HEADER TRANSFERASE 06-JAN-16 5HES
TITLE HUMAN LEUCINE ZIPPER- AND STERILE ALPHA MOTIF-CONTAINING KINASE (ZAK,
TITLE 2 MLT, HCCS-4, MRK, AZK, MLTK) IN COMPLEX WITH VEMURAFENIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE MLT;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 5-309;
COMPND 5 SYNONYM: HUMAN CERVICAL CANCER SUPPRESSOR GENE 4 PROTEIN,HCCS-4,
COMPND 6 LEUCINE ZIPPER- AND STERILE ALPHA MOTIF-CONTAINING KINASE,MLK-LIKE
COMPND 7 MITOGEN-ACTIVATED PROTEIN TRIPLE KINASE,MIXED LINEAGE KINASE-RELATED
COMPND 8 KINASE,MRK,STERILE ALPHA MOTIF- AND LEUCINE ZIPPER-CONTAINING KINASE
COMPND 9 AZK;
COMPND 10 EC: 2.7.11.25;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ZAK, MLTK, HCCS4;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE, COMPLEX, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.MATHEA,E.SALAH,K.R.ABDUL AZEEZ,C.TALLANT,M.SZKLARZ,A.CHAIKUAD,
AUTHOR 2 B.SHRESTHA,F.J.SORRELL,J.M.ELKINS,L.SHRESTHA,N.BURGESS-BROWN,F.VON
AUTHOR 3 DELFT,C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,S.KNAPP
REVDAT 5 10-JAN-24 5HES 1 HETSYN
REVDAT 4 25-OCT-17 5HES 1 HETSYN
REVDAT 3 29-JUN-16 5HES 1 JRNL
REVDAT 2 06-APR-16 5HES 1 JRNL
REVDAT 1 30-MAR-16 5HES 0
JRNL AUTH S.MATHEA,K.R.ABDUL AZEEZ,E.SALAH,C.TALLANT,F.WOLFREYS,
JRNL AUTH 2 R.KONIETZNY,R.FISCHER,H.J.LOU,P.E.BRENNAN,G.SCHNAPP,
JRNL AUTH 3 A.PAUTSCH,B.M.KESSLER,B.E.TURK,S.KNAPP
JRNL TITL STRUCTURE OF THE HUMAN PROTEIN KINASE ZAK IN COMPLEX WITH
JRNL TITL 2 VEMURAFENIB.
JRNL REF ACS CHEM.BIOL. V. 11 1595 2016
JRNL REFN ESSN 1554-8937
JRNL PMID 26999302
JRNL DOI 10.1021/ACSCHEMBIO.6B00043
REMARK 2
REMARK 2 RESOLUTION. 2.14 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.14
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 78.70
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 44222
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE
REMARK 3 FREE R VALUE TEST SET SELECTION : NULL
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : NULL
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) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 REFLECTION IN BIN (WORKING SET) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE SET COUNT : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4526
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 74
REMARK 3 SOLVENT ATOMS : 179
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): NULL
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): NULL
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : NULL
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): NULL ; NULL ; NULL
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): NULL ; NULL ; NULL
REMARK 3 GENERAL PLANES REFINED ATOMS (A): NULL ; NULL ; NULL
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): 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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : NULL
REMARK 3 ION PROBE RADIUS : NULL
REMARK 3 SHRINKAGE RADIUS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5HES COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-JAN-16.
