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Database: PDB
Entry: 2VSH 2VSI
LinkDB: 2VSH 2VSI
Original site: 2VSH 2VSI 
HEADER    TRANSFERASE                             23-APR-08   2VSH              
TITLE     SYNTHESIS OF CDP-ACTIVATED RIBITOL FOR TEICHOIC ACID PRECURSORS IN    
TITLE    2 STREPTOCOCCUS PNEUMONIAE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE;  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TARI;                                                       
COMPND   5 EC: 2.7.7.60                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 1313;                                                
SOURCE   4 STRAIN: R36A;                                                        
SOURCE   5 ATCC: 12214                                                          
KEYWDS    TRANSFERASE, NUCLEOTIDYLTRANSFERASE, TARI SPR1149 CDP RIBITOL         
KEYWDS   2 STREPTOCOCCUS PNEUMONIAE TECHOIC TRANSFERASE, ISOPRENE BIOSYNTHESIS  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BAUR,J.MARLES-WRIGHT,S.BUCKENMAIER,R.J.LEWIS,W.VOLLMER              
REVDAT   3   13-DEC-23 2VSH    1       LINK                                     
REVDAT   2   10-FEB-09 2VSH    1       JRNL   REMARK                            
REVDAT   1   30-DEC-08 2VSH    0                                                
JRNL        AUTH   S.BAUR,J.MARLES-WRIGHT,S.BUCKENMAIER,R.J.LEWIS,W.VOLLMER     
JRNL        TITL   SYNTHESIS OF CDP-ACTIVATED RIBITOL FOR TEICHOIC ACID         
JRNL        TITL 2 PRECURSORS IN STREPTOCOCCUS PNEUMONIAE.                      
JRNL        REF    J.BACTERIOL.                  V. 191  1200 2009              
JRNL        REFN                   ISSN 0021-9193                               
JRNL        PMID   19074383                                                     
JRNL        DOI    10.1128/JB.01120-08                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0040                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
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) : 29.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 35141                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1805                            
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) : 2442                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.48                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 137                          
REMARK   3   BIN FREE R VALUE                    : 0.3060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3515                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 71                                      
REMARK   3   SOLVENT ATOMS            : 240                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.13                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.29000                                              
REMARK   3    B22 (A**2) : -0.76000                                             
REMARK   3    B33 (A**2) : -1.54000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.177         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.172         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.129         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.044         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.916                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3678 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4964 ; 1.278 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   452 ; 5.599 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   158 ;35.127 ;25.127       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   667 ;16.058 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;19.692 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   587 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2640 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1751 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2521 ; 0.302 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   268 ; 0.225 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     4 ; 0.046 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    56 ; 0.217 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.207 ; 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):  2306 ; 0.540 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3659 ; 0.870 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1520 ; 1.397 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1299 ; 2.184 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   139                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.4488 -18.5217  -5.5312              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1516 T22:  -0.1737                                     
REMARK   3      T33:  -0.1592 T12:   0.0084                                     
REMARK   3      T13:   0.0028 T23:  -0.0586                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9244 L22:   3.0900                                     
REMARK   3      L33:   2.4082 L12:   0.5245                                     
REMARK   3      L13:   0.1117 L23:   0.0912                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0035 S12:   0.1335 S13:  -0.0446                       
REMARK   3      S21:  -0.1165 S22:  -0.0247 S23:  -0.0668                       
REMARK   3      S31:  -0.1105 S32:   0.1558 S33:   0.0212                       
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   140        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6737 -22.2817  18.2248              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0007 T22:   0.0661                                     
REMARK   3      T33:  -0.1032 T12:  -0.0034                                     
REMARK   3      T13:   0.0032 T23:   0.0094                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  13.5685 L22:   2.7952                                     
REMARK   3      L33:   2.2411 L12:  -5.9834                                     
REMARK   3      L13:  -5.4271 L23:   2.4982                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1527 S12:  -1.1558 S13:  -0.2302                       
