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Database: PDB
Entry: 1A0J
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HEADER    SERINE PROTEASE                         01-DEC-97   1A0J              
TITLE     CRYSTAL STRUCTURE OF A NON-PSYCHROPHILIC TRYPSIN FROM A COLD-ADAPTED  
TITLE    2 FISH SPECIES.                                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 OTHER_DETAILS: BENZAMIDINE INHIBITOR IN THE ACTIVE SITE. THE AMINO   
COMPND   6 ACID NUMBERING SCHEME USED IS ADOPTED FROM CHYMOTRYPSINOGEN.         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMO SALAR;                                    
SOURCE   3 ORGANISM_COMMON: ATLANTIC SALMON;                                    
SOURCE   4 ORGANISM_TAXID: 8030;                                                
SOURCE   5 ORGAN: PANCREAS                                                      
KEYWDS    SERINE PROTEINASE, TRYPSIN, HYDROLASE, SERINE PROTEASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.-K.SCHROEDER,N.P.WILLASSEN,A.O.SMALAAS                              
REVDAT   3   13-JUL-11 1A0J    1       VERSN                                    
REVDAT   2   24-FEB-09 1A0J    1       VERSN                                    
REVDAT   1   13-JAN-99 1A0J    0                                                
JRNL        AUTH   H.K.SCHRODER,N.P.WILLASSEN,A.O.SMALAS                        
JRNL        TITL   STRUCTURE OF A NON-PSYCHROPHILIC TRYPSIN FROM A COLD-ADAPTED 
JRNL        TITL 2 FISH SPECIES.                                                
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  54   780 1998              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   9757092                                                      
JRNL        DOI    10.1107/S0907444997018611                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 73.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 68062                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.173                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3866                            
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 34.21                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2986                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2347                       
REMARK   3   BIN FREE R VALUE                    : 0.2121                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 163                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6640                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 87                                      
REMARK   3   SOLVENT ATOMS            : 379                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.93                          
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) : 0.18                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.35                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.09                            
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  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  : PARAM19X.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  4  : TOPH19X.PRO                                    
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  NCS RESTRAINTS WERE INCLUDED IN THE FIRST REFINEMENT ROUNDS, THEN   
REMARK   3  LEFT OUT. THE ELECTRON DENSITY INDICATES A                          
REMARK   3  CALCIUM ION FOR ONLY ONE OF THE FOUR MOLECULES (MOL A).             
REMARK   3                                                                      
REMARK   3  THE ELECTRON DENSITY INDICATES A CALCIUM ION FOR ONLY ONE           
REMARK   3  OF THE FOUR MOLECULES (MOL A).                                      
REMARK   4                                                                      
REMARK   4 1A0J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : AUG-96                             
REMARK 200  TEMPERATURE           (KELVIN) : 295                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM1A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.873                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGEPLATE                         
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, XDS                         
