HEADER TRANSFERASE/TRANSFERASE INHIBITOR 15-DEC-15 5FD2
TITLE B-RAF WILD-TYPE KINASE DOMAIN IN COMPLEX WITH A PURINYLPYRIDINYLAMINO-
TITLE 2 BASED INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE B-RAF;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 433-726;
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 OTHER_DETAILS: KINASE DOMAIN
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: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BTI-TN-5B1-4;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PFASTBAC DUAL
KEYWDS PHOSPHOTRANSFERASE, INHIBITOR, MELANOMA, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.A.WHITTINGTON,L.F.EPSTEIN
REVDAT 2 06-MAR-24 5FD2 1 REMARK
REVDAT 1 04-MAY-16 5FD2 0
JRNL AUTH L.LIU,M.R.LEE,J.L.KIM,D.A.WHITTINGTON,H.BREGMAN,Z.HUA,
JRNL AUTH 2 R.T.LEWIS,M.W.MARTIN,N.NISHIMURA,M.POTASHMAN,K.YANG,S.YI,
JRNL AUTH 3 K.R.VAIDA,L.F.EPSTEIN,C.BABIJ,M.FERNANDO,J.CARNAHAN,
JRNL AUTH 4 M.H.NORMAN
JRNL TITL PURINYLPYRIDINYLAMINO-BASED DFG-IN/ ALPHA C-HELIX-OUT B-RAF
JRNL TITL 2 INHIBITORS: APPLYING MUTANT VERSUS WILD-TYPE B-RAF
JRNL TITL 3 SELECTIVITY INDICES FOR COMPOUND PROFILING.
JRNL REF BIOORG.MED.CHEM. V. 24 2215 2016
JRNL REFN ESSN 1464-3391
JRNL PMID 27085672
JRNL DOI 10.1016/J.BMC.2016.03.055
REMARK 2
REMARK 2 RESOLUTION. 2.89 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 2.89
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 15408
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) : 0.217
REMARK 3 R VALUE (WORKING SET) : 0.213
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.800
REMARK 3 FREE R VALUE TEST SET COUNT : 952
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.89
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.96
REMARK 3 REFLECTION IN BIN (WORKING SET) : 770
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 71.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.3040
REMARK 3 BIN FREE R VALUE SET COUNT : 51
REMARK 3 BIN FREE R VALUE : 0.3720
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3978
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 62
REMARK 3 SOLVENT ATOMS : 32
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 79.30
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.90
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.60000
REMARK 3 B22 (A**2) : -0.39000
REMARK 3 B33 (A**2) : 0.98000
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): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.424
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.294
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.219
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.920
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.856
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4131 ; 0.008 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2821 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5584 ; 1.200 ; 1.974
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6847 ; 0.833 ; 3.001
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 492 ; 5.853 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 180 ;32.659 ;23.667
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 737 ;16.963 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;13.476 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 612 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4493 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 835 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 1 4
