HEADER TRANSFERASE 03-NOV-14 4D58
TITLE FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH BIS-ANILINO
TITLE 2 PYRIMIDINE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FOCAL ADHESION KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: KINASE DOMAIN, RESIDUES 411-686;
COMPND 5 SYNONYM: FADK 1, FOCAL ADHESION KINASE-RELATED NONKINASE, FRNK, P41/
COMPND 6 P43FRNK, PROTEIN-TYROSINE KINASE 2, P125FAK, PP125FAK;
COMPND 7 EC: 2.7.10.2;
COMPND 8 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 3 ORGANISM_COMMON: CHICKEN;
SOURCE 4 ORGANISM_TAXID: 9031;
SOURCE 5 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PACG2T
KEYWDS TRANSFERASE, KINASE INHIBITOR, ATP-BINDING, INTEGRIN SIGNALING
EXPDTA X-RAY DIFFRACTION
AUTHOR J.LE COQ,A.LIN,D.LIETHA
REVDAT 3 20-DEC-23 4D58 1 REMARK
REVDAT 2 03-APR-19 4D58 1 SOURCE
REVDAT 1 18-FEB-15 4D58 0
JRNL AUTH J.ZHOU,A.BRONOWSKA,J.LE COQ,D.LIETHA,F.GRATER
JRNL TITL ALLOSTERIC REGULATION OF FOCAL ADHESION KINASE BY PIP2 AND
JRNL TITL 2 ATP.
JRNL REF BIOPHYS.J. V. 108 698 2015
JRNL REFN ISSN 0006-3495
JRNL PMID 25650936
JRNL DOI 10.1016/J.BPJ.2014.11.3454
REMARK 2
REMARK 2 RESOLUTION. 1.95 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 1.95
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 61.68
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 38091
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) : 0.197
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.228
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 2030
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) : 1.95
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2767
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.79
REMARK 3 BIN R VALUE (WORKING SET) : 0.2710
REMARK 3 BIN FREE R VALUE SET COUNT : 136
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4153
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 48
REMARK 3 SOLVENT ATOMS : 185
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.05000
REMARK 3 B22 (A**2) : 0.71000
REMARK 3 B33 (A**2) : -0.72000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.83000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.180
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.154
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.400
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4311 ; 0.009 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4161 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5834 ; 1.267 ; 1.978
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9574 ; 0.817 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 518 ; 5.201 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 192 ;33.238 ;23.281
