GenomeNet

Database: PDB
Entry: 3SUA
LinkDB: 3SUA
Original site: 3SUA 
HEADER    APOPTOSIS/SIGNALING PROTEIN             11-JUL-11   3SUA              
TITLE     CRYSTAL STRUCTURE OF THE INTRACELLULAR DOMAIN OF PLEXIN-B1 IN COMPLEX 
TITLE    2 WITH RAC1                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1;                
COMPND   3 CHAIN: A, B, C;                                                      
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: D, E, F;                                                      
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 3SUA    1       JRNL                                     
REVDAT   1   07-SEP-11 3SUA    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.    4.39 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) : 4.39                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.81                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 25522                          
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)  : 0.235                          
REMARK   3   R VALUE            (WORKING SET)  : 0.234                          
REMARK   3   FREE R VALUE                      : 0.264                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.160                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1318                           
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               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 4.39                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 4.57                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : NULL                     
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2799                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2521                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2662                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2513                   
REMARK   3   BIN FREE R VALUE                        : 0.2673                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.89                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 137                      
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            : 16394                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 99                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 171.72                         
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 124.57                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 37.52890                                             
REMARK   3    B22 (A**2) : 16.07630                                             
REMARK   3    B33 (A**2) : -53.60520                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 1.11                
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      : 0.781                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.748                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 16840  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 22892  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 5886   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 396    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 2378   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 16840  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 3      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 2194   ; 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   : 19665  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.16                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.25                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 22.76                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION:   D 2033    D 2129                                     
REMARK   3    ORIGIN FOR THE GROUP (A):   -2.1442   33.8480  -17.7339           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0341 T22:   -0.0655                                    
REMARK   3     T33:    0.0478 T12:   -0.1484                                    
REMARK   3     T13:   -0.2226 T23:    0.1926                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6590 L22:    0.3229                                    
REMARK   3     L33:    0.0000 L12:   -0.0047                                    
REMARK   3     L13:    1.1653 L23:    1.1281                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0955 S12:    0.1820 S13:   -0.1218                     
REMARK   3     S21:    0.2568 S22:   -0.0483 S23:    0.0148                     
REMARK   3     S31:    0.0246 S32:   -0.0151 S33:   -0.0473                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION:   E 2033    E 2129                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -20.5936   86.0822  -60.6926           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4470 T22:   -0.1550                                    
REMARK   3     T33:    0.6079 T12:    0.1154                                    
REMARK   3     T13:    0.3040 T23:    0.0431                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1266 L22:    1.0941                                    
REMARK   3     L33:    0.3920 L12:    0.7293                                    
REMARK   3     L13:   -1.5880 L23:   -0.2285                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.6041 S12:    0.1732 S13:    0.7204                     
REMARK   3     S21:   -0.2524 S22:   -0.1196 S23:   -0.3213                     
REMARK   3     S31:    0.0926 S32:   -0.3406 S33:   -0.4844                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION:   F 2033    F 2129                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -20.0874   17.6546  -84.8482           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2611 T22:   -0.1786                                    
REMARK   3     T33:    0.4569 T12:    0.1397                                    
REMARK   3     T13:    0.0796 T23:   -0.0841                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    1.4115                                    
REMARK   3     L33:    0.0678 L12:   -1.6995                                    
REMARK   3     L13:   -0.8035 L23:    0.6095                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2434 S12:   -0.2716 S13:   -0.0255                     
REMARK   3     S21:   -0.3332 S22:   -0.2413 S23:   -0.1988                     
REMARK   3     S31:   -0.1028 S32:   -0.2214 S33:   -0.0021                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION:   D 1880    D 1890                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -32.2663   56.9827  -24.6399           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0986 T22:    0.1801                                    
REMARK   3     T33:   -0.1480 T12:    0.1831                                    
REMARK   3     T13:   -0.0771 T23:   -0.2077                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    1.7865                                    
REMARK   3     L33:    0.0000 L12:    1.4701                                    
REMARK   3     L13:   -2.2768 L23:   -2.8798                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2178 S12:    0.2359 S13:   -0.0031                     
REMARK   3     S21:    0.5554 S22:   -0.1496 S23:    0.2615                     
REMARK   3     S31:   -0.3032 S32:    0.1834 S33:   -0.0682                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION:   E 1880    E 1890                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -44.4482   57.2610  -71.6564           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4189 T22:   -0.1121                                    
REMARK   3     T33:    0.5297 T12:    0.0756                                    
REMARK   3     T13:    0.0042 T23:   -0.1246                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    3.0035                                    
REMARK   3     L33:    0.0000 L12:   -0.5380                                    
REMARK   3     L13:    0.7555 L23:    0.6763                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2237 S12:    0.1605 S13:    0.1557                     
REMARK   3     S21:    0.3721 S22:    0.1939 S23:   -0.0466                     
REMARK   3     S31:    0.2044 S32:    0.1632 S33:   -0.4176                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION:   F 1880    F 1890                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -33.9139   14.9102  -48.8671           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2654 T22:   -0.2076                                    
REMARK   3     T33:    0.3462 T12:   -0.1101                                    
REMARK   3     T13:   -0.0295 T23:   -0.0162                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.8168 L22:    0.0832                                    
REMARK   3     L33:    2.1162 L12:    0.0609                                    
REMARK   3     L13:    0.5910 L23:    0.3537                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3592 S12:    0.1367 S13:    0.1346                     
REMARK   3     S21:    0.2041 S22:   -0.4665 S23:   -0.2256                     
REMARK   3     S31:    0.1330 S32:   -0.1944 S33:    0.1073                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION:   A  200    A  201                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -52.9946   80.2740  -26.5700           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3151 T22:    0.4337                                    
REMARK   3     T33:   -0.0493 T12:    0.3040                                    
REMARK   3     T13:    0.2809 T23:   -0.1413                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    1.4689 L12:   -0.3191                                    
REMARK   3     L13:   -0.2217 L23:   -0.1373                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1595 S12:    0.0668 S13:    0.0473                     
REMARK   3     S21:    0.3819 S22:    0.3409 S23:   -0.4355                     
REMARK   3     S31:    0.2273 S32:   -0.5275 S33:   -0.1813                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION:   B  200    B  201                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -62.9444   36.3024  -85.4289           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.5269 T22:    0.0546                                    
REMARK   3     T33:    0.2142 T12:    0.1616                                    
REMARK   3     T13:   -0.0507 T23:   -0.1289                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4443 L22:    2.9567                                    
REMARK   3     L33:    0.5632 L12:    0.0421                                    
