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Database: PDB
Entry: 1QL9
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Original site: 1QL9 
HEADER    HYDROLASE                               24-AUG-99   1QL9              
TITLE     FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH RAT TRYPSIN              
TITLE    2 MUTANT X99RT                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TRYPSINOGEN, BETA-TRYPSIN;                                  
COMPND   5 EC: 3.4.21.4;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 OTHER_DETAILS: VARIANT X99RT\: RAT TRYPSIN CONTAINING THE            
COMPND   9  "99"-LOOP OF FACTOR XA                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 ORGAN: PANCREAS;                                                     
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR: YEAST;                                     
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PYT                                       
KEYWDS    SERINE PROTEASE, HYDROLASE, SERINE PROTEINASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.T.STUBBS                                                            
REVDAT   4   02-JUN-09 1QL9    1       HEADER SEQADV JRNL                       
REVDAT   3   24-FEB-09 1QL9    1       VERSN                                    
REVDAT   2   17-MAR-05 1QL9    1       JRNL                                     
REVDAT   1   25-AUG-00 1QL9    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.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 UROKINASE                                       
REMARK   1  REF    J.MED.CHEM.                   V.  41  5445 1998              
REMARK   1  REFN                   ISSN 0022-2623                               
REMARK   1  PMID   9876114                                                      
REMARK   1  DOI    10.1021/JM981068G                                            
REMARK   1 REFERENCE 2                                                          
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 3                                                          
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  PMID   7498454                                                      
REMARK   1  DOI    10.1016/0014-5793(95)01190-P                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.3  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.3                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.00                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.001                          
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 14100                          
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) : 0.189                           
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           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.34                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.9                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 714                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.263                        
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            : 1670                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 70                                      
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) : 10.0                            
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) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.69                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.7                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.21                            
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1QL9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-AUG-99.                  
REMARK 100 THE PDBE ID CODE IS EBI-2920.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 287.0                              
REMARK 200  PH                             : 7.00                               
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/MSC RU-H3R                  
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16310                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.10000                            
REMARK 200  R SYM                      (I) : 0.10000                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.45600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): NULL                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS:                                          
REMARK 280 25MM TRIS PH7, 10MM CACL2, 40% MGSO4                                 
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       62.07000            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       62.07000            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       62.07000            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       62.07000            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       62.07000            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       62.07000            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       62.07000            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       62.07000            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       62.07000            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       62.07000            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       62.07000            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       62.07000            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       62.07000            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       62.07000            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       62.07000            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       62.07000            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       62.07000            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       62.07000            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       62.07000            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       62.07000            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       62.07000            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       62.07000            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       62.07000            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       62.07000            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       62.07000            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       62.07000            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       62.07000            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       62.07000            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       62.07000            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       62.07000            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       62.07000            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       62.07000            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       62.07000            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       62.07000            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       62.07000            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       62.07000            
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 GENERATING THE BIOMOLECULE                                           
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE 223 AMINO ACIDS OF RAT TRYPSIN ARE IDENTIFIED BY THE             
REMARK 400 RESIDUE NUMBERS OF THE HOMOLOGOUS CHYMOTRYPSINOGEN.                  
