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Database: PDB
Entry: 1TVF
LinkDB: 1TVF
Original site: 1TVF 
HEADER    PENICILLIN BINDING                      29-JUN-04   1TVF              
TITLE     CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 4 (PBP4) FROM         
TITLE    2 STAPHYLOCOCCUS AUREUS                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PENICILLIN BINDING PROTEIN 4;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PBP4;                                                       
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 GENE: PBP4;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21DE3;                                   
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET T7                                    
KEYWDS    STRUCTURAL GENOMICS, NYSGXRC TARGET, T72, PBP4, SAV0642, SA0598, PSI, 
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX RESEARCH CENTER FOR       
KEYWDS   3 STRUCTURAL GENOMICS, PENICILLIN BINDING                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.R.RAJASHANKAR,S.S.RAY,J.B.BONANNO,M.PINHO,A.TOMASZ,S.K.BURLEY,NEW   
AUTHOR   2 YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)           
REVDAT   6   23-AUG-23 1TVF    1       REMARK                                   
REVDAT   5   03-FEB-21 1TVF    1       AUTHOR JRNL   REMARK SEQADV              
REVDAT   4   24-FEB-09 1TVF    1       VERSN                                    
REVDAT   3   05-APR-05 1TVF    1       AUTHOR JRNL                              
REVDAT   2   25-JAN-05 1TVF    1       AUTHOR KEYWDS REMARK                     
REVDAT   1   06-JUL-04 1TVF    0                                                
JRNL        AUTH   K.R.RAJASHANKAR,S.S.RAY,J.B.BONANNO,M.PINHO,A.TOMASZ,        
JRNL        AUTH 2 S.K.BURLEY                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF PENICILLIN-BINDING PROTEIN 4 (PBP4)     
JRNL        TITL 2 FROM STAPHYLOCOCCUS AUREUS                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.68                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 425919.560                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 67366                          
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 SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3423                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.003                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.13                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10502                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1870                       
REMARK   3   BIN FREE R VALUE                    : 0.2280                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 548                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5796                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 781                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 9.50                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.66000                                             
REMARK   3    B22 (A**2) : 2.23000                                              
REMARK   3    B33 (A**2) : 1.43000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.11                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.15                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.024                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.370                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.280 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.810 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.250 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.090 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 54.87                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : CIS_PEPTIDE.PARAM                              
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: UNIDENTIFIED ELECTRON DENSITY IS          
REMARK   3  OBSERVED NEAR THE ACTIVE SITE.                                      
REMARK   4                                                                      
REMARK   4 1TVF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JUN-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022939.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-OCT-01; NULL                    
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : NSLS; NSLS                         
REMARK 200  BEAMLINE                       : X9A; X9A                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98; 1.25                         
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111);         
REMARK 200                                   SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL                          
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH; NULL                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67865                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.1000                            
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) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.19600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS, MOLECULAR             
REMARK 200  REPLACEMENT                                                         
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: ARP/WARP AUTOBUILT MODEL USING PHASES FROM TWO       
REMARK 200  TA6BR12 CLUSTERS AND A POOR MOLECULAR REPLACEMENT SOLUTION. MR      
REMARK 200  WAS CARRIED OUT USING A MODEL DERIVED FROM PDB ENTRY 1HD8, WHICH    
REMARK 200  IS A MUTANT OF PBP5, SHARING ~26% IDENTITY WITH PBP4 OVER A 245     
REMARK 200  RESIDUE RANGE. PHASE COMBINATION WITH MR SOLUTION WAS NECESSARY,    
REMARK 200  AS TA6BR12 CLUSTERS OCCUPIED POSITIONS ON THE SYMMETRY PLANES       
REMARK 200  RESULTING IN CENTROSYMMETRIC PHASES AND HENCE UNINTERPRETABLE       
REMARK 200  MAPS.                                                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG 4000, 100MM CITRATE BUFFER,      
REMARK 280  200MM AMMONIUM SULFATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       24.35650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.88750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.09450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.88750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.35650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.09450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 300 REMARK: EACH MONOMER SEEM TO FORM A BIOLOGICAL UNIT.                 