REMARK   3     L13:   -1.5196 L23:    0.5593                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2353 S12:    0.5564 S13:   -0.1115                     
REMARK   3     S21:    0.5526 S22:    0.1655 S23:    0.0406                     
REMARK   3     S31:   -0.2129 S32:   -0.0358 S33:   -0.4008                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION:   C  200    C  201                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  -43.5672    7.6169  -20.1306           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1479 T22:    0.2050                                    
REMARK   3     T33:    0.0901 T12:   -0.3040                                    
REMARK   3     T13:    0.3040 T23:    0.2126                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0000 L22:    0.0000                                    
REMARK   3     L33:    0.0688 L12:    0.6148                                    
REMARK   3     L13:   -1.4755 L23:   -0.2915                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1973 S12:    0.3674 S13:   -0.1408                     
REMARK   3     S21:    0.2879 S22:    0.3539 S23:   -0.0762                     
REMARK   3     S31:    0.1071 S32:   -0.2288 S33:   -0.1566                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3SUA 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 RCSB066659.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9763                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25525                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.390                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
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                              
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   (%): 66.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
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       71.17000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      129.08000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      112.12500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      129.08000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       71.17000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      112.12500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       71.17000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      112.12500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      129.08000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      112.12500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       71.17000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      129.08000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: 2410 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
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: 3                                                       
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: 2400 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12360 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 91780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
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     HIS B   179                                                      
REMARK 465     HIS B   180                                                      
REMARK 465     HIS B   181                                                      
REMARK 465     HIS B   182                                                      
REMARK 465     HIS B   183                                                      
REMARK 465     HIS B   184                                                      
REMARK 465     HIS C   179                                                      
REMARK 465     HIS C   180                                                      
REMARK 465     HIS C   181                                                      
REMARK 465     HIS C   182                                                      
REMARK 465     HIS C   183                                                      
REMARK 465     HIS C   184                                                      
REMARK 465     MET D  1503                                                      
REMARK 465     GLY D  1504                                                      
REMARK 465     HIS D  1505                                                      
REMARK 465     HIS D  1506                                                      
REMARK 465     HIS D  1507                                                      
REMARK 465     HIS D  1508                                                      
REMARK 465     HIS D  1509                                                      
REMARK 465     HIS D  1510                                                      
REMARK 465     TYR D  1511                                                      
REMARK 465     ARG D  1512                                                      
REMARK 465     ARG D  1513                                                      
REMARK 465     LYS D  1514                                                      
REMARK 465     SER D  1515                                                      
REMARK 465     LYS D  1516                                                      
REMARK 465     GLN D  1517                                                      
REMARK 465     ALA D  1518                                                      
REMARK 465     LEU D  1519                                                      
REMARK 465     ARG D  1520                                                      
REMARK 465     ASP D  1521                                                      
REMARK 465     TYR D  1522                                                      
REMARK 465     LYS D  1523                                                      
REMARK 465     LYS D  1524                                                      
REMARK 465     VAL D  1525                                                      
REMARK 465     GLN D  1526                                                      
REMARK 465     ILE D  1527                                                      
REMARK 465     GLN D  1528                                                      
REMARK 465     LEU D  1529                                                      
REMARK 465     GLU D  1530                                                      
REMARK 465     ASN D  1531                                                      
REMARK 465     LEU D  1532                                                      
REMARK 465     GLU D  1533                                                      
REMARK 465     SER D  1534                                                      
REMARK 465     SER D  1535                                                      
REMARK 465     VAL D  1536                                                      
REMARK 465     ARG D  1537                                                      
REMARK 465     ASP D  1538                                                      
REMARK 465     ARG D  1539                                                      
REMARK 465     CYS D  1540                                                      
REMARK 465     LYS D  1541                                                      
REMARK 465     LYS D  1542                                                      
REMARK 465     GLU D  1543                                                      
REMARK 465     PHE D  1544                                                      
REMARK 465     THR D  1545                                                      
REMARK 465     ASP D  1546                                                      
REMARK 465     LEU D  1547                                                      
REMARK 465     MET D  1548                                                      
REMARK 465     THR D  1549                                                      
REMARK 465     GLU D  1550                                                      
REMARK 465     MET D  1551                                                      
REMARK 465     THR D  1552                                                      
REMARK 465     ASP D  1553                                                      
REMARK 465     LEU D  1554                                                      
REMARK 465     THR D  1555                                                      
REMARK 465     SER D  1556                                                      
REMARK 465     ASP D  1557                                                      
REMARK 465     LEU D  1558                                                      
REMARK 465     LEU D  1559                                                      
REMARK 465     GLY D  1560                                                      
REMARK 465     SER D  1561                                                      
REMARK 465     GLY D  1562                                                      
REMARK 465     GLY D  1758                                                      
REMARK 465     PRO D  1759                                                      
REMARK 465     GLY D  1760                                                      
REMARK 465     ALA D  1761                                                      
REMARK 465     GLY D  1762                                                      
REMARK 465     GLU D  1763                                                      
REMARK 465     LYS D  1855                                                      
REMARK 465     HIS D  1856                                                      
REMARK 465     VAL D  1857                                                      
REMARK 465     LEU D  1858                                                      
REMARK 465     ARG D  1859                                                      
REMARK 465     GLU D  1860                                                      
REMARK 465     ASN D  1861                                                      
REMARK 465     GLN D  1862                                                      
REMARK 465     ASP D  1863                                                      
REMARK 465     TYR D  1864                                                      
REMARK 465     VAL D  1865                                                      
REMARK 465     PRO D  1866                                                      
REMARK 465     GLY D  1867                                                      
REMARK 465     GLU D  1868                                                      
REMARK 465     ARG D  1869                                                      
REMARK 465     THR D  1870                                                      
REMARK 465     PRO D  1871                                                      
REMARK 465     MET D  1872                                                      
REMARK 465     LEU D  1873                                                      
