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Database: PDB
Entry: 4C5C
LinkDB: 4C5C
Original site: 4C5C 
HEADER    LIGASE                                  10-SEP-13   4C5C              
TITLE     THE X-RAY CRYSTAL STRUCTURE OF D-ALANYL-D-ALANINE LIGASE IN COMPLEX   
TITLE    2 WITH ADP 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: 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 4C5C    1       JRNL                                     
REVDAT   1   21-JAN-15 4C5C    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.    1.40 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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 101827                         
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4300                            
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) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7180                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.54                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 273                          
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
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          : 103                                     
REMARK   3   SOLVENT ATOMS            : 652                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.88000                                             
REMARK   3    B22 (A**2) : -0.47000                                             
REMARK   3    B33 (A**2) : 1.35000                                              
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): 0.067         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.067         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.041         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.053         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4788 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6494 ; 1.662 ; 2.005       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   612 ; 5.722 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   182 ;35.785 ;24.945       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   814 ;12.411 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    22 ;17.907 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   738 ; 0.096 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3522 ; 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):  3044 ; 0.886 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4844 ; 1.602 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1744 ; 2.941 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1650 ; 4.394 ; 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):   4.6430  39.8400  50.2270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0260 T22:   0.0459                                     
REMARK   3      T33:   0.0210 T12:   0.0071                                     
REMARK   3      T13:  -0.0034 T23:   0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5999 L22:   0.5870                                     
REMARK   3      L33:   0.9195 L12:   0.1360                                     
REMARK   3      L13:   0.0109 L23:   0.2178                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0151 S12:   0.1306 S13:   0.0483                       
REMARK   3      S21:  -0.0762 S22:  -0.0005 S23:   0.0400                       
REMARK   3      S31:  -0.0748 S32:  -0.0445 S33:   0.0156                       
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):  22.0170  31.2900  71.5560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0496 T22:   0.0680                                     
REMARK   3      T33:   0.0408 T12:  -0.0021                                     
REMARK   3      T13:  -0.0017 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9777 L22:   0.2596                                     
REMARK   3      L33:   1.1900 L12:   0.0584                                     
REMARK   3      L13:   0.4645 L23:   0.1494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0480 S12:  -0.1705 S13:  -0.0700                       
REMARK   3      S21:   0.0606 S22:   0.0157 S23:  -0.0296                       
REMARK   3      S31:   0.0279 S32:   0.1100 S33:  -0.0637                       
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):  -2.9540  32.7190  65.9720              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0166 T22:   0.0353                                     
REMARK   3      T33:   0.0299 T12:  -0.0050                                     
REMARK   3      T13:   0.0149 T23:  -0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6931 L22:   0.4501                                     
REMARK   3      L33:   0.6235 L12:   0.1458                                     
REMARK   3      L13:  -0.0425 L23:  -0.0345                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0062 S12:  -0.0258 S13:  -0.0335                       
REMARK   3      S21:   0.0415 S22:  -0.0224 S23:   0.0842                       
REMARK   3      S31:  -0.0112 S32:  -0.0642 S33:   0.0162                       
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):  19.0940  58.1500  50.3880              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0399 T22:   0.0417                                     
REMARK   3      T33:   0.0387 T12:  -0.0032                                     
REMARK   3      T13:   0.0037 T23:  -0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7372 L22:   0.9028                                     
REMARK   3      L33:   0.4625 L12:   0.3340                                     
REMARK   3      L13:  -0.0418 L23:  -0.0180                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0607 S12:   0.1461 S13:  -0.0454                       
REMARK   3      S21:  -0.1412 S22:   0.0629 S23:  -0.1098                       
REMARK   3      S31:   0.0527 S32:   0.0053 S33:  -0.0021                       
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):   1.4350  66.5920  71.2400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0521 T22:   0.0723                                     
REMARK   3      T33:   0.0526 T12:  -0.0042                                     
REMARK   3      T13:  -0.0067 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8066 L22:   0.5378                                     
REMARK   3      L33:   1.8651 L12:  -0.0531                                     
REMARK   3      L13:  -0.4272 L23:  -0.0641                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0514 S12:  -0.1528 S13:   0.0264                       
REMARK   3      S21:   0.0751 S22:   0.0103 S23:   0.0309                       
REMARK   3      S31:  -0.0056 S32:  -0.1894 S33:  -0.0617                       
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):  26.3670  65.1730  66.2430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0205 T22:   0.0185                                     
REMARK   3      T33:   0.0616 T12:  -0.0055                                     
REMARK   3      T13:  -0.0288 T23:  -0.0052                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9422 L22:   0.6191                                     
REMARK   3      L33:   0.6932 L12:   0.2795                                     
REMARK   3      L13:   0.0778 L23:   0.0567                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0294 S12:  -0.0379 S13:   0.0378                       
REMARK   3      S21:   0.0718 S22:  -0.0078 S23:  -0.1398                       
REMARK   3      S31:   0.0093 S32:   0.0451 S33:  -0.0215                       
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 4C5C 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_1290058249.                                   
