GenomeNet

Database: PDB
Entry: 1SLW
LinkDB: 1SLW
Original site: 1SLW 
HEADER    COMPLEX (SERINE PROTEASE/INHIBITOR)     07-FEB-96   1SLW              
TITLE     RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN; NICKEL-    
TITLE    2 BOUND                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ECOTIN;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: TRYPSIN INHIBITOR;                                          
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES;                                                       
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: ANIONIC TRYPSIN;                                           
COMPND   9 CHAIN: B;                                                            
COMPND  10 EC: 3.4.21.4;                                                        
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: RAT ANIONIC TRYPSIN;                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PTACTAC;                                  
SOURCE   8 EXPRESSION_SYSTEM_GENE: ECOTIN;                                      
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE  11 ORGANISM_COMMON: NORWAY RAT;                                         
SOURCE  12 ORGANISM_TAXID: 10116;                                               
SOURCE  13 GENE: RAT ANIONIC TRYPSIN;                                           
SOURCE  14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE;                         
SOURCE  15 EXPRESSION_SYSTEM_COMMON: BAKER'S YEAST;                             
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 4932;                                       
SOURCE  17 EXPRESSION_SYSTEM_PLASMID: PST;                                      
SOURCE  18 EXPRESSION_SYSTEM_GENE: RAT ANIONIC TRYPSIN                          
KEYWDS    SERINE PROTEASE, INHIBITOR, COMPLEX, METAL BINDING SITES, PROTEIN     
KEYWDS   2 ENGINEERING, PROTEASE-SUBSTRATE INTERACTIONS, METALLOPROTEINS,       
KEYWDS   3 COMPLEX (SERINE PROTEASE-INHIBITOR) COMPLEX                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.S.BRINEN,R.J.FLETTERICK                                             
REVDAT   3   13-JUL-11 1SLW    1       VERSN                                    
REVDAT   2   24-FEB-09 1SLW    1       VERSN                                    
REVDAT   1   11-JUL-96 1SLW    0                                                
JRNL        AUTH   L.S.BRINEN,W.S.WILLETT,C.S.CRAIK,R.J.FLETTERICK              
JRNL        TITL   X-RAY STRUCTURES OF A DESIGNED BINDING SITE IN TRYPSIN SHOW  
JRNL        TITL 2 METAL-DEPENDENT GEOMETRY.                                    
JRNL        REF    BIOCHEMISTRY                  V.  35  5999 1996              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   8634241                                                      
JRNL        DOI    10.1021/BI9530200                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.E.MCGRATH,T.ERPEL,C.BYSTROFF,R.J.FLETTERICK                
REMARK   1  TITL   MACROMOLECULAR CHELATION AS AN IMPROVED MECHANISM OF         
REMARK   1  TITL 2 PROTEASE INHIBITION: STRUCTURE OF THE ECOTIN-TRYPSIN COMPLEX 
REMARK   1  REF    EMBO J.                       V.  13  1502 1994              
REMARK   1  REFN                   ISSN 0261-4189                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 1.500                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 90.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 7886                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2616                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 52                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.09                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.14                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARAM19X.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SLW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-95                          
REMARK 200  TEMPERATURE           (KELVIN) : 198                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
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                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17281                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.05400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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       43.19000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.11500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       43.19000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       28.11500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 9290 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       -7.96445            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      162.26466            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 SITE DIRECTED MUTAGENESIS WAS PERFORMED IN ORDER TO                  
REMARK 400 DESIGN A METAL BINDING SITE AT THE INTERFACE OF TRYPSIN              
REMARK 400 N143H,E151H AND ECOTIN A86H.  METAL BINDING TAKES PLACE              
REMARK 400 AT THE SITE OF THESE MUTATIONS.                                      