REMARK 400                                                                      
REMARK 400 THE BINDING MODE OF THE INHIBITOR IS NOT AS EXPECTED: THE            
REMARK 400 CHLORINATED NAPHTHALENE MOIETY REACHES DEEP INTO THE                 
REMARK 400 PRIMARY SPECIFICITY POCKET, WHERE THE BURIED WATER MOLECULE          
REMARK 400 W416 IS DISPLACED BY THE CHLORINE ATOM                               
REMARK 400 (COMPARE WITH DAIICHI STRUCTURE 1MTW.PDB). CONCOMMITANT              
REMARK 400 WITH THIS, (I) THE HYDROXYL FUNCTION OF SER190 (ALA IN FXA)          
REMARK 400 ROTATES AWAY FROM THE INHIBITOR (II) A NEW WATER MOLECULE            
REMARK 400 (PROVOCATIVELY LABELLED W416) APPEARS, COORDINATED BY                
REMARK 400 ASP189OD2, GLY219O, ASN224O, AND W329 (W415) (III) THE               
REMARK 400 PEPTIDE BOND SER217-GLY219 FLIPS                                     
REMARK 400 (MAYBE TO ALLOW CLOSER APPROACH OF GLY219O TO W216) (IV)             
REMARK 400 THE SIDE CHAIN OF TYR217 FLIPS UP TO FORM ONE SIDE OF A              
REMARK 400 NOVEL "HYDROPHOBIC BOX", MIMICKING THE FACTOR XA STRUCTURE           
REMARK 400 (ALTHOUGH WITH A DIFFERENT APPROACH TO PHE174) THE                   
REMARK 400 PIPERIDINYLPYRIDINE MOITIES OCCUPY LOCATIONS STRONGLY                
REMARK 400 REMINISCENT OF THE DX9065A:TRYPSIN COMPLEXES                         
REMARK 400 (CF 1MTS.PDB, 1MTU.PDB, 1MTV.PDB); THE WEAKLY BASIC                  
REMARK 400 PYRIDINE WOULD OCCUPY THE "CATION HOLE" OF FACTOR XA                 
REMARK 400                                                                      
REMARK 400 THE SAME INHIBITOR HAS ALSO BEEN CRYSTALLIZED (A) WITH               
REMARK 400 BOVINE TRYPSIN AT PH 8 (SEE PDB FILE EBI-2917), WHICH SHOWS          
REMARK 400 SIMILAR STRUCTURAL REARRANGEMENTS, AND (B) WITH BOVINE               
REMARK 400 TRYPSIN AT PH7, WHERE IT BINDS IN THE REVERSE DIRECTION              
REMARK 400 (SEE PDB FILE EBI-2919)                                              
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 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      -66.06   -135.67                                   
REMARK 500    ASN A 115     -159.29   -152.95                                   
REMARK 500    SER A 214      -70.03   -117.05                                   
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 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  70   OE1                                                    
REMARK 620 2 ASN A  72   O    85.2                                              
REMARK 620 3 VAL A  75   O   170.4  86.5                                        
REMARK 620 4 GLU A  77   OE1  99.1  77.1  83.7                                  
REMARK 620 5 GLU A  80   OE2  97.7 158.0  91.9  80.9                            
REMARK 620 6 HOH A2016   O    81.9 105.9  95.8 176.9  96.1                      
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                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZEN A 999                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1QL7   RELATED DB: PDB                                   
REMARK 900  FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH BOVINE TRYPSIN         
REMARK 900 RELATED ID: 1QL8   RELATED DB: PDB                                   
REMARK 900  FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH BOVINE TRYPSIN         
REMARK 900 RELATED ID: 1MTW   RELATED DB: PDB                                   
REMARK 900  FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH BOVINE TRYPSIN         
REMARK 900 RELATED ID: 1MTS   RELATED DB: PDB                                   
REMARK 900  FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH BOVINE TRYPSIN         
REMARK 900 RELATED ID: 1MTU   RELATED DB: PDB                                   
REMARK 900  FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH BOVINE TRYPSIN         
REMARK 900 RELATED ID: 1MTV   RELATED DB: PDB                                   
REMARK 900  FACTOR XA SPECIFIC INHIBITOR IN COMPLEX WITH BOVINE TRYPSIN         
REMARK 900 SEE ALSO THE PDB ENTRIES:                                            
REMARK 900  1ANB 1ANC 1AND 1ANE 1AMH 1SLU 1SLV 1SLW 1SLX 1DPO 3TGI 3TGJ         
DBREF  1QL9 A   16   245  UNP    P00763   TRY2_RAT        24    246             
SEQADV 1QL9 GLU A   97  UNP  P00763    LYS   102 ENGINEERED MUTATION            
SEQADV 1QL9 TYR A   99  UNP  P00763    LEU   104 ENGINEERED MUTATION            
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    ZEN  A 999      34                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ZEN [4-(6-CHLORO-NAPHTHALENE-2-SULFONYL)-                            
HETNAM   2 ZEN  PIPERAZIN-1-YL]- (3,4,5,6-TETRAHYDRO-2H-[1,4']                  
HETNAM   3 ZEN  BIPYRIDINYL-4-YL)- METHANONE                                    
FORMUL   2   CA    CA 2+                                                        
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  ZEN    C25 H27 CL N4 O3 S                                           
FORMUL   5  HOH   *70(H2 O1)                                                    
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  ALA A  244  1                                  11    
SHEET    1   A 7 GLN A  81  ASN A  84  0                                        
SHEET    2   A 7 GLN A  64  LEU A  68 -1  N  LEU A  68   O  GLN A  81           
SHEET    3   A 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
SHEET    4   A 7 HIS A  40  ASN A  48 -1  N  GLY A  44   O  VAL A  31           
SHEET    5   A 7 TRP A  51  SER A  54 -1  N  VAL A  53   O  SER A  45           
SHEET    6   A 7 MET A 104  LEU A 108 -1  N  ILE A 106   O  VAL A  52           
SHEET    7   A 7 ALA A  85  LYS A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    1   B 2 GLN A 135  GLY A 140  0                                        
SHEET    2   B 2 GLN A 156  PRO A 161 -1  N  ALA A 160   O  CYS A 136           
SHEET    1   C 4 MET A 180  VAL A 183  0                                        
SHEET    2   C 4 GLY A 226  LYS A 230 -1  N  TYR A 228   O  VAL A 181           
SHEET    3   C 4 GLU A 204  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    4   C 4 PRO A 198  CYS A 201 -1  N  CYS A 201   O  GLU A 204           
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  2.03  
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                 OE1 GLU A  70     1555   1555  2.34  
LINK        CA    CA A 480                 O   ASN A  72     1555   1555  2.25  
LINK        CA    CA A 480                 O   VAL A  75     1555   1555  2.22  
LINK        CA    CA A 480                 OE1 GLU A  77     1555   1555  3.07  
LINK        CA    CA A 480                 OE2 GLU A  80     1555   1555  2.41  
LINK        CA    CA A 480                 O   HOH A2016     1555   1555  2.21  
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC1  6 GLU A  80  HOH A2016                                          
SITE     1 AC2  5 HIS A  57  GLN A 192  GLY A 193  SER A 195                    
SITE     2 AC2  5 ZEN A 999                                                     
SITE     1 AC3 20 THR A  98  TYR A  99  LEU A 145  GLY A 148                    
SITE     2 AC3 20 VAL A 149  LYS A 175  SER A 190  GLN A 192                    
SITE     3 AC3 20 SER A 195  VAL A 213  TRP A 215  GLY A 216                    
SITE     4 AC3 20 TYR A 217  GLY A 219  CYS A 220  GLY A 226                    
SITE     5 AC3 20 VAL A 227  TYR A 228  SO4 A 600  HOH A2070                    
CRYST1  124.140  124.140  124.140  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      0.008055  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008055  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008055        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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