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Database: PDB
Entry: 1H9H
LinkDB: 1H9H
Original site: 1H9H 
HEADER    HYDROLASE INHIBITOR                     12-MAR-01   1H9H              
TITLE     COMPLEX OF EETI-II WITH PORCINE TRYPSIN                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: E;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TRYPSIN INHIBITOR II;                                      
COMPND   7 CHAIN: I;                                                            
COMPND   8 SYNONYM: EETI-II;                                                    
COMPND   9 MUTATION: YES;                                                       
COMPND  10 OTHER_DETAILS: C-TERMINAL TAG OF 6 HISTIDINES                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 ORGAN: PANCREAS;                                                     
SOURCE   6 SECRETION: SALIVA;                                                   
SOURCE   7 OTHER_DETAILS: SIGMA;                                                
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: ECBALLIUM ELATERIUM;                            
SOURCE  11 ORGANISM_COMMON: SQUIRTING CUCUMBER;                                 
SOURCE  12 ORGANISM_TAXID: 3679                                                 
KEYWDS    HYDROLASE INHIBITOR, COMPLEX (SERINE PROTEASE/INHIBITOR),             
KEYWDS   2 TRYPSIN, SQUASH INHIBITOR, CYSTINE KNOT, HYDROLASE                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.KRAETZNER,A.WENTZEL,H.KOLMAR,I.USON                                 
REVDAT   3   24-FEB-09 1H9H    1       VERSN                                    
REVDAT   2   06-MAY-08 1H9H    1       VERSN  REMARK CISPEP                     
REVDAT   1   26-JUL-04 1H9H    0                                                
JRNL        AUTH   R.KRAETZNER,J.E.DEBRECZENI,T.PAPE,T.R.SCHNEIDER,             
JRNL        AUTH 2 A.WENTZEL,H.KOLMAR,G.M.SHELDRICK,I.USON                      
JRNL        TITL   STRUCTURE OF ECBALLIUM ELATERIUM TRYPSIN INHIBITOR           
JRNL        TITL 2 II (EETI-II): A RIGID MOLECULAR SCAFFOLD                     
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  61  1255 2005              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   16131759                                                     
JRNL        DOI    10.1107/S0907444905021207                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.WENTZEL,A.CHRISTMANN,R.KRAETZNER,H.KOLMAR                  
REMARK   1  TITL   SEQUENCE REQUIREMENTS OF THE GPNG BETA-TURN OF THE           
REMARK   1  TITL 2 ECBALLIUM ELATERIUM TRYPSIN INHIBITOR II EXPLORED            
REMARK   1  TITL 3 BY COMBINATORIAL LIBRARY SCREENING                           
REMARK   1  REF    J.BIOL.CHEM.                  V. 274 21037 1999              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   10409654                                                     
REMARK   1  DOI    10.1074/JBC.274.30.21037                                     
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.HEITZ,D.LE-NGUYEN,L.CHICHE                                 
REMARK   1  TITL   MIN-21 AND MIN-23, THE SMALLEST PEPTIDES THAT FOLD           
REMARK   1  TITL 2 LIKE A CYSTINE-STABILIZED BETA-SHEET MOTIF:                  
REMARK   1  TITL 3 DESIGN, SOLUTION STRUCTURE, AND THERMAL STABILITY            
REMARK   1  REF    BIOCHEMISTRY                  V.  38 10615 1999              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1  PMID   10441159                                                     
REMARK   1  DOI    10.1021/BI990821K                                            
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   L.CHICHE,C.GABORIAUD,A.HEITZ,J.P.MORNON,B.CASTRO,            
REMARK   1  AUTH 2 P.A.KOLLMAN                                                  
REMARK   1  TITL   USE OF RESTRAINED MOLECULAR DYNAMICS IN WATER TO             
REMARK   1  TITL 2 DETERMINE THREE-DIMENSIONAL PROTEIN STRUCTURE:               
REMARK   1  TITL 3 PREDICTION OF THE THREE-DIMENSIONAL STRUCTURE OF             
REMARK   1  TITL 4 ECBALLIUM ELATERIUM TRYPSIN INHIBITOR II                     
REMARK   1  REF    PROTEINS: STRUCT.,FUNCT.,     V.   6   405 1989              
REMARK   1  REF  2 GENET.                                                       
REMARK   1  REFN                   ISSN 0887-3585                               
REMARK   1  PMID   2622910                                                      
REMARK   1  DOI    10.1002/PROT.340060407                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.5  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.5                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.2349                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.2331                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.2758                 
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.0                    
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2475                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 49346                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.2137                 
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.2118                 
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.2537                 
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.1                    
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 2050                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 40554                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1911                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 1                                             
REMARK   3   SOLVENT ATOMS      : 177                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1994.85                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1746.90                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 17                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 8170                    
REMARK   3   NUMBER OF RESTRAINTS                     : 7778                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.009                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.028                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.0294                  
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.054                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.056                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.016                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.068                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2          
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1H9H COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAR-01.                  
