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Database: PDB
Entry: 2VRW
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Original site: 2VRW 
HEADER    SIGNALING PROTEIN                       16-APR-08   2VRW              
TITLE     CRITICAL STRUCTURAL ROLE FOR THE PH AND C1 DOMAINS OF THE             
TITLE    2 VAV1 EXCHANGE FACTOR                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-184;                                            
COMPND   5 SYNONYM: P21-RAC1, RAS- LIKE PROTEIN TC25, CELL MIGRATION-INDUCING   
COMPND   6  GENE 5 PROTEIN, RAC1;                                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROTO-ONCOGENE VAV;                                        
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: RESIDUES 170-575;                                          
COMPND  12 SYNONYM: P95VAV, VAV1;                                               
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1;                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PET24B                                    
KEYWDS    LIPOPROTEIN, GTP-BINDING, METAL-BINDING, PROTO-ONCOGENE,              
KEYWDS   2 PHOSPHOPROTEIN, EXCHANGE FACTOR, RAC, VAV, GTPASE, MEMBRANE, SH2     
KEYWDS   3 DOMAIN, SH3 DOMAIN, METHYLATION, ZINC-FINGER, PRENYLATION,           
KEYWDS   4 GUANINE-NUCLEOTIDE RELEASING FACTOR, PHORBOL-ESTER BINDING,          
KEYWDS   5 ADP-RIBOSYLATION, NUCLEOTIDE-BINDING, SIGNALING PROTEIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.RAPLEY,V.TYBULEWICZ,K.RITTINGER                                     
REVDAT   4   13-JUL-11 2VRW    1       VERSN                                    
REVDAT   3   24-FEB-09 2VRW    1       VERSN                                    
REVDAT   2   08-JUL-08 2VRW    1       JRNL   REMARK                            
REVDAT   1   17-JUN-08 2VRW    0                                                
JRNL        AUTH   J.RAPLEY,V.TYBULEWICZ,K.RITTINGER                            
JRNL        TITL   CRUCIAL STRUCTURAL ROLE FOR THE PH AND C1 DOMAINS OF THE     
JRNL        TITL 2 VAV1 EXCHANGE FACTOR.                                        
JRNL        REF    EMBO REP.                     V.   9   655 2008              
JRNL        REFN                   ISSN 1469-221X                               
JRNL        PMID   18511940                                                     
JRNL        DOI    10.1038/EMBOR.2008.80                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 1.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 54863                          
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) : 0.205                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.251                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2937                            
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) : 1.85                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.90                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3906                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 202                          
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4410                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 471                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.03000                                             
REMARK   3    B22 (A**2) : -0.58000                                             
REMARK   3    B33 (A**2) : 0.26000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.36000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.142         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.098         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.338         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4498 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6069 ; 1.031 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   545 ; 5.242 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   217 ;34.943 ;23.917       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   835 ;13.546 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    34 ;16.614 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   671 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3377 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2151 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3089 ; 0.298 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   420 ; 0.125 ; 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):    68 ; 0.171 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.153 ; 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):  2821 ; 0.542 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4400 ; 0.901 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1901 ; 1.463 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1668 ; 2.328 ; 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  : 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     1        A   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5140 -28.5920  16.8848              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0301 T22:  -0.0357                                     
REMARK   3      T33:  -0.0252 T12:  -0.0295                                     
REMARK   3      T13:  -0.0283 T23:   0.0407                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9408 L22:   1.3813                                     
REMARK   3      L33:   1.1312 L12:  -0.7714                                     
