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Database: PDB
Entry: 4AN7
LinkDB: 4AN7
Original site: 4AN7 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           15-MAR-12   4AN7              
TITLE     KUNITZ TYPE TRYPSIN INHIBITOR COMPLEX WITH PORCINE TRYPSIN            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRYPSIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.21.4;                                                        
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TRYPSIN INHIBITOR;                                         
COMPND   7 CHAIN: B                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SUS SCROFA;                                     
SOURCE   3 ORGANISM_COMMON: PIG;                                                
SOURCE   4 ORGANISM_TAXID: 9823;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: TAMARINDUS INDICA;                              
SOURCE   7 ORGANISM_COMMON: TAMARIND;                                           
SOURCE   8 ORGANISM_TAXID: 58860                                                
KEYWDS    HYDROLASE-HYDROLASE INHIBITOR COMPLEX, KUNITZ, PROTEASE INHIBITOR     
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.N.PATIL,A.CHAUDHARY,P.KUMAR                                         
REVDAT   3   05-JUL-17 4AN7    1       REMARK                                   
REVDAT   2   19-DEC-12 4AN7    1       JRNL                                     
REVDAT   1   07-NOV-12 4AN7    0                                                
JRNL        AUTH   D.N.PATIL,A.CHAUDHARY,A.K.SHARMA,S.TOMAR,P.KUMAR             
JRNL        TITL   STRUCTURAL BASIS FOR DUAL INHIBITORY ROLE OF TAMARIND KUNITZ 
JRNL        TITL 2 INHIBITOR (TKI) AGAINST FACTOR XA AND TRYPSIN.               
JRNL        REF    FEBS J.                       V. 279  4547 2012              
JRNL        REFN                   ISSN 1742-464X                               
JRNL        PMID   23094997                                                     
JRNL        DOI    10.1111/FEBS.12042                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.23 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.23                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 16883                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.246                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 911                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.23                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.29                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 759                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 58.87                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2720                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 51                           
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2864                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 155                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.16000                                             
REMARK   3    B22 (A**2) : 1.88000                                              
REMARK   3    B33 (A**2) : 0.28000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.367         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.241         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.182         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 14.065        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.948                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2920 ; 0.009 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2792 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3949 ; 1.361 ; 1.960       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6415 ; 0.741 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   365 ; 6.918 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   117 ;42.226 ;24.872       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   483 ;14.880 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;18.945 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   445 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3271 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   637 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    16        A   245                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.2090 -27.4860 -33.1980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0687 T22:   0.0806                                     
REMARK   3      T33:   0.0136 T12:  -0.0085                                     
REMARK   3      T13:   0.0040 T23:  -0.0186                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6206 L22:   1.1779                                     
REMARK   3      L33:   0.9247 L12:  -0.0234                                     
REMARK   3      L13:   0.1488 L23:  -0.0477                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0248 S12:   0.1072 S13:   0.0563                       
REMARK   3      S21:  -0.1269 S22:   0.0050 S23:   0.0156                       
REMARK   3      S31:  -0.0187 S32:   0.0350 S33:   0.0198                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   173                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.9350  -8.6730 -11.4460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2332 T22:   0.1027                                     
REMARK   3      T33:   0.1439 T12:  -0.0273                                     
REMARK   3      T13:   0.0034 T23:  -0.0433                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0032 L22:   3.0953                                     
REMARK   3      L33:   5.0905 L12:  -0.4277                                     
REMARK   3      L13:  -0.9380 L23:   2.4150                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1490 S12:  -0.1428 S13:   0.2884                       
REMARK   3      S21:   0.0187 S22:   0.0030 S23:  -0.1055                       
REMARK   3      S31:  -0.5626 S32:   0.0566 S33:  -0.1520                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4AN7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290051713.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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          : BRUKER AXS MICROSTAR-H             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : DENZO                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17821                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.220                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : 3.300                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.26                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 40.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1AVW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM PHOSPHATE, 20% PEG3350    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,-Y,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,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  1.000000  0.000000  0.000000       30.54200            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.80600            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       30.54200            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       45.80600            
