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Database: PDB
Entry: 1VJS
LinkDB: 1VJS
Original site: 1VJS 
HEADER    HYDROLASE                               02-OCT-96   1VJS              
TITLE     STRUCTURE OF ALPHA-AMYLASE PRECURSOR                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA-AMYLASE;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BLA;                                                        
COMPND   5 EC: 3.2.1.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS LICHENIFORMIS;                         
SOURCE   3 ORGANISM_TAXID: 1402;                                                
SOURCE   4 STRAIN: BACILLUS LICHENIFORMIS;                                      
SOURCE   5 ATCC: 27811                                                          
KEYWDS    HYDROLASE, GLYCOSIDASE, CARBOHYDRATE METABOLISM                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.K.SONG,K.Y.HWANG,C.CHANG,S.W.SUH                                    
REVDAT   3   24-FEB-09 1VJS    1       VERSN                                    
REVDAT   2   01-APR-03 1VJS    1       JRNL                                     
REVDAT   1   12-MAR-97 1VJS    0                                                
JRNL        AUTH   K.Y.HWANG,H.K.SONG,C.CHANG,J.LEE,S.Y.LEE,K.K.KIM,            
JRNL        AUTH 2 S.CHOE,R.M.SWEET,S.W.SUH                                     
JRNL        TITL   CRYSTAL STRUCTURE OF THERMOSTABLE ALPHA-AMYLASE              
JRNL        TITL 2 FROM BACILLUS LICHENIFORMIS REFINED AT 1.7 A                 
JRNL        TITL 3 RESOLUTION                                                   
JRNL        EDIT   K.H.PARK, J.F.ROBYT, Y.D.CHOI                                
JRNL        REF    MOL.CELL                      V.   7   251 1997              
JRNL        PUBL   AMSTERDAM : ELSEVIER                                         
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   9163741                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   S.Y.LEE,S.KIM,R.M.SWEET,S.W.SUH                              
REMARK   1  TITL   CRYSTALLIZATION AND A PRELIMINARY X-RAY                      
REMARK   1  TITL 2 CRYSTALLOGRAPHIC STUDY OF ALPHA-AMYLASE FROM                 
REMARK   1  TITL 3 BACILLUS LICHENIFORMIS                                       
REMARK   1  REF    ARCH.BIOCHEM.BIOPHYS.         V. 291   255 1991              
REMARK   1  REFN                   ISSN 0003-9861                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 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) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
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             : 58601                          
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) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3800                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 290                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.70                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.72                            
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  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:  TYR 150, WHICH IS WELL DEFINED IN        
REMARK   3  THE ELECTRON DENSITY, IS IN THE DISALLOWED REGION IN THE            
REMARK   3  RAMACHANDRAN PLOT.                                                  
REMARK   4                                                                      
REMARK   4 1VJS 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        : 30-JUN-93                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-6A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : FUJI                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : WEIS                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 60922                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.6                               
REMARK 200  DATA REDUNDANCY                : 8.300                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR 3.1                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 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+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