REMARK 465     GLU D  1874                                                      
REMARK 465     ASP D  1875                                                      
REMARK 465     VAL D  1876                                                      
REMARK 465     ASP D  1877                                                      
REMARK 465     GLU D  1878                                                      
REMARK 465     GLY D  1879                                                      
REMARK 465     ASP D  1891                                                      
REMARK 465     GLU D  1892                                                      
REMARK 465     PRO D  1893                                                      
REMARK 465     GLU D  1894                                                      
REMARK 465     PRO D  1895                                                      
REMARK 465     PRO D  1896                                                      
REMARK 465     ARG D  1897                                                      
REMARK 465     PRO D  1898                                                      
REMARK 465     ARG D  1899                                                      
REMARK 465     ARG D  1900                                                      
REMARK 465     GLY D  1901                                                      
REMARK 465     SER D  1902                                                      
REMARK 465     LEU D  1903                                                      
REMARK 465     ARG D  1904                                                      
REMARK 465     GLY D  1905                                                      
REMARK 465     GLY D  1906                                                      
REMARK 465     GLU D  1907                                                      
REMARK 465     ARG D  1908                                                      
REMARK 465     GLU D  1909                                                      
REMARK 465     ARG D  1910                                                      
REMARK 465     ALA D  1911                                                      
REMARK 465     LYS D  1912                                                      
REMARK 465     ALA D  1913                                                      
REMARK 465     ILE D  1914                                                      
REMARK 465     PRO D  1915                                                      
REMARK 465     ASP D  2024                                                      
REMARK 465     HIS D  2025                                                      
REMARK 465     LYS D  2026                                                      
REMARK 465     LEU D  2027                                                      
REMARK 465     GLY D  2028                                                      
REMARK 465     ARG D  2029                                                      
REMARK 465     ASP D  2030                                                      
REMARK 465     SER D  2031                                                      
REMARK 465     ASN D  2130                                                      
REMARK 465     LYS D  2131                                                      
REMARK 465     VAL D  2132                                                      
REMARK 465     THR D  2133                                                      
REMARK 465     ASP D  2134                                                      
REMARK 465     LEU D  2135                                                      
REMARK 465     MET E  1503                                                      
REMARK 465     GLY E  1504                                                      
REMARK 465     HIS E  1505                                                      
REMARK 465     HIS E  1506                                                      
REMARK 465     HIS E  1507                                                      
REMARK 465     HIS E  1508                                                      
REMARK 465     HIS E  1509                                                      
REMARK 465     HIS E  1510                                                      
REMARK 465     TYR E  1511                                                      
REMARK 465     ARG E  1512                                                      
REMARK 465     ARG E  1513                                                      
REMARK 465     LYS E  1514                                                      
REMARK 465     SER E  1515                                                      
REMARK 465     LYS E  1516                                                      
REMARK 465     GLN E  1517                                                      
REMARK 465     ALA E  1518                                                      
REMARK 465     LEU E  1519                                                      
REMARK 465     ARG E  1520                                                      
REMARK 465     ASP E  1521                                                      
REMARK 465     TYR E  1522                                                      
REMARK 465     LYS E  1523                                                      
REMARK 465     LYS E  1524                                                      
REMARK 465     VAL E  1525                                                      
REMARK 465     GLN E  1526                                                      
REMARK 465     ILE E  1527                                                      
REMARK 465     GLN E  1528                                                      
REMARK 465     LEU E  1529                                                      
REMARK 465     GLU E  1530                                                      
REMARK 465     ASN E  1531                                                      
REMARK 465     LEU E  1532                                                      
REMARK 465     GLU E  1533                                                      
REMARK 465     SER E  1534                                                      
REMARK 465     SER E  1535                                                      
REMARK 465     VAL E  1536                                                      
REMARK 465     ARG E  1537                                                      
REMARK 465     ASP E  1538                                                      
REMARK 465     ARG E  1539                                                      
REMARK 465     CYS E  1540                                                      
REMARK 465     LYS E  1541                                                      
REMARK 465     LYS E  1542                                                      
REMARK 465     GLU E  1543                                                      
REMARK 465     PHE E  1544                                                      
REMARK 465     THR E  1545                                                      
REMARK 465     ASP E  1546                                                      
REMARK 465     LEU E  1547                                                      
REMARK 465     MET E  1548                                                      
REMARK 465     THR E  1549                                                      
REMARK 465     GLU E  1550                                                      
REMARK 465     MET E  1551                                                      
REMARK 465     THR E  1552                                                      
REMARK 465     ASP E  1553                                                      
REMARK 465     LEU E  1554                                                      
REMARK 465     THR E  1555                                                      
REMARK 465     SER E  1556                                                      
REMARK 465     ASP E  1557                                                      
REMARK 465     LEU E  1558                                                      
REMARK 465     LEU E  1559                                                      
REMARK 465     GLY E  1560                                                      
REMARK 465     SER E  1561                                                      
REMARK 465     GLY E  1562                                                      
REMARK 465     GLY E  1758                                                      
REMARK 465     PRO E  1759                                                      
REMARK 465     GLY E  1760                                                      
REMARK 465     ALA E  1761                                                      
REMARK 465     GLY E  1762                                                      
REMARK 465     GLU E  1763                                                      
REMARK 465     LYS E  1855                                                      
REMARK 465     HIS E  1856                                                      
REMARK 465     VAL E  1857                                                      
REMARK 465     LEU E  1858                                                      
REMARK 465     ARG E  1859                                                      
REMARK 465     GLU E  1860                                                      
REMARK 465     ASN E  1861                                                      
REMARK 465     GLN E  1862                                                      
REMARK 465     ASP E  1863                                                      
REMARK 465     TYR E  1864                                                      
REMARK 465     VAL E  1865                                                      
REMARK 465     PRO E  1866                                                      
REMARK 465     GLY E  1867                                                      
REMARK 465     GLU E  1868                                                      
REMARK 465     ARG E  1869                                                      
REMARK 465     THR E  1870                                                      
REMARK 465     PRO E  1871                                                      
REMARK 465     MET E  1872                                                      
REMARK 465     LEU E  1873                                                      
REMARK 465     GLU E  1874                                                      
REMARK 465     ASP E  1875                                                      
REMARK 465     VAL E  1876                                                      
REMARK 465     ASP E  1877                                                      
REMARK 465     GLU E  1878                                                      
REMARK 465     GLY E  1879                                                      
