HEADER TRANSFERASE/TRANSFERASE INHIBITOR 26-JAN-15 4XV9
TITLE B-RAF KINASE DOMAIN IN COMPLEX WITH PLX5568
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE B-RAF;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 444-705;
COMPND 5 SYNONYM: PROTO-ONCOGENE B-RAF,P94,V-RAF MURINE SARCOMA VIRAL ONCOGENE
COMPND 6 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,C.ZHANG,W.WANG
REVDAT 3 28-FEB-24 4XV9 1 JRNL REMARK
REVDAT 2 04-NOV-15 4XV9 1 JRNL
REVDAT 1 28-OCT-15 4XV9 0
JRNL AUTH C.ZHANG,W.SPEVAK,Y.ZHANG,E.A.BURTON,Y.MA,G.HABETS,J.ZHANG,
JRNL AUTH 2 J.LIN,T.EWING,B.MATUSOW,G.TSANG,A.MARIMUTHU,H.CHO,G.WU,
JRNL AUTH 3 W.WANG,D.FONG,H.NGUYEN,S.SHI,P.WOMACK,M.NESPI,R.SHELLOOE,
JRNL AUTH 4 H.CARIAS,B.POWELL,E.LIGHT,L.SANFTNER,J.WALTERS,J.TSAI,
JRNL AUTH 5 B.L.WEST,G.VISOR,H.REZAEI,P.S.LIN,K.NOLOP,P.N.IBRAHIM,
JRNL AUTH 6 P.HIRTH,G.BOLLAG
JRNL TITL RAF INHIBITORS THAT EVADE PARADOXICAL MAPK PATHWAY
JRNL TITL 2 ACTIVATION.
JRNL REF NATURE V. 526 583 2015
JRNL REFN ESSN 1476-4687
JRNL PMID 26466569
JRNL DOI 10.1038/NATURE14982
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.1.25
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 18.63
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 24901
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) : 0.206
REMARK 3 R VALUE (WORKING SET) : 0.205
REMARK 3 FREE R VALUE : 0.238
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1266
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) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1804
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.2230
REMARK 3 BIN FREE R VALUE SET COUNT : 92
REMARK 3 BIN FREE R VALUE : 0.2450
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2079
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 39
REMARK 3 SOLVENT ATOMS : 251
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.42
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.26000
REMARK 3 B22 (A**2) : 0.26000
REMARK 3 B33 (A**2) : -0.51000
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): 0.167
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.151
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.115
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.107
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.921
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2224 ; 0.006 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): 2000 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3016 ; 1.144 ; 1.973
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4666 ; 0.758 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 273 ; 5.008 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 323 ; 0.059 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2476 ; 0.003 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 456 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 472 ; 0.172 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2361 ; 0.205 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): 1245 ; 0.080 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 173 ; 0.119 ; 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): 16 ; 0.113 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 54 ; 0.227 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 28 ; 0.078 ; 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): 1339 ; 0.199 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2169 ; 0.379 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 885 ; 0.625 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 847 ; 1.026 ; 4.500
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 : 3
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1136 A 1151
REMARK 3 ORIGIN FOR THE GROUP (A): 80.4150 21.0410 4.4460
REMARK 3 T TENSOR
REMARK 3 T11: 0.1461 T22: 0.1468
REMARK 3 T33: 0.1479 T12: -0.0001
REMARK 3 T13: 0.0019 T23: -0.0155
REMARK 3 L TENSOR
REMARK 3 L11: 0.8515 L22: 2.3533
REMARK 3 L33: 2.2046 L12: 0.7170
REMARK 3 L13: 0.1118 L23: -1.0284
REMARK 3 S TENSOR
REMARK 3 S11: -0.0368 S12: -0.0313 S13: -0.0705
REMARK 3 S21: -0.0230 S22: 0.0137 S23: 0.0503
REMARK 3 S31: -0.0600 S32: 0.0127 S33: 0.0230
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 12
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 448 A 466
REMARK 3 RESIDUE RANGE : A 467 A 484
REMARK 3 RESIDUE RANGE : A 485 A 534
REMARK 3 RESIDUE RANGE : A 535 A 582
REMARK 3 RESIDUE RANGE : A 583 A 587
REMARK 3 RESIDUE RANGE : A 588 A 597
REMARK 3 RESIDUE RANGE : A 613 A 667
REMARK 3 RESIDUE RANGE : A 668 A 705
REMARK 3 RESIDUE RANGE : A 706 A 721
REMARK 3 RESIDUE RANGE : A 801 A 801
REMARK 3 RESIDUE RANGE : A 802 A 802
REMARK 3 RESIDUE RANGE : A 901 A 1070
REMARK 3 ORIGIN FOR THE GROUP (A): 77.6100 20.2480 0.7820
REMARK 3 T TENSOR
REMARK 3 T11: 0.0448 T22: 0.0011
