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Database: PDB
Entry: 4BJP
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HEADER    TRANSFERASE                             19-APR-13   4BJP              
TITLE     CRYSTAL STRUCTURE OF E. COLI PENICILLIN BINDING PROTEIN 3             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PENICILLIN BINDING PROTEIN TRANSPEPTIDASE DOMAIN PROTEIN;  
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 67-577;                                           
COMPND   5 SYNONYM: DD-TRANSPEPTIDASE;                                          
COMPND   6 EC: 2.4.1.129;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.SAUVAGE,M.JORIS,R.HERMAN,F.KERFF,M.ROCABOY,P.CHARLIER               
REVDAT   2   18-JUN-14 4BJP    1       JRNL                                     
REVDAT   1   07-MAY-14 4BJP    0                                                
JRNL        AUTH   E.SAUVAGE,A.DEROUAUX,C.FRAIPONT,M.JORIS,R.HERMAN,M.ROCABOY,  
JRNL        AUTH 2 M.SCHLOESSER,J.DUMAS,F.KERFF,M.NGUYEN-DISTECHE,P.CHARLIER    
JRNL        TITL   CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 3 (PBP3)     
JRNL        TITL 2 FROM ESCHERICHIA COLI.                                       
JRNL        REF    PLOS ONE                      V.   9 98042 2014              
JRNL        REFN                   ISSN 1932-6203                               
JRNL        PMID   24875494                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0098042                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.74                          
REMARK   3   NUMBER OF REFLECTIONS             : 19669                          
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) : 0.20107                         
REMARK   3   R VALUE            (WORKING SET) : 0.19876                         
REMARK   3   FREE R VALUE                     : 0.24493                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1038                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.500                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.565                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1371                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.12                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.212                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 81                           
REMARK   3   BIN FREE R VALUE                    : 0.241                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3105                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 169                                     
REMARK   3   SOLVENT ATOMS            : 135                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.164                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01                                                 
REMARK   3    B22 (A**2) : 0.01                                                 
REMARK   3    B33 (A**2) : -0.02                                                
REMARK   3    B12 (A**2) : 0.01                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.380         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.260         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.163         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.026        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.928                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3304 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4443 ; 1.415 ; 2.008       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   403 ; 6.430 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   126 ;34.821 ;23.333       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   522 ;16.464 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    25 ;19.189 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   502 ; 0.100 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2365 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2034 ; 0.555 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3282 ; 1.011 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1270 ; 1.742 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1161 ; 2.859 ; 4.500       
REMARK   3                                                                      
REMARK   3  ANISOTROPIC THERMAL FACTOR RESTRAINTS.   COUNT   RMS    WEIGHT      
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    71        A    92                          
REMARK   3    ORIGIN FOR THE GROUP (A): -20.7775  63.8131  30.5576              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2348 T22:   0.1901                                     
REMARK   3      T33:   0.1913 T12:   0.1440                                     
REMARK   3      T13:   0.0178 T23:  -0.0033                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8312 L22:   0.8948                                     
REMARK   3      L33:   1.5167 L12:   0.4484                                     
REMARK   3      L13:   1.0147 L23:   0.1231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1641 S12:  -0.2391 S13:   0.2307                       
REMARK   3      S21:   0.2555 S22:   0.0204 S23:   0.2541                       
REMARK   3      S31:  -0.3625 S32:  -0.4170 S33:   0.1438                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   113        A   151                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.5240  72.0445  28.5654              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1661 T22:   0.6553                                     
REMARK   3      T33:   0.9795 T12:   0.2207                                     
REMARK   3      T13:   0.0717 T23:  -0.0920                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3235 L22:   4.5993                                     