REMARK 100 THE DEPOSITION ID IS D_1000216879.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2
REMARK 200 DATA SCALING SOFTWARE : XIA2
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 44222
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 78.700
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 10.30
REMARK 200 R MERGE (I) : 0.06100
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.14
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.21
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.9
REMARK 200 DATA REDUNDANCY IN SHELL : 10.10
REMARK 200 R MERGE FOR SHELL (I) : 1.30200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 3DTC
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.08
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS-PROPANE PH 6.5, 200 MM
REMARK 280 SODIUM MALONATE, 20% PEG3350, 10% ETHYLENE GLYCOL, VAPOR
REMARK 280 DIFFUSION, SITTING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
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+1/4
REMARK 290 4555 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 66.67250
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 33.33625
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 100.00875
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 3
REMARK 465 MET A 4
REMARK 465 GLY A 5
REMARK 465 THR A 162
REMARK 465 HIS A 163
REMARK 465 MET A 164
REMARK 465 SER A 165
REMARK 465 LEU A 166
REMARK 465 VAL A 167
REMARK 465 ASP A 300
REMARK 465 LEU A 301
REMARK 465 SER A 302
REMARK 465 PHE A 303
REMARK 465 LYS A 304
REMARK 465 GLU A 305
REMARK 465 GLN A 306
REMARK 465 GLU A 307
REMARK 465 LEU A 308
REMARK 465 LYS A 309
REMARK 465 SER B 3
REMARK 465 MET B 4
REMARK 465 GLY B 5
REMARK 465 ALA B 6
REMARK 465 ALA B 154
REMARK 465 SER B 155
REMARK 465 ARG B 156
REMARK 465 PHE B 157
REMARK 465 HIS B 158
REMARK 465 ASN B 159
REMARK 465 HIS B 160
REMARK 465 TPO B 161
REMARK 465 THR B 162
REMARK 465 HIS B 163
REMARK 465 MET B 164
REMARK 465 SER B 165
REMARK 465 LEU B 166
REMARK 465 VAL B 167
REMARK 465 ARG B 299
REMARK 465 ASP B 300
REMARK 465 LEU B 301
REMARK 465 SER B 302
REMARK 465 PHE B 303
REMARK 465 LYS B 304
REMARK 465 GLU B 305
REMARK 465 GLN B 306
REMARK 465 GLU B 307
REMARK 465 LEU B 308
REMARK 465 LYS B 309
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 HIS A 160 CG ND1 CD2 CE1 NE2
REMARK 470 ARG A 233 CZ NH1 NH2
REMARK 470 ARG A 284 CZ NH1 NH2
REMARK 470 ARG A 299 NE CZ NH1 NH2
REMARK 470 LYS B 12 CE NZ
REMARK 470 LYS B 40 CE NZ
REMARK 470 MET B 104 CE
REMARK 470 ARG B 233 CZ NH1 NH2
REMARK 470 GLU B 298 CD OE1 OE2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 CG GLU A 51 O1P TPO A 161 2.09
REMARK 500 NE2 HIS A 158 O2P TPO A 161 2.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
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 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 83 CD GLU A 83 OE2 0.089
