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Database: PDB
Entry: 5JM9
LinkDB: 5JM9
Original site: 5JM9 
HEADER    HYDROLASE                               28-APR-16   5JM9              
TITLE     STRUCTURE OF S. CEREVESIAE MAPE1 DODECAMER                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VACUOLAR AMINOPEPTIDASE 1;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: AMINOPEPTIDASE YSCI,LEUCINE AMINOPEPTIDASE IV,LAPIV,        
COMPND   5 LYSOSOMAL AMINOPEPTIDASE III,POLYPEPTIDASE,VACUOLAR AMINOPEPTIDASE I;
COMPND   6 EC: 3.4.11.22;                                                       
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: APE1, API, LAP4, YSC1, YKL103C, YKL455;                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: RIL;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PETM33                                     
KEYWDS    DODECAMER, AMINOPEPTIDASE, VACUOLE, CVT, HYDROLASE                    
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    C.SACHSE,C.BERTIPAGLIA                                                
REVDAT   6   30-AUG-17 5JM9    1       REMARK                                   
REVDAT   5   02-AUG-17 5JM9    1                                                
REVDAT   4   13-JUL-16 5JM9    1       JRNL                                     
REVDAT   3   29-JUN-16 5JM9    1       JRNL                                     
REVDAT   2   22-JUN-16 5JM9    1       JRNL                                     
REVDAT   1   15-JUN-16 5JM9    0                                                
JRNL        AUTH   C.BERTIPAGLIA,S.SCHNEIDER,A.J.JAKOBI,A.K.TARAFDER,Y.S.BYKOV, 
JRNL        AUTH 2 A.PICCO,W.KUKULSKI,J.KOSINSKI,W.J.HAGEN,A.C.RAVICHANDRAN,    
JRNL        AUTH 3 M.WILMANNS,M.KAKSONEN,J.A.BRIGGS,C.SACHSE                    
JRNL        TITL   HIGHER-ORDER ASSEMBLIES OF OLIGOMERIC CARGO RECEPTOR         
JRNL        TITL 2 COMPLEXES FORM THE MEMBRANE SCAFFOLD OF THE CVT VESICLE.     
JRNL        REF    EMBO REP.                     V.  17  1044 2016              
JRNL        REFN                   ESSN 1469-3178                               
JRNL        PMID   27266708                                                     
JRNL        DOI    10.15252/EMBR.201541960                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.   24.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : EMAN, UCSF CHIMERA, EMAN, SPIDER,         
REMARK   3                            SPIDER                                    
REMARK   3   RECONSTRUCTION SCHEMA  : BACK PROJECTION                           
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 4R8F                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : CROSS-CORRELATION COEFFICIENT       
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)  : 24.00                          
REMARK   3   NUMBER OF PARTICLES               : 5481                           
REMARK   3   CTF CORRECTION METHOD             : NONE                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 5JM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220862.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : MATURE AMINOPEPTIDASE-1           
REMARK 245                                    DODECAMER                         
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                             : 7.50                              
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/PHILIPS CM12               
REMARK 245   DETECTOR TYPE                     : TVIPS TEMCAM-F415 (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)  : 40.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 53000                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : LAB6                           
REMARK 245   ACCELERATION VOLTAGE (KV)         : 120                            
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
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 350   BIOMT1   2  0.833400 -0.288300 -0.471600      109.10000            
REMARK 350   BIOMT2   2  0.288800 -0.500400  0.816200       46.65000            
REMARK 350   BIOMT3   2 -0.471300 -0.816400 -0.333800      308.80000            
REMARK 350   BIOMT1   3 -0.667700 -0.578000 -0.469200      319.82100            
REMARK 350   BIOMT2   3 -0.576500  0.002768  0.817100       89.03790            
REMARK 350   BIOMT3   3 -0.470900  0.816100 -0.335100      116.68300            
REMARK 350   BIOMT1   4 -0.166000  0.866500 -0.470700       90.79020            
REMARK 350   BIOMT2   4  0.290000  0.499100  0.816600      -71.43600            
REMARK 350   BIOMT3   4  0.942500 -0.000907 -0.334100       46.25120            
REMARK 350   BIOMT1   5 -0.500000 -0.866000  0.000074      278.73300            
REMARK 350   BIOMT2   5  0.866000 -0.500000  0.000489       74.62150            
