HEADER TRANSCRIPTION/PROTEIN BINDING/INHIBITOR 09-MAY-10 3MY1
TITLE STRUCTURE OF CDK9/CYCLINT1 IN COMPLEX WITH DRB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CELL DIVISION PROTEIN KINASE 9;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 2-330;
COMPND 5 SYNONYM: CYCLIN-DEPENDENT KINASE 9, SERINE/THREONINE-PROTEIN KINASE
COMPND 6 PITALRE, CELL DIVISION CYCLE 2-LIKE PROTEIN KINASE 4, C-2K;
COMPND 7 EC: 2.7.11.22, 2.7.11.23;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: CYCLIN-T1;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: UNP RESIDUES 2-259;
COMPND 13 SYNONYM: CYCLIN-T, CYCT1;
COMPND 14 ENGINEERED: YES;
COMPND 15 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CDC2L4, CDK9;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULO VIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PVL1392;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: CCNT1;
SOURCE 16 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: SF9;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULO VIRUS;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PVL1392
KEYWDS CDK-CYCLIN COMPLEX, PHOSPHORYLATED, TRANSCRIPTION-PROTEIN BINDING-
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.BAUMLI,L.N.JOHNSON
REVDAT 3 01-NOV-23 3MY1 1 REMARK SEQADV LINK
REVDAT 2 29-JUN-11 3MY1 1 JRNL HEADER
REVDAT 1 29-SEP-10 3MY1 0
JRNL AUTH S.BAUMLI,J.A.ENDICOTT,L.N.JOHNSON
JRNL TITL HALOGEN BONDS FORM THE BASIS FOR SELECTIVE P-TEFB INHIBITION
JRNL TITL 2 BY DRB
JRNL REF CHEM.BIOL. V. 17 931 2010
JRNL REFN ISSN 1074-5521
JRNL PMID 20851342
JRNL DOI 10.1016/J.CHEMBIOL.2010.07.012
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.6.1_357)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.48
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.110
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.4
REMARK 3 NUMBER OF REFLECTIONS : 27344
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.175
REMARK 3 R VALUE (WORKING SET) : 0.173
REMARK 3 FREE R VALUE : 0.214
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020
REMARK 3 FREE R VALUE TEST SET COUNT : 2747
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.4800 - 7.5822 0.96 2501 131 0.1459 0.1661
REMARK 3 2 7.5822 - 6.0257 0.99 2597 149 0.1514 0.2132
REMARK 3 3 6.0257 - 5.2661 0.99 2589 123 0.1475 0.1653
REMARK 3 4 5.2661 - 4.7856 1.00 2607 155 0.1325 0.1911
REMARK 3 5 4.7856 - 4.4432 1.00 2601 144 0.1365 0.1752
REMARK 3 6 4.4432 - 4.1815 1.00 2637 118 0.1369 0.1896
REMARK 3 7 4.1815 - 3.9723 1.00 2591 160 0.1437 0.1867
REMARK 3 8 3.9723 - 3.7996 1.00 2609 124 0.1630 0.2601
REMARK 3 9 3.7996 - 3.6534 1.00 2557 139 0.1644 0.1614
REMARK 3 10 3.6534 - 3.5274 1.00 2585 162 0.1633 0.2359
REMARK 3 11 3.5274 - 3.4172 1.00 2621 135 0.1753 0.2218
