GenomeNet

Database: PDB
Entry: 2RA3
LinkDB: 2RA3
Original site: 2RA3 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           14-SEP-07   2RA3              
TITLE     HUMAN CATIONIC TRYPSIN COMPLEXED WITH BOVINE PANCREATIC               
TITLE    2 TRYPSIN INHIBITOR (BPTI)                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN-1;                                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: TRYPSIN I, CATIONIC TRYPSINOGEN, SERINE PROTEASE            
COMPND   5 1;                                                                   
COMPND   6 EC: 3.4.21.4;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;                              
COMPND  11 CHAIN: I, C;                                                         
COMPND  12 SYNONYM: BASIC PROTEASE INHIBITOR, BPI, BPTI, APROTININ              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PRSS1, TRP1, TRY1, TRYP1;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3);                             
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  11 ORGANISM_COMMON: CATTLE;                                             
SOURCE  12 ORGANISM_TAXID: 9913;                                                
SOURCE  13 STRAIN: A1153                                                        
KEYWDS    HUMAN CATIONIC TRYPSIN, SERINE PROTEASE, BOVINE PANCREATIC            
KEYWDS   2 TRYPSIN INHIBITOR, BPTI, CALCIUM, DIGESTION, DISEASE                 
KEYWDS   3 MUTATION, HYDROLASE, METAL-BINDING, SECRETED, SULFATION,             
KEYWDS   4 ZYMOGEN, PHARMACEUTICAL, PROTEASE INHIBITOR, SERINE                  
KEYWDS   5 PROTEASE INHIBITOR, HYDROLASE/HYDROLASE INHIBITOR COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.SALAMEH,A.S.SOARES,E.S.RADISKY                                    
REVDAT   4   24-FEB-09 2RA3    1       VERSN                                    
REVDAT   3   18-MAR-08 2RA3    1       REMARK                                   
REVDAT   2   26-FEB-08 2RA3    1       JRNL                                     
REVDAT   1   11-DEC-07 2RA3    0                                                
JRNL        AUTH   M.A.SALAMEH,A.S.SOARES,A.HOCKLA,E.S.RADISKY                  
JRNL        TITL   STRUCTURAL BASIS FOR ACCELERATED CLEAVAGE OF                 
JRNL        TITL 2 BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI) BY                
JRNL        TITL 3 HUMAN MESOTRYPSIN.                                           
JRNL        REF    J.BIOL.CHEM.                  V. 283  4115 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18077447                                                     
JRNL        DOI    10.1074/JBC.M708268200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.13                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 115064                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.154                           
REMARK   3   R VALUE            (WORKING SET) : 0.153                           
REMARK   3   FREE R VALUE                     : 0.178                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 11506                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 17.34                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.36                          
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2RA3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB044614.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.95                               
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 115118                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.460                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.144                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.1                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 46.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.46500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: PDB ENTRIES 1TRN AND 2PTC                            
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.13                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS HYDROCHLORIDE PH 8.5,          
REMARK 280  1.6M AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 298.0K                                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.09350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.09350            
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        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       45.59150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       93.27300            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       45.59150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       93.27300            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       45.09350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       45.59150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       93.27300            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       45.09350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       45.59150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       93.27300            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 23350 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 40830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -746.2 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1 -1.000000  0.000000  0.000000       45.59150            
REMARK 350   BIOMT2   1  0.000000 -1.000000  0.000000      -93.27300            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000      -45.09350            
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -45.59150            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      -93.27300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, I                                  
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000      -45.09350            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 340  LIES ON A SPECIAL POSITION.                          