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: 1920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.1 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     PHE A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     THR A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     ASP A    13                                                      
REMARK 465     ASP A    14                                                      
REMARK 465     LYS A    15                                                      
REMARK 465     ASP B     1                                                      
REMARK 465     GLN B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     LYS B    28                                                      
REMARK 465     PHE B    96                                                      
REMARK 465     ASP B    97                                                      
REMARK 465     GLU B    98                                                      
REMARK 465     GLN B    99                                                      
REMARK 465     SER B   100                                                      
REMARK 465     SER B   101                                                      
REMARK 465     GLU B   102                                                      
REMARK 465     LYS B   103                                                      
REMARK 465     GLY B   104                                                      
REMARK 465     LYS B   136                                                      
REMARK 465     SER B   137                                                      
REMARK 465     GLU B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     GLY B   140                                                      
REMARK 465     GLU B   141                                                      
REMARK 465     GLU B   176                                                      
REMARK 465     GLU B   177                                                      
REMARK 465     SER B   178                                                      
REMARK 465     SER B   179                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     GLU B   181                                                      
REMARK 465     TRP B   182                                                      
REMARK 465     SER B   183                                                      
REMARK 465     ILE B   184                                                      
REMARK 465     VAL B   185                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CD   GLU A   135     OE2  GLU A   135     2554     2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASN A  34   C     SER A  37   N       0.265                       
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    ILE A  27       74.59   -107.35                                   
REMARK 500    HIS A  71      -67.87   -128.80                                   
REMARK 500    ALA A  86      -62.88   -100.94                                   
REMARK 500    SER A 214      -67.39   -131.29                                   
REMARK 500    ARG B  66       39.38    -94.13                                   
REMARK 500    ALA B  91       59.79    -92.50                                   
REMARK 500    ASP B 113      134.22    -27.32                                   
REMARK 500    SER B 115       91.48      8.18                                   
REMARK 500    GLU B 126     -112.21     46.82                                   
REMARK 500    ASP B 128     -137.43   -120.08                                   
REMARK 500    ASN B 153     -147.10   -137.49                                   
REMARK 500    LYS B 162       73.28   -165.11                                   
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 A1246  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A2046   O                                                      
REMARK 620 2 GLU A  70   OE1  84.2                                              
REMARK 620 3 ASN A  72   O    95.2  93.1                                        
REMARK 620 4 VAL A  75   O   113.9 160.9  79.8                                  
REMARK 620 5 GLU A  80   OE2  76.9 103.7 160.4  87.1                            
REMARK 620 6 HOH A2047   O   160.4  78.3  94.6  84.6  98.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 DETERMINATION METHOD: DSSP                                           
REMARK 700 THE SHEETS PRESENTED AS "AB" 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 A 1246                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AKS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE FIRST ACTIVE AUTOLYSATE FORM OF THE         
REMARK 900 PORCINE ALPHA TRYPSIN                                                
REMARK 900 RELATED ID: 1AN1   RELATED DB: PDB                                   
REMARK 900 LEECH-DERIVED TRYPTASE INHIBITOR/TRYPSIN COMPLEX                     
REMARK 900 RELATED ID: 1AVW   RELATED DB: PDB                                   
REMARK 900 COMPLEX PORCINE PANCREATIC TRYPSIN/SOYBEAN TRYPSIN INHIBITOR,        
REMARK 900 ORTHORHOMBIC CRYSTAL FORM                                            
REMARK 900 RELATED ID: 1AVX   RELATED DB: PDB                                   
REMARK 900 COMPLEX PORCINE PANCREATIC TRYPSIN/SOYBEAN TRYPSIN INHIBITOR,        
REMARK 900 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 INHIBITOR OF              
REMARK 900 CUCURBITACEAE FAMILY (THEORETICAL MODEL) BOUND TO TRYPSIN            
REMARK 900 RELATED ID: 1DF2   RELATED DB: PDB                                   
REMARK 900 KNOWLEDGE BASED MODEL OF A SERINE PROTEASE INHIBITOR OF              
REMARK 900 CUCURBITACEAE FAMILY (THEORETICAL MODEL) BOUND TO TRYPSIN            
REMARK 900 RELATED ID: 1EJA   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF PORCINE TRYPSIN COMPLEXED WITH BDELLASTASIN , AN        
REMARK 900 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 INHIBITOR                 
REMARK 900 OFCUCURBITACEAE FAMILY (THEORETICAL MODEL) BOUND TO TRYPSIN.         
