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Database: PDB
Entry: 4C5B
LinkDB: 4C5B
Original site: 4C5B 
HEADER    LIGASE                                  10-SEP-13   4C5B              
TITLE     THE X-RAY CRYSTAL STRUCTURE OF D-ALANYL-D-ALANINE LIGASE IN COMPLEX   
TITLE    2 WITH ATP AND D-ALA-D-ALA                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE--D-ALANINE LIGASE;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: D-ALA-D-ALA LIGASE, D-ALANYLALANINE SYNTHETASE, D-ALANYL-D- 
COMPND   5 ALANINE LIGASE;                                                      
COMPND   6 EC: 6.3.2.4;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K-12;                                                        
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: STAR-ROSETTA;                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET;                                       
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PPROEX                                    
KEYWDS    LIGASE, DDLB                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BATSON,V.MAJCE,A.J.LLOYD,D.REA,C.W.G.FISHWICK,K.J.SIMMONS,V.FULOP,  
AUTHOR   2 D.I.ROPER                                                            
REVDAT   2   24-JAN-18 4C5B    1       JRNL                                     
REVDAT   1   21-JAN-15 4C5B    0                                                
JRNL        AUTH   S.BATSON,C.DE CHIARA,V.MAJCE,A.J.LLOYD,S.GOBEC,D.REA,        
JRNL        AUTH 2 V.FULOP,C.W.THOROUGHGOOD,K.J.SIMMONS,C.G.DOWSON,             
JRNL        AUTH 3 C.W.G.FISHWICK,L.P.S.DE CARVALHO,D.I.ROPER                   
JRNL        TITL   INHIBITION OF D-ALA:D-ALA LIGASE THROUGH A PHOSPHORYLATED    
JRNL        TITL 2 FORM OF THE ANTIBIOTIC D-CYCLOSERINE.                        
JRNL        REF    NAT COMMUN                    V.   8  1939 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   29208891                                                     
JRNL        DOI    10.1038/S41467-017-02118-7                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0102                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.99                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 87714                          
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) : 0.171                           
REMARK   3   R VALUE            (WORKING SET) : 0.170                           
REMARK   3   FREE R VALUE                     : 0.200                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3729                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6275                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.33                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2630                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 258                          
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4610                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 107                                     
REMARK   3   SOLVENT ATOMS            : 766                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.63                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.29000                                              
REMARK   3    B22 (A**2) : -0.41000                                             
REMARK   3    B33 (A**2) : 0.11000                                              
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.075         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.076         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.046         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.445         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4791 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6491 ; 1.571 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   612 ; 5.835 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   182 ;35.301 ;24.945       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   814 ;13.838 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;18.120 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   738 ; 0.098 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3535 ; 0.008 ; 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):  3050 ; 0.908 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4844 ; 1.644 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1741 ; 2.729 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1647 ; 4.233 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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     1        A   111                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.2290  39.8760  50.0270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0161 T22:   0.0111                                     
REMARK   3      T33:   0.0865 T12:  -0.0029                                     
REMARK   3      T13:   0.0035 T23:   0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4075 L22:   0.4582                                     
REMARK   3      L33:   0.5676 L12:   0.1004                                     