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (AGROVATA, SCALA)             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 76357                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 81.2                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.12300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 3.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.79                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 52.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 3PTB BOVINE TRYPSIN, WITH CORRECT AMINO    
REMARK 200  ACID SEQUENCE SUPERIMPOSED ONTO ANIONIC SALMON TRYPSIN 2TBS.        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.6                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.95350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.39350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.55350            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.39350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.95350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       41.55350            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10040 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 31150 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -162.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000       32.95350            
REMARK 350   BIOMT2   1  0.000000 -1.000000  0.000000       41.55350            
REMARK 350   BIOMT3   1  0.000000  0.000000 -1.000000      154.78700            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, B                               
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     GLU B   77                                                       
REMARK 475     GLY D   78                                                       
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     ARG A   23   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A   24   CA   CB   CG   CD   CE   NZ                         
REMARK 480     ASN A   25   CB   CG   OD1  ND2                                  
REMARK 480     SER A   37   CA   CB   OG                                        
REMARK 480     TYR A   39   CD1  CE1                                            
REMARK 480     PHE A   41   CD1  CE1                                            
REMARK 480     LYS A   60   CD   CE   NZ                                        
REMARK 480     ARG A   97   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A  110   CG   CE   NZ                                        
REMARK 480     ARG A  135   CD   NE   CZ   NH1  NH2                             
REMARK 480     ARG A  222   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG B   23   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     LYS B   24   O    CB   CG   CD   CE                              
REMARK 480     ASN B   25   CA   C    O    CG   OD1  ND2                        
REMARK 480     TYR B   39   CD1  CE1  CZ                                        
REMARK 480     GLU B   70   CB   CG                                             
REMARK 480     ASN B   76   N    CA   CB   CG   OD1  ND2                        
REMARK 480     GLY B   78   O                                                   
REMARK 480     THR B   79   OG1  CG2                                            
REMARK 480     GLU B   80   CG   CD   OE1  OE2                                  
REMARK 480     PHE B   82   CD1  CE1                                            
REMARK 480     ARG B   97   NE   CZ   NH1  NH2                                  
REMARK 480     LYS B  110   CD   CE   NZ                                        
REMARK 480     SER B  116   CA   CB   OG                                        
REMARK 480     TYR B  117   CD1  CD2  CE1  CE2  CZ   OH                         
REMARK 480     ARG B  135   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLN B  192   CD   OE1  NE2                                       
REMARK 480     ARG C   23   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS C   24   CB   CG   CD   NZ                                   
REMARK 480     ASN C   25   CB   CG   OD1  ND2                                  
REMARK 480     TYR C   39   CB   CG   CD1  CD2  OH                              
REMARK 480     HIS C   40   N    CG   ND1  CD2  CE1  NE2                        
REMARK 480     LYS C   60   CE   NZ                                             
REMARK 480     ARG C   62   CG   CD   NE   NH2                                  
REMARK 480     ALA C   74   N    O    CB                                        
REMARK 480     ASN C   76   CA   C    O    CB   CG   OD1  ND2                   