REMARK 350   BIOMT3   5 -0.000387  0.000309  1.000000        0.00924            
REMARK 350   BIOMT1   6 -0.666800  0.577500 -0.471100      183.80000            
REMARK 350   BIOMT2   6  0.577100  0.000144 -0.816700      146.00000            
REMARK 350   BIOMT3   6 -0.471500 -0.816400 -0.333300      308.80000            
REMARK 350   BIOMT1   7  0.833100  0.286600 -0.473000       41.72000            
REMARK 350   BIOMT2   7 -0.290200 -0.501500 -0.815000      307.10000            
REMARK 350   BIOMT3   7 -0.470800  0.816300 -0.334600      116.60000            
REMARK 350   BIOMT1   8 -0.168000 -0.865500 -0.471800      295.20000            
REMARK 350   BIOMT2   8 -0.288300  0.500900 -0.816100      189.00000            
REMARK 350   BIOMT3   8  0.942700 -0.001091 -0.333700       46.20000            
REMARK 350   BIOMT1   9 -0.500000  0.866000 -0.000392       74.74000            
REMARK 350   BIOMT2   9 -0.866000 -0.500000  0.000311      278.70000            
REMARK 350   BIOMT3   9  0.000074  0.000495  1.000000       -0.06700            
REMARK 350   BIOMT1  10 -0.166400 -0.288900  0.942800       60.45000            
REMARK 350   BIOMT2  10 -0.866200  0.499600  0.000199      160.90000            
REMARK 350   BIOMT3  10 -0.471100 -0.816600 -0.333400      308.80000            
REMARK 350   BIOMT1  11 -0.165300  0.291100  0.942300       -8.10400            
REMARK 350   BIOMT2  11  0.866400  0.499400 -0.002296      -42.76000            
REMARK 350   BIOMT3  11 -0.471300  0.816000 -0.334700      116.70000            
REMARK 350   BIOMT1  12  0.333800 -0.001004  0.942700      -32.54000            
REMARK 350   BIOMT2  12 -0.000897 -1.000000 -0.000747      235.80000            
REMARK 350   BIOMT3  12  0.942700 -0.000596 -0.333800       46.16000            
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     MET A   -43                                                      
REMARK 465     GLU A   -42                                                      
REMARK 465     GLU A   -41                                                      
REMARK 465     GLN A   -40                                                      
REMARK 465     ARG A   -39                                                      
REMARK 465     GLU A   -38                                                      
REMARK 465     ILE A   -37                                                      
REMARK 465     LEU A   -36                                                      
REMARK 465     GLU A   -35                                                      
REMARK 465     GLN A   -34                                                      
REMARK 465     LEU A   -33                                                      
REMARK 465     LYS A   -32                                                      
REMARK 465     LYS A   -31                                                      
REMARK 465     THR A   -30                                                      
REMARK 465     LEU A   -29                                                      
REMARK 465     GLN A   -28                                                      
REMARK 465     MET A   -27                                                      
REMARK 465     LEU A   -26                                                      
REMARK 465     THR A   -25                                                      
REMARK 465     VAL A   -24                                                      
REMARK 465     GLU A   -23                                                      
REMARK 465     PRO A   -22                                                      
REMARK 465     SER A   -21                                                      
REMARK 465     LYS A   -20                                                      
REMARK 465     ASN A   -19                                                      
REMARK 465     ASN A   -18                                                      
REMARK 465     GLN A   -17                                                      
REMARK 465     ILE A   -16                                                      
REMARK 465     ALA A   -15                                                      
REMARK 465     ASN A   -14                                                      
REMARK 465     GLU A   -13                                                      
REMARK 465     GLU A   -12                                                      
REMARK 465     LYS A   -11                                                      
REMARK 465     GLU A   -10                                                      
REMARK 465     LYS A    -9                                                      
REMARK 465     LYS A    -8                                                      
REMARK 465     GLU A    -7                                                      