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        : NULL                               
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   : 106127                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
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     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.6                               
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       25.61500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.06000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       48.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.06000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.61500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       48.90000            
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: 4700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23940 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -79.1 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 A  2236     O    HOH A  2237              1.97            
REMARK 500   O    HOH A  2057     O    HOH A  2158              2.04            
REMARK 500   O    HOH A  2057     O    HOH A  2157              2.09            
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   O    HOH A  2011     O    HOH A  2133     4556     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  99   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
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 A2001        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH A2107        DISTANCE =  6.18 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 A1314  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 310   O1A                                                    
REMARK 620 2 ATP A 310   O3B  89.3                                              
REMARK 620 3 ATP A 310   PG  131.1  42.4                                        
REMARK 620 4 ATP A 310   O2G 163.0  73.7  32.1                                  
REMARK 620 5 ASP A 257   OD2 104.6 165.9 123.6  92.4                            
REMARK 620 6 HOH A2272   O    91.8  91.4  95.6  88.8  90.7                      
REMARK 620 7 GLU A 270   OE2  91.9  89.1  82.4  87.8  87.9 176.3                
REMARK 620 N                    1     2     3     4     5     6                 
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 ATP A 310   O1B                                                    
REMARK 620 2 ATP A 310   O3G  95.8                                              
REMARK 620 3 ASN A 272   OD1 173.2  91.0                                        
REMARK 620 4 HOH A2194   O    91.8 101.3  86.8                                  
REMARK 620 5 GLU A 270   OE1  87.1 163.2  86.3  95.1                            
REMARK 620 6 GLU A 270   OE2  87.7 102.5  90.9 156.1  61.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1315  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 280   NE2                                                    
REMARK 620 2 HOH A2278   O    95.4                                              
REMARK 620 3 HOH A2322   O    91.6 172.8                                        
REMARK 620 4 HOH A2323   O    89.8  88.6  90.0                                  
REMARK 620 5 HOH A2343   O   172.5  91.8  81.1  88.5                            
REMARK 620 6 HOH A2273   O    97.3  90.6  89.9 172.9  84.5                      
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 ATP B 310   O1A                                                    
REMARK 620 2 ATP B 310   O3B  90.5                                              
REMARK 620 3 ATP B 310   PG  133.5  43.3                                        
REMARK 620 4 ATP B 310   O2G 165.1  74.7  32.3                                  
REMARK 620 5 ASP B 257   OD2 102.9 166.5 123.2  91.9                            
REMARK 620 6 HOH B2236   O    90.6  90.7  94.8  87.2  89.8                      
REMARK 620 7 GLU B 270   OE2  93.5  91.7  84.1  89.4  86.9 175.2                
REMARK 620 N                    1     2     3     4     5     6                 
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 ATP B 310   O1B                                                    
REMARK 620 2 ATP B 310   O3G  96.4                                              
REMARK 620 3 HOH B2165   O    93.6 101.8                                        
REMARK 620 4 GLU B 270   OE2  86.5 102.9 155.0                                  
REMARK 620 5 ASN B 272   OD1 173.0  90.5  86.3  90.6                            
REMARK 620 6 GLU B 270   OE1  86.8 163.2  94.4  60.7  86.3                      
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 HIS B 280   NE2                                                    
REMARK 620 2 HOH B2241   O    89.6                                              
REMARK 620 3 HOH B2286   O    92.2  94.8                                        
REMARK 620 4 HOH B2240   O    99.0  85.4 168.7                                  