REMARK 900 RELATED ID: 1FMG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.04% POLYDOCANOL     
REMARK 900 RELATED ID: 1FN6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH 0.1% POLYDOCANOL      
REMARK 900 RELATED ID: 1FNI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN 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: 1H9I   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF EETI-II MUTANT WITH PORCINE TRYPSIN                       
REMARK 900 RELATED ID: 1LDT   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF LEECH-DERIVED TRYPTASE INHIBITOR WITH PORCINE TRYPSIN     
REMARK 900 RELATED ID: 1LT2   RELATED DB: PDB                                   
REMARK 900 PREDICTION OF TERTIARY STRUCTURE OF LEUCAENA LEUCOCEPHALATRYPSIN     
REMARK 900 INHIBITOR/TRYPSIN COMPLEX.                                           
REMARK 900 RELATED ID: 1MCT   RELATED DB: PDB                                   
REMARK 900 TRYPSIN COMPLEXED WITH INHIBITOR FROM BITTER GOURD                   
REMARK 900 RELATED ID: 1QQU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PORCINE BETA TRYPSIN WITH BOUND ACETATE ION     
REMARK 900 RELATED ID: 1S5S   RELATED DB: PDB                                   
REMARK 900 PORCINE TRYPSIN COMPLEXED WITH GUANIDINE-3- PROPANOLINHIBITOR        
REMARK 900 RELATED ID: 1S6F   RELATED DB: PDB                                   
REMARK 900 PORCINE TRYPSIN COVALENT COMPLEX WITH BORATE AND GUANIDINE-3         
REMARK 900 INHIBITOR                                                            
REMARK 900 RELATED ID: 1S6H   RELATED DB: PDB                                   
REMARK 900 PORCINE TRYPSIN COMPLEXED WITH GUANIDINE-3- 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 ETHYLENE GLYCOL            
REMARK 900 RELATED ID: 1S83   RELATED DB: PDB                                   
REMARK 900 PORCINE TRYPSIN COMPLEXED WITH 4-AMINO PROPANOL                      
REMARK 900 RELATED ID: 1S84   RELATED DB: PDB                                   
REMARK 900 PORCINE TRYPSIN COVALENT COMPLEX WITH 4-AMINO BUTANOL, BORATE AND    
REMARK 900 ETHYLENE GLYCOL                                                      
REMARK 900 RELATED ID: 1S85   RELATED DB: PDB                                   
REMARK 900 PORCINE TRYPSIN COMPLEXED WITH P-HYDROXYMETHYL BENZAMIDINEAND BORATE 
REMARK 900 RELATED ID: 1TFX   RELATED DB: PDB                                   
REMARK 900 COMPLEX OF THE SECOND KUNITZ DOMAIN OF TISSUE FACTOR PATHWAY         
REMARK 900 INHIBITOR WITH PORCINE TRYPSIN                                       
REMARK 900 RELATED ID: 1TX6   RELATED DB: PDB                                   
REMARK 900 TRYPSIN:BBI COMPLEX                                                  
REMARK 900 RELATED ID: 1UHB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PORCINE ALPHA TRYPSIN BOUND WITH                
REMARK 900 AUTOCATALYTICALY PRODUCED NATIVE PEPTIDE AT 2.15 A RESOLUTION        
REMARK 900 RELATED ID: 1V6D   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF THE TRYPSIN COMPLEX WITH                    
REMARK 900 SYNTHETICHETEROCHIRAL PEPTIDE                                        
REMARK 900 RELATED ID: 1YF4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TRYPSIN-VASOPRESSIN COMPLEX                     
REMARK 900 RELATED ID: 2A31   RELATED DB: PDB                                   
REMARK 900 TRYPSIN IN COMPLEX WITH BORATE                                       
REMARK 900 RELATED ID: 2A32   RELATED DB: PDB                                   
REMARK 900 TRYPSIN IN COMPLEX WITH BENZENE BORONIC ACID                         
