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Database: PDB
Entry: 1NYC
LinkDB: 1NYC
Original site: 1NYC 
HEADER    HYDROLASE INHIBITOR                     12-FEB-03   1NYC              
TITLE     STAPHOSTATINS RESEMBLE LIPOCALINS, NOT CYSTATINS IN FOLD.             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYSTEINE PROTEASE INHIBITOR;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: STAPHOSTATIN B;                                             
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;            
SOURCE   3 ORGANISM_TAXID: 196620;                                              
SOURCE   4 STRAIN: MW2;                                                         
SOURCE   5 GENE: STAPHOSTATIN B (SSPC);                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)[PLYSS];                          
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-5T-SSPC                              
KEYWDS    STAPHOSTATIN B, SSPC, CYSTEINE PROTEASE INHIBITOR, HYDROLASE          
KEYWDS   2 INHIBITOR                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.RZYCHON,R.FILIPEK,A.SABAT,K.KOSOWSKA,A.DUBIN,J.POTEMPA,M.BOCHTLER   
REVDAT   4   13-JUL-11 1NYC    1       VERSN                                    
REVDAT   3   24-FEB-09 1NYC    1       VERSN                                    
REVDAT   2   23-DEC-03 1NYC    1       TITLE                                    
REVDAT   1   30-SEP-03 1NYC    0                                                
JRNL        AUTH   M.RZYCHON,R.FILIPEK,A.SABAT,K.KOSOWSKA,A.DUBIN,J.POTEMPA,    
JRNL        AUTH 2 M.BOCHTLER                                                   
JRNL        TITL   STAPHOSTATINS RESEMBLE LIPOCALINS, NOT CYSTATINS IN FOLD.    
JRNL        REF    PROTEIN SCI.                  V.  12  2252 2003              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   14500882                                                     
JRNL        DOI    10.1110/PS.03247703                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   I.MASSIMI,E.PARK,K.RICE,W.MUELLER-ESTERL,D.SAUDER,           
REMARK   1  AUTH 2 M. J.MCGAVIN                                                 
REMARK   1  TITL   IDENTIFICATION OF A NOVEL MATURATION MECHANISM AND           
REMARK   1  TITL 2 RESTRICTED SUBSTRATE SPECIFICITY FOR THE SSPB CYSTEINE       
REMARK   1  TITL 3 PROTEASE OF STAPHYLOCOCCUS AUREUS                            
REMARK   1  REF    J.BIOL.CHEM.                  V. 277 41770 2002              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  DOI    10.1074/JBC.M207162200                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.RZYCHON,A.SABAT,K.KOSOWSKA,J.POTEMPA,A.DUBIN               
REMARK   1  TITL   STAPHOSTATINS: AN EXPANDING NEW GROUP OF PROTEINASE          
REMARK   1  TITL 2 INHIBITORS WITH A UNIQUE SPECIFICITY FOR THE REGULATION OF   
REMARK   1  TITL 3 STAPHOPAINS, STAPHYLOCOCCUS SPP. CYSTEINE PROTEINASES.       
REMARK   1  REF    MOL.MICROBIOL.                V.  49  1051 2003              
REMARK   1  REFN                   ISSN 0950-382X                               
REMARK   1  DOI    10.1046/J.1365-2958.2003.03613.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 50616                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2661                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3632                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 197                          
REMARK   3   BIN FREE R VALUE                    : 0.3110                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1844                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 7                                       
REMARK   3   SOLVENT ATOMS            : 260                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.15000                                             
REMARK   3    B22 (A**2) : 1.19000                                              
REMARK   3    B33 (A**2) : -0.04000                                             
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): 0.064         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.065         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.960                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1872 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1602 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2534 ; 1.651 ; 1.911       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3740 ; 3.772 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   218 ; 5.722 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   280 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2070 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   384 ; 0.010 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   334 ; 0.233 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1806 ; 0.298 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   954 ; 0.116 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   170 ; 0.162 ; 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):    17 ; 0.217 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    62 ; 0.294 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    25 ; 0.174 ; 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):  1090 ; 1.186 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1778 ; 2.353 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   782 ; 3.480 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   756 ; 5.846 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1NYC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-FEB-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB018347.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-NOV-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.60                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.05                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 75079                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.18800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: MLPHARE                                               
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, SODIUM ACETATE, PEG    
REMARK 280  4000, GLYCEROL, MANGANESE CHLORIDE, PH 4.6, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 294K, PH 4.60                             
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       17.09800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.63550            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.52450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.63550            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.09800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.52450            
