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Database: PDB
Entry: 1FY8
LinkDB: 1FY8
Original site: 1FY8 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           28-SEP-00   1FY8              
TITLE     CRYSTAL STRUCTURE OF THE DELTAILE16VAL17 RAT ANIONIC TRYPSINOGEN-BPTI 
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN II, ANIONIC;                                       
COMPND   3 CHAIN: E;                                                            
COMPND   4 SYNONYM: TRYPSINOGEN;                                                
COMPND   5 EC: 3.4.21.4;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;                              
COMPND   9 CHAIN: I;                                                            
COMPND  10 SYNONYM: BPTI                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;                                  
SOURCE   3 ORGANISM_COMMON: BLACK RAT;                                          
SOURCE   4 ORGANISM_TAXID: 10117;                                               
SOURCE   5 ORGAN: PANCREAS;                                                     
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PYT;                                      
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  13 ORGANISM_COMMON: CATTLE;                                             
SOURCE  14 ORGANISM_TAXID: 9913                                                 
KEYWDS    PROTEIN-PROTEIN COMPLEX, PROTEASE-INHIBITOR COMPLEX, BETA BARREL,     
KEYWDS   2 HYDROLASE-HYDROLASE INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.PASTERNAK,A.WHITE,C.J.JEFFERY,D.RINGE,L.HEDSTROM                    
REVDAT   4   04-OCT-17 1FY8    1       REMARK                                   
REVDAT   3   24-FEB-09 1FY8    1       VERSN                                    
REVDAT   2   04-JUL-01 1FY8    1       JRNL                                     
REVDAT   1   08-NOV-00 1FY8    0                                                
JRNL        AUTH   A.PASTERNAK,A.WHITE,C.J.JEFFERY,N.MEDINA,M.CAHOON,D.RINGE,   
JRNL        AUTH 2 L.HEDSTROM                                                   
JRNL        TITL   THE ENERGETIC COST OF INDUCED FIT CATALYSIS: CRYSTAL         
JRNL        TITL 2 STRUCTURES OF TRYPSINOGEN MUTANTS WITH ENHANCED ACTIVITY AND 
JRNL        TITL 3 INHIBITOR AFFINITY.                                          
JRNL        REF    PROTEIN SCI.                  V.  10  1331 2001              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   11420435                                                     
JRNL        DOI    10.1110/PS.44101                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
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) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 16038                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.183                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1603                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
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            : 2057                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 16                                      
REMARK   3   SOLVENT ATOMS            : 218                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : 1.500                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FY8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-SEP-00.                  
REMARK 100 THE DEPOSITION ID IS D_1000012007.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAY-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : R-AXIS                             
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 160328                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.2                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.05900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.10000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, LITHIUM SULFATE, TRIS, PH      
REMARK 280  8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.37333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.68667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  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        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       20.68667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       41.37333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU E     6                                                      
REMARK 465     ALA E     7                                                      
REMARK 465     PHE E     8                                                      
REMARK 465     PRO E     9                                                      
REMARK 465     VAL E    10                                                      
REMARK 465     ASP E    11                                                      
REMARK 465     ASP E    12                                                      
REMARK 465     ASP E    13                                                      
REMARK 465     THR E   144                                                      
REMARK 465     LEU E   145                                                      
REMARK 465     SER E   146                                                      
REMARK 465     SER E   147                                                      