REMARK 900 RELATED ID: 4AN6   RELATED DB: PDB                                   
REMARK 900 KUNTIZ TYPE TRYPSIN INHIBITOR WITH FACTOR XA INHIBITORY ACTIVITY     
DBREF  4AN7 A    8   245  UNP    P00761   TRYP_PIG         1    231             
DBREF  4AN7 B    1   185  UNP    F4ZZG4   F4ZZG4_TAMIN     1    185             
SEQADV 4AN7 ILE B   53  UNP  F4ZZG4    LEU    53 CONFLICT                       
SEQADV 4AN7 ASN B  153  UNP  F4ZZG4    ASP   153 CONFLICT                       
SEQRES   1 A  231  PHE PRO THR ASP ASP ASP ASP LYS ILE VAL GLY GLY TYR          
SEQRES   2 A  231  THR CYS ALA ALA ASN SER ILE PRO TYR GLN VAL SER LEU          
SEQRES   3 A  231  ASN SER GLY SER HIS PHE CYS GLY GLY SER LEU ILE ASN          
SEQRES   4 A  231  SER GLN TRP VAL VAL SER ALA ALA HIS CYS TYR LYS SER          
SEQRES   5 A  231  ARG ILE GLN VAL ARG LEU GLY GLU HIS ASN ILE ASP VAL          
SEQRES   6 A  231  LEU GLU GLY ASN GLU GLN PHE ILE ASN ALA ALA LYS ILE          
SEQRES   7 A  231  ILE THR HIS PRO ASN PHE ASN GLY ASN THR LEU ASP ASN          
SEQRES   8 A  231  ASP ILE MET LEU ILE LYS LEU SER SER PRO ALA THR LEU          
SEQRES   9 A  231  ASN SER ARG VAL ALA THR VAL SER LEU PRO ARG SER CYS          
SEQRES  10 A  231  ALA ALA ALA GLY THR GLU CYS LEU ILE SER GLY TRP GLY          
SEQRES  11 A  231  ASN THR LYS SER SER GLY SER SER TYR PRO SER LEU LEU          
SEQRES  12 A  231  GLN CYS LEU LYS ALA PRO VAL LEU SER ASP SER SER CYS          
SEQRES  13 A  231  LYS SER SER TYR PRO GLY GLN ILE THR GLY ASN MET ILE          
SEQRES  14 A  231  CYS VAL GLY PHE LEU GLU GLY GLY LYS ASP SER CYS GLN          
SEQRES  15 A  231  GLY ASP SER GLY GLY PRO VAL VAL CYS ASN GLY GLN LEU          
SEQRES  16 A  231  GLN GLY ILE VAL SER TRP GLY TYR GLY CYS ALA GLN LYS          
SEQRES  17 A  231  ASN LYS PRO GLY VAL TYR THR LYS VAL CYS ASN TYR VAL          
SEQRES  18 A  231  ASN TRP ILE GLN GLN THR ILE ALA ALA ASN                      
SEQRES   1 B  185  ASP TYR THR VAL HIS ASP THR ASP GLY LYS PRO VAL LEU          
SEQRES   2 B  185  ASN ASN ALA GLY GLN TYR TYR ILE LEU PRO ALA LYS GLN          
SEQRES   3 B  185  GLY LYS GLY GLY GLY LEU GLY LEU SER ASN ASP ASP ASP          
SEQRES   4 B  185  GLY ASN CYS PRO LEU THR VAL SER GLN THR PRO ILE ASP          
SEQRES   5 B  185  ILE PRO ILE GLY LEU PRO VAL ARG PHE SER SER ARG ALA          
SEQRES   6 B  185  ARG ILE SER HIS ILE THR THR ALA LEU SER LEU ASN ILE          
SEQRES   7 B  185  GLU PHE THR ILE ALA PRO ALA CYS ALA PRO LYS PRO ALA          
SEQRES   8 B  185  ARG TRP ARG ILE PHE ASP GLU GLN SER SER GLU LYS GLY          
SEQRES   9 B  185  TYR THR PRO VAL LYS ILE SER ASP ASP PHE SER SER ALA          
SEQRES  10 B  185  ALA PRO PHE GLN ILE LYS LYS PHE GLU GLU ASP TYR LYS          
SEQRES  11 B  185  LEU VAL TYR CYS SER LYS SER GLU SER GLY GLU ARG LYS          
SEQRES  12 B  185  CYS VAL ASP LEU GLY ILE LYS ILE ASP ASN GLU LYS ASN          
SEQRES  13 B  185  ARG ARG LEU VAL LEU LYS GLU GLY ASP PRO PHE LYS VAL          
SEQRES  14 B  185  LYS PHE LYS LYS VAL ASP GLU GLU SER SER GLU GLU TRP          
SEQRES  15 B  185  SER ILE VAL                                                  
HET     CA  A1246       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *155(H2 O)                                                    
HELIX    1   1 ALA A   55  TYR A   59  5                                   5    
HELIX    2   2 SER A  164  TYR A  172  1                                   9    
HELIX    3   3 TYR A  234  ASN A  245  1                                  12    