REMARK 500 TYR B 78 CZ TYR B 78 CE2 0.095
REMARK 500 GLU B 198 CD GLU B 198 OE1 0.067
REMARK 500 GLU B 198 CD GLU B 198 OE2 0.078
REMARK 500
REMARK 500 REMARK: NULL
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 ASP A 103 CB - CG - OD1 ANGL. DEV. = 6.9 DEGREES
REMARK 500 ARG A 132 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ARG A 137 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 CYS A 150 CA - CB - SG ANGL. DEV. = 9.3 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH1 ANGL. DEV. = 6.2 DEGREES
REMARK 500 ARG A 156 NE - CZ - NH2 ANGL. DEV. = -5.4 DEGREES
REMARK 500 ARG A 224 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG A 224 NE - CZ - NH2 ANGL. DEV. = -3.1 DEGREES
REMARK 500 ASP B 14 CB - CG - OD1 ANGL. DEV. = 8.5 DEGREES
REMARK 500 ARG B 32 NE - CZ - NH1 ANGL. DEV. = 3.5 DEGREES
REMARK 500 ARG B 137 NE - CZ - NH1 ANGL. DEV. = 4.6 DEGREES
REMARK 500 ARG B 137 NE - CZ - NH2 ANGL. DEV. = -3.3 DEGREES
REMARK 500 ASP B 188 CB - CG - OD1 ANGL. DEV. = 5.8 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 PHE A 19 -135.09 -107.62
REMARK 500 SER A 29 52.66 -99.47
REMARK 500 GLU A 51 -116.66 -99.36
REMARK 500 ASN A 95 32.33 -90.70
REMARK 500 ARG A 132 -14.81 81.63
REMARK 500 HIS A 158 60.72 -155.22
REMARK 500 HIS A 160 -126.53 126.14
REMARK 500 ASN A 279 35.93 -89.38
REMARK 500 PHE B 19 -137.24 -113.67
REMARK 500 SER B 29 49.24 -106.86
REMARK 500 ASN B 95 40.76 -92.61
REMARK 500 ASP B 133 44.87 -152.59
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 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 032 B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 402
DBREF 5HES A 5 309 UNP Q9NYL2 MLTK_HUMAN 5 309
DBREF 5HES B 5 309 UNP Q9NYL2 MLTK_HUMAN 5 309
SEQADV 5HES SER A 3 UNP Q9NYL2 EXPRESSION TAG
SEQADV 5HES MET A 4 UNP Q9NYL2 EXPRESSION TAG
SEQADV 5HES SER B 3 UNP Q9NYL2 EXPRESSION TAG
SEQADV 5HES MET B 4 UNP Q9NYL2 EXPRESSION TAG
SEQRES 1 A 307 SER MET GLY ALA SER PHE VAL GLN ILE LYS PHE ASP ASP
SEQRES 2 A 307 LEU GLN PHE PHE GLU ASN CYS GLY GLY GLY SER PHE GLY
SEQRES 3 A 307 SER VAL TYR ARG ALA LYS TRP ILE SER GLN ASP LYS GLU
SEQRES 4 A 307 VAL ALA VAL LYS LYS LEU LEU LYS ILE GLU LYS GLU ALA
SEQRES 5 A 307 GLU ILE LEU SER VAL LEU SER HIS ARG ASN ILE ILE GLN
SEQRES 6 A 307 PHE TYR GLY VAL ILE LEU GLU PRO PRO ASN TYR GLY ILE
SEQRES 7 A 307 VAL THR GLU TYR ALA SER LEU GLY SER LEU TYR ASP TYR
SEQRES 8 A 307 ILE ASN SER ASN ARG SER GLU GLU MET ASP MET ASP HIS
SEQRES 9 A 307 ILE MET THR TRP ALA THR ASP VAL ALA LYS GLY MET HIS
SEQRES 10 A 307 TYR LEU HIS MET GLU ALA PRO VAL LYS VAL ILE HIS ARG
SEQRES 11 A 307 ASP LEU LYS SER ARG ASN VAL VAL ILE ALA ALA ASP GLY
SEQRES 12 A 307 VAL LEU LYS ILE CYS ASP PHE GLY ALA SER ARG PHE HIS
SEQRES 13 A 307 ASN HIS TPO THR HIS MET SER LEU VAL GLY THR PHE PRO
SEQRES 14 A 307 TRP MET ALA PRO GLU VAL ILE GLN SER LEU PRO VAL SER
