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Database: PDB
Entry: 4BBW
LinkDB: 4BBW
Original site: 4BBW 
HEADER    HYDROLASE                               28-SEP-12   4BBW              
TITLE     THE CRYSTAL STRUCTURE OF SIALIDASE VPI 5482 (BTSA) FROM               
TITLE    2 BACTEROIDES THETAIOTAOMICRON                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SIALIDASE (NEURAMINIDASE);                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SIALIDASE VPI5482;                                          
COMPND   5 EC: 3.2.1.18;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACTEROIDES THETAIOTAOMICRON;                   
SOURCE   3 ORGANISM_TAXID: 818;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI,;                                
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE, NEURAMIDASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.-H.PARK,H.-N.SONG,T.-Y.JUNG,M.-H.LEE,E.-J.WOO                       
REVDAT   1   14-AUG-13 4BBW    0                                                
JRNL        AUTH   K.PARK,M.KIM,H.AHN,D.LEE,J.KIM,Y.KIM,E.WOO                   
JRNL        TITL   STRUCTURAL AND BIOCHEMICAL CHARACTERIZATION OF THE BROAD     
JRNL        TITL 2 SUBSTRATE SPECIFICITY OF BACTEROIDES THETAIOTAOMICRON        
JRNL        TITL 3 COMMENSAL SIALIDASE.                                         
JRNL        REF    BIOCHIM.BIOPHYS.ACTA          V.1834  1510 2013              
JRNL        REFN                   ISSN 0006-3002                               
JRNL        PMID   23665536                                                     
JRNL        DOI    10.1016/J.BBAPAP.2013.04.028                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.300                          
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.610                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.34                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.37                          
REMARK   3   NUMBER OF REFLECTIONS             : 28688                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.2109                          
REMARK   3   R VALUE            (WORKING SET) : 0.2084                          
REMARK   3   FREE R VALUE                     : 0.2592                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1454                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.6182 -  4.9532    1.00     3114   165  0.1861 0.2044        
REMARK   3     2  4.9532 -  3.9323    1.00     2974   135  0.1625 0.2399        
REMARK   3     3  3.9323 -  3.4354    1.00     2924   173  0.1916 0.2230        
REMARK   3     4  3.4354 -  3.1214    0.99     2869   170  0.2162 0.2679        
REMARK   3     5  3.1214 -  2.8977    0.99     2903   138  0.2307 0.2809        
REMARK   3     6  2.8977 -  2.7269    0.99     2868   143  0.2473 0.3982        
REMARK   3     7  2.7269 -  2.5904    0.92     2649   145  0.2545 0.3181        
REMARK   3     8  2.5904 -  2.4776    0.86     2474   132  0.2683 0.2876        
REMARK   3     9  2.4776 -  2.3822    0.81     2311   128  0.2745 0.3562        
REMARK   3    10  2.3822 -  2.3000    0.76     2148   125  0.3021 0.3202        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.360                                         
REMARK   3   B_SOL              : 46.123                                        
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.33             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.01            
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.123                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -22.0326                                             
REMARK   3    B22 (A**2) : -10.0386                                             
REMARK   3    B33 (A**2) : 32.0711                                              
REMARK   3    B12 (A**2) : 0.0000                                               
REMARK   3    B13 (A**2) : 0.0000                                               
REMARK   3    B23 (A**2) : 0.0000                                               
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           4170                                  