REMARK   3      S21:   0.1359 S22:   0.1494 S23:   0.0987                       
REMARK   3      S31:   0.0365 S32:   0.2319 S33:   0.0033                       
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   168        A   233                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6455 -21.7108   2.1811              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1084 T22:  -0.1848                                     
REMARK   3      T33:  -0.1387 T12:   0.0153                                     
REMARK   3      T13:   0.0188 T23:  -0.0297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1292 L22:   1.6300                                     
REMARK   3      L33:   1.3711 L12:  -0.2042                                     
REMARK   3      L13:   0.0040 L23:  -0.5810                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0160 S12:  -0.1480 S13:  -0.1941                       
REMARK   3      S21:   0.1417 S22:   0.0484 S23:   0.0000                       
REMARK   3      S31:  -0.0005 S32:  -0.0964 S33:  -0.0323                       
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     0        B   139                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.1737  -6.0295  38.0946              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0352 T22:  -0.0886                                     
REMARK   3      T33:  -0.1503 T12:   0.0132                                     
REMARK   3      T13:   0.0153 T23:  -0.0474                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7527 L22:   0.6905                                     
REMARK   3      L33:   2.4701 L12:   1.0532                                     
REMARK   3      L13:  -0.4666 L23:  -0.7020                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0388 S12:  -0.2567 S13:   0.2111                       
REMARK   3      S21:   0.1407 S22:  -0.0160 S23:   0.0873                       
REMARK   3      S31:  -0.1405 S32:   0.0714 S33:  -0.0228                       
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   140        B   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.4781 -23.7597  11.7618              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0757 T22:  -0.0683                                     
REMARK   3      T33:  -0.1685 T12:  -0.0441                                     
REMARK   3      T13:   0.0096 T23:   0.0102                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0238 L22:   7.3950                                     
REMARK   3      L33:   4.8814 L12:  -3.2998                                     
REMARK   3      L13:  -2.5484 L23:   4.5690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0155 S12:  -0.1801 S13:  -0.1641                       
REMARK   3      S21:  -0.1426 S22:  -0.0755 S23:   0.0911                       
REMARK   3      S31:  -0.0625 S32:  -0.0495 S33:   0.0600                       
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   168        B   232                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1746 -16.0639  29.6684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0093 T22:  -0.0717                                     
REMARK   3      T33:  -0.1038 T12:   0.0023                                     
REMARK   3      T13:   0.0136 T23:  -0.0804                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3042 L22:   0.7755                                     
REMARK   3      L33:   3.0345 L12:   1.4334                                     
REMARK   3      L13:  -1.5950 L23:  -0.7066                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1395 S12:   0.0044 S13:  -0.4462                       
REMARK   3      S21:  -0.0483 S22:  -0.0044 S23:  -0.1118                       
REMARK   3      S31:   0.3314 S32:  -0.0658 S33:   0.1438                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 2VSH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290036018.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 140                                
REMARK 200  PH                             : 6.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36985                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.480                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
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) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1VPA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 6.75 35 % V/W PEG 300    
REMARK 280  200 MM CACL2                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.09500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.09500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       40.50000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.69000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       40.50000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.69000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.09500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       40.50000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.69000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.09500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       40.50000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       46.69000            
REMARK 290   SMTRY3   8  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 4120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24310 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.8 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B2039  LIES ON A SPECIAL POSITION.                          
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     GLY A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     MET A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     ASP A   235                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     THR B    11                                                      
REMARK 465     GLY B    12                                                      
REMARK 465     THR B    13                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     MET B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     ILE B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     LEU B    20                                                      