REMARK 3 1 B 1 B 1 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 41 ; 0.160 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 41 ;23.240 ; 2.000
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
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 448 A 533
REMARK 3 ORIGIN FOR THE GROUP (A): 12.6779 26.7259 2.6504
REMARK 3 T TENSOR
REMARK 3 T11: 0.0882 T22: 0.0879
REMARK 3 T33: 0.3367 T12: -0.0223
REMARK 3 T13: 0.0073 T23: -0.0462
REMARK 3 L TENSOR
REMARK 3 L11: 2.6886 L22: 4.9886
REMARK 3 L33: 3.9956 L12: -3.1713
REMARK 3 L13: 0.2338 L23: -2.2139
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: 0.0263 S13: -0.5198
REMARK 3 S21: -0.1222 S22: 0.0020 S23: 0.3286
REMARK 3 S31: 0.2016 S32: 0.0489 S33: -0.0097
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 534 A 720
REMARK 3 ORIGIN FOR THE GROUP (A): 1.5209 28.4278 -19.9378
REMARK 3 T TENSOR
REMARK 3 T11: 0.0972 T22: 0.1638
REMARK 3 T33: 0.1411 T12: -0.0946
REMARK 3 T13: -0.0303 T23: 0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 2.7949 L22: 4.0515
REMARK 3 L33: 4.9893 L12: 2.3208
REMARK 3 L13: 0.2363 L23: 0.4701
REMARK 3 S TENSOR
REMARK 3 S11: -0.1256 S12: 0.2734 S13: -0.0468
REMARK 3 S21: -0.3050 S22: 0.2215 S23: 0.2102
REMARK 3 S31: 0.1120 S32: -0.0197 S33: -0.0959
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 : B 449 B 533
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0894 46.0918 -63.8600
REMARK 3 T TENSOR
REMARK 3 T11: 2.4221 T22: 1.4325
REMARK 3 T33: 1.0807 T12: 0.0033
REMARK 3 T13: -0.9866 T23: 0.2349
REMARK 3 L TENSOR
REMARK 3 L11: 12.4001 L22: 0.8982
REMARK 3 L33: 3.6884 L12: -1.0825
REMARK 3 L13: -2.1095 L23: -1.2934
REMARK 3 S TENSOR
REMARK 3 S11: 1.8744 S12: 1.0171 S13: -0.6609
REMARK 3 S21: -0.9626 S22: -0.6498 S23: 0.3451
REMARK 3 S31: 1.2275 S32: 0.0669 S33: -1.2246
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 534 B 720
REMARK 3 ORIGIN FOR THE GROUP (A): 16.6990 49.4796 -38.8390
REMARK 3 T TENSOR
REMARK 3 T11: 0.5820 T22: 0.4621
REMARK 3 T33: 0.2433 T12: -0.1956
REMARK 3 T13: -0.1809 T23: 0.0622
REMARK 3 L TENSOR
REMARK 3 L11: 5.9052 L22: 3.9855
REMARK 3 L33: 3.8213 L12: 2.0072
REMARK 3 L13: 1.8788 L23: -0.3011
REMARK 3 S TENSOR
REMARK 3 S11: 0.0279 S12: 0.0407 S13: 0.1066
REMARK 3 S21: -0.6055 S22: 0.1382 S23: 0.3614
REMARK 3 S31: -0.0615 S32: -0.2943 S33: -0.1661
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 5FD2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216383.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CLSI
REMARK 200 BEAMLINE : 08ID-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX-300
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16728
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.880
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.300
REMARK 200 R MERGE (I) : 0.10100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.88
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.20
REMARK 200 R MERGE FOR SHELL (I) : 0.72700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.600
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: EPMR
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TACSIMATE, TRIS, PH 8.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 122.62650
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 122.62650
