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Database: PDB
Entry: 1BRA
LinkDB: 1BRA
Original site: 1BRA 
HEADER    PROTEINASE/INHIBITOR                    17-DEC-92   1BRA              
TITLE     RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF TRYPSIN         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS RATTUS;                                  
SOURCE   3 ORGANISM_COMMON: BLACK RAT;                                          
SOURCE   4 ORGANISM_TAXID: 10117                                                
KEYWDS    PROTEINASE/INHIBITOR, PROTEINASE-INHIBITOR COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.J.PERONA,M.E.MCGRATH,R.J.FLETTERICK                                 
REVDAT   4   29-NOV-17 1BRA    1       HELIX                                    
REVDAT   3   24-FEB-09 1BRA    1       VERSN                                    
REVDAT   2   01-APR-03 1BRA    1       JRNL                                     
REVDAT   1   30-APR-94 1BRA    0                                                
JRNL        AUTH   J.J.PERONA,C.A.TSU,M.E.MCGRATH,C.S.CRAIK,R.J.FLETTERICK      
JRNL        TITL   RELOCATING A NEGATIVE CHARGE IN THE BINDING POCKET OF        
JRNL        TITL 2 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 COMPLEXED WITH THE 
REMARK   1  TITL 2 PROTEIN INHIBITORS APPI AND BPTI                             
REMARK   1  REF    J.MOL.BIOL.                   V. 230   919 1993              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 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 + TEST SET) : 0.156                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
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                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1666                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 137                                     
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  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.012 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 3.200 ; 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 1BRA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000172022.                                   
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: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       62.20000            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       62.20000            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       62.20000            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       62.20000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       62.20000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       62.20000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       62.20000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       62.20000            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       62.20000            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       62.20000            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       62.20000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       62.20000            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       62.20000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       62.20000            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       62.20000            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       62.20000            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       62.20000            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       62.20000            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       62.20000            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       62.20000            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       62.20000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       62.20000            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       62.20000            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       62.20000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       62.20000            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       62.20000            
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 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 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      124.40000            
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    CYS A  42   CA  -  C   -  O   ANGL. DEV. = -12.6 DEGREES          
REMARK 500    ASN A  48   N   -  CA  -  CB  ANGL. DEV. =  12.9 DEGREES          
REMARK 500    LYS A  60   N   -  CA  -  CB  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    ARG A  62   NE  -  CZ  -  NH1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ARG A  62   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.8 DEGREES          
REMARK 500    ARG A  67   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ILE A  73   CA  -  CB  -  CG2 ANGL. DEV. =  12.8 DEGREES          
REMARK 500    GLU A  77   OE1 -  CD  -  OE2 ANGL. DEV. =  11.4 DEGREES          
REMARK 500    GLU A  77   CG  -  CD  -  OE2 ANGL. DEV. = -19.7 DEGREES          
REMARK 500    PHE A  82   CB  -  CG  -  CD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    PHE A  82   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ASP A  95   CB  -  CG  -  OD1 ANGL. DEV. =   6.3 DEGREES          
REMARK 500    ASP A  95   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A  96   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP A 102   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ASP A 102   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    SER A 146   CA  -  CB  -  OG  ANGL. DEV. = -19.6 DEGREES          
REMARK 500    GLU A 151   CA  -  CB  -  CG  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    GLU A 151   OE1 -  CD  -  OE2 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    LEU A 154   O   -  C   -  N   ANGL. DEV. =   9.8 DEGREES          
REMARK 500    CYS A 168   CB  -  CA  -  C   ANGL. DEV. =   8.6 DEGREES          
REMARK 500    ASP A 178   CA  -  CB  -  CG  ANGL. DEV. = -17.4 DEGREES          
REMARK 500    ASP A 178   CB  -  CG  -  OD1 ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    SER A 190   CB  -  CA  -  C   ANGL. DEV. =  19.7 DEGREES          
REMARK 500    ASP A 194   CB  -  CG  -  OD1 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    VAL A 199   CB  -  CA  -  C   ANGL. DEV. =  11.4 DEGREES          
REMARK 500    VAL A 199   N   -  CA  -  CB  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    VAL A 199   CG1 -  CB  -  CG2 ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    VAL A 227   CB  -  CA  -  C   ANGL. DEV. =  11.5 DEGREES          
REMARK 500    THR A 229   CA  -  CB  -  OG1 ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ASP A 240   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500    ASP A 240   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 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      -71.17   -128.89                                   
REMARK 500    ASN A 115     -155.66   -152.95                                   
REMARK 500    SER A 214      -63.05   -121.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 BENZAMIDINE IS AN ANALOG OF ARGININE WHICH POSSESSES A               
REMARK 600 POSITIVELY CHARGED AMIDINIUM GROUP RATHER THAN A                     
REMARK 600 GUANIDINIUM.  TWO BENZAMIDINES ARE MODELLED PER TRYPSIN.             