REMARK 100 THE PDBE ID CODE IS EBI-5935.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-APR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.70                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9326                             
REMARK 200  MONOCHROMATOR                  : DIAMOND (111), GE(220)             
REMARK 200  OPTICS                         : TOROIDAL MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49533                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 8.050                              
REMARK 200  R MERGE                    (I) : 0.05320                            
REMARK 200  R SYM                      (I) : 0.02780                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.2400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.48                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37550                            
REMARK 200  R SYM FOR SHELL            (I) : 0.27790                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.390                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1LDT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 3 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
REMARK 290      13555   Y+3/4,X+1/4,-Z+1/4                                      
REMARK 290      14555   -Y+3/4,-X+3/4,-Z+3/4                                    
REMARK 290      15555   Y+1/4,-X+1/4,Z+3/4                                      
REMARK 290      16555   -Y+1/4,X+3/4,Z+1/4                                      
REMARK 290      17555   X+3/4,Z+1/4,-Y+1/4                                      
REMARK 290      18555   -X+1/4,Z+3/4,Y+1/4                                      
REMARK 290      19555   -X+3/4,-Z+3/4,-Y+3/4                                    
REMARK 290      20555   X+1/4,-Z+1/4,Y+3/4                                      
REMARK 290      21555   Z+3/4,Y+1/4,-X+1/4                                      
REMARK 290      22555   Z+1/4,-Y+1/4,X+3/4                                      
REMARK 290      23555   -Z+1/4,Y+3/4,X+1/4                                      
REMARK 290      24555   -Z+3/4,-Y+3/4,-X+3/4                                    
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       60.52500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.52500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.52500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.52500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.52500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.52500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       60.52500            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       60.52500            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       60.52500            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       60.52500            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       60.52500            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       60.52500            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       60.52500            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       60.52500            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       60.52500            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       60.52500            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       60.52500            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       60.52500            
REMARK 290   SMTRY1  13  0.000000  1.000000  0.000000       90.78750            
REMARK 290   SMTRY2  13  1.000000  0.000000  0.000000       30.26250            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       30.26250            
REMARK 290   SMTRY1  14  0.000000 -1.000000  0.000000       90.78750            
REMARK 290   SMTRY2  14 -1.000000  0.000000  0.000000       90.78750            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       90.78750            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       30.26250            
REMARK 290   SMTRY2  15 -1.000000  0.000000  0.000000       30.26250            
REMARK 290   SMTRY3  15  0.000000  0.000000  1.000000       90.78750            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       30.26250            
REMARK 290   SMTRY2  16  1.000000  0.000000  0.000000       90.78750            
REMARK 290   SMTRY3  16  0.000000  0.000000  1.000000       30.26250            
REMARK 290   SMTRY1  17  1.000000  0.000000  0.000000       90.78750            
REMARK 290   SMTRY2  17  0.000000  0.000000  1.000000       30.26250            