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     GLY C    57                                                      
REMARK 465     ALA C    58                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   23   CD    OE1   OE2                                     
REMARK 480     LYS A  236   NZ                                                  
REMARK 480     ARG C   53   CZ    NH1   NH2                                     
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   OH   TYR C    23     O    HOH C   105              1.94            
REMARK 500   O    HOH C    71     O    HOH C   122              1.98            
REMARK 500   O    ALA C    25     O    HOH C   105              2.01            
REMARK 500   O    PRO B   128     O    HOH B   361              2.11            
REMARK 500   O    ALA C    27     N    LEU C    29              2.11            
REMARK 500   CE2  TYR C    23     O    HOH C    85              2.14            
REMARK 500   NE   ARG C    42     O4   SO4 C    60              2.18            
REMARK 500   O4   SO4 A    14     O    HOH A   346              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   OE1  GLN A    64     NH1  ARG C    53     3655     2.10            
REMARK 500   OE1  GLN A    64     NH1  ARG C    53     3655     2.17            
REMARK 500   OD1  ASN A    34     NH1  ARG C    53     3655     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 117   C     VAL A 118   N       0.251                       
REMARK 500    GLU B  74   C     GLU B  74   O       0.223                       
REMARK 500    GLU B  74   C     VAL B  75   N       0.186                       
REMARK 500    GLU B  77   CD    GLU B  77   OE2     0.066                       
REMARK 500    HIS B 117   C     VAL B 118   N       0.174                       
REMARK 500    CYS C  55   CB    CYS C  55   SG     -0.140                       
REMARK 500    CYS C  55   CB    CYS C  55   SG      0.122                       
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 B  62   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    GLU B  74   O   -  C   -  N   ANGL. DEV. = -12.9 DEGREES          
REMARK 500    ASP B 189   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASN C  24   N   -  CA  -  C   ANGL. DEV. =  29.6 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    HIS A  71      -65.87   -120.43                                   
REMARK 500    SER A 214      -79.61   -122.79                                   
REMARK 500    ASP B 150       78.23   -153.11                                   
REMARK 500    SER B 214      -76.69   -124.32                                   
REMARK 500    ASN I  44      108.69   -160.33                                   
REMARK 500    PHE C   4       -8.59    -46.41                                   
REMARK 500    ALA C  25     -131.42     51.26                                   
REMARK 500    LYS C  26       33.66    -95.61                                   
REMARK 500    ASN C  44      110.95   -164.16                                   
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                              CA A   1  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE2                                                    
REMARK 620 2 ASN A  72   O    89.6                                              
REMARK 620 3 VAL A  75   O   162.0  83.7                                        
REMARK 620 4 GLU A  80   OE2 102.3 160.5  88.9                                  
REMARK 620 5 HOH A 274   O    89.5  83.2 106.2  81.6                            
REMARK 620 6 HOH A 311   O    79.6 106.8  86.3  90.6 165.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B   1  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B  70   OE2                                                    
REMARK 620 2 ASN B  72   O    87.4                                              
REMARK 620 3 VAL B  75   O   163.3  85.3                                        
REMARK 620 4 GLU B  77   OE2  90.3  82.5 103.6                                  
REMARK 620 5 GLU B  80   OE2 101.6 163.3  89.3  83.4                            
REMARK 620 6 HOH B 291   O    80.0 103.4  87.1 168.4  92.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 1                    
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 6                   