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 775 ;13.354 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 35 ;21.307 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 641 ; 0.072 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4765 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 994 ; 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 : NULL
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 414 A 503
REMARK 3 ORIGIN FOR THE GROUP (A): 31.5128 33.9577 16.7262
REMARK 3 T TENSOR
REMARK 3 T11: 0.0382 T22: 0.0235
REMARK 3 T33: 0.1015 T12: -0.0092
REMARK 3 T13: 0.0227 T23: -0.0386
REMARK 3 L TENSOR
REMARK 3 L11: 1.1925 L22: 1.3330
REMARK 3 L33: 2.5765 L12: -0.7291
REMARK 3 L13: 0.1571 L23: -0.6473
REMARK 3 S TENSOR
REMARK 3 S11: -0.1208 S12: 0.0690 S13: 0.0208
REMARK 3 S21: 0.1288 S22: 0.0356 S23: -0.1569
REMARK 3 S31: 0.0782 S32: 0.0496 S33: 0.0852
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 504 A 684
REMARK 3 ORIGIN FOR THE GROUP (A): 14.0338 39.4404 -1.8640
REMARK 3 T TENSOR
REMARK 3 T11: 0.0197 T22: 0.0333
REMARK 3 T33: 0.0748 T12: -0.0239
REMARK 3 T13: 0.0161 T23: -0.0278
REMARK 3 L TENSOR
REMARK 3 L11: 1.1969 L22: 0.9156
REMARK 3 L33: 1.4652 L12: 0.3124
REMARK 3 L13: 0.0672 L23: -0.4463
REMARK 3 S TENSOR
REMARK 3 S11: -0.0532 S12: 0.1172 S13: -0.0804
REMARK 3 S21: -0.0594 S22: 0.0498 S23: 0.0411
REMARK 3 S31: 0.1464 S32: -0.1469 S33: 0.0035
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 415 B 503
REMARK 3 ORIGIN FOR THE GROUP (A): 26.0741 5.7893 32.7172
REMARK 3 T TENSOR
REMARK 3 T11: 0.1101 T22: 0.1436
REMARK 3 T33: 0.0936 T12: -0.0571
REMARK 3 T13: -0.0312 T23: -0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 0.6602 L22: 1.5737
REMARK 3 L33: 3.4627 L12: -0.4804
REMARK 3 L13: -0.6071 L23: -0.6879
REMARK 3 S TENSOR
REMARK 3 S11: -0.0643 S12: -0.1080 S13: 0.0860
REMARK 3 S21: 0.2672 S22: 0.0839 S23: -0.2362
REMARK 3 S31: -0.2134 S32: 0.4838 S33: -0.0196
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 504 B 685
REMARK 3 ORIGIN FOR THE GROUP (A): 10.3251 4.1883 12.5668
REMARK 3 T TENSOR
REMARK 3 T11: 0.0400 T22: 0.0326
REMARK 3 T33: 0.0725 T12: -0.0004
REMARK 3 T13: 0.0377 T23: 0.0023
REMARK 3 L TENSOR
REMARK 3 L11: 1.1064 L22: 1.3519
REMARK 3 L33: 2.0084 L12: -0.2008
REMARK 3 L13: 0.3822 L23: 0.1249
REMARK 3 S TENSOR
REMARK 3 S11: 0.0383 S12: -0.1215 S13: -0.0152
REMARK 3 S21: 0.0319 S22: 0.0410 S23: 0.1057
REMARK 3 S31: -0.1848 S32: -0.1569 S33: -0.0794
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. VALUES WITH TLS ADDED
REMARK 4
REMARK 4 4D58 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1290062077.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 13-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00004
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40150
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950
REMARK 200 RESOLUTION RANGE LOW (A) : 61.680
