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Database: PDB
Entry: 3BJI
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Original site: 3BJI 
HEADER    SIGNALING PROTEIN                       04-DEC-07   3BJI              
TITLE     STRUCTURAL BASIS OF PROMISCUOUS GUANINE NUCLEOTIDE EXCHANGE           
TITLE    2 BY THE T-CELL ESSENTIAL VAV1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE VAV;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: VAV1 DH/PH/CRD;                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1                 
COMPND   8 PRECURSOR;                                                           
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 FRAGMENT: RAC1;                                                      
COMPND  11 SYNONYM: P21-RAC1, RAS- LIKE PROTEIN TC25, CELL MIGRATION-           
COMPND  12 INDUCING GENE 5 PROTEIN;                                             
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 GENE: VAV1, VAV;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (AI);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: RAC1;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(AI);                                  
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    PROTEIN-PROTEIN INTERACTION, GEF/GTPASE, ATYPICAL CYSTEINE            
KEYWDS   2 RICH DOMAIN, GUANINE-NUCLEOTIDE RELEASING FACTOR, METAL-             
KEYWDS   3 BINDING, PHORBOL-ESTER BINDING, PHOSPHOPROTEIN, PROTO-               
KEYWDS   4 ONCOGENE, SH2 DOMAIN, SH3 DOMAIN, ZINC, ZINC-FINGER, ADP-            
KEYWDS   5 RIBOSYLATION, ALTERNATIVE SPLICING, GTP-BINDING,                     
KEYWDS   6 LIPOPROTEIN, MEMBRANE, METHYLATION, NUCLEOTIDE-BINDING,              
KEYWDS   7 POLYMORPHISM, PRENYLATION, SIGNALING PROTEIN, STRUCTURAL             
KEYWDS   8 GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, ACCELERATED           
KEYWDS   9 TECHNOLOGIES CENTER FOR GENE TO 3D STRUCTURE, ATCG3D                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.E.CHRENCIK,A.BROOUN,P.KUHN,ACCELERATED TECHNOLOGIES CENTER          
AUTHOR   2 FOR GENE TO 3D STRUCTURE (ATCG3D)                                    
REVDAT   3   01-SEP-09 3BJI    1       AUTHOR KEYWDS REMARK                     
REVDAT   2   24-FEB-09 3BJI    1       VERSN                                    
REVDAT   1   15-JUL-08 3BJI    0                                                
JRNL        AUTH   J.E.CHRENCIK,A.BROOUN,H.ZHANG,I.I.MATHEWS,G.L.HURA,          
JRNL        AUTH 2 S.A.FOSTER,J.J.PERRY,M.STREIFF,P.RAMAGE,H.WIDMER,            
JRNL        AUTH 3 G.M.BOKOCH,J.A.TAINER,G.WECKBECKER,P.KUHN                    
JRNL        TITL   STRUCTURAL BASIS OF GUANINE NUCLEOTIDE EXCHANGE              
JRNL        TITL 2 MEDIATED BY THE T-CELL ESSENTIAL VAV1.                       
JRNL        REF    J.MOL.BIOL.                   V. 380   828 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18589439                                                     
JRNL        DOI    10.1016/J.JMB.2008.05.024                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 36156                          
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) : 0.225                           
REMARK   3   R VALUE            (WORKING SET) : 0.221                           
REMARK   3   FREE R VALUE                     : 0.293                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1939                            
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) : 1861                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 105                          
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8359                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 60                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.51                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.12000                                             
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.10000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.127         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.375         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.270         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.481        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.923                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.873                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8550 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5686 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11577 ; 1.825 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 13869 ; 1.448 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1076 ;14.024 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   382 ;36.972 ;24.241       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1428 ;21.201 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    47 ;20.349 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1307 ; 0.276 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9567 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1735 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2205 ; 0.243 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  6017 ; 0.212 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4096 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4745 ; 0.097 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   