GenomeNet

Database: PDB
Entry: 2P2L
LinkDB: 2P2L
Original site: 2P2L 
HEADER    UNKNOWN FUNCTION                        07-MAR-07   2P2L              
TITLE     RAC1-GDP-ZINC COMPLEX                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: P21-RAC1, RAS- LIKE PROTEIN TC25, CELL MIGRATION-INDUCING   
COMPND   5 GENE 5 PROTEIN;                                                      
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RAC1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX4T3                                   
KEYWDS    RHO FAMILY GTPASE, UNKNOWN FUNCTION                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.PREHNA,C.E.STEBBINS                                                 
REVDAT   3   13-JUL-11 2P2L    1       VERSN                                    
REVDAT   2   24-FEB-09 2P2L    1       VERSN                                    
REVDAT   1   01-MAY-07 2P2L    0                                                
JRNL        AUTH   G.PREHNA,C.E.STEBBINS                                        
JRNL        TITL   A RAC1-GDP TRIMER COMPLEX BINDS ZINC WITH TETRAHEDRAL AND    
JRNL        TITL 2 OCTAHEDRAL COORDINATION, DISPLACING MAGNESIUM.               
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  63   628 2007              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   17452788                                                     
JRNL        DOI    10.1107/S0907444907010888                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 77.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 67009                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3560                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4859                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 285                          
REMARK   3   BIN FREE R VALUE                    : 0.2930                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4141                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 804                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.63000                                              
REMARK   3    B22 (A**2) : 0.63000                                              
REMARK   3    B33 (A**2) : -0.94000                                             
REMARK   3    B12 (A**2) : 0.31000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.111         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.110         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.917         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4319 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3943 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5894 ; 1.627 ; 2.009       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9211 ; 0.911 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   528 ; 6.697 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   167 ;34.036 ;24.431       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   723 ;15.685 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;21.019 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   682 ; 0.105 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4651 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   808 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   946 ; 0.225 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4042 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2137 ; 0.178 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2263 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   626 ; 0.193 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.115 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     9 ; 0.052 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    16 ; 0.147 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    40 ; 0.311 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    47 ; 0.264 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):     2 ; 0.089 ; 0.200       
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):  3437 ; 1.278 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1069 ; 0.223 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4334 ; 1.474 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1963 ; 2.412 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1560 ; 3.447 ; 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  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    44                          
REMARK   3    RESIDUE RANGE :   A    49        A   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3553   9.8709 -12.4509              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1076 T22:  -0.0902                                     
REMARK   3      T33:  -0.1122 T12:  -0.0239                                     
REMARK   3      T13:  -0.0238 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3431 L22:   1.8347                                     
REMARK   3      L33:   1.7199 L12:  -0.6230                                     
REMARK   3      L13:  -0.2746 L23:  -0.2804                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0874 S12:  -0.0794 S13:   0.0445                       
REMARK   3      S21:   0.0526 S22:  -0.0488 S23:  -0.1221                       
REMARK   3      S31:  -0.0514 S32:   0.1365 S33:  -0.0387                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    48                          
REMARK   3    RESIDUE RANGE :   B    50        B   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.7280  45.2761 -13.1626              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0998 T22:  -0.0940                                     
REMARK   3      T33:  -0.1034 T12:   0.0068                                     
REMARK   3      T13:   0.0117 T23:  -0.0366                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3185 L22:   2.1068                                     
REMARK   3      L33:   1.6632 L12:   0.6837                                     
REMARK   3      L13:   0.0614 L23:   0.1684                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0127 S12:  -0.0573 S13:   0.1280                       
REMARK   3      S21:   0.0391 S22:   0.0470 S23:   0.0710                       
REMARK   3      S31:  -0.0069 S32:   0.1505 S33:  -0.0343                       
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 :   C     1        C   179                          
REMARK   3    ORIGIN FOR THE GROUP (A): -35.1557  26.9882 -11.4688              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0614 T22:  -0.1357                                     
REMARK   3      T33:  -0.1002 T12:  -0.0106                                     
REMARK   3      T13:   0.0236 T23:   0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1750 L22:   0.7824                                     
REMARK   3      L33:   1.2968 L12:  -0.0149                                     
REMARK   3      L13:  -0.3264 L23:   0.0962                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0213 S12:   0.0363 S13:  -0.0870                       
REMARK   3      S21:   0.0573 S22:   0.0024 S23:   0.0521                       
REMARK   3      S31:   0.0239 S32:  -0.0374 S33:   0.0189                       
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2P2L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAR-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041887.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JAN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 90                                 
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X3A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.284                              
REMARK 200  MONOCHROMATOR                  : DOUBLE FLAT CRYSTAL MONOCHROMATOR  
REMARK 200  OPTICS                         : DOUBLE CRYSTAL MONOCHROMATOR.      
