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Database: PDB
Entry: 1PXV
LinkDB: 1PXV
Original site: 1PXV 
HEADER    HYDROLASE                               07-JUL-03   1PXV              
TITLE     THE STAPHOSTATIN-STAPHOPAIN COMPLEX: A FORWARD BINDING INHIBITOR IN   
TITLE    2 COMPLEX WITH ITS TARGET CYSTEINE PROTEASE                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYSTEINE PROTEASE;                                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 3.4.22.-;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYSTEINE PROTEASE INHIBITOR;                               
COMPND   9 CHAIN: C, D;                                                         
COMPND  10 EC: 3.4.22.-;                                                        
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 GENE: STAPHOPAIN B;                                                  
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: E. COLI BL21 (DE3);                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PET15;                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE  11 ORGANISM_TAXID: 1280;                                                
SOURCE  12 GENE: STAPHOSTATIN B;                                                
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  15 EXPRESSION_SYSTEM_STRAIN: E. COLI BL21 (DE3)[PLYSS];                 
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PGEX-5T                               
KEYWDS    CYSTEINE PROTEASE INHIBITOR, HYDROLASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.FILIPEK,M.RZYCHON,A.OLEKSY,M.GRUCA,A.DUBIN,J.POTEMPA,M.BOCHTLER     
REVDAT   4   27-OCT-21 1PXV    1       REMARK SEQADV                            
REVDAT   3   24-FEB-09 1PXV    1       VERSN                                    
REVDAT   2   23-NOV-04 1PXV    1       COMPND MASTER                            
REVDAT   1   21-OCT-03 1PXV    0                                                
JRNL        AUTH   R.FILIPEK,M.RZYCHON,A.OLEKSY,M.GRUCA,A.DUBIN,J.POTEMPA,      
JRNL        AUTH 2 M.BOCHTLER                                                   
JRNL        TITL   THE STAPHOSTATIN-STAPHOPAIN COMPLEX: A FORWARD BINDING       
JRNL        TITL 2 INHIBITOR IN COMPLEX WITH ITS TARGET CYSTEINE PROTEASE.      
JRNL        REF    J.BIOL.CHEM.                  V. 278 40959 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   12874290                                                     
JRNL        DOI    10.1074/JBC.M302926200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.RZYCHON,R.FILIPEK,A.SABAT,K.KOSOWSKA,A.DUBIN,J.POTEMPA,    
REMARK   1  AUTH 2 M.BOCHTLER                                                   
REMARK   1  TITL   STAPHOSTATINS RESEMBLE LIPOCALINS, NOT CYSTATINS IN FOLD.    
REMARK   1  REF    PROTEIN SCI.                  V.  12  2252 2003              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1  DOI    10.1110/PS.03247703                                          
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   1 REFERENCE 3                                                          
REMARK   1  AUTH   I.MASSIMI,E.PARK,K.RICE,W.MULLER-ESTERL,D.SAUDER,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   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 64796                          
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) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.191                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3406                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4300                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2270                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 214                          
REMARK   3   BIN FREE R VALUE                    : 0.2700                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4816                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 458                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 35.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.21000                                              
REMARK   3    B22 (A**2) : 0.36000                                              
REMARK   3    B33 (A**2) : -0.56000                                             
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): 0.123         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.117         
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      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4867 ; 0.020 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  4032 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6610 ; 1.565 ; 1.912       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  9405 ; 3.935 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   583 ; 4.644 ; 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):   698 ; 0.117 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5515 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   975 ; 0.011 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   955 ; 0.240 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  4600 ; 0.310 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2339 ; 0.115 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   383 ; 0.180 ; 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):    30 ; 0.222 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    82 ; 0.371 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.206 ; 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):  2921 ; 1.933 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4690 ; 3.032 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1946 ; 2.272 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1920 ; 3.473 ; 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  : 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 1PXV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-JUL-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000019681.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JAN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.3                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66436                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.18200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, FFFEAR                                        
