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Database: PDB
Entry: 1ZYP
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Original site: 1ZYP 
HEADER    OXIDOREDUCTASE                          10-JUN-05   1ZYP              
TITLE     SYNCHROTRON REDUCED FORM OF THE N-TERMINAL DOMAIN OF                  
TITLE    2 SALMONELLA TYPHIMURIUM AHPF                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALKYL HYDROPEROXIDE REDUCTASE SUBUNIT F;                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 1-202;                                            
COMPND   5 SYNONYM: ALKYL HYDROPEROXIDE REDUCTASE F52A PROTEIN;                 
COMPND   6 EC: 1.6.4.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;                         
SOURCE   3 ORGANISM_TAXID: 602;                                                 
SOURCE   4 GENE: AHPF;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    THIOREDOXIN, DISULFIDE, PEROXIREDOXIN, THIOLATE, ALKYL                
KEYWDS   2 HYDROPEROXIDE REDUCTASE, SYNCHROTRON RADIATION, PKA,                 
KEYWDS   3 RADIATION DAMAGE, OXIDOREDUCTASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.R.ROBERTS,Z.A.WOOD,T.J.JONSSON,L.B.POOLE,P.A.KARPLUS                
REVDAT   3   24-FEB-09 1ZYP    1       VERSN                                    
REVDAT   2   14-MAR-06 1ZYP    1       JRNL                                     
REVDAT   1   21-JUN-05 1ZYP    0                                                
JRNL        AUTH   B.R.ROBERTS,Z.A.WOOD,T.J.JONSSON,L.B.POOLE,                  
JRNL        AUTH 2 P.A.KARPLUS                                                  
JRNL        TITL   OXIDIZED AND SYNCHROTRON CLEAVED STRUCTURES OF THE           
JRNL        TITL 2 DISULFIDE REDOX CENTER IN THE N-TERMINAL DOMAIN OF           
JRNL        TITL 3 SALMONELLA TYPHIMURIUM AHPF                                  
JRNL        REF    PROTEIN SCI.                  V.  14  2414 2005              
JRNL        REFN                   ISSN 0961-8368                               
JRNL        PMID   16131664                                                     
JRNL        DOI    10.1110/PS.051459705                                         
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 19094                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1881                            
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            : 3040                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 142                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 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) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ZYP COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUN-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033275.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.01                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19094                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.270                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.3                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.3                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30-35% PEG 4000, 0.2M AMMONIUM           
REMARK 280  ACETATE, 0.1M TRIS , PH 8.6, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.63450            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       53.97150            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       53.97150            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       21.31725            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       53.97150            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       53.97150            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       63.95175            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       53.97150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       53.97150            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       21.31725            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       53.97150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       53.97150            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       63.95175            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       42.63450            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     THR A   197                                                      