REMARK 3 T33: 0.0984 T12: -0.0009
REMARK 3 T13: 0.0390 T23: -0.0090
REMARK 3 L TENSOR
REMARK 3 L11: 0.9855 L22: 1.4470
REMARK 3 L33: 2.5082 L12: 0.3691
REMARK 3 L13: -0.2157 L23: -1.0573
REMARK 3 S TENSOR
REMARK 3 S11: -0.0183 S12: 0.1147 S13: -0.1627
REMARK 3 S21: -0.0513 S22: 0.0928 S23: 0.1569
REMARK 3 S31: 0.2080 S32: -0.1813 S33: -0.0745
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 1071 A 1135
REMARK 3 ORIGIN FOR THE GROUP (A): 79.3600 22.5070 3.1830
REMARK 3 T TENSOR
REMARK 3 T11: 0.1394 T22: 0.1403
REMARK 3 T33: 0.2433 T12: -0.0118
REMARK 3 T13: 0.0286 T23: -0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 1.1644 L22: 0.6992
REMARK 3 L33: 2.5131 L12: 0.2779
REMARK 3 L13: 0.1909 L23: -0.1740
REMARK 3 S TENSOR
REMARK 3 S11: -0.0113 S12: 0.1447 S13: -0.0565
REMARK 3 S21: -0.0267 S22: -0.0121 S23: 0.1006
REMARK 3 S31: 0.1915 S32: -0.1412 S33: 0.0233
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 : 1.40
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 4XV9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-15.
REMARK 100 THE DEPOSITION ID IS D_1000206350.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 21-NOV-06
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 : SSRL
REMARK 200 BEAMLINE : BL9-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : SIDE-SCATTERING CUBEROOT I-BEAM
REMARK 200 BENT SINGLE CRYSTAL,ASYMETRIC
REMARK 200 CUT 12.2 DEGS.
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 26185
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 119.523
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 13.60
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 56.16
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES AT PH6.0, 35% (V/V) 2-METHYL-
REMARK 280 2,4-PENTANEDIOL 0.2M LI2SO4, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+3/4
REMARK 290 4555 Y,-X,Z+1/4
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z+1/2
REMARK 290 7555 Y,X,-Z+1/4
REMARK 290 8555 -Y,-X,-Z+3/4
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 26.25350
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 39.38025
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 13.12675
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 26.25350
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 13.12675
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 39.38025
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 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 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 0.000000 -1.000000 0.000000 119.29700
REMARK 350 BIOMT2 2 -1.000000 0.000000 0.000000 119.29700
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -13.12675
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 SER A 446
REMARK 465 SER A 447
REMARK 465 THR A 599
REMARK 465 VAL 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 GLY A 723
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 522 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 ARG A 575 -11.80 81.85
REMARK 500 ASP A 576 41.76 -148.18
REMARK 500 ASP A 587 18.05 56.55
REMARK 500 ASP A 587 19.05 56.55
REMARK 500 ASN A 588 -46.14 -133.39
REMARK 500 ASN A 588 -48.82 -133.40
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1149 DISTANCE = 5.89 ANGSTROMS
REMARK 525 HOH A1150 DISTANCE = 6.19 ANGSTROMS
REMARK 525 HOH A1151 DISTANCE = 6.34 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 1OO A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 802
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4K04 RELATED DB: PDB
REMARK 900 RELATED ID: 4K16 RELATED DB: PDB
REMARK 900 RELATED ID: 4K1A RELATED DB: PDB
DBREF 4XV9 A 442 705 UNP P15056 BRAF_HUMAN 442 705
SEQADV 4XV9 MET A 432 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 LYS A 433 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 LYS A 434 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 GLY A 435 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 HIS A 436 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 HIS A 437 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 HIS A 438 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 HIS A 439 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 HIS A 440 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 HIS A 441 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 SER A 443 UNP P15056 ARG 443 ENGINEERED MUTATION
SEQADV 4XV9 ALA A 543 UNP P15056 ILE 543 ENGINEERED MUTATION
SEQADV 4XV9 SER A 544 UNP P15056 ILE 544 ENGINEERED MUTATION
SEQADV 4XV9 LYS A 551 UNP P15056 ILE 551 ENGINEERED MUTATION
SEQADV 4XV9 ARG A 562 UNP P15056 GLN 562 ENGINEERED MUTATION
SEQADV 4XV9 ASN A 588 UNP P15056 LEU 588 ENGINEERED MUTATION
SEQADV 4XV9 SER A 630 UNP P15056 LYS 630 ENGINEERED MUTATION
