GenomeNet

Database: PDB
Entry: 1A5H
LinkDB: 1A5H
Original site: 1A5H 
HEADER    HYDROLASE                               17-FEB-98   1A5H              
TITLE     CATALYTIC DOMAIN OF HUMAN TWO-CHAIN TISSUE PLASMINOGEN ACTIVATOR      
TITLE    2 COMPLEX OF A BIS-BENZAMIDINE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TISSUE PLASMINOGEN ACTIVATOR;                              
COMPND   3 CHAIN: C, D;                                                         
COMPND   4 FRAGMENT: HEAVY CHAIN FRAGMENT, CATALYTIC DOMAIN;                    
COMPND   5 EC: 3.4.21.68;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TISSUE PLASMINOGEN ACTIVATOR;                              
COMPND   9 CHAIN: A, B;                                                         
COMPND  10 FRAGMENT: LIGHT CHAIN, CATALYTIC DOMAIN;                             
COMPND  11 SYNONYM: TC-TPA(BISB);                                               
COMPND  12 EC: 3.4.21.68;                                                       
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   9 ORGANISM_COMMON: HUMAN;                                              
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TRYPSIN LIKE SERINE PROTEASE, FIBRINOLYTIC ENZYME, HYDROLASE          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.RENATUS,W.BODE,M.T.STUBBS                                           
REVDAT   4   05-SEP-18 1A5H    1       REMARK                                   
REVDAT   3   24-FEB-09 1A5H    1       VERSN                                    
REVDAT   2   10-MAY-00 1A5H    1       COMPND SOURCE HEADER                     
REVDAT   1   20-APR-99 1A5H    0                                                
JRNL        AUTH   M.RENATUS,W.BODE,R.HUBER,J.STURZEBECHER,D.PRASA,S.FISCHER,   
JRNL        AUTH 2 U.KOHNERT,M.T.STUBBS                                         
JRNL        TITL   STRUCTURAL MAPPING OF THE ACTIVE SITE SPECIFICITY            
JRNL        TITL 2 DETERMINANTS OF HUMAN TISSUE-TYPE PLASMINOGEN ACTIVATOR.     
JRNL        TITL 3 IMPLICATIONS FOR THE DESIGN OF LOW MOLECULAR WEIGHT          
JRNL        TITL 4 SUBSTRATES AND INHIBITORS.                                   
JRNL        REF    J.BIOL.CHEM.                  V. 272 21713 1997              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   9268299                                                      
JRNL        DOI    10.1074/JBC.272.35.21713                                     
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.BODE,M.RENATUS                                             
REMARK   1  TITL   TISSUE-TYPE PLASMINOGEN ACTIVATOR: VARIANTS AND              
REMARK   1  TITL 2 CRYSTAL/SOLUTION STRUCTURES DEMARCATE STRUCTURAL             
REMARK   1  TITL 3 DETERMINANTS OF FUNCTION                                     
REMARK   1  REF    CURR.OPIN.STRUCT.BIOL.        V.   7   865 1997              
REMARK   1  REFN                   ISSN 0959-440X                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   D.LAMBA,M.BAUER,R.HUBER,S.FISCHER,R.RUDOLPH,U.KOHNERT,W.BODE 
REMARK   1  TITL   THE 2.3 A CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF       
REMARK   1  TITL 2 RECOMBINANT TWO-CHAIN HUMAN TISSUE-TYPE PLASMINOGEN          
REMARK   1  TITL 3 ACTIVATOR                                                    
REMARK   1  REF    J.MOL.BIOL.                   V. 258   117 1996              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 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) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 7.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.2500                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 81.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 9017                           
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) : 0.178                           
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           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.00                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 60.38                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 657                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2367                       
