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HEADER TRANSFERASE 26-MAY-15 5BNJ
TITLE CDK8/CYCC IN COMPLEX WITH 8-{3-CHLORO-5-[4-(1-METHYL-1H-PYRAZOL-4-YL)-
TITLE 2 PHENYL]-PYRIDIN- 4-YL}-2,8-DIAZA-SPIRO[4.5]DECAN-1-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 8;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 3-405;
COMPND 5 SYNONYM: CELL DIVISION PROTEIN KINASE 8,MEDIATOR COMPLEX SUBUNIT
COMPND 6 CDK8,MEDIATOR OF RNA POLYMERASE II TRANSCRIPTION SUBUNIT CDK8,PROTEIN
COMPND 7 KINASE K35;
COMPND 8 EC: 2.7.11.22,2.7.11.23;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: CYCLIN-C;
COMPND 12 CHAIN: B;
COMPND 13 SYNONYM: SRB11 HOMOLOG,HSRB11;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CDK8;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 11 ORGANISM_COMMON: HUMAN;
SOURCE 12 ORGANISM_TAXID: 9606;
SOURCE 13 GENE: CCNC;
SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS CDK8 KINASE / CYCLIN C, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR D.MUSIL,J.BLAGG,D.WIENKE
REVDAT 5 25-NOV-15 5BNJ 1 JRNL
REVDAT 4 11-NOV-15 5BNJ 1 JRNL
REVDAT 3 28-OCT-15 5BNJ 1 JRNL
REVDAT 2 21-OCT-15 5BNJ 1 JRNL
REVDAT 1 14-OCT-15 5BNJ 0
JRNL AUTH T.DALE,P.A.CLARKE,C.ESDAR,D.WAALBOER,O.ADENIJI-POPOOLA,
JRNL AUTH 2 M.J.ORTIZ-RUIZ,A.MALLINGER,R.S.SAMANT,P.CZODROWSKI,D.MUSIL,
JRNL AUTH 3 D.SCHWARZ,K.SCHNEIDER,M.STUBBS,K.EWAN,E.FRASER,R.TEPOELE,
JRNL AUTH 4 W.COURT,G.BOX,M.VALENTI,A.DE HAVEN BRANDON,S.GOWAN,
JRNL AUTH 5 F.ROHDICH,F.RAYNAUD,R.SCHNEIDER,O.POESCHKE,A.BLAUKAT,
JRNL AUTH 6 P.WORKMAN,K.SCHIEMANN,S.A.ECCLES,D.WIENKE,J.BLAGG
JRNL TITL A SELECTIVE CHEMICAL PROBE FOR EXPLORING THE ROLE OF CDK8
JRNL TITL 2 AND CDK19 IN HUMAN DISEASE.
JRNL REF NAT.CHEM.BIOL. V. 11 973 2015
JRNL REFN ESSN 1552-4469
JRNL PMID 26502155
JRNL DOI 10.1038/NCHEMBIO.1952
REMARK 2
REMARK 2 RESOLUTION. 2.64 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.64
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 86.27
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 3 NUMBER OF REFLECTIONS : 24989
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.226
REMARK 3 FREE R VALUE : 0.273
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.400
REMARK 3 FREE R VALUE TEST SET COUNT : 888
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) : 2.64
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.71
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1823
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.43
REMARK 3 BIN R VALUE (WORKING SET) : 0.3600
REMARK 3 BIN FREE R VALUE SET COUNT : 57
REMARK 3 BIN FREE R VALUE : 0.4140
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4836
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 36
REMARK 3 SOLVENT ATOMS : 57
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 46.60
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.84000
REMARK 3 B22 (A**2) : -3.14000
REMARK 3 B33 (A**2) : 3.97000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.588
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.327
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.234
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.401
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.931
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5004 ; 0.009 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4535 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6800 ; 1.082 ; 1.963
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10450 ; 0.884 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 604 ; 5.398 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 219 ;34.668 ;23.425
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 809 ;11.964 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;13.424 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 746 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5510 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1054 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 932 ; 0.157 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4076 ; 0.123 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2407 ; 0.159 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2482 ; 0.074 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 104 ; 0.098 ; 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): 7 ; 0.106 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 45 ; 0.137 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 5 ; 0.074 ; 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): 3971 ; 1.300 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1214 ; 0.161 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4901 ; 1.494 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2352 ; 1.938 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1899 ; 2.948 ; 6.000
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 : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
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 5BNJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-MAY-15.