REMARK 200                                   SI(111) OR SI(220) OPTIONS.        
REMARK 200                                   SAGITALL FOCUSING. CYLINDRICALLY   
REMARK 200                                   BENT ULE MIRROR WITH PT AND RH     
REMARK 200                                   COATING.                           
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70803                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 77.620                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: AND MOLECULAR REPLACEMENT    
REMARK 200 SOFTWARE USED: SOLVE, PHASER                                         
REMARK 200 STARTING MODEL: 1MH1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES PH6.0, 15MM ZNSO4, 10%         
REMARK 280  PEGMME 550., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      127.07867            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       63.53933            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       63.53933            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      127.07867            
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 300 REMARK: NORMALLY A MONOMER. IN THIS CRYSTAL STRUCTURE ZINC INDUCES   
REMARK 300 A TRIMER.                                                            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -269.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14140 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 46980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -604.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -63.53933            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A1057  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1075  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     LYS A    -1                                                      
REMARK 465     LEU A     0                                                      
REMARK 465     MET A    45                                                      
REMARK 465     VAL A    46                                                      
REMARK 465     ASP A    47                                                      
REMARK 465     PRO A   180                                                      
REMARK 465     PRO A   181                                                      
REMARK 465     VAL A   182                                                      
REMARK 465     LYS A   183                                                      
REMARK 465     LYS A   184                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     LYS B    -1                                                      
REMARK 465     LEU B     0                                                      
REMARK 465     LYS B    49                                                      
REMARK 465     PRO B   180                                                      
REMARK 465     PRO B   181                                                      
REMARK 465     VAL B   182                                                      
REMARK 465     LYS B   183                                                      
REMARK 465     LYS B   184                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     SER C    -2                                                      
REMARK 465     LYS C    -1                                                      
REMARK 465     LEU C     0                                                      
REMARK 465     PRO C   180                                                      
REMARK 465     PRO C   181                                                      
REMARK 465     VAL C   182                                                      
REMARK 465     LYS C   183                                                      
REMARK 465     LYS C   184                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1062     O    HOH A  1169              1.73            
REMARK 500   O    HOH A   946     O    HOH A  1152              1.78            
REMARK 500   OG1  THR C   125     O    HOH C   438              1.92            
REMARK 500   N    GLY B    60     O    HOH B   455              1.92            
REMARK 500   OD2  ASP C   122     O    HOH C   339              1.97            
REMARK 500   C    GLN B   162     O    HOH B   434              2.04            
REMARK 500   O    HOH C   236     O    HOH C   363              2.06            
REMARK 500   O    HOH C   354     O    HOH C   463              2.07            
REMARK 500   O    HOH C   343     O    HOH C   447              2.07            
REMARK 500   O    HOH B   304     O    HOH B   434              2.10            
REMARK 500   O    HOH A  1099     O    HOH A  1144              2.11            
REMARK 500   O    HOH C   412     O    HOH C   438              2.12            
REMARK 500   O    HOH A  1128     O    HOH A  1160              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   445     O    HOH C   427     4565     1.96            
REMARK 500   O    HOH B   351     O    HOH C   363     4565     1.97            
REMARK 500   O    HOH A  1140     O    HOH A  1169     4555     2.02            
