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Database: PDB
Entry: 1EZS
LinkDB: 1EZS
Original site: 1EZS 
HEADER    HYDROLASE/INHIBITOR                     11-MAY-00   1EZS              
TITLE     CRYSTAL STRUCTURE OF ECOTIN MUTANT M84R, W67A, G68A, Y69A,            
TITLE    2 D70A BOUND TO RAT ANIONIC TRYPSIN II                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ECOTIN;                                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: TRYPSIN II, ANIONIC;                                       
COMPND   8 CHAIN: C, D;                                                         
COMPND   9 EC: 3.4.21.4;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: 25A6;                                      
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PTACTACECOTIN;                            
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  11 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  12 ORGANISM_TAXID: 10116;                                               
SOURCE  13 TISSUE: PANCREAS;                                                    
SOURCE  14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  15 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PYTD102N TRYPSIN                          
KEYWDS    PROTEIN-PROTEIN INTERACTIONS, MACROMOLECULAR COMPLEX,                 
KEYWDS   2 PROTEASE INHIBITOR, HYDROLASE/INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.A.GILLMOR,T.TAKEUCHI,S.Q.YANG,C.S.CRAIK,R.J.FLETTERICK              
REVDAT   3   24-FEB-09 1EZS    1       VERSN                                    
REVDAT   2   01-APR-03 1EZS    1       JRNL                                     
REVDAT   1   23-JUN-00 1EZS    0                                                
JRNL        AUTH   S.A.GILLMOR,T.TAKEUCHI,S.Q.YANG,C.S.CRAIK,                   
JRNL        AUTH 2 R.J.FLETTERICK                                               
JRNL        TITL   COMPROMISE AND ACCOMMODATION IN ECOTIN, A DIMERIC            
JRNL        TITL 2 MACROMOLECULAR INHIBITOR OF SERINE PROTEASES.                
JRNL        REF    J.MOL.BIOL.                   V. 299   993 2000              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10843853                                                     
JRNL        DOI    10.1006/JMBI.2000.3812                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.851                                         
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.200                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 92.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 29880                          
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 SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1511                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4429                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2860                       
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 226                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.022                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5244                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 86                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.34                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.39                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.56                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.640 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.190 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.050 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.110 ; 2.500                
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  : PARAM.WAT                                      
REMARK   3  PARAMETER FILE  3  : PARAM19.ION                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : TOPH.WAT                                       
REMARK   3  TOPOLOGY FILE  3   : TOPH19.ION                                     
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: USED BULK SOLVENT CORRECTION, B-          
REMARK   3  FACTOR REFINEMENT, POSITIONAL REFINEMENT, AND SIMULATED             
REMARK   3  ANNEALING                                                           
REMARK   4                                                                      
REMARK   4 1EZS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011068.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-JAN-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
