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Database: PDB
Entry: 2I8C
LinkDB: 2I8C
Original site: 2I8C 
HEADER    LYASE                                   01-SEP-06   2I8C              
TITLE     ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS D-ALANINE:D-ALANINE    
TITLE    2 LIGASE REVEALED BY CRYSTALLOGRAPHIC STUDIES                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: D-ALANINE-D-ALANINE LIGASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: D-ALANYLALANINE SYNTHETASE, D-ALA-D-ALA LIGASE;             
COMPND   5 EC: 6.3.2.4;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;            
SOURCE   3 ORGANISM_TAXID: 93062;                                               
SOURCE   4 STRAIN: COL;                                                         
SOURCE   5 GENE: DDL;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: M15[PREP4];                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PQE-60                                    
KEYWDS    D-ALANINE:D-ALANINE LIGASE, ADP COMPLEX, STAPHYLOCOCCUS AUREUS, LYASE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LIU,J.S.CHANG,J.T.HERBERG,M.HORNG,P.K.TOMICH,A.H.LIN,K.R.MAROTTI    
REVDAT   4   13-JUL-11 2I8C    1       VERSN                                    
REVDAT   3   24-FEB-09 2I8C    1       VERSN                                    
REVDAT   2   24-OCT-06 2I8C    1       JRNL                                     
REVDAT   1   26-SEP-06 2I8C    0                                                
JRNL        AUTH   S.LIU,J.S.CHANG,J.T.HERBERG,M.M.HORNG,P.K.TOMICH,A.H.LIN,    
JRNL        AUTH 2 K.R.MAROTTI                                                  
JRNL        TITL   ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS               
JRNL        TITL 2 D-ALANINE:D-ALANINE LIGASE REVEALED BY CRYSTALLOGRAPHIC      
JRNL        TITL 3 STUDIES.                                                     
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 103 15178 2006              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   17015835                                                     
JRNL        DOI    10.1073/PNAS.0604905103                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0008                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23741                          
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) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1254                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.46                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.52                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1329                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.00                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 78                           
REMARK   3   BIN FREE R VALUE                    : 0.3440                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5496                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 65                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 40.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 45.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.43000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : -2.73000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.44000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 1.024         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.329         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.242         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.820        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.912                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5669 ; 0.018 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3775 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7684 ; 1.776 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9286 ; 0.981 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   688 ; 7.761 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   278 ;42.023 ;25.971       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1002 ;19.356 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;21.081 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   849 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6256 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1050 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1320 ; 0.232 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3834 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2701 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3081 ; 0.095 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   127 ; 0.152 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.091 ; 0.200       
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):    30 ; 0.189 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    49 ; 0.255 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.191 ; 0.200       
