HEADER TRANSFERASE/TRANSFERASE INHIBITOR 16-AUG-10 3OG7
TITLE B-RAF KINASE V600E ONCOGENIC MUTANT IN COMPLEX WITH PLX4032
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: AKAP9-BRAF FUSION PROTEIN;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 1175-1446);
COMPND 5 SYNONYM: PROTO-ONCOGENE B-RAF, P94, V-RAF MURINE SARCOMA VIRAL
COMPND 6 ONCOGENE HOMOLOG B1;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 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: BRAF, BRAF1, RAFB1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS B-RAF, BRAF, PROTO-ONCOGENE, V600E, KINASE, TRANSFERASE, TRANSFERASE-
KEYWDS 2 TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.ZHANG,K.Y.ZHANG,C.ZHANG
REVDAT 5 21-FEB-24 3OG7 1 REMARK SEQADV HETSYN
REVDAT 4 02-MAY-18 3OG7 1 HEADER KEYWDS
REVDAT 3 25-OCT-17 3OG7 1 HETSYN
REVDAT 2 06-OCT-10 3OG7 1 JRNL
REVDAT 1 22-SEP-10 3OG7 0
JRNL AUTH G.BOLLAG,P.HIRTH,J.TSAI,J.ZHANG,P.N.IBRAHIM,H.CHO,W.SPEVAK,
JRNL AUTH 2 C.ZHANG,Y.ZHANG,G.HABETS,E.A.BURTON,B.WONG,G.TSANG,B.L.WEST,
JRNL AUTH 3 B.POWELL,R.SHELLOOE,A.MARIMUTHU,H.NGUYEN,K.Y.ZHANG,
JRNL AUTH 4 D.R.ARTIS,J.SCHLESSINGER,F.SU,B.HIGGINS,R.IYER,K.D'ANDREA,
JRNL AUTH 5 A.KOEHLER,M.STUMM,P.S.LIN,R.J.LEE,J.GRIPPO,I.PUZANOV,
JRNL AUTH 6 K.B.KIM,A.RIBAS,G.A.MCARTHUR,J.A.SOSMAN,P.B.CHAPMAN,
JRNL AUTH 7 K.T.FLAHERTY,X.XU,K.L.NATHANSON,K.NOLOP
JRNL TITL CLINICAL EFFICACY OF A RAF INHIBITOR NEEDS BROAD TARGET
JRNL TITL 2 BLOCKADE IN BRAF-MUTANT MELANOMA.
JRNL REF NATURE V. 467 596 2010
JRNL REFN ISSN 0028-0836
JRNL PMID 20823850
JRNL DOI 10.1038/NATURE09454
REMARK 2
REMARK 2 RESOLUTION. 2.45 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.5_2
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 : TWIN_LSQ_F
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 21.30
REMARK 3 MIN(FOBS/SIGMA_FOBS) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 21223
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.214
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.190
REMARK 3 FREE R VALUE TEST SET COUNT : 1146
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 21.2756 - 4.8839 0.94 2744 156 0.1766 0.2014
REMARK 3 2 4.8839 - 3.8842 0.95 2646 129 0.1679 0.2228
REMARK 3 3 3.8842 - 3.3955 0.95 2639 130 0.2012 0.2405
REMARK 3 4 3.3955 - 3.0861 0.95 2615 142 0.2319 0.2977
REMARK 3 5 3.0861 - 2.8654 0.95 2581 142 0.2690 0.3498
REMARK 3 6 2.8654 - 2.6968 0.95 2581 137 0.2837 0.3466
REMARK 3 7 2.6968 - 2.5620 0.95 2602 129 0.3023 0.3415
REMARK 3 8 2.5620 - 2.4507 0.94 2570 142 0.3323 0.3173
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 : 0.33
REMARK 3 B_SOL : 47.40
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : NULL
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 65.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 24.09380
REMARK 3 B22 (A**2) : -6.25230
REMARK 3 B33 (A**2) : -17.84150
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: 0.0860
REMARK 3 OPERATOR: -H,L,K
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.003 4119
REMARK 3 ANGLE : 0.649 5553
REMARK 3 CHIRALITY : 0.048 600
REMARK 3 PLANARITY : 0.004 707
REMARK 3 DIHEDRAL : 16.634 1535
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A
REMARK 3 ORIGIN FOR THE GROUP (A): -1.3512 -12.8290 -19.0118
REMARK 3 T TENSOR
REMARK 3 T11: 0.2830 T22: 0.1799
REMARK 3 T33: 0.1414 T12: 0.0279
REMARK 3 T13: 0.0065 T23: -0.0149
REMARK 3 L TENSOR
REMARK 3 L11: 0.4271 L22: 0.5813
REMARK 3 L33: 0.3905 L12: 0.2092
REMARK 3 L13: 0.1909 L23: 0.5345
REMARK 3 S TENSOR
REMARK 3 S11: 0.0295 S12: 0.1294 S13: 0.0517
REMARK 3 S21: 0.4450 S22: 0.0815 S23: 0.0308
REMARK 3 S31: 0.2817 S32: 0.0987 S33: -0.0896