REMARK 620 5 HOH B2306   O   173.1  96.7  84.7  84.1                            
REMARK 620 6 HOH B2238   O    94.1 175.4  87.7  91.4  79.6                      
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 B2308   O                                                      
REMARK 620 2 HOH B2187   O   176.1                                              
REMARK 620 3 HOH B2181   O    83.8  97.5                                        
REMARK 620 4 HOH B2182   O    89.6  94.3  77.7                                  
REMARK 620 5 HOH B2307   O    89.8  89.3 171.4  96.6                            
REMARK 620 6 HOH B2186   O    94.6  82.4  70.0 146.8 116.4                      
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 ATP A 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1313                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1314                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1307                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1308                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1310                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1315                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1309                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1316                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 1317                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
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: BC4                                                 
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: 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                                             
DBREF  4C5C A    1   306  UNP    C4ZRI7   C4ZRI7_ECOBW     1    306             
DBREF  4C5C B    1   306  UNP    C4ZRI7   C4ZRI7_ECOBW     1    306             
SEQADV 4C5C MET A  -23  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C SER A  -22  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C TYR A  -21  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C TYR A  -20  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS A  -19  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS A  -18  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS A  -17  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS A  -16  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS A  -15  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS A  -14  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C ASP A  -13  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C TYR A  -12  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C ILE A  -11  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C PRO A  -10  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C THR A   -9  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C THR A   -8  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C GLU A   -7  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C ASN A   -6  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C LEU A   -5  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C TYR A   -4  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C PHE A   -3  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C ASN A   -2  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C GLY A   -1  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C ALA A    0  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C MET B  -23  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C SER B  -22  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C TYR B  -21  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C TYR B  -20  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS B  -19  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS B  -18  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS B  -17  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS B  -16  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS B  -15  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C HIS B  -14  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C ASP B  -13  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C TYR B  -12  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C ILE B  -11  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C PRO B  -10  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C THR B   -9  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C THR B   -8  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C GLU B   -7  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C ASN B   -6  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C LEU B   -5  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C TYR B   -4  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C PHE B   -3  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C ASN B   -2  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C GLY B   -1  UNP  C4ZRI7              EXPRESSION TAG                 