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):  4359 ; 1.049 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1395 ; 0.156 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5558 ; 1.262 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2551 ; 2.019 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2126 ; 3.000 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A   125                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.0618   0.1384  -5.1667              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1046 T22:  -0.1077                                     
REMARK   3      T33:  -0.0408 T12:   0.0077                                     
REMARK   3      T13:   0.0813 T23:   0.0285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7808 L22:   1.3270                                     
REMARK   3      L33:   5.7606 L12:   0.2724                                     
REMARK   3      L13:  -1.1879 L23:  -0.2377                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1226 S12:   0.2375 S13:  -0.2388                       
REMARK   3      S21:  -0.1696 S22:  -0.1002 S23:  -0.2294                       
REMARK   3      S31:   0.4059 S32:   0.1284 S33:   0.2229                       
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   126        A   219                          
REMARK   3    ORIGIN FOR THE GROUP (A):   9.8604 -17.0895  21.1107              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0534 T22:  -0.1045                                     
REMARK   3      T33:  -0.1024 T12:  -0.1061                                     
REMARK   3      T13:   0.0012 T23:  -0.0520                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5157 L22:   3.7927                                     
REMARK   3      L33:   3.0962 L12:  -0.7930                                     
REMARK   3      L13:   1.5560 L23:  -1.7869                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1224 S12:   0.0544 S13:  -0.2991                       
REMARK   3      S21:  -0.0020 S22:   0.1666 S23:   0.0634                       
REMARK   3      S31:   0.5358 S32:  -0.3884 S33:  -0.2890                       
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   220        A   358                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8683   1.6629   3.2677              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1865 T22:   0.0140                                     
REMARK   3      T33:  -0.0222 T12:   0.0280                                     
REMARK   3      T13:  -0.0032 T23:   0.0235                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4132 L22:   2.3930                                     
REMARK   3      L33:   2.3071 L12:   2.1474                                     
REMARK   3      L13:  -1.0320 L23:  -0.5962                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0038 S12:   0.3594 S13:   0.0502                       
REMARK   3      S21:  -0.0875 S22:   0.0048 S23:   0.1813                       
REMARK   3      S31:   0.0007 S32:  -0.4556 S33:  -0.0010                       
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   125                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.5439   2.6099  17.4732              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1370 T22:   0.0406                                     
REMARK   3      T33:   0.0098 T12:  -0.0793                                     
REMARK   3      T13:  -0.0128 T23:   0.1539                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4258 L22:   1.5517                                     
REMARK   3      L33:   5.1590 L12:  -0.1139                                     
REMARK   3      L13:   0.4286 L23:   1.0388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0993 S12:   0.5111 S13:   0.4058                       
REMARK   3      S21:  -0.1618 S22:  -0.1086 S23:  -0.1511                       
REMARK   3      S31:  -0.6578 S32:   0.8387 S33:   0.2079                       
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   126        B   219                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.9971  15.0435  26.7164              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0474 T22:  -0.1404                                     
REMARK   3      T33:  -0.0831 T12:   0.0417                                     
REMARK   3      T13:   0.0001 T23:  -0.0728                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5515 L22:   3.8327                                     
REMARK   3      L33:   4.2450 L12:  -1.4914                                     
REMARK   3      L13:   0.6239 L23:  -0.4549                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1479 S12:  -0.0320 S13:   0.1087                       
REMARK   3      S21:  -0.0112 S22:   0.1126 S23:   0.0325                       
REMARK   3      S31:  -0.4705 S32:  -0.3250 S33:   0.0353                       
