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Database: PDB
Entry: 3TH5
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Original site: 3TH5 
HEADER    SIGNALING PROTEIN                       18-AUG-11   3TH5              
TITLE     CRYSTAL STRUCTURE OF WILD-TYPE RAC1                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 2-177;                                        
COMPND   5 SYNONYM: CELL MIGRATION-INDUCING GENE 5 PROTEIN, RAS-LIKE PROTEIN    
COMPND   6 TC25, P21-RAC1;                                                      
COMPND   7 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: RAC1, TC25, MIG5;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: MODIFIED PET-28                       
KEYWDS    ROSSMANN FOLD, GTPASE, GTP BINDING, PROTEIN BINDING, SIGNALING        
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.H.HA,T.J.BOGGON                                                     
REVDAT   4   12-DEC-12 3TH5    1       REMARK                                   
REVDAT   3   19-SEP-12 3TH5    1       JRNL                                     
REVDAT   2   29-AUG-12 3TH5    1       JRNL                                     
REVDAT   1   18-JUL-12 3TH5    0                                                
JRNL        AUTH   M.KRAUTHAMMER,Y.KONG,B.H.HA,P.EVANS,A.BACCHIOCCHI,           
JRNL        AUTH 2 J.P.MCCUSKER,E.CHENG,M.J.DAVIS,G.GOH,M.CHOI,S.ARIYAN,        
JRNL        AUTH 3 D.NARAYAN,K.DUTTON-REGESTER,A.CAPATANA,E.C.HOLMAN,           
JRNL        AUTH 4 M.BOSENBERG,M.SZNOL,H.M.KLUGER,D.E.BRASH,D.F.STERN,          
JRNL        AUTH 5 M.A.MATERIN,R.S.LO,S.MANE,S.MA,K.K.KIDD,N.K.HAYWARD,         
JRNL        AUTH 6 R.P.LIFTON,J.SCHLESSINGER,T.J.BOGGON,R.HALABAN               
JRNL        TITL   EXOME SEQUENCING IDENTIFIES RECURRENT SOMATIC RAC1 MUTATIONS 
JRNL        TITL 2 IN MELANOMA.                                                 
JRNL        REF    NAT.GENET.                    V.  44  1006 2012              
JRNL        REFN                   ISSN 1061-4036                               
JRNL        PMID   22842228                                                     
JRNL        DOI    10.1038/NG.2359                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 17830                          
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) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 910                             
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1259                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.10                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 63                           
REMARK   3   BIN FREE R VALUE                    : 0.4210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2710                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 23                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 48.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.48000                                              
REMARK   3    B22 (A**2) : -2.34000                                             
REMARK   3    B33 (A**2) : 0.87000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.04000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.253         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.250         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 21.911        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.937                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2863 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3915 ; 1.106 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   352 ; 5.041 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   116 ;39.487 ;24.397       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   482 ;14.714 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;14.567 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   451 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2107 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1744 ; 0.204 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2842 ; 0.385 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1119 ; 0.500 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1069 ; 0.827 ; 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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      2       A     177      4                      
REMARK   3           1     B      2       B     177      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):   1311 ;  0.23 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    B (A**2):   1311 ;  0.12 ;  2.00           
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     2        A    76                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.6680  -6.6970  -2.2400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2623 T22:   0.7249                                     
REMARK   3      T33:   0.5935 T12:   0.0258                                     
REMARK   3      T13:  -0.0463 T23:  -0.0106                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6763 L22:   5.6796                                     
REMARK   3      L33:   8.9141 L12:   1.2895                                     
REMARK   3      L13:   1.7593 L23:  -0.0740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2774 S12:  -0.2464 S13:   1.6547                       
REMARK   3      S21:  -0.1156 S22:   0.1816 S23:   0.2893                       
REMARK   3      S31:  -0.9330 S32:  -0.2306 S33:   0.0958                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    77        A   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.6580 -21.1840  -3.7070              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1577 T22:   0.8582                                     
REMARK   3      T33:   0.2593 T12:  -0.0107                                     
REMARK   3      T13:  -0.0297 T23:   0.0461                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5940 L22:   3.1818                                     
REMARK   3      L33:   6.0691 L12:   0.9611                                     
REMARK   3      L13:   0.3057 L23:  -0.3342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0760 S12:  -0.0933 S13:  -0.0102                       
REMARK   3      S21:  -0.2231 S22:   0.1027 S23:   0.0196                       
REMARK   3      S31:   0.3048 S32:  -0.3128 S33:  -0.1787                       