REMARK 465     GLY A   198                                                      
REMARK 465     ALA A   199                                                      
REMARK 465     GLU A   200                                                      
REMARK 465     LYS A   201                                                      
REMARK 465     ARG A   202                                                      
REMARK 465     THR B   197                                                      
REMARK 465     GLY B   198                                                      
REMARK 465     ALA B   199                                                      
REMARK 465     GLU B   200                                                      
REMARK 465     LYS B   201                                                      
REMARK 465     ARG B   202                                                      
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    THR A   4      -39.37    -35.56                                   
REMARK 500    ASP A  28     -166.11   -123.56                                   
REMARK 500    ASN A  56       25.44    -73.24                                   
REMARK 500    LEU A  83     -154.02    -94.56                                   
REMARK 500    ALA B  12      -73.31    -70.10                                   
REMARK 500    ASP B  28     -157.46   -108.22                                   
REMARK 500    SER B  30      151.11    -46.61                                   
REMARK 500    LEU B  58      151.49    -46.73                                   
REMARK 500    PRO B  59       55.45    -93.51                                   
REMARK 500    LEU B  83     -140.87    -93.97                                   
REMARK 500    VAL B 168      106.86    -58.50                                   
REMARK 500    MET B 169      -96.32    -63.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1HYU   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE INTACT AHPF PROTEIN                                 
REMARK 900 RELATED ID: 1ZYN   RELATED DB: PDB                                   
REMARK 900 OXIDIZED FORM OF THE NTD DOMAIN OF AHPF                              
DBREF  1ZYP A    1   202  UNP    P19480   AHPF_SALTY       1    202             
DBREF  1ZYP B    1   202  UNP    P19480   AHPF_SALTY       1    202             
SEQRES   1 A  202  MET LEU ASP THR ASN MET LYS THR GLN LEU ARG ALA TYR          
SEQRES   2 A  202  LEU GLU LYS LEU THR LYS PRO VAL GLU LEU ILE ALA THR          
SEQRES   3 A  202  LEU ASP ASP SER ALA LYS SER ALA GLU ILE LYS GLU LEU          
SEQRES   4 A  202  LEU ALA GLU ILE ALA GLU LEU SER ASP LYS VAL THR PHE          
SEQRES   5 A  202  LYS GLU ASP ASN THR LEU PRO VAL ARG LYS PRO SER PHE          
SEQRES   6 A  202  LEU ILE THR ASN PRO GLY SER GLN GLN GLY PRO ARG PHE          
SEQRES   7 A  202  ALA GLY SER PRO LEU GLY HIS GLU PHE THR SER LEU VAL          
SEQRES   8 A  202  LEU ALA LEU LEU TRP THR GLY GLY HIS PRO SER LYS GLU          
SEQRES   9 A  202  ALA GLN SER LEU LEU GLU GLN ILE ARG ASP ILE ASP GLY          
SEQRES  10 A  202  ASP PHE GLU PHE GLU THR TYR TYR SER LEU SER CYS HIS          
SEQRES  11 A  202  ASN CYS PRO ASP VAL VAL GLN ALA LEU ASN LEU MET ALA          
SEQRES  12 A  202  VAL LEU ASN PRO ARG ILE LYS HIS THR ALA ILE ASP GLY          
SEQRES  13 A  202  GLY THR PHE GLN ASN GLU ILE THR GLU ARG ASN VAL MET          
SEQRES  14 A  202  GLY VAL PRO ALA VAL PHE VAL ASN GLY LYS GLU PHE GLY          
SEQRES  15 A  202  GLN GLY ARG MET THR LEU THR GLU ILE VAL ALA LYS VAL          
SEQRES  16 A  202  ASP THR GLY ALA GLU LYS ARG                                  
SEQRES   1 B  202  MET LEU ASP THR ASN MET LYS THR GLN LEU ARG ALA TYR          
SEQRES   2 B  202  LEU GLU LYS LEU THR LYS PRO VAL GLU LEU ILE ALA THR          
SEQRES   3 B  202  LEU ASP ASP SER ALA LYS SER ALA GLU ILE LYS GLU LEU          
SEQRES   4 B  202  LEU ALA GLU ILE ALA GLU LEU SER ASP LYS VAL THR PHE          
SEQRES   5 B  202  LYS GLU ASP ASN THR LEU PRO VAL ARG LYS PRO SER PHE          
SEQRES   6 B  202  LEU ILE THR ASN PRO GLY SER GLN GLN GLY PRO ARG PHE          
SEQRES   7 B  202  ALA GLY SER PRO LEU GLY HIS GLU PHE THR SER LEU VAL          