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          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29967                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY                : 2.100                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.19600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.91                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN: 15MG/ML COMPLEX IN 10MM         
REMARK 280  TRIS PH 8.0 WELL: 0.15M SODIUM CACODYLATE, 0.3M SODIUM              
REMARK 280  ACETATE, 14% PEG 4K, PH 6.5, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 291K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS THE TWO-ECOTIN, TWO-TRYPSIN       
REMARK 300 HETERO TETRAMER IN THE ASYMMETRIC UNIT                               
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7740 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -54.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     ALA A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     LYS A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     LEU A    64                                                      
REMARK 465     GLU A    65                                                      
REMARK 465     GLY A    66                                                      
REMARK 465     ALA A    67                                                      
REMARK 465     ALA A    68                                                      
REMARK 465     ALA A    69                                                      
REMARK 465     ALA B   201                                                      
REMARK 465     GLU B   202                                                      
REMARK 465     SER B   203                                                      
REMARK 465     VAL B   204                                                      
REMARK 465     GLN B   205                                                      
REMARK 465     PRO B   206                                                      
REMARK 465     LEU B   207                                                      
REMARK 465     GLU B   208                                                      
REMARK 465     LYS B   209                                                      
REMARK 465     ILE B   210                                                      
REMARK 465     ALA B   211                                                      
REMARK 465     LEU B   264                                                      
REMARK 465     GLU B   265                                                      
REMARK 465     GLY B   266                                                      
REMARK 465     ALA B   267                                                      
REMARK 465     ALA B   268                                                      
REMARK 465     ALA B   269                                                      
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     PRO A  12    CG   CD                                             
REMARK 470     LYS A  18    CG   CD   CE   NZ                                   
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     LYS A  62    CG   CD   CE   NZ                                   
REMARK 470     THR A  63    OG1  CG2                                            
REMARK 470     LYS A  91    CG   CD   CE   NZ                                   
REMARK 470     LYS A  92    CG   CD   CE   NZ                                   
REMARK 470     LYS A  95    CG   CD   CE   NZ                                   
REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
REMARK 470     LYS A 135    CG   CD   CE   NZ                                   
REMARK 470     ARG A 142    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO B 212    CG   CD                                             
REMARK 470     LYS B 218    CG   CD   CE   NZ                                   
REMARK 470     LYS B 258    CG   CD   CE   NZ                                   
REMARK 470     LYS B 262    CG   CD   CE   NZ                                   
REMARK 470     THR B 263    OG1  CG2                                            
REMARK 470     LYS B 291    CG   CD   CE   NZ                                   
REMARK 470     LYS B 292    CG   CD   CE   NZ                                   
REMARK 470     LYS B 295    CG   CD   CE   NZ                                   
REMARK 470     LYS B 331    CG   CD   CE   NZ                                   
REMARK 470     LYS B 335    CG   CD   CE   NZ                                   
REMARK 470     ARG B 342    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  17      132.36     78.51                                   
REMARK 500    GLU A  31      -70.44    -53.69                                   
REMARK 500    ASP A  49     -158.39    -98.26                                   
