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Database: PDB
Entry: 4C5A
LinkDB: 4C5A
Original site: 4C5A 
HEADER    LIGASE                                  10-SEP-13   4C5A              
TITLE     THE X-RAY CRYSTAL STRUCTURES OF D-ALANYL-D-ALANINE LIGASE IN COMPLEX  
TITLE    2 ADP AND D-CYCLOSERINE PHOSPHATE                                      
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;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PEPTIDE;                                                   
COMPND  10 CHAIN: C;                                                            
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI K-12;                          
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_VARIANT: ROSETTA;                                  
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: PET;                                       
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPROEX;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES                                                       
KEYWDS    LIGASE, DDLB, ANTIBIOTIC                                              
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 4C5A    1       SOURCE JRNL                              
REVDAT   1   21-JAN-15 4C5A    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.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.76                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 67309                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2861                            
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4861                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.60                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 210                          
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4661                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 92                                      
REMARK   3   SOLVENT ATOMS            : 347                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.09000                                             
REMARK   3    B22 (A**2) : -0.49000                                             
REMARK   3    B33 (A**2) : 0.58000                                              
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): 0.113         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.109         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.066         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.887         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4835 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6558 ; 1.603 ; 2.006       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   616 ; 5.778 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   187 ;35.264 ;24.973       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   819 ;15.021 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;22.193 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   741 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3565 ; 0.007 ; 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):  3053 ; 0.858 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4861 ; 1.594 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1782 ; 2.555 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1697 ; 3.959 ; 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   112                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4296  39.5985  50.7772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1538 T22:   0.1464                                     
REMARK   3      T33:   0.1683 T12:  -0.0025                                     
REMARK   3      T13:  -0.0017 T23:   0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2915 L22:   0.2457                                     
REMARK   3      L33:   0.4612 L12:   0.0924                                     
REMARK   3      L13:   0.1491 L23:   0.0878                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0389 S12:   0.0327 S13:   0.0429                       
REMARK   3      S21:  -0.0409 S22:   0.0196 S23:   0.0000                       
REMARK   3      S31:  -0.0468 S32:   0.0285 S33:   0.0192                       
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   181                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.8582  31.1969  70.5640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1530 T22:   0.1604                                     
REMARK   3      T33:   0.1671 T12:   0.0172                                     
REMARK   3      T13:  -0.0153 T23:  -0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4654 L22:   0.5321                                     
REMARK   3      L33:   0.5621 L12:  -0.1450                                     
REMARK   3      L13:  -0.0036 L23:   0.1591                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0071 S12:  -0.0539 S13:   0.0343                       
REMARK   3      S21:   0.0399 S22:   0.0638 S23:  -0.0806                       
REMARK   3      S31:   0.0327 S32:   0.0272 S33:  -0.0566                       
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   182        A   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):   0.0152  32.2676  66.5092              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1436 T22:   0.1643                                     
REMARK   3      T33:   0.1601 T12:  -0.0005                                     
REMARK   3      T13:   0.0180 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5479 L22:   0.3021                                     
REMARK   3      L33:   0.3783 L12:   0.0585                                     
REMARK   3      L13:   0.1704 L23:   0.0577                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0188 S12:  -0.0839 S13:  -0.0171                       
REMARK   3      S21:   0.0293 S22:  -0.0207 S23:   0.0468                       
REMARK   3      S31:   0.0052 S32:  -0.0725 S33:   0.0395                       
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     3        B   138                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9131  58.6188  55.6283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1757 T22:   0.1401                                     
REMARK   3      T33:   0.1564 T12:  -0.0255                                     
REMARK   3      T13:  -0.0082 T23:  -0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3207 L22:   0.2755                                     
REMARK   3      L33:   1.0456 L12:   0.2343                                     
REMARK   3      L13:   0.1014 L23:   0.0968                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0420 S12:   0.0309 S13:  -0.0053                       
REMARK   3      S21:  -0.0373 S22:   0.0319 S23:   0.0048                       
REMARK   3      S31:  -0.1328 S32:   0.0045 S33:   0.0101                       
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   139        B   276                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.1305  66.4283  68.7717              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2175 T22:   0.1034                                     
REMARK   3      T33:   0.1635 T12:  -0.0464                                     
REMARK   3      T13:  -0.0331 T23:  -0.0123                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8025 L22:   0.2526                                     
REMARK   3      L33:   0.6307 L12:  -0.0884                                     
REMARK   3      L13:   0.0244 L23:   0.0498                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0144 S12:   0.0416 S13:   0.1026                       
REMARK   3      S21:   0.0335 S22:  -0.0177 S23:  -0.0566                       
REMARK   3      S31:  -0.2221 S32:   0.0628 S33:   0.0321                       
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   277        B   306                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7157  63.1997  54.1035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1620 T22:   0.5793                                     
REMARK   3      T33:   0.1407 T12:   0.0272                                     
REMARK   3      T13:  -0.0616 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9079 L22:  10.5405                                     
REMARK   3      L33:  12.2793 L12:  -0.3617                                     
REMARK   3      L13:   1.8745 L23:   4.0612                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0649 S12:   1.1883 S13:   0.0532                       
REMARK   3      S21:  -0.4439 S22:  -0.5260 S23:  -0.9112                       
REMARK   3      S31:  -1.5905 S32:  -0.4858 S33:   0.5909                       
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 4C5A 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_1290058248.                                   
