GenomeNet

Database: PDB
Entry: 1R4P
LinkDB: 1R4P
Original site: 1R4P 
HEADER    TOXIN                                   07-OCT-03   1R4P              
TITLE     SHIGA TOXIN TYPE 2                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SHIGA-LIKE TOXIN TYPE II A SUBUNIT;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SLTII A SUBUNIT;                                            
COMPND   5 EC: 3.2.2.22;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SHIGA-LIKE TOXIN TYPE II B SUBUNIT;                        
COMPND   9 CHAIN: B, C, D, E, F;                                                
COMPND  10 SYNONYM: SLTII B SUBUNIT;                                            
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: STX2A;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PLPSH3;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  12 ORGANISM_TAXID: 562;                                                 
SOURCE  13 GENE: STX2B;                                                         
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PLPSH3                                    
KEYWDS    AB5 TOXIN, TOXIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.E.FRASER,M.FUJINAGA,M.M.CHERNEY,A.R.MELTON-CELSA,E.M.TWIDDY,        
AUTHOR   2 A.D.O'BRIEN,M.N.G.JAMES                                              
REVDAT   4   11-OCT-17 1R4P    1       REMARK                                   
REVDAT   3   24-FEB-09 1R4P    1       VERSN                                    
REVDAT   2   29-JUN-04 1R4P    1       JRNL                                     
REVDAT   1   11-MAY-04 1R4P    0                                                
JRNL        AUTH   M.E.FRASER,M.FUJINAGA,M.M.CHERNEY,A.R.MELTON-CELSA,          
JRNL        AUTH 2 E.M.TWIDDY,A.D.O'BRIEN,M.N.G.JAMES                           
JRNL        TITL   STRUCTURE OF SHIGA TOXIN TYPE 2 (STX2) FROM ESCHERICHIA COLI 
JRNL        TITL 2 O157:H7.                                                     
JRNL        REF    J.BIOL.CHEM.                  V. 279 27511 2004              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   15075327                                                     
JRNL        DOI    10.1074/JBC.M401939200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.77 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.77                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 66890                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 3376                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.77                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.88                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040                       
REMARK   3   BIN FREE R VALUE                    : 0.2390                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 557                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.010                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4961                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 511                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.000                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1R4P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000020433.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC MIRRORS                      
REMARK 200  OPTICS                         : OSMIC MIRRORS                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66890                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.770                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.77                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4 (ALMN, BRUTE                                     
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4 M SODIUM FORMATE, 0.1 M MES, 50 MM 3   
REMARK 280  -(1-PYRIDINO)-1-PROPANESULFONATE, 1% ETHYLENE GLYCOL, PH 6.0,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 294K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       19.76667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       39.53333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       29.65000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       49.41667            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        9.88333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16970 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 21650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F                      