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       42.70000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       59.95000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       59.95000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       64.05000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       59.95000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       59.95000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       21.35000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       59.95000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.95000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       64.05000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       59.95000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.95000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       21.35000            
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       42.70000            
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: 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     TRP A   182                                                      
REMARK 465     ASP A   183                                                      
REMARK 465     TRP A   184                                                      
REMARK 465     GLU A   185                                                      
REMARK 465     VAL A   186                                                      
REMARK 465     SER A   187                                                      
REMARK 465     ASN A   188                                                      
REMARK 465     GLU A   189                                                      
REMARK 465     ASN A   190                                                      
REMARK 465     GLY A   191                                                      
REMARK 465     ASN A   192                                                      
REMARK 465     ARG A   483                                                      
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    TYR A  10       56.88    -92.74                                   
REMARK 500    ALA A  58       82.29     50.71                                   
REMARK 500    LEU A  64       41.81    -88.00                                   
REMARK 500    ALA A 109      151.11    -48.90                                   
REMARK 500    ARG A 125        7.63    -62.92                                   
REMARK 500    TYR A 150      -32.08     71.43                                   
REMARK 500    ASP A 266      109.62   -161.91                                   
REMARK 500    SER A 337       55.95   -164.75                                   
REMARK 500    PHE A 403       59.61   -103.43                                   
REMARK 500    ASN A 421       19.18     57.92                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 750        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A 775        DISTANCE =  5.00 ANGSTROMS                       
DBREF  1VJS A    1   483  UNP    P06278   AMY_BACLI       30    512             
SEQRES   1 A  483  ALA ASN LEU ASN GLY THR LEU MET GLN TYR PHE GLU TRP          
SEQRES   2 A  483  TYR MET PRO ASN ASP GLY GLN HIS TRP LYS ARG LEU GLN          
SEQRES   3 A  483  ASN ASP SER ALA TYR LEU ALA GLU HIS GLY ILE THR ALA          
SEQRES   4 A  483  VAL TRP ILE PRO PRO ALA TYR LYS GLY THR SER GLN ALA          
SEQRES   5 A  483  ASP VAL GLY TYR GLY ALA TYR ASP LEU TYR ASP LEU GLY          
SEQRES   6 A  483  GLU PHE HIS GLN LYS GLY THR VAL ARG THR LYS TYR GLY          
SEQRES   7 A  483  THR LYS GLY GLU LEU GLN SER ALA ILE LYS SER LEU HIS          
SEQRES   8 A  483  SER ARG ASP ILE ASN VAL TYR GLY ASP VAL VAL ILE ASN          
SEQRES   9 A  483  HIS LYS GLY GLY ALA ASP ALA THR GLU ASP VAL THR ALA          
SEQRES  10 A  483  VAL GLU VAL ASP PRO ALA ASP ARG ASN ARG VAL ILE SER          
SEQRES  11 A  483  GLY GLU HIS LEU ILE LYS ALA TRP THR HIS PHE HIS PHE          
SEQRES  12 A  483  PRO GLY ARG GLY SER THR TYR SER ASP PHE LYS TRP HIS          
SEQRES  13 A  483  TRP TYR HIS PHE ASP GLY THR ASP TRP ASP GLU SER ARG          
SEQRES  14 A  483  LYS LEU ASN ARG ILE TYR LYS PHE GLN GLY LYS ALA TRP          
SEQRES  15 A  483  ASP TRP GLU VAL SER ASN GLU ASN GLY ASN TYR ASP TYR          
SEQRES  16 A  483  LEU MET TYR ALA ASP ILE ASP TYR ASP HIS PRO ASP VAL          
SEQRES  17 A  483  ALA ALA GLU ILE LYS ARG TRP GLY THR TRP TYR ALA ASN          
SEQRES  18 A  483  GLU LEU GLN LEU ASP GLY PHE ARG LEU ASP ALA VAL LYS          
SEQRES  19 A  483  HIS ILE LYS PHE SER PHE LEU ARG ASP TRP VAL ASN HIS          
SEQRES  20 A  483  VAL ARG GLU LYS THR GLY LYS GLU MET PHE THR VAL ALA          
SEQRES  21 A  483  GLU TYR TRP GLN ASN ASP LEU GLY ALA LEU GLU ASN TYR          
SEQRES  22 A  483  LEU ASN LYS THR ASN PHE ASN HIS SER VAL PHE ASP VAL          
