 C ATOM 5662 CG PHE A 804 13.873 -14.093 168.059 1.00 89.34 C ANISOU 5662 CG PHE A 804 9028 14899 10019 -5007 671 2037 C ATOM 5663 CD1 PHE A 804 14.229 -15.240 167.402 1.00 89.94 C ANISOU 5663 CD1 PHE A 804 9323 14656 10195 -5195 566 2059 C ATOM 5664 CD2 PHE A 804 13.586 -12.979 167.326 1.00 87.35 C ANISOU 5664 CD2 PHE A 804 8554 14881 9755 -4809 713 1916 C ATOM 5665 CE1 PHE A 804 14.318 -15.276 166.030 1.00 89.69 C ANISOU 5665 CE1 PHE A 804 9286 14546 10247 -5196 506 1962 C ATOM 5666 CE2 PHE A 804 13.670 -13.002 165.958 1.00 87.28 C ANISOU 5666 CE2 PHE A 804 8534 14798 9830 -4810 651 1827 C ATOM 5667 CZ PHE A 804 14.030 -14.153 165.307 1.00 88.46 C ANISOU 5667 CZ PHE A 804 8901 14635 10075 -5009 548 1849 C ATOM 5668 N GLU A 805 16.671 -12.915 170.093 1.00 89.63 N ANISOU 5668 N GLU A 805 9322 14624 10111 -4594 803 2101 N ATOM 5669 CA GLU A 805 17.868 -12.279 169.574 1.00 88.50 C ANISOU 5669 CA GLU A 805 9258 14301 10068 -4382 820 2036 C ATOM 5670 C GLU A 805 19.184 -12.980 169.863 1.00 90.16 C ANISOU 5670 C GLU A 805 9762 14133 10360 -4422 774 2124 C ATOM 5671 O GLU A 805 20.028 -13.051 169.002 1.00 88.96 O ANISOU 5671 O GLU A 805 9788 13669 10345 -4277 716 2050 O ATOM 5672 CB GLU A 805 17.935 -10.819 170.005 1.00 89.21 C ANISOU 5672 CB GLU A 805 9150 14675 10071 -4125 932 1972 C ATOM 5673 CG GLU A 805 17.240 -9.870 169.046 1.00 89.59 C ANISOU 5673 CG GLU A 805 8943 15004 10092 -3981 966 1844 C ATOM 5674 CD GLU A 805 17.217 -8.433 169.519 1.00 89.67 C ANISOU 5674 CD GLU A 805 8859 15144 10068 -3628 1042 1735 C ATOM 5675 OE1 GLU A 805 18.126 -8.012 170.247 1.00 87.18 O ANISOU 5675 OE1 GLU A 805 8673 14704 9748 -3515 1069 1761 O ATOM 5676 OE2 GLU A 805 16.285 -7.714 169.150 1.00 91.96 O ANISOU 5676 OE2 GLU A 805 8953 15655 10333 -3461 1068 1624 O ATOM 5677 N ASP A 806 19.349 -13.489 171.069 1.00 94.00 N ANISOU 5677 N ASP A 806 10336 14602 10776 -4533 775 2244 N ATOM 5678 CA ASP A 806 20.561 -14.169 171.510 1.00 92.47 C ANISOU 5678 CA ASP A 806 10423 14055 10656 -4554 725 2333 C ATOM 5679 C ASP A 806 20.928 -15.363 170.634 1.00 89.39 C ANISOU 5679 C ASP A 806 10272 13294 10398 -4707 604 2351 C ATOM 5680 O ASP A 806 21.964 -15.991 170.880 1.00 91.94 O ANISOU 5680 O ASP A 806 10845 13292 10797 -4708 548 2415 O ATOM 5681 CB ASP A 806 20.414 -14.618 172.965 1.00 94.73 C ANISOU 5681 CB ASP A 806 10741 14425 10827 -4639 750 2460 C ATOM 5682 CG ASP A 806 21.364 -13.899 173.892 1.00 97.65 C ANISOU 5682 CG ASP A 806 11152 14795 11155 -4907 689 2544 C ATOM 5683 OD1 ASP A 806 22.486 -13.566 173.451 1.00 98.74 O ANISOU 5683 OD1 ASP A 806 11171 15057 11289 -5008 668 2489 O ATOM 5684 OD2 ASP A 806 20.986 -13.662 175.059 1.00 98.46 O ANISOU 5684 OD2 ASP A 806 11408 14777 11226 -5018 658 2666 O ATOM 5685 N SER A 807 20.121 -15.698 169.626 1.00 80.99 N ANISOU 5685 N SER A 807 9145 12268 9360 -4825 558 2291 N ATOM 5686 CA SER A 807 20.442 -16.803 168.731 1.00 78.27 C ANISOU 5686 CA SER A 807 9029 11575 9137 -4958 443 2287 C ATOM 5687 C SER A 807 20.313 -16.411 167.262 1.00 75.35 C ANISOU 5687 C SER A 807 8595 11185 8849 -4910 415 2151 C ATOM 5688 O SER A 807 20.149 -17.285 166.410 1.00 74.08 O ANISOU 5688 O SER A 807 8556 10834 8756 -5049 325 2126 O ATOM 5689 CB SER A 807 19.562 -18.017 169.028 1.00 81.71 C ANISOU 5689 CB SER A 807 9513 12017 9515 -5219 388 2374 C ATOM 5690 OG SER A 807 19.960 -19.127 168.243 1.00 82.42 O ANISOU 5690 OG SER A 807 9852 11744 9721 -5332 275 2370 O ATOM 5691 N ILE A 808 20.382 -15.118 166.951 1.00 69.76 N ANISOU 5691 N ILE A 808 7706 10666 8134 -4699 485 2053 N ATOM 5692 CA ILE A 808 20.439 -14.654 165.570 1.00 68.03 C ANISOU 5692 CA ILE A 808 7461 10385 8004 -4550 446 1892 C ATOM 5693 C ILE A 808 21.871 -14.759 165.070 1.00 66.03 C ANISOU 5693 C ILE A 808 7469 9723 7896 -4349 386 1821 C ATOM 5694 O ILE A 808 22.816 -14.389 165.773 1.00 64.74 O ANISOU 5694 O ILE A 808 7394 9452 7750 -4161 414 1833 O ATOM 5695 CB ILE A 808 19.924 -13.209 165.461 1.00 66.96 C ANISOU 5695 CB ILE A 808 7052 10586 7803 -4313 530 1785 C ATOM 5696 CG1 ILE A 808 18.477 -13.118 165.935 1.00 69.14 C ANISOU 5696 CG1 ILE A 808 7050 11290 7929 -4502 591 1850 C ATOM 5697 CG2 ILE A 808 20.057 -12.699 164.036 1.00 65.48 C ANISOU 5697 CG2 ILE A 808 6854 10320 7706 -4147 485 1627 C ATOM 5698 CD1 ILE A 808 17.903 -11.730 165.852 1.00 68.39 C ANISOU 5698 CD1 ILE A 808 6684 11535 7765 -4263 670 1745 C ATOM 5699 N LEU A 809 22.038 -15.252 163.851 1.00 65.84 N ANISOU 5699 N LEU A 809 7561 9485 7971 -4386 303 1741 N ATOM 5700 CA LEU A 809 23.364 -15.485 163.309 1.00 64.25 C ANISOU 5700 CA LEU A 809 7609 8900 7905 -4218 242 1672 C ATOM 5701 C LEU A 809 23.881 -14.245 162.583 1.00 61.79 C ANISOU 5701 C LEU A 809 7222 8615 7639 -3891 271 1514 C ATOM 5702 O LEU A 809 23.117 -13.394 162.124 1.00 61.50 O ANISOU 5702 O LEU A 809 6970 8844 7552 -3825 309 1441 O ATOM 5703 CB LEU A 809 23.350 -16.685 162.367 1.00 65.44 C ANISOU 5703 CB LEU A 809 7943 8786 8133 -4419 137 1659 C ATOM 5704 CG LEU A 809 22.736 -17.945 162.967 1.00 68.16 C ANISOU 5704 CG LEU A 809 8370 9095 8431 -4776 97 1815 C ATOM 5705 CD1 LEU A 809 22.849 -19.095 161.997 1.00 69.25 C ANISOU 5705 CD1 LEU A 809 8724 8930 8658 -4946 -15 1785 C ATOM 5706 CD2 LEU A 809 23.411 -18.281 164.283 1.00 68.41 C ANISOU 5706 CD2 LEU A 809 8533 9012 8446 -4771 115 1952 C ATOM 5707 N PHE A 810 25.203 -14.150 162.495 1.00 60.11 N ANISOU 5707 N PHE A 810 7192 8126 7521 -3684 249 1467 N ATOM 5708 CA PHE A 810 25.860 -13.028 161.848 1.00 57.80 C ANISOU 5708 CA PHE A 810 6862 7821 7277 -3382 272 1329 C ATOM 5709 C PHE A 810 26.954 -13.541 160.930 1.00 56.89 C ANISOU 5709 C PHE A 810 6973 7354 7289 -3297 197 1250 C ATOM 5710 O PHE A 810 27.650 -14.507 161.251 1.00 57.46 O ANISOU 5710 O PHE A 810 7253 7163 7416 -3363 148 1312 O ATOM 5711 CB PHE A 810 26.443 -12.052 162.876 1.00 56.47 C ANISOU 5711 CB PHE A 810 6642 7744 7071 -3165 346 1344 C ATOM 5712 CG PHE A 810 25.400 -11.366 163.698 1.00 57.22 C ANISOU 5712 CG PHE A 810 6501 8206 7036 -3198 429 1392 C ATOM 5713 CD1 PHE A 810 24.849 -10.173 163.278 1.00 56.43 C ANISOU 5713 CD1 PHE A 810 6199 8349 6893 -3042 477 1295 C ATOM 5714 CD2 PHE A 810 24.950 -11.927 164.877 1.00 58.88 C ANISOU 5714 CD2 PHE A 810 6690 8523 7161 -3386 456 1533 C ATOM 5715 CE1 PHE A 810 23.878 -9.551 164.022 1.00 57.29 C ANISOU 5715 CE1 PHE A 810 6086 8801 6879 -3056 553 1329 C ATOM 5716 CE2 PHE A 810 23.980 -11.304 165.623 1.00 59.72 C ANISOU 5716 CE2 PHE A 810 6568 8985 7137 -3412 537 1570 C ATOM 5717 CZ PHE A 810 23.447 -10.112 165.195 1.00 58.92 C ANISOU 5717 CZ PHE A 810 6264 9125 6998 -3239 586 1463 C ATOM 5718 N SER A 811 27.081 -12.905 159.776 1.00 56.44 N ANISOU 5718 N SER A 811 6873 7297 7273 -3148 188 1114 N ATOM 5719 CA SER A 811 28.147 -13.210 158.840 1.00 57.93 C ANISOU 5719 CA SER A 811 7249 7189 7571 -3032 130 1021 C ATOM 5720 C SER A 811 28.710 -11.894 158.344 1.00 60.84 C ANISOU 5720 C SER A 811 7540 7621 7957 -2747 171 907 C ATOM 5721 O SER A 811 27.958 -10.963 158.044 1.00 65.40 O ANISOU 5721 O SER A 811 7927 8446 8476 -2693 210 861 O ATOM 5722 CB SER A 811 27.652 -14.046 157.659 1.00 57.59 C ANISOU 5722 CB SER A 811 7268 7052 7562 -3202 56 965 C ATOM 5723 OG SER A 811 26.668 -13.334 156.949 1.00 57.14 O ANISOU 5723 OG SER A 811 7008 7253 7449 -3210 75 900 O ATOM 5724 N TYR A 812 30.029 -11.814 158.272 1.00 51.12 N ANISOU 5724 N TYR A 812 6455 6167 6801 -2568 160 865 N ATOM 5725 CA TYR A 812 30.701 -10.592 157.875 1.00 49.11 C ANISOU 5725 CA TYR A 812 6149 5949 6563 -2308 197 768 C ATOM 5726 C TYR A 812 31.530 -10.857 156.630 1.00 48.41 C ANISOU 5726 C TYR A 812 6194 5638 6560 -2221 145 658 C ATOM 5727 O TYR A 812 32.061 -11.956 156.452 1.00 49.14 O ANISOU 5727 O TYR A 812 6463 5491 6715 -2293 89 666 O ATOM 5728 CB TYR A 812 31.568 -10.059 159.022 1.00 48.13 C ANISOU 5728 CB TYR A 812 6047 5808 6431 -2157 242 817 C ATOM 5729 CG TYR A 812 30.747 -9.598 160.207 1.00 48.72 C ANISOU 5729 CG TYR A 812 5970 6135 6405 -2211 304 907 C ATOM 5730 CD1 TYR A 812 30.243 -10.507 161.125 1.00 50.39 C ANISOU 5730 CD1 TYR A 812 6205 6365 6576 -2416 298 1033 C ATOM 5731 CD2 TYR A 812 30.465 -8.254 160.396 1.00 47.74 C ANISOU 5731 CD2 TYR A 812 5685 6231 6223 -2057 366 864 C ATOM 5732 CE1 TYR A 812 29.482 -10.094 162.193 1.00 51.05 C ANISOU 5732 CE1 TYR A 812 6142 6699 6556 -2468 360 1111 C ATOM 5733 CE2 TYR A 812 29.709 -7.829 161.466 1.00 48.41 C ANISOU 5733 CE2 TYR A 812 5629 6554 6209 -2094 426 933 C ATOM 5734 CZ TYR A 812 29.219 -8.752 162.362 1.00 50.05 C ANISOU 5734 CZ TYR A 812 5850 6796 6371 -2300 426 1055 C ATOM 5735 OH TYR A 812 28.464 -8.324 163.426 1.00 50.82 O ANISOU 5735 OH TYR A 812 5798 7151 6359 -2336 491 1122 O ATOM 5736 N GLN A 813 31.607 -9.856 155.758 1.00 49.14 N ANISOU 5736 N GLN A 813 6203 5815 6650 -2068 163 555 N ATOM 5737 CA GLN A 813 32.430 -9.942 154.559 1.00 49.43 C ANISOU 5737 CA GLN A 813 6349 5676 6755 -1966 126 444 C ATOM 5738 C GLN A 813 33.863 -9.602 154.935 1.00 48.40 C ANISOU 5738 C GLN A 813 6315 5399 6675 -1770 144 430 C ATOM 5739 O GLN A 813 34.165 -8.462 155.296 1.00 47.04 O ANISOU 5739 O GLN A 813 6058 5338 6477 -1614 194 422 O ATOM 5740 CB GLN A 813 31.905 -9.002 153.478 1.00 53.09 C ANISOU 5740 CB GLN A 813 6684 6300 7185 -1893 134 352 C ATOM 5741 CG GLN A 813 32.770 -8.931 152.231 1.00 54.69 C ANISOU 5741 CG GLN A 813 6983 6354 7442 -1775 106 236 C ATOM 5742 CD GLN A 813 32.622 -10.144 151.348 1.00 56.74 C ANISOU 5742 CD GLN A 813 7360 6462 7737 -1923 38 191 C ATOM 5743 OE1 GLN A 813 31.562 -10.375 150.754 1.00 59.61 O ANISOU 5743 OE1 GLN A 813 7653 6934 8063 -2067 9 175 O ATOM 5744 NE2 GLN A 813 33.685 -10.929 151.249 1.00 57.72 N ANISOU 5744 NE2 GLN A 813 7664 6335 7932 -1886 9 166 N ATOM 5745 N VAL A 814 34.748 -10.592 154.860 1.00 45.41 N ANISOU 5745 N VAL A 814 6115 4772 6366 -1776 100 427 N ATOM 