HEADER TRANSCRIPTION/TRANSFERASE/INHIBITOR 06-JUL-15 5CEI
TITLE CRYSTAL STRUCTURE OF CDK8:CYCLIN C COMPLEX WITH COMPOUND 22
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: CYCLIN-DEPENDENT KINASE 8;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-403;
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_TAXID: 7108;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: CCNC;
SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE, INHIBITOR, CDK8, CYCLIN DEPENDENT KINASE, CYCLIN,
KEYWDS 2 TRANSCRIPTION-TRANSFERASE-INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.KIEFER,E.V.SCHNEIDER,K.MASKOS,M.F.T.KOEHLER
REVDAT 3 06-MAR-24 5CEI 1 REMARK
REVDAT 2 11-MAY-16 5CEI 1 JRNL
REVDAT 1 10-FEB-16 5CEI 0
JRNL AUTH M.F.KOEHLER,P.BERGERON,E.M.BLACKWOOD,K.BOWMAN,K.R.CLARK,
JRNL AUTH 2 R.FIRESTEIN,J.R.KIEFER,K.MASKOS,M.L.MCCLELAND,L.ORREN,
JRNL AUTH 3 L.SALPHATI,S.SCHMIDT,E.V.SCHNEIDER,J.WU,M.H.BERESINI
JRNL TITL DEVELOPMENT OF A POTENT, SPECIFIC CDK8 KINASE INHIBITOR
JRNL TITL 2 WHICH PHENOCOPIES CDK8/19 KNOCKOUT CELLS.
JRNL REF ACS MED.CHEM.LETT. V. 7 223 2016
JRNL REFN ISSN 1948-5875
JRNL PMID 26985305
JRNL DOI 10.1021/ACSMEDCHEMLETT.5B00278
REMARK 2
REMARK 2 RESOLUTION. 2.24 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 2.24
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.84
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 40213
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 : 0.227
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 3.490
REMARK 3 FREE R VALUE TEST SET COUNT : 1402
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 47.8538 - 4.8245 0.95 3980 146 0.1744 0.2224
REMARK 3 2 4.8245 - 3.8299 0.97 3892 157 0.1392 0.1932
REMARK 3 3 3.8299 - 3.3459 0.97 3832 157 0.1544 0.1997
REMARK 3 4 3.3459 - 3.0401 0.98 3898 126 0.1676 0.2265
REMARK 3 5 3.0401 - 2.8222 0.99 3917 137 0.1748 0.2821
REMARK 3 6 2.8222 - 2.6558 0.98 3847 145 0.1889 0.2416
REMARK 3 7 2.6558 - 2.5228 0.99 3857 122 0.1924 0.2640
REMARK 3 8 2.5228 - 2.4130 0.99 3902 145 0.2038 0.2624
REMARK 3 9 2.4130 - 2.3201 1.00 3874 142 0.2275 0.2643
REMARK 3 10 2.3201 - 2.2400 0.97 3812 125 0.2877 0.3143
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 : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.290
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.290
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 36.84
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 48.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
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 : 0.007 5319
REMARK 3 ANGLE : 0.975 7161
REMARK 3 CHIRALITY : 0.038 757
REMARK 3 PLANARITY : 0.005 903
REMARK 3 DIHEDRAL : 13.623 2005
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 126 )