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     HIS A   243                                                      
REMARK 465     GLN A   244                                                      
REMARK 465     GLY A   245                                                      
REMARK 465     ALA A   246                                                      
REMARK 465     ARG A   247                                                      
REMARK 465     SER A   248                                                      
REMARK 465     VAL A   249                                                      
REMARK 465     ARG A   250                                                      
REMARK 465     ALA A   251                                                      
REMARK 465     VAL A   252                                                      
REMARK 465     ASN A   253                                                      
REMARK 465     GLU A   254                                                      
REMARK 465     GLU A   255                                                      
REMARK 465     SER A   256                                                      
REMARK 465     GLN A   257                                                      
REMARK 465     PRO A   258                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  4013     O    HOH B  4050              2.11            
REMARK 500   O    HOH A  4004     O    HOH A  4236              2.14            
REMARK 500   O    HOH B  4036     O    HOH B  4037              2.17            
REMARK 500   O    HOH A  4186     O    HOH F  4052              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH C  3066     O    HOH D  3039     4664     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 219   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG A 219   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    LEU C  44   CA  -  CB  -  CG  ANGL. DEV. =  18.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  60       18.61     55.93                                   
REMARK 500    LEU A  76       16.39     59.97                                   
REMARK 500    THR A 165      -80.18   -116.11                                   
REMARK 500    CYS A 241       39.42    -94.61                                   
REMARK 500    ASP A 265       19.85   -144.65                                   
REMARK 500    ALA B  63       19.06   -150.62                                   
REMARK 500    ALA E  63       18.51   -149.76                                   
REMARK 500    ALA F  63       16.72   -145.86                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A4001  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A4021   O                                                      
REMARK 620 2 HOH A4173   O    94.6                                              
REMARK 620 3 HOH A4168   O    97.7  87.7                                        
REMARK 620 4 THR A  22   O    91.5  90.1 170.7                                  
REMARK 620 5 SER A  25   O    83.2 174.2  87.4  95.2                            
REMARK 620 6 HOH A4110   O   172.1  91.0  76.9  94.1  90.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A4002  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A4035   O                                                      
REMARK 620 2 ARG A 266   O   100.5                                              
REMARK 620 3 ASN A 279   OD1  93.4 118.3                                        
REMARK 620 4 FMT A3004   O1   93.4 109.1 129.8                                  
REMARK 620 5 HOH C3065   O   171.0  78.0  95.1  78.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A4003  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A4078   O                                                      
REMARK 620 2 SER A  15   O    83.1                                              
REMARK 620 3 SER A  15   OG   97.3  78.9                                        
REMARK 620 4 SER A  19   OG  103.3  88.6 154.4                                  
REMARK 620 5 HOH A4153   O   167.5  85.5  75.5  81.4                            
REMARK 620 6 HOH A4217   O   106.6 163.0  85.9 102.2  83.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B4005  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY B  61   O                                                      
REMARK 620 2 THR B  55   O   142.3                                              
REMARK 620 3 SER B  53   OG   80.4  79.3                                        