REMARK   3      L13:   0.2338 L23:   0.1048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0365 S12:   0.0506 S13:   0.0740                       
REMARK   3      S21:  -0.0605 S22:   0.0115 S23:   0.0218                       
REMARK   3      S31:  -0.0648 S32:   0.0403 S33:   0.0249                       
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   112        A   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):  25.0970  31.6890  69.9430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0108 T22:   0.0278                                     
REMARK   3      T33:   0.0829 T12:   0.0006                                     
REMARK   3      T13:  -0.0051 T23:  -0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0665 L22:   0.6890                                     
REMARK   3      L33:   1.0452 L12:  -0.2664                                     
REMARK   3      L13:  -0.0671 L23:   0.0134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0065 S12:  -0.1056 S13:   0.0794                       
REMARK   3      S21:   0.0435 S22:   0.0326 S23:  -0.0654                       
REMARK   3      S31:   0.0104 S32:   0.1047 S33:  -0.0392                       
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   180        A   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.2940  32.6420  66.5000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0094 T22:   0.0236                                     
REMARK   3      T33:   0.0779 T12:  -0.0017                                     
REMARK   3      T13:   0.0169 T23:  -0.0019                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6989 L22:   0.3307                                     
REMARK   3      L33:   0.5298 L12:   0.0519                                     
REMARK   3      L13:   0.0337 L23:   0.0027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0160 S12:  -0.0944 S13:   0.0022                       
REMARK   3      S21:   0.0250 S22:  -0.0091 S23:   0.0495                       
REMARK   3      S31:   0.0027 S32:  -0.0511 S33:   0.0251                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   111                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.0270  57.9740  49.4600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0200 T22:   0.0216                                     
REMARK   3      T33:   0.1080 T12:  -0.0044                                     
REMARK   3      T13:   0.0066 T23:  -0.0345                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4580 L22:   0.4787                                     
REMARK   3      L33:   0.9437 L12:   0.1644                                     
REMARK   3      L13:  -0.2003 L23:  -0.1152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0074 S12:   0.0821 S13:  -0.0801                       
REMARK   3      S21:  -0.0358 S22:   0.0221 S23:  -0.0900                       
REMARK   3      S31:   0.0063 S32:  -0.0466 S33:  -0.0147                       
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 :   B   112        B   179                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.8190  66.1510  71.0450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0618 T22:   0.0483                                     
REMARK   3      T33:   0.0701 T12:  -0.0183                                     
REMARK   3      T13:   0.0148 T23:  -0.0176                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9966 L22:   0.7786                                     
REMARK   3      L33:   0.2826 L12:   0.4811                                     
REMARK   3      L13:   0.4082 L23:   0.3055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1443 S12:  -0.3048 S13:   0.0587                       
REMARK   3      S21:   0.0973 S22:  -0.1205 S23:   0.0571                       
REMARK   3      S31:   0.0192 S32:  -0.0930 S33:  -0.0238                       
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 :   B   180        B   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.4130  65.2550  65.2460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0438 T22:   0.0118                                     
REMARK   3      T33:   0.1231 T12:  -0.0098                                     
REMARK   3      T13:  -0.0277 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5465 L22:   0.3893                                     
REMARK   3      L33:   0.7206 L12:   0.2233                                     
REMARK   3      L13:  -0.0552 L23:   0.1869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0412 S12:  -0.0101 S13:  -0.0176                       
REMARK   3      S21:   0.0886 S22:   0.0010 S23:  -0.1419                       
REMARK   3      S31:   0.0069 S32:   0.0314 S33:  -0.0422                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES WITH TLS ADDED                                  
REMARK   4                                                                      
REMARK   4 4C5B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 10-SEP-13.                  
REMARK 100 THE DEPOSITION ID IS D_1290058251.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