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     GLY A    90                                                      
REMARK 465     LYS A    91                                                      
REMARK 465     LEU B   114                                                      
REMARK 465     ASN B   115                                                      
REMARK 465     ALA B   116                                                      
REMARK 465     ARG B   117                                                      
REMARK 465     SER B   146                                                      
REMARK 465     SER B   147                                                      
REMARK 465     GLY B   148                                                      
REMARK 465     VAL B   149                                                      
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     GLN A  15    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  18    CG   CD   CE   NZ                                   
REMARK 470     GLU A  47    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  58    CG   CD   CE   NZ                                   
REMARK 470     ASP A  89    CG   OD1  OD2                                       
REMARK 470     LYS A 135    CG   CD   CE   NZ                                   
REMARK 470     ARG A 142    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN B  25    CG   OD1                                            
REMARK 470     ARG B  62    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 113    CG   CD   CE   NZ                                   
REMARK 470     ASN B 150    CG   OD1                                            
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  33       -3.06    -59.77                                   
REMARK 500    MET A  84       43.27   -103.48                                   
REMARK 500    VAL B  27       70.94   -113.59                                   
REMARK 500    SER B  37     -117.62   -103.75                                   
REMARK 500    ASP B  49       13.71    -63.93                                   
REMARK 500    GLN B  50        2.89   -157.78                                   
REMARK 500    GLU B  70      150.82    -49.61                                   
REMARK 500    HIS B  71      -55.41   -150.70                                   
REMARK 500    GLU B  80      -85.25    -98.64                                   
REMARK 500    GLN B  81       71.81     65.90                                   
REMARK 500    PRO B  92        4.08    -65.32                                   
REMARK 500    PRO B 111      173.67    -58.45                                   
REMARK 500    ALA B 119      129.40   -170.51                                   
REMARK 500    SER B 127      150.35    172.65                                   
REMARK 500    TRP B 141       40.83   -100.44                                   
REMARK 500    SER B 214      -77.80   -126.67                                   
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 B 246  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  72   O                                                      
REMARK 620 2 VAL B  75   O    98.4                                              
REMARK 620 3 ACT B 247   C   153.8 107.0                                        
REMARK 620 4 ACT B 247   O   127.8 105.4  38.6                                  
REMARK 620 5 ACT B 247   OXT 145.8  98.8  36.3  74.8                            
REMARK 620 6 GLU B  77   OE2  82.5 105.7  96.6 131.6  64.5                      
REMARK 620 7 GLU B  70   OE1  76.3 142.0  79.6  56.4 106.3 110.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI B 248  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  86   NE2                                                    
REMARK 620 2 HIS B 151   NE2  87.2                                              
REMARK 620 3 HIS B 143   NE2  77.4  88.3                                        
REMARK 620 4 HOH B 253   O    98.1  92.8 175.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: NI1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NICKEL BINDING SITE.                               
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 246                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 247                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI B 248                  
DBREF  1SLW A    1   142  UNP    P23827   ECOT_ECOLI      21    162             
DBREF  1SLW B   16   245  UNP    P00763   TRY2_RAT        24    246             
SEQADV 1SLW HIS A   86  UNP  P23827    ALA   106 ENGINEERED                     
SEQADV 1SLW ILE B  121  UNP  P00763    VAL   126 ENGINEERED                     
SEQADV 1SLW HIS B  143  UNP  P00763    ASN   146 ENGINEERED                     
SEQADV 1SLW HIS B  151  UNP  P00763    GLU   154 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 TRP GLY TYR ASP TYR TYR VAL PHE ASP LYS VAL SER          
SEQRES   7 A  142  SER PRO VAL SER THR MET MET HIS 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  223  ILE VAL GLY GLY TYR THR CYS GLN GLU ASN SER VAL PRO          
SEQRES   2 B  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 B  223  GLY SER LEU ILE ASN ASP GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 B  223  HIS CYS TYR LYS SER ARG ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 B  223  HIS ASN ILE ASN VAL LEU GLU GLY ASN GLU GLN PHE VAL          
SEQRES   6 B  223  ASN ALA ALA LYS ILE ILE LYS HIS PRO ASN PHE ASP ARG          
SEQRES   7 B  223  LYS THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU SER          
SEQRES   8 B  223  SER PRO VAL LYS LEU ASN ALA ARG VAL ALA THR ILE ALA          
SEQRES   9 B  223  LEU PRO SER SER CYS ALA PRO ALA GLY THR GLN CYS LEU          
