HEADER TRANSFERASE 15-FEB-16 5I5Z
TITLE CDK8-CYCC IN COMPLEX WITH 8-(1-METHYL-2,2-DIOXO-2,3-DIHYDRO-1H-2L6-
TITLE 2 BENZO[C]ISOTHIAZOL-5-YL)-[1,6]NAPHTHYRIDINE-2-CARBOXYLIC ACID
TITLE 3 METHYLAMIDE
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,A.MALLINGER
REVDAT 3 10-JAN-24 5I5Z 1 REMARK
REVDAT 2 06-JUL-16 5I5Z 1 JRNL
REVDAT 1 13-APR-16 5I5Z 0
JRNL AUTH A.MALLINGER,K.SCHIEMANN,C.RINK,J.SEJBERG,M.A.HONEY,
JRNL AUTH 2 P.CZODROWSKI,M.STUBBS,O.POESCHKE,M.BUSCH,R.SCHNEIDER,
JRNL AUTH 3 D.SCHWARZ,D.MUSIL,R.BURKE,K.URBAHNS,P.WORKMAN,D.WIENKE,
JRNL AUTH 4 P.A.CLARKE,F.I.RAYNAUD,S.A.ECCLES,C.ESDAR,F.ROHDICH,J.BLAGG
JRNL TITL 2,8-DISUBSTITUTED-1,6-NAPHTHYRIDINES AND
JRNL TITL 2 4,6-DISUBSTITUTED-ISOQUINOLINES WITH POTENT, SELECTIVE
JRNL TITL 3 AFFINITY FOR CDK8/19.
JRNL REF ACS MED.CHEM.LETT. V. 7 573 2016
JRNL REFN ISSN 1948-5875
JRNL PMID 27326329
JRNL DOI 10.1021/ACSMEDCHEMLETT.6B00022
REMARK 2
REMARK 2 RESOLUTION. 2.60 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 85.98
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 3 NUMBER OF REFLECTIONS : 25840
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) : 0.239
REMARK 3 R VALUE (WORKING SET) : 0.237
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.500
REMARK 3 FREE R VALUE TEST SET COUNT : 926
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) : 2.60
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.67
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1885
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.3650
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.4450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 5064
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 32
REMARK 3 SOLVENT ATOMS : 49
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.72
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.13000
REMARK 3 B22 (A**2) : -0.57000
REMARK 3 B33 (A**2) : 1.70000
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): 0.586
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.321
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.257
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.361
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.905
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.867
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 5095 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 4612 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6912 ; 1.224 ; 1.964
REMARK 3 BOND ANGLES OTHERS (DEGREES): 10660 ; 0.933 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 606 ; 6.060 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 233 ;33.638 ;23.391
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 853 ;13.768 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;18.286 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 749 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5597 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1081 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 989 ; 0.180 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 4195 ; 0.134 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2433 ; 0.166 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2593 ; 0.074 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 89 ; 0.103 ; 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): 1 ; 0.084 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 47 ; 0.154 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 4 ; 0.080 ; 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): 3987 ; 1.655 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1218 ; 0.299 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4926 ; 2.089 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2457 ; 3.071 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1986 ; 4.332 ; 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 : NULL
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 5I5Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-FEB-16.