REMARK 620 4 SER B  60   OG  104.0  97.8 175.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA F4004  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER F  60   OG                                                     
REMARK 620 2 SER F  53   OG  154.3                                              
REMARK 620 3 GLY F  61   O   105.0  89.6                                        
REMARK 620 4 THR F  55   O    73.7  82.5 147.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 4001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 4002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 4003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA F 4004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 4005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PS F 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PS B 1002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PS C 1003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1PS D 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO F 2005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT D 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 3004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 3005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 3007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 3008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 3009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 3010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT F 3011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT C 3012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 3013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT E 3014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 3015                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1DM0   RELATED DB: PDB                                   
REMARK 900 SHIGA TOXIN                                                          
REMARK 900 RELATED ID: 1R4Q   RELATED DB: PDB                                   
DBREF  1R4P A    1   297  UNP    Q9R398   Q9R398_ECOLI    23    319             
DBREF  1R4P B    1    70  UNP    Q57249   Q57249_ENTCL    20     89             
DBREF  1R4P C    1    70  UNP    Q57249   Q57249_ENTCL    20     89             
DBREF  1R4P D    1    70  UNP    Q57249   Q57249_ENTCL    20     89             
DBREF  1R4P E    1    70  UNP    Q57249   Q57249_ENTCL    20     89             
DBREF  1R4P F    1    70  UNP    Q57249   Q57249_ENTCL    20     89             
SEQRES   1 A  297  ARG GLU PHE THR ILE ASP PHE SER THR GLN GLN SER TYR          
SEQRES   2 A  297  VAL SER SER LEU ASN SER ILE ARG THR GLU ILE SER THR          
SEQRES   3 A  297  PRO LEU GLU HIS ILE SER GLN GLY THR THR SER VAL SER          
SEQRES   4 A  297  VAL ILE ASN HIS THR PRO PRO GLY SER TYR PHE ALA VAL          
SEQRES   5 A  297  ASP ILE ARG GLY LEU ASP VAL TYR GLN ALA ARG PHE ASP          
SEQRES   6 A  297  HIS LEU ARG LEU ILE ILE GLU GLN ASN ASN LEU TYR VAL          
SEQRES   7 A  297  ALA GLY PHE VAL ASN THR ALA THR ASN THR PHE TYR ARG          
SEQRES   8 A  297  PHE SER ASP PHE THR HIS ILE SER VAL PRO GLY VAL THR          
SEQRES   9 A  297  THR VAL SER MET THR THR ASP SER SER TYR THR THR LEU          
SEQRES  10 A  297  GLN ARG VAL ALA ALA LEU GLU ARG SER GLY MET GLN ILE          
SEQRES  11 A  297  SER ARG HIS SER LEU VAL SER SER TYR LEU ALA LEU MET          
SEQRES  12 A  297  GLU PHE SER GLY ASN THR MET THR ARG ASP ALA SER ARG          
SEQRES  13 A  297  ALA VAL LEU ARG PHE VAL THR VAL THR ALA GLU ALA LEU          
SEQRES  14 A  297  ARG PHE ARG GLN ILE GLN ARG GLU PHE ARG GLN ALA LEU          
SEQRES  15 A  297  SER GLU THR ALA PRO VAL TYR THR MET THR PRO GLY ASP          
SEQRES  16 A  297  VAL ASP LEU THR LEU ASN TRP GLY ARG ILE SER ASN VAL          
SEQRES  17 A  297  LEU PRO GLU TYR ARG GLY GLU ASP GLY VAL ARG VAL GLY          
SEQRES  18 A  297  ARG ILE SER PHE ASN ASN ILE SER ALA ILE LEU GLY THR          
SEQRES  19 A  297  VAL ALA VAL ILE LEU ASN CYS HIS HIS GLN GLY ALA ARG          
SEQRES  20 A  297  SER VAL ARG ALA VAL ASN GLU GLU SER GLN PRO GLU CYS          
SEQRES  21 A  297  GLN ILE THR GLY ASP ARG PRO VAL ILE LYS ILE ASN ASN          
SEQRES  22 A  297  THR LEU TRP GLU SER ASN THR ALA ALA ALA PHE LEU ASN          
SEQRES  23 A  297  ARG LYS SER GLN PHE LEU TYR THR THR GLY LYS                  
SEQRES   1 B   70  ALA ASP CYS ALA LYS GLY LYS ILE GLU PHE SER LYS TYR          
SEQRES   2 B   70  ASN GLU ASP ASP THR PHE THR VAL LYS VAL ASP GLY LYS          
SEQRES   3 B   70  GLU TYR TRP THR SER ARG TRP ASN LEU GLN PRO LEU LEU          
