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Database: PDB
Entry: 3FP6
LinkDB: 3FP6
Original site: 3FP6 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           04-JAN-09   3FP6              
TITLE     ANIONIC TRYPSIN IN COMPLEX WITH BOVINE PANCREATIC TRYPSIN             
TITLE    2 INHIBITOR (BPTI) DETERMINED TO THE 1.49 A RESOLUTION LIMIT           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANIONIC TRYPSIN-2;                                         
COMPND   3 CHAIN: E;                                                            
COMPND   4 SYNONYM: ANIONIC TRYPSIN II, PRETRYPSINOGEN II, SERINE               
COMPND   5 PROTEASE 2;                                                          
COMPND   6 EC: 3.4.21.4;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PANCREATIC TRYPSIN INHIBITOR;                              
COMPND  10 CHAIN: I;                                                            
COMPND  11 SYNONYM: BASIC PROTEASE INHIBITOR, BPTI, BPI, APROTININ              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: PRSS2, TRY2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: DLM101;                                    
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PYT;                                      
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  14 ORGANISM_COMMON: BOVINE,COW,DOMESTIC CATTLE,DOMESTIC COW;            
SOURCE  15 ORGANISM_TAXID: 9913                                                 
KEYWDS    ENZYME-INHIBITOR COMPLEX, CALCIUM, DIGESTION, HYDROLASE,              
KEYWDS   2 METAL-BINDING, PROTEASE, SECRETED, SERINE PROTEASE,                  
KEYWDS   3 ZYMOGEN, PHARMACEUTICAL, PROTEASE INHIBITOR, SERINE                  
KEYWDS   4 PROTEASE INHIBITOR, HYDROLASE/HYDROLASE INHIBITOR COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.ZAKHAROVA,M.P.HORVATH,D.P.GOLDENBERG                                
REVDAT   2   18-AUG-09 3FP6    1       JRNL                                     
REVDAT   1   17-FEB-09 3FP6    0                                                
JRNL        AUTH   E.ZAKHAROVA,M.P.HORVATH,D.P.GOLDENBERG                       
JRNL        TITL   STRUCTURE OF A SERINE PROTEASE POISED TO                     
JRNL        TITL 2 RESYNTHESIZE A PEPTIDE BOND.                                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106 11034 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19549826                                                     
JRNL        DOI    10.1073/PNAS.0902463106                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS1.2                                               
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) : 1.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
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)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 48502                          
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) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3859                            
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           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.49                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.58                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.90                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 7221                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2729                       
REMARK   3   BIN FREE R VALUE                    : 0.2845                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 8.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 645                          
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            : 2233                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 89                                      
REMARK   3   SOLVENT ATOMS            : 315                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 20.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.10                          
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) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.16                            
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) : 0.19                            
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) : 1.45                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.22                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 0.940 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.480 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.450 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.090 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : CNS SOLVE                                            
REMARK   3   KSOL        : 0.40                                                 
REMARK   3   BSOL        : 36.47                                                
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.PARAM                                  
REMARK   3  PARAMETER FILE  2  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : LIGAND.PARAM                                   
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : LIGAND.TOP                                     
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: SIMULATED ANNEALING TORSION ANGLE         
REMARK   3  REFINEMENT, POSITIONAL REFINEMENT, RESTRAINED ISOTROPIC             
REMARK   3  INDIVIDUAL B-VALUE REFINEMENT, COUPLED WITH MODEL ADJUSTMENT        
REMARK   3  ON THE BASIS OF SIGMA-A WEIGHTED AND COMPOSITE SIMULATED            
REMARK   3  ANNEALING OMIT ELECTRON DENSITY MAPS                                
REMARK   4                                                                      
REMARK   4 3FP6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-JAN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB050868.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-DEC-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.5                                
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          : NONIUS FR-591 (6 KW)               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : OSMIC CONFOCAL MAX-FLUX            
REMARK 200                                   (GREEN)                            
REMARK 200  OPTICS                         : OSMIC CONFOCAL MAX-FLUX            
REMARK 200                                   (GREEN)                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NONIUS KAPPA CCD                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48520                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.42700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 3TGI                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M LITHIUM SULFATE, 0.1M TRIS,         
REMARK 280  16% (W/V) PEG 4000, PH 7.5, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 295K                                                    
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       40.90133            
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       20.45067            
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       20.45067            
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       40.90133            
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 300 REMARK: AUTHORS STATE THAT THE QUATERNARY STRUCTURE IS A             
REMARK 300 HETERODIMER.                                                         
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: 3460 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH E 717  LIES ON A SPECIAL POSITION.                          