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 10                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 12                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 14                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 247                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 248                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 249                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 1                    
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4                   
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 5                   
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 7                   
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 8                   
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 11                  
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 15                  
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 247                 
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 248                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 249                 
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 250                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 59                  
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 60                  
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 61                  
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 62                  
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 63                  
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 59                  
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 60                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2R9P   RELATED DB: PDB                                   
REMARK 900 HUMAN MESOTRYPSIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN           
REMARK 900 INHIBITOR                                                            
DBREF  2RA3 A   16   246  UNP    P07477   TRY1_HUMAN      24    247             
DBREF  2RA3 B   16   246  UNP    P07477   TRY1_HUMAN      24    247             
DBREF  2RA3 I    1    58  UNP    P00974   BPT1_BOVIN      36     93             
DBREF  2RA3 C    1    58  UNP    P00974   BPT1_BOVIN      36     93             
SEQADV 2RA3 HIS A  117  UNP  P07477    ARG   122 ENGINEERED                     
SEQADV 2RA3 ALA A  195  UNP  P07477    SER   200 ENGINEERED                     
SEQADV 2RA3 HIS B  117  UNP  P07477    ARG   122 ENGINEERED                     
SEQADV 2RA3 ALA B  195  UNP  P07477    SER   200 ENGINEERED                     
SEQRES   1 A  224  ILE VAL GLY GLY TYR ASN CYS GLU GLU ASN SER VAL PRO          
SEQRES   2 A  224  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 A  224  GLY SER LEU ILE ASN GLU GLN TRP VAL VAL SER ALA GLY          
SEQRES   4 A  224  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  224  HIS ASN ILE GLU VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  224  ASN ALA ALA LYS ILE ILE ARG HIS PRO GLN TYR ASP ARG          
SEQRES   7 A  224  LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  224  SER ARG ALA VAL ILE ASN ALA HIS VAL SER THR ILE SER          
SEQRES   9 A  224  LEU PRO THR ALA PRO PRO ALA THR GLY THR LYS CYS LEU          
SEQRES  10 A  224  ILE SER GLY TRP GLY ASN THR ALA SER SER GLY ALA ASP          
SEQRES  11 A  224  TYR PRO ASP GLU LEU GLN CYS LEU ASP ALA PRO VAL LEU          
SEQRES  12 A  224  SER GLN ALA LYS CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 A  224  THR SER ASN MET PHE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  224  LYS ASP SER CYS GLN GLY ASP ALA GLY GLY PRO VAL VAL          
SEQRES  15 A  224  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY ASP          
SEQRES  16 A  224  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  224  VAL TYR ASN TYR VAL LYS TRP ILE LYS ASN THR ILE ALA          
SEQRES  18 A  224  ALA ASN SER                                                  
SEQRES   1 B  224  ILE VAL GLY GLY TYR ASN CYS GLU GLU ASN SER VAL PRO          
SEQRES   2 B  224  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 B  224  GLY SER LEU ILE ASN GLU GLN TRP VAL VAL SER ALA GLY          
SEQRES   4 B  224  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 B  224  HIS ASN ILE GLU VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 B  224  ASN ALA ALA LYS ILE ILE ARG HIS PRO GLN TYR ASP ARG          
SEQRES   7 B  224  LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 B  224  SER ARG ALA VAL ILE ASN ALA HIS VAL SER THR ILE SER          