REMARK 200 STARTING MODEL: 1CV8, 1NYC                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.83                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 M (NH4)2SO4 AND 5% ISOPROPANOL, 100    
REMARK 280  MM GUANIDINIUM HYDROCHLORIDE, PH 6.3, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 294K                                              
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       36.74250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.46350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.48300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.46350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.74250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.48300            
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, 3, 4                                              
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 8730 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -111.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -97.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -73.48500            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     GLY C    -1                                                      
REMARK 475     VAL C   109                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     PHE A  219   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     GLN A  314   CG   CD   OE1  NE2                                  
REMARK 480     HIS B  212   CB   CG   ND1  CD2  CE1  NE2                        
REMARK 480     HIS B  213   CB   CG   ND1  CD2  CE1  NE2                        
REMARK 480     PHE B  219   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     GLN B  314   CG   CD   OE1  NE2                                  
REMARK 480     GLN C    3   CG   CD   OE1  NE2                                  
REMARK 480     ASP C   12   CG   OD1  OD2                                       
REMARK 480     THR C   13   CB   OG1  CG2                                       
REMARK 480     THR C   14   CB   OG1  CG2                                       
REMARK 480     LYS C   15   CG   CD   CE   NZ                                   
REMARK 480     LEU C   16   CG   CD1  CD2                                       
REMARK 480     GLN D    3   CG   CD   OE1  NE2                                  
REMARK 480     ASP D   12   CG   OD1  OD2                                       
REMARK 480     THR D   13   OG1  CG2                                            
REMARK 480     THR D   14   C    OG1  CG2                                       
REMARK 480     LYS D   15   CG   CD   CE   NZ                                   
REMARK 480     LEU D   16   CG   CD1  CD2                                       
REMARK 480     THR D   17   OG1  CG2                                            
REMARK 480     HIS D   18   CG   ND1  CD2  CE1  NE2                             
REMARK 480     LEU D   19   CG   CD1  CD2                                       
REMARK 480     GLU D   20   CG   CD   OE1  OE2                                  
REMARK 480     GLN D   21   CG   CD   OE1  NE2                                  
REMARK 480     THR D   22   OG1  CG2                                            
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 C 109   C     VAL C 109   OXT     0.177                       
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    PHE A 238     -114.49   -111.61                                   
REMARK 500    ALA A 283     -169.97   -104.92                                   
REMARK 500    PHE B 238     -112.02   -110.23                                   
REMARK 500    SER C   0      139.97   -170.40                                   
REMARK 500    ASP C  82      -67.05   -101.86                                   
REMARK 500    LEU C 108     -159.77   -148.90                                   
REMARK 500    THR D  14       -7.37    -56.26                                   
REMARK 500    ASP D  82      -75.64    -92.16                                   
REMARK 500    LEU D 108     -166.54   -116.07                                   
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 B 459                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 462                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 463                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GAI B 464                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NYC   RELATED DB: PDB                                   
REMARK 900 FREE STAPHOSTATIN B                                                  
REMARK 900 RELATED ID: 1CV8   RELATED DB: PDB                                   
REMARK 900 STAPHOPAIN A                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 AT THE TIME OF PROCESSING, THERE WAS NO DATABASE                     
REMARK 999 SEQUENCE AVAILABLE FOR THE PROTEINS FROM STAPHYLOCOCCUS              
REMARK 999 AUREUS, STRAIN V8 THAT WERE CRYSTALLIZED HERE.                       
REMARK 999 THE CLOSEST HOMOLOGUES WITH PROTEIN SEQUENCES IN A                   
REMARK 999 DATABASE WERE FROM STAPHYLOCOCCUS AUREUS SUBSP.                      
REMARK 999 AUREUS MW2. THE AUTHOR CLAIMS THAT THE RESIDUE                       
REMARK 999 CONFLICTS BETWEEN STRAIN V8 AND STRAIN MW2                           
REMARK 999 NOTED HERE ARE GENUINE, CONFIRMED STRAIN DIFFERENCES.                