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN B
REMARK 3 ORIGIN FOR THE GROUP (A): 1.4917 8.6212 6.0490
REMARK 3 T TENSOR
REMARK 3 T11: -0.0793 T22: 0.1906
REMARK 3 T33: 0.0369 T12: 0.0770
REMARK 3 T13: 0.1264 T23: -0.0440
REMARK 3 L TENSOR
REMARK 3 L11: 0.9070 L22: -0.0294
REMARK 3 L33: 1.4032 L12: 0.0673
REMARK 3 L13: -0.0545 L23: 0.1136
REMARK 3 S TENSOR
REMARK 3 S11: -0.0650 S12: -0.0999 S13: 0.5313
REMARK 3 S21: 0.1643 S22: -0.0917 S23: -0.0431
REMARK 3 S31: 0.6296 S32: 0.1890 S33: 0.1035
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN L AND RESSEQ 1:1
REMARK 3 ORIGIN FOR THE GROUP (A): 1.8508 -2.7808 -20.0870
REMARK 3 T TENSOR
REMARK 3 T11: 0.2232 T22: 0.2843
REMARK 3 T33: 0.2448 T12: 0.0830
REMARK 3 T13: 0.0676 T23: 0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 0.3324 L22: 0.2201
REMARK 3 L33: 0.0130 L12: 0.0881
REMARK 3 L13: 0.0256 L23: 0.0536
REMARK 3 S TENSOR
REMARK 3 S11: 0.0039 S12: -0.0108 S13: 0.0148
REMARK 3 S21: -0.0181 S22: -0.0394 S23: 0.0296
REMARK 3 S31: 0.0173 S32: 0.0067 S33: 0.0485
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 3OG7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-10.
REMARK 100 THE DEPOSITION ID IS D_1000061075.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 28-MAR-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM 3.3.15
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.15
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 22230
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.450
REMARK 200 RESOLUTION RANGE LOW (A) : 110.128
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.07200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.58
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 4.50
REMARK 200 R MERGE FOR SHELL (I) : 0.52400
REMARK 200 R SYM FOR SHELL (I) : 0.52400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 47.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BISTRIS AT PH 6.0, 12.5% 2,5
REMARK 280 -HEXANEDIOL, AND 12% PEG3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
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 25.38500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 55.06400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 52.21200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 55.06400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 25.38500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 52.21200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 MET A 432
REMARK 465 LYS A 433
REMARK 465 LYS A 434
REMARK 465 GLY A 435
REMARK 465 HIS A 436
REMARK 465 HIS A 437
REMARK 465 HIS A 438
REMARK 465 HIS A 439
REMARK 465 HIS A 440
REMARK 465 HIS A 441
REMARK 465 GLY A 442
REMARK 465 SER A 443
REMARK 465 ARG A 444
REMARK 465 ASP A 445
REMARK 465 ALA A 446
REMARK 465 ALA A 447
REMARK 465 ASP A 448
REMARK 465 GLU A 545
REMARK 465 THR A 546
REMARK 465 LYS A 547
REMARK 465 LEU A 597
REMARK 465 ALA A 598
REMARK 465 THR A 599
REMARK 465 GLU A 600
REMARK 465 LYS A 601
REMARK 465 SER A 602
REMARK 465 ARG A 603
REMARK 465 TRP A 604
REMARK 465 SER A 605
REMARK 465 GLY A 606
REMARK 465 SER A 607
REMARK 465 HIS A 608
REMARK 465 GLN A 609
REMARK 465 PHE A 610
REMARK 465 GLU A 611
REMARK 465 GLN A 612
REMARK 465 LEU A 613
REMARK 465 SER A 614
REMARK 465 MET A 627
REMARK 465 GLN A 628
REMARK 465 ASP A 629
REMARK 465 SER A 630
REMARK 465 MET B 432
REMARK 465 LYS B 433
REMARK 465 LYS B 434
REMARK 465 GLY B 435
REMARK 465 HIS B 436
REMARK 465 HIS B 437
REMARK 465 HIS B 438
REMARK 465 HIS B 439
REMARK 465 HIS B 440
REMARK 465 HIS B 441
REMARK 465 GLY B 442
REMARK 465 SER B 443
REMARK 465 ARG B 444
REMARK 465 ASP B 445
