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Database: PDB
Entry: 5W3J
LinkDB: 5W3J
Original site: 5W3J 
HEADER    HYDROLASE                               07-JUN-17   5W3J              
TITLE     YEAST MICROTUBULE STABILIZED WITH TAXOL ASSEMBLED FROM MUTATED TUBULIN
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUBULIN ALPHA-1 CHAIN;                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TUBULIN BETA CHAIN;                                        
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: BETA-TUBULIN;                                               
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /    
SOURCE   7 S288C);                                                              
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 559292;                                     
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE  11 S288C);                                                              
SOURCE  12 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  13 ORGANISM_TAXID: 559292;                                              
SOURCE  14 EXPRESSION_SYSTEM: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /    
SOURCE  15 S288C);                                                              
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 559292                                      
KEYWDS    CYTOSKELETON, TUBULIN, HYDROLASE                                      
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.C.HOWES,E.A.GEYER,B.LAFRANCE,R.ZHANG,E.H.KELLOGG,S.WESTERMANN,      
AUTHOR   2 L.M.RICE,E.NOGALES                                                   
REVDAT   7   18-DEC-19 5W3J    1       SCALE                                    
REVDAT   6   27-NOV-19 5W3J    1       REMARK                                   
REVDAT   5   29-AUG-18 5W3J    1       COMPND SOURCE                            
REVDAT   4   15-AUG-18 5W3J    1       CRYST1                                   
REVDAT   3   08-NOV-17 5W3J    1       REMARK                                   
REVDAT   2   20-SEP-17 5W3J    1       JRNL   REMARK                            
REVDAT   1   19-JUL-17 5W3J    0                                                
JRNL        AUTH   S.C.HOWES,E.A.GEYER,B.LAFRANCE,R.ZHANG,E.H.KELLOGG,          
JRNL        AUTH 2 S.WESTERMANN,L.M.RICE,E.NOGALES                              
JRNL        TITL   STRUCTURAL DIFFERENCES BETWEEN YEAST AND MAMMALIAN           
JRNL        TITL 2 MICROTUBULES REVEALED BY CRYO-EM.                            
JRNL        REF    J. CELL BIOL.                 V. 216  2669 2017              
JRNL        REFN                   ESSN 1540-8140                               
JRNL        PMID   28652389                                                     
JRNL        DOI    10.1083/JCB.201612195                                        
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : CTFFIND, FREALIGN                         
REMARK   3   RECONSTRUCTION SCHEMA  : FOURIER SPACE                             
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 4.000                          
REMARK   3   NUMBER OF PARTICLES               : 30101                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 5W3J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228363.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : HELICAL                           
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : HELICAL ARRAY                     
REMARK 245   PARTICLE TYPE                  : HELICAL                           
REMARK 245   NAME OF SAMPLE                 : YEAST MICROTUBULE STABILIZED      
REMARK 245                                    WITH TAXOL ASSEMBLED FROM         
REMARK 245                                    MUTATED TUBULIN                   
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 6.90                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN                      
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 28.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
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 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     TYR A   441                                                      
REMARK 465     ALA A   442                                                      
