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Database: PDB
Entry: 5IJ9
LinkDB: 5IJ9
Original site: 5IJ9 
HEADER    STRUCTURAL PROTEIN                      01-MAR-16   5IJ9              
TITLE     CRYO EM DENSITY OF MICROTUBULE ASSEMBLED FROM HUMAN TUBB3-D417H MUTANT
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUBULIN ALPHA-1B CHAIN;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA-TUBULIN UBIQUITOUS,TUBULIN K-ALPHA-1,TUBULIN ALPHA-   
COMPND   5 UBIQUITOUS CHAIN;                                                    
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: TUBULIN BETA-3 CHAIN;                                      
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: TUBULIN BETA-4 CHAIN,TUBULIN BETA-III;                      
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TUBA1B;                                                        
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: TUBB3, TUBB4;                                                  
SOURCE  13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 7111                                        
KEYWDS    HUMAN, MICROTUBULES, MUTANT TUBULIN, HYDROLYSIS, STRUCTURAL PROTEIN   
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.C.TI,M.C.PAMULA,S.C.HOWES,C.DUELLBERG,N.I.CADE,R.E.KLEINER,S.FORTH, 
AUTHOR   2 T.SURREY,E.NOGALES,T.M.KAPOOR                                        
REVDAT   3   25-DEC-19 5IJ9    1       REMARK                                   
REVDAT   2   27-SEP-17 5IJ9    1       REMARK                                   
REVDAT   1   20-APR-16 5IJ9    0                                                
JRNL        AUTH   S.C.TI,M.C.PAMULA,S.C.HOWES,C.DUELLBERG,N.I.CADE,            
JRNL        AUTH 2 R.E.KLEINER,S.FORTH,T.SURREY,E.NOGALES,T.M.KAPOOR            
JRNL        TITL   MUTATIONS IN HUMAN TUBULIN PROXIMAL TO THE KINESIN-BINDING   
JRNL        TITL 2 SITE ALTER DYNAMIC INSTABILITY AT MICROTUBULE PLUS- AND      
JRNL        TITL 3 MINUS-ENDS.                                                  
JRNL        REF    DEV.CELL                      V.  37    72 2016              
JRNL        REFN                   ISSN 1534-5807                               
JRNL        PMID   27046833                                                     
JRNL        DOI    10.1016/J.DEVCEL.2016.03.003                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : LEGINON, FREALIGN                         
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
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)  : 3.700                          
REMARK   3   NUMBER OF PARTICLES               : 26959                          
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 5IJ9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218859.                                   
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                 : MICROTUBULE ASSEMBLED FROM        
REMARK 245                                    RECOMBINANT HUMAN TUBULIN BETA-   
REMARK 245                                    3 D417H MUTANT DECORATED WITH     
REMARK 245                                    KINESIN                           
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)  : 27.60                          
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     SER A    38                                                      
REMARK 465     ASP A    39                                                      
REMARK 465     LYS A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     ILE A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     GLY A    44                                                      
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   O    ASP A    46     H    PHE A    49              1.54            
REMARK 500   O    SER A    48     OG1  THR A    51              2.06            
REMARK 500   O    ASN A   186     OG1  THR A   190              2.09            