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            : 4066                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 91                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.20                          
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) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.428                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.15                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.320                           
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  : PARAM19.SOL                                    
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1A5H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000170416.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-SEP-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 280                                
REMARK 200  PH                             : 4.5                                
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 RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS                            
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, XSCALE                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12586                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.08800                            
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) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25000                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: 1RTF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 4.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-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  1.000000  0.000000  0.000000       75.91500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       30.25000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       75.91500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       30.25000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, B                                  
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 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     TYR C     6                                                      
REMARK 475     HIS A    37                                                      
REMARK 475     ARG A    37A                                                     
REMARK 475     ARG A    37B                                                     
REMARK 475     SER A    37C                                                     
REMARK 475     PRO A    37D                                                     
REMARK 475     GLY A    37E                                                     
REMARK 475     ASP A   110A                                                     
REMARK 475     SER A   110B                                                     
REMARK 475     SER A   110C                                                     
REMARK 475     ARG A   243                                                      
REMARK 475     PRO A   244                                                      
REMARK 475     TYR D     6                                                      
REMARK 475     HIS B    37                                                      
REMARK 475     ARG B    37A                                                     
REMARK 475     ARG B    37B                                                     
REMARK 475     SER B    37C                                                     
REMARK 475     PRO B    37D                                                     
REMARK 475     GLY B    37E                                                     
REMARK 475     ASP B   110A                                                     
REMARK 475     SER B   110B                                                     
REMARK 475     SER B   110C                                                     
REMARK 475     ARG B   110D                                                     
REMARK 475     ARG B   243                                                      
REMARK 475     PRO B   244                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A   38   CG   CD   OE1  OE2                                  
REMARK 480     GLN A   60   CB   CG   CD   OE1  NE2                             
