HEADER TRANSFERASE 18-SEP-01 1K05
TITLE CRYSTAL STRUCTURE OF THE FOCAL ADHESION TARGETING DOMAIN OF FOCAL
TITLE 2 ADHESION KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: FOCAL ADHESION KINASE 1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: FADK 1;
COMPND 5 EC: 2.7.1.112;
COMPND 6 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: FAK;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: B834(DE3)PLYSS;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P2
KEYWDS UP-DOWN-UP-DOWN FOUR HELICAL BUNDLE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.T.AROLD,M.K.HOELLERER,M.E.M.NOBLE
REVDAT 5 07-FEB-24 1K05 1 REMARK
REVDAT 4 24-FEB-09 1K05 1 VERSN
REVDAT 3 01-APR-03 1K05 1 JRNL
REVDAT 2 27-MAR-02 1K05 1 JRNL
REVDAT 1 30-JAN-02 1K05 0
JRNL AUTH S.T.AROLD,M.K.HOELLERER,M.E.NOBLE
JRNL TITL THE STRUCTURAL BASIS OF LOCALIZATION AND SIGNALING BY THE
JRNL TITL 2 FOCAL ADHESION TARGETING DOMAIN.
JRNL REF STRUCTURE V. 10 319 2002
JRNL REFN ISSN 0969-2126
JRNL PMID 12005431
JRNL DOI 10.1016/S0969-2126(02)00717-7
REMARK 2
REMARK 2 RESOLUTION. 2.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS 1.0
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : CNS
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.30
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : 96.9
REMARK 3 NUMBER OF REFLECTIONS : 21585
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.285
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 1000
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 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) : 2.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.95
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 92.30
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : 0.5030
REMARK 3 BIN FREE R VALUE : 0.5110
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 39
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3251
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 6
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 90.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.80
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -34.88900
REMARK 3 B22 (A**2) : 18.40000
REMARK 3 B33 (A**2) : 16.48900
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.350
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : ISOTROPIC
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : PROTEIN_REP.PARAM
REMARK 3 PARAMETER FILE 2 : WATER_REP.PARAM
REMARK 3 PARAMETER FILE 3 : ION.PARAM
REMARK 3 PARAMETER FILE 4 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 2 : NULL
REMARK 3 TOPOLOGY FILE 3 : NULL
REMARK 3 TOPOLOGY FILE 4 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1K05 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-SEP-01.
REMARK 100 THE DEPOSITION ID IS D_1000014393.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-SEP-00
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID14-3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.931
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20719
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.900
REMARK 200 RESOLUTION RANGE LOW (A) : 31.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.900
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.9
REMARK 200 DATA REDUNDANCY : 2.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.9
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.62600
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIRAS
REMARK 200 SOFTWARE USED: SHARP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 71.95
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.42
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, NACL, GLYCEROL, PH 7.0, VAPOR
REMARK 280 DIFFUSION, HANGING DROP, TEMPERATURE 296K
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 48.94250
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 48.94250
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 43.74200
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 111.05050
