HEADER TRANSFERASE/TRANSFERASE INHIBITOR 27-FEB-15 4YHT
TITLE BRAF COMPLEXED WITH AN INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE B-RAF;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 449-720;
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: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469
KEYWDS KINASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR L.M.SHEWCHUK,B.G.LAWHORN
REVDAT 4 28-FEB-24 4YHT 1 JRNL REMARK
REVDAT 3 22-JUN-16 4YHT 1 JRNL
REVDAT 2 15-JUN-16 4YHT 1 JRNL
REVDAT 1 16-MAR-16 4YHT 0
JRNL AUTH B.G.LAWHORN,J.PHILP,A.P.GRAVES,L.SHEWCHUK,D.A.HOLT,
JRNL AUTH 2 G.J.GATTO,L.S.KALLANDER
JRNL TITL GSK114: A SELECTIVE INHIBITOR FOR ELUCIDATING THE BIOLOGICAL
JRNL TITL 2 ROLE OF TNNI3K.
JRNL REF BIOORG.MED.CHEM.LETT. V. 26 3355 2016
JRNL REFN ESSN 1464-3405
JRNL PMID 27246618
JRNL DOI 10.1016/J.BMCL.2016.05.033
REMARK 2
REMARK 2 RESOLUTION. 3.05 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0073
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) : 3.05
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 15207
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) : 0.200
REMARK 3 R VALUE (WORKING SET) : 0.199
REMARK 3 FREE R VALUE : 0.233
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 806
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) : 3.05
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.13
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1105
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.65
REMARK 3 BIN R VALUE (WORKING SET) : 0.2520
REMARK 3 BIN FREE R VALUE SET COUNT : 63
REMARK 3 BIN FREE R VALUE : 0.3100
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4052
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 68
REMARK 3 SOLVENT ATOMS : 72
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 49.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.55000
REMARK 3 B22 (A**2) : -0.55000
REMARK 3 B33 (A**2) : 1.10000
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): 0.381
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.283
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.849
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4210 ; 0.007 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5693 ; 1.173 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 508 ; 5.483 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 181 ;36.064 ;24.033
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 727 ;15.511 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 23 ;22.323 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 630 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3173 ; 0.004 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 2050 ; 1.616 ; 2.414
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2552 ; 2.814 ; 3.604
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2160 ; 1.733 ; 2.458
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 : 5
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 448 A 626 2
REMARK 3 1 B 448 B 626 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 638 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 1 A (A**2): 664 ; 3.510 ; 0.500
REMARK 3 MEDIUM THERMAL 1 A (A**2): 638 ; 4.080 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