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   220        B   360                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6281  -2.7546  33.3310              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0274 T22:  -0.1511                                     
REMARK   3      T33:  -0.0992 T12:   0.0132                                     
REMARK   3      T13:  -0.0255 T23:   0.0428                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4116 L22:   2.3253                                     
REMARK   3      L33:   3.5670 L12:  -0.8824                                     
REMARK   3      L13:  -0.5849 L23:   1.1119                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0024 S12:  -0.0219 S13:  -0.0648                       
REMARK   3      S21:   0.2654 S22:  -0.1238 S23:  -0.1483                       
REMARK   3      S31:  -0.0070 S32:   0.0930 S33:   0.1262                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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                                                           
REMARK   4                                                                      
REMARK   4 2I8C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-SEP-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039264.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-OCT-01                          
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               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23741                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.460                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 79.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : 0.07000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.62100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 2I87                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       33.48600            
REMARK 290   SMTRY3   2  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: 6570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 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     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     TYR A   246                                                      
REMARK 465     ASP A   247                                                      
REMARK 465     TYR A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     SER A   250                                                      
REMARK 465     LYS A   251                                                      
REMARK 465     TYR A   252                                                      
REMARK 465     LYS A   253                                                      
REMARK 465     ASP A   254                                                      
REMARK 465     GLY A   255                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     HIS A   359                                                      
REMARK 465     HIS A   360                                                      
REMARK 465     HIS A   361                                                      
REMARK 465     HIS A   362                                                      
REMARK 465     HIS A   363                                                      
REMARK 465     HIS A   364                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     TYR B   246                                                      
REMARK 465     ASP B   247                                                      
REMARK 465     TYR B   248                                                      
REMARK 465     LYS B   249                                                      
REMARK 465     SER B   250                                                      
REMARK 465     LYS B   251                                                      
REMARK 465     TYR B   252                                                      
REMARK 465     LYS B   253                                                      
REMARK 465     ASP B   254                                                      
REMARK 465     GLY B   255                                                      
REMARK 465     LYS B   256                                                      
REMARK 465     HIS B   361                                                      
REMARK 465     HIS B   362                                                      
REMARK 465     HIS B   363                                                      
REMARK 465     HIS B   364                                                      
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    GLU A  16        9.53    -65.96                                   
REMARK 500    ASN A  54       75.28     48.70                                   
REMARK 500    LEU A  67     -108.85     56.41                                   
REMARK 500    ASN A  69       47.99   -104.40                                   
REMARK 500    LEU A  94       65.13   -112.49                                   
REMARK 500    LEU A  95       74.82   -153.87                                   
REMARK 500    HIS A  96     -113.09     -3.03                                   