REMARK   3   ANGLE     :  1.316           5652                                  
REMARK   3   CHIRALITY :  0.095            628                                  
REMARK   3   PLANARITY :  0.005            725                                  
REMARK   3   DIHEDRAL  : 15.429           1541                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4BBW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-SEP-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-54215.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 4.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 6C1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD (QUANTUM 210)                  
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : HKL2000                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52341                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.31                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.00                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY                : 3.48                               
REMARK 200  R MERGE                    (I) : 0.28                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.50                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.43                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 68.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.7                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.50                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.72                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M NAH2PO4,0.4M K2HPO4,                
REMARK 280  PHOSPHATE-CITRATE 100MM PH4.2                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       70.68850            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       47.01150            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.68850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       47.01150            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     MSE A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     ARG A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     TYR A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     PHE A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     ILE A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     GLY A    15                                                      
REMARK 465     CYS A    16                                                      
REMARK 465     SER A    17                                                      
REMARK 465     ILE A    18                                                      
REMARK 465     PHE A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     LYS A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     ASP A    24                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A   170     O    HOH A  2028              2.19            
REMARK 500   O    ASP A   229     NH1  ARG A   298              2.16            
REMARK 500   O    LEU A   230     O    HOH A  2130              2.17            
REMARK 500   OG   SER A   239     O    HOH A  2135              2.19            
REMARK 500   OG   SER A   439     O    HOH A  2209              2.17            
REMARK 500   O    ASP A   517     O    HOH A  2236              2.12            
REMARK 500   O    ILE A   543     O    HOH A  2226              2.06            
REMARK 500   O    HOH A  2014     O    HOH A  2099              2.16            
REMARK 500   O    HOH A  2020     O    HOH A  2022              2.15            
REMARK 500   O    HOH A  2032     O    HOH A  2070              2.15            
REMARK 500   O    HOH A  2053     O    HOH A  2077              1.99            
REMARK 500   O    HOH A  2055     O    HOH A  2119              2.19            
REMARK 500   O    HOH A  2061     O    HOH A  2133              2.01            
REMARK 500   O    HOH A  2064     O    HOH A  2129              2.17            
REMARK 500   O    HOH A  2096     O    HOH A  2200              1.84            
REMARK 500   O    HOH A  2108     O    HOH A  2109              1.87            