DBREF  1PXV A  220   393  UNP    Q70UQ8   SSPB_STAAU     220    393             
DBREF  1PXV B  220   393  UNP    Q70UQ8   SSPB_STAAU     220    393             
DBREF  1PXV C    1   109  UNP    Q9EYW6   SSPC_STAAU       1    109             
DBREF  1PXV D    1   109  UNP    Q9EYW6   SSPC_STAAU       1    109             
SEQADV 1PXV GLY A  211  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1PXV HIS A  212  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV HIS A  213  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV HIS A  214  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV HIS A  215  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV HIS A  216  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV HIS A  217  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV GLU A  218  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1PXV PHE A  219  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1PXV ALA A  243  UNP  Q70UQ8    CYS   243 ENGINEERED MUTATION            
SEQADV 1PXV ALA A  283  UNP  Q70UQ8    SER   283 SEE REMARK 999                 
SEQADV 1PXV ASN A  310  UNP  Q70UQ8    GLU   310 SEE REMARK 999                 
SEQADV 1PXV GLY B  211  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1PXV HIS B  212  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV HIS B  213  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV HIS B  214  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV HIS B  215  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV HIS B  216  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV HIS B  217  UNP  Q70UQ8              EXPRESSION TAG                 
SEQADV 1PXV GLU B  218  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1PXV PHE B  219  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1PXV ALA B  243  UNP  Q70UQ8    CYS   243 ENGINEERED MUTATION            
SEQADV 1PXV ALA B  283  UNP  Q70UQ8    SER   283 SEE REMARK 999                 
SEQADV 1PXV ASN B  310  UNP  Q70UQ8    GLU   310 SEE REMARK 999                 
SEQADV 1PXV GLY C   -1  UNP  Q9EYW6              CLONING ARTIFACT               
SEQADV 1PXV SER C    0  UNP  Q9EYW6              CLONING ARTIFACT               
SEQADV 1PXV PHE C   70  UNP  Q9EYW6    ILE    70 SEE REMARK 999                 
SEQADV 1PXV GLY D   -1  UNP  Q9EYW6              CLONING ARTIFACT               
SEQADV 1PXV SER D    0  UNP  Q9EYW6              CLONING ARTIFACT               
SEQADV 1PXV PHE D   70  UNP  Q9EYW6    ILE    70 SEE REMARK 999                 
SEQRES   1 A  183  GLY HIS HIS HIS HIS HIS HIS GLU PHE ASP GLN VAL GLN          
SEQRES   2 A  183  TYR GLU ASN THR LEU LYS ASN PHE LYS ILE ARG GLU GLN          
SEQRES   3 A  183  GLN PHE ASP ASN SER TRP ALA ALA GLY PHE SER MET ALA          
SEQRES   4 A  183  ALA LEU LEU ASN ALA THR LYS ASN THR ASP THR TYR ASN          
SEQRES   5 A  183  ALA HIS ASP ILE MET ARG THR LEU TYR PRO GLU VAL SER          
SEQRES   6 A  183  GLU GLN ASP LEU PRO ASN CYS ALA THR PHE PRO ASN GLN          
SEQRES   7 A  183  MET ILE GLU TYR GLY LYS SER GLN GLY ARG ASP ILE HIS          
SEQRES   8 A  183  TYR GLN GLU GLY VAL PRO SER TYR ASN GLN VAL ASP GLN          
SEQRES   9 A  183  LEU THR LYS ASP ASN VAL GLY ILE MET ILE LEU ALA GLN          
SEQRES  10 A  183  SER VAL SER GLN ASN PRO ASN ASP PRO HIS LEU GLY HIS          
SEQRES  11 A  183  ALA LEU ALA VAL VAL GLY ASN ALA LYS ILE ASN ASP GLN          
SEQRES  12 A  183  GLU LYS LEU ILE TYR TRP ASN PRO TRP ASP THR GLU LEU          
SEQRES  13 A  183  SER ILE GLN ASP ALA ASP SER SER LEU LEU HIS LEU SER          
SEQRES  14 A  183  PHE ASN ARG ASP TYR ASN TRP TYR GLY SER MET ILE GLY          
SEQRES  15 A  183  TYR                                                          
SEQRES   1 B  183  GLY HIS HIS HIS HIS HIS HIS GLU PHE ASP GLN VAL GLN          
SEQRES   2 B  183  TYR GLU ASN THR LEU LYS ASN PHE LYS ILE ARG GLU GLN          
SEQRES   3 B  183  GLN PHE ASP ASN SER TRP ALA ALA GLY PHE SER MET ALA          
SEQRES   4 B  183  ALA LEU LEU ASN ALA THR LYS ASN THR ASP THR TYR ASN          
SEQRES   5 B  183  ALA HIS ASP ILE MET ARG THR LEU TYR PRO GLU VAL SER          
SEQRES   6 B  183  GLU GLN ASP LEU PRO ASN CYS ALA THR PHE PRO ASN GLN          