REMARK 290   SMTRY3  17  0.000000 -1.000000  0.000000       30.26250            
REMARK 290   SMTRY1  18 -1.000000  0.000000  0.000000       30.26250            
REMARK 290   SMTRY2  18  0.000000  0.000000  1.000000       90.78750            
REMARK 290   SMTRY3  18  0.000000  1.000000  0.000000       30.26250            
REMARK 290   SMTRY1  19 -1.000000  0.000000  0.000000       90.78750            
REMARK 290   SMTRY2  19  0.000000  0.000000 -1.000000       90.78750            
REMARK 290   SMTRY3  19  0.000000 -1.000000  0.000000       90.78750            
REMARK 290   SMTRY1  20  1.000000  0.000000  0.000000       30.26250            
REMARK 290   SMTRY2  20  0.000000  0.000000 -1.000000       30.26250            
REMARK 290   SMTRY3  20  0.000000  1.000000  0.000000       90.78750            
REMARK 290   SMTRY1  21  0.000000  0.000000  1.000000       90.78750            
REMARK 290   SMTRY2  21  0.000000  1.000000  0.000000       30.26250            
REMARK 290   SMTRY3  21 -1.000000  0.000000  0.000000       30.26250            
REMARK 290   SMTRY1  22  0.000000  0.000000  1.000000       30.26250            
REMARK 290   SMTRY2  22  0.000000 -1.000000  0.000000       30.26250            
REMARK 290   SMTRY3  22  1.000000  0.000000  0.000000       90.78750            
REMARK 290   SMTRY1  23  0.000000  0.000000 -1.000000       30.26250            
REMARK 290   SMTRY2  23  0.000000  1.000000  0.000000       90.78750            
REMARK 290   SMTRY3  23  1.000000  0.000000  0.000000       30.26250            
REMARK 290   SMTRY1  24  0.000000  0.000000 -1.000000       90.78750            
REMARK 290   SMTRY2  24  0.000000 -1.000000  0.000000       90.78750            
REMARK 290   SMTRY3  24 -1.000000  0.000000  0.000000       90.78750            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  1                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1800 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.5 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  ENGINEERED MUTATION MET 7 ILE IN CHAIN I                            
REMARK 400  DUE TO RADIATION DAMAGE CYSTEINES WERE MODELLED PARTLY              
REMARK 400  CLEAVED AND OXYDIZED TO SERINE                                      
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     HIS I    31                                                      
REMARK 465     HIS I    32                                                      
REMARK 465     HIS I    33                                                      
REMARK 465     HIS I    34                                                      
REMARK 465     HIS I    35                                                      
REMARK 465     HIS I    36                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG E  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E  77    CD   OE1  OE2                                       
REMARK 470     SER E 110    OG                                                  
REMARK 470     CYS E 128    SG                                                  
REMARK 470     GLU E 135    CD   OE1  OE2                                       
REMARK 470     SER E 147    OG                                                  
REMARK 470     LYS E 222    CE   NZ                                             
REMARK 470     LYS E 230    CE   NZ                                             
REMARK 470     LYS I  10    CG   CD   CE   NZ                                   
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    TYR E  20   CB  -  CG  -  CD2 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    TYR E  59   CB  -  CG  -  CD2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG E  66   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG I   4   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG I   8   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 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 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 E  71      -60.89   -128.05                                   
REMARK 500    SER E 214      -68.11   -125.27                                   
REMARK 500    ARG I   4       36.13    -93.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620   SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E1246  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E  70   OE1                                                    
REMARK 620 2 ASN E  72   O    84.4                                              
REMARK 620 3 VAL E  75   O   159.2  82.5                                        