REMARK 465     GLU B   233                                                      
REMARK 465     LYS B   234                                                      
REMARK 465     ASP B   235                                                      
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 B 115   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 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    ARG A 115       72.39   -113.41                                   
REMARK 500    ASP A 157      173.83    179.09                                   
REMARK 500    GLN A 168     -164.54   -123.79                                   
REMARK 500    ASN A 216       52.19    -69.48                                   
REMARK 500    ARG B 115       75.42   -113.53                                   
REMARK 500    GLN B 168     -162.35   -122.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2019        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A2044        DISTANCE =  6.01 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1234  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  97   OD2                                                    
REMARK 620 2 ASP A  97   OD1  50.9                                              
REMARK 620 3 HOH A2075   O    86.9  81.9                                        
REMARK 620 4 HOH A2076   O    89.0  86.9 168.2                                  
REMARK 620 5 HOH B2029   O    79.6 130.5  97.5  92.6                            
REMARK 620 6 HOH B2030   O   148.9 160.0  94.4  94.9  69.4                      
REMARK 620 7 HOH B2034   O   131.1  81.0  76.9  97.6 147.5  79.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A1240  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2127   O                                                      
REMARK 620 2 HOH A2132   O    66.9                                              
REMARK 620 N                    1                                               
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1234                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1235                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PE A1236                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A1237                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1238                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A1239                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A1240                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P6G B1233                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VSI   RELATED DB: PDB                                   
REMARK 900 SYNTHESIS OF CDP-ACTIVATED RIBITOL FOR TEICHOIC ACID PRECURSORS IN   
REMARK 900 STREPTOCOCCUS PNEUMONIAE                                             
DBREF  2VSH A    0     0  PDB    2VSH     2VSH             0      0             
DBREF  2VSH A    1   235  UNP    A5MSS9   A5MSS9_STRPN     1    235             
DBREF  2VSH B    0     0  PDB    2VSH     2VSH             0      0             
DBREF  2VSH B    1   235  UNP    A5MSS9   A5MSS9_STRPN     1    235             
SEQRES   1 A  236  HIS MET ILE TYR ALA GLY ILE LEU ALA GLY GLY THR GLY          
SEQRES   2 A  236  THR ARG MET GLY ILE SER ASN LEU PRO LYS GLN PHE LEU          
SEQRES   3 A  236  GLU LEU GLY ASP ARG PRO ILE LEU ILE HIS THR ILE GLU          
SEQRES   4 A  236  LYS PHE VAL LEU GLU PRO SER ILE GLU LYS ILE VAL VAL          
SEQRES   5 A  236  GLY VAL HIS GLY ASP TRP VAL SER HIS ALA GLU ASP LEU          
SEQRES   6 A  236  VAL ASP LYS TYR LEU PRO LEU TYR LYS GLU ARG ILE ILE          
SEQRES   7 A  236  ILE THR LYS GLY GLY ALA ASP ARG ASN THR SER ILE LYS          
SEQRES   8 A  236  ASN ILE ILE GLU ALA ILE ASP ALA TYR ARG PRO LEU THR          
SEQRES   9 A  236  PRO GLU ASP ILE VAL VAL THR HIS ASP SER VAL ARG PRO          
SEQRES  10 A  236  PHE ILE THR LEU ARG MET ILE GLN ASP ASN ILE GLN LEU          
SEQRES  11 A  236  ALA GLN ASN HIS ASP ALA VAL ASP THR VAL VAL GLU ALA          
SEQRES  12 A  236  VAL ASP THR ILE VAL GLU SER THR ASN GLY GLN PHE ILE          
SEQRES  13 A  236  THR ASP ILE PRO ASN ARG ALA HIS LEU TYR GLN GLY GLN          
SEQRES  14 A  236  THR PRO GLN THR PHE ARG CYS LYS ASP PHE MET ASP LEU          
SEQRES  15 A  236  TYR GLY SER LEU SER ASP GLU GLU LYS GLU ILE LEU THR          
SEQRES  16 A  236  ASP ALA CYS LYS ILE PHE VAL ILE LYS GLY LYS ASP VAL          
SEQRES  17 A  236  ALA LEU ALA LYS GLY GLU TYR SER ASN LEU LYS ILE THR          
SEQRES  18 A  236  THR VAL THR ASP LEU LYS ILE ALA LYS SER MET ILE GLU          
SEQRES  19 A  236  LYS ASP                                                      
SEQRES   1 B  236  HIS MET ILE TYR ALA GLY ILE LEU ALA GLY GLY THR GLY          
SEQRES   2 B  236  THR ARG MET GLY ILE SER ASN LEU PRO LYS GLN PHE LEU          
SEQRES   3 B  236  GLU LEU GLY ASP ARG PRO ILE LEU ILE HIS THR ILE GLU          
SEQRES   4 B  236  LYS PHE VAL LEU GLU PRO SER ILE GLU LYS ILE VAL VAL          
SEQRES   5 B  236  GLY VAL HIS GLY ASP TRP VAL SER HIS ALA GLU ASP LEU          
SEQRES   6 B  236  VAL ASP LYS TYR LEU PRO LEU TYR LYS GLU ARG ILE ILE          
SEQRES   7 B  236  ILE THR LYS GLY GLY ALA ASP ARG ASN THR SER ILE LYS          
SEQRES   8 B  236  ASN ILE ILE GLU ALA ILE ASP ALA TYR ARG PRO LEU THR          
SEQRES   9 B  236  PRO GLU ASP ILE VAL VAL THR HIS ASP SER VAL ARG PRO          
SEQRES  10 B  236  PHE ILE THR LEU ARG MET ILE GLN ASP ASN ILE GLN LEU          
SEQRES  11 B  236  ALA GLN ASN HIS ASP ALA VAL ASP THR VAL VAL GLU ALA          
SEQRES  12 B  236  VAL ASP THR ILE VAL GLU SER THR ASN GLY GLN PHE ILE          
SEQRES  13 B  236  THR ASP ILE PRO ASN ARG ALA HIS LEU TYR GLN GLY GLN          
SEQRES  14 B  236  THR PRO GLN THR PHE ARG CYS LYS ASP PHE MET ASP LEU          
SEQRES  15 B  236  TYR GLY SER LEU SER ASP GLU GLU LYS GLU ILE LEU THR          
SEQRES  16 B  236  ASP ALA CYS LYS ILE PHE VAL ILE LYS GLY LYS ASP VAL          
SEQRES  17 B  236  ALA LEU ALA LYS GLY GLU TYR SER ASN LEU LYS ILE THR          
SEQRES  18 B  236  THR VAL THR ASP LEU LYS ILE ALA LYS SER MET ILE GLU          