REMARK 500   O    HOH A  2170     O    HOH A  2171              2.06            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    VAL A  26       88.41     52.60                                   
REMARK 500    LYS A  66      -32.12    104.04                                   
REMARK 500    ASN A  69       53.97     72.50                                   
REMARK 500    THR A  83     -169.71   -111.50                                   
REMARK 500    ASN A 107       52.34   -140.53                                   
REMARK 500    GLN A 124       69.68     34.13                                   
REMARK 500    PRO A 181      150.98    -49.81                                   
REMARK 500    ARG A 204      -54.04   -123.99                                   
REMARK 500    LEU A 230      -98.06     38.92                                   
REMARK 500    GLU A 232     -179.10   -177.85                                   
REMARK 500    SER A 256      119.47   -169.01                                   
REMARK 500    GLU A 259       47.55    -96.92                                   
REMARK 500    ASN A 268       36.94   -141.42                                   
REMARK 500    ASN A 282       15.07     57.25                                   
REMARK 500    VAL A 337       -6.68   -141.66                                   
REMARK 500    ARG A 371       37.04     70.69                                   
REMARK 500    HIS A 390     -102.65   -101.03                                   
REMARK 500    THR A 398     -104.14   -121.82                                   
REMARK 500    ARG A 418     -108.74    -63.51                                   
REMARK 500    LYS A 442      -43.30   -155.73                                   
REMARK 500    VAL A 448       86.02     63.54                                   
REMARK 500    ASP A 489       51.68   -110.52                                   
REMARK 500    ILE A 543      -67.70    -93.91                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ARG A 204        24.5      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 230        24.4      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4BBW A    1   544  UNP    Q8AAK9   Q8AAK9_BACTN     1    544             
SEQRES   1 A  544  MSE LYS ARG ASN HIS TYR LEU PHE THR LEU ILE LEU LEU          
SEQRES   2 A  544  LEU GLY CYS SER ILE PHE VAL LYS ALA SER ASP THR VAL          
SEQRES   3 A  544  PHE VAL HIS GLN THR GLN ILE PRO ILE LEU ILE GLU ARG          
SEQRES   4 A  544  GLN ASP ASN VAL LEU PHE TYR PHE ARG LEU ASP ALA LYS          
SEQRES   5 A  544  GLU SER ARG MSE MSE ASP GLU ILE VAL LEU ASP PHE GLY          
SEQRES   6 A  544  LYS SER VAL ASN LEU SER ASP VAL GLN ALA VAL LYS LEU          
SEQRES   7 A  544  TYR TYR GLY GLY THR GLU ALA LEU GLN ASP LYS GLY LYS          
SEQRES   8 A  544  LYS ARG PHE ALA PRO VAL ASP TYR ILE SER SER HIS ARG          
SEQRES   9 A  544  PRO GLY ASN THR LEU ALA ALA ILE PRO SER TYR SER ILE          
SEQRES  10 A  544  LYS CYS ALA GLU ALA LEU GLN PRO SER ALA LYS VAL VAL          
SEQRES  11 A  544  LEU LYS SER HIS TYR LYS LEU PHE PRO GLY ILE ASN PHE          
SEQRES  12 A  544  PHE TRP ILE SER LEU GLN MSE LYS PRO GLU THR SER LEU          
SEQRES  13 A  544  PHE THR LYS ILE SER SER GLU LEU GLN SER VAL LYS ILE          
SEQRES  14 A  544  ASP GLY LYS GLU ALA ILE CYS GLU GLU ARG SER PRO LYS          
SEQRES  15 A  544  ASP ILE ILE HIS ARG MSE ALA VAL GLY VAL ARG HIS ALA          
SEQRES  16 A  544  GLY ASP ASP GLY SER ALA SER PHE ARG ILE PRO GLY LEU          
SEQRES  17 A  544  VAL THR SER ASN LYS GLY THR LEU LEU GLY VAL TYR ASP          
SEQRES  18 A  544  VAL ARG TYR ASN SER SER VAL ASP LEU GLN GLU TYR VAL          
SEQRES  19 A  544  ASP VAL GLY LEU SER ARG SER THR ASP GLY GLY LYS THR          
SEQRES  20 A  544  TRP GLU LYS MSE ARG LEU PRO LEU SER PHE GLY GLU TYR          
SEQRES  21 A  544  ASP GLY LEU PRO ALA ALA GLN ASN GLY VAL GLY ASP PRO          
SEQRES  22 A  544  SER ILE LEU VAL ASP THR GLN THR ASN THR ILE TRP VAL          
SEQRES  23 A  544  VAL ALA ALA TRP THR HIS GLY MSE GLY ASN GLN ARG ALA          
SEQRES  24 A  544  TRP TRP SER SER HIS PRO GLY MSE ASP LEU TYR GLN THR          
SEQRES  25 A  544  ALA GLN LEU VAL MSE ALA LYS SER THR ASP ASP GLY LYS          
SEQRES  26 A  544  THR TRP SER LYS PRO ILE ASN ILE THR GLU GLN VAL LYS          
