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Database: PDB
Entry: 3SU8
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Original site: 3SU8 
HEADER    APOPTOSIS/SIGNALING PROTEIN             11-JUL-11   3SU8              
TITLE     CRYSTAL STRUCTURE OF A TRUNCATED INTRACELLULAR DOMAIN OF PLEXIN-B1 IN 
TITLE    2 COMPLEX WITH RAC1                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 1-177;                                        
COMPND   5 SYNONYM: CELL MIGRATION-INDUCING GENE 5 PROTEIN, RAS-LIKE PROTEIN    
COMPND   6 TC25, P21-RAC1;                                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PLEXIN-B1;                                                 
COMPND  10 CHAIN: X;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 1533-2135;                                    
COMPND  12 SYNONYM: SEMAPHORIN RECEPTOR SEP;                                    
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: RAC1, TC25, MIG5;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: PLXNB1, KIAA0407, PLXN5, SEP;                                  
SOURCE  13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    AXON GUIDANCE, SIGNAL TRANSDUCTION, APOPTOSIS-SIGNALING PROTEIN       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.H.BELL,A.R.ARICESCU,E.Y.JONES,C.SIEBOLD                             
REVDAT   2   05-OCT-11 3SU8    1       JRNL                                     
REVDAT   1   28-SEP-11 3SU8    0                                                
JRNL        AUTH   C.H.BELL,A.R.ARICESCU,E.Y.JONES,C.SIEBOLD                    
JRNL        TITL   A DUAL BINDING MODE FOR RHOGTPASES IN PLEXIN SIGNALLING.     
JRNL        REF    PLOS BIOL.                    V.   9 01134 2011              
JRNL        REFN                   ISSN 1544-9173                               
JRNL        PMID   21912513                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.1001134                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.9.2                                         
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 15648                          
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)  : 0.208                          
REMARK   3   R VALUE            (WORKING SET)  : 0.207                          
REMARK   3   FREE R VALUE                      : 0.238                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.020                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 786                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 8                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.20                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.42                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2807                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2547                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2684                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2528                   
REMARK   3   BIN FREE R VALUE                        : 0.2956                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.38                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 123                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5729                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 72.26                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.70700                                              
REMARK   3    B22 (A**2) : -2.31200                                             
REMARK   3    B33 (A**2) : 1.60500                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 10.63220                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.68                
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.904                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.854                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5885   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 7997   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2069   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 139    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 837    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5885   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 1      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 760    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 6397   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.93                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 1.60                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 18.52                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION:   X 1560    X 1699                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   22.4945  -18.8426   31.6460           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0009 T22:   -0.1207                                    
REMARK   3     T33:   -0.0734 T12:    0.0317                                    
REMARK   3     T13:    0.1005 T23:    0.0395                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6345 L22:    1.6404                                    
REMARK   3     L33:    3.3850 L12:    0.2950                                    