REMARK 500    PRO A  98     -147.59    -29.71                                   
REMARK 500    ASP A 113       31.33     73.20                                   
REMARK 500    SER A 184     -136.81   -150.51                                   
REMARK 500    ASN A 228      -88.95   -107.62                                   
REMARK 500    ASP A 299       39.64    -99.37                                   
REMARK 500    ASN A 305      -60.09    -93.87                                   
REMARK 500    ASN B  45       46.87    -77.58                                   
REMARK 500    ASP B  46        4.74   -151.65                                   
REMARK 500    ASN B  54       74.92     50.36                                   
REMARK 500    GLU B  58       55.39    -90.47                                   
REMARK 500    ILE B  59      106.82    -11.46                                   
REMARK 500    LEU B  73      171.10    -59.40                                   
REMARK 500    HIS B  96      -62.88    -19.14                                   
REMARK 500    ASN B  99      101.62     55.54                                   
REMARK 500    GLU B 101     -165.26     47.21                                   
REMARK 500    SER B 183       68.88    -65.00                                   
REMARK 500    VAL B 185     -159.57    -85.53                                   
REMARK 500    SER B 188      144.66   -173.14                                   
REMARK 500    ASN B 228      -88.60   -114.45                                   
REMARK 500    ASP B 264       78.46    -67.04                                   
REMARK 500    PHE B 313       22.21   -140.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER A  184     VAL A  185                 -148.02                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 306   OE2                                                    
REMARK 620 2 ADP B 400   O2A  70.6                                              
REMARK 620 3 ADP B 400   O2B 114.7  94.4                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP B 400                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2I80   RELATED DB: PDB                                   
REMARK 900 ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS D-ALANINE:D-          
REMARK 900 ALANINE LIGASE REVEALED BY CRYSTALLOGRAPHIC STUDIES                  
REMARK 900 RELATED ID: 2I87   RELATED DB: PDB                                   
REMARK 900 ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS D-ALANINE:D-          
REMARK 900 ALANINE LIGASE REVEALED BY CRYSTALLOGRAPHIC STUDIES                  
DBREF  2I8C A    1   356  UNP    Q5HEB7   DDL_STAAC        1    356             
DBREF  2I8C B    1   356  UNP    Q5HEB7   DDL_STAAC        1    356             
SEQADV 2I8C ARG A  357  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I8C SER A  358  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I8C HIS A  359  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C HIS A  360  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C HIS A  361  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C HIS A  362  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C HIS A  363  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C HIS A  364  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C ARG B  357  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I8C SER B  358  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I8C HIS B  359  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C HIS B  360  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C HIS B  361  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C HIS B  362  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C HIS B  363  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I8C HIS B  364  UNP  Q5HEB7              EXPRESSION TAG                 
SEQRES   1 A  364  MET THR LYS GLU ASN ILE CYS ILE VAL PHE GLY GLY LYS          
SEQRES   2 A  364  SER ALA GLU HIS GLU VAL SER ILE LEU THR ALA GLN ASN          
SEQRES   3 A  364  VAL LEU ASN ALA ILE ASP LYS ASP LYS TYR HIS VAL ASP          
SEQRES   4 A  364  ILE ILE TYR ILE THR ASN ASP GLY ASP TRP ARG LYS GLN          
SEQRES   5 A  364  ASN ASN ILE THR ALA GLU ILE LYS SER THR ASP GLU LEU          
SEQRES   6 A  364  HIS LEU GLU ASN GLY GLU ALA LEU GLU ILE SER GLN LEU          
SEQRES   7 A  364  LEU LYS GLU SER SER SER GLY GLN PRO TYR ASP ALA VAL          
SEQRES   8 A  364  PHE PRO LEU LEU HIS GLY PRO ASN GLY GLU ASP GLY THR          
SEQRES   9 A  364  ILE GLN GLY LEU PHE GLU VAL LEU ASP VAL PRO TYR VAL          
SEQRES  10 A  364  GLY ASN GLY VAL LEU SER ALA ALA SER SER MET ASP LYS          
SEQRES  11 A  364  LEU VAL MET LYS GLN LEU PHE GLU HIS ARG GLY LEU PRO          
SEQRES  12 A  364  GLN LEU PRO TYR ILE SER PHE LEU ARG SER GLU TYR GLU          
SEQRES  13 A  364  LYS TYR GLU HIS ASN ILE LEU LYS LEU VAL ASN ASP LYS          
SEQRES  14 A  364  LEU ASN TYR PRO VAL PHE VAL LYS PRO ALA ASN LEU GLY          
SEQRES  15 A  364  SER SER VAL GLY ILE SER LYS CYS ASN ASN GLU ALA GLU          
