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Database: PDB
Entry: 2I87
LinkDB: 2I87
Original site: 2I87 
HEADER    LIGASE                                  01-SEP-06   2I87              
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, APO, LIGASE                               
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 2I87    1       VERSN                                    
REVDAT   3   24-FEB-09 2I87    1       VERSN                                    
REVDAT   2   24-OCT-06 2I87    1       JRNL                                     
REVDAT   1   03-OCT-06 2I87    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.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.06                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 44470                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2336                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3276                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.63                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1880                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 181                          
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5479                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 91                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 37.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.84                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.07000                                             
REMARK   3    B22 (A**2) : 0.27000                                              
REMARK   3    B33 (A**2) : -0.20000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.01000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.204         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.121         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.699         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5593 ; 0.024 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3746 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7567 ; 1.991 ; 1.967       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9214 ; 1.034 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   683 ; 7.330 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   277 ;39.448 ;25.957       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1001 ;16.746 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;17.457 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   839 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6195 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1033 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1276 ; 0.230 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4000 ; 0.206 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2750 ; 0.194 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  3100 ; 0.097 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   195 ; 0.170 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     2 ; 0.013 ; 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):    37 ; 0.248 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    58 ; 0.221 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.278 ; 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):  4305 ; 1.567 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1388 ; 0.357 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5534 ; 1.933 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2471 ; 3.074 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2033 ; 4.256 ; 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):  26.1095   0.0007  -5.1906              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0912 T22:  -0.0183                                     
REMARK   3      T33:  -0.0665 T12:   0.0001                                     
REMARK   3      T13:   0.0216 T23:   0.0125                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8176 L22:   1.0428                                     
REMARK   3      L33:   3.8172 L12:   0.0960                                     
REMARK   3      L13:  -1.1314 L23:  -0.5410                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0808 S12:   0.2836 S13:  -0.1780                       
REMARK   3      S21:  -0.1294 S22:  -0.0572 S23:  -0.1273                       
REMARK   3      S31:   0.3010 S32:   0.1069 S33:   0.1380                       
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):  10.0311 -16.9728  20.9210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0290 T22:  -0.0949                                     
REMARK   3      T33:  -0.0577 T12:  -0.1019                                     
REMARK   3      T13:  -0.0025 T23:  -0.0197                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7842 L22:   1.9108                                     
REMARK   3      L33:   2.3811 L12:  -0.7507                                     
REMARK   3      L13:   1.0821 L23:  -0.8895                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1414 S12:  -0.0567 S13:  -0.2658                       
REMARK   3      S21:  -0.0581 S22:   0.0818 S23:   0.1248                       
REMARK   3      S31:   0.5534 S32:  -0.3375 S33:  -0.2232                       
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   220                          
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9584   1.6338   3.1506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1432 T22:  -0.0335                                     
REMARK   3      T33:  -0.0202 T12:   0.0095                                     
REMARK   3      T13:  -0.0153 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3343 L22:   1.9984                                     
REMARK   3      L33:   1.6377 L12:   1.2442                                     
REMARK   3      L13:  -0.3259 L23:  -0.0209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0238 S12:   0.1753 S13:   0.1533                       
REMARK   3      S21:  -0.0569 S22:   0.0100 S23:   0.2097                       
REMARK   3      S31:  -0.0641 S32:  -0.2265 S33:  -0.0338                       
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):  42.5284   2.4622  17.2792              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0702 T22:   0.0822                                     
REMARK   3      T33:  -0.0433 T12:  -0.0660                                     
REMARK   3      T13:  -0.0338 T23:   0.0996                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4722 L22:   0.8558                                     
REMARK   3      L33:   3.1648 L12:   0.0115                                     
REMARK   3      L13:   0.4896 L23:   0.9196                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0618 S12:   0.4833 S13:   0.2837                       
REMARK   3      S21:   0.0097 S22:   0.0337 S23:  -0.1253                       
REMARK   3      S31:  -0.3656 S32:   0.6357 S33:   0.0281                       
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):  10.9505  14.9154  26.2898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0616 T22:  -0.0774                                     
REMARK   3      T33:  -0.0117 T12:   0.0646                                     
REMARK   3      T13:   0.0546 T23:  -0.0368                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7547 L22:   2.1390                                     
REMARK   3      L33:   4.3812 L12:  -1.0082                                     
REMARK   3      L13:   0.5391 L23:  -1.2032                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1099 S12:  -0.1268 S13:   0.0779                       
REMARK   3      S21:   0.3554 S22:   0.1852 S23:   0.0990                       
REMARK   3      S31:  -0.7323 S32:  -0.3419 S33:  -0.0753                       
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):  28.6661  -2.6782  32.9995              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0196 T22:  -0.1035                                     
REMARK   3      T33:  -0.1024 T12:   0.0054                                     
REMARK   3      T13:  -0.0153 T23:   0.0104                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8050 L22:   1.4840                                     
REMARK   3      L33:   1.8605 L12:  -0.3121                                     
REMARK   3      L13:  -0.0870 L23:   0.6152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0029 S12:  -0.0648 S13:  -0.0218                       
REMARK   3      S21:   0.2393 S22:  -0.0528 S23:  -0.0226                       
REMARK   3      S31:   0.0319 S32:   0.1055 S33:   0.0499                       
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 2I87 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 RCSB039259.                                      