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   984     O    HOH A  1106              2.13            
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    ASP B 130   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B 197   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  25       42.36    -71.38                                   
REMARK 500    TYR A  38       46.52   -107.20                                   
REMARK 500    TYR A  40       43.30    -61.07                                   
REMARK 500    ALA A  74     -132.06     49.99                                   
REMARK 500    ASN A 117      167.45    177.79                                   
REMARK 500    ARG A 188     -127.20     54.60                                   
REMARK 500    ALA A 230       59.88   -155.29                                   
REMARK 500    SER A 251      120.60    -37.70                                   
REMARK 500    LEU A 258      -60.84   -131.13                                   
REMARK 500    ASN A 267     -141.75     55.27                                   
REMARK 500    LEU A 294      -49.94   -178.23                                   
REMARK 500    ASP A 358       65.45     31.71                                   
REMARK 500    ASN A 371     -179.31   -171.77                                   
REMARK 500    THR B  25       41.84    -75.86                                   
REMARK 500    ALA B  74     -135.80     53.10                                   
REMARK 500    GLU B 114       -1.59     69.47                                   
REMARK 500    ASN B 117      169.83    177.09                                   
REMARK 500    ARG B 188     -119.03     50.00                                   
REMARK 500    ALA B 230       62.86   -163.00                                   
REMARK 500    SER B 251      124.06    -38.22                                   
REMARK 500    LEU B 258      -56.55   -129.50                                   
REMARK 500    ASN B 267     -142.71     54.99                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 208         0.08    SIDE CHAIN                              
REMARK 500    TYR B 208         0.07    SIDE CHAIN                              
REMARK 500    TYR B 291         0.08    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 801                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 802                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 803                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 804                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 805                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL A 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE UNL B 901                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-T72   RELATED DB: TARGETDB                       
DBREF  1TVF A   21   383  UNP    Q53613   Q53613_STAAU    21    383             
DBREF  1TVF B   21   383  UNP    Q53613   Q53613_STAAU    21    383             
SEQADV 1TVF GLY A   15  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF PRO A   16  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF HIS A   17  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF THR A   18  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF SER A   19  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF SER A   20  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF GLY B   15  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF PRO B   16  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF HIS B   17  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF THR B   18  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF SER B   19  UNP  Q53613              CLONING ARTIFACT               
SEQADV 1TVF SER B   20  UNP  Q53613              CLONING ARTIFACT               
SEQRES   1 A  369  GLY PRO HIS THR SER SER TYR ALA GLN ALA THR ASN SER          
SEQRES   2 A  369  ASP VAL THR PRO VAL GLN ALA ALA ASN GLN TYR GLY TYR          
SEQRES   3 A  369  ALA GLY LEU SER ALA ALA TYR GLU PRO THR SER ALA VAL          
