GenomeNet

Database: PDB
Entry: 1H9I
LinkDB: 1H9I
Original site: 1H9I 
HEADER    HYDROLASE/INHIBITOR                     12-MAR-01   1H9I              
TITLE     COMPLEX OF EETI-II MUTANT 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 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES;                                                       
COMPND  11 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                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.KRAETZNER,A.WENTZEL,H.KOLMAR,I.USON                                 
REVDAT   2   24-FEB-09 1H9I    1       VERSN                                    
REVDAT   1   26-JUL-04 1H9I    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.    1.9  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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
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) : 0.1423                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.1416                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.1755                 
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.0                    
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 1287                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 25902                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.1364                 
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.1356                 
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.1707                 
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.0                    
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 1216                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 24158                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 1883                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 1                                             
REMARK   3   SOLVENT ATOMS      : 135                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 1958.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 1741.00                 
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 13                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 8079                    
REMARK   3   NUMBER OF RESTRAINTS                     : 7813                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.007                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.026                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.0277                  
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.041                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.050                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.018                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.070                   
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 1H9I 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-5944.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 298.0                              
REMARK 200  PH                             : 6.70                               
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          : MAC M18XHF                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54187                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : OSMIC MIRROR SYSTEM                
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
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   : 26024                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : 0.06830                            
REMARK 200  R SYM                      (I) : 0.04050                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.8400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.31                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21710                            
REMARK 200  R SYM FOR SHELL            (I) : 0.10310                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.890                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1LDT                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       69.93100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       69.93100            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       16.83350            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       69.93100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       69.93100            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       16.83350            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       69.93100            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       69.93100            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       16.83350            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       69.93100            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       69.93100            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       16.83350            
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 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  CHAIN I ENGINEERED MUTATIONS MET 7 ILE,GLY 22 THR,PRO 23 ASN        
REMARK 400  AND GLY 25 LYS                                                      
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    CZ   NH1  NH2                                       
REMARK 470     LYS E 145    CE   NZ                                             
REMARK 470     SER E 147    OG                                                  
REMARK 470     LYS E 222    CE   NZ                                             
REMARK 470     ARG I   8    NE   CZ   NH1  NH2                                  
REMARK 470     LYS I  10    CG   CD   CE   NZ                                   
REMARK 470     ASN I  23    CG   OD1  ND2                                       
REMARK 470     ASN I  24    CG   OD1  ND2                                       
REMARK 470     LYS I  25    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  59   CB  -  CG  -  CD1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    TYR E  59   CB  -  CG  -  CD2 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG I   4   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 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      -64.59   -133.03                                   
REMARK 500    SER E 214      -67.95   -125.14                                   
REMARK 500    ARG I   4       35.08    -97.97                                   
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    86.1                                              
REMARK 620 3 HOH E2031   O    83.8  93.0                                        
REMARK 620 4 HOH E2039   O    93.9  92.1 174.3                                  
REMARK 620 5 GLU E  80   OE2  99.0 170.4  95.7  79.5                            
REMARK 620 6 VAL E  75   O   163.9  79.8  89.1  94.4  96.1                      
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: 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: 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: 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 900 RELATED ID: 2ETI   RELATED DB: PDB                                   
REMARK 900  TRYPSIN INHIBITOR II (EETI II)                                      
REMARK 900 RELATED ID: 2LET   RELATED DB: PDB                                   
REMARK 900  TRYPSIN INHIBITOR II MUTANT WITH ILE 5                              
REMARK 900  REPLACED BY LEU (I5L) (NMR, 20 STRUCTURES)                          
DBREF  1H9I E   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1H9I I    1    30  UNP    P12071   ITR2_ECBEL       1     30             
DBREF  1H9I I   31    36  PDB    1H9I     1H9I            31     36             
SEQADV 1H9I THR I   22  UNP  P12071    GLY    22 MUTATION                       
SEQADV 1H9I ASN I   23  UNP  P12071    PRO    23 MUTATION                       
SEQADV 1H9I LYS I   25  UNP  P12071    GLY    25 MUTATION                       
SEQADV 1H9I ILE I    7  UNP  P12071    MET     7 MUTATION                       
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 THR ASN ASN LYS 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   *135(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  244  1                                  11    
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  2.01  
SSBOND   2 CYS E   42    CYS E   58                          1555   1555  2.01  
SSBOND   3 CYS E  128    CYS E  232                          1555   1555  2.06  
SSBOND   4 CYS E  136    CYS E  201                          1555   1555  2.00  
SSBOND   5 CYS E  168    CYS E  182                          1555   1555  1.99  
SSBOND   6 CYS E  191    CYS E  220                          1555   1555  2.04  
SSBOND   7 CYS I    2    CYS I   19                          1555   1555  2.00  
SSBOND   8 CYS I    9    CYS I   21                          1555   1555  2.04  
SSBOND   9 CYS I   15    CYS I   27                          1555   1555  2.03  
LINK        CA    CA E1246                 OE1 GLU E  70     1555   1555  2.35  
LINK        CA    CA E1246                 O   ASN E  72     1555   1555  2.34  
LINK        CA    CA E1246                 O   HOH E2031     1555   1555  2.50  
LINK        CA    CA E1246                 O   HOH E2039     1555   1555  2.68  
LINK        CA    CA E1246                 OE2 GLU E  80     1555   1555  2.43  
LINK        CA    CA E1246                 O   VAL E  75     1555   1555  2.44  
SITE     1 AC1  6 GLU E  70  ASN E  72  VAL E  75  GLU E  80                    
SITE     2 AC1  6 HOH E2031  HOH E2039                                          
CRYST1  139.862  139.862   33.667  90.00  90.00  90.00 I 4           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      0.007150  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007150  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029703        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system