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 626 A 630 2
REMARK 3 1 B 626 B 630 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 A (A): 13 ; 0.030 ; 0.500
REMARK 3 TIGHT THERMAL 2 A (A**2): 12 ; 1.950 ; 0.500
REMARK 3 MEDIUM THERMAL 2 A (A**2): 13 ; 1.320 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 3
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 631 A 661 2
REMARK 3 1 B 631 B 661 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 3 A (A): 130 ; 0.040 ; 0.500
REMARK 3 TIGHT THERMAL 3 A (A**2): 124 ; 1.410 ; 0.500
REMARK 3 MEDIUM THERMAL 3 A (A**2): 130 ; 2.090 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 4
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 663 A 719 2
REMARK 3 1 B 663 B 719 2
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 4 A (A): 210 ; 0.040 ; 0.500
REMARK 3 TIGHT THERMAL 4 A (A**2): 224 ; 1.790 ; 0.500
REMARK 3 MEDIUM THERMAL 4 A (A**2): 210 ; 2.900 ; 2.000
REMARK 3
REMARK 3 NCS GROUP NUMBER : 5
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 2001 A 2001 1
REMARK 3 1 B 2001 B 2001 1
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 TIGHT THERMAL 5 A (A**2): 28 ; 3.290 ; 0.500
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
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 2001
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4230 -22.8490 -28.2970
REMARK 3 T TENSOR
REMARK 3 T11: 0.2449 T22: 0.3368
REMARK 3 T33: 0.0456 T12: -0.0225
REMARK 3 T13: -0.0172 T23: -0.0468
REMARK 3 L TENSOR
REMARK 3 L11: 1.2585 L22: 2.4152
REMARK 3 L33: 2.2727 L12: 1.2105
REMARK 3 L13: 0.7533 L23: 1.6206
REMARK 3 S TENSOR
REMARK 3 S11: -0.1258 S12: 0.1742 S13: 0.0210
REMARK 3 S21: -0.0743 S22: 0.1412 S23: -0.1669
REMARK 3 S31: -0.0922 S32: 0.0287 S33: -0.0154
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 : B 448 B 2001
REMARK 3 ORIGIN FOR THE GROUP (A): -32.4730 -43.1870 -44.0400
REMARK 3 T TENSOR
REMARK 3 T11: 0.2994 T22: 0.3363
REMARK 3 T33: 0.0229 T12: -0.0320
REMARK 3 T13: -0.0005 T23: -0.0593
REMARK 3 L TENSOR
REMARK 3 L11: 1.7709 L22: 0.7653
REMARK 3 L33: 2.0023 L12: 0.7466
REMARK 3 L13: 1.4912 L23: 0.2785
REMARK 3 S TENSOR
REMARK 3 S11: -0.0394 S12: 0.0189 S13: -0.0892
REMARK 3 S21: -0.0439 S22: 0.1175 S23: -0.0121
REMARK 3 S31: -0.0644 S32: 0.0418 S33: -0.0780
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 USED IF PRESENT IN
REMARK 3 THE INPUT U VALUES : WITH TLS ADDED
REMARK 4
REMARK 4 4YHT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207486.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-DEC-09
REMARK 200 TEMPERATURE (KELVIN) : 93
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16082
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.050
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 8.700
REMARK 200 R MERGE (I) : 0.15300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.05
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 8.70
REMARK 200 R MERGE FOR SHELL (I) : 0.69200
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.0, 650 MM NACL, 3-6 %
REMARK 280 PEG 8000, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 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+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 80.75200