SEQRES   4 B   70  GLN SER ALA GLN LEU THR GLY MET THR VAL THR ILE LYS          
SEQRES   5 B   70  SER SER THR CYS GLU SER GLY SER GLY PHE ALA GLU VAL          
SEQRES   6 B   70  GLN PHE ASN ASN ASP                                          
SEQRES   1 C   70  ALA ASP CYS ALA LYS GLY LYS ILE GLU PHE SER LYS TYR          
SEQRES   2 C   70  ASN GLU ASP ASP THR PHE THR VAL LYS VAL ASP GLY LYS          
SEQRES   3 C   70  GLU TYR TRP THR SER ARG TRP ASN LEU GLN PRO LEU LEU          
SEQRES   4 C   70  GLN SER ALA GLN LEU THR GLY MET THR VAL THR ILE LYS          
SEQRES   5 C   70  SER SER THR CYS GLU SER GLY SER GLY PHE ALA GLU VAL          
SEQRES   6 C   70  GLN PHE ASN ASN ASP                                          
SEQRES   1 D   70  ALA ASP CYS ALA LYS GLY LYS ILE GLU PHE SER LYS TYR          
SEQRES   2 D   70  ASN GLU ASP ASP THR PHE THR VAL LYS VAL ASP GLY LYS          
SEQRES   3 D   70  GLU TYR TRP THR SER ARG TRP ASN LEU GLN PRO LEU LEU          
SEQRES   4 D   70  GLN SER ALA GLN LEU THR GLY MET THR VAL THR ILE LYS          
SEQRES   5 D   70  SER SER THR CYS GLU SER GLY SER GLY PHE ALA GLU VAL          
SEQRES   6 D   70  GLN PHE ASN ASN ASP                                          
SEQRES   1 E   70  ALA ASP CYS ALA LYS GLY LYS ILE GLU PHE SER LYS TYR          
SEQRES   2 E   70  ASN GLU ASP ASP THR PHE THR VAL LYS VAL ASP GLY LYS          
SEQRES   3 E   70  GLU TYR TRP THR SER ARG TRP ASN LEU GLN PRO LEU LEU          
SEQRES   4 E   70  GLN SER ALA GLN LEU THR GLY MET THR VAL THR ILE LYS          
SEQRES   5 E   70  SER SER THR CYS GLU SER GLY SER GLY PHE ALA GLU VAL          
SEQRES   6 E   70  GLN PHE ASN ASN ASP                                          
SEQRES   1 F   70  ALA ASP CYS ALA LYS GLY LYS ILE GLU PHE SER LYS TYR          
SEQRES   2 F   70  ASN GLU ASP ASP THR PHE THR VAL LYS VAL ASP GLY LYS          
SEQRES   3 F   70  GLU TYR TRP THR SER ARG TRP ASN LEU GLN PRO LEU LEU          
SEQRES   4 F   70  GLN SER ALA GLN LEU THR GLY MET THR VAL THR ILE LYS          
SEQRES   5 F   70  SER SER THR CYS GLU SER GLY SER GLY PHE ALA GLU VAL          
SEQRES   6 F   70  GLN PHE ASN ASN ASP                                          
HET     NA  A4001       1                                                       
HET     NA  A4002       1                                                       
HET     NA  A4003       1                                                       
HET    EDO  A2003       4                                                       
HET    EDO  A2004       4                                                       
HET    FMT  A3001       3                                                       
HET    FMT  A3004       3                                                       
HET    FMT  A3009       3                                                       
HET    FMT  A3010       3                                                       
HET    FMT  A3013       3                                                       
HET    FMT  A3015       6                                                       
HET     NA  B4005       1                                                       
HET    1PS  B1002      13                                                       
HET    FMT  B3006       3                                                       
HET    1PS  C1003      13                                                       
HET    FMT  C3007       3                                                       
HET    FMT  C3012       3                                                       
HET    1PS  D1004      13                                                       
HET    EDO  D2002       4                                                       
HET    FMT  D3003       3                                                       
HET    FMT  E3002       3                                                       
HET    FMT  E3008       3                                                       
HET    FMT  E3014       3                                                       
HET     NA  F4004       1                                                       
HET    1PS  F1001      13                                                       
HET    EDO  F2001       4                                                       
HET    EDO  F2005       4                                                       
HET    FMT  F3005       3                                                       
HET    FMT  F3011       3                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     FMT FORMIC ACID                                                      