REMARK   3     L13:   -0.1104 L23:    0.5144                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1753 S12:    0.0027 S13:   -0.2015                     
REMARK   3     S21:    0.3594 S22:   -0.0168 S23:    0.2888                     
REMARK   3     S31:   -0.0877 S32:   -0.4187 S33:   -0.1585                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION:   X 1700    X 1890                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   18.1161  -35.0871   -6.5955           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1318 T22:    0.0638                                    
REMARK   3     T33:   -0.1140 T12:   -0.0680                                    
REMARK   3     T13:   -0.0787 T23:    0.0620                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.9918 L22:    2.5340                                    
REMARK   3     L33:    2.5095 L12:    1.3267                                    
REMARK   3     L13:    0.9047 L23:    1.0358                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0474 S12:   -0.0902 S13:   -0.3226                     
REMARK   3     S21:   -0.3124 S22:    0.0092 S23:    0.3209                     
REMARK   3     S31:    0.0419 S32:   -0.4128 S33:   -0.0566                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION:   X 1891    X 1908                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   42.9258  -54.8410   15.6567           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1704 T22:   -0.0149                                    
REMARK   3     T33:    0.1142 T12:    0.0882                                    
REMARK   3     T13:    0.0811 T23:    0.1255                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3308 L22:    4.2102                                    
REMARK   3     L33:    3.6457 L12:   -2.3222                                    
REMARK   3     L13:   -4.2652 L23:   -3.5144                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0065 S12:    0.2761 S13:    0.1682                     
REMARK   3     S21:   -0.1570 S22:    0.0799 S23:    0.0653                     
REMARK   3     S31:   -0.1530 S32:   -0.0743 S33:   -0.0864                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION:   X 1909    X 1999                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   38.7754  -19.8821   14.5173           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0163 T22:   -0.1167                                    
REMARK   3     T33:   -0.1362 T12:    0.0175                                    
REMARK   3     T13:    0.0908 T23:   -0.0084                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.7625 L22:    2.6173                                    
REMARK   3     L33:    3.5366 L12:   -0.1447                                    
REMARK   3     L13:   -0.5699 L23:    1.3133                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0983 S12:   -0.0707 S13:    0.0874                     
REMARK   3     S21:    0.0833 S22:    0.0985 S23:   -0.3179                     
REMARK   3     S31:   -0.3215 S32:    0.0580 S33:   -0.1968                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION:   X 2000    X 2129                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   30.0475  -18.8971   26.5785           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1529 T22:   -0.2654                                    
REMARK   3     T33:   -0.1894 T12:    0.0962                                    
REMARK   3     T13:   -0.0279 T23:    0.0791                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.3926 L22:    2.5630                                    
REMARK   3     L33:    4.2521 L12:    0.6145                                    
REMARK   3     L13:   -1.0554 L23:    0.6881                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2215 S12:   -0.1683 S13:   -0.0124                     
REMARK   3     S21:    0.2966 S22:    0.0559 S23:   -0.0036                     
REMARK   3     S31:   -0.0865 S32:    0.0262 S33:   -0.2774                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION:   A    1    A  178                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -4.6276  -50.4964  -29.8580           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3039 T22:   -0.1810                                    
REMARK   3     T33:   -0.0549 T12:   -0.1633                                    
REMARK   3     T13:   -0.1876 T23:   -0.0360                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.6866 L22:    6.7327                                    
REMARK   3     L33:    4.0910 L12:    3.6070                                    
REMARK   3     L13:    1.3450 L23:    0.8928                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1325 S12:   -0.1743 S13:   -0.0456                     
REMARK   3     S21:   -0.3893 S22:   -0.1196 S23:    0.1370                     
REMARK   3     S31:   -0.0839 S32:    0.0668 S33:    0.2521                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3SU8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066657.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL; NULL                         
REMARK 200  TEMPERATURE           (KELVIN) : NULL; NULL                         