257 ; 0.180 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     4 ; 0.059 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     3 ; 0.169 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    30 ; 0.205 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    71 ; 0.227 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.350 ; 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):  5550 ; 0.691 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2180 ; 0.094 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8624 ; 1.190 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3403 ; 1.428 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2953 ; 2.305 ; 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 : 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 3BJI COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-FEB-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB045597.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36156                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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) : 2.67                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: 1FOE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG-3350, 100 MM HEPES, PH 7.5,      
REMARK 280  200 MM AMMONIUM CHLORIDE, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       37.53950            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2590 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   458                                                      
REMARK 465     SER A   459                                                      
REMARK 465     GLY A   460                                                      
REMARK 465     ASP A   461                                                      
REMARK 465     ARG A   462                                                      
REMARK 465     GLY A   566                                                      
REMARK 465     SER B   458                                                      
REMARK 465     SER B   459                                                      
REMARK 465     GLY B   460                                                      
REMARK 465     ASP B   461                                                      
REMARK 465     ARG B   462                                                      
REMARK 465     ASP B   463                                                      
REMARK 465     ASP B   476                                                      
REMARK 465     GLN B   477                                                      
REMARK 465     GLY B   478                                                      
REMARK 465     ALA B   479                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     GLU D    31                                                      
REMARK 465     VAL D    46                                                      
REMARK 465     ASP D    47                                                      
REMARK 465     GLY D    48                                                      
REMARK 465     ASP D   124                                                      
REMARK 465     THR D   125                                                      
REMARK 465     ILE D   126                                                      
REMARK 465     GLU D   127                                                      
REMARK 465     LYS D   128                                                      
REMARK 465     LEU D   129                                                      
REMARK 465     LEU D   177                                                      
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     LYS A 194    CE   NZ                                             
REMARK 470     LYS A 222    CD   CE   NZ                                        
REMARK 470     ARG A 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 229    CE   NZ                                             
REMARK 470     ARG A 245    CZ   NH1  NH2                                       
REMARK 470     LYS A 252    CD   CE   NZ                                        
REMARK 470     THR A 260    OG1  CG2                                            
REMARK 470     ASN A 265    CG   OD1  ND2                                       
REMARK 470     TYR A 267    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 307    CD   CE   NZ                                        
REMARK 470     GLU A 309    CD   OE1  OE2                                       
REMARK 470     ARG A 319    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 323    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 345    CD   CE   NZ                                        
REMARK 470     GLU A 352    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 357    NE   CZ   NH1  NH2                                  
REMARK 470     GLN A 368    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 381    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 390    CG1  CG2  CD1                                       
REMARK 470     ASN A 392    CG   OD1  ND2                                       
REMARK 470     GLN A 395    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 416    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 435    CD   CE   NZ                                        