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                       : I04                                
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 91443                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.100                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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 1IOW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 36.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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                                                                      
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       26.50000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.74500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.81000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.74500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.50000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.81000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -84.4 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -23                                                      
REMARK 465     SER A   -22                                                      
REMARK 465     TYR A   -21                                                      
REMARK 465     TYR A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     ASP A   -13                                                      
REMARK 465     TYR A   -12                                                      
REMARK 465     ILE A   -11                                                      
REMARK 465     PRO A   -10                                                      
REMARK 465     THR A    -9                                                      
REMARK 465     THR A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     TYR A    -4                                                      
REMARK 465     PHE A    -3                                                      
REMARK 465     ASN A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET B   -23                                                      
REMARK 465     SER B   -22                                                      
REMARK 465     TYR B   -21                                                      
REMARK 465     TYR B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     ASP B   -13                                                      
REMARK 465     TYR B   -12                                                      
REMARK 465     ILE B   -11                                                      
REMARK 465     PRO B   -10                                                      
REMARK 465     THR B    -9                                                      
REMARK 465     THR B    -8                                                      
REMARK 465     GLU B    -7                                                      
REMARK 465     ASN B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     TYR B    -4                                                      
REMARK 465     PHE B    -3                                                      
REMARK 465     ASN B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ALA B     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  2010     O    HOH B  2020              2.11            
REMARK 500   NH1  ARG B   168     O    HOH B  2230              2.11            
REMARK 500   O1   GOL A  1315     O    HOH A  2051              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O3   GOL A  1315     O    HOH A  2388     4556     2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2045        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A2085        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A2125        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH A2177        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B2012        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH B2361        DISTANCE =  5.82 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1313  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 310   O1B                                                    
REMARK 620 2 CO3 A 313   O2   97.7                                              
REMARK 620 3 GLU A 270   OE2  86.6 102.7                                        
REMARK 620 4 HOH A2254   O    91.7 103.8 153.4                                  
REMARK 620 5 GLU A 270   OE1  86.6 162.7  60.6  92.8                            
REMARK 620 6 ASN A 272   OD1 172.0  90.2  91.7  86.4  85.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1314  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 310   O2B                                                    
REMARK 620 2 ADP A 310   O1A  84.5                                              
REMARK 620 3 CO3 A 313   O3   83.5 168.0                                        
REMARK 620 4 ASP A 257   OD2 176.1  99.4  92.6                                  
REMARK 620 5 HOH A2326   O    90.6  91.3  89.0  89.0                            