REMARK 465     ASN A    -6                                                      
REMARK 465     GLU A    -5                                                      
REMARK 465     ASN A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     TRP A    -2                                                      
REMARK 465     CYS A    -1                                                      
REMARK 465     ILE A     0                                                      
REMARK 465     LEU A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     PRO A   165                                                      
REMARK 465     HIS A   166                                                      
REMARK 465     PHE A   167                                                      
REMARK 465     GLY A   168                                                      
REMARK 465     LYS A   169                                                      
REMARK 465     PRO A   170                                                      
REMARK 465     ALA A   171                                                      
REMARK 465     GLU A   172                                                      
REMARK 465     GLY A   173                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     PHE A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     ILE A   185                                                      
REMARK 465     GLY A   186                                                      
REMARK 465     PHE A   187                                                      
REMARK 465     PRO A   188                                                      
REMARK 465     THR A   189                                                      
REMARK 465     PRO A   190                                                      
REMARK 465     ASP A   191                                                      
REMARK 465     GLU A   192                                                      
REMARK 465     GLU A   193                                                      
REMARK 465     GLY A   194                                                      
REMARK 465     ASN A   195                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     ASN A   404                                                      
REMARK 465     ASN A   405                                                      
REMARK 465     SER A   406                                                      
REMARK 465     ARG A   407                                                      
REMARK 465     SER A   408                                                      
REMARK 465     GLY A   409                                                      
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    ASN A   4      -19.72     69.13                                   
REMARK 500    ILE A   8      -27.89     67.01                                   
REMARK 500    ASN A 143       43.67   -140.28                                   
REMARK 500    SER A 299       -5.94     74.49                                   
REMARK 500    HIS A 358       45.83   -146.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-8167   RELATED DB: EMDB                              
DBREF  5JM9 A  -43   470  UNP    P14904   AMPL_YEAST       1    514             
SEQRES   1 A  514  MET GLU GLU GLN ARG GLU ILE LEU GLU GLN LEU LYS LYS          
SEQRES   2 A  514  THR LEU GLN MET LEU THR VAL GLU PRO SER LYS ASN ASN          
SEQRES   3 A  514  GLN ILE ALA ASN GLU GLU LYS GLU LYS LYS GLU ASN GLU          
SEQRES   4 A  514  ASN SER TRP CYS ILE LEU GLU HIS ASN TYR GLU ASP ILE          
SEQRES   5 A  514  ALA GLN GLU PHE ILE ASP PHE ILE TYR LYS ASN PRO THR          
SEQRES   6 A  514  THR TYR HIS VAL VAL SER PHE PHE ALA GLU LEU LEU ASP          
SEQRES   7 A  514  LYS HIS ASN PHE LYS TYR LEU SER GLU LYS SER ASN TRP          
SEQRES   8 A  514  GLN ASP SER ILE GLY GLU ASP GLY GLY LYS PHE TYR THR          
SEQRES   9 A  514  ILE ARG ASN GLY THR ASN LEU SER ALA PHE ILE LEU GLY          
SEQRES  10 A  514  LYS ASN TRP ARG ALA GLU LYS GLY VAL GLY VAL ILE GLY          
SEQRES  11 A  514  SER HIS VAL ASP ALA LEU THR VAL LYS LEU LYS PRO VAL          
SEQRES  12 A  514  SER PHE LYS ASP THR ALA GLU GLY TYR GLY ARG ILE ALA          
SEQRES  13 A  514  VAL ALA PRO TYR GLY GLY THR LEU ASN GLU LEU TRP LEU          
SEQRES  14 A  514  ASP ARG ASP LEU GLY ILE GLY GLY ARG LEU LEU TYR LYS          
SEQRES  15 A  514  LYS LYS GLY THR ASN GLU ILE LYS SER ALA LEU VAL ASP          
SEQRES  16 A  514  SER THR PRO LEU PRO VAL CYS ARG ILE PRO SER LEU ALA          
SEQRES  17 A  514  PRO HIS PHE GLY LYS PRO ALA GLU GLY PRO PHE ASP LYS          
SEQRES  18 A  514  GLU ASP GLN THR ILE PRO VAL ILE GLY PHE PRO THR PRO          
SEQRES  19 A  514  ASP GLU GLU GLY ASN GLU PRO PRO THR ASP ASP GLU LYS          