REMARK 470     ARG A 437    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 455    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 457    CG   OD1  OD2                                       
REMARK 470     ASP A 463    CG   OD1  OD2                                       
REMARK 470     LYS A 465    CG   CD   CE   NZ                                   
REMARK 470     LYS A 466    CE   NZ                                             
REMARK 470     SER A 468    OG                                                  
REMARK 470     GLN A 477    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 487    CE   NZ                                             
REMARK 470     ARG A 489    CZ   NH1  NH2                                       
REMARK 470     LYS A 493    CD   CE   NZ                                        
REMARK 470     GLU A 497    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 550    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 208    CE   NZ                                             
REMARK 470     LYS B 222    CD   CE   NZ                                        
REMARK 470     ARG B 226    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 245    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 252    CD   CE   NZ                                        
REMARK 470     LYS B 272    CD   CE   NZ                                        
REMARK 470     LYS B 292    CD   CE   NZ                                        
REMARK 470     GLU B 302    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 305    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 307    CE   NZ                                             
REMARK 470     GLU B 309    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 314    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 349    CD   OE1  OE2                                       
REMARK 470     ARG B 381    NH1  NH2                                            
REMARK 470     ASN B 392    CG   OD1  ND2                                       
REMARK 470     ASP B 394    CG   OD1  OD2                                       
REMARK 470     VAL B 414    CG1  CG2                                            
REMARK 470     GLU B 415    CG   CD   OE1                                       
REMARK 470     ARG B 416    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 417    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS B 419    CG   CD   CE   NZ                                   
REMARK 470     LYS B 435    CG   CD   CE   NZ                                   
REMARK 470     ARG B 436    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 453    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 455    CD   NE   CZ   NH1  NH2                             
REMARK 470     ASP B 457    CG   OD1  OD2                                       
REMARK 470     ASN B 464    CG   OD1  ND2                                       
REMARK 470     LYS B 465    CG   CD   CE   NZ                                   
REMARK 470     LYS B 466    CE   NZ                                             
REMARK 470     SER B 468    OG                                                  
REMARK 470     GLN B 480    CD   OE1  NE2                                       
REMARK 470     ARG B 489    CZ   NH1  NH2                                       
REMARK 470     GLU B 490    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 492    CE   NZ                                             
REMARK 470     LYS B 493    CD   CE   NZ                                        
REMARK 470     LYS B 494    CE   NZ                                             
REMARK 470     GLU B 524    CD   OE1  OE2                                       
REMARK 470     MET C   1    CB   CG   SD   CE                                   
REMARK 470     GLN C   2    CG   CD   OE1  NE2                                  
REMARK 470     PHE C  28    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU C  31    CG   CD   OE1  OE2                                  
REMARK 470     ILE C  33    CG1  CG2  CD1                                       
REMARK 470     LYS C  49    CG   CD   CE   NZ                                   
REMARK 470     LYS C 123    CG   CD   CE   NZ                                   
REMARK 470     ASP C 124    CG   OD1  OD2                                       
REMARK 470     GLU C 127    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 128    CG   CD   CE   NZ                                   
REMARK 470     GLU C 131    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 132    CG   CD   CE   NZ                                   
REMARK 470     LYS C 133    CG   CD   CE   NZ                                   
REMARK 470     LYS C 153    CD   CE   NZ                                        
REMARK 470     LEU C 160    CG   CD1  CD2                                       
REMARK 470     THR C 161    OG1  CG2                                            
REMARK 470     ARG C 163    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 166    CE   NZ                                             
REMARK 470     ASP C 170    CG   OD1  OD2                                       
REMARK 470     ARG C 174    NE   CZ   NH1  NH2                                  
REMARK 470     LEU C 177    CG   CD1  CD2                                       
REMARK 470     LEU D  19    CG   CD1  CD2                                       
REMARK 470     ASN D  26    CG   OD1  ND2                                       