5746 CA VAL A 814 36.148 -10.365 155.175 1.00 44.31 C ANISOU 5746 CA VAL A 814 6064 4497 6276 -1593 111 413 C ATOM 5747 C VAL A 814 36.767 -9.466 154.114 1.00 42.89 C ANISOU 5747 C VAL A 814 5853 4332 6110 -1419 127 294 C ATOM 5748 O VAL A 814 36.391 -9.510 152.941 1.00 43.05 O ANISOU 5748 O VAL A 814 5862 4363 6131 -1449 105 211 O ATOM 5749 CB VAL A 814 36.877 -11.716 155.274 1.00 45.35 C ANISOU 5749 CB VAL A 814 6392 4361 6477 -1637 53 434 C ATOM 5750 CG1 VAL A 814 38.299 -11.533 155.728 1.00 44.42 C ANISOU 5750 CG1 VAL A 814 6349 4124 6404 -1451 62 432 C ATOM 5751 CG2 VAL A 814 36.133 -12.634 156.217 1.00 46.98 C ANISOU 5751 CG2 VAL A 814 6636 4553 6662 -1840 30 559 C ATOM 5752 N ASP A 815 37.710 -8.619 154.530 1.00 41.57 N ANISOU 5752 N ASP A 815 5671 4176 5948 -1245 164 287 N ATOM 5753 CA ASP A 815 38.467 -7.771 153.611 1.00 40.28 C ANISOU 5753 CA ASP A 815 5493 4014 5798 -1083 179 186 C ATOM 5754 C ASP A 815 39.916 -8.237 153.580 1.00 40.02 C ANISOU 5754 C ASP A 815 5588 3787 5830 -971 161 157 C ATOM 5755 O ASP A 815 40.663 -8.013 154.537 1.00 39.57 O ANISOU 5755 O ASP A 815 5545 3709 5779 -890 179 209 O ATOM 5756 CB ASP A 815 38.386 -6.304 154.012 1.00 40.37 C ANISOU 5756 CB ASP A 815 5377 4205 5756 -973 233 192 C ATOM 5757 CG ASP A 815 39.222 -5.420 153.116 1.00 41.03 C ANISOU 5757 CG ASP A 815 5459 4282 5851 -819 246 101 C ATOM 5758 OD1 ASP A 815 39.506 -5.832 151.975 1.00 41.82 O ANISOU 5758 OD1 ASP A 815 5615 4295 5979 -816 219 24 O ATOM 5759 OD2 ASP A 815 39.604 -4.317 153.546 1.00 43.02 O ANISOU 5759 OD2 ASP A 815 5656 4613 6077 -707 283 106 O ATOM 5760 N SER A 816 40.305 -8.883 152.479 1.00 40.40 N ANISOU 5760 N SER A 816 5726 3705 5921 -963 126 71 N ATOM 5761 CA SER A 816 41.661 -9.370 152.264 1.00 40.34 C ANISOU 5761 CA SER A 816 5833 3523 5972 -844 109 24 C ATOM 5762 C SER A 816 42.489 -8.428 151.416 1.00 39.12 C ANISOU 5762 C SER A 816 5635 3417 5811 -691 139 -68 C ATOM 5763 O SER A 816 43.663 -8.707 151.170 1.00 39.04 O ANISOU 5763 O SER A 816 5696 3296 5842 -579 132 -116 O ATOM 5764 CB SER A 816 41.646 -10.736 151.575 1.00 41.76 C ANISOU 5764 CB SER A 816 6150 3516 6199 -920 50 -23 C ATOM 5765 OG SER A 816 40.600 -11.545 152.049 1.00 43.05 O ANISOU 5765 OG SER A 816 6345 3656 6355 -1106 18 52 O ATOM 5766 N LYS A 817 41.911 -7.336 150.953 1.00 38.30 N ANISOU 5766 N LYS A 817 5418 3480 5655 -683 170 -93 N ATOM 5767 CA LYS A 817 42.556 -6.551 149.918 1.00 37.42 C ANISOU 5767 CA LYS A 817 5280 3406 5531 -570 190 -184 C ATOM 5768 C LYS A 817 43.771 -5.817 150.474 1.00 36.42 C ANISOU 5768 C LYS A 817 5141 3285 5412 -428 223 -172 C ATOM 5769 O LYS A 817 43.690 -5.163 151.513 1.00 35.89 O ANISOU 5769 O LYS A 817 5019 3295 5323 -411 247 -100 O ATOM 5770 CB LYS A 817 41.553 -5.566 149.320 1.00 36.96 C ANISOU 5770 CB LYS A 817 5112 3520 5411 -601 206 -201 C ATOM 5771 CG LYS A 817 42.211 -4.396 148.617 1.00 35.86 C ANISOU 5771 CG LYS A 817 4930 3451 5245 -478 236 -258 C ATOM 5772 CD LYS A 817 41.238 -3.545 147.856 1.00 35.65 C ANISOU 5772 CD LYS A 817 4815 3570 5159 -502 239 -280 C ATOM 5773 CE LYS A 817 41.968 -2.823 146.757 1.00 35.01 C ANISOU 5773 CE LYS A 817 4738 3508 5057 -408 251 -354 C ATOM 5774 NZ LYS A 817 43.029 -1.955 147.252 1.00 34.05 N ANISOU 5774 NZ LYS A 817 4611 3391 4937 -294 286 -337 N ATOM 5775 N PHE A 818 44.906 -5.936 149.793 1.00 36.27 N ANISOU 5775 N PHE A 818 5170 3194 5418 -328 223 -245 N ATOM 5776 CA PHE A 818 46.056 -5.128 150.148 1.00 35.37 C ANISOU 5776 CA PHE A 818 5026 3112 5301 -203 254 -242 C ATOM 5777 C PHE A 818 46.029 -3.825 149.352 1.00 34.43 C ANISOU 5777 C PHE A 818 4830 3122 5129 -162 286 -287 C ATOM 5778 O PHE A 818 45.141 -3.580 148.540 1.00 34.49 O ANISOU 5778 O PHE A 818 4807 3193 5104 -217 282 -318 O ATOM 5779 CB PHE A 818 47.358 -5.903 149.939 1.00 35.83 C ANISOU 5779 CB PHE A 818 5163 3044 5409 -110 241 -290 C ATOM 5780 CG PHE A 818 47.477 -6.561 148.599 1.00 36.50 C ANISOU 5780 CG PHE A 818 5303 3063 5504 -105 224 -395 C ATOM 5781 CD1 PHE A 818 47.592 -5.812 147.439 1.00 35.99 C ANISOU 5781 CD1 PHE A 818 5191 3089 5396 -75 249 -472 C ATOM 5782 CD2 PHE A 818 47.510 -7.932 148.498 1.00 37.76 C ANISOU 5782 CD2 PHE A 818 5571 3064 5713 -129 182 -419 C ATOM 5783 CE1 PHE A 818 47.705 -6.417 146.222 1.00 36.69 C ANISOU 5783 CE1 PHE A 818 5330 3127 5484 -70 236 -573 C ATOM 5784 CE2 PHE A 818 47.628 -8.536 147.281 1.00 38.48 C ANISOU 5784 CE2 PHE A 818 5721 3092 5809 -120 166 -527 C ATOM 5785 CZ PHE A 818 47.726 -7.777 146.143 1.00 37.93 C ANISOU 5785 CZ PHE A 818 5593 3129 5690 -90 196 -606 C ATOM 5786 N ASN A 819 47.011 -2.970 149.607 1.00 34.07 N ANISOU 5786 N ASN A 819 4755 3118 5072 -68 313 -284 N ATOM 5787 CA ASN A 819 47.164 -1.693 148.911 1.00 32.85 C ANISOU 5787 CA ASN A 819 4544 3070 4868 -26 340 -318 C ATOM 5788 C ASN A 819 45.969 -0.772 149.115 1.00 32.46 C ANISOU 5788 C ASN A 819 4432 3129 4772 -72 348 -277 C ATOM 5789 O ASN A 819 45.557 -0.058 148.206 1.00 32.22 O ANISOU 5789 O ASN A 819 4371 3171 4700 -73 352 -311 O ATOM 5790 CB ASN A 819 47.430 -1.880 147.421 1.00 33.11 C ANISOU 5790 CB ASN A 819 4597 3095 4889 -13 339 -411 C ATOM 5791 CG ASN A 819 47.991 -0.638 146.791 1.00 32.40 C ANISOU 5791 CG ASN A 819 4465 3097 4750 41 367 -436 C ATOM 5792 OD1 ASN A 819 48.702 0.116 147.443 1.00 31.84 O ANISOU 5792 OD1 ASN A 819 4370 3056 4671 90 386 -401 O ATOM 5793 ND2 ASN A 819 47.662 -0.396 145.536 1.00 32.51 N ANISOU 5793 ND2 ASN A 819 4474 3156 4724 23 366 -492 N ATOM 5794 N ARG A 820 45.423 -0.759 150.317 1.00 32.48 N ANISOU 5794 N ARG A 820 4414 3152 4775 -103 349 -204 N ATOM 5795 CA ARG A 820 44.524 0.317 150.687 1.00 32.08 C ANISOU 5795 CA ARG A 820 4296 3219 4675 -110 364 -168 C ATOM 5796 C ARG A 820 45.368 1.501 151.143 1.00 31.29 C ANISOU 5796 C ARG A 820 4184 3153 4552 -25 388 -158 C ATOM 5797 O ARG A 820 46.594 1.489 151.047 1.00 31.06 O ANISOU 5797 O ARG A 820 4186 3074 4542 26 393 -180 O ATOM 5798 CB ARG A 820 43.544 -0.138 151.753 1.00 32.58 C ANISOU 5798 CB ARG A 820 4333 3311 4735 -181 361 -100 C ATOM 5799 CG ARG A 820 42.705 -1.322 151.373 1.00 33.52 C ANISOU 5799 CG ARG A 820 4468 3394 4874 -288 333 -102 C ATOM 5800 CD ARG A 820 41.433 -1.309 152.173 1.00 33.98 C ANISOU 5800 CD ARG A 820 4462 3550 4899 -365 337 -38 C ATOM 5801 NE ARG A 820 40.542 -2.404 151.815 1.00 35.02 N ANISOU 5801 NE ARG A 820 4602 3661 5042 -491 308 -35 N ATOM 5802 CZ ARG A 820 39.620 -2.342 150.854 1.00 35.37 C ANISOU 5802 CZ ARG A 820 4601 3778 5061 -544 292 -73 C ATOM 5803 NH1 ARG A 820 39.460 -1.237 150.148 1.00 34.77 N ANISOU 5803 NH1 ARG A 820 4471 3795 4946 -472 302 -113 N ATOM 5804 NH2 ARG A 820 38.856 -3.388 150.605 1.00 36.43 N ANISOU 5804 NH2 ARG A 820 4749 3889 5205 -674 261 -67 N ATOM 5805 N LYS A 821 44.715 2.553 151.618 1.00 30.98 N ANISOU 5805 N LYS A 821 4099 3205 4469 -9 401 -130 N ATOM 5806 CA LYS A 821 45.410 3.735 152.108 1.00 30.37 C ANISOU 5806 CA LYS A 821 4021 3153 4364 60 418 -122 C ATOM 5807 C LYS A 821 46.390 3.369 153.222 1.00 32.73 C ANISOU 5807 C LYS A 821 4345 3401 4688 77 422 -87 C ATOM 5808 O LYS A 821 46.005 2.775 154.233 1.00 36.79 O ANISOU 5808 O LYS A 821 4855 3913 5211 45 421 -37 O ATOM 5809 CB LYS A 821 44.377 4.752 152.591 1.00 30.31 C ANISOU 5809 CB LYS A 821 3969 3241 4307 77 427 -98 C ATOM 5810 CG LYS A 821 44.865 5.684 153.685 1.00 29.97 C ANISOU 5810 CG LYS A 821 3934 3215 4237 130 442 -73 C ATOM 5811 CD LYS A 821 44.186 7.021 153.645 1.00 29.87 C ANISOU 5811 CD LYS A 821 3904 3275 4173 182 447 -82 C ATOM 5812 CE LYS A 821 43.560 7.340 154.971 1.00 30.37 C ANISOU 5812 CE LYS A 821 3936 3401 4203 199 463 -47 C ATOM 5813 NZ LYS A 821 43.305 8.791 155.121 1.00 30.04 N ANISOU 5813 NZ LYS A 821 3903 3400 4111 277 466 -65 N ATOM 5814 N ILE A 822 47.665 3.724 153.034 1.00 29.96 N ANISOU 5814 N ILE A 822 4019 3021 4345 124 426 -110 N ATOM 5815 CA ILE A 822 48.727 3.123 153.840 1.00 30.08 C ANISOU 5815 CA ILE A 822 4054 2983 4391 144 421 -86 C ATOM 5816 C ILE A 822 48.940 3.853 155.168 1.00 29.85 C ANISOU 5816 C ILE A 822 4017 2994 4331 163 428 -40 C ATOM 5817 O ILE A 822 49.367 3.242 156.149 1.00 30.11 O ANISOU 5817 O ILE A 822 4060 3000 4381 164 420 2 O ATOM 5818 CB ILE A 822 50.034 3.060 153.033 1.00 30.00 C ANISOU 5818 CB ILE A 822 4059 2943 4399 184 422 -134 C ATOM 5819 CG1 ILE A 822 50.492 4.462 152.652 1.00 29.49 C ANISOU 5819 CG1 ILE A 822 3982 2936 4288 206 436 -155 C ATOM 5820 CG2 ILE A 822 49.856 2.218 151.794 1.00 30.38 C ANISOU 5820 CG2 ILE A 822 4122 2948 4472 169 415 -187 C ATOM 5821 CD1 ILE A 822 51.853 4.504 152.019 1.00 29.52 C ANISOU 5821 CD1 ILE A 822 3983 2936 4296 236 441 -192 C ATOM 5822 N SER A 823 48.636 5.141 155.238 1.00 30.25 N ANISOU 5822 N SER A 823 4056 3105 4334 181 440 -47 N ATOM 5823 CA SER A 823 48.958 5.930 156.409 1.00 29.34 C ANISOU 5823 CA SER A 823 3942 3022 4183 203 445 -19 C ATOM 5824 C SER A 823 48.122 7.195 156.380 1.00 30.82 C ANISOU 5824 C SER A 823 4124 3266 4318 223 455 -32 C ATOM 5825 O SER A 823 47.388 7.456 155.429 1.00 36.09 O ANISOU 5825 O SER A 823 4783 3950 4979 224 455 -58 O ATOM 5826 CB SER A 823 50.435 6.282 156.431 1.00 29.14 C ANISOU 5826 CB SER A 823 3933 2978 4161 228 439 -32 C ATOM 5827 OG SER A 823 50.644 7.439 155.659 1.00 28.84 O ANISOU 5827 OG SER A 823 3907 2958 4093 238 443 -69 O ATOM 5828 N ASP A 824 48.238 7.982 157.433 1.00 29.16 N ANISOU 5828 N ASP A 824 3924 3086 4068 246 459 -18 N ATOM 5829 CA ASP A 824 47.776 9.347 157.374 1.00 29.08 C ANISOU 5829 CA ASP A 824 3933 3109 4009 284 462 -42 C ATOM 5830 C ASP A 824 48.628 10.124 156.386 1.00 28.80 C ANISOU 5830 C ASP A 824 3936 3035 3972 290 451 -75 C ATOM 5831 O ASP A 824 49.733 9.717 156.030 1.00 28.67 O ANISOU 5831 O ASP A 824 3923 2986 3983 268 446 -79 O ATOM 5832 CB ASP A 824 47.831 9.987 158.759 1.00 29.25 C ANISOU 5832 CB ASP A 824 3968 3162 3984 306 467 -28 C ATOM 5833 