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        : 1                                  
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                  : MIRROR                             
REMARK 200  OPTICS                         : MIRRORS                            
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   : 46823                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.00000                            
REMARK 200  R SYM                      (I) : 0.03800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 26.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.16200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.16200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB CODE 1EHI                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
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       33.20400            
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: 4800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29080 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 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     ALA B    72                                                      
REMARK 465     ASN B    99                                                      
REMARK 465     GLY B   100                                                      
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: 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   NZ   LYS B   189     O    GLY B   327     2656     2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  18   CB    GLU A  18   CG      0.120                       
REMARK 500    GLU A 101   CB    GLU A 101   CG      0.134                       
REMARK 500    GLU A 101   CD    GLU A 101   OE1     0.078                       
REMARK 500    GLU A 222   CG    GLU A 222   CD     -0.183                       
REMARK 500    ASN B 192   CG    ASN B 192   ND2     0.169                       
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 152   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG A 152   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    ARG A 219   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    GLU A 222   OE1 -  CD  -  OE2 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ASP A 293   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    LEU B 131   CB  -  CG  -  CD2 ANGL. DEV. = -10.4 DEGREES          
REMARK 500    ARG B 219   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  13       34.72    -69.89                                   
REMARK 500    LEU A  67     -116.94     55.71                                   
REMARK 500    LEU A  94       51.18   -111.64                                   
REMARK 500    HIS A  96     -159.28    -97.81                                   
REMARK 500    SER A 184       -0.80     57.46                                   
REMARK 500    ASN A 228      -83.13   -116.43                                   
REMARK 500    ASP A 356      -34.82    -38.73                                   
REMARK 500    ALA B  15       35.39    -79.92                                   
REMARK 500    ASN B  54       75.45     50.88                                   
REMARK 500    ASN B 228      -86.37   -124.78                                   
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 ALA B   15     GLU B   16                  143.83                    
REMARK 500 GLY B   97     PRO B   98                  149.18                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 402                 
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: 2I8C   RELATED DB: PDB                                   
REMARK 900 ALLOSTERIC INHIBITION OF STAPHYLOCOCCUS AUREUS D-ALANINE:D-          
REMARK 900 ALANINE LIGASE REVEALED BY CRYSTALLOGRAPHIC STUDIES                  
DBREF  2I87 A    1   356  UNP    Q5HEB7   DDL_STAAC        1    356             
DBREF  2I87 B    1   356  UNP    Q5HEB7   DDL_STAAC        1    356             
SEQADV 2I87 ARG A  357  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I87 SER A  358  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I87 HIS A  359  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 HIS A  360  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 HIS A  361  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 HIS A  362  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 HIS A  363  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 HIS A  364  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 ARG B  357  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I87 SER B  358  UNP  Q5HEB7              CLONING ARTIFACT               
SEQADV 2I87 HIS B  359  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 HIS B  360  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 HIS B  361  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 HIS B  362  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 HIS B  363  UNP  Q5HEB7              EXPRESSION TAG                 
SEQADV 2I87 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 402       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5  HOH   *91(H2 O)                                                     
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  ASP A  129  1                                  10    
HELIX    7   7 ASP A  129  GLY A  141  1                                  13    
HELIX    8   8 ARG A  152  LEU A  170  1                                  19    
HELIX    9   9 ASN A  192  GLN A  205  1                                  14    
HELIX   10  10 ASP A  266  THR A  284  1                                  19    
HELIX   11  11 SER A  317  MET A  326  1                                  10    
HELIX   12  12 SER A  329  SER A  358  1                                  30    
HELIX   13  13 GLU B   16  ILE B   31  1                                  16    
HELIX   14  14 SER B   61  HIS B   66  5                                   6    
HELIX   15  15 GLU B   74  GLU B   81  1                                   8    
HELIX   16  16 GLY B  103  ASP B  113  1                                  11    
HELIX   17  17 GLY B  120  ASP B  129  1                                  10    
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  PHE B  204  1                                  13    
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  HIS B  360  1                                  32    
SHEET    1   A 5 GLU A  71  LEU A  73  0                                        
SHEET    2   A 5 TRP A  49  GLN A  52 -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 TRP B  49  GLN B  52  0                                        
SHEET    2   E 4 TYR B  36  ILE B  43 -1  N  ILE B  40   O  GLN B  52           
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  CYS B 190   N  VAL B 174           
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  PHE B 294   N  ILE B 221           
SHEET    4   H 4 ILE B 302  ASN B 308 -1  O  TYR B 303   N  PHE B 295           
CISPEP   1 TYR A  172    PRO A  173          0         3.42                     
CISPEP   2 ILE A  261    PRO A  262          0        -0.12                     
CISPEP   3 TYR B  172    PRO B  173          0        -7.51                     
CISPEP   4 ILE B  261    PRO B  262          0        -1.87                     
SITE     1 AC1  4 ARG A 291  ASN A 308  PRO A 311  GLY A 312                    
SITE     1 AC2  4 ARG B 291  ASN B 308  PRO B 311  GLY B 312                    
CRYST1   67.661   66.408   78.590  90.00  96.24  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      0.014780  0.000000  0.001616        0.00000                         
SCALE2      0.000000  0.015058  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012800        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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