REMARK 100 THE DEPOSITION ID IS D_1000210132.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-MAY-14
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06DA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25877
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.640
REMARK 200 RESOLUTION RANGE LOW (A) : 86.270
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.8
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.08100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.64
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.52300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: REFMAC 5.2.0005
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2 M SODIUM FORMATE, PH
REMARK 280 6.9,, VAPOR DIFFUSION, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-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 SMTRY1 2 -1.000000 0.000000 0.000000 35.39350
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 86.26600
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.74450
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 86.26600
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.39350
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.74450
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4230 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 29710 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 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 LYS A 118
REMARK 465 LYS A 119
REMARK 465 PRO A 120
REMARK 465 VAL A 121
REMARK 465 LYS A 185
REMARK 465 PRO A 186
REMARK 465 LEU A 187
REMARK 465 ALA A 188
REMARK 465 ASP A 189
REMARK 465 LEU A 190
REMARK 465 ASP A 191
REMARK 465 PRO A 192
REMARK 465 VAL A 193
REMARK 465 VAL A 194
REMARK 465 VAL A 195
REMARK 465 GLU A 239
REMARK 465 ASP A 240
REMARK 465 ILE A 241
REMARK 465 LYS A 242
REMARK 465 THR A 243
REMARK 465 SER A 244
REMARK 465 GLU A 363
REMARK 465 PRO A 364
REMARK 465 ASP A 365
REMARK 465 ASP A 366
REMARK 465 LYS A 367
REMARK 465 GLY A 368
REMARK 465 ASP A 369
REMARK 465 LYS A 370
REMARK 465 LYS A 371
REMARK 465 ASN A 372
REMARK 465 GLN A 373
REMARK 465 GLN A 374
REMARK 465 GLN A 375
REMARK 465 GLN A 376
REMARK 465 GLN A 377
REMARK 465 GLY A 378
REMARK 465 ASN A 379
REMARK 465 ASN A 380
REMARK 465 HIS A 381
REMARK 465 THR A 382
REMARK 465 ASN A 383
REMARK 465 GLY A 384
REMARK 465 THR A 385
REMARK 465 GLY A 386
REMARK 465 HIS A 387
REMARK 465 PRO A 388
REMARK 465 GLY A 389