REMARK 500   O    GLY A   146     OG1  THR A   150              2.12            
REMARK 500   OG   SER A    48     O    ARG A   243              2.16            
REMARK 500   NE2  GLN B    11     O1B  GDP B   501              2.19            
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    THR A  73     -119.84     40.26                                   
REMARK 500    LEU A  86      -64.77    -90.18                                   
REMARK 500    TYR A 108      -62.31   -128.67                                   
REMARK 500    ILE A 110      -60.52    -98.40                                   
REMARK 500    ILE A 114      -57.15   -121.38                                   
REMARK 500    HIS A 192      -70.54    -57.02                                   
REMARK 500    HIS A 197      -61.57   -129.00                                   
REMARK 500    THR A 225      -70.18    -55.85                                   
REMARK 500    MET A 313      -62.88    -90.52                                   
REMARK 500    PHE A 404       -2.35     68.37                                   
REMARK 500    GLN B  11     -119.40     59.40                                   
REMARK 500    GLU B  45      -73.16    -51.45                                   
REMARK 500    HIS B  57       -4.89     76.57                                   
REMARK 500    THR B 107      -77.28   -101.22                                   
REMARK 500    LYS B 174      -70.20    -90.79                                   
REMARK 500    VAL B 180       -3.27     67.15                                   
REMARK 500    LYS B 216       72.04     54.75                                   
REMARK 500    ALA B 218      -68.62   -129.94                                   
REMARK 500    CYS B 303      167.43    174.65                                   
REMARK 500    SER B 339       -9.29     87.17                                   
REMARK 500    ASN B 347       72.25     56.98                                   
REMARK 500    PHE B 394       -2.34     67.64                                   
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 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  71   OE2                                                    
REMARK 620 2 GTP A 501   O1G  93.5                                              
REMARK 620 3 GTP A 501   O3B 145.0  52.6                                        
REMARK 620 4 GTP A 501   O1B 114.7  64.7  62.6                                  
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 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP B 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-8095   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 5IJ0   RELATED DB: PDB                                   
REMARK 900 RELATED ID: EMD-8094   RELATED DB: EMDB                              
DBREF  5IJ9 A    1   437  UNP    P68363   TBA1B_HUMAN      1    437             
DBREF  5IJ9 B    1   426  UNP    Q13509   TBB3_HUMAN       1    426             
SEQADV 5IJ9 HIS B  417  UNP  Q13509    ASP   417 ENGINEERED MUTATION            
SEQRES   1 A  437  MET ARG GLU CYS ILE SER ILE HIS VAL GLY GLN ALA GLY          
SEQRES   2 A  437  VAL GLN ILE GLY ASN ALA CYS TRP GLU LEU TYR CYS LEU          
SEQRES   3 A  437  GLU HIS GLY ILE GLN PRO ASP GLY GLN MET PRO SER ASP          
SEQRES   4 A  437  LYS THR ILE GLY GLY GLY ASP ASP SER PHE ASN THR PHE          
SEQRES   5 A  437  PHE SER GLU THR GLY ALA GLY LYS HIS VAL PRO ARG ALA          
SEQRES   6 A  437  VAL PHE VAL ASP LEU GLU PRO THR VAL ILE ASP GLU VAL          
SEQRES   7 A  437  ARG THR GLY THR TYR ARG GLN LEU PHE HIS PRO GLU GLN          
SEQRES   8 A  437  LEU ILE THR GLY LYS GLU ASP ALA ALA ASN ASN TYR ALA          
SEQRES   9 A  437  ARG GLY HIS TYR THR ILE GLY LYS GLU ILE ILE ASP LEU          
SEQRES  10 A  437  VAL LEU ASP ARG ILE ARG LYS LEU ALA ASP GLN CYS THR          
