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Database: PDB
Entry: 1TAW
LinkDB: 1TAW
Original site: 1TAW 
HEADER    COMPLEX (SERINE PROTEASE/INHIBITOR)     19-DEC-96   1TAW              
TITLE     BOVINE TRYPSIN COMPLEXED TO APPI                                      
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: PROTEASE INHIBITOR DOMAIN OF ALZHEIMER'S AMYLOID           
COMPND   7 BETA-PROTEIN PRECURSOR;                                              
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: RESIDUES 289 - 342 OF ALZHEIMER'S AMYLOID BETA-            
COMPND  10 PROTEIN PRECURSOR;                                                   
COMPND  11 SYNONYM: APPI;                                                       
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 ORGAN: PANCREATIC;                                                   
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 ORGAN: PANCREATIC;                                                   
SOURCE  11 GENE: A4;                                                            
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  14 EXPRESSION_SYSTEM_STRAIN: 27C7;                                      
SOURCE  15 EXPRESSION_SYSTEM_PLASMID: PA4G32R;                                  
SOURCE  16 EXPRESSION_SYSTEM_GENE: A4                                           
KEYWDS    SERINE PROTEASE, KUNITZ TYPE INHIBITOR, COMPLEX, PROTEASE-            
KEYWDS   2 SUBSTRATE INTERACTIONS, COMPLEX (SERINE PROTEASE/INHIBITOR)          
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.R.HYNES,A.A.KOSSIAKOFF                                              
REVDAT   2   24-FEB-09 1TAW    1       VERSN                                    
REVDAT   1   24-JUN-97 1TAW    0                                                
JRNL        AUTH   A.J.SCHEIDIG,T.R.HYNES,L.A.PELLETIER,J.A.WELLS,              
JRNL        AUTH 2 A.A.KOSSIAKOFF                                               
JRNL        TITL   CRYSTAL STRUCTURES OF BOVINE CHYMOTRYPSIN AND                
JRNL        TITL 2 TRYPSIN COMPLEXED TO THE INHIBITOR DOMAIN OF                 
JRNL        TITL 3 ALZHEIMER'S AMYLOID BETA-PROTEIN PRECURSOR (APPI)            
JRNL        TITL 4 AND BASIC PANCREATIC TRYPSIN INHIBITOR (BPTI):               
JRNL        TITL 5 ENGINEERING OF INHIBITORS WITH ALTERED                       
JRNL        TITL 6 SPECIFICITIES.                                               
JRNL        REF    PROTEIN SCI.                  V.   6  1806 1997              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   9300481                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.R.HYNES,M.RANDAL,L.A.KENNEDY,C.EIGENBROT,                  
REMARK   1  AUTH 2 A.A.KOSSIAKOFF                                               
REMARK   1  TITL   X-RAY CRYSTAL STRUCTURE OF THE PROTEASE INHIBITOR            
REMARK   1  TITL 2 DOMAIN OF ALZHEIMER'S AMYLOID BETA-PROTEIN                   
REMARK   1  TITL 3 PRECURSOR                                                    
REMARK   1  REF    BIOCHEMISTRY                  V.  29 10018 1990              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 10000000.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 76.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 22374                          
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) : 0.184                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
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            : 2044                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 153                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.23                          
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) : 0.23                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.32                            
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) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.46                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 25.98                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.30                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : PARAM19.SOL                                    
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   : TOPH19.SOL                                     