REMARK 465 ASN A 390
REMARK 465 GLN A 391
REMARK 465 ASP A 392
REMARK 465 SER A 393
REMARK 465 SER A 394
REMARK 465 HIS A 395
REMARK 465 THR A 396
REMARK 465 GLN A 397
REMARK 465 GLY A 398
REMARK 465 PRO A 399
REMARK 465 PRO A 400
REMARK 465 LEU A 401
REMARK 465 LYS A 402
REMARK 465 LYS A 403
REMARK 465 ASN B 265
REMARK 465 SER B 266
REMARK 465 GLU B 267
REMARK 465 GLY B 268
REMARK 465 GLU B 269
REMARK 465 GLN B 270
REMARK 465 GLY B 271
REMARK 465 PRO B 272
REMARK 465 ASN B 273
REMARK 465 GLY B 274
REMARK 465 SER B 275
REMARK 465 GLN B 276
REMARK 465 ASN B 277
REMARK 465 SER B 278
REMARK 465 SER B 279
REMARK 465 TYR B 280
REMARK 465 SER B 281
REMARK 465 GLN B 282
REMARK 465 SER B 283
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 LYS A 0 CE NZ
REMARK 470 LYS A 6 CD CE NZ
REMARK 470 LYS A 8 CD CE NZ
REMARK 470 LYS A 37 NZ
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 ASP A 42 CG OD1 OD2
REMARK 470 LYS A 44 CG CD CE NZ
REMARK 470 ASP A 46 CG OD1 OD2
REMARK 470 GLU A 55 CD OE1 OE2
REMARK 470 ARG A 65 CZ NH1 NH2
REMARK 470 LYS A 74 CG CD CE NZ
REMARK 470 LYS A 83 CD CE NZ
REMARK 470 LYS A 92 CE NZ
REMARK 470 LYS A 109 CD CE NZ
REMARK 470 ARG A 112 CZ NH1 NH2
REMARK 470 SER A 114 OG
REMARK 470 LYS A 115 CG CD CE NZ
REMARK 470 ASN A 117 CG OD1 ND2
REMARK 470 ARG A 125 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 179 CG CD1 CD2
REMARK 470 PHE A 180 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 209 CD NE CZ NH1 NH2
REMARK 470 ARG A 237 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 238 CG CD OE1 NE2
REMARK 470 LYS A 265 CG CD CE NZ
REMARK 470 LYS A 271 CG CD CE NZ
REMARK 470 LYS A 281 CE NZ
REMARK 470 ASN A 290 CG OD1 ND2
REMARK 470 LYS A 295 CG CD CE NZ
REMARK 470 LYS A 301 CG CD CE NZ
REMARK 470 LYS A 303 CD CE NZ
REMARK 470 GLU A 327 CD OE1 OE2
REMARK 470 GLN A 350 CG CD OE1 NE2
REMARK 470 LYS A 355 CG CD CE NZ
REMARK 470 GLU A 357 CD OE1 OE2
REMARK 470 THR A 360 OG1 CG2
REMARK 470 GLU A 362 CD OE1 OE2
REMARK 470 LYS B 18 NZ
REMARK 470 GLN B 19 CG CD OE1 NE2
REMARK 470 LYS B 23 CG CD CE NZ
REMARK 470 LYS B 30 CD CE NZ
REMARK 470 LYS B 56 CD CE NZ
REMARK 470 GLN B 60 CG CD OE1 NE2
REMARK 470 ARG B 75 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 79 CE NZ
REMARK 470 GLU B 99 CG CD OE1 OE2
REMARK 470 PHE B 100 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 117 CD CE NZ
REMARK 470 LYS B 126 CD CE NZ
REMARK 470 GLU B 127 CG CD OE1 OE2