REMARK 465 ALA B 446
REMARK 465 ALA B 447
REMARK 465 ASP B 448
REMARK 465 LYS B 601
REMARK 465 SER B 602
REMARK 465 ARG B 603
REMARK 465 TRP B 604
REMARK 465 SER B 605
REMARK 465 GLY B 606
REMARK 465 SER B 607
REMARK 465 HIS B 608
REMARK 465 GLN B 609
REMARK 465 PHE B 610
REMARK 465 GLU B 611
REMARK 465 GLN B 612
REMARK 465 LEU B 613
REMARK 465 SER B 614
REMARK 465 MET B 627
REMARK 465 GLN B 628
REMARK 465 ASP B 629
REMARK 465 SER B 630
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 PRO A 453 151.21 -47.95
REMARK 500 ARG A 575 -15.01 78.91
REMARK 500 ASP A 576 55.71 -154.93
REMARK 500 ASN A 660 56.53 -91.77
REMARK 500 ASN A 684 36.26 -75.66
REMARK 500 TRP B 476 92.18 -160.90
REMARK 500 THR B 521 -59.15 -129.61
REMARK 500 ALA B 522 21.78 -74.49
REMARK 500 PRO B 523 -87.45 -114.92
REMARK 500 ALA B 543 30.14 -91.55
REMARK 500 ASP B 576 38.22 -154.00
REMARK 500 ASP B 587 -15.42 76.91
REMARK 500 PHE B 595 -84.66 -52.94
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 ALA B 522 PRO B 523 143.03
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 032 A 1
DBREF 3OG7 A 449 720 UNP Q5IBP5 Q5IBP5_HUMAN 1175 1446
DBREF 3OG7 B 449 720 UNP Q5IBP5 Q5IBP5_HUMAN 1175 1446
SEQADV 3OG7 MET A 432 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 LYS A 433 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 LYS A 434 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 GLY A 435 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS A 436 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS A 437 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS A 438 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS A 439 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS A 440 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS A 441 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 GLY A 442 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 SER A 443 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ARG A 444 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ASP A 445 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ALA A 446 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ALA A 447 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ASP A 448 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ALA A 522 UNP Q5IBP5 LYS 1248 ENGINEERED MUTATION
SEQADV 3OG7 ALA A 543 UNP Q5IBP5 ILE 1269 ENGINEERED MUTATION
SEQADV 3OG7 SER A 544 UNP Q5IBP5 ILE 1270 ENGINEERED MUTATION
SEQADV 3OG7 LYS A 551 UNP Q5IBP5 ILE 1277 ENGINEERED MUTATION
SEQADV 3OG7 ARG A 562 UNP Q5IBP5 GLN 1288 ENGINEERED MUTATION
SEQADV 3OG7 ASN A 588 UNP Q5IBP5 LEU 1314 ENGINEERED MUTATION
SEQADV 3OG7 GLU A 600 UNP Q5IBP5 VAL 1326 VARIANT
SEQADV 3OG7 SER A 630 UNP Q5IBP5 LYS 1356 ENGINEERED MUTATION
SEQADV 3OG7 GLU A 667 UNP Q5IBP5 PHE 1393 ENGINEERED MUTATION
SEQADV 3OG7 SER A 673 UNP Q5IBP5 TYR 1399 ENGINEERED MUTATION
SEQADV 3OG7 ARG A 688 UNP Q5IBP5 ALA 1414 ENGINEERED MUTATION
SEQADV 3OG7 SER A 706 UNP Q5IBP5 LEU 1432 ENGINEERED MUTATION
SEQADV 3OG7 ARG A 709 UNP Q5IBP5 GLN 1435 ENGINEERED MUTATION
SEQADV 3OG7 GLU A 713 UNP Q5IBP5 SER 1439 ENGINEERED MUTATION
SEQADV 3OG7 GLU A 716 UNP Q5IBP5 LEU 1442 ENGINEERED MUTATION
SEQADV 3OG7 GLU A 720 UNP Q5IBP5 SER 1446 ENGINEERED MUTATION