SEQRES  19 B  236  LYS ASP                                                      
HET     CA  A1234       1                                                       
HET    PEG  A1235       7                                                       
HET    1PE  A1236      16                                                       
HET    PG4  A1237      13                                                       
HET    PEG  A1238       7                                                       
HET    PEG  A1239       7                                                       
HET     CA  A1240       1                                                       
HET    P6G  B1233      19                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETSYN     1PE PEG400                                                           
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   4  PEG    3(C4 H10 O3)                                                 
FORMUL   5  1PE    C10 H22 O6                                                   
FORMUL   6  PG4    C8 H18 O5                                                    
FORMUL  10  P6G    C12 H26 O7                                                   
FORMUL  11  HOH   *240(H2 O)                                                    
HELIX    1   1 PRO A   21  PHE A   24  5                                   4    
HELIX    2   2 ILE A   32  LEU A   42  1                                  11    
HELIX    3   3 TRP A   57  LEU A   69  1                                  13    
HELIX    4   4 PRO A   70  GLU A   74  5                                   5    
HELIX    5   5 ASP A   84  ARG A  100  1                                  17    
HELIX    6   6 THR A  119  HIS A  133  1                                  15    
HELIX    7   7 ASN A  160  ALA A  162  5                                   3    
HELIX    8   8 CYS A  175  SER A  184  1                                  10    
HELIX    9   9 SER A  186  LEU A  193  1                                   8    
HELIX   10  10 ASP A  195  LYS A  203  1                                   9    
HELIX   11  11 THR A  221  ILE A  232  1                                  12    
HELIX   12  12 PRO B   21  PHE B   24  5                                   4    
HELIX   13  13 ILE B   32  LEU B   42  1                                  11    
HELIX   14  14 TRP B   57  LEU B   69  1                                  13    
HELIX   15  15 PRO B   70  GLU B   74  5                                   5    
HELIX   16  16 ASP B   84  ARG B  100  1                                  17    
HELIX   17  17 THR B  119  ASN B  132  1                                  14    
HELIX   18  18 ASN B  160  ALA B  162  5                                   3    
HELIX   19  19 CYS B  175  SER B  184  1                                  10    
HELIX   20  20 SER B  186  LEU B  193  1                                   8    
HELIX   21  21 ASP B  195  LYS B  203  1                                   9    
HELIX   22  22 THR B  221  ILE B  232  1                                  12    
SHEET    1  AA 7 ILE A  76  LYS A  80  0                                        
SHEET    2  AA 7 ILE A  49  VAL A  53  1  O  ILE A  49   N  ILE A  77           
SHEET    3  AA 7 ILE A   2  ALA A   8  1  O  ALA A   4   N  VAL A  50           
SHEET    4  AA 7 ILE A 107  ASP A 112  1  O  ILE A 107   N  TYR A   3           
SHEET    5  AA 7 LEU A 164  ARG A 174 -1  O  GLN A 171   N  THR A 110           
SHEET    6  AA 7 ALA A 135  GLU A 141 -1  O  VAL A 136   N  THR A 172           
SHEET    7  AA 7 VAL A 207  LYS A 211  1  O  ALA A 208   N  ASP A 137           
SHEET    1  AB 6 ILE A  76  LYS A  80  0                                        
SHEET    2  AB 6 ILE A  49  VAL A  53  1  O  ILE A  49   N  ILE A  77           
SHEET    3  AB 6 ILE A   2  ALA A   8  1  O  ALA A   4   N  VAL A  50           
SHEET    4  AB 6 ILE A 107  ASP A 112  1  O  ILE A 107   N  TYR A   3           
SHEET    5  AB 6 LEU A 164  ARG A 174 -1  O  GLN A 171   N  THR A 110           
SHEET    6  AB 6 ILE B 146  GLU B 148 -1  O  VAL B 147   N  TYR A 165           
SHEET    1  AC 2 GLU A  26  LEU A  27  0                                        
SHEET    2  AC 2 ARG A  30  PRO A  31 -1  O  ARG A  30   N  LEU A  27           
SHEET    1  AD 6 ILE A 146  GLU A 148  0                                        
SHEET    2  AD 6 LEU B 164  ARG B 174 -1  O  TYR B 165   N  VAL A 147           
SHEET    3  AD 6 ILE B 107  ASP B 112 -1  O  VAL B 108   N  PHE B 173           
SHEET    4  AD 6 ILE B   2  ALA B   8  1  O  TYR B   3   N  VAL B 109           
SHEET    5  AD 6 ILE B  46  VAL B  53  1  N  GLU B  47   O  ILE B   2           
SHEET    6  AD 6 ILE B  76  LYS B  80  1  O  ILE B  77   N  VAL B  51           
SHEET    1  AE 4 ILE A 146  GLU A 148  0                                        
SHEET    2  AE 4 LEU B 164  ARG B 174 -1  O  TYR B 165   N  VAL A 147           
SHEET    3  AE 4 ALA B 135  GLU B 141 -1  O  VAL B 136   N  THR B 172           
SHEET    4  AE 4 VAL B 207  LYS B 211  1  O  ALA B 208   N  ASP B 137           
SHEET    1  BA 2 GLU B  26  LEU B  27  0                                        
SHEET    2  BA 2 ARG B  30  PRO B  31 -1  O  ARG B  30   N  LEU B  27           
LINK         OD2 ASP A  97                CA    CA A1234     1555   1555  2.48  
LINK         OD1 ASP A  97                CA    CA A1234     1555   1555  2.61  
LINK        CA    CA A1234                 O   HOH A2075     1555   1555  2.45  
LINK        CA    CA A1234                 O   HOH A2076     1555   1555  2.46  
LINK        CA    CA A1234                 O   HOH B2029     1555   6444  2.28  
LINK        CA    CA A1234                 O   HOH B2030     1555   6444  2.37  
LINK        CA    CA A1234                 O   HOH B2034     1555   6444  2.34  
LINK        CA    CA A1240                 O   HOH A2127     1555   1555  3.06  
LINK        CA    CA A1240                 O   HOH A2132     1555   1555  2.47  
CISPEP   1 THR A  169    PRO A  170          0         5.03                     
CISPEP   2 THR B  169    PRO B  170          0        10.59                     
SITE     1 AC1  6 ASP A  97  HOH A2075  HOH A2076  HOH B2029                    
SITE     2 AC1  6 HOH B2030  HOH B2034                                          