SEQRES   7 B  183  MET ILE GLU TYR GLY LYS SER GLN GLY ARG ASP ILE HIS          
SEQRES   8 B  183  TYR GLN GLU GLY VAL PRO SER TYR ASN GLN VAL ASP GLN          
SEQRES   9 B  183  LEU THR LYS ASP ASN VAL GLY ILE MET ILE LEU ALA GLN          
SEQRES  10 B  183  SER VAL SER GLN ASN PRO ASN ASP PRO HIS LEU GLY HIS          
SEQRES  11 B  183  ALA LEU ALA VAL VAL GLY ASN ALA LYS ILE ASN ASP GLN          
SEQRES  12 B  183  GLU LYS LEU ILE TYR TRP ASN PRO TRP ASP THR GLU LEU          
SEQRES  13 B  183  SER ILE GLN ASP ALA ASP SER SER LEU LEU HIS LEU SER          
SEQRES  14 B  183  PHE ASN ARG ASP TYR ASN TRP TYR GLY SER MET ILE GLY          
SEQRES  15 B  183  TYR                                                          
SEQRES   1 C  111  GLY SER MET TYR GLN LEU GLN PHE ILE ASN LEU VAL TYR          
SEQRES   2 C  111  ASP THR THR LYS LEU THR HIS LEU GLU GLN THR ASN ILE          
SEQRES   3 C  111  ASN LEU PHE ILE GLY ASN TRP SER ASN HIS GLN LEU GLN          
SEQRES   4 C  111  LYS SER ILE CYS ILE ARG HIS GLY ASP ASP THR SER HIS          
SEQRES   5 C  111  ASN GLN TYR HIS ILE LEU PHE ILE ASP THR ALA HIS GLN          
SEQRES   6 C  111  ARG ILE LYS PHE SER SER PHE ASP ASN GLU GLU ILE ILE          
SEQRES   7 C  111  TYR ILE LEU ASP TYR ASP ASP THR GLN HIS ILE LEU MET          
SEQRES   8 C  111  GLN THR SER SER LYS GLN GLY ILE GLY THR SER ARG PRO          
SEQRES   9 C  111  ILE VAL TYR GLU ARG LEU VAL                                  
SEQRES   1 D  111  GLY SER MET TYR GLN LEU GLN PHE ILE ASN LEU VAL TYR          
SEQRES   2 D  111  ASP THR THR LYS LEU THR HIS LEU GLU GLN THR ASN ILE          
SEQRES   3 D  111  ASN LEU PHE ILE GLY ASN TRP SER ASN HIS GLN LEU GLN          
SEQRES   4 D  111  LYS SER ILE CYS ILE ARG HIS GLY ASP ASP THR SER HIS          
SEQRES   5 D  111  ASN GLN TYR HIS ILE LEU PHE ILE ASP THR ALA HIS GLN          
SEQRES   6 D  111  ARG ILE LYS PHE SER SER PHE ASP ASN GLU GLU ILE ILE          
SEQRES   7 D  111  TYR ILE LEU ASP TYR ASP ASP THR GLN HIS ILE LEU MET          
SEQRES   8 D  111  GLN THR SER SER LYS GLN GLY ILE GLY THR SER ARG PRO          
SEQRES   9 D  111  ILE VAL TYR GLU ARG LEU VAL                                  
HET    SO4  A 460       5                                                       
HET    SO4  A 462       5                                                       
HET    SO4  A 463       5                                                       
HET    SO4  B 459       5                                                       
HET    SO4  B 461       5                                                       
HET    GAI  B 464       4                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GAI GUANIDINE                                                        
FORMUL   5  SO4    5(O4 S 2-)                                                   
FORMUL  10  GAI    C H5 N3                                                      
FORMUL  11  HOH   *458(H2 O)                                                    
HELIX    1   1 TRP A  242  ASN A  257  1                                  16    
HELIX    2   2 ASN A  262  TYR A  271  1                                  10    
HELIX    3   3 ASP A  278  CYS A  282  5                                   5    
HELIX    4   4 PHE A  285  GLN A  296  1                                  12    
HELIX    5   5 SER A  308  ASP A  318  1                                  11    
HELIX    6   6 SER A  379  ASN A  381  5                                   3    
HELIX    7   7 TRP B  242  LYS B  256  1                                  15    
HELIX    8   8 ASN B  262  TYR B  271  1                                  10    
HELIX    9   9 ASP B  278  CYS B  282  5                                   5    
HELIX   10  10 PHE B  285  GLN B  296  1                                  12    
HELIX   11  11 SER B  308  ASP B  318  1                                  11    
HELIX   12  12 ASP C   12  LEU C   16  5                                   5    
HELIX   13  13 THR C   17  LEU C   26  1                                  10    
HELIX   14  14 ASP D   12  LEU D   16  5                                   5    
HELIX   15  15 THR D   17  LEU D   26  1                                  10    
SHEET    1   A 6 VAL A 222  THR A 227  0                                        
