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Database: PDB
Entry: 1F7Z
LinkDB: 1F7Z
Original site: 1F7Z 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           28-JUN-00   1F7Z              
TITLE     RAT TRYPSINOGEN K15A COMPLEXED WITH BOVINE PANCREATIC                 
TITLE    2 TRYPSIN INHIBITOR                                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN II, ANIONIC;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: 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 NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   6 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PYT;                                      
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  12 ORGANISM_COMMON: CATTLE;                                             
SOURCE  13 ORGANISM_TAXID: 9913;                                                
SOURCE  14 TISSUE: PANCREAS                                                     
KEYWDS    SERINE PROTEASE, TRYPSIN PRECURSOR, HYDROLASE/HYDROLASE               
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.PASTERNAK,A.WHITE,C.J.JEFFERY,N.MEDINA,M.CAHOON,D.RINGE,            
AUTHOR   2 L.HEDSTROM                                                           
REVDAT   2   24-FEB-09 1F7Z    1       VERSN                                    
REVDAT   1   04-JUL-01 1F7Z    0                                                
JRNL        AUTH   A.PASTERNAK,A.WHITE,C.J.JEFFERY,N.MEDINA,M.CAHOON,           
JRNL        AUTH 2 D.RINGE,L.HEDSTROM                                           
JRNL        TITL   THE ENERGETIC COST OF INDUCED FIT CATALYSIS:                 
JRNL        TITL 2 CRYSTAL STRUCTURES OF TRYPSINOGEN MUTANTS WITH               
JRNL        TITL 3 ENHANCED ACTIVITY AND 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   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : CNS                                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
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)   (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 44058                          
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) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 4305                            
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            : 2039                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 153                                     
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) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1F7Z COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-JUL-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011354.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44058                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.61                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.03600                            
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: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       41.38400            
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       20.69200            
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       20.69200            
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       41.38400            
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: 1750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     VAL A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     ASP A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     ASN A   143                                                      
REMARK 465     THR A   144                                                      
REMARK 465     LEU A   145                                                      
REMARK 465     SER A   146                                                      
REMARK 465     SER A   147                                                      
REMARK 465     GLY A   148                                                      
REMARK 465     VAL A   149                                                      
REMARK 465     ASN A   150                                                      
REMARK 465     GLU A   151                                                      
REMARK 465     PRO A   152                                                      
REMARK 465     GLY I    57                                                      
REMARK 465     ALA I    58                                                      
REMARK 465     ILE I    59                                                      
REMARK 465     GLY I    60                                                      
REMARK 465     PRO I    61                                                      
REMARK 465     TRP I    62                                                      
REMARK 465     GLU I    63                                                      
REMARK 465     ASN I    64                                                      
REMARK 465     LEU I    65                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 195    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   570     O    HOH A   610              0.70            
REMARK 500   N    ASP A   153     O    HOH A   613              1.72            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  71      -64.15   -132.68                                   
REMARK 500    SER A 214      -69.10   -124.54                                   
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 800  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  72   O                                                      
REMARK 620 2 VAL A  75   O    84.2                                              
REMARK 620 3 GLU A  70   OE1  89.3 165.1                                        
REMARK 620 4 HOH A 570   O   101.0  84.3  83.8                                  
REMARK 620 5 HOH A 610   O   104.4  86.3  82.3   3.8                            
REMARK 620 6 GLU A  80   OE2 159.4  84.1 105.7  94.7  91.7                      