REMARK 600 BEN 246 BINDS IN THE PRIMARY SPECIFICITY POCKET; BEN 247             
REMARK 600 BINDS NONSPECIFICALLY ON THE SURFACE OF THE MOLECULE AT A            
REMARK 600 LATTICE CONTACT.  RAT TRYPSIN CRYSTALS IN THIS CUBIC SPACE           
REMARK 600 GROUP DO NOT GROW IN THE ABSENCE OF ADDED BENZAMIDINE IN             
REMARK 600 THE CRYSTALLIZATION DROP.                                            
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 302  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE1                                                    
REMARK 620 2 VAL A  75   O   165.2                                              
REMARK 620 3 GLU A  77   OE1  93.9  95.1                                        
REMARK 620 4 GLU A  80   OE2  98.6  94.2  82.9                                  
REMARK 620 5 HOH A 261   O    79.2  91.9 172.9  96.7                            
REMARK 620 6 ASN A  72   O    90.1  78.8  85.7 166.1  95.5                      
REMARK 620 N                    1     2     3     4     5                       
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 CLASSES   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 246                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 SEQUENCE ADVISORY NOTICE:                                            
REMARK 999 SEQUENCE FOR THIS STRUCTURE WAS TAKEN FROM GENEMBL WHICH             
REMARK 999 DIFFERS FROM SWISSPROT SEQUENCE AT POSITIONS 61 AND 65.              
DBREF  1BRA A   16   245  UNP    P00763   TRY2_RAT        24    246             
SEQADV 1BRA GLY A  189  UNP  P00763    ASP   194 CONFLICT                       
SEQADV 1BRA ASP A  226  UNP  P00763    GLY   227 CONFLICT                       
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN ASP 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 ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL          
SEQRES   6 A  223  ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG          
SEQRES   7 A  223  LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  223  SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA          
SEQRES   9 A  223  LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN          
SEQRES  11 A  223  GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU          
SEQRES  12 A  223  PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 A  223  THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  223  LYS GLY SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 A  223  GLY CYS ALA LEU PRO ASP ASN PRO ASP VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA          
SEQRES  18 A  223  ALA ASN                                                      
HET     CA  A 302       1                                                       
HET    BEN  A 246       9                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     BEN BENZAMIDINE                                                      
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  BEN    C7 H8 N2                                                     
FORMUL   4  HOH   *137(H2 O)                                                    
HELIX    1 SHA PRO A  164  TYR A  172  1IRREGULAR AFTER CYS 168            9    
HELIX    2 31A LYS A  230  VAL A  235  5LEADS INTO TERMINAL ALPHA-HLX      6    
HELIX    3 TEA TYR A  234  ASN A  245  1C-TERMINAL HELIX                  12    
SHEET    1 S1A 7 TYR A  20  TYR A  20  0                                        
SHEET    2 S1A 7 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3 S1A 7 CYS A 136  GLY A 140 -1  O  CYS A 136   N  ALA A 160           
SHEET    4 S1A 7 GLY A 197  CYS A 201 -1  N  VAL A 200   O  LEU A 137           
SHEET    5 S1A 7 GLU A 204  TRP A 215 -1  N  VAL A 213   O  GLY A 197           
SHEET    6 S1A 7 ASP A 226  VAL A 231 -1  N  VAL A 227   O  TRP A 215           
SHEET    7 S1A 7 ASN A 179  VAL A 183 -1  N  VAL A 183   O  ASP A 226           
SHEET    1 S2A 4 GLY A  43  SER A  45  0                                        
SHEET    2 S2A 4 VAL A  52  ALA A  55 -1  N  VAL A  53   O  SER A  45           
SHEET    3 S2A 4 ILE A 103  LYS A 107 -1  O  MET A 104   N  SER A  54           
SHEET    4 S2A 4 LYS A  87  HIS A  91 -1  N  HIS A  91   O  ILE A 103           
SHEET    1 S3A 2 ILE A  63  VAL A  66  0                                        
SHEET    2 S3A 2 GLN A  81  ALA A  85 -1  N  GLN A  81   O  VAL A  66           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.05  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.04  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.01  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.05  
LINK        CA    CA A 302                 OE1 GLU A  70     1555   1555  2.11  
LINK        CA    CA A 302                 O   VAL A  75     1555   1555  1.96  
LINK        CA    CA A 302                 OE1 GLU A  77     1555   1555  2.25  
LINK        CA    CA A 302                 OE2 GLU A  80     1555   1555  1.98  
LINK        CA    CA A 302                 O   HOH A 261     1555   1555  2.18  
LINK        CA    CA A 302                 O   ASN A  72     1555   1555  2.35  
SITE     1 CAT  3 HIS A  57  ASP A 102  SER A 195                               
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 261                                          
SITE     1 AC2 10 SER A 190  GLN A 192  SER A 195  VAL A 213                    
SITE     2 AC2 10 SER A 214  GLY A 216  GLY A 219  ASP A 226                    
SITE     3 AC2 10 HOH A 359  HOH A 391                                          
CRYST1  124.400  124.400  124.400  90.00  90.00  90.00 I 2 3        24          
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      0.008039  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008039  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008039        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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