REMARK 3 12 3.4172 - 3.3196 1.00 2624 130 0.1903 0.2310
REMARK 3 13 3.3196 - 3.2322 1.00 2640 110 0.1932 0.2883
REMARK 3 14 3.2322 - 3.1534 1.00 2593 159 0.2106 0.2638
REMARK 3 15 3.1534 - 3.0818 1.00 2546 140 0.2038 0.2661
REMARK 3 16 3.0818 - 3.0162 1.00 2664 118 0.2155 0.2408
REMARK 3 17 3.0162 - 2.9559 0.99 2652 145 0.2270 0.2779
REMARK 3 18 2.9559 - 2.9001 0.99 2547 126 0.2491 0.2579
REMARK 3 19 2.9001 - 2.8484 1.00 2587 150 0.2708 0.2759
REMARK 3 20 2.8484 - 2.8001 0.99 2593 129 0.2933 0.3261
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : 0.31
REMARK 3 B_SOL : 60.82
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.410
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.460
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 84.37
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -9.59270
REMARK 3 B22 (A**2) : -9.59270
REMARK 3 B33 (A**2) : 19.18540
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.008 4763
REMARK 3 ANGLE : 1.158 6452
REMARK 3 CHIRALITY : 0.071 720
REMARK 3 PLANARITY : 0.005 811
REMARK 3 DIHEDRAL : 16.852 1766
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 6:108)
REMARK 3 ORIGIN FOR THE GROUP (A): 47.8812 -11.6093 -20.9891
REMARK 3 T TENSOR
REMARK 3 T11: 0.4936 T22: 0.7714
REMARK 3 T33: 0.5524 T12: 0.0807
REMARK 3 T13: 0.0091 T23: -0.0784
REMARK 3 L TENSOR
REMARK 3 L11: 1.4386 L22: 1.4466
REMARK 3 L33: 0.7395 L12: 0.4110
REMARK 3 L13: -0.7768 L23: 0.3674
REMARK 3 S TENSOR
REMARK 3 S11: 0.0270 S12: 0.3235 S13: -0.4744
REMARK 3 S21: -0.1542 S22: 0.0909 S23: -0.2726
REMARK 3 S31: 0.2322 S32: 0.4755 S33: -0.1493
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND (RESSEQ 109:327)
REMARK 3 ORIGIN FOR THE GROUP (A): 48.1316 -20.4164 6.1543
REMARK 3 T TENSOR
REMARK 3 T11: 1.0560 T22: 0.5046
REMARK 3 T33: 0.8551 T12: -0.1620
REMARK 3 T13: -0.2375 T23: 0.1975
REMARK 3 L TENSOR
REMARK 3 L11: 1.8665 L22: 0.9444
REMARK 3 L33: 1.9365 L12: -0.7991
REMARK 3 L13: -0.5398 L23: 0.1644
REMARK 3 S TENSOR
REMARK 3 S11: 0.2772 S12: -0.1673 S13: -0.9310
REMARK 3 S21: 0.7661 S22: -0.2429 S23: 0.0655
REMARK 3 S31: 0.9806 S32: 0.0354 S33: -0.1103
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 21.4659 3.8125 -19.9075
REMARK 3 T TENSOR
REMARK 3 T11: 0.2952 T22: 0.4580
REMARK 3 T33: 0.3896 T12: -0.0408
REMARK 3 T13: -0.0782 T23: -0.1010
REMARK 3 L TENSOR
REMARK 3 L11: 1.9738 L22: 1.3583
REMARK 3 L33: 1.8426 L12: -0.5654
REMARK 3 L13: -0.4748 L23: 0.2254
REMARK 3 S TENSOR
REMARK 3 S11: 0.0729 S12: 0.2131 S13: 0.3520
REMARK 3 S21: -0.0039 S22: 0.0437 S23: -0.1048
REMARK 3 S31: -0.1414 S32: 0.0162 S33: -0.0643
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3MY1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-10.