REMARK 465     GLU A   443                                                      
REMARK 465     GLU A   444                                                      
REMARK 465     GLU A   445                                                      
REMARK 465     GLU A   446                                                      
REMARK 465     PHE A   447                                                      
REMARK 465     ALA B   428                                                      
REMARK 465     THR B   429                                                      
REMARK 465     VAL B   430                                                      
REMARK 465     GLU B   431                                                      
REMARK 465     ASP B   432                                                      
REMARK 465     ASP B   433                                                      
REMARK 465     GLU B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     VAL B   436                                                      
REMARK 465     ASP B   437                                                      
REMARK 465     GLU B   438                                                      
REMARK 465     ASN B   439                                                      
REMARK 465     GLY B   440                                                      
REMARK 465     ASP B   441                                                      
REMARK 465     PHE B   442                                                      
REMARK 465     GLY B   443                                                      
REMARK 465     ALA B   444                                                      
REMARK 465     PRO B   445                                                      
REMARK 465     GLN B   446                                                      
REMARK 465     ASN B   447                                                      
REMARK 465     GLN B   448                                                      
REMARK 465     ASP B   449                                                      
REMARK 465     GLU B   450                                                      
REMARK 465     PRO B   451                                                      
REMARK 465     ILE B   452                                                      
REMARK 465     THR B   453                                                      
REMARK 465     GLU B   454                                                      
REMARK 465     ASN B   455                                                      
REMARK 465     PHE B   456                                                      
REMARK 465     GLU B   457                                                      
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    ARG A   2     -103.23   -126.65                                   
REMARK 500    ASP A  38       80.63     57.97                                   
REMARK 500    LEU A  40     -111.75     55.86                                   
REMARK 500    SER A  41     -142.67    -94.72                                   
REMARK 500    LYS A  42      155.26     67.48                                   
REMARK 500    LYS A  44       34.36    -86.60                                   
REMARK 500    THR A  52      138.51     66.53                                   
REMARK 500    PHE A  53      -68.68     61.05                                   
REMARK 500    THR A  57     -138.40   -112.83                                   
REMARK 500    LEU A  87      -76.19    -72.99                                   
REMARK 500    ALA A 101     -134.65     59.00                                   
REMARK 500    THR A 110      -76.05    -95.15                                   
REMARK 500    GLN A 134      -69.88    -90.50                                   
REMARK 500    TYR A 162      -96.50    -94.94                                   
REMARK 500    GLN A 177      -90.30   -104.29                                   
REMARK 500    VAL A 183       31.87    -93.41                                   
REMARK 500    HIS A 198      -52.54   -144.69                                   
REMARK 500    PHE A 245     -153.98   -139.46                                   
REMARK 500    ARG A 265     -166.86   -106.87                                   