REMARK 480     GLU C   77   N    CA   CB   CG   OE2                             
REMARK 480     GLU C   80   CG   CD   OE1  OE2                                  
REMARK 480     PHE C   82   CD1  CD2  CE1  CE2  CZ                              
REMARK 480     ASN C  115   C    CB                                             
REMARK 480     SER C  116   CB   OG                                             
REMARK 480     TYR C  117   CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 480     TYR C  117   OH                                                  
REMARK 480     ARG C  135   CG   CD   CZ   NH1  NH2                             
REMARK 480     ARG C  222   CG   CD   CZ   NH1  NH2                             
REMARK 480     ARG C  235   CD   NH1                                            
REMARK 480     ARG D   23   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     LYS D   24   CB   CG   CD   CE   NZ                              
REMARK 480     ASN D   25   CG   OD1  ND2                                       
REMARK 480     GLU D   70   CB   CG   OE1  OE2                                  
REMARK 480     VAL D   75   CB   CG1  CG2                                       
REMARK 480     ASN D   76   N    CA   O    CB   CG   OD1  ND2                   
REMARK 480     GLU D   77   N    CA   C    O    CB   CG   CD                    
REMARK 480     GLU D   77   OE1                                                 
REMARK 480     THR D   79   CB   OG1  CG2                                       
REMARK 480     ARG D   97   CG   CD   NH1  NH2                                  
REMARK 480     SER D  116   OG                                                  
REMARK 480     TYR D  117   CB   CG   CD2  CE2  CZ   OH                         
REMARK 480     ARG D  135   CD   NE   CZ   NH1  NH2                             
REMARK 480     GLN D  192   CG   CD   OE1  NE2                                  
REMARK 480     TYR D  217   CD1  CD2  CE2  OH                                   
REMARK 480     ARG D  222   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG D  235   CG   CD   CZ   NH1  NH2                             
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 B  40   NE2   HIS B  40   CD2    -0.067                       
REMARK 500    HIS B  57   NE2   HIS B  57   CD2    -0.075                       
REMARK 500    HIS B  71   NE2   HIS B  71   CD2    -0.067                       
REMARK 500    HIS B  91   NE2   HIS B  91   CD2    -0.079                       
REMARK 500    HIS C  40   NE2   HIS C  40   CD2    -0.069                       
REMARK 500    HIS C  57   NE2   HIS C  57   CD2    -0.069                       
REMARK 500    HIS C  91   NE2   HIS C  91   CD2    -0.073                       
REMARK 500    HIS D  40   NE2   HIS D  40   CD2    -0.066                       
REMARK 500    HIS D  71   NE2   HIS D  71   CD2    -0.069                       
REMARK 500    HIS D  91   NE2   HIS D  91   CD2    -0.067                       
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    TRP A  51   CD1 -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    TRP A  51   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    TRP A  51   CG  -  CD2 -  CE3 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG A  62   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  66   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    TRP A 141   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP A 141   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TRP A 215   CD1 -  CG  -  CD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TRP A 215   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    TRP A 237   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP A 237   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TRP B  51   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    TRP B  51   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG B  66   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    VAL B 138   CB  -  CA  -  C   ANGL. DEV. = -13.6 DEGREES          