CG ASP A 824 46.752 9.472 159.668 1.00 32.08 C ANISOU 5833 CG ASP A 824 4283 3584 4322 303 485 3 C ATOM 5834 OD1 ASP A 824 45.995 8.584 159.241 1.00 40.15 O ANISOU 5834 OD1 ASP A 824 5264 4621 5370 271 490 19 O ATOM 5835 OD2 ASP A 824 46.657 9.945 160.811 1.00 32.10 O ANISOU 5835 OD2 ASP A 824 4292 3628 4276 323 493 11 O ATOM 5836 N ALA A 825 48.101 11.257 155.943 1.00 28.83 N ANISOU 5836 N ALA A 825 3968 3047 3940 321 446 -97 N ATOM 5837 CA ALA A 825 48.755 12.039 154.904 1.00 28.70 C ANISOU 5837 CA ALA A 825 3996 2997 3914 315 433 -119 C ATOM 5838 C ALA A 825 49.720 13.084 155.438 1.00 28.74 C ANISOU 5838 C ALA A 825 4057 2974 3886 311 422 -123 C ATOM 5839 O ALA A 825 50.583 13.538 154.683 1.00 28.70 O ANISOU 5839 O ALA A 825 4083 2945 3876 279 413 -132 O ATOM 5840 CB ALA A 825 47.707 12.738 154.034 1.00 28.87 C ANISOU 5840 CB ALA A 825 4030 3029 3911 350 424 -133 C ATOM 5841 N THR A 826 49.584 13.496 156.699 1.00 28.91 N ANISOU 5841 N THR A 826 4096 3008 3881 333 422 -118 N ATOM 5842 CA THR A 826 50.475 14.510 157.242 1.00 29.06 C ANISOU 5842 CA THR A 826 4178 2999 3864 319 405 -127 C ATOM 5843 C THR A 826 51.921 14.056 157.117 1.00 28.92 C ANISOU 5843 C THR A 826 4141 2978 3868 259 401 -117 C ATOM 5844 O THR A 826 52.254 12.896 157.362 1.00 28.79 O ANISOU 5844 O THR A 826 4066 2983 3889 249 411 -100 O ATOM 5845 CB THR A 826 50.144 14.809 158.700 1.00 29.34 C ANISOU 5845 CB THR A 826 4226 3058 3864 350 408 -128 C ATOM 5846 OG1 THR A 826 48.763 15.136 158.826 1.00 29.60 O ANISOU 5846 OG1 THR A 826 4257 3116 3873 417 417 -140 O ATOM 5847 CG2 THR A 826 50.937 15.985 159.179 1.00 29.63 C ANISOU 5847 CG2 THR A 826 4344 3057 3857 332 384 -147 C ATOM 5848 N ILE A 827 52.772 14.971 156.689 1.00 29.06 N ANISOU 5848 N ILE A 827 4209 2970 3862 219 385 -127 N ATOM 5849 CA ILE A 827 54.184 14.706 156.484 1.00 29.08 C ANISOU 5849 CA ILE A 827 4185 2991 3874 159 381 -121 C ATOM 5850 C ILE A 827 54.925 15.399 157.626 1.00 29.72 C ANISOU 5850 C ILE A 827 4300 3075 3916 129 360 -120 C ATOM 5851 O ILE A 827 54.905 16.629 157.744 1.00 31.25 O ANISOU 5851 O ILE A 827 4577 3230 4066 110 340 -134 O ATOM 5852 CB ILE A 827 54.633 15.175 155.096 1.00 29.16 C ANISOU 5852 CB ILE A 827 4214 2990 3875 116 380 -129 C ATOM 5853 CG1 ILE A 827 54.026 14.249 154.038 1.00 28.89 C ANISOU 5853 CG1 ILE A 827 4133 2967 3878 144 400 -134 C ATOM 5854 CG2 ILE A 827 56.122 15.172 154.959 1.00 29.39 C ANISOU 5854 CG2 ILE A 827 4213 3057 3896 49 377 -125 C ATOM 5855 CD1 ILE A 827 54.297 14.650 152.595 1.00 29.02 C ANISOU 5855 CD1 ILE A 827 4167 2984 3876 107 402 -142 C ATOM 5856 N TYR A 828 55.538 14.602 158.498 1.00 29.42 N ANISOU 5856 N TYR A 828 4205 3078 3893 125 360 -104 N ATOM 5857 CA TYR A 828 55.970 15.053 159.815 1.00 29.74 C ANISOU 5857 CA TYR A 828 4271 3136 3894 109 339 -102 C ATOM 5858 C TYR A 828 57.471 15.264 159.855 1.00 30.07 C ANISOU 5858 C TYR A 828 4291 3214 3921 37 319 -98 C ATOM 5859 O TYR A 828 58.241 14.401 159.429 1.00 30.03 O ANISOU 5859 O TYR A 828 4208 3253 3951 30 326 -85 O ATOM 5860 CB TYR A 828 55.585 14.044 160.892 1.00 29.69 C ANISOU 5860 CB TYR A 828 4217 3162 3901 151 347 -77 C ATOM 5861 CG TYR A 828 54.113 13.941 161.202 1.00 29.58 C ANISOU 5861 CG TYR A 828 4218 3139 3883 209 367 -79 C ATOM 5862 CD1 TYR A 828 53.516 14.814 162.086 1.00 29.90 C ANISOU 5862 CD1 TYR A 828 4313 3178 3867 233 363 -98 C ATOM 5863 CD2 TYR A 828 53.329 12.938 160.639 1.00 29.31 C ANISOU 5863 CD2 TYR A 828 4135 3104 3895 238 389 -63 C ATOM 5864 CE1 TYR A 828 52.183 14.715 162.384 1.00 29.94 C ANISOU 5864 CE1 TYR A 828 4315 3199 3862 290 385 -102 C ATOM 5865 CE2 TYR A 828 51.984 12.835 160.939 1.00 29.34 C ANISOU 5865 CE2 TYR A 828 4137 3122 3889 279 407 -61 C ATOM 5866 CZ TYR A 828 51.419 13.726 161.814 1.00 29.66 C ANISOU 5866 CZ TYR A 828 4221 3178 3872 308 407 -80 C ATOM 5867 OH TYR A 828 50.090 13.644 162.130 1.00 29.84 O ANISOU 5867 OH TYR A 828 4225 3235 3876 355 429 -81 O ATOM 5868 N ALA A 829 57.880 16.406 160.383 1.00 30.52 N ANISOU 5868 N ALA A 829 4415 3257 3923 -14 291 -113 N ATOM 5869 CA ALA A 829 59.272 16.604 160.728 1.00 30.99 C ANISOU 5869 CA ALA A 829 4445 3371 3958 -91 266 -107 C ATOM 5870 C ALA A 829 59.569 15.974 162.088 1.00 31.15 C ANISOU 5870 C ALA A 829 4420 3446 3969 -70 251 -90 C ATOM 5871 O ALA A 829 58.672 15.731 162.900 1.00 31.01 O ANISOU 5871 O ALA A 829 4423 3414 3946 -11 258 -87 O ATOM 5872 CB ALA A 829 59.603 18.092 160.737 1.00 31.55 C ANISOU 5872 CB ALA A 829 4618 3399 3971 -173 235 -129 C ATOM 5873 N THR A 830 60.845 15.669 162.310 1.00 31.53 N ANISOU 5873 N THR A 830 4397 3570 4012 -116 231 -75 N ATOM 5874 CA THR A 830 61.340 15.229 163.608 1.00 31.88 C ANISOU 5874 CA THR A 830 4403 3676 4035 -109 205 -54 C ATOM 5875 C THR A 830 62.560 16.058 163.971 1.00 32.62 C ANISOU 5875 C THR A 830 4495 3826 4073 -210 164 -64 C ATOM 5876 O THR A 830 63.200 16.656 163.107 1.00 32.86 O ANISOU 5876 O THR A 830 4524 3866 4095 -285 162 -75 O ATOM 5877 CB THR A 830 61.721 13.742 163.629 1.00 31.79 C ANISOU 5877 CB THR A 830 4284 3717 4077 -47 212 -17 C ATOM 5878 OG1 THR A 830 62.880 13.545 162.822 1.00 32.07 O ANISOU 5878 OG1 THR A 830 4242 3815 4130 -79 209 -18 O ATOM 5879 CG2 THR A 830 60.598 12.876 163.093 1.00 31.18 C ANISOU 5879 CG2 THR A 830 4208 3580 4057 31 249 -8 C ATOM 5880 N ARG A 831 62.854 16.109 165.272 1.00 33.07 N ANISOU 5880 N ARG A 831 4554 3928 4085 -221 131 -57 N ATOM 5881 CA ARG A 831 64.069 16.716 165.804 1.00 33.90 C ANISOU 5881 CA ARG A 831 4641 4108 4133 -319 84 -62 C ATOM 5882 C ARG A 831 64.565 15.932 167.010 1.00 34.29 C ANISOU 5882 C ARG A 831 4619 4246 4163 -288 53 -29 C ATOM 5883 O ARG A 831 63.836 15.148 167.615 1.00 33.97 O ANISOU 5883 O ARG A 831 4577 4192 4140 -202 66 -5 O ATOM 5884 CB ARG A 831 63.877 18.180 166.217 1.00 34.38 C ANISOU 5884 CB ARG A 831 4832 4107 4123 -400 57 -106 C ATOM 5885 CG ARG A 831 63.288 19.081 165.120 1.00 34.16 C ANISOU 5885 CG ARG A 831 4901 3971 4105 -426 77 -134 C ATOM 5886 CD ARG A 831 64.313 19.495 164.042 1.00 34.53 C ANISOU 5886 CD ARG A 831 4915 4052 4154 -534 70 -126 C ATOM 5887 NE ARG A 831 63.817 20.656 163.307 1.00 34.66 N ANISOU 5887 NE ARG A 831 5062 3954 4152 -583 70 -150 N ATOM 5888 CZ ARG A 831 62.956 20.590 162.284 1.00 34.05 C ANISOU 5888 CZ ARG A 831 5017 3804 4116 -523 106 -149 C ATOM 5889 NH1 ARG A 831 62.555 21.718 161.688 1.00 34.34 N ANISOU 5889 NH1 ARG A 831 5183 3735 4130 -568 95 -165 N ATOM 5890 NH2 ARG A 831 62.485 19.407 161.856 1.00 33.26 N ANISOU 5890 NH2 ARG A 831 4826 3732 4078 -421 149 -130 N ATOM 5891 N GLN A 832 65.826 16.167 167.344 1.00 35.08 N ANISOU 5891 N GLN A 832 4659 4447 4224 -366 10 -24 N ATOM 5892 CA GLN A 832 66.439 15.639 168.551 1.00 35.68 C ANISOU 5892 CA GLN A 832 4673 4620 4264 -354 -34 7 C ATOM 5893 C GLN A 832 66.261 16.646 169.680 1.00 36.21 C ANISOU 5893 C GLN A 832 4840 4676 4243 -420 -70 -25 C ATOM 5894 O GLN A 832 66.721 17.787 169.572 1.00 36.75 O ANISOU 5894 O GLN A 832 4964 4738 4263 -534 -96 -64 O ATOM 5895 CB GLN A 832 67.917 15.372 168.304 1.00 36.42 C ANISOU 5895 CB GLN A 832 4634 4847 4355 -400 -65 27 C ATOM 5896 CG GLN A 832 68.192 14.571 167.056 1.00 36.08 C ANISOU 5896 CG GLN A 832 4499 4820 4389 -343 -26 40 C ATOM 5897 CD GLN A 832 67.648 13.171 167.159 1.00 35.60 C ANISOU 5897 CD GLN A 832 4404 4730 4395 -199 -6 78 C ATOM 5898 OE1 GLN A 832 67.046 12.651 166.218 1.00 36.11 O ANISOU 5898 OE1 GLN A 832 4473 4723 4523 -137 40 73 O ATOM 5899 NE2 GLN A 832 67.849 12.548 168.309 1.00 36.04 N ANISOU 5899 NE2 GLN A 832 4428 4835 4429 -153 -45 118 N ATOM 5900 N ALA A 833 65.598 16.236 170.759 1.00 37.80 N ANISOU 5900 N ALA A 833 5070 4874 4417 -355 -74 -10 N ATOM 5901 CA ALA A 833 65.443 17.128 171.902 1.00 39.34 C ANISOU 5901 CA ALA A 833 5358 5072 4518 -408 -108 -48 C ATOM 5902 C ALA A 833 65.265 16.318 173.176 1.00 40.63 C ANISOU 5902 C ALA A 833 5491 5303 4644 -346 -125 -6 C ATOM 5903 O ALA A 833 64.951 15.125 173.143 1.00 40.15 O ANISOU 5903 O ALA A 833 5368 5252 4637 -255 -102 52 O ATOM 5904 CB ALA A 833 64.258 18.078 171.720 1.00 39.15 C ANISOU 5904 CB ALA A 833 5476 4921 4479 -398 -75 -108 C ATOM 5905 N LYS A 834 65.477 16.992 174.305 1.00 47.94 N ANISOU 5905 N LYS A 834 6470 6273 5471 -404 -168 -35 N ATOM 5906 CA LYS A 834 65.131 16.477 175.623 1.00 46.87 C ANISOU 5906 CA LYS A 834 6338 6197 5274 -356 -182 -5 C ATOM 5907 C LYS A 834 63.882 17.207 176.092 1.00 44.52 C ANISOU 5907 C LYS A 834 6169 5825 4923 -332 -148 -66 C ATOM 5908 O LYS A 834 63.887 18.434 176.214 1.00 42.98 O ANISOU 5908 O LYS A 834 6074 5586 4671 -397 -165 -143 O ATOM 5909 CB LYS A 834 66.273 16.672 176.613 1.00 52.91 C ANISOU 5909 CB LYS A 834 7064 7087 5953 -434 -258 2 C ATOM 5910 CG LYS A 834 67.605 16.100 176.172 1.00 56.67 C ANISOU 5910 CG LYS A 834 7403 7661 6470 -459 -298 52 C ATOM 5911 CD LYS A 834 68.674 16.384 177.229 1.00 59.31 C ANISOU 5911 CD LYS A 834 7697 8131 6706 -542 -380 55 C ATOM 5912 CE LYS A 834 70.065 16.013 176.744 1.00 60.57 C ANISOU 5912 CE LYS A 834 7710 8408 6897 -577 -422 92 C ATOM 5913 NZ LYS A 834 70.877 17.209 176.387 1.00 63.88 N ANISOU 5913 NZ LYS A 834 8142 8855 7274 -731 -455 32 N ATOM 5914 N VAL A 835 62.814 16.457 176.331 1.00 39.37 N ANISOU 5914 N VAL A 835 5514 5156 4287 -238 -100 -32 N ATOM 5915 CA VAL A 835 61.526 17.008 176.731 1.00 38.90 C ANISOU 5915 CA VAL A 835 5552 5046 4180 -193 -57 -85 C ATOM 5916 C VAL A 835 61.050 16.246 177.958 1.00 43.57 C ANISOU 5916 C VAL A 835 6122 5725 4707 -148 -51 -36 C ATOM 5917 O VAL A 835 61.220 15.025 178.042 1.00 48.13 O ANISOU 5917 O VAL A 835 6614 6347 5324 -115 -53 55 O ATOM 5918 CB VAL A 835 60.481 16.909 175.590 1.00 36.73 C ANISOU 5918 CB VAL A 835 5293 4671 3993 -127 7 -94 C ATOM 5919 CG1 VAL A 835 59.152 17.523 176.008 1.00 36.86 C ANISOU 5919 CG1 VAL A 835 5398 4653 3955 -70 51 -153 C ATOM 5920 