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 49.89150
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.89150
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.37600
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.89150
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 49.89150
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 121.12800
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 49.89150
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.89150
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 40.37600
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 49.89150
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.89150
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 121.12800
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 0.00000
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 80.75200
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
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 SER A 601
REMARK 465 ARG A 602
REMARK 465 TRP A 603
REMARK 465 SER A 604
REMARK 465 GLY A 605
REMARK 465 SER A 606
REMARK 465 HIS A 607
REMARK 465 GLN A 608
REMARK 465 PHE A 609
REMARK 465 GLU A 610
REMARK 465 GLN A 611
REMARK 465 LEU A 612
REMARK 465 SER A 613
REMARK 465 LYS A 629
REMARK 465 ASN A 630
REMARK 465 SER A 719
REMARK 465 ARG B 602
REMARK 465 TRP B 603
REMARK 465 SER B 604
REMARK 465 GLY B 605
REMARK 465 SER B 606
REMARK 465 HIS B 607
REMARK 465 GLN B 608
REMARK 465 PHE B 609
REMARK 465 GLU B 610
REMARK 465 GLN B 611
REMARK 465 LEU B 612
REMARK 465 SER B 613
REMARK 465 LYS B 629
REMARK 465 ASN B 630
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 521 CG CD CE NZ
REMARK 470 LYS A 546 CG CD CE NZ
REMARK 470 LYS A 551 CD CE NZ
REMARK 470 ARG A 670 NE CZ NH1 NH2
REMARK 470 LYS A 686 CD CE NZ
REMARK 470 ARG A 718 CD NE CZ NH1 NH2
REMARK 470 LYS B 521 CG CD CE NZ
REMARK 470 LYS B 546 CG CD CE NZ
REMARK 470 LYS B 551 CD CE NZ
REMARK 470 LYS B 600 CG CD CE NZ
REMARK 470 SER B 601 OG
REMARK 470 ARG B 718 CG CD NE CZ NH1 NH2
REMARK 470 SER B 719 OG
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 ARG A 461 NH1 - CZ - NH2 ANGL. DEV. = 12.2 DEGREES
REMARK 500 ARG A 461 NE - CZ - NH2 ANGL. DEV. = -13.6 DEGREES
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 TRP A 475 101.08 -161.24
REMARK 500 ASP A 575 31.31 -152.63
REMARK 500 ASP A 586 -9.86 63.91
REMARK 500 LEU A 587 -62.42 -99.83
REMARK 500 ASP A 593 88.64 59.89
REMARK 500 MET A 626 17.50 59.13
REMARK 500 ASP B 575 30.08 -151.87
REMARK 500 ASP B 586 -10.87 62.17
REMARK 500 LEU B 587 -60.48 -99.12
REMARK 500 ASP B 593 90.89 54.11
REMARK 500 MET B 626 16.99 56.17
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 GOL A 1001
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4EF A 1002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 801
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4EF B 802
DBREF 4YHT A 448 719 UNP P15056 BRAF_HUMAN 449 720
DBREF 4YHT B 448 719 UNP P15056 BRAF_HUMAN 449 720
SEQADV 4YHT THR A 542 UNP P15056 ILE 543 ENGINEERED MUTATION
SEQADV 4YHT ASN A 543 UNP P15056 ILE 544 ENGINEERED MUTATION
SEQADV 4YHT THR A 550 UNP P15056 ILE 551 ENGINEERED MUTATION
SEQADV 4YHT THR A 705 UNP P15056 LEU 706 ENGINEERED MUTATION
SEQADV 4YHT THR A 715 UNP P15056 LEU 716 ENGINEERED MUTATION