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 36.89500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 40.04400
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 36.89500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 40.04400
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 122.62650
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 36.89500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 40.04400
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 122.62650
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 36.89500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 40.04400
REMARK 290 SMTRY3 8 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 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 HIS A 427
REMARK 465 HIS A 428
REMARK 465 HIS A 429
REMARK 465 HIS A 430
REMARK 465 HIS A 431
REMARK 465 HIS A 432
REMARK 465 GLU A 433
REMARK 465 ASP A 434
REMARK 465 ARG A 435
REMARK 465 ASN A 436
REMARK 465 ARG A 437
REMARK 465 MET A 438
REMARK 465 LYS A 439
REMARK 465 THR A 440
REMARK 465 LEU A 441
REMARK 465 GLY A 442
REMARK 465 ARG A 443
REMARK 465 ARG A 444
REMARK 465 ASP A 445
REMARK 465 SER A 446
REMARK 465 SER A 447
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 LEU A 721
REMARK 465 PRO A 722
REMARK 465 LYS A 723
REMARK 465 ILE A 724
REMARK 465 HIS A 725
REMARK 465 ARG A 726
REMARK 465 HIS B 427
REMARK 465 HIS B 428
REMARK 465 HIS B 429
REMARK 465 HIS B 430
REMARK 465 HIS B 431
REMARK 465 HIS B 432
REMARK 465 GLU B 433
REMARK 465 ASP B 434
REMARK 465 ARG B 435
REMARK 465 ASN B 436
REMARK 465 ARG B 437
REMARK 465 MET B 438
REMARK 465 LYS B 439
REMARK 465 THR B 440
REMARK 465 LEU B 441
REMARK 465 GLY B 442
REMARK 465 ARG B 443
REMARK 465 ARG B 444
REMARK 465 ASP B 445
REMARK 465 SER B 446
REMARK 465 SER B 447
REMARK 465 ASP B 448
REMARK 465 VAL B 459
REMARK 465 GLY B 460
REMARK 465 GLN B 461
REMARK 465 ARG B 462
REMARK 465 ILE B 463
REMARK 465 GLY B 464
REMARK 465 SER B 465
REMARK 465 GLY B 466
REMARK 465 SER B 467
REMARK 465 PHE B 468
REMARK 465 ASN B 486
REMARK 465 VAL B 487
REMARK 465 THR B 488
REMARK 465 ALA B 489
REMARK 465 PRO B 490
REMARK 465 THR B 491
REMARK 465 PRO B 492
REMARK 465 GLN B 493
REMARK 465 GLN B 494
REMARK 465 LEU B 495
REMARK 465 GLN B 496
REMARK 465 LEU B 597
REMARK 465 ALA B 598
REMARK 465 THR B 599
REMARK 465 VAL B 600
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 LEU B 721
REMARK 465 PRO B 722
REMARK 465 LYS B 723
REMARK 465 ILE B 724
REMARK 465 HIS B 725
REMARK 465 ARG B 726
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 B 483 CG CD CE NZ
REMARK 470 LYS B 507 CG CD CE NZ
REMARK 470 LYS B 522 CG CD CE NZ
REMARK 470 LYS B 547 CG CD CE NZ
REMARK 470 LYS B 630 CG CD CE NZ
REMARK 470 LYS B 687 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 -6.15 69.83
REMARK 500 ASP A 576 32.94 -158.28
REMARK 500 LEU A 588 14.99 95.51
REMARK 500 MET A 627 93.54 -54.71
REMARK 500 ILE B 457 -66.85 -134.45
REMARK 500 THR B 521 51.53 -158.59
REMARK 500 LYS B 522 87.31 -165.67
REMARK 500 PRO B 523 -96.40 -69.84
REMARK 500 GLU B 545 80.84 46.94
REMARK 500 ARG B 575 -12.71 64.99
REMARK 500 ASP B 576 51.48 -157.76
REMARK 500 ASP B 587 15.08 54.88
REMARK 500 LEU B 588 -61.62 -128.12
REMARK 500 ASP B 594 33.77 88.44
REMARK 500 MET B 627 96.53 -14.96
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 5XJ A 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5XJ B 801
