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Database: PDB
Entry: 1OW7
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HEADER    TRANSFERASE                             28-MAR-03   1OW7              
TITLE     PAXILLIN LD4 MOTIF BOUND TO THE FOCAL ADHESION TARGETING              
TITLE    2 (FAT) DOMAIN OF THE FOCAL ADHESION KINASE                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FOCAL ADHESION KINASE 1;                                   
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: FOCAL ADHESION TARGETING DOMAIN;                           
COMPND   5 SYNONYM: FADK 1, PP125FAK, PROTEIN- TYROSINE KINASE 2;               
COMPND   6 EC: 2.7.1.112;                                                       
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PAXILLIN;                                                  
COMPND  10 CHAIN: D, E, F;                                                      
COMPND  11 FRAGMENT: PAXILLIN LD4 MOTIF;                                        
COMPND  12 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: PTK2 OR FAK1 OR FAK;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P2;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: SEQUENCE DERIVED FROM HUMAN PAXILLIN                  
KEYWDS    4 HELICAL BUNDLE, AMPHIPHATIC HELIX, TRANSFERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.K.HOELLERER,M.E.M.NOBLE,G.LABESSE,J.M.WERNER,S.T.AROLD              
REVDAT   2   24-FEB-09 1OW7    1       VERSN                                    
REVDAT   1   21-OCT-03 1OW7    0                                                
JRNL        AUTH   M.K.HOELLERER,M.E.M.NOBLE,G.LABESSE,J.M.WERNER,              
JRNL        AUTH 2 S.T.AROLD                                                    
JRNL        TITL   MOLECULAR RECOGNITION OF PAXILLIN LD MOTIFS BY THE           
JRNL        TITL 2 FOCAL ADHESION TARGETING DOMAIN                              
JRNL        REF    STRUCTURE                     V.  11  1207 2003              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   14527389                                                     
JRNL        DOI    10.1016/J.STR.2003.08.010                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 111.80                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 78.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23071                          
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) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.237                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1189                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 785                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 48                           
REMARK   3   BIN FREE R VALUE                    : 0.4630                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3470                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 50                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 76.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 74.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 7.65000                                              
REMARK   3    B22 (A**2) : -3.19000                                             
REMARK   3    B33 (A**2) : -4.46000                                             
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): 0.460         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.311         
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      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3509 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3367 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4744 ; 1.713 ; 2.010       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  7895 ; 3.480 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   442 ; 1.430 ; 5.000       
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):   585 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3761 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   538 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1038 ; 0.251 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3922 ; 0.294 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1835 ; 0.107 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    57 ; 0.174 ; 0.200       
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):    15 ; 0.278 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    73 ; 0.309 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.142 ; 0.200       
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):  2252 ; 2.828 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3644 ; 5.037 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1257 ; 4.743 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1100 ; 7.598 ; 4.500       
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 : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: 1) THE SECOND LD4 MOTIF (CHAIN F,         
REMARK   3  BOUND TO MOLECULE C) WAS FITTED INTO THE UNBIASED 3FO-2FC MAPS      
REMARK   3  (CNS). ITS POSITION AND ORIENTATION WERE INFERRED FROM              
REMARK   3  HOMOLOGY WITH THE WELL-DEFINED OTHER LD4 - FAT INTERACTION          
REMARK   3  (CHAINS A AND C), AND ARE SUPPORTED BY NMR DATA(SEE                 
REMARK   3  PUBLICATION). 2) THE CRYSTAL DIFFRACTED ANISOTROPICALLY TO 2.8      
REMARK   3  AND 2.6 A RESOLUTION. THE WEAK, BUT CONSISTENT, DATA TO 2.6 A       
REMARK   3  WERE INCLUDED, AS THEY SIGNIFICANTLY IMPROVED THE ELECTRON          
REMARK   3  DENSITY.                                                            
REMARK   4                                                                      
REMARK   4 1OW7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-MAR-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018728.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SILICON                            
REMARK 200  OPTICS                         : TWO CRYSTALS MONOCHROMATOR         
REMARK 200                                   BETWEEN TWO CYLINDRICAL            
REMARK 200                                   PARABOLIC MIRRORS                  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23071                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.7                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : 0.06400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.86000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.62000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDBENTRY 1K05                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CHLORIDE, GLYCEROL, HEPES,        
REMARK 280  PH 6.3, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K             
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       48.09950            
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       48.09950            
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       44.49700            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      109.83250            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.49700            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      109.83250            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       48.09950            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.49700            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      109.83250            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       48.09950            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.49700            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      109.83250            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B  60  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C   4  LIES ON A SPECIAL POSITION.                          