REMARK 3 ORIGIN FOR THE GROUP (A): 4.0553 65.6282 54.9007
REMARK 3 T TENSOR
REMARK 3 T11: 0.4133 T22: 0.2929
REMARK 3 T33: 0.3488 T12: 0.0046
REMARK 3 T13: -0.0329 T23: 0.0584
REMARK 3 L TENSOR
REMARK 3 L11: 0.4773 L22: 2.1091
REMARK 3 L33: 0.8962 L12: -0.5999
REMARK 3 L13: -0.2346 L23: 0.9574
REMARK 3 S TENSOR
REMARK 3 S11: 0.1553 S12: 0.2329 S13: 0.1097
REMARK 3 S21: -0.3338 S22: -0.1691 S23: 0.1572
REMARK 3 S31: -0.1700 S32: -0.1127 S33: 0.0035
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 127 THROUGH 362 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7158 39.6219 57.5180
REMARK 3 T TENSOR
REMARK 3 T11: 0.2476 T22: 0.2607
REMARK 3 T33: 0.2476 T12: 0.0159
REMARK 3 T13: -0.0285 T23: 0.0100
REMARK 3 L TENSOR
REMARK 3 L11: 1.8388 L22: 2.1767
REMARK 3 L33: 1.3483 L12: 0.3439
REMARK 3 L13: -0.2458 L23: -0.0550
REMARK 3 S TENSOR
REMARK 3 S11: -0.0060 S12: 0.1758 S13: -0.0566
REMARK 3 S21: -0.0603 S22: 0.0536 S23: 0.1284
REMARK 3 S31: 0.0384 S32: -0.0708 S33: -0.0547
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B' AND (RESID -3 THROUGH 17 )
REMARK 3 ORIGIN FOR THE GROUP (A): 9.7048 64.2591 78.3370
REMARK 3 T TENSOR
REMARK 3 T11: 0.2613 T22: 0.3498
REMARK 3 T33: 0.2803 T12: -0.0541
REMARK 3 T13: 0.0724 T23: -0.0112
REMARK 3 L TENSOR
REMARK 3 L11: 2.6788 L22: 8.3020
REMARK 3 L33: 4.3964 L12: -2.3883
REMARK 3 L13: -0.2761 L23: 1.2535
REMARK 3 S TENSOR
REMARK 3 S11: 0.1232 S12: 0.0052 S13: 0.2004
REMARK 3 S21: -0.3629 S22: 0.0649 S23: -0.0535
REMARK 3 S31: 0.1735 S32: 0.5206 S33: -0.1684
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 18 THROUGH 54 )
REMARK 3 ORIGIN FOR THE GROUP (A): -5.3998 78.5175 87.7440
REMARK 3 T TENSOR
REMARK 3 T11: 0.2945 T22: 0.2683
REMARK 3 T33: 0.3322 T12: -0.0292
REMARK 3 T13: 0.0665 T23: 0.0143
REMARK 3 L TENSOR
REMARK 3 L11: 2.7990 L22: 3.4194
REMARK 3 L33: 2.1121 L12: 0.1609
REMARK 3 L13: 0.0692 L23: 0.5767
REMARK 3 S TENSOR
REMARK 3 S11: -0.1604 S12: -0.0456 S13: 0.3715
REMARK 3 S21: -0.1443 S22: 0.2281 S23: -0.1676
REMARK 3 S31: -0.3339 S32: 0.1604 S33: -0.0669
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 55 THROUGH 75 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.7123 66.7069 80.7870
REMARK 3 T TENSOR
REMARK 3 T11: 0.2460 T22: 0.2393
REMARK 3 T33: 0.2074 T12: 0.0072
REMARK 3 T13: 0.0393 T23: -0.0050
REMARK 3 L TENSOR
REMARK 3 L11: 4.3582 L22: 4.5776
REMARK 3 L33: 3.1368 L12: 0.8689
REMARK 3 L13: 0.1960 L23: 0.5871
REMARK 3 S TENSOR
REMARK 3 S11: -0.0450 S12: 0.0693 S13: -0.2789
REMARK 3 S21: -0.2192 S22: 0.1019 S23: -0.1935
REMARK 3 S31: 0.2288 S32: 0.1965 S33: -0.0485
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 76 THROUGH 264 )
REMARK 3 ORIGIN FOR THE GROUP (A): -4.0563 67.2481 87.3844
REMARK 3 T TENSOR