REMARK 500    TRP B 141   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    TRP B 141   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TRP B 215   CD1 -  CG  -  CD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    TRP B 215   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    TRP B 237   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    TRP B 237   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    TRP C  51   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP C  51   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    HIS C  57   CA  -  CB  -  CG  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    ARG C  97   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    TRP C 141   CD1 -  CG  -  CD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    TRP C 141   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TRP C 215   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP C 215   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TRP C 237   CD1 -  CG  -  CD2 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    TRP C 237   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    TRP D  51   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    TRP D  51   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    VAL D 138   CB  -  CA  -  C   ANGL. DEV. = -15.8 DEGREES          
REMARK 500    TRP D 141   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP D 141   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TRP D 215   CD1 -  CG  -  CD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TRP D 215   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    TYR D 217   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    TRP D 237   CD1 -  CG  -  CD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    TRP D 237   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 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    ASN A 115     -161.37   -162.54                                   
REMARK 500    ASN B  76       47.18    -83.84                                   
REMARK 500    THR B  79       -7.29    -57.63                                   
REMARK 500    ASN B 115     -161.52   -174.20                                   
REMARK 500    ASN C 115     -154.52   -160.10                                   
REMARK 500    SER C 214      -64.06   -120.91                                   
REMARK 500    SER D  37       77.22   -153.66                                   
REMARK 500    GLU D  77       55.84   -158.03                                   
REMARK 500    SER D 214      -61.45   -122.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A  39         0.06    SIDE CHAIN                              
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 247  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A  75   O                                                      
REMARK 620 2 GLU A  77   OE1 117.4                                              
REMARK 620 3 GLU A  80   OE2  88.2  84.4                                        
REMARK 620 4 GLU A  70   OE2 138.8 103.7 100.4                                  
REMARK 620 5 ASN A  72   O    87.3  71.4 149.8 102.5                            
REMARK 620 N                    1     2     3     4                             
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 247                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 248                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 249                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 246                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN B 246                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN C 246                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN D 246                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE AMINO ACID NUMBERING SCHEME USED IS ADOPTED FROM                 
REMARK 999 CHYMOTRYPSINOGEN.                                                    
DBREF  1A0J A   16   245  UNP    P35033   TRY3_SALSA      16    238             
DBREF  1A0J B   16   245  UNP    P35033   TRY3_SALSA      16    238             
DBREF  1A0J C   16   245  UNP    P35033   TRY3_SALSA      16    238             
DBREF  1A0J D   16   245  UNP    P35033   TRY3_SALSA      16    238             
SEQRES   1 A  223  ILE VAL GLY GLY TYR GLU CYS ARG LYS ASN SER ALA SER          
SEQRES   2 A  223  TYR GLN ALA SER LEU GLN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE SER SER THR TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  HIS ASN ILE ALA VAL ASN GLU GLY THR GLU GLN PHE ILE          
SEQRES   6 A  223  ASP SER VAL LYS VAL ILE MET HIS PRO SER TYR ASN SER          
SEQRES   7 A  223  ARG ASN LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  223  LYS PRO ALA SER LEU ASN SER TYR VAL SER THR VAL ALA          