DBREF 5FD2 A 433 726 UNP P15056 BRAF_HUMAN 433 726
DBREF 5FD2 B 433 726 UNP P15056 BRAF_HUMAN 433 726
SEQADV 5FD2 HIS A 427 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS A 428 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS A 429 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS A 430 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS A 431 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS A 432 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS B 427 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS B 428 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS B 429 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS B 430 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS B 431 UNP P15056 EXPRESSION TAG
SEQADV 5FD2 HIS B 432 UNP P15056 EXPRESSION TAG
SEQRES 1 A 300 HIS HIS HIS HIS HIS HIS GLU ASP ARG ASN ARG MET LYS
SEQRES 2 A 300 THR LEU GLY ARG ARG ASP SER SER ASP ASP TRP GLU ILE
SEQRES 3 A 300 PRO ASP GLY GLN ILE THR VAL GLY GLN ARG ILE GLY SER
SEQRES 4 A 300 GLY SER PHE GLY THR VAL TYR LYS GLY LYS TRP HIS GLY
SEQRES 5 A 300 ASP VAL ALA VAL LYS MET LEU ASN VAL THR ALA PRO THR
SEQRES 6 A 300 PRO GLN GLN LEU GLN ALA PHE LYS ASN GLU VAL GLY VAL
SEQRES 7 A 300 LEU ARG LYS THR ARG HIS VAL ASN ILE LEU LEU PHE MET
SEQRES 8 A 300 GLY TYR SER THR LYS PRO GLN LEU ALA ILE VAL THR GLN
SEQRES 9 A 300 TRP CYS GLU GLY SER SER LEU TYR HIS HIS LEU HIS ILE
SEQRES 10 A 300 ILE GLU THR LYS PHE GLU MET ILE LYS LEU ILE ASP ILE
SEQRES 11 A 300 ALA ARG GLN THR ALA GLN GLY MET ASP TYR LEU HIS ALA
SEQRES 12 A 300 LYS SER ILE ILE HIS ARG ASP LEU LYS SER ASN ASN ILE
SEQRES 13 A 300 PHE LEU HIS GLU ASP LEU THR VAL LYS ILE GLY ASP PHE
SEQRES 14 A 300 GLY LEU ALA THR VAL LYS SER ARG TRP SER GLY SER HIS
SEQRES 15 A 300 GLN PHE GLU GLN LEU SER GLY SER ILE LEU TRP MET ALA
SEQRES 16 A 300 PRO GLU VAL ILE ARG MET GLN ASP LYS ASN PRO TYR SER
SEQRES 17 A 300 PHE GLN SER ASP VAL TYR ALA PHE GLY ILE VAL LEU TYR
SEQRES 18 A 300 GLU LEU MET THR GLY GLN LEU PRO TYR SER ASN ILE ASN
SEQRES 19 A 300 ASN ARG ASP GLN ILE ILE PHE MET VAL GLY ARG GLY TYR
SEQRES 20 A 300 LEU SER PRO ASP LEU SER LYS VAL ARG SER ASN CYS PRO
SEQRES 21 A 300 LYS ALA MET LYS ARG LEU MET ALA GLU CYS LEU LYS LYS
SEQRES 22 A 300 LYS ARG ASP GLU ARG PRO LEU PHE PRO GLN ILE LEU ALA
SEQRES 23 A 300 SER ILE GLU LEU LEU ALA ARG SER LEU PRO LYS ILE HIS
SEQRES 24 A 300 ARG
SEQRES 1 B 300 HIS HIS HIS HIS HIS HIS GLU ASP ARG ASN ARG MET LYS
SEQRES 2 B 300 THR LEU GLY ARG ARG ASP SER SER ASP ASP TRP GLU ILE
SEQRES 3 B 300 PRO ASP GLY GLN ILE THR VAL GLY GLN ARG ILE GLY SER
SEQRES 4 B 300 GLY SER PHE GLY THR VAL TYR LYS GLY LYS TRP HIS GLY
SEQRES 5 B 300 ASP VAL ALA VAL LYS MET LEU ASN VAL THR ALA PRO THR
SEQRES 6 B 300 PRO GLN GLN LEU GLN ALA PHE LYS ASN GLU VAL GLY VAL
SEQRES 7 B 300 LEU ARG LYS THR ARG HIS VAL ASN ILE LEU LEU PHE MET
SEQRES 8 B 300 GLY TYR SER THR LYS PRO GLN LEU ALA ILE VAL THR GLN
SEQRES 9 B 300 TRP CYS GLU GLY SER SER LEU TYR HIS HIS LEU HIS ILE
SEQRES 10 B 300 ILE GLU THR LYS PHE GLU MET ILE LYS LEU ILE ASP ILE
SEQRES 11 B 300 ALA ARG GLN THR ALA GLN GLY MET ASP TYR LEU HIS ALA
SEQRES 12 B 300 LYS SER ILE ILE HIS ARG ASP LEU LYS SER ASN ASN ILE
SEQRES 13 B 300 PHE LEU HIS GLU ASP LEU THR VAL LYS ILE GLY ASP PHE
SEQRES 14 B 300 GLY LEU ALA THR VAL LYS SER ARG TRP SER GLY SER HIS
SEQRES 15 B 300 GLN PHE GLU GLN LEU SER GLY SER ILE LEU TRP MET ALA