REMARK 620 6 GLU A 270   OE2  94.5  91.1  89.8  85.7 174.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1308  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 310   O1B                                                    
REMARK 620 2 ADP B 310   O1A  83.6                                              
REMARK 620 3 CO3 B 313   O3   81.7 165.3                                        
REMARK 620 4 ASP B 257   OD2 172.7 103.6  91.1                                  
REMARK 620 5 HOH B2278   O    91.8  91.2  88.4  89.1                            
REMARK 620 6 GLU B 270   OE2  92.9  93.2  88.4  85.8 173.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1307  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 310   O3B                                                    
REMARK 620 2 CO3 B 313   O2   95.9                                              
REMARK 620 3 GLU B 270   OE2  86.6 101.2                                        
REMARK 620 4 ASN B 272   OD1 171.3  92.5  90.0                                  
REMARK 620 5 HOH B2198   O    93.3 104.6 154.1  86.3                            
REMARK 620 6 GLU B 270   OE1  87.3 161.4  60.7  84.1  93.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1309  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2285   O                                                      
REMARK 620 2 HIS B 280   NE2  87.8                                              
REMARK 620 3 HOH B2334   O   177.0  90.9                                        
REMARK 620 4 HOH B2336   O    88.6  84.9  88.6                                  
REMARK 620 5 HOH B2357   O    88.5 176.2  92.7  94.1                            
REMARK 620 6 HOH B2281   O    89.8  88.1  92.9 172.9  92.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1310  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2224   O                                                      
REMARK 620 2 HOH B2359   O    99.1                                              
REMARK 620 3 HOH B2360   O    88.4  83.2                                        
REMARK 620 4 HOH B2361   O   173.2  76.9  85.7                                  
REMARK 620 5 HOH B2225   O    87.2 172.8  93.7  96.4                            
REMARK 620 6 HOH B2358   O   101.4  91.9 169.7  84.4  90.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 A 313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1314                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1315                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1316                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IMD A 1317                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO3 B 313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Di-peptide DAL A 311 and DAL A    
REMARK 800  312                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: Binding site for Di-peptide DAL B 311 and DAL B    
REMARK 800  312                                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4C5A   RELATED DB: PDB                                   
REMARK 900 THE X-RAY CRYSTAL STRUCTURES OF D-ALANYL-D-ALANINE LIGASE IN         
REMARK 900 COMPLEX ADP AND D-CYCLOSERINE PHOSPHATE                              
REMARK 900 RELATED ID: 4C5C   RELATED DB: PDB                                   
REMARK 900 THE X-RAY CRYSTAL STRUCTURE OF D-ALANYL-D-ALANINE LIGASE IN COMPLEX  
REMARK 900 WITH ADP AND D-ALA-D-ALA                                             
DBREF  4C5B A    1   306  UNP    C4ZRI7   C4ZRI7_ECOBW     1    306             
DBREF  4C5B B    1   306  UNP    C4ZRI7   C4ZRI7_ECOBW     1    306             
SEQADV 4C5B MET A  -23  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B SER A  -22  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B TYR A  -21  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B TYR A  -20  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS A  -19  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS A  -18  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS A  -17  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS A  -16  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS A  -15  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS A  -14  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B ASP A  -13  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B TYR A  -12  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B ILE A  -11  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B PRO A  -10  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B THR A   -9  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B THR A   -8  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B GLU A   -7  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B ASN A   -6  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B LEU A   -5  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B TYR A   -4  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B PHE A   -3  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B ASN A   -2  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B GLY A   -1  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B ALA A    0  