REMARK   3      L13:   0.7795 L23:  -0.1047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1580 S12:   0.1519 S13:   0.1391                       
REMARK   3      S21:  -0.0534 S22:   0.0393 S23:   0.0722                       
REMARK   3      S31:  -0.1139 S32:   0.0403 S33:   0.1187                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   190        B   373                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.0518 -43.2341  34.7584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0190 T22:  -0.0311                                     
REMARK   3      T33:  -0.0337 T12:  -0.0062                                     
REMARK   3      T13:   0.0126 T23:   0.0042                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5288 L22:   1.2227                                     
REMARK   3      L33:   0.5868 L12:   0.6008                                     
REMARK   3      L13:   0.4449 L23:   0.2923                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0201 S12:   0.0040 S13:   0.0121                       
REMARK   3      S21:   0.0428 S22:   0.0158 S23:   0.0322                       
REMARK   3      S31:   0.0312 S32:  -0.0406 S33:  -0.0358                       
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   374        B   508                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.7588 -57.4588   1.9478              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0107 T22:  -0.0356                                     
REMARK   3      T33:  -0.0549 T12:   0.0125                                     
REMARK   3      T13:   0.0067 T23:  -0.0405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1124 L22:   0.6104                                     
REMARK   3      L33:   3.1994 L12:  -0.1691                                     
REMARK   3      L13:  -0.4719 L23:   0.1915                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0251 S12:   0.1084 S13:  -0.0379                       
REMARK   3      S21:  -0.0530 S22:  -0.0439 S23:   0.0588                       
REMARK   3      S31:   0.2326 S32:   0.1855 S33:   0.0188                       
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   509        B   564                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.3111 -45.8784  24.8559              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0651 T22:  -0.0341                                     
REMARK   3      T33:  -0.0200 T12:   0.0006                                     
REMARK   3      T13:  -0.0076 T23:  -0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9054 L22:   2.1745                                     
REMARK   3      L33:   1.5486 L12:   1.0536                                     
REMARK   3      L13:  -0.5063 L23:   0.7488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0792 S12:   0.0040 S13:   0.0134                       
REMARK   3      S21:   0.0070 S22:   0.0644 S23:  -0.0533                       
REMARK   3      S31:   0.0137 S32:   0.0438 S33:   0.0148                       
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          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2VRW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-APR-08.                  
REMARK 100 THE PDBE ID CODE IS EBI-35944.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-NOV-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX10.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.117                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DEN                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57653                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.85                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.5                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.20                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.3                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.46                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.80                               
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 50.91                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BICINE PH9.0 10% PEG 6000          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -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        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       61.38150            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.07150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       61.38150            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.07150            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 3010 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.7 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 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     CYS A   178                                                      
REMARK 465     PRO A   179                                                      
REMARK 465     PRO A   180                                                      
REMARK 465     PRO A   181                                                      
REMARK 465     VAL A   182                                                      
REMARK 465     LYS A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     ASP B   171                                                      
REMARK 465     GLU B   172                                                      