HETNAM     1PS 3-PYRIDINIUM-1-YLPROPANE-1-SULFONATE                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     1PS 1-(3-SULFOPROPYL) PYRIDINIUM, PPS                                
FORMUL   7   NA    5(NA 1+)                                                     
FORMUL  10  EDO    5(C2 H6 O2)                                                  
FORMUL  12  FMT    15(C H2 O2)                                                  
FORMUL  19  1PS    4(C8 H11 N O3 S)                                             
FORMUL  36  HOH   *511(H2 O)                                                    
HELIX    1   1 THR A    9  ILE A   24  1                                  16    
HELIX    2   2 SER A   93  THR A   96  5                                   4    
HELIX    3   3 SER A  113  ALA A  122  1                                  10    
HELIX    4   4 SER A  131  PHE A  145  1                                  15    
HELIX    5   5 THR A  151  THR A  165  1                                  15    
HELIX    6   6 THR A  165  PHE A  171  1                                   7    
HELIX    7   7 PHE A  171  GLN A  180  1                                  10    
HELIX    8   8 ALA A  181  SER A  183  5                                   3    
HELIX    9   9 THR A  192  ASN A  201  1                                  10    
HELIX   10  10 ASN A  201  LEU A  209  1                                   9    
HELIX   11  11 PRO A  210  TYR A  212  5                                   3    
HELIX   12  12 ASN A  227  VAL A  235  1                                   9    
HELIX   13  13 SER A  278  LEU A  285  1                                   8    
HELIX   14  14 SER A  289  GLY A  296  1                                   8    
HELIX   15  15 ASN B   34  GLY B   46  1                                  13    
HELIX   16  16 ASN C   34  GLY C   46  1                                  13    
HELIX   17  17 ASN D   34  GLY D   46  1                                  13    
HELIX   18  18 ASN E   34  GLY E   46  1                                  13    
HELIX   19  19 ASN F   34  GLY F   46  1                                  13    
SHEET    1   A 6 GLU A   2  ASP A   6  0                                        
SHEET    2   A 6 TYR A  49  ARG A  55  1  O  ASP A  53   N  PHE A   3           
SHEET    3   A 6 LEU A  67  GLU A  72 -1  O  ILE A  71   N  PHE A  50           
SHEET    4   A 6 VAL A  78  ASN A  83 -1  O  VAL A  82   N  ARG A  68           
SHEET    5   A 6 THR A  88  ARG A  91 -1  O  TYR A  90   N  PHE A  81           
SHEET    6   A 6 THR A 104  SER A 107  1  O  VAL A 106   N  PHE A  89           
SHEET    1   B 3 SER A  25  GLN A  33  0                                        
SHEET    2   B 3 THR A  36  ILE A  41 -1  O  VAL A  40   N  THR A  26           
SHEET    3   B 3 VAL A 237  ILE A 238  1  O  ILE A 238   N  SER A  39           
SHEET    1   C 2 GLN A 129  ILE A 130  0                                        
SHEET    2   C 2 TYR A 189  THR A 190 -1  O  TYR A 189   N  ILE A 130           
SHEET    1   D 4 ILE A 223  PHE A 225  0                                        
SHEET    2   D 4 VAL A 218  VAL A 220 -1  N  VAL A 220   O  ILE A 223           
SHEET    3   D 4 THR A 274  GLU A 277  1  O  LEU A 275   N  ARG A 219           
SHEET    4   D 4 VAL A 268  ILE A 271 -1  N  ILE A 271   O  THR A 274           
SHEET    1   E 7 ASP B   2  GLY B   6  0                                        
SHEET    2   E 7 THR B  48  LYS B  52 -1  O  VAL B  49   N  GLY B   6           
SHEET    3   E 7 GLU B  64  ASN B  68 -1  O  GLU B  64   N  LYS B  52           
SHEET    4   E 7 ILE C   8  TYR C  13 -1  O  SER C  11   N  PHE B  67           
SHEET    5   E 7 PHE C  19  VAL C  23 -1  O  THR C  20   N  LYS C  12           
SHEET    6   E 7 LYS C  26  THR C  30 -1  O  LYS C  26   N  VAL C  23           
SHEET    7   E 7 SER C  60  GLY C  61  1  O  SER C  60   N  TRP C  29           
SHEET    1   F 7 SER B  60  GLY B  61  0                                        
SHEET    2   F 7 LYS B  26  THR B  30  1  N  TRP B  29   O  SER B  60           
SHEET    3   F 7 PHE B  19  VAL B  23 -1  N  VAL B  23   O  LYS B  26           
SHEET    4   F 7 ILE B   8  TYR B  13 -1  N  LYS B  12   O  THR B  20           
SHEET    5   F 7 GLU F  64  ASN F  68 -1  O  PHE F  67   N  SER B  11           
SHEET    6   F 7 THR F  48  LYS F  52 -1  N  THR F  48   O  ASN F  68           
SHEET    7   F 7 ASP F   2  GLY F   6 -1  N  GLY F   6   O  VAL F  49           
SHEET    1   G 7 ASP C   2  GLY C   6  0                                        