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B MET B  -23  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B SER B  -22  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B TYR B  -21  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B TYR B  -20  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS B  -19  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS B  -18  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS B  -17  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS B  -16  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS B  -15  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B HIS B  -14  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B ASP B  -13  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B TYR B  -12  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B ILE B  -11  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B PRO B  -10  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B THR B   -9  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B THR B   -8  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B GLU B   -7  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B ASN B   -6  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B LEU B   -5  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B TYR B   -4  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B PHE B   -3  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B ASN B   -2  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B GLY B   -1  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5B ALA B    0  UNP  C4ZRI7              EXPRESSION TAG                 
SEQRES   1 A  330  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ILE          
SEQRES   2 A  330  PRO THR THR GLU ASN LEU TYR PHE ASN GLY ALA MET THR          
SEQRES   3 A  330  ASP LYS ILE ALA VAL LEU LEU GLY GLY THR SER ALA GLU          
SEQRES   4 A  330  ARG GLU VAL SER LEU ASN SER GLY ALA ALA VAL LEU ALA          
SEQRES   5 A  330  GLY LEU ARG GLU GLY GLY ILE ASP ALA TYR PRO VAL ASP          
SEQRES   6 A  330  PRO LYS GLU VAL ASP VAL THR GLN LEU LYS SER MET GLY          
SEQRES   7 A  330  PHE GLN LYS VAL PHE ILE ALA LEU HIS GLY ARG GLY GLY          
SEQRES   8 A  330  GLU ASP GLY THR LEU GLN GLY MET LEU GLU LEU MET GLY          
SEQRES   9 A  330  LEU PRO TYR THR GLY SER GLY VAL MET ALA SER ALA LEU          
SEQRES  10 A  330  SER MET ASP LYS LEU ARG SER LYS LEU LEU TRP GLN GLY          
SEQRES  11 A  330  ALA GLY LEU PRO VAL ALA PRO TRP VAL ALA LEU THR ARG          
SEQRES  12 A  330  ALA GLU PHE GLU LYS GLY LEU SER ASP LYS GLN LEU ALA          
SEQRES  13 A  330  GLU ILE SER ALA LEU GLY LEU PRO VAL ILE VAL LYS PRO          
SEQRES  14 A  330  SER ARG GLU GLY SER SER VAL GLY MET SER LYS VAL VAL          
SEQRES  15 A  330  ALA GLU ASN ALA LEU GLN ASP ALA LEU ARG LEU ALA PHE          
SEQRES  16 A  330  GLN HIS ASP GLU GLU VAL LEU ILE GLU LYS TRP LEU SER          
SEQRES  17 A  330  GLY PRO GLU PHE THR VAL ALA ILE LEU GLY GLU GLU ILE          
SEQRES  18 A  330  LEU PRO SER ILE ARG ILE GLN PRO SER GLY THR PHE TYR          
SEQRES  19 A  330  ASP TYR GLU ALA LYS TYR LEU SER ASP GLU THR GLN TYR          
SEQRES  20 A  330  PHE CYS PRO ALA GLY LEU GLU ALA SER GLN GLU ALA ASN          
SEQRES  21 A  330  LEU GLN ALA LEU VAL LEU LYS ALA TRP THR THR LEU GLY          
SEQRES  22 A  330  CYS LYS GLY TRP GLY ARG ILE ASP VAL MET LEU ASP SER          
SEQRES  23 A  330  ASP GLY GLN PHE TYR LEU LEU GLU ALA ASN THR SER PRO          
SEQRES  24 A  330  GLY MET THR SER HIS SER LEU VAL PRO MET ALA ALA ARG          
SEQRES  25 A  330  GLN ALA GLY MET SER PHE SER GLN LEU VAL VAL ARG ILE          
SEQRES  26 A  330  LEU GLU LEU ALA ASP                                          
SEQRES   1 B  330  MET SER TYR TYR HIS HIS HIS HIS HIS HIS ASP TYR ILE          
SEQRES   2 B  330  PRO THR THR GLU ASN LEU TYR PHE ASN GLY ALA MET THR          
SEQRES   3 B  330  ASP LYS ILE ALA VAL LEU LEU GLY GLY THR SER ALA GLU          
SEQRES   4 B  330  ARG GLU VAL SER LEU ASN SER GLY ALA ALA VAL LEU ALA          
SEQRES   5 B  330  GLY LEU ARG GLU GLY GLY ILE ASP ALA TYR PRO VAL ASP          
SEQRES   6 B  330  PRO LYS GLU VAL ASP VAL THR GLN LEU LYS SER MET GLY          
SEQRES   7 B  330  PHE GLN LYS VAL PHE ILE ALA LEU HIS GLY ARG GLY GLY          
SEQRES   8 B  330  GLU ASP GLY THR LEU GLN GLY MET LEU GLU LEU MET GLY          
SEQRES   9 B  330  LEU PRO TYR THR GLY SER GLY VAL MET ALA SER ALA LEU          
SEQRES  10 B  330  SER MET ASP LYS LEU ARG SER LYS LEU LEU TRP GLN GLY          
SEQRES  11 B  330  ALA GLY LEU PRO VAL ALA PRO TRP VAL ALA LEU THR ARG          
SEQRES  12 B  330  ALA GLU PHE GLU LYS GLY LEU SER ASP LYS GLN LEU ALA          
SEQRES  13 B  330  GLU ILE SER ALA LEU GLY LEU PRO VAL ILE VAL LYS PRO          
SEQRES  14 B  330  SER ARG GLU GLY SER SER VAL GLY MET SER LYS VAL VAL          
SEQRES  15 B  330  ALA GLU ASN ALA LEU GLN ASP ALA LEU ARG LEU ALA PHE          
SEQRES  16 B  330  GLN HIS ASP GLU GLU VAL LEU ILE GLU LYS TRP LEU SER          
SEQRES  17 B  330  GLY PRO GLU PHE THR VAL ALA ILE LEU GLY GLU GLU ILE          