SEQRES   9 B  224  LEU PRO THR ALA PRO PRO ALA THR GLY THR LYS CYS LEU          
SEQRES  10 B  224  ILE SER GLY TRP GLY ASN THR ALA SER SER GLY ALA ASP          
SEQRES  11 B  224  TYR PRO ASP GLU LEU GLN CYS LEU ASP ALA PRO VAL LEU          
SEQRES  12 B  224  SER GLN ALA LYS CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 B  224  THR SER ASN MET PHE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 B  224  LYS ASP SER CYS GLN GLY ASP ALA GLY GLY PRO VAL VAL          
SEQRES  15 B  224  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY ASP          
SEQRES  16 B  224  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 B  224  VAL TYR ASN TYR VAL LYS TRP ILE LYS ASN THR ILE ALA          
SEQRES  18 B  224  ALA ASN SER                                                  
SEQRES   1 I   58  ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO          
SEQRES   2 I   58  CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS          
SEQRES   3 I   58  ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG          
SEQRES   4 I   58  ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET          
SEQRES   5 I   58  ARG THR CYS GLY GLY ALA                                      
SEQRES   1 C   58  ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO          
SEQRES   2 C   58  CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS          
SEQRES   3 C   58  ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG          
SEQRES   4 C   58  ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET          
SEQRES   5 C   58  ARG THR CYS GLY GLY ALA                                      
HET     CA  A   1       1                                                       
HET    SO4  A   6       5                                                       
HET    SO4  A  10       5                                                       
HET    SO4  A  12       5                                                       
HET    SO4  A  14       5                                                       
HET    SO4  A 247       5                                                       
HET    SO4  A 248       5                                                       
HET    SO4  A 249       5                                                       
HET     CA  B   1       1                                                       
HET    SO4  B   4       5                                                       
HET    SO4  B   5       5                                                       
HET    SO4  B   7       5                                                       
HET    SO4  B   8       5                                                       
HET    SO4  B  11       5                                                       
HET    SO4  B  15       5                                                       
HET    SO4  B 247       5                                                       
HET    SO4  B 248       5                                                       
HET    SO4  B 249       5                                                       
HET    SO4  B 250       5                                                       
HET    SO4  I  59       5                                                       
HET    SO4  I  60       5                                                       
HET    SO4  I  61       5                                                       
HET    SO4  I  62       5                                                       
HET    SO4  I  63       5                                                       
HET    SO4  C  59       5                                                       
HET    SO4  C  60      10                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5   CA    2(CA 2+)                                                     
FORMUL   6  SO4    24(O4 S 2-)                                                  
FORMUL  31  HOH   *643(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 SER A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  ASN A  245  1                                  12    
HELIX    4   4 GLU B   23  ASN B   25  5                                   3    
HELIX    5   5 ALA B   55  TYR B   59  5                                   5    
HELIX    6   6 SER B  164  TYR B  172  1                                   9    
HELIX    7   7 TYR B  234  ASN B  245  1                                  12    
HELIX    8   8 PRO I    2  GLU I    7  5                                   6    