SEQRES 15 A 307 GLU THR CYS ASP THR TYR SER TYR GLY VAL VAL LEU TRP
SEQRES 16 A 307 GLU MET LEU THR ARG GLU VAL PRO PHE LYS GLY LEU GLU
SEQRES 17 A 307 GLY LEU GLN VAL ALA TRP LEU VAL VAL GLU LYS ASN GLU
SEQRES 18 A 307 ARG LEU THR ILE PRO SER SER CYS PRO ARG SER PHE ALA
SEQRES 19 A 307 GLU LEU LEU HIS GLN CYS TRP GLU ALA ASP ALA LYS LYS
SEQRES 20 A 307 ARG PRO SER PHE LYS GLN ILE ILE SER ILE LEU GLU SER
SEQRES 21 A 307 MET SER ASN ASP THR SER LEU PRO ASP LYS CYS ASN SER
SEQRES 22 A 307 PHE LEU HIS ASN LYS ALA GLU TRP ARG CYS GLU ILE GLU
SEQRES 23 A 307 ALA THR LEU GLU ARG LEU LYS LYS LEU GLU ARG ASP LEU
SEQRES 24 A 307 SER PHE LYS GLU GLN GLU LEU LYS
SEQRES 1 B 307 SER MET GLY ALA SER PHE VAL GLN ILE LYS PHE ASP ASP
SEQRES 2 B 307 LEU GLN PHE PHE GLU ASN CYS GLY GLY GLY SER PHE GLY
SEQRES 3 B 307 SER VAL TYR ARG ALA LYS TRP ILE SER GLN ASP LYS GLU
SEQRES 4 B 307 VAL ALA VAL LYS LYS LEU LEU LYS ILE GLU LYS GLU ALA
SEQRES 5 B 307 GLU ILE LEU SER VAL LEU SER HIS ARG ASN ILE ILE GLN
SEQRES 6 B 307 PHE TYR GLY VAL ILE LEU GLU PRO PRO ASN TYR GLY ILE
SEQRES 7 B 307 VAL THR GLU TYR ALA SER LEU GLY SER LEU TYR ASP TYR
SEQRES 8 B 307 ILE ASN SER ASN ARG SER GLU GLU MET ASP MET ASP HIS
SEQRES 9 B 307 ILE MET THR TRP ALA THR ASP VAL ALA LYS GLY MET HIS
SEQRES 10 B 307 TYR LEU HIS MET GLU ALA PRO VAL LYS VAL ILE HIS ARG
SEQRES 11 B 307 ASP LEU LYS SER ARG ASN VAL VAL ILE ALA ALA ASP GLY
SEQRES 12 B 307 VAL LEU LYS ILE CYS ASP PHE GLY ALA SER ARG PHE HIS
SEQRES 13 B 307 ASN HIS TPO THR HIS MET SER LEU VAL GLY THR PHE PRO
SEQRES 14 B 307 TRP MET ALA PRO GLU VAL ILE GLN SER LEU PRO VAL SER
SEQRES 15 B 307 GLU THR CYS ASP THR TYR SER TYR GLY VAL VAL LEU TRP
SEQRES 16 B 307 GLU MET LEU THR ARG GLU VAL PRO PHE LYS GLY LEU GLU
SEQRES 17 B 307 GLY LEU GLN VAL ALA TRP LEU VAL VAL GLU LYS ASN GLU
SEQRES 18 B 307 ARG LEU THR ILE PRO SER SER CYS PRO ARG SER PHE ALA
SEQRES 19 B 307 GLU LEU LEU HIS GLN CYS TRP GLU ALA ASP ALA LYS LYS
SEQRES 20 B 307 ARG PRO SER PHE LYS GLN ILE ILE SER ILE LEU GLU SER
SEQRES 21 B 307 MET SER ASN ASP THR SER LEU PRO ASP LYS CYS ASN SER
SEQRES 22 B 307 PHE LEU HIS ASN LYS ALA GLU TRP ARG CYS GLU ILE GLU
SEQRES 23 B 307 ALA THR LEU GLU ARG LEU LYS LYS LEU GLU ARG ASP LEU
SEQRES 24 B 307 SER PHE LYS GLU GLN GLU LEU LYS
MODRES 5HES TPO A 161 THR MODIFIED RESIDUE
HET TPO A 161 11
HET 032 A 401 33
HET EDO A 402 4
HET 032 B 401 33
HET EDO B 402 4
HETNAM TPO PHOSPHOTHREONINE
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
HETNAM EDO 1,2-ETHANEDIOL
HETSYN TPO PHOSPHONOTHREONINE
HETSYN 032 VEMURAFENIB; PLX4032
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 3 032 2(C23 H18 CL F2 N3 O3 S)
FORMUL 4 EDO 2(C2 H6 O2)
FORMUL 7 HOH *179(H2 O)
HELIX 1 AA1 LYS A 12 ASP A 14 5 3
HELIX 2 AA2 GLY A 23 SER A 26 5 4
HELIX 3 AA3 SER A 37 ASP A 39 5 3
HELIX 4 AA4 LYS A 52 SER A 58 1 7
HELIX 5 AA5 LEU A 90 ASN A 95 1 6