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   : 70170                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.100                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66000                            
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       26.89500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       54.99500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.75500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       54.99500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       26.89500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.75500            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5770 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -75.2 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
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   N    MET A     1     C    ALA C     8              1.34            
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    ASP B  46      108.10    -59.53                                   
REMARK 500    THR B 278     -106.35    -69.33                                   
REMARK 500    SER B 279      -36.45   -156.69                                   
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 A2010        DISTANCE =  6.05 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 A 331  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 310   O1A                                                    
REMARK 620 2 ADP A 310   O2B  84.7                                              
REMARK 620 3 DS0 A 311   O9  168.6  84.5                                        
REMARK 620 4 GLU A 270   OE2  95.5  90.6  88.2                                  
REMARK 620 5 ASP A 257   OD2 102.2 173.1  88.7  88.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 330  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 310   O1B                                                    
REMARK 620 2 DS0 A 311   O10  98.3                                              
REMARK 620 3 GLU A 270   OE2  87.5 105.0                                        
REMARK 620 4 ASN A 272   OD1 170.5  91.2  89.0                                  
REMARK 620 5 HOH A2135   O    91.8 102.0 152.9  87.3                            
REMARK 620 6 GLU A 270   OE1  86.5 164.7  60.5  84.1  92.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 331  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 310   O1A                                                    
REMARK 620 2 ADP B 310   O1B  84.1                                              
REMARK 620 3 DS0 B 311   O9  166.7  82.6                                        
REMARK 620 4 ASP B 257   OD2 105.9 166.8  87.1                                  
REMARK 620 5 HOH B2077   O    94.1  92.9  87.5  94.9                            
REMARK 620 6 GLU B 270   OE2  92.9  82.3  84.3  88.6 171.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 330  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP B 310   O3B                                                    
REMARK 620 2 DS0 B 311   O10  98.2                                              
REMARK 620 3 ASN B 272   OD1 172.9  89.0                                        
REMARK 620 4 GLU B 270   OE2  89.7 103.8  88.3                                  
REMARK 620 5 GLU B 270   OE1  88.1 162.6  85.0  59.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DS0 A 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 330                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 331                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DS0 B 311                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 330                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 331                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1307                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1308                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4C5B   RELATED DB: PDB                                   
REMARK 900 THE X-RAY CRYSTAL STRUCTURE OF D-ALANYL-D-ALANINE LIGASE IN COMPLEX  
REMARK 900 WITH ATP AND D-ALA-D-ALA                                             
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  4C5A A    1   306  UNP    C4ZRI7   C4ZRI7_ECOBW     1    306             
DBREF  4C5A B    1   306  UNP    C4ZRI7   C4ZRI7_ECOBW     1    306             
DBREF  4C5A C    1     8  PDB    4C5A     4C5A             1      8             