REMARK   3      L33:   2.0827 L12:  -0.0508                                     
REMARK   3      L13:  -0.2552 L23:  -2.8989                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3814 S12:  -0.0087 S13:   0.5576                       
REMARK   3      S21:   0.3636 S22:   1.1936 S23:  -0.2151                       
REMARK   3      S31:  -0.2959 S32:  -1.0459 S33:  -0.8122                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   163        A   285                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.0817  53.0469  23.1296              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1361 T22:   0.1064                                     
REMARK   3      T33:   0.1284 T12:   0.0205                                     
REMARK   3      T13:  -0.0006 T23:   0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2466 L22:   1.0563                                     
REMARK   3      L33:   1.2209 L12:  -0.2066                                     
REMARK   3      L13:   0.0291 L23:  -0.0965                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0107 S12:  -0.1407 S13:   0.0965                       
REMARK   3      S21:   0.0990 S22:  -0.0004 S23:   0.1250                       
REMARK   3      S31:  -0.1232 S32:  -0.1830 S33:   0.0111                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   286        A   432                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5189  27.4836  16.3364              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1322 T22:   0.1312                                     
REMARK   3      T33:   0.1379 T12:  -0.0086                                     
REMARK   3      T13:  -0.0113 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2024 L22:   1.1950                                     
REMARK   3      L33:   1.1877 L12:  -0.4054                                     
REMARK   3      L13:  -0.5033 L23:   0.3606                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0364 S12:   0.1284 S13:  -0.1356                       
REMARK   3      S21:  -0.1034 S22:  -0.0665 S23:   0.0784                       
REMARK   3      S31:   0.0350 S32:  -0.0944 S33:   0.0301                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   433        A   502                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.0673  40.5378  15.9496              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1309 T22:   0.1126                                     
REMARK   3      T33:   0.1516 T12:  -0.0050                                     
REMARK   3      T13:   0.0163 T23:   0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0405 L22:   1.0405                                     
REMARK   3      L33:   1.7137 L12:  -0.4220                                     
REMARK   3      L13:  -0.0119 L23:   0.0200                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0100 S12:   0.0538 S13:   0.0590                       
REMARK   3      S21:  -0.0600 S22:  -0.0161 S23:   0.0065                       
REMARK   3      S31:  -0.0034 S32:  -0.0434 S33:   0.0061                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   503        A   567                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6252  42.5027  10.4974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1749 T22:   0.1561                                     
REMARK   3      T33:   0.1010 T12:   0.0671                                     
REMARK   3      T13:   0.0212 T23:   0.0191                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2152 L22:   3.3287                                     
REMARK   3      L33:   2.3241 L12:   0.9804                                     
REMARK   3      L13:   0.4136 L23:   0.3618                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0022 S12:   0.0806 S13:  -0.0080                       
REMARK   3      S21:  -0.1227 S22:   0.0050 S23:   0.0461                       
REMARK   3      S31:   0.0222 S32:  -0.0357 S33:  -0.0027                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 4BJP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-APR-13.                  
REMARK 100 THE PDBE ID CODE IS EBI-56558.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAR-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 3                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97628                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 315R)                 
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20753                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.50                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 82.70                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 14.0                               
REMARK 200  R MERGE                    (I) : 0.17                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 10.4                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.90                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3EQU                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       46.41700            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       92.83400            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       69.62550            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      116.04250            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       23.20850            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       46.41700            
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        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       92.83400            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      116.04250            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       69.62550            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       23.20850            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 37230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -82.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       69.62550            
