HEADER NUCLEAR PROTEIN 21-JUN-06 2IVX
TITLE CRYSTAL STRUCTURE OF HUMAN CYCLIN T2 AT 1.8 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-T2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: RESIDUES 7-263;
COMPND 5 SYNONYM: HUMAN CYCLIN T2, CYCT2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_VARIANT: R3;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR: PNIC28-BSA4
KEYWDS TRANSCRIPTION REGULATION, CELL DIVISION, PHOSPHORYLATION, NUCLEAR
KEYWDS 2 PROTEIN, CYCLIN, CELL CYCLE, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.E.DEBRECZENI,A.N.BULLOCK,O.FEDOROV,P.SAVITSKY,G.BERRIDGE,S.DAS,
AUTHOR 2 A.C.W.PIKE,A.TURNBULL,E.UGOCHUKWU,E.PAPAGRIGORIOU,F.GORREC,
AUTHOR 3 M.SUNDSTROM,A.EDWARDS,C.ARROWSMITH,J.WEIGELT,F.VON DELFT,S.KNAPP
REVDAT 7 08-MAY-19 2IVX 1 REMARK
REVDAT 6 28-FEB-18 2IVX 1 SOURCE JRNL
REVDAT 5 24-JAN-18 2IVX 1 TITLE AUTHOR
REVDAT 4 13-JUL-11 2IVX 1 VERSN
REVDAT 3 24-FEB-09 2IVX 1 VERSN
REVDAT 2 01-JUL-08 2IVX 1 VERSN AUTHOR JRNL
REVDAT 1 19-JUL-06 2IVX 0
JRNL AUTH S.BAUMLI,G.LOLLI,E.D.LOWE,S.TROIANI,L.RUSCONI,A.N.BULLOCK,
JRNL AUTH 2 J.E.DEBRECZENI,S.KNAPP,L.N.JOHNSON
JRNL TITL THE STRUCTURE OF P-TEFB (CDK9/CYCLIN T1), ITS COMPLEX WITH
JRNL TITL 2 FLAVOPIRIDOL AND REGULATION BY PHOSPHORYLATION.
JRNL REF EMBO J. V. 27 1907 2008
JRNL REFN ESSN 1460-2075
JRNL PMID 18566585
JRNL DOI 10.1038/EMBOJ.2008.121
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.76
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 51982
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.191
REMARK 3 FREE R VALUE : 0.223
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1702
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3502
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 116
REMARK 3 BIN FREE R VALUE : 0.3490
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4089
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 327
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.61
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.27000
REMARK 3 B22 (A**2) : 0.36000
REMARK 3 B33 (A**2) : 0.30000
REMARK 3 B12 (A**2) : 0.28000
REMARK 3 B13 (A**2) : 0.54000
REMARK 3 B23 (A**2) : 0.23000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.126
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.119
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.082
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.022
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.945
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.928
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4241 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2811 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5767 ; 1.131 ; 1.935
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6880 ; 0.903 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 521 ; 4.751 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 189 ;35.817 ;24.074
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 737 ;11.902 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;13.779 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 676 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4627 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 843 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 933 ; 0.214 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2778 ; 0.171 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2111 ; 0.172 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1885 ; 0.084 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 197 ; 0.133 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 20 ; 0.135 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 62 ; 0.252 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 26 ; 0.151 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2699 ; 0.673 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4204 ; 0.954 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1809 ; 1.677 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1557 ; 2.467 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 7 A 150