SEQRES   9 A  223  LEU PRO SER SER CYS ALA SER SER GLY THR ARG CYS LEU          
SEQRES  10 A  223  VAL SER GLY TRP GLY ASN LEU SER GLY SER SER SER ASN          
SEQRES  11 A  223  TYR PRO ASP THR LEU ARG CYS LEU ASP LEU PRO ILE LEU          
SEQRES  12 A  223  SER SER SER SER CYS ASN SER ALA TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR SER ASN MET PHE CYS ALA GLY PHE MET GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY TYR          
SEQRES  16 A  223  GLY CYS ALA GLN ARG ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR ARG SER TRP ILE SER SER THR MET SER          
SEQRES  18 A  223  SER ASN                                                      
SEQRES   1 B  223  ILE VAL GLY GLY TYR GLU CYS ARG LYS ASN SER ALA SER          
SEQRES   2 B  223  TYR GLN ALA SER LEU GLN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 B  223  GLY SER LEU ILE SER SER THR TRP VAL VAL SER ALA ALA          
SEQRES   4 B  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 B  223  HIS ASN ILE ALA VAL ASN GLU GLY THR GLU GLN PHE ILE          
SEQRES   6 B  223  ASP SER VAL LYS VAL ILE MET HIS PRO SER TYR ASN SER          
SEQRES   7 B  223  ARG ASN LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 B  223  LYS PRO ALA SER LEU ASN SER TYR VAL SER THR VAL ALA          
SEQRES   9 B  223  LEU PRO SER SER CYS ALA SER SER GLY THR ARG CYS LEU          
SEQRES  10 B  223  VAL SER GLY TRP GLY ASN LEU SER GLY SER SER SER ASN          
SEQRES  11 B  223  TYR PRO ASP THR LEU ARG CYS LEU ASP LEU PRO ILE LEU          
SEQRES  12 B  223  SER SER SER SER CYS ASN SER ALA TYR PRO GLY GLN ILE          
SEQRES  13 B  223  THR SER ASN MET PHE CYS ALA GLY PHE MET GLU GLY GLY          
SEQRES  14 B  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 B  223  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY TYR          
SEQRES  16 B  223  GLY CYS ALA GLN ARG ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 B  223  VAL CYS ASN TYR ARG SER TRP ILE SER SER THR MET SER          
SEQRES  18 B  223  SER ASN                                                      
SEQRES   1 C  223  ILE VAL GLY GLY TYR GLU CYS ARG LYS ASN SER ALA SER          
SEQRES   2 C  223  TYR GLN ALA SER LEU GLN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 C  223  GLY SER LEU ILE SER SER THR TRP VAL VAL SER ALA ALA          
SEQRES   4 C  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 C  223  HIS ASN ILE ALA VAL ASN GLU GLY THR GLU GLN PHE ILE          
SEQRES   6 C  223  ASP SER VAL LYS VAL ILE MET HIS PRO SER TYR ASN SER          
SEQRES   7 C  223  ARG ASN LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 C  223  LYS PRO ALA SER LEU ASN SER TYR VAL SER THR VAL ALA          
SEQRES   9 C  223  LEU PRO SER SER CYS ALA SER SER GLY THR ARG CYS LEU          
SEQRES  10 C  223  VAL SER GLY TRP GLY ASN LEU SER GLY SER SER SER ASN          
SEQRES  11 C  223  TYR PRO ASP THR LEU ARG CYS LEU ASP LEU PRO ILE LEU          
SEQRES  12 C  223  SER SER SER SER CYS ASN SER ALA TYR PRO GLY GLN ILE          
SEQRES  13 C  223  THR SER ASN MET PHE CYS ALA GLY PHE MET GLU GLY GLY          
SEQRES  14 C  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 C  223  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY TYR          
SEQRES  16 C  223  GLY CYS ALA GLN ARG ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 C  223  VAL CYS ASN TYR ARG SER TRP ILE SER SER THR MET SER          
SEQRES  18 C  223  SER ASN                                                      
SEQRES   1 D  223  ILE VAL GLY GLY TYR GLU CYS ARG LYS ASN SER ALA SER          
SEQRES   2 D  223  TYR GLN ALA SER LEU GLN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 D  223  GLY SER LEU ILE SER SER THR TRP VAL VAL SER ALA ALA          
SEQRES   4 D  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 D  223  HIS ASN ILE ALA VAL ASN GLU GLY THR GLU GLN PHE ILE          
SEQRES   6 D  223  ASP SER VAL LYS VAL ILE MET HIS PRO SER TYR ASN SER          
SEQRES   7 D  223  ARG ASN LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 D  223  LYS PRO ALA SER LEU ASN SER TYR VAL SER THR VAL ALA          
SEQRES   9 D  223  LEU PRO SER SER CYS ALA SER SER GLY THR ARG CYS LEU          
SEQRES  10 D  223  VAL SER GLY TRP GLY ASN LEU SER GLY SER SER SER ASN          
SEQRES  11 D  223  TYR PRO ASP THR LEU ARG CYS LEU ASP LEU PRO ILE LEU          
SEQRES  12 D  223  SER SER SER SER CYS ASN SER ALA TYR PRO GLY GLN ILE          