REMARK 500   O    HOH B   290     O    HOH C   427     4565     2.16            
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    PRO A  50   C   -  N   -  CA  ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG A 120   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 163   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 120   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    LYS C 123   N   -  CA  -  C   ANGL. DEV. = -19.2 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    ALA A  59     -105.72   -101.43                                   
REMARK 500    PRO A  73     -175.83    -67.90                                   
REMARK 500    LYS A  96      -58.36   -129.56                                   
REMARK 500    ASP B  47     -131.23     50.75                                   
REMARK 500    ALA B  59     -103.85   -101.78                                   
REMARK 500    PRO B  73     -170.85    -68.78                                   
REMARK 500    LYS B  96      -57.71   -128.11                                   
REMARK 500    ASP C  47       55.08     27.94                                   
REMARK 500    ALA C  59     -107.74   -101.58                                   
REMARK 500    PRO C  73     -174.18    -68.09                                   
REMARK 500    LYS C  96      -55.97   -131.02                                   
REMARK 500    ASP C 122      145.68    142.39                                   
REMARK 500    ASP C 124       45.01    -64.95                                   
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 ASP C  122     LYS C  123                  114.64                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASP B 121        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ASP C 124        18.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 979        DISTANCE =  5.58 ANGSTROMS                       
REMARK 525    HOH A 999        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH A1013        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH A1020        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH A1025        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH A1032        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A1053        DISTANCE =  6.73 ANGSTROMS                       
REMARK 525    HOH A1062        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH A1096        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH A1106        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH A1115        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH A1121        DISTANCE =  6.42 ANGSTROMS                       
REMARK 525    HOH A1123        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH A1129        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH A1130        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH A1145        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH A1165        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH A1169        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A1172        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH B 342        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH B 347        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH B 368        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH B 369        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH B 372        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH B 373        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH B 374        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH B 377        DISTANCE =  6.32 ANGSTROMS                       
REMARK 525    HOH B 385        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH B 389        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH B 401        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH B 402        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH B 450        DISTANCE =  6.91 ANGSTROMS                       
REMARK 525    HOH B 456        DISTANCE =  7.32 ANGSTROMS                       
REMARK 525    HOH B 460        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH C 258        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH C 296        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH C 310        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH C 321        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH C 341        DISTANCE =  5.72 ANGSTROMS                       
REMARK 525    HOH C 367        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH C 378        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH C 386        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH C 400        DISTANCE =  7.25 ANGSTROMS                       
REMARK 525    HOH C 402        DISTANCE =  5.64 ANGSTROMS                       
REMARK 525    HOH C 413        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH C 420        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH C 429        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH C 430        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH C 436        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH C 440        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH C 464        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH C 465        DISTANCE =  6.44 ANGSTROMS                       