REMARK 100 THE DEPOSITION ID IS D_1000059136.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 27-SEP-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00550
REMARK 200 MONOCHROMATOR : SINGLE SILICON (111)
REMARK 200 MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27472
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 38.490
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 5.600
REMARK 200 R MERGE (I) : 0.06600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 5.70
REMARK 200 R MERGE FOR SHELL (I) : 0.59700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: RIGID BODY REFINEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRY 3BLH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 70.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.23
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG 1000, 100MM SODIUM/POTASSIUM
REMARK 280 PHOSPHATE AT PH 6.2, 500MM NACL, 2MM TCEP AS A RESERVOIR
REMARK 280 SOLUTION, EVAPORATION, TEMPERATURE 277K, PH 6.5
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z
REMARK 290 3555 -X+Y,-X,Z
REMARK 290 4555 X+2/3,Y+1/3,Z+1/3
REMARK 290 5555 -Y+2/3,X-Y+1/3,Z+1/3
REMARK 290 6555 -X+Y+2/3,-X+1/3,Z+1/3
REMARK 290 7555 X+1/3,Y+2/3,Z+2/3
REMARK 290 8555 -Y+1/3,X-Y+2/3,Z+2/3
REMARK 290 9555 -X+Y+1/3,-X+2/3,Z+2/3
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 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 86.89450
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 50.16856
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 33.07367
REMARK 290 SMTRY1 5 -0.500000 -0.866025 0.000000 86.89450
REMARK 290 SMTRY2 5 0.866025 -0.500000 0.000000 50.16856
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 33.07367
REMARK 290 SMTRY1 6 -0.500000 0.866025 0.000000 86.89450
REMARK 290 SMTRY2 6 -0.866025 -0.500000 0.000000 50.16856
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.07367
REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 100.33713
REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 66.14733
REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 100.33713
REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 66.14733
REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 100.33713
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 66.14733
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1770 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 GLY A 0
REMARK 465 PRO A 1
REMARK 465 ALA A 2
REMARK 465 LYS A 3
REMARK 465 GLN A 4
REMARK 465 TYR A 5
REMARK 465 ALA A 89
REMARK 465 SER A 90
REMARK 465 PRO A 91
REMARK 465 TYR A 92
REMARK 465 ASN A 93
REMARK 465 ARG A 94
REMARK 465 CYS A 95
REMARK 465 LEU A 328
REMARK 465 SER A 329
REMARK 465 THR A 330
REMARK 465 GLY B 0
REMARK 465 PRO B 1
REMARK 465 GLU B 2
REMARK 465 GLY B 3