SEQRES  13 D  223  THR SER ASN MET PHE CYS ALA GLY PHE MET GLU GLY GLY          
SEQRES  14 D  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 D  223  CYS ASN GLY GLN LEU GLN GLY VAL VAL SER TRP GLY TYR          
SEQRES  16 D  223  GLY CYS ALA GLN ARG ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 D  223  VAL CYS ASN TYR ARG SER TRP ILE SER SER THR MET SER          
SEQRES  18 D  223  SER ASN                                                      
HET     CA  A 247       1                                                       
HET    SO4  A 248       5                                                       
HET    SO4  A 249       5                                                       
HET    SO4  B 248       5                                                       
HET    SO4  B 249       5                                                       
HET    SO4  C 248       5                                                       
HET    SO4  C 249       5                                                       
HET    SO4  D 248       5                                                       
HET    SO4  D 249       5                                                       
HET    SO4  D 250       5                                                       
HET    SO4  D 251       5                                                       
HET    BEN  A 246       9                                                       
HET    BEN  B 246       9                                                       
HET    BEN  C 246       9                                                       
HET    BEN  D 246       9                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     BEN BENZAMIDINE                                                      
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  SO4    10(O4 S 2-)                                                  
FORMUL  16  BEN    4(C7 H8 N2)                                                  
FORMUL  20  HOH   *379(H2 O)                                                    
HELIX    1   1 ALA A   56  CYS A   58  5                                   3    
HELIX    2   2 SER A  165  ALA A  171  1                                   7    
HELIX    3   3 VAL A  231  SER A  243  5                                  13    
HELIX    4   4 ALA B   56  CYS B   58  5                                   3    
HELIX    5   5 SER B  165  ALA B  171  1                                   7    
HELIX    6   6 VAL B  231  SER B  243  5                                  13    
HELIX    7   7 ALA C   56  CYS C   58  5                                   3    
HELIX    8   8 SER C  165  ALA C  171  1                                   7    
HELIX    9   9 VAL C  231  SER C  243  5                                  13    
HELIX   10  10 ALA D   56  CYS D   58  5                                   3    
HELIX   11  11 SER D  165  ALA D  171  1                                   7    
HELIX   12  12 VAL D  231  SER D  243  5                                  13    
SHEET    1   A 4 HIS A  40  SER A  45  0                                        
SHEET    2   A 4 GLN A  30  SER A  37 -1  N  SER A  37   O  HIS A  40           
SHEET    3   A 4 GLN A  64  LEU A  67 -1  N  ARG A  66   O  SER A  32           
SHEET    4   A 4 GLN A  81  ASP A  84 -1  N  ILE A  83   O  VAL A  65           
SHEET    1   B 3 TRP A  51  SER A  54  0                                        
SHEET    2   B 3 MET A 104  LEU A 108 -1  N  ILE A 106   O  VAL A  52           
SHEET    3   B 3 SER A  85  MET A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    1   C 2 ARG A 135  GLY A 140  0                                        
SHEET    2   C 2 ARG A 156  PRO A 161 -1  N  LEU A 160   O  CYS A 136           
SHEET    1   D 4 MET A 180  ALA A 183  0                                        
SHEET    2   D 4 GLY A 226  LYS A 230 -1  N  TYR A 228   O  PHE A 181           
SHEET    3   D 4 GLN A 204  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    4   D 4 PRO A 198  CYS A 201 -1  N  CYS A 201   O  GLN A 204           
SHEET    1   E 7 GLN B  81  ASP B  84  0                                        
SHEET    2   E 7 GLN B  64  LEU B  67 -1  N  LEU B  67   O  GLN B  81           
SHEET    3   E 7 GLN B  30  SER B  37 -1  N  GLN B  34   O  GLN B  64           
SHEET    4   E 7 TYR B  39  SER B  48 -1  N  GLY B  44   O  ALA B  31           
SHEET    5   E 7 TRP B  51  SER B  54 -1  N  VAL B  53   O  SER B  45           
SHEET    6   E 7 MET B 104  LEU B 108 -1  N  ILE B 106   O  VAL B  52           