SEQADV 4YHT THR B 542 UNP P15056 ILE 543 ENGINEERED MUTATION
SEQADV 4YHT ASN B 543 UNP P15056 ILE 544 ENGINEERED MUTATION
SEQADV 4YHT THR B 550 UNP P15056 ILE 551 ENGINEERED MUTATION
SEQADV 4YHT THR B 705 UNP P15056 LEU 706 ENGINEERED MUTATION
SEQADV 4YHT THR B 715 UNP P15056 LEU 716 ENGINEERED MUTATION
SEQRES 1 A 272 ASP TRP GLU ILE PRO ASP GLY GLN ILE THR VAL GLY GLN
SEQRES 2 A 272 ARG ILE GLY SER GLY SER PHE GLY THR VAL TYR LYS GLY
SEQRES 3 A 272 LYS TRP HIS GLY ASP VAL ALA VAL LYS MET LEU ASN VAL
SEQRES 4 A 272 THR ALA PRO THR PRO GLN GLN LEU GLN ALA PHE LYS ASN
SEQRES 5 A 272 GLU VAL GLY VAL LEU ARG LYS THR ARG HIS VAL ASN ILE
SEQRES 6 A 272 LEU LEU PHE MET GLY TYR SER THR LYS PRO GLN LEU ALA
SEQRES 7 A 272 ILE VAL THR GLN TRP CYS GLU GLY SER SER LEU TYR HIS
SEQRES 8 A 272 HIS LEU HIS THR ASN GLU THR LYS PHE GLU MET THR LYS
SEQRES 9 A 272 LEU ILE ASP ILE ALA ARG GLN THR ALA GLN GLY MET ASP
SEQRES 10 A 272 TYR LEU HIS ALA LYS SER ILE ILE HIS ARG ASP LEU LYS
SEQRES 11 A 272 SER ASN ASN ILE PHE LEU HIS GLU ASP LEU THR VAL LYS
SEQRES 12 A 272 ILE GLY ASP PHE GLY LEU ALA THR VAL LYS SER ARG TRP
SEQRES 13 A 272 SER GLY SER HIS GLN PHE GLU GLN LEU SER GLY SER ILE
SEQRES 14 A 272 LEU TRP MET ALA PRO GLU VAL ILE ARG MET GLN ASP LYS
SEQRES 15 A 272 ASN PRO TYR SER PHE GLN SER ASP VAL TYR ALA PHE GLY
SEQRES 16 A 272 ILE VAL LEU TYR GLU LEU MET THR GLY GLN LEU PRO TYR
SEQRES 17 A 272 SER ASN ILE ASN ASN ARG ASP GLN ILE ILE PHE MET VAL
SEQRES 18 A 272 GLY ARG GLY TYR LEU SER PRO ASP LEU SER LYS VAL ARG
SEQRES 19 A 272 SER ASN CYS PRO LYS ALA MET LYS ARG LEU MET ALA GLU
SEQRES 20 A 272 CYS LEU LYS LYS LYS ARG ASP GLU ARG PRO THR PHE PRO
SEQRES 21 A 272 GLN ILE LEU ALA SER ILE GLU THR LEU ALA ARG SER
SEQRES 1 B 272 ASP TRP GLU ILE PRO ASP GLY GLN ILE THR VAL GLY GLN
SEQRES 2 B 272 ARG ILE GLY SER GLY SER PHE GLY THR VAL TYR LYS GLY
SEQRES 3 B 272 LYS TRP HIS GLY ASP VAL ALA VAL LYS MET LEU ASN VAL
SEQRES 4 B 272 THR ALA PRO THR PRO GLN GLN LEU GLN ALA PHE LYS ASN
SEQRES 5 B 272 GLU VAL GLY VAL LEU ARG LYS THR ARG HIS VAL ASN ILE
SEQRES 6 B 272 LEU LEU PHE MET GLY TYR SER THR LYS PRO GLN LEU ALA
SEQRES 7 B 272 ILE VAL THR GLN TRP CYS GLU GLY SER SER LEU TYR HIS
SEQRES 8 B 272 HIS LEU HIS THR ASN GLU THR LYS PHE GLU MET THR LYS
SEQRES 9 B 272 LEU ILE ASP ILE ALA ARG GLN THR ALA GLN GLY MET ASP
SEQRES 10 B 272 TYR LEU HIS ALA LYS SER ILE ILE HIS ARG ASP LEU LYS
SEQRES 11 B 272 SER ASN ASN ILE PHE LEU HIS GLU ASP LEU THR VAL LYS
SEQRES 12 B 272 ILE GLY ASP PHE GLY LEU ALA THR VAL LYS SER ARG TRP
SEQRES 13 B 272 SER GLY SER HIS GLN PHE GLU GLN LEU SER GLY SER ILE
SEQRES 14 B 272 LEU TRP MET ALA PRO GLU VAL ILE ARG MET GLN ASP LYS
SEQRES 15 B 272 ASN PRO TYR SER PHE GLN SER ASP VAL TYR ALA PHE GLY
SEQRES 16 B 272 ILE VAL LEU TYR GLU LEU MET THR GLY GLN LEU PRO TYR
SEQRES 17 B 272 SER ASN ILE ASN ASN ARG ASP GLN ILE ILE PHE MET VAL
SEQRES 18 B 272 GLY ARG GLY TYR LEU SER PRO ASP LEU SER LYS VAL ARG
SEQRES 19 B 272 SER ASN CYS PRO LYS ALA MET LYS ARG LEU MET ALA GLU
SEQRES 20 B 272 CYS LEU LYS LYS LYS ARG ASP GLU ARG PRO THR PHE PRO
SEQRES 21 B 272 GLN ILE LEU ALA SER ILE GLU THR LEU ALA ARG SER
HET GOL A1001 6
HET 4EF A1002 28
HET GOL B 801 6
HET 4EF B 802 28
HETNAM GOL GLYCEROL