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.800
REMARK 200 R MERGE (I) : 0.04000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.06
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 3.70
REMARK 200 R MERGE FOR SHELL (I) : 0.32000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: PDB ENTRY 2JKK
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 44.59
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS PH 8.5, 75 MM LISO4, 22%
REMARK 280 PEG4000, 10 MM TCEP
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 61.68400
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER A 411
REMARK 465 THR A 412
REMARK 465 ARG A 413
REMARK 465 GLY A 566
REMARK 465 LEU A 567
REMARK 465 SER A 568
REMARK 465 ARG A 569
REMARK 465 TYR A 570
REMARK 465 MET A 571
REMARK 465 GLU A 572
REMARK 465 ASP A 573
REMARK 465 SER A 574
REMARK 465 THR A 575
REMARK 465 TYR A 576
REMARK 465 TYR A 577
REMARK 465 LYS A 578
REMARK 465 ALA A 579
REMARK 465 SER A 580
REMARK 465 LYS A 581
REMARK 465 GLY A 582
REMARK 465 LYS A 583
REMARK 465 SER B 411
REMARK 465 THR B 412
REMARK 465 ARG B 413
REMARK 465 GLU B 572
REMARK 465 ASP B 573
REMARK 465 SER B 574
REMARK 465 THR B 575
REMARK 465 TYR B 576
REMARK 465 TYR B 577
REMARK 465 LYS B 578
REMARK 465 ALA B 579
REMARK 465 SER B 580
REMARK 465 LYS B 581
REMARK 465 GLY B 582
REMARK 465 LYS B 583
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 ASN A 446 111.54 -162.02
REMARK 500 ARG A 545 -10.56 82.65
REMARK 500 ASP A 546 54.98 -146.35
REMARK 500 GLU B 445 -67.33 59.34
REMARK 500 ARG B 545 -10.05 80.81
REMARK 500 ASP B 546 56.17 -147.94
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 SO4 B 1687
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1688
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1689
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BI9 B 1690
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4D4R RELATED DB: PDB
REMARK 900 FOCAL ADHESION KINASE CATALYTIC DOMAIN
REMARK 900 RELATED ID: 4D4S RELATED DB: PDB
REMARK 900 FOCAL ADHESION KINASE CATALYTIC DOMAIN
REMARK 900 RELATED ID: 4D4V RELATED DB: PDB
REMARK 900 FOCAL ADHESION KINASE CATALYTIC DOMAIN
REMARK 900 RELATED ID: 4D4Y RELATED DB: PDB
REMARK 900 FOCAL ADHESION KINASE CATALYTIC DOMAIN
REMARK 900 RELATED ID: 4D55 RELATED DB: PDB
REMARK 900 FOCAL ADHESION KINASE CATALYTIC DOMAIN
REMARK 900 RELATED ID: 4D5H RELATED DB: PDB
REMARK 900 FOCAL ADHESION KINASE CATALYTIC DOMAIN
REMARK 900 RELATED ID: 4D5K RELATED DB: PDB
REMARK 900 FOCAL ADHESION KINASE CATALYTIC DOMAIN
DBREF 4D58 A 411 686 UNP Q00944 FAK1_CHICK 411 686
DBREF 4D58 B 411 686 UNP Q00944 FAK1_CHICK 411 686
SEQRES 1 A 276 SER THR ARG ASP TYR GLU ILE GLN ARG GLU ARG ILE GLU
SEQRES 2 A 276 LEU GLY ARG CYS ILE GLY GLU GLY GLN PHE GLY ASP VAL