SHEET    7   E 7 SER B  85  MET B  90 -1  N  ILE B  89   O  LEU B 105           
SHEET    1   F 2 ARG B 135  GLY B 140  0                                        
SHEET    2   F 2 ARG B 156  PRO B 161 -1  N  LEU B 160   O  CYS B 136           
SHEET    1   G 4 MET B 180  ALA B 183  0                                        
SHEET    2   G 4 GLY B 226  LYS B 230 -1  N  TYR B 228   O  PHE B 181           
SHEET    3   G 4 GLN B 204  TRP B 215 -1  N  TRP B 215   O  VAL B 227           
SHEET    4   G 4 PRO B 198  CYS B 201 -1  N  CYS B 201   O  GLN B 204           
SHEET    1   H 4 HIS C  40  SER C  45  0                                        
SHEET    2   H 4 GLN C  30  SER C  37 -1  N  SER C  37   O  HIS C  40           
SHEET    3   H 4 ILE C  63  LEU C  67 -1  N  ARG C  66   O  SER C  32           
SHEET    4   H 4 GLN C  81  ASP C  84 -1  N  ILE C  83   O  VAL C  65           
SHEET    1   I 3 TRP C  51  SER C  54  0                                        
SHEET    2   I 3 MET C 104  LEU C 108 -1  N  ILE C 106   O  VAL C  52           
SHEET    3   I 3 SER C  85  MET C  90 -1  N  ILE C  89   O  LEU C 105           
SHEET    1   J 2 ARG C 135  GLY C 140  0                                        
SHEET    2   J 2 ARG C 156  PRO C 161 -1  N  LEU C 160   O  CYS C 136           
SHEET    1   K 4 MET C 180  ALA C 183  0                                        
SHEET    2   K 4 GLY C 226  LYS C 230 -1  N  TYR C 228   O  PHE C 181           
SHEET    3   K 4 GLN C 204  TRP C 215 -1  N  TRP C 215   O  VAL C 227           
SHEET    4   K 4 PRO C 198  CYS C 201 -1  N  CYS C 201   O  GLN C 204           
SHEET    1   L 7 GLN D  81  ASP D  84  0                                        
SHEET    2   L 7 GLN D  64  LEU D  67 -1  N  LEU D  67   O  GLN D  81           
SHEET    3   L 7 GLN D  30  SER D  37 -1  N  GLN D  34   O  GLN D  64           
SHEET    4   L 7 TYR D  39  SER D  48 -1  N  GLY D  44   O  ALA D  31           
SHEET    5   L 7 TRP D  51  SER D  54 -1  N  VAL D  53   O  SER D  45           
SHEET    6   L 7 MET D 104  LEU D 108 -1  N  ILE D 106   O  VAL D  52           
SHEET    7   L 7 SER D  85  MET D  90 -1  N  ILE D  89   O  LEU D 105           
SHEET    1   M 2 ARG D 135  GLY D 140  0                                        
SHEET    2   M 2 ARG D 156  PRO D 161 -1  N  LEU D 160   O  CYS D 136           
SHEET    1   N 4 MET D 180  ALA D 183  0                                        
SHEET    2   N 4 GLY D 226  LYS D 230 -1  N  TYR D 228   O  PHE D 181           
SHEET    3   N 4 GLN D 204  TRP D 215 -1  N  TRP D 215   O  VAL D 227           
SHEET    4   N 4 PRO D 198  CYS D 201 -1  N  CYS D 201   O  GLN D 204           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.02  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  1.99  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.03  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  1.99  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.01  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.05  
SSBOND   7 CYS B   22    CYS B  157                          1555   1555  1.98  
SSBOND   8 CYS B   42    CYS B   58                          1555   1555  2.00  
SSBOND   9 CYS B  128    CYS B  232                          1555   1555  2.01  
SSBOND  10 CYS B  136    CYS B  201                          1555   1555  2.03  
SSBOND  11 CYS B  168    CYS B  182                          1555   1555  2.03  
SSBOND  12 CYS B  191    CYS B  220                          1555   1555  2.01  
SSBOND  13 CYS C   22    CYS C  157                          1555   1555  2.00  
SSBOND  14 CYS C   42    CYS C   58                          1555   1555  2.01  
SSBOND  15 CYS C  128    CYS C  232                          1555   1555  2.02  
SSBOND  16 CYS C  136    CYS C  201                          1555   1555  2.00  
SSBOND  17 CYS C  168    CYS C  182                          1555   1555  2.02  
SSBOND  18 CYS C  191    CYS C  220                          1555   1555  2.03  
SSBOND  19 CYS D   22    CYS D  157                          1555   1555  2.01  
SSBOND  20 CYS D   42    CYS D   58                          1555   1555  1.99  
SSBOND  21 CYS D  128    CYS D  232                          1555   1555  2.02  
SSBOND  22 CYS D  136    CYS D  201                          1555   1555  2.02  
SSBOND  23 CYS D  168    CYS D  182                          1555   1555  2.02  
SSBOND  24 CYS D  191    CYS D  220                          1555   1555  2.00  