REMARK 620 7 GLU A  77   OE1  82.0  96.8  95.5 176.9 173.1  82.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 990                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 991                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 800                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3TGI   RELATED DB: PDB                                   
REMARK 900 3TGI CONTAINS WILD-TYPE RAT ANIONIC TRYPSIN COMPLEXED WITH           
REMARK 900 BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI)                           
REMARK 900 RELATED ID: 1F5R   RELATED DB: PDB                                   
REMARK 900 1F5R CONTAINS MUTANT RAT ANIONIC TRYPSIN COMPLEXED WITH              
REMARK 900 BOVINE PANCREATIC TRYPSIN INHIBITOR (BPTI)                           
DBREF  1F7Z A    7   245  UNP    P00763   TRY2_RAT        15    246             
DBREF  1F7Z I    1    65  UNP    P00974   BPT1_BOVIN      36    100             
SEQADV 1F7Z GLU A    6  UNP  P00763              CLONING ARTIFACT               
SEQADV 1F7Z ALA A   15  UNP  P00763    LYS    23 ENGINEERED                     
SEQRES   1 A  233  GLU ALA PHE PRO VAL ASP ASP ASP ASP ALA ILE VAL GLY          
SEQRES   2 A  233  GLY TYR THR CYS GLN GLU ASN SER VAL PRO TYR GLN VAL          
SEQRES   3 A  233  SER LEU ASN SER GLY TYR HIS PHE CYS GLY GLY SER LEU          
SEQRES   4 A  233  ILE ASN ASP GLN TRP VAL VAL SER ALA ALA HIS CYS TYR          
SEQRES   5 A  233  LYS SER ARG ILE GLN VAL ARG LEU GLY GLU HIS ASN ILE          
SEQRES   6 A  233  ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL ASN ALA ALA          
SEQRES   7 A  233  LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG LYS THR LEU          
SEQRES   8 A  233  ASN ASN ASP ILE MET LEU ILE LYS LEU SER SER PRO VAL          
SEQRES   9 A  233  LYS LEU ASN ALA ARG VAL ALA THR VAL ALA LEU PRO SER          
SEQRES  10 A  233  SER CYS ALA PRO ALA GLY THR GLN CYS LEU ILE SER GLY          
SEQRES  11 A  233  TRP GLY ASN THR LEU SER SER GLY VAL ASN GLU PRO ASP          
SEQRES  12 A  233  LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU PRO GLN ALA          
SEQRES  13 A  233  ASP CYS GLU ALA SER TYR PRO GLY LYS ILE THR ASP ASN          
SEQRES  14 A  233  MET VAL CYS VAL GLY PHE LEU GLU GLY GLY LYS ASP SER          
SEQRES  15 A  233  CYS GLN GLY ASP SER GLY GLY PRO VAL VAL CYS ASN GLY          
SEQRES  16 A  233  GLU LEU GLN GLY ILE VAL SER TRP GLY TYR GLY CYS ALA          
SEQRES  17 A  233  LEU PRO ASP ASN PRO GLY VAL TYR THR LYS VAL CYS ASN          
SEQRES  18 A  233  TYR VAL ASP TRP ILE GLN ASP THR ILE ALA ALA ASN              
SEQRES   1 I   65  ARG PRO ASP PHE CYS LEU GLU PRO PRO TYR THR GLY PRO          
SEQRES   2 I   65  CYS LYS ALA ARG ILE ILE ARG TYR PHE TYR ASN ALA LYS          
SEQRES   3 I   65  ALA GLY LEU CYS GLN THR PHE VAL TYR GLY GLY CYS ARG          
SEQRES   4 I   65  ALA LYS ARG ASN ASN PHE LYS SER ALA GLU ASP CYS MET          
SEQRES   5 I   65  ARG THR CYS GLY GLY ALA ILE GLY PRO TRP GLU ASN LEU          
HET    SO4  I 990       5                                                       
HET    SO4  I 991       5                                                       
HET     CA  A 800       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  SO4    2(O4 S 2-)                                                   
FORMUL   5   CA    CA 2+                                                        
FORMUL   6  HOH   *153(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 PRO A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  ALA A  244  1                                  11    
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 A  20  THR A  21  0                                        
SHEET    2   A 7 GLN A 156  PRO A 161 -1  N  CYS A 157   O  TYR A  20           
SHEET    3   A 7 GLN A 135  GLY A 140 -1  N  CYS A 136   O  ALA A 160           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  PRO A 198   N  SER A 139           
SHEET    5   A 7 GLU A 204  TRP A 215 -1  O  GLU A 204   N  CYS A 201           
SHEET    6   A 7 GLY A 226  LYS A 230 -1  N  VAL A 227   O  TRP A 215           
SHEET    7   A 7 MET A 180  VAL A 183 -1  O  VAL A 181   N  TYR A 228           
SHEET    1   B 7 GLN A  30  ASN A  34  0                                        
SHEET    2   B 7 HIS A  40  ASN A  48 -1  N  PHE A  41   O  LEU A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  TRP A  51   N  ILE A  47           
SHEET    4   B 7 MET A 104  LEU A 108 -1  O  MET A 104   N  SER A  54           
SHEET    5   B 7 GLN A  81  LYS A  90 -1  N  ALA A  86   O  LYS A 107           
SHEET    6   B 7 GLN A  64  LEU A  68 -1  N  VAL A  66   O  VAL A  83           
SHEET    7   B 7 GLN A  30  ASN A  34 -1  O  SER A  32   N  ARG A  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 A   22    CYS A  157                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.03  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.03  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.03  
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  2.03  
LINK        CA    CA A 800                 O   ASN A  72     1555   1555  2.38  
LINK        CA    CA A 800                 O   VAL A  75     1555   1555  2.33  
LINK        CA    CA A 800                 OE1 GLU A  70     1555   1555  2.18  
LINK        CA    CA A 800                 O   HOH A 570     1555   1555  1.67  
LINK        CA    CA A 800                 O   HOH A 610     1555   1555  2.35  
LINK        CA    CA A 800                 OE2 GLU A  80     1555   1555  2.35  
LINK        CA    CA A 800                 OE1 GLU A  77     1555   1555  2.43  
SITE     1 AC1  2 ARG I  42  HOH I 615                                          
SITE     1 AC2  3 ARG I  20  TYR I  35  HOH I 650                               
SITE     1 AC3  7 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC3  7 GLU A  80  HOH A 570  HOH A 610                               
CRYST1   92.696   92.696   62.076  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      0.010788  0.006228 -0.000001        0.00000                         
SCALE2      0.000000  0.012457 -0.000001        0.00000                         
SCALE3      0.000000  0.000000  0.016109        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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