REMARK 500    ILE A 266       86.12     58.05                                   
REMARK 500    HIS A 267       57.93   -143.99                                   
REMARK 500    PRO A 275       72.75    -65.33                                   
REMARK 500    GLN A 343       73.32     56.49                                   
REMARK 500    THR A 350      -92.89   -121.18                                   
REMARK 500    ASN A 366       38.33    -88.26                                   
REMARK 500    ARG A 403       76.60     56.28                                   
REMARK 500    ALA A 404      -82.90    -76.31                                   
REMARK 500    HIS B  37      -68.68    -91.48                                   
REMARK 500    ALA B  54     -135.15    -87.09                                   
REMARK 500    SER B  79     -141.52    -92.19                                   
REMARK 500    ILE B  81      -16.09   -151.30                                   
REMARK 500    PRO B  87       28.28    -75.26                                   
REMARK 500    TYR B 106       -6.07   -152.12                                   
REMARK 500    THR B 107      -76.19   -101.04                                   
REMARK 500    LEU B 112      -99.21    -79.56                                   
REMARK 500    VAL B 113      -73.52     58.08                                   
REMARK 500    GLN B 131      -68.41   -123.05                                   
REMARK 500    PHE B 167       78.52   -111.55                                   
REMARK 500    THR B 175       88.95     56.95                                   
REMARK 500    VAL B 180       43.59    -89.54                                   
REMARK 500    HIS B 195      -44.73   -137.03                                   
REMARK 500    ARG B 213      -57.10   -123.36                                   
REMARK 500    GLN B 219       78.92     56.49                                   
REMARK 500    HIS B 264       17.48   -143.58                                   
REMARK 500    PRO B 272     -153.52    -89.44                                   
REMARK 500    SER B 278       47.96    -99.99                                   
REMARK 500    MET B 300       31.40    -88.69                                   
REMARK 500    LEU B 311      -69.75   -123.89                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A  11   OE1                                                    
REMARK 620 2 GLU A  72   OE1  72.6                                              
REMARK 620 3 GTP A 500   O1G 105.8 113.1                                        
REMARK 620 4 GTP A 500   O3G 124.8 158.2  53.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GTP A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TA1 B 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-8757   RELATED DB: EMDB                              
REMARK 900 YEAST MICROTUBULE STABILIZED WITH TAXOL ASSEMBLED FROM MUTATED       
REMARK 900 TUBULIN                                                              
REMARK 900 RELATED ID: EMD-8755   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8759   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8758   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-8756   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 5W3F   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5W3H   RELATED DB: PDB                                   
DBREF  5W3J A    1   447  UNP    P09733   TBA1_YEAST       1    447             
DBREF  5W3J B    1   457  UNP    P02557   TBB_YEAST        1    457             
SEQADV 5W3J LYS B   19  UNP  P02557    ALA    19 ENGINEERED MUTATION            
SEQADV 5W3J VAL B   23  UNP  P02557    THR    23 ENGINEERED MUTATION            
SEQADV 5W3J ASP B   26  UNP  P02557    GLY    26 ENGINEERED MUTATION            
SEQADV 5W3J HIS B  227  UNP  P02557    ASN   227 ENGINEERED MUTATION            
SEQADV 5W3J PHE B  270  UNP  P02557    TYR   270 ENGINEERED MUTATION            
SEQRES   1 A  447  MET ARG GLU VAL ILE SER ILE ASN VAL GLY GLN ALA GLY          
SEQRES   2 A  447  CYS GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR SER LEU          
SEQRES   3 A  447  GLU HIS GLY ILE LYS PRO ASP GLY HIS LEU GLU ASP GLY          
SEQRES   4 A  447  LEU SER LYS PRO LYS GLY GLY GLU GLU GLY PHE SER THR          