SITE     1 AC2  4 HIS A  54  GLY A  55  LYS A  80  HOH A2161                    
SITE     1 AC3  5 ASP A 134  LEU A 181  LYS A 203  GLY A 204                    
SITE     2 AC3  5 LYS A 205                                                     
SITE     1 AC4  4 ARG A 100  PRO A 101  LEU B 102  LYS B 176                    
SITE     1 AC5  3 GLY A 204  ASP A 206  PHE B 154                               
SITE     1 AC6  6 THR A 119  LEU A 120  ARG A 121  SER A 186                    
SITE     2 AC6  6 GLU A 188  HOH A2088                                          
SITE     1 AC7  2 HOH A2127  HOH A2132                                          
SITE     1 AC8  7 ASP B 134  ASP B 177  LEU B 181  LYS B 203                    
SITE     2 AC8  7 GLY B 204  LYS B 205  HOH B2078                               
CRYST1   81.000   93.380  144.190  90.00  90.00  90.00 C 2 2 21     16          
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      0.012346  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010709  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006935        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
HEADER    TRANSFERASE                             23-APR-08   2VSI              
TITLE     SYNTHESIS OF CDP-ACTIVATED RIBITOL FOR TEICHOIC ACID PRECURSORS IN    
TITLE    2 STREPTOCOCCUS PNEUMONIAE                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-C-METHYL-D-ERYTHRITOL 4-PHOSPHATE CYTIDYLYLTRANSFERASE;  
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TARI;                                                       
COMPND   5 EC: 2.7.7.60                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOCOCCUS PNEUMONIAE;                       
SOURCE   3 ORGANISM_TAXID: 1313;                                                
SOURCE   4 STRAIN: R36A;                                                        
SOURCE   5 ATCC: 12214                                                          
KEYWDS    SPR1149 TARI CDP RIBITOL STREPTOCOCCUS PNEUMONIAE,                    
KEYWDS   2 NUCLEOTIDYLTRANSFERASE, TRANSFERASE, ISOPRENE BIOSYNTHESIS           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BAUR,J.MARLES-WRIGHT,S.BUCKENMAIER,R.J.LEWIS,W.VOLLMER              
REVDAT   4   13-DEC-23 2VSI    1       LINK                                     
REVDAT   3   04-APR-18 2VSI    1       REMARK                                   
REVDAT   2   10-FEB-09 2VSI    1       JRNL   REMARK                            
REVDAT   1   30-DEC-08 2VSI    0                                                
JRNL        AUTH   S.BAUR,J.MARLES-WRIGHT,S.BUCKENMAIER,R.J.LEWIS,W.VOLLMER     
JRNL        TITL   SYNTHESIS OF CDP-ACTIVATED RIBITOL FOR TEICHOIC ACID         
JRNL        TITL 2 PRECURSORS IN STREPTOCOCCUS PNEUMONIAE.                      
JRNL        REF    J.BACTERIOL.                  V. 191  1200 2009              
JRNL        REFN                   ISSN 0021-9193                               
JRNL        PMID   19074383                                                     
JRNL        DOI    10.1128/JB.01120-08                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 56.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 12215                          
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) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 624                             
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) : 2.75                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.82                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 906                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.27                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 49                           
REMARK   3   BIN FREE R VALUE                    : 0.4090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3556                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 51                                      
REMARK   3   SOLVENT ATOMS            : 10                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.27000                                              
REMARK   3    B22 (A**2) : -1.99000                                             
REMARK   3    B33 (A**2) : 0.72000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.428         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.353         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 38.687        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.935                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.897                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3675 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4991 ; 1.193 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   450 ; 5.543 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   157 ;35.435 ;25.159       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   663 ;17.262 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;15.458 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   594 ; 0.074 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2664 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1665 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2510 ; 0.303 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   137 ; 0.143 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    49 ; 0.163 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     6 ; 0.124 ; 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):  2312 ; 0.258 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3677 ; 0.459 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1516 ; 0.590 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1313 ; 0.947 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     0        A   139                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.5348 -18.4417  -5.4510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1037 T22:  -0.3305                                     
REMARK   3      T33:  -0.1083 T12:   0.0057                                     
REMARK   3      T13:  -0.0245 T23:  -0.1294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9695 L22:   2.0161                                     