SHEET    2   A 6 GLY A 339  ILE A 350 -1  O  ASN A 347   N  ASN A 226           
SHEET    3   A 6 ILE A 322  GLN A 327 -1  N  ALA A 326   O  HIS A 340           
SHEET    4   A 6 ARG A 382  ILE A 391 -1  O  ASN A 385   N  GLN A 327           
SHEET    5   A 6 GLN A 353  TRP A 359  0                                        
SHEET    6   A 6 SER A 367  ASP A 370 -1  O  GLN A 369   N  LEU A 356           
SHEET    1   B 5 HIS A 301  GLU A 304  0                                        
SHEET    2   B 5 ARG A 382  ILE A 391 -1  O  ILE A 391   N  HIS A 301           
SHEET    3   B 5 ILE A 322  GLN A 327 -1  N  GLN A 327   O  ASN A 385           
SHEET    4   B 5 GLY A 339  ILE A 350 -1  O  HIS A 340   N  ALA A 326           
SHEET    5   B 5 LEU A 375  LEU A 378  0                                        
SHEET    1   C 6 VAL B 222  THR B 227  0                                        
SHEET    2   C 6 GLY B 339  ILE B 350 -1  O  ASN B 347   N  ASN B 226           
SHEET    3   C 6 ILE B 322  SER B 328 -1  N  ILE B 324   O  LEU B 342           
SHEET    4   C 6 ARG B 382  ILE B 391 -1  O  ASN B 385   N  GLN B 327           
SHEET    5   C 6 GLN B 353  TRP B 359  0                                        
SHEET    6   C 6 SER B 367  ASP B 370 -1  O  GLN B 369   N  LEU B 356           
SHEET    1   D 5 HIS B 301  GLU B 304  0                                        
SHEET    2   D 5 ARG B 382  ILE B 391 -1  O  SER B 389   N  GLN B 303           
SHEET    3   D 5 ILE B 322  SER B 328 -1  N  GLN B 327   O  ASN B 385           
SHEET    4   D 5 GLY B 339  ILE B 350 -1  O  LEU B 342   N  ILE B 324           
SHEET    5   D 5 LEU B 375  LEU B 378  0                                        
SHEET    1   E 9 GLN C   3  VAL C  10  0                                        
SHEET    2   E 9 LYS C  38  HIS C  44  1  O  CYS C  41   N  ILE C   7           
SHEET    3   E 9 GLY C  29  ASN C  33 -1  N  TRP C  31   O  ILE C  40           
SHEET    4   E 9 ILE C 103  ARG C 107 -1  O  GLU C 106   N  SER C  32           
SHEET    5   E 9 HIS C  86  SER C  93 -1  N  ILE C  87   O  TYR C 105           
SHEET    6   E 9 ASN C  72  ASP C  83 -1  N  ILE C  78   O  GLN C  90           
SHEET    7   E 9 ARG C  64  SER C  69 -1  N  PHE C  67   O  TYR C  77           
SHEET    8   E 9 GLN C  52  ASP C  59 -1  N  ASP C  59   O  ARG C  64           
SHEET    9   E 9 GLN C   3  VAL C  10  1  N  VAL C  10   O  TYR C  53           
SHEET    1   F 9 GLN D   3  VAL D  10  0                                        
SHEET    2   F 9 LYS D  38  HIS D  44  1  O  ARG D  43   N  LEU D   9           
SHEET    3   F 9 GLY D  29  ASN D  33 -1  N  ASN D  33   O  LYS D  38           
SHEET    4   F 9 ILE D 103  ARG D 107 -1  O  GLU D 106   N  SER D  32           
SHEET    5   F 9 HIS D  86  SER D  93 -1  N  ILE D  87   O  TYR D 105           
SHEET    6   F 9 ASN D  72  ASP D  83 -1  N  ILE D  78   O  GLN D  90           
SHEET    7   F 9 ARG D  64  SER D  69 -1  N  PHE D  67   O  TYR D  77           
SHEET    8   F 9 GLN D  52  ASP D  59 -1  N  ASP D  59   O  ARG D  64           
SHEET    9   F 9 GLN D   3  VAL D  10  1  N  VAL D  10   O  TYR D  53           
SITE     1 AC1  5 HOH A 606  LYS B 232  ARG B 234  HOH B 576                    
SITE     2 AC1  5 HOH B 590                                                     
SITE     1 AC2  2 LYS A 232  ARG A 234                                          
SITE     1 AC3  7 ASN B 381  ARG B 382  ASP B 383  HOH B 541                    
SITE     2 AC3  7 HOH B 626  HIS D  62  ARG D  64                               
SITE     1 AC4  4 ARG A 382  ASP A 383  HIS C  62  ARG C  64                    
SITE     1 AC5  7 HIS A 213  HIS A 214  HIS A 215  HIS A 217                    
SITE     2 AC5  7 HIS B 213  HIS B 215  HIS B 217                               
SITE     1 AC6  2 GLU A 291  LYS A 294                                          
CRYST1   73.485   94.966  110.927  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      0.013608  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010530  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009015        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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