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Database: PDB
Entry: 1ETR
LinkDB: 1ETR
Original site: 1ETR 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           06-JUL-92   1ETR              
TITLE     REFINED 2.3 ANGSTROMS X-RAY CRYSTAL STRUCTURE OF BOVINE THROMBIN      
TITLE    2 COMPLEXES FORMED WITH THE BENZAMIDINE AND ARGININE-BASED THROMBIN    
TITLE    3 INHIBITORS NAPAP, 4-TAPAP AND MQPA: A STARTING POINT FOR IMPROVING   
TITLE    4 ANTITHROMBOTICS                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPSILON-THROMBIN;                                          
COMPND   3 CHAIN: L;                                                            
COMPND   4 EC: 3.4.21.5;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: EPSILON-THROMBIN;                                          
COMPND   8 CHAIN: H;                                                            
COMPND   9 EC: 3.4.21.5;                                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: COW;                                                
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   7 ORGANISM_COMMON: COW;                                                
SOURCE   8 ORGANISM_TAXID: 9913                                                 
KEYWDS    SERINE PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.BODE,H.BRANDSTETTER                                                 
REVDAT   5   13-JUL-11 1ETR    1       VERSN                                    
REVDAT   4   25-AUG-09 1ETR    1       SOURCE                                   
REVDAT   3   24-FEB-09 1ETR    1       VERSN                                    
REVDAT   2   01-APR-03 1ETR    1       JRNL                                     
REVDAT   1   31-JAN-94 1ETR    0                                                
JRNL        AUTH   H.BRANDSTETTER,D.TURK,H.W.HOEFFKEN,D.GROSSE,J.STURZEBECHER,  
JRNL        AUTH 2 P.D.MARTIN,B.F.EDWARDS,W.BODE                                
JRNL        TITL   REFINED 2.3 A X-RAY CRYSTAL STRUCTURE OF BOVINE THROMBIN     
JRNL        TITL 2 COMPLEXES FORMED WITH THE BENZAMIDINE AND ARGININE-BASED     
JRNL        TITL 3 THROMBIN INHIBITORS NAPAP, 4-TAPAP AND MQPA. A STARTING      
JRNL        TITL 4 POINT FOR IMPROVING ANTITHROMBOTICS.                         
JRNL        REF    J.MOL.BIOL.                   V. 226  1085 1992              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   1518046                                                      
JRNL        DOI    10.1016/0022-2836(92)91054-S                                 
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.BODE,H.BRANDSTETTER,D.TURK,M.BAUER,J.STUERZEBECHER         
REMARK   1  TITL   CRYSTALLOGRAPHIC DETERMINATION OF THROMBIN COMPLEXES WITH    
REMARK   1  TITL 2 SMALL SYNTHETIC INHIBITORS AS A STARTING POINT FOR THE       
REMARK   1  TITL 3 RECEPTOR-BASED DESIGN OF ANTITHROMBOTICS                     
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   W.BODE                                                       
REMARK   1  TITL   X-RAY CRYSTAL STRUCTURE OF THROMBIN IN COMPLEX WITH          
REMARK   1  TITL 2 D-PHE-PRO-ARG AND WITH SMALL BENZAMIDINE AND ARGININE-BASED  
REMARK   1  TITL 3 "NON-PEPTIDIC" INHIBITORS                                    