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     2        B    76                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.3570 -40.1460 -27.3570              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2766 T22:   0.8137                                     
REMARK   3      T33:   0.6506 T12:   0.0370                                     
REMARK   3      T13:   0.0592 T23:  -0.0580                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.5918 L22:   5.6657                                     
REMARK   3      L33:   7.8487 L12:   1.3888                                     
REMARK   3      L13:  -2.5051 L23:  -0.7769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2911 S12:  -0.0883 S13:  -1.6185                       
REMARK   3      S21:  -0.0718 S22:   0.3042 S23:  -0.3715                       
REMARK   3      S31:   1.3454 S32:   0.0227 S33:  -0.0131                       
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    77        B   177                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.3090 -25.6200 -28.2400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0385 T22:   0.8921                                     
REMARK   3      T33:   0.2870 T12:   0.0138                                     
REMARK   3      T13:   0.0157 T23:  -0.0602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3630 L22:   6.4646                                     
REMARK   3      L33:   5.4203 L12:  -0.0391                                     
REMARK   3      L13:  -0.1218 L23:  -0.8359                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1017 S12:   0.0620 S13:   0.0129                       
REMARK   3      S21:  -0.0093 S22:   0.1128 S23:  -0.4189                       
REMARK   3      S31:  -0.1188 S32:   0.4167 S33:  -0.0112                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3TH5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB067471.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-AUG-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97921                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18169                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.29500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3SBD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.65                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG4000, 7% ISOPROPANOL, 0.1M        
REMARK 280  HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K      
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       48.92550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -26                                                      
REMARK 465     GLY A   -25                                                      
REMARK 465     SER A   -24                                                      
REMARK 465     SER A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     GLY A   -14                                                      
REMARK 465     LEU A   -13                                                      
REMARK 465     VAL A   -12                                                      
REMARK 465     PRO A   -11                                                      
REMARK 465     ARG A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     MET A    -6                                                      
REMARK 465     GLU A    -5                                                      
REMARK 465     ASN A    -4                                                      
REMARK 465     LEU A    -3                                                      
REMARK 465     TYR A    -2                                                      
REMARK 465     PHE A    -1                                                      
REMARK 465     GLN A     0                                                      
REMARK 465     GLY A     1                                                      
REMARK 465     MET B   -26                                                      
REMARK 465     GLY B   -25                                                      
REMARK 465     SER B   -24                                                      
REMARK 465     SER B   -23                                                      
REMARK 465     HIS B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     GLY B   -14                                                      
REMARK 465     LEU B   -13                                                      
REMARK 465     VAL B   -12                                                      
REMARK 465     PRO B   -11                                                      
REMARK 465     ARG B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     MET B    -6                                                      
REMARK 465     GLU B    -5                                                      
REMARK 465     ASN B    -4                                                      
REMARK 465     LEU B    -3                                                      
REMARK 465     TYR B    -2                                                      
REMARK 465     PHE B    -1                                                      
REMARK 465     GLN B     0                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     GLU B    31                                                      
REMARK 465     TYR B    32                                                      
REMARK 465     ILE B    33                                                      
REMARK 465     PRO B    34                                                      
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    VAL A  36      -61.68    -95.17                                   
REMARK 500    PHE A  37      122.35   -172.20                                   
REMARK 500    LYS A  96      -53.32   -124.28                                   
REMARK 500    ALA B  13       15.22     86.51                                   
REMARK 500    PHE B  37      130.18   -172.42                                   
REMARK 500    LYS B  96      -53.47   -120.67                                   
REMARK 500    ASP B 121       64.38   -108.55                                   
REMARK 500    LYS B 123      -81.26    -51.55                                   
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                              MG A1002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  35   OG1                                                    
REMARK 620 2 GNP A1001   O2G  92.6                                              
REMARK 620 3 GNP A1001   O2B 168.7  86.2                                        
REMARK 620 4 THR A  17   OG1  82.5 171.8  97.4                                  