REMARK 465 GLU B 4
REMARK 465 ARG B 5
REMARK 465 LYS B 6
REMARK 465 ASN B 7
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 CYS A 10 70.32 -152.85
REMARK 500 SER A 17 -9.77 -56.88
REMARK 500 LEU A 22 -53.00 -126.59
REMARK 500 GLN A 27 178.04 -56.45
REMARK 500 GLU A 32 74.56 64.48
REMARK 500 ARG A 39 2.34 -67.17
REMARK 500 LEU A 51 -75.47 -40.05
REMARK 500 GLU A 53 -74.24 -41.92
REMARK 500 ASN A 54 -69.83 -99.90
REMARK 500 GLU A 55 82.43 52.69
REMARK 500 ASP A 149 42.30 -166.51
REMARK 500 LYS A 151 139.51 -173.01
REMARK 500 ASP A 167 82.27 55.85
REMARK 500 LYS A 178 -168.30 -114.30
REMARK 500 VAL A 190 131.12 70.44
REMARK 500 THR A 191 152.21 -41.78
REMARK 500 ASP A 205 68.90 -114.42
REMARK 500 PRO A 208 -35.40 -37.23
REMARK 500 ARG A 225 10.16 51.18
REMARK 500 LEU A 244 -34.78 -144.72
REMARK 500 TYR A 262 -81.34 -59.58
REMARK 500 LEU A 265 18.30 -151.64
REMARK 500 ARG A 273 106.23 -53.82
REMARK 500 LYS A 274 53.01 -117.54
REMARK 500 ALA A 301 0.26 -67.40
REMARK 500 LYS A 325 -12.74 -146.31
REMARK 500 HIS B 113 67.72 -150.30
REMARK 500 GLN B 115 -62.02 -91.70
REMARK 500 GLU B 116 155.58 -44.18
REMARK 500 PRO B 119 -179.22 -57.38
REMARK 500 THR B 121 -32.17 -39.56
REMARK 500 ARG B 165 56.91 35.66
REMARK 500 SER B 215 170.05 -56.84
REMARK 500 ASN B 250 -14.03 65.30
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 PO4 A 332
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 333
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RFZ A 336
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 261
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 262
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 263
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 265
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3BLH RELATED DB: PDB
REMARK 900 RELATED ID: 3BLQ RELATED DB: PDB
REMARK 900 RELATED ID: 3BLR RELATED DB: PDB
REMARK 900 RELATED ID: 3MY5 RELATED DB: PDB
DBREF 3MY1 A 2 330 UNP P50750 CDK9_HUMAN 2 330
DBREF 3MY1 B 2 259 UNP O60563 CCNT1_HUMAN 2 259
SEQADV 3MY1 GLY A 0 UNP P50750 EXPRESSION TAG
SEQADV 3MY1 PRO A 1 UNP P50750 EXPRESSION TAG
SEQADV 3MY1 GLY B 0 UNP O60563 EXPRESSION TAG
SEQADV 3MY1 PRO B 1 UNP O60563 EXPRESSION TAG
SEQADV 3MY1 ARG B 77 UNP O60563 GLN 77 ENGINEERED MUTATION
SEQADV 3MY1 GLY B 96 UNP O60563 GLU 96 ENGINEERED MUTATION
SEQADV 3MY1 LEU B 241 UNP O60563 PHE 241 ENGINEERED MUTATION
SEQRES 1 A 331 GLY PRO ALA LYS GLN TYR ASP SER VAL GLU CYS PRO PHE
SEQRES 2 A 331 CYS ASP GLU VAL SER LYS TYR GLU LYS LEU ALA LYS ILE
SEQRES 3 A 331 GLY GLN GLY THR PHE GLY GLU VAL PHE LYS ALA ARG HIS
SEQRES 4 A 331 ARG LYS THR GLY GLN LYS VAL ALA LEU LYS LYS VAL LEU
SEQRES 5 A 331 MET GLU ASN GLU LYS GLU GLY PHE PRO ILE THR ALA LEU
SEQRES 6 A 331 ARG GLU ILE LYS ILE LEU GLN LEU LEU LYS HIS GLU ASN