SEQRES 3 A 276 HIS GLN GLY ILE TYR MET SER PRO GLU ASN PRO ALA MET
SEQRES 4 A 276 ALA VAL ALA ILE LYS THR CYS LYS ASN CYS THR SER ASP
SEQRES 5 A 276 SER VAL ARG GLU LYS PHE LEU GLN GLU ALA LEU THR MET
SEQRES 6 A 276 ARG GLN PHE ASP HIS PRO HIS ILE VAL LYS LEU ILE GLY
SEQRES 7 A 276 VAL ILE THR GLU ASN PRO VAL TRP ILE ILE MET GLU LEU
SEQRES 8 A 276 CYS THR LEU GLY GLU LEU ARG SER PHE LEU GLN VAL ARG
SEQRES 9 A 276 LYS PHE SER LEU ASP LEU ALA SER LEU ILE LEU TYR ALA
SEQRES 10 A 276 TYR GLN LEU SER THR ALA LEU ALA TYR LEU GLU SER LYS
SEQRES 11 A 276 ARG PHE VAL HIS ARG ASP ILE ALA ALA ARG ASN VAL LEU
SEQRES 12 A 276 VAL SER ALA THR ASP CYS VAL LYS LEU GLY ASP PHE GLY
SEQRES 13 A 276 LEU SER ARG TYR MET GLU ASP SER THR TYR TYR LYS ALA
SEQRES 14 A 276 SER LYS GLY LYS LEU PRO ILE LYS TRP MET ALA PRO GLU
SEQRES 15 A 276 SER ILE ASN PHE ARG ARG PHE THR SER ALA SER ASP VAL
SEQRES 16 A 276 TRP MET PHE GLY VAL CYS MET TRP GLU ILE LEU MET HIS
SEQRES 17 A 276 GLY VAL LYS PRO PHE GLN GLY VAL LYS ASN ASN ASP VAL
SEQRES 18 A 276 ILE GLY ARG ILE GLU ASN GLY GLU ARG LEU PRO MET PRO
SEQRES 19 A 276 PRO ASN CYS PRO PRO THR LEU TYR SER LEU MET THR LYS
SEQRES 20 A 276 CYS TRP ALA TYR ASP PRO SER ARG ARG PRO ARG PHE THR
SEQRES 21 A 276 GLU LEU LYS ALA GLN LEU SER THR ILE LEU GLU GLU GLU
SEQRES 22 A 276 LYS LEU GLN
SEQRES 1 B 276 SER THR ARG ASP TYR GLU ILE GLN ARG GLU ARG ILE GLU
SEQRES 2 B 276 LEU GLY ARG CYS ILE GLY GLU GLY GLN PHE GLY ASP VAL
SEQRES 3 B 276 HIS GLN GLY ILE TYR MET SER PRO GLU ASN PRO ALA MET
SEQRES 4 B 276 ALA VAL ALA ILE LYS THR CYS LYS ASN CYS THR SER ASP
SEQRES 5 B 276 SER VAL ARG GLU LYS PHE LEU GLN GLU ALA LEU THR MET
SEQRES 6 B 276 ARG GLN PHE ASP HIS PRO HIS ILE VAL LYS LEU ILE GLY
SEQRES 7 B 276 VAL ILE THR GLU ASN PRO VAL TRP ILE ILE MET GLU LEU
SEQRES 8 B 276 CYS THR LEU GLY GLU LEU ARG SER PHE LEU GLN VAL ARG
SEQRES 9 B 276 LYS PHE SER LEU ASP LEU ALA SER LEU ILE LEU TYR ALA
SEQRES 10 B 276 TYR GLN LEU SER THR ALA LEU ALA TYR LEU GLU SER LYS
SEQRES 11 B 276 ARG PHE VAL HIS ARG ASP ILE ALA ALA ARG ASN VAL LEU
SEQRES 12 B 276 VAL SER ALA THR ASP CYS VAL LYS LEU GLY ASP PHE GLY
SEQRES 13 B 276 LEU SER ARG TYR MET GLU ASP SER THR TYR TYR LYS ALA
SEQRES 14 B 276 SER LYS GLY LYS LEU PRO ILE LYS TRP MET ALA PRO GLU
SEQRES 15 B 276 SER ILE ASN PHE ARG ARG PHE THR SER ALA SER ASP VAL
SEQRES 16 B 276 TRP MET PHE GLY VAL CYS MET TRP GLU ILE LEU MET HIS
SEQRES 17 B 276 GLY VAL LYS PRO PHE GLN GLY VAL LYS ASN ASN ASP VAL
SEQRES 18 B 276 ILE GLY ARG ILE GLU ASN GLY GLU ARG LEU PRO MET PRO
SEQRES 19 B 276 PRO ASN CYS PRO PRO THR LEU TYR SER LEU MET THR LYS
SEQRES 20 B 276 CYS TRP ALA TYR ASP PRO SER ARG ARG PRO ARG PHE THR
SEQRES 21 B 276 GLU LEU LYS ALA GLN LEU SER THR ILE LEU GLU GLU GLU
SEQRES 22 B 276 LYS LEU GLN
HET SO4 B1687 5
HET SO4 B1688 5
HET SO4 B1689 5
