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Database: PDB
Entry: 1F5R
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Original site: 1F5R 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           15-JUN-00   1F5R              
TITLE     RAT TRYPSINOGEN MUTANT 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,M.CAHOON,D.RINGE,L.HEDSTROM                       
REVDAT   2   24-FEB-09 1F5R    1       VERSN                                    
REVDAT   1   04-JUL-01 1F5R    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   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.PASTERNAK,D.RINGE,L.HEDSTROM                               
REMARK   1  TITL   COMPARISON OF ANIONIC AND CATIONIC TRYPSINOGENS:             
REMARK   1  TITL 2 THE ANIONIC ACTIVATION DOMAIN IS MORE FLEXIBLE IN            
REMARK   1  TITL 3 SOLUTION AND DIFFERS IN ITS MODE OF BPTI BINDING             
REMARK   1  TITL 4 IN THE CRYSTAL STRUCTURE                                     
REMARK   1  REF    PROTEIN SCI.                  V.   8   253 1999              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.PASTERNAK,X.LIU,T.-Y.LIN,L.HEDSTROM                        
REMARK   1  TITL   ACTIVATING A ZYMOGEN WITHOUT PROTEOLYTIC                     
REMARK   1  TITL 2 PROCESSING: MUTATION OF LYS15 AND ASN194 ACTIVATES           
REMARK   1  TITL 3 TRYPSINOGEN.                                                 
REMARK   1  REF    BIOCHEMISTRY                  V.  37 16201 1998              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  DOI    10.1021/BI980951D                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.69                          
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)   (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 34897                          
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) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3489                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4328                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE                    : 0.3150                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.40                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 505                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.014                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2101                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 270                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.26000                                              
REMARK   3    B22 (A**2) : 0.26000                                              
REMARK   3    B33 (A**2) : -0.52000                                             
REMARK   3    B12 (A**2) : -0.93000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.19                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.17                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.17                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.30                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.78                            
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) : 0.580 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.040 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 0.720 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 1.150 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 48.06                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1F5R COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011276.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-DEC-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 277.                               
REMARK 200  PH                             : 6.5                                
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 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   : 195481                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 21.690                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.6                               
REMARK 200  DATA REDUNDANCY                : 5.450                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.5600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.68                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.92                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24200                            
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   (%): 48.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 22% PEG 3380, 300 MM AMMONIUM            
REMARK 280  ACETATE, 100 MM SODIUM ACETATE, , PH 6.5, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 298.0K                                    
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       41.41733            
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       20.70867            
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       20.70867            
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       41.41733            
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: 1460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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     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     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 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    ASP A  49        0.95    -56.27                                   
REMARK 500    HIS A  71      -66.10   -136.96                                   
REMARK 500    ASP A 153      -71.63   -139.80                                   
REMARK 500    SER A 214      -69.71   -123.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH I 688        DISTANCE =  6.90 ANGSTROMS                       
REMARK 525    HOH A 749        DISTANCE =  7.10 ANGSTROMS                       
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    83.9                                              
REMARK 620 3 GLU A  70   OE1  93.9 146.8                                        
REMARK 620 4 HOH A 535   O   116.2  76.4  75.0                                  
REMARK 620 5 GLU A  80   OE2 165.3  82.9 100.7  66.8                            
REMARK 620 6 GLU A  77   OE1  91.7 114.9  98.2 151.4  87.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 800                  
DBREF  1F5R A    7   245  UNP    P00763   TRY2_RAT        15    246             
DBREF  1F5R I    1    65  UNP    P00974   BPT1_BOVIN      36    100             
SEQADV 1F5R GLU A    6  UNP  P00763              CLONING ARTIFACT               
SEQADV 1F5R     A       UNP  P00763    ILE    24 DELETION                       
SEQADV 1F5R     A       UNP  P00763    VAL    25 DELETION                       
SEQADV 1F5R LYS A  156  UNP  P00763    GLN   159 ENGINEERED                     
SEQRES   1 A  231  GLU ALA PHE PRO VAL ASP ASP ASP ASP LYS GLY GLY TYR          
SEQRES   2 A  231  THR CYS GLN GLU ASN SER VAL PRO TYR GLN VAL SER LEU          
SEQRES   3 A  231  ASN SER GLY TYR HIS PHE CYS GLY GLY SER LEU ILE ASN          
SEQRES   4 A  231  ASP GLN TRP VAL VAL SER ALA ALA HIS CYS TYR LYS SER          
SEQRES   5 A  231  ARG ILE GLN VAL ARG LEU GLY GLU HIS ASN ILE ASN VAL          
SEQRES   6 A  231  LEU GLU GLY ASN GLU GLN PHE VAL ASN ALA ALA LYS ILE          
SEQRES   7 A  231  ILE LYS HIS PRO ASN PHE ASP ARG LYS THR LEU ASN ASN          
SEQRES   8 A  231  ASP ILE MET LEU ILE LYS LEU SER SER PRO VAL LYS LEU          
SEQRES   9 A  231  ASN ALA ARG VAL ALA THR VAL ALA LEU PRO SER SER CYS          
SEQRES  10 A  231  ALA PRO ALA GLY THR GLN CYS LEU ILE SER GLY TRP GLY          
SEQRES  11 A  231  ASN THR LEU SER SER GLY VAL ASN GLU PRO ASP LEU LEU          
SEQRES  12 A  231  LYS CYS LEU ASP ALA PRO LEU LEU PRO GLN ALA ASP CYS          
SEQRES  13 A  231  GLU ALA SER TYR PRO GLY LYS ILE THR ASP ASN MET VAL          
SEQRES  14 A  231  CYS VAL GLY PHE LEU GLU GLY GLY LYS ASP SER CYS GLN          
SEQRES  15 A  231  GLY ASP SER GLY GLY PRO VAL VAL CYS ASN GLY GLU LEU          
SEQRES  16 A  231  GLN GLY ILE VAL SER TRP GLY TYR GLY CYS ALA LEU PRO          
SEQRES  17 A  231  ASP ASN PRO GLY VAL TYR THR LYS VAL CYS ASN TYR VAL          
SEQRES  18 A  231  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     CA  A 800       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *270(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 LYS 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  2.04  
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  2.51  
LINK        CA    CA A 800                 O   VAL A  75     1555   1555  2.32  
LINK        CA    CA A 800                 OE1 GLU A  70     1555   1555  2.32  
LINK        CA    CA A 800                 O   HOH A 535     1555   1555  2.92  
LINK        CA    CA A 800                 OE2 GLU A  80     1555   1555  2.42  
LINK        CA    CA A 800                 OE1 GLU A  77     1555   1555  2.52  
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC1  6 GLU A  80  HOH A 535                                          
CRYST1   92.568   92.568   62.126  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      0.010803  0.006237  0.000000        0.00000                         
SCALE2      0.000000  0.012474  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016096        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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