REMARK 3 T11: 0.2405 T22: 0.2419
REMARK 3 T33: 0.3038 T12: -0.0385
REMARK 3 T13: 0.0299 T23: -0.0126
REMARK 3 L TENSOR
REMARK 3 L11: 1.3834 L22: 1.3419
REMARK 3 L33: 2.3201 L12: -0.4417
REMARK 3 L13: -0.2862 L23: -0.3424
REMARK 3 S TENSOR
REMARK 3 S11: 0.0651 S12: -0.0617 S13: 0.0435
REMARK 3 S21: -0.0651 S22: 0.0098 S23: 0.0289
REMARK 3 S31: -0.0125 S32: 0.0579 S33: -0.0821
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 5CEI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211481.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-FEB-12
REMARK 200 TEMPERATURE (KELVIN) : 93
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 : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.999996
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 : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40329
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.240
REMARK 200 RESOLUTION RANGE LOW (A) : 47.843
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.6
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.44900
REMARK 200 R SYM FOR SHELL (I) : 0.44900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.37
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350 AND 0.20 M SODIUM
REMARK 280 FORMATE, 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 35.56400
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.72400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 35.04500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 83.72400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.56400
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 35.04500
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6120 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28930 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 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 ASP A -2
REMARK 465 ASP A -1
REMARK 465 ASN A 117
REMARK 465 LYS A 118
REMARK 465 LYS A 119
REMARK 465 PRO A 120
REMARK 465 VAL A 121
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 ASP A 240
REMARK 465 ILE A 241
REMARK 465 LYS A 242
REMARK 465 THR A 243
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 115 CG CD CE NZ
REMARK 470 GLU A 357 CG CD OE1 OE2
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 LYS A 6 CD CE NZ
REMARK 480 ARG A 15 NE CZ NH1 NH2
REMARK 480 GLU A 23 CG CD OE1 OE2
REMARK 480 ARG A 29 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 39 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 47 NZ
REMARK 480 ILE A 59 CD1
REMARK 480 LYS A 74 CG CD CE NZ
REMARK 480 LYS A 83 CE NZ
REMARK 480 LYS A 109 CE NZ
REMARK 480 ARG A 112 CZ NH1 NH2
REMARK 480 GLN A 122 CD OE1 NE2
REMARK 480 LEU A 123 CG CD1 CD2
REMARK 480 ARG A 125 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 185 NZ