SEQRES  18 B  330  LEU PRO SER ILE ARG ILE GLN PRO SER GLY THR PHE TYR          
SEQRES  19 B  330  ASP TYR GLU ALA LYS TYR LEU SER ASP GLU THR GLN TYR          
SEQRES  20 B  330  PHE CYS PRO ALA GLY LEU GLU ALA SER GLN GLU ALA ASN          
SEQRES  21 B  330  LEU GLN ALA LEU VAL LEU LYS ALA TRP THR THR LEU GLY          
SEQRES  22 B  330  CYS LYS GLY TRP GLY ARG ILE ASP VAL MET LEU ASP SER          
SEQRES  23 B  330  ASP GLY GLN PHE TYR LEU LEU GLU ALA ASN THR SER PRO          
SEQRES  24 B  330  GLY MET THR SER HIS SER LEU VAL PRO MET ALA ALA ARG          
SEQRES  25 B  330  GLN ALA GLY MET SER PHE SER GLN LEU VAL VAL ARG ILE          
SEQRES  26 B  330  LEU GLU LEU ALA ASP                                          
HET    ADP  A 310      27                                                       
HET    DAL  A 311       5                                                       
HET    DAL  A 312       6                                                       
HET    CO3  A 313       4                                                       
HET     MG  A1313       1                                                       
HET     MG  A1314       1                                                       
HET    GOL  A1315       6                                                       
HET    GOL  A1316       6                                                       
HET    IMD  A1317       5                                                       
HET    ADP  B 310      27                                                       
HET    DAL  B 311       5                                                       
HET    DAL  B 312       6                                                       
HET    CO3  B 313       4                                                       
HET     MG  B1307       1                                                       
HET     MG  B1308       1                                                       
HET     MG  B1309       1                                                       
HET     MG  B1310       1                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     DAL D-ALANINE                                                        
HETNAM     CO3 CARBONATE ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     IMD IMIDAZOLE                                                        
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   4  DAL    4(C3 H7 N O2)                                                
FORMUL   6  CO3    2(C O3 2-)                                                   
FORMUL   7   MG    6(MG 2+)                                                     
FORMUL   9  GOL    2(C3 H8 O3)                                                  
FORMUL  11  IMD    C3 H5 N2 1+                                                  
FORMUL  20  HOH   *766(H2 O)                                                    
HELIX    1   1 GLU A   15  GLY A   33  1                                  19    
HELIX    2   2 ASP A   46  LEU A   50  5                                   5    
HELIX    3   3 GLY A   70  GLY A   80  1                                  11    
HELIX    4   4 GLY A   87  ASP A   96  1                                  10    
HELIX    5   5 ASP A   96  ALA A  107  1                                  12    
HELIX    6   6 ARG A  119  LYS A  124  1                                   6    
HELIX    7   7 SER A  127  GLY A  138  1                                  12    
HELIX    8   8 ALA A  159  ASN A  161  5                                   3    
HELIX    9   9 ALA A  162  GLN A  172  1                                  11    
HELIX   10  10 ASP A  211  LEU A  217  1                                   7    
HELIX   11  11 GLU A  230  GLY A  249  1                                  20    
HELIX   12  12 SER A  281  ALA A  290  1                                  10    
HELIX   13  13 SER A  293  LEU A  304  1                                  12    
HELIX   14  14 GLU B   15  GLY B   33  1                                  19    
HELIX   15  15 ASP B   46  LEU B   50  5                                   5    
HELIX   16  16 GLY B   70  GLY B   80  1                                  11    
HELIX   17  17 GLY B   87  ASP B   96  1                                  10    
HELIX   18  18 ASP B   96  ALA B  107  1                                  12    
HELIX   19  19 ARG B  119  GLY B  125  1                                   7    
HELIX   20  20 SER B  127  ALA B  136  1                                  10    
HELIX   21  21 ALA B  159  ASN B  161  5                                   3    
HELIX   22  22 ALA B  162  PHE B  171  1                                  10    
HELIX   23  23 ASP B  211  LEU B  217  1                                   7    
HELIX   24  24 GLU B  230  GLY B  249  1                                  20    
HELIX   25  25 SER B  281  ALA B  290  1                                  10    
HELIX   26  26 SER B  293  LEU B  304  1                                  12    
SHEET    1  AA 3 ASP A  36  VAL A  40  0                                        
SHEET    2  AA 3 LYS A   4  LEU A   8  1  O  ILE A   5   N  TYR A  38           