HETNAM 4EF 3-[(5-CHLORO-7H-PYRROLO[2,3-D]PYRIMIDIN-4-YL)AMINO]-N-
HETNAM 2 4EF METHYL-4-(MORPHOLIN-4-YL)BENZENESULFONAMIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 GOL 2(C3 H8 O3)
FORMUL 4 4EF 2(C17 H19 CL N6 O3 S)
FORMUL 7 HOH *72(H2 O)
HELIX 1 AA1 THR A 490 ARG A 505 1 16
HELIX 2 AA2 SER A 535 THR A 542 1 8
HELIX 3 AA3 GLU A 548 LYS A 569 1 22
HELIX 4 AA4 LYS A 577 ASN A 579 5 3
HELIX 5 AA5 GLU A 585 LEU A 587 5 3
HELIX 6 AA6 SER A 615 MET A 619 5 5
HELIX 7 AA7 ALA A 620 MET A 626 1 7
HELIX 8 AA8 SER A 633 GLY A 651 1 19
HELIX 9 AA9 ASN A 660 GLY A 671 1 12
HELIX 10 AB1 ASP A 676 VAL A 680 5 5
HELIX 11 AB2 PRO A 685 LEU A 696 1 12
HELIX 12 AB3 LYS A 699 ARG A 703 5 5
HELIX 13 AB4 THR A 705 THR A 715 1 11
HELIX 14 AB5 THR B 490 ARG B 505 1 16
HELIX 15 AB6 SER B 535 THR B 542 1 8
HELIX 16 AB7 GLU B 548 LYS B 569 1 22
HELIX 17 AB8 LYS B 577 ASN B 579 5 3
HELIX 18 AB9 GLU B 585 LEU B 587 5 3
HELIX 19 AC1 SER B 615 MET B 619 5 5
HELIX 20 AC2 ALA B 620 MET B 626 1 7
HELIX 21 AC3 SER B 633 GLY B 651 1 19
HELIX 22 AC4 ASN B 660 GLY B 671 1 12
HELIX 23 AC5 ASP B 676 VAL B 680 5 5
HELIX 24 AC6 PRO B 685 LEU B 696 1 12
HELIX 25 AC7 LYS B 699 ARG B 703 5 5
HELIX 26 AC8 THR B 705 THR B 715 1 11
SHEET 1 AA1 5 THR A 457 GLY A 465 0
SHEET 2 AA1 5 GLY A 468 LYS A 474 -1 O LYS A 472 N GLN A 460
SHEET 3 AA1 5 ASP A 478 MET A 483 -1 O VAL A 479 N GLY A 473
SHEET 4 AA1 5 ALA A 525 GLN A 529 -1 O THR A 528 N ALA A 480
SHEET 5 AA1 5 PHE A 515 SER A 519 -1 N GLY A 517 O VAL A 527
SHEET 1 AA2 2 ILE A 571 ILE A 572 0
SHEET 2 AA2 2 THR A 598 VAL A 599 -1 O THR A 598 N ILE A 572
SHEET 1 AA3 2 ILE A 581 HIS A 584 0
SHEET 2 AA3 2 THR A 588 ILE A 591 -1 O THR A 588 N HIS A 584
SHEET 1 AA4 5 THR B 457 GLY B 465 0
SHEET 2 AA4 5 GLY B 468 LYS B 474 -1 O LYS B 472 N GLN B 460
SHEET 3 AA4 5 ASP B 478 MET B 483 -1 O VAL B 479 N GLY B 473
SHEET 4 AA4 5 ALA B 525 GLN B 529 -1 O THR B 528 N ALA B 480
SHEET 5 AA4 5 PHE B 515 SER B 519 -1 N GLY B 517 O VAL B 527
SHEET 1 AA5 2 ILE B 571 ILE B 572 0
SHEET 2 AA5 2 THR B 598 VAL B 599 -1 O THR B 598 N ILE B 572
SHEET 1 AA6 2 ILE B 581 HIS B 584 0
SHEET 2 AA6 2 THR B 588 ILE B 591 -1 O THR B 588 N HIS B 584
CISPEP 1 LYS A 521 PRO A 522 0 5.77
CISPEP 2 LYS B 521 PRO B 522 0 5.39
SITE 1 AC1 4 ASN A 511 ARG A 557 GLN A 561 ASP B 478
SITE 1 AC2 15 ILE A 462 VAL A 470 ALA A 480 LYS A 482
SITE 2 AC2 15 LEU A 513 THR A 528 GLN A 529 TRP A 530
SITE 3 AC2 15 CYS A 531 GLY A 533 ASN A 579 PHE A 582
SITE 4 AC2 15 ASP A 593 HOH A1114 HOH A1124
SITE 1 AC3 4 SER B 674 PRO B 675 ALA B 693 LYS B 698
SITE 1 AC4 15 ILE B 462 SER B 464 VAL B 470 ALA B 480
SITE 2 AC4 15 LYS B 482 LEU B 513 THR B 528 GLN B 529
SITE 3 AC4 15 TRP B 530 CYS B 531 GLY B 533 ASN B 579
SITE 4 AC4 15 PHE B 582 ASP B 593 HOH B 912
CRYST1 99.783 99.783 161.504 90.00 90.00 90.00 P 41 21 2 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 0.010022 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010022 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006192 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 -0.078417 -0.994866 -0.063966 -57.77695 1
MTRIX2 2 -0.994774 0.073879 0.070467 -48.83678 1
MTRIX3 2 -0.065379 0.069157 -0.995461 -71.07220 1
(ATOM LINES ARE NOT SHOWN.)
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