SEQRES   5 A  447  PHE PHE HIS GLU THR GLY TYR GLY LYS PHE VAL PRO ARG          
SEQRES   6 A  447  ALA ILE TYR VAL ASP LEU GLU PRO ASN VAL ILE ASP GLU          
SEQRES   7 A  447  VAL ARG ASN GLY PRO TYR LYS ASP LEU PHE HIS PRO GLU          
SEQRES   8 A  447  GLN LEU ILE SER GLY LYS GLU ASP ALA ALA ASN ASN TYR          
SEQRES   9 A  447  ALA ARG GLY HIS TYR THR VAL GLY ARG GLU ILE LEU GLY          
SEQRES  10 A  447  ASP VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS          
SEQRES  11 A  447  ASP GLY LEU GLN GLY PHE LEU PHE THR HIS SER LEU GLY          
SEQRES  12 A  447  GLY GLY THR GLY SER GLY LEU GLY SER LEU LEU LEU GLU          
SEQRES  13 A  447  GLU LEU SER ALA GLU TYR GLY LYS LYS SER LYS LEU GLU          
SEQRES  14 A  447  PHE ALA VAL TYR PRO ALA PRO GLN VAL SER THR SER VAL          
SEQRES  15 A  447  VAL GLU PRO TYR ASN THR VAL LEU THR THR HIS THR THR          
SEQRES  16 A  447  LEU GLU HIS ALA ASP CYS THR PHE MET VAL ASP ASN GLU          
SEQRES  17 A  447  ALA ILE TYR ASP MET CYS LYS ARG ASN LEU ASP ILE PRO          
SEQRES  18 A  447  ARG PRO SER PHE ALA ASN LEU ASN ASN LEU ILE ALA GLN          
SEQRES  19 A  447  VAL VAL SER SER VAL THR ALA SER LEU ARG PHE ASP GLY          
SEQRES  20 A  447  SER LEU ASN VAL ASP LEU ASN GLU PHE GLN THR ASN LEU          
SEQRES  21 A  447  VAL PRO TYR PRO ARG ILE HIS PHE PRO LEU VAL SER TYR          
SEQRES  22 A  447  SER PRO VAL LEU SER LYS SER LYS ALA PHE HIS GLU SER          
SEQRES  23 A  447  ASN SER VAL SER GLU ILE THR ASN ALA CYS PHE GLU PRO          
SEQRES  24 A  447  GLY ASN GLN MET VAL LYS CYS ASP PRO ARG ASP GLY LYS          
SEQRES  25 A  447  TYR MET ALA THR CYS LEU LEU TYR ARG GLY ASP VAL VAL          
SEQRES  26 A  447  THR ARG ASP VAL GLN ARG ALA VAL GLU GLN VAL LYS ASN          
SEQRES  27 A  447  LYS LYS THR VAL GLN LEU VAL ASP TRP CYS PRO THR GLY          
SEQRES  28 A  447  PHE LYS ILE GLY ILE CYS TYR GLU PRO PRO THR ALA THR          
SEQRES  29 A  447  PRO ASN SER GLN LEU ALA THR VAL ASP ARG ALA VAL CYS          
SEQRES  30 A  447  MET LEU SER ASN THR THR SER ILE ALA GLU ALA TRP LYS          
SEQRES  31 A  447  ARG ILE ASP ARG LYS PHE ASP LEU MET TYR ALA LYS ARG          
SEQRES  32 A  447  ALA PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU          
SEQRES  33 A  447  GLY GLU PHE THR GLU ALA ARG GLU ASP LEU ALA ALA LEU          
SEQRES  34 A  447  GLU ARG ASP TYR ILE GLU VAL GLY ALA ASP SER TYR ALA          
SEQRES  35 A  447  GLU GLU GLU GLU PHE                                          
SEQRES   1 B  457  MET ARG GLU ILE ILE HIS ILE SER THR GLY GLN CYS GLY          
SEQRES   2 B  457  ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE CYS ASP          
SEQRES   3 B  457  GLU HIS GLY LEU ASP PHE ASN GLY THR TYR HIS GLY HIS          
SEQRES   4 B  457  ASP ASP ILE GLN LYS GLU ARG LEU ASN VAL TYR PHE ASN          
SEQRES   5 B  457  GLU ALA SER SER GLY LYS TRP VAL PRO ARG SER ILE ASN          
SEQRES   6 B  457  VAL ASP LEU GLU PRO GLY THR ILE ASP ALA VAL ARG ASN          
SEQRES   7 B  457  SER ALA ILE GLY ASN LEU PHE ARG PRO ASP ASN TYR ILE          
SEQRES   8 B  457  PHE GLY GLN SER SER ALA GLY ASN VAL TRP ALA LYS GLY          
SEQRES   9 B  457  HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL MET          
SEQRES  10 B  457  ASP VAL ILE ARG ARG GLU ALA GLU GLY CYS ASP SER LEU          
SEQRES  11 B  457  GLN GLY PHE GLN ILE THR HIS SER LEU GLY GLY GLY THR          
SEQRES  12 B  457  GLY SER GLY MET GLY THR LEU LEU ILE SER LYS ILE ARG          
SEQRES  13 B  457  GLU GLU PHE PRO ASP ARG MET MET ALA THR PHE SER VAL          
SEQRES  14 B  457  LEU PRO SER PRO LYS THR SER ASP THR VAL VAL GLU PRO          
SEQRES  15 B  457  TYR ASN ALA THR LEU SER VAL HIS GLN LEU VAL GLU HIS          
SEQRES  16 B  457  SER ASP GLU THR PHE CYS ILE ASP ASN GLU ALA LEU TYR          
SEQRES  17 B  457  ASP ILE CYS GLN ARG THR LEU LYS LEU ASN GLN PRO SER          
SEQRES  18 B  457  TYR GLY ASP LEU ASN HIS LEU VAL SER SER VAL MET SER          
SEQRES  19 B  457  GLY VAL THR THR SER LEU ARG TYR PRO GLY GLN LEU ASN          
SEQRES  20 B  457  SER ASP LEU ARG LYS LEU ALA VAL ASN LEU VAL PRO PHE          
SEQRES  21 B  457  PRO ARG LEU HIS PHE PHE MET VAL GLY PHE ALA PRO LEU          
SEQRES  22 B  457  THR ALA ILE GLY SER GLN SER PHE ARG SER LEU THR VAL          