REMARK 480 ARG A 237 CZ NH1 NH2
REMARK 480 GLN A 238 CG CD OE1 NE2
REMARK 480 SER A 244 OG
REMARK 480 LYS A 265 CD CE NZ
REMARK 480 LYS A 271 CG CD CE NZ
REMARK 480 LYS A 272 CE NZ
REMARK 480 LYS A 281 CD CE NZ
REMARK 480 ARG A 284 CZ NH1 NH2
REMARK 480 LYS A 295 CE NZ
REMARK 480 LYS A 301 CD CE NZ
REMARK 480 LYS A 303 CE NZ
REMARK 480 GLN A 350 CG CD OE1 NE2
REMARK 480 LYS A 355 CD CE NZ
REMARK 480 ASP B -3 CG OD1 OD2
REMARK 480 LYS B -1 CG CD CE NZ
REMARK 480 LYS B 18 NZ
REMARK 480 LEU B 22 CD1 CD2
REMARK 480 LYS B 23 CG CD CE NZ
REMARK 480 LYS B 27 CE NZ
REMARK 480 LYS B 30 CD CE NZ
REMARK 480 LYS B 56 CD CE NZ
REMARK 480 GLN B 60 CD OE1 NE2
REMARK 480 LYS B 79 CE NZ
REMARK 480 VAL B 102 CG1 CG2
REMARK 480 LYS B 117 CD CE NZ
REMARK 480 LYS B 126 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 GLU B 137 CD OE1 OE2
REMARK 480 GLN B 164 CD OE1 NE2
REMARK 480 GLU B 169 CD OE1 OE2
REMARK 480 MET B 171 CE
REMARK 480 GLN B 210 CD OE1 NE2
REMARK 480 LYS B 211 CD CE NZ
REMARK 480 GLN B 215 CD OE1 NE2
REMARK 480 SER B 221 OG
REMARK 480 GLU B 225 CG CD OE1 OE2
REMARK 480 LYS B 226 CE NZ
REMARK 480 LYS B 236 CD CE NZ
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O2 EDO B 307 O HOH B 401 2.13
REMARK 500
REMARK 500 REMARK: NULL
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 7.10 -152.09
REMARK 500 ASP A 46 29.59 44.46
REMARK 500 ASP A 151 39.68 -153.63
REMARK 500 LEU A 316 55.54 -90.76
REMARK 500 SER B 221 76.08 -106.34
REMARK 500 ASP B 223 97.82 -64.52
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLN A 238 GLU A 239 145.19
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 A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 50R A 508
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 509
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue FMT B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 307
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4G6L RELATED DB: PDB
DBREF 5CEI A 1 403 UNP P49336 CDK8_HUMAN 1 403
DBREF 5CEI B 1 283 UNP P24863 CCNC_HUMAN 1 283
SEQADV 5CEI ASP A -2 UNP P49336 EXPRESSION TAG
SEQADV 5CEI ASP A -1 UNP P49336 EXPRESSION TAG
SEQADV 5CEI LYS A 0 UNP P49336 EXPRESSION TAG
SEQADV 5CEI ASP B -3 UNP P24863 EXPRESSION TAG
SEQADV 5CEI ASP B -2 UNP P24863 EXPRESSION TAG
SEQADV 5CEI LYS B -1 UNP P24863 EXPRESSION TAG
SEQADV 5CEI ALA B 0 UNP P24863 EXPRESSION TAG
SEQRES 1 A 406 ASP ASP LYS MET ASP TYR ASP PHE LYS VAL LYS LEU SER
SEQRES 2 A 406 SER GLU ARG GLU ARG VAL GLU ASP LEU PHE GLU TYR GLU
SEQRES 3 A 406 GLY CYS LYS VAL GLY ARG GLY THR TYR GLY HIS VAL TYR
SEQRES 4 A 406 LYS ALA LYS ARG LYS ASP GLY LYS ASP ASP LYS ASP TYR
SEQRES 5 A 406 ALA LEU LYS GLN ILE GLU GLY THR GLY ILE SER MET SER