REMARK 470     VAL D  44    CG1  CG2                                            
REMARK 470     MET D  45    CG   SD                                             
REMARK 470     LYS D  49    CD   CE   NZ                                        
REMARK 470     GLU D  91    CG   CD   OE1  OE2                                  
REMARK 470     VAL D 113    CG1  CG2                                            
REMARK 470     LEU D 117    CG   CD1  CD2                                       
REMARK 470     LEU D 119    CG   CD1  CD2                                       
REMARK 470     ARG D 120    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 121    CG   OD1  OD2                                       
REMARK 470     LYS D 130    CG   CD   CE   NZ                                   
REMARK 470     GLU D 131    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 132    CG   CD   CE   NZ                                   
REMARK 470     LYS D 133    CD   CE   NZ                                        
REMARK 470     ILE D 137    CG1  CG2  CD1                                       
REMARK 470     LYS D 147    CG   CD   CE   NZ                                   
REMARK 470     LYS D 153    CG   CD   CE   NZ                                   
REMARK 470     LEU D 160    CG   CD1  CD2                                       
REMARK 470     ARG D 163    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS D 166    CG   CD   CE   NZ                                   
REMARK 470     ARG D 174    CG   CD   NE   CZ   NH1  NH2                        
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    CYS A 549   CB    CYS A 549   SG     -0.181                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 198   N   -  CA  -  CB  ANGL. DEV. = -41.3 DEGREES          
REMARK 500    ARG A 226   N   -  CA  -  C   ANGL. DEV. = -20.6 DEGREES          
REMARK 500    ALA A 350   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    ASN A 392   N   -  CA  -  C   ANGL. DEV. = -19.0 DEGREES          
REMARK 500    ARG A 416   N   -  CA  -  C   ANGL. DEV. =  34.6 DEGREES          
REMARK 500    ARG A 417   N   -  CA  -  CB  ANGL. DEV. = -17.0 DEGREES          
REMARK 500    LYS A 493   N   -  CA  -  C   ANGL. DEV. = -21.3 DEGREES          
REMARK 500    CYS A 549   CB  -  CA  -  C   ANGL. DEV. = -12.5 DEGREES          
REMARK 500    CYS A 564   CA  -  CB  -  SG  ANGL. DEV. =   9.9 DEGREES          
REMARK 500    ARG B 375   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    SER B 396   N   -  CA  -  C   ANGL. DEV. = -19.8 DEGREES          
REMARK 500    ARG B 416   N   -  CA  -  CB  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    ILE B 506   N   -  CA  -  C   ANGL. DEV. = -21.7 DEGREES          
REMARK 500    PRO C  29   CB  -  CA  -  C   ANGL. DEV. = -18.9 DEGREES          
REMARK 500    GLN C 162   N   -  CA  -  C   ANGL. DEV. =  19.2 DEGREES          
REMARK 500    VAL D  14   CB  -  CA  -  C   ANGL. DEV. = -21.0 DEGREES          
REMARK 500    PRO D  87   C   -  N   -  CA  ANGL. DEV. =  19.0 DEGREES          
REMARK 500    PRO D  87   C   -  N   -  CD  ANGL. DEV. = -15.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 220      -62.95   -144.77                                   
REMARK 500    ARG A 226      -30.06   -144.40                                   
REMARK 500    ILE A 238     -123.19     44.49                                   
REMARK 500    THR A 260      -72.89    -72.31                                   
REMARK 500    PRO A 261      168.68    -47.83                                   
REMARK 500    ARG A 314      -31.73    -39.08                                   
REMARK 500    ASN A 316       30.43   -144.47                                   
REMARK 500    ALA A 350      -74.56    -79.12                                   
REMARK 500    GLN A 477       53.53   -102.11                                   
REMARK 500    LYS A 493      -45.37   -130.77                                   
REMARK 500    GLN A 533        0.34     80.91                                   
REMARK 500    PHE B 220      -57.77   -123.92                                   
REMARK 500    ILE B 238     -122.78     53.34                                   
REMARK 500    SER B 312       -7.25    -56.77                                   
REMARK 500    ALA B 315       55.14   -118.02                                   
REMARK 500    ASN B 317       51.50   -145.23                                   
REMARK 500    GLU B 391       32.81    -99.22                                   
REMARK 500    LEU B 393      104.76   -168.41                                   
REMARK 500    LYS B 404      -64.93    -93.93                                   
REMARK 500    SER B 413     -160.56   -119.76                                   
REMARK 500    ARG B 437      -63.79   -106.86                                   
REMARK 500    TRP B 467       18.28     55.40                                   
REMARK 500    MET B 520      128.47    -37.37                                   
REMARK 500    CYS B 532      -55.38   -133.36                                   
REMARK 500    GLN B 533       45.18   -155.01                                   
REMARK 500    PHE B 540      116.42   -162.28                                   
REMARK 500    PHE C  28       61.60   -153.67                                   
REMARK 500    LYS C  96      -57.19   -125.25                                   
REMARK 500    ASP C 124        5.39    -65.50                                   
