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Database: PDB
Entry: 2N1F
LinkDB: 2N1F
Original site: 2N1F 
HEADER    APOPTOSIS                               01-APR-15   2N1F              
TITLE     STRUCTURE AND ASSEMBLY OF THE MOUSE ASC FILAMENT BY COMBINED NMR      
TITLE    2 SPECTROSCOPY AND CRYO-ELECTRON MICROSCOPY                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APOPTOSIS-ASSOCIATED SPECK-LIKE PROTEIN;                   
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O;                  
COMPND   4 FRAGMENT: PYRIN DOMAIN (UNP RESIDUES 2-90);                          
COMPND   5 SYNONYM: MASC;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: PYCARD, ASC;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    MOUSE ASC FILAMENT, ASC APOPTOSIS-ASSOCIATED SPECK LIKE PROTEIN       
KEYWDS   2 CONTAINING A CARD, PYRIN DOMAIN, INFLAMMASOMES, DEATH DOMAIN,        
KEYWDS   3 APOPTOSIS                                                            
EXPDTA    SOLID-STATE NMR; ELECTRON MICROSCOPY                                  
NUMMDL    10                                                                    
AUTHOR    L.SBORGI,F.RAVOTTI,V.DANDEY,M.DICK,A.MAZUR,S.RECKEL,M.CHAMI,          
AUTHOR   2 S.SCHERER,A.BOCKMANN,E.EGELMAN,H.STAHLBERG,P.BROZ,B.MEIER,S.HILLER   
REVDAT   4   18-JUL-18 2N1F    1       REMARK                                   
REVDAT   3   11-NOV-15 2N1F    1       JRNL                                     
REVDAT   2   28-OCT-15 2N1F    1       JRNL                                     
REVDAT   1   14-OCT-15 2N1F    0                                                
JRNL        AUTH   L.SBORGI,F.RAVOTTI,V.P.DANDEY,M.S.DICK,A.MAZUR,S.RECKEL,     
JRNL        AUTH 2 M.CHAMI,S.SCHERER,M.HUBER,A.BOCKMANN,E.H.EGELMAN,            
JRNL        AUTH 3 H.STAHLBERG,P.BROZ,B.H.MEIER,S.HILLER                        
JRNL        TITL   STRUCTURE AND ASSEMBLY OF THE MOUSE ASC INFLAMMASOME BY      
JRNL        TITL 2 COMBINED NMR SPECTROSCOPY AND CRYO-ELECTRON MICROSCOPY.      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 112 13237 2015              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   26464513                                                     
JRNL        DOI    10.1073/PNAS.1507579112                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : XPLOR-NIH                                            
REMARK   3   AUTHORS     : SCHWIETERS, KUSZEWSKI, TJANDRA AND CLORE             
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2N1F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000104300.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 288                                
REMARK 210  PH                             : NULL                               
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : AMBIENT                            
REMARK 210  SAMPLE CONTENTS                : 15 MG [U-100% 13C; U-100% 15N]     
REMARK 210                                   ASC FILAMENT, 90% H2O/10% D2O      
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NCACX; NCOCX; NCACB; CANCO; CCC;   
REMARK 210                                   20MSDARR; N(CO)CACB; CAN(CO)CA;    
REMARK 210                                   N(CA)CBCX; 100MSPDSD               
REMARK 210  SPECTROMETER FIELD STRENGTH    : 850 MHZ                            
REMARK 210  SPECTROMETER MODEL             : AVANCE                             
REMARK 210  SPECTROMETER MANUFACTURER      : BRUKER                             
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : CYANA                              
REMARK 210   METHOD USED                   : SIMULATED ANNEALING                
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : 100                                
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 10                                 
REMARK 210 CONFORMERS, SELECTION CRITERIA  : STRUCTURES WITH THE LOWEST         
REMARK 210                                   ENERGY                             
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1                   
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 217                                                                      
REMARK 217 SOLID STATE NMR STUDY                                                
REMARK 217 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLID              
REMARK 217 STATE NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT           
REMARK 217 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 217 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : HELICAL                           
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : FILAMENT                          
REMARK 245   PARTICLE TYPE                  : HELICAL                           
REMARK 245   NAME OF SAMPLE                 : MOUSE ASC-PYD FILAMENT; ASC       
REMARK 245                                    FILAMENT                          
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : GRIDS WERE BLOTTED FOR ONE        
REMARK 245                                    SECOND BEFORE PLUNGING INTO       
REMARK 245                                    LIQUID ETHANE (FEI VITROBOT       
REMARK 245                                    MARK IV).                         