REMARK 500    TYR A  71      101.49     87.04                                   
REMARK 500    ARG A  84       48.26   -108.40                                   
REMARK 500    ASP A  89     -152.56   -120.52                                   
REMARK 500    GLU B 217      132.26     75.56                                   
REMARK 500    GLU B 231      -72.31    -59.15                                   
REMARK 500    ASP B 249     -153.64    -95.61                                   
REMARK 500    TYR B 271      102.25     83.21                                   
REMARK 500    ARG B 284       44.76   -107.25                                   
REMARK 500    ASP B 289     -155.37   -127.06                                   
REMARK 500    SER C 437       49.60   -142.33                                   
REMARK 500    ASP C 449       -7.56    -53.54                                   
REMARK 500    HIS C 471      -54.86   -138.60                                   
REMARK 500    ASP C 479       47.16    -95.65                                   
REMARK 500    ASN C 515     -154.38   -156.74                                   
REMARK 500    SER C 614      -57.60   -126.08                                   
REMARK 500    SER D 737       47.81   -141.76                                   
REMARK 500    HIS D 771      -55.64   -137.93                                   
REMARK 500    ASP D 779       45.24    -91.92                                   
REMARK 500    ASN D 815     -152.99   -153.97                                   
REMARK 500    SER D 914      -55.12   -129.70                                   
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 C 650  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 480   OE2                                                    
REMARK 620 2 GLU C 470   OE1  99.9                                              
REMARK 620 3 GLU C 477   OE1  79.1  82.3                                        
REMARK 620 4 GLU C 470   OE2  89.4  45.3 123.6                                  
REMARK 620 5 ASN C 472   O   165.2  84.0  87.3 103.2                            
REMARK 620 6 VAL C 475   O    91.2 168.1  95.4 140.2  84.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D 950  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN D 772   O                                                      
REMARK 620 2 VAL D 775   O    84.0                                              
REMARK 620 3 GLU D 777   OE1  85.7  88.2                                        
REMARK 620 4 GLU D 780   OE2 162.3  92.6  76.9                                  
REMARK 620 5 GLU D 770   OE2 102.9 146.3 124.8  89.5                            
REMARK 620 6 GLU D 770   OE1  85.9 165.4  80.6  93.9  46.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 950                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 650                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AZZ   RELATED DB: PDB                                   
REMARK 900 1AZZ CONTAINS ECOTIN BOUND TO COLLAGENASE                            
REMARK 900 RELATED ID: 1ECY   RELATED DB: PDB                                   
REMARK 900 1ECY CONTAINS ECOTIN ALONE                                           
REMARK 900 RELATED ID: 1ECZ   RELATED DB: PDB                                   
REMARK 900 1ECZ CONTAINS ECOTIN ALONE                                           
REMARK 900 RELATED ID: 1SLU   RELATED DB: PDB                                   
REMARK 900 1SLU CONTAINS MUTANT ECOTIN BOUND TO MUTANT TRYPSIN                  
REMARK 900 RELATED ID: 1SLV   RELATED DB: PDB                                   
REMARK 900 1SLV CONTAINS MUTANT ECOTIN BOUND TO MUTANT TRYPSIN                  
REMARK 900 RELATED ID: 1SLW   RELATED DB: PDB                                   
REMARK 900 1SLW CONTAINS MUTANT ECOTIN BOUND TO MUTANT TRYPSIN                  
REMARK 900 RELATED ID: 1SLX   RELATED DB: PDB                                   
REMARK 900 1SLX CONTAINS MUTANT ECOTIN BOUND TO MUTANT TRYPSIN                  
REMARK 900 RELATED ID: 1EZU   RELATED DB: PDB                                   
REMARK 900 1EZU CONTAINS MUTANT ECOTIN BOUND TO MUTANT TRYPSIN                  
DBREF  1EZS A    1   142  UNP    P23827   ECOT_ECOLI      21    162             
DBREF  1EZS B  201   342  UNP    P23827   ECOT_ECOLI      21    162             
DBREF  1EZS C  416   645  UNP    P00763   TRY2_RAT        24    246             
DBREF  1EZS D  716   945  UNP    P00763   TRY2_RAT        24    246             
SEQADV 1EZS ALA A   67  UNP  P23827    TRP    87 ENGINEERED                     
SEQADV 1EZS ALA A   68  UNP  P23827    GLY    88 ENGINEERED                     
SEQADV 1EZS ALA A   69  UNP  P23827    TYR    89 ENGINEERED                     