SEQADV 4XV9 GLU A 667 UNP P15056 PHE 667 ENGINEERED MUTATION
SEQADV 4XV9 SER A 673 UNP P15056 TYR 673 ENGINEERED MUTATION
SEQADV 4XV9 ARG A 688 UNP P15056 ALA 688 ENGINEERED MUTATION
SEQADV 4XV9 SER A 706 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 PHE A 707 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 PRO A 708 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 ARG A 709 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 ILE A 710 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 LEU A 711 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 ALA A 712 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 GLU A 713 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 ILE A 714 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 GLU A 715 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 GLU A 716 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 LEU A 717 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 ALA A 718 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 ARG A 719 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 GLU A 720 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 LEU A 721 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 SER A 722 UNP P15056 EXPRESSION TAG
SEQADV 4XV9 GLY A 723 UNP P15056 EXPRESSION TAG
SEQRES 1 A 292 MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY SER ARG
SEQRES 2 A 292 ASP SER SER ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE
SEQRES 3 A 292 THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR
SEQRES 4 A 292 VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS
SEQRES 5 A 292 MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN
SEQRES 6 A 292 ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG
SEQRES 7 A 292 HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR LYS
SEQRES 8 A 292 PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER
SEQRES 9 A 292 SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS PHE
SEQRES 10 A 292 GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR ALA
SEQRES 11 A 292 ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS
SEQRES 12 A 292 ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP
SEQRES 13 A 292 ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR VAL
SEQRES 14 A 292 LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU
SEQRES 15 A 292 SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG
SEQRES 16 A 292 MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP VAL
SEQRES 17 A 292 TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY
SEQRES 18 A 292 GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE
SEQRES 19 A 292 ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP LEU
SEQRES 20 A 292 SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS ARG
SEQRES 21 A 292 LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG
SEQRES 22 A 292 PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU LEU
SEQRES 23 A 292 ALA ARG GLU LEU SER GLY
HET 1OO A 801 34
HET SO4 A 802 5
HETNAM 1OO N-{3-[(5-CHLORO-1H-PYRROLO[2,3-B]PYRIDIN-3-YL)
HETNAM 2 1OO CARBONYL]-2,4-DIFLUOROPHENYL}-4-(TRIFLUOROMETHYL)
HETNAM 3 1OO BENZENESULFONAMIDE
HETNAM SO4 SULFATE ION
FORMUL 2 1OO C21 H11 CL F5 N3 O3 S
FORMUL 3 SO4 O4 S 2-
FORMUL 4 HOH *251(H2 O)
HELIX 1 AA1 THR A 491 ARG A 506 1 16
HELIX 2 AA2 SER A 536 ALA A 543 1 8
HELIX 3 AA3 GLU A 549 LYS A 570 1 22
HELIX 4 AA4 LYS A 578 ASN A 580 5 3
HELIX 5 AA5 GLU A 586 ASN A 588 5 3
HELIX 6 AA6 LEU A 613 MET A 620 5 8
HELIX 7 AA7 ALA A 621 MET A 627 1 7
HELIX 8 AA8 SER A 634 GLY A 652 1 19
HELIX 9 AA9 ASN A 661 ARG A 671 1 11
HELIX 10 AB1 ASP A 677 VAL A 681 5 5
HELIX 11 AB2 PRO A 686 LEU A 697 1 12
HELIX 12 AB3 LYS A 700 ARG A 704 5 5
HELIX 13 AB4 SER A 706 SER A 722 1 17
SHEET 1 AA1 5 THR A 458 GLY A 466 0
SHEET 2 AA1 5 GLY A 469 LYS A 475 -1 O LYS A 473 N GLY A 460
SHEET 3 AA1 5 ASP A 479 LEU A 485 -1 O VAL A 480 N GLY A 474
SHEET 4 AA1 5 ALA A 526 GLN A 530 -1 O ILE A 527 N LYS A 483
SHEET 5 AA1 5 PHE A 516 SER A 520 -1 N GLY A 518 O VAL A 528
SHEET 1 AA2 2 ILE A 582 HIS A 585 0
SHEET 2 AA2 2 THR A 589 ILE A 592 -1 O THR A 589 N HIS A 585
CISPEP 1 LYS A 522 PRO A 523 0 4.95
SITE 1 AC1 20 ILE A 463 VAL A 471 ALA A 481 LYS A 483
SITE 2 AC1 20 LEU A 505 ILE A 513 LEU A 514 THR A 529
SITE 3 AC1 20 GLN A 530 TRP A 531 CYS A 532 LEU A 567
SITE 4 AC1 20 HIS A 574 PHE A 583 ILE A 592 ASP A 594
SITE 5 AC1 20 PHE A 595 HOH A 915 HOH A 919 HOH A1008
SITE 1 AC2 4 PRO A 686 LYS A 687 ARG A 688 HOH A 995
CRYST1 119.297 119.297 52.507 90.00 90.00 90.00 P 43 2 2 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 0.008382 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008382 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019045 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