REMARK 500    LYS C 133       43.06     82.16                                   
REMARK 500    THR C 161     -166.64   -165.09                                   
REMARK 500    ASP D  11      134.82    -32.65                                   
REMARK 500    ALA D  13       47.17     34.10                                   
REMARK 500    SER D  86      123.81   -172.77                                   
REMARK 500    PRO D  87      -79.57     27.97                                   
REMARK 500    LYS D  96      -59.26   -126.88                                   
REMARK 500    LYS D 116       63.21     64.95                                   
REMARK 500    CYS D 157     -178.08   -178.40                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLN A  225     ARG A  226                  -95.85                    
REMARK 500 GLU A  349     ALA A  350                  100.82                    
REMARK 500 ILE A  390     GLU A  391                 -138.16                    
REMARK 500 GLU A  391     ASN A  392                  146.91                    
REMARK 500 ARG A  416     ARG A  417                  -89.35                    
REMARK 500 LYS A  435     ARG A  436                 -100.31                    
REMARK 500 GLY A  478     ALA A  479                 -136.92                    
REMARK 500 LYS A  492     LYS A  493                  -91.65                    
REMARK 500 PRO B  261     GLY B  262                  -38.37                    
REMARK 500 GLY B  262     ALA B  263                  -85.35                    
REMARK 500 ALA B  263     ALA B  264                 -136.19                    
REMARK 500 GLN B  313     ARG B  314                  131.65                    
REMARK 500 ARG B  314     ALA B  315                 -132.98                    
REMARK 500 ALA B  315     ASN B  316                  -65.07                    
REMARK 500 ASN B  392     LEU B  393                  -78.55                    
REMARK 500 GLN B  395     SER B  396                  -66.26                    
REMARK 500 SER B  396     LEU B  397                 -145.72                    
REMARK 500 MET B  420     ASP B  421                 -143.54                    
REMARK 500 ASN B  505     ILE B  506                 -125.06                    
REMARK 500 ASN B  510     ALA B  511                  148.66                    
REMARK 500 ALA B  531     CYS B  532                  -97.71                    
REMARK 500 CYS B  532     GLN B  533                   39.71                    
REMARK 500 LYS C  130     GLU C  131                  145.44                    
REMARK 500 THR C  161     GLN C  162                   78.49                    
REMARK 500 ALA D   13     VAL D   14                   92.50                    
REMARK 500 SER D   86     PRO D   87                   67.46                    
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 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: (11X,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 349        21.3      L          L   OUTSIDE RANGE          
REMARK 500     ALA A 350        24.1      L          L   OUTSIDE RANGE          
REMARK 500     ARG A 416        15.4      L          L   OUTSIDE RANGE          
REMARK 500     ARG A 417        51.9      L          L   OUTSIDE RANGE          
REMARK 500     LYS A 493        47.5      L          L   OUTSIDE RANGE          
REMARK 500     ASP B 394        23.2      L          L   OUTSIDE RANGE          
REMARK 500     ARG B 416        24.5      L          L   OUTSIDE RANGE          
REMARK 500     THR C 161        16.1      L          L   OUTSIDE RANGE          
REMARK 500     GLN C 162        11.6      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 A   4  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 516   ND1                                                    
REMARK 620 2 CYS A 546   SG  125.0                                              
REMARK 620 3 CYS A 549   SG   95.3 118.7                                        
REMARK 620 4 CYS A 564   SG   89.9 124.5  95.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A   1  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 529   SG                                                     
REMARK 620 2 CYS A 532   SG   98.8                                              
REMARK 620 3 HIS A 554   ND1  93.2 100.0                                        
REMARK 620 4 CYS A 557   SG  120.4 117.9 121.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   2  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 516   ND1                                                    
REMARK 620 2 CYS B 546   SG  120.6                                              
REMARK 620 3 CYS B 549   SG  102.3 103.0                                        
REMARK 620 4 CYS B 564   SG  110.3 117.3  99.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B   3  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 529   SG                                                     
REMARK 620 2 CYS B 532   SG  107.3                                              
REMARK 620 3 HIS B 554   ND1 106.2 103.8                                        
REMARK 620 4 CYS B 557   SG  105.6 115.2 118.1                                  
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 A 1                    
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2                    