REMARK 465     ASP E  1891                                                      
REMARK 465     GLU E  1892                                                      
REMARK 465     PRO E  1893                                                      
REMARK 465     GLU E  1894                                                      
REMARK 465     PRO E  1895                                                      
REMARK 465     PRO E  1896                                                      
REMARK 465     ARG E  1897                                                      
REMARK 465     PRO E  1898                                                      
REMARK 465     ARG E  1899                                                      
REMARK 465     ARG E  1900                                                      
REMARK 465     GLY E  1901                                                      
REMARK 465     SER E  1902                                                      
REMARK 465     LEU E  1903                                                      
REMARK 465     ARG E  1904                                                      
REMARK 465     GLY E  1905                                                      
REMARK 465     GLY E  1906                                                      
REMARK 465     GLU E  1907                                                      
REMARK 465     ARG E  1908                                                      
REMARK 465     GLU E  1909                                                      
REMARK 465     ARG E  1910                                                      
REMARK 465     ALA E  1911                                                      
REMARK 465     LYS E  1912                                                      
REMARK 465     ALA E  1913                                                      
REMARK 465     ASP E  2024                                                      
REMARK 465     HIS E  2025                                                      
REMARK 465     LYS E  2026                                                      
REMARK 465     LEU E  2027                                                      
REMARK 465     GLY E  2028                                                      
REMARK 465     ARG E  2029                                                      
REMARK 465     ASP E  2030                                                      
REMARK 465     SER E  2031                                                      
REMARK 465     ASN E  2130                                                      
REMARK 465     LYS E  2131                                                      
REMARK 465     VAL E  2132                                                      
REMARK 465     THR E  2133                                                      
REMARK 465     ASP E  2134                                                      
REMARK 465     LEU E  2135                                                      
REMARK 465     MET F  1503                                                      
REMARK 465     GLY F  1504                                                      
REMARK 465     HIS F  1505                                                      
REMARK 465     HIS F  1506                                                      
REMARK 465     HIS F  1507                                                      
REMARK 465     HIS F  1508                                                      
REMARK 465     HIS F  1509                                                      
REMARK 465     HIS F  1510                                                      
REMARK 465     TYR F  1511                                                      
REMARK 465     ARG F  1512                                                      
REMARK 465     ARG F  1513                                                      
REMARK 465     LYS F  1514                                                      
REMARK 465     SER F  1515                                                      
REMARK 465     LYS F  1516                                                      
REMARK 465     GLN F  1517                                                      
REMARK 465     ALA F  1518                                                      
REMARK 465     LEU F  1519                                                      
REMARK 465     ARG F  1520                                                      
REMARK 465     ASP F  1521                                                      
REMARK 465     TYR F  1522                                                      
REMARK 465     LYS F  1523                                                      
REMARK 465     LYS F  1524                                                      
REMARK 465     VAL F  1525                                                      
REMARK 465     GLN F  1526                                                      
REMARK 465     ILE F  1527                                                      
REMARK 465     GLN F  1528                                                      
REMARK 465     LEU F  1529                                                      
REMARK 465     GLU F  1530                                                      
REMARK 465     ASN F  1531                                                      
REMARK 465     LEU F  1532                                                      
REMARK 465     GLU F  1533                                                      
REMARK 465     SER F  1534                                                      
REMARK 465     SER F  1535                                                      
REMARK 465     VAL F  1536                                                      
REMARK 465     ARG F  1537                                                      
REMARK 465     ASP F  1538                                                      
REMARK 465     ARG F  1539                                                      
REMARK 465     CYS F  1540                                                      
REMARK 465     LYS F  1541                                                      
REMARK 465     LYS F  1542                                                      
REMARK 465     GLU F  1543                                                      
REMARK 465     PHE F  1544                                                      
REMARK 465     THR F  1545                                                      
REMARK 465     ASP F  1546                                                      
REMARK 465     LEU F  1547                                                      
REMARK 465     MET F  1548                                                      
REMARK 465     THR F  1549                                                      
REMARK 465     GLU F  1550                                                      
REMARK 465     MET F  1551                                                      
REMARK 465     THR F  1552                                                      
REMARK 465     ASP F  1553                                                      
REMARK 465     LEU F  1554                                                      
REMARK 465     THR F  1555                                                      
REMARK 465     SER F  1556                                                      
REMARK 465     ASP F  1557                                                      
REMARK 465     LEU F  1558                                                      
REMARK 465     LEU F  1559                                                      
REMARK 465     GLY F  1560                                                      
REMARK 465     SER F  1561                                                      
REMARK 465     GLY F  1562                                                      
REMARK 465     GLY F  1758                                                      
REMARK 465     PRO F  1759                                                      
REMARK 465     GLY F  1760                                                      
REMARK 465     ALA F  1761                                                      
REMARK 465     GLY F  1762                                                      
REMARK 465     GLU F  1763                                                      
REMARK 465     LYS F  1855                                                      
REMARK 465     HIS F  1856                                                      
REMARK 465     VAL F  1857                                                      
REMARK 465     LEU F  1858                                                      
REMARK 465     ARG F  1859                                                      
REMARK 465     GLU F  1860                                                      
REMARK 465     ASN F  1861                                                      
REMARK 465     GLN F  1862                                                      
REMARK 465     ASP F  1863                                                      
REMARK 465     TYR F  1864                                                      
REMARK 465     VAL F  1865                                                      
REMARK 465     PRO F  1866                                                      
REMARK 465     GLY F  1867                                                      
REMARK 465     GLU F  1868                                                      
REMARK 465     ARG F  1869                                                      
REMARK 465     THR F  1870                                                      
REMARK 465     PRO F  1871                                                      
REMARK 465     MET F  1872                                                      
REMARK 465     LEU F  1873                                                      
REMARK 465     GLU F  1874                                                      
REMARK 465     ASP F  1875                                                      
REMARK 465     VAL F  1876                                                      
REMARK 465     ASP F  1877                                                      
REMARK 465     GLU F  1878                                                      
REMARK 465     GLY F  1879                                                      
REMARK 465     ASP F  1891                                                      
REMARK 465     GLU F  1892                                                      
REMARK 465     PRO F  1893                                                      
REMARK 465     GLU F  1894                                                      
REMARK 465     PRO F  1895                                                      
REMARK 465     PRO F  1896                                                      
REMARK 465     ARG F  1897                                                      
REMARK 465     PRO F  1898                                                      