CG2 VAL A 835 61.009 17.553 174.300 1.00 36.37 C ANISOU 5920 CG2 VAL A 835 5263 4546 4011 -176 0 -126 C ATOM 5921 N GLY A 836 60.457 16.959 178.908 1.00 41.30 N ANISOU 5921 N GLY A 836 5917 5460 4315 -144 -45 -96 N ATOM 5922 CA GLY A 836 59.885 16.311 180.072 1.00 46.96 C ANISOU 5922 CA GLY A 836 6618 6270 4955 -106 -30 -52 C ATOM 5923 C GLY A 836 60.894 15.651 180.992 1.00 49.14 C ANISOU 5923 C GLY A 836 6834 6659 5180 -147 -93 20 C ATOM 5924 O GLY A 836 61.706 16.334 181.615 1.00 50.04 O ANISOU 5924 O GLY A 836 6977 6824 5214 -214 -150 -22 O ATOM 5925 N LYS A 837 60.826 14.332 181.092 1.00 65.97 N ANISOU 5925 N LYS A 837 8885 8827 7354 -108 -88 131 N ATOM 5926 CA LYS A 837 61.660 13.540 181.987 1.00 73.42 C ANISOU 5926 CA LYS A 837 9774 9879 8242 -127 -148 214 C ATOM 5927 C LYS A 837 62.893 12.857 181.433 1.00 76.55 C ANISOU 5927 C LYS A 837 10079 10277 8730 -129 -198 280 C ATOM 5928 O LYS A 837 63.429 11.991 182.091 1.00 79.62 O ANISOU 5928 O LYS A 837 10410 10735 9108 -110 -241 375 O ATOM 5929 CB LYS A 837 60.810 12.456 182.647 1.00 77.53 C ANISOU 5929 CB LYS A 837 10284 10448 8724 -81 -116 300 C ATOM 5930 CG LYS A 837 59.997 12.877 183.869 1.00 80.20 C ANISOU 5930 CG LYS A 837 10688 10870 8916 -92 -95 255 C ATOM 5931 CD LYS A 837 58.726 12.046 183.995 1.00 81.74 C ANISOU 5931 CD LYS A 837 10878 11081 9099 -46 -26 312 C ATOM 5932 CE LYS A 837 58.652 11.230 185.283 1.00 84.66 C ANISOU 5932 CE LYS A 837 11246 11584 9336 -63 -43 385 C ATOM 5933 NZ LYS A 837 57.838 9.983 185.136 1.00 85.63 N ANISOU 5933 NZ LYS A 837 11331 11713 9491 -41 -9 510 N ATOM 5934 N ASP A 838 63.334 13.196 180.236 1.00 69.04 N ANISOU 5934 N ASP A 838 9112 9256 7863 -147 -195 233 N ATOM 5935 CA ASP A 838 64.496 12.533 179.675 1.00 67.05 C ANISOU 5935 CA ASP A 838 8765 9023 7688 -148 -238 278 C ATOM 5936 C ASP A 838 65.744 13.384 179.751 1.00 64.47 C ANISOU 5936 C ASP A 838 8423 8772 7301 -239 -303 229 C ATOM 5937 O ASP A 838 65.666 14.588 179.634 1.00 62.67 O ANISOU 5937 O ASP A 838 8278 8524 7012 -308 -302 139 O ATOM 5938 CB ASP A 838 64.275 12.108 178.206 1.00 65.58 C ANISOU 5938 CB ASP A 838 8558 8730 7629 -117 -190 261 C ATOM 5939 CG ASP A 838 62.849 12.283 177.714 1.00 66.19 C ANISOU 5939 CG ASP A 838 8679 8716 7753 -55 -116 270 C ATOM 5940 OD1 ASP A 838 61.970 11.541 178.144 1.00 69.73 O ANISOU 5940 OD1 ASP A 838 9117 9179 8198 -8 -107 346 O ATOM 5941 OD2 ASP A 838 62.616 13.133 176.853 1.00 66.77 O ANISOU 5941 OD2 ASP A 838 8798 8706 7867 -59 -70 205 O ATOM 5942 N LYS A 839 66.898 12.765 179.978 1.00 65.07 N ANISOU 5942 N LYS A 839 8395 8938 7391 -240 -364 287 N ATOM 5943 CA LYS A 839 68.157 13.516 179.997 1.00 66.73 C ANISOU 5943 CA LYS A 839 8561 9222 7570 -335 -421 243 C ATOM 5944 C LYS A 839 69.144 13.039 178.947 1.00 67.83 C ANISOU 5944 C LYS A 839 8571 9398 7803 -304 -439 286 C ATOM 5945 O LYS A 839 70.326 13.310 178.989 1.00 70.61 O ANISOU 5945 O LYS A 839 8845 9854 8127 -372 -494 275 O ATOM 5946 CB LYS A 839 68.781 13.681 181.380 1.00 65.71 C ANISOU 5946 CB LYS A 839 8428 9226 7312 -398 -498 247 C ATOM 5947 CG LYS A 839 69.394 15.067 181.577 1.00 64.41 C ANISOU 5947 CG LYS A 839 8277 9108 7087 -536 -545 164 C ATOM 5948 CD LYS A 839 69.121 15.629 182.972 1.00 65.30 C ANISOU 5948 CD LYS A 839 8364 9373 7074 -602 -633 174 C ATOM 5949 CE LYS A 839 69.184 17.157 183.015 1.00 65.88 C ANISOU 5949 CE LYS A 839 8580 9424 7028 -688 -640 80 C ATOM 5950 NZ LYS A 839 70.544 17.772 182.980 1.00 66.98 N ANISOU 5950 NZ LYS A 839 8748 9569 7131 -836 -682 -6 N ATOM 5951 N ALA A 840 68.601 12.318 177.999 1.00 74.59 N ANISOU 5951 N ALA A 840 9399 10180 8764 -202 -393 333 N ATOM 5952 CA ALA A 840 69.312 11.821 176.872 1.00 74.71 C ANISOU 5952 CA ALA A 840 9323 10187 8878 -172 -380 335 C ATOM 5953 C ALA A 840 68.486 12.398 175.735 1.00 74.06 C ANISOU 5953 C ALA A 840 9311 9975 8854 -193 -306 270 C ATOM 5954 O ALA A 840 67.278 12.459 175.836 1.00 74.85 O ANISOU 5954 O ALA A 840 9505 9975 8960 -165 -257 259 O ATOM 5955 CB ALA A 840 69.229 10.327 176.870 1.00 75.99 C ANISOU 5955 CB ALA A 840 9414 10343 9116 -41 -385 422 C ATOM 5956 N ASP A 841 69.120 12.838 174.666 1.00 66.19 N ANISOU 5956 N ASP A 841 8264 8991 7892 -246 -300 230 N ATOM 5957 CA ASP A 841 68.386 13.395 173.557 1.00 57.72 C ANISOU 5957 CA ASP A 841 7252 7801 6877 -260 -235 179 C ATOM 5958 C ASP A 841 67.549 12.304 172.998 1.00 50.91 C ANISOU 5958 C ASP A 841 6392 6846 6106 -141 -182 215 C ATOM 5959 O ASP A 841 67.955 11.185 172.992 1.00 49.83 O ANISOU 5959 O ASP A 841 6173 6741 6020 -56 -195 271 O ATOM 5960 CB ASP A 841 69.344 13.850 172.489 1.00 55.00 C ANISOU 5960 CB ASP A 841 6834 7507 6555 -332 -239 149 C ATOM 5961 CG ASP A 841 69.426 15.325 172.378 1.00 53.05 C ANISOU 5961 CG ASP A 841 6673 7238 6245 -474 -248 82 C ATOM 5962 OD1 ASP A 841 68.928 16.021 173.254 1.00 52.20 O ANISOU 5962 OD1 ASP A 841 6665 7104 6064 -516 -269 55 O ATOM 5963 OD2 ASP A 841 70.013 15.798 171.404 1.00 53.03 O ANISOU 5963 OD2 ASP A 841 6643 7242 6263 -546 -235 56 O ATOM 5964 N GLU A 842 66.371 12.646 172.534 1.00 46.26 N ANISOU 5964 N GLU A 842 5901 6140 5535 -135 -127 181 N ATOM 5965 CA GLU A 842 65.413 11.726 171.940 1.00 45.06 C ANISOU 5965 CA GLU A 842 5760 5896 5463 -43 -76 208 C ATOM 5966 C GLU A 842 64.921 12.293 170.614 1.00 38.00 C ANISOU 5966 C GLU A 842 4904 4916 4619 -62 -24 153 C ATOM 5967 O GLU A 842 65.048 13.488 170.345 1.00 36.37 O ANISOU 5967 O GLU A 842 4746 4697 4375 -144 -25 99 O ATOM 5968 CB GLU A 842 64.227 11.481 172.886 1.00 48.79 C ANISOU 5968 CB GLU A 842 6308 6331 5900 -8 -59 232 C ATOM 5969 CG GLU A 842 63.661 10.080 172.847 1.00 51.42 C ANISOU 5969 CG GLU A 842 6619 6623 6296 81 -41 301 C ATOM 5970 CD GLU A 842 64.300 9.167 173.873 1.00 53.99 C ANISOU 5970 CD GLU A 842 6896 7022 6594 117 -96 380 C ATOM 5971 OE1 GLU A 842 64.297 9.512 175.071 1.00 54.74 O ANISOU 5971 OE1 GLU A 842 7019 7182 6598 84 -125 393 O ATOM 5972 OE2 GLU A 842 64.812 8.102 173.482 1.00 57.33 O ANISOU 5972 OE2 GLU A 842 7259 7440 7085 184 -113 427 O ATOM 5973 N THR A 843 64.350 11.424 169.783 1.00 37.37 N ANISOU 5973 N THR A 843 4809 4769 4621 11 17 171 N ATOM 5974 CA THR A 843 63.736 11.833 168.523 1.00 34.17 C ANISOU 5974 CA THR A 843 4440 4282 4261 4 66 127 C ATOM 5975 C THR A 843 62.266 12.151 168.765 1.00 33.37 C ANISOU 5975 C THR A 843 4433 4101 4146 21 101 112 C ATOM 5976 O THR A 843 61.467 11.254 169.040 1.00 33.17 O ANISOU 5976 O THR A 843 4409 4046 4146 81 120 150 O ATOM 5977 CB THR A 843 63.876 10.744 167.467 1.00 35.17 C ANISOU 5977 CB THR A 843 4502 4385 4476 71 89 144 C ATOM 5978 OG1 THR A 843 65.264 10.468 167.249 1.00 37.61 O ANISOU 5978 OG1 THR A 843 4711 4786 4792 69 58 152 O ATOM 5979 CG2 THR A 843 63.246 11.202 166.157 1.00 34.84 C ANISOU 5979 CG2 THR A 843 4498 4269 4470 57 136 99 C ATOM 5980 N TYR A 844 61.906 13.420 168.651 1.00 33.30 N ANISOU 5980 N TYR A 844 4502 4057 4094 -32 109 57 N ATOM 5981 CA TYR A 844 60.531 13.863 168.836 1.00 34.60 C ANISOU 5981 CA TYR A 844 4751 4158 4239 -4 143 31 C ATOM 5982 C TYR A 844 59.915 14.231 167.493 1.00 32.95 C ANISOU 5982 C TYR A 844 4571 3869 4078 5 180 -2 C ATOM 5983 O TYR A 844 60.538 14.930 166.690 1.00 37.01 O ANISOU 5983 O TYR A 844 5096 4369 4596 -49 171 -29 O ATOM 5984 CB TYR A 844 60.467 15.055 169.789 1.00 37.45 C ANISOU 5984 CB TYR A 844 5193 4529 4507 -49 120 -13 C ATOM 5985 CG TYR A 844 60.343 14.652 171.231 1.00 37.53 C ANISOU 5985 CG TYR A 844 5199 4606 4457 -31 103 16 C ATOM 5986 CD1 TYR A 844 61.456 14.263 171.968 1.00 38.42 C ANISOU 5986 CD1 TYR A 844 5254 4804 4540 -62 54 53 C ATOM 5987 CD2 TYR A 844 59.111 14.644 171.859 1.00 36.58 C ANISOU 5987 CD2 TYR A 844 5123 4476 4301 18 135 10 C ATOM 5988 CE1 TYR A 844 61.338 13.887 173.287 1.00 37.62 C ANISOU 5988 CE1 TYR A 844 5151 4767 4374 -47 35 86 C ATOM 5989 CE2 TYR A 844 58.986 14.265 173.177 1.00 39.83 C ANISOU 5989 CE2 TYR A 844 5530 4960 4646 28 122 41 C ATOM 5990 CZ TYR A 844 60.101 13.888 173.887 1.00 38.02 C ANISOU 5990 CZ TYR A 844 5254 4806 4387 -6 71 81 C ATOM 5991 OH TYR A 844 59.961 13.512 175.204 1.00 39.33 O ANISOU 5991 OH TYR A 844 5419 5047 4477 2 56 118 O ATOM 5992 N VAL A 845 58.703 13.750 167.248 1.00 31.88 N ANISOU 5992 N VAL A 845 4447 3692 3975 66 218 7 N ATOM 5993 CA VAL A 845 57.923 14.197 166.105 1.00 31.40 C ANISOU 5993 CA VAL A 845 4423 3563 3946 80 249 -26 C ATOM 5994 C VAL A 845 57.382 15.584 166.415 1.00 31.67 C ANISOU 5994 C VAL A 845 4556 3559 3917 70 245 -79 C ATOM 5995 O VAL A 845 56.834 15.823 167.495 1.00 32.00 O ANISOU 5995 O VAL A 845 4633 3623 3904 94 245 -90 O ATOM 5996 CB VAL A 845 56.786 13.206 165.796 1.00 30.97 C ANISOU 5996 CB VAL A 845 4340 3488 3940 143 286 0 C ATOM 5997 CG1 VAL A 845 55.850 13.765 164.745 1.00 30.59 C ANISOU 5997 CG1 VAL A 845 4331 3382 3910 163 313 -35 C ATOM 5998 CG2 VAL A 845 57.341 11.883 165.333 1.00 30.83 C ANISOU 5998 CG2 VAL A 845 4245 3479 3989 155 285 43 C ATOM 5999 N LEU A 846 57.541 16.504 165.473 1.00 31.63 N ANISOU 5999 N LEU A 846 4604 3499 3916 37 240 -113 N ATOM 6000 CA LEU A 846 57.002 17.839 165.652 1.00 32.00 C ANISOU 6000 CA LEU A 846 4763 3487 3910 38 231 -165 C ATOM 6001 C LEU A 846 55.543 17.904 165.230 1.00 33.79 C ANISOU 6001 C LEU A 846 5015 3671 4151 124 265 -181 C ATOM 6002 O LEU A 846 55.060 17.102 164.429 1.00 34.35 O ANISOU 6002 O LEU A 846 5027 3745 4280 156 293 -155 O ATOM 6003 CB LEU A 846 57.791 18.864 164.850 1.00 33.39 C ANISOU 6003 CB LEU A 846 5000 3610 4076 -43 203 -187 C ATOM 6004 CG LEU A 846 59.297 18.944 165.042 1.00 34.24 C ANISOU 6004 CG LEU A 846 5073 3771 4166 -146 167 -174 C ATOM 6005 CD1 LEU A 846 59.777 20.213 164.386 1.00 35.18 C ANISOU 6005 CD1 LEU A 846 5286 3826 4257 -235 139 -200 C ATOM 6006 CD2 LEU A 846 59.664 18.932 166.507 1.00 33.97 C ANISOU 6006 CD2 LEU A 846 5038 3795 4075 -160 139 -179 C ATOM 6007 N GLY A 