SEQRES 7 A 331 VAL VAL ASN LEU ILE GLU ILE CYS ARG THR LYS ALA SER
SEQRES 8 A 331 PRO TYR ASN ARG CYS LYS GLY SER ILE TYR LEU VAL PHE
SEQRES 9 A 331 ASP PHE CYS GLU HIS ASP LEU ALA GLY LEU LEU SER ASN
SEQRES 10 A 331 VAL LEU VAL LYS PHE THR LEU SER GLU ILE LYS ARG VAL
SEQRES 11 A 331 MET GLN MET LEU LEU ASN GLY LEU TYR TYR ILE HIS ARG
SEQRES 12 A 331 ASN LYS ILE LEU HIS ARG ASP MET LYS ALA ALA ASN VAL
SEQRES 13 A 331 LEU ILE THR ARG ASP GLY VAL LEU LYS LEU ALA ASP PHE
SEQRES 14 A 331 GLY LEU ALA ARG ALA PHE SER LEU ALA LYS ASN SER GLN
SEQRES 15 A 331 PRO ASN ARG TYR TPO ASN ARG VAL VAL THR LEU TRP TYR
SEQRES 16 A 331 ARG PRO PRO GLU LEU LEU LEU GLY GLU ARG ASP TYR GLY
SEQRES 17 A 331 PRO PRO ILE ASP LEU TRP GLY ALA GLY CYS ILE MET ALA
SEQRES 18 A 331 GLU MET TRP THR ARG SER PRO ILE MET GLN GLY ASN THR
SEQRES 19 A 331 GLU GLN HIS GLN LEU ALA LEU ILE SER GLN LEU CYS GLY
SEQRES 20 A 331 SER ILE THR PRO GLU VAL TRP PRO ASN VAL ASP ASN TYR
SEQRES 21 A 331 GLU LEU TYR GLU LYS LEU GLU LEU VAL LYS GLY GLN LYS
SEQRES 22 A 331 ARG LYS VAL LYS ASP ARG LEU LYS ALA TYR VAL ARG ASP
SEQRES 23 A 331 PRO TYR ALA LEU ASP LEU ILE ASP LYS LEU LEU VAL LEU
SEQRES 24 A 331 ASP PRO ALA GLN ARG ILE ASP SER ASP ASP ALA LEU ASN
SEQRES 25 A 331 HIS ASP PHE PHE TRP SER ASP PRO MET PRO SER ASP LEU
SEQRES 26 A 331 LYS GLY MET LEU SER THR
SEQRES 1 B 260 GLY PRO GLU GLY GLU ARG LYS ASN ASN ASN LYS ARG TRP
SEQRES 2 B 260 TYR PHE THR ARG GLU GLN LEU GLU ASN SER PRO SER ARG
SEQRES 3 B 260 ARG PHE GLY VAL ASP PRO ASP LYS GLU LEU SER TYR ARG
SEQRES 4 B 260 GLN GLN ALA ALA ASN LEU LEU GLN ASP MET GLY GLN ARG
SEQRES 5 B 260 LEU ASN VAL SER GLN LEU THR ILE ASN THR ALA ILE VAL
SEQRES 6 B 260 TYR MET HIS ARG PHE TYR MET ILE GLN SER PHE THR ARG
SEQRES 7 B 260 PHE PRO GLY ASN SER VAL ALA PRO ALA ALA LEU PHE LEU
SEQRES 8 B 260 ALA ALA LYS VAL GLU GLY GLN PRO LYS LYS LEU GLU HIS
SEQRES 9 B 260 VAL ILE LYS VAL ALA HIS THR CYS LEU HIS PRO GLN GLU
SEQRES 10 B 260 SER LEU PRO ASP THR ARG SER GLU ALA TYR LEU GLN GLN
SEQRES 11 B 260 VAL GLN ASP LEU VAL ILE LEU GLU SER ILE ILE LEU GLN
SEQRES 12 B 260 THR LEU GLY PHE GLU LEU THR ILE ASP HIS PRO HIS THR
SEQRES 13 B 260 HIS VAL VAL LYS CYS THR GLN LEU VAL ARG ALA SER LYS
SEQRES 14 B 260 ASP LEU ALA GLN THR SER TYR PHE MET ALA THR ASN SER
SEQRES 15 B 260 LEU HIS LEU THR THR PHE SER LEU GLN TYR THR PRO PRO
SEQRES 16 B 260 VAL VAL ALA CYS VAL CYS ILE HIS LEU ALA CYS LYS TRP
SEQRES 17 B 260 SER ASN TRP GLU ILE PRO VAL SER THR ASP GLY LYS HIS
SEQRES 18 B 260 TRP TRP GLU TYR VAL ASP ALA THR VAL THR LEU GLU LEU
SEQRES 19 B 260 LEU ASP GLU LEU THR HIS GLU LEU LEU GLN ILE LEU GLU
SEQRES 20 B 260 LYS THR PRO ASN ARG LEU LYS ARG ILE TRP ASN TRP ARG
MODRES 3MY1 TPO A 186 THR PHOSPHOTHREONINE
HET TPO A 186 11
HET PO4 A 332 5
HET GOL A 333 6
HET RFZ A 336 20
HET GOL B 261 6
