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Database: PDB
Entry: 1Y4H
LinkDB: 1Y4H
Original site: 1Y4H 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           30-NOV-04   1Y4H              
TITLE     WILD TYPE STAPHOPAIN-STAPHOSTATIN COMPLEX                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYSTEINE PROTEASE;                                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 220-393;                                          
COMPND   5 SYNONYM: STAPHOPAIN B;                                               
COMPND   6 EC: 3.4.22.-;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: CYSTEINE PROTEASE INHIBITOR;                               
COMPND  10 CHAIN: C, D;                                                         
COMPND  11 SYNONYM: STAPHOSTATIN B;                                             
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE   3 ORGANISM_TAXID: 1280;                                                
SOURCE   4 GENE: SSPB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PETDUET;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS;                          
SOURCE  12 ORGANISM_TAXID: 1280;                                                
SOURCE  13 GENE: SSPC;                                                          
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PETDUET                                   
KEYWDS    CYSTEINE PROTEASE, INHIBITOR, STAPHOPAIN B, STAPHOSTATIN B,           
KEYWDS   2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.FILIPEK,J.POTEMPA,M.BOCHTLER                                        
REVDAT   5   24-JAN-18 1Y4H    1       JRNL                                     
REVDAT   4   13-JUL-11 1Y4H    1       VERSN                                    
REVDAT   3   24-FEB-09 1Y4H    1       VERSN                                    
REVDAT   2   19-APR-05 1Y4H    1       JRNL                                     
REVDAT   1   18-JAN-05 1Y4H    0                                                
JRNL        AUTH   R.FILIPEK,J.POTEMPA,M.BOCHTLER                               
JRNL        TITL   A COMPARISON OF STAPHOSTATIN B WITH STANDARD MECHANISM       
JRNL        TITL 2 SERINE PROTEASE INHIBITORS.                                  
JRNL        REF    J.BIOL.CHEM.                  V. 280 14669 2005              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15644332                                                     
JRNL        DOI    10.1074/JBC.M411792200                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   R.FILIPEK,M.RZYCHON,A.OLEKSY,M.GRUCA,A.DUBIN,J.POTEMPA,      
REMARK   1  AUTH 2 M.BOCHTLER                                                   
REMARK   1  TITL   THE STAPHOSTATIN-STAPHOPAIN COMPLEX: A FORWARD BINDING       
REMARK   1  TITL 2 INHIBITOR IN COMPLEX WITH ITS TARGET CYSTEINE PROTEASE.      
REMARK   1  REF    J.BIOL.CHEM.                  V. 278 40959 2003              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
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 REFERENCE 3                                                          
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 REFERENCE 4                                                          
REMARK   1  AUTH   R.FILIPEK,R.SZCZEPANOWSKI,A.SABAT,J.POTEMPA,M.BOCHTLER       
REMARK   1  TITL   PROSTAPHOPAIN B STRUCTURE: A COMPARISON OF                   
REMARK   1  TITL 2 PROREGION-MEDIATED AND STAPHOSTATIN-MEDIATED PROTEASE        
REMARK   1  TITL 3 INHIBITION.                                                  
REMARK   1  REF    BIOCHEMISTRY                  V.  43 14306 2004              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.93 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 1.93                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 50784                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.217                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2716                            
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) : 1.93                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.98                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3740                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2380                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 193                          
REMARK   3   BIN FREE R VALUE                    : 0.3060                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4614                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 170                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 34.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.76000                                              
REMARK   3    B22 (A**2) : 0.20000                                              
REMARK   3    B33 (A**2) : -0.99000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.05000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.145         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.131         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.095         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.608         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.952                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4742 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6446 ; 1.509 ; 1.926       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   560 ; 5.666 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   264 ;40.651 ;25.530       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   792 ;12.880 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    16 ;22.754 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   690 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3688 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1851 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3172 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   248 ; 0.114 ; 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):    58 ; 0.284 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.262 ; 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):  2906 ; 1.605 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4558 ; 1.838 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2133 ; 3.136 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1888 ; 4.568 ; 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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   221        A   393                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9780   6.1550   9.3940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0059 T22:   0.0749                                     