SEQRES   4 A  369  ASN VAL SER GLN THR GLY GLN LEU LEU TYR GLN TYR ASN          
SEQRES   5 A  369  ILE ASP THR LYS TRP ASN PRO ALA SER MET THR LYS LEU          
SEQRES   6 A  369  MET THR MET TYR LEU THR LEU GLU ALA VAL ASN LYS GLY          
SEQRES   7 A  369  GLN LEU SER LEU ASP ASP THR VAL THR MET THR ASN LYS          
SEQRES   8 A  369  GLU TYR ILE MET SER THR LEU PRO GLU LEU SER ASN THR          
SEQRES   9 A  369  LYS LEU TYR PRO GLY GLN VAL TRP THR ILE ALA ASP LEU          
SEQRES  10 A  369  LEU GLN ILE THR VAL SER ASN SER SER ASN ALA ALA ALA          
SEQRES  11 A  369  LEU ILE LEU ALA LYS LYS VAL SER LYS ASN THR SER ASP          
SEQRES  12 A  369  PHE VAL ASP LEU MET ASN ASN LYS ALA LYS ALA ILE GLY          
SEQRES  13 A  369  MET LYS ASN THR HIS PHE VAL ASN PRO THR GLY ALA GLU          
SEQRES  14 A  369  ASN SER ARG LEU ARG SER PHE ALA PRO THR LYS TYR LYS          
SEQRES  15 A  369  ASP GLN GLU ARG THR VAL THR THR ALA ARG ASP TYR ALA          
SEQRES  16 A  369  ILE LEU ASP LEU HIS VAL ILE LYS GLU THR PRO LYS ILE          
SEQRES  17 A  369  LEU ASP PHE THR LYS GLN LEU ALA PRO THR THR HIS ALA          
SEQRES  18 A  369  VAL THR TYR TYR THR PHE ASN PHE SER LEU GLU GLY ALA          
SEQRES  19 A  369  LYS MET SER LEU PRO GLY THR ASP GLY LEU LYS THR GLY          
SEQRES  20 A  369  SER SER ASP THR ALA ASN TYR ASN HIS THR ILE THR THR          
SEQRES  21 A  369  LYS ARG GLY LYS PHE ARG ILE ASN GLN VAL ILE MET GLY          
SEQRES  22 A  369  ALA GLY ASP TYR LYS ASN LEU GLY GLY GLU LYS GLN ARG          
SEQRES  23 A  369  ASN MET MET GLY ASN ALA LEU MET GLU ARG SER PHE ASP          
SEQRES  24 A  369  GLN TYR LYS TYR VAL LYS ILE LEU SER LYS GLY GLU GLN          
SEQRES  25 A  369  ARG ILE ASN GLY LYS LYS TYR TYR VAL GLU ASN ASP LEU          
SEQRES  26 A  369  TYR ASP VAL LEU PRO SER ASP PHE SER LYS LYS ASP TYR          
SEQRES  27 A  369  LYS LEU VAL VAL GLU ASP GLY LYS VAL HIS ALA ASP TYR          
SEQRES  28 A  369  PRO ARG GLU PHE ILE ASN LYS ASP TYR GLY PRO PRO THR          
SEQRES  29 A  369  VAL GLU VAL HIS GLN                                          
SEQRES   1 B  369  GLY PRO HIS THR SER SER TYR ALA GLN ALA THR ASN SER          
SEQRES   2 B  369  ASP VAL THR PRO VAL GLN ALA ALA ASN GLN TYR GLY TYR          
SEQRES   3 B  369  ALA GLY LEU SER ALA ALA TYR GLU PRO THR SER ALA VAL          
SEQRES   4 B  369  ASN VAL SER GLN THR GLY GLN LEU LEU TYR GLN TYR ASN          
SEQRES   5 B  369  ILE ASP THR LYS TRP ASN PRO ALA SER MET THR LYS LEU          
SEQRES   6 B  369  MET THR MET TYR LEU THR LEU GLU ALA VAL ASN LYS GLY          
SEQRES   7 B  369  GLN LEU SER LEU ASP ASP THR VAL THR MET THR ASN LYS          
SEQRES   8 B  369  GLU TYR ILE MET SER THR LEU PRO GLU LEU SER ASN THR          
SEQRES   9 B  369  LYS LEU TYR PRO GLY GLN VAL TRP THR ILE ALA ASP LEU          
SEQRES  10 B  369  LEU GLN ILE THR VAL SER ASN SER SER ASN ALA ALA ALA          
SEQRES  11 B  369  LEU ILE LEU ALA LYS LYS VAL SER LYS ASN THR SER ASP          
SEQRES  12 B  369  PHE VAL ASP LEU MET ASN ASN LYS ALA LYS ALA ILE GLY          
SEQRES  13 B  369  MET LYS ASN THR HIS PHE VAL ASN PRO THR GLY ALA GLU          
SEQRES  14 B  369  ASN SER ARG LEU ARG SER PHE ALA PRO THR LYS TYR LYS          
SEQRES  15 B  369  ASP GLN GLU ARG THR VAL THR THR ALA ARG ASP TYR ALA          
SEQRES  16 B  369  ILE LEU ASP LEU HIS VAL ILE LYS GLU THR PRO LYS ILE          
SEQRES  17 B  369  LEU ASP PHE THR LYS GLN LEU ALA PRO THR THR HIS ALA          
SEQRES  18 B  369  VAL THR TYR TYR THR PHE ASN PHE SER LEU GLU GLY ALA          
SEQRES  19 B  369  LYS MET SER LEU PRO GLY THR ASP GLY LEU LYS THR GLY          
SEQRES  20 B  369  SER SER ASP THR ALA ASN TYR ASN HIS THR ILE THR THR          
SEQRES  21 B  369  LYS ARG GLY LYS PHE ARG ILE ASN GLN VAL ILE MET GLY          
SEQRES  22 B  369  ALA GLY ASP TYR LYS ASN LEU GLY GLY GLU LYS GLN ARG          
SEQRES  23 B  369  ASN MET MET GLY ASN ALA LEU MET GLU ARG SER PHE ASP          
SEQRES  24 B  369  GLN TYR LYS TYR VAL LYS ILE LEU SER LYS GLY GLU GLN          