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   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     ARG A  1050                                                      
REMARK 465     PRO A  1051                                                      
REMARK 465     HIS A  1052                                                      
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     PRO B   906                                                      
REMARK 465     GLN B   907                                                      
REMARK 465     GLU B   908                                                      
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     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     GLN C   907                                                      
REMARK 465     GLU C   908                                                      
REMARK 465     GLN C  1048                                                      
REMARK 465     THR C  1049                                                      
REMARK 465     ARG C  1050                                                      
REMARK 465     PRO C  1051                                                      
REMARK 465     HIS C  1052                                                      
REMARK 465     ALA D     1                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     ALA F     1                                                      
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    SER A 920      -39.71    -39.13                                   
REMARK 500    TYR A1007       32.90    -91.74                                   
REMARK 500    MET A1009       13.73     81.75                                   
REMARK 500    MET B1009       -3.32     72.96                                   
REMARK 500    ASN C 916       21.89    -71.05                                   
REMARK 500    LYS C 941      -94.67    -97.28                                   
REMARK 500    ILE C 942      -47.69      4.76                                   
REMARK 500    PRO C 944      -78.50    -55.50                                   
REMARK 500    ALA C 945      142.87    -29.64                                   
REMARK 500    TYR C1016       -1.48    -56.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1K05   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE FOCAL ADHESION TARGETING DOMAIN OF          
REMARK 900 FOCAL ADHESION KINASE                                                
DBREF  1OW7 A  892  1052  UNP    Q05397   FAK1_HUMAN     892   1052             
DBREF  1OW7 B  892  1052  UNP    Q05397   FAK1_HUMAN     892   1052             
DBREF  1OW7 C  892  1052  UNP    Q05397   FAK1_HUMAN     892   1052             
DBREF  1OW7 D    1    13  PDB    1OW7     1OW7             1     13             
DBREF  1OW7 E    1    13  PDB    1OW7     1OW7             1     13             
DBREF  1OW7 F    1    13  PDB    1OW7     1OW7             1     13             
SEQRES   1 A  161  SER SER PRO ALA ASP SER TYR ASN GLU GLY VAL LYS LEU          
SEQRES   2 A  161  GLN PRO GLN GLU ILE SER PRO PRO PRO THR ALA ASN LEU          
SEQRES   3 A  161  ASP ARG SER ASN ASP LYS VAL TYR GLU ASN VAL THR GLY          
SEQRES   4 A  161  LEU VAL LYS ALA VAL ILE GLU MET SER SER LYS ILE GLN          
SEQRES   5 A  161  PRO ALA PRO PRO GLU GLU TYR VAL PRO MET VAL LYS GLU          
SEQRES   6 A  161  VAL GLY LEU ALA LEU ARG THR LEU LEU ALA THR VAL ASP          
SEQRES   7 A  161  GLU THR ILE PRO LEU LEU PRO ALA SER THR HIS ARG GLU          
SEQRES   8 A  161  ILE GLU MET ALA GLN LYS LEU LEU ASN SER ASP LEU GLY          
SEQRES   9 A  161  GLU LEU ILE ASN LYS MET LYS LEU ALA GLN GLN TYR VAL          
SEQRES  10 A  161  MET THR SER LEU GLN GLN GLU TYR LYS LYS GLN MET LEU          
SEQRES  11 A  161  THR ALA ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN LEU          
SEQRES  12 A  161  LEU ASP VAL ILE ASP GLN ALA ARG LEU LYS MET LEU GLY          