LINK        CA    CA A 247                 O   VAL A  75     1555   1555  2.39  
LINK        CA    CA A 247                 OE1 GLU A  77     1555   1555  2.91  
LINK        CA    CA A 247                 OE2 GLU A  80     1555   1555  2.86  
LINK        CA    CA A 247                 OE2 GLU A  70     1555   1555  2.94  
LINK        CA    CA A 247                 O   ASN A  72     1555   1555  2.44  
SITE     1 AC1  5 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC1  5 GLU A  80                                                     
SITE     1 AC2  5 HIS A  40  HIS A  57  GLN A 192  GLY A 193                    
SITE     2 AC2  5 SER A 195                                                     
SITE     1 AC3  4 PRO A 152  ASP A 153  THR A 154  ARG A 156                    
SITE     1 AC4  6 HIS B  57  GLN B 192  GLY B 193  SER B 195                    
SITE     2 AC4  6 BEN B 246  HOH B 323                                          
SITE     1 AC5  4 PRO B 152  ASP B 153  THR B 154  ARG B 156                    
SITE     1 AC6  6 HIS C  57  GLN C 192  GLY C 193  SER C 195                    
SITE     2 AC6  6 BEN C 246  HOH C 614                                          
SITE     1 AC7  5 GLU C  21  PRO C 152  ASP C 153  THR C 154                    
SITE     2 AC7  5 ARG C 156                                                     
SITE     1 AC8  6 TYR A  39  HIS D  57  GLN D 192  GLY D 193                    
SITE     2 AC8  6 SER D 195  BEN D 246                                          
SITE     1 AC9  6 ASN A  76  ARG B 235  PRO D 152  ASP D 153                    
SITE     2 AC9  6 THR D 154  ARG D 156                                          
SITE     1 BC1  6 SER A 148  SER A 149  ASN C  95  ARG C  97                    
SITE     2 BC1  6 ARG D  62  HOH D 490                                          
SITE     1 BC2  5 SER C  96  LYS D  60  SER D  61  HOH D 474                    
SITE     2 BC2  5 HOH D 503                                                     
SITE     1 BC3  6 ASP A 189  SER A 190  SER A 195  GLY A 219                    
SITE     2 BC3  6 CYS A 220  GLY A 226                                          
SITE     1 BC4  6 ASP B 189  SER B 190  SER B 195  GLY B 219                    
SITE     2 BC4  6 GLY B 226  SO4 B 248                                          
SITE     1 BC5  8 ASP C 189  SER C 190  CYS C 191  SER C 195                    
SITE     2 BC5  8 GLY C 219  GLY C 226  SO4 C 248  HOH C 312                    
SITE     1 BC6  7 ASP D 189  SER D 190  CYS D 191  SER D 195                    
SITE     2 BC6  7 GLY D 219  GLY D 226  SO4 D 248                               
CRYST1   65.907   83.107  154.787  90.00  90.00  90.00 P 21 21 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      0.015173  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012033  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006460        0.00000                         
MTRIX1   1 -0.573450 -0.321655  0.753454       25.56022    1                    
MTRIX2   1 -0.367037 -0.721359 -0.587303      120.97440    1                    
MTRIX3   1  0.732420 -0.613334  0.295604       41.05470    1                    
MTRIX1   2 -0.054285 -0.335982 -0.940303      107.68916    1                    
MTRIX2   2 -0.413757 -0.849473  0.327415       66.42438    1                    
MTRIX3   2 -0.908767  0.406831 -0.092901       85.58722    1                    
MTRIX1   3 -0.504313  0.863056  0.028337      -16.28458    1                    
MTRIX2   3 -0.835345 -0.479281 -0.269237       72.87833    1                    
MTRIX3   3 -0.218785 -0.159451  0.962657       48.48168    1                    
MTRIX1   4 -0.569275  0.814531 -0.111647       28.27138    1                    
MTRIX2   4  0.757198  0.572348  0.314752      -35.09442    1                    
MTRIX3   4  0.320276  0.094642 -0.942585      104.65495    1                    
MTRIX1   5  0.032942 -0.454114 -0.890334       74.37251    1                    
MTRIX2   5  0.430334  0.810460 -0.397452      -19.85422    1                    
MTRIX3   5  0.902069 -0.370048  0.222119       61.08286    1                    
MTRIX1   6 -0.289240 -0.515202  0.806788      -19.95494    1                    
MTRIX2   6  0.459541  0.664614  0.589161      -71.18546    1                    
MTRIX3   6 -0.839739  0.541161  0.044524       99.16763    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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