SHEET    1  AA 7 TYR A  20  THR A  21  0                                        
SHEET    2  AA 7 GLN A 156  PRO A 161 -1  O  CYS A 157   N  TYR A  20           
SHEET    3  AA 7 GLU A 135  GLY A 140 -1  O  CYS A 136   N  ALA A 160           
SHEET    4  AA 7 PRO A 198  CYS A 201 -1  O  PRO A 198   N  SER A 139           
SHEET    5  AA 7 GLN A 204  TRP A 215 -1  O  GLN A 204   N  CYS A 201           
SHEET    6  AA 7 GLY A 226  LYS A 230 -1  O  VAL A 227   N  TRP A 215           
SHEET    7  AA 7 MET A 180  VAL A 183 -1  O  ILE A 181   N  TYR A 228           
SHEET    1  AB 7 GLN A  30  ASN A  34  0                                        
SHEET    2  AB 7 HIS A  40  ASN A  48 -1  N  PHE A  41   O  LEU A  33           
SHEET    3  AB 7 TRP A  51  SER A  54 -1  O  TRP A  51   N  ILE A  47           
SHEET    4  AB 7 MET A 104  LEU A 108 -1  O  MET A 104   N  SER A  54           
SHEET    5  AB 7 GLN A  81  THR A  90 -1  N  ALA A  86   O  LYS A 107           
SHEET    6  AB 7 GLN A  64  LEU A  67 -1  O  VAL A  65   N  ILE A  83           
SHEET    7  AB 7 GLN A  30  ASN A  34 -1  O  SER A  32   N  ARG A  66           
SHEET    1  BA 2 TYR B  19  PRO B  23  0                                        
SHEET    2  BA 2 VAL B 169  LYS B 173 -1  O  LYS B 170   N  LEU B  22           
SHEET    1  BB 2 LEU B  32  SER B  35  0                                        
SHEET    2  BB 2 THR B  45  GLN B  48 -1  O  THR B  45   N  SER B  35           
SHEET    1  BC 4 VAL B  59  SER B  62  0                                        
SHEET    2  BC 4 ASN B  77  PHE B  80 -1  O  ASN B  77   N  SER B  62           
SHEET    3  BC 4 ALA B  91  ARG B  94 -1  O  ALA B  91   N  PHE B  80           
SHEET    4  BC 4 LYS B 109  SER B 111 -1  O  LYS B 109   N  ARG B  94           
SHEET    1  BD 4 PHE B 120  PHE B 125  0                                        
SHEET    2  BD 4 ASP B 128  CYS B 134 -1  O  ASP B 128   N  PHE B 125           
SHEET    3  BD 4 CYS B 144  ILE B 149 -1  O  VAL B 145   N  TYR B 133           
SHEET    4  BD 4 LEU B 159  LEU B 161 -1  O  VAL B 160   N  GLY B 148           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.05  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.04  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.03  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.04  
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   42    CYS B   86                          1555   1555  2.00  
SSBOND   8 CYS B  134    CYS B  144                          1555   1555  2.02  
LINK        CA    CA A1246                 O   HOH A2046     1555   1555  2.55  
LINK        CA    CA A1246                 OE1 GLU A  70     1555   1555  2.26  
LINK        CA    CA A1246                 O   ASN A  72     1555   1555  2.28  
LINK        CA    CA A1246                 O   VAL A  75     1555   1555  2.29  
LINK        CA    CA A1246                 OE2 GLU A  80     1555   1555  2.45  
LINK        CA    CA A1246                 O   HOH A2047     1555   1555  2.27  
CISPEP   1 LYS B   89    PRO B   90          0        -3.98                     
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  80                    
SITE     2 AC1  6 HOH A2046  HOH A2047                                          
CRYST1   61.084   67.120   91.612  90.00  90.00  90.00 P 21 2 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      0.016371  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014899  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010916        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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