SHEET    2   G 7 VAL C  49  LYS C  52 -1  O  VAL C  49   N  GLY C   6           
SHEET    3   G 7 GLU C  64  ASN C  68 -1  O  GLN C  66   N  THR C  50           
SHEET    4   G 7 ASP D   2  TYR D  13 -1  O  SER D  11   N  PHE C  67           
SHEET    5   G 7 PHE D  19  VAL D  23 -1  O  THR D  20   N  LYS D  12           
SHEET    6   G 7 LYS D  26  THR D  30 -1  O  LYS D  26   N  VAL D  23           
SHEET    7   G 7 SER D  60  GLY D  61  1  O  SER D  60   N  TRP D  29           
SHEET    1   H 9 ASP C   2  GLY C   6  0                                        
SHEET    2   H 9 VAL C  49  LYS C  52 -1  O  VAL C  49   N  GLY C   6           
SHEET    3   H 9 GLU C  64  ASN C  68 -1  O  GLN C  66   N  THR C  50           
SHEET    4   H 9 ASP D   2  TYR D  13 -1  O  SER D  11   N  PHE C  67           
SHEET    5   H 9 THR D  48  LYS D  52 -1  O  VAL D  49   N  GLY D   6           
SHEET    6   H 9 GLU D  64  ASN D  68 -1  O  ASN D  68   N  THR D  48           
SHEET    7   H 9 ILE E   8  TYR E  13 -1  O  SER E  11   N  PHE D  67           
SHEET    8   H 9 PHE E  19  VAL E  23 -1  O  THR E  20   N  LYS E  12           
SHEET    9   H 9 LYS E  26  THR E  30 -1  O  LYS E  26   N  VAL E  23           
SHEET    1   I 7 ASP E   2  GLY E   6  0                                        
SHEET    2   I 7 THR E  48  LYS E  52 -1  O  VAL E  49   N  GLY E   6           
SHEET    3   I 7 GLU E  64  ASN E  68 -1  O  ASN E  68   N  THR E  48           
SHEET    4   I 7 ILE F   8  TYR F  13 -1  O  SER F  11   N  PHE E  67           
SHEET    5   I 7 PHE F  19  VAL F  23 -1  O  THR F  20   N  LYS F  12           
SHEET    6   I 7 LYS F  26  THR F  30 -1  O  LYS F  26   N  VAL F  23           
SHEET    7   I 7 SER F  60  GLY F  61  1  O  SER F  60   N  TRP F  29           
SSBOND   1 CYS A  241    CYS A  260                          1555   1555  1.98  
SSBOND   2 CYS B    3    CYS B   56                          1555   1555  2.04  
SSBOND   3 CYS C    3    CYS C   56                          1555   1555  2.00  
SSBOND   4 CYS D    3    CYS D   56                          1555   1555  2.02  
SSBOND   5 CYS E    3    CYS E   56                          1555   1555  2.05  
SSBOND   6 CYS F    3    CYS F   56                          1555   1555  2.05  
LINK        NA    NA A4001                 O   HOH A4021     1555   1555  2.41  
LINK        NA    NA A4001                 O   HOH A4173     1555   1555  2.39  
LINK        NA    NA A4001                 O   HOH A4168     1555   1555  2.32  
LINK        NA    NA A4001                 O   THR A  22     1555   1555  2.24  
LINK        NA    NA A4001                 O   SER A  25     1555   1555  2.36  
LINK        NA    NA A4001                 O   HOH A4110     1555   1555  2.17  
LINK        NA    NA A4002                 O   HOH A4035     1555   1555  2.58  
LINK        NA    NA A4002                 O   ARG A 266     1555   1555  2.51  
LINK        NA    NA A4002                 OD1 ASN A 279     1555   1555  2.20  
LINK        NA    NA A4002                 O1  FMT A3004     1555   1555  2.31  
LINK        NA    NA A4002                 O   HOH C3065     1555   1555  2.25  
LINK        NA    NA A4003                 O   HOH A4078     1555   1555  2.18  
LINK        NA    NA A4003                 O   SER A  15     1555   1555  2.48  
LINK        NA    NA A4003                 OG  SER A  15     1555   1555  2.53  
LINK        NA    NA A4003                 OG  SER A  19     1555   1555  2.18  
LINK        NA    NA A4003                 O   HOH A4153     1555   1555  2.42  
LINK        NA    NA A4003                 O   HOH A4217     1555   1555  2.32  
LINK        NA    NA B4005                 O   GLY B  61     1555   1555  2.39  
LINK        NA    NA B4005                 O   THR B  55     1555   1555  2.29  
LINK        NA    NA F4004                 OG  SER F  60     1555   1555  2.47  
LINK        NA    NA F4004                 OG  SER F  53     1555   1555  2.36  
LINK        NA    NA F4004                 O   GLY F  61     1555   1555  2.19  
LINK        NA    NA F4004                 O   THR F  55     1555   1555  2.28  
LINK         OG  SER B  53                NA    NA B4005     1555   1555  2.64  
LINK         OG  SER B  60                NA    NA B4005     1555   1555  2.64  
SITE     1 AC1  6 THR A  22  SER A  25  HOH A4021  HOH A4110                    
SITE     2 AC1  6 HOH A4168  HOH A4173                                          
SITE     1 AC2  6 ARG A 266  SER A 278  ASN A 279  FMT A3004                    