REMARK 480     GLU A   60A  CB   CG   CD   OE1  OE2                             
REMARK 480     ARG A   60B  CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     GLU A   78   CB   CG   CD   OE1  OE2                             
REMARK 480     SER A  110   C    O                                              
REMARK 480     ARG A  110D  CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     GLN A  113   CB   CG   CD   OE1  NE2                             
REMARK 480     GLN A  129   CB   CG   CD   OE1  NE2                             
REMARK 480     GLN A  169B  CB   CG   CD   OE1  NE2                             
REMARK 480     LYS A  222   CB   CG   CD   CE   NZ                              
REMARK 480     ARG A  239   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     ASP A  240   CB   CG   OD1  OD2                                  
REMARK 480     ASP B   23   CB   CG   OD1  OD2                                  
REMARK 480     GLU B   60A  CB   CG   CD   OE1  OE2                             
REMARK 480     ARG B   60B  CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     GLU B   78   CB   CG   CD   OE1  OE2                             
REMARK 480     GLU B   93   CB   CG   CD   OE1  OE2                             
REMARK 480     SER B  110   C    O    OG                                        
REMARK 480     GLN B  113   CB   CG   CD   OE1  NE2                             
REMARK 480     LYS B  222   CG   CD   CE   NZ                                   
REMARK 480     ASP B  223   CB   CG   OD1  OD2                                  
REMARK 480     ARG B  239   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  27       56.90   -147.09                                   
REMARK 500    LYS A  36     -163.29   -112.77                                   
REMARK 500    LEU A  41      -67.29    -90.96                                   
REMARK 500    ARG A  60B      70.91     46.68                                   
REMARK 500    PRO A  61      -52.77    -28.93                                   
REMARK 500    HIS A  62        8.21    -64.25                                   
REMARK 500    ASN A 101       34.12     76.76                                   
REMARK 500    CYS A 111      -80.20   -112.61                                   
REMARK 500    SER A 214      -69.79   -104.84                                   
REMARK 500    HIS B  27       57.34   -146.06                                   
REMARK 500    PRO B  28      -19.02    -47.31                                   
REMARK 500    LEU B  41      -65.52    -91.82                                   
REMARK 500    SER B  54     -169.50   -162.29                                   
REMARK 500    GLN B  60        4.24    -66.75                                   
REMARK 500    ARG B  60B      70.81     42.48                                   
REMARK 500    HIS B  62        8.36    -62.97                                   
REMARK 500    ASN B 101       34.87     71.89                                   
REMARK 500    CYS B 111      -82.47   -117.99                                   
REMARK 500    SER B 214      -68.85   -104.40                                   
REMARK 500    MET B 242       86.58    -68.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1122        DISTANCE =  6.53 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BBA A 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BBA B 250                 
DBREF  1A5H C    1     6  UNP    P00750   TPA_HUMAN      298    304             
DBREF  1A5H A   16   244  UNP    P00750   TPA_HUMAN      311    562             
DBREF  1A5H D    1     6  UNP    P00750   TPA_HUMAN      298    304             
DBREF  1A5H B   16   244  UNP    P00750   TPA_HUMAN      311    562             
SEQRES   1 C    7  THR CYS GLY LEU ARG GLN TYR                                  
SEQRES   1 A  252  ILE LYS GLY GLY LEU PHE ALA ASP ILE ALA SER HIS PRO          
SEQRES   2 A  252  TRP GLN ALA ALA ILE PHE ALA LYS HIS ARG ARG SER PRO          
SEQRES   3 A  252  GLY GLU ARG PHE LEU CYS GLY GLY ILE LEU ILE SER SER          
SEQRES   4 A  252  CYS TRP ILE LEU SER ALA ALA HIS CYS PHE GLN GLU ARG          
SEQRES   5 A  252  PHE PRO PRO HIS HIS LEU THR VAL ILE LEU GLY ARG THR          
SEQRES   6 A  252  TYR ARG VAL VAL PRO GLY GLU GLU GLU GLN LYS PHE GLU          