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 3                    
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 4                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FOE   RELATED DB: PDB                                   
REMARK 900 TIAM1/RAC CRYSTAL STRUCTURE                                          
REMARK 900 RELATED ID: 1F5X   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF VAV1                                           
REMARK 900 RELATED ID: ATCG3D_16   RELATED DB: TARGETDB                         
DBREF  3BJI A  189   565  UNP    P15498   VAV_HUMAN      189    565             
DBREF  3BJI B  189   565  UNP    P15498   VAV_HUMAN      189    565             
DBREF  3BJI C    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  3BJI D    1   177  UNP    P63000   RAC1_HUMAN       1    177             
SEQADV 3BJI GLY A  566  UNP  P15498              EXPRESSION TAG                 
SEQADV 3BJI GLY B  566  UNP  P15498              EXPRESSION TAG                 
SEQRES   1 A  378  MET THR GLU TYR ASP LYS ARG CYS CYS CYS LEU ARG GLU          
SEQRES   2 A  378  ILE GLN GLN THR GLU GLU LYS TYR THR ASP THR LEU GLY          
SEQRES   3 A  378  SER ILE GLN GLN HIS PHE LEU LYS PRO LEU GLN ARG PHE          
SEQRES   4 A  378  LEU LYS PRO GLN ASP ILE GLU ILE ILE PHE ILE ASN ILE          
SEQRES   5 A  378  GLU ASP LEU LEU ARG VAL HIS THR HIS PHE LEU LYS GLU          
SEQRES   6 A  378  MET LYS GLU ALA LEU GLY THR PRO GLY ALA ALA ASN LEU          
SEQRES   7 A  378  TYR GLN VAL PHE ILE LYS TYR LYS GLU ARG PHE LEU VAL          
SEQRES   8 A  378  TYR GLY ARG TYR CYS SER GLN VAL GLU SER ALA SER LYS          
SEQRES   9 A  378  HIS LEU ASP ARG VAL ALA ALA ALA ARG GLU ASP VAL GLN          
SEQRES  10 A  378  MET LYS LEU GLU GLU CYS SER GLN ARG ALA ASN ASN GLY          
SEQRES  11 A  378  ARG PHE THR LEU ARG ASP LEU LEU MET VAL PRO MET GLN          
SEQRES  12 A  378  ARG VAL LEU LYS TYR HIS LEU LEU LEU GLN GLU LEU VAL          
SEQRES  13 A  378  LYS HIS THR GLN GLU ALA MET GLU LYS GLU ASN LEU ARG          
SEQRES  14 A  378  LEU ALA LEU ASP ALA MET ARG ASP LEU ALA GLN CYS VAL          
SEQRES  15 A  378  ASN GLU VAL LYS ARG ASP ASN GLU THR LEU ARG GLN ILE          
SEQRES  16 A  378  THR ASN PHE GLN LEU SER ILE GLU ASN LEU ASP GLN SER          
SEQRES  17 A  378  LEU ALA HIS TYR GLY ARG PRO LYS ILE ASP GLY GLU LEU          
SEQRES  18 A  378  LYS ILE THR SER VAL GLU ARG ARG SER LYS MET ASP ARG          
SEQRES  19 A  378  TYR ALA PHE LEU LEU ASP LYS ALA LEU LEU ILE CYS LYS          
SEQRES  20 A  378  ARG ARG GLY ASP SER TYR ASP LEU LYS ASP PHE VAL ASN          
SEQRES  21 A  378  LEU HIS SER PHE GLN VAL ARG ASP ASP SER SER GLY ASP          
SEQRES  22 A  378  ARG ASP ASN LYS LYS TRP SER HIS MET PHE LEU LEU ILE          
SEQRES  23 A  378  GLU ASP GLN GLY ALA GLN GLY TYR GLU LEU PHE PHE LYS          
SEQRES  24 A  378  THR ARG GLU LEU LYS LYS LYS TRP MET GLU GLN PHE GLU          
SEQRES  25 A  378  MET ALA ILE SER ASN ILE TYR PRO GLU ASN ALA THR ALA          
SEQRES  26 A  378  ASN GLY HIS ASP PHE GLN MET PHE SER PHE GLU GLU THR          
SEQRES  27 A  378  THR SER CYS LYS ALA CYS GLN MET LEU LEU ARG GLY THR          
SEQRES  28 A  378  PHE TYR GLN GLY TYR ARG CYS HIS ARG CYS ARG ALA SER          
SEQRES  29 A  378  ALA HIS LYS GLU CYS LEU GLY ARG VAL PRO PRO CYS GLY          
SEQRES  30 A  378  GLY                                                          
SEQRES   1 B  378  MET THR GLU TYR ASP LYS ARG CYS CYS CYS LEU ARG GLU          
SEQRES   2 B  378  ILE GLN GLN THR GLU GLU LYS TYR THR ASP THR LEU GLY          
SEQRES   3 B  378  SER ILE GLN GLN HIS PHE LEU LYS PRO LEU GLN ARG PHE          
SEQRES   4 B  378  LEU LYS PRO GLN ASP ILE GLU ILE ILE PHE ILE ASN ILE          
SEQRES   5 B  378  GLU ASP LEU LEU ARG VAL HIS THR HIS PHE LEU LYS GLU          
SEQRES   6 B  378  MET LYS GLU ALA LEU GLY THR PRO GLY ALA ALA ASN LEU          
SEQRES   7 B  378  TYR GLN VAL PHE ILE LYS TYR LYS GLU ARG PHE LEU VAL          
SEQRES   8 B  378  TYR GLY ARG TYR CYS SER GLN VAL GLU SER ALA SER LYS          
SEQRES   9 B  378  HIS LEU ASP ARG VAL ALA ALA ALA ARG GLU ASP VAL GLN          
SEQRES  10 B  378  MET LYS LEU GLU GLU CYS SER GLN ARG ALA ASN ASN GLY          
SEQRES  11 B  378  ARG PHE THR LEU ARG ASP LEU LEU MET VAL PRO MET GLN          
SEQRES  12 B  378  ARG VAL LEU LYS TYR HIS LEU LEU LEU GLN GLU LEU VAL          
SEQRES  13 B  378  LYS HIS THR GLN GLU ALA MET GLU LYS GLU ASN LEU ARG          
SEQRES  14 B  378  LEU ALA LEU ASP ALA MET ARG ASP LEU ALA GLN CYS VAL          
SEQRES  15 B  378  ASN GLU VAL LYS ARG ASP ASN GLU THR LEU ARG GLN ILE          
SEQRES  16 B  378  THR ASN PHE GLN LEU SER ILE GLU ASN LEU ASP GLN SER          
SEQRES  17 B  378  LEU ALA HIS TYR GLY ARG PRO LYS ILE ASP GLY GLU LEU          
SEQRES  18 B  378  LYS ILE THR SER VAL GLU ARG ARG SER LYS MET ASP ARG          
SEQRES  19 B  378  TYR ALA PHE LEU LEU ASP LYS ALA LEU LEU ILE CYS LYS          
SEQRES  20 B  378  ARG ARG GLY ASP SER TYR ASP LEU LYS ASP PHE VAL ASN          
SEQRES  21 B  378  LEU HIS SER PHE GLN VAL ARG ASP ASP SER SER GLY ASP          
SEQRES  22 B  378  ARG ASP ASN LYS LYS TRP SER HIS MET PHE LEU LEU ILE          
SEQRES  23 B  378  GLU ASP GLN GLY ALA GLN GLY TYR GLU LEU PHE PHE LYS          
SEQRES  24 B  378  THR ARG GLU LEU LYS LYS LYS TRP MET GLU GLN PHE GLU          
SEQRES  25 B  378  MET ALA ILE SER ASN ILE TYR PRO GLU ASN ALA THR ALA          