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 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1114   O                                                      
REMARK 620 2 HOH A1148   O    89.7                                              
REMARK 620 3 GDP A 200   O3B  91.9  92.3                                        
REMARK 620 4 HOH A 915   O   174.4  95.3  90.2                                  
REMARK 620 5 THR A  17   OG1  86.0 174.4  91.4  88.8                            
REMARK 620 6 THR A  35   O    89.0  84.9 177.1  89.2  91.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  63   OD1                                                    
REMARK 620 2 ASP A  63   OD2  54.0                                              
REMARK 620 3 GLU A 100   OE2 153.1 104.7                                        
REMARK 620 4 HIS A 104   NE2  85.1 114.7  91.4                                  
REMARK 620 5 HIS A 103   NE2  93.7 120.2 112.5 109.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 901  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A1125   O                                                      
REMARK 620 2 ASP A  38   OD1 111.3                                              
REMARK 620 3 ASP A  38   OD2  79.2  52.8                                        
REMARK 620 4 ASP C  38   OD1 109.6 107.9  81.2                                  
REMARK 620 5 ASP C  38   OD2  78.3 160.2 115.6  52.4                            
REMARK 620 6 ASP B  38   OD1 110.0 108.3 161.0 109.7  83.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 902  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 127   OE1                                                    
REMARK 620 2 GLU A 131   OE2 119.2                                              
REMARK 620 3 GLU C 127   OE2 139.8  92.7                                        
REMARK 620 4 GLU C 127   OE1  88.1 120.7  53.0                                  
REMARK 620 5 GLU C 131   OE2  97.9  98.8 100.8 130.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 431   O                                                      
REMARK 620 2 HOH B 412   O    93.1                                              
REMARK 620 3 HOH B 421   O    92.4 173.0                                        
REMARK 620 4 THR B  17   OG1 174.3  90.2  83.9                                  
REMARK 620 5 GDP B 200   O3B  93.1  91.9  92.0  91.4                            
REMARK 620 6 THR B  35   O    86.1  86.2  90.0  89.6 177.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  63   OD2                                                    
REMARK 620 2 GLU B 100   OE2 105.0                                              
REMARK 620 3 HIS B 104   NE2 114.3  98.8                                        
REMARK 620 4 HIS C 103   NE2 115.7 110.5 111.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C  35   O                                                      
REMARK 620 2 GDP C 200   O3B 177.0                                              
REMARK 620 3 HOH C 443   O    87.8  95.2                                        
REMARK 620 4 HOH C 424   O    88.6  88.4 175.4                                  
REMARK 620 5 HOH C 434   O    87.0  93.1  88.6  94.1                            
REMARK 620 6 THR C  17   OG1  87.9  92.2  87.0  90.0 173.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 202  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  63   OD1                                                    
REMARK 620 2 ASP C  63   OD2  53.1                                              
REMARK 620 3 GLU C 100   OE2 152.2 103.5                                        
REMARK 620 4 HIS C 104   NE2  85.7 114.5  93.0                                  
REMARK 620 5 HIS B 103   NE2  95.0 118.5 110.9 112.8                            
REMARK 620 N                    1     2     3     4                             
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 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 202                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 901                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 902                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP C 200                 
DBREF  2P2L A    1   184  UNP    P63000   RAC1_HUMAN       1    184             
DBREF  2P2L B    1   184  UNP    P63000   RAC1_HUMAN       1    184             
DBREF  2P2L C    1   184  UNP    P63000   RAC1_HUMAN       1    184             
SEQADV 2P2L GLY A   -3  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L SER A   -2  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L LYS A   -1  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L LEU A    0  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L SER A   78  UNP  P63000    PHE    78 CONFLICT                       
