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Database: PDB
Entry: 1KAS
LinkDB: 1KAS
Original site: 1KAS 
HEADER    ACYLTRANSFERASE                         22-DEC-97   1KAS              
TITLE     BETA-KETOACYL-ACP SYNTHASE II FROM ESCHERICHIA COLI                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-KETOACYL ACP SYNTHASE II;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.3.1.41;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562                                                  
KEYWDS    ACYLTRANSFERASE, CONDENSING ENZYME, FATTY ACID ELONGATION, LIPID      
KEYWDS   2 METABOLISM, ALPHA-BETA PROTEIN, FIVE-LAYERED FOLD, ALPHA-BETA-ALPHA- 
KEYWDS   3 BETA-ALPHA                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.HUANG,J.JIA,P.EDWARDS,K.DEHESH,G.SCHNEIDER,Y.LINDQVIST              
REVDAT   5   07-FEB-24 1KAS    1       REMARK                                   
REVDAT   4   13-JUL-11 1KAS    1       VERSN                                    
REVDAT   3   24-FEB-09 1KAS    1       VERSN                                    
REVDAT   2   20-APR-99 1KAS    1       COMPND REMARK SOURCE JRNL                
REVDAT   2 2                   1       KEYWDS                                   
REVDAT   1   02-MAR-99 1KAS    0                                                
JRNL        AUTH   W.HUANG,J.JIA,P.EDWARDS,K.DEHESH,G.SCHNEIDER,Y.LINDQVIST     
JRNL        TITL   CRYSTAL STRUCTURE OF BETA-KETOACYL-ACYL CARRIER PROTEIN      
JRNL        TITL 2 SYNTHASE II FROM E.COLI REVEALS THE MOLECULAR ARCHITECTURE   
JRNL        TITL 3 OF CONDENSING ENZYMES.                                       
JRNL        REF    EMBO J.                       V.  17  1183 1998              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   9482715                                                      
JRNL        DOI    10.1093/EMBOJ/17.5.1183                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 18580                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.242                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.279                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1810                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3004                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 31                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.004 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.018 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1KAS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000174390.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : MAY-97                             
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1050                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18580                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 8.000                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.5                               
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
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) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.27100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIPLE ISOMORPHOUS         
REMARK 200  REPLACEMENT                                                         
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.0                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.94333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       97.88667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       97.88667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       48.94333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 5950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26380 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -52.0 KCAL/MOL                        
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   BIOMT1   2 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  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     SER A     1                                                      
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    ALA A 162     -126.00     48.11                                   
REMARK 500    LYS A 192       75.18   -156.11                                   
REMARK 500    TRP A 222       -1.08     74.40                                   
REMARK 500    ALA A 235      132.94   -171.71                                   
REMARK 500    ALA A 255     -178.28    175.89                                   
REMARK 500    TYR A 267      -74.27   -136.76                                   
REMARK 500    SER A 306       29.59     86.00                                   
REMARK 500    LEU A 342     -107.29     42.59                                   
REMARK 500    ASP A 376       -1.71   -150.65                                   
REMARK 500    HIS A 382      -31.48   -130.15                                   
REMARK 500    SER A 388      -54.78   -120.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ACT                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: ACTIVE SITE RESIDUE.                               
DBREF  1KAS A    1   412  UNP    P0AAI5   FABF_ECOLI       1    412             
SEQRES   1 A  412  SER LYS ARG ARG VAL VAL VAL THR GLY LEU GLY MET LEU          