REMARK 620 5 HOH A 188   O    97.6  99.8  93.7  87.4                            
REMARK 620 6 HOH A 187   O    83.4  81.6  85.3  91.2 178.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1002  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  17   OG1                                                    
REMARK 620 2 GNP B1001   O2B  95.5                                              
REMARK 620 3 GNP B1001   O2G 158.6  86.6                                        
REMARK 620 4 THR B  35   OG1  81.4 152.1  86.8                                  
REMARK 620 5 HOH B 186   O   109.5 100.9  90.9 106.3                            
REMARK 620 6 HOH B 184   O    79.8  79.7  79.6  72.5 170.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1002                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3SBD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3SBE   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GZL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4GZM   RELATED DB: PDB                                   
DBREF  3TH5 A    2   177  UNP    P63000   RAC1_HUMAN       2    177             
DBREF  3TH5 B    2   177  UNP    P63000   RAC1_HUMAN       2    177             
SEQADV 3TH5 MET A  -26  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLY A  -25  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 SER A  -24  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 SER A  -23  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS A  -22  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS A  -21  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS A  -20  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS A  -19  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS A  -18  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS A  -17  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 SER A  -16  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 SER A  -15  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLY A  -14  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 LEU A  -13  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 VAL A  -12  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 PRO A  -11  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 ARG A  -10  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLY A   -9  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 SER A   -8  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS A   -7  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 MET A   -6  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLU A   -5  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 ASN A   -4  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 LEU A   -3  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 TYR A   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 PHE A   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLN A    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLY A    1  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 MET B  -26  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLY B  -25  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 SER B  -24  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 SER B  -23  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS B  -22  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS B  -21  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS B  -20  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS B  -19  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS B  -18  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS B  -17  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 SER B  -16  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 SER B  -15  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLY B  -14  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 LEU B  -13  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 VAL B  -12  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 PRO B  -11  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 ARG B  -10  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLY B   -9  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 SER B   -8  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 HIS B   -7  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 MET B   -6  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLU B   -5  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 ASN B   -4  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 LEU B   -3  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 TYR B   -2  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 PHE B   -1  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLN B    0  UNP  P63000              EXPRESSION TAG                 
SEQADV 3TH5 GLY B    1  UNP  P63000              EXPRESSION TAG                 
SEQRES   1 A  204  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  204  LEU VAL PRO ARG GLY SER HIS MET GLU ASN LEU TYR PHE          
SEQRES   3 A  204  GLN GLY GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY          
SEQRES   4 A  204  ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR          
SEQRES   5 A  204  ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP          
SEQRES   6 A  204  ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL          
SEQRES   7 A  204  ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR          
SEQRES   8 A  204  ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL          
SEQRES   9 A  204  PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE          
SEQRES  10 A  204  GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS          
SEQRES  11 A  204  HIS CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS          
SEQRES  12 A  204  LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU          
SEQRES  13 A  204  LYS GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY          
SEQRES  14 A  204  LEU ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU          
SEQRES  15 A  204  GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL          
SEQRES  16 A  204  PHE ASP GLU ALA ILE ARG ALA VAL LEU                          
SEQRES   1 B  204  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  204  LEU VAL PRO ARG GLY SER HIS MET GLU ASN LEU TYR PHE          
SEQRES   3 B  204  GLN GLY GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY          
SEQRES   4 B  204  ALA VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR          
SEQRES   5 B  204  ASN ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP          