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL; Y                            
REMARK 200  RADIATION SOURCE               : NULL; ESRF                         
REMARK 200  BEAMLINE                       : NULL; ID23-2                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL; 0.8726                       
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL; NULL                         
REMARK 200  DETECTOR MANUFACTURER          : NULL; NULL                         
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       91.72500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.90500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       91.72500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.90500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 36310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, X                                  
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     HIS A   179                                                      
REMARK 465     HIS A   180                                                      
REMARK 465     HIS A   181                                                      
REMARK 465     HIS A   182                                                      
REMARK 465     HIS A   183                                                      
REMARK 465     HIS A   184                                                      
REMARK 465     MET X  1525                                                      
REMARK 465     GLY X  1526                                                      
REMARK 465     HIS X  1527                                                      
REMARK 465     HIS X  1528                                                      
REMARK 465     HIS X  1529                                                      
REMARK 465     HIS X  1530                                                      
REMARK 465     HIS X  1531                                                      
REMARK 465     HIS X  1532                                                      
REMARK 465     GLU X  1533                                                      
REMARK 465     SER X  1534                                                      
REMARK 465     SER X  1535                                                      
REMARK 465     VAL X  1536                                                      
REMARK 465     ARG X  1537                                                      
REMARK 465     ASP X  1538                                                      
REMARK 465     ARG X  1539                                                      
REMARK 465     CYS X  1540                                                      
REMARK 465     LYS X  1541                                                      
REMARK 465     LYS X  1542                                                      
REMARK 465     GLU X  1543                                                      
REMARK 465     PHE X  1544                                                      
REMARK 465     THR X  1545                                                      
REMARK 465     ASP X  1546                                                      
REMARK 465     LEU X  1547                                                      
REMARK 465     MET X  1548                                                      
REMARK 465     THR X  1549                                                      
REMARK 465     GLU X  1550                                                      
REMARK 465     MET X  1551                                                      
REMARK 465     THR X  1552                                                      
REMARK 465     ASP X  1553                                                      
REMARK 465     LEU X  1554                                                      
REMARK 465     THR X  1555                                                      
REMARK 465     SER X  1556                                                      
REMARK 465     ASP X  1557                                                      
REMARK 465     LEU X  1558                                                      
REMARK 465     LEU X  1559                                                      
REMARK 465     GLY X  1758                                                      
REMARK 465     PRO X  1759                                                      
REMARK 465     GLY X  1760                                                      
REMARK 465     ALA X  1761                                                      
REMARK 465     GLY X  1762                                                      
REMARK 465     GLU X  1763                                                      
REMARK 465     LYS X  1855                                                      
REMARK 465     HIS X  1856                                                      
REMARK 465     VAL X  1857                                                      
REMARK 465     LEU X  1858                                                      
REMARK 465     ARG X  1859                                                      
REMARK 465     GLU X  1860                                                      
REMARK 465     ASN X  1861                                                      