REMARK   3      T33:  -0.1513 T12:  -0.0301                                     
REMARK   3      T13:  -0.0147 T23:   0.0198                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8215 L22:   1.6731                                     
REMARK   3      L33:   2.3747 L12:   0.0261                                     
REMARK   3      L13:   0.1917 L23:   0.0218                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0778 S12:   0.1797 S13:   0.0081                       
REMARK   3      S21:  -0.3556 S22:   0.0797 S23:   0.1153                       
REMARK   3      S31:  -0.0833 S32:  -0.1799 S33:  -0.0019                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   221        B   393                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8100  34.9200  23.0640              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0211 T22:  -0.0158                                     
REMARK   3      T33:  -0.0933 T12:   0.0847                                     
REMARK   3      T13:   0.0373 T23:   0.0296                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8861 L22:   1.4996                                     
REMARK   3      L33:   4.2049 L12:   0.0986                                     
REMARK   3      L13:   0.1791 L23:  -0.7398                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0245 S12:   0.0403 S13:   0.0950                       
REMARK   3      S21:  -0.1500 S22:   0.1553 S23:  -0.0202                       
REMARK   3      S31:  -0.5001 S32:  -0.4095 S33:  -0.1307                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.7520 -10.8650  30.4000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0859 T22:   0.0626                                     
REMARK   3      T33:  -0.1111 T12:   0.0194                                     
REMARK   3      T13:   0.0202 T23:   0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2027 L22:   1.9436                                     
REMARK   3      L33:   2.2526 L12:   0.6737                                     
REMARK   3      L13:  -1.0706 L23:  -0.8283                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0077 S12:  -0.1090 S13:  -0.1270                       
REMARK   3      S21:  -0.1042 S22:  -0.1144 S23:  -0.0547                       
REMARK   3      S31:   0.1057 S32:   0.3230 S33:   0.1067                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D     1        D   109                          
REMARK   3    ORIGIN FOR THE GROUP (A):  45.0950  20.2580  40.9120              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0981 T22:   0.0414                                     
REMARK   3      T33:  -0.0567 T12:   0.0543                                     
REMARK   3      T13:  -0.0270 T23:  -0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3416 L22:   1.5743                                     
REMARK   3      L33:   2.6031 L12:   0.4826                                     
REMARK   3      L13:  -0.3981 L23:  -0.2811                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1579 S12:  -0.3104 S13:  -0.2349                       
REMARK   3      S21:   0.0712 S22:  -0.0706 S23:  -0.1489                       
REMARK   3      S31:   0.2070 S32:   0.3711 S33:  -0.0873                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1Y4H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-DEC-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000031104.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.4                                
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                         : MONOCHROMATIC                      
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   : 53525                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.930                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.04700                            
REMARK 200  R SYM                      (I) : 0.04700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 30.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.96                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.32000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1PXV                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M (NH4)2SO4, 9% ISOPROPANOL , PH 6.4,   
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 294.15K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       38.76000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: 3190 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 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: 2530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 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: 6940 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -105.0 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 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       89.52237            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -38.76000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       80.69023            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     SER A   208                                                      
REMARK 465     SER A   209                                                      
REMARK 465     HIS A   210                                                      
REMARK 465     HIS A   211                                                      
REMARK 465     HIS A   212                                                      
REMARK 465     HIS A   213                                                      
REMARK 465     HIS A   214                                                      
REMARK 465     HIS A   215                                                      
REMARK 465     SER A   216                                                      
REMARK 465     GLN A   217                                                      