REMARK 465     ARG F  1899                                                      
REMARK 465     ARG F  1900                                                      
REMARK 465     GLY F  1901                                                      
REMARK 465     SER F  1902                                                      
REMARK 465     LEU F  1903                                                      
REMARK 465     ARG F  1904                                                      
REMARK 465     GLY F  1905                                                      
REMARK 465     GLY F  1906                                                      
REMARK 465     GLU F  1907                                                      
REMARK 465     ARG F  1908                                                      
REMARK 465     GLU F  1909                                                      
REMARK 465     ARG F  1910                                                      
REMARK 465     ALA F  1911                                                      
REMARK 465     LYS F  1912                                                      
REMARK 465     ASP F  2024                                                      
REMARK 465     HIS F  2025                                                      
REMARK 465     LYS F  2026                                                      
REMARK 465     LEU F  2027                                                      
REMARK 465     GLY F  2028                                                      
REMARK 465     ARG F  2029                                                      
REMARK 465     ASP F  2030                                                      
REMARK 465     SER F  2031                                                      
REMARK 465     ASN F  2130                                                      
REMARK 465     LYS F  2131                                                      
REMARK 465     VAL F  2132                                                      
REMARK 465     THR F  2133                                                      
REMARK 465     ASP F  2134                                                      
REMARK 465     LEU F  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 D2108    CG   CD   OE1  OE2                                  
REMARK 470     GLU E2108    CG   CD   OE1  OE2                                  
REMARK 470     GLU F2108    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   ND2  ASN A    39     O    GLY D  1813              1.90            
REMARK 500   CD1  LEU C    19     CD1  LEU C   165              1.94            
REMARK 500   O    ARG E  1984     ND2  ASN E  1988              1.97            
REMARK 500   CE2  TYR F  2078     O    GLY F  2080              2.14            
REMARK 500   O    SER F  1980     CB   ARG F  1984              2.19            
REMARK 500   CE2  TYR D  2078     O    GLY D  2080              2.19            
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    GLN A 162   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    HIS D1814   N   -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    SER D1980   CB  -  CA  -  C   ANGL. DEV. =  13.8 DEGREES          
REMARK 500    SER D1980   N   -  CA  -  C   ANGL. DEV. = -22.8 DEGREES          
REMARK 500    HIS E1814   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    ILE E1917   N   -  CA  -  C   ANGL. DEV. =  19.1 DEGREES          
REMARK 500    SER E1980   CB  -  CA  -  C   ANGL. DEV. =  13.0 DEGREES          
REMARK 500    SER E1980   N   -  CA  -  C   ANGL. DEV. = -20.8 DEGREES          
REMARK 500    PHE F1577   N   -  CA  -  C   ANGL. DEV. =  17.4 DEGREES          
REMARK 500    HIS F1814   N   -  CA  -  C   ANGL. DEV. =  17.0 DEGREES          
REMARK 500    ILE F1917   N   -  CA  -  C   ANGL. DEV. =  19.6 DEGREES          
REMARK 500    SER F1980   CB  -  CA  -  C   ANGL. DEV. =  14.4 DEGREES          
REMARK 500    SER F1980   N   -  CA  -  C   ANGL. DEV. = -21.3 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    VAL A  36      -76.74    -87.64                                   
REMARK 500    PHE A  37       27.94   -144.46                                   
REMARK 500    HIS A 104      -72.08    -94.53                                   
REMARK 500    LYS A 153      161.45    178.67                                   
REMARK 500    VAL B  36      -77.46    -87.55                                   
REMARK 500    PHE B  37       28.14   -143.41                                   
REMARK 500    HIS B 104      -72.30    -94.77                                   
REMARK 500    VAL C  36      -77.44    -88.19                                   
REMARK 500    PHE C  37       27.43   -143.88                                   
REMARK 500    HIS C 104      -72.33    -94.77                                   
REMARK 500    LYS C 153      161.51    178.34                                   
REMARK 500    PRO D1564       92.45    -69.87                                   
REMARK 500    PHE D1577       65.47   -118.77                                   
REMARK 500    ARG D1581      -62.41     79.22                                   
REMARK 500    ARG D1587      151.92    170.88                                   
REMARK 500    LEU D1589      -34.10    -38.96                                   
REMARK 500    LEU D1645       30.12    -85.98                                   
REMARK 500    LYS D1670      -88.71    -77.25                                   
REMARK 500    LEU D1674        1.65    -69.09                                   
REMARK 500    THR D1679       50.67    -68.56                                   
REMARK 500    SER D1702      -52.64   -130.52                                   
REMARK 500    SER D1725        3.95    -65.25                                   
REMARK 500    VAL D1726      -72.82   -114.11                                   
REMARK 500    VAL D1771     -164.48   -106.39                                   
REMARK 500    ASP D1773      -34.50    -39.26                                   
REMARK 500    TYR D1789       54.36   -159.16                                   
REMARK 500    HIS D1814       71.45     64.56                                   
REMARK 500    ASP D1821     -151.84   -150.98                                   
REMARK 500    HIS D1885      -66.14   -133.06                                   
REMARK 500    ILE D1917      -60.11   -100.90                                   
REMARK 500    TYR D1918       46.87     76.93                                   
REMARK 500    LYS D1931      -62.36    -28.05                                   
REMARK 500    LEU D1941       38.81    -92.31                                   
REMARK 500    ASN D1979       48.23    -70.68                                   
REMARK 500    SER D1980      -96.99   -144.48                                   
REMARK 500    ARG D1984      -66.22   -105.07                                   
REMARK 500    PHE D1985      -71.01    -80.71                                   
REMARK 500    GLN D1994        2.16    -65.29                                   
REMARK 500    ILE D2033      -71.34    -80.83                                   
REMARK 500    LEU D2036       48.72    -88.61                                   
REMARK 500    LEU D2037      -61.94   -127.13                                   
REMARK 500    TRP D2076      -71.53    -71.46                                   
REMARK 500    ASP D2081      104.15    -52.92                                   
REMARK 500    PHE E1577       57.85   -115.06                                   
REMARK 500    ARG E1581      -61.46     79.74                                   
REMARK 500    ARG E1587      152.71    171.02                                   
REMARK 500    LEU E1589      -34.93    -39.06                                   
REMARK 500    LYS E1670      -89.41    -76.40                                   
REMARK 500    LEU E1674        2.13    -69.21                                   
REMARK 500    THR E1679       51.20    -69.18                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      97 RAMACHANDRAN OUTLIERS.                        
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    TYR A  72        24.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL A  85        23.4      L          L   OUTSIDE RANGE           
REMARK 500    TRP A  97        24.6      L          L   OUTSIDE RANGE           
REMARK 500    GLN A 162        23.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU B  67        24.9      L          L   OUTSIDE RANGE           
REMARK 500    TYR B  72        24.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL B  85        23.5      L          L   OUTSIDE RANGE           
REMARK 500    TRP B  97        24.7      L          L   OUTSIDE RANGE           
REMARK 500    TYR C  72        23.9      L          L   OUTSIDE RANGE           
REMARK 500    VAL C  85        23.3      L          L   OUTSIDE RANGE           
REMARK 500    TRP C  97        24.6      L          L   OUTSIDE RANGE           
REMARK 500    MET D1675        24.2      L          L   OUTSIDE RANGE           
REMARK 500    GLN D1765        22.6      L          L   OUTSIDE RANGE           
REMARK 500    LYS D1790        23.2      L          L   OUTSIDE RANGE           
REMARK 500    HIS D1814        21.4      L          L   OUTSIDE RANGE           
REMARK 500    ILE D1917        20.7      L          L   OUTSIDE RANGE           
REMARK 500    SER D1980        47.4      L          L   OUTSIDE RANGE           
REMARK 500    ILE D2042        24.5      L          L   OUTSIDE RANGE           
REMARK 500    PHE E1577        23.4      L          L   OUTSIDE RANGE           
REMARK 500    MET E1675        24.0      L          L   OUTSIDE RANGE           
REMARK 500    GLN E1765        23.5      L          L   OUTSIDE RANGE           
REMARK 500    LYS E1790        23.3      L          L   OUTSIDE RANGE           
REMARK 500    HIS E1814        21.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE E1917        20.4      L          L   OUTSIDE RANGE           
REMARK 500    SER E1980        45.9      L          L   OUTSIDE RANGE           
REMARK 500    ILE E2042        24.9      L          L   OUTSIDE RANGE           
REMARK 500    PHE F1577        21.7      L          L   OUTSIDE RANGE           
REMARK 500    MET F1675        24.0      L          L   OUTSIDE RANGE           
REMARK 500    GLN F1765        23.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS F1790        23.1      L          L   OUTSIDE RANGE           
REMARK 500    HIS F1814        22.2      L          L   OUTSIDE RANGE           
REMARK 500    ILE F1917        19.7      L          L   OUTSIDE RANGE           
REMARK 500    SER F1980        46.0      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 GNP A 200   O2G                                                    
REMARK 620 2 GNP A 200   O3G  86.4                                              