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     ARG E  62    NE   NH1  NH2                                       
REMARK 470     LYS E  97    CD   CE   NZ                                        
REMARK 470     LYS E 113    CD   CE   NZ                                        
REMARK 470     LYS I  26    CG   CD   CE   NZ                                   
REMARK 470     GLU I  49    CG   CD   OE1  OE2                                  
REMARK 470     ALA I  58    O                                                   
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 E  49       -4.01    -59.01                                   
REMARK 500    HIS E  71      -62.32   -126.18                                   
REMARK 500    SER E 214      -70.00   -126.14                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     ASN E  25        24.2      L          L   OUTSIDE RANGE          
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 E 802        DISTANCE =  5.17 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 E 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  70   OE1                                                    
REMARK 620 2 ASN E  72   O    87.9                                              
REMARK 620 3 VAL E  75   O   159.6  84.9                                        
REMARK 620 4 GLU E  77   OE1  93.2  86.9 105.4                                  
REMARK 620 5 GLU E  80   OE2 103.7 165.6  86.8  84.0                            
REMARK 620 6 HOH E 776   O    79.2 102.4  83.7 167.7  88.3                      
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 EDO E 501                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 502                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 503                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 504                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 505                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 506                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E 507                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 E 509                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 601                  
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 E 602                 
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I 508                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 603                 
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 604                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 605                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3TGI   RELATED DB: PDB                                   
REMARK 900 ANIONIC TRYPSIN COMPLEXED WITH BOVINE PANCREATIC TRYPSIN             
REMARK 900 INHIBITOR (BPTI) DETERMINED TO THE 1.8 A RESOLUTION LIMIT            
REMARK 900 RELATED ID: 3FP7   RELATED DB: PDB                                   
REMARK 900 ANIONIC TRYPSIN VARIANT S195A IN COMPLEX WITH BPTI                   
REMARK 900 DETERMINED TO THE 1.46 A RESOLUTION LIMIT                            
REMARK 900 RELATED ID: 3FP8   RELATED DB: PDB                                   
REMARK 900 ANIONIC TRYPSIN VARIANT S195A IN COMPLEX WITH CLEAVED BPTI           
REMARK 900 (LYS15/ALA16) DETERMINED TO THE 1.46 A RESOLUTION LIMIT              
DBREF  3FP6 E   16   245  UNP    P00763   TRY2_RAT        24    246             
DBREF  3FP6 I    1    58  UNP    P00974   BPT1_BOVIN      36     93             
SEQRES   1 E  223  ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO          
SEQRES   2 E  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 E  223  GLY SER LEU ILE ASN ASP GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 E  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 E  223  HIS ASN ILE ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL          
SEQRES   6 E  223  ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG          
SEQRES   7 E  223  LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 E  223  SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA          
SEQRES   9 E  223  LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU          
SEQRES  10 E  223  ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN          
SEQRES  11 E  223  GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU          
SEQRES  12 E  223  PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 E  223  THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 E  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 E  223  CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 E  223  GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS          
SEQRES  17 E  223  VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA          
SEQRES  18 E  223  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    EDO  E 501       4                                                       
HET    EDO  E 502       4                                                       
HET    EDO  E 503       4                                                       
HET    EDO  E 504       4                                                       
HET    EDO  E 505       4                                                       