REMARK 465     ASP A   218                                                      
REMARK 465     PRO A   219                                                      
REMARK 465     ASP A   220                                                      
REMARK 465     MET B   206                                                      
REMARK 465     GLY B   207                                                      
REMARK 465     SER B   208                                                      
REMARK 465     SER B   209                                                      
REMARK 465     HIS B   210                                                      
REMARK 465     HIS B   211                                                      
REMARK 465     HIS B   212                                                      
REMARK 465     HIS B   213                                                      
REMARK 465     HIS B   214                                                      
REMARK 465     HIS B   215                                                      
REMARK 465     SER B   216                                                      
REMARK 465     GLN B   217                                                      
REMARK 465     ASP B   218                                                      
REMARK 465     PRO B   219                                                      
REMARK 465     ASP B   220                                                      
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     -115.87   -116.70                                   
REMARK 500    ASP A 352        0.36     85.21                                   
REMARK 500    PHE B 238     -107.93   -113.71                                   
REMARK 500    ALA B 283     -169.91   -109.26                                   
REMARK 500    ASN D  72       65.27   -100.98                                   
REMARK 500    ASP D  82      -72.20   -104.17                                   
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 CL C 450                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 451                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 452                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 453                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 462                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 463                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 464                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PXV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1NYC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1X9Y   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1CV8   RELATED DB: PDB                                   
DBREF  1Y4H A  220   393  UNP    Q70UQ8   SSPB_STAAU     220    393             
DBREF  1Y4H B  220   393  UNP    Q70UQ8   SSPB_STAAU     220    393             
DBREF  1Y4H C    1   109  UNP    Q9EYW6   SSPC_STAAU       1    109             
DBREF  1Y4H D    1   109  UNP    Q9EYW6   SSPC_STAAU       1    109             
SEQADV 1Y4H MET A  206  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H GLY A  207  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H SER A  208  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H SER A  209  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS A  210  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS A  211  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS A  212  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS A  213  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS A  214  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS A  215  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H SER A  216  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H GLN A  217  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H ASP A  218  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H PRO A  219  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H MET B  206  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H GLY B  207  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H SER B  208  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H SER B  209  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS B  210  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS B  211  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS B  212  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS B  213  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS B  214  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H HIS B  215  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H SER B  216  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H GLN B  217  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H ASP B  218  UNP  Q70UQ8              CLONING ARTIFACT               
SEQADV 1Y4H PRO B  219  UNP  Q70UQ8              CLONING ARTIFACT               
SEQRES   1 A  188  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 A  188  PRO ASP GLN VAL GLN TYR GLU ASN THR LEU LYS ASN PHE          
SEQRES   3 A  188  LYS ILE ARG GLU GLN GLN PHE ASP ASN SER TRP CYS ALA          
SEQRES   4 A  188  GLY PHE SER MET ALA ALA LEU LEU ASN ALA THR LYS ASN          
SEQRES   5 A  188  THR ASP THR TYR ASN ALA HIS ASP ILE MET ARG THR LEU          
SEQRES   6 A  188  TYR PRO GLU VAL SER GLU GLN ASP LEU PRO ASN CYS ALA          
SEQRES   7 A  188  THR PHE PRO ASN GLN MET ILE GLU TYR GLY LYS SER GLN          
SEQRES   8 A  188  GLY ARG ASP ILE HIS TYR GLN GLU GLY VAL PRO SER TYR          
SEQRES   9 A  188  ASN GLN VAL ASP GLN LEU THR LYS ASP ASN VAL GLY ILE          
SEQRES  10 A  188  MET ILE LEU ALA GLN SER VAL SER GLN ASN PRO ASN ASP          
SEQRES  11 A  188  PRO HIS LEU GLY HIS ALA LEU ALA VAL VAL GLY ASN ALA          
SEQRES  12 A  188  LYS ILE ASN ASP GLN GLU LYS LEU ILE TYR TRP ASN PRO          
SEQRES  13 A  188  TRP ASP THR GLU LEU SER ILE GLN ASP ALA ASP SER SER          
SEQRES  14 A  188  LEU LEU HIS LEU SER PHE ASN ARG ASP TYR ASN TRP TYR          
SEQRES  15 A  188  GLY SER MET ILE GLY TYR                                      
SEQRES   1 B  188  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER GLN ASP          
SEQRES   2 B  188  PRO ASP GLN VAL GLN TYR GLU ASN THR LEU LYS ASN PHE          
SEQRES   3 B  188  LYS ILE ARG GLU GLN GLN PHE ASP ASN SER TRP CYS ALA          