SEQRES  26 B  378  ASN GLY HIS ASP PHE GLN MET PHE SER PHE GLU GLU THR          
SEQRES  27 B  378  THR SER CYS LYS ALA CYS GLN MET LEU LEU ARG GLY THR          
SEQRES  28 B  378  PHE TYR GLN GLY TYR ARG CYS HIS ARG CYS ARG ALA SER          
SEQRES  29 B  378  ALA HIS LYS GLU CYS LEU GLY ARG VAL PRO PRO CYS GLY          
SEQRES  30 B  378  GLY                                                          
SEQRES   1 C  177  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 C  177  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 C  177  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 C  177  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 C  177  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 C  177  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 C  177  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 C  177  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 C  177  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 C  177  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 C  177  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 C  177  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 C  177  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 C  177  ASP GLU ALA ILE ARG ALA VAL LEU                              
SEQRES   1 D  177  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 D  177  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 D  177  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 D  177  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 D  177  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 D  177  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 D  177  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 D  177  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 D  177  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 D  177  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 D  177  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 D  177  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 D  177  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 D  177  ASP GLU ALA ILE ARG ALA VAL LEU                              
HET     ZN  A   1       1                                                       
HET     ZN  A   4       1                                                       
HET     ZN  B   2       1                                                       
HET     ZN  B   3       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   9  HOH   *60(H2 O)                                                     
HELIX    1   1 THR A  190  HIS A  219  1                                  30    
HELIX    2   2 PHE A  220  GLN A  225  1                                   6    
HELIX    3   3 LYS A  229  ILE A  238  1                                  10    
HELIX    4   4 ASN A  239  THR A  260  1                                  22    
HELIX    5   5 LEU A  266  LYS A  274  1                                   9    
HELIX    6   6 GLU A  275  PHE A  277  5                                   3    
HELIX    7   7 LEU A  278  ARG A  301  1                                  24    
HELIX    8   8 ARG A  301  ASN A  317  1                                  17    
HELIX    9   9 THR A  321  MET A  327  1                                   7    
HELIX   10  10 MET A  327  LEU A  334  1                                   8    
HELIX   11  11 LYS A  335  LYS A  345  1                                  11    
HELIX   12  12 ALA A  350  SER A  389  1                                  40    
HELIX   13  13 SER A  396  GLY A  401  5                                   6    
HELIX   14  14 THR A  488  TYR A  507  1                                  20    
HELIX   15  15 THR A  512  HIS A  516  5                                   5    
HELIX   16  16 HIS A  554  VAL A  561  5                                   8    
HELIX   17  17 THR B  190  PHE B  220  1                                  31    
HELIX   18  18 PHE B  220  GLN B  225  1                                   6    
HELIX   19  19 LYS B  229  ILE B  238  1                                  10    
HELIX   20  20 ASN B  239  GLY B  259  1                                  21    
HELIX   21  21 ASN B  265  LYS B  274  1                                  10    
HELIX   22  22 GLU B  275  PHE B  277  5                                   3    
HELIX   23  23 LEU B  278  ARG B  301  1                                  24    
HELIX   24  24 ARG B  301  SER B  312  1                                  12    
HELIX   25  25 GLN B  313  ALA B  315  5                                   3    
HELIX   26  26 THR B  321  LEU B  326  1                                   6    
HELIX   27  27 MET B  327  LEU B  334  1                                   8    
HELIX   28  28 LYS B  335  HIS B  346  1                                  12    
HELIX   29  29 GLU B  349  ILE B  390  1                                  42    
HELIX   30  30 SER B  396  GLY B  401  5                                   6    
HELIX   31  31 THR B  488  ASN B  505  1                                  18    
HELIX   32  32 THR B  512  HIS B  516  5                                   5    
HELIX   33  33 HIS B  554  LEU B  558  5                                   5    
HELIX   34  34 GLY C   15  ASN C   26  1                                  12    
HELIX   35  35 LEU C   67  TYR C   72  5                                   6    
HELIX   36  36 SER C   86  LYS C   96  1                                  11    