REMARK 3 ORIGIN FOR THE GROUP (A): -13.8337 29.5995 55.2825
REMARK 3 T TENSOR
REMARK 3 T11: -0.1134 T22: -0.0976
REMARK 3 T33: -0.1586 T12: -0.0216
REMARK 3 T13: 0.0037 T23: 0.0248
REMARK 3 L TENSOR
REMARK 3 L11: 2.0564 L22: 2.4670
REMARK 3 L33: 2.4529 L12: -0.3399
REMARK 3 L13: -0.0234 L23: 0.2800
REMARK 3 S TENSOR
REMARK 3 S11: -0.0465 S12: 0.0893 S13: 0.1699
REMARK 3 S21: -0.2493 S22: 0.0139 S23: -0.1877
REMARK 3 S31: -0.0908 S32: 0.1469 S33: 0.0326
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 151 A 262
REMARK 3 ORIGIN FOR THE GROUP (A): -22.5238 14.0905 73.4968
REMARK 3 T TENSOR
REMARK 3 T11: -0.1160 T22: -0.0966
REMARK 3 T33: -0.1298 T12: 0.0055
REMARK 3 T13: -0.0120 T23: 0.0183
REMARK 3 L TENSOR
REMARK 3 L11: 2.6403 L22: 3.2177
REMARK 3 L33: 1.7487 L12: 1.7257
REMARK 3 L13: -1.2715 L23: -1.3678
REMARK 3 S TENSOR
REMARK 3 S11: 0.1008 S12: -0.2169 S13: -0.0053
REMARK 3 S21: 0.1522 S22: -0.1330 S23: -0.0858
REMARK 3 S31: -0.0045 S32: 0.0330 S33: 0.0322
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 9 B 150
REMARK 3 ORIGIN FOR THE GROUP (A): 8.2312 23.4484 33.8842
REMARK 3 T TENSOR
REMARK 3 T11: -0.1264 T22: -0.0808
REMARK 3 T33: -0.1494 T12: 0.0238
REMARK 3 T13: 0.0113 T23: -0.0075
REMARK 3 L TENSOR
REMARK 3 L11: 2.1343 L22: 2.5397
REMARK 3 L33: 2.0888 L12: 0.1054
REMARK 3 L13: 0.0476 L23: -0.3430
REMARK 3 S TENSOR
REMARK 3 S11: -0.0790 S12: -0.1621 S13: 0.0016
REMARK 3 S21: 0.2351 S22: 0.0438 S23: 0.2652
REMARK 3 S31: -0.0361 S32: -0.1685 S33: 0.0352
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 151 B 263
REMARK 3 ORIGIN FOR THE GROUP (A): 16.5896 8.0431 15.5345
REMARK 3 T TENSOR
REMARK 3 T11: -0.1089 T22: -0.1033
REMARK 3 T33: -0.0871 T12: -0.0139
REMARK 3 T13: -0.0188 T23: -0.0342
REMARK 3 L TENSOR
REMARK 3 L11: 2.7256 L22: 3.3578
REMARK 3 L33: 1.7359 L12: -1.7432
REMARK 3 L13: -1.1478 L23: 1.3059
REMARK 3 S TENSOR
REMARK 3 S11: 0.1060 S12: 0.2370 S13: -0.1055
REMARK 3 S21: -0.1934 S22: -0.1457 S23: 0.1900
REMARK 3 S31: 0.0025 S32: -0.0713 S33: 0.0396
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 2IVX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-JUN-06.
REMARK 100 THE DEPOSITION ID IS D_1290029172.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAR-06
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X10SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
REMARK 200 MONOCHROMATOR : SI 111
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 53530
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 41.860
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 200 DATA REDUNDANCY : 3.570
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.67
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 5.360
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXCD, SHELXD, SHELXE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NA-FORMATE, 0.1M BIS-TRIS-PROPANE
REMARK 280 PH 8.5, 20%PEG3350, 10% ETHYLENE GLYCOL, 150 NL SITTING DROP,
REMARK 280 VAPOR DIFFUSION, SITTING DROP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PQS
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 400
REMARK 400 COMPOUND
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLN 130 TO ARG
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, GLN 130 TO ARG
REMARK 400
REMARK 400 REGULATORY SUBUNIT OF THE CYCLIN-DEPENDENT KINASE PAIR
REMARK 400 (CDK9/CYCLIN T) COMPLEX, ALSO CALLED POSITIVE TRANSCRIPTION
REMARK 400 ELONGATION FACTOR B (P-TEFB), WHICH IS PROPOSED TO FACILITATE THE
REMARK 400 TRANSITION FROM ABORTIVE TO PRODUCTION ELONGATION BY
REMARK 400 PHOSPHORYLATING THE CTD (CARBOXY-TERMINAL DOMAIN) OF THE LARGE
REMARK 400 SUBUNIT OF RNA POLYMERASE II (RNAP II).