REMARK 470 ARG B 131 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 137 CG CD OE1 OE2
REMARK 470 LEU B 145 CG CD1 CD2
REMARK 470 ARG B 157 CD NE CZ NH1 NH2
REMARK 470 MET B 171 CG SD CE
REMARK 470 LYS B 211 CD CE NZ
REMARK 470 GLN B 215 CD OE1 NE2
REMARK 470 GLU B 225 CG CD OE1 OE2
REMARK 470 LYS B 226 CE NZ
REMARK 470 LYS B 236 CD CE NZ
REMARK 470 LYS B 256 CE NZ
REMARK 470 LYS B 261 CG CD CE NZ
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 TYR A 22 3.62 -150.93
REMARK 500 ALA A 116 -72.77 -83.43
REMARK 500 ARG A 150 -2.58 76.10
REMARK 500 ASP A 151 51.34 -161.15
REMARK 500 GLU A 165 35.84 -95.06
REMARK 500 PHE A 234 50.29 -111.60
REMARK 500 ASN A 290 43.11 -101.66
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 4TV A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 302
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4F7N RELATED DB: PDB
DBREF 5BNJ A 1 403 UNP P49336 CDK8_HUMAN 1 403
DBREF 5BNJ B 1 283 UNP P24863 CCNC_HUMAN 1 283
SEQADV 5BNJ ASP A -1 UNP P49336 EXPRESSION TAG
SEQADV 5BNJ LYS A 0 UNP P49336 EXPRESSION TAG
SEQADV 5BNJ LYS B -1 UNP P24863 EXPRESSION TAG
SEQADV 5BNJ ALA B 0 UNP P24863 EXPRESSION TAG
SEQRES 1 A 405 ASP LYS MET ASP TYR ASP PHE LYS VAL LYS LEU SER SER
SEQRES 2 A 405 GLU ARG GLU ARG VAL GLU ASP LEU PHE GLU TYR GLU GLY
SEQRES 3 A 405 CYS LYS VAL GLY ARG GLY THR TYR GLY HIS VAL TYR LYS
SEQRES 4 A 405 ALA LYS ARG LYS ASP GLY LYS ASP ASP LYS ASP TYR ALA
SEQRES 5 A 405 LEU LYS GLN ILE GLU GLY THR GLY ILE SER MET SER ALA
SEQRES 6 A 405 CYS ARG GLU ILE ALA LEU LEU ARG GLU LEU LYS HIS PRO
SEQRES 7 A 405 ASN VAL ILE SER LEU GLN LYS VAL PHE LEU SER HIS ALA
SEQRES 8 A 405 ASP ARG LYS VAL TRP LEU LEU PHE ASP TYR ALA GLU HIS
SEQRES 9 A 405 ASP LEU TRP HIS ILE ILE LYS PHE HIS ARG ALA SER LYS
SEQRES 10 A 405 ALA ASN LYS LYS PRO VAL GLN LEU PRO ARG GLY MET VAL
SEQRES 11 A 405 LYS SER LEU LEU TYR GLN ILE LEU ASP GLY ILE HIS TYR
SEQRES 12 A 405 LEU HIS ALA ASN TRP VAL LEU HIS ARG ASP LEU LYS PRO
SEQRES 13 A 405 ALA ASN ILE LEU VAL MET GLY GLU GLY PRO GLU ARG GLY
SEQRES 14 A 405 ARG VAL LYS ILE ALA ASP MET GLY PHE ALA ARG LEU PHE
SEQRES 15 A 405 ASN SER PRO LEU LYS PRO LEU ALA ASP LEU ASP PRO VAL
SEQRES 16 A 405 VAL VAL THR PHE TRP TYR ARG ALA PRO GLU LEU LEU LEU
SEQRES 17 A 405 GLY ALA ARG HIS TYR THR LYS ALA ILE ASP ILE TRP ALA
SEQRES 18 A 405 ILE GLY CYS ILE PHE ALA GLU LEU LEU THR SER GLU PRO
SEQRES 19 A 405 ILE PHE HIS CYS ARG GLN GLU ASP ILE LYS THR SER ASN