SEQRES  11 A  437  GLY LEU GLN GLY PHE LEU VAL PHE HIS SER PHE GLY GLY          
SEQRES  12 A  437  GLY THR GLY SER GLY PHE THR SER LEU LEU MET GLU ARG          
SEQRES  13 A  437  LEU SER VAL ASP TYR GLY LYS LYS SER LYS LEU GLU PHE          
SEQRES  14 A  437  SER ILE TYR PRO ALA PRO GLN VAL SER THR ALA VAL VAL          
SEQRES  15 A  437  GLU PRO TYR ASN SER ILE LEU THR THR HIS THR THR LEU          
SEQRES  16 A  437  GLU HIS SER ASP CYS ALA PHE MET VAL ASP ASN GLU ALA          
SEQRES  17 A  437  ILE TYR ASP ILE CYS ARG ARG ASN LEU ASP ILE GLU ARG          
SEQRES  18 A  437  PRO THR TYR THR ASN LEU ASN ARG LEU ILE SER GLN ILE          
SEQRES  19 A  437  VAL SER SER ILE THR ALA SER LEU ARG PHE ASP GLY ALA          
SEQRES  20 A  437  LEU ASN VAL ASP LEU THR GLU PHE GLN THR ASN LEU VAL          
SEQRES  21 A  437  PRO TYR PRO ARG ILE HIS PHE PRO LEU ALA THR TYR ALA          
SEQRES  22 A  437  PRO VAL ILE SER ALA GLU LYS ALA TYR HIS GLU GLN LEU          
SEQRES  23 A  437  SER VAL ALA GLU ILE THR ASN ALA CYS PHE GLU PRO ALA          
SEQRES  24 A  437  ASN GLN MET VAL LYS CYS ASP PRO ARG HIS GLY LYS TYR          
SEQRES  25 A  437  MET ALA CYS CYS LEU LEU TYR ARG GLY ASP VAL VAL PRO          
SEQRES  26 A  437  LYS ASP VAL ASN ALA ALA ILE ALA THR ILE LYS THR LYS          
SEQRES  27 A  437  ARG SER ILE GLN PHE VAL ASP TRP CYS PRO THR GLY PHE          
SEQRES  28 A  437  LYS VAL GLY ILE ASN TYR GLN PRO PRO THR VAL VAL PRO          
SEQRES  29 A  437  GLY GLY ASP LEU ALA LYS VAL GLN ARG ALA VAL CYS MET          
SEQRES  30 A  437  LEU SER ASN THR THR ALA ILE ALA GLU ALA TRP ALA ARG          
SEQRES  31 A  437  LEU ASP HIS LYS PHE ASP LEU MET TYR ALA LYS ARG ALA          
SEQRES  32 A  437  PHE VAL HIS TRP TYR VAL GLY GLU GLY MET GLU GLU GLY          
SEQRES  33 A  437  GLU PHE SER GLU ALA ARG GLU ASP MET ALA ALA LEU GLU          
SEQRES  34 A  437  LYS ASP TYR GLU GLU VAL GLY VAL                              
SEQRES   1 B  426  MET ARG GLU ILE VAL HIS ILE GLN ALA GLY GLN CYS GLY          
SEQRES   2 B  426  ASN GLN ILE GLY ALA LYS PHE TRP GLU VAL ILE SER ASP          
SEQRES   3 B  426  GLU HIS GLY ILE ASP PRO SER GLY ASN TYR VAL GLY ASP          
SEQRES   4 B  426  SER ASP LEU GLN LEU GLU ARG ILE SER VAL TYR TYR ASN          
SEQRES   5 B  426  GLU ALA SER SER HIS LYS TYR VAL PRO ARG ALA ILE LEU          
SEQRES   6 B  426  VAL ASP LEU GLU PRO GLY THR MET ASP SER VAL ARG SER          
SEQRES   7 B  426  GLY ALA PHE GLY HIS LEU PHE ARG PRO ASP ASN PHE ILE          
SEQRES   8 B  426  PHE GLY GLN SER GLY ALA GLY ASN ASN TRP ALA LYS GLY          
SEQRES   9 B  426  HIS TYR THR GLU GLY ALA GLU LEU VAL ASP SER VAL LEU          
SEQRES  10 B  426  ASP VAL VAL ARG LYS GLU CYS GLU ASN CYS ASP CYS LEU          
SEQRES  11 B  426  GLN GLY PHE GLN LEU THR HIS SER LEU GLY GLY GLY THR          
SEQRES  12 B  426  GLY SER GLY MET GLY THR LEU LEU ILE SER LYS VAL ARG          
SEQRES  13 B  426  GLU GLU TYR PRO ASP ARG ILE MET ASN THR PHE SER VAL          
SEQRES  14 B  426  VAL PRO SER PRO LYS VAL SER ASP THR VAL VAL GLU PRO          
SEQRES  15 B  426  TYR ASN ALA THR LEU SER ILE HIS GLN LEU VAL GLU ASN          
SEQRES  16 B  426  THR ASP GLU THR TYR CYS ILE ASP ASN GLU ALA LEU TYR          
SEQRES  17 B  426  ASP ILE CYS PHE ARG THR LEU LYS LEU ALA THR PRO THR          
SEQRES  18 B  426  TYR GLY ASP LEU ASN HIS LEU VAL SER ALA THR MET SER          
SEQRES  19 B  426  GLY VAL THR THR SER LEU ARG PHE PRO GLY GLN LEU ASN          
SEQRES  20 B  426  ALA ASP LEU ARG LYS LEU ALA VAL ASN MET VAL PRO PHE          
SEQRES  21 B  426  PRO ARG LEU HIS PHE PHE MET PRO GLY PHE ALA PRO LEU          
SEQRES  22 B  426  THR ALA ARG GLY SER GLN GLN TYR ARG ALA LEU THR VAL          
SEQRES  23 B  426  PRO GLU LEU THR GLN GLN MET PHE ASP ALA LYS ASN MET          
SEQRES  24 B  426  MET ALA ALA CYS ASP PRO ARG HIS GLY ARG TYR LEU THR          
SEQRES  25 B  426  VAL ALA THR VAL PHE ARG GLY ARG MET SER MET LYS GLU          