REMARK 465     GLN X  1862                                                      
REMARK 465     ASP X  1863                                                      
REMARK 465     TYR X  1864                                                      
REMARK 465     VAL X  1865                                                      
REMARK 465     PRO X  1866                                                      
REMARK 465     GLY X  1867                                                      
REMARK 465     GLU X  1868                                                      
REMARK 465     ARG X  1869                                                      
REMARK 465     THR X  1870                                                      
REMARK 465     PRO X  1871                                                      
REMARK 465     MET X  1872                                                      
REMARK 465     LEU X  1873                                                      
REMARK 465     GLU X  1874                                                      
REMARK 465     ASP X  1875                                                      
REMARK 465     VAL X  1876                                                      
REMARK 465     ASP X  1877                                                      
REMARK 465     GLU X  1878                                                      
REMARK 465     GLY X  1879                                                      
REMARK 465     ASN X  2130                                                      
REMARK 465     LYS X  2131                                                      
REMARK 465     VAL X  2132                                                      
REMARK 465     THR X  2133                                                      
REMARK 465     ASP X  2134                                                      
REMARK 465     LEU X  2135                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU X2108    CG   CD   OE1  OE2                                  
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    SER X  1980     CB   ARG X  1984              2.14            
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    ALA X1669   CB  -  CA  -  C   ANGL. DEV. = -10.0 DEGREES          
REMARK 500    SER X1980   CB  -  CA  -  C   ANGL. DEV. =  24.0 DEGREES          
REMARK 500    SER X1980   N   -  CA  -  C   ANGL. DEV. = -22.4 DEGREES          
REMARK 500    LEU X2027   CB  -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  37       53.22   -158.27                                   
REMARK 500    LYS A  96      -55.92   -124.01                                   
REMARK 500    LYS A 116       69.79     62.72                                   
REMARK 500    ARG X1581      -45.91     74.08                                   
REMARK 500    HIS X1586       74.77   -100.73                                   
REMARK 500    LYS X1670     -130.16   -106.24                                   
REMARK 500    ARG X1678     -167.64   -127.51                                   
REMARK 500    VAL X1726      -71.20    -82.99                                   
REMARK 500    HIS X1885      -74.18   -122.53                                   
REMARK 500    PRO X1893       38.43    -84.07                                   
REMARK 500    ARG X1904      -66.51     61.65                                   
REMARK 500    ARG X1908      -58.08     66.28                                   
REMARK 500    ASP X1969      108.02    -56.35                                   
REMARK 500    SER X1980      -92.26    -92.52                                   
REMARK 500    PHE X1985      -72.75   -106.74                                   
REMARK 500    LEU X2027      155.04     82.77                                   
REMARK 500    ARG X2029     -111.21     45.41                                   
REMARK 500    ASP X2030       -1.21    -57.76                                   
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 SER X 1980     LEU X 1981                 -149.12                    
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    TRP A  97        24.4      L          L   OUTSIDE RANGE           
REMARK 500    SER X1980        46.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU X1981        24.9      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  17   OG1                                                    
REMARK 620 2 THR A  35   OG1  95.5                                              
REMARK 620 3 GNP A 200   O2G 141.7  92.3                                        
REMARK 620 4 GNP A 200   O2B  77.6 151.8  78.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP A 200                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3SUA   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 S1625T CONFLICT IN UNP ENTRY O43157                                  
DBREF  3SU8 A    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  3SU8 X 1533  2135  UNP    O43157   PLXB1_HUMAN   1533   2135             