SEQRES   7 A  252  VAL GLU LYS TYR ILE VAL HIS LYS GLU PHE ASP ASP ASP          
SEQRES   8 A  252  THR TYR ASP ASN ASP ILE ALA LEU LEU GLN LEU LYS SER          
SEQRES   9 A  252  ASP SER SER ARG CYS ALA GLN GLU SER SER VAL VAL ARG          
SEQRES  10 A  252  THR VAL CYS LEU PRO PRO ALA ASP LEU GLN LEU PRO ASP          
SEQRES  11 A  252  TRP THR GLU CYS GLU LEU SER GLY TYR GLY LYS HIS GLU          
SEQRES  12 A  252  ALA LEU SER PRO PHE TYR SER GLU ARG LEU LYS GLU ALA          
SEQRES  13 A  252  HIS VAL ARG LEU TYR PRO SER SER ARG CYS THR SER GLN          
SEQRES  14 A  252  HIS LEU LEU ASN ARG THR VAL THR ASP ASN MET LEU CYS          
SEQRES  15 A  252  ALA GLY ASP THR ARG SER GLY GLY PRO GLN ALA ASN LEU          
SEQRES  16 A  252  HIS ASP ALA CYS GLN GLY ASP SER GLY GLY PRO LEU VAL          
SEQRES  17 A  252  CYS LEU ASN ASP GLY ARG MET THR LEU VAL GLY ILE ILE          
SEQRES  18 A  252  SER TRP GLY LEU GLY CYS GLY GLN LYS ASP VAL PRO GLY          
SEQRES  19 A  252  VAL TYR THR LYS VAL THR ASN TYR LEU ASP TRP ILE ARG          
SEQRES  20 A  252  ASP ASN MET ARG PRO                                          
SEQRES   1 D    7  THR CYS GLY LEU ARG GLN TYR                                  
SEQRES   1 B  252  ILE LYS GLY GLY LEU PHE ALA ASP ILE ALA SER HIS PRO          
SEQRES   2 B  252  TRP GLN ALA ALA ILE PHE ALA LYS HIS ARG ARG SER PRO          
SEQRES   3 B  252  GLY GLU ARG PHE LEU CYS GLY GLY ILE LEU ILE SER SER          
SEQRES   4 B  252  CYS TRP ILE LEU SER ALA ALA HIS CYS PHE GLN GLU ARG          
SEQRES   5 B  252  PHE PRO PRO HIS HIS LEU THR VAL ILE LEU GLY ARG THR          
SEQRES   6 B  252  TYR ARG VAL VAL PRO GLY GLU GLU GLU GLN LYS PHE GLU          
SEQRES   7 B  252  VAL GLU LYS TYR ILE VAL HIS LYS GLU PHE ASP ASP ASP          
SEQRES   8 B  252  THR TYR ASP ASN ASP ILE ALA LEU LEU GLN LEU LYS SER          
SEQRES   9 B  252  ASP SER SER ARG CYS ALA GLN GLU SER SER VAL VAL ARG          
SEQRES  10 B  252  THR VAL CYS LEU PRO PRO ALA ASP LEU GLN LEU PRO ASP          
SEQRES  11 B  252  TRP THR GLU CYS GLU LEU SER GLY TYR GLY LYS HIS GLU          
SEQRES  12 B  252  ALA LEU SER PRO PHE TYR SER GLU ARG LEU LYS GLU ALA          
SEQRES  13 B  252  HIS VAL ARG LEU TYR PRO SER SER ARG CYS THR SER GLN          
SEQRES  14 B  252  HIS LEU LEU ASN ARG THR VAL THR ASP ASN MET LEU CYS          
SEQRES  15 B  252  ALA GLY ASP THR ARG SER GLY GLY PRO GLN ALA ASN LEU          
SEQRES  16 B  252  HIS ASP ALA CYS GLN GLY ASP SER GLY GLY PRO LEU VAL          
SEQRES  17 B  252  CYS LEU ASN ASP GLY ARG MET THR LEU VAL GLY ILE ILE          
SEQRES  18 B  252  SER TRP GLY LEU GLY CYS GLY GLN LYS ASP VAL PRO GLY          
SEQRES  19 B  252  VAL TYR THR LYS VAL THR ASN TYR LEU ASP TRP ILE ARG          
SEQRES  20 B  252  ASP ASN MET ARG PRO                                          
HET    BBA  A 250      36                                                       
HET    BBA  B 250      36                                                       
HETNAM     BBA 2,7-BIS-(4-AMIDINOBENZYLIDENE)-CYCLOHEPTAN-1-ONE                 
HETSYN     BBA BIS-BENZAMIDINE                                                  
FORMUL   5  BBA    2(C23 H28 N4 O)                                              
FORMUL   7  HOH   *91(H2 O)                                                     
HELIX    1   1 ILE A   24  SER A   26  5                                   3    
HELIX    2   2 ARG A   37A SER A   37C 5                                   3    
HELIX    3   3 ALA A   56  PHE A   59  5                                   4    
HELIX    4   4 PRO A   61  HIS A   63  5                                   3    
HELIX    5   5 SER A  169A LEU A  171  5                                   4    
HELIX    6   6 THR A  232  ASN A  241  5                                  10    
HELIX    7   7 ILE B   24  SER B   26  5                                   3    
HELIX    8   8 ARG B   37A SER B   37C 5                                   3    
HELIX    9   9 ALA B   56  PHE B   59  5                                   4    
HELIX   10  10 PRO B   61  HIS B   63  5                                   3    
HELIX   11  11 SER B  169A HIS B  170  5                                   3    
HELIX   12  12 VAL B  231  ASN B  241  5                                  11    