REMARK 620 3 THR A  35   OG1  83.2 124.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP B 200   O2G                                                    
REMARK 620 2 GNP B 200   O3G  86.5                                              
REMARK 620 3 THR B  35   OG1  82.7 123.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 201  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GNP C 200   O2G                                                    
REMARK 620 2 GNP C 200   O3G  86.3                                              
REMARK 620 3 THR C  35   OG1  82.7 123.6                                        
REMARK 620 N                    1     2                                         
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 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP B 200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 201                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GNP C 200                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3SU8   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 S1625T CONFLICT IN UNP ENTRY O43157                                  
DBREF  3SUA A    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  3SUA B    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  3SUA C    1   177  UNP    P63000   RAC1_HUMAN       1    177             
DBREF  3SUA D 1511  2135  UNP    O43157   PLXB1_HUMAN   1511   2135             
DBREF  3SUA E 1511  2135  UNP    O43157   PLXB1_HUMAN   1511   2135             
DBREF  3SUA F 1511  2135  UNP    O43157   PLXB1_HUMAN   1511   2135             
SEQADV 3SUA LYS A  178  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS A  179  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS A  180  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS A  181  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS A  182  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS A  183  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS A  184  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA LYS B  178  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS B  179  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS B  180  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS B  181  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS B  182  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS B  183  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS B  184  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA LYS C  178  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS C  179  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS C  180  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS C  181  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS C  182  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS C  183  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA HIS C  184  UNP  P63000              EXPRESSION TAG                 
SEQADV 3SUA MET D 1503  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA GLY D 1504  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS D 1505  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS D 1506  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS D 1507  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS D 1508  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS D 1509  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS D 1510  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA THR D 1625  UNP  O43157    SER  1625 SEE REMARK 999                 
SEQADV 3SUA MET E 1503  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA GLY E 1504  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS E 1505  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS E 1506  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS E 1507  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS E 1508  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS E 1509  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS E 1510  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA THR E 1625  UNP  O43157    SER  1625 SEE REMARK 999                 
SEQADV 3SUA MET F 1503  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA GLY F 1504  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS F 1505  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS F 1506  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS F 1507  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS F 1508  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS F 1509  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA HIS F 1510  UNP  O43157              EXPRESSION TAG                 
SEQADV 3SUA THR F 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 B  184  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 B  184  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 B  184  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 B  184  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 B  184  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 B  184  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 B  184  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 B  184  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 B  184  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 B  184  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 B  184  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 B  184  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 B  184  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 B  184  ASP GLU ALA ILE ARG ALA VAL LEU LYS HIS HIS HIS HIS          
SEQRES  15 B  184  HIS HIS                                                      
SEQRES   1 C  184  MET GLN ALA ILE LYS CYS VAL VAL VAL GLY ASP GLY ALA          
SEQRES   2 C  184  VAL GLY LYS THR CYS LEU LEU ILE SER TYR THR THR ASN          
SEQRES   3 C  184  ALA PHE PRO GLY GLU TYR ILE PRO THR VAL PHE ASP ASN          
SEQRES   4 C  184  TYR SER ALA ASN VAL MET VAL ASP GLY LYS PRO VAL ASN          
SEQRES   5 C  184  LEU GLY LEU TRP ASP THR ALA GLY GLN GLU ASP TYR ASP          
SEQRES   6 C  184  ARG LEU ARG PRO LEU SER TYR PRO GLN THR ASP VAL PHE          
SEQRES   7 C  184  LEU ILE CYS PHE SER LEU VAL SER PRO ALA SER PHE GLU          
SEQRES   8 C  184  ASN VAL ARG ALA LYS TRP TYR PRO GLU VAL ARG HIS HIS          
SEQRES   9 C  184  CYS PRO ASN THR PRO ILE ILE LEU VAL GLY THR LYS LEU          
SEQRES  10 C  184  ASP LEU ARG ASP ASP LYS ASP THR ILE GLU LYS LEU LYS          
SEQRES  11 C  184  GLU LYS LYS LEU THR PRO ILE THR TYR PRO GLN GLY LEU          
SEQRES  12 C  184  ALA MET ALA LYS GLU ILE GLY ALA VAL LYS TYR LEU GLU          
SEQRES  13 C  184  CYS SER ALA LEU THR GLN ARG GLY LEU LYS THR VAL PHE          
SEQRES  14 C  184  ASP GLU ALA ILE ARG ALA VAL LEU LYS HIS HIS HIS HIS          
SEQRES  15 C  184  HIS HIS                                                      
SEQRES   1 D  633  MET GLY HIS HIS HIS HIS HIS HIS TYR ARG ARG LYS SER          
SEQRES   2 D  633  LYS GLN ALA LEU ARG ASP TYR LYS LYS VAL GLN ILE GLN          
SEQRES   3 D  633  LEU GLU ASN LEU GLU SER SER VAL ARG ASP ARG CYS LYS          
SEQRES   4 D  633  LYS GLU PHE THR ASP LEU MET THR GLU MET THR ASP LEU          
SEQRES   5 D  633  THR SER ASP LEU LEU GLY SER GLY ILE PRO PHE LEU ASP          
SEQRES   6 D  633  TYR LYS VAL TYR ALA GLU ARG ILE PHE PHE PRO GLY HIS          
SEQRES   7 D  633  ARG GLU SER PRO LEU HIS ARG ASP LEU GLY VAL PRO GLU          
SEQRES   8 D  633  SER ARG ARG PRO THR VAL GLU GLN GLY LEU GLY GLN LEU          
SEQRES   9 D  633  SER ASN LEU LEU ASN SER LYS LEU PHE LEU THR LYS PHE          
SEQRES  10 D  633  ILE HIS THR LEU GLU THR GLN ARG THR PHE SER ALA ARG          
SEQRES  11 D  633  ASP ARG ALA TYR VAL ALA SER LEU LEU THR VAL ALA LEU          
SEQRES  12 D  633  HIS GLY LYS LEU GLU TYR PHE THR ASP ILE LEU ARG THR          
SEQRES  13 D  633  LEU LEU SER ASP LEU VAL ALA GLN TYR VAL ALA LYS ASN          
SEQRES  14 D  633  PRO LYS LEU MET LEU ARG ARG THR GLU THR VAL VAL GLU          
SEQRES  15 D  633  LYS LEU LEU THR ASN TRP MET SER ILE CYS LEU TYR THR          
SEQRES  16 D  633  PHE VAL ARG ASP SER VAL GLY GLU PRO LEU TYR MET LEU          
SEQRES  17 D  633  PHE ARG GLY ILE LYS HIS GLN VAL ASP LYS GLY PRO VAL          
SEQRES  18 D  633  ASP SER VAL THR GLY LYS ALA LYS TYR THR LEU ASN ASP          
SEQRES  19 D  633  ASN ARG LEU LEU ARG GLU ASP VAL GLU TYR ARG PRO LEU          
SEQRES  20 D  633  THR LEU ASN ALA LEU LEU ALA VAL GLY PRO GLY ALA GLY          
SEQRES  21 D  633  GLU ALA GLN GLY VAL PRO VAL LYS VAL LEU ASP CYS ASP          
SEQRES  22 D  633  THR ILE SER GLN ALA LYS GLU LYS MET LEU ASP GLN LEU          
SEQRES  23 D  633  TYR LYS GLY VAL PRO LEU THR GLN ARG PRO ASP PRO ARG          
SEQRES  24 D  633  THR LEU ASP VAL GLU TRP ARG SER GLY VAL ALA GLY HIS          
SEQRES  25 D  633  LEU ILE LEU SER ASP GLU ASP VAL THR SER GLU VAL GLN          
SEQRES  26 D  633  GLY LEU TRP ARG ARG LEU ASN THR LEU GLN HIS TYR LYS          
SEQRES  27 D  633  VAL PRO ASP GLY ALA THR VAL ALA LEU VAL PRO CYS LEU          
SEQRES  28 D  633  THR LYS HIS VAL LEU ARG GLU ASN GLN ASP TYR VAL PRO          
SEQRES  29 D  633  GLY GLU ARG THR PRO MET LEU GLU ASP VAL ASP GLU GLY          
SEQRES  30 D  633  GLY ILE ARG PRO TRP HIS LEU VAL LYS PRO SER ASP GLU          
SEQRES  31 D  633  PRO GLU PRO PRO ARG PRO ARG ARG GLY SER LEU ARG GLY          
SEQRES  32 D  633  GLY GLU ARG GLU ARG ALA LYS ALA ILE PRO GLU ILE TYR          
SEQRES  33 D  633  LEU THR ARG LEU LEU SER MET LYS GLY THR LEU GLN LYS          
SEQRES  34 D  633  PHE VAL ASP ASP LEU PHE GLN VAL ILE LEU SER THR SER          
SEQRES  35 D  633  ARG PRO VAL PRO LEU ALA VAL LYS TYR PHE PHE ASP LEU          
SEQRES  36 D  633  LEU ASP GLU GLN ALA GLN GLN HIS GLY ILE SER ASP GLN          
SEQRES  37 D  633  ASP THR ILE HIS ILE TRP LYS THR ASN SER LEU PRO LEU          
SEQRES  38 D  633  ARG PHE TRP ILE ASN ILE ILE LYS ASN PRO GLN PHE VAL          
SEQRES  39 D  633  PHE ASP VAL GLN THR SER ASP ASN MET ASP ALA VAL LEU          
SEQRES  40 D  633  LEU VAL ILE ALA GLN THR PHE MET ASP ALA CYS THR LEU          
SEQRES  41 D  633  ALA ASP HIS LYS LEU GLY ARG ASP SER PRO ILE ASN LYS          
SEQRES  42 D  633  LEU LEU TYR ALA ARG ASP ILE PRO ARG TYR LYS ARG MET          
SEQRES  43 D  633  VAL GLU ARG TYR TYR ALA ASP ILE ARG GLN THR VAL PRO          
SEQRES  44 D  633  ALA SER ASP GLN GLU MET ASN SER VAL LEU ALA GLU LEU          
SEQRES  45 D  633  SER TRP ASN TYR SER GLY ASP LEU GLY ALA ARG VAL ALA          
SEQRES  46 D  633  LEU HIS GLU LEU TYR LYS TYR ILE ASN LYS TYR TYR ASP          
SEQRES  47 D  633  GLN ILE ILE THR ALA LEU GLU GLU ASP GLY THR ALA GLN          
SEQRES  48 D  633  LYS MET GLN LEU GLY TYR ARG LEU GLN GLN ILE ALA ALA          
SEQRES  49 D  633  ALA VAL GLU ASN LYS VAL THR ASP LEU                          
SEQRES   1 E  633  MET GLY HIS HIS HIS HIS HIS HIS TYR ARG ARG LYS SER          