SEQADV 3SU8 LYS A  178  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SU8 HIS A  179  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SU8 HIS A  180  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SU8 HIS A  181  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SU8 HIS A  182  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SU8 HIS A  183  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SU8 HIS A  184  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SU8 MET X 1525  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SU8 GLY X 1526  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SU8 HIS X 1527  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SU8 HIS X 1528  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SU8 HIS X 1529  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SU8 HIS X 1530  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SU8 HIS X 1531  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SU8 HIS X 1532  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SU8 THR X 1625  UNP  O43157    SER  1625 SEE REMARK 999                 
SEQRES   1 A  184  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 A  184  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 A  184  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 A  184  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 A  184  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 A  184  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 A  184  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 A  184  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 A  184  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 A  184  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 A  184  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 A  184  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 A  184  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 A  184  ASP GLU ALA ILE ARG ALA VAL LEU LYS HIS HIS HIS HIS          
SEQRES  15 A  184  HIS HIS                                                      
SEQRES   1 X  611  MET GLY HIS HIS HIS HIS HIS HIS GLU SER SER VAL ARG          
SEQRES   2 X  611  ASP ARG CYS LYS LYS GLU PHE THR ASP LEU MET THR GLU          
SEQRES   3 X  611  MET THR ASP LEU THR SER ASP LEU LEU GLY SER GLY ILE          
SEQRES   4 X  611  PRO PHE LEU ASP TYR LYS VAL TYR ALA GLU ARG ILE PHE          
SEQRES   5 X  611  PHE PRO GLY HIS ARG GLU SER PRO LEU HIS ARG ASP LEU          
SEQRES   6 X  611  GLY VAL PRO GLU SER ARG ARG PRO THR VAL GLU GLN GLY          
SEQRES   7 X  611  LEU GLY GLN LEU SER ASN LEU LEU ASN SER LYS LEU PHE          
SEQRES   8 X  611  LEU THR LYS PHE ILE HIS THR LEU GLU THR GLN ARG THR          
SEQRES   9 X  611  PHE SER ALA ARG ASP ARG ALA TYR VAL ALA SER LEU LEU          
SEQRES  10 X  611  THR VAL ALA LEU HIS GLY LYS LEU GLU TYR PHE THR ASP          
SEQRES  11 X  611  ILE LEU ARG THR LEU LEU SER ASP LEU VAL ALA GLN TYR          
SEQRES  12 X  611  VAL ALA LYS ASN PRO LYS LEU MET LEU ARG ARG THR GLU          
SEQRES  13 X  611  THR VAL VAL GLU LYS LEU LEU THR ASN TRP MET SER ILE          
SEQRES  14 X  611  CYS LEU TYR THR PHE VAL ARG ASP SER VAL GLY GLU PRO          
SEQRES  15 X  611  LEU TYR MET LEU PHE ARG GLY ILE LYS HIS GLN VAL ASP          
SEQRES  16 X  611  LYS GLY PRO VAL ASP SER VAL THR GLY LYS ALA LYS TYR          
SEQRES  17 X  611  THR LEU ASN ASP ASN ARG LEU LEU ARG GLU ASP VAL GLU          
SEQRES  18 X  611  TYR ARG PRO LEU THR LEU ASN ALA LEU LEU ALA VAL GLY          
SEQRES  19 X  611  PRO GLY ALA GLY GLU ALA GLN GLY VAL PRO VAL LYS VAL          
SEQRES  20 X  611  LEU ASP CYS ASP THR ILE SER GLN ALA LYS GLU LYS MET          
SEQRES  21 X  611  LEU ASP GLN LEU TYR LYS GLY VAL PRO LEU THR GLN ARG          
SEQRES  22 X  611  PRO ASP PRO ARG THR LEU ASP VAL GLU TRP ARG SER GLY          
SEQRES  23 X  611  VAL ALA GLY HIS LEU ILE LEU SER ASP GLU ASP VAL THR          
SEQRES  24 X  611  SER GLU VAL GLN GLY LEU TRP ARG ARG LEU ASN THR LEU          
SEQRES  25 X  611  GLN HIS TYR LYS VAL PRO ASP GLY ALA THR VAL ALA LEU          
SEQRES  26 X  611  VAL PRO CYS LEU THR LYS HIS VAL LEU ARG GLU ASN GLN          
SEQRES  27 X  611  ASP TYR VAL PRO GLY GLU ARG THR PRO MET LEU GLU ASP          
SEQRES  28 X  611  VAL ASP GLU GLY GLY ILE ARG PRO TRP HIS LEU VAL LYS          
SEQRES  29 X  611  PRO SER ASP GLU PRO GLU PRO PRO ARG PRO ARG ARG GLY          
SEQRES  30 X  611  SER LEU ARG GLY GLY GLU ARG GLU ARG ALA LYS ALA ILE          
SEQRES  31 X  611  PRO GLU ILE TYR LEU THR ARG LEU LEU SER MET LYS GLY          
SEQRES  32 X  611  THR LEU GLN LYS PHE VAL ASP ASP LEU PHE GLN VAL ILE          
SEQRES  33 X  611  LEU SER THR SER ARG PRO VAL PRO LEU ALA VAL LYS TYR          
SEQRES  34 X  611  PHE PHE ASP LEU LEU ASP GLU GLN ALA GLN GLN HIS GLY          
SEQRES  35 X  611  ILE SER ASP GLN ASP THR ILE HIS ILE TRP LYS THR ASN          
SEQRES  36 X  611  SER LEU PRO LEU ARG PHE TRP ILE ASN ILE ILE LYS ASN          
SEQRES  37 X  611  PRO GLN PHE VAL PHE ASP VAL GLN THR SER ASP ASN MET          
SEQRES  38 X  611  ASP ALA VAL LEU LEU VAL ILE ALA GLN THR PHE MET ASP          
SEQRES  39 X  611  ALA CYS THR LEU ALA ASP HIS LYS LEU GLY ARG ASP SER          
SEQRES  40 X  611  PRO ILE ASN LYS LEU LEU TYR ALA ARG ASP ILE PRO ARG          
SEQRES  41 X  611  TYR LYS ARG MET VAL GLU ARG TYR TYR ALA ASP ILE ARG          
SEQRES  42 X  611  GLN THR VAL PRO ALA SER ASP GLN GLU MET ASN SER VAL          
SEQRES  43 X  611  LEU ALA GLU LEU SER TRP ASN TYR SER GLY ASP LEU GLY          
SEQRES  44 X  611  ALA ARG VAL ALA LEU HIS GLU LEU TYR LYS TYR ILE ASN          