847 54.892 18.925 165.731 1.00 32.20 N ANISOU 6007 N GLY A 847 4902 3438 3893 164 261 -228 N ATOM 6008 CA GLY A 847 53.524 19.245 165.452 1.00 32.18 C ANISOU 6008 CA GLY A 847 4942 3390 3894 247 282 -255 C ATOM 6009 C GLY A 847 53.546 20.730 165.287 1.00 32.85 C ANISOU 6009 C GLY A 847 5164 3382 3934 242 249 -311 C ATOM 6010 O GLY A 847 54.491 21.336 165.653 1.00 33.29 O ANISOU 6010 O GLY A 847 5279 3411 3958 159 211 -325 O ATOM 6011 N LYS A 848 52.537 21.306 164.688 1.00 33.54 N ANISOU 6011 N LYS A 848 5305 3419 4018 329 258 -340 N ATOM 6012 CA LYS A 848 52.495 22.744 164.535 1.00 38.93 C ANISOU 6012 CA LYS A 848 6138 3994 4659 335 219 -392 C ATOM 6013 C LYS A 848 51.096 23.318 164.600 1.00 41.24 C ANISOU 6013 C LYS A 848 6477 4260 4931 474 233 -434 C ATOM 6014 O LYS A 848 50.171 22.706 164.137 1.00 46.85 O ANISOU 6014 O LYS A 848 7109 5013 5680 539 265 -411 O ATOM 6015 CB LYS A 848 53.298 23.171 163.307 1.00 40.63 C ANISOU 6015 CB LYS A 848 6404 4129 4904 244 189 -367 C ATOM 6016 CG LYS A 848 52.543 23.760 162.153 1.00 38.72 C ANISOU 6016 CG LYS A 848 6186 3832 4695 300 193 -355 C ATOM 6017 CD LYS A 848 53.212 25.021 161.677 1.00 39.70 C ANISOU 6017 CD LYS A 848 6464 3826 4793 247 142 -369 C ATOM 6018 CE LYS A 848 53.822 24.898 160.302 1.00 39.40 C ANISOU 6018 CE LYS A 848 6405 3775 4789 143 135 -315 C ATOM 6019 NZ LYS A 848 52.890 24.537 159.225 1.00 38.07 N ANISOU 6019 NZ LYS A 848 6206 3601 4656 214 153 -291 N ATOM 6020 N ILE A 849 50.958 24.498 165.176 1.00 38.99 N ANISOU 6020 N ILE A 849 6317 3915 4583 522 208 -501 N ATOM 6021 CA ILE A 849 49.676 25.166 165.255 1.00 39.59 C ANISOU 6021 CA ILE A 849 6459 3951 4633 668 211 -554 C ATOM 6022 C ILE A 849 49.702 25.992 164.014 1.00 36.36 C ANISOU 6022 C ILE A 849 6152 3411 4251 666 172 -544 C ATOM 6023 O ILE A 849 50.556 26.778 163.846 1.00 36.66 O ANISOU 6023 O ILE A 849 6318 3336 4274 580 122 -553 O ATOM 6024 CB ILE A 849 49.589 26.052 166.476 1.00 37.09 C ANISOU 6024 CB ILE A 849 6252 3608 4234 727 195 -638 C ATOM 6025 CG1 ILE A 849 49.774 25.211 167.715 1.00 36.97 C ANISOU 6025 CG1 ILE A 849 6130 3738 4178 730 236 -642 C ATOM 6026 CG2 ILE A 849 48.264 26.742 166.532 1.00 38.01 C ANISOU 6026 CG2 ILE A 849 6451 3666 4324 892 190 -699 C ATOM 6027 CD1 ILE A 849 49.877 26.005 168.969 1.00 37.95 C ANISOU 6027 CD1 ILE A 849 6359 3841 4218 710 209 -712 C ATOM 6028 N LYS A 850 48.750 25.790 163.138 1.00 38.46 N ANISOU 6028 N LYS A 850 6362 3695 4554 750 190 -521 N ATOM 6029 CA LYS A 850 48.789 26.429 161.825 1.00 39.91 C ANISOU 6029 CA LYS A 850 6630 3770 4764 740 153 -495 C ATOM 6030 C LYS A 850 48.528 27.925 161.926 1.00 44.30 C ANISOU 6030 C LYS A 850 7380 4178 5274 814 100 -552 C ATOM 6031 O LYS A 850 49.170 28.713 161.229 1.00 43.09 O ANISOU 6031 O LYS A 850 7354 3895 5121 738 50 -534 O ATOM 6032 CB LYS A 850 47.786 25.760 160.881 1.00 40.25 C ANISOU 6032 CB LYS A 850 6562 3881 4850 816 181 -459 C ATOM 6033 N ASP A 851 47.599 28.336 162.784 1.00 46.40 N ANISOU 6033 N ASP A 851 7674 4459 5495 962 109 -622 N ATOM 6034 CA ASP A 851 47.312 29.754 162.956 1.00 49.54 C ANISOU 6034 CA ASP A 851 8269 4707 5848 1055 55 -688 C ATOM 6035 C ASP A 851 46.872 30.007 164.390 1.00 44.68 C ANISOU 6035 C ASP A 851 7673 4136 5166 1155 74 -778 C ATOM 6036 O ASP A 851 45.864 29.453 164.836 1.00 41.42 O ANISOU 6036 O ASP A 851 7135 3861 4741 1276 126 -800 O ATOM 6037 CB ASP A 851 46.243 30.202 161.969 1.00 55.87 C ANISOU 6037 CB ASP A 851 9101 5461 6666 1198 37 -680 C ATOM 6038 CG ASP A 851 45.960 31.693 162.048 1.00 65.19 C ANISOU 6038 CG ASP A 851 10503 6462 7803 1306 -28 -744 C ATOM 6039 OD1 ASP A 851 46.875 32.500 161.807 1.00 74.12 O ANISOU 6039 OD1 ASP A 851 11803 7432 8926 1195 -86 -735 O ATOM 6040 OD2 ASP A 851 44.818 32.067 162.361 1.00 67.10 O ANISOU 6040 OD2 ASP A 851 10753 6724 8018 1503 -22 -803 O ATOM 6041 N ILE A 852 47.633 30.845 165.104 1.00 42.59 N ANISOU 6041 N ILE A 852 7564 3764 4854 1096 32 -832 N ATOM 6042 CA ILE A 852 47.368 31.119 166.513 1.00 42.40 C ANISOU 6042 CA ILE A 852 7572 3781 4756 1173 46 -926 C ATOM 6043 C ILE A 852 46.271 32.143 166.728 1.00 43.68 C ANISOU 6043 C ILE A 852 7855 3869 4873 1386 28 -1018 C ATOM 6044 O ILE A 852 45.916 32.421 167.880 1.00 44.59 O ANISOU 6044 O ILE A 852 7998 4027 4918 1477 45 -1108 O ATOM 6045 CB ILE A 852 48.651 31.604 167.215 1.00 42.59 C ANISOU 6045 CB ILE A 852 7718 3724 4740 1017 2 -954 C ATOM 6046 CG1 ILE A 852 49.116 32.921 166.608 1.00 43.69 C ANISOU 6046 CG1 ILE A 852 8089 3636 4876 976 -81 -971 C ATOM 6047 CG2 ILE A 852 49.743 30.581 167.068 1.00 41.23 C ANISOU 6047 CG2 ILE A 852 7414 3644 4608 826 19 -867 C ATOM 6048 CD1 ILE A 852 50.422 33.417 167.150 1.00 44.20 C ANISOU 6048 CD1 ILE A 852 8272 3619 4904 794 -131 -990 C ATOM 6049 N TYR A 853 45.715 32.710 165.667 1.00 44.10 N ANISOU 6049 N TYR A 853 7979 3818 4959 1476 -6 -1000 N ATOM 6050 CA TYR A 853 44.712 33.753 165.800 1.00 45.74 C ANISOU 6050 CA TYR A 853 8315 3939 5126 1694 -34 -1087 C ATOM 6051 C TYR A 853 43.282 33.231 165.731 1.00 45.74 C ANISOU 6051 C TYR A 853 8145 4107 5126 1889 24 -1096 C ATOM 6052 O TYR A 853 42.348 34.011 165.929 1.00 51.40 O ANISOU 6052 O TYR A 853 8937 4789 5803 2098 10 -1176 O ATOM 6053 CB TYR A 853 44.930 34.823 164.736 1.00 46.56 C ANISOU 6053 CB TYR A 853 8623 3813 5255 1691 -118 -1063 C ATOM 6054 CG TYR A 853 46.335 35.370 164.714 1.00 46.72 C ANISOU 6054 CG TYR A 853 8808 3671 5272 1479 -178 -1044 C ATOM 6055 CD1 TYR A 853 46.791 36.208 165.719 1.00 48.00 C ANISOU 6055 CD1 TYR A 853 9144 3722 5370 1463 -216 -1138 C ATOM 6056 CD2 TYR A 853 47.203 35.053 163.684 1.00 45.71 C ANISOU 6056 CD2 TYR A 853 8660 3512 5198 1290 -196 -937 C ATOM 6057 CE1 TYR A 853 48.065 36.714 165.697 1.00 48.27 C ANISOU 6057 CE1 TYR A 853 9324 3620 5397 1255 -274 -1120 C ATOM 6058 CE2 TYR A 853 48.484 35.550 163.656 1.00 45.99 C ANISOU 6058 CE2 TYR A 853 8829 3421 5223 1087 -248 -917 C ATOM 6059 CZ TYR A 853 48.909 36.381 164.671 1.00 47.27 C ANISOU 6059 CZ TYR A 853 9161 3476 5324 1065 -289 -1007 C ATOM 6060 OH TYR A 853 50.180 36.897 164.670 1.00 47.69 O ANISOU 6060 OH TYR A 853 9346 3412 5362 849 -345 -988 O ATOM 6061 N THR A 854 43.086 31.946 165.468 1.00 44.28 N ANISOU 6061 N THR A 854 7737 4106 4982 1828 86 -1021 N ATOM 6062 CA THR A 854 41.791 31.314 165.663 1.00 44.33 C ANISOU 6062 CA THR A 854 7558 4310 4974 1980 149 -1033 C ATOM 6063 C THR A 854 41.658 30.879 167.118 1.00 44.55 C ANISOU 6063 C THR A 854 7502 4490 4933 1995 210 -1093 C ATOM 6064 O THR A 854 42.649 30.752 167.838 1.00 44.21 O ANISOU 6064 O THR A 854 7502 4426 4870 1857 208 -1099 O ATOM 6065 CB THR A 854 41.633 30.105 164.740 1.00 42.81 C ANISOU 6065 CB THR A 854 7174 4240 4852 1893 184 -926 C ATOM 6066 OG1 THR A 854 42.627 29.133 165.067 1.00 42.08 O ANISOU 6066 OG1 THR A 854 7001 4206 4783 1694 213 -871 O ATOM 6067 CG2 THR A 854 41.798 30.509 163.269 1.00 43.11 C ANISOU 6067 CG2 THR A 854 7292 4139 4947 1868 125 -863 C ATOM 6068 N GLN A 855 40.418 30.662 167.562 1.00 50.34 N ANISOU 6068 N GLN A 855 8109 5393 5623 2162 263 -1137 N ATOM 6069 CA GLN A 855 40.239 30.137 168.912 1.00 52.46 C ANISOU 6069 CA GLN A 855 8278 5835 5819 2165 329 -1181 C ATOM 6070 C GLN A 855 40.830 28.739 169.023 1.00 54.03 C ANISOU 6070 C GLN A 855 8317 6156 6056 1966 372 -1081 C ATOM 6071 O GLN A 855 41.562 28.442 169.970 1.00 58.21 O ANISOU 6071 O GLN A 855 8854 6716 6547 1861 386 -1088 O ATOM 6072 CB GLN A 855 38.767 30.140 169.327 1.00 56.08 C ANISOU 6072 CB GLN A 855 8613 6476 6217 2376 384 -1242 C ATOM 6073 CG GLN A 855 38.422 31.235 170.335 1.00 58.22 C ANISOU 6073 CG GLN A 855 9015 6715 6389 2551 378 -1384 C ATOM 6074 CD GLN A 855 38.943 30.946 171.738 1.00 58.51 C ANISOU 6074 CD GLN A 855 9045 6840 6346 2469 418 -1427 C ATOM 6075 OE1 GLN A 855 39.271 29.819 172.071 1.00 57.98 O ANISOU 6075 OE1 GLN A 855 8834 6908 6287 2316 464 -1350 O ATOM 6076 NE2 GLN A 855 39.033 31.974 172.558 1.00 60.63 N ANISOU 6076 NE2 GLN A 855 9479 7023 6534 2570 395 -1551 N ATOM 6077 N ASP A 856 40.546 27.873 168.048 1.00 44.39 N ANISOU 6077 N ASP A 856 6960 4998 4907 1914 388 -988 N ATOM 6078 CA ASP A 856 41.204 26.573 168.018 1.00 42.72 C ANISOU 6078 CA ASP A 856 6625 4864 4742 1726 417 -892 C ATOM 6079 C ASP A 856 42.716 26.711 168.042 1.00 40.51 C ANISOU 6079 C ASP A 856 6463 4440 4488 1560 371 -868 C ATOM 6080 O ASP A 856 43.405 25.893 168.659 1.00 39.80 O ANISOU 6080 O ASP A 856 6310 4418 4395 1432 393 -828 O ATOM 6081 CB ASP A 856 40.789 25.779 166.783 1.00 42.28 C ANISOU 6081 CB ASP A 856 6447 4852 4767 1691 424 -805 C ATOM 6082 CG ASP A 856 39.390 25.239 166.883 1.00 44.00 C ANISOU 6082 CG ASP A 856 6492 5266 4959 1799 479 -806 C ATOM 6083 OD1 ASP A 856 38.798 25.297 167.980 1.00 43.66 O ANISOU 6083 OD1 ASP A 856 6401 5352 4837 1882 523 -862 O ATOM 6084 OD2 ASP A 856 38.887 24.731 165.860 1.00 48.45 O ANISOU 6084 OD2 ASP A 856 6962 5868 5578 1792 479 -749 O ATOM 6085 N GLY A 857 43.251 27.737 167.385 1.00 40.83 N ANISOU 6085 N GLY A 857 6676 4289 4550 1558 306 -888 N ATOM 6086 CA GLY A 857 44.688 27.935 167.408 1.00 40.39 C ANISOU 6086 CA GLY A 857 6726 4110 4509 1392 261 -868 C ATOM 6087 C GLY A 857 45.192 28.335 168.779 1.00 41.15 C ANISOU 6087 C GLY A 857 6901 4208 4526 1373 258 -939 C ATOM 6088 O GLY A 857 46.247 27.874 169.223 1.00 40.55 O ANISOU 6088 O GLY A 857 6811 4147 4450 1221 252 -906 O ATOM 6089 N TYR A 858 44.441 29.187 169.476 1.00 42.58 N ANISOU 6089 N TYR A 858 7163 4383 4633 1532 259 -1041 N ATOM 6090 CA TYR A 858 44.874 29.644 170.789 1.00 43.49 C ANISOU 6090 CA TYR A 858 7367 4498 4660 1521 253 -1123 C ATOM 6091 C TYR A 858 44.623 28.592 171.860 1.00 43.18 C ANISOU 6091 C TYR A 858 7160 4675 4570 1503 323 -1109 C ATOM 6092 O TYR A 858 45.493 28.357 172.700 1.00 43.06 O ANISOU 6092 O TYR A 858 7158 4687 4517 1386 317 -1108 O ATOM 6093 CB TYR A 