SEQRES 6 A 406 ALA CYS ARG GLU ILE ALA LEU LEU ARG GLU LEU LYS HIS
SEQRES 7 A 406 PRO ASN VAL ILE SER LEU GLN LYS VAL PHE LEU SER HIS
SEQRES 8 A 406 ALA ASP ARG LYS VAL TRP LEU LEU PHE ASP TYR ALA GLU
SEQRES 9 A 406 HIS ASP LEU TRP HIS ILE ILE LYS PHE HIS ARG ALA SER
SEQRES 10 A 406 LYS ALA ASN LYS LYS PRO VAL GLN LEU PRO ARG GLY MET
SEQRES 11 A 406 VAL LYS SER LEU LEU TYR GLN ILE LEU ASP GLY ILE HIS
SEQRES 12 A 406 TYR LEU HIS ALA ASN TRP VAL LEU HIS ARG ASP LEU LYS
SEQRES 13 A 406 PRO ALA ASN ILE LEU VAL MET GLY GLU GLY PRO GLU ARG
SEQRES 14 A 406 GLY ARG VAL LYS ILE ALA ASP MET GLY PHE ALA ARG LEU
SEQRES 15 A 406 PHE ASN SER PRO LEU LYS PRO LEU ALA ASP LEU ASP PRO
SEQRES 16 A 406 VAL VAL VAL THR PHE TRP TYR ARG ALA PRO GLU LEU LEU
SEQRES 17 A 406 LEU GLY ALA ARG HIS TYR THR LYS ALA ILE ASP ILE TRP
SEQRES 18 A 406 ALA ILE GLY CYS ILE PHE ALA GLU LEU LEU THR SER GLU
SEQRES 19 A 406 PRO ILE PHE HIS CYS ARG GLN GLU ASP ILE LYS THR SER
SEQRES 20 A 406 ASN PRO TYR HIS HIS ASP GLN LEU ASP ARG ILE PHE ASN
SEQRES 21 A 406 VAL MET GLY PHE PRO ALA ASP LYS ASP TRP GLU ASP ILE
SEQRES 22 A 406 LYS LYS MET PRO GLU HIS SER THR LEU MET LYS ASP PHE
SEQRES 23 A 406 ARG ARG ASN THR TYR THR ASN CYS SER LEU ILE LYS TYR
SEQRES 24 A 406 MET GLU LYS HIS LYS VAL LYS PRO ASP SER LYS ALA PHE
SEQRES 25 A 406 HIS LEU LEU GLN LYS LEU LEU THR MET ASP PRO ILE LYS
SEQRES 26 A 406 ARG ILE THR SER GLU GLN ALA MET GLN ASP PRO TYR PHE
SEQRES 27 A 406 LEU GLU ASP PRO LEU PRO THR SER ASP VAL PHE ALA GLY
SEQRES 28 A 406 CYS GLN ILE PRO TYR PRO LYS ARG GLU PHE LEU THR GLU
SEQRES 29 A 406 GLU GLU PRO ASP ASP LYS GLY ASP LYS LYS ASN GLN GLN
SEQRES 30 A 406 GLN GLN GLN GLY ASN ASN HIS THR ASN GLY THR GLY HIS
SEQRES 31 A 406 PRO GLY ASN GLN ASP SER SER HIS THR GLN GLY PRO PRO
SEQRES 32 A 406 LEU LYS LYS
SEQRES 1 B 287 ASP ASP LYS ALA MET ALA GLY ASN PHE TRP GLN SER SER
SEQRES 2 B 287 HIS TYR LEU GLN TRP ILE LEU ASP LYS GLN ASP LEU LEU
SEQRES 3 B 287 LYS GLU ARG GLN LYS ASP LEU LYS PHE LEU SER GLU GLU
SEQRES 4 B 287 GLU TYR TRP LYS LEU GLN ILE PHE PHE THR ASN VAL ILE
SEQRES 5 B 287 GLN ALA LEU GLY GLU HIS LEU LYS LEU ARG GLN GLN VAL
SEQRES 6 B 287 ILE ALA THR ALA THR VAL TYR PHE LYS ARG PHE TYR ALA
SEQRES 7 B 287 ARG TYR SER LEU LYS SER ILE ASP PRO VAL LEU MET ALA
SEQRES 8 B 287 PRO THR CYS VAL PHE LEU ALA SER LYS VAL GLU GLU PHE
SEQRES 9 B 287 GLY VAL VAL SER ASN THR ARG LEU ILE ALA ALA ALA THR
SEQRES 10 B 287 SER VAL LEU LYS THR ARG PHE SER TYR ALA PHE PRO LYS
SEQRES 11 B 287 GLU PHE PRO TYR ARG MET ASN HIS ILE LEU GLU CYS GLU
SEQRES 12 B 287 PHE TYR LEU LEU GLU LEU MET ASP CYS CYS LEU ILE VAL
SEQRES 13 B 287 TYR HIS PRO TYR ARG PRO LEU LEU GLN TYR VAL GLN ASP
SEQRES 14 B 287 MET GLY GLN GLU ASP MET LEU LEU PRO LEU ALA TRP ARG