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 ALA A 263
REMARK 465 ALA B 7
REMARK 465 SER B 8
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 15 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 16 CG CD OE1 OE2
REMARK 470 GLU A 19 CD OE1 OE2
REMARK 470 GLU A 95 CG CD OE1 OE2
REMARK 470 LYS A 99 CE NZ
REMARK 470 LYS A 121 CE NZ
REMARK 470 ASP A 123 CG OD1 OD2
REMARK 470 GLN A 127 CG CD OE1 NE2
REMARK 470 ILE A 134 CD1
REMARK 470 LYS A 205 CE NZ
REMARK 470 ASN A 208 OD1 ND2
REMARK 470 GLU A 210 CD OE1 OE2
REMARK 470 LYS A 246 CD CE NZ
REMARK 470 ARG A 250 CZ NH1 NH2
REMARK 470 LYS A 252 CE NZ
REMARK 470 ARG B 15 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 16 CD OE1 OE2
REMARK 470 LYS B 76 CE NZ
REMARK 470 LYS B 121 CD CE NZ
REMARK 470 ASP B 123 CG OD1 OD2
REMARK 470 ARG B 130 CD NE CZ NH1 NH2
REMARK 470 LYS B 167 CE NZ
REMARK 470 LYS B 191 CD CE NZ
REMARK 470 ASN B 208 OD1 ND2
REMARK 470 GLU B 210 CD OE1 OE2
REMARK 470 ARG B 250 CZ NH1 NH2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 THR A 247 68.03 -110.27
REMARK 500 THR B 247 69.91 -110.64
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1265
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1264
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1265
DBREF 2IVX A 7 263 UNP O60583 CCNT2_HUMAN 7 263
DBREF 2IVX B 7 263 UNP O60583 CCNT2_HUMAN 7 263
SEQADV 2IVX ARG A 130 UNP O60583 GLN 130 ENGINEERED MUTATION
SEQADV 2IVX ARG B 130 UNP O60583 GLN 130 ENGINEERED MUTATION
SEQRES 1 A 257 ALA SER SER ARG TRP PHE PHE THR ARG GLU GLN LEU GLU
SEQRES 2 A 257 ASN THR PRO SER ARG ARG CYS GLY VAL GLU ALA ASP LYS
SEQRES 3 A 257 GLU LEU SER CYS ARG GLN GLN ALA ALA ASN LEU ILE GLN
SEQRES 4 A 257 GLU MET GLY GLN ARG LEU ASN VAL SER GLN LEU THR ILE
SEQRES 5 A 257 ASN THR ALA ILE VAL TYR MET HIS ARG PHE TYR MET HIS
SEQRES 6 A 257 HIS SER PHE THR LYS PHE ASN LYS ASN ILE ILE SER SER
SEQRES 7 A 257 THR ALA LEU PHE LEU ALA ALA LYS VAL GLU GLU GLN ALA
SEQRES 8 A 257 ARG LYS LEU GLU HIS VAL ILE LYS VAL ALA HIS ALA CYS
SEQRES 9 A 257 LEU HIS PRO LEU GLU PRO LEU LEU ASP THR LYS CYS ASP
SEQRES 10 A 257 ALA TYR LEU GLN GLN THR ARG GLU LEU VAL ILE LEU GLU
SEQRES 11 A 257 THR ILE MET LEU GLN THR LEU GLY PHE GLU ILE THR ILE
SEQRES 12 A 257 GLU HIS PRO HIS THR ASP VAL VAL LYS CYS THR GLN LEU
SEQRES 13 A 257 VAL ARG ALA SER LYS ASP LEU ALA GLN THR SER TYR PHE
SEQRES 14 A 257 MET ALA THR ASN SER LEU HIS LEU THR THR PHE CYS LEU
SEQRES 15 A 257 GLN TYR LYS PRO THR VAL ILE ALA CYS VAL CYS ILE HIS
SEQRES 16 A 257 LEU ALA CYS LYS TRP SER ASN TRP GLU ILE PRO VAL SER
SEQRES 17 A 257 THR ASP GLY LYS HIS TRP TRP GLU TYR VAL ASP PRO THR
SEQRES 18 A 257 VAL THR LEU GLU LEU LEU ASP GLU LEU THR HIS GLU PHE
SEQRES 19 A 257 LEU GLN ILE LEU GLU LYS THR PRO ASN ARG LEU LYS LYS
SEQRES 20 A 257 ILE ARG ASN TRP ARG ALA ASN GLN ALA ALA
SEQRES 1 B 257 ALA SER SER ARG TRP PHE PHE THR ARG GLU GLN LEU GLU
SEQRES 2 B 257 ASN THR PRO SER ARG ARG CYS GLY VAL GLU ALA ASP LYS
SEQRES 3 B 257 GLU LEU SER CYS ARG GLN GLN ALA ALA ASN LEU ILE GLN
SEQRES 4 B 257 GLU MET GLY GLN ARG LEU ASN VAL SER GLN LEU THR ILE