SEQADV 2P2L GLY B   -3  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L SER B   -2  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L LYS B   -1  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L LEU B    0  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L SER B   78  UNP  P63000    PHE    78 CONFLICT                       
SEQADV 2P2L GLY C   -3  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L SER C   -2  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L LYS C   -1  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L LEU C    0  UNP  P63000              CLONING ARTIFACT               
SEQADV 2P2L SER C   78  UNP  P63000    PHE    78 CONFLICT                       
SEQRES   1 A  188  GLY SER LYS LEU MET GLN ALA ILE LYS CYS VAL VAL VAL          
SEQRES   2 A  188  GLY ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER          
SEQRES   3 A  188  TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR          
SEQRES   4 A  188  VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY          
SEQRES   5 A  188  LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN          
SEQRES   6 A  188  GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN          
SEQRES   7 A  188  THR ASP VAL SER LEU ILE CYS PHE SER LEU VAL SER PRO          
SEQRES   8 A  188  ALA SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU          
SEQRES   9 A  188  VAL ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL          
SEQRES  10 A  188  GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE          
SEQRES  11 A  188  GLU LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR          
SEQRES  12 A  188  PRO GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL          
SEQRES  13 A  188  LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU          
SEQRES  14 A  188  LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS          
SEQRES  15 A  188  PRO PRO PRO VAL LYS LYS                                      
SEQRES   1 B  188  GLY SER LYS LEU MET GLN ALA ILE LYS CYS VAL VAL VAL          
SEQRES   2 B  188  GLY ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER          
SEQRES   3 B  188  TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR          
SEQRES   4 B  188  VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY          
SEQRES   5 B  188  LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN          
SEQRES   6 B  188  GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN          
SEQRES   7 B  188  THR ASP VAL SER LEU ILE CYS PHE SER LEU VAL SER PRO          
SEQRES   8 B  188  ALA SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU          
SEQRES   9 B  188  VAL ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL          
SEQRES  10 B  188  GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE          
SEQRES  11 B  188  GLU LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR          
SEQRES  12 B  188  PRO GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL          
SEQRES  13 B  188  LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU          
SEQRES  14 B  188  LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS          
SEQRES  15 B  188  PRO PRO PRO VAL LYS LYS                                      
SEQRES   1 C  188  GLY SER LYS LEU MET GLN ALA ILE LYS CYS VAL VAL VAL          
SEQRES   2 C  188  GLY ASP GLY ALA VAL GLY LYS THR CYS LEU LEU ILE SER          
SEQRES   3 C  188  TYR THR THR ASN ALA PHE PRO GLY GLU TYR ILE PRO THR          
SEQRES   4 C  188  VAL PHE ASP ASN TYR SER ALA ASN VAL MET VAL ASP GLY          
SEQRES   5 C  188  LYS PRO VAL ASN LEU GLY LEU TRP ASP THR ALA GLY GLN          
SEQRES   6 C  188  GLU ASP TYR ASP ARG LEU ARG PRO LEU SER TYR PRO GLN          
SEQRES   7 C  188  THR ASP VAL SER LEU ILE CYS PHE SER LEU VAL SER PRO          
SEQRES   8 C  188  ALA SER PHE GLU ASN VAL ARG ALA LYS TRP TYR PRO GLU          
SEQRES   9 C  188  VAL ARG HIS HIS CYS PRO ASN THR PRO ILE ILE LEU VAL          
SEQRES  10 C  188  GLY THR LYS LEU ASP LEU ARG ASP ASP LYS ASP THR ILE          
SEQRES  11 C  188  GLU LYS LEU LYS GLU LYS LYS LEU THR PRO ILE THR TYR          
SEQRES  12 C  188  PRO GLN GLY LEU ALA MET ALA LYS GLU ILE GLY ALA VAL          
SEQRES  13 C  188  LYS TYR LEU GLU CYS SER ALA LEU THR GLN ARG GLY LEU          
SEQRES  14 C  188  LYS THR VAL PHE ASP GLU ALA ILE ARG ALA VAL LEU CYS          
SEQRES  15 C  188  PRO PRO PRO VAL LYS LYS                                      
HET     ZN  A 201       1                                                       
HET     ZN  A 202       1                                                       
HET     ZN  B 201       1                                                       
HET     ZN  B 202       1                                                       
HET     ZN  C 201       1                                                       
HET     ZN  C 202       1                                                       
HET     ZN  A 901       1                                                       
HET     ZN  A 902       1                                                       
HET    GDP  A 200      28                                                       
HET    GDP  B 200      28                                                       