SEQADV 4C5A MET A  -23  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A SER A  -22  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A TYR A  -21  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A TYR A  -20  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS A  -19  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS A  -18  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS A  -17  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS A  -16  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS A  -15  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS A  -14  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A ASP A  -13  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A TYR A  -12  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A ILE A  -11  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A PRO A  -10  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A THR A   -9  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A THR A   -8  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A GLU A   -7  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A ASN A   -6  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A LEU A   -5  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A TYR A   -4  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A PHE A   -3  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A ASN A   -2  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A GLY A   -1  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A ALA A    0  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A MET B  -23  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A SER B  -22  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A TYR B  -21  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A TYR B  -20  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS B  -19  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS B  -18  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS B  -17  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS B  -16  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS B  -15  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A HIS B  -14  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A ASP B  -13  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A TYR B  -12  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A ILE B  -11  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A PRO B  -10  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A THR B   -9  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A THR B   -8  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A GLU B   -7  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A ASN B   -6  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A LEU B   -5  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A TYR B   -4  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A PHE B   -3  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A ASN B   -2  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A GLY B   -1  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5A 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                                          
SEQRES   1 C    8  GLU ASN LEU TYR PHE GLN GLY ALA                              
HET    ADP  A 310      27                                                       
HET    DS0  A 311      11                                                       
HET     MG  A 330       1                                                       
HET     MG  A 331       1                                                       
HET    GOL  A1307       6                                                       
HET    GOL  A1308       6                                                       
HET    ADP  B 310      27                                                       
HET    DS0  B 311      11                                                       
HET     MG  B 330       1                                                       
HET     MG  B 331       1                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     DS0 [(4R)-4-AZANYL-4,5-DIHYDRO-1,2-OXAZOL-3-YL] DIHYDROGEN           
HETNAM   2 DS0  PHOSPHATE                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   4  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   5  DS0    2(C3 H7 N2 O5 P)                                             
FORMUL   6   MG    4(MG 2+)                                                     
FORMUL   8  GOL    2(C3 H8 O3)                                                  
FORMUL  14  HOH   *347(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  GLY A  125  1                                   7    
HELIX    7   7 SER A  127  LEU A  137  1                                  11    
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 LEU B   50  GLY B   54  5                                   5    
HELIX   17  17 GLY B   70  GLY B   80  1                                  11    
HELIX   18  18 GLY B   87  ASP B   96  1                                  10    
HELIX   19  19 ASP B   96  ALA B  107  1                                  12    
HELIX   20  20 ARG B  119  GLY B  125  1                                   7    
HELIX   21  21 SER B  127  ALA B  136  1                                  10    
HELIX   22  22 ALA B  159  ASN B  161  5                                   3    
HELIX   23  23 ALA B  162  PHE B  171  1                                  10    
HELIX   24  24 ASP B  211  LEU B  217  1                                   7    
HELIX   25  25 GLU B  230  GLY B  249  1                                  20    
HELIX   26  26 SER B  281  ALA B  290  1                                  10    
HELIX   27  27 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         O1A ADP A 310                MG    MG A 331     1555   1555  2.01  
LINK         O1B ADP A 310                MG    MG A 330     1555   1555  2.02  
LINK         O2B ADP A 310                MG    MG A 331     1555   1555  2.14  