SEQRES  25 B  369  ARG ILE ASN GLY LYS LYS TYR TYR VAL GLU ASN ASP LEU          
SEQRES  26 B  369  TYR ASP VAL LEU PRO SER ASP PHE SER LYS LYS ASP TYR          
SEQRES  27 B  369  LYS LEU VAL VAL GLU ASP GLY LYS VAL HIS ALA ASP TYR          
SEQRES  28 B  369  PRO ARG GLU PHE ILE ASN LYS ASP TYR GLY PRO PRO THR          
SEQRES  29 B  369  VAL GLU VAL HIS GLN                                          
HET    SO4  A 801       5                                                       
HET    SO4  A 802       5                                                       
HET    SO4  A 803       5                                                       
HET    UNL  A 900       9                                                       
HET    SO4  B 804       5                                                       
HET    SO4  B 805       5                                                       
HET    UNL  B 901       9                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     UNL UNKNOWN LIGAND                                                   
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL  10  HOH   *781(H2 O)                                                    
HELIX    1   1 GLY A   15  ALA A   22  1                                   8    
HELIX    2   2 THR A   30  TYR A   38  1                                   9    
HELIX    3   3 SER A   44  GLU A   48  5                                   5    
HELIX    4   4 PRO A   73  SER A   75  5                                   3    
HELIX    5   5 MET A   76  LYS A   91  1                                  16    
HELIX    6   6 THR A  103  SER A  110  1                                   8    
HELIX    7   7 ILE A  128  ASN A  138  1                                  11    
HELIX    8   8 SER A  140  SER A  152  1                                  13    
HELIX    9   9 ASN A  154  ILE A  169  1                                  16    
HELIX   10  10 GLU A  183  ARG A  188  1                                   6    
HELIX   11  11 SER A  189  ALA A  191  5                                   3    
HELIX   12  12 PRO A  192  LYS A  196  5                                   5    
HELIX   13  13 THR A  204  THR A  219  1                                  16    
HELIX   14  14 LYS A  221  LYS A  227  1                                   7    
HELIX   15  15 GLY A  296  GLN A  314  1                                  19    
HELIX   16  16 SER A  348  TYR A  352  5                                   5    
HELIX   17  17 GLY B   15  TYR B   21  1                                   7    
HELIX   18  18 THR B   30  GLY B   39  1                                  10    
HELIX   19  19 SER B   44  GLU B   48  5                                   5    
HELIX   20  20 PRO B   73  SER B   75  5                                   3    
HELIX   21  21 MET B   76  LYS B   91  1                                  16    
HELIX   22  22 THR B  103  SER B  110  1                                   8    
HELIX   23  23 ILE B  128  ASN B  138  1                                  11    
HELIX   24  24 SER B  140  SER B  152  1                                  13    
HELIX   25  25 ASN B  154  GLY B  170  1                                  17    
HELIX   26  26 GLU B  183  ARG B  188  1                                   6    
HELIX   27  27 SER B  189  ALA B  191  5                                   3    
HELIX   28  28 PRO B  192  LYS B  196  5                                   5    
HELIX   29  29 THR B  204  THR B  219  1                                  16    
HELIX   30  30 LYS B  221  LYS B  227  1                                   7    
HELIX   31  31 GLY B  296  GLN B  314  1                                  19    
HELIX   32  32 SER B  348  TYR B  352  5                                   5    
SHEET    1   A 5 LEU A  61  TYR A  65  0                                        
SHEET    2   A 5 SER A  51  SER A  56 -1  N  ASN A  54   O  LEU A  62           
SHEET    3   A 5 PHE A 279  ALA A 288 -1  O  ASN A 282   N  VAL A  55           
SHEET    4   A 5 ASN A 267  ARG A 276 -1  N  ILE A 272   O  GLN A 283           