SEQRES   4 B  188  GLY PHE SER MET ALA ALA LEU LEU ASN ALA THR LYS ASN          
SEQRES   5 B  188  THR ASP THR TYR ASN ALA HIS ASP ILE MET ARG THR LEU          
SEQRES   6 B  188  TYR PRO GLU VAL SER GLU GLN ASP LEU PRO ASN CYS ALA          
SEQRES   7 B  188  THR PHE PRO ASN GLN MET ILE GLU TYR GLY LYS SER GLN          
SEQRES   8 B  188  GLY ARG ASP ILE HIS TYR GLN GLU GLY VAL PRO SER TYR          
SEQRES   9 B  188  ASN GLN VAL ASP GLN LEU THR LYS ASP ASN VAL GLY ILE          
SEQRES  10 B  188  MET ILE LEU ALA GLN SER VAL SER GLN ASN PRO ASN ASP          
SEQRES  11 B  188  PRO HIS LEU GLY HIS ALA LEU ALA VAL VAL GLY ASN ALA          
SEQRES  12 B  188  LYS ILE ASN ASP GLN GLU LYS LEU ILE TYR TRP ASN PRO          
SEQRES  13 B  188  TRP ASP THR GLU LEU SER ILE GLN ASP ALA ASP SER SER          
SEQRES  14 B  188  LEU LEU HIS LEU SER PHE ASN ARG ASP TYR ASN TRP TYR          
SEQRES  15 B  188  GLY SER MET ILE GLY TYR                                      
SEQRES   1 C  109  MET TYR GLN LEU GLN PHE ILE ASN LEU VAL TYR ASP THR          
SEQRES   2 C  109  THR LYS LEU THR HIS LEU GLU GLN THR ASN ILE ASN LEU          
SEQRES   3 C  109  PHE ILE GLY ASN TRP SER ASN HIS GLN LEU GLN LYS SER          
SEQRES   4 C  109  ILE CYS ILE ARG HIS GLY ASP ASP THR SER HIS ASN GLN          
SEQRES   5 C  109  TYR HIS ILE LEU PHE ILE ASP THR ALA HIS GLN ARG ILE          
SEQRES   6 C  109  LYS PHE SER SER PHE ASP ASN GLU GLU ILE ILE TYR ILE          
SEQRES   7 C  109  LEU ASP TYR ASP ASP THR GLN HIS ILE LEU MET GLN THR          
SEQRES   8 C  109  SER SER LYS GLN GLY ILE GLY THR SER ARG PRO ILE VAL          
SEQRES   9 C  109  TYR GLU ARG LEU VAL                                          
SEQRES   1 D  109  MET TYR GLN LEU GLN PHE ILE ASN LEU VAL TYR ASP THR          
SEQRES   2 D  109  THR LYS LEU THR HIS LEU GLU GLN THR ASN ILE ASN LEU          
SEQRES   3 D  109  PHE ILE GLY ASN TRP SER ASN HIS GLN LEU GLN LYS SER          
SEQRES   4 D  109  ILE CYS ILE ARG HIS GLY ASP ASP THR SER HIS ASN GLN          
SEQRES   5 D  109  TYR HIS ILE LEU PHE ILE ASP THR ALA HIS GLN ARG ILE          
SEQRES   6 D  109  LYS PHE SER SER PHE ASP ASN GLU GLU ILE ILE TYR ILE          
SEQRES   7 D  109  LEU ASP TYR ASP ASP THR GLN HIS ILE LEU MET GLN THR          
SEQRES   8 D  109  SER SER LYS GLN GLY ILE GLY THR SER ARG PRO ILE VAL          
SEQRES   9 D  109  TYR GLU ARG LEU VAL                                          
HET     CL  A 453       1                                                       
HET    SO4  A 461       5                                                       
HET    SO4  A 463       5                                                       
HET    SO4  B 460       5                                                       
HET     CL  C 450       1                                                       
HET     CL  C 452       1                                                       
HET    SO4  C 462       5                                                       
HET    SO4  C 464       5                                                       
HET     CL  D 451       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5   CL    4(CL 1-)                                                     
FORMUL   6  SO4    5(O4 S 2-)                                                   
FORMUL  14  HOH   *170(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 TRP B  242  ASN B  257  1                                  16    
HELIX    7   7 ASN B  262  TYR B  271  1                                  10    
HELIX    8   8 ASP B  278  CYS B  282  5                                   5    
HELIX    9   9 PHE B  285  GLN B  296  1                                  12    
HELIX   10  10 SER B  308  ASP B  318  1                                  11    
HELIX   11  11 ASP C   12  LEU C   16  5                                   5    
HELIX   12  12 THR C   17  LEU C   26  1                                  10    
HELIX   13  13 ASP D   12  LEU D   16  5                                   5    
HELIX   14  14 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  SER A 328 -1  N  ILE A 322   O  VAL A 344           
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  SER A 389   N  GLN A 303           
SHEET    3   B 5 ILE A 322  SER A 328 -1  N  GLN A 327   O  ASN A 385           
SHEET    4   B 5 GLY A 339  ILE A 350 -1  O  VAL A 344   N  ILE A 322           
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  GLN B 327 -1  N  ILE B 322   O  VAL B 344           
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  ILE B 391   N  HIS B 301           
SHEET    3   D 5 ILE B 322  GLN B 327 -1  N  GLN B 327   O  ASN B 385           
SHEET    4   D 5 GLY B 339  ILE B 350 -1  O  VAL B 344   N  ILE B 322           
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  SER C  39   N  GLN C   3           
SHEET    3   E 9 GLY C  29  ASN C  33 -1  N  GLY C  29   O  ILE C  42           
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  76   O  SER C  92           
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  SER D  39   N  GLN D   3           
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 ILE D  75  ASP D  83 -1  N  ILE D  76   O  SER D  92           
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  1 HIS C  50                                                     
SITE     1 AC2  1 HIS D  50                                                     
SITE     1 AC3  2 HIS C  18  HOH C 480                                          
SITE     1 AC4  1 HIS A 337                                                     
SITE     1 AC5  3 LYS B 232  ARG B 234  ASP B 259                               
SITE     1 AC6  2 LYS A 232  ARG A 234                                          
SITE     1 AC7  3 THR C  22  ASN C  25  HOH C 473                               
SITE     1 AC8  2 LYS A 256  ARG A 298                                          
SITE     1 AC9  1 ARG C 101                                                     
CRYST1   57.948   77.520   84.891  90.00 108.10  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017257  0.000000  0.005641        0.00000                         
SCALE2      0.000000  0.012900  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012393        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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