HELIX    9   9 SER I   47  GLY I   56  1                                  10    
HELIX   10  10 PRO C    2  GLU C    7  5                                   6    
HELIX   11  11 ALA C   25  GLY C   28  5                                   4    
HELIX   12  12 SER C   47  GLY C   56  1                                  10    
SHEET    1   A 7 TYR A  20  ASN A  21  0                                        
SHEET    2   A 7 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   A 7 LYS A 135  GLY A 140 -1  N  ILE A 138   O  LEU A 158           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   A 7 GLN A 204  TRP A 215 -1  O  GLN A 204   N  CYS A 201           
SHEET    6   A 7 GLY A 226  LYS A 230 -1  O  VAL A 227   N  TRP A 215           
SHEET    7   A 7 MET A 180  VAL A 183 -1  N  PHE A 181   O  TYR A 228           
SHEET    1   B 7 GLN A  30  ASN A  34  0                                        
SHEET    2   B 7 HIS A  40  ASN A  48 -1  O  CYS A  42   N  LEU A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   B 7 MET A 104  LEU A 108 -1  O  ILE A 106   N  VAL A  52           
SHEET    5   B 7 GLN A  81  ARG A  90 -1  N  ALA A  86   O  LYS A 107           
SHEET    6   B 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
SHEET    7   B 7 GLN A  30  ASN A  34 -1  N  SER A  32   O  ARG A  66           
SHEET    1   C 7 TYR B  20  ASN B  21  0                                        
SHEET    2   C 7 GLN B 156  PRO B 161 -1  O  CYS B 157   N  TYR B  20           
SHEET    3   C 7 LYS B 135  GLY B 140 -1  N  CYS B 136   O  ALA B 160           
SHEET    4   C 7 PRO B 198  CYS B 201 -1  O  VAL B 200   N  LEU B 137           
SHEET    5   C 7 GLN B 204  TRP B 215 -1  O  GLN B 204   N  CYS B 201           
SHEET    6   C 7 GLY B 226  LYS B 230 -1  O  VAL B 227   N  TRP B 215           
SHEET    7   C 7 MET B 180  VAL B 183 -1  N  PHE B 181   O  TYR B 228           
SHEET    1   D 7 GLN B  30  ASN B  34  0                                        
SHEET    2   D 7 HIS B  40  ASN B  48 -1  O  CYS B  42   N  LEU B  33           
SHEET    3   D 7 TRP B  51  SER B  54 -1  O  VAL B  53   N  SER B  45           
SHEET    4   D 7 MET B 104  LEU B 108 -1  O  ILE B 106   N  VAL B  52           
SHEET    5   D 7 GLN B  81  ARG B  90 -1  N  ILE B  89   O  LEU B 105           
SHEET    6   D 7 GLN B  64  LEU B  67 -1  N  LEU B  67   O  GLN B  81           
SHEET    7   D 7 GLN B  30  ASN B  34 -1  N  SER B  32   O  ARG B  66           
SHEET    1   E 2 ILE I  18  ASN I  24  0                                        
SHEET    2   E 2 LEU I  29  TYR I  35 -1  O  TYR I  35   N  ILE I  18           
SHEET    1   F 2 ILE C  18  TYR C  23  0                                        
SHEET    2   F 2 CYS C  30  TYR C  35 -1  O  TYR C  35   N  ILE C  18           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.06  
SSBOND   3 CYS A  136    CYS A  201                          1555   1555  2.06  
SSBOND   4 CYS A  168    CYS A  182                          1555   1555  2.06  
SSBOND   5 CYS A  191    CYS A  220                          1555   1555  2.11  
SSBOND   6 CYS B   22    CYS B  157                          1555   1555  2.04  
SSBOND   7 CYS B   42    CYS B   58                          1555   1555  2.05  
SSBOND   8 CYS B  136    CYS B  201                          1555   1555  2.07  
SSBOND   9 CYS B  168    CYS B  182                          1555   1555  2.09  
SSBOND  10 CYS B  191    CYS B  220                          1555   1555  2.14  
SSBOND  11 CYS I    5    CYS I   55                          1555   1555  2.05  
SSBOND  12 CYS I   14    CYS I   38                          1555   1555  2.10  
SSBOND  13 CYS I   30    CYS I   51                          1555   1555  2.10  
SSBOND  14 CYS C    5    CYS C   55                          1555   1555  2.03  
SSBOND  15 CYS C   14    CYS C   38                          1555   1555  2.06  
SSBOND  16 CYS C   30    CYS C   51                          1555   1555  2.09  
LINK         OE2 GLU A  70                CA    CA A   1     1555   1555  2.24  
LINK         O   ASN A  72                CA    CA A   1     1555   1555  2.34  
LINK         O   VAL A  75                CA    CA A   1     1555   1555  2.34  
LINK         OE2 GLU A  80                CA    CA A   1     1555   1555  2.39  
LINK         OE2 GLU B  70                CA    CA B   1     1555   1555  2.26  
LINK         O   ASN B  72                CA    CA B   1     1555   1555  2.30  
LINK         O   VAL B  75                CA    CA B   1     1555   1555  2.31  