REMARK   3      L33:   3.5578 L12:   0.4536                                     
REMARK   3      L13:   0.1393 L23:  -0.4612                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0121 S12:   0.3314 S13:  -0.1789                       
REMARK   3      S21:  -0.1036 S22:  -0.0629 S23:   0.0340                       
REMARK   3      S31:  -0.0389 S32:   0.1335 S33:   0.0508                       
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   140        A   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6649 -21.5977  18.2146              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1023 T22:   0.0836                                     
REMARK   3      T33:  -0.1519 T12:  -0.0200                                     
REMARK   3      T13:  -0.0055 T23:   0.0374                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7906 L22:   5.8843                                     
REMARK   3      L33:   3.3087 L12:  -4.2363                                     
REMARK   3      L13:  -4.9414 L23:   3.8098                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1089 S12:  -1.3816 S13:  -0.5398                       
REMARK   3      S21:   0.5952 S22:  -0.5098 S23:   0.0918                       
REMARK   3      S31:   0.3805 S32:  -0.2499 S33:   0.6186                       
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   168        A   233                          
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6433 -21.4774   2.2566              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0253 T22:  -0.4061                                     
REMARK   3      T33:  -0.0556 T12:   0.0380                                     
REMARK   3      T13:   0.0316 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8052 L22:   2.0844                                     
REMARK   3      L33:   2.3071 L12:   0.0652                                     
REMARK   3      L13:   0.3168 L23:  -0.0796                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0359 S12:  -0.0398 S13:  -0.6132                       
REMARK   3      S21:   0.3447 S22:  -0.0360 S23:   0.3107                       
REMARK   3      S31:   0.1425 S32:  -0.1474 S33:   0.0719                       
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     0        B   139                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8369  -5.2038  37.6658              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0041 T22:   0.3560                                     
REMARK   3      T33:  -0.0900 T12:  -0.0288                                     
REMARK   3      T13:   0.0627 T23:  -0.2763                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7521 L22:   1.9253                                     
REMARK   3      L33:   6.3448 L12:   2.5833                                     
REMARK   3      L13:   0.8507 L23:  -0.5205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2307 S12:  -1.1371 S13:   0.5136                       
REMARK   3      S21:   0.3074 S22:  -0.5003 S23:   0.2806                       
REMARK   3      S31:   0.0360 S32:  -0.4146 S33:   0.2696                       
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   140        B   167                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.3831 -23.1864  11.8913              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0587 T22:   0.0063                                     
REMARK   3      T33:  -0.0054 T12:  -0.1350                                     
REMARK   3      T13:   0.0309 T23:   0.1132                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7204 L22:   4.8447                                     
REMARK   3      L33:  10.1428 L12:  -2.8870                                     
REMARK   3      L13:  -4.1773 L23:   7.0099                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2619 S12:  -1.2881 S13:  -0.3752                       
REMARK   3      S21:  -0.2345 S22:  -0.4269 S23:  -0.0092                       
REMARK   3      S31:   0.0920 S32:   0.1062 S33:   0.1650                       
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   168        B   232                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1352 -15.2258  29.4847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0818 T22:   0.2606                                     
REMARK   3      T33:  -0.0863 T12:  -0.0387                                     
REMARK   3      T13:   0.0430 T23:  -0.1047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.3832 L22:   0.6641                                     
REMARK   3      L33:   3.6594 L12:   1.0827                                     
REMARK   3      L13:  -0.0290 L23:   0.7264                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1309 S12:  -1.1552 S13:  -0.4994                       
REMARK   3      S21:   0.1625 S22:  -0.1439 S23:  -0.0580                       
REMARK   3      S31:   0.5888 S32:  -0.2643 S33:   0.2749                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 2VSI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290036022.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 140                                
REMARK 200  PH                             : 6.75                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU R-AXIS                      
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU IMAGE PLATE                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 14243                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1VPA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES PH 6.75 35 % V/W PEG 300    
REMARK 280  200 MM CACL2                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       71.79000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       71.79000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       40.47000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.19000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       40.47000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.19000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       71.79000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       40.47000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.19000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       71.79000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       40.47000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       46.19000            
