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Database: PDB
Entry: 1BRC
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HEADER    COMPLEX(PROTEINASE/INHIBITOR)           17-DEC-92   1BRC              
TITLE     RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF                 
TITLE    2 TRYPSIN                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: E;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: AMYLOID BETA-PROTEIN PRECURSOR INHIBITOR DOMAIN            
COMPND   8 (APPI);                                                              
COMPND   9 CHAIN: I;                                                            
COMPND  10 ENGINEERED: YES                                                      
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: UNIDENTIFIED;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 32644;                                      
SOURCE   7 MOL_ID: 2                                                            
KEYWDS    COMPLEX(PROTEINASE/INHIBITOR)                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.PERONA,R.J.FLETTERICK                                             
REVDAT   3   24-FEB-09 1BRC    1       VERSN                                    
REVDAT   2   01-APR-03 1BRC    1       JRNL                                     
REVDAT   1   31-MAY-94 1BRC    0                                                
JRNL        AUTH   J.J.PERONA,C.A.TSU,M.E.MCGRATH,C.S.CRAIK,                    
JRNL        AUTH 2 R.J.FLETTERICK                                               
JRNL        TITL   RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET           
JRNL        TITL 2 OF TRYPSIN.                                                  
JRNL        REF    J.MOL.BIOL.                   V. 230   934 1993              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   8478942                                                      
JRNL        DOI    10.1006/JMBI.1993.1211                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.J.PERONA,C.A.TSU,C.S.CRAIK,R.J.FLETTERICK                  
REMARK   1  TITL   CRYSTAL STRUCTURES OF RAT ANIONIC TRYPSIN                    
REMARK   1  TITL 2 COMPLEXED WITH THE PROTEIN INHIBITORS APPI AND BPTI          
REMARK   1  REF    J.MOL.BIOL.                   V. 230   919 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   T.R.HYNES,M.RANDAL,L.A.KENNEDY,C.EIGENBROT,                  
REMARK   1  AUTH 2 A.A.KOSSIAKOFF                                               
REMARK   1  TITL   X-RAY CRYSTAL STRUCTURE OF THE PROTEASE INHIBITOR            
REMARK   1  TITL 2 DOMAIN OF ALZHEIMER'S AMYLOID BETA-PROTEIN                   
REMARK   1  TITL 3 PRECURSOR                                                    
REMARK   1  REF    BIOCHEMISTRY                  V.  29 10018 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2054                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 141                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.80                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1BRC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.66                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.66667            
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       20.83333            
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       20.83333            
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       41.66667            
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: 1320 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE APPI INHIBITOR REPRESENTS A KUNITZ-TYPE (BPTI-LIKE)              
REMARK 400 SERINE PROTEASE INHIBITOR WHICH POSSESSES 45 PER CENT                
REMARK 400 SEQUENCE IDENTITY AND A HIGH DEGREE OF STRUCTURAL                    
REMARK 400 SIMILARITY WITH BPTI.  THIS INHIBITOR DOMAIN IS DERIVED              
REMARK 400 FROM THE AMYLOID BETA-PROTEIN PRECURSOR POLYPEPTIDE, AND IS          
REMARK 400 INVOLVED IN THE ABNORMAL DEPOSITION OF CEREBRAL AMYLOID              
REMARK 400 DEPOSITS IN INDIVIDUALS WITH ALZHEIMER'S DISEASE.                    
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  96    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E  97    CG   CD   CE   NZ                                   
REMARK 470     GLU E 151    CG   CD   OE1  OE2                                  
REMARK 470     GLN E 165    CG   CD   OE1  NE2                                  
REMARK 470     GLN E 239    CG   CD   OE1  NE2                                  
REMARK 470     GLN I   8    CG   CD   OE1  NE2                                  
REMARK 470     GLU I  10    CG   CD   OE1  OE2                                  
REMARK 470     GLU I  27    CG   CD   OE1  OE2                                  
REMARK 470     ARG I  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU I  49    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS E  91   NE2   HIS E  91   CD2    -0.068                       
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    TRP E  51   CD1 -  CG  -  CD2 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    TRP E  51   CB  -  CG  -  CD1 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    TRP E  51   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    TRP E  51   CG  -  CD2 -  CE3 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    VAL E 183   CG1 -  CB  -  CG2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    TRP E 215   CD1 -  CG  -  CD2 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    TRP E 215   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    TRP E 215   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TRP E 237   CD1 -  CG  -  CD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    TRP E 237   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    TRP I  21   CD1 -  CG  -  CD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    TRP I  21   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    CYS I  38   CA  -  CB  -  SG  ANGL. DEV. =   7.1 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    VAL E  27       69.41   -111.51                                   
REMARK 500    ASP E  49      -29.90    -32.04                                   
REMARK 500    HIS E  71      -56.80   -125.51                                   
REMARK 500    ASN E 115     -166.73   -170.15                                   
REMARK 500    SER E 214      -71.15   -127.56                                   
REMARK 500    ARG I   2      -65.05     41.95                                   
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 310        DISTANCE =  9.04 ANGSTROMS                       
REMARK 525    HOH E 323        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH E 339        DISTANCE =  7.98 ANGSTROMS                       
REMARK 525    HOH E 438        DISTANCE =  5.00 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CAT                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD RESIDUES, CONSERVED IN ALL         
REMARK 800  SERINE PROTEASES OF THE TRYPSIN AND SUBTILISIN STRUCTURAL           
REMARK 800  CLASSES                                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE ADVISORY NOTICE                                             
REMARK 999      DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE.                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT ENTRY NAME: TRY2_RAT                                 
REMARK 999                                                                      
REMARK 999      SWISS-PROT RESIDUE      PDB SEQRES                              
REMARK 999                                                                      
REMARK 999        NAME   NUMBER         NAME   CHAIN  SEQ/INSERT CODE           
REMARK 999        ASP       84          ASN     E       79                      
REMARK 999        ILE       88          VAL     E       83                      
REMARK 999                                                                      
REMARK 999 THE SEQUENCE FOR TRYPSIN IN THIS STRUCTURE WAS TAKEN FROM            
REMARK 999 GENEMBL WHICH DIFFERS FROM THE SWISSPROT SEQUENCE.                   