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     VAL A    67                                                      
REMARK 465     SER A    68                                                      
REMARK 465     THR A    69                                                      
REMARK 465     SER A    70                                                      
REMARK 465     ALA A    93                                                      
REMARK 465     ASP A    94                                                      
REMARK 465     PRO A    95                                                      
REMARK 465     LYS A    96                                                      
REMARK 465     GLU A    97                                                      
REMARK 465     VAL A    98                                                      
REMARK 465     HIS A    99                                                      
REMARK 465     ASP A   100                                                      
REMARK 465     ALA A   101                                                      
REMARK 465     GLY A   102                                                      
REMARK 465     GLY A   103                                                      
REMARK 465     ILE A   104                                                      
REMARK 465     SER A   105                                                      
REMARK 465     VAL A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     ASP A   108                                                      
REMARK 465     ARG A   109                                                      
REMARK 465     TRP A   110                                                      
REMARK 465     LYS A   111                                                      
REMARK 465     ALA A   112                                                      
REMARK 465     ILE A   119                                                      
REMARK 465     PRO A   120                                                      
REMARK 465     LEU A   121                                                      
REMARK 465     ASP A   122                                                      
REMARK 465     GLN A   123                                                      
REMARK 465     LEU A   124                                                      
REMARK 465     SER A   125                                                      
REMARK 465     ALA A   126                                                      
REMARK 465     ARG A   127                                                      
REMARK 465     ILE A   128                                                      
REMARK 465     ASN A   129                                                      
REMARK 465     ALA A   130                                                      
REMARK 465     ASN A   131                                                      
REMARK 465     PRO A   132                                                      
REMARK 465     LYS A   133                                                      
REMARK 465     GLY A   134                                                      
REMARK 465     ARG A   135                                                      
REMARK 465     PHE A   136                                                      
REMARK 465     ILE A   137                                                      
REMARK 465     TYR A   138                                                      
REMARK 465     LEU A   139                                                      
REMARK 465     ALA A   140                                                      
REMARK 465     ARG A   141                                                      
REMARK 465     LYS A   152                                                      
REMARK 465     LYS A   153                                                      
REMARK 465     LEU A   154                                                      
REMARK 465     LYS A   155                                                      
REMARK 465     LEU A   156                                                      
REMARK 465     PRO A   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     ILE A   159                                                      
REMARK 465     HIS A   160                                                      
REMARK 465     LEU A   161                                                      
REMARK 465     ARG A   162                                                      
REMARK 465     GLY A   202                                                      
REMARK 465     GLN A   203                                                      
REMARK 465     PRO A   204                                                      
REMARK 465     GLY A   205                                                      
REMARK 465     GLU A   206                                                      
REMARK 465     ARG A   207                                                      
REMARK 465     ILE A   208                                                      
REMARK 465     VAL A   209                                                      
REMARK 465     ARG A   210                                                      
REMARK 465     LYS A   211                                                      
REMARK 465     ASP A   212                                                      
REMARK 465     ARG A   213                                                      
REMARK 465     TYR A   214                                                      
REMARK 465     GLY A   215                                                      