HET GOL B 262 6
HET GOL B 263 6
HET GOL B 265 6
HETNAM TPO PHOSPHOTHREONINE
HETNAM PO4 PHOSPHATE ION
HETNAM GOL GLYCEROL
HETNAM RFZ 5,6-DICHLORO-1-BETA-D-RIBOFURANOSYL-1H-BENZIMIDAZOLE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 PO4 O4 P 3-
FORMUL 4 GOL 5(C3 H8 O3)
FORMUL 5 RFZ C12 H12 CL2 N2 O4
FORMUL 10 HOH *36(H2 O)
HELIX 1 1 GLU A 15 SER A 17 5 3
HELIX 2 2 PRO A 60 LEU A 73 1 14
HELIX 3 3 LEU A 110 ASN A 116 1 7
HELIX 4 4 THR A 122 ASN A 143 1 22
HELIX 5 5 LYS A 151 ALA A 153 5 3
HELIX 6 6 PRO A 196 LEU A 201 1 6
HELIX 7 7 PRO A 208 GLU A 221 1 14
HELIX 8 8 THR A 233 GLY A 246 1 14
HELIX 9 9 ASN A 255 TYR A 259 5 5
HELIX 10 10 TYR A 262 GLU A 266 5 5
HELIX 11 11 LYS A 274 ALA A 281 1 8
HELIX 12 12 ASP A 285 LEU A 296 1 12
HELIX 13 13 ASP A 299 ARG A 303 5 5
HELIX 14 14 ASP A 305 ASN A 311 1 7
HELIX 15 15 HIS A 312 SER A 317 5 6
HELIX 16 16 THR B 15 ASN B 21 1 7
HELIX 17 17 SER B 24 GLY B 28 5 5
HELIX 18 18 ASP B 30 LEU B 52 1 23
HELIX 19 19 SER B 55 TYR B 70 1 16
HELIX 20 20 PRO B 79 GLY B 96 1 18
HELIX 21 21 LYS B 100 HIS B 113 1 14
HELIX 22 22 SER B 123 LEU B 144 1 22
HELIX 23 23 HIS B 152 LEU B 163 1 12
HELIX 24 24 SER B 167 THR B 185 1 19
HELIX 25 25 THR B 186 GLN B 190 5 5
HELIX 26 26 THR B 192 SER B 208 1 17
HELIX 27 27 HIS B 220 VAL B 225 5 6
HELIX 28 28 THR B 230 THR B 248 1 19
HELIX 29 29 ARG B 251 TRP B 256 5 6
SHEET 1 A 5 TYR A 19 LYS A 24 0
SHEET 2 A 5 VAL A 33 HIS A 38 -1 O ARG A 37 N GLU A 20
SHEET 3 A 5 LYS A 44 LYS A 49 -1 O VAL A 45 N ALA A 36
SHEET 4 A 5 TYR A 100 ASP A 104 -1 O PHE A 103 N ALA A 46
SHEET 5 A 5 LEU A 81 CYS A 85 -1 N ILE A 82 O VAL A 102
SHEET 1 B 3 HIS A 108 ASP A 109 0
SHEET 2 B 3 VAL A 155 ILE A 157 -1 O ILE A 157 N HIS A 108
SHEET 3 B 3 LEU A 163 LEU A 165 -1 O LYS A 164 N LEU A 156
SHEET 1 C 2 ILE A 145 LEU A 146 0
SHEET 2 C 2 ARG A 172 ALA A 173 -1 O ARG A 172 N LEU A 146
LINK C TYR A 185 N TPO A 186 1555 1555 1.33
LINK C TPO A 186 N ASN A 187 1555 1555 1.33
CISPEP 1 ASP A 318 PRO A 319 0 2.51
SITE 1 AC1 6 ARG A 65 LYS A 68 ILE A 69 ARG A 172
SITE 2 AC1 6 ALA A 173 GOL B 262
SITE 1 AC2 7 GLU A 55 GLU A 57 GLY A 58 PHE A 59
SITE 2 AC2 7 PRO A 60 ILE A 61 LYS B 93
SITE 1 AC3 8 ALA A 46 PHE A 103 ASP A 104 CYS A 106
SITE 2 AC3 8 ASN A 154 LEU A 156 ASP A 167 HOH A 343
SITE 1 AC4 5 TYR B 37 PRO B 79 GLY B 80 ASN B 81
SITE 2 AC4 5 HOH B 283
SITE 1 AC5 5 ARG A 65 LYS A 68 PO4 A 332 LYS B 93
SITE 2 AC5 5 VAL B 94
SITE 1 AC6 3 ASN B 257 TRP B 258 ARG B 259
SITE 1 AC7 4 HIS B 154 THR B 179 TRP B 258 ARG B 259
CRYST1 173.789 173.789 99.221 90.00 90.00 120.00 H 3 9
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 0.005754 0.003322 0.000000 0.00000
SCALE2 0.000000 0.006644 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010079 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
