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Database: PDB
Entry: 1AVW
LinkDB: 1AVW
Original site: 1AVW 
HEADER    COMPLEX (PROTEINASE/INHIBITOR)          21-SEP-97   1AVW              
TITLE     COMPLEX PORCINE PANCREATIC TRYPSIN/SOYBEAN TRYPSIN                    
TITLE    2 INHIBITOR, ORTHORHOMBIC CRYSTAL FORM                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PPT;                                                        
COMPND   5 EC: 3.4.21.4;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TRYPSIN INHIBITOR;                                         
COMPND   8 CHAIN: B;                                                            
COMPND   9 SYNONYM: STI                                                         
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 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: GLYCINE MAX;                                    
SOURCE   8 ORGANISM_COMMON: SOYBEAN;                                            
SOURCE   9 ORGANISM_TAXID: 3847;                                                
SOURCE  10 ORGAN: SEED                                                          
KEYWDS    COMPLEX (PROTEINASE/INHIBITOR), PORCINE TRYPSIN, SOYBEAN              
KEYWDS   2 TRYPSIN INHIBITOR, KUNITZ-TYPE, BETA-TREFOIL FOLD                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.K.SONG,S.W.SUH                                                      
REVDAT   3   24-FEB-09 1AVW    1       VERSN                                    
REVDAT   2   18-NOV-98 1AVW    2       SOURCE COMPND REMARK KEYWDS              
REVDAT   2 2                   2       HEADER CONECT LINK                       
REVDAT   1   28-OCT-98 1AVW    0                                                
JRNL        AUTH   H.K.SONG,S.W.SUH                                             
JRNL        TITL   KUNITZ-TYPE SOYBEAN TRYPSIN INHIBITOR REVISITED:             
JRNL        TITL 2 REFINED STRUCTURE OF ITS COMPLEX WITH PORCINE                
JRNL        TITL 3 TRYPSIN REVEALS AN INSIGHT INTO THE INTERACTION              
JRNL        TITL 4 BETWEEN A HOMOLOGOUS INHIBITOR FROM ERYTHRINA                
JRNL        TITL 5 CAFFRA AND TISSUE-TYPE PLASMINOGEN ACTIVATOR.                
JRNL        REF    J.MOL.BIOL.                   V. 275   347 1998              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9466914                                                      
JRNL        DOI    10.1006/JMBI.1997.1469                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   H.K.SONG                                                     
REMARK   1  TITL   CRYSTAL STRUCTURE ANALYSES OF HUMAN                          
REMARK   1  TITL 2 A1-ANTITRYPSIN, SOYBEAN KUNITZ-TYPE TRYPSIN                  
REMARK   1  TITL 3 INHIBITOR, AND BARLEY CHITINASE                              
REMARK   1  REF    THESIS, SEOUL NATIONAL                     1997              
REMARK   1  REF  2 UNIVERSITY                                                   
REMARK   1  PUBL   SEOUL : SEOUL NATIONAL UNIVERSITY (THESIS)                   
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.K.LEE,H.K.SONG,K.Y.HWANG,K.K.KIM,S.W.SUH                   
REMARK   1  TITL   CRYSTALLIZATION OF KUNITZ-TYPE SOYBEAN TRYPSIN               
REMARK   1  TITL 2 INHIBITOR                                                    
REMARK   1  REF    MOL.CELLS                     V.   3   335 1993              
REMARK   1  REFN                   ISSN 1016-8478                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.K.LEE                                                      
REMARK   1  TITL   CRYSTALLIZATION AND PRELIMINARY X-RAY                        
REMARK   1  TITL 2 CRYSTALLOGRAPHIC STUDY OF KUNITZ-TYPE SOYBEAN                
REMARK   1  TITL 3 TRYPSIN INHIBITOR                                            
REMARK   1  REF    THESIS, SEOUL NATIONAL                     1993              
REMARK   1  REF  2 UNIVERSITY                                                   
REMARK   1  PUBL   SEOUL : SEOUL NATIONAL UNIVERSITY (THESIS)                   
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 0.000                          
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 31038                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2898                                    
REMARK   3   NUCLEIC ACID ATOMS       : NULL                                    
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 0.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.32                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AVW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : SEP-94                             
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12C                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE AREA DETECTOR          
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   : 52687                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.0                               
REMARK 200  DATA REDUNDANCY                : 7.800                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1MCT FOR TRYPSIN AND PDB ENTRY 1TIE        
REMARK 200  FOR THE INHIBITOR                                                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
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                                                                      