REMARK 465     ARG A   216                                                      
REMARK 465     VAL A   217                                                      
REMARK 465     ILE A   218                                                      
REMARK 465     GLU A   219                                                      
REMARK 465     ASP A   220                                                      
REMARK 465     ILE A   221                                                      
REMARK 465     SER A   222                                                      
REMARK 465     SER A   223                                                      
REMARK 465     THR A   224                                                      
REMARK 465     ASP A   225                                                      
REMARK 465     SER A   226                                                      
REMARK 465     GLN A   227                                                      
REMARK 465     ALA A   228                                                      
REMARK 465     ALA A   537                                                      
REMARK 465     GLY A   538                                                      
REMARK 465     LYS A   539                                                      
REMARK 465     TYR A   540                                                      
REMARK 465     TYR A   541                                                      
REMARK 465     GLY A   542                                                      
REMARK 465     GLY A   543                                                      
REMARK 465     LEU A   568                                                      
REMARK 465     THR A   569                                                      
REMARK 465     THR A   570                                                      
REMARK 465     GLY A   571                                                      
REMARK 465     ASP A   572                                                      
REMARK 465     LYS A   573                                                      
REMARK 465     ASN A   574                                                      
REMARK 465     GLU A   575                                                      
REMARK 465     PHE A   576                                                      
REMARK 465     VAL A   577                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   S    SO4 A   603     S    SO4 A   603    11555     0.89            
REMARK 500   S    SO4 A   603     O1   SO4 A   603    11555     1.70            
REMARK 500   S    SO4 A   603     O3   SO4 A   603    11555     1.66            
REMARK 500   S    SO4 A   603     O4   SO4 A   603    11555     0.95            
REMARK 500   O1   SO4 A   603     O1   SO4 A   603    11555     0.98            
REMARK 500   O1   SO4 A   603     O4   SO4 A   603    11555     1.91            
REMARK 500   O2   SO4 A   603     O3   SO4 A   603    11555     2.17            
REMARK 500   O2   SO4 A   603     O4   SO4 A   603    11555     1.81            
REMARK 500   O3   SO4 A   603     O4   SO4 A   603    11555     0.66            
REMARK 500   O4   SO4 A   603     O4   SO4 A   603    11555     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    ARG A 457   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 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    SER A 280     -161.52   -115.16                                   
REMARK 500    ASN A 337      -88.91   -109.29                                   
REMARK 500    GLN A 523       96.15   -160.28                                   
REMARK 500    PRO A 565      154.33    -47.50                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CXS A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CXS A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CXS A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 628                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 629                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 630                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 631                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 641                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 642                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 643                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 644                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 645                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 646                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 647                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 649                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 650                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  CL A 660                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4BJQ   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF E. COLI PENICILLIN BINDING PROTEIN             
REMARK 900   3, DOMAIN V88-S165                                                 
DBREF  4BJP A   67   577  UNP    J2XFH0   J2XFH0_ECOLX    67    577             
SEQRES   1 A  511  VAL SER THR SER ARG GLY MET ILE THR ASP ARG SER GLY          
SEQRES   2 A  511  ARG PRO LEU ALA VAL SER VAL PRO VAL LYS ALA ILE TRP          
SEQRES   3 A  511  ALA ASP PRO LYS GLU VAL HIS ASP ALA GLY GLY ILE SER          
SEQRES   4 A  511  VAL GLY ASP ARG TRP LYS ALA LEU ALA ASN ALA LEU ASN          
SEQRES   5 A  511  ILE PRO LEU ASP GLN LEU SER ALA ARG ILE ASN ALA ASN          
SEQRES   6 A  511  PRO LYS GLY ARG PHE ILE TYR LEU ALA ARG GLN VAL ASN          
SEQRES   7 A  511  PRO ASP MET ALA ASP TYR ILE LYS LYS LEU LYS LEU PRO          
SEQRES   8 A  511  GLY ILE HIS LEU ARG GLU GLU SER ARG ARG TYR TYR PRO          
SEQRES   9 A  511  SER GLY GLU VAL THR ALA HIS LEU ILE GLY PHE THR ASN          