REMARK 100 THE DEPOSITION ID IS D_1000218342.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-JUL-12
REMARK 200 TEMPERATURE (KELVIN) : 100
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 : X06SA
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 : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 27530
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.600
REMARK 200 RESOLUTION RANGE LOW (A) : 85.980
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 4.100
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.2
REMARK 200 DATA REDUNDANCY IN SHELL : 3.90
REMARK 200 R MERGE FOR SHELL (I) : 0.50300
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: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 4F6S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 59.40
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.2 M SODIUM FORMATE, PH
REMARK 280 6.9, VAPOR DIFFUSION, HANGING DROP, 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 35.37450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 85.97650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.64100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 85.97650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.37450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.64100
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: 29330 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 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 GLN A 122
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 PRO A 363
REMARK 465 PRO A 364
REMARK 465 LEU A 365
REMARK 465 LYS A 366
REMARK 465 LYS A 367
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 ASP A -1 CG OD1 OD2
REMARK 480 LYS A 0 CG CD CE NZ
REMARK 480 ASP A 42 CG OD1 OD2
REMARK 480 LYS A 44 CG CD CE NZ
REMARK 480 ASP A 46 CG OD1 OD2
REMARK 480 LYS A 74 CG CD CE NZ
REMARK 480 LYS A 83 CE NZ
REMARK 480 LYS A 92 CE NZ
REMARK 480 LYS A 109 CG CD CE NZ
REMARK 480 LYS A 115 CG CD CE NZ
REMARK 480 LEU A 179 CG CD1 CD2
REMARK 480 ARG A 209 CD NE CZ NH1 NH2
REMARK 480 ARG A 237 CG CD NE CZ NH1 NH2
REMARK 480 SER A 244 OG
REMARK 480 LYS A 265 CG CD CE NZ
REMARK 480 LYS A 271 CG CD CE NZ
REMARK 480 LYS A 272 CG CD CE NZ
REMARK 480 ASN A 290 CG OD1 ND2
REMARK 480 LYS A 295 CD CE NZ
REMARK 480 LYS A 299 CG CD CE NZ
REMARK 480 LYS A 303 CE NZ
REMARK 480 LYS A 355 CG CD CE NZ
REMARK 480 GLU A 362 CG CD OE1 OE2
REMARK 480 LYS B -1 CD CE NZ
REMARK 480 GLN B 19 CG CD OE1 NE2
REMARK 480 LYS B 23 CG CD CE NZ
REMARK 480 LYS B 30 CE NZ
REMARK 480 GLN B 41 CD OE1 NE2
REMARK 480 LYS B 56 CD CE NZ
REMARK 480 LYS B 117 CG CD CE NZ
REMARK 480 LYS B 126 CG CD CE NZ
REMARK 480 GLU B 127 CG CD OE1 OE2
REMARK 480 ARG B 131 CG CD NE CZ NH1 NH2
REMARK 480 LYS B 211 CE NZ
REMARK 480 ARG B 214 NE CZ NH1 NH2
REMARK 480 GLU B 225 CD OE1 OE2
REMARK 480 LYS B 236 CG CD CE NZ
REMARK 480 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 LYS A 0 35.22 -93.97
REMARK 500 ASP A 42 78.50 -67.59
REMARK 500 ASP A 151 48.41 -164.18
REMARK 500 GLU A 165 33.31 -93.39
REMARK 500 ALA A 177 91.43 64.17
REMARK 500 LEU A 316 45.38 -95.23
REMARK 500 ALA B 0 118.38 -39.00
REMARK 500 PHE B 120 27.85 -140.91