SEQRES  26 B  426  VAL ASP GLU GLN MET LEU ALA ILE GLN SER LYS ASN SER          
SEQRES  27 B  426  SER TYR PHE VAL GLU TRP ILE PRO ASN ASN VAL LYS VAL          
SEQRES  28 B  426  ALA VAL CYS ASP ILE PRO PRO ARG GLY LEU LYS MET SER          
SEQRES  29 B  426  SER THR PHE ILE GLY ASN SER THR ALA ILE GLN GLU LEU          
SEQRES  30 B  426  PHE LYS ARG ILE SER GLU GLN PHE THR ALA MET PHE ARG          
SEQRES  31 B  426  ARG LYS ALA PHE LEU HIS TRP TYR THR GLY GLU GLY MET          
SEQRES  32 B  426  ASP GLU MET GLU PHE THR GLU ALA GLU SER ASN MET ASN          
SEQRES  33 B  426  HIS LEU VAL SER GLU TYR GLN GLN TYR GLN                      
HET    GTP  A 501      32                                                       
HET     MG  A 502       1                                                       
HET    GDP  B 501      28                                                       
HETNAM     GTP GUANOSINE-5'-TRIPHOSPHATE                                        
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   3  GTP    C10 H16 N5 O14 P3                                            
FORMUL   4   MG    MG 2+                                                        
FORMUL   5  GDP    C10 H15 N5 O11 P2                                            
HELIX    1 AA1 GLY A   10  HIS A   28  1                                  19    
HELIX    2 AA2 ASP A   46  ASN A   50  5                                   5    
HELIX    3 AA3 PRO A   72  GLY A   81  1                                  10    
HELIX    4 AA4 THR A   82  LEU A   86  5                                   5    
HELIX    5 AA5 ASN A  102  TYR A  108  1                                   7    
HELIX    6 AA6 ILE A  110  GLU A  113  5                                   4    
HELIX    7 AA7 ILE A  114  GLN A  128  1                                  15    
HELIX    8 AA8 GLY A  143  GLY A  162  1                                  20    
HELIX    9 AA9 VAL A  182  GLU A  196  1                                  15    
HELIX   10 AB1 ASP A  205  ASP A  218  1                                  14    
HELIX   11 AB2 THR A  223  PHE A  244  1                                  22    
HELIX   12 AB3 ASP A  251  VAL A  260  1                                  10    
HELIX   13 AB4 GLU A  279  GLU A  284  1                                   6    
HELIX   14 AB5 SER A  287  PHE A  296  1                                  10    
HELIX   15 AB6 GLU A  297  GLN A  301  5                                   5    
HELIX   16 AB7 ASP A  306  GLY A  310  5                                   5    
HELIX   17 AB8 VAL A  324  LYS A  338  1                                  15    
HELIX   18 AB9 THR A  382  LYS A  401  1                                  20    
HELIX   19 AC1 PHE A  404  GLU A  411  1                                   8    
HELIX   20 AC2 GLU A  414  VAL A  437  1                                  24    
HELIX   21 AC3 GLN B   11  HIS B   28  1                                  18    
HELIX   22 AC4 SER B   40  GLU B   45  1                                   6    
HELIX   23 AC5 ARG B   46  VAL B   49  5                                   4    
HELIX   24 AC6 GLU B   69  GLY B   79  1                                  11    
HELIX   25 AC7 ALA B   80  LEU B   84  5                                   5    
HELIX   26 AC8 ARG B   86  ASP B   88  5                                   3    
HELIX   27 AC9 ASN B  100  THR B  107  1                                   8    
HELIX   28 AD1 GLY B  109  ASN B  126  1                                  18    
HELIX   29 AD2 GLY B  141  TYR B  159  1                                  19    
HELIX   30 AD3 VAL B  180  THR B  196  1                                  17    
HELIX   31 AD4 ASP B  203  THR B  214  1                                  12    
HELIX   32 AD5 THR B  221  PHE B  242  1                                  22    
HELIX   33 AD6 ASP B  249  VAL B  258  1                                  10    