858 44.193 30.965 171.147 1.00 45.31 C ANISOU 6093 CB TYR A 858 7759 4632 4823 1706 227 -1249 C ATOM 6094 CG TYR A 858 44.317 31.341 172.612 1.00 46.45 C ANISOU 6094 CG TYR A 858 7969 4823 4859 1735 237 -1351 C ATOM 6095 CD1 TYR A 858 45.446 31.985 173.102 1.00 46.93 C ANISOU 6095 CD1 TYR A 858 8195 4751 4885 1616 178 -1393 C ATOM 6096 CD2 TYR A 858 43.293 31.078 173.501 1.00 47.20 C ANISOU 6096 CD2 TYR A 858 7957 5101 4875 1878 305 -1410 C ATOM 6097 CE1 TYR A 858 45.550 32.326 174.442 1.00 48.06 C ANISOU 6097 CE1 TYR A 858 8399 4941 4920 1640 185 -1492 C ATOM 6098 CE2 TYR A 858 43.393 31.421 174.828 1.00 48.33 C ANISOU 6098 CE2 TYR A 858 8159 5296 4908 1906 317 -1507 C ATOM 6099 CZ TYR A 858 44.511 32.039 175.294 1.00 48.74 C ANISOU 6099 CZ TYR A 858 8380 5211 4929 1790 256 -1550 C ATOM 6100 OH TYR A 858 44.552 32.352 176.630 1.00 49.95 O ANISOU 6100 OH TYR A 858 8587 5430 4963 1823 268 -1652 O ATOM 6101 N ASP A 859 43.458 27.936 171.846 1.00 46.31 N ANISOU 6101 N ASP A 859 7397 5235 4963 1606 387 -1091 N ATOM 6102 CA ASP A 859 43.220 26.865 172.812 1.00 49.10 C ANISOU 6102 CA ASP A 859 7590 5796 5268 1567 453 -1059 C ATOM 6103 C ASP A 859 44.285 25.788 172.715 1.00 47.64 C ANISOU 6103 C ASP A 859 7332 5628 5139 1368 448 -951 C ATOM 6104 O ASP A 859 44.715 25.244 173.735 1.00 48.27 O ANISOU 6104 O ASP A 859 7369 5804 5166 1293 467 -936 O ATOM 6105 CB ASP A 859 41.847 26.221 172.627 1.00 54.05 C ANISOU 6105 CB ASP A 859 8044 6600 5895 1674 519 -1036 C ATOM 6106 CG ASP A 859 40.718 27.197 172.750 1.00 59.35 C ANISOU 6106 CG ASP A 859 8756 7289 6505 1891 530 -1143 C ATOM 6107 OD1 ASP A 859 40.518 27.754 173.843 1.00 65.47 O ANISOU 6107 OD1 ASP A 859 9586 8112 7178 1977 547 -1240 O ATOM 6108 OD2 ASP A 859 40.023 27.398 171.745 1.00 62.36 O ANISOU 6108 OD2 ASP A 859 9113 7642 6939 1983 521 -1132 O ATOM 6109 N ALA A 860 44.704 25.440 171.502 1.00 43.45 N ANISOU 6109 N ALA A 860 6784 5014 4712 1289 422 -873 N ATOM 6110 CA ALA A 860 45.806 24.499 171.376 1.00 39.11 C ANISOU 6110 CA ALA A 860 6177 4467 4215 1115 411 -782 C ATOM 6111 C ALA A 860 47.069 25.063 172.008 1.00 39.41 C ANISOU 6111 C ALA A 860 6339 4420 4215 1017 361 -814 C ATOM 6112 O ALA A 860 47.847 24.331 172.632 1.00 38.99 O ANISOU 6112 O ALA A 860 6230 4432 4151 906 362 -766 O ATOM 6113 CB ALA A 860 46.047 24.154 169.910 1.00 38.03 C ANISOU 6113 CB ALA A 860 6013 4251 4186 1059 392 -710 C ATOM 6114 N PHE A 861 47.273 26.371 171.878 1.00 40.28 N ANISOU 6114 N PHE A 861 6619 4382 4301 1056 311 -893 N ATOM 6115 CA PHE A 861 48.470 26.988 172.421 1.00 40.72 C ANISOU 6115 CA PHE A 861 6802 4351 4318 949 255 -927 C ATOM 6116 C PHE A 861 48.523 26.832 173.935 1.00 41.42 C ANISOU 6116 C PHE A 861 6876 4559 4305 950 276 -973 C ATOM 6117 O PHE A 861 49.569 26.501 174.498 1.00 41.22 O ANISOU 6117 O PHE A 861 6842 4560 4260 820 252 -944 O ATOM 6118 CB PHE A 861 48.520 28.462 172.023 1.00 41.76 C ANISOU 6118 CB PHE A 861 7137 4293 4438 997 197 -1008 C ATOM 6119 CG PHE A 861 49.635 29.217 172.667 1.00 42.53 C ANISOU 6119 CG PHE A 861 7380 4298 4481 887 136 -1058 C ATOM 6120 CD1 PHE A 861 49.468 29.804 173.913 1.00 43.82 C ANISOU 6120 CD1 PHE A 861 7630 4482 4538 945 132 -1162 C ATOM 6121 CD2 PHE A 861 50.851 29.338 172.038 1.00 42.06 C ANISOU 6121 CD2 PHE A 861 7368 4145 4470 720 83 -1006 C ATOM 6122 CE1 PHE A 861 50.489 30.490 174.507 1.00 44.61 C ANISOU 6122 CE1 PHE A 861 7866 4501 4585 833 71 -1211 C ATOM 6123 CE2 PHE A 861 51.877 30.034 172.632 1.00 42.89 C ANISOU 6123 CE2 PHE A 861 7599 4176 4520 604 23 -1051 C ATOM 6124 CZ PHE A 861 51.694 30.608 173.865 1.00 44.15 C ANISOU 6124 CZ PHE A 861 7850 4348 4578 658 15 -1154 C ATOM 6125 N MET A 862 47.396 27.060 174.611 1.00 43.85 N ANISOU 6125 N MET A 862 7171 4951 4539 1100 320 -1043 N ATOM 6126 CA MET A 862 47.390 27.026 176.066 1.00 44.80 C ANISOU 6126 CA MET A 862 7289 5188 4544 1110 341 -1098 C ATOM 6127 C MET A 862 47.526 25.605 176.599 1.00 42.42 C ANISOU 6127 C MET A 862 6813 5065 4240 1024 385 -998 C ATOM 6128 O MET A 862 48.174 25.391 177.625 1.00 42.81 O ANISOU 6128 O MET A 862 6865 5182 4218 947 375 -998 O ATOM 6129 CB MET A 862 46.124 27.682 176.602 1.00 47.58 C ANISOU 6129 CB MET A 862 7671 5595 4812 1303 381 -1207 C ATOM 6130 CG MET A 862 45.998 29.159 176.273 1.00 54.66 C ANISOU 6130 CG MET A 862 8769 6304 5696 1405 329 -1319 C ATOM 6131 SD MET A 862 47.343 30.190 176.901 1.00 55.48 S ANISOU 6131 SD MET A 862 9091 6246 5741 1287 242 -1397 S ATOM 6132 CE MET A 862 47.338 29.751 178.629 1.00 56.53 C ANISOU 6132 CE MET A 862 9162 6582 5733 1279 284 -1444 C ATOM 6133 N LYS A 863 46.913 24.625 175.932 1.00 41.47 N ANISOU 6133 N LYS A 863 6547 5020 4191 1035 430 -910 N ATOM 6134 CA LYS A 863 47.101 23.235 176.331 1.00 40.87 C ANISOU 6134 CA LYS A 863 6322 5083 4124 943 463 -803 C ATOM 6135 C LYS A 863 48.580 22.891 176.415 1.00 40.11 C ANISOU 6135 C LYS A 863 6247 4935 4057 788 408 -746 C ATOM 6136 O LYS A 863 49.031 22.273 177.382 1.00 40.25 O ANISOU 6136 O LYS A 863 6219 5055 4020 721 411 -709 O ATOM 6137 CB LYS A 863 46.399 22.298 175.349 1.00 42.64 C ANISOU 6137 CB LYS A 863 6414 5348 4441 954 501 -717 C ATOM 6138 CG LYS A 863 44.923 22.103 175.594 1.00 45.42 C ANISOU 6138 CG LYS A 863 6671 5841 4746 1073 570 -737 C ATOM 6139 CD LYS A 863 44.416 20.846 174.892 1.00 47.66 C ANISOU 6139 CD LYS A 863 6804 6195 5108 1030 605 -629 C ATOM 6140 CE LYS A 863 44.980 19.593 175.557 1.00 52.72 C ANISOU 6140 CE LYS A 863 7364 6924 5744 903 614 -529 C ATOM 6141 NZ LYS A 863 44.632 18.324 174.869 1.00 52.80 N ANISOU 6141 NZ LYS A 863 7251 6975 5836 843 638 -423 N ATOM 6142 N ILE A 864 49.352 23.290 175.403 1.00 42.00 N ANISOU 6142 N ILE A 864 6552 5027 4379 729 358 -736 N ATOM 6143 CA ILE A 864 50.790 23.046 175.400 1.00 40.59 C ANISOU 6143 CA ILE A 864 6385 4810 4228 585 305 -687 C ATOM 6144 C ILE A 864 51.489 23.978 176.376 1.00 43.23 C ANISOU 6144 C ILE A 864 6843 5117 4465 546 257 -769 C ATOM 6145 O ILE A 864 52.526 23.631 176.949 1.00 44.42 O ANISOU 6145 O ILE A 864 6976 5310 4592 437 223 -734 O ATOM 6146 CB ILE A 864 51.350 23.212 173.975 1.00 40.87 C ANISOU 6146 CB ILE A 864 6444 4714 4371 531 272 -653 C ATOM 6147 CG1 ILE A 864 50.558 22.368 172.976 1.00 40.42 C ANISOU 6147 CG1 ILE A 864 6276 4680 4401 578 317 -587 C ATOM 6148 CG2 ILE A 864 52.814 22.835 173.927 1.00 40.57 C ANISOU 6148 CG2 ILE A 864 6385 4667 4361 386 225 -597 C ATOM 6149 CD1 ILE A 864 50.860 22.707 171.532 1.00 39.90 C ANISOU 6149 CD1 ILE A 864 6247 4489 4424 552 291 -571 C ATOM 6150 N TYR A 865 50.933 25.167 176.584 1.00 41.20 N ANISOU 6150 N TYR A 865 6717 4789 4149 637 251 -880 N ATOM 6151 CA TYR A 865 51.584 26.173 177.408 1.00 42.38 C ANISOU 6151 CA TYR A 865 7011 4885 4208 597 197 -972 C ATOM 6152 C TYR A 865 51.491 25.810 178.879 1.00 43.12 C ANISOU 6152 C TYR A 865 7065 5135 4185 603 219 -994 C ATOM 6153 O TYR A 865 52.491 25.837 179.603 1.00 43.50 O ANISOU 6153 O TYR A 865 7141 5209 4178 495 174 -995 O ATOM 6154 CB TYR A 865 50.937 27.528 177.143 1.00 43.43 C ANISOU 6154 CB TYR A 865 7307 4878 4316 710 182 -1089 C ATOM 6155 CG TYR A 865 51.475 28.671 177.947 1.00 44.87 C ANISOU 6155 CG TYR A 865 7666 4979 4402 680 124 -1200 C ATOM 6156 CD1 TYR A 865 52.605 29.358 177.541 1.00 45.06 C ANISOU 6156 CD1 TYR A 865 7810 4859 4450 545 46 -1207 C ATOM 6157 CD2 TYR A 865 50.835 29.086 179.098 1.00 46.17 C ANISOU 6157 CD2 TYR A 865 7882 5213 4447 784 148 -1304 C ATOM 6158 CE1 TYR A 865 53.092 30.412 178.266 1.00 46.50 C ANISOU 6158 CE1 TYR A 865 8165 4958 4544 504 -13 -1312 C ATOM 6159 CE2 TYR A 865 51.312 30.137 179.829 1.00 47.60 C ANISOU 6159 CE2 TYR A 865 8237 5312 4537 758 92 -1417 C ATOM 6160 CZ TYR A 865 52.441 30.798 179.412 1.00 47.76 C ANISOU 6160 CZ TYR A 865 8383 5178 4587 614 9 -1420 C ATOM 6161 OH TYR A 865 52.920 31.849 180.153 1.00 49.32 O ANISOU 6161 OH TYR A 865 8762 5287 4690 573 -53 -1535 O ATOM 6162 N LYS A 866 50.290 25.473 179.339 1.00 45.75 N ANISOU 6162 N LYS A 866 7327 5586 4470 726 289 -1010 N ATOM 6163 CA LYS A 866 50.117 25.112 180.733 1.00 45.58 C ANISOU 6163 CA LYS A 866 7264 5730 4325 733 318 -1026 C ATOM 6164 C LYS A 866 50.849 23.826 181.069 1.00 44.81 C ANISOU 6164 C LYS A 866 7038 5742 4244 610 313 -897 C ATOM 6165 O LYS A 866 51.262 23.631 182.213 1.00 44.56 O ANISOU 6165 O LYS A 866 7003 5816 4112 561 302 -898 O ATOM 6166 CB LYS A 866 48.633 24.988 181.048 1.00 48.84 C ANISOU 6166 CB LYS A 866 7611 6261 4684 885 400 -1062 C ATOM 6167 CG LYS A 866 47.894 26.287 180.857 1.00 54.13 C ANISOU 6167 CG LYS A 866 8410 6833 5322 1033 400 -1200 C ATOM 6168 CD LYS A 866 46.637 26.330 181.699 1.00 58.16 C ANISOU 6168 CD LYS A 866 8871 7508 5721 1180 476 -1269 C ATOM 6169 CE LYS A 866 45.499 25.582 181.025 1.00 59.61 C ANISOU 6169 CE LYS A 866 8897 7786 5966 1258 545 -1200 C ATOM 6170 NZ LYS A 866 44.971 26.306 179.832 1.00 62.57 N ANISOU 6170 NZ LYS A 866 9330 8016 6428 1366 532 -1242 N ATOM 6171 N LYS A 867 51.047 22.957 180.092 1.00 45.32 N ANISOU 6171 N LYS A 867 7005 5781 4431 563 318 -787 N ATOM 6172 CA LYS A 867 51.672 21.673 180.351 1.00 45.71 C ANISOU 6172 CA LYS A 867 6937 5925 4506 467 313 -663 C ATOM 6173 C LYS A 867 53.197 21.757 180.338 1.00 45.35 C ANISOU 6173 C LYS A 867 6925 5824 4480 339 235 -637 C ATOM 6174 O LYS A 867 53.852 21.222 181.234 1.00 48.29 O ANISOU 6174 O LYS A 867 7259 6294 4794 271 210 -591 O ATOM 6175 CB LYS A 867 51.183 20.648 179.327 1.00 46.47 C ANISOU 6175 CB LYS A 867 6916 6019 4720 479 352 -563 C ATOM 6176 CG LYS A 867 52.002 19.377 179.314 1.00 47.80 C ANISOU 6176 CG LYS A 867 6987 6232 4943 382 332 -436 C ATOM 6177 CD LYS A 867 51.459 18.413 178.300 1.00 48.40 C ANISOU 6177 CD LYS A 867 6965 6293 5131 398 369 -353 C ATOM 6178 CE LYS A 867 52.191 17.072 178.353 1.00 49.03 C ANISOU 6178 CE LYS A 867 6956 6411 5261 319 349 -229 C ATOM 6179 NZ LYS