HELIX 6 AA6 SER A 96 MET A 102 5 7
HELIX 7 AA7 ASP A 103 GLU A 124 1 22
HELIX 8 AA8 LYS A 135 ARG A 137 5 3
HELIX 9 AA9 THR A 169 MET A 173 5 5
HELIX 10 AB1 ALA A 174 GLN A 179 1 6
HELIX 11 AB2 GLU A 185 ARG A 202 1 18
HELIX 12 AB3 GLU A 210 LYS A 221 1 12
HELIX 13 AB4 PRO A 232 TRP A 243 1 12
HELIX 14 AB5 ASP A 246 ARG A 250 5 5
HELIX 15 AB6 SER A 252 ASP A 266 1 15
HELIX 16 AB7 SER A 268 ASN A 279 1 12
HELIX 17 AB8 ASN A 279 ARG A 299 1 21
HELIX 18 AB9 LYS B 12 ASP B 14 5 3
HELIX 19 AC1 GLY B 23 SER B 26 5 4
HELIX 20 AC2 LYS B 52 LEU B 60 5 9
HELIX 21 AC3 SER B 89 ASN B 95 1 7
HELIX 22 AC4 SER B 96 MET B 102 5 7
HELIX 23 AC5 ASP B 103 GLU B 124 1 22
HELIX 24 AC6 LYS B 135 ARG B 137 5 3
HELIX 25 AC7 THR B 169 MET B 173 5 5
HELIX 26 AC8 ALA B 174 GLN B 179 1 6
HELIX 27 AC9 GLU B 185 ARG B 202 1 18
HELIX 28 AD1 GLU B 210 ASN B 222 1 13
HELIX 29 AD2 PRO B 232 GLU B 244 1 13
HELIX 30 AD3 ASP B 246 ARG B 250 5 5
HELIX 31 AD4 SER B 252 SER B 264 1 13
HELIX 32 AD5 SER B 268 HIS B 278 1 11
HELIX 33 AD6 ASN B 279 LEU B 297 1 19
SHEET 1 AA1 5 LEU A 16 ASN A 21 0
SHEET 2 AA1 5 VAL A 30 TRP A 35 -1 O ARG A 32 N PHE A 19
SHEET 3 AA1 5 LYS A 40 LEU A 47 -1 O LYS A 40 N TRP A 35
SHEET 4 AA1 5 ASN A 77 GLU A 83 -1 O ILE A 80 N LYS A 45
SHEET 5 AA1 5 PHE A 68 GLU A 74 -1 N GLU A 74 O ASN A 77
SHEET 1 AA2 3 GLY A 88 SER A 89 0
SHEET 2 AA2 3 VAL A 139 ILE A 141 -1 O ILE A 141 N GLY A 88
SHEET 3 AA2 3 LEU A 147 ILE A 149 -1 O LYS A 148 N VAL A 140
SHEET 1 AA3 6 GLN B 10 ILE B 11 0
SHEET 2 AA3 6 PHE B 68 GLU B 74 1 O VAL B 71 N ILE B 11
SHEET 3 AA3 6 ASN B 77 GLU B 83 -1 O VAL B 81 N TYR B 69
SHEET 4 AA3 6 LYS B 40 LEU B 47 -1 N LYS B 45 O ILE B 80
SHEET 5 AA3 6 VAL B 30 TRP B 35 -1 N TRP B 35 O LYS B 40
SHEET 6 AA3 6 LEU B 16 ASN B 21 -1 N PHE B 19 O ARG B 32
SHEET 1 AA4 2 VAL B 139 ILE B 141 0
SHEET 2 AA4 2 LEU B 147 ILE B 149 -1 O LYS B 148 N VAL B 140
LINK C HIS A 160 N TPO A 161 1555 1555 1.34
LINK O3P TPO A 161 SG CYS A 285 1555 3655 1.69
CISPEP 1 PRO A 75 PRO A 76 0 11.72
CISPEP 2 PRO B 75 PRO B 76 0 11.65
SITE 1 AC1 18 GLY A 23 PHE A 27 VAL A 30 ALA A 43
SITE 2 AC1 18 LYS A 45 ILE A 66 ILE A 80 THR A 82
SITE 3 AC1 18 GLU A 83 TYR A 84 ALA A 85 ASP A 92
SITE 4 AC1 18 CYS A 150 ASP A 151 PHE A 152 GLY A 153
SITE 5 AC1 18 HOH A 501 HOH A 527
SITE 1 AC2 4 ARG A 63 ASP A 144 LYS A 148 PRO B 126
SITE 1 AC3 16 GLY B 23 PHE B 27 VAL B 30 ALA B 43
SITE 2 AC3 16 LYS B 45 ILE B 66 THR B 82 GLU B 83
SITE 3 AC3 16 TYR B 84 ALA B 85 ASP B 92 CYS B 150
SITE 4 AC3 16 ASP B 151 PHE B 152 GLY B 153 HOH B 548
SITE 1 AC4 3 PRO A 126 ASP B 144 LYS B 148
CRYST1 78.712 78.712 133.345 90.00 90.00 90.00 P 41 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 0.012705 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012705 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007499 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