HELIX   34 AD7 SER B  278  ARG B  282  5                                   5    
HELIX   35 AD8 THR B  285  PHE B  294  1                                  10    
HELIX   36 AD9 ASP B  295  MET B  299  5                                   5    
HELIX   37 AE1 SER B  322  ASN B  337  1                                  16    
HELIX   38 AE2 THR B  372  ARG B  391  1                                  20    
HELIX   39 AE3 PHE B  394  GLU B  401  1                                   8    
HELIX   40 AE4 ASP B  404  TYR B  425  1                                  22    
SHEET    1 AA1 6 LEU A  92  THR A  94  0                                        
SHEET    2 AA1 6 ALA A  65  ASP A  69  1  N  PHE A  67   O  ILE A  93           
SHEET    3 AA1 6 GLU A   3  VAL A   9  1  N  HIS A   8   O  VAL A  68           
SHEET    4 AA1 6 LEU A 132  SER A 140  1  O  PHE A 138   N  ILE A   7           
SHEET    5 AA1 6 SER A 165  ILE A 171  1  O  PHE A 169   N  VAL A 137           
SHEET    6 AA1 6 CYS A 200  VAL A 204  1  O  PHE A 202   N  GLU A 168           
SHEET    1 AA2 2 PHE A  53  GLU A  55  0                                        
SHEET    2 AA2 2 HIS A  61  PRO A  63 -1  O  VAL A  62   N  SER A  54           
SHEET    1 AA3 4 LEU A 269  ALA A 273  0                                        
SHEET    2 AA3 4 ARG A 373  SER A 379 -1  O  SER A 379   N  LEU A 269           
SHEET    3 AA3 4 CYS A 315  GLY A 321 -1  N  CYS A 316   O  LEU A 378           
SHEET    4 AA3 4 PHE A 351  ILE A 355  1  O  GLY A 354   N  LEU A 317           
SHEET    1 AA411 PHE B  90  PHE B  92  0                                        
SHEET    2 AA411 ALA B  63  ASP B  67  1  N  LEU B  65   O  ILE B  91           
SHEET    3 AA411 ARG B   2  GLN B   8  1  N  GLN B   8   O  VAL B  66           
SHEET    4 AA411 CYS B 129  SER B 138  1  O  GLN B 134   N  ILE B   7           
SHEET    5 AA411 ILE B 163  VAL B 169  1  O  ILE B 163   N  PHE B 133           
SHEET    6 AA411 GLU B 198  ILE B 202  1  O  TYR B 200   N  THR B 166           
SHEET    7 AA411 PHE B 265  ALA B 271  1  O  PHE B 266   N  CYS B 201           
SHEET    8 AA411 MET B 363  ASN B 370 -1  O  SER B 365   N  ALA B 271           
SHEET    9 AA411 THR B 312  GLY B 319 -1  N  ARG B 318   O  SER B 364           
SHEET   10 AA411 VAL B 349  CYS B 354  1  O  CYS B 354   N  PHE B 317           
SHEET   11 AA411 GLY B 244  GLN B 245 -1  N  GLN B 245   O  VAL B 353           
SHEET    1 AA5 2 TYR B  51  GLU B  53  0                                        
SHEET    2 AA5 2 TYR B  59  PRO B  61 -1  O  VAL B  60   N  ASN B  52           
LINK         OE2 GLU A  71                MG    MG A 502     1555   1555  2.55  
LINK         O1G GTP A 501                MG    MG A 502     1555   1555  2.98  
LINK         O3B GTP A 501                MG    MG A 502     1555   1555  2.73  
LINK         O1B GTP A 501                MG    MG A 502     1555   1555  2.09  
CISPEP   1 ALA A  273    PRO A  274          0        -4.45                     
CISPEP   2 ALA B  271    PRO B  272          0        -3.97                     
SITE     1 AC1 20 GLY A  10  GLN A  11  ALA A  12  GLN A  15                    
SITE     2 AC1 20 ASP A  98  ALA A  99  ALA A 100  ASN A 101                    
SITE     3 AC1 20 SER A 140  GLY A 144  THR A 145  ILE A 171                    
SITE     4 AC1 20 THR A 179  GLU A 183  ASN A 206  TYR A 224                    
SITE     5 AC1 20 ASN A 228   MG A 502  LEU B 246  LYS B 252                    
SITE     1 AC2  3 ASP A  69  GLU A  71  GTP A 501                               
SITE     1 AC3 12 GLN B  11  CYS B  12  GLN B  15  ASN B  99                    
SITE     2 AC3 12 SER B 138  GLY B 141  GLY B 142  THR B 143                    
SITE     3 AC3 12 ASP B 177  ASN B 204  TYR B 222  ASN B 226                    
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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