HELIX   37  37 LYS C   96  CYS C  105  1                                  10    
HELIX   38  38 LYS C  116  ARG C  120  5                                   5    
HELIX   39  39 ASP C  122  LYS C  130  1                                   9    
HELIX   40  40 THR C  138  ILE C  149  1                                  12    
HELIX   41  41 GLY C  164  LEU C  177  1                                  14    
HELIX   42  42 GLY D   15  ASN D   26  1                                  12    
HELIX   43  43 LEU D   67  TYR D   72  5                                   6    
HELIX   44  44 PRO D   87  LYS D   96  1                                  10    
HELIX   45  45 LYS D   96  CYS D  105  1                                  10    
HELIX   46  46 THR D  138  ILE D  149  1                                  12    
HELIX   47  47 GLY D  164  VAL D  176  1                                  13    
SHEET    1   A 7 ASP A 442  ASN A 448  0                                        
SHEET    2   A 7 ALA A 430  LYS A 435 -1  N  ILE A 433   O  ASP A 445           
SHEET    3   A 7 MET A 420  LEU A 427 -1  N  LEU A 427   O  ALA A 430           
SHEET    4   A 7 PRO A 403  THR A 412 -1  N  LEU A 409   O  ARG A 422           
SHEET    5   A 7 GLY A 481  PHE A 486 -1  O  PHE A 485   N  LYS A 410           
SHEET    6   A 7 HIS A 469  GLU A 475 -1  N  PHE A 471   O  LEU A 484           
SHEET    7   A 7 PHE A 452  ASP A 456 -1  N  ARG A 455   O  LEU A 472           
SHEET    1   B 3 PHE A 518  PHE A 521  0                                        
SHEET    2   B 3 GLY A 543  CYS A 546 -1  O  ARG A 545   N  GLN A 519           
SHEET    3   B 3 SER A 552  ALA A 553 -1  O  ALA A 553   N  TYR A 544           
SHEET    1   C 7 TYR B 441  ASN B 448  0                                        
SHEET    2   C 7 ALA B 430  ARG B 436 -1  N  ILE B 433   O  ASP B 445           
SHEET    3   C 7 MET B 420  LEU B 427 -1  N  PHE B 425   O  LEU B 432           
SHEET    4   C 7 PRO B 403  THR B 412 -1  N  ILE B 411   O  MET B 420           
SHEET    5   C 7 TYR B 482  PHE B 486 -1  O  PHE B 485   N  LYS B 410           
SHEET    6   C 7 HIS B 469  ILE B 474 -1  N  PHE B 471   O  LEU B 484           
SHEET    7   C 7 GLN B 453  ASP B 456 -1  N  ARG B 455   O  LEU B 472           
SHEET    1   D 2 PHE B 518  PHE B 521  0                                        
SHEET    2   D 2 GLY B 543  CYS B 546 -1  O  ARG B 545   N  GLN B 519           
SHEET    1   E 6 TYR C  40  VAL C  46  0                                        
SHEET    2   E 6 LYS C  49  TRP C  56 -1  O  LEU C  55   N  TYR C  40           
SHEET    3   E 6 ILE C   4  GLY C  10  1  N  ILE C   4   O  GLY C  54           
SHEET    4   E 6 VAL C  77  SER C  83  1  O  CYS C  81   N  VAL C   9           
SHEET    5   E 6 ILE C 110  THR C 115  1  O  THR C 115   N  PHE C  82           
SHEET    6   E 6 LYS C 153  GLU C 156  1  O  LEU C 155   N  GLY C 114           
SHEET    1   F 6 TYR D  40  VAL D  44  0                                        
SHEET    2   F 6 VAL D  51  TRP D  56 -1  O  LEU D  53   N  ALA D  42           
SHEET    3   F 6 LYS D   5  VAL D   9  1  N  VAL D   8   O  TRP D  56           
SHEET    4   F 6 VAL D  77  SER D  83  1  O  LEU D  79   N  VAL D   9           
SHEET    5   F 6 ILE D 110  THR D 115  1  O  VAL D 113   N  ILE D  80           
SHEET    6   F 6 LYS D 153  CYS D 157  1  O  LYS D 153   N  LEU D 112           
LINK         ND1 HIS A 516                ZN    ZN A   4     1555   1555  2.04  
LINK         SG  CYS A 529                ZN    ZN A   1     1555   1555  2.14  
LINK         SG  CYS A 532                ZN    ZN A   1     1555   1555  2.25  
LINK         SG  CYS A 546                ZN    ZN A   4     1555   1555  2.05  
LINK         SG  CYS A 549                ZN    ZN A   4     1555   1555  2.00  
LINK         ND1 HIS A 554                ZN    ZN A   1     1555   1555  2.21  
LINK         SG  CYS A 557                ZN    ZN A   1     1555   1555  2.18  
LINK         SG  CYS A 564                ZN    ZN A   4     1555   1555  2.48  
LINK         ND1 HIS B 516                ZN    ZN B   2     1555   1555  1.85  
LINK         SG  CYS B 529                ZN    ZN B   3     1555   1555  2.31  
LINK         SG  CYS B 532                ZN    ZN B   3     1555   1555  2.43  
LINK         SG  CYS B 546                ZN    ZN B   2     1555   1555  2.31  
LINK         SG  CYS B 549                ZN    ZN B   2     1555   1555  2.27  
LINK         ND1 HIS B 554                ZN    ZN B   3     1555   1555  1.86  
LINK         SG  CYS B 557                ZN    ZN B   3     1555   1555  2.01  
LINK         SG  CYS B 564                ZN    ZN B   2     1555   1555  2.29  
CISPEP   1 SER A  389    ILE A  390          0       -28.51                     
SITE     1 AC1  4 CYS A 529  CYS A 532  HIS A 554  CYS A 557                    
SITE     1 AC2  4 HIS B 516  CYS B 546  CYS B 549  CYS B 564                    
SITE     1 AC3  4 CYS B 529  CYS B 532  HIS B 554  CYS B 557                    
SITE     1 AC4  4 HIS A 516  CYS A 546  CYS A 549  CYS A 564                    
CRYST1   78.948   75.079  114.857  90.00 103.87  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012667  0.000000  0.003129        0.00000                         
SCALE2      0.000000  0.013319  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008968        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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