SEQRES  13 A  161  GLN THR ARG PRO HIS                                          
SEQRES   1 B  161  SER SER PRO ALA ASP SER TYR ASN GLU GLY VAL LYS LEU          
SEQRES   2 B  161  GLN PRO GLN GLU ILE SER PRO PRO PRO THR ALA ASN LEU          
SEQRES   3 B  161  ASP ARG SER ASN ASP LYS VAL TYR GLU ASN VAL THR GLY          
SEQRES   4 B  161  LEU VAL LYS ALA VAL ILE GLU MET SER SER LYS ILE GLN          
SEQRES   5 B  161  PRO ALA PRO PRO GLU GLU TYR VAL PRO MET VAL LYS GLU          
SEQRES   6 B  161  VAL GLY LEU ALA LEU ARG THR LEU LEU ALA THR VAL ASP          
SEQRES   7 B  161  GLU THR ILE PRO LEU LEU PRO ALA SER THR HIS ARG GLU          
SEQRES   8 B  161  ILE GLU MET ALA GLN LYS LEU LEU ASN SER ASP LEU GLY          
SEQRES   9 B  161  GLU LEU ILE ASN LYS MET LYS LEU ALA GLN GLN TYR VAL          
SEQRES  10 B  161  MET THR SER LEU GLN GLN GLU TYR LYS LYS GLN MET LEU          
SEQRES  11 B  161  THR ALA ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN LEU          
SEQRES  12 B  161  LEU ASP VAL ILE ASP GLN ALA ARG LEU LYS MET LEU GLY          
SEQRES  13 B  161  GLN THR ARG PRO HIS                                          
SEQRES   1 C  161  SER SER PRO ALA ASP SER TYR ASN GLU GLY VAL LYS LEU          
SEQRES   2 C  161  GLN PRO GLN GLU ILE SER PRO PRO PRO THR ALA ASN LEU          
SEQRES   3 C  161  ASP ARG SER ASN ASP LYS VAL TYR GLU ASN VAL THR GLY          
SEQRES   4 C  161  LEU VAL LYS ALA VAL ILE GLU MET SER SER LYS ILE GLN          
SEQRES   5 C  161  PRO ALA PRO PRO GLU GLU TYR VAL PRO MET VAL LYS GLU          
SEQRES   6 C  161  VAL GLY LEU ALA LEU ARG THR LEU LEU ALA THR VAL ASP          
SEQRES   7 C  161  GLU THR ILE PRO LEU LEU PRO ALA SER THR HIS ARG GLU          
SEQRES   8 C  161  ILE GLU MET ALA GLN LYS LEU LEU ASN SER ASP LEU GLY          
SEQRES   9 C  161  GLU LEU ILE ASN LYS MET LYS LEU ALA GLN GLN TYR VAL          
SEQRES  10 C  161  MET THR SER LEU GLN GLN GLU TYR LYS LYS GLN MET LEU          
SEQRES  11 C  161  THR ALA ALA HIS ALA LEU ALA VAL ASP ALA LYS ASN LEU          
SEQRES  12 C  161  LEU ASP VAL ILE ASP GLN ALA ARG LEU LYS MET LEU GLY          
SEQRES  13 C  161  GLN THR ARG PRO HIS                                          
SEQRES   1 D   13  ALA THR ARG GLU LEU ASP GLU LEU MET ALA SER LEU SER          
SEQRES   1 E   13  ALA THR ARG GLU LEU ASP GLU LEU MET ALA SER LEU SER          
SEQRES   1 F   13  ALA THR ARG GLU LEU ASP GLU LEU MET ALA SER LEU SER          
FORMUL   7  HOH   *50(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 THR A  979  TYR A 1007  1                                  29    
HELIX    5   5 LEU A 1012  GLY A 1047  1                                  36    
HELIX    6   6 ASP B  922  ILE B  942  1                                  21    
HELIX    7   7 PRO B  946  GLU B  970  1                                  25    
HELIX    8   8 THR B  971  LEU B  975  5                                   5    
HELIX    9   9 PRO B  976  SER B  978  5                                   3    
HELIX   10  10 THR B  979  TYR B 1007  1                                  29    
HELIX   11  11 SER B 1011  LEU B 1046  1                                  36    
HELIX   12  12 ASP C  922  LYS C  941  1                                  20    
HELIX   13  13 PRO C  946  ILE C  972  1                                  27    
HELIX   14  14 THR C  979  TYR C 1007  1                                  29    
HELIX   15  15 THR C 1010  GLY C 1047  1                                  38    
HELIX   16  16 GLU D    4  LEU D   12  1                                   9    
HELIX   17  17 GLU E    4  ALA E   10  1                                   7    
HELIX   18  18 THR F    2  LEU F   12  1                                  11    
CRYST1   88.994  219.665   96.199  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      0.011237  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004552  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010395        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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