SEQRES  27 A  544  ASP PRO SER TRP TYR PHE LEU LEU GLN GLY PRO GLY ARG          
SEQRES  28 A  544  GLY ILE THR MSE SER ASP GLY THR LEU VAL PHE PRO THR          
SEQRES  29 A  544  GLN PHE ILE ASP SER THR ARG VAL PRO ASN ALA GLY ILE          
SEQRES  30 A  544  MSE TYR SER LYS ASP ARG GLY LYS THR TRP LYS MSE HIS          
SEQRES  31 A  544  ASN MSE ALA ARG THR ASN THR THR GLU ALA GLN VAL VAL          
SEQRES  32 A  544  GLU THR GLU PRO GLY VAL LEU MSE LEU ASN MSE ARG ASP          
SEQRES  33 A  544  ASN ARG GLY GLY SER ARG ALA VAL ALA ILE THR LYS ASP          
SEQRES  34 A  544  LEU GLY LYS THR TRP THR GLU HIS PRO SER SER ARG LYS          
SEQRES  35 A  544  ALA LEU GLN GLU PRO VAL CYS MSE ALA SER LEU ILE HIS          
SEQRES  36 A  544  VAL GLU ALA GLU ASP ASN VAL LEU ASP LYS ASP ILE LEU          
SEQRES  37 A  544  LEU PHE SER ASN PRO ASN THR THR ARG GLY ARG ASN HIS          
SEQRES  38 A  544  ILE THR ILE LYS ALA SER LEU ASP ASP GLY LEU THR TRP          
SEQRES  39 A  544  LEU PRO GLU HIS GLN LEU MSE LEU ASP GLU GLY GLU GLY          
SEQRES  40 A  544  TRP GLY TYR SER CYS LEU THR MSE ILE ASP ARG GLU THR          
SEQRES  41 A  544  ILE GLY ILE LEU TYR GLU SER SER ALA ALA HIS MSE THR          
SEQRES  42 A  544  PHE GLN ALA VAL LYS LEU LYS ASP LEU ILE ARG                  
MODRES 4BBW MSE A   56  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A   57  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  150  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  188  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  251  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  294  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  307  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  317  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  355  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  378  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  389  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  392  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  411  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  414  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  450  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  501  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  515  MET  SELENOMETHIONINE                                   
MODRES 4BBW MSE A  532  MET  SELENOMETHIONINE                                   
HET    MSE  A  56       8                                                       
HET    MSE  A  57       8                                                       
HET    MSE  A 150       8                                                       
HET    MSE  A 188       8                                                       
HET    MSE  A 251       8                                                       
HET    MSE  A 294       8                                                       
HET    MSE  A 307       8                                                       
HET    MSE  A 317       8                                                       
HET    MSE  A 355       8                                                       
HET    MSE  A 378       8                                                       
HET    MSE  A 389       8                                                       
HET    MSE  A 392       8                                                       
HET    MSE  A 411       8                                                       
HET    MSE  A 414       8                                                       
HET    MSE  A 450       8                                                       
HET    MSE  A 501       8                                                       
HET    MSE  A 515       8                                                       
HET    MSE  A 532       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   2  MSE    18(C5 H11 N O2 SE)                                           
FORMUL   3  HOH   *238(H2 O)                                                    
HELIX    1   1 ASN A   69  SER A   71  5                                   3    
HELIX    2   2 ALA A   85  LYS A   92  5                                   8    