SEQRES   6 B  204  ASN TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL          
SEQRES   7 B  204  ASN LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR          
SEQRES   8 B  204  ASP ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL          
SEQRES   9 B  204  PHE LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE          
SEQRES  10 B  204  GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS          
SEQRES  11 B  204  HIS CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS          
SEQRES  12 B  204  LEU ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU          
SEQRES  13 B  204  LYS GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY          
SEQRES  14 B  204  LEU ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU          
SEQRES  15 B  204  GLU CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL          
SEQRES  16 B  204  PHE ASP GLU ALA ILE ARG ALA VAL LEU                          
HET    GNP  A1001      32                                                       
HET     MG  A1002       1                                                       
HET    GNP  B1001      32                                                       
HET     MG  B1002       1                                                       
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
HETNAM      MG MAGNESIUM ION                                                    
FORMUL   3  GNP    2(C10 H17 N6 O13 P3)                                         
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   7  HOH   *23(H2 O)                                                     
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 GLN A   61  ASP A   65  5                                   5    
HELIX    3   3 LEU A   67  TYR A   72  5                                   6    
HELIX    4   4 SER A   86  LYS A   96  1                                  11    
HELIX    5   5 LYS A   96  CYS A  105  1                                  10    
HELIX    6   6 LYS A  116  ASP A  121  5                                   6    
HELIX    7   7 ASP A  122  GLU A  131  1                                  10    
HELIX    8   8 THR A  138  ILE A  149  1                                  12    
HELIX    9   9 GLY A  164  ALA A  175  1                                  12    
HELIX   10  10 GLY B   15  ASN B   26  1                                  12    
HELIX   11  11 GLN B   61  ASP B   65  5                                   5    
HELIX   12  12 LEU B   67  TYR B   72  5                                   6    
HELIX   13  13 SER B   86  LYS B   96  1                                  11    
HELIX   14  14 LYS B   96  CYS B  105  1                                  10    
HELIX   15  15 LYS B  116  ASP B  121  1                                   6    
HELIX   16  16 ASP B  122  GLU B  131  1                                  10    
HELIX   17  17 THR B  138  ILE B  149  1                                  12    
HELIX   18  18 GLY B  164  ALA B  175  1                                  12    
SHEET    1   A 6 PHE A  37  VAL A  46  0                                        
SHEET    2   A 6 LYS A  49  THR A  58 -1  O  LEU A  55   N  TYR A  40           
SHEET    3   A 6 ALA A   3  GLY A  10  1  N  CYS A   6   O  GLY A  54           
SHEET    4   A 6 VAL A  77  SER A  83  1  O  LEU A  79   N  VAL A   7           
SHEET    5   A 6 ILE A 110  THR A 115  1  O  ILE A 111   N  PHE A  78           
SHEET    6   A 6 LYS A 153  GLU A 156  1  O  LYS A 153   N  LEU A 112           
SHEET    1   B 6 ASP B  38  VAL B  46  0                                        
SHEET    2   B 6 LYS B  49  ASP B  57 -1  O  LEU B  55   N  TYR B  40           
SHEET    3   B 6 ALA B   3  GLY B  10  1  N  ILE B   4   O  GLY B  54           
SHEET    4   B 6 VAL B  77  SER B  83  1  O  LEU B  79   N  VAL B   9           
SHEET    5   B 6 ILE B 110  THR B 115  1  O  VAL B 113   N  ILE B  80           
SHEET    6   B 6 LYS B 153  GLU B 156  1  O  LEU B 155   N  GLY B 114           
LINK         OG1 THR A  35                MG    MG A1002     1555   1555  1.84  
LINK         OG1 THR B  17                MG    MG B1002     1555   1555  1.88  
LINK         O2G GNP A1001                MG    MG A1002     1555   1555  1.94  
LINK         O2B GNP B1001                MG    MG B1002     1555   1555  1.99  
LINK         O2B GNP A1001                MG    MG A1002     1555   1555  2.00  
LINK         O2G GNP B1001                MG    MG B1002     1555   1555  2.00  
LINK         OG1 THR A  17                MG    MG A1002     1555   1555  2.12  
LINK         OG1 THR B  35                MG    MG B1002     1555   1555  2.23  
LINK        MG    MG B1002                 O   HOH B 186     1555   1555  1.95  
LINK        MG    MG A1002                 O   HOH A 188     1555   1555  2.03  
LINK        MG    MG B1002                 O   HOH B 184     1555   1555  2.26  
LINK        MG    MG A1002                 O   HOH A 187     1555   1555  2.40  
SITE     1 AC1 21 GLY A  12  ALA A  13  VAL A  14  GLY A  15                    
SITE     2 AC1 21 LYS A  16  THR A  17  CYS A  18  PHE A  28                    
SITE     3 AC1 21 TYR A  32  THR A  35  GLY A  60  LYS A 116                    
SITE     4 AC1 21 ASP A 118  LEU A 119  SER A 158  ALA A 159                    
SITE     5 AC1 21 LEU A 160  HOH A 180  HOH A 187  HOH A 188                    
SITE     6 AC1 21  MG A1002                                                     
SITE     1 AC2  5 THR A  17  THR A  35  HOH A 187  HOH A 188                    
SITE     2 AC2  5 GNP A1001                                                     
SITE     1 AC3 19 GLY B  12  ALA B  13  VAL B  14  GLY B  15                    
SITE     2 AC3 19 LYS B  16  THR B  17  CYS B  18  PHE B  28                    
SITE     3 AC3 19 THR B  35  GLY B  60  LYS B 116  ASP B 118                    
SITE     4 AC3 19 LEU B 119  SER B 158  ALA B 159  LEU B 160                    
SITE     5 AC3 19 HOH B 184  HOH B 186   MG B1002                               
SITE     1 AC4  6 THR B  17  THR B  35  ASP B  57  HOH B 184                    
SITE     2 AC4  6 HOH B 186  GNP B1001                                          
CRYST1   40.925   97.851   51.733  90.00  96.59  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      0.024435  0.000000  0.002823        0.00000                         
SCALE2      0.000000  0.010220  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019459        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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