SEQRES 16 B 300 PRO GLU VAL ILE ARG MET GLN ASP LYS ASN PRO TYR SER
SEQRES 17 B 300 PHE GLN SER ASP VAL TYR ALA PHE GLY ILE VAL LEU TYR
SEQRES 18 B 300 GLU LEU MET THR GLY GLN LEU PRO TYR SER ASN ILE ASN
SEQRES 19 B 300 ASN ARG ASP GLN ILE ILE PHE MET VAL GLY ARG GLY TYR
SEQRES 20 B 300 LEU SER PRO ASP LEU SER LYS VAL ARG SER ASN CYS PRO
SEQRES 21 B 300 LYS ALA MET LYS ARG LEU MET ALA GLU CYS LEU LYS LYS
SEQRES 22 B 300 LYS ARG ASP GLU ARG PRO LEU PHE PRO GLN ILE LEU ALA
SEQRES 23 B 300 SER ILE GLU LEU LEU ALA ARG SER LEU PRO LYS ILE HIS
SEQRES 24 B 300 ARG
HET 5XJ A 801 31
HET 5XJ B 801 31
HETNAM 5XJ 6-[2-[[3-(DIMETHYLSULFAMOYLAMINO)-2,6-BIS(FLUORANYL)
HETNAM 2 5XJ PHENYL]AMINO]PYRIDIN-3-YL]-7~{H}-PURINE
FORMUL 3 5XJ 2(C18 H16 F2 N8 O2 S)
FORMUL 5 HOH *32(H2 O)
HELIX 1 AA1 THR A 491 ARG A 506 1 16
HELIX 2 AA2 LEU A 537 ILE A 543 1 7
HELIX 3 AA3 GLU A 549 LYS A 570 1 22
HELIX 4 AA4 LEU A 597 TRP A 604 1 8
HELIX 5 AA5 SER A 616 MET A 620 5 5
HELIX 6 AA6 ALA A 621 ARG A 626 1 6
HELIX 7 AA7 SER A 634 GLY A 652 1 19
HELIX 8 AA8 ASN A 661 ARG A 671 1 11
HELIX 9 AA9 ASP A 677 VAL A 681 5 5
HELIX 10 AB1 PRO A 686 LEU A 697 1 12
HELIX 11 AB2 LYS A 700 ARG A 704 5 5
HELIX 12 AB3 LEU A 706 ALA A 718 1 13
HELIX 13 AB4 PHE B 498 LYS B 507 1 10
HELIX 14 AB5 LEU B 537 HIS B 542 1 6
HELIX 15 AB6 GLU B 549 LYS B 570 1 22
HELIX 16 AB7 LYS B 578 ASN B 580 5 3
HELIX 17 AB8 SER B 616 MET B 620 5 5
HELIX 18 AB9 ALA B 621 ARG B 626 1 6
HELIX 19 AC1 SER B 634 GLY B 652 1 19
HELIX 20 AC2 ASN B 661 ARG B 671 1 11
HELIX 21 AC3 ASP B 677 VAL B 681 5 5
HELIX 22 AC4 PRO B 686 LYS B 698 1 13
HELIX 23 AC5 LYS B 700 ARG B 704 5 5
HELIX 24 AC6 LEU B 706 ARG B 719 1 14
SHEET 1 AA1 5 THR A 458 GLY A 464 0
SHEET 2 AA1 5 GLY A 469 LYS A 475 -1 O VAL A 471 N ILE A 463
SHEET 3 AA1 5 ASP A 479 LEU A 485 -1 O MET A 484 N THR A 470
SHEET 4 AA1 5 ALA A 526 GLN A 530 -1 O THR A 529 N ALA A 481
SHEET 5 AA1 5 PHE A 516 SER A 520 -1 N MET A 517 O VAL A 528
SHEET 1 AA2 3 GLY A 534 SER A 536 0
SHEET 2 AA2 3 ILE A 582 HIS A 585 -1 O LEU A 584 N SER A 535
SHEET 3 AA2 3 VAL A 590 ILE A 592 -1 O LYS A 591 N PHE A 583
SHEET 1 AA3 4 TYR B 472 LYS B 475 0
SHEET 2 AA3 4 ASP B 479 MET B 484 -1 O VAL B 480 N GLY B 474
SHEET 3 AA3 4 LEU B 525 GLN B 530 -1 O ILE B 527 N LYS B 483
SHEET 4 AA3 4 PHE B 516 THR B 521 -1 N GLY B 518 O VAL B 528
SHEET 1 AA4 3 GLY B 534 SER B 536 0
SHEET 2 AA4 3 ILE B 582 HIS B 585 -1 O LEU B 584 N SER B 535
SHEET 3 AA4 3 THR B 589 ILE B 592 -1 O THR B 589 N HIS B 585
CISPEP 1 LYS A 522 PRO A 523 0 3.14
CISPEP 2 LYS B 522 PRO B 523 0 9.06
SITE 1 AC1 15 VAL A 471 ALA A 481 LYS A 483 LEU A 505
SITE 2 AC1 15 LEU A 514 THR A 529 GLN A 530 TRP A 531
SITE 3 AC1 15 CYS A 532 PHE A 583 ASP A 594 PHE A 595
SITE 4 AC1 15 GLY A 596 HOH A 902 HOH A 909
SITE 1 AC2 11 VAL B 471 ALA B 481 LYS B 483 LEU B 514
SITE 2 AC2 11 GLN B 530 TRP B 531 CYS B 532 GLY B 593
SITE 3 AC2 11 ASP B 594 PHE B 595 GLY B 596
CRYST1 73.790 80.088 245.253 90.00 90.00 90.00 C 2 2 21 16
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 0.013552 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012486 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004077 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 0.148307 -0.877989 -0.455126 34.58801 1
MTRIX2 2 -0.928681 -0.281838 0.241078 64.27910 1
MTRIX3 2 -0.339936 0.386914 -0.857171 -67.78677 1
(ATOM LINES ARE NOT SHOWN.)
END