REMARK 290   SMTRY3   8  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: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 3470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24230 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.9 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     GLY A    12                                                      
REMARK 465     THR A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     MET A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     ASP A   235                                                      
REMARK 465     ARG B    14                                                      
REMARK 465     MET B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     ILE B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     GLU B   233                                                      
REMARK 465     LYS B   234                                                      
REMARK 465     ASP B   235                                                      
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    ARG B 100   CZ    ARG B 100   NH1     0.088                       
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 B 100   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 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    SER A 149      107.90   -160.15                                   
REMARK 500    GLN A 168     -169.84   -126.99                                   
REMARK 500    ASN A 216       46.11    -68.99                                   
REMARK 500    ALA B   8       36.69   -142.82                                   
REMARK 500    PRO B  21      138.95    -32.43                                   
REMARK 500    ASP B  29      -28.93   -141.92                                   
REMARK 500    GLU B  47      -78.92    -50.47                                   
REMARK 500    TYR B  72       30.43    -82.97                                   
REMARK 500    PRO B 101      130.12    -37.94                                   
REMARK 500    PRO B 104      -23.58    -38.69                                   
REMARK 500    PHE B 117       32.09    -96.87                                   
REMARK 500    ASP B 157      133.84    177.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN               
REMARK 700 ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW,          
REMARK 700 TWO SHEETS ARE DEFINED.                                              
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDF A1234                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CDF B1233                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B1234                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VSH   RELATED DB: PDB                                   
REMARK 900 SYNTHESIS OF CDP-ACTIVATED RIBITOL FOR TEICHOIC ACID PRECURSORS IN   
REMARK 900 STREPTOCOCCUS PNEUMONIAE                                             
DBREF  2VSI A    0     0  PDB    2VSI     2VSI             0      0             
DBREF  2VSI A    1   235  UNP    A5MSS9   A5MSS9_STRPN     1    235             
DBREF  2VSI B    0     0  PDB    2VSI     2VSI             0      0             
DBREF  2VSI B    1   235  UNP    A5MSS9   A5MSS9_STRPN     1    235             
SEQRES   1 A  236  HIS MET ILE TYR ALA GLY ILE LEU ALA GLY GLY THR GLY          
SEQRES   2 A  236  THR ARG MET GLY ILE SER ASN LEU PRO LYS GLN PHE LEU          
SEQRES   3 A  236  GLU LEU GLY ASP ARG PRO ILE LEU ILE HIS THR ILE GLU          
SEQRES   4 A  236  LYS PHE VAL LEU GLU PRO SER ILE GLU LYS ILE VAL VAL          
SEQRES   5 A  236  GLY VAL HIS GLY ASP TRP VAL SER HIS ALA GLU ASP LEU          
SEQRES   6 A  236  VAL ASP LYS TYR LEU PRO LEU TYR LYS GLU ARG ILE ILE          
SEQRES   7 A  236  ILE THR LYS GLY GLY ALA ASP ARG ASN THR SER ILE LYS          
SEQRES   8 A  236  ASN ILE ILE GLU ALA ILE ASP ALA TYR ARG PRO LEU THR          
SEQRES   9 A  236  PRO GLU ASP ILE VAL VAL THR HIS ASP SER VAL ARG PRO          
SEQRES  10 A  236  PHE ILE THR LEU ARG MET ILE GLN ASP ASN ILE GLN LEU          
SEQRES  11 A  236  ALA GLN ASN HIS ASP ALA VAL ASP THR VAL VAL GLU ALA          
SEQRES  12 A  236  VAL ASP THR ILE VAL GLU SER THR ASN GLY GLN PHE ILE          
SEQRES  13 A  236  THR ASP ILE PRO ASN ARG ALA HIS LEU TYR GLN GLY GLN          
SEQRES  14 A  236  THR PRO GLN THR PHE ARG CYS LYS ASP PHE MET ASP LEU          
SEQRES  15 A  236  TYR GLY SER LEU SER ASP GLU GLU LYS GLU ILE LEU THR          
SEQRES  16 A  236  ASP ALA CYS LYS ILE PHE VAL ILE LYS GLY LYS ASP VAL          
SEQRES  17 A  236  ALA LEU ALA LYS GLY GLU TYR SER ASN LEU LYS ILE THR          
SEQRES  18 A  236  THR VAL THR ASP LEU LYS ILE ALA LYS SER MET ILE GLU          
SEQRES  19 A  236  LYS ASP                                                      
SEQRES   1 B  236  HIS MET ILE TYR ALA GLY ILE LEU ALA GLY GLY THR GLY          
SEQRES   2 B  236  THR ARG MET GLY ILE SER ASN LEU PRO LYS GLN PHE LEU          
SEQRES   3 B  236  GLU LEU GLY ASP ARG PRO ILE LEU ILE HIS THR ILE GLU          
SEQRES   4 B  236  LYS PHE VAL LEU GLU PRO SER ILE GLU LYS ILE VAL VAL          
SEQRES   5 B  236  GLY VAL HIS GLY ASP TRP VAL SER HIS ALA GLU ASP LEU          
SEQRES   6 B  236  VAL ASP LYS TYR LEU PRO LEU TYR LYS GLU ARG ILE ILE          
SEQRES   7 B  236  ILE THR LYS GLY GLY ALA ASP ARG ASN THR SER ILE LYS          
SEQRES   8 B  236  ASN ILE ILE GLU ALA ILE ASP ALA TYR ARG PRO LEU THR          
SEQRES   9 B  236  PRO GLU ASP ILE VAL VAL THR HIS ASP SER VAL ARG PRO          
SEQRES  10 B  236  PHE ILE THR LEU ARG MET ILE GLN ASP ASN ILE GLN LEU          
SEQRES  11 B  236  ALA GLN ASN HIS ASP ALA VAL ASP THR VAL VAL GLU ALA          
SEQRES  12 B  236  VAL ASP THR ILE VAL GLU SER THR ASN GLY GLN PHE ILE          
SEQRES  13 B  236  THR ASP ILE PRO ASN ARG ALA HIS LEU TYR GLN GLY GLN          
SEQRES  14 B  236  THR PRO GLN THR PHE ARG CYS LYS ASP PHE MET ASP LEU          