SEQRES  16 A  364  LEU LYS GLU GLY ILE LYS GLU ALA PHE GLN PHE ASP ARG          
SEQRES  17 A  364  LYS LEU VAL ILE GLU GLN GLY VAL ASN ALA ARG GLU ILE          
SEQRES  18 A  364  GLU VAL ALA VAL LEU GLY ASN ASP TYR PRO GLU ALA THR          
SEQRES  19 A  364  TRP PRO GLY GLU VAL VAL LYS ASP VAL ALA PHE TYR ASP          
SEQRES  20 A  364  TYR LYS SER LYS TYR LYS ASP GLY LYS VAL GLN LEU GLN          
SEQRES  21 A  364  ILE PRO ALA ASP LEU ASP GLU ASP VAL GLN LEU THR LEU          
SEQRES  22 A  364  ARG ASN MET ALA LEU GLU ALA PHE LYS ALA THR ASP CYS          
SEQRES  23 A  364  SER GLY LEU VAL ARG ALA ASP PHE PHE VAL THR GLU ASP          
SEQRES  24 A  364  ASN GLN ILE TYR ILE ASN GLU THR ASN ALA MET PRO GLY          
SEQRES  25 A  364  PHE THR ALA PHE SER MET TYR PRO LYS LEU TRP GLU ASN          
SEQRES  26 A  364  MET GLY LEU SER TYR PRO GLU LEU ILE THR LYS LEU ILE          
SEQRES  27 A  364  GLU LEU ALA LYS GLU ARG HIS GLN ASP LYS GLN LYS ASN          
SEQRES  28 A  364  LYS TYR LYS ILE ASP ARG SER HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  364  MET THR LYS GLU ASN ILE CYS ILE VAL PHE GLY GLY LYS          
SEQRES   2 B  364  SER ALA GLU HIS GLU VAL SER ILE LEU THR ALA GLN ASN          
SEQRES   3 B  364  VAL LEU ASN ALA ILE ASP LYS ASP LYS TYR HIS VAL ASP          
SEQRES   4 B  364  ILE ILE TYR ILE THR ASN ASP GLY ASP TRP ARG LYS GLN          
SEQRES   5 B  364  ASN ASN ILE THR ALA GLU ILE LYS SER THR ASP GLU LEU          
SEQRES   6 B  364  HIS LEU GLU ASN GLY GLU ALA LEU GLU ILE SER GLN LEU          
SEQRES   7 B  364  LEU LYS GLU SER SER SER GLY GLN PRO TYR ASP ALA VAL          
SEQRES   8 B  364  PHE PRO LEU LEU HIS GLY PRO ASN GLY GLU ASP GLY THR          
SEQRES   9 B  364  ILE GLN GLY LEU PHE GLU VAL LEU ASP VAL PRO TYR VAL          
SEQRES  10 B  364  GLY ASN GLY VAL LEU SER ALA ALA SER SER MET ASP LYS          
SEQRES  11 B  364  LEU VAL MET LYS GLN LEU PHE GLU HIS ARG GLY LEU PRO          
SEQRES  12 B  364  GLN LEU PRO TYR ILE SER PHE LEU ARG SER GLU TYR GLU          
SEQRES  13 B  364  LYS TYR GLU HIS ASN ILE LEU LYS LEU VAL ASN ASP LYS          
SEQRES  14 B  364  LEU ASN TYR PRO VAL PHE VAL LYS PRO ALA ASN LEU GLY          
SEQRES  15 B  364  SER SER VAL GLY ILE SER LYS CYS ASN ASN GLU ALA GLU          
SEQRES  16 B  364  LEU LYS GLU GLY ILE LYS GLU ALA PHE GLN PHE ASP ARG          
SEQRES  17 B  364  LYS LEU VAL ILE GLU GLN GLY VAL ASN ALA ARG GLU ILE          
SEQRES  18 B  364  GLU VAL ALA VAL LEU GLY ASN ASP TYR PRO GLU ALA THR          
SEQRES  19 B  364  TRP PRO GLY GLU VAL VAL LYS ASP VAL ALA PHE TYR ASP          
SEQRES  20 B  364  TYR LYS SER LYS TYR LYS ASP GLY LYS VAL GLN LEU GLN          
SEQRES  21 B  364  ILE PRO ALA ASP LEU ASP GLU ASP VAL GLN LEU THR LEU          
SEQRES  22 B  364  ARG ASN MET ALA LEU GLU ALA PHE LYS ALA THR ASP CYS          
SEQRES  23 B  364  SER GLY LEU VAL ARG ALA ASP PHE PHE VAL THR GLU ASP          
SEQRES  24 B  364  ASN GLN ILE TYR ILE ASN GLU THR ASN ALA MET PRO GLY          
SEQRES  25 B  364  PHE THR ALA PHE SER MET TYR PRO LYS LEU TRP GLU ASN          
SEQRES  26 B  364  MET GLY LEU SER TYR PRO GLU LEU ILE THR LYS LEU ILE          
SEQRES  27 B  364  GLU LEU ALA LYS GLU ARG HIS GLN ASP LYS GLN LYS ASN          
SEQRES  28 B  364  LYS TYR LYS ILE ASP ARG SER HIS HIS HIS HIS HIS HIS          
HET    SO4  A 401       5                                                       
HET    SO4  B 401       5                                                       
HET     MG  B 402       1                                                       
HET    ADP  A 400      27                                                       
HET    ADP  B 400      27                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5   MG    MG 2+                                                        
FORMUL   6  ADP    2(C10 H15 N5 O10 P2)                                         
HELIX    1   1 GLU A   16  ALA A   30  1                                  15    
HELIX    2   2 SER A   61  LEU A   65  5                                   5    
HELIX    3   3 HIS A   66  GLY A   70  5                                   5    
HELIX    4   4 SER A   76  GLU A   81  5                                   6    
HELIX    5   5 GLY A  103  ASP A  113  1                                  11    
HELIX    6   6 GLY A  120  MET A  128  1                                   9    
HELIX    7   7 ASP A  129  GLY A  141  1                                  13    
HELIX    8   8 ARG A  152  TYR A  158  1                                   7    
HELIX    9   9 TYR A  158  LEU A  170  1                                  13    
HELIX   10  10 ASN A  192  PHE A  204  1                                  13    
HELIX   11  11 ASP A  266  THR A  284  1                                  19    
HELIX   12  12 SER A  317  MET A  326  1                                  10    
HELIX   13  13 SER A  329  ARG A  357  1                                  29    
HELIX   14  14 GLU B   16  ILE B   31  1                                  16    