HET    GDP  C 200      28                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   4   ZN    8(ZN 2+)                                                     
FORMUL  12  GDP    3(C10 H15 N5 O11 P2)                                         
FORMUL  15  HOH   *804(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 SER A   86  LYS A   96  1                                  11    
HELIX    4   4 LYS A   96  CYS A  105  1                                  10    
HELIX    5   5 LYS A  116  ARG A  120  5                                   5    
HELIX    6   6 ASP A  122  LYS A  132  1                                  11    
HELIX    7   7 THR A  138  ILE A  149  1                                  12    
HELIX    8   8 GLY A  164  CYS A  178  1                                  15    
HELIX    9   9 GLY B   15  ASN B   26  1                                  12    
HELIX   10  10 GLN B   61  ASP B   65  5                                   5    
HELIX   11  11 SER B   86  LYS B   96  1                                  11    
HELIX   12  12 LYS B   96  CYS B  105  1                                  10    
HELIX   13  13 LYS B  116  ARG B  120  5                                   5    
HELIX   14  14 ASP B  122  LYS B  132  1                                  11    
HELIX   15  15 THR B  138  GLY B  150  1                                  13    
HELIX   16  16 GLY B  164  CYS B  178  1                                  15    
HELIX   17  17 GLY C   15  ASN C   26  1                                  12    
HELIX   18  18 GLN C   61  ASP C   65  5                                   5    
HELIX   19  19 SER C   86  LYS C   96  1                                  11    
HELIX   20  20 LYS C   96  CYS C  105  1                                  10    
HELIX   21  21 LYS C  116  ASP C  121  1                                   6    
HELIX   22  22 ASP C  124  LYS C  132  1                                   9    
HELIX   23  23 THR C  138  ILE C  149  1                                  12    
HELIX   24  24 GLY C  164  CYS C  178  1                                  15    
SHEET    1   A 7 LYS A 153  GLU A 156  0                                        
SHEET    2   A 7 ILE A 110  THR A 115  1  N  LEU A 112   O  LEU A 155           
SHEET    3   A 7 VAL A  77  SER A  83  1  N  ILE A  80   O  VAL A 113           
SHEET    4   A 7 GLN A   2  VAL A   9  1  N  VAL A   9   O  LEU A  79           
SHEET    5   A 7 VAL A  51  TRP A  56  1  O  GLY A  54   N  ILE A   4           
SHEET    6   A 7 TYR A  40  VAL A  44 -1  N  TYR A  40   O  LEU A  55           
SHEET    7   A 7 ILE B  33  PRO B  34 -1  O  ILE B  33   N  SER A  41           
SHEET    1   B 7 ILE A  33  PRO A  34  0                                        
SHEET    2   B 7 TYR C  40  VAL C  46 -1  O  SER C  41   N  ILE A  33           
SHEET    3   B 7 LYS C  49  TRP C  56 -1  O  VAL C  51   N  VAL C  44           
SHEET    4   B 7 GLN C   2  GLY C  10  1  N  ILE C   4   O  GLY C  54           
SHEET    5   B 7 VAL C  77  SER C  83  1  O  CYS C  81   N  VAL C   9           
SHEET    6   B 7 ILE C 110  THR C 115  1  O  VAL C 113   N  ILE C  80           
SHEET    7   B 7 LYS C 153  GLU C 156  1  O  LEU C 155   N  GLY C 114           
SHEET    1   C 7 LYS B 153  GLU B 156  0                                        
SHEET    2   C 7 ILE B 110  THR B 115  1  N  GLY B 114   O  LEU B 155           
SHEET    3   C 7 VAL B  77  SER B  83  1  N  ILE B  80   O  VAL B 113           
SHEET    4   C 7 GLN B   2  GLY B  10  1  N  VAL B   9   O  CYS B  81           
SHEET    5   C 7 VAL B  51  TRP B  56  1  O  GLY B  54   N  ILE B   4           
SHEET    6   C 7 TYR B  40  VAL B  44 -1  N  VAL B  44   O  VAL B  51           
SHEET    7   C 7 TYR C  32  PRO C  34 -1  O  ILE C  33   N  SER B  41           
LINK        ZN    ZN A 201                 O   HOH A1114     1555   1555  2.11  
LINK        ZN    ZN A 201                 O   HOH A1148     1555   1555  2.13  
LINK        ZN    ZN A 201                 O3B GDP A 200     1555   1555  2.10  
LINK        ZN    ZN A 201                 O   HOH A 915     1555   1555  2.18  
LINK        ZN    ZN A 201                 OG1 THR A  17     1555   1555  2.15  
LINK        ZN    ZN A 201                 O   THR A  35     1555   1555  2.27  
LINK        ZN    ZN A 202                 OD1 ASP A  63     1555   1555  2.71  
LINK        ZN    ZN A 202                 OD2 ASP A  63     1555   1555  1.98  
LINK        ZN    ZN A 202                 OE2 GLU A 100     1555   1555  2.08  
LINK        ZN    ZN A 202                 NE2 HIS A 104     1555   1555  2.00  
LINK        ZN    ZN A 901                 O   HOH A1125     1555   1555  2.01  
LINK        ZN    ZN A 901                 OD1 ASP A  38     1555   1555  1.97  
LINK        ZN    ZN A 901                 OD2 ASP A  38     1555   1555  2.71  
LINK        ZN    ZN A 901                 OD1 ASP C  38     1555   1555  2.03  
LINK        ZN    ZN A 901                 OD2 ASP C  38     1555   1555  2.75  
LINK        ZN    ZN A 901                 OD1 ASP B  38     1555   1555  2.02  
LINK        ZN    ZN A 902                 OE1 GLU A 127     1555   1555  2.13  
LINK        ZN    ZN A 902                 OE2 GLU A 131     1555   1555  1.99  