LINK         OE2 GLU B  77                CA    CA B   1     1555   1555  2.40  
LINK         OE2 GLU B  80                CA    CA B   1     1555   1555  2.39  
LINK        CA    CA A   1                 O   HOH A 274     1555   1555  2.44  
LINK        CA    CA A   1                 O   HOH A 311     1555   1555  2.47  
LINK        CA    CA B   1                 O   HOH B 291     1555   1555  2.40  
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  80                    
SITE     2 AC1  6 HOH A 274  HOH A 311                                          
SITE     1 AC2  6 LYS A  60  SER A  61  HOH A 398  HOH A 462                    
SITE     2 AC2  6 HOH A 468  LYS C  46                                          
SITE     1 AC3  4 THR A 132  SER A 164  GLN A 165  HOH A 351                    
SITE     1 AC4  4 THR A 177  SER A 178  SO4 A 247  HOH A 465                    
SITE     1 AC5  3 ARG A  90  HOH A 346  HOH A 383                               
SITE     1 AC6  6 SO4 A  12  ASN A 100  SER A 178  ASN A 179                    
SITE     2 AC6  6 HOH A 338  HOH A 465                                          
SITE     1 AC7  3 SER A 110  ARG A 111  HOH A 381                               
SITE     1 AC8  5 LYS A  97  LEU A  99  TRP A 215  HOH A 337                    
SITE     2 AC8  5 ARG C  39                                                     
SITE     1 AC9  6 GLU B  70  ASN B  72  VAL B  75  GLU B  77                    
SITE     2 AC9  6 GLU B  80  HOH B 291                                          
SITE     1 BC1  8 PHE B 184  LEU B 185  GLU B 186  HOH B 268                    
SITE     2 BC1  8 HOH B 329  HOH B 334  HOH B 400  HOH B 427                    
SITE     1 BC2  8 PRO A 173  LYS A 175  LYS A 224  HOH A 367                    
SITE     2 BC2  8 HOH A 394  ASN B 115  ALA B 116  HOH B 384                    
SITE     1 BC3  7 LYS B  60  SER B  61  HOH B 399  HOH B 489                    
SITE     2 BC3  7 HOH B 513  HOH B 517  LYS I  46                               
SITE     1 BC4  4 LYS B  87  HOH B 368  HOH B 418  ARG I  42                    
SITE     1 BC5 10 ASN B 100  PRO B 129  ALA B 130  THR B 132                    
SITE     2 BC5 10 ASN B 179  SO4 B 248  HOH B 383  HOH B 387                    
SITE     3 BC5 10 HOH B 389  HOH B 485                                          
SITE     1 BC6  3 SER B 110  ARG B 111  HOH B 501                               
SITE     1 BC7  2 ASN B  21  GLN B 156                                          
SITE     1 BC8  7 SO4 B  11  THR B 132  GLN B 165  THR B 177                    
SITE     2 BC8  7 SER B 178  HOH B 288  HOH B 405                               
SITE     1 BC9  5 LYS B  97  LEU B  99  LYS B 175  TRP B 215                    
SITE     2 BC9  5 ARG I  39                                                     
SITE     1 CC1  6 ILE B  47  ASN B  48  LYS B 239  ILE B 242                    
SITE     2 CC1  6 HOH B 330  HOH B 511                                          
SITE     1 CC2  7 GLU I   7  ARG I  42  HOH I  66  HOH I  80                    
SITE     2 CC2  7 HOH I  88  HOH I  91  HOH I 107                               
SITE     1 CC3  9 ARG I  20  TYR I  35  GLY I  37  ALA I  40                    
SITE     2 CC3  9 HOH I  72  HOH I  79  HOH I 104  HOH I 120                    
SITE     3 CC3  9 HOH I 128                                                     
SITE     1 CC4  6 ASN B  84  SER B 109  SER B 110  HOH B 490                    
SITE     2 CC4  6 ARG I   1  PRO I   2                                          
SITE     1 CC5  3 TYR I  10  THR I  11  GLY I  12                               
SITE     1 CC6 10 TYR A 151  PRO A 152  ASP A 153  HOH A 251                    
SITE     2 CC6 10 HOH A 291  ARG C  17  TYR I  23  GLY I  28                    
SITE     3 CC6 10 HOH I 100  HOH I 121                                          
SITE     1 CC7  6 ARG C  20  TYR C  35  GLY C  37  ALA C  40                    
SITE     2 CC7  6 HOH C  73  HOH C  77                                          
SITE     1 CC8  5 PHE C   4  LYS C  41  ARG C  42  HOH C  84                    
SITE     2 CC8  5 HOH C 109                                                     
CRYST1   91.183  186.546   90.187  90.00  90.00  90.00 C 2 2 21     16          
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      0.010967  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005361  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011088        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system