SEQRES   2 E  633  LYS GLN ALA LEU ARG ASP TYR LYS LYS VAL GLN ILE GLN          
SEQRES   3 E  633  LEU GLU ASN LEU GLU SER SER VAL ARG ASP ARG CYS LYS          
SEQRES   4 E  633  LYS GLU PHE THR ASP LEU MET THR GLU MET THR ASP LEU          
SEQRES   5 E  633  THR SER ASP LEU LEU GLY SER GLY ILE PRO PHE LEU ASP          
SEQRES   6 E  633  TYR LYS VAL TYR ALA GLU ARG ILE PHE PHE PRO GLY HIS          
SEQRES   7 E  633  ARG GLU SER PRO LEU HIS ARG ASP LEU GLY VAL PRO GLU          
SEQRES   8 E  633  SER ARG ARG PRO THR VAL GLU GLN GLY LEU GLY GLN LEU          
SEQRES   9 E  633  SER ASN LEU LEU ASN SER LYS LEU PHE LEU THR LYS PHE          
SEQRES  10 E  633  ILE HIS THR LEU GLU THR GLN ARG THR PHE SER ALA ARG          
SEQRES  11 E  633  ASP ARG ALA TYR VAL ALA SER LEU LEU THR VAL ALA LEU          
SEQRES  12 E  633  HIS GLY LYS LEU GLU TYR PHE THR ASP ILE LEU ARG THR          
SEQRES  13 E  633  LEU LEU SER ASP LEU VAL ALA GLN TYR VAL ALA LYS ASN          
SEQRES  14 E  633  PRO LYS LEU MET LEU ARG ARG THR GLU THR VAL VAL GLU          
SEQRES  15 E  633  LYS LEU LEU THR ASN TRP MET SER ILE CYS LEU TYR THR          
SEQRES  16 E  633  PHE VAL ARG ASP SER VAL GLY GLU PRO LEU TYR MET LEU          
SEQRES  17 E  633  PHE ARG GLY ILE LYS HIS GLN VAL ASP LYS GLY PRO VAL          
SEQRES  18 E  633  ASP SER VAL THR GLY LYS ALA LYS TYR THR LEU ASN ASP          
SEQRES  19 E  633  ASN ARG LEU LEU ARG GLU ASP VAL GLU TYR ARG PRO LEU          
SEQRES  20 E  633  THR LEU ASN ALA LEU LEU ALA VAL GLY PRO GLY ALA GLY          
SEQRES  21 E  633  GLU ALA GLN GLY VAL PRO VAL LYS VAL LEU ASP CYS ASP          
SEQRES  22 E  633  THR ILE SER GLN ALA LYS GLU LYS MET LEU ASP GLN LEU          
SEQRES  23 E  633  TYR LYS GLY VAL PRO LEU THR GLN ARG PRO ASP PRO ARG          
SEQRES  24 E  633  THR LEU ASP VAL GLU TRP ARG SER GLY VAL ALA GLY HIS          
SEQRES  25 E  633  LEU ILE LEU SER ASP GLU ASP VAL THR SER GLU VAL GLN          
SEQRES  26 E  633  GLY LEU TRP ARG ARG LEU ASN THR LEU GLN HIS TYR LYS          
SEQRES  27 E  633  VAL PRO ASP GLY ALA THR VAL ALA LEU VAL PRO CYS LEU          
SEQRES  28 E  633  THR LYS HIS VAL LEU ARG GLU ASN GLN ASP TYR VAL PRO          
SEQRES  29 E  633  GLY GLU ARG THR PRO MET LEU GLU ASP VAL ASP GLU GLY          
SEQRES  30 E  633  GLY ILE ARG PRO TRP HIS LEU VAL LYS PRO SER ASP GLU          
SEQRES  31 E  633  PRO GLU PRO PRO ARG PRO ARG ARG GLY SER LEU ARG GLY          
SEQRES  32 E  633  GLY GLU ARG GLU ARG ALA LYS ALA ILE PRO GLU ILE TYR          
SEQRES  33 E  633  LEU THR ARG LEU LEU SER MET LYS GLY THR LEU GLN LYS          
SEQRES  34 E  633  PHE VAL ASP ASP LEU PHE GLN VAL ILE LEU SER THR SER          
SEQRES  35 E  633  ARG PRO VAL PRO LEU ALA VAL LYS TYR PHE PHE ASP LEU          
SEQRES  36 E  633  LEU ASP GLU GLN ALA GLN GLN HIS GLY ILE SER ASP GLN          
SEQRES  37 E  633  ASP THR ILE HIS ILE TRP LYS THR ASN SER LEU PRO LEU          
SEQRES  38 E  633  ARG PHE TRP ILE ASN ILE ILE LYS ASN PRO GLN PHE VAL          
SEQRES  39 E  633  PHE ASP VAL GLN THR SER ASP ASN MET ASP ALA VAL LEU          
SEQRES  40 E  633  LEU VAL ILE ALA GLN THR PHE MET ASP ALA CYS THR LEU          
SEQRES  41 E  633  ALA ASP HIS LYS LEU GLY ARG ASP SER PRO ILE ASN LYS          
SEQRES  42 E  633  LEU LEU TYR ALA ARG ASP ILE PRO ARG TYR LYS ARG MET          
SEQRES  43 E  633  VAL GLU ARG TYR TYR ALA ASP ILE ARG GLN THR VAL PRO          
SEQRES  44 E  633  ALA SER ASP GLN GLU MET ASN SER VAL LEU ALA GLU LEU          
SEQRES  45 E  633  SER TRP ASN TYR SER GLY ASP LEU GLY ALA ARG VAL ALA          
SEQRES  46 E  633  LEU HIS GLU LEU TYR LYS TYR ILE ASN LYS TYR TYR ASP          
SEQRES  47 E  633  GLN ILE ILE THR ALA LEU GLU GLU ASP GLY THR ALA GLN          
SEQRES  48 E  633  LYS MET GLN LEU GLY TYR ARG LEU GLN GLN ILE ALA ALA          
SEQRES  49 E  633  ALA VAL GLU ASN LYS VAL THR ASP LEU                          
SEQRES   1 F  633  MET GLY HIS HIS HIS HIS HIS HIS TYR ARG ARG LYS SER          
SEQRES   2 F  633  LYS GLN ALA LEU ARG ASP TYR LYS LYS VAL GLN ILE GLN          
SEQRES   3 F  633  LEU GLU ASN LEU GLU SER SER VAL ARG ASP ARG CYS LYS          
SEQRES   4 F  633  LYS GLU PHE THR ASP LEU MET THR GLU MET THR ASP LEU          
SEQRES   5 F  633  THR SER ASP LEU LEU GLY SER GLY ILE PRO PHE LEU ASP          
SEQRES   6 F  633  TYR LYS VAL TYR ALA GLU ARG ILE PHE PHE PRO GLY HIS          
SEQRES   7 F  633  ARG GLU SER PRO LEU HIS ARG ASP LEU GLY VAL PRO GLU          
SEQRES   8 F  633  SER ARG ARG PRO THR VAL GLU GLN GLY LEU GLY GLN LEU          
SEQRES   9 F  633  SER ASN LEU LEU ASN SER LYS LEU PHE LEU THR LYS PHE          
SEQRES  10 F  633  ILE HIS THR LEU GLU THR GLN ARG THR PHE SER ALA ARG          
SEQRES  11 F  633  ASP ARG ALA TYR VAL ALA SER LEU LEU THR VAL ALA LEU          
SEQRES  12 F  633  HIS GLY LYS LEU GLU TYR PHE THR ASP ILE LEU ARG THR          
SEQRES  13 F  633  LEU LEU SER ASP LEU VAL ALA GLN TYR VAL ALA LYS ASN          
SEQRES  14 F  633  PRO LYS LEU MET LEU ARG ARG THR GLU THR VAL VAL GLU          
SEQRES  15 F  633  LYS LEU LEU THR ASN TRP MET SER ILE CYS LEU TYR THR          
SEQRES  16 F  633  PHE VAL ARG ASP SER VAL GLY GLU PRO LEU TYR MET LEU          
SEQRES  17 F  633  PHE ARG GLY ILE LYS HIS GLN VAL ASP LYS GLY PRO VAL          
SEQRES  18 F  633  ASP SER VAL THR GLY LYS ALA LYS TYR THR LEU ASN ASP          
SEQRES  19 F  633  ASN ARG LEU LEU ARG GLU ASP VAL GLU TYR ARG PRO LEU          
SEQRES  20 F  633  THR LEU ASN ALA LEU LEU ALA VAL GLY PRO GLY ALA GLY          
SEQRES  21 F  633  GLU ALA GLN GLY VAL PRO VAL LYS VAL LEU ASP CYS ASP          
SEQRES  22 F  633  THR ILE SER GLN ALA LYS GLU LYS MET LEU ASP GLN LEU          
SEQRES  23 F  633  TYR LYS GLY VAL PRO LEU THR GLN ARG PRO ASP PRO ARG          
SEQRES  24 F  633  THR LEU ASP VAL GLU TRP ARG SER GLY VAL ALA GLY HIS          
SEQRES  25 F  633  LEU ILE LEU SER ASP GLU ASP VAL THR SER GLU VAL GLN          
SEQRES  26 F  633  GLY LEU TRP ARG ARG LEU ASN THR LEU GLN HIS TYR LYS          
SEQRES  27 F  633  VAL PRO ASP GLY ALA THR VAL ALA LEU VAL PRO CYS LEU          
SEQRES  28 F  633  THR LYS HIS VAL LEU ARG GLU ASN GLN ASP TYR VAL PRO          
SEQRES  29 F  633  GLY GLU ARG THR PRO MET LEU GLU ASP VAL ASP GLU GLY          
SEQRES  30 F  633  GLY ILE ARG PRO TRP HIS LEU VAL LYS PRO SER ASP GLU          
SEQRES  31 F  633  PRO GLU PRO PRO ARG PRO ARG ARG GLY SER LEU ARG GLY          
SEQRES  32 F  633  GLY GLU ARG GLU ARG ALA LYS ALA ILE PRO GLU ILE TYR          
SEQRES  33 F  633  LEU THR ARG LEU LEU SER MET LYS GLY THR LEU GLN LYS          
SEQRES  34 F  633  PHE VAL ASP ASP LEU PHE GLN VAL ILE LEU SER THR SER          
SEQRES  35 F  633  ARG PRO VAL PRO LEU ALA VAL LYS TYR PHE PHE ASP LEU          
SEQRES  36 F  633  LEU ASP GLU GLN ALA GLN GLN HIS GLY ILE SER ASP GLN          
SEQRES  37 F  633  ASP THR ILE HIS ILE TRP LYS THR ASN SER LEU PRO LEU          
SEQRES  38 F  633  ARG PHE TRP ILE ASN ILE ILE LYS ASN PRO GLN PHE VAL          
SEQRES  39 F  633  PHE ASP VAL GLN THR SER ASP ASN MET ASP ALA VAL LEU          
SEQRES  40 F  633  LEU VAL ILE ALA GLN THR PHE MET ASP ALA CYS THR LEU          
SEQRES  41 F  633  ALA ASP HIS LYS LEU GLY ARG ASP SER PRO ILE ASN LYS          
SEQRES  42 F  633  LEU LEU TYR ALA ARG ASP ILE PRO ARG TYR LYS ARG MET          
SEQRES  43 F  633  VAL GLU ARG TYR TYR ALA ASP ILE ARG GLN THR VAL PRO          
SEQRES  44 F  633  ALA SER ASP GLN GLU MET ASN SER VAL LEU ALA GLU LEU          
SEQRES  45 F  633  SER TRP ASN TYR SER GLY ASP LEU GLY ALA ARG VAL ALA          
SEQRES  46 F  633  LEU HIS GLU LEU TYR LYS TYR ILE ASN LYS TYR TYR ASP          
SEQRES  47 F  633  GLN ILE ILE THR ALA LEU GLU GLU ASP GLY THR ALA GLN          
SEQRES  48 F  633  LYS MET GLN LEU GLY TYR ARG LEU GLN GLN ILE ALA ALA          
SEQRES  49 F  633  ALA VAL GLU ASN LYS VAL THR ASP LEU                          
HET     MG  A 201       1                                                       
HET    GNP  A 200      32                                                       
HET     MG  B 201       1                                                       
HET    GNP  B 200      32                                                       
HET     MG  C 201       1                                                       
HET    GNP  C 200      32                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER                      
FORMUL   7   MG    3(MG 2+)                                                     
FORMUL   8  GNP    3(C10 H17 N6 O13 P3)                                         
HELIX    1   1 GLY A   15  ASN A   26  1                                  12    
HELIX    2   2 GLU A   62  ARG A   66  5                                   5    
HELIX    3   3 LEU A   67  TYR A   72  5                                   6    
HELIX    4   4 SER A   86  LYS A   96  1                                  11    
HELIX    5   5 LYS A   96  CYS A  105  1                                  10    
HELIX    6   6 LYS A  116  ASP A  121  1                                   6    
HELIX    7   7 ASP A  122  LYS A  132  1                                  11    
HELIX    8   8 THR A  138  GLY A  150  1                                  13    
HELIX    9   9 GLY A  164  LYS A  178  1                                  15    
HELIX   10  10 GLY B   15  ASN B   26  1                                  12    
HELIX   11  11 GLU B   62  ARG B   66  5                                   5    
HELIX   12  12 LEU B   67  TYR B   72  5                                   6    
HELIX   13  13 SER B   86  LYS B   96  1                                  11    
HELIX   14  14 LYS B   96  CYS B  105  1                                  10    
HELIX   15  15 LYS B  116  ASP B  121  1                                   6    
HELIX   16  16 ASP B  122  LYS B  132  1                                  11    
HELIX   17  17 THR B  138  GLY B  150  1                                  13    
HELIX   18  18 GLY B  164  LYS B  178  1                                  15    
HELIX   19  19 GLY C   15  ASN C   26  1                                  12    
HELIX   20  20 GLU C   62  ARG C   66  5                                   5    
HELIX   21  21 LEU C   67  TYR C   72  5                                   6    
HELIX   22  22 SER C   86  LYS C   96  1                                  11    
HELIX   23  23 LYS C   96  CYS C  105  1                                  10    
HELIX   24  24 LYS C  116  ASP C  121  1                                   6    
HELIX   25  25 ASP C  122  LYS C  132  1                                  11    
HELIX   26  26 THR C  138  GLY C  150  1                                  13    
HELIX   27  27 GLY C  164  LYS C  178  1                                  15    
HELIX   28  28 ASP D 1567  PHE D 1577  1                                  11    
HELIX   29  29 ARG D 1595  ASN D 1611  1                                  17    
HELIX   30  30 SER D 1612  GLN D 1626  1                                  15    
HELIX   31  31 SER D 1630  LEU D 1645  1                                  16    