SHEET    3  AA 3 LYS A  57  ILE A  60  1  O  LYS A  57   N  ALA A   6           
SHEET    1  AB 4 TRP A 114  THR A 118  0                                        
SHEET    2  AB 4 GLU A 176  LYS A 181 -1  O  VAL A 177   N  LEU A 117           
SHEET    3  AB 4 VAL A 141  PRO A 145 -1  O  ILE A 142   N  GLU A 180           
SHEET    4  AB 4 SER A 155  VAL A 157 -1  O  SER A 155   N  VAL A 143           
SHEET    1  AC 2 GLU A 196  ILE A 197  0                                        
SHEET    2  AC 2 GLU A 187  LEU A 193 -1  O  LEU A 193   N  GLU A 196           
SHEET    1  AD 4 GLN A 222  PHE A 224  0                                        
SHEET    2  AD 4 ILE A 201  GLN A 204 -1  O  ARG A 202   N  PHE A 224           
SHEET    3  AD 4 GLU A 187  LEU A 193 -1  O  GLU A 187   N  ILE A 203           
SHEET    4  AD 4 GLU A 196  ILE A 197 -1  O  GLU A 196   N  LEU A 193           
SHEET    1  AE 5 GLN A 222  PHE A 224  0                                        
SHEET    2  AE 5 ILE A 201  GLN A 204 -1  O  ARG A 202   N  PHE A 224           
SHEET    3  AE 5 GLU A 187  LEU A 193 -1  O  GLU A 187   N  ILE A 203           
SHEET    4  AE 5 TRP A 253  LEU A 260 -1  O  GLY A 254   N  ILE A 192           
SHEET    5  AE 5 PHE A 266  ASN A 272 -1  O  TYR A 267   N  MET A 259           
SHEET    1  BA 3 ASP B  36  VAL B  40  0                                        
SHEET    2  BA 3 LYS B   4  LEU B   8  1  O  ILE B   5   N  TYR B  38           
SHEET    3  BA 3 LYS B  57  ILE B  60  1  O  LYS B  57   N  ALA B   6           
SHEET    1  BB 4 TRP B 114  THR B 118  0                                        
SHEET    2  BB 4 GLU B 176  LYS B 181 -1  O  VAL B 177   N  LEU B 117           
SHEET    3  BB 4 VAL B 141  PRO B 145 -1  O  ILE B 142   N  GLU B 180           
SHEET    4  BB 4 SER B 155  VAL B 157 -1  O  SER B 155   N  VAL B 143           
SHEET    1  BC 2 GLU B 196  ILE B 197  0                                        
SHEET    2  BC 2 GLU B 187  LEU B 193 -1  O  LEU B 193   N  GLU B 196           
SHEET    1  BD 4 GLN B 222  PHE B 224  0                                        
SHEET    2  BD 4 ILE B 201  GLN B 204 -1  O  ARG B 202   N  PHE B 224           
SHEET    3  BD 4 GLU B 187  LEU B 193 -1  O  GLU B 187   N  ILE B 203           
SHEET    4  BD 4 GLU B 196  ILE B 197 -1  O  GLU B 196   N  LEU B 193           
SHEET    1  BE 5 GLN B 222  PHE B 224  0                                        
SHEET    2  BE 5 ILE B 201  GLN B 204 -1  O  ARG B 202   N  PHE B 224           
SHEET    3  BE 5 GLU B 187  LEU B 193 -1  O  GLU B 187   N  ILE B 203           
SHEET    4  BE 5 TRP B 253  LEU B 260 -1  O  GLY B 254   N  ILE B 192           
SHEET    5  BE 5 PHE B 266  ASN B 272 -1  O  TYR B 267   N  MET B 259           
LINK         O1B ADP A 310                MG    MG A1313     1555   1555  2.07  
LINK         O2B ADP A 310                MG    MG A1314     1555   1555  2.03  
LINK         O1A ADP A 310                MG    MG A1314     1555   1555  2.06  
LINK         C   DAL A 311                 N   DAL A 312     1555   1555  1.33  
LINK         O3  CO3 A 313                MG    MG A1314     1555   1555  2.10  
LINK         O2  CO3 A 313                MG    MG A1313     1555   1555  1.98  
LINK        MG    MG A1313                 OE2 GLU A 270     1555   1555  2.17  
LINK        MG    MG A1313                 O   HOH A2254     1555   1555  2.06  
LINK        MG    MG A1313                 OE1 GLU A 270     1555   1555  2.25  
LINK        MG    MG A1313                 OD1 ASN A 272     1555   1555  2.15  
LINK        MG    MG A1314                 OD2 ASP A 257     1555   1555  2.08  
LINK        MG    MG A1314                 O   HOH A2326     1555   1555  2.13  
LINK        MG    MG A1314                 OE2 GLU A 270     1555   1555  2.13  
LINK         O1B ADP B 310                MG    MG B1308     1555   1555  2.12  
LINK         O3B ADP B 310                MG    MG B1307     1555   1555  2.03  
LINK         O1A ADP B 310                MG    MG B1308     1555   1555  1.99  
LINK         C   DAL B 311                 N   DAL B 312     1555   1555  1.33  
LINK         O3  CO3 B 313                MG    MG B1308     1555   1555  2.12  
LINK         O2  CO3 B 313                MG    MG B1307     1555   1555  1.95  
LINK        MG    MG B1307                 OE2 GLU B 270     1555   1555  2.18  
LINK        MG    MG B1307                 OD1 ASN B 272     1555   1555  2.12  
LINK        MG    MG B1307                 O   HOH B2198     1555   1555  2.09  
LINK        MG    MG B1307                 OE1 GLU B 270     1555   1555  2.26  
LINK        MG    MG B1308                 OD2 ASP B 257     1555   1555  2.02  
LINK        MG    MG B1308                 O   HOH B2278     1555   1555  2.11  
LINK        MG    MG B1308                 OE2 GLU B 270     1555   1555  2.10  
LINK        MG    MG B1309                 O   HOH B2285     1555   1555  2.15  
LINK        MG    MG B1309                 NE2 HIS B 280     1555   1555  2.27  
LINK        MG    MG B1309                 O   HOH B2334     1555   1555  2.07  
LINK        MG    MG B1309                 O   HOH B2336     1555   1555  2.00  