SEQADV 1EZS ALA A   70  UNP  P23827    ASP    90 ENGINEERED                     
SEQADV 1EZS ARG A   84  UNP  P23827    MET   104 ENGINEERED                     
SEQADV 1EZS ALA B  267  UNP  P23827    TRP    87 ENGINEERED                     
SEQADV 1EZS ALA B  268  UNP  P23827    GLY    88 ENGINEERED                     
SEQADV 1EZS ALA B  269  UNP  P23827    TYR    89 ENGINEERED                     
SEQADV 1EZS ALA B  270  UNP  P23827    ASP    90 ENGINEERED                     
SEQADV 1EZS ARG B  284  UNP  P23827    MET   104 ENGINEERED                     
SEQADV 1EZS ASP C  479  UNP  P00763    ASN    84 SEE REMARK 999                 
SEQADV 1EZS ASN C  502  UNP  P00763    ASP   107 ENGINEERED                     
SEQADV 1EZS ASP D  779  UNP  P00763    ASN    84 SEE REMARK 999                 
SEQADV 1EZS ASN D  802  UNP  P00763    ASP   107 ENGINEERED                     
SEQRES   1 A  142  ALA GLU SER VAL GLN PRO LEU GLU LYS ILE ALA PRO TYR          
SEQRES   2 A  142  PRO GLN ALA GLU LYS GLY MET LYS ARG GLN VAL ILE GLN          
SEQRES   3 A  142  LEU THR PRO GLN GLU ASP GLU SER THR LEU LYS VAL GLU          
SEQRES   4 A  142  LEU LEU ILE GLY GLN THR LEU GLU VAL ASP CYS ASN LEU          
SEQRES   5 A  142  HIS ARG LEU GLY GLY LYS LEU GLU ASN LYS THR LEU GLU          
SEQRES   6 A  142  GLY ALA ALA ALA ALA TYR TYR VAL PHE ASP LYS VAL SER          
SEQRES   7 A  142  SER PRO VAL SER THR ARG MET ALA CYS PRO ASP GLY LYS          
SEQRES   8 A  142  LYS GLU LYS LYS PHE VAL THR ALA TYR LEU GLY ASP ALA          
SEQRES   9 A  142  GLY MET LEU ARG TYR ASN SER LYS LEU PRO ILE VAL VAL          
SEQRES  10 A  142  TYR THR PRO ASP ASN VAL ASP VAL LYS TYR ARG VAL TRP          
SEQRES  11 A  142  LYS ALA GLU GLU LYS ILE ASP ASN ALA VAL VAL ARG              
SEQRES   1 B  142  ALA GLU SER VAL GLN PRO LEU GLU LYS ILE ALA PRO TYR          
SEQRES   2 B  142  PRO GLN ALA GLU LYS GLY MET LYS ARG GLN VAL ILE GLN          
SEQRES   3 B  142  LEU THR PRO GLN GLU ASP GLU SER THR LEU LYS VAL GLU          
SEQRES   4 B  142  LEU LEU ILE GLY GLN THR LEU GLU VAL ASP CYS ASN LEU          
SEQRES   5 B  142  HIS ARG LEU GLY GLY LYS LEU GLU ASN LYS THR LEU GLU          
SEQRES   6 B  142  GLY ALA ALA ALA ALA TYR TYR VAL PHE ASP LYS VAL SER          
SEQRES   7 B  142  SER PRO VAL SER THR ARG MET ALA CYS PRO ASP GLY LYS          
SEQRES   8 B  142  LYS GLU LYS LYS PHE VAL THR ALA TYR LEU GLY ASP ALA          
SEQRES   9 B  142  GLY MET LEU ARG TYR ASN SER LYS LEU PRO ILE VAL VAL          
SEQRES  10 B  142  TYR THR PRO ASP ASN VAL ASP VAL LYS TYR ARG VAL TRP          
SEQRES  11 B  142  LYS ALA GLU GLU LYS ILE ASP ASN ALA VAL VAL ARG              
SEQRES   1 C  223  ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO          
SEQRES   2 C  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 C  223  GLY SER LEU ILE ASN ASP GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 C  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 C  223  HIS ASN ILE ASN VAL LEU GLU GLY ASP GLU GLN PHE VAL          
SEQRES   6 C  223  ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG          
SEQRES   7 C  223  LYS THR LEU ASN ASN ASN ILE MET LEU ILE LYS LEU SER          
SEQRES   8 C  223  SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA          
SEQRES   9 C  223  LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU          
SEQRES  10 C  223  ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN          
SEQRES  11 C  223  GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU          
SEQRES  12 C  223  PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 C  223  THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 C  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 C  223  CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 C  223  GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS          
SEQRES  17 C  223  VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA          
SEQRES  18 C  223  ALA ASN                                                      
SEQRES   1 D  223  ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO          
SEQRES   2 D  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 D  223  GLY SER LEU ILE ASN ASP GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 D  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 D  223  HIS ASN ILE ASN VAL LEU GLU GLY ASP GLU GLN PHE VAL          
SEQRES   6 D  223  ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG          
SEQRES   7 D  223  LYS THR LEU ASN ASN ASN ILE MET LEU ILE LYS LEU SER          
SEQRES   8 D  223  SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR VAL ALA          
SEQRES   9 D  223  LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU          