SEQADV 4C5C 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    ATP  A 310      31                                                       
HET    DAL  A 311       5                                                       
HET    DAL  A 312       6                                                       
HET     MG  A1313       1                                                       
HET     MG  A1314       1                                                       
HET     MG  A1315       1                                                       
HET    GOL  A1316       6                                                       
HET    GOL  A1317       6                                                       
HET    ATP  B 310      31                                                       
HET    DAL  B 311       5                                                       
HET    DAL  B 312       6                                                       
HET     MG  B1307       1                                                       
HET     MG  B1308       1                                                       
HET     MG  B1309       1                                                       
HET     MG  B1310       1                                                       
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     DAL D-ALANINE                                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   4  DAL    4(C3 H7 N O2)                                                
FORMUL   6   MG    7(MG 2+)                                                     
FORMUL   9  GOL    2(C3 H8 O3)                                                  
FORMUL  18  HOH   *652(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 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  LEU B  137  1                                  11    
HELIX   21  21 ALA B  159  GLN B  172  1                                  14    
HELIX   22  22 ASP B  211  LEU B  217  1                                   7    
HELIX   23  23 GLU B  230  GLY B  249  1                                  20    
HELIX   24  24 SER B  281  ALA B  290  1                                  10    
HELIX   25  25 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 ATP A 310                MG    MG A1314     1555   1555  1.97  
LINK         O1B ATP A 310                MG    MG A1313     1555   1555  2.02  
LINK         O3B ATP A 310                MG    MG A1314     1555   1555  2.19  
LINK         PG  ATP A 310                MG    MG A1314     1555   1555  2.71  
LINK         O2G ATP A 310                MG    MG A1314     1555   1555  2.03  
LINK         O3G ATP A 310                MG    MG A1313     1555   1555  1.96  
LINK         C   DAL A 311                 N   DAL A 312     1555   1555  1.34  
LINK        MG    MG A1313                 OD1 ASN A 272     1555   1555  2.16  
LINK        MG    MG A1313                 O   HOH A2194     1555   1555  2.10  
LINK        MG    MG A1313                 OE1 GLU A 270     1555   1555  2.20  
LINK        MG    MG A1313                 OE2 GLU A 270     1555   1555  2.13  
LINK        MG    MG A1314                 OD2 ASP A 257     1555   1555  2.05  
LINK        MG    MG A1314                 O   HOH A2272     1555   1555  2.10  
LINK        MG    MG A1314                 OE2 GLU A 270     1555   1555  2.13  
LINK        MG    MG A1315                 NE2 HIS A 280     1555   1555  2.17  
LINK        MG    MG A1315                 O   HOH A2278     1555   1555  2.27  
LINK        MG    MG A1315                 O   HOH A2322     1555   1555  1.95  
LINK        MG    MG A1315                 O   HOH A2323     1555   1555  2.02  
LINK        MG    MG A1315                 O   HOH A2343     1555   1555  2.21  
LINK        MG    MG A1315                 O   HOH A2273     1555   1555  1.92  
LINK         O1A ATP B 310                MG    MG B1308     1555   1555  1.93  
LINK         O1B ATP B 310                MG    MG B1307     1555   1555  2.02  
LINK         O3B ATP B 310                MG    MG B1308     1555   1555  2.11  
LINK         PG  ATP B 310                MG    MG B1308     1555   1555  2.69  
LINK         O2G ATP B 310                MG    MG B1308     1555   1555  2.13  
LINK         O3G ATP B 310                MG    MG B1307     1555   1555  1.95  
LINK         C   DAL B 311                 N   DAL B 312     1555   1555  1.33  
LINK        MG    MG B1307                 O   HOH B2165     1555   1555  2.09  
LINK        MG    MG B1307                 OE2 GLU B 270     1555   1555  2.19  
LINK        MG    MG B1307                 OD1 ASN B 272     1555   1555  2.16  
LINK        MG    MG B1307                 OE1 GLU B 270     1555   1555  2.23  
LINK        MG    MG B1308                 OD2 ASP B 257     1555   1555  2.11  
LINK        MG    MG B1308                 O   HOH B2236     1555   1555  2.12  
LINK        MG    MG B1308                 OE2 GLU B 270     1555   1555  2.08  