REMARK 465     ILE B   173                                                      
REMARK 465     TYR B   174                                                      
REMARK 465     GLU B   175                                                      
REMARK 465     ASP B   176                                                      
REMARK 465     LEU B   177                                                      
REMARK 465     MET B   178                                                      
REMARK 465     ARG B   179                                                      
REMARK 465     LEU B   180                                                      
REMARK 465     GLU B   181                                                      
REMARK 465     SER B   182                                                      
REMARK 465     VAL B   183                                                      
REMARK 465     PRO B   184                                                      
REMARK 465     THR B   185                                                      
REMARK 465     PRO B   186                                                      
REMARK 465     PRO B   187                                                      
REMARK 465     LYS B   188                                                      
REMARK 465     MET B   189                                                      
REMARK 465     ASP B   457                                                      
REMARK 465     SER B   458                                                      
REMARK 465     SER B   459                                                      
REMARK 465     GLY B   460                                                      
REMARK 465     GLU B   461                                                      
REMARK 465     ARG B   462                                                      
REMARK 465     ASP B   463                                                      
REMARK 465     ASN B   464                                                      
REMARK 465     GLY B   565                                                      
REMARK 465     ARG B   566                                                      
REMARK 465     HIS B   567                                                      
REMARK 465     GLY B   568                                                      
REMARK 465     GLN B   569                                                      
REMARK 465     ASP B   570                                                      
REMARK 465     PHE B   571                                                      
REMARK 465     ALA B   572                                                      
REMARK 465     GLY B   573                                                      
REMARK 465     THR B   574                                                      
REMARK 465     MET B   575                                                      
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     ASP B 456    CG   OD1  OD2                                       
REMARK 470     SER B 468    OG                                                  
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 B 556   CD    GLU B 556   OE2     0.076                       
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    ASN A  26      -65.38     73.60                                   
REMARK 500    LYS A  96      -57.68   -129.00                                   
REMARK 500    VAL B 238     -122.03     48.30                                   
REMARK 500    ASN B 316       19.50   -149.38                                   
REMARK 500    TYR B 541       58.48     33.43                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    GLU A  62        24.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1565  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 516   ND1                                                    
REMARK 620 2 CYS B 546   SG  108.6                                              
REMARK 620 3 CYS B 549   SG  109.3 107.1                                        
REMARK 620 4 CYS B 564   SG  107.9 113.2 110.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1566  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 532   SG                                                     
REMARK 620 2 HIS B 554   ND1  98.2                                              
REMARK 620 3 CYS B 529   SG  110.9 101.8                                        
REMARK 620 4 CYS B 557   SG  115.6 115.8 112.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1565                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  ZN B1566                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1E96   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF THE RAC/P67PHOX COMPLEX                                
REMARK 900 RELATED ID: 1I4D   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP                              
REMARK 900  COMPLEXED WITHARFAPTIN (P21)                                        
REMARK 900 RELATED ID: 1FOE   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF RAC1 IN COMPLEX WITH                           
REMARK 900  THE GUANINENUCLEOTIDE EXCHANGE REGION OF TIAM1                      
REMARK 900 RELATED ID: 1MH1   RELATED DB: PDB                                   
REMARK 900  SMALL G-PROTEIN                                                     
REMARK 900 RELATED ID: 1I4L   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF RAC1-GDP IN                           