SEQRES   8 B  202  LEU ALA LEU LEU TRP THR GLY GLY HIS PRO SER LYS GLU          
SEQRES   9 B  202  ALA GLN SER LEU LEU GLU GLN ILE ARG ASP ILE ASP GLY          
SEQRES  10 B  202  ASP PHE GLU PHE GLU THR TYR TYR SER LEU SER CYS HIS          
SEQRES  11 B  202  ASN CYS PRO ASP VAL VAL GLN ALA LEU ASN LEU MET ALA          
SEQRES  12 B  202  VAL LEU ASN PRO ARG ILE LYS HIS THR ALA ILE ASP GLY          
SEQRES  13 B  202  GLY THR PHE GLN ASN GLU ILE THR GLU ARG ASN VAL MET          
SEQRES  14 B  202  GLY VAL PRO ALA VAL PHE VAL ASN GLY LYS GLU PHE GLY          
SEQRES  15 B  202  GLN GLY ARG MET THR LEU THR GLU ILE VAL ALA LYS VAL          
SEQRES  16 B  202  ASP THR GLY ALA GLU LYS ARG                                  
FORMUL   3  HOH   *142(H2 O)                                                    
HELIX    1   1 ASP A    3  GLU A   15  1                                  13    
HELIX    2   2 SER A   30  GLU A   45  1                                  16    
HELIX    3   3 LEU A   83  HIS A   85  5                                   3    
HELIX    4   4 GLU A   86  GLY A   98  1                                  13    
HELIX    5   5 ALA A  105  ASP A  114  1                                  10    
HELIX    6   6 ASN A  131  ASN A  146  1                                  16    
HELIX    7   7 PHE A  159  ARG A  166  1                                   8    
HELIX    8   8 THR A  187  VAL A  195  1                                   9    
HELIX    9   9 ASP B    3  LEU B   14  1                                  12    
HELIX   10  10 GLU B   15  LEU B   17  5                                   3    
HELIX   11  11 SER B   30  GLU B   45  1                                  16    
HELIX   12  12 LEU B   83  HIS B   85  5                                   3    
HELIX   13  13 GLU B   86  GLY B   98  1                                  13    
HELIX   14  14 ALA B  105  ASP B  114  1                                  10    
HELIX   15  15 ASN B  131  LEU B  145  1                                  15    
HELIX   16  16 PHE B  159  ARG B  166  1                                   8    
HELIX   17  17 THR B  187  VAL B  195  1                                   9    
SHEET    1   A 8 VAL A  50  GLU A  54  0                                        
SHEET    2   A 8 VAL A  21  THR A  26  1  N  LEU A  23   O  THR A  51           
SHEET    3   A 8 SER A  64  THR A  68 -1  O  THR A  68   N  GLU A  22           
SHEET    4   A 8 ARG A  77  ALA A  79 -1  O  PHE A  78   N  PHE A  65           
SHEET    5   A 8 ILE A 149  ASP A 155  1  O  ALA A 153   N  ALA A  79           
SHEET    6   A 8 PHE A 119  TYR A 125  1  N  THR A 123   O  ILE A 154           
SHEET    7   A 8 ALA A 173  VAL A 176 -1  O  PHE A 175   N  GLU A 122           
SHEET    8   A 8 LYS A 179  GLN A 183 -1  O  LYS A 179   N  VAL A 176           
SHEET    1   B 8 VAL B  50  GLU B  54  0                                        
SHEET    2   B 8 VAL B  21  THR B  26  1  N  LEU B  23   O  LYS B  53           
SHEET    3   B 8 SER B  64  THR B  68 -1  O  LEU B  66   N  ILE B  24           
SHEET    4   B 8 ARG B  77  ALA B  79 -1  O  PHE B  78   N  PHE B  65           
SHEET    5   B 8 ILE B 149  ASP B 155  1  O  ALA B 153   N  ALA B  79           
SHEET    6   B 8 PHE B 119  TYR B 125  1  N  PHE B 121   O  LYS B 150           
SHEET    7   B 8 ALA B 173  VAL B 176 -1  O  PHE B 175   N  GLU B 122           
SHEET    8   B 8 LYS B 179  GLN B 183 -1  O  PHE B 181   N  VAL B 174           
SSBOND   1 CYS A  129    CYS A  132                          1555   1555  2.81  
SSBOND   2 CYS B  129    CYS B  132                          1555   1555  2.99  
CISPEP   1 LYS A   62    PRO A   63          0        -0.08                     
CISPEP   2 VAL A  171    PRO A  172          0         0.03                     
CISPEP   3 LYS B   62    PRO B   63          0        -0.06                     
CISPEP   4 VAL B  171    PRO B  172          0        -0.08                     
CRYST1  107.943  107.943   85.269  90.00  90.00  90.00 P 41 21 2    16          
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      0.009264  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009264  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011728        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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