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       29.45500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.73000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.16500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.73000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.45500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.16500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP B   625                                                      
REMARK 465     ASP B   626                                                      
REMARK 465     GLN B   639                                                      
REMARK 465     ALA B   640                                                      
REMARK 465     GLU B   641                                                      
REMARK 465     ASP B   642                                                      
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 A 117    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 125    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B 598    CG   OD1  OD2                                       
REMARK 470     GLU B 609    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B 611    CB   CG   CD   CE   NZ                              
REMARK 470     ASP B 612    CB   CG   OD1  OD2                                  
REMARK 470     SER B 624    CB   OG                                             
REMARK 470     GLU B 627    CB   CG   CD   OE1  OE2                             
REMARK 470     GLN B 638    CB   CG   CD   OE1  NE2                             
REMARK 470     ASP B 643    CB   CG   OD1  OD2                                  
REMARK 470     LYS B 644    CB   CG   CD   CE   NZ                              
REMARK 470     HIS B 654    CB   CG   ND1  CD2  CE1  NE2                        
REMARK 470     ASP B 655    CB   CG   OD1  OD2                                  
REMARK 470     LYS B 665    CB   CG   CD   CE   NZ                              
REMARK 470     ASN B 666    CB   CG   OD1  ND2                                  
REMARK 470     LYS B 667    CB   CG   CD   CE   NZ                              
REMARK 470     ASP B 677    CB   CG   OD1  OD2                                  
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    ARG B 563   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.1 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                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  71      -59.25   -129.87                                   
REMARK 500    SER A 214      -70.18   -124.65                                   
REMARK 500    ARG B 563       39.55    -89.30                                   
REMARK 500    GLU B 601       32.47    -82.84                                   
REMARK 500    ILE B 607     -162.13   -109.67                                   
REMARK 500    LYS B 667     -113.82    -96.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS B  667     PRO B  668                  -52.76                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A  66         0.13    SIDE_CHAIN                              
REMARK 500    TYR B 517         0.09    SIDE_CHAIN                              
REMARK 500    ARG B 530         0.07    SIDE_CHAIN                              
REMARK 500    ARG B 563         0.20    SIDE_CHAIN                              
REMARK 500    TYR B 631         0.07    SIDE_CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 700  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  70   OE1                                                    
REMARK 620 2 ASN A  72   O    88.0                                              
REMARK 620 3 VAL A  75   O   161.1  85.4                                        
REMARK 620 4 GLU A  77   OE1  96.9  85.8 100.2                                  
REMARK 620 5 GLU A  80   OE2  98.3 168.0  91.5  83.3                            
REMARK 620 6 HOH A 872   O    75.0 102.2  89.2 168.2  89.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AVE                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: CATALYTIC TRIAD.                                   
REMARK 800 SITE_IDENTIFIER: IRY                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: P1 SITE.                                           
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 700                  
DBREF  1AVW A   16   245  UNP    P00761   TRYP_PIG         9    231             
DBREF  1AVW B  501   677  UNP    P01070   ITRA_SOYBN      25    201             
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS ALA ALA ASN SER ILE PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY SER HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  HIS ASN ILE ASP VAL LEU GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  223  ASN ALA ALA LYS ILE ILE THR HIS PRO ASN PHE ASN GLY          
SEQRES   7 A  223  ASN THR LEU ASP ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 A  223  SER PRO ALA THR LEU ASN SER ARG VAL ALA THR VAL SER          
SEQRES   9 A  223  LEU PRO ARG SER CYS ALA ALA ALA GLY THR GLU CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY SER SER          
SEQRES  11 A  223  TYR PRO SER LEU LEU GLN CYS LEU LYS ALA PRO VAL LEU          
SEQRES  12 A  223  SER ASP SER SER CYS LYS SER SER TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR GLY ASN MET ILE CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS ASN GLY GLN LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL ASN TRP ILE GLN GLN THR ILE ALA          