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   W.BODE,D.TURK,A.KARSHIKOV                                    
REMARK   1  TITL   THE REFINED 1.9-ANGSTROMS X-RAY CRYSTAL STRUCTURE OF         
REMARK   1  TITL 2 D-PHE-PRO-ARG CHLOROMETHYLKETONE-INHIBITED HUMAN             
REMARK   1  TITL 3 ALPHA-THROMBIN: STRUCTURE ANALYSIS, OVERALL STRUCTURE,       
REMARK   1  TITL 4 ELECTROSTATIC PROPERTIES, DETAILED ACTIVE-SITE GEOMETRY, AND 
REMARK   1  TITL 5 STRUCTURE-FUNCTION RELATIONSHIPS                             
REMARK   1  REF    PROTEIN SCI.                  V.   1   426 1992              
REMARK   1  REFN                   ISSN 0961-8368                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   D.TURK,J.STUERZEBECHER,W.BODE                                
REMARK   1  TITL   GEOMETRY OF BINDING OF THE NALPHA-TOSYLATED PIPERIDIDES OF   
REMARK   1  TITL 2 M-AMIDINO-, P-AMIDINO-AND P-GUANIDINO PHENYLALANINE TO       
REMARK   1  TITL 3 THROMBIN AND TRYPSIN: X-RAY CRYSTAL STRUCTURES OF THEIR      
REMARK   1  TITL 4 TRYPSIN COMPLEXES AND MODELING OF THEIR THROMBIN COMPLEXES   
REMARK   1  REF    FEBS LETT.                    V. 287   133 1991              
REMARK   1  REFN                   ISSN 0014-5793                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   W.BODE,D.TURK,J.STUERZEBECHER                                
REMARK   1  TITL   GEOMETRY OF BINDING OF THE BENZAMIDINE-AND ARGININE-BASED    
REMARK   1  TITL 2 INHIBITORS N-ALPHA-(2-NAPHTHYL-SULPHONYL-GLYCYL)-DL-P-       
REMARK   1  TITL 3 AMIDINOPHENYLALANYL-PIPERIDINE (NAPAP) AND                   
REMARK   1  TITL 4 (2R,4R)-4-METHYL-1-[N-ALPHA-(3-METHYL-1,2,3,4-TETRAHYDRO-8-  
REMARK   1  TITL 5 QUINOLINESULPHONYL)-L-ARGINYL]-2-PIPERIDINE CARBOXYLIC ACID  
REMARK   1  TITL 6 (MQPA) TO HUMAN ALPHA-THROMBIN: X-RAY CRYSTALLOGRAPHIC       
REMARK   1  TITL 7 DETERMINATION OF THE NAPAP-TRYPSIN COMPLEX AND MODELING OF   
REMARK   1  TITL 8 NAPAP-THROMBIN AND MQPA-THROMBIN                             
REMARK   1  REF    EUR.J.BIOCHEM.                V. 193   175 1990              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   W.BODE,I.MAYR,U.BAUMANN,R.HUBER,S.R.STONE,J.HOFSTEENGE       
REMARK   1  TITL   THE REFINED 1.9 ANGSTROMS CRYSTAL STRUCTURE OF HUMAN         
REMARK   1  TITL 2 ALPHA-THROMBIN: INTERACTION WITH D-PHE-PRO-ARG               
REMARK   1  TITL 3 CHLOROMETHYLKETONE AND SIGNIFICANCE OF THE TYR-PRO-PRO-TRP   
REMARK   1  TITL 4 INSERTION SEGMENT                                            
REMARK   1  REF    EMBO J.                       V.   8  3467 1989              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
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            : 2384                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 152                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.26                            
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:                                           
REMARK   3  THERE IS A CLEAVAGE IN THE CHAIN AT THR 149A - SER 149B IN          
REMARK   3  THE INSERTION LOOP OF THROMBIN.  THE AUTHORS DO NOT SEE             
REMARK   3  THIS CLEAVAGE DUE TO DISORDER AT BOTH FLANKING REGIONS.             