SEQRES  10 A  511  VAL ASP SER GLN GLY ILE GLU GLY VAL GLU LYS SER PHE          
SEQRES  11 A  511  ASP LYS TRP LEU THR GLY GLN PRO GLY GLU ARG ILE VAL          
SEQRES  12 A  511  ARG LYS ASP ARG TYR GLY ARG VAL ILE GLU ASP ILE SER          
SEQRES  13 A  511  SER THR ASP SER GLN ALA ALA HIS ASN LEU ALA LEU SER          
SEQRES  14 A  511  ILE ASP GLU ARG LEU GLN ALA LEU VAL TYR ARG GLU LEU          
SEQRES  15 A  511  ASN ASN ALA VAL ALA PHE ASN LYS ALA GLU SER GLY SER          
SEQRES  16 A  511  ALA VAL LEU VAL ASP VAL ASN THR GLY GLU VAL LEU ALA          
SEQRES  17 A  511  MET ALA ASN SER PRO SER TYR ASN PRO ASN ASN LEU SER          
SEQRES  18 A  511  GLY THR PRO LYS GLU ALA MET ARG ASN ARG THR ILE THR          
SEQRES  19 A  511  ASP VAL PHE GLU PRO GLY SER THR VAL LYS PRO MET VAL          
SEQRES  20 A  511  VAL MET THR ALA LEU GLN ARG GLY VAL VAL ARG GLU ASN          
SEQRES  21 A  511  SER VAL LEU ASN THR ILE PRO TYR ARG ILE ASN GLY HIS          
SEQRES  22 A  511  GLU ILE LYS ASP VAL ALA ARG TYR SER GLU LEU THR LEU          
SEQRES  23 A  511  THR GLY VAL LEU GLN LYS SER SER ASN VAL GLY VAL SER          
SEQRES  24 A  511  LYS LEU ALA LEU ALA MET PRO SER SER ALA LEU VAL ASP          
SEQRES  25 A  511  THR TYR SER ARG PHE GLY LEU GLY LYS ALA THR ASN LEU          
SEQRES  26 A  511  GLY LEU VAL GLY GLU ARG SER GLY LEU TYR PRO GLN LYS          
SEQRES  27 A  511  GLN ARG TRP SER ASP ILE GLU ARG ALA THR PHE SER PHE          
SEQRES  28 A  511  GLY TYR GLY LEU MET VAL THR PRO LEU GLN LEU ALA ARG          
SEQRES  29 A  511  VAL TYR ALA THR ILE GLY SER TYR GLY ILE TYR ARG PRO          
SEQRES  30 A  511  LEU SER ILE THR LYS VAL ASP PRO PRO VAL PRO GLY GLU          
SEQRES  31 A  511  ARG VAL PHE PRO GLU SER ILE VAL ARG THR VAL VAL HIS          
SEQRES  32 A  511  MET MET GLU SER VAL ALA LEU PRO GLY GLY GLY GLY VAL          
SEQRES  33 A  511  LYS ALA ALA ILE LYS GLY TYR ARG ILE ALA ILE LYS THR          
SEQRES  34 A  511  GLY THR ALA LYS LYS VAL GLY PRO ASP GLY ARG TYR ILE          
SEQRES  35 A  511  ASN LYS TYR ILE ALA TYR THR ALA GLY VAL ALA PRO ALA          
SEQRES  36 A  511  SER GLN PRO ARG PHE ALA LEU VAL VAL VAL ILE ASN ASP          
SEQRES  37 A  511  PRO GLN ALA GLY LYS TYR TYR GLY GLY ALA VAL SER ALA          
SEQRES  38 A  511  PRO VAL PHE GLY ALA ILE MET GLY GLY VAL LEU ARG THR          
SEQRES  39 A  511  MET ASN ILE GLU PRO ASP ALA LEU THR THR GLY ASP LYS          
SEQRES  40 A  511  ASN GLU PHE VAL                                              
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    CXS  A 611      14                                                       
HET    CXS  A 612      14                                                       
HET    CXS  A 613      14                                                       
HET    GOL  A 621       6                                                       
HET    GOL  A 622       6                                                       
HET    GOL  A 623       6                                                       
HET    GOL  A 624       6                                                       
HET    GOL  A 625       6                                                       
HET    GOL  A 626       6                                                       
HET    GOL  A 627       6                                                       
HET    GOL  A 628       6                                                       
HET    GOL  A 629       6                                                       
HET    GOL  A 630       6                                                       
HET    GOL  A 631       6                                                       
HET    EDO  A 641       4                                                       
HET    EDO  A 642       4                                                       
HET    EDO  A 643       4                                                       
HET    EDO  A 644       4                                                       
HET    EDO  A 645       4                                                       
HET    EDO  A 646       4                                                       
HET    EDO  A 647       4                                                       
HET    EDO  A 648       4                                                       
HET    EDO  A 649       4                                                       
HET    EDO  A 650       4                                                       
HET     CL  A 660       1                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     CXS 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  EDO    10(C2 H6 O2)                                                 
FORMUL   3  CXS    3(C9 H19 N O3 S)                                             
FORMUL   4  SO4    4(O4 S 2-)                                                   
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  GOL    11(C3 H8 O3)                                                 
FORMUL   7  HOH   *135(H2 O)                                                    
HELIX    1   1 LEU A  113  ASN A  118  1                                   6    
HELIX    2   2 ASN A  144  TYR A  150  1                                   7    
HELIX    3   3 SER A  171  VAL A  174  5                                   4    
HELIX    4   4 THR A  175  GLY A  180  1                                   6    
HELIX    5   5 GLU A  190  PHE A  196  1                                   7    
HELIX    6   6 PHE A  196  THR A  201  1                                   6    
HELIX    7   7 ASP A  237  ASN A  255  1                                  19    
HELIX    8   8 PRO A  290  MET A  294  5                                   5    
HELIX    9   9 ASN A  296  ASP A  301  1                                   6    
HELIX   10  10 PRO A  305  THR A  308  5                                   4    
HELIX   11  11 VAL A  309  ARG A  320  1                                  12    