SEQRES  10 D  223  ILE SER GLY TRP GLY ASN THR LEU SER SER GLY VAL ASN          
SEQRES  11 D  223  GLU PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU          
SEQRES  12 D  223  PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 D  223  THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 D  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 D  223  CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 D  223  GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS          
SEQRES  17 D  223  VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA          
SEQRES  18 D  223  ALA ASN                                                      
HET     CA  D 950       1                                                       
HET     CA  C 650       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   5   CA    2(CA 2+)                                                     
FORMUL   7  HOH   *86(H2 O)                                                     
HELIX    1   1 ASP A   32  SER A   34  5                                   3    
HELIX    2   2 LEU A  101  ALA A  104  5                                   4    
HELIX    3   3 ASP B  232  SER B  234  5                                   3    
HELIX    4   4 LEU B  301  ALA B  304  5                                   4    
HELIX    5   5 ALA C  455  TYR C  459  5                                   5    
HELIX    6   6 PRO C  564  TYR C  572  1                                   9    
HELIX    7   7 TYR C  634  ASN C  645  1                                  12    
HELIX    8   8 ALA D  755  TYR D  759  5                                   5    
HELIX    9   9 PRO D  864  TYR D  872  1                                   9    
HELIX   10  10 TYR D  934  ASN D  945  1                                  12    
SHEET    1   A 5 VAL B 340  VAL B 341  0                                        
SHEET    2   A 5 MET A  20  ILE A  25 -1  N  VAL A  24   O  VAL B 340           
SHEET    3   A 5 ILE A 115  PRO A 120 -1  N  ILE A 115   O  ILE A  25           
SHEET    4   A 5 TYR A  72  ASP A  75  1  O  TYR A  72   N  TYR A 118           
SHEET    5   A 5 LYS A  58  ASN A  61 -1  N  LYS A  58   O  ASP A  75           
SHEET    1   B14 GLU A  93  THR A  98  0                                        
SHEET    2   B14 LEU A  36  VAL A  48 -1  O  GLN A  44   N  VAL A  97           
SHEET    3   B14 MET A 106  ARG A 108 -1  N  LEU A 107   O  VAL A  38           
SHEET    4   B14 LEU A  36  VAL A  48 -1  O  VAL A  38   N  LEU A 107           
SHEET    5   B14 ASP A 124  ALA A 132 -1  N  ASP A 124   O  GLY A  43           
SHEET    6   B14 ASP B 337  ASN B 338 -1  N  ASP B 337   O  TYR A 127           
SHEET    7   B14 ASP A 124  ALA A 132 -1  O  TYR A 127   N  ASP B 337           
SHEET    8   B14 ASP B 324  ALA B 332 -1  O  LYS B 331   N  LYS A 131           
SHEET    9   B14 ASP A 137  ASN A 138 -1  N  ASP A 137   O  TYR B 327           
SHEET   10   B14 ASP B 324  ALA B 332 -1  O  TYR B 327   N  ASP A 137           
SHEET   11   B14 LEU B 236  VAL B 248 -1  O  LYS B 237   N  TRP B 330           
SHEET   12   B14 MET B 306  ARG B 308 -1  N  LEU B 307   O  VAL B 238           
SHEET   13   B14 LEU B 236  VAL B 248 -1  O  VAL B 238   N  LEU B 307           
SHEET   14   B14 GLU B 293  THR B 298 -1  O  GLU B 293   N  VAL B 248           
SHEET    1   C 5 VAL A 140  VAL A 141  0                                        
SHEET    2   C 5 MET B 220  ILE B 225 -1  O  VAL B 224   N  VAL A 140           
SHEET    3   C 5 ILE B 315  PRO B 320 -1  N  ILE B 315   O  ILE B 225           
SHEET    4   C 5 TYR B 272  ASP B 275  1  O  TYR B 272   N  TYR B 318           
SHEET    5   C 5 LYS B 258  ASN B 261 -1  O  LYS B 258   N  ASP B 275           
SHEET    1   D11 TYR C 420  THR C 421  0                                        
SHEET    2   D11 GLN C 556  PRO C 561 -1  N  CYS C 557   O  TYR C 420           
SHEET    3   D11 GLN C 535  GLY C 540 -1  N  CYS C 536   O  ALA C 560           
SHEET    4   D11 PRO C 598  CYS C 601 -1  O  PRO C 598   N  SER C 539           
SHEET    5   D11 GLU C 604  GLY C 616 -1  O  GLU C 604   N  CYS C 601           
SHEET    6   D11 VAL B 281  THR B 283 -1  N  SER B 282   O  GLY C 616           
SHEET    7   D11 HIS B 253  ARG B 254 -1  N  ARG B 254   O  VAL B 281           
SHEET    8   D11 VAL B 281  THR B 283 -1  O  VAL B 281   N  ARG B 254           
SHEET    9   D11 GLU C 604  GLY C 616 -1  O  GLY C 616   N  SER B 282           
SHEET   10   D11 GLY C 626  LYS C 630 -1  N  VAL C 627   O  TRP C 615           
SHEET   11   D11 MET C 580  VAL C 583 -1  O  VAL C 581   N  TYR C 628           
SHEET    1   E 7 GLN C 481  LYS C 490  0                                        
SHEET    2   E 7 GLN C 464  LEU C 468 -1  N  VAL C 465   O  VAL C 483           