A 867 51.724 16.167 177.258 1.00 50.82 N ANISOU 6179 NZ LYS A 867 7115 6581 5615 322 369 -165 N ATOM 6180 N ASP A 868 53.769 22.440 179.345 1.00 40.90 N ANISOU 6180 N ASP A 868 6432 5117 3993 302 194 -665 N ATOM 6181 CA ASP A 868 55.215 22.510 179.169 1.00 40.76 C ANISOU 6181 CA ASP A 868 6428 5059 4002 173 123 -636 C ATOM 6182 C ASP A 868 55.556 23.518 178.076 1.00 40.64 C ANISOU 6182 C ASP A 868 6513 4880 4049 144 88 -686 C ATOM 6183 O ASP A 868 55.629 23.167 176.897 1.00 39.67 O ANISOU 6183 O ASP A 868 6340 4698 4033 135 98 -630 O ATOM 6184 CB ASP A 868 55.777 21.124 178.834 1.00 39.78 C ANISOU 6184 CB ASP A 868 6157 5000 3957 120 124 -505 C ATOM 6185 CG ASP A 868 57.296 21.079 178.834 1.00 39.84 C ANISOU 6185 CG ASP A 868 6150 5011 3976 -3 53 -471 C ATOM 6186 OD1 ASP A 868 57.935 22.140 178.969 1.00 40.56 O ANISOU 6186 OD1 ASP A 868 6343 5045 4021 -68 1 -544 O ATOM 6187 OD2 ASP A 868 57.855 19.974 178.677 1.00 39.26 O ANISOU 6187 OD2 ASP A 868 5963 4997 3957 -35 46 -371 O ATOM 6188 N LYS A 869 55.778 24.772 178.469 1.00 41.74 N ANISOU 6188 N LYS A 869 6802 4942 4115 124 45 -790 N ATOM 6189 CA LYS A 869 56.142 25.814 177.518 1.00 44.20 C ANISOU 6189 CA LYS A 869 7234 5087 4473 81 4 -835 C ATOM 6190 C LYS A 869 57.364 25.436 176.707 1.00 41.17 C ANISOU 6190 C LYS A 869 6785 4690 4169 -55 -35 -753 C ATOM 6191 O LYS A 869 57.512 25.895 175.571 1.00 40.85 O ANISOU 6191 O LYS A 869 6790 4534 4198 -83 -48 -747 O ATOM 6192 CB LYS A 869 56.422 27.132 178.245 1.00 48.32 C ANISOU 6192 CB LYS A 869 7935 5532 4893 48 -52 -954 C ATOM 6193 CG LYS A 869 55.377 27.539 179.262 1.00 52.05 C ANISOU 6193 CG LYS A 869 8473 6041 5261 180 -18 -1052 C ATOM 6194 CD LYS A 869 55.756 28.792 180.041 1.00 55.03 C ANISOU 6194 CD LYS A 869 9037 6341 5532 140 -79 -1177 C ATOM 6195 CE LYS A 869 57.262 28.976 180.139 1.00 59.57 C ANISOU 6195 CE LYS A 869 9634 6903 6097 -56 -161 -1153 C ATOM 6196 NZ LYS A 869 57.655 30.280 180.746 1.00 66.17 N ANISOU 6196 NZ LYS A 869 10671 7635 6836 -116 -230 -1278 N ATOM 6197 N SER A 870 58.263 24.631 177.273 1.00 41.05 N ANISOU 6197 N SER A 870 6664 4796 4137 -137 -57 -689 N ATOM 6198 CA SER A 870 59.477 24.257 176.561 1.00 40.56 C ANISOU 6198 CA SER A 870 6525 4744 4141 -257 -94 -617 C ATOM 6199 C SER A 870 59.197 23.376 175.351 1.00 39.24 C ANISOU 6199 C SER A 870 6249 4567 4095 -212 -47 -536 C ATOM 6200 O SER A 870 60.114 23.141 174.559 1.00 38.86 O ANISOU 6200 O SER A 870 6141 4517 4106 -296 -69 -485 O ATOM 6201 CB SER A 870 60.456 23.549 177.504 1.00 40.87 C ANISOU 6201 CB SER A 870 6467 4930 4132 -332 -131 -567 C ATOM 6202 OG SER A 870 60.019 22.248 177.853 1.00 40.22 O ANISOU 6202 OG SER A 870 6257 4956 4070 -254 -86 -489 O ATOM 6203 N LYS A 871 57.970 22.872 175.206 1.00 38.66 N ANISOU 6203 N LYS A 871 6142 4498 4050 -86 16 -524 N ATOM 6204 CA LYS A 871 57.612 22.124 174.002 1.00 37.53 C ANISOU 6204 CA LYS A 871 5912 4331 4015 -46 58 -460 C ATOM 6205 C LYS A 871 57.669 23.011 172.768 1.00 37.41 C ANISOU 6205 C LYS A 871 5981 4183 4051 -71 45 -488 C ATOM 6206 O LYS A 871 58.109 22.569 171.707 1.00 36.70 O ANISOU 6206 O LYS A 871 5826 4080 4040 -109 49 -434 O ATOM 6207 CB LYS A 871 56.228 21.500 174.153 1.00 37.13 C ANISOU 6207 CB LYS A 871 5816 4319 3974 81 123 -448 C ATOM 6208 CG LYS A 871 56.215 20.249 175.003 1.00 36.98 C ANISOU 6208 CG LYS A 871 5683 4432 3937 91 142 -378 C ATOM 6209 CD LYS A 871 54.813 19.895 175.461 1.00 37.04 C ANISOU 6209 CD LYS A 871 5667 4492 3914 196 203 -383 C ATOM 6210 CE LYS A 871 53.947 19.392 174.325 1.00 36.18 C ANISOU 6210 CE LYS A 871 5503 4345 3897 256 250 -349 C ATOM 6211 NZ LYS A 871 54.409 18.066 173.889 1.00 35.40 N ANISOU 6211 NZ LYS A 871 5293 4280 3879 217 253 -250 N ATOM 6212 N PHE A 872 57.254 24.269 172.889 1.00 38.22 N ANISOU 6212 N PHE A 872 6236 4184 4103 -50 26 -574 N ATOM 6213 CA PHE A 872 57.356 25.190 171.765 1.00 38.32 C ANISOU 6213 CA PHE A 872 6349 4057 4154 -84 3 -594 C ATOM 6214 C PHE A 872 58.804 25.360 171.343 1.00 38.47 C ANISOU 6214 C PHE A 872 6358 4073 4186 -248 -47 -561 C ATOM 6215 O PHE A 872 59.687 25.588 172.171 1.00 39.20 O ANISOU 6215 O PHE A 872 6464 4212 4217 -343 -93 -578 O ATOM 6216 CB PHE A 872 56.759 26.546 172.120 1.00 39.45 C ANISOU 6216 CB PHE A 872 6676 4080 4232 -33 -21 -695 C ATOM 6217 CG PHE A 872 55.281 26.518 172.311 1.00 39.44 C ANISOU 6217 CG PHE A 872 6683 4080 4220 140 31 -734 C ATOM 6218 CD1 PHE A 872 54.449 26.149 171.275 1.00 38.64 C ANISOU 6218 CD1 PHE A 872 6528 3958 4194 225 73 -696 C ATOM 6219 CD2 PHE A 872 54.722 26.868 173.519 1.00 40.34 C ANISOU 6219 CD2 PHE A 872 6853 4230 4243 217 38 -810 C ATOM 6220 CE1 PHE A 872 53.090 26.121 171.447 1.00 38.74 C ANISOU 6220 CE1 PHE A 872 6533 3994 4194 381 119 -730 C ATOM 6221 CE2 PHE A 872 53.370 26.843 173.696 1.00 40.46 C ANISOU 6221 CE2 PHE A 872 6860 4271 4243 377 90 -847 C ATOM 6222 CZ PHE A 872 52.547 26.466 172.654 1.00 39.67 C ANISOU 6222 CZ PHE A 872 6696 4156 4221 459 130 -805 C ATOM 6223 N LEU A 873 59.050 25.245 170.045 1.00 37.87 N ANISOU 6223 N LEU A 873 6249 3956 4184 -284 -40 -513 N ATOM 6224 CA LEU A 873 60.407 25.381 169.542 1.00 38.08 C ANISOU 6224 CA LEU A 873 6248 4001 4221 -441 -80 -478 C ATOM 6225 C LEU A 873 60.921 26.803 169.661 1.00 39.34 C ANISOU 6225 C LEU A 873 6577 4053 4319 -554 -143 -535 C ATOM 6226 O LEU A 873 62.140 27.001 169.700 1.00 39.89 O ANISOU 6226 O LEU A 873 6626 4166 4365 -707 -187 -518 O ATOM 6227 CB LEU A 873 60.479 24.918 168.089 1.00 37.24 C ANISOU 6227 CB LEU A 873 6066 3884 4198 -447 -50 -418 C ATOM 6228 CG LEU A 873 60.830 23.450 167.878 1.00 36.30 C ANISOU 6228 CG LEU A 873 5758 3896 4138 -424 -13 -349 C ATOM 6229 CD1 LEU A 873 59.895 22.564 168.647 1.00 35.79 C ANISOU 6229 CD1 LEU A 873 5634 3885 4078 -294 26 -344 C ATOM 6230 CD2 LEU A 873 60.767 23.114 166.417 1.00 35.60 C ANISOU 6230 CD2 LEU A 873 5620 3784 4122 -419 18 -308 C ATOM 6231 N MET A 874 60.024 27.788 169.725 1.00 39.94 N ANISOU 6231 N MET A 874 6819 3989 4366 -483 -152 -602 N ATOM 6232 CA MET A 874 60.458 29.170 169.847 1.00 41.31 C ANISOU 6232 CA MET A 874 7181 4033 4481 -588 -219 -659 C ATOM 6233 C MET A 874 60.929 29.455 171.256 1.00 42.28 C ANISOU 6233 C MET A 874 7346 4204 4515 -642 -260 -719 C ATOM 6234 O MET A 874 61.880 30.215 171.459 1.00 44.97 O ANISOU 6234 O MET A 874 7772 4509 4805 -801 -325 -740 O ATOM 6235 CB MET A 874 59.337 30.131 169.471 1.00 41.80 C ANISOU 6235 CB MET A 874 7419 3920 4542 -475 -221 -715 C ATOM 6236 CG MET A 874 59.559 31.510 170.005 1.00 45.10 C ANISOU 6236 CG MET A 874 8056 4194 4884 -542 -292 -798 C ATOM 6237 SD MET A 874 58.420 32.633 169.254 1.00 45.56 S ANISOU 6237 SD MET A 874 8324 4031 4957 -417 -305 -844 S ATOM 6238 CE MET A 874 56.993 32.305 170.256 1.00 46.93 C ANISOU 6238 CE MET A 874 8473 4258 5101 -172 -250 -922 C ATOM 6239 N TYR A 875 60.253 28.868 172.240 1.00 45.81 N ANISOU 6239 N TYR A 875 7737 4736 4932 -517 -225 -745 N ATOM 6240 CA TYR A 875 60.722 28.971 173.610 1.00 45.96 C ANISOU 6240 CA TYR A 875 7772 4832 4859 -566 -261 -793 C ATOM 6241 C TYR A 875 62.192 28.602 173.704 1.00 43.76 C ANISOU 6241 C TYR A 875 7389 4666 4573 -741 -303 -738 C ATOM 6242 O TYR A 875 62.959 29.253 174.416 1.00 45.65 O ANISOU 6242 O TYR A 875 7702 4909 4734 -864 -367 -783 O ATOM 6243 CB TYR A 875 59.883 28.078 174.524 1.00 45.74 C ANISOU 6243 CB TYR A 875 7648 4922 4808 -419 -206 -796 C ATOM 6244 CG TYR A 875 60.205 28.273 175.976 1.00 46.02 C ANISOU 6244 CG TYR A 875 7719 5032 4733 -453 -240 -854 C ATOM 6245 CD1 TYR A 875 61.192 27.528 176.596 1.00 46.71 C ANISOU 6245 CD1 TYR A 875 7680 5273 4795 -546 -264 -801 C ATOM 6246 CD2 TYR A 875 59.533 29.218 176.725 1.00 47.43 C ANISOU 6246 CD2 TYR A 875 8062 5131 4828 -385 -253 -966 C ATOM 6247 CE1 TYR A 875 61.500 27.723 177.935 1.00 46.99 C ANISOU 6247 CE1 TYR A 875 7750 5385 4720 -582 -301 -853 C ATOM 6248 CE2 TYR A 875 59.832 29.414 178.057 1.00 47.98 C ANISOU 6248 CE2 TYR A 875 8170 5275 4787 -418 -285 -1027 C ATOM 6249 CZ TYR A 875 60.810 28.666 178.656 1.00 47.49 C ANISOU 6249 CZ TYR A 875 7979 5369 4697 -522 -310 -968 C ATOM 6250 OH TYR A 875 61.087 28.869 179.984 1.00 49.44 O ANISOU 6250 OH TYR A 875 8265 5695 4824 -556 -346 -1027 O ATOM 6251 N ARG A 876 62.608 27.588 172.960 1.00 41.93 N ANISOU 6251 N ARG A 876 6985 4529 4418 -754 -272 -644 N ATOM 6252 CA ARG A 876 63.982 27.128 173.033 1.00 42.09 C ANISOU 6252 CA ARG A 876 6879 4681 4433 -896 -307 -589 C ATOM 6253 C ARG A 876 64.908 27.844 172.066 1.00 42.63 C ANISOU 6253 C ARG A 876 6985 4696 4515 -1062 -347 -572 C ATOM 6254 O ARG A 876 66.076 28.062 172.400 1.00 43.49 O ANISOU 6254 O ARG A 876 7062 4885 4578 -1219 -402 -566 O ATOM 6255 CB ARG A 876 64.041 25.623 172.780 1.00 40.86 C ANISOU 6255 CB ARG A 876 6515 4662 4347 -818 -257 -502 C ATOM 6256 CG ARG A 876 63.372 24.835 173.879 1.00 40.57 C ANISOU 6256 CG ARG A 876 6426 4707 4281 -695 -229 -503 C ATOM 6257 CD ARG A 876 63.582 23.350 173.729 1.00 39.62 C ANISOU 6257 CD ARG A 876 6117 4712 4223 -638 -195 -412 C ATOM 6258 NE ARG A 876 62.708 22.611 174.631 1.00 39.32 N ANISOU 6258 NE ARG A 876 6048 4728 4164 -515 -160 -404 N ATOM 6259 CZ ARG A 876 62.936 21.370 175.042 1.00 38.95 C ANISOU 6259 CZ ARG A 876 5865 4799 4134 -475 -150 -331 C ATOM 6260 NH1 ARG A 876 64.014 20.723 174.636 1.00 38.82 N ANISOU 6260 NH1 ARG A 876 5727 4862 4162 -530 -173 -269 N ATOM 6261 NH2 ARG A 876 62.084 20.778 175.862 1.00 38.82 N ANISOU 6261 NH2 ARG A 876 5836 4824 4089 -378 -118 -320 N ATOM 6262 N HIS A 877 64.430 28.217 170.878 1.00 42.23 N ANISOU 6262 N HIS A 877 6999 4525 4523 -1041 -322 -559 N ATOM 6263 CA HIS A 877 65.291 28.806 169.862 1.00 42.73 C ANISOU 6263 CA HIS A 877 7086 4551 4599 -1204 -352 -527 C ATOM 6264 C HIS A 877 65.055 30.291 169.668 1.00 43.92 C ANISOU 6264 C HIS A 877 7476 4503 4708 -1276 -401 -585 C ATOM 6265 O HIS