HELIX   12  12 LEU A  352  LYS A  358  1                                   7    
HELIX   13  13 SER A  360  ALA A  370  1                                  11    
HELIX   14  14 SER A  373  PHE A  383  1                                  11    
HELIX   15  15 SER A  408  PHE A  417  1                                  10    
HELIX   16  16 THR A  424  SER A  437  1                                  14    
HELIX   17  17 PRO A  460  GLU A  472  1                                  13    
HELIX   18  18 SER A  473  LEU A  476  5                                   4    
HELIX   19  19 GLY A  481  ALA A  485  5                                   5    
HELIX   20  20 SER A  546  MET A  561  1                                  16    
SHEET    1  AA 4 GLU A 164  TYR A 168  0                                        
SHEET    2  AA 4 PRO A  81  VAL A  88 -1  O  VAL A  84   N  TYR A 168           
SHEET    3  AA 4 ILE A  74  THR A  75 -1  O  ILE A  74   N  LEU A  82           
SHEET    4  AA 4 LEU A 232  ALA A 233  1  O  LEU A 232   N  THR A  75           
SHEET    1  AB 5 VAL A 272  SER A 278  0                                        
SHEET    2  AB 5 SER A 259  ASP A 266 -1  O  GLY A 260   N  SER A 278           
SHEET    3  AB 5 PHE A 526  ASN A 533 -1  O  ALA A 527   N  VAL A 265           
SHEET    4  AB 5 TYR A 507  ALA A 519 -1  O  ALA A 513   N  ILE A 532           
SHEET    5  AB 5 ALA A 492  VAL A 501 -1  O  ALA A 492   N  VAL A 518           
SHEET    1  AC 2 VAL A 328  ASN A 330  0                                        
SHEET    2  AC 2 GLU A 349  THR A 351 -1  O  LEU A 350   N  LEU A 329           
SHEET    1  AD 2 TYR A 334  ARG A 335  0                                        
SHEET    2  AD 2 GLU A 340  ILE A 341 -1  O  ILE A 341   N  TYR A 334           
SHEET    1  AE 2 ILE A 440  TYR A 441  0                                        
SHEET    2  AE 2 GLU A 456  ARG A 457 -1  O  GLU A 456   N  TYR A 441           
CISPEP   1 SER A  278    PRO A  279          0         0.68                     
CISPEP   2 PRO A  451    PRO A  452          0         0.87                     
CISPEP   3 ALA A  519    PRO A  520          0        -9.55                     
SITE     1 AC1  7 ASN A 330  LYS A 366  GLN A 405  ARG A 406                    
SITE     2 AC1  7 CXS A 612  HOH A2053  HOH A2099                               
SITE     1 AC2  1 ARG A 457                                                     
SITE     1 AC3  3 LYS A 387  HOH A2132  HOH A2133                               
SITE     1 AC4  3 ARG A  77  LYS A 448  HOH A2004                               
SITE     1 AC5  6 GLU A 304  GLU A 349  MET A 422  GLY A 505                    
SITE     2 AC5  6 ARG A 506  TYR A 507                                          
SITE     1 AC6  5 LYS A 366  ALA A 370  GLN A 403  ARG A 406                    
SITE     2 AC6  5 SO4 A 601                                                     
SITE     1 AC7 10 ARG A 324  GLU A 325  ASN A 326  ARG A 397                    
SITE     2 AC7 10 SER A 398  GLY A 399  LEU A 400  GOL A 624                    
SITE     3 AC7 10 HOH A2049  HOH A2050                                          
SITE     1 AC8  7 LEU A 318  GLN A 319  GLY A 321  ARG A 382                    
SITE     2 AC8  7 GOL A 622  HOH A2045  HOH A2046                               
SITE     1 AC9  3 PHE A 459  PRO A 460  GOL A 621                               
SITE     1 BC1  7 SER A 259  GLY A 260  SER A 261  ASP A 301                    
SITE     2 BC1  7 ILE A 512  VAL A 531  ASN A 533                               
SITE     1 BC2  4 THR A 351  THR A 353  ARG A 397  CXS A 613                    
SITE     1 BC3  1 ASN A 255                                                     
SITE     1 BC4  1 ARG A  80                                                     
SITE     1 BC5  5 LEU A 232  ALA A 233  THR A 447  ASP A 450                    
SITE     2 BC5  5 PRO A 451                                                     
SITE     1 BC6  4 ARG A 320  GLY A 321  SER A 374  ASP A 378                    
SITE     1 BC7  6 ASN A 390  LEU A 444  SER A 445  PRO A 454                    
SITE     2 BC7  6 GLY A 455  HOH A2108                                          
SITE     1 BC8  6 SER A 307  SER A 359  THR A 495  GLY A 496                    
SITE     2 BC8  6 THR A 497  TYR A 514                                          
SITE     1 BC9  3 SER A 462  ARG A 465  THR A 466                               
SITE     1 CC1  1 ARG A 397                                                     
SITE     1 CC2  8 LEU A  82  TYR A 169  PRO A 170  SER A 171                    
SITE     2 CC2  8 GLY A 172  THR A 175  ALA A 176  PRO A 283                    
SITE     1 CC3  2 GLN A 403  GLN A 405                                          
SITE     1 CC4  1 GLY A 395                                                     
SITE     1 CC5  4 PHE A 303  GLU A 304  LYS A 499  VAL A 501                    
SITE     1 CC6  2 HIS A 230  ASN A 231                                          
SITE     1 CC7  5 SER A 195  PHE A 196  ASP A 197  LYS A 198                    
SITE     2 CC7  5 TRP A 199                                                     
SITE     1 CC8  4 LEU A 369  ALA A 370  MET A 371  PRO A 372                    
SITE     1 CC9  5 GLY A 321  ARG A 324  ASP A 378  ARG A 382                    
SITE     2 CC9  5 GLN A 403                                                     
SITE     1 DC1  3 GLU A 258  LYS A 500  ASN A 533                               
CRYST1  119.025  119.025  139.251  90.00  90.00 120.00 P 61 2 2     12          
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      0.008402  0.004851  0.000000        0.00000                         
SCALE2      0.000000  0.009701  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007181        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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