SEQRES  45 X  611  LYS TYR TYR ASP GLN ILE ILE THR ALA LEU GLU GLU ASP          
SEQRES  46 X  611  GLY THR ALA GLN LYS MET GLN LEU GLY TYR ARG LEU GLN          
SEQRES  47 X  611  GLN ILE ALA ALA ALA VAL GLU ASN LYS VAL THR ASP LEU          
HET     MG  A 201       1                                                       
HET    GNP  A 200      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  GNP    C10 H17 N6 O13 P3                                            
HELIX    1   1 GLY A   15  THR A   25  1                                  11    
HELIX    2   2 GLN A   61  ASP A   65  5                                   5    
HELIX    3   3 LEU A   67  SER A   71  5                                   5    
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 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  LYS A  178  1                                  15    
HELIX    9   9 ASP X 1567  PHE X 1577  1                                  11    
HELIX   10  10 ARG X 1595  ASN X 1611  1                                  17    
HELIX   11  11 SER X 1612  THR X 1625  1                                  14    
HELIX   12  12 SER X 1630  LEU X 1645  1                                  16    
HELIX   13  13 LYS X 1648  LYS X 1670  1                                  23    
HELIX   14  14 ASN X 1671  MET X 1675  5                                   5    
HELIX   15  15 THR X 1681  SER X 1702  1                                  22    
HELIX   16  16 VAL X 1703  ASP X 1719  1                                  17    
HELIX   17  17 ASN X 1735  LEU X 1739  5                                   5    
HELIX   18  18 THR X 1776  TYR X 1789  1                                  14    
HELIX   19  19 ASP X 1799  ARG X 1801  5                                   3    
HELIX   20  20 THR X 1835  LYS X 1840  1                                   6    
HELIX   21  21 PRO X 1915  LEU X 1929  1                                  15    
HELIX   22  22 LEU X 1929  LEU X 1941  1                                  13    
HELIX   23  23 PRO X 1948  HIS X 1965  1                                  18    
HELIX   24  24 ASP X 1969  ASN X 1979  1                                  11    
HELIX   25  25 PHE X 1985  ASN X 1992  1                                   8    
HELIX   26  26 PRO X 1993  VAL X 1996  5                                   4    
HELIX   27  27 SER X 2002  THR X 2021  1                                  20    
HELIX   28  28 PRO X 2032  TYR X 2038  1                                   7    
HELIX   29  29 ASP X 2041  THR X 2059  1                                  19    
HELIX   30  30 SER X 2063  TYR X 2078  1                                  16    
HELIX   31  31 GLY X 2083  TYR X 2098  1                                  16    
HELIX   32  32 TYR X 2098  ASP X 2109  1                                  12    
HELIX   33  33 ASP X 2109  GLN X 2116  1                                   8    
HELIX   34  34 GLN X 2116  GLU X 2129  1                                  14    
SHEET    1   A 6 ASN A  39  VAL A  46  0                                        
SHEET    2   A 6 LYS A  49  ASP A  57 -1  O  LEU A  55   N  TYR A  40           
SHEET    3   A 6 GLN A   2  GLY A  10  1  N  ILE A   4   O  GLY A  54           
SHEET    4   A 6 VAL A  77  SER A  83  1  O  CYS A  81   N  VAL A   9           
SHEET    5   A 6 ILE A 110  THR A 115  1  O  VAL A 113   N  ILE A  80           
SHEET    6   A 6 LYS A 153  GLU A 156  1  O  LEU A 155   N  GLY A 114           
SHEET    1   B 5 VAL X1767  LEU X1772  0                                        
SHEET    2   B 5 PRO X1748  LEU X1755 -1  N  LEU X1749   O  VAL X1771           
SHEET    3   B 5 THR X1846  PRO X1851  1  O  VAL X1847   N  ASN X1752           
SHEET    4   B 5 LEU X1803  ARG X1808 -1  N  ASP X1804   O  VAL X1850           
SHEET    5   B 5 LEU X1815  LEU X1817 -1  O  LEU X1817   N  VAL X1805           
SHEET    1   C 3 GLU X1825  GLN X1827  0                                        
SHEET    2   C 3 TRP X1830  ARG X1832 -1  O  ARG X1832   N  GLU X1825           
SHEET    3   C 3 ARG X1882  TRP X1884  1  O  TRP X1884   N  ARG X1831           
LINK         OG1 THR A  17                MG    MG A 201     1555   1555  1.95  
LINK         OG1 THR A  35                MG    MG A 201     1555   1555  2.00  
LINK        MG    MG A 201                 O2G GNP A 200     1555   1555  2.17  
LINK        MG    MG A 201                 O2B GNP A 200     1555   1555  2.35  
SITE     1 AC1  4 THR A  17  THR A  35  ASP A  57  GNP A 200                    
SITE     1 AC2 23 ASP A  11  GLY A  12  ALA A  13  VAL A  14                    
SITE     2 AC2 23 GLY A  15  LYS A  16  THR A  17  CYS A  18                    
SITE     3 AC2 23 PHE A  28  GLY A  30  TYR A  32  PRO A  34                    
SITE     4 AC2 23 THR A  35  THR A  58  GLY A  60  GLN A  61                    
SITE     5 AC2 23 LYS A 116  ASP A 118  LEU A 119  SER A 158                    
SITE     6 AC2 23 ALA A 159  LEU A 160   MG A 201                               
CRYST1  183.450   63.810   84.550  90.00 107.53  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005451  0.000000  0.001722        0.00000                         
SCALE2      0.000000  0.015672  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012403        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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