SEQRES   2 A  412  SER PRO VAL GLY ASN THR VAL GLU SER THR TRP LYS ALA          
SEQRES   3 A  412  LEU LEU ALA GLY GLN SER GLY ILE SER LEU ILE ASP HIS          
SEQRES   4 A  412  PHE ASP THR SER ALA TYR ALA THR LYS PHE ALA GLY LEU          
SEQRES   5 A  412  VAL LYS ASP PHE ASN CYS GLU ASP ILE ILE SER ARG LYS          
SEQRES   6 A  412  GLU GLN ARG LYS MET ASP ALA PHE ILE GLN TYR GLY ILE          
SEQRES   7 A  412  VAL ALA GLY VAL GLN ALA MET GLN ASP SER GLY LEU GLU          
SEQRES   8 A  412  ILE THR GLU GLU ASN ALA THR ARG ILE GLY ALA ALA ILE          
SEQRES   9 A  412  GLY SER GLY ILE GLY GLY LEU GLY LEU ILE GLU GLU ASN          
SEQRES  10 A  412  HIS THR SER LEU MET ASN GLY GLY PRO ARG LYS ILE SER          
SEQRES  11 A  412  PRO PHE PHE VAL PRO SER THR ILE VAL ASN MET VAL ALA          
SEQRES  12 A  412  GLY HIS LEU THR ILE MET TYR GLY LEU ARG GLY PRO SER          
SEQRES  13 A  412  ILE SER ILE ALA THR ALA CYS THR SER GLY VAL HIS ASN          
SEQRES  14 A  412  ILE GLY HIS ALA ALA ARG ILE ILE ALA TYR GLY ASP ALA          
SEQRES  15 A  412  ASP VAL MET VAL ALA GLY GLY ALA GLU LYS ALA SER THR          
SEQRES  16 A  412  PRO LEU GLY VAL GLY GLY PHE GLY ALA ALA ARG ALA LEU          
SEQRES  17 A  412  SER THR ARG ASN ASP ASN PRO GLN ALA ALA SER ARG PRO          
SEQRES  18 A  412  TRP ASP LYS GLU ARG ASP GLY PHE VAL LEU GLY ASP GLY          
SEQRES  19 A  412  ALA GLY MET LEU VAL LEU GLU GLU TYR GLU HIS ALA LYS          
SEQRES  20 A  412  LYS ARG GLY ALA LYS ILE TYR ALA GLU LEU VAL GLY PHE          
SEQRES  21 A  412  GLY MET SER SER ASP ALA TYR HIS MET THR SER PRO PRO          
SEQRES  22 A  412  GLU ASN GLY ALA GLY ALA ALA LEU ALA MET ALA ASN ALA          
SEQRES  23 A  412  LEU ARG ASP ALA GLY ILE GLU ALA SER GLN ILE GLY TYR          
SEQRES  24 A  412  VAL ASN ALA HIS GLY THR SER THR PRO ALA GLY ASP LYS          
SEQRES  25 A  412  ALA GLU ALA GLN ALA VAL LYS THR ILE PHE GLY GLU ALA          
SEQRES  26 A  412  ALA SER ARG VAL LEU VAL SER SER THR LYS SER MET THR          
SEQRES  27 A  412  GLY HIS LEU LEU GLY ALA ALA GLY ALA VAL GLU SER ILE          
SEQRES  28 A  412  TYR SER ILE LEU ALA LEU ARG ASP GLN ALA VAL PRO PRO          
SEQRES  29 A  412  THR ILE ASN LEU ASP ASN PRO ASP GLU GLY CYS ASP LEU          
SEQRES  30 A  412  ASP PHE VAL PRO HIS GLU ALA ARG GLN VAL SER GLY MET          
SEQRES  31 A  412  GLU TYR THR LEU CYS ASN SER PHE GLY PHE GLY GLY THR          
SEQRES  32 A  412  ASN GLY SER LEU ILE PHE LYS LYS ILE                          
FORMUL   2  HOH   *31(H2 O)                                                     
HELIX    1   1 VAL A   20  LEU A   28  1                                   9    
HELIX    2   2 ARG A   64  LYS A   69  1                                   6    
HELIX    3   3 ALA A   72  SER A   88  1                                  17    
HELIX    4   4 ALA A   97  ARG A   99  5                                   3    
HELIX    5   5 LEU A  111  GLY A  124  1                                  14    
HELIX    6   6 PRO A  126  LYS A  128  5                                   3    
HELIX    7   7 PHE A  133  THR A  137  1                                   5    
HELIX    8   8 VAL A  139  TYR A  150  5                                  12    
HELIX    9   9 ALA A  162  TYR A  179  5                                  18    
HELIX   10  10 PRO A  196  ALA A  204  1                                   9    
HELIX   11  11 PRO A  215  ALA A  218  1                                   4    
HELIX   12  12 TYR A  243  ARG A  249  1                                   7    
HELIX   13  13 ALA A  277  ALA A  290  1                                  14    
HELIX   14  14 ALA A  294  GLN A  296  5                                   3    
HELIX   15  15 PRO A  308  PHE A  322  1                                  15    
HELIX   16  16 THR A  334  THR A  338  5                                   5    
HELIX   17  17 LEU A  342  ASP A  359  5                                  18    
SHEET    1   A 9 ILE A 100  GLY A 105  0                                        
SHEET    2   A 9 VAL A 184  GLU A 191  1  N  VAL A 184   O  GLY A 101           
SHEET    3   A 9 GLY A 234  GLU A 242 -1  N  LEU A 240   O  MET A 185           
SHEET    4   A 9 VAL A   5  LEU A  13 -1  N  LEU A  13   O  ALA A 235           
SHEET    5   A 9 ALA A 255  SER A 264 -1  N  LEU A 257   O  VAL A   5           
SHEET    6   A 9 THR A 403  LYS A 410 -1  N  LYS A 410   O  GLU A 256           
SHEET    7   A 9 TYR A 392  GLY A 399 -1  N  GLY A 399   O  THR A 403           
SHEET    8   A 9 ILE A 297  ASN A 301  1  N  GLY A 298   O  TYR A 392           
SHEET    9   A 9 LEU A 330  SER A 332  1  N  LEU A 330   O  VAL A 300           
SHEET    1   B 2 ILE A  34  LEU A  36  0                                        
SHEET    2   B 2 PHE A  49  GLY A  51 -1  N  ALA A  50   O  SER A  35           
SITE     1 ACT  1 CYS A 163                                                     
CRYST1   76.410   76.410  146.830  90.00  90.00 120.00 P 31 2 1      6          
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      0.013087  0.007556  0.000000        0.00000                         
SCALE2      0.000000  0.015112  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006811        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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