REMARK 900  COMPLEX WITHARFAPTIN (P41)                                          
REMARK 900 RELATED ID: 1HE1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN THE                        
REMARK 900   GAP DOMAIN OF THE PSEUDOMONAS AERUGINOSA                           
REMARK 900  EXOS TOXIN AND HUMAN RAC                                            
REMARK 900 RELATED ID: 1RYF   RELATED DB: PDB                                   
REMARK 900  ALTERNATIVE SPLICING OF RAC1 GENERATES RAC1B                        
REMARK 900  , A SELF-ACTIVATING GTPASE                                          
REMARK 900 RELATED ID: 1K1Z   RELATED DB: PDB                                   
REMARK 900  SOLUTION STRUCTURE OF N-TERMINAL SH3 DOMAIN                         
REMARK 900   MUTANT(P33G) OFMURINE VAV                                          
REMARK 900 RELATED ID: 1RYH   RELATED DB: PDB                                   
REMARK 900  ALTERNATIVE SPLICING OF RAC1 GENERATES RAC1B                        
REMARK 900  , A SELF-ACTIVATING GTPASE                                          
REMARK 900 RELATED ID: 1HH4   RELATED DB: PDB                                   
REMARK 900  RAC1-RHOGDI COMPLEX INVOLVED IN NADPH                               
REMARK 900  OXIDASE ACTIVATION                                                  
REMARK 900 RELATED ID: 1GCP   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF VAV SH3 DOMAIN                                 
REMARK 900 RELATED ID: 1G4U   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE SALMONELLA TYROSINE                        
REMARK 900  PHOSPHATASEAND GTPASE ACTIVATING PROTEIN SPTP                       
REMARK 900  BOUND TO RAC1                                                       
REMARK 900 RELATED ID: 2FJU   RELATED DB: PDB                                   
REMARK 900  ACTIVATED RAC1 BOUND TO ITS EFFECTOR                                
REMARK 900  PHOSPHOLIPASE C BETA 2                                              
REMARK 900 RELATED ID: 1F5X   RELATED DB: PDB                                   
REMARK 900  NMR STRUCTURE OF THE Y174 AUTOINHIBITED DBL                         
REMARK 900   HOMOLGY DOMAIN                                                     
REMARK 900 RELATED ID: 1I4T   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE ANALYSIS OF RAC1-GMPPNP IN                        
REMARK 900   COMPLEX WITHARFAPTIN                                               
REMARK 900 RELATED ID: 1GCQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF VAV AND GRB2 SH3                               
REMARK 900  DOMAINS                                                             
DBREF  2VRW A    1   184  UNP    P63000   RAC1_HUMAN       1    184             
DBREF  2VRW B  170   575  UNP    P27870   VAV_MOUSE      170    575             
SEQRES   1 A  184  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 A  184  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 A  184  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 A  184  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 A  184  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 A  184  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 A  184  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 A  184  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 A  184  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 A  184  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 A  184  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 A  184  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 A  184  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 A  184  ASP GLU ALA ILE ARG ALA VAL LEU CYS PRO PRO PRO VAL          
SEQRES  15 A  184  LYS LYS                                                      
SEQRES   1 B  406  GLY ASP GLU ILE TYR GLU ASP LEU MET ARG LEU GLU SER          
SEQRES   2 B  406  VAL PRO THR PRO PRO LYS MET THR GLU TYR ASP LYS ARG          
SEQRES   3 B  406  CYS CYS CYS LEU ARG GLU ILE GLN GLN THR GLU GLU LYS          
SEQRES   4 B  406  TYR THR ASP THR LEU GLY SER ILE GLN GLN HIS PHE MET          
SEQRES   5 B  406  LYS PRO LEU GLN ARG PHE LEU LYS PRO GLN ASP MET GLU          
SEQRES   6 B  406  THR ILE PHE VAL ASN ILE GLU GLU LEU PHE SER VAL HIS          
SEQRES   7 B  406  THR HIS PHE LEU LYS GLU LEU LYS ASP ALA LEU ALA GLY          
SEQRES   8 B  406  PRO GLY ALA THR THR LEU TYR GLN VAL PHE ILE LYS TYR          
SEQRES   9 B  406  LYS GLU ARG PHE LEU VAL TYR GLY ARG TYR CYS SER GLN          
SEQRES  10 B  406  VAL GLU SER ALA SER LYS HIS LEU ASP GLN VAL ALA THR          
SEQRES  11 B  406  ALA ARG GLU ASP VAL GLN MET LYS LEU GLU GLU CYS SER          
SEQRES  12 B  406  GLN ARG ALA ASN ASN GLY ARG PHE THR LEU ARG ASP LEU          
SEQRES  13 B  406  LEU MET VAL PRO MET GLN ARG VAL LEU LYS TYR HIS LEU          
SEQRES  14 B  406  LEU LEU GLN GLU LEU VAL LYS HIS THR GLN ASP ALA THR          
SEQRES  15 B  406  GLU LYS GLU ASN LEU ARG LEU ALA LEU ASP ALA MET ARG          
SEQRES  16 B  406  ASP LEU ALA GLN CYS VAL ASN GLU VAL LYS ARG ASP ASN          
SEQRES  17 B  406  GLU THR LEU ARG GLN ILE THR ASN PHE GLN LEU SER ILE          
SEQRES  18 B  406  GLU ASN LEU ASP GLN SER LEU ALA ASN TYR GLY ARG PRO          
SEQRES  19 B  406  LYS ILE ASP GLY GLU LEU LYS ILE THR SER VAL GLU ARG          
SEQRES  20 B  406  ARG SER LYS THR ASP ARG TYR ALA PHE LEU LEU ASP LYS          
SEQRES  21 B  406  ALA LEU LEU ILE CYS LYS ARG ARG GLY ASP SER TYR ASP          
SEQRES  22 B  406  LEU LYS ALA SER VAL ASN LEU HIS SER PHE GLN VAL ARG          