REMARK   3  NOTE THAT THE OCCUPANCY OF RESIDUES 148 - 149E IS GIVEN AS          
REMARK   3  0.0 INDICATING THAT THEY WERE NOT SEEN IN THE ELECTRON              
REMARK   3  DENSITY MAPS.                                                       
REMARK   4                                                                      
REMARK   4 1ETR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
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   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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  0.000000 -1.000000  0.000000       43.85500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       43.85500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       51.49000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       43.85500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       43.85500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       51.49000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       43.85500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       43.85500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       51.49000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       43.85500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       43.85500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       51.49000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H                                  
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR L   -12                                                      
REMARK 465     SER L   -11                                                      
REMARK 465     GLU L   -10                                                      
REMARK 465     ASP L    -9                                                      
REMARK 465     HIS L    -8                                                      
REMARK 465     PHE L    -7                                                      
REMARK 465     GLN L    -6                                                      
REMARK 465     PRO L    -5                                                      
REMARK 465     PHE L    -4                                                      
REMARK 465     PHE L    -3                                                      
REMARK 465     ASN L    -2                                                      
REMARK 465     GLU L    -1                                                      
REMARK 465     LYS L     0                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     THR L    1H                                                      
REMARK 475     PHE L    1G                                                      
REMARK 475     GLY L    1F                                                      
REMARK 475     ALA L    1E                                                      
REMARK 475     GLY L    1D                                                      
REMARK 475     GLU L    1C                                                      
REMARK 475     ALA L    1B                                                      
REMARK 475     ASP L    1A                                                      
REMARK 475     GLU L   14L                                                      
REMARK 475     GLY L   14M                                                      
REMARK 475     ARG L   15                                                       
REMARK 475     TRP H  148                                                       
REMARK 475     THR H  149                                                       
REMARK 475     THR H  149A                                                      
REMARK 475     SER H  149B                                                      
REMARK 475     VAL H  149C                                                      
REMARK 475     ALA H  149D                                                      
REMARK 475     GLU H  149E                                                      
REMARK 475     LYS H  236                                                       
REMARK 475     TRP H  237                                                       
REMARK 475     ILE H  238                                                       
REMARK 475     GLN H  239                                                       
REMARK 475     LYS H  240                                                       
REMARK 475     VAL H  241                                                       
REMARK 475     ILE H  242                                                       
REMARK 475     ASP H  243                                                       
REMARK 475     ARG H  244                                                       
REMARK 475     LEU H  245                                                       
REMARK 475     GLY H  246                                                       
REMARK 475     SER H  247                                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS H 131   NE2   HIS H 131   CD2    -0.068                       
REMARK 500    HIS H 230   NE2   HIS H 230   CD2    -0.075                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TRP H  29   CD1 -  CG  -  CD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TRP H  29   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ARG H  35   CB  -  CG  -  CD  ANGL. DEV. = -15.9 DEGREES          