SEQRES 15 B 287 ILE VAL ASN ASP THR TYR ARG THR ASP LEU CYS LEU LEU
SEQRES 16 B 287 TYR PRO PRO PHE MET ILE ALA LEU ALA CYS LEU HIS VAL
SEQRES 17 B 287 ALA CYS VAL VAL GLN GLN LYS ASP ALA ARG GLN TRP PHE
SEQRES 18 B 287 ALA GLU LEU SER VAL ASP MET GLU LYS ILE LEU GLU ILE
SEQRES 19 B 287 ILE ARG VAL ILE LEU LYS LEU TYR GLU GLN TRP LYS ASN
SEQRES 20 B 287 PHE ASP GLU ARG LYS GLU MET ALA THR ILE LEU SER LYS
SEQRES 21 B 287 MET PRO LYS PRO LYS PRO PRO PRO ASN SER GLU GLY GLU
SEQRES 22 B 287 GLN GLY PRO ASN GLY SER GLN ASN SER SER TYR SER GLN
SEQRES 23 B 287 SER
HET EDO A 501 4
HET EDO A 502 4
HET EDO A 503 4
HET EDO A 504 4
HET FMT A 505 3
HET FMT A 506 3
HET FMT A 507 3
HET 50R A 508 21
HET EDO A 509 4
HET EDO B 301 4
HET EDO B 302 4
HET FMT B 303 3
HET FMT B 304 3
HET FMT B 305 3
HET FMT B 306 3
HET EDO B 307 4
HETNAM EDO 1,2-ETHANEDIOL
HETNAM FMT FORMIC ACID
HETNAM 50R 4-(4-IODOPHENOXY)-N-METHYLTHIENO[2,3-C]PYRIDINE-2-
HETNAM 2 50R CARBOXAMIDE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 EDO 8(C2 H6 O2)
FORMUL 7 FMT 7(C H2 O2)
FORMUL 10 50R C15 H11 I N2 O2 S
FORMUL 19 HOH *180(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 SER A 114 1 11
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 ILE B 15 1 8
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 LEU B 55 1 23
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 209 1 17
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 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 ASP A 48 ILE A 54 -1 O LEU A 51 N TYR A 36
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 -1.62
SITE 1 AC1 4 ARG A 71 GLU A 72 SER B 9 GLN B 13
SITE 1 AC2 1 TYR A 141
SITE 1 AC3 6 GLU A 17 PHE A 20 GLU A 21 TYR A 22
SITE 2 AC3 6 GLU A 23 LYS A 41
SITE 1 AC4 3 LYS A 301 VAL A 302 LYS A 303
SITE 1 AC5 5 LYS A 52 GLU A 66 ALA A 172 ASP A 173
SITE 2 AC5 5 50R A 508
SITE 1 AC6 3 GLU A 165 ARG A 166 ARG A 168
SITE 1 AC7 2 ARG A 168 SER A 343
SITE 1 AC8 15 VAL A 27 TYR A 32 VAL A 35 ALA A 50
SITE 2 AC8 15 LYS A 52 ILE A 79 TYR A 99 ALA A 100
SITE 3 AC8 15 ASP A 103 ALA A 155 LEU A 158 ASP A 173
SITE 4 AC8 15 ARG A 356 FMT A 505 HOH A 668
SITE 1 AC9 4 ASP A 305 HIS A 310 LYS B 242 ASN B 243
SITE 1 AD1 1 HOH B 414
SITE 1 AD2 4 GLU B 35 GLU B 239 GLN B 240 ASN B 243
SITE 1 AD3 4 ALA B 0 ALA B 2 VAL B 152 ARG B 157
SITE 1 AD4 4 PHE B 31 SER B 255 LYS B 256 MET B 257
SITE 1 AD5 2 ARG B 58 GLN B 59
SITE 1 AD6 2 LEU B 57 GLN B 59
SITE 1 AD7 6 ILE B 42 ASN B 46 TRP B 241 PHE B 244
SITE 2 AD7 6 GLU B 246 HOH B 401
CRYST1 71.128 70.090 167.448 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 0.014059 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014267 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005972 0.00000
(ATOM LINES ARE NOT SHOWN.)
END