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| Title: | | RNA POLYMERASE II ELONGATION COMPLEX WITH UTP, UPDATED 11/2006 | |
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| Molecular Description: |
DNA-directed RNA polymerase II largest subunit (E.C.2.7.7.6)/DNA-directed RNA polymerase II 140 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerase II 45 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerases I
II
and III 27 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerases I
II
and III 23 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerases I
II
and III 14.5 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerase II 14.2 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerases I
II
and III 8.3 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerase II 13.6 kDa polypeptide (E.C.2.7.7.6)/DNA-directed RNA polymerases I
II
and III 7.7 kDa polypeptide (E.C.2.7.7.6)/DNA/RNA |
 |
| Structural Features: | A DOUBLE HELIX, OVERHANGING BASES, NICKED |
|
| Nucleic Acid Sequence: |
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|
| Protein Sequence: |
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| Primary Citation: | Wang, D., Bushnell, D.A., Westover, K.D., Kaplan, C.D., Kornberg, R.D.
Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis
Cell(Cambridge,Mass.)
, 127,
pp. 941 - 954, 2006.
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| Experimental Information: | X-RAY DIFFRACTION |
|
| Space Group: |
C
1
2
1
|
|
| Cell Constants: |
| a = 169.647 | b = 222.338 | c = 194.316 | (Ångstroms) |
 = 90.00 |  = 101.67 |  = 90.00 | (degrees) |
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| Refinement: | The structure was refined using the REFMAC 5.2.0019 program.
The R value is
27.0
for 37247 reflections
in the resolution range 40.00 to
4.30 Ångstroms
. |
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