REMARK 620 4 HOH E2044   O    79.8  97.7  86.0                                  
REMARK 620 5 HOH E2050   O    90.5  92.0 105.9 165.5                            
REMARK 620 6 GLU E  80   OE2 100.9 174.5  92.9  84.8  86.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "B" IN EACH CHAIN ON SHEET RECORDS           
REMARK 700 BELOW IS ACTUALLY AN  6-STRANDED BARREL THIS IS REPRESENTED BY       
REMARK 700 A  7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS              
REMARK 700 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  CA E1246                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AKS   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF THE FIRST ACTIVE                               
REMARK 900  AUTOLYSATE FORM OF THE PORCINE ALPHA TRYPSIN                        
REMARK 900 RELATED ID: 1AN1   RELATED DB: PDB                                   
REMARK 900  LEECH-DERIVED TRYPTASE INHIBITOR/TRYPSIN                            
REMARK 900  COMPLEX                                                             
REMARK 900 RELATED ID: 1AVW   RELATED DB: PDB                                   
REMARK 900  COMPLEX PORCINE PANCREATIC TRYPSIN/SOYBEAN                          
REMARK 900  TRYPSIN INHIBITOR, ORTHORHOMBIC CRYSTAL FORM                        
REMARK 900 RELATED ID: 1AVX   RELATED DB: PDB                                   
REMARK 900  COMPLEX PORCINE PANCREATIC TRYPSIN/SOYBEAN                          
REMARK 900  TRYPSIN INHIBITOR, TETRAGONAL CRYSTAL FORM                          
REMARK 900 RELATED ID: 1C9P   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF BDELLASTASIN WITH PORCINE TRYPSIN                        
REMARK 900 RELATED ID: 1D3O   RELATED DB: PDB                                   
REMARK 900  KNOWLEDGE BASED MODEL OF A SERINE PROTEASE                          
REMARK 900  INHIBITOR OF CUCURBITACEAE FAMILY (THEORETICAL                      
REMARK 900  MODEL) BOUND TO TRYPSIN                                             
REMARK 900 RELATED ID: 1DF2   RELATED DB: PDB                                   
REMARK 900  KNOWLEDGE BASED MODEL OF A SERINE PROTEASE                          
REMARK 900  INHIBITOR OF CUCURBITACEAE FAMILY (THEORETICAL                      
REMARK 900  MODEL) BOUND TO TRYPSIN                                             
REMARK 900 RELATED ID: 1EJA   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF PORCINE TRYPSIN COMPLEXED WITH                         
REMARK 900  BDELLASTASIN, AN ANTISTASIN-TYPE INHIBITOR                          
REMARK 900 RELATED ID: 1EPT   RELATED DB: PDB                                   
REMARK 900  PORCINE E-TRYPSIN                                                   
REMARK 900 RELATED ID: 1EWU   RELATED DB: PDB                                   
REMARK 900  KNOWLEDGE BASED MODEL OF A SERINE PROTEASE                          
REMARK 900  INHIBITOR OFCUCURBITACEAE FAMILY (THEORETICAL                       
REMARK 900  MODEL) BOUND TO TRYPSIN.                                            
REMARK 900 RELATED ID: 1FMG   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN                           
REMARK 900  WITH 0.04%POLYDOCANOL                                               
REMARK 900 RELATED ID: 1FN6   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN                           
REMARK 900  WITH 0.1%POLYDOCANOL                                                
REMARK 900 RELATED ID: 1FNI   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN                           
REMARK 900  WITH 0.01%POLYDOCANOL                                               
REMARK 900 RELATED ID: 1H9H   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF EETI-II WITH PORCINE TRYPSIN                             
REMARK 900 RELATED ID: 1LDT   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF LEECH-DERIVED TRYPTASE INHIBITOR                         
REMARK 900  WITH PORCINE TRYPSIN                                                
REMARK 900 RELATED ID: 1LT2   RELATED DB: PDB                                   
REMARK 900  PREDICTION OF TERTIARY STRUCTURE OF LEUCAENA                        
REMARK 900  LEUCOCEPHALATRYPSIN INHIBITOR/TRYPSIN COMPLEX.                      
REMARK 900 RELATED ID: 1MCT   RELATED DB: PDB                                   
REMARK 900  TRYPSIN COMPLEXED WITH INHIBITOR FROM BITTER                        
REMARK 900  GOURD                                                               
REMARK 900 RELATED ID: 1QQU   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN                           
REMARK 900  WITH BOUND ACETATE ION                                              