HELIX   32  32 LYS D 1648  LYS D 1670  1                                  23    
HELIX   33  33 ASN D 1671  MET D 1675  5                                   5    
HELIX   34  34 VAL D 1682  SER D 1702  1                                  21    
HELIX   35  35 VAL D 1703  LYS D 1720  1                                  18    
HELIX   36  36 THR D 1776  TYR D 1789  1                                  14    
HELIX   37  37 ASP D 1799  ARG D 1801  5                                   3    
HELIX   38  38 THR D 1835  LYS D 1840  1                                   6    
HELIX   39  39 TYR D 1918  LEU D 1941  1                                  24    
HELIX   40  40 PRO D 1948  HIS D 1965  1                                  18    
HELIX   41  41 ASP D 1969  ASN D 1979  1                                  11    
HELIX   42  42 PHE D 1985  ASN D 1992  1                                   8    
HELIX   43  43 PRO D 1993  VAL D 1996  5                                   4    
HELIX   44  44 SER D 2002  THR D 2021  1                                  20    
HELIX   45  45 ASN D 2034  ALA D 2039  1                                   6    
HELIX   46  46 ASP D 2041  THR D 2059  1                                  19    
HELIX   47  47 SER D 2063  ASN D 2077  1                                  15    
HELIX   48  48 GLY D 2083  ASP D 2109  1                                  27    
HELIX   49  49 ASP D 2109  MET D 2115  1                                   7    
HELIX   50  50 GLN D 2116  GLU D 2129  1                                  14    
HELIX   51  51 ASP E 1567  PHE E 1577  1                                  11    
HELIX   52  52 ARG E 1595  ASN E 1611  1                                  17    
HELIX   53  53 SER E 1612  GLN E 1626  1                                  15    
HELIX   54  54 SER E 1630  LEU E 1645  1                                  16    
HELIX   55  55 LYS E 1648  LYS E 1670  1                                  23    
HELIX   56  56 ASN E 1671  MET E 1675  5                                   5    
HELIX   57  57 VAL E 1682  SER E 1702  1                                  21    
HELIX   58  58 VAL E 1703  LYS E 1720  1                                  18    
HELIX   59  59 THR E 1776  TYR E 1789  1                                  14    
HELIX   60  60 ASP E 1799  ARG E 1801  5                                   3    
HELIX   61  61 THR E 1835  LYS E 1840  1                                   6    
HELIX   62  62 TYR E 1918  LEU E 1941  1                                  24    
HELIX   63  63 PRO E 1948  HIS E 1965  1                                  18    
HELIX   64  64 ASP E 1969  ASN E 1979  1                                  11    
HELIX   65  65 PHE E 1985  ASN E 1992  1                                   8    
HELIX   66  66 SER E 2002  THR E 2021  1                                  20    
HELIX   67  67 ASN E 2034  ALA E 2039  1                                   6    
HELIX   68  68 ASP E 2041  THR E 2059  1                                  19    
HELIX   69  69 SER E 2063  ASN E 2077  1                                  15    
HELIX   70  70 GLY E 2083  ASP E 2109  1                                  27    
HELIX   71  71 ASP E 2109  MET E 2115  1                                   7    
HELIX   72  72 GLN E 2116  GLU E 2129  1                                  14    
HELIX   73  73 ASP F 1567  PHE F 1577  1                                  11    
HELIX   74  74 ARG F 1595  ASN F 1611  1                                  17    
HELIX   75  75 SER F 1612  GLN F 1626  1                                  15    
HELIX   76  76 SER F 1630  LEU F 1645  1                                  16    
HELIX   77  77 LYS F 1648  VAL F 1668  1                                  21    
HELIX   78  78 ASN F 1671  MET F 1675  5                                   5    
HELIX   79  79 VAL F 1682  SER F 1702  1                                  21    
HELIX   80  80 VAL F 1703  LYS F 1720  1                                  18    
HELIX   81  81 THR F 1776  TYR F 1789  1                                  14    
HELIX   82  82 ASP F 1799  ARG F 1801  5                                   3    
HELIX   83  83 THR F 1835  LYS F 1840  1                                   6    
HELIX   84  84 TYR F 1918  LEU F 1941  1                                  24    
HELIX   85  85 PRO F 1948  HIS F 1965  1                                  18    
HELIX   86  86 ASP F 1969  ASN F 1979  1                                  11    
HELIX   87  87 PHE F 1985  ASN F 1992  1                                   8    
HELIX   88  88 SER F 2002  THR F 2021  1                                  20    
HELIX   89  89 ASN F 2034  ALA F 2039  1                                   6    
HELIX   90  90 ASP F 2041  THR F 2059  1                                  19    
HELIX   91  91 SER F 2063  ASN F 2077  1                                  15    
HELIX   92  92 GLY F 2083  ASP F 2109  1                                  27    
HELIX   93  93 ASP F 2109  MET F 2115  1                                   7    
HELIX   94  94 GLN F 2116  GLU F 2129  1                                  14    
SHEET    1   A 4 ALA A  42  VAL A  46  0                                        
SHEET    2   A 4 LYS A  49  TRP A  56 -1  O  LEU A  53   N  ALA A  42           
SHEET    3   A 4 GLN A   2  VAL A   7  1  N  ILE A   4   O  ASN A  52           
SHEET    4   A 4 VAL A  77  PHE A  78  1  N  VAL A  77   O  LYS A   5           
SHEET    1   B 3 CYS A  81  SER A  83  0                                        
SHEET    2   B 3 LEU A 112  THR A 115  1  O  THR A 115   N  PHE A  82           
SHEET    3   B 3 TYR A 154  GLU A 156  1  O  LEU A 155   N  LEU A 112           
SHEET    1   C 4 ALA B  42  VAL B  46  0                                        
SHEET    2   C 4 LYS B  49  TRP B  56 -1  O  LEU B  53   N  ALA B  42           
SHEET    3   C 4 GLN B   2  VAL B   7  1  N  ILE B   4   O  ASN B  52           
SHEET    4   C 4 VAL B  77  PHE B  78  1  N  VAL B  77   O  LYS B   5           
SHEET    1   D 3 CYS B  81  SER B  83  0                                        
SHEET    2   D 3 LEU B 112  THR B 115  1  O  THR B 115   N  PHE B  82           
SHEET    3   D 3 TYR B 154  GLU B 156  1  O  LEU B 155   N  LEU B 112           
SHEET    1   E 6 ALA C  42  VAL C  46  0                                        
SHEET    2   E 6 LYS C  49  TRP C  56 -1  O  LEU C  53   N  ALA C  42           
SHEET    3   E 6 GLN C   2  GLY C  10  1  N  VAL C   8   O  TRP C  56           
SHEET    4   E 6 VAL C  77  SER C  83  1  O  CYS C  81   N  VAL C   9           
SHEET    5   E 6 LEU C 112  THR C 115  1  O  THR C 115   N  PHE C  82           
SHEET    6   E 6 TYR C 154  GLU C 156  1  O  LEU C 155   N  LEU C 112           
SHEET    1   F 5 VAL D1767  LEU D1772  0                                        
SHEET    2   F 5 PRO D1748  LEU D1755 -1  N  ALA D1753   O  VAL D1767           
SHEET    3   F 5 THR D1846  PRO D1851  1  O  VAL D1847   N  LEU D1754           
SHEET    4   F 5 LEU D1803  ARG D1808 -1  N  ASP D1804   O  VAL D1850           
SHEET    5   F 5 LEU D1815  LEU D1817 -1  O  LEU D1815   N  TRP D1807           
SHEET    1   G 3 VAL D1826  GLN D1827  0                                        
SHEET    2   G 3 TRP D1830  ARG D1832 -1  O  TRP D1830   N  GLN D1827           
SHEET    3   G 3 ARG D1882  TRP D1884  1  O  ARG D1882   N  ARG D1831           
SHEET    1   H 5 VAL E1767  LEU E1772  0                                        
SHEET    2   H 5 PRO E1748  LEU E1755 -1  N  ALA E1753   O  VAL E1767           
SHEET    3   H 5 THR E1846  PRO E1851  1  O  VAL E1847   N  LEU E1754           
SHEET    4   H 5 LEU E1803  ARG E1808 -1  N  ASP E1804   O  VAL E1850           
SHEET    5   H 5 LEU E1815  LEU E1817 -1  O  LEU E1815   N  TRP E1807           
SHEET    1   I 3 VAL E1826  GLN E1827  0                                        
SHEET    2   I 3 TRP E1830  ARG E1832 -1  O  TRP E1830   N  GLN E1827           
SHEET    3   I 3 ARG E1882  TRP E1884  1  O  ARG E1882   N  ARG E1831           
SHEET    1   J 5 VAL F1767  LEU F1772  0                                        
SHEET    2   J 5 PRO F1748  LEU F1755 -1  N  ALA F1753   O  VAL F1767           
SHEET    3   J 5 THR F1846  PRO F1851  1  O  VAL F1847   N  LEU F1754           
SHEET    4   J 5 LEU F1803  ARG F1808 -1  N  ASP F1804   O  VAL F1850           
SHEET    5   J 5 LEU F1815  LEU F1817 -1  O  LEU F1815   N  TRP F1807           
SHEET    1   K 3 GLU F1825  GLN F1827  0                                        
SHEET    2   K 3 TRP F1830  ARG F1832 -1  O  ARG F1832   N  GLU F1825           
SHEET    3   K 3 ARG F1882  TRP F1884  1  O  ARG F1882   N  ARG F1831           
LINK        MG    MG A 201                 O2G GNP A 200     1555   1555  1.95  
LINK        MG    MG B 201                 O2G GNP B 200     1555   1555  1.95  
LINK        MG    MG B 201                 O3G GNP B 200     1555   1555  1.96  
LINK        MG    MG C 201                 O2G GNP C 200     1555   1555  1.97  
LINK        MG    MG C 201                 O3G GNP C 200     1555   1555  1.98  
LINK        MG    MG A 201                 O3G GNP A 200     1555   1555  1.99  
LINK         OG1 THR A  35                MG    MG A 201     1555   1555  2.48  
LINK         OG1 THR B  35                MG    MG B 201     1555   1555  2.49  
LINK         OG1 THR C  35                MG    MG C 201     1555   1555  2.50  
SITE     1 AC1  3 THR A  17  THR A  35  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                               
SITE     1 AC3  3 THR B  17  THR B  35  GNP B 200                               
SITE     1 AC4 23 ASP B  11  GLY B  12  ALA B  13  VAL B  14                    
SITE     2 AC4 23 GLY B  15  LYS B  16  THR B  17  CYS B  18                    
SITE     3 AC4 23 PHE B  28  GLY B  30  TYR B  32  PRO B  34                    
SITE     4 AC4 23 THR B  35  THR B  58  GLY B  60  GLN B  61                    
SITE     5 AC4 23 LYS B 116  ASP B 118  LEU B 119  SER B 158                    
SITE     6 AC4 23 ALA B 159  LEU B 160   MG B 201                               
SITE     1 AC5  3 THR C  17  THR C  35  GNP C 200                               
SITE     1 AC6 23 ASP C  11  GLY C  12  ALA C  13  VAL C  14                    
SITE     2 AC6 23 GLY C  15  LYS C  16  THR C  17  CYS C  18                    
SITE     3 AC6 23 PHE C  28  GLY C  30  TYR C  32  PRO C  34                    
SITE     4 AC6 23 THR C  35  THR C  58  GLY C  60  GLN C  61                    
SITE     5 AC6 23 LYS C 116  ASP C 118  LEU C 119  SER C 158                    
SITE     6 AC6 23 ALA C 159  LEU C 160   MG C 201                               
CRYST1  142.340  224.250  258.160  90.00  90.00  90.00 I 21 21 21   24          
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      0.007025  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004459  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003874        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system