REMARK 465     GLY E   148                                                      
REMARK 465     VAL E   149                                                      
REMARK 465     ASN E   150                                                      
REMARK 465     GLU E   151                                                      
REMARK 465     GLY I    57                                                      
REMARK 465     ALA I    58                                                      
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   C    MET E   180     O    HOH E   567              0.44            
REMARK 500   C    ASN E    93     O    HOH E   701              0.44            
REMARK 500   N    VAL E   181     O    HOH E   567              0.93            
REMARK 500   O    ASN E    93     O    HOH E   701              1.03            
REMARK 500   CE2  TYR E   234     O    HOH E   655              1.05            
REMARK 500   CZ   TYR E   234     O    HOH E   655              1.13            
REMARK 500   O    MET I    52     O    HOH I   622              1.20            
REMARK 500   N    PHE E    94     O    HOH E   701              1.52            
REMARK 500   O    MET E   180     O    HOH E   567              1.59            
REMARK 500   CA   MET E   180     O    HOH E   567              1.64            
REMARK 500   CA   ASN E    93     O    HOH E   701              1.72            
REMARK 500   CE1  TYR E   234     O    HOH E   646              1.75            
REMARK 500   C    MET I    52     O    HOH I   622              1.80            
REMARK 500   O    HOH E   635     O    HOH E   690              1.83            
REMARK 500   N    GLY I    56     O    HOH I   622              1.83            
REMARK 500   OH   TYR E   234     O    HOH E   655              1.89            
REMARK 500   CB   ALA I    40     O    HOH I   611              1.93            
REMARK 500   CD2  TYR E   234     O    HOH E   655              2.12            
REMARK 500   CA   VAL E   181     O    HOH E   567              2.17            
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   CD1  ILE E    89     O    HOH E   545     6444     1.76            
REMARK 500   CD1  LEU E   105     O    HOH E   556     6444     1.77            
REMARK 500   O    HOH E   617     O    HOH E   712     6444     1.82            
REMARK 500   OE2  GLU I     7     O    HOH I   633     6344     1.92            
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 E  96   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ARG E  96   NE  -  CZ  -  NH2 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG I  17   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 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 E  71      -63.87   -132.96                                   
REMARK 500    ASP E 153      -60.92   -135.72                                   
REMARK 500    SER E 214      -72.29   -123.69                                   
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 E 500  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  70   OE1                                                    
REMARK 620 2 ASN E  72   O    90.7                                              
REMARK 620 3 VAL E  75   O   158.6  84.9                                        
REMARK 620 4 GLU E  77   OE1  96.3  87.7 104.4                                  
REMARK 620 5 GLU E  80   OE2 102.7 162.2  86.6  79.2                            
REMARK 620 6 HOH E 524   O    76.2 102.3  84.3 167.4  92.4                      
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 E 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 990                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 991                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 992                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1F7Z   RELATED DB: PDB                                   
REMARK 900 1F7Z IS THE CRYSTAL STRUCTURE OF K15A TRYPSINOGEN COMPLEXED WITH     
REMARK 900 BPTI                                                                 
REMARK 900 RELATED ID: 1F5R   RELATED DB: PDB                                   
REMARK 900 1F5R IS THE CRYSTAL STRUCTURE OF DELTAI16V17/Q156K TRYPSINOGEN       
REMARK 900 COMPLEXED WITH BPTI                                                  
REMARK 900 RELATED ID: 3TGK   RELATED DB: PDB                                   
REMARK 900 3TGK IS THE CRYSTAL STRUCTURE OF DELTAI16V17/D194N TRYPSINOGEN       
REMARK 900 COMPLEXED WITH BPTI                                                  
DBREF  1FY8 E    6   245  UNP    P00763   TRY2_RAT        14    246             
DBREF  1FY8 I    1    58  UNP    P00974   BPT1_BOVIN      36     93             
SEQADV 1FY8 GLU E    6  UNP  P00763    VAL    14 CONFLICT                       
SEQADV 1FY8     E       UNP  P00763    ILE    24 DELETION                       
SEQADV 1FY8     E       UNP  P00763    VAL    25 DELETION                       
SEQRES   1 E  231  GLU ALA PHE PRO VAL ASP ASP ASP ASP LYS GLY GLY TYR          
SEQRES   2 E  231  THR CYS GLN GLU ASN SER VAL PRO TYR GLN VAL SER LEU          
SEQRES   3 E  231  ASN SER GLY TYR HIS PHE CYS GLY GLY SER LEU ILE ASN          
SEQRES   4 E  231  ASP GLN TRP VAL VAL SER ALA ALA HIS CYS TYR LYS SER          
SEQRES   5 E  231  ARG ILE GLN VAL ARG LEU GLY GLU HIS ASN ILE ASN VAL          