SEQRES  23 A  483  PRO LEU HIS TYR GLN PHE HIS ALA ALA SER THR GLN GLY          
SEQRES  24 A  483  GLY GLY TYR ASP MET ARG LYS LEU LEU ASN SER THR VAL          
SEQRES  25 A  483  VAL SER LYS HIS PRO LEU LYS ALA VAL THR PHE VAL ASP          
SEQRES  26 A  483  ASN HIS ASP THR GLN PRO GLY GLN SER LEU GLU SER THR          
SEQRES  27 A  483  VAL GLN THR TRP PHE LYS PRO LEU ALA TYR ALA PHE ILE          
SEQRES  28 A  483  LEU THR ARG GLU SER GLY TYR PRO GLN VAL PHE TYR GLY          
SEQRES  29 A  483  ASP MET TYR GLY THR LYS GLY ASP SER GLN ARG GLU ILE          
SEQRES  30 A  483  PRO ALA LEU LYS HIS LYS ILE GLU PRO ILE LEU LYS ALA          
SEQRES  31 A  483  ARG LYS GLN TYR ALA TYR GLY ALA GLN HIS ASP TYR PHE          
SEQRES  32 A  483  ASP HIS HIS ASP ILE VAL GLY TRP THR ARG GLU GLY ASP          
SEQRES  33 A  483  SER SER VAL ALA ASN SER GLY LEU ALA ALA LEU ILE THR          
SEQRES  34 A  483  ASP GLY PRO GLY GLY ALA LYS ARG MET TYR VAL GLY ARG          
SEQRES  35 A  483  GLN ASN ALA GLY GLU THR TRP HIS ASP ILE THR GLY ASN          
SEQRES  36 A  483  ARG SER GLU PRO VAL VAL ILE ASN SER GLU GLY TRP GLY          
SEQRES  37 A  483  GLU PHE HIS VAL ASN GLY GLY SER VAL SER ILE TYR VAL          
SEQRES  38 A  483  GLN ARG                                                      
FORMUL   2  HOH   *290(H2 O)                                                    
HELIX    1   1 HIS A   21  ASN A   27  1                                   7    
HELIX    2   2 SER A   29  GLU A   34  1                                   6    
HELIX    3   3 LYS A   80  ARG A   93  1                                  14    
HELIX    4   4 TRP A  157  HIS A  159  5                                   3    
HELIX    5   5 ASP A  194  MET A  197  5                                   4    
HELIX    6   6 PRO A  206  LEU A  223  1                                  18    
HELIX    7   7 VAL A  233  HIS A  235  5                                   3    
HELIX    8   8 PHE A  238  THR A  252  1                                  15    
HELIX    9   9 LEU A  267  LYS A  276  1                                  10    
HELIX   10  10 VAL A  286  THR A  297  1                                  12    
HELIX   11  11 MET A  304  LEU A  308  5                                   5    
HELIX   12  12 VAL A  312  LYS A  315  1                                   4    
HELIX   13  13 PRO A  317  LYS A  319  5                                   3    
HELIX   14  14 THR A  341  THR A  353  1                                  13    
HELIX   15  15 TYR A  363  TYR A  367  1                                   5    
HELIX   16  16 LYS A  381  GLN A  393  1                                  13    
HELIX   17  17 ARG A  442  ASN A  444  5                                   3    
SHEET    1   A 7 VAL A 321  PHE A 323  0                                        
SHEET    2   A 7 TYR A 358  PHE A 362  1  N  TYR A 358   O  THR A 322           
SHEET    3   A 7 LEU A   7  GLN A   9  1  N  LEU A   7   O  VAL A 361           
SHEET    4   A 7 ALA A  39  TRP A  41  1  N  ALA A  39   O  MET A   8           
SHEET    5   A 7 ASN A  96  VAL A 101  1  N  ASN A  96   O  VAL A  40           
SHEET    6   A 7 GLY A 227  LEU A 230  1  N  GLY A 227   O  GLY A  99           
SHEET    7   A 7 PHE A 257  ALA A 260  1  N  PHE A 257   O  PHE A 228           
SHEET    1   B 3 TYR A 175  PHE A 177  0                                        
SHEET    2   B 3 ALA A 111  GLU A 119 -1  N  VAL A 118   O  LYS A 176           
SHEET    3   B 3 HIS A 133  HIS A 140 -1  N  HIS A 140   O  ALA A 111           
SHEET    1   C 4 GLN A 399  TYR A 402  0                                        
SHEET    2   C 4 ILE A 408  ARG A 413 -1  N  THR A 412   O  HIS A 400           
SHEET    3   C 4 LEU A 424  THR A 429 -1  N  ILE A 428   O  VAL A 409           
SHEET    4   C 4 VAL A 477  VAL A 481 -1  N  TYR A 480   O  ALA A 425           
SHEET    1   D 2 GLY A 434  TYR A 439  0                                        
SHEET    2   D 2 TRP A 467  VAL A 472 -1  N  VAL A 472   O  GLY A 434           
SHEET    1   E 2 PHE A 160  THR A 163  0                                        
SHEET    2   E 2 ALA A 199  ILE A 201 -1  N  ASP A 200   O  ASP A 161           
CRYST1  119.900  119.900   85.400  90.00  90.00  90.00 P 43 21 2     8          
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      0.008340  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008340  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011710        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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