REMARK 500    TRP H  51   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    TRP H  51   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TRP H  60D  CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    TYR H  94   CB  -  CG  -  CD2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    TYR H  94   CB  -  CG  -  CD1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    TRP H  96   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG H 101   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    HIS H 131   CB  -  CG  -  CD2 ANGL. DEV. = -10.0 DEGREES          
REMARK 500    TRP H 141   CD1 -  CG  -  CD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    TRP H 141   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG H 145   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    TRP H 148   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    TRP H 148   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    VAL H 157   CB  -  CA  -  C   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    VAL H 157   CG1 -  CB  -  CG2 ANGL. DEV. =  11.4 DEGREES          
REMARK 500    VAL H 157   CA  -  CB  -  CG1 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    ARG H 165   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    TRP H 207   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    TRP H 207   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    TRP H 215   CD1 -  CG  -  CD2 ANGL. DEV. =   5.3 DEGREES          
REMARK 500    TRP H 215   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.3 DEGREES          
REMARK 500    ARG H 221   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 DEGREES          
REMARK 500    TYR H 225   CB  -  CG  -  CD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TYR H 228   CB  -  CG  -  CD1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    TRP H 237   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP H 237   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    LEU H 245   CA  -  CB  -  CG  ANGL. DEV. =  14.4 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    ALA L   1E     -46.49     69.79                                   
REMARK 500    ALA L   1B     -74.14     42.67                                   
REMARK 500    PHE L   7      -81.39   -122.35                                   
REMARK 500    GLN L  11       56.72     17.20                                   
REMARK 500    PRO H  28        0.78    -68.45                                   
REMARK 500    SER H  48      174.89    171.79                                   
REMARK 500    ASP H  60E      -2.95     53.64                                   
REMARK 500    ASN H  60G      73.71   -157.33                                   
REMARK 500    HIS H  71      -45.99   -131.75                                   
REMARK 500    TYR H  76      108.65    -52.82                                   
REMARK 500    TYR H  94      120.77    -36.32                                   
REMARK 500    LYS H  97       47.99   -101.80                                   
REMARK 500    GLU H  97A     -86.87    175.24                                   
REMARK 500    TRP H 148     -111.37   -103.04                                   
REMARK 500    THR H 149A    -140.68   -115.28                                   
REMARK 500    ASP H 189      154.46    178.41                                   
REMARK 500    CYS H 191     -159.46   -148.38                                   
REMARK 500    ASN H 205       18.00     59.12                                   
REMARK 500    SER H 214      -83.52   -104.68                                   
REMARK 500    LYS H 240      -71.20    -47.10                                   
REMARK 500    ARG H 244      -54.80     82.19                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP H   63     LEU H   64                 -146.39                    
REMARK 500 THR H  147     TRP H  148                  144.76                    
REMARK 500 GLU H  149E    VAL H  150                 -140.30                    
REMARK 500 LEU H  245     GLY H  246                 -124.54                    
REMARK 500 GLY H  246     SER H  247                  140.05                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR H 204A        0.07    SIDE CHAIN                              
REMARK 500    TYR H 225         0.12    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 THE ARGINYL SIDE-CHAIN OF INHIBITOR MQPA BINDS TO S1                 
REMARK 600 SPECIFICITY POCKET, PIPERIDINE TO S2 AND QUINOLINE TO                
REMARK 600 "ARYL BINDING SITE".                                                 
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: NULL                                                  
REMARK 630 MOLECULE NAME: AMINO{[(4S)-5-[(2R,4R)-2-CARBOXY-4-METHYLPIPERIDIN-   
REMARK 630 1-YL]-4-({[(3R)-3-METHYL-1,2,3,4-TETRAHYDROQUINOLIN-8-YL]SULFONYL}   
REMARK 630 AMINO)-5-OXOPENTYL]AMINO}METHANIMINIUM                               
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     MIT H     1                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    34T ARG MCP                                              
REMARK 630 DETAILS: NULL                                                        
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEETS PRESENTED AS *S1* AND *S2* ON SHEET RECORDS               
REMARK 700 BELOW ARE ACTUALLY SIX-STRANDED BETA-BARRELS.  THESE ARE             
REMARK 700 REPRESENTED BY SEVEN-STRANDED SHEETS IN WHICH THE FIRST AND          
REMARK 700 LAST STRANDS ARE IDENTICAL.                                          
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MIT H 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ETS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1ETT   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE NUMBERING OF THROMBIN RESIDUES IS BASED ON TOPOLOGICAL           
