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Database: PDB
Entry: 1FN6
LinkDB: 1FN6
Original site: 1FN6 
HEADER    HYDROLASE                               21-AUG-00   1FN6              
TITLE     CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.1%                   
TITLE    2 POLYDOCANOL                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.4                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: PANCREAS                                                      
KEYWDS    SERINE PROTEASE, HYDROLASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DEEPTHI,A.JOHNSON,V.PATTABHI                                        
REVDAT   4   24-FEB-09 1FN6    1       VERSN                                    
REVDAT   3   01-APR-03 1FN6    1       JRNL                                     
REVDAT   2   07-NOV-01 1FN6    1       JRNL                                     
REVDAT   1   13-SEP-00 1FN6    0                                                
JRNL        AUTH   S.DEEPTHI,A.JOHNSON,V.PATTABHI                               
JRNL        TITL   STRUCTURES OF PORCINE BETA-TRYPSIN-DETERGENT                 
JRNL        TITL 2 COMPLEXES: THE STABILIZATION OF PROTEINS THROUGH             
JRNL        TITL 3 HYDROPHILIC BINDING OF POLYDOCANOL.                          
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  57  1506 2001              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   11679713                                                     
JRNL        DOI    10.1107/S0907444901011143                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.JOHNSON,N.GAUTHAM,V.PATTABHI                               
REMARK   1  TITL   CRYSTAL STRUCTURE AT 1.63 ANGSTROMS RESOLUTION OF            
REMARK   1  TITL 2 THE NATIVE FORM OF PORCINE BETA TRYPSIN :                    
REMARK   1  TITL 3 REVEALING AN ACETATE ION BINDING SITE AND                    
REMARK   1  TITL 4 FUNCTIONAL WATER NETWORK                                     
REMARK   1  REF    BIOCHIM.BIOPHYS.ACTA          V.1435     7 1999              
REMARK   1  REFN                   ISSN 0006-3002                               
REMARK   1  DOI    10.1016/S0167-4838(99)00202-2                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.JOHNSON,S.KRISHNASWAMY,P.V.SUNDARAM,V.PATTABHI             
REMARK   1  TITL   THE FIRST STRUCTURE AT 1.8 ANGSTROMS RESOLUTION OF           
REMARK   1  TITL 2 AN ACTIVE AUTOLYSATE FORM OF PORCINE ALPHA TRYPSIN           
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  53   311 1997              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  DOI    10.1107/S0907444997000358                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR, REFMAC                                       
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 17473                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R                          
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM R VALUE (WORKING +       
REMARK   3                                      TEST SET) : 0.162               
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.161                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 608                             
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1642                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 158                                     
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1FN6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-AUG-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011733.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-MAR-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 6.70                               
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          : COPPER K-ALPHA                     
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MARXDS                             
REMARK 200  DATA SCALING SOFTWARE          : MARSCALE                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17686                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 26.260                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.6                               
REMARK 200  DATA REDUNDANCY                : 3.840                              
REMARK 200  R MERGE                    (I) : 0.06770                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.6100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44950                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.350                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: 1QQU                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.70, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       38.95200            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.61900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       27.02150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       23.61900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       38.95200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       27.02150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 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   O3   SO4 A   433     O    HOH A   511              2.10            
REMARK 500   NH2  ARG A    62     O    HOH A   529              2.15            
REMARK 500   OE1  GLN A   240     O    HOH A   592              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OH   TYR A   217     OE1  GLN A   239     3645     2.08            
REMARK 500   NE   ARG A    62     O    HOH A   554     3645     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  62   CD  -  NE  -  CZ  ANGL. DEV. =  11.0 DEGREES          
REMARK 500    ASN A  97   CB  -  CA  -  C   ANGL. DEV. = -19.6 DEGREES          
REMARK 500    ASP A 189   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    GLN A 221   CA  -  CB  -  CG  ANGL. DEV. =  25.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  71      -54.23   -128.45                                   
REMARK 500    LEU A  99       19.21     59.28                                   
REMARK 500    ASN A 115     -162.86   -166.63                                   
REMARK 500    SER A 146      -74.54    -56.18                                   
REMARK 500    SER A 150       92.10    156.23                                   
REMARK 500    SER A 214      -67.59   -125.10                                   
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 432  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A  75   O                                                      
REMARK 620 2 ASN A  72   O    84.4                                              
REMARK 620 3 GLU A  77   OE1 111.8  91.8                                        
REMARK 620 4 HOH A 469   O    79.2  91.8 168.7                                  
REMARK 620 5 GLU A  80   OE2  94.9 175.4  84.3  92.5                            
REMARK 620 6 GLU A  70   OE1 150.6  85.0  95.8  73.8  97.6                      
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 432                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 433                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 436                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 438                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MOH A 434                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QQU   RELATED DB: PDB                                   
REMARK 900 1QQU CONTAINS THE SAME PROTEIN WITH BOUND ACETATE ION.               