SEQRES  23 B  457  PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET          
SEQRES  24 B  457  MET ALA ALA ALA ASP PRO ARG ASN GLY ARG TYR LEU THR          
SEQRES  25 B  457  VAL ALA ALA PHE PHE ARG GLY LYS VAL SER VAL LYS GLU          
SEQRES  26 B  457  VAL GLU ASP GLU MET HIS LYS VAL GLN SER LYS ASN SER          
SEQRES  27 B  457  ASP TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL GLN THR          
SEQRES  28 B  457  ALA VAL CYS SER VAL ALA PRO GLN GLY LEU ASP MET ALA          
SEQRES  29 B  457  ALA THR PHE ILE ALA ASN SER THR SER ILE GLN GLU LEU          
SEQRES  30 B  457  PHE LYS ARG VAL GLY ASP GLN PHE SER ALA MET PHE LYS          
SEQRES  31 B  457  ARG LYS ALA PHE LEU HIS TRP TYR THR SER GLU GLY MET          
SEQRES  32 B  457  ASP GLU LEU GLU PHE SER GLU ALA GLU SER ASN MET ASN          
SEQRES  33 B  457  ASP LEU VAL SER GLU TYR GLN GLN TYR GLN GLU ALA THR          
SEQRES  34 B  457  VAL GLU ASP ASP GLU GLU VAL ASP GLU ASN GLY ASP PHE          
SEQRES  35 B  457  GLY ALA PRO GLN ASN GLN ASP GLU PRO ILE THR GLU ASN          
SEQRES  36 B  457  PHE GLU                                                      
HET    GTP  A 500      32                                                       
HET     MG  A 501       1                                                       
HET    GDP  B 501      28                                                       
HET    TA1  B 502      62                                                       
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     TA1 TAXOL                                                            
FORMUL   3  GTP    C10 H16 N5 O14 P3                                            
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  GDP    C10 H15 N5 O11 P2                                            
FORMUL   6  TA1    C47 H51 N O14                                                
HELIX    1 AA1 GLY A   10  HIS A   28  1                                  19    
HELIX    2 AA2 GLY A   46  SER A   51  1                                   6    
HELIX    3 AA3 GLU A   72  ASN A   81  1                                  10    
HELIX    4 AA4 HIS A   89  LEU A   93  5                                   5    
HELIX    5 AA5 THR A  110  ILE A  115  1                                   6    
HELIX    6 AA6 ILE A  115  GLN A  129  1                                  15    
HELIX    7 AA7 SER A  148  TYR A  162  1                                  15    
HELIX    8 AA8 PRO A  185  LEU A  196  1                                  12    
HELIX    9 AA9 ASP A  206  ARG A  216  1                                  11    
HELIX   10 AB1 SER A  224  THR A  240  1                                  17    
HELIX   11 AB2 THR A  240  PHE A  245  1                                   6    
HELIX   12 AB3 ASP A  252  PHE A  256  5                                   5    
HELIX   13 AB4 SER A  288  ALA A  295  1                                   8    
HELIX   14 AB5 GLU A  298  GLN A  302  5                                   5    
HELIX   15 AB6 VAL A  325  ASN A  338  1                                  14    
HELIX   16 AB7 SER A  384  LYS A  402  1                                  19    
HELIX   17 AB8 VAL A  406  GLY A  411  1                                   6    
HELIX   18 AB9 GLY A  417  ASP A  439  1                                  23    
HELIX   19 AC1 GLY B   10  HIS B   28  1                                  19    
HELIX   20 AC2 GLN B   43  LEU B   47  5                                   5    
HELIX   21 AC3 GLU B   69  ASN B   78  1                                  10    
HELIX   22 AC4 SER B  115  CYS B  127  1                                  13    
HELIX   23 AC5 GLY B  142  PHE B  159  1                                  18    
HELIX   24 AC6 VAL B  180  GLN B  191  1                                  12    
HELIX   25 AC7 ASN B  204  GLN B  212  1                                   9    
HELIX   26 AC8 SER B  221  THR B  237  1                                  17    
HELIX   27 AC9 ARG B  251  ASN B  256  1                                   6    
HELIX   28 AD1 THR B  285  PHE B  294  1                                  10    
HELIX   29 AD2 SER B  322  ASN B  337  1                                  16    
HELIX   30 AD3 SER B  371  SER B  373  5                                   3    