SHEET    1   A 7 GLN A  81  GLU A  84  0                                        
SHEET    2   A 7 LEU A  64  LEU A  68 -1  N  LEU A  68   O  GLN A  81           
SHEET    3   A 7 GLN A  30  ALA A  35 -1  N  PHE A  34   O  THR A  65           
SHEET    4   A 7 ARG A  39  SER A  48 -1  N  GLY A  44   O  ALA A  31           
SHEET    5   A 7 TRP A  51  SER A  54 -1  N  LEU A  53   O  ILE A  45           
SHEET    6   A 7 ALA A 104  LEU A 108 -1  N  LEU A 106   O  ILE A  52           
SHEET    7   A 7 VAL A  85  VAL A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    1   B 2 GLU A 135  GLY A 140  0                                        
SHEET    2   B 2 LYS A 156  ARG A 161 -1  N  VAL A 160   O  CYS A 136           
SHEET    1   C 4 MET A 180  ALA A 183  0                                        
SHEET    2   C 4 GLY A 226  LYS A 230 -1  N  TYR A 228   O  LEU A 181           
SHEET    3   C 4 ARG A 206  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    4   C 4 PRO A 198  ASN A 203 -1  N  ASN A 203   O  ARG A 206           
SHEET    1   D 7 GLN B  81  GLU B  84  0                                        
SHEET    2   D 7 LEU B  64  LEU B  68 -1  N  LEU B  68   O  GLN B  81           
SHEET    3   D 7 GLN B  30  LYS B  36 -1  N  PHE B  34   O  THR B  65           
SHEET    4   D 7 GLU B  38  SER B  48 -1  N  GLY B  44   O  ALA B  31           
SHEET    5   D 7 TRP B  51  SER B  54 -1  N  LEU B  53   O  ILE B  45           
SHEET    6   D 7 ALA B 104  LEU B 108 -1  N  LEU B 106   O  ILE B  52           
SHEET    7   D 7 VAL B  85  VAL B  90 -1  N  ILE B  89   O  LEU B 105           
SHEET    1   E 2 GLU B 135  GLY B 140  0                                        
SHEET    2   E 2 LYS B 156  ARG B 161 -1  N  VAL B 160   O  CYS B 136           
SHEET    1   F 4 MET B 180  ALA B 183  0                                        
SHEET    2   F 4 GLY B 226  LYS B 230 -1  N  TYR B 228   O  LEU B 181           
SHEET    3   F 4 ARG B 206  TRP B 215 -1  N  TRP B 215   O  VAL B 227           
SHEET    4   F 4 PRO B 198  ASN B 203 -1  N  ASN B 203   O  ARG B 206           
SSBOND   1 CYS C    1    CYS A  122                          1555   1555  2.05  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.03  
SSBOND   3 CYS A   50    CYS A  111                          1555   1555  2.04  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.04  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.02  
SSBOND   7 CYS D    1    CYS B  122                          1555   1555  2.05  
SSBOND   8 CYS B   42    CYS B   58                          1555   1555  2.03  
SSBOND   9 CYS B   50    CYS B  111                          1555   1555  2.03  
SSBOND  10 CYS B  136    CYS B  201                          1555   1555  2.03  
SSBOND  11 CYS B  168    CYS B  182                          1555   1555  2.05  
SSBOND  12 CYS B  191    CYS B  220                          1555   1555  2.03  
SITE     1 AC1 14 ASP A  97  THR A  98  TYR A  99  PRO A 186E                   
SITE     2 AC1 14 ASP A 189  ALA A 190  GLN A 192  SER A 195                    
SITE     3 AC1 14 TRP A 215  GLY A 216  GLY A 219  CYS A 220                    
SITE     4 AC1 14 GLY A 226  HOH A1130                                          
SITE     1 AC2 12 ASP B  97  THR B  98  TYR B  99  PRO B 186E                   
SITE     2 AC2 12 ASP B 189  ALA B 190  GLN B 192  SER B 195                    
SITE     3 AC2 12 ILE B 213  TRP B 215  GLY B 216  GLY B 219                    
CRYST1  151.830   60.500   62.610  90.00 110.50  90.00 C 1 2 1       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      0.006586  0.000000  0.002463        0.00000                         
SCALE2      0.000000  0.016529  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017052        0.00000                         
MTRIX1   1  0.803136  0.001692  0.595794      -22.57170    1                    
MTRIX2   1  0.036418 -0.998266 -0.046257       91.93190    1                    
MTRIX3   1  0.594682  0.058848 -0.801804       62.33930    1                    
MTRIX1   2  0.757677  0.005193  0.652610      -23.84180    1                    
MTRIX2   2  0.006892 -0.999976 -0.000045       91.38040    1                    
MTRIX3   2  0.652594  0.004532 -0.757694       62.95840    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system