DBREF  1BRC E   16   245  UNP    P00763   TRY2_RAT        24    246             
DBREF  1BRC I    1    56  UNP    P05067   A4_HUMAN       287    342             
SEQADV 1BRC GLY E  189  UNP  P00763    ASP   194 CONFLICT                       
SEQADV 1BRC ASP E  226  UNP  P00763    GLY   227 CONFLICT                       
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 GLY 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 ASP 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   56  VAL ARG GLU VAL CYS SER GLU GLN ALA GLU THR GLY PRO          
SEQRES   2 I   56  CYS ARG ALA MET ILE SER ARG TRP TYR PHE ASP VAL THR          
SEQRES   3 I   56  GLU GLY LYS CYS ALA PRO PHE PHE TYR GLY GLY CYS GLY          
SEQRES   4 I   56  GLY ASN ARG ASN ASN PHE ASP THR GLU GLU TYR CYS MET          
SEQRES   5 I   56  ALA VAL CYS GLY                                              
FORMUL   3  HOH   *141(H2 O)                                                    
HELIX    1 SHA PRO E  164  TYR E  172  1IRREGULAR AFTER CYS 168            9    
HELIX    2 31A LYS E  230  VAL E  235  5LEADS INTO TERMINAL ALPHA-HLX      6    
HELIX    3 TEA TYR E  234  ASN E  245  1C-TERMINAL HELIX                  12    
HELIX    4  H2 THR I   47  GLY I   56  1                                  10    
SHEET    1 S1A 7 TYR E  20  TYR E  20  0                                        
SHEET    2 S1A 7 GLN E 156  PRO E 161 -1  O  CYS E 157   N  TYR E  20           
SHEET    3 S1A 7 CYS E 136  GLY E 140 -1  O  CYS E 136   N  ALA E 160           
SHEET    4 S1A 7 GLY E 197  CYS E 201 -1  N  VAL E 200   O  LEU E 137           
SHEET    5 S1A 7 GLU E 204  TRP E 215 -1  N  VAL E 213   O  GLY E 197           
SHEET    6 S1A 7 ASP E 226  VAL E 231 -1  N  VAL E 227   O  TRP E 215           
SHEET    7 S1A 7 ASN E 179  VAL E 183 -1  N  VAL E 183   O  ASP E 226           
SHEET    1 S2A 4 GLY E  43  SER E  45  0                                        
SHEET    2 S2A 4 VAL E  52  ALA E  55 -1  N  VAL E  53   O  SER E  45           
SHEET    3 S2A 4 ILE E 103  LYS E 107 -1  O  MET E 104   N  SER E  54           
SHEET    4 S2A 4 LYS E  87  HIS E  91 -1  N  HIS E  91   O  ILE E 103           
SHEET    1 S3A 2 ILE E  63  VAL E  66  0                                        
SHEET    2 S3A 2 GLN E  81  ALA E  85 -1  N  GLN E  81   O  VAL E  66           
SHEET    1  S4 3 LYS I  29  TYR I  35  0                                        
SHEET    2  S4 3 ILE I  18  ASP I  24 -1  N  ILE I  18   O  TYR I  35           
SHEET    3  S4 3 PHE I  45  PHE I  45 -1  N  PHE I  45   O  TRP I  21           
SSBOND   1 CYS E   22    CYS E  157                          1555   1555  2.02  
SSBOND   2 CYS E   42    CYS E   58                          1555   1555  2.02  
SSBOND   3 CYS E  128    CYS E  232                          1555   1555  2.02  
SSBOND   4 CYS E  136    CYS E  201                          1555   1555  2.01  
SSBOND   5 CYS E  168    CYS E  182                          1555   1555  2.00  
SSBOND   6 CYS E  191    CYS E  220                          1555   1555  2.02  
SSBOND   7 CYS I    5    CYS I   55                          1555   1555  2.02  
SSBOND   8 CYS I   14    CYS I   38                          1555   1555  2.02  
SSBOND   9 CYS I   30    CYS I   51                          1555   1555  2.01  
SITE     1 CAT  3 HIS E  57  ASP E 102  SER E 195                               
CRYST1   93.100   93.100   62.500  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      0.010741  0.006201  0.000000        0.00000                         
SCALE2      0.000000  0.012403  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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