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 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 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     VAL A  109                                                       
REMARK 475     VAL B  109                                                       
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    VAL A 109   C     VAL A 109   OXT    -0.253                       
REMARK 500    VAL B 109   C     VAL B 109   OXT    -0.446                       
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    ASN A  72      101.71   -160.65                                   
REMARK 500    SER A  92     -159.93   -138.15                                   
REMARK 500    ASP B  46     -165.04   -161.04                                   
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 A 328        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH A 383        DISTANCE =  5.03 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 261                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 262                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 263                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SEQUENCE REPRESENTS THE V8 STRAIN SEQUENCE                       
REMARK 999 OF STAPHOSTATIN B. PLEASE REFER TO THE PRIMARY                       
REMARK 999 CITATION FOR FURTHER INFORMATION CONCERNING                          
REMARK 999 THE SEQUENCE DISCREPANCY.                                            
DBREF  1NYC A    1   109  UNP    Q7A189   SSPC_STAAW       1    109             
DBREF  1NYC B    1   109  UNP    Q7A189   SSPC_STAAW       1    109             
SEQADV 1NYC GLY A   -1  UNP  Q7A189              CLONING ARTIFACT               
SEQADV 1NYC SER A    0  UNP  Q7A189              CLONING ARTIFACT               
SEQADV 1NYC PHE A   70  UNP  Q7A189    ILE    70 SEE REMARK 999                 
SEQADV 1NYC GLY B   -1  UNP  Q7A189              CLONING ARTIFACT               
SEQADV 1NYC SER B    0  UNP  Q7A189              CLONING ARTIFACT               
SEQADV 1NYC PHE B   70  UNP  Q7A189    ILE    70 SEE REMARK 999                 
SEQRES   1 A  111  GLY SER MET TYR GLN LEU GLN PHE ILE ASN LEU VAL TYR          
SEQRES   2 A  111  ASP THR THR LYS LEU THR HIS LEU GLU GLN THR ASN ILE          
SEQRES   3 A  111  ASN LEU PHE ILE GLY ASN TRP SER ASN HIS GLN LEU GLN          
SEQRES   4 A  111  LYS SER ILE CYS ILE ARG HIS GLY ASP ASP THR SER HIS          
SEQRES   5 A  111  ASN GLN TYR HIS ILE LEU PHE ILE ASP THR ALA HIS GLN          
SEQRES   6 A  111  ARG ILE LYS PHE SER SER PHE ASP ASN GLU GLU ILE ILE          
SEQRES   7 A  111  TYR ILE LEU ASP TYR ASP ASP THR GLN HIS ILE LEU MET          
SEQRES   8 A  111  GLN THR SER SER LYS GLN GLY ILE GLY THR SER ARG PRO          
SEQRES   9 A  111  ILE VAL TYR GLU ARG LEU VAL                                  
SEQRES   1 B  111  GLY SER MET TYR GLN LEU GLN PHE ILE ASN LEU VAL TYR          
SEQRES   2 B  111  ASP THR THR LYS LEU THR HIS LEU GLU GLN THR ASN ILE          
SEQRES   3 B  111  ASN LEU PHE ILE GLY ASN TRP SER ASN HIS GLN LEU GLN          
SEQRES   4 B  111  LYS SER ILE CYS ILE ARG HIS GLY ASP ASP THR SER HIS          
SEQRES   5 B  111  ASN GLN TYR HIS ILE LEU PHE ILE ASP THR ALA HIS GLN          
SEQRES   6 B  111  ARG ILE LYS PHE SER SER PHE ASP ASN GLU GLU ILE ILE          
SEQRES   7 B  111  TYR ILE LEU ASP TYR ASP ASP THR GLN HIS ILE LEU MET          
SEQRES   8 B  111  GLN THR SER SER LYS GLN GLY ILE GLY THR SER ARG PRO          
SEQRES   9 B  111  ILE VAL TYR GLU ARG LEU VAL                                  
HET     CL  A 261       1                                                       
HET     CL  A 262       1                                                       
HET    SO4  A 263       5                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   5  SO4    O4 S 2-                                                      
FORMUL   6  HOH   *260(H2 O)                                                    
HELIX    1   1 ASP A   12  LEU A   16  5                                   5    
HELIX    2   2 THR A   17  LEU A   26  1                                  10    
HELIX    3   3 ASP B   12  LEU B   16  5                                   5    
HELIX    4   4 THR B   17  LEU B   26  1                                  10    
SHEET    1   A18 TYR A   2  VAL A  10  0                                        
SHEET    2   A18 LYS A  38  GLY A  45  1  O  CYS A  41   N  ILE A   7           
SHEET    3   A18 GLY A  29  ASN A  33 -1  N  GLY A  29   O  ILE A  42           
SHEET    4   A18 ILE A 103  ARG A 107 -1  O  GLU A 106   N  SER A  32           
SHEET    5   A18 HIS A  86  SER A  93 -1  N  ILE A  87   O  TYR A 105           
SHEET    6   A18 ASN A  72  ASP A  83 -1  N  ILE A  76   O  SER A  92           
SHEET    7   A18 ARG A  64  SER A  69 -1  N  PHE A  67   O  TYR A  77           
SHEET    8   A18 GLN A  52  ASP A  59 -1  N  HIS A  54   O  SER A  68           
SHEET    9   A18 TYR A   2  VAL A  10  1  N  VAL A  10   O  TYR A  53           
SHEET   10   A18 TYR B   2  VAL B  10 -1  O  TYR B   2   N  LEU A   4           
SHEET   11   A18 GLN B  52  ASP B  59  1  O  TYR B  53   N  VAL B  10           
SHEET   12   A18 ARG B  64  SER B  69 -1  O  ARG B  64   N  ASP B  59           
SHEET   13   A18 ASN B  72  ASP B  83 -1  O  TYR B  77   N  PHE B  67           
SHEET   14   A18 HIS B  86  SER B  93 -1  O  LEU B  88   N  ASP B  80           
SHEET   15   A18 ILE B 103  ARG B 107 -1  O  TYR B 105   N  ILE B  87           
SHEET   16   A18 GLY B  29  ASN B  33 -1  N  SER B  32   O  GLU B 106           
SHEET   17   A18 LYS B  38  HIS B  44 -1  O  ILE B  40   N  TRP B  31           
SHEET   18   A18 TYR B   2  VAL B  10  1  N  GLN B   3   O  SER B  39           
SITE     1 AC1  3 HIS A  50  ASN A  51  GLY B  -1                               
SITE     1 AC2  3 GLY A  -1  ASN B  51  ARG B 101                               
SITE     1 AC3  7 THR A  22  ASN A  25  HOH A 271  HOH A 312                    
SITE     2 AC3  7 TYR B  81  ASP B  83  THR B  84                               
CRYST1   34.196   77.049  101.271  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      0.029243  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012979  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009874        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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