SEQRES 20 A 405 PRO TYR HIS HIS ASP GLN LEU ASP ARG ILE PHE ASN VAL
SEQRES 21 A 405 MET GLY PHE PRO ALA ASP LYS ASP TRP GLU ASP ILE LYS
SEQRES 22 A 405 LYS MET PRO GLU HIS SER THR LEU MET LYS ASP PHE ARG
SEQRES 23 A 405 ARG ASN THR TYR THR ASN CYS SER LEU ILE LYS TYR MET
SEQRES 24 A 405 GLU LYS HIS LYS VAL LYS PRO ASP SER LYS ALA PHE HIS
SEQRES 25 A 405 LEU LEU GLN LYS LEU LEU THR MET ASP PRO ILE LYS ARG
SEQRES 26 A 405 ILE THR SER GLU GLN ALA MET GLN ASP PRO TYR PHE LEU
SEQRES 27 A 405 GLU ASP PRO LEU PRO THR SER ASP VAL PHE ALA GLY CYS
SEQRES 28 A 405 GLN ILE PRO TYR PRO LYS ARG GLU PHE LEU THR GLU GLU
SEQRES 29 A 405 GLU PRO ASP ASP LYS GLY ASP LYS LYS ASN GLN GLN GLN
SEQRES 30 A 405 GLN GLN GLY ASN ASN HIS THR ASN GLY THR GLY HIS PRO
SEQRES 31 A 405 GLY ASN GLN ASP SER SER HIS THR GLN GLY PRO PRO LEU
SEQRES 32 A 405 LYS LYS
SEQRES 1 B 285 LYS ALA MET ALA GLY ASN PHE TRP GLN SER SER HIS TYR
SEQRES 2 B 285 LEU GLN TRP ILE LEU ASP LYS GLN ASP LEU LEU LYS GLU
SEQRES 3 B 285 ARG GLN LYS ASP LEU LYS PHE LEU SER GLU GLU GLU TYR
SEQRES 4 B 285 TRP LYS LEU GLN ILE PHE PHE THR ASN VAL ILE GLN ALA
SEQRES 5 B 285 LEU GLY GLU HIS LEU LYS LEU ARG GLN GLN VAL ILE ALA
SEQRES 6 B 285 THR ALA THR VAL TYR PHE LYS ARG PHE TYR ALA ARG TYR
SEQRES 7 B 285 SER LEU LYS SER ILE ASP PRO VAL LEU MET ALA PRO THR
SEQRES 8 B 285 CYS VAL PHE LEU ALA SER LYS VAL GLU GLU PHE GLY VAL
SEQRES 9 B 285 VAL SER ASN THR ARG LEU ILE ALA ALA ALA THR SER VAL
SEQRES 10 B 285 LEU LYS THR ARG PHE SER TYR ALA PHE PRO LYS GLU PHE
SEQRES 11 B 285 PRO TYR ARG MET ASN HIS ILE LEU GLU CYS GLU PHE TYR
SEQRES 12 B 285 LEU LEU GLU LEU MET ASP CYS CYS LEU ILE VAL TYR HIS
SEQRES 13 B 285 PRO TYR ARG PRO LEU LEU GLN TYR VAL GLN ASP MET GLY
SEQRES 14 B 285 GLN GLU ASP MET LEU LEU PRO LEU ALA TRP ARG ILE VAL
SEQRES 15 B 285 ASN ASP THR TYR ARG THR ASP LEU CYS LEU LEU TYR PRO
SEQRES 16 B 285 PRO PHE MET ILE ALA LEU ALA CYS LEU HIS VAL ALA CYS
SEQRES 17 B 285 VAL VAL GLN GLN LYS ASP ALA ARG GLN TRP PHE ALA GLU
SEQRES 18 B 285 LEU SER VAL ASP MET GLU LYS ILE LEU GLU ILE ILE ARG
SEQRES 19 B 285 VAL ILE LEU LYS LEU TYR GLU GLN TRP LYS ASN PHE ASP
SEQRES 20 B 285 GLU ARG LYS GLU MET ALA THR ILE LEU SER LYS MET PRO
SEQRES 21 B 285 LYS PRO LYS PRO PRO PRO ASN SER GLU GLY GLU GLN GLY
SEQRES 22 B 285 PRO ASN GLY SER GLN ASN SER SER TYR SER GLN SER
HET 4TV A 501 30
HET FMT B 301 3
HET FMT B 302 3
HETNAM 4TV 8-{3-CHLORO-5-[4-(1-METHYL-1H-PYRAZOL-4-YL)