HELIX   31 AD4 ILE B  374  ARG B  391  1                                  18    
HELIX   32 AD5 LEU B  395  SER B  400  1                                   6    
HELIX   33 AD6 ASP B  404  GLU B  427  1                                  24    
SHEET    1 AA1 5 ALA A  66  VAL A  69  0                                        
SHEET    2 AA1 5 GLU A   3  VAL A   9  1  N  ASN A   8   O  VAL A  69           
SHEET    3 AA1 5 LEU A 133  THR A 139  1  O  LEU A 137   N  ILE A   7           
SHEET    4 AA1 5 SER A 166  GLU A 169  1  O  SER A 166   N  PHE A 136           
SHEET    5 AA1 5 CYS A 201  THR A 202  1  O  CYS A 201   N  GLU A 169           
SHEET    1 AA2 2 PHE A  54  GLU A  56  0                                        
SHEET    2 AA2 2 PHE A  62  PRO A  64 -1  O  VAL A  63   N  HIS A  55           
SHEET    1 AA3 4 SER A 272  TYR A 273  0                                        
SHEET    2 AA3 4 ARG A 374  MET A 378 -1  O  MET A 378   N  SER A 272           
SHEET    3 AA3 4 TYR A 313  GLY A 322 -1  N  ARG A 321   O  ALA A 375           
SHEET    4 AA3 4 PHE A 352  LYS A 353  1  O  LYS A 353   N  LEU A 318           
SHEET    1 AA4 4 SER A 272  TYR A 273  0                                        
SHEET    2 AA4 4 ARG A 374  MET A 378 -1  O  MET A 378   N  SER A 272           
SHEET    3 AA4 4 TYR A 313  GLY A 322 -1  N  ARG A 321   O  ALA A 375           
SHEET    4 AA4 4 ASN A 381  THR A 382 -1  O  ASN A 381   N  MET A 314           
SHEET    1 AA5 6 ILE B  64  VAL B  66  0                                        
SHEET    2 AA5 6 GLU B   3  THR B   9  1  N  SER B   8   O  VAL B  66           
SHEET    3 AA5 6 LEU B 130  THR B 136  1  O  GLN B 134   N  ILE B   7           
SHEET    4 AA5 6 MET B 163  PHE B 167  1  O  PHE B 167   N  ILE B 135           
SHEET    5 AA5 6 GLU B 198  ASP B 203  1  O  GLU B 198   N  THR B 166           
SHEET    6 AA5 6 VAL B 169  LEU B 170  1  N  LEU B 170   O  ILE B 202           
SHEET    1 AA6 6 ILE B  64  VAL B  66  0                                        
SHEET    2 AA6 6 GLU B   3  THR B   9  1  N  SER B   8   O  VAL B  66           
SHEET    3 AA6 6 LEU B 130  THR B 136  1  O  GLN B 134   N  ILE B   7           
SHEET    4 AA6 6 MET B 163  PHE B 167  1  O  PHE B 167   N  ILE B 135           
SHEET    5 AA6 6 GLU B 198  ASP B 203  1  O  GLU B 198   N  THR B 166           
SHEET    6 AA6 6 PHE B 265  MET B 267  1  O  PHE B 266   N  CYS B 201           
SHEET    1 AA7 2 PHE B  51  GLU B  53  0                                        
SHEET    2 AA7 2 TRP B  59  PRO B  61 -1  O  VAL B  60   N  ASN B  52           
SHEET    1 AA8 4 PHE B 270  ALA B 271  0                                        
SHEET    2 AA8 4 MET B 363  ASN B 370 -1  O  ALA B 365   N  ALA B 271           
SHEET    3 AA8 4 THR B 312  GLY B 319 -1  N  ALA B 314   O  ILE B 368           
SHEET    4 AA8 4 VAL B 349  GLN B 350  1  O  GLN B 350   N  VAL B 313           
LINK         OE1 GLN A  11                MG    MG A 501     1555   1555  2.26  
LINK         OE1 GLU A  72                MG    MG A 501     1555   1555  2.90  
LINK         O1G GTP A 500                MG    MG A 501     1555   1555  2.43  
LINK         O3G GTP A 500                MG    MG A 501     1555   1555  2.99  
CISPEP   1 ALA B  271    PRO B  272          0        -1.27                     
SITE     1 AC1 16 GLY A  10  GLN A  11  ALA A  12  GLN A  15                    
SITE     2 AC1 16 ALA A 101  SER A 141  GLY A 143  GLY A 144                    
SITE     3 AC1 16 THR A 146  THR A 180  ASN A 207  PHE A 225                    
SITE     4 AC1 16 LEU A 228  ASN A 229   MG A 501  LYS B 252                    
SITE     1 AC2  3 GLN A  11  GLU A  72  GTP A 500                               
SITE     1 AC3 14 GLN B  11  CYS B  12  GLN B  15  GLY B  98                    
SITE     2 AC3 14 ASN B  99  GLY B 141  GLY B 142  THR B 143                    
SITE     3 AC3 14 GLY B 144  ASP B 177  ASN B 204  LEU B 207                    
SITE     4 AC3 14 TYR B 222  ASN B 226                                          
SITE     1 AC4  8 VAL B  23  ASP B  26  GLU B  27  HIS B 227                    
SITE     2 AC4  8 THR B 274  GLN B 359  GLY B 360  LEU B 361                    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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