SHEET    5   A 5 THR A 255  SER A 263 -1  N  GLY A 261   O  ASN A 269           
SHEET    1   B 2 THR A  99  THR A 101  0                                        
SHEET    2   B 2 VAL A 125  THR A 127 -1  O  TRP A 126   N  VAL A 100           
SHEET    1   C 2 THR A 232  THR A 233  0                                        
SHEET    2   C 2 VAL A 236  THR A 237 -1  O  VAL A 236   N  THR A 233           
SHEET    1   D 2 TYR A 315  LEU A 321  0                                        
SHEET    2   D 2 LEU A 339  PRO A 344 -1  O  LEU A 339   N  ILE A 320           
SHEET    1   E 5 GLY A 324  ILE A 328  0                                        
SHEET    2   E 5 LYS A 331  VAL A 335 -1  O  VAL A 335   N  GLY A 324           
SHEET    3   E 5 VAL A 379  HIS A 382 -1  O  HIS A 382   N  TYR A 334           
SHEET    4   E 5 LYS A 360  ASP A 364 -1  N  VAL A 361   O  VAL A 379           
SHEET    5   E 5 LYS A 353  GLU A 357 -1  N  VAL A 355   O  HIS A 362           
SHEET    1   F 5 LEU B  61  TYR B  65  0                                        
SHEET    2   F 5 SER B  51  SER B  56 -1  N  ASN B  54   O  LEU B  62           
SHEET    3   F 5 PHE B 279  ALA B 288 -1  O  ASN B 282   N  VAL B  55           
SHEET    4   F 5 ASN B 267  ARG B 276 -1  N  TYR B 268   O  ALA B 288           
SHEET    5   F 5 THR B 255  SER B 263 -1  N  GLY B 261   O  ASN B 269           
SHEET    1   G 2 THR B  99  THR B 101  0                                        
SHEET    2   G 2 VAL B 125  THR B 127 -1  O  TRP B 126   N  VAL B 100           
SHEET    1   H 2 THR B 232  THR B 233  0                                        
SHEET    2   H 2 VAL B 236  THR B 237 -1  O  VAL B 236   N  THR B 233           
SHEET    1   I 2 TYR B 315  LEU B 321  0                                        
SHEET    2   I 2 LEU B 339  PRO B 344 -1  O  LEU B 339   N  ILE B 320           
SHEET    1   J 5 GLY B 324  ILE B 328  0                                        
SHEET    2   J 5 LYS B 331  VAL B 335 -1  O  LYS B 331   N  ILE B 328           
SHEET    3   J 5 VAL B 379  HIS B 382 -1  O  HIS B 382   N  TYR B 334           
SHEET    4   J 5 LYS B 360  ASP B 364 -1  N  VAL B 361   O  VAL B 379           
SHEET    5   J 5 LYS B 353  GLU B 357 -1  N  VAL B 355   O  HIS B 362           
CISPEP   1 GLY A  257    LEU A  258          0         2.31                     
CISPEP   2 GLY B  257    LEU B  258          0         0.51                     
SITE     1 AC1  7 ASN A 154  THR A 155  SER A 156  PRO A 192                    
SITE     2 AC1  7 THR A 193  HOH A1031  HOH A1196                               
SITE     1 AC2  8 GLN A 124  VAL A 125  LYS A 172  HIS A 234                    
SITE     2 AC2  8 HOH A1023  HOH A1129  HOH A1224  HOH A1227                    
SITE     1 AC3  6 ASP A 197  GLN A 198  GLU A 199  ARG A 200                    
SITE     2 AC3  6 HOH A1061  HOH A1230                                          
SITE     1 AC4  3 GLN B 198  GLU B 199  ARG B 200                               
SITE     1 AC5  8 GLN B 124  VAL B 125  LYS B 172  HIS B 234                    
SITE     2 AC5  8 HOH B1111  HOH B1262  HOH B1272  HOH B1285                    
SITE     1 AC6 14 GLY A  15  PRO A  16  HIS A  17  THR A  18                    
SITE     2 AC6 14 SER A  75  SER A 116  SER A 139  PHE A 241                    
SITE     3 AC6 14 THR A 260  GLY A 261  SER A 262  HOH A 941                    
SITE     4 AC6 14 HOH A 996  HOH A1048                                          
SITE     1 AC7 14 GLY B  15  PRO B  16  HIS B  17  THR B  18                    
SITE     2 AC7 14 SER B  75  SER B 116  SER B 139  PHE B 241                    
SITE     3 AC7 14 THR B 260  GLY B 261  SER B 262  HOH B 910                    
SITE     4 AC7 14 HOH B 963  HOH B1042                                          
CRYST1   48.713  140.189  145.775  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.020528  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006860        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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