HETNAM 2 4TV PHENYL]PYRIDIN-4-YL}-2,8-DIAZASPIRO[4.5]DECAN-1-ONE
HETNAM FMT FORMIC ACID
FORMUL 3 4TV C23 H24 CL N5 O
FORMUL 4 FMT 2(C H2 O2)
FORMUL 6 HOH *57(H2 O)
HELIX 1 AA1 ASP A 2 ARG A 13 1 12
HELIX 2 AA2 ARG A 15 LEU A 19 1 5
HELIX 3 AA3 SER A 60 ARG A 71 1 12
HELIX 4 AA4 LEU A 104 ASN A 117 1 14
HELIX 5 AA5 GLY A 126 ASN A 145 1 20
HELIX 6 AA6 ALA A 201 LEU A 206 1 6
HELIX 7 AA7 THR A 212 SER A 230 1 19
HELIX 8 AA8 HIS A 248 GLY A 260 1 13
HELIX 9 AA9 TRP A 267 MET A 273 5 7
HELIX 10 AB1 GLU A 275 PHE A 283 1 9
HELIX 11 AB2 ARG A 284 THR A 289 5 6
HELIX 12 AB3 SER A 292 HIS A 300 1 9
HELIX 13 AB4 SER A 306 LEU A 316 1 11
HELIX 14 AB5 ASP A 319 ARG A 323 5 5
HELIX 15 AB6 THR A 325 GLN A 331 1 7
HELIX 16 AB7 ASP A 332 GLU A 337 5 6
HELIX 17 AB8 ASN B 4 GLN B 7 5 4
HELIX 18 AB9 SER B 8 TRP B 14 1 7
HELIX 19 AC1 ASP B 17 GLN B 26 1 10
HELIX 20 AC2 SER B 33 LEU B 55 1 23
HELIX 21 AC3 ARG B 58 TYR B 76 1 19
HELIX 22 AC4 ASP B 82 GLU B 98 1 17
HELIX 23 AC5 SER B 104 ARG B 119 1 16
HELIX 24 AC6 ARG B 131 MET B 146 1 16
HELIX 25 AC7 PRO B 155 GLY B 167 1 13
HELIX 26 AC8 GLN B 168 TYR B 184 1 17
HELIX 27 AC9 ARG B 185 THR B 186 5 2
HELIX 28 AD1 ASP B 187 LEU B 191 5 5
HELIX 29 AD2 PRO B 193 GLN B 209 1 17
HELIX 30 AD3 ALA B 213 GLU B 219 1 7
HELIX 31 AD4 ASP B 223 PHE B 244 1 22
HELIX 32 AD5 ASP B 245 MET B 257 1 13
SHEET 1 AA1 3 PHE A 20 GLU A 21 0
SHEET 2 AA1 3 GLY A 33 ARG A 40 -1 O LYS A 39 N GLU A 21
SHEET 3 AA1 3 LYS A 26 ARG A 29 -1 N GLY A 28 O VAL A 35
SHEET 1 AA2 5 PHE A 20 GLU A 21 0
SHEET 2 AA2 5 GLY A 33 ARG A 40 -1 O LYS A 39 N GLU A 21
SHEET 3 AA2 5 TYR A 49 ILE A 54 -1 O TYR A 49 N ALA A 38
SHEET 4 AA2 5 LYS A 92 ASP A 98 -1 O LEU A 95 N LYS A 52
SHEET 5 AA2 5 LEU A 81 SER A 87 -1 N PHE A 85 O TRP A 94
SHEET 1 AA3 3 HIS A 102 ASP A 103 0
SHEET 2 AA3 3 ILE A 157 VAL A 159 -1 O VAL A 159 N HIS A 102
SHEET 3 AA3 3 VAL A 169 ILE A 171 -1 O LYS A 170 N LEU A 158
CISPEP 1 ASP A 338 PRO A 339 0 3.13
SITE 1 AC1 10 VAL A 27 TYR A 32 ALA A 50 LYS A 52
SITE 2 AC1 10 PHE A 97 ASP A 98 ALA A 100 HIS A 106
SITE 3 AC1 10 ASP A 173 ARG A 356
SITE 1 AC2 2 GLU A 14 GLU B 144
SITE 1 AC3 2 ARG A 71 ASP B 147
CRYST1 70.787 71.489 172.532 90.00 90.00 90.00 P 21 21 21 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 0.014127 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013988 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005796 0.00000
(ATOM LINES ARE NOT SHOWN.)
END