REMARK 900 RELATED ID: 1R0T   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF TRYPSIN-SECOND DOMAIN                          
REMARK 900  OF THE OVOMUCOIDTURKEY EGG WHITE INHIBITOR                          
REMARK 900  COMPLEX                                                             
REMARK 900 RELATED ID: 1S5S   RELATED DB: PDB                                   
REMARK 900  PORCINE TRYPSIN COMPLEXED WITH GUANIDINE-3-                         
REMARK 900  PROPANOLINHIBITOR                                                   
REMARK 900 RELATED ID: 1S6F   RELATED DB: PDB                                   
REMARK 900  PORCINE TRYPSIN COVALENT COMPLEX WITH BORATE                        
REMARK 900  AND GUANIDINE-3 INHIBITOR                                           
REMARK 900 RELATED ID: 1S6H   RELATED DB: PDB                                   
REMARK 900  PORCINE TRYPSIN COMPLEXED WITH GUANIDINE-3-                         
REMARK 900  PROPANOLINHIBITOR                                                   
REMARK 900 RELATED ID: 1S81   RELATED DB: PDB                                   
REMARK 900  PORCINE TRYPSIN WITH NO INHIBITOR BOUND                             
REMARK 900 RELATED ID: 1S82   RELATED DB: PDB                                   
REMARK 900  PORCINE TRYPSIN COMPLEXED WITH BORATE AND                           
REMARK 900  ETHYLENE GLYCOL                                                     
REMARK 900 RELATED ID: 1S83   RELATED DB: PDB                                   
REMARK 900  PORCINE TRYPSIN COMPLEXED WITH 4-AMINO                              
REMARK 900  PROPANOL                                                            
REMARK 900 RELATED ID: 1S84   RELATED DB: PDB                                   
REMARK 900  PORCINE TRYPSIN COVALENT COMPLEX WITH 4-                            
REMARK 900  AMINO BUTANOL,BORATE AND ETHYLENE GLYCOL                            
REMARK 900 RELATED ID: 1S85   RELATED DB: PDB                                   
REMARK 900  PORCINE TRYPSIN COMPLEXED WITH P-HYDROXYMETHYL                      
REMARK 900   BENZAMIDINEAND BORATE                                              
REMARK 900 RELATED ID: 1TFX   RELATED DB: PDB                                   
REMARK 900  COMPLEX OF THE SECOND KUNITZ DOMAIN OF                              
REMARK 900  TISSUE FACTOR PATHWAY INHIBITOR WITH PORCINE                        
REMARK 900  TRYPSIN                                                             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999  THE MICROHETEROGENEITY FOR THE CYSTEINE/SERINES AT RESIDUES         
REMARK 999  22,42,58, 136, 157, 191, 201, 220 (CHAIN E) AND RESIDUES            
REMARK 999  15, 27 (CHAIN I) ARE THE RESULT OF RADIATION DAMAGE                 
REMARK 999  DURING DATA COLLECTION THAT CAUSED THE REDUCTION OF THE             
REMARK 999  DI-SUPHIDES AND OXIDATION OF THE CYS TO SER                         
DBREF  1H9H E   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1H9H I    1    30  UNP    P12071   ITR2_ECBEL       1     30             
DBREF  1H9H I   31    36  PDB    1H9H     1H9H            31     36             
SEQADV 1H9H ILE I    7  UNP  P12071    MET     7 ENGINEERED MUTATION            
SEQADV 1H9H SER E   22  UNP  P00761    CYS    22 MICROHETEROGENEITY             
SEQADV 1H9H SER E   42  UNP  P00761    CYS    42 MICROHETEROGENEITY             
SEQADV 1H9H SER E   58  UNP  P00761    CYS    58 MICROHETEROGENEITY             
SEQADV 1H9H SER E  136  UNP  P00761    CYS   136 MICROHETEROGENEITY             
SEQADV 1H9H SER E  157  UNP  P00761    CYS   157 MICROHETEROGENEITY             
SEQADV 1H9H SER E  191  UNP  P00761    CYS   191 MICROHETEROGENEITY             
SEQADV 1H9H SER E  201  UNP  P00761    CYS   201 MICROHETEROGENEITY             
SEQADV 1H9H SER E  220  UNP  P00761    CYS   220 MICROHETEROGENEITY             
SEQADV 1H9H SER I   15  UNP  P12071    CYS    15 MICROHETEROGENEITY             
SEQADV 1H9H SER I   27  UNP  P12071    CYS    27 MICROHETEROGENEITY             
SEQRES   1 E  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 E  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 E  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 E  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 E  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 E  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 E  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 E  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 E  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 E  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 E  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 E  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 E  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 E  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 E  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 E  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 E  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 E  223  ALA ASN                                                      