REMARK   3  TOPOLOGY FILE  3   : TOPH19.ION                                     
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1TAW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : JAN-92                             
REMARK 200  TEMPERATURE           (KELVIN) : 277                                
REMARK 200  PH                             : 6.5                                
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          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ENRAF-NONIUS FAST                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MADNES                             
REMARK 200  DATA SCALING SOFTWARE          : PROCOR                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22374                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 76.6                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.25000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 2PTC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.74                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.5                                   
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       47.02500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.92500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       47.02500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.92500            
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 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        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  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     VAL B     1                                                      
REMARK 465     ARG B     2                                                      
REMARK 465     SER B    57                                                      
REMARK 465     ALA B    58                                                      
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    SER A  49       -7.83    -55.99                                   
REMARK 500    ASP A  71      -65.17   -132.30                                   
REMARK 500    SER A 150      100.34   -169.93                                   
REMARK 500    SER A 214      -72.42   -129.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 246  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 VAL A  75   O                                                      
REMARK 620 2 HOH A 322   O    73.4                                              
REMARK 620 3 GLU A  70   OE1 138.9  68.0                                        
REMARK 620 4 ASN A  72   O    84.3  82.1  77.2                                  
REMARK 620 5 GLU A  80   OE2  97.3  83.4  91.8 164.3                            
REMARK 620 6 HOH A 275   O   129.4 156.5  88.5  93.7  97.2                      
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 A 246                  
DBREF  1TAW A   16   245  UNP    P00760   TRY1_BOVIN      21    243             
DBREF  1TAW B    1    58  UNP    P05067   A4_HUMAN       287    344             
SEQADV 1TAW THR A  165  UNP  P00760    ASP   165 CONFLICT                       
SEQRES   1 A  223  ILE VAL GLY GLY TYR THR CYS GLY ALA ASN THR VAL PRO          
SEQRES   2 A  223  TYR GLN VAL SER LEU ASN SER GLY TYR HIS PHE CYS GLY          
SEQRES   3 A  223  GLY SER LEU ILE ASN SER GLN TRP VAL VAL SER ALA ALA          
SEQRES   4 A  223  HIS CYS TYR LYS SER GLY ILE GLN VAL ARG LEU GLY GLU          
SEQRES   5 A  223  ASP ASN ILE ASN VAL VAL GLU GLY ASN GLU GLN PHE ILE          
SEQRES   6 A  223  SER ALA SER LYS SER ILE VAL HIS PRO SER TYR ASN SER          
SEQRES   7 A  223  ASN THR LEU ASN ASN ASP ILE MET LEU ILE LYS LEU LYS          
SEQRES   8 A  223  SER ALA ALA SER LEU ASN SER ARG VAL ALA SER ILE SER          
SEQRES   9 A  223  LEU PRO THR SER CYS ALA SER ALA GLY THR GLN CYS LEU          
SEQRES  10 A  223  ILE SER GLY TRP GLY ASN THR LYS SER SER GLY THR SER          
SEQRES  11 A  223  TYR PRO ASP VAL LEU LYS CYS LEU LYS ALA PRO ILE LEU          
SEQRES  12 A  223  SER THR SER SER CYS LYS SER ALA TYR PRO GLY GLN ILE          
SEQRES  13 A  223  THR SER ASN MET PHE CYS ALA GLY TYR LEU GLU GLY GLY          
SEQRES  14 A  223  LYS ASP SER CYS GLN GLY ASP SER GLY GLY PRO VAL VAL          
SEQRES  15 A  223  CYS SER GLY LYS LEU GLN GLY ILE VAL SER TRP GLY SER          