REMARK 900 RELATED ID: 1FMG   RELATED DB: PDB                                   
REMARK 900 1FMG CONTAINS THE SAME PROTEIN.                                      
REMARK 900 RELATED ID: 1FNI   RELATED DB: PDB                                   
REMARK 900 1FNI CONTAINS THE SAME PROTEIN.                                      
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE 223 AMINO ACIDS OF TRYPSIN ARE IDENTIFIED BY THE                 
REMARK 999 RESIDUE NUMBERS OF THE HOMOLOGOUS CHYMOTRYPSINOGEN.                  
DBREF  1FN6 A   16   245  UNP    P00761   TRYP_PIG         9    231             
SEQADV 1FN6 ASN A  165  UNP  P00761    ASP   153 SEE REMARK 999                 
SEQADV 1FN6 GLN A  186  UNP  P00761    GLU   175 SEE REMARK 999                 
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 A  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 A  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 A  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 A  223  SER ASN SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLN GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 A  223  ALA ASN                                                      
HET     CA  A 432       1                                                       
HET    SO4  A 433       5                                                       
HET    EDO  A 436       4                                                       
HET    EDO  A 438       4                                                       
HET    MOH  A 434       2                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     MOH METHANOL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  EDO    2(C2 H6 O2)                                                  
FORMUL   6  MOH    C H4 O                                                       
FORMUL   7  HOH   *156(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 SER A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  ALA A  244  1                                  11    
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 GLU 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 GLN A 204  TRP A 215 -1  O  GLN 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  ILE 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  THR A  90 -1  N  ALA A  86   O  LYS A 107           
SHEET    6   B 7 GLN A  64  LEU A  67 -1  N  VAL A  65   O  ILE A  83           
SHEET    7   B 7 GLN A  30  ASN A  34 -1  O  SER A  32   N  ARG A  66           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.06  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.09  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.12  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.13  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.10  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.18  
LINK        CA    CA A 432                 O   VAL A  75     1555   1555  2.45  
LINK        CA    CA A 432                 O   ASN A  72     1555   1555  2.43  
LINK        CA    CA A 432                 OE1 GLU A  77     1555   1555  2.50  
LINK        CA    CA A 432                 O   HOH A 469     1555   1555  2.64  
LINK        CA    CA A 432                 OE2 GLU A  80     1555   1555  2.39  
LINK        CA    CA A 432                 OE1 GLU A  70     1555   1555  2.46  
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 469                                          
SITE     1 AC2  6 HIS A  57  CYS A 128  GLN A 192  GLY A 193                    
SITE     2 AC2  6 SER A 195  HOH A 511                                          
SITE     1 AC3  9 ALA A  23  ASN A  25  SER A  26  ILE A  27                    
SITE     2 AC3  9 PRO A  28  GLU A  70  HIS A  71  LEU A 155                    
SITE     3 AC3  9 HOH A 451A                                                    
SITE     1 AC4  8 ARG A 125  CYS A 191  GLN A 192  GLY A 216                    
SITE     2 AC4  8 GLY A 219  HOH A 491  HOH A 494  HOH A 510                    
SITE     1 AC5  4 GLN A 192  CYS A 232  VAL A 235  ASN A 236                    
CRYST1   77.904   54.043   47.238  90.00  90.00  90.00 P 21 21 21    4          
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      0.012836  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018504  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021169        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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