SEQRES   6 E  231  LEU GLU GLY ASN GLU GLN PHE VAL ASN ALA ALA LYS ILE          
SEQRES   7 E  231  ILE LYS HIS PRO ASN PHE ASP ARG LYS THR LEU ASN ASN          
SEQRES   8 E  231  ASP ILE MET LEU ILE LYS LEU SER SER PRO VAL LYS LEU          
SEQRES   9 E  231  ASN ALA ARG VAL ALA THR VAL ALA LEU PRO SER SER CYS          
SEQRES  10 E  231  ALA PRO ALA GLY THR GLN CYS LEU ILE SER GLY TRP GLY          
SEQRES  11 E  231  ASN THR LEU SER SER GLY VAL ASN GLU PRO ASP LEU LEU          
SEQRES  12 E  231  GLN CYS LEU ASP ALA PRO LEU LEU PRO GLN ALA ASP CYS          
SEQRES  13 E  231  GLU ALA SER TYR PRO GLY LYS ILE THR ASP ASN MET VAL          
SEQRES  14 E  231  CYS VAL GLY PHE LEU GLU GLY GLY LYS ASP SER CYS GLN          
SEQRES  15 E  231  GLY ASP SER GLY GLY PRO VAL VAL CYS ASN GLY GLU LEU          
SEQRES  16 E  231  GLN GLY ILE VAL SER TRP GLY TYR GLY CYS ALA LEU PRO          
SEQRES  17 E  231  ASP ASN PRO GLY VAL TYR THR LYS VAL CYS ASN TYR VAL          
SEQRES  18 E  231  ASP TRP ILE GLN ASP THR ILE ALA ALA ASN                      
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                                      
HET     CA  E 500       1                                                       
HET    SO4  I 990       5                                                       
HET    SO4  I 991       5                                                       
HET    SO4  I 992       5                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   7  HOH   *218(H2 O)                                                    
HELIX    1   1 ALA E   55  TYR E   59  5                                   5    
HELIX    2   2 PRO E  164  TYR E  172  1                                   9    
HELIX    3   3 TYR E  234  ASN E  245  1                                  12    
HELIX    4   4 PRO I    2  GLU I    7  5                                   6    
HELIX    5   5 SER I   47  GLY I   56  1                                  10    
SHEET    1   A 7 TYR E  20  THR E  21  0                                        
SHEET    2   A 7 GLN E 156  PRO E 161 -1  N  CYS E 157   O  TYR E  20           
SHEET    3   A 7 GLN E 135  GLY E 140 -1  N  CYS E 136   O  ALA E 160           
SHEET    4   A 7 PRO E 198  CYS E 201 -1  O  PRO E 198   N  SER E 139           
SHEET    5   A 7 GLU E 204  TRP E 215 -1  O  GLU E 204   N  CYS E 201           
SHEET    6   A 7 GLY E 226  LYS E 230 -1  N  VAL E 227   O  TRP E 215           
SHEET    7   A 7 MET E 180  VAL E 183 -1  O  VAL E 181   N  TYR E 228           
SHEET    1   B 7 GLN E  30  ASN E  34  0                                        
SHEET    2   B 7 HIS E  40  ASN E  48 -1  N  PHE E  41   O  LEU E  33           
SHEET    3   B 7 TRP E  51  SER E  54 -1  O  TRP E  51   N  ILE E  47           
SHEET    4   B 7 MET E 104  LEU E 108 -1  O  MET E 104   N  SER E  54           
SHEET    5   B 7 GLN E  81  LYS E  90 -1  N  ALA E  86   O  LYS E 107           
SHEET    6   B 7 GLN E  64  LEU E  68 -1  N  VAL E  66   O  VAL E  83           
SHEET    7   B 7 GLN E  30  ASN E  34 -1  O  SER E  32   N  ARG E  67           
SHEET    1   C 2 ILE I  18  ASN I  24  0                                        
SHEET    2   C 2 LEU I  29  TYR I  35 -1  O  LEU I  29   N  ASN I  24           
SSBOND   1 CYS E   22    CYS E  157                          1555   1555  2.03  
SSBOND   2 CYS E   42    CYS E   58                          1555   1555  2.03  
SSBOND   3 CYS E  128    CYS E  232                          1555   1555  2.03  
SSBOND   4 CYS E  136    CYS E  201                          1555   1555  2.03  
SSBOND   5 CYS E  168    CYS E  182                          1555   1555  2.03  
SSBOND   6 CYS E  191    CYS E  220                          1555   1555  2.02  
SSBOND   7 CYS I    5    CYS I   55                          1555   1555  2.03  
SSBOND   8 CYS I   14    CYS I   38                          1555   1555  2.03  
SSBOND   9 CYS I   30    CYS I   51                          1555   1555  2.02  
LINK         OE1 GLU E  70                CA    CA E 500     1555   1555  2.28  
LINK         O   ASN E  72                CA    CA E 500     1555   1555  2.40  
LINK         O   VAL E  75                CA    CA E 500     1555   1555  2.33  
LINK         OE1 GLU E  77                CA    CA E 500     1555   1555  2.56  
LINK         OE2 GLU E  80                CA    CA E 500     1555   1555  2.28  
LINK        CA    CA E 500                 O   HOH E 524     1555   1555  2.46  
SITE     1 AC1  6 GLU E  70  ASN E  72  VAL E  75  GLU E  77                    
SITE     2 AC1  6 GLU E  80  HOH E 524                                          
SITE     1 AC2  4 GLU I   7  ARG I  42  HOH I 538  HOH I 661                    
SITE     1 AC3  5 GLN E 239  ARG I  20  TYR I  35  HOH I 611                    
SITE     2 AC3  5 HOH I 717                                                     
SITE     1 AC4  2 LYS E  60  ARG I  20                                          
CRYST1   92.600   92.600   62.060  90.00  90.00 120.00 P 32 2 1      6          
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      0.010799  0.006235  0.000000        0.00000                         
SCALE2      0.000000  0.012470  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016113        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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