SEQRES  10 B  223  ILE SER GLY TRP GLY HIS THR LEU SER SER GLY VAL ASN          
SEQRES  11 B  223  HIS PRO ASP LEU LEU GLN CYS LEU ASP ALA PRO LEU LEU          
SEQRES  12 B  223  PRO GLN ALA ASP CYS GLU ALA SER TYR PRO GLY LYS ILE          
SEQRES  13 B  223  THR ASP ASN MET VAL CYS VAL GLY PHE LEU GLU GLY GLY          
SEQRES  14 B  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 B  223  CYS ASN GLY GLU LEU GLN GLY ILE VAL SER TRP GLY TYR          
SEQRES  16 B  223  GLY CYS ALA LEU PRO ASP ASN PRO GLY VAL TYR THR LYS          
SEQRES  17 B  223  VAL CYS ASN TYR VAL ASP TRP ILE GLN ASP THR ILE ALA          
SEQRES  18 B  223  ALA ASN                                                      
HET     CA  B 246       1                                                       
HET    ACT  B 247       4                                                       
HET     NI  B 248       1                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACT ACETATE ION                                                      
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5   NI    NI 2+                                                        
FORMUL   6  HOH   *52(H2 O)                                                     
HELIX    1   1 GLU A   33  THR A   35  5                                   3    
HELIX    2   2 GLY A  102  GLY A  105  5                                   4    
HELIX    3   3 ALA B   56  CYS B   58  5                                   3    
HELIX    4   4 GLN B  165  SER B  171  1                                   7    
HELIX    5   5 VAL B  231  ASN B  233  5                                   3    
HELIX    6   6 VAL B  235  ALA B  243  1                                   9    
SHEET    1   A 2 MET A  20  ILE A  25  0                                        
SHEET    2   A 2 ILE A 115  PRO A 120 -1  N  THR A 119   O  LYS A  21           
SHEET    1   B 3 ASP A 124  LYS A 131  0                                        
SHEET    2   B 3 LEU A  36  GLY A  43 -1  N  GLY A  43   O  ASP A 124           
SHEET    3   B 3 MET A 106  ARG A 108 -1  N  LEU A 107   O  VAL A  38           
SHEET    1   C 2 GLY A  43  VAL A  48  0                                        
SHEET    2   C 2 GLU A  93  THR A  98 -1  N  VAL A  97   O  GLN A  44           
SHEET    1   D 2 LYS A  58  LEU A  64  0                                        
SHEET    2   D 2 TYR A  69  ASP A  75 -1  N  ASP A  75   O  LYS A  58           
SHEET    1   E 7 PHE B  82  ASN B  84  0                                        
SHEET    2   E 7 GLN B  64  ARG B  66 -1  N  VAL B  65   O  VAL B  83           
SHEET    3   E 7 GLN B  30  ASN B  34 -1  N  ASN B  34   O  GLN B  64           
SHEET    4   E 7 HIS B  40  ASN B  48 -1  N  GLY B  44   O  VAL B  31           
SHEET    5   E 7 TRP B  51  SER B  54 -1  N  VAL B  53   O  SER B  45           
SHEET    6   E 7 MET B 104  LEU B 108 -1  N  ILE B 106   O  VAL B  52           
SHEET    7   E 7 ALA B  85  LYS B  90 -1  N  ILE B  89   O  LEU B 105           
SHEET    1   F 2 GLN B 135  GLY B 140  0                                        
SHEET    2   F 2 GLN B 156  PRO B 161 -1  N  ALA B 160   O  CYS B 136           
SHEET    1   G 4 MET B 180  VAL B 183  0                                        
SHEET    2   G 4 GLY B 226  LYS B 230 -1  N  TYR B 228   O  VAL B 181           
SHEET    3   G 4 GLU B 204  TRP B 215 -1  N  TRP B 215   O  VAL B 227           
SHEET    4   G 4 PRO B 198  CYS B 201 -1  N  CYS B 201   O  GLU B 204           
SSBOND   1 CYS A   50    CYS A   87                          1555   1555  2.03  
SSBOND   2 CYS B   22    CYS B  157                          1555   1555  2.03  
SSBOND   3 CYS B   42    CYS B   58                          1555   1555  2.03  
SSBOND   4 CYS B  128    CYS B  232                          1555   1555  2.03  
SSBOND   5 CYS B  136    CYS B  201                          1555   1555  2.03  
SSBOND   6 CYS B  168    CYS B  182                          1555   1555  2.03  
SSBOND   7 CYS B  191    CYS B  220                          1555   1555  2.03  
LINK        CA    CA B 246                 O   ASN B  72     1555   1555  1.86  
LINK        CA    CA B 246                 O   VAL B  75     1555   1555  1.84  
LINK        CA    CA B 246                 C   ACT B 247     1555   1555  2.01  
LINK        CA    CA B 246                 O   ACT B 247     1555   1555  1.66  
LINK        CA    CA B 246                 OXT ACT B 247     1555   1555  1.93  
LINK        NI    NI B 248                 NE2 HIS A  86     1555   1555  2.15  
LINK        NI    NI B 248                 NE2 HIS B 151     1555   1555  2.24  
LINK        CA    CA B 246                 OE2 GLU B  77     1555   1555  2.66  
LINK        CA    CA B 246                 OE1 GLU B  70     1555   1555  3.06  
LINK        NI    NI B 248                 NE2 HIS B 143     1555   1555  2.61  
LINK        NI    NI B 248                 O   HOH B 253     1555   1555  2.50  
SITE     1 NI1  4 HIS A  86  HIS B 143  HIS B 151  HOH B 253                    
SITE     1 AC1  5 GLU B  70  ASN B  72  VAL B  75  GLU B  77                    
SITE     2 AC1  5 ACT B 247                                                     
SITE     1 AC2  7 GLU B  70  ASN B  72  VAL B  75  LEU B  76                    
SITE     2 AC2  7 GLU B  77  ASN B  79   CA B 246                               
SITE     1 AC3  4 HIS A  86  HIS B 143  HIS B 151  HOH B 253                    
CRYST1   86.380   56.230   81.230  90.00  92.81  90.00 C 1 2 1       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      0.011577  0.000000  0.000568        0.00000                         
SCALE2      0.000000  0.017784  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012326        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system