LINK        MG    MG B1309                 NE2 HIS B 280     1555   1555  2.15  
LINK        MG    MG B1309                 O   HOH B2241     1555   1555  1.83  
LINK        MG    MG B1309                 O   HOH B2286     1555   1555  1.95  
LINK        MG    MG B1309                 O   HOH B2240     1555   1555  2.25  
LINK        MG    MG B1309                 O   HOH B2306     1555   1555  2.31  
LINK        MG    MG B1309                 O   HOH B2238     1555   1555  1.99  
LINK        MG    MG B1310                 O   HOH B2308     1555   1555  1.96  
LINK        MG    MG B1310                 O   HOH B2187     1555   1555  2.30  
LINK        MG    MG B1310                 O   HOH B2181     1555   1555  2.47  
LINK        MG    MG B1310                 O   HOH B2182     1555   1555  2.07  
LINK        MG    MG B1310                 O   HOH B2307     1555   1555  2.00  
LINK        MG    MG B1310                 O   HOH B2186     1555   1555  2.56  
CISPEP   1 LEU A  139    PRO A  140          0        -2.37                     
CISPEP   2 GLY A  185    PRO A  186          0         5.40                     
CISPEP   3 CYS A  225    PRO A  226          0        -0.59                     
CISPEP   4 LEU B  139    PRO B  140          0         2.73                     
CISPEP   5 GLY B  185    PRO B  186          0         4.31                     
CISPEP   6 CYS B  225    PRO B  226          0        -2.61                     
SITE     1 AC1 30 LYS A  97  ILE A 142  LYS A 144  GLU A 148                    
SITE     2 AC1 30 GLY A 149  SER A 150  SER A 151  MET A 154                    
SITE     3 AC1 30 GLU A 180  LYS A 181  TRP A 182  LEU A 183                    
SITE     4 AC1 30 GLU A 187  PHE A 209  TYR A 210  LYS A 215                    
SITE     5 AC1 30 ARG A 255  ASP A 257  MET A 259  LEU A 269                    
SITE     6 AC1 30 GLU A 270  ASN A 272  DAL A 311  DAL A 312                    
SITE     7 AC1 30  MG A1313   MG A1314  HOH A2194  HOH A2197                    
SITE     8 AC1 30 HOH A2263  HOH A2272                                          
SITE     1 AC2  5 GLU A 270  ASN A 272  ATP A 310   MG A1314                    
SITE     2 AC2  5 HOH A2194                                                     
SITE     1 AC3  5 ASP A 257  GLU A 270  ATP A 310   MG A1313                    
SITE     2 AC3  5 HOH A2272                                                     
SITE     1 AC4 30 LYS B  97  ILE B 142  LYS B 144  GLU B 148                    
SITE     2 AC4 30 GLY B 149  SER B 150  SER B 151  MET B 154                    
SITE     3 AC4 30 GLU B 180  LYS B 181  TRP B 182  LEU B 183                    
SITE     4 AC4 30 GLU B 187  PHE B 209  TYR B 210  LYS B 215                    
SITE     5 AC4 30 ARG B 255  ASP B 257  MET B 259  LEU B 269                    
SITE     6 AC4 30 GLU B 270  ASN B 272  DAL B 311  DAL B 312                    
SITE     7 AC4 30  MG B1307   MG B1308  HOH B2165  HOH B2166                    
SITE     8 AC4 30 HOH B2225  HOH B2236                                          
SITE     1 AC5  5 GLU B 270  ASN B 272  ATP B 310   MG B1308                    
SITE     2 AC5  5 HOH B2165                                                     
SITE     1 AC6  5 ASP B 257  GLU B 270  ATP B 310   MG B1307                    
SITE     2 AC6  5 HOH B2236                                                     
SITE     1 AC7  6 HOH B2181  HOH B2182  HOH B2186  HOH B2187                    
SITE     2 AC7  6 HOH B2307  HOH B2308                                          
SITE     1 AC8  6 HIS A 280  HOH A2273  HOH A2278  HOH A2322                    
SITE     2 AC8  6 HOH A2323  HOH A2343                                          
SITE     1 AC9  6 HIS B 280  HOH B2238  HOH B2240  HOH B2241                    
SITE     2 AC9  6 HOH B2286  HOH B2306                                          
SITE     1 BC1  6 ASN A  21  TYR A 212  ARG A 288  HOH A2274                    
SITE     2 BC1  6 HOH A2327  HOH A2344                                          
SITE     1 BC2  8 LEU A  20  PRO A  39  ASP A  41  ASP A 165                    
SITE     2 BC2  8 ARG A 168  HOH A2046  HOH A2213  HOH A2218                    
SITE     1 BC3 11 GLU A  15  HIS A  63  SER A 150  TYR A 216                    
SITE     2 BC3 11 ARG A 255  GLY A 276  SER A 281  LEU A 282                    
SITE     3 BC3 11 ATP A 310  HOH A2095  HOH A2308                               
SITE     1 BC4 12 GLU B  15  HIS B  63  SER B 150  TYR B 216                    
SITE     2 BC4 12 ARG B 255  GLY B 276  SER B 281  LEU B 282                    
SITE     3 BC4 12 ATP B 310  HOH B2018  HOH B2081  HOH B2274                    
CRYST1   51.230   97.800  110.120  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      0.019520  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010225  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009081        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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