REMARK 999 EQUIVALENCES WITH CHYMOTRYPSINOGEN.                                  
DBREF  1ETR L  -12    15  UNP    P00735   THRB_BOVIN     318    366             
DBREF  1ETR H   16   247  UNP    P00735   THRB_BOVIN     367    625             
SEQRES   1 L   49  THR SER GLU ASP HIS PHE GLN PRO PHE PHE ASN GLU LYS          
SEQRES   2 L   49  THR PHE GLY ALA GLY GLU ALA ASP CYS GLY LEU ARG PRO          
SEQRES   3 L   49  LEU PHE GLU LYS LYS GLN VAL GLN ASP GLN THR GLU LYS          
SEQRES   4 L   49  GLU LEU PHE GLU SER TYR ILE GLU GLY ARG                      
SEQRES   1 H  259  ILE VAL GLU GLY GLN ASP ALA GLU VAL GLY LEU SER PRO          
SEQRES   2 H  259  TRP GLN VAL MET LEU PHE ARG LYS SER PRO GLN GLU LEU          
SEQRES   3 H  259  LEU CYS GLY ALA SER LEU ILE SER ASP ARG TRP VAL LEU          
SEQRES   4 H  259  THR ALA ALA HIS CYS LEU LEU TYR PRO PRO TRP ASP LYS          
SEQRES   5 H  259  ASN PHE THR VAL ASP ASP LEU LEU VAL ARG ILE GLY LYS          
SEQRES   6 H  259  HIS SER ARG THR ARG TYR GLU ARG LYS VAL GLU LYS ILE          
SEQRES   7 H  259  SER MET LEU ASP LYS ILE TYR ILE HIS PRO ARG TYR ASN          
SEQRES   8 H  259  TRP LYS GLU ASN LEU ASP ARG ASP ILE ALA LEU LEU LYS          
SEQRES   9 H  259  LEU LYS ARG PRO ILE GLU LEU SER ASP TYR ILE HIS PRO          
SEQRES  10 H  259  VAL CYS LEU PRO ASP LYS GLN THR ALA ALA LYS LEU LEU          
SEQRES  11 H  259  HIS ALA GLY PHE LYS GLY ARG VAL THR GLY TRP GLY ASN          
SEQRES  12 H  259  ARG ARG GLU THR TRP THR THR SER VAL ALA GLU VAL GLN          
SEQRES  13 H  259  PRO SER VAL LEU GLN VAL VAL ASN LEU PRO LEU VAL GLU          
SEQRES  14 H  259  ARG PRO VAL CYS LYS ALA SER THR ARG ILE ARG ILE THR          
SEQRES  15 H  259  ASP ASN MET PHE CYS ALA GLY TYR LYS PRO GLY GLU GLY          
SEQRES  16 H  259  LYS ARG GLY ASP ALA CYS GLU GLY ASP SER GLY GLY PRO          
SEQRES  17 H  259  PHE VAL MET LYS SER PRO TYR ASN ASN ARG TRP TYR GLN          
SEQRES  18 H  259  MET GLY ILE VAL SER TRP GLY GLU GLY CYS ASP ARG ASP          
SEQRES  19 H  259  GLY LYS TYR GLY PHE TYR THR HIS VAL PHE ARG LEU LYS          
SEQRES  20 H  259  LYS TRP ILE GLN LYS VAL ILE ASP ARG LEU GLY SER              
HET    MIT  H   1      42                                                       
HETNAM     MIT AMINO{[(4S)-5-[(2R,4R)-2-CARBOXY-4-METHYLPIPERIDIN-1-            
HETNAM   2 MIT  YL]-4-({[(3R)-3-METHYL-1,2,3,4-TETRAHYDROQUINOLIN-8-            
HETNAM   3 MIT  YL]SULFONYL}AMINO)-5-OXOPENTYL]AMINO}METHANIMINIUM              
HETSYN     MIT MQPA, MD-805; MITSUBISHI INHIBITOR                               
FORMUL   3  MIT    C23 H37 N6 O5 S 1+                                           
FORMUL   4  HOH   *152(H2 O)                                                    
HELIX    1   1 GLU L   14C SER L   14I 13.6/13                             7    
HELIX    2   2 ALA H   55  LEU H   59  5                                   5    
HELIX    3   3 TYR H   60A ASP H   60E 5                                   5    
HELIX    4   4 ASP H  125  LEU H  129C 13.6/13                             8    
HELIX    5   5 GLU H  164  LYS H  169  13.6/13                             6    
HELIX    6   6 CYS H  168  THR H  172  5                                   5    
HELIX    7   7 VAL H  231  LYS H  235  5                                   5    
HELIX    8   8 LEU H  234  ASP H  243  13.6/13                            10    
SHEET    1  S1 7 LYS H  81  ASN H  95  0                                        
SHEET    2  S1 7 ASP H 100  LYS H 109 -1                                        
SHEET    3  S1 7 VAL H  52  THR H  54 -1                                        
SHEET    4  S1 7 GLU H  39  LEU H  46 -1                                        
SHEET    5  S1 7 TRP H  29  ARG H  35 -1                                        
SHEET    6  S1 7 VAL H  66  ILE H  68 -1                                        
SHEET    7  S1 7 LYS H  81  ASN H  95 -1                                        
SHEET    1  S2 7 VAL H 150  LEU H 162  0                                        
SHEET    2  S2 7 PHE H 134  ARG H 144 -1                                        
SHEET    3  S2 7 PHE H 199  SER H 203 -1                                        
SHEET    4  S2 7 ARG H 206  TRP H 215 -1                                        
SHEET    5  S2 7 GLY H 226  THR H 229 -1                                        
SHEET    6  S2 7 PHE H 181  ALA H 183 -1                                        
SHEET    7  S2 7 VAL H 150  LEU H 162 -1                                        
SSBOND   1 CYS L    1    CYS H  122                          1555   1555  2.02  
SSBOND   2 CYS H   42    CYS H   58                          1555   1555  2.01  
SSBOND   3 CYS H  168    CYS H  182                          1555   1555  2.05  
SSBOND   4 CYS H  191    CYS H  220                          1555   1555  2.00  
CISPEP   1 SER H   36A   PRO H   37          0        -3.57                     
SITE     1 AC1 13 HIS H  57  TYR H  60A LEU H  99  ASP H 189                    
SITE     2 AC1 13 ALA H 190  CYS H 191  SER H 195  TRP H 215                    
SITE     3 AC1 13 GLY H 216  GLY H 219  HOH H 561  HOH H 616                    
SITE     4 AC1 13 HOH H 632                                                     
CRYST1   87.710   87.710  102.980  90.00  90.00  90.00 P 42 21 2     8          
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      0.011401  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011401  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009711        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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