REMARK 500 PHE B 128 104.76 -55.58
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 68U A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 301
DBREF 5I5Z A 1 362 UNP P49336 CDK8_HUMAN 1 362
DBREF 5I5Z B 1 264 UNP P24863 CCNC_HUMAN 1 264
SEQADV 5I5Z ASP A -2 UNP P49336 EXPRESSION TAG
SEQADV 5I5Z ASP A -1 UNP P49336 EXPRESSION TAG
SEQADV 5I5Z LYS A 0 UNP P49336 EXPRESSION TAG
SEQADV 5I5Z PRO A 363 UNP P49336 EXPRESSION TAG
SEQADV 5I5Z PRO A 364 UNP P49336 EXPRESSION TAG
SEQADV 5I5Z LEU A 365 UNP P49336 EXPRESSION TAG
SEQADV 5I5Z LYS A 366 UNP P49336 EXPRESSION TAG
SEQADV 5I5Z LYS A 367 UNP P49336 EXPRESSION TAG
SEQADV 5I5Z LYS B -1 UNP P24863 EXPRESSION TAG
SEQADV 5I5Z ALA B 0 UNP P24863 EXPRESSION TAG
SEQRES 1 A 370 ASP ASP LYS MET ASP TYR ASP PHE LYS VAL LYS LEU SER
SEQRES 2 A 370 SER GLU ARG GLU ARG VAL GLU ASP LEU PHE GLU TYR GLU
SEQRES 3 A 370 GLY CYS LYS VAL GLY ARG GLY THR TYR GLY HIS VAL TYR
SEQRES 4 A 370 LYS ALA LYS ARG LYS ASP GLY LYS ASP ASP LYS ASP TYR
SEQRES 5 A 370 ALA LEU LYS GLN ILE GLU GLY THR GLY ILE SER MET SER
SEQRES 6 A 370 ALA CYS ARG GLU ILE ALA LEU LEU ARG GLU LEU LYS HIS
SEQRES 7 A 370 PRO ASN VAL ILE SER LEU GLN LYS VAL PHE LEU SER HIS
SEQRES 8 A 370 ALA ASP ARG LYS VAL TRP LEU LEU PHE ASP TYR ALA GLU
SEQRES 9 A 370 HIS ASP LEU TRP HIS ILE ILE LYS PHE HIS ARG ALA SER
SEQRES 10 A 370 LYS ALA ASN LYS LYS PRO VAL GLN LEU PRO ARG GLY MET
SEQRES 11 A 370 VAL LYS SER LEU LEU TYR GLN ILE LEU ASP GLY ILE HIS
SEQRES 12 A 370 TYR LEU HIS ALA ASN TRP VAL LEU HIS ARG ASP LEU LYS
SEQRES 13 A 370 PRO ALA ASN ILE LEU VAL MET GLY GLU GLY PRO GLU ARG
SEQRES 14 A 370 GLY ARG VAL LYS ILE ALA ASP MET GLY PHE ALA ARG LEU
SEQRES 15 A 370 PHE ASN SER PRO LEU LYS PRO LEU ALA ASP LEU ASP PRO
SEQRES 16 A 370 VAL VAL VAL THR PHE TRP TYR ARG ALA PRO GLU LEU LEU
SEQRES 17 A 370 LEU GLY ALA ARG HIS TYR THR LYS ALA ILE ASP ILE TRP
SEQRES 18 A 370 ALA ILE GLY CYS ILE PHE ALA GLU LEU LEU THR SER GLU
SEQRES 19 A 370 PRO ILE PHE HIS CYS ARG GLN GLU ASP ILE LYS THR SER
SEQRES 20 A 370 ASN PRO TYR HIS HIS ASP GLN LEU ASP ARG ILE PHE ASN
SEQRES 21 A 370 VAL MET GLY PHE PRO ALA ASP LYS ASP TRP GLU ASP ILE
SEQRES 22 A 370 LYS LYS MET PRO GLU HIS SER THR LEU MET LYS ASP PHE
SEQRES 23 A 370 ARG ARG ASN THR TYR THR ASN CYS SER LEU ILE LYS TYR
SEQRES 24 A 370 MET GLU LYS HIS LYS VAL LYS PRO ASP SER LYS ALA PHE
SEQRES 25 A 370 HIS LEU LEU GLN LYS LEU LEU THR MET ASP PRO ILE LYS
SEQRES 26 A 370 ARG ILE THR SER GLU GLN ALA MET GLN ASP PRO TYR PHE
SEQRES 27 A 370 LEU GLU ASP PRO LEU PRO THR SER ASP VAL PHE ALA GLY
SEQRES 28 A 370 CYS GLN ILE PRO TYR PRO LYS ARG GLU PHE LEU THR GLU
SEQRES 29 A 370 GLU PRO PRO LEU LYS LYS
SEQRES 1 B 266 LYS ALA MET ALA GLY ASN PHE TRP GLN SER SER HIS TYR
SEQRES 2 B 266 LEU GLN TRP ILE LEU ASP LYS GLN ASP LEU LEU LYS GLU
SEQRES 3 B 266 ARG GLN LYS ASP LEU LYS PHE LEU SER GLU GLU GLU TYR
SEQRES 4 B 266 TRP LYS LEU GLN ILE PHE PHE THR ASN VAL ILE GLN ALA
SEQRES 5 B 266 LEU GLY GLU HIS LEU LYS LEU ARG GLN GLN VAL ILE ALA
SEQRES 6 B 266 THR ALA THR VAL TYR PHE LYS ARG PHE TYR ALA ARG TYR
SEQRES 7 B 266 SER LEU LYS SER ILE ASP PRO VAL LEU MET ALA PRO THR