SEQRES  16 A  223  GLY CYS ALA GLN LYS ASN LYS PRO GLY VAL TYR THR LYS          
SEQRES  17 A  223  VAL CYS ASN TYR VAL SER TRP ILE LYS GLN THR ILE ALA          
SEQRES  18 A  223  SER ASN                                                      
SEQRES   1 B   58  VAL ARG GLU VAL CYS SER GLU GLN ALA GLU THR GLY PRO          
SEQRES   2 B   58  CYS ARG ALA MET ILE SER ARG TRP TYR PHE ASP VAL THR          
SEQRES   3 B   58  GLU GLY LYS CYS ALA PRO PHE PHE TYR GLY GLY CYS GLY          
SEQRES   4 B   58  GLY ASN ARG ASN ASN PHE ASP THR GLU GLU TYR CYS MET          
SEQRES   5 B   58  ALA VAL CYS GLY SER ALA                                      
HET     CA  A 246       1                                                       
HETNAM      CA CALCIUM ION                                                      
FORMUL   3   CA    CA 2+                                                        
FORMUL   4  HOH   *153(H2 O)                                                    
HELIX    1   1 ALA A   56  CYS A   58  5                                   3    
HELIX    2   2 THR A  165  ALA A  171  1                                   7    
HELIX    3   3 VAL A  231  ALA A  243  5                                  13    
HELIX    4   4 VAL B    4  SER B    6  5                                   3    
HELIX    5   5 GLU B   48  VAL B   54  1                                   7    
SHEET    1   A 7 GLN A  81  SER A  84  0                                        
SHEET    2   A 7 GLN A  64  LEU A  67 -1  N  LEU A  67   O  GLN A  81           
SHEET    3   A 7 GLN A  30  ASN A  34 -1  N  ASN A  34   O  GLN A  64           
SHEET    4   A 7 HIS A  40  ASN A  48 -1  N  GLY A  44   O  VAL A  31           
SHEET    5   A 7 TRP A  51  SER A  54 -1  N  VAL A  53   O  SER A  45           
SHEET    6   A 7 MET A 104  LEU A 108 -1  N  ILE A 106   O  VAL A  52           
SHEET    7   A 7 ALA A  85  VAL A  90 -1  N  ILE A  89   O  LEU A 105           
SHEET    1   B 2 GLN A 135  GLY A 140  0                                        
SHEET    2   B 2 LYS A 156  PRO A 161 -1  N  ALA A 160   O  CYS A 136           
SHEET    1   C 4 MET A 180  ALA A 183  0                                        
SHEET    2   C 4 GLY A 226  LYS A 230 -1  N  TYR A 228   O  PHE A 181           
SHEET    3   C 4 LYS A 204  TRP A 215 -1  N  TRP A 215   O  VAL A 227           
SHEET    4   C 4 PRO A 198  CYS A 201 -1  N  CYS A 201   O  LYS A 204           
SHEET    1   D 2 ILE B  18  ASP B  24  0                                        
SHEET    2   D 2 LYS B  29  TYR B  35 -1  N  TYR B  35   O  ILE B  18           
SSBOND   1 CYS A   22    CYS A  157                          1555   1555  2.03  
SSBOND   2 CYS A   42    CYS A   58                          1555   1555  2.02  
SSBOND   3 CYS A  128    CYS A  232                          1555   1555  2.04  
SSBOND   4 CYS A  136    CYS A  201                          1555   1555  2.03  
SSBOND   5 CYS A  168    CYS A  182                          1555   1555  2.02  
SSBOND   6 CYS A  191    CYS A  220                          1555   1555  2.02  
SSBOND   7 CYS B    5    CYS B   55                          1555   1555  2.03  
SSBOND   8 CYS B   14    CYS B   38                          1555   1555  2.03  
SSBOND   9 CYS B   30    CYS B   51                          1555   1555  2.01  
LINK        CA    CA A 246                 O   VAL A  75     1555   1555  2.18  
LINK        CA    CA A 246                 O   HOH A 322     1555   1555  2.37  
LINK        CA    CA A 246                 OE1 GLU A  70     1555   1555  2.39  
LINK        CA    CA A 246                 O   ASN A  72     1555   1555  2.32  
LINK        CA    CA A 246                 OE2 GLU A  80     1555   1555  2.48  
LINK        CA    CA A 246                 O   HOH A 275     1555   1555  2.30  
SITE     1 AC1  6 GLU A  70  ASN A  72  VAL A  75  GLU A  80                    
SITE     2 AC1  6 HOH A 275  HOH A 322                                          
CRYST1   94.050   49.850   68.800  90.00  96.31  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      0.010633  0.000000  0.001176        0.00000                         
SCALE2      0.000000  0.020060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014623        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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