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 43.74200
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 111.05050
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 48.94250
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 43.74200
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 111.05050
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 48.94250
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 43.74200
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 111.05050
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7
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 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 350
REMARK 350 BIOMOLECULE: 3
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: C
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: 4
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4730 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28480 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 48.94250
REMARK 350
REMARK 350 BIOMOLECULE: 5
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 48.94250
REMARK 350
REMARK 350 BIOMOLECULE: 6
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6100 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 28160 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -43.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C
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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 48.94250
REMARK 350
REMARK 350 BIOMOLECULE: 7
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1780 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
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 350 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 48.94250
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 LEU A 891
REMARK 465 SER A 892
REMARK 465 SER A 893
REMARK 465 PRO A 894
REMARK 465 ALA A 895
REMARK 465 ASP A 896
REMARK 465 SER A 897
REMARK 465 TYR A 898
REMARK 465 ASN A 899
REMARK 465 GLU A 900
REMARK 465 GLY A 901
REMARK 465 VAL A 902
REMARK 465 LYS A 903
REMARK 465 LEU A 904
REMARK 465 GLN A 905
REMARK 465 PRO A 906
REMARK 465 GLN A 907
REMARK 465 GLU A 908
REMARK 465 ILE A 909
REMARK 465 SER A 910
REMARK 465 PRO A 911
REMARK 465 PRO A 912
REMARK 465 PRO A 913
REMARK 465 THR A 914
REMARK 465 ALA A 915
REMARK 465 PRO A 1051
REMARK 465 HIS A 1052
REMARK 465 LEU B 891
REMARK 465 SER B 892
REMARK 465 SER B 893
REMARK 465 PRO B 894
REMARK 465 ALA B 895
REMARK 465 ASP B 896
REMARK 465 SER B 897
REMARK 465 TYR B 898
REMARK 465 ASN B 899
REMARK 465 GLU B 900
REMARK 465 GLY B 901
REMARK 465 VAL B 902
REMARK 465 LYS B 903
REMARK 465 LEU B 904
REMARK 465 GLN B 905
REMARK 465 GLN B 1048
REMARK 465 THR B 1049
REMARK 465 ARG B 1050
REMARK 465 PRO B 1051
REMARK 465 HIS B 1052
REMARK 465 LEU C 891
REMARK 465 SER C 892
REMARK 465 SER C 893
REMARK 465 PRO C 894
REMARK 465 ALA C 895
REMARK 465 ASP C 896
REMARK 465 SER C 897
REMARK 465 TYR C 898
REMARK 465 ASN C 899
REMARK 465 GLU C 900
REMARK 465 GLY C 901
REMARK 465 VAL C 902
REMARK 465 LYS C 903
REMARK 465 LEU C 904
REMARK 465 GLN C 905
REMARK 465 PRO C 906
REMARK 465 THR C 1049
REMARK 465 ARG C 1050
REMARK 465 PRO C 1051
REMARK 465 HIS C 1052
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 GLU A 948 4.37 -65.01
REMARK 500 PRO A 973 -7.99 -52.46
REMARK 500 PRO A 976 128.92 -39.98
REMARK 500 SER A 978 -75.72 -51.31
REMARK 500 HIS A 980 -64.29 -17.48
REMARK 500 TYR A1007 43.90 -77.16
REMARK 500 VAL A1008 -109.82 -40.20
REMARK 500 GLN A1014 -8.57 -53.44
REMARK 500 GLU B 908 95.84 -164.00
REMARK 500 THR B 914 144.54 -38.50
REMARK 500 PRO B 944 73.07 -107.81
REMARK 500 HIS B 980 -73.34 -22.68
REMARK 500 LEU B1012 -9.99 -50.08
REMARK 500 ARG C 919 2.99 -58.21
REMARK 500 MET C 938 -70.34 -40.94
REMARK 500 ILE C 942 -57.39 -19.56
REMARK 500 GLN C 943 -67.52 -21.14
REMARK 500 PRO C 944 79.25 -114.32
REMARK 500 GLU C 949 -44.49 -131.07
REMARK 500 LEU C 974 28.85 -66.38