A 877 65.776 30.922 168.890 1.00 44.59 O ANISOU 6265 O HIS A 877 7609 4545 4790 -1436 -434 -557 O ATOM 6266 CB HIS A 877 65.121 28.070 168.534 1.00 41.55 C ANISOU 6266 CB HIS A 877 6820 4426 4539 -1151 -293 -455 C ATOM 6267 CG HIS A 877 65.458 26.617 168.611 1.00 40.56 C ANISOU 6267 CG HIS A 877 6473 4478 4459 -1089 -251 -397 C ATOM 6268 ND1 HIS A 877 66.538 26.139 169.316 1.00 40.99 N ANISOU 6268 ND1 HIS A 877 6403 4690 4480 -1168 -282 -378 N ATOM 6269 CD2 HIS A 877 64.831 25.532 168.106 1.00 39.29 C ANISOU 6269 CD2 HIS A 877 6200 4355 4373 -949 -187 -357 C ATOM 6270 CE1 HIS A 877 66.574 24.822 169.229 1.00 40.04 C ANISOU 6270 CE1 HIS A 877 6110 4690 4415 -1071 -239 -326 C ATOM 6271 NE2 HIS A 877 65.547 24.429 168.501 1.00 39.00 N ANISOU 6271 NE2 HIS A 877 5987 4483 4349 -943 -181 -314 N ATOM 6272 N ASP A 878 64.091 30.870 170.365 1.00 44.39 N ANISOU 6272 N ASP A 878 7690 4446 4732 -1165 -408 -664 N ATOM 6273 CA ASP A 878 63.916 32.314 170.322 1.00 46.08 C ANISOU 6273 CA ASP A 878 8151 4457 4898 -1227 -466 -730 C ATOM 6274 C ASP A 878 63.306 32.807 171.629 1.00 46.57 C ANISOU 6274 C ASP A 878 8343 4464 4886 -1138 -489 -836 C ATOM 6275 O ASP A 878 62.215 33.388 171.626 1.00 46.84 O ANISOU 6275 O ASP A 878 8526 4353 4918 -995 -480 -897 O ATOM 6276 CB ASP A 878 63.022 32.684 169.156 1.00 47.45 C ANISOU 6276 CB ASP A 878 8418 4480 5132 -1133 -440 -712 C ATOM 6277 CG ASP A 878 63.050 34.158 168.831 1.00 50.11 C ANISOU 6277 CG ASP A 878 9011 4598 5432 -1226 -509 -753 C ATOM 6278 OD1 ASP A 878 63.911 34.858 169.390 1.00 55.85 O ANISOU 6278 OD1 ASP A 878 9830 5298 6091 -1397 -578 -787 O ATOM 6279 OD2 ASP A 878 62.230 34.615 167.994 1.00 49.90 O ANISOU 6279 OD2 ASP A 878 9093 4423 5442 -1133 -500 -747 O ATOM 6280 N PRO A 879 63.971 32.598 172.777 1.00 47.10 N ANISOU 6280 N PRO A 879 8358 4654 4884 -1210 -520 -865 N ATOM 6281 CA PRO A 879 63.329 32.985 174.059 1.00 47.90 C ANISOU 6281 CA PRO A 879 8573 4723 4905 -1110 -533 -970 C ATOM 6282 C PRO A 879 62.999 34.459 174.148 1.00 49.51 C ANISOU 6282 C PRO A 879 9056 4699 5056 -1130 -592 -1070 C ATOM 6283 O PRO A 879 62.079 34.816 174.884 1.00 51.04 O ANISOU 6283 O PRO A 879 9360 4829 5203 -981 -582 -1163 O ATOM 6284 CB PRO A 879 64.370 32.591 175.116 1.00 48.40 C ANISOU 6284 CB PRO A 879 8534 4958 4896 -1235 -572 -970 C ATOM 6285 CG PRO A 879 65.646 32.447 174.367 1.00 48.39 C ANISOU 6285 CG PRO A 879 8431 5030 4927 -1433 -603 -886 C ATOM 6286 CD PRO A 879 65.309 31.968 173.007 1.00 47.09 C ANISOU 6286 CD PRO A 879 8183 4841 4868 -1371 -543 -804 C ATOM 6287 N GLN A 880 63.687 35.317 173.388 1.00 55.54 N ANISOU 6287 N GLN A 880 9939 5337 5826 -1305 -651 -1051 N ATOM 6288 CA GLN A 880 63.365 36.739 173.402 1.00 58.02 C ANISOU 6288 CA GLN A 880 10543 5407 6097 -1324 -714 -1140 C ATOM 6289 C GLN A 880 61.940 36.977 172.914 1.00 56.42 C ANISOU 6289 C GLN A 880 10437 5059 5940 -1088 -670 -1170 C ATOM 6290 O GLN A 880 61.145 37.644 173.584 1.00 59.09 O ANISOU 6290 O GLN A 880 10944 5281 6228 -955 -684 -1280 O ATOM 6291 CB GLN A 880 64.365 37.519 172.556 1.00 60.12 C ANISOU 6291 CB GLN A 880 10907 5571 6366 -1569 -783 -1091 C ATOM 6292 CG GLN A 880 65.813 37.256 172.930 1.00 59.05 C ANISOU 6292 CG GLN A 880 10647 5604 6186 -1811 -825 -1052 C ATOM 6293 CD GLN A 880 66.805 38.054 172.109 1.00 59.42 C ANISOU 6293 CD GLN A 880 10785 5567 6226 -2072 -891 -1001 C ATOM 6294 OE1 GLN A 880 66.683 39.266 171.977 1.00 62.34 O ANISOU 6294 OE1 GLN A 880 11415 5709 6562 -2143 -957 -1052 O ATOM 6295 NE2 GLN A 880 67.801 37.372 171.560 1.00 57.66 N ANISOU 6295 NE2 GLN A 880 10348 5531 6030 -2216 -875 -900 N ATOM 6296 N THR A 881 61.595 36.431 171.748 1.00 57.39 N ANISOU 6296 N THR A 881 10452 5199 6155 -1026 -617 -1077 N ATOM 6297 CA THR A 881 60.231 36.576 171.254 1.00 54.27 C ANISOU 6297 CA THR A 881 10123 4694 5804 -799 -575 -1098 C ATOM 6298 C THR A 881 59.233 35.983 172.234 1.00 50.41 C ANISOU 6298 C THR A 881 9554 4310 5290 -582 -515 -1163 C ATOM 6299 O THR A 881 58.199 36.592 172.529 1.00 50.25 O ANISOU 6299 O THR A 881 9673 4175 5244 -407 -513 -1251 O ATOM 6300 CB THR A 881 60.076 35.903 169.893 1.00 54.41 C ANISOU 6300 CB THR A 881 10001 4754 5918 -778 -524 -983 C ATOM 6301 OG1 THR A 881 61.119 36.334 169.017 1.00 57.50 O ANISOU 6301 OG1 THR A 881 10434 5091 6321 -999 -572 -912 O ATOM 6302 CG2 THR A 881 58.760 36.279 169.288 1.00 55.97 C ANISOU 6302 CG2 THR A 881 10299 4815 6153 -571 -503 -1003 C ATOM 6303 N PHE A 882 59.527 34.796 172.752 1.00 48.33 N ANISOU 6303 N PHE A 882 9065 4267 5030 -589 -466 -1119 N ATOM 6304 CA PHE A 882 58.566 34.141 173.622 1.00 47.83 C ANISOU 6304 CA PHE A 882 8911 4320 4942 -397 -403 -1163 C ATOM 6305 C PHE A 882 58.365 34.936 174.903 1.00 49.43 C ANISOU 6305 C PHE A 882 9275 4473 5035 -358 -440 -1295 C ATOM 6306 O PHE A 882 57.227 35.214 175.299 1.00 49.88 O ANISOU 6306 O PHE A 882 9401 4490 5062 -163 -410 -1376 O ATOM 6307 CB PHE A 882 59.017 32.717 173.926 1.00 46.44 C ANISOU 6307 CB PHE A 882 8480 4378 4789 -431 -355 -1079 C ATOM 6308 CG PHE A 882 57.924 31.850 174.455 1.00 45.64 C ANISOU 6308 CG PHE A 882 8257 4399 4687 -238 -277 -1085 C ATOM 6309 CD1 PHE A 882 57.574 31.894 175.792 1.00 46.41 C ANISOU 6309 CD1 PHE A 882 8377 4566 4689 -169 -270 -1166 C ATOM 6310 CD2 PHE A 882 57.230 30.996 173.611 1.00 44.24 C ANISOU 6310 CD2 PHE A 882 7941 4271 4598 -135 -210 -1010 C ATOM 6311 CE1 PHE A 882 56.558 31.104 176.277 1.00 45.80 C ANISOU 6311 CE1 PHE A 882 8186 4614 4604 -6 -196 -1165 C ATOM 6312 CE2 PHE A 882 56.216 30.204 174.093 1.00 43.64 C ANISOU 6312 CE2 PHE A 882 7754 4311 4518 23 -141 -1011 C ATOM 6313 CZ PHE A 882 55.881 30.256 175.432 1.00 44.44 C ANISOU 6313 CZ PHE A 882 7874 4488 4521 85 -132 -1085 C ATOM 6314 N GLU A 883 59.463 35.344 175.543 1.00 50.45 N ANISOU 6314 N GLU A 883 9465 4606 5095 -544 -509 -1324 N ATOM 6315 CA GLU A 883 59.389 35.981 176.849 1.00 62.63 C ANISOU 6315 CA GLU A 883 11146 6129 6523 -525 -545 -1452 C ATOM 6316 C GLU A 883 59.039 37.459 176.757 1.00 53.80 C ANISOU 6316 C GLU A 883 10321 4752 5367 -497 -608 -1563 C ATOM 6317 O GLU A 883 58.382 37.987 177.658 1.00 54.98 O ANISOU 6317 O GLU A 883 10598 4857 5437 -368 -612 -1689 O ATOM 6318 CB GLU A 883 60.716 35.791 177.588 1.00 64.24 C ANISOU 6318 CB GLU A 883 11291 6454 6663 -740 -599 -1438 C ATOM 6319 CG GLU A 883 60.735 36.346 179.000 1.00 67.42 C ANISOU 6319 CG GLU A 883 11817 6864 6935 -739 -640 -1568 C ATOM 6320 CD GLU A 883 59.947 35.497 179.982 1.00 68.56 C ANISOU 6320 CD GLU A 883 11830 7190 7031 -565 -566 -1593 C ATOM 6321 OE1 GLU A 883 59.387 34.457 179.568 1.00 70.76 O ANISOU 6321 OE1 GLU A 883 11921 7583 7382 -452 -486 -1504 O ATOM 6322 OE2 GLU A 883 59.891 35.873 181.172 1.00 71.36 O ANISOU 6322 OE2 GLU A 883 12271 7574 7267 -548 -589 -1700 O ATOM 6323 N LYS A 884 59.448 38.140 175.690 1.00 54.23 N ANISOU 6323 N LYS A 884 10495 4634 5475 -609 -659 -1520 N ATOM 6324 CA LYS A 884 59.282 39.584 175.602 1.00 56.19 C ANISOU 6324 CA LYS A 884 11048 4614 5686 -615 -736 -1616 C ATOM 6325 C LYS A 884 58.228 40.027 174.600 1.00 56.14 C ANISOU 6325 C LYS A 884 11144 4438 5749 -436 -718 -1608 C ATOM 6326 O LYS A 884 58.026 41.230 174.438 1.00 57.84 O ANISOU 6326 O LYS A 884 11625 4409 5941 -421 -786 -1680 O ATOM 6327 CB LYS A 884 60.621 40.259 175.273 1.00 59.10 C ANISOU 6327 CB LYS A 884 11529 4886 6040 -910 -830 -1582 C ATOM 6328 CG LYS A 884 61.820 39.545 175.865 1.00 59.04 C ANISOU 6328 CG LYS A 884 11339 5098 5996 -1111 -840 -1534 C ATOM 6329 CD LYS A 884 63.022 40.456 175.938 1.00 60.95 C ANISOU 6329 CD LYS A 884 11737 5238 6182 -1391 -946 -1551 C ATOM 6330 CE LYS A 884 63.609 40.726 174.571 1.00 61.01 C ANISOU 6330 CE LYS A 884 11762 5156 6262 -1556 -972 -1439 C ATOM 6331 NZ LYS A 884 65.061 41.033 174.689 1.00 62.54 N ANISOU 6331 NZ LYS A 884 11958 5397 6407 -1871 -1050 -1408 N ATOM 6332 N VAL A 885 57.545 39.101 173.931 1.00 55.53 N ANISOU 6332 N VAL A 885 10872 4475 5752 -300 -635 -1524 N ATOM 6333 CA VAL A 885 56.467 39.479 173.025 1.00 54.31 C ANISOU 6333 CA VAL A 885 10798 4181 5655 -114 -619 -1519 C ATOM 6334 C VAL A 885 55.196 38.729 173.393 1.00 53.41 C ANISOU 6334 C VAL A 885 10532 4214 5548 147 -526 -1548 C ATOM 6335 O VAL A 885 54.151 39.338 173.640 1.00 54.45 O ANISOU 6335 O VAL A 885 10787 4250 5651 358 -523 -1645 O ATOM 6336 CB VAL A 885 56.844 39.215 171.559 1.00 53.23 C ANISOU 6336 CB VAL A 885 10592 4019 5614 -220 -618 -1378 C ATOM 6337 CG1 VAL A 885 55.677 39.529 170.673 1.00 53.23 C ANISOU 6337 CG1 VAL A 885 10658 3898 5667 -15 -601 -1370 C ATOM 6338 CG2 VAL A 885 58.049 40.037 171.158 1.00 54.35 C ANISOU 6338 CG2 VAL A 885 10892 4018 5741 -484 -708 -1347 C ATOM 6339 N ILE A 886 55.282 37.403 173.464 1.00 51.62 N ANISOU 6339 N ILE A 886 10036 4223 5355 134 -453 -1466 N ATOM 6340 CA ILE A 886 54.073 36.602 173.596 1.00 50.67 C ANISOU 6340 CA ILE A 886 9754 4246 5254 355 -363 -1466 C ATOM 6341 C ILE A 886 53.589 36.532 175.042 1.00 51.43 C ANISOU 6341 C ILE A 886 9841 4451 5249 469 -333 -1576 C ATOM 6342 O ILE A 886 52.381 36.586 175.297 1.00 51.79 O ANISOU 6342 O ILE A 886 9881 4523 5274 691 -285 -1641 O ATOM 6343 CB ILE A 886 54.318 35.217 172.987 1.00 48.58 C ANISOU 6343 CB ILE A 886 9225 4165 5069 293 -301 -1328 C ATOM 6344 CG1 ILE A 886 54.446 35.384 171.477 1.00 48.03 C ANISOU 6344 CG1 ILE A 886 9177 3981 5090 242 -320 -1238 C ATOM 6345 CG2 ILE A 886 53.212 34.251 173.358 1.00 47.68 C ANISOU 6345 CG2 ILE A 886 8928 4230 4960 478 -210 -1325 C ATOM 6346 CD1 ILE A 886 54.198 34.157 170.704 1.00 46.18 C ANISOU 6346 CD1 ILE A 886 8714 3894 4939 266 -251 -1128 C ATOM 6347 N GLU A 887 54.500 36.422 176.014 1.00 51.80 N ANISOU 6347 N GLU A 887 9881 4575 5226 322 -359 -1602 N ATOM 6348 CA GLU A 887 54.077 36.416 177.415 1.00 52.70 C ANISOU 6348 CA GLU A 887 10000 4794 5229 421 -334 -1712 C ATOM 6349 C GLU A 887