LINK         O9  DS0 A 311                MG    MG A 331     1555   1555  2.03  
LINK         O10 DS0 A 311                MG    MG A 330     1555   1555  1.97  
LINK        MG    MG A 330                 OE2 GLU A 270     1555   1555  2.14  
LINK        MG    MG A 330                 OD1 ASN A 272     1555   1555  2.18  
LINK        MG    MG A 330                 O   HOH A2135     1555   1555  2.10  
LINK        MG    MG A 330                 OE1 GLU A 270     1555   1555  2.26  
LINK        MG    MG A 331                 OE2 GLU A 270     1555   1555  2.10  
LINK        MG    MG A 331                 OD2 ASP A 257     1555   1555  2.02  
LINK         O1A ADP B 310                MG    MG B 331     1555   1555  1.90  
LINK         O3B ADP B 310                MG    MG B 330     1555   1555  2.10  
LINK         O1B ADP B 310                MG    MG B 331     1555   1555  2.20  
LINK         O10 DS0 B 311                MG    MG B 330     1555   1555  1.96  
LINK         O9  DS0 B 311                MG    MG B 331     1555   1555  2.16  
LINK        MG    MG B 330                 OD1 ASN B 272     1555   1555  2.27  
LINK        MG    MG B 330                 OE2 GLU B 270     1555   1555  2.11  
LINK        MG    MG B 330                 OE1 GLU B 270     1555   1555  2.21  
LINK        MG    MG B 331                 OD2 ASP B 257     1555   1555  1.98  
LINK        MG    MG B 331                 O   HOH B2077     1555   1555  2.12  
LINK        MG    MG B 331                 OE2 GLU B 270     1555   1555  2.12  
CISPEP   1 LEU A  139    PRO A  140          0         1.81                     
CISPEP   2 GLY A  185    PRO A  186          0         8.12                     
CISPEP   3 CYS A  225    PRO A  226          0         8.56                     
CISPEP   4 LEU B  139    PRO B  140          0         1.33                     
CISPEP   5 GLY B  185    PRO B  186          0         7.63                     
CISPEP   6 CYS B  225    PRO B  226          0        -0.02                     
SITE     1 AC1 26 LYS A  97  ILE A 142  LYS A 144  GLU A 148                    
SITE     2 AC1 26 GLY A 149  SER A 150  SER A 151  MET A 154                    
SITE     3 AC1 26 GLU A 180  LYS A 181  TRP A 182  LEU A 183                    
SITE     4 AC1 26 GLU A 187  PHE A 209  TYR A 210  LYS A 215                    
SITE     5 AC1 26 ASP A 257  MET A 259  LEU A 269  GLU A 270                    
SITE     6 AC1 26 DS0 A 311   MG A 330   MG A 331  HOH A2135                    
SITE     7 AC1 26 HOH A2137  HOH A2238                                          
SITE     1 AC2 17 GLU A  15  GLY A 149  SER A 150  LYS A 215                    
SITE     2 AC2 17 TYR A 216  ARG A 255  ASP A 257  GLU A 270                    
SITE     3 AC2 17 ASN A 272  PRO A 275  GLY A 276  ADP A 310                    
SITE     4 AC2 17  MG A 330   MG A 331  HOH A2028  HOH A2080                    
SITE     5 AC2 17 HOH A2190                                                     
SITE     1 AC3  6 GLU A 270  ASN A 272  ADP A 310  DS0 A 311                    
SITE     2 AC3  6  MG A 331  HOH A2135                                          
SITE     1 AC4  5 ASP A 257  GLU A 270  ADP A 310  DS0 A 311                    
SITE     2 AC4  5  MG A 330                                                     
SITE     1 AC5 25 LYS B  97  ILE B 142  LYS B 144  GLU B 148                    
SITE     2 AC5 25 GLY B 149  SER B 150  SER B 151  MET B 154                    
SITE     3 AC5 25 GLU B 180  LYS B 181  TRP B 182  LEU B 183                    
SITE     4 AC5 25 GLU B 187  PHE B 209  TYR B 210  LYS B 215                    
SITE     5 AC5 25 ASP B 257  MET B 259  GLU B 270  DS0 B 311                    
SITE     6 AC5 25  MG B 330   MG B 331  HOH B2059  HOH B2077                    
SITE     7 AC5 25 HOH B2101                                                     
SITE     1 AC6 19 GLU B  15  HIS B  63  GLY B 149  SER B 150                    
SITE     2 AC6 19 LYS B 215  TYR B 216  ARG B 255  ASP B 257                    
SITE     3 AC6 19 GLU B 270  ASN B 272  PRO B 275  GLY B 276                    
SITE     4 AC6 19 ADP B 310   MG B 330   MG B 331  HOH B2006                    
SITE     5 AC6 19 HOH B2020  HOH B2077  HOH B2078                               
SITE     1 AC7  5 GLU B 270  ASN B 272  ADP B 310  DS0 B 311                    
SITE     2 AC7  5  MG B 331                                                     
SITE     1 AC8  6 ASP B 257  GLU B 270  ADP B 310  DS0 B 311                    
SITE     2 AC8  6  MG B 330  HOH B2077                                          
SITE     1 AC9  8 GLU A  17  VAL A  18  TYR A 212  LEU A 217                    
SITE     2 AC9  8 ARG A 288  HOH A2034  HOH A2035  HOH A2239                    
SITE     1 BC1  6 ASP A  41  GLU A  44  ASN A 161  GLN A 164                    
SITE     2 BC1  6 ASP A 165  ARG A 168                                          
CRYST1   53.790   97.510  109.990  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      0.018591  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010255  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009092        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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