SEQRES 8 B 266 CYS VAL PHE LEU ALA SER LYS VAL GLU GLU PHE GLY VAL
SEQRES 9 B 266 VAL SER ASN THR ARG LEU ILE ALA ALA ALA THR SER VAL
SEQRES 10 B 266 LEU LYS THR ARG PHE SER TYR ALA PHE PRO LYS GLU PHE
SEQRES 11 B 266 PRO TYR ARG MET ASN HIS ILE LEU GLU CYS GLU PHE TYR
SEQRES 12 B 266 LEU LEU GLU LEU MET ASP CYS CYS LEU ILE VAL TYR HIS
SEQRES 13 B 266 PRO TYR ARG PRO LEU LEU GLN TYR VAL GLN ASP MET GLY
SEQRES 14 B 266 GLN GLU ASP MET LEU LEU PRO LEU ALA TRP ARG ILE VAL
SEQRES 15 B 266 ASN ASP THR TYR ARG THR ASP LEU CYS LEU LEU TYR PRO
SEQRES 16 B 266 PRO PHE MET ILE ALA LEU ALA CYS LEU HIS VAL ALA CYS
SEQRES 17 B 266 VAL VAL GLN GLN LYS ASP ALA ARG GLN TRP PHE ALA GLU
SEQRES 18 B 266 LEU SER VAL ASP MET GLU LYS ILE LEU GLU ILE ILE ARG
SEQRES 19 B 266 VAL ILE LEU LYS LEU TYR GLU GLN TRP LYS ASN PHE ASP
SEQRES 20 B 266 GLU ARG LYS GLU MET ALA THR ILE LEU SER LYS MET PRO
SEQRES 21 B 266 LYS PRO LYS PRO PRO PRO
HET 68U A 401 26
HET FMT A 402 3
HET FMT B 301 3
HETNAM 68U N-METHYL-8-(1-METHYL-2,2-DIOXO-2,3-DIHYDRO-1H-
HETNAM 2 68U 2LAMBDA~6~,1-BENZOTHIAZOL-5-YL)-1,6-NAPHTHYRIDINE-2-
HETNAM 3 68U CARBOXAMIDE
HETNAM FMT FORMIC ACID
FORMUL 3 68U C18 H16 N4 O3 S
FORMUL 4 FMT 2(C H2 O2)
FORMUL 6 HOH *49(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 ALA A 116 1 13
HELIX 5 AA5 GLY A 126 ASN A 145 1 20
HELIX 6 AA6 LYS A 153 ALA A 155 5 3
HELIX 7 AA7 ARG A 178 SER A 182 5 5
HELIX 8 AA8 ALA A 201 LEU A 206 1 6
HELIX 9 AA9 THR A 212 SER A 230 1 19
HELIX 10 AB1 HIS A 248 GLY A 260 1 13
HELIX 11 AB2 TRP A 267 MET A 273 5 7
HELIX 12 AB3 GLU A 275 PHE A 283 1 9
HELIX 13 AB4 ARG A 284 THR A 289 5 6
HELIX 14 AB5 SER A 292 HIS A 300 1 9
HELIX 15 AB6 SER A 306 LEU A 316 1 11
HELIX 16 AB7 ASP A 319 ARG A 323 5 5
HELIX 17 AB8 THR A 325 GLN A 331 1 7
HELIX 18 AB9 ASP A 332 GLU A 337 5 6
HELIX 19 AC1 ASN B 4 GLN B 7 5 4
HELIX 20 AC2 SER B 8 TRP B 14 1 7
HELIX 21 AC3 ASP B 17 GLN B 26 1 10
HELIX 22 AC4 LYS B 27 PHE B 31 5 5
HELIX 23 AC5 SER B 33 LYS B 56 1 24
HELIX 24 AC6 ARG B 58 TYR B 76 1 19
HELIX 25 AC7 ASP B 82 GLU B 98 1 17
HELIX 26 AC8 SER B 104 PHE B 120 1 17
HELIX 27 AC9 ARG B 131 MET B 146 1 16
HELIX 28 AD1 PRO B 155 GLY B 167 1 13
HELIX 29 AD2 GLN B 168 TYR B 184 1 17
HELIX 30 AD3 ASP B 187 TYR B 192 1 6
HELIX 31 AD4 PRO B 193 GLN B 210 1 18
HELIX 32 AD5 ALA B 213 GLU B 219 1 7
HELIX 33 AD6 ASP B 223 PHE B 244 1 22
HELIX 34 AD7 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 GLY A 30 -1 N VAL A 27 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 PHE A 97 N ALA A 50
SHEET 5 AA2 5 LEU A 81 SER A 87 -1 N GLN A 82 O LEU A 96
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 -2.75
SITE 1 AC1 14 VAL A 27 TYR A 32 VAL A 35 ALA A 50
SITE 2 AC1 14 LYS A 52 PHE A 97 ASP A 98 ALA A 100
SITE 3 AC1 14 ASP A 103 HIS A 106 ALA A 155 LEU A 158
SITE 4 AC1 14 ARG A 356 HOH A 511
SITE 1 AC2 3 LYS A 83 VAL A 84 ASP B 147
SITE 1 AC3 2 ALA B 0 ARG B 157
CRYST1 70.749 71.282 171.953 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 0.014134 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014029 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005816 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