SEQRES  18 A  223  ALA ASN                                                      
SEQRES   1 B  177  ASP PHE VAL LEU ASP ASN GLU GLY ASN PRO LEU GLU ASN          
SEQRES   2 B  177  GLY GLY THR TYR TYR ILE LEU SER ASP ILE THR ALA PHE          
SEQRES   3 B  177  GLY GLY ILE ARG ALA ALA PRO THR GLY ASN GLU ARG CYS          
SEQRES   4 B  177  PRO LEU THR VAL VAL GLN SER ARG ASN GLU LEU ASP LYS          
SEQRES   5 B  177  GLY ILE GLY THR ILE ILE SER SER PRO TYR ARG ILE ARG          
SEQRES   6 B  177  PHE ILE ALA GLU GLY HIS PRO LEU SER LEU LYS PHE ASP          
SEQRES   7 B  177  SER PHE ALA VAL ILE MET LEU CYS VAL GLY ILE PRO THR          
SEQRES   8 B  177  GLU TRP SER VAL VAL GLU ASP LEU PRO GLU GLY PRO ALA          
SEQRES   9 B  177  VAL LYS ILE GLY GLU ASN LYS ASP ALA MET ASP GLY TRP          
SEQRES  10 B  177  PHE ARG LEU GLU ARG VAL SER ASP ASP GLU PHE ASN ASN          
SEQRES  11 B  177  TYR LYS LEU VAL PHE CYS PRO GLN GLN ALA GLU ASP ASP          
SEQRES  12 B  177  LYS CYS GLY ASP ILE GLY ILE SER ILE ASP HIS ASP ASP          
SEQRES  13 B  177  GLY THR ARG ARG LEU VAL VAL SER LYS ASN LYS PRO LEU          
SEQRES  14 B  177  VAL VAL GLN PHE GLN LYS LEU ASP                              
HET     CA  A 700       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *142(H2 O)                                                    
HELIX    1   1 ALA A   56  CYS A   58  5                                   3    
HELIX    2   2 ASP A  165  SER A  171  1                                   7    
HELIX    3   3 VAL A  231  ASN A  233  5                                   3    
HELIX    4   4 VAL A  235  ALA A  243  1                                   9    
HELIX    5   5 MET B  584  CYS B  586  5                                   3    
SHEET    1   A 7 GLN A  81  ASN A  84  0                                        
SHEET    2   A 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
SHEET    3   A 7 GLN A  30  SER A  37 -1  N  ASN A  34   O  GLN A  64           
SHEET    4   A 7 SER A  39  ASN A  48 -1  N  GLY A  44   O  VAL A  31           
SHEET    5   A 7 TRP A  51  SER A  54 -1  N  VAL A  53   O  SER A  45           
SHEET    6   A 7 MET A 104  LEU A 108 -1  N  ILE A 106   O  VAL A  52           
SHEET    7   A 7 ALA A  85  THR A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    1   B 2 GLU A 135  GLY A 140  0                                        
SHEET    2   B 2 GLN A 156  PRO A 161 -1  N  ALA A 160   O  CYS A 136           
SHEET    1   C 4 MET A 180  VAL A 183  0                                        
SHEET    2   C 4 GLY A 226  LYS A 230 -1  N  TYR A 228   O  ILE A 181           
SHEET    3   C 4 GLN A 204  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    4   C 4 PRO A 198  CYS A 201 -1  N  CYS A 201   O  GLN A 204           
SHEET    1   D 4 VAL B 671  LYS B 675  0                                        
SHEET    2   D 4 GLY B 515  SER B 521 -1  N  LEU B 520   O  GLN B 672           
SHEET    3   D 4 THR B 556  SER B 559 -1  N  ILE B 558   O  GLY B 515           
SHEET    4   D 4 SER B 574  PHE B 577 -1  N  LYS B 576   O  ILE B 557           
SHEET    1   E 2 ILE B 529  ALA B 532  0                                        
SHEET    2   E 2 THR B 542  GLN B 545 -1  N  VAL B 544   O  ARG B 530           
SHEET    1   F 2 SER B 594  VAL B 596  0                                        
SHEET    2   F 2 ALA B 604  LYS B 606 -1  N  LYS B 606   O  SER B 594           
SHEET    1   G 3 GLY B 616  ARG B 622  0                                        
SHEET    2   G 3 TYR B 631  PRO B 637 -1  N  CYS B 636   O  TRP B 617           
SHEET    3   G 3 CYS B 645  ASP B 647 -1  N  GLY B 646   O  PHE B 635           
SHEET    1   H 2 ILE B 648  ILE B 652  0                                        
SHEET    2   H 2 ARG B 659  VAL B 663 -1  N  VAL B 662   O  GLY B 649           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.02  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.02  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.03  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.02  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.02  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.03  
SSBOND   7 CYS B  539    CYS B  586                          1555   1555  2.02  
SSBOND   8 CYS B  636    CYS B  645                          1555   1555  2.03  
LINK        CA    CA A 700                 OE1 GLU A  70     1555   1555  2.37  
LINK        CA    CA A 700                 O   ASN A  72     1555   1555  2.26  
LINK        CA    CA A 700                 O   VAL A  75     1555   1555  2.25  
LINK        CA    CA A 700                 OE1 GLU A  77     1555   1555  2.30  
LINK        CA    CA A 700                 OE2 GLU A  80     1555   1555  2.28  
LINK        CA    CA A 700                 O   HOH A 872     1555   1555  2.30  
SITE     1 AVE  3 HIS A  57  ASP A 102  SER A 195                               
SITE     1 IRY  1 ARG B 563                                                     
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  77                    
SITE     2 AC1  6 GLU A  80  HOH A 872                                          
CRYST1   58.910   62.330  151.460  90.00  90.00  90.00 P 21 21 21    4          
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      0.016975  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016044  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006602        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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