HELIX    3   3 ILE A  112  SER A  116  5                                   5    
HELIX    4   4 GLY A  196  SER A  200  5                                   5    
HELIX    5   5 GLU A  259  LEU A  263  5                                   5    
HELIX    6   6 PRO A  264  ASN A  268  5                                   5    
HELIX    7   7 ARG A  298  SER A  303  1                                   6    
HELIX    8   8 ILE A  333  LYS A  338  1                                   6    
HELIX    9   9 GLU A  457  ASN A  461  5                                   5    
HELIX   10  10 LEU A  495  GLU A  497  5                                   3    
HELIX   11  11 LEU A  539  ILE A  543  1                                   5    
SHEET    1  AA 6 ILE A 117  LEU A 123  0                                        
SHEET    2  AA 6 VAL A  73  TYR A  80 -1  O  VAL A  76   N  ALA A 122           
SHEET    3  AA 6 ILE A 141  MSE A 150 -1  O  TRP A 145   N  TYR A  79           
SHEET    4  AA 6 VAL A  43  ASP A  50 -1  N  LEU A  44   O  ILE A 146           
SHEET    5  AA 6 PHE A  27  GLN A  30 -1  O  PHE A  27   N  ARG A  48           
SHEET    6  AA 6 GLU A 177  GLU A 178  1  O  GLU A 177   N  VAL A  28           
SHEET    1  AB 2 ILE A  35  LEU A  36  0                                        
SHEET    2  AB 2 HIS A 186  ARG A 193  1  O  ARG A 187   N  ILE A  35           
SHEET    1  AC 2 LYS A 159  ILE A 160  0                                        
SHEET    2  AC 2 HIS A 186  ARG A 193 -1  O  HIS A 186   N  ILE A 160           
SHEET    1  AD 5 SER A 511  MSE A 515  0                                        
SHEET    2  AD 5 THR A 520  TYR A 525 -1  O  GLY A 522   N  THR A 514           
SHEET    3  AD 5 MSE A 532  LYS A 538 -1  O  THR A 533   N  TYR A 525           
SHEET    4  AD 5 HIS A 186  ARG A 193 -1  O  VAL A 190   N  PHE A 534           
SHEET    5  AD 5 LYS A 159  ILE A 160 -1  O  ILE A 160   N  HIS A 186           
SHEET    1  AE 5 SER A 511  MSE A 515  0                                        
SHEET    2  AE 5 THR A 520  TYR A 525 -1  O  GLY A 522   N  THR A 514           
SHEET    3  AE 5 MSE A 532  LYS A 538 -1  O  THR A 533   N  TYR A 525           
SHEET    4  AE 5 HIS A 186  ARG A 193 -1  O  VAL A 190   N  PHE A 534           
SHEET    5  AE 5 ILE A  35  LEU A  36  1  O  ILE A  35   N  ALA A 189           
SHEET    1  AF 4 LYS A 128  LYS A 136  0                                        
SHEET    2  AF 4 MSE A  56  ASP A  63 -1  O  MSE A  57   N  TYR A 135           
SHEET    3  AF 4 GLU A 163  ILE A 169 -1  O  GLU A 163   N  ASP A  63           
SHEET    4  AF 4 LYS A 172  GLU A 173 -1  O  LYS A 172   N  ILE A 169           
SHEET    1  AG 2 SER A 202  PHE A 203  0                                        
SHEET    2  AG 2 LEU A 216  ARG A 223  1  O  ARG A 223   N  SER A 202           
SHEET    1  AH 2 GLY A 207  THR A 210  0                                        
SHEET    2  AH 2 LEU A 216  ARG A 223 -1  O  LEU A 217   N  VAL A 209           
SHEET    1  AI 4 ARG A 252  LEU A 255  0                                        
SHEET    2  AI 4 VAL A 234  SER A 241 -1  O  VAL A 236   N  LEU A 255           
SHEET    3  AI 4 LEU A 216  ARG A 223 -1  O  LEU A 216   N  SER A 241           
SHEET    4  AI 4 GLY A 207  THR A 210 -1  O  GLY A 207   N  VAL A 219           
SHEET    1  AJ 4 ARG A 252  LEU A 255  0                                        
SHEET    2  AJ 4 VAL A 234  SER A 241 -1  O  VAL A 236   N  LEU A 255           
SHEET    3  AJ 4 LEU A 216  ARG A 223 -1  O  LEU A 216   N  SER A 241           
SHEET    4  AJ 4 SER A 202  PHE A 203  1  O  SER A 202   N  ARG A 223           
SHEET    1  AK 5 ILE A 331  ASN A 332  0                                        
SHEET    2  AK 5 GLN A 314  SER A 320 -1  O  MSE A 317   N  ILE A 331           
SHEET    3  AK 5 ILE A 284  TRP A 290 -1  O  ILE A 284   N  SER A 320           
SHEET    4  AK 5 VAL A 270  VAL A 277 -1  O  GLY A 271   N  ALA A 289           
SHEET    5  AK 5 GLY A 350  ARG A 351  1  O  GLY A 350   N  ILE A 275           
SHEET    1  AL 2 PHE A 344  GLN A 347  0                                        
SHEET    2  AL 2 LEU A 360  ILE A 367 -1  O  GLN A 365   N  LEU A 346           
SHEET    1  AM 2 ILE A 353  THR A 354  0                                        
