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Database: PDB
Entry: 1J14
LinkDB: 1J14
Original site: 1J14 
HEADER    HYDROLASE                               30-NOV-02   1J14              
TITLE     BENZAMIDINE IN COMPLEX WITH RAT TRYPSIN MUTANT X99RT                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN II, ANIONIC;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TRYPSINOGEN, BETA-TRYPSIN, PRETRYPSINOGEN II;               
COMPND   5 EC: 3.4.21.4;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 TISSUE: PANCREAS;                                                    
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PYT                                       
KEYWDS    SERINE PROTEASE, HYDROLASE, SERINE PROTEINASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.T.STUBBS                                                            
REVDAT   3   24-FEB-09 1J14    1       VERSN                                    
REVDAT   2   11-FEB-03 1J14    1       JRNL                                     
REVDAT   1   23-DEC-02 1J14    0                                                
JRNL        AUTH   S.REYDA,C.SOHN,G.KLEBE,K.RALL,D.ULLMANN,                     
JRNL        AUTH 2 H.D.JAKUBKE,M.T.STUBBS                                       
JRNL        TITL   RECONSTRUCTING THE BINDING SITE OF FACTOR XA IN              
JRNL        TITL 2 TRYPSIN REVEALS LIGAND-INDUCED STRUCTURAL                    
JRNL        TITL 3 PLASTICITY                                                   
JRNL        REF    J.MOL.BIOL.                   V. 325   963 2003              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12527302                                                     
JRNL        DOI    10.1016/S0022-2836(02)01337-2                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.T.STUBBS,S.REYDA,F.DULLWEBER,M.MOELLER,G.KLEBE,            
REMARK   1  AUTH 2 D.DORSCH,W.W.K.R.MEDERSKI,H.WURZIGER                         
REMARK   1  TITL   PH-DEPENDENT BINDING MODES OBSERVED IN TRYPSIN               
REMARK   1  TITL 2 CRYSTALS: LESSONS FOR STRUCTURE-BASED DRUG DESIGN            
REMARK   1  REF    CHEMBIOCHEM                   V.   3   246 2002              
REMARK   1  REFN                   ISSN 1439-4227                               
REMARK   1  DOI    10.1002/1439-7633(20020301)3:2/3<246::AID-CBIC246>3          
REMARK   1  DOI  2 .0.CO;2-#                                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   M.RENATUS,W.BODE,R.HUBER,J.STUERZEBECHER,M.T.STUBBS          
REMARK   1  TITL   STRUCTURAL AND FUNCTIONAL ANALYSES OF                        
REMARK   1  TITL 2 BENZAMIDINE-BASED INHIBITORS IN COMPLEX WITH                 
REMARK   1  TITL 3 TRYPSIN: IMPLICATIONS FOR THE INHIBITION OF FACTOR           
REMARK   1  TITL 4 XA, TPA, AND UROKINAS                                        
REMARK   1  REF    J.MED.CHEM.                   V.  41  5445 1998              
REMARK   1  REFN                   ISSN 0022-2623                               
REMARK   1  DOI    10.1021/JM981068G                                            
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.T.STUBBS                                                   
REMARK   1  TITL   STRUCTURAL ASPECTS OF FACTOR XA INHIBITION                   
REMARK   1  REF    CURR.PHARM.DES.               V.   2   543 1996              
REMARK   1  REFN                   ISSN 1381-6128                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   M.T.STUBBS,R.HUBER,W.BODE                                    
REMARK   1  TITL   CRYSTAL STRUCTURES OF FACTOR XA SPECIFIC                     
REMARK   1  TITL 2 INHIBITORS IN COMPLEX WITH TRYPSIN: STRUCTURAL               
REMARK   1  TITL 3 GROUNDS FOR INHIBITION OF FACTOR XA AND                      
REMARK   1  TITL 4 SELECTIVITY AGAINST THROMBIN                                 
REMARK   1  REF    FEBS LETT.                    V. 375   103 1995              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1  DOI    10.1016/0014-5793(95)01190-P                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 12480                          
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) : 0.193                           
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            : 1744                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 64                                      
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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
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 1J14 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 06-DEC-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB005498.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 287                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12713                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.840                             
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: SINGLE WAVELENGTH                              
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   (%): 62.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0                                   
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       62.26000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       62.26000            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       62.26000            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       62.26000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       62.26000            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       62.26000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       62.26000            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       62.26000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       62.26000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       62.26000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       62.26000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       62.26000            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       62.26000            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       62.26000            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       62.26000            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       62.26000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       62.26000            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       62.26000            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       62.26000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       62.26000            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       62.26000            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       