REMARK 500 ARG C 981 -72.70 -56.60
REMARK 500 LEU C1046 40.90 -77.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1K04 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE FOCAL ADHESION TARGETING DOMAIN OF FOCAL
REMARK 900 ADHESION KINASE. CRYSTAL FORM II: FOUR HELICAL BUNDLE; HELIX
REMARK 900 EXCHANGED DIMER
DBREF 1K05 A 891 1052 UNP Q05397 FAK1_HUMAN 891 1052
DBREF 1K05 B 891 1052 UNP Q05397 FAK1_HUMAN 891 1052
DBREF 1K05 C 891 1052 UNP Q05397 FAK1_HUMAN 891 1052
SEQRES 1 A 162 LEU SER SER PRO ALA ASP SER TYR ASN GLU GLY VAL LYS
SEQRES 2 A 162 LEU GLN PRO GLN GLU ILE SER PRO PRO PRO THR ALA ASN
SEQRES 3 A 162 LEU ASP ARG SER ASN ASP LYS VAL TYR GLU ASN VAL THR
SEQRES 4 A 162 GLY LEU VAL LYS ALA VAL ILE GLU MET SER SER LYS ILE
SEQRES 5 A 162 GLN PRO ALA PRO PRO GLU GLU TYR VAL PRO MET VAL LYS
SEQRES 6 A 162 GLU VAL GLY LEU ALA LEU ARG THR LEU LEU ALA THR VAL
SEQRES 7 A 162 ASP GLU THR ILE PRO LEU LEU PRO ALA SER THR HIS ARG
SEQRES 8 A 162 GLU ILE GLU MET ALA GLN LYS LEU LEU ASN SER ASP LEU
SEQRES 9 A 162 GLY GLU LEU ILE ASN LYS MET LYS LEU ALA GLN GLN TYR
SEQRES 10 A 162 VAL MET THR SER LEU GLN GLN GLU TYR LYS LYS GLN MET
SEQRES 11 A 162 LEU THR ALA ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN
SEQRES 12 A 162 LEU LEU ASP VAL ILE ASP GLN ALA ARG LEU LYS MET LEU
SEQRES 13 A 162 GLY GLN THR ARG PRO HIS
SEQRES 1 B 162 LEU SER SER PRO ALA ASP SER TYR ASN GLU GLY VAL LYS
SEQRES 2 B 162 LEU GLN PRO GLN GLU ILE SER PRO PRO PRO THR ALA ASN
SEQRES 3 B 162 LEU ASP ARG SER ASN ASP LYS VAL TYR GLU ASN VAL THR
SEQRES 4 B 162 GLY LEU VAL LYS ALA VAL ILE GLU MET SER SER LYS ILE
SEQRES 5 B 162 GLN PRO ALA PRO PRO GLU GLU TYR VAL PRO MET VAL LYS
SEQRES 6 B 162 GLU VAL GLY LEU ALA LEU ARG THR LEU LEU ALA THR VAL
SEQRES 7 B 162 ASP GLU THR ILE PRO LEU LEU PRO ALA SER THR HIS ARG
SEQRES 8 B 162 GLU ILE GLU MET ALA GLN LYS LEU LEU ASN SER ASP LEU
SEQRES 9 B 162 GLY GLU LEU ILE ASN LYS MET LYS LEU ALA GLN GLN TYR
SEQRES 10 B 162 VAL MET THR SER LEU GLN GLN GLU TYR LYS LYS GLN MET
SEQRES 11 B 162 LEU THR ALA ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN
SEQRES 12 B 162 LEU LEU ASP VAL ILE ASP GLN ALA ARG LEU LYS MET LEU
SEQRES 13 B 162 GLY GLN THR ARG PRO HIS
SEQRES 1 C 162 LEU SER SER PRO ALA ASP SER TYR ASN GLU GLY VAL LYS
SEQRES 2 C 162 LEU GLN PRO GLN GLU ILE SER PRO PRO PRO THR ALA ASN
SEQRES 3 C 162 LEU ASP ARG SER ASN ASP LYS VAL TYR GLU ASN VAL THR
SEQRES 4 C 162 GLY LEU VAL LYS ALA VAL ILE GLU MET SER SER LYS ILE
SEQRES 5 C 162 GLN PRO ALA PRO PRO GLU GLU TYR VAL PRO MET VAL LYS
SEQRES 6 C 162 GLU VAL GLY LEU ALA LEU ARG THR LEU LEU ALA THR VAL
SEQRES 7 C 162 ASP GLU THR ILE PRO LEU LEU PRO ALA SER THR HIS ARG
SEQRES 8 C 162 GLU ILE GLU MET ALA GLN LYS LEU LEU ASN SER ASP LEU
SEQRES 9 C 162 GLY GLU LEU ILE ASN LYS MET LYS LEU ALA GLN GLN TYR
SEQRES 10 C 162 VAL MET THR SER LEU GLN GLN GLU TYR LYS LYS GLN MET
SEQRES 11 C 162 LEU THR ALA ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN
SEQRES 12 C 162 LEU LEU ASP VAL ILE ASP GLN ALA ARG LEU LYS MET LEU
SEQRES 13 C 162 GLY GLN THR ARG PRO HIS
FORMUL 4 HOH *6(H2 O)
HELIX 1 1 ASP A 922 ILE A 942 1 21
HELIX 2 2 PRO A 946 ILE A 972 1 27
HELIX 3 3 PRO A 973 LEU A 975 5 3
HELIX 4 4 PRO A 976 TYR A 1007 1 32
HELIX 5 5 LEU A 1012 GLY A 1047 1 36
HELIX 6 6 ASP B 918 ASN B 921 5 4
HELIX 7 7 ASP B 922 ILE B 942 1 21
HELIX 8 8 PRO B 946 ILE B 972 1 27
HELIX 9 9 PRO B 973 LEU B 975 5 3
HELIX 10 10 PRO B 976 TYR B 1007 1 32
HELIX 11 11 SER B 1011 GLY B 1047 1 37
HELIX 12 12 ASP C 918 ASN C 921 5 4
HELIX 13 13 ASP C 922 GLN C 943 1 22
HELIX 14 14 PRO C 946 ILE C 972 1 27
HELIX 15 15 PRO C 976 TYR C 1007 1 32
HELIX 16 16 THR C 1010 LEU C 1046 1 37
CRYST1 87.484 222.101 97.885 90.00 90.00 90.00 C 2 2 21 24
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 0.011431 0.000000 0.000000 0.00000
SCALE2 0.000000 0.004502 0.000000 0.00000
SCALE3 0.000000 0.000000 0.010216 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