HET    EDO  E 506       4                                                       
HET    EDO  E 507       4                                                       
HET    PG4  E 509      26                                                       
HET     CA  E 601       1                                                       
HET    SO4  E 602      15                                                       
HET    EDO  I 508       4                                                       
HET    SO4  I 603       5                                                       
HET    SO4  I 604       5                                                       
HET    SO4  I 605       5                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    8(C2 H6 O2)                                                  
FORMUL  10  PG4    C8 H18 O5                                                    
FORMUL  11   CA    CA 2+                                                        
FORMUL  12  SO4    4(O4 S 2-)                                                   
FORMUL  17  HOH   *299(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  O  CYS E 157   N  TYR E  20           
SHEET    3   A 7 GLN E 135  GLY E 140 -1  N  ILE E 138   O  LEU E 158           
SHEET    4   A 7 PRO E 198  CYS E 201 -1  O  VAL E 200   N  LEU E 137           
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  O  VAL E 227   N  TRP E 215           
SHEET    7   A 7 MET E 180  VAL E 183 -1  N  VAL E 181   O  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  O  CYS E  42   N  LEU E  33           
SHEET    3   B 7 TRP E  51  SER E  54 -1  O  VAL E  53   N  SER E  45           
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  ILE E  89   O  LEU E 105           
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  N  SER E  32   O  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  TYR I  35   N  ILE I  18           
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  2.04  
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         OE1 GLU E  70                CA    CA E 601     1555   1555  2.24  
LINK         O   ASN E  72                CA    CA E 601     1555   1555  2.30  
LINK         O   VAL E  75                CA    CA E 601     1555   1555  2.27  
LINK         OE1 GLU E  77                CA    CA E 601     1555   1555  2.49  
LINK         OE2 GLU E  80                CA    CA E 601     1555   1555  2.29  
LINK        CA    CA E 601                 O   HOH E 776     1555   1555  2.28  
SITE     1 AC1  9 ASN E  34  GLY E  38  TYR E  39  HIS E  40                    
SITE     2 AC1  9 ARG E  67  ILE E  73  HOH E 709  HOH E 718                    
SITE     3 AC1  9 HOH E 779                                                     
SITE     1 AC2  3 ASN E 100  ASN E 101  ASN E 179                               
SITE     1 AC3  4 TYR E  59  ILE E  88  LYS E  90  ASP E 236                    
SITE     1 AC4  7 ASN E 143  CYS E 191  GLN E 192  HOH E 784                    
SITE     2 AC4  7 HOH E 884  HOH E 890  VAL I  34                               
SITE     1 AC5  6 ILE E  47  ASN E  48  LEU E 123  GLN E 239                    
SITE     2 AC5  6 HOH E 823  HOH E 830                                          
SITE     1 AC6  6 LYS E  97  THR E  98  TRP E 215  TYR E 217                    
SITE     2 AC6  6 HOH E 864  HOH E 900                                          
SITE     1 AC7  9 TYR E 217  GLY E 219  HOH E 895  ASP I   3                    
SITE     2 AC7  9 TYR I  10  GLY I  12  PRO I  13  EDO I 508                    
SITE     3 AC7  9 HOH I 713                                                     
SITE     1 AC8  7 GLY E  18  PHE E 184A GLU E 186  GLY E 187                    
SITE     2 AC8  7 GLY E 188  LYS E 188A HOH E 911                               
SITE     1 AC9  6 GLU E  70  ASN E  72  VAL E  75  GLU E  77                    
SITE     2 AC9  6 GLU E  80  HOH E 776                                          
SITE     1 BC1  6 LYS E 175  HOH E 858  HOH E 900  ARG I  39                    
SITE     2 BC1  6 ARG I  42  HOH I 718                                          
SITE     1 BC2  6 EDO E 507  ASP I   3  PHE I   4  TYR I  10                    
SITE     2 BC2  6 LYS I  41  SO4 I 605                                          
SITE     1 BC3  8 ARG I  20  TYR I  35  ALA I  40  HOH I 717                    
SITE     2 BC3  8 HOH I 741  HOH I 748  HOH I 751  HOH I 752                    
SITE     1 BC4  9 LYS E  60  HOH E 751  HOH E 852  ILE I  18                    
SITE     2 BC4  9 ILE I  19  ARG I  20  HOH I 742  HOH I 761                    
SITE     3 BC4  9 HOH I 763                                                     
SITE     1 BC5  7 LYS I  41  ARG I  42  EDO I 508  HOH I 701                    
SITE     2 BC5  7 HOH I 708  HOH I 730  HOH I 731                               
CRYST1   91.634   91.634   61.352  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      0.010913  0.006301  0.000000        0.00000                         
SCALE2      0.000000  0.012601  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016299        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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