SITE     2 AC2  6 HOH A4035  HOH C3065                                          
SITE     1 AC3  5 SER A  15  SER A  19  HOH A4078  HOH A4153                    
SITE     2 AC3  5 HOH A4217                                                     
SITE     1 AC4  4 SER F  53  THR F  55  SER F  60  GLY F  61                    
SITE     1 AC5  4 SER B  53  THR B  55  SER B  60  GLY B  61                    
SITE     1 AC6  5 ASN F  14  ASP F  16  THR F  18  TRP F  29                    
SITE     2 AC6  5 HOH F4018                                                     
SITE     1 AC7  7 ASN B  14  ASP B  16  THR B  18  TRP B  29                    
SITE     2 AC7  7 HOH B4010  HOH B4044  HOH B4046                               
SITE     1 AC8 10 ASN C  14  GLU C  15  ASP C  16  THR C  18                    
SITE     2 AC8 10 TRP C  29  FMT C3012  HOH C3033  HOH C3037                    
SITE     3 AC8 10 HOH C3057  SER D  58                                          
SITE     1 AC9 10 SER C  58  ASN D  14  GLU D  15  ASP D  16                    
SITE     2 AC9 10 THR D  18  TRP D  29  FMT D3003  HOH D3020                    
SITE     3 AC9 10 HOH D3040  HOH D3047                                          
SITE     1 BC1  8 SER A 229  PHE A 291  TYR B  13  SER F  31                    
SITE     2 BC1  8 ARG F  32  TRP F  33  ASN F  34  EDO F2005                    
SITE     1 BC2  6 THR A  35  LYS A 288  GLY A 296  HOH A4059                    
SITE     2 BC2  6 HOH A4159  TRP D  33                                          
SITE     1 BC3  9 GLN A  33  GLY A  34  THR A  35  THR A  36                    
SITE     2 BC3  9 LYS A 288  LEU A 292  HOH A4159  TRP C  33                    
SITE     3 BC3  9 ASN C  34                                                     
SITE     1 BC4  5 PHE A   3  THR A   4  SER A  16  SER A  19                    
SITE     2 BC4  5 ILE A  20                                                     
SITE     1 BC5  6 ARG A 176  HOH A4235  SER F  31  TRP F  33                    
SITE     2 BC5  6 EDO F2001  FMT F3005                                          
SITE     1 BC6  5 GLN A 175  ARG A 176  ARG A 179  HOH A4042                    
SITE     2 BC6  5 TRP F  33                                                     
SITE     1 BC7  7 ARG A 179  THR A 294  HOH A4105  ARG E  32                    
SITE     2 BC7  7 TRP E  33  ASN E  34  HOH E3033                               
SITE     1 BC8  5 THR D  20  GLY D  59  1PS D1004  HOH D3042                    
SITE     2 BC8  5 HOH D3058                                                     
SITE     1 BC9  8 ASN A 207  THR A 263  ASP A 265  ARG A 266                    
SITE     2 BC9  8 PRO A 267   NA A4002  HOH A4142  HOH C3065                    
SITE     1 CC1  6 ASN A 227  SER A 229  ALA A 230  SER F  31                    
SITE     2 CC1  6 ARG F  32  EDO F2005                                          
SITE     1 CC2  7 ASN B  68  ASN B  69  HOH B4026  HOH B4053                    
SITE     2 CC2  7 ILE C   8  GLU C   9  GLN C  43                               
SITE     1 CC3  3 ARG C  32  TRP C  33  HOH C3016                               
SITE     1 CC4  5 HOH A4090  THR E  30  SER E  31  ARG E  32                    
SITE     2 CC4  5 PHE E  62                                                     
SITE     1 CC5  4 ARG A 266  VAL A 268  HOH A4106  HOH A4161                    
SITE     1 CC6  4 THR A 110  VAL A 120  THR A 149  HOH A4130                    
SITE     1 CC7  7 ASN E  68  ASN E  69  ILE F   8  GLU F   9                    
SITE     2 CC7  7 GLN F  43  HOH F4033  HOH F4041                               
SITE     1 CC8  6 THR C  20  GLY C  59  1PS C1003  HOH C3034                    
SITE     2 CC8  6 HOH C3060  HOH C3063                                          
SITE     1 CC9  4 GLN A 129  ILE A 130  SER A 131  SER A 134                    
SITE     1 DC1  7 ARG A 219  ARG A 222  THR E  45  GLY E  46                    
SITE     2 DC1  7 MET E  47  ASN E  69  ASP E  70                               
SITE     1 DC2  6 TYR A  77  VAL A  78  SER A 112  VAL A 162                    
SITE     2 DC2  6 HOH A4031  HOH A4237                                          
CRYST1  143.960  143.960   59.300  90.00  90.00 120.00 P 61         30          
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      0.006946  0.004010  0.000000        0.00000                         
SCALE2      0.000000  0.008021  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016863        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system