LINK        MG    MG B1309                 O   HOH B2357     1555   1555  1.98  
LINK        MG    MG B1309                 O   HOH B2281     1555   1555  2.16  
LINK        MG    MG B1310                 O   HOH B2224     1555   1555  2.09  
LINK        MG    MG B1310                 O   HOH B2359     1555   1555  2.07  
LINK        MG    MG B1310                 O   HOH B2360     1555   1555  2.17  
LINK        MG    MG B1310                 O   HOH B2361     1555   1555  2.27  
LINK        MG    MG B1310                 O   HOH B2225     1555   1555  2.01  
LINK        MG    MG B1310                 O   HOH B2358     1555   1555  2.01  
CISPEP   1 LEU A  139    PRO A  140          0        -1.93                     
CISPEP   2 GLY A  185    PRO A  186          0         6.26                     
CISPEP   3 CYS A  225    PRO A  226          0         4.15                     
CISPEP   4 LEU B  139    PRO B  140          0        -1.39                     
CISPEP   5 GLY B  185    PRO B  186          0         5.64                     
CISPEP   6 CYS B  225    PRO B  226          0         1.44                     
SITE     1 AC1 27 LYS A  97  ILE A 142  LYS A 144  GLU A 148                    
SITE     2 AC1 27 GLY A 149  SER A 150  SER A 151  MET A 154                    
SITE     3 AC1 27 GLU A 180  LYS A 181  TRP A 182  LEU A 183                    
SITE     4 AC1 27 GLU A 187  PHE A 209  TYR A 210  LYS A 215                    
SITE     5 AC1 27 ASP A 257  MET A 259  LEU A 269  GLU A 270                    
SITE     6 AC1 27 CO3 A 313   MG A1313   MG A1314  HOH A2254                    
SITE     7 AC1 27 HOH A2256  HOH A2326  HOH A2404                               
SITE     1 AC2 13 GLY A 149  SER A 150  LYS A 215  ARG A 255                    
SITE     2 AC2 13 ASP A 257  GLU A 270  ASN A 272  ADP A 310                    
SITE     3 AC2 13 DAL A 311  DAL A 312   MG A1313   MG A1314                    
SITE     4 AC2 13 HOH A2326                                                     
SITE     1 AC3  6 GLU A 270  ASN A 272  ADP A 310  CO3 A 313                    
SITE     2 AC3  6  MG A1314  HOH A2254                                          
SITE     1 AC4  6 ASP A 257  GLU A 270  ADP A 310  CO3 A 313                    
SITE     2 AC4  6  MG A1313  HOH A2326                                          
SITE     1 AC5  7 GLU A  17  VAL A  18  TYR A 212  LEU A 217                    
SITE     2 AC5  7 ARG A 288  HOH A2051  HOH A2388                               
SITE     1 AC6  8 PRO A  39  ASP A  41  GLN A 164  ASP A 165                    
SITE     2 AC6  8 ARG A 168  HOH A2081  HOH A2276  HOH A2405                    
SITE     1 AC7  6 LYS A 215  TYR A 216  HIS A 280  HOH A2281                    
SITE     2 AC7  6 HOH A2324  HOH A2374                                          
SITE     1 AC8 26 LYS B  97  ILE B 142  LYS B 144  GLU B 148                    
SITE     2 AC8 26 GLY B 149  SER B 150  SER B 151  MET B 154                    
SITE     3 AC8 26 GLU B 180  LYS B 181  TRP B 182  LEU B 183                    
SITE     4 AC8 26 GLU B 187  PHE B 209  TYR B 210  LYS B 215                    
SITE     5 AC8 26 ASP B 257  MET B 259  GLU B 270  CO3 B 313                    
SITE     6 AC8 26  MG B1307   MG B1308  HOH B2198  HOH B2200                    
SITE     7 AC8 26 HOH B2278  HOH B2356                                          
SITE     1 AC9 12 SER B 150  LYS B 215  ARG B 255  ASP B 257                    
SITE     2 AC9 12 GLU B 270  ASN B 272  ADP B 310  DAL B 311                    
SITE     3 AC9 12 DAL B 312   MG B1307   MG B1308  HOH B2278                    
SITE     1 BC1  6 GLU B 270  ASN B 272  ADP B 310  CO3 B 313                    
SITE     2 BC1  6  MG B1308  HOH B2198                                          
SITE     1 BC2  6 ASP B 257  GLU B 270  ADP B 310  CO3 B 313                    
SITE     2 BC2  6  MG B1307  HOH B2278                                          
SITE     1 BC3  6 HOH B2224  HOH B2225  HOH B2358  HOH B2359                    
SITE     2 BC3  6 HOH B2360  HOH B2361                                          
SITE     1 BC4  6 HIS B 280  HOH B2281  HOH B2285  HOH B2334                    
SITE     2 BC4  6 HOH B2336  HOH B2357                                          
SITE     1 BC5 11 GLU A  15  HIS A  63  SER A 150  TYR A 216                    
SITE     2 BC5 11 ARG A 255  GLY A 276  SER A 281  LEU A 282                    
SITE     3 BC5 11 CO3 A 313  HOH A2149  HOH A2366                               
SITE     1 BC6 11 GLU B  15  HIS B  63  SER B 150  TYR B 216                    
SITE     2 BC6 11 ARG B 255  GLY B 276  SER B 281  LEU B 282                    
SITE     3 BC6 11 CO3 B 313  HOH B2108  HOH B2319                               
CRYST1   53.000   97.620  109.490  90.00  90.00  90.00 P 21 21 21    8          
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      0.018868  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010244  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009133        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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