SEQRES  20 A  514  LYS SER PRO LEU PHE GLY LYS HIS CYS ILE HIS LEU LEU          
SEQRES  21 A  514  ARG TYR VAL ALA LYS LEU ALA GLY VAL GLU VAL SER GLU          
SEQRES  22 A  514  LEU ILE GLN MET ASP LEU ASP LEU PHE ASP VAL GLN LYS          
SEQRES  23 A  514  GLY THR ILE GLY GLY ILE GLY LYS HIS PHE LEU PHE ALA          
SEQRES  24 A  514  PRO ARG LEU ASP ASP ARG LEU CYS SER PHE ALA ALA MET          
SEQRES  25 A  514  ILE ALA LEU ILE CYS TYR ALA LYS ASP VAL ASN THR GLU          
SEQRES  26 A  514  GLU SER ASP LEU PHE SER THR VAL THR LEU TYR ASP ASN          
SEQRES  27 A  514  GLU GLU ILE GLY SER LEU THR ARG GLN GLY ALA LYS GLY          
SEQRES  28 A  514  GLY LEU LEU GLU SER VAL VAL GLU ARG SER SER SER ALA          
SEQRES  29 A  514  PHE THR LYS LYS PRO VAL ASP LEU HIS THR VAL TRP ALA          
SEQRES  30 A  514  ASN SER ILE ILE LEU SER ALA ASP VAL ASN HIS LEU TYR          
SEQRES  31 A  514  ASN PRO ASN PHE PRO GLU VAL TYR LEU LYS ASN HIS PHE          
SEQRES  32 A  514  PRO VAL PRO ASN VAL GLY ILE THR LEU SER LEU ASP PRO          
SEQRES  33 A  514  ASN GLY HIS MET ALA THR ASP VAL VAL GLY THR ALA LEU          
SEQRES  34 A  514  VAL GLU GLU LEU ALA ARG ARG ASN GLY ASP LYS VAL GLN          
SEQRES  35 A  514  TYR PHE GLN ILE LYS ASN ASN SER ARG SER GLY GLY THR          
SEQRES  36 A  514  ILE GLY PRO SER LEU ALA SER GLN THR GLY ALA ARG THR          
SEQRES  37 A  514  ILE ASP LEU GLY ILE ALA GLN LEU SER MET HIS SER ILE          
SEQRES  38 A  514  ARG ALA ALA THR GLY SER LYS ASP VAL GLY LEU GLY VAL          
SEQRES  39 A  514  LYS PHE PHE ASN GLY PHE PHE LYS HIS TRP ARG SER VAL          
SEQRES  40 A  514  TYR ASP GLU PHE GLY GLU LEU                                  
HELIX    1 AA1 ILE A    8  ASN A   19  1                                  12    
HELIX    2 AA2 THR A   21  LYS A   35  1                                  15    
HELIX    3 AA3 ARG A   77  GLY A   81  5                                   5    
HELIX    4 AA4 ASN A  121  LEU A  125  5                                   5    
HELIX    5 AA5 THR A  199  LYS A  204  1                                   6    
HELIX    6 AA6 CYS A  212  GLY A  224  1                                  13    
HELIX    7 AA7 GLU A  226  SER A  228  5                                   3    
HELIX    8 AA8 ARG A  257  ASP A  277  1                                  21    
HELIX    9 AA9 VAL A  278  SER A  283  5                                   6    
HELIX   10 AB1 GLY A  304  GLY A  307  5                                   4    
HELIX   11 AB2 GLY A  308  THR A  322  1                                  15    
HELIX   12 AB3 ASP A  327  ASN A  334  1                                   8    
HELIX   13 AB4 PHE A  350  TYR A  354  5                                   5    
HELIX   14 AB5 ASP A  379  GLY A  394  1                                  16    
HELIX   15 AB6 THR A  411  GLY A  421  1                                  11    
HELIX   16 AB7 LYS A  444  GLU A  466  1                                  23    
SHEET    1 AA1 9 LYS A  39  TYR A  40  0                                        
SHEET    2 AA1 9 GLY A  56  ARG A  62  1  O  LYS A  57   N  LYS A  39           
SHEET    3 AA1 9 ASN A  66  LEU A  72 -1  O  ASN A  66   N  ARG A  62           
SHEET    4 AA1 9 PHE A 286  TYR A 292 -1  O  LEU A 291   N  LEU A  67           
SHEET    5 AA1 9 GLY A  83  HIS A  88  1  N  SER A  87   O  TYR A 292           
SHEET    6 AA1 9 ILE A 336  ALA A 340  1  O  LEU A 338   N  GLY A  86           
SHEET    7 AA1 9 ARG A 423  GLY A 428  1  O  ILE A 425   N  ILE A 337           
SHEET    8 AA1 9 ILE A 366  LEU A 370 -1  N  THR A 367   O  GLY A 428           
SHEET    9 AA1 9 VAL A 397  GLN A 401  1  O  GLN A 398   N  LEU A 368           
SHEET    1 AA2 6 LYS A 146  ASP A 151  0                                        
SHEET    2 AA2 6 LEU A 129  TYR A 137 -1  N  LEU A 135   O  ALA A 148           
SHEET    3 AA2 6 LEU A 230  ASP A 239 -1  O  GLN A 232   N  LEU A 136           
SHEET    4 AA2 6 THR A  93  ALA A 105 -1  N  VAL A  94   O  LEU A 237           
SHEET    5 AA2 6 TYR A 108  TYR A 116 -1  O  TYR A 116   N  THR A  93           
SHEET    6 AA2 6 ILE A 182  PRO A 183 -1  O  ILE A 182   N  ILE A 111           
SHEET    1 AA3 3 THR A 244  GLY A 246  0                                        
SHEET    2 AA3 3 PHE A 252  ALA A 255 -1  O  PHE A 254   N  THR A 244           
SHEET    3 AA3 3 ALA A 439  GLY A 442 -1  O  ALA A 439   N  ALA A 255           
CISPEP   1 ASP A    7    ILE A    8          0       -11.74                     
CISPEP   2 THR A  153    PRO A  154          0         5.86                     
CISPEP   3 ASP A  259    ASP A  260          0        -1.92                     
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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