LINK        ZN    ZN B 201                 O   HOH B 431     1555   1555  2.12  
LINK        ZN    ZN B 201                 O   HOH B 412     1555   1555  2.18  
LINK        ZN    ZN B 201                 O   HOH B 421     1555   1555  2.13  
LINK        ZN    ZN B 201                 OG1 THR B  17     1555   1555  2.17  
LINK        ZN    ZN B 201                 O3B GDP B 200     1555   1555  2.18  
LINK        ZN    ZN B 201                 O   THR B  35     1555   1555  2.25  
LINK        ZN    ZN B 202                 OD2 ASP B  63     1555   1555  1.98  
LINK        ZN    ZN B 202                 OE2 GLU B 100     1555   1555  2.09  
LINK        ZN    ZN B 202                 NE2 HIS B 104     1555   1555  1.99  
LINK        ZN    ZN C 201                 O   THR C  35     1555   1555  2.24  
LINK        ZN    ZN C 201                 O3B GDP C 200     1555   1555  2.07  
LINK        ZN    ZN C 201                 O   HOH C 443     1555   1555  2.08  
LINK        ZN    ZN C 201                 O   HOH C 424     1555   1555  2.18  
LINK        ZN    ZN C 201                 O   HOH C 434     1555   1555  2.10  
LINK        ZN    ZN C 201                 OG1 THR C  17     1555   1555  2.16  
LINK        ZN    ZN C 202                 OD1 ASP C  63     1555   1555  2.71  
LINK        ZN    ZN C 202                 OD2 ASP C  63     1555   1555  1.96  
LINK        ZN    ZN C 202                 OE2 GLU C 100     1555   1555  2.10  
LINK        ZN    ZN C 202                 NE2 HIS C 104     1555   1555  1.98  
LINK        ZN    ZN A 202                 NE2 HIS A 103     1555   6554  2.07  
LINK        ZN    ZN A 902                 OE2 GLU C 127     1555   4455  2.71  
LINK        ZN    ZN A 902                 OE1 GLU C 127     1555   4455  2.06  
LINK        ZN    ZN A 902                 OE2 GLU C 131     1555   4455  1.89  
LINK        ZN    ZN B 202                 NE2 HIS C 103     1555   6554  2.09  
LINK        ZN    ZN C 202                 NE2 HIS B 103     1555   6554  2.05  
CISPEP   1 TYR A   72    PRO A   73          0       -18.07                     
CISPEP   2 TYR B   72    PRO B   73          0       -18.54                     
CISPEP   3 TYR C   72    PRO C   73          0       -15.65                     
SITE     1 AC1  6 THR A  17  THR A  35  GDP A 200  HOH A 915                    
SITE     2 AC1  6 HOH A1114  HOH A1148                                          
SITE     1 AC2  4 ASP A  63  GLU A 100  HIS A 103  HIS A 104                    
SITE     1 AC3  6 THR B  17  THR B  35  GDP B 200  HOH B 412                    
SITE     2 AC3  6 HOH B 421  HOH B 431                                          
SITE     1 AC4  4 ASP B  63  GLU B 100  HIS B 104  HIS C 103                    
SITE     1 AC5  6 THR C  17  THR C  35  GDP C 200  HOH C 424                    
SITE     2 AC5  6 HOH C 434  HOH C 443                                          
SITE     1 AC6  4 HIS B 103  ASP C  63  GLU C 100  HIS C 104                    
SITE     1 AC7  4 ASP A  38  HOH A1125  ASP B  38  ASP C  38                    
SITE     1 AC8  4 GLU A 127  GLU A 131  GLU C 127  GLU C 131                    
SITE     1 AC9 25 ALA A  13  VAL A  14  GLY A  15  LYS A  16                    
SITE     2 AC9 25 THR A  17  CYS A  18  PHE A  28  ILE A  33                    
SITE     3 AC9 25 LYS A 116  ASP A 118  LEU A 119  SER A 158                    
SITE     4 AC9 25 ALA A 159  LEU A 160   ZN A 201  HOH A 908                    
SITE     5 AC9 25 HOH A 915  HOH A 929  HOH A 965  HOH A 977                    
SITE     6 AC9 25 HOH A1024  HOH A1030  HOH A1073  HOH A1114                    
SITE     7 AC9 25 HOH A1148                                                     
SITE     1 BC1 28 ASN A  43  ASP B  11  ALA B  13  VAL B  14                    
SITE     2 BC1 28 GLY B  15  LYS B  16  THR B  17  CYS B  18                    
SITE     3 BC1 28 PHE B  28  ILE B  33  LYS B 116  ASP B 118                    
SITE     4 BC1 28 LEU B 119  SER B 158  ALA B 159  LEU B 160                    
SITE     5 BC1 28  ZN B 201  HOH B 204  HOH B 207  HOH B 222                    
SITE     6 BC1 28 HOH B 239  HOH B 282  HOH B 333  HOH B 343                    
SITE     7 BC1 28 HOH B 412  HOH B 421  HOH B 431  HOH B 453                    
SITE     1 BC2 27 ASN B  43  ALA C  13  VAL C  14  GLY C  15                    
SITE     2 BC2 27 LYS C  16  THR C  17  CYS C  18  PHE C  28                    
SITE     3 BC2 27 ILE C  33  LYS C 116  ASP C 118  LEU C 119                    
SITE     4 BC2 27 SER C 158  ALA C 159  LEU C 160   ZN C 201                    
SITE     5 BC2 27 HOH C 204  HOH C 209  HOH C 228  HOH C 270                    
SITE     6 BC2 27 HOH C 303  HOH C 330  HOH C 337  HOH C 354                    
SITE     7 BC2 27 HOH C 424  HOH C 434  HOH C 443                               
CRYST1   89.727   89.727  190.618  90.00  90.00 120.00 P 32 2 1     18          
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      0.011145  0.006435  0.000000        0.00000                         
SCALE2      0.000000  0.012869  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005246        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system