62.26000            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       62.26000            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       62.26000            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       62.26000            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       62.26000            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       62.26000            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       62.26000            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       62.26000            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       62.26000            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       62.26000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       62.26000            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       62.26000            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       62.26000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       62.26000            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       62.26000            
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 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: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  49      -10.61    -49.73                                   
REMARK 500    HIS A  71      -71.06   -137.22                                   
REMARK 500    ASN A 115     -168.65   -162.98                                   
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 480  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  80   OE2                                                    
REMARK 620 2 HOH A 261   O    88.6                                              
REMARK 620 3 GLU A  70   OE1  98.3  75.4                                        
REMARK 620 4 ASN A  72   O   168.1 103.3  85.3                                  
REMARK 620 5 VAL A  75   O    89.3  89.3 162.7  90.5                            
REMARK 620 6 GLU A  77   OE1  84.3 172.9 106.0  83.8  90.1                      
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 480                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 600                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BEN A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QL7   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1QL8   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1QL9   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1J15   RELATED DB: PDB                                   
REMARK 900 BENZAMIDINE IN COMPLEX WITH RAT TRYPSIN MUTANT X99/175/              
REMARK 900 190RT AT ROOM TEMPERATURE                                            
REMARK 900 RELATED ID: 1J16   RELATED DB: PDB                                   
REMARK 900 BENZAMIDINE IN COMPLEX WITH RAT TRYPSIN MUTANT X99/175/              
REMARK 900 190RT AT 100K                                                        
REMARK 900 RELATED ID: 1J17   RELATED DB: PDB                                   
REMARK 900 FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH RAT TRYPSIN             
REMARK 900 MUTANT X99/175/190RT                                                 
DBREF  1J14 A   16   245  UNP    P00763   TRY2_RAT        24    246             
SEQADV 1J14 GLU A   97  UNP  P00763    LYS   102 ENGINEERED                     
SEQADV 1J14 TYR A   99  UNP  P00763    LEU   104 ENGINEERED                     
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  GLU THR TYR 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 ASP 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 GLY 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 480       1                                                       
HET    SO4  A 600       5                                                       
HET    BEN  A   1       9                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     BEN BENZAMIDINE                                                      
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  BEN    C7 H8 N2                                                     
FORMUL   5  HOH   *64(H2 O)                                                     
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 PRO A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  ASN A  245  1                                  12    
SHEET    1   A 7 TYR A  20  THR A  21  0                                        
SHEET    2   A 7 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3   A 7 GLN A 135  GLY A 140 -1  N  CYS A 136   O  ALA A 160           
SHEET    4   A 7 PRO A 198  CYS A 201 -1  O  VAL A 200   N  LEU A 137           
SHEET    5   A 7 GLU A 204  TRP A 215 -1  O  GLN A 210   N  VAL A 199           
SHEET    6   A 7 GLY A 226  LYS A 230 -1  O  VAL A 227   N  TRP A 215           
SHEET    7   A 7 MET A 180  VAL A 183 -1  N  VAL A 181   O  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  O  CYS A  42   N  LEU A  33           
SHEET    3   B 7 TRP A  51  SER A  54 -1  O  VAL A  53   N  SER A  45           
SHEET    4   B 7 MET A 104  LEU A 108 -1  O  ILE A 106   N  VAL A  52           
SHEET    5   B 7 GLN A  81  LYS A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    6   B 7 GLN A  64  LEU A  68 -1  N  VAL A  66   O  VAL A  83           
SHEET    7   B 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.04  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.04  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.03  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.03  
LINK        CA    CA A 480                 OE2 GLU A  80     1555   1555  2.48  
LINK        CA    CA A 480                 O   HOH A 261     1555   1555  2.17  
LINK        CA    CA A 480                 OE1 GLU A  70     1555   1555  2.51  
LINK        CA    CA A 480                 O   ASN A  72     1555   1555  2.34  
LINK        CA    CA A 480                 O   VAL A  75     1555   1555  2.25  
LINK        CA    CA A 480                 OE1 GLU A  77     1555   1555  2.68  
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  6 BEN A   1  HIS A  57  GLN A 192  GLY A 193                    
SITE     2 AC2  6 SER A 195  HOH A 726                                          
SITE     1 AC3  9 ASP A 189  SER A 190  GLN A 192  SER A 195                    
SITE     2 AC3  9 VAL A 213  GLY A 216  GLY A 219  GLY A 226                    
SITE     3 AC3  9 SO4 A 600                                                     
CRYST1  124.520  124.520  124.520  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      0.008031  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008031  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008031        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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