SEQADV 3OG7 MET B 432 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 LYS B 433 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 LYS B 434 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 GLY B 435 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS B 436 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS B 437 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS B 438 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS B 439 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS B 440 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 HIS B 441 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 GLY B 442 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 SER B 443 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ARG B 444 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ASP B 445 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ALA B 446 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ALA B 447 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ASP B 448 UNP Q5IBP5 EXPRESSION TAG
SEQADV 3OG7 ALA B 522 UNP Q5IBP5 LYS 1248 ENGINEERED MUTATION
SEQADV 3OG7 ALA B 543 UNP Q5IBP5 ILE 1269 ENGINEERED MUTATION
SEQADV 3OG7 SER B 544 UNP Q5IBP5 ILE 1270 ENGINEERED MUTATION
SEQADV 3OG7 LYS B 551 UNP Q5IBP5 ILE 1277 ENGINEERED MUTATION
SEQADV 3OG7 ARG B 562 UNP Q5IBP5 GLN 1288 ENGINEERED MUTATION
SEQADV 3OG7 ASN B 588 UNP Q5IBP5 LEU 1314 ENGINEERED MUTATION
SEQADV 3OG7 GLU B 600 UNP Q5IBP5 VAL 1326 VARIANT
SEQADV 3OG7 SER B 630 UNP Q5IBP5 LYS 1356 ENGINEERED MUTATION
SEQADV 3OG7 GLU B 667 UNP Q5IBP5 PHE 1393 ENGINEERED MUTATION
SEQADV 3OG7 SER B 673 UNP Q5IBP5 TYR 1399 ENGINEERED MUTATION
SEQADV 3OG7 ARG B 688 UNP Q5IBP5 ALA 1414 ENGINEERED MUTATION
SEQADV 3OG7 SER B 706 UNP Q5IBP5 LEU 1432 ENGINEERED MUTATION
SEQADV 3OG7 ARG B 709 UNP Q5IBP5 GLN 1435 ENGINEERED MUTATION
SEQADV 3OG7 GLU B 713 UNP Q5IBP5 SER 1439 ENGINEERED MUTATION
SEQADV 3OG7 GLU B 716 UNP Q5IBP5 LEU 1442 ENGINEERED MUTATION
SEQADV 3OG7 GLU B 720 UNP Q5IBP5 SER 1446 ENGINEERED MUTATION
SEQRES 1 A 289 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY SER ARG
SEQRES 2 A 289 ASP ALA ALA ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE
SEQRES 3 A 289 THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR
SEQRES 4 A 289 VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS
SEQRES 5 A 289 MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN
SEQRES 6 A 289 ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG
SEQRES 7 A 289 HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR ALA
SEQRES 8 A 289 PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER
SEQRES 9 A 289 SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS PHE
SEQRES 10 A 289 GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR ALA
SEQRES 11 A 289 ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS
SEQRES 12 A 289 ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP
SEQRES 13 A 289 ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR GLU
SEQRES 14 A 289 LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU
SEQRES 15 A 289 SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG
SEQRES 16 A 289 MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP VAL
SEQRES 17 A 289 TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY
SEQRES 18 A 289 GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE
SEQRES 19 A 289 ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP LEU
SEQRES 20 A 289 SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS ARG
SEQRES 21 A 289 LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG
SEQRES 22 A 289 PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU LEU
SEQRES 23 A 289 ALA ARG GLU
SEQRES 1 B 289 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY SER ARG
SEQRES 2 B 289 ASP ALA ALA ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE
SEQRES 3 B 289 THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR
SEQRES 4 B 289 VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS
SEQRES 5 B 289 MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN
SEQRES 6 B 289 ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG
SEQRES 7 B 289 HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR ALA
SEQRES 8 B 289 PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER
SEQRES 9 B 289 SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS PHE
SEQRES 10 B 289 GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR ALA
SEQRES 11 B 289 ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS
SEQRES 12 B 289 ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP
SEQRES 13 B 289 ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR GLU
SEQRES 14 B 289 LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU
SEQRES 15 B 289 SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG
SEQRES 16 B 289 MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP VAL
SEQRES 17 B 289 TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY
SEQRES 18 B 289 GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE
SEQRES 19 B 289 ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP LEU
SEQRES 20 B 289 SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS ARG
SEQRES 21 B 289 LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG
SEQRES 22 B 289 PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU LEU
SEQRES 23 B 289 ALA ARG GLU
HET 032 A 1 33
HETNAM 032 N-(3-{[5-(4-CHLOROPHENYL)-1H-PYRROLO[2,3-B]PYRIDIN-3-
HETNAM 2 032 YL]CARBONYL}-2,4-DIFLUOROPHENYL)PROPANE-1-SULFONAMIDE
HETSYN 032 VEMURAFENIB; PLX4032
FORMUL 3 032 C23 H18 CL F2 N3 O3 S
FORMUL 4 HOH *65(H2 O)
HELIX 1 1 THR A 491 ARG A 506 1 16
HELIX 2 2 LEU A 537 HIS A 542 1 6
HELIX 3 3 GLU A 549 LYS A 570 1 22
HELIX 4 4 ALA A 621 ARG A 626 1 6
HELIX 5 5 SER A 634 GLY A 652 1 19
HELIX 6 6 ASN A 661 ARG A 671 1 11
HELIX 7 7 PRO A 686 LEU A 697 1 12
HELIX 8 8 LYS A 700 ARG A 704 5 5
HELIX 9 9 SER A 706 LEU A 717 1 12
HELIX 10 10 THR B 491 ARG B 506 1 16
HELIX 11 11 SER B 536 HIS B 542 1 7
HELIX 12 12 GLU B 549 LYS B 570 1 22
HELIX 13 13 GLU B 586 ASN B 588 5 3
HELIX 14 14 GLY B 615 MET B 620 5 6
HELIX 15 15 ALA B 621 ARG B 626 1 6
HELIX 16 16 SER B 634 GLY B 652 1 19
HELIX 17 17 ASN B 661 GLY B 672 1 12
HELIX 18 18 ASP B 677 VAL B 681 5 5
HELIX 19 19 PRO B 686 LEU B 697 1 12
HELIX 20 20 LYS B 700 ARG B 704 5 5
HELIX 21 21 SER B 706 GLU B 720 1 15
SHEET 1 A 5 THR A 458 SER A 465 0
SHEET 2 A 5 GLY A 469 LYS A 475 -1 O VAL A 471 N ILE A 463
SHEET 3 A 5 ASP A 479 LEU A 485 -1 O VAL A 480 N GLY A 474
SHEET 4 A 5 ALA A 526 GLN A 530 -1 O ILE A 527 N LYS A 483
SHEET 5 A 5 PHE A 516 SER A 520 -1 N GLY A 518 O VAL A 528
SHEET 1 B 3 GLY A 534 SER A 536 0
SHEET 2 B 3 ILE A 582 HIS A 585 -1 O LEU A 584 N SER A 535
SHEET 3 B 3 THR A 589 ILE A 592 -1 O LYS A 591 N PHE A 583
SHEET 1 C 5 THR B 458 SER B 465 0
SHEET 2 C 5 THR B 470 LYS B 475 -1 O LYS B 473 N GLY B 460
SHEET 3 C 5 ASP B 479 LEU B 485 -1 O MET B 484 N THR B 470
SHEET 4 C 5 LEU B 525 GLN B 530 -1 O THR B 529 N ALA B 481
SHEET 5 C 5 PHE B 516 SER B 520 -1 N GLY B 518 O VAL B 528
SHEET 1 D 2 ILE B 582 HIS B 585 0
SHEET 2 D 2 THR B 589 ILE B 592 -1 O THR B 589 N HIS B 585
CISPEP 1 ALA A 522 PRO A 523 0 -0.27
SITE 1 AC1 13 VAL A 471 ALA A 481 LYS A 483 LEU A 505
SITE 2 AC1 13 LEU A 514 THR A 529 GLN A 530 TRP A 531
SITE 3 AC1 13 CYS A 532 PHE A 583 ASP A 594 PHE A 595
SITE 4 AC1 13 GLY A 596
CRYST1 50.770 104.424 110.128 90.00 90.00 90.00 P 21 21 21 8
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 0.019697 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009576 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009080 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