SEQRES 5 B 257 ASN THR ALA ILE VAL TYR MET HIS ARG PHE TYR MET HIS
SEQRES 6 B 257 HIS SER PHE THR LYS PHE ASN LYS ASN ILE ILE SER SER
SEQRES 7 B 257 THR ALA LEU PHE LEU ALA ALA LYS VAL GLU GLU GLN ALA
SEQRES 8 B 257 ARG LYS LEU GLU HIS VAL ILE LYS VAL ALA HIS ALA CYS
SEQRES 9 B 257 LEU HIS PRO LEU GLU PRO LEU LEU ASP THR LYS CYS ASP
SEQRES 10 B 257 ALA TYR LEU GLN GLN THR ARG GLU LEU VAL ILE LEU GLU
SEQRES 11 B 257 THR ILE MET LEU GLN THR LEU GLY PHE GLU ILE THR ILE
SEQRES 12 B 257 GLU HIS PRO HIS THR ASP VAL VAL LYS CYS THR GLN LEU
SEQRES 13 B 257 VAL ARG ALA SER LYS ASP LEU ALA GLN THR SER TYR PHE
SEQRES 14 B 257 MET ALA THR ASN SER LEU HIS LEU THR THR PHE CYS LEU
SEQRES 15 B 257 GLN TYR LYS PRO THR VAL ILE ALA CYS VAL CYS ILE HIS
SEQRES 16 B 257 LEU ALA CYS LYS TRP SER ASN TRP GLU ILE PRO VAL SER
SEQRES 17 B 257 THR ASP GLY LYS HIS TRP TRP GLU TYR VAL ASP PRO THR
SEQRES 18 B 257 VAL THR LEU GLU LEU LEU ASP GLU LEU THR HIS GLU PHE
SEQRES 19 B 257 LEU GLN ILE LEU GLU LYS THR PRO ASN ARG LEU LYS LYS
SEQRES 20 B 257 ILE ARG ASN TRP ARG ALA ASN GLN ALA ALA
HET EDO A1263 4
HET EDO A1264 4
HET EDO A1265 4
HET EDO A1266 4
HET EDO B1264 4
HET EDO B1265 4
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 6(C2 H6 O2)
FORMUL 9 HOH *327(H2 O)
HELIX 1 1 SER A 8 PHE A 12 5 5
HELIX 2 2 THR A 14 ASN A 20 1 7
HELIX 3 3 THR A 21 CYS A 26 1 6
HELIX 4 4 GLU A 29 LEU A 51 1 23
HELIX 5 5 SER A 54 TYR A 69 1 16
HELIX 6 6 ASN A 78 GLU A 94 1 17
HELIX 7 7 LYS A 99 HIS A 112 1 14
HELIX 8 8 CYS A 122 LEU A 143 1 22
HELIX 9 9 HIS A 151 VAL A 163 1 13
HELIX 10 10 SER A 166 THR A 184 1 19
HELIX 11 11 THR A 185 GLN A 189 5 5
HELIX 12 12 LYS A 191 ASN A 208 1 18
HELIX 13 13 HIS A 219 VAL A 224 5 6
HELIX 14 14 THR A 229 LYS A 246 1 18
HELIX 15 15 THR A 247 ALA A 262 1 16
HELIX 16 16 THR B 14 ASN B 20 1 7
HELIX 17 17 SER B 23 GLY B 27 5 5
HELIX 18 18 GLU B 29 ASN B 52 1 24
HELIX 19 19 SER B 54 TYR B 69 1 16
HELIX 20 20 ASN B 78 GLU B 94 1 17
HELIX 21 21 LYS B 99 HIS B 112 1 14
HELIX 22 22 CYS B 122 LEU B 143 1 22
HELIX 23 23 HIS B 151 VAL B 163 1 13
HELIX 24 24 SER B 166 THR B 184 1 19
HELIX 25 25 THR B 185 GLN B 189 5 5
HELIX 26 26 LYS B 191 ASN B 208 1 18
HELIX 27 27 HIS B 219 VAL B 224 5 6
HELIX 28 28 THR B 229 LYS B 246 1 18
HELIX 29 29 THR B 247 ALA B 263 1 17
SITE 1 AC1 6 HIS A 201 CYS A 204 TRP A 209 ILE A 211
SITE 2 AC1 6 TRP A 220 HOH A2155
SITE 1 AC2 7 ARG A 67 GLU A 150 CYS A 187 PRO A 192
SITE 2 AC2 7 HOH A2001 HOH A2103 HOH A2156
SITE 1 AC3 4 PHE A 74 THR A 75 LYS A 76 ASN A 78
SITE 1 AC4 4 LYS A 32 CYS A 36 PHE A 74 THR A 75
SITE 1 AC5 6 HIS B 201 CYS B 204 TRP B 209 ILE B 211
SITE 2 AC5 6 TRP B 220 HOH B2171
SITE 1 AC6 2 CYS B 36 THR B 75
CRYST1 43.032 58.636 65.634 110.63 102.41 90.12 P 1 2
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 0.023239 0.000049 0.005503 0.00000
SCALE2 0.000000 0.017054 0.006607 0.00000
SCALE3 0.000000 0.000000 0.016730 0.00000
MTRIX1 1 -0.999910 -0.009380 -0.010040 -4.80372 1
MTRIX2 1 -0.009360 0.999950 -0.002800 -6.16668 1
MTRIX3 1 0.010070 -0.002710 -0.999950 89.48531 1
(ATOM LINES ARE NOT SHOWN.)
END