SHEET    3   E 7 GLN C 430  ASN C 434 -1  O  SER C 432   N  ARG C 466           
SHEET    4   E 7 HIS C 440  ASN C 448 -1  N  PHE C 441   O  LEU C 433           
SHEET    5   E 7 TRP C 451  SER C 454 -1  O  TRP C 451   N  ILE C 447           
SHEET    6   E 7 MET C 504  LEU C 508 -1  N  MET C 504   O  SER C 454           
SHEET    7   E 7 GLN C 481  LYS C 490 -1  N  ALA C 486   O  LYS C 507           
SHEET    1   F11 TYR D 720  THR D 721  0                                        
SHEET    2   F11 GLN D 856  PRO D 861 -1  N  CYS D 857   O  TYR D 720           
SHEET    3   F11 GLN D 835  GLY D 840 -1  N  CYS D 836   O  ALA D 860           
SHEET    4   F11 PRO D 898  CYS D 901 -1  O  PRO D 898   N  SER D 839           
SHEET    5   F11 GLU D 904  GLY D 916 -1  O  GLU D 904   N  CYS D 901           
SHEET    6   F11 VAL A  81  THR A  83 -1  N  SER A  82   O  GLY D 916           
SHEET    7   F11 HIS A  53  ARG A  54 -1  O  ARG A  54   N  VAL A  81           
SHEET    8   F11 VAL A  81  THR A  83 -1  N  VAL A  81   O  ARG A  54           
SHEET    9   F11 GLU D 904  GLY D 916 -1  O  GLY D 916   N  SER A  82           
SHEET   10   F11 GLY D 926  LYS D 930 -1  N  VAL D 927   O  TRP D 915           
SHEET   11   F11 MET D 880  VAL D 883 -1  O  VAL D 881   N  TYR D 928           
SHEET    1   G 7 GLN D 781  LYS D 790  0                                        
SHEET    2   G 7 GLN D 764  LEU D 768 -1  N  VAL D 765   O  VAL D 783           
SHEET    3   G 7 GLN D 730  ASN D 734 -1  O  SER D 732   N  ARG D 766           
SHEET    4   G 7 HIS D 740  ASN D 748 -1  N  PHE D 741   O  LEU D 733           
SHEET    5   G 7 TRP D 751  SER D 754 -1  O  TRP D 751   N  ILE D 747           
SHEET    6   G 7 MET D 804  LEU D 808 -1  N  MET D 804   O  SER D 754           
SHEET    7   G 7 GLN D 781  LYS D 790 -1  N  ALA D 786   O  LYS D 807           
SSBOND   1 CYS A   50    CYS A   87                          1555   1555  2.03  
SSBOND   2 CYS B  250    CYS B  287                          1555   1555  2.03  
SSBOND   3 CYS C  422    CYS C  557                          1555   1555  2.02  
SSBOND   4 CYS C  442    CYS C  458                          1555   1555  2.02  
SSBOND   5 CYS C  528    CYS C  632                          1555   1555  2.03  
SSBOND   6 CYS C  536    CYS C  601                          1555   1555  2.02  
SSBOND   7 CYS C  568    CYS C  582                          1555   1555  2.03  
SSBOND   8 CYS C  591    CYS C  620                          1555   1555  2.02  
SSBOND   9 CYS D  722    CYS D  857                          1555   1555  2.02  
SSBOND  10 CYS D  742    CYS D  758                          1555   1555  2.01  
SSBOND  11 CYS D  828    CYS D  932                          1555   1555  2.02  
SSBOND  12 CYS D  836    CYS D  901                          1555   1555  2.02  
SSBOND  13 CYS D  868    CYS D  882                          1555   1555  2.03  
SSBOND  14 CYS D  891    CYS D  920                          1555   1555  2.02  
LINK        CA    CA C 650                 OE2 GLU C 480     1555   1555  2.42  
LINK        CA    CA C 650                 OE1 GLU C 470     1555   1555  2.31  
LINK        CA    CA C 650                 OE1 GLU C 477     1555   1555  2.49  
LINK        CA    CA C 650                 OE2 GLU C 470     1555   1555  3.11  
LINK        CA    CA C 650                 O   ASN C 472     1555   1555  2.48  
LINK        CA    CA C 650                 O   VAL C 475     1555   1555  2.56  
LINK        CA    CA D 950                 O   ASN D 772     1555   1555  2.48  
LINK        CA    CA D 950                 O   VAL D 775     1555   1555  2.63  
LINK        CA    CA D 950                 OE1 GLU D 777     1555   1555  2.52  
LINK        CA    CA D 950                 OE2 GLU D 780     1555   1555  2.42  
LINK        CA    CA D 950                 OE2 GLU D 770     1555   1555  2.96  
LINK        CA    CA D 950                 OE1 GLU D 770     1555   1555  2.43  
SITE     1 AC1  5 GLU D 770  ASN D 772  VAL D 775  GLU D 777                    
SITE     2 AC1  5 GLU D 780                                                     
SITE     1 AC2  5 GLU C 470  ASN C 472  VAL C 475  GLU C 477                    
SITE     2 AC2  5 GLU C 480                                                     
CRYST1   45.828   59.682   71.044 103.57  93.27  94.62 P 1           2          
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      0.021821  0.001764  0.001723        0.00000                         
SCALE2      0.000000  0.016810  0.004165        0.00000                         
SCALE3      0.000000  0.000000  0.014525        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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