HET BI9 B1690 33
HETNAM SO4 SULFATE ION
HETNAM BI9 2-({5-CHLORO-2-[(2-METHOXY-4-MORPHOLIN-4-YLPHENYL)
HETNAM 2 BI9 AMINO]PYRIMIDIN-4-YL}AMINO)-N-METHYLBENZAMIDE
FORMUL 3 SO4 3(O4 S 2-)
FORMUL 6 BI9 C23 H25 CL N6 O3
FORMUL 7 HOH *185(H2 O)
HELIX 1 1 GLN A 418 GLU A 420 5 3
HELIX 2 2 SER A 461 GLN A 477 1 17
HELIX 3 3 GLU A 506 ARG A 514 1 9
HELIX 4 4 ASP A 519 LYS A 540 1 22
HELIX 5 5 ALA A 548 ARG A 550 5 3
HELIX 6 6 PRO A 585 MET A 589 5 5
HELIX 7 7 ALA A 590 ARG A 597 1 8
HELIX 8 8 THR A 600 MET A 617 1 18
HELIX 9 9 LYS A 627 ASN A 629 5 3
HELIX 10 10 ASP A 630 ASN A 637 1 8
HELIX 11 11 PRO A 648 TRP A 659 1 12
HELIX 12 12 ASP A 662 ARG A 666 5 5
HELIX 13 13 ARG A 668 GLN A 686 1 19
HELIX 14 14 GLN B 418 GLU B 420 5 3
HELIX 15 15 SER B 461 GLN B 477 1 17
HELIX 16 16 LEU B 507 ARG B 514 1 8
HELIX 17 17 LYS B 515 LEU B 518 5 4
HELIX 18 18 ASP B 519 LYS B 540 1 22
HELIX 19 19 ALA B 548 ARG B 550 5 3
HELIX 20 20 GLY B 566 TYR B 570 5 5
HELIX 21 21 PRO B 585 MET B 589 5 5
HELIX 22 22 ALA B 590 ARG B 597 1 8
HELIX 23 23 THR B 600 MET B 617 1 18
HELIX 24 24 LYS B 627 ASN B 629 5 3
HELIX 25 25 ASP B 630 ASN B 637 1 8
HELIX 26 26 PRO B 648 TRP B 659 1 12
HELIX 27 27 ASP B 662 ARG B 666 5 5
HELIX 28 28 ARG B 668 LEU B 685 1 18
SHEET 1 AA 5 ILE A 422 GLY A 429 0
SHEET 2 AA 5 VAL A 436 TYR A 441 -1 O VAL A 436 N ILE A 428
SHEET 3 AA 5 MET A 449 THR A 455 -1 O MET A 449 N TYR A 441
SHEET 4 AA 5 TRP A 496 GLU A 500 -1 O ILE A 497 N LYS A 454
SHEET 5 AA 5 LEU A 486 ILE A 490 -1 N ILE A 487 O ILE A 498
SHEET 1 AB 2 VAL A 552 ALA A 556 0
SHEET 2 AB 2 CYS A 559 LEU A 562 -1 O CYS A 559 N SER A 555
SHEET 1 BA 5 ILE B 422 GLY B 429 0
SHEET 2 BA 5 GLY B 434 MET B 442 -1 O VAL B 436 N ILE B 428
SHEET 3 BA 5 ALA B 448 CYS B 456 -1 O MET B 449 N TYR B 441
SHEET 4 BA 5 TRP B 496 GLU B 500 -1 O ILE B 497 N LYS B 454
SHEET 5 BA 5 LEU B 486 ILE B 490 -1 N ILE B 487 O ILE B 498
SHEET 1 BB 3 GLY B 505 GLU B 506 0
SHEET 2 BB 3 VAL B 552 ALA B 556 -1 N VAL B 554 O GLY B 505
SHEET 3 BB 3 CYS B 559 LEU B 562 -1 O CYS B 559 N SER B 555
CISPEP 1 ASN A 493 PRO A 494 0 -3.83
CISPEP 2 ASN B 493 PRO B 494 0 0.73
SITE 1 AC1 5 LYS A 621 ASP B 519 LEU B 520 HOH B2031
SITE 2 AC1 5 HOH B2090
SITE 1 AC2 3 ARG B 508 GLN B 512 LYS B 621
SITE 1 AC3 5 SER B 601 ARG B 668 HOH B2042 HOH B2057
SITE 2 AC3 5 HOH B2091
SITE 1 AC4 15 ILE B 428 VAL B 436 GLN B 438 ALA B 452
SITE 2 AC4 15 LYS B 454 MET B 499 GLU B 500 LEU B 501
SITE 3 AC4 15 CYS B 502 THR B 503 GLY B 505 GLU B 506
SITE 4 AC4 15 LEU B 553 GLY B 563 HOH B2048
CRYST1 44.983 123.368 50.843 90.00 94.65 90.00 P 1 21 1 4
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 0.022231 0.000000 0.001808 0.00000
SCALE2 0.000000 0.008106 0.000000 0.00000
SCALE3 0.000000 0.000000 0.019733 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