HELIX   15  15 GLU B   74  GLU B   81  1                                   8    
HELIX   16  16 GLY B  103  LEU B  112  1                                  10    
HELIX   17  17 GLY B  120  SER B  127  1                                   8    
HELIX   18  18 ASP B  129  GLY B  141  1                                  13    
HELIX   19  19 ARG B  152  LEU B  170  1                                  19    
HELIX   20  20 ASN B  192  GLN B  205  1                                  14    
HELIX   21  21 ASP B  266  THR B  284  1                                  19    
HELIX   22  22 SER B  317  MET B  326  1                                  10    
HELIX   23  23 SER B  329  SER B  358  1                                  30    
SHEET    1   A 5 GLU A  71  ALA A  72  0                                        
SHEET    2   A 5 TRP A  49  ILE A  55 -1  N  LYS A  51   O  GLU A  71           
SHEET    3   A 5 TYR A  36  ILE A  43 -1  N  TYR A  42   O  ARG A  50           
SHEET    4   A 5 GLU A   4  GLY A  11  1  N  GLU A   4   O  HIS A  37           
SHEET    5   A 5 ALA A  90  LEU A  94  1  O  LEU A  94   N  VAL A   9           
SHEET    1   B 4 TYR A 147  LEU A 151  0                                        
SHEET    2   B 4 LYS A 209  GLN A 214 -1  O  ILE A 212   N  ILE A 148           
SHEET    3   B 4 VAL A 174  PRO A 178 -1  N  LYS A 177   O  VAL A 211           
SHEET    4   B 4 SER A 188  CYS A 190 -1  O  CYS A 190   N  VAL A 174           
SHEET    1   C 4 GLU A 232  ALA A 233  0                                        
SHEET    2   C 4 ARG A 219  GLY A 227 -1  N  LEU A 226   O  GLU A 232           
SHEET    3   C 4 GLY A 237  VAL A 239 -1  O  GLY A 237   N  GLU A 222           
SHEET    4   C 4 LEU A 259  GLN A 260 -1  O  GLN A 260   N  GLU A 238           
SHEET    1   D 4 GLU A 232  ALA A 233  0                                        
SHEET    2   D 4 ARG A 219  GLY A 227 -1  N  LEU A 226   O  GLU A 232           
SHEET    3   D 4 GLY A 288  VAL A 296 -1  O  PHE A 294   N  ILE A 221           
SHEET    4   D 4 ILE A 302  ASN A 308 -1  O  TYR A 303   N  PHE A 295           
SHEET    1   E 4 ARG B  50  GLN B  52  0                                        
SHEET    2   E 4 TYR B  36  ILE B  43 -1  N  TYR B  42   O  ARG B  50           
SHEET    3   E 4 GLU B   4  GLY B  11  1  N  ILE B   6   O  HIS B  37           
SHEET    4   E 4 ALA B  90  PRO B  93  1  O  PHE B  92   N  CYS B   7           
SHEET    1   F 4 TYR B 147  LEU B 151  0                                        
SHEET    2   F 4 LYS B 209  GLN B 214 -1  O  ILE B 212   N  ILE B 148           
SHEET    3   F 4 VAL B 174  PRO B 178 -1  N  PHE B 175   O  GLU B 213           
SHEET    4   F 4 SER B 188  CYS B 190 -1  O  SER B 188   N  VAL B 176           
SHEET    1   G 4 GLU B 232  ALA B 233  0                                        
SHEET    2   G 4 ARG B 219  GLY B 227 -1  N  LEU B 226   O  GLU B 232           
SHEET    3   G 4 GLY B 237  VAL B 239 -1  O  GLY B 237   N  GLU B 222           
SHEET    4   G 4 LEU B 259  GLN B 260 -1  O  GLN B 260   N  GLU B 238           
SHEET    1   H 4 GLU B 232  ALA B 233  0                                        
SHEET    2   H 4 ARG B 219  GLY B 227 -1  N  LEU B 226   O  GLU B 232           
SHEET    3   H 4 GLY B 288  VAL B 296 -1  O  VAL B 296   N  ARG B 219           
SHEET    4   H 4 ILE B 302  ASN B 308 -1  O  GLU B 306   N  ASP B 293           
LINK        MG    MG B 402                 OE2 GLU B 306     1555   1555  2.19  
LINK        MG    MG B 402                 O2A ADP B 400     1555   1555  2.21  
LINK        MG    MG B 402                 O2B ADP B 400     1555   1555  2.10  
CISPEP   1 TYR A  172    PRO A  173          0         3.85                     
CISPEP   2 ILE A  261    PRO A  262          0        -3.34                     
CISPEP   3 TYR B  172    PRO B  173          0        -2.26                     
CISPEP   4 ILE B  261    PRO B  262          0        -6.74                     
SITE     1 AC1  4 HIS A  96  ARG A 291  ASN A 308  GLY A 312                    
SITE     1 AC2  3 ARG B 291  ASN B 308  GLY B 312                               
SITE     1 AC3  2 GLU B 306  ADP B 400                                          
SITE     1 AC4 12 LYS A 130  LEU A 145  PHE A 175  LYS A 177                    
SITE     2 AC4 12 SER A 183  GLU A 213  GLN A 214  GLY A 215                    
SITE     3 AC4 12 VAL A 216  GLU A 220  ASN A 305  GLU A 306                    
SITE     1 AC5 12 PHE B 175  LYS B 177  SER B 183  GLU B 213                    
SITE     2 AC5 12 GLN B 214  GLY B 215  VAL B 216  GLU B 220                    
SITE     3 AC5 12 PHE B 295  ASN B 305  GLU B 306   MG B 402                    
CRYST1   67.802   66.972   78.992  90.00  96.05  90.00 P 1 21 1      4          
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      0.014749  0.000000  0.001563        0.00000                         
SCALE2      0.000000  0.014932  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012730        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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