SEQRES  23 B  406  ASP ASP SER SER GLY GLU ARG ASP ASN LYS LYS TRP SER          
SEQRES  24 B  406  HIS MET PHE LEU LEU ILE GLU ASP GLN GLY ALA GLN GLY          
SEQRES  25 B  406  TYR GLU LEU PHE PHE LYS THR ARG GLU LEU LYS LYS LYS          
SEQRES  26 B  406  TRP MET GLU GLN PHE GLU MET ALA ILE SER ASN ILE TYR          
SEQRES  27 B  406  PRO GLU ASN ALA THR ALA ASN GLY HIS ASP PHE GLN MET          
SEQRES  28 B  406  PHE SER PHE GLU GLU THR THR SER CYS LYS ALA CYS GLN          
SEQRES  29 B  406  MET LEU LEU ARG GLY THR PHE TYR GLN GLY TYR ARG CYS          
SEQRES  30 B  406  TYR ARG CYS ARG ALA PRO ALA HIS LYS GLU CYS LEU GLY          
SEQRES  31 B  406  ARG VAL PRO PRO CYS GLY ARG HIS GLY GLN ASP PHE ALA          
SEQRES  32 B  406  GLY THR MET                                                  
HET     ZN  B1565       1                                                       
HET     ZN  B1566       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  HOH   *471(H2 O)                                                    
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 LEU A   67  TYR A   72  5                                   6    
HELIX    3   3 SER A   86  LYS A   96  1                                  11    
HELIX    4   4 LYS A   96  CYS A  105  1                                  10    
HELIX    5   5 LYS A  116  ASP A  121  1                                   6    
HELIX    6   6 ASP A  122  LYS A  132  1                                  11    
HELIX    7   7 THR A  138  ILE A  149  1                                  12    
HELIX    8   8 GLY A  164  LEU A  177  1                                  14    
HELIX    9   9 THR B  190  PHE B  220  1                                  31    
HELIX   10  10 PHE B  220  GLN B  225  1                                   6    
HELIX   11  11 LYS B  229  VAL B  238  1                                  10    
HELIX   12  12 ASN B  239  GLY B  260  1                                  22    
HELIX   13  13 PRO B  261  THR B  264  5                                   4    
HELIX   14  14 THR B  265  LYS B  274  1                                  10    
HELIX   15  15 GLU B  275  PHE B  277  5                                   3    
HELIX   16  16 LEU B  278  ASN B  317  1                                  40    
HELIX   17  17 THR B  321  LEU B  326  1                                   6    
HELIX   18  18 MET B  327  LEU B  334  1                                   8    
HELIX   19  19 LYS B  335  THR B  347  1                                  13    
HELIX   20  20 ASP B  349  SER B  389  1                                  41    
HELIX   21  21 SER B  396  GLY B  401  5                                   6    
HELIX   22  22 THR B  488  TYR B  507  1                                  20    
HELIX   23  23 THR B  512  HIS B  516  5                                   5    
HELIX   24  24 HIS B  554  VAL B  561  5                                   8    
SHEET    1  AA 6 TYR A  40  VAL A  46  0                                        
SHEET    2  AA 6 LYS A  49  TRP A  56 -1  O  LYS A  49   N  VAL A  46           
SHEET    3  AA 6 ALA A   3  GLY A  10  1  O  ILE A   4   N  GLY A  54           
SHEET    4  AA 6 VAL A  77  SER A  83  1  O  VAL A  77   N  VAL A   7           
SHEET    5  AA 6 ILE A 110  THR A 115  1  O  ILE A 111   N  ILE A  80           
SHEET    6  AA 6 LYS A 153  GLU A 156  1  O  LYS A 153   N  LEU A 112           
SHEET    1  BA 8 ILE B 390  GLU B 391  0                                        
SHEET    2  BA 8 SER B 440  ASN B 448  1  O  TYR B 441   N  GLU B 391           
SHEET    3  BA 8 ALA B 430  ARG B 437 -1  O  LEU B 431   N  VAL B 447           
SHEET    4  BA 8 THR B 420  LEU B 427 -1  O  TYR B 423   N  CYS B 434           
SHEET    5  BA 8 PRO B 403  THR B 412 -1  N  LYS B 404   O  LEU B 426           
SHEET    6  BA 8 GLY B 481  PHE B 486 -1  O  GLU B 483   N  THR B 412           
SHEET    7  BA 8 HIS B 469  GLU B 475 -1  O  HIS B 469   N  PHE B 486           
SHEET    8  BA 8 PHE B 452  ARG B 455 -1  O  GLN B 453   N  ILE B 474           
SHEET    1  BB 3 PHE B 518  PHE B 521  0                                        
SHEET    2  BB 3 GLY B 543  CYS B 546 -1  O  GLY B 543   N  PHE B 521           
SHEET    3  BB 3 PRO B 552  ALA B 553 -1  O  ALA B 553   N  TYR B 544           
LINK        ZN    ZN B1565                 ND1 HIS B 516     1555   1555  2.10  
LINK        ZN    ZN B1565                 SG  CYS B 546     1555   1555  2.29  
LINK        ZN    ZN B1565                 SG  CYS B 549     1555   1555  2.29  
LINK        ZN    ZN B1565                 SG  CYS B 564     1555   1555  2.43  
LINK        ZN    ZN B1566                 ND1 HIS B 554     1555   1555  2.16  
LINK        ZN    ZN B1566                 SG  CYS B 529     1555   1555  2.32  
LINK        ZN    ZN B1566                 SG  CYS B 557     1555   1555  2.29  
LINK        ZN    ZN B1566                 SG  CYS B 532     1555   1555  2.30  
SITE     1 AC1  4 HIS B 516  CYS B 546  CYS B 549  CYS B 564                    
SITE     1 AC2  4 CYS B 529  CYS B 532  HIS B 554  CYS B 557                    
CRYST1  122.763   62.143  103.281  90.00 118.80  90.00 C 1 2 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      0.008146  0.000000  0.004478        0.00000                         
SCALE2      0.000000  0.016092  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011049        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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