SEQRES   1 I   36  GLY CYS PRO ARG ILE LEU ILE ARG CYS LYS GLN ASP SER          
SEQRES   2 I   36  ASP CYS LEU ALA GLY CYS VAL CYS GLY PRO ASN GLY PHE          
SEQRES   3 I   36  CYS GLY SER PRO HIS HIS HIS HIS HIS HIS                      
HET     CA  E1246       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *177(H2 O1)                                                   
HELIX    1   1 ALA E   55  TYR E   59  5                                   5    
HELIX    2   2 SER E  164  TYR E  172  1                                   9    
HELIX    3   3 TYR E  234  ALA E  243  1                                  10    
HELIX    4   4 GLN I   11  CYS I   15  5                                   5    
SHEET    1  EA 7 TYR E  20  THR E  21  0                                        
SHEET    2  EA 7 GLN E 156  PRO E 161 -1  O  CYS E 157   N  TYR E  20           
SHEET    3  EA 7 GLU E 135  GLY E 140 -1  O  CYS E 136   N  ALA E 160           
SHEET    4  EA 7 PRO E 198  CYS E 201 -1  O  PRO E 198   N  SER E 139           
SHEET    5  EA 7 GLN E 204  GLY E 216 -1  O  GLN E 204   N  CYS E 201           
SHEET    6  EA 7 GLY E 226  LYS E 230 -1  O  VAL E 227   N  TRP E 215           
SHEET    7  EA 7 MET E 180  VAL E 183 -1  O  ILE E 181   N  TYR E 228           
SHEET    1  EB 6 TYR E  20  THR E  21  0                                        
SHEET    2  EB 6 GLN E 156  PRO E 161 -1  O  CYS E 157   N  TYR E  20           
SHEET    3  EB 6 GLU E 135  GLY E 140 -1  O  CYS E 136   N  ALA E 160           
SHEET    4  EB 6 PRO E 198  CYS E 201 -1  O  PRO E 198   N  SER E 139           
SHEET    5  EB 6 GLN E 204  GLY E 216 -1  O  GLN E 204   N  CYS E 201           
SHEET    6  IB 6 CYS I   2  PRO I   3 -1  O  CYS I   2   N  GLY E 216           
SHEET    1  EC 7 GLN E  30  ASN E  34  0                                        
SHEET    2  EC 7 HIS E  40  ASN E  48 -1  N  PHE E  41   O  LEU E  33           
SHEET    3  EC 7 TRP E  51  SER E  54 -1  O  TRP E  51   N  ILE E  47           
SHEET    4  EC 7 MET E 104  LEU E 108 -1  O  MET E 104   N  SER E  54           
SHEET    5  EC 7 GLN E  81  THR E  90 -1  N  ALA E  86   O  LYS E 107           
SHEET    6  EC 7 GLN E  64  LEU E  67 -1  O  VAL E  65   N  ILE E  83           
SHEET    7  EC 7 GLN E  30  ASN E  34 -1  O  SER E  32   N  ARG E  66           
SHEET    1  IA 2 VAL I  20  CYS I  21  0                                        
SHEET    2  IA 2 CYS I  27  GLY I  28 -1  O  GLY I  28   N  VAL I  20           
SSBOND   1 CYS E   22    CYS E  157                          1555   1555  2.05  
SSBOND   2 CYS E   42    CYS E   58                          1555   1555  2.05  
SSBOND   3 CYS E  136    CYS E  201                          1555   1555  2.01  
SSBOND   4 CYS E  168    CYS E  182                          1555   1555  2.06  
SSBOND   5 CYS E  191    CYS E  220                          1555   1555  2.04  
SSBOND   6 CYS I    2    CYS I   19                          1555   1555  2.03  
SSBOND   7 CYS I    9    CYS I   21                          1555   1555  2.09  
SSBOND   8 CYS I   15    CYS I   27                          1555   1555  2.04  
LINK        CA    CA E1246                 OE1 GLU E  70     1555   1555  2.35  
LINK        CA    CA E1246                 O   ASN E  72     1555   1555  2.28  
LINK        CA    CA E1246                 O   VAL E  75     1555   1555  2.28  
LINK        CA    CA E1246                 O   HOH E2044     1555   1555  2.62  
LINK        CA    CA E1246                 O   HOH E2050     1555   1555  2.41  
LINK        CA    CA E1246                 OE2 GLU E  80     1555   1555  2.32  
SITE     1 AC1  6 GLU E  70  ASN E  72  VAL E  75  GLU E  80                    
SITE     2 AC1  6 HOH E2044  HOH E2050                                          
CRYST1  121.050  121.050  121.050  90.00  90.00  90.00 P 41 3 2     24          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008261  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008261  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008261        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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