SHEET    2  AM 2 LEU A 360  ILE A 367  1  O  VAL A 361   N  ILE A 353           
SHEET    1  AN 2 LYS A 388  MSE A 389  0                                        
SHEET    2  AN 2 PRO A 373  SER A 380  1  O  TYR A 379   N  LYS A 388           
SHEET    1  AO 2 ARG A 394  THR A 395  0                                        
SHEET    2  AO 2 PRO A 373  SER A 380 -1  N  ALA A 375   O  ARG A 394           
SHEET    1  AP 4 THR A 397  GLU A 406  0                                        
SHEET    2  AP 4 VAL A 409  ASP A 416 -1  O  VAL A 409   N  THR A 405           
SHEET    3  AP 4 ALA A 423  THR A 427 -1  O  ALA A 423   N  MSE A 414           
SHEET    4  AP 4 THR A 435  GLU A 436 -1  O  THR A 435   N  ILE A 426           
SHEET    1  AQ 4 SER A 452  VAL A 456  0                                        
SHEET    2  AQ 4 ILE A 467  PRO A 473 -1  O  ILE A 467   N  VAL A 456           
SHEET    3  AQ 4 ILE A 482  SER A 487 -1  O  THR A 483   N  ASN A 472           
SHEET    4  AQ 4 GLN A 499  ASP A 503 -1  O  LEU A 500   N  ILE A 484           
LINK         N   MSE A  56                 C   ARG A  55     1555   1555  1.33  
LINK         C   MSE A  56                 N   MSE A  57     1555   1555  1.33  
LINK         C   MSE A  57                 N   ASP A  58     1555   1555  1.33  
LINK         N   MSE A 150                 C   GLN A 149     1555   1555  1.34  
LINK         C   MSE A 150                 N   LYS A 151     1555   1555  1.33  
LINK         N   MSE A 188                 C   ARG A 187     1555   1555  1.33  
LINK         C   MSE A 188                 N   ALA A 189     1555   1555  1.33  
LINK         N   MSE A 251                 C   LYS A 250     1555   1555  1.34  
LINK         C   MSE A 251                 N   ARG A 252     1555   1555  1.33  
LINK         N   MSE A 294                 C   GLY A 293     1555   1555  1.33  
LINK         C   MSE A 294                 N   GLY A 295     1555   1555  1.33  
LINK         N   MSE A 307                 C   GLY A 306     1555   1555  1.32  
LINK         C   MSE A 307                 N   ASP A 308     1555   1555  1.34  
LINK         N   MSE A 317                 C   VAL A 316     1555   1555  1.33  
LINK         C   MSE A 317                 N   ALA A 318     1555   1555  1.33  
LINK         N   MSE A 355                 C   THR A 354     1555   1555  1.33  
LINK         C   MSE A 355                 N   SER A 356     1555   1555  1.34  
LINK         C   MSE A 378                 N   TYR A 379     1555   1555  1.32  
LINK         N   MSE A 378                 C   ILE A 377     1555   1555  1.33  
LINK         C   MSE A 389                 N   HIS A 390     1555   1555  1.33  
LINK         N   MSE A 389                 C   LYS A 388     1555   1555  1.33  
LINK         C   MSE A 392                 N   ALA A 393     1555   1555  1.33  
LINK         N   MSE A 392                 C   ASN A 391     1555   1555  1.33  
LINK         C   MSE A 411                 N   LEU A 412     1555   1555  1.33  
LINK         N   MSE A 411                 C   LEU A 410     1555   1555  1.33  
LINK         C   MSE A 414                 N   ARG A 415     1555   1555  1.33  
LINK         N   MSE A 414                 C   ASN A 413     1555   1555  1.33  
LINK         C   MSE A 450                 N   ALA A 451     1555   1555  1.33  
LINK         N   MSE A 450                 C   CYS A 449     1555   1555  1.32  
LINK         C   MSE A 501                 N   LEU A 502     1555   1555  1.33  
LINK         N   MSE A 501                 C   LEU A 500     1555   1555  1.32  
LINK         C   MSE A 515                 N   ILE A 516     1555   1555  1.32  
LINK         N   MSE A 515                 C   THR A 514     1555   1555  1.33  
LINK         C   MSE A 532                 N   THR A 533     1555   1555  1.33  
LINK         N   MSE A 532                 C   HIS A 531     1555   1555  1.33  
CRYST1  141.377   94.023   50.533  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007073  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010636  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019789        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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