SEQRES  15 B  236  TYR GLY SER LEU SER ASP GLU GLU LYS GLU ILE LEU THR          
SEQRES  16 B  236  ASP ALA CYS LYS ILE PHE VAL ILE LYS GLY LYS ASP VAL          
SEQRES  17 B  236  ALA LEU ALA LYS GLY GLU TYR SER ASN LEU LYS ILE THR          
SEQRES  18 B  236  THR VAL THR ASP LEU LYS ILE ALA LYS SER MET ILE GLU          
SEQRES  19 B  236  LYS ASP                                                      
HET    CDF  A1234      25                                                       
HET    CDF  B1233      25                                                       
HET     CA  B1234       1                                                       
HETNAM     CDF 4-AMINO-1-{5-O-[(R)-HYDROXY(PHOSPHONOOXY)PHOSPHORYL]-            
HETNAM   2 CDF  ALPHA-D-ARABINOFURANOSYL}PYRIMIDIN-2(1H)-ONE                    
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  CDF    2(C9 H15 N3 O11 P2)                                          
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  HOH   *10(H2 O)                                                     
HELIX    1   1 PRO A   21  PHE A   24  5                                   4    
HELIX    2   2 ILE A   32  LEU A   42  1                                  11    
HELIX    3   3 TRP A   57  LEU A   69  1                                  13    
HELIX    4   4 PRO A   70  GLU A   74  5                                   5    
HELIX    5   5 ASP A   84  ARG A  100  1                                  17    
HELIX    6   6 THR A  119  ALA A  130  1                                  12    
HELIX    7   7 CYS A  175  TYR A  182  1                                   8    
HELIX    8   8 SER A  186  LEU A  193  1                                   8    
HELIX    9   9 ASP A  195  LYS A  203  1                                   9    
HELIX   10  10 THR A  221  ILE A  232  1                                  12    
HELIX   11  11 ILE B   32  GLU B   43  1                                  12    
HELIX   12  12 HIS B   54  ASP B   56  5                                   3    
HELIX   13  13 TRP B   57  LEU B   69  1                                  13    
HELIX   14  14 PRO B   70  GLU B   74  5                                   5    
HELIX   15  15 ASP B   84  ARG B  100  1                                  17    
HELIX   16  16 THR B  119  GLN B  131  1                                  13    
HELIX   17  17 ASN B  160  ALA B  162  5                                   3    
HELIX   18  18 CYS B  175  LEU B  185  1                                  11    
HELIX   19  19 GLU B  188  LEU B  193  1                                   6    
HELIX   20  20 ASP B  195  LYS B  203  1                                   9    
HELIX   21  21 THR B  221  ILE B  232  1                                  12    
SHEET    1  AA 7 ILE A  76  LYS A  80  0                                        
SHEET    2  AA 7 ILE A  49  VAL A  53  1  O  ILE A  49   N  ILE A  77           
SHEET    3  AA 7 ILE A   2  ALA A   8  1  O  ALA A   4   N  VAL A  50           
SHEET    4  AA 7 ILE A 107  ASP A 112  1  O  ILE A 107   N  TYR A   3           
SHEET    5  AA 7 LEU A 164  ARG A 174 -1  O  GLN A 171   N  THR A 110           
SHEET    6  AA 7 ALA A 135  GLU A 141 -1  O  VAL A 136   N  THR A 172           
SHEET    7  AA 7 VAL A 207  LYS A 211  1  O  ALA A 208   N  ASP A 137           
SHEET    1  AB 6 ILE A  76  LYS A  80  0                                        
SHEET    2  AB 6 ILE A  49  VAL A  53  1  O  ILE A  49   N  ILE A  77           
SHEET    3  AB 6 ILE A   2  ALA A   8  1  O  ALA A   4   N  VAL A  50           
SHEET    4  AB 6 ILE A 107  ASP A 112  1  O  ILE A 107   N  TYR A   3           
SHEET    5  AB 6 LEU A 164  ARG A 174 -1  O  GLN A 171   N  THR A 110           
SHEET    6  AB 6 ILE B 146  GLU B 148 -1  O  VAL B 147   N  TYR A 165           
SHEET    1  AC 2 GLU A  26  LEU A  27  0                                        
SHEET    2  AC 2 ARG A  30  PRO A  31 -1  O  ARG A  30   N  LEU A  27           
SHEET    1  AD 6 ILE A 146  GLU A 148  0                                        
SHEET    2  AD 6 LEU B 164  ARG B 174 -1  O  TYR B 165   N  VAL A 147           
SHEET    3  AD 6 ILE B 107  ASP B 112 -1  O  VAL B 108   N  PHE B 173           
SHEET    4  AD 6 ILE B   2  LEU B   7  1  O  TYR B   3   N  VAL B 109           
SHEET    5  AD 6 ILE B  49  VAL B  53  1  O  VAL B  50   N  ILE B   6           
SHEET    6  AD 6 ILE B  76  LYS B  80  1  O  ILE B  77   N  VAL B  51           
SHEET    1  AE 4 ILE A 146  GLU A 148  0                                        
SHEET    2  AE 4 LEU B 164  ARG B 174 -1  O  TYR B 165   N  VAL A 147           
SHEET    3  AE 4 ALA B 135  GLU B 141 -1  O  VAL B 136   N  THR B 172           
SHEET    4  AE 4 VAL B 207  LYS B 211  1  O  ALA B 208   N  ASP B 137           
SHEET    1  BA 2 GLU B  26  LEU B  27  0                                        
SHEET    2  BA 2 ARG B  30  PRO B  31 -1  O  ARG B  30   N  LEU B  27           
LINK         OE2 GLU B 105                CA    CA B1234     1555   1555  2.80  
CISPEP   1 THR A  169    PRO A  170          0         8.65                     
CISPEP   2 THR B  169    PRO B  170          0         5.43                     
SITE     1 AC1 13 LEU A   7  ALA A   8  GLY A   9  GLY A  10                    
SITE     2 AC1 13 GLY A  82  ALA A  83  ASP A  84  ARG A  85                    
SITE     3 AC1 13 SER A  88  ASP A 112  SER A 113  VAL A 114                    
SITE     4 AC1 13 LYS A 218                                                     
SITE     1 AC2 14 LEU B   7  ALA B   8  GLY B   9  GLN B  23                    
SITE     2 AC2 14 GLY B  82  ALA B  83  ASP B  84  ARG B  85                    
SITE     3 AC2 14 SER B  88  ASP B 112  SER B 113  VAL B 114                    
SITE     4 AC2 14 LYS B 218  THR B 220                                          
SITE     1 AC3  1 GLU B 105                                                     
CRYST1   80.940   92.380  143.580  90.00  90.00  90.00 C 2 2 21     16          
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      0.012355  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010825  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006965        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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