REMARK 245   SAMPLE BUFFER                  : 25 MM TRIS, 300 MM SODIUM         
REMARK 245                                    CHLORIDE                          
REMARK 245   PH                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 10-OCT-14                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : DIRECT ELECTRON DE-10 (5K X    
REMARK 245                                       4K)                            
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : -12.00                         
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : 12.00                          
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : DIFFRACTION                    
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 20.00                          
REMARK 245   ILLUMINATION MODE                 : SPOT SCAN                      
REMARK 245   NOMINAL MAGNIFICATION             : 22500                          
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : TUNGSTEN HAIRPIN               
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 300 REMARK: THE HELICAL PARAMETERS GENERATE THE FILAMENT FROM ANY        
REMARK 300 SINGLE CHAIN.                                                        
REMARK 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR                   
REMARK 300 HELICAL SYMMETRY WITH THE FOLLOWING PARAMETERS:                      
REMARK 300 ROTATION PER SUBUNIT (TWIST) = 53.00 DEGREES                         
REMARK 300 RISE PER SUBUNIT (HEIGHT) = 14.20 ANGSTROMS                          
REMARK 300 IN ADDITION, THERE IS 3-FOLD CIRCULAR                                
REMARK 300 SYMMETRY AROUND THE HELIX AXIS                                       
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: PENTADECAMERIC                    
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O                         
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
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   OD1  ASP D    54     NH2  ARG E    41              2.07            
REMARK 500   OD1  ASP I    54     NH2  ARG J    41              2.08            
REMARK 500   OD1  ASP L    54     NH2  ARG M    41              2.08            
REMARK 500   OD1  ASP F    54     NH2  ARG G    41              2.09            
REMARK 500   OD1  ASP K    54     NH2  ARG L    41              2.09            
REMARK 500   OD1  ASP H    54     NH2  ARG I    41              2.10            
REMARK 500   OD1  ASP M    54     NH2  ARG N    41              2.11            
REMARK 500   OD1  ASP C    54     NH2  ARG D    41              2.11            
REMARK 500   OD1  ASP A    54     NH2  ARG B    41              2.11            
REMARK 500   OD1  ASP G    54     NH2  ARG H    41              2.11            
REMARK 500   OD1  ASP B    54     NH2  ARG C    41              2.12            
REMARK 500   OD1  ASP N    54     NH2  ARG O    41              2.12            
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  7 ARG A   3      -10.89    -46.07                                   
REMARK 500  7 ARG B   3      -10.73    -46.16                                   
REMARK 500  7 ARG C   3      -10.75    -46.16                                   
REMARK 500  7 ARG D   3      -10.83    -46.08                                   
REMARK 500  7 ARG E   3      -10.83    -46.10                                   
REMARK 500  7 ARG F   3      -10.93    -45.97                                   
REMARK 500  7 ARG G   3      -10.84    -46.08                                   
REMARK 500  7 ARG H   3      -10.72    -46.16                                   
REMARK 500  7 ARG I   3      -10.75    -46.11                                   
REMARK 500  7 ARG J   3      -10.81    -46.05                                   
REMARK 500  7 ARG K   3      -10.81    -46.12                                   
REMARK 500  7 ARG L   3      -10.87    -46.10                                   
REMARK 500  7 ARG M   3      -10.74    -46.15                                   
REMARK 500  7 ARG N   3      -10.76    -46.13                                   
REMARK 500  7 ARG O   3      -10.82    -46.06                                   
REMARK 500 10 ARG A   3       -7.47    -48.15                                   
REMARK 500 10 ARG B   3       -7.33    -48.22                                   
REMARK 500 10 ARG C   3       -7.35    -48.22                                   
REMARK 500 10 ARG D   3       -7.48    -48.14                                   
REMARK 500 10 ARG E   3       -7.43    -48.16                                   
REMARK 500 10 ARG F   3       -7.45    -48.11                                   
REMARK 500 10 ARG G   3       -7.39    -48.17                                   
REMARK 500 10 ARG H   3       -7.35    -48.15                                   
REMARK 500 10 ARG I   3       -7.40    -48.14                                   
REMARK 500 10 ARG J   3       -7.27    -48.26                                   
REMARK 500 10 ARG K   3       -7.44    -48.17                                   
REMARK 500 10 ARG L   3       -7.35    -48.18                                   
REMARK 500 10 ARG M   3       -7.31    -48.20                                   
REMARK 500 10 ARG N   3       -7.39    -48.17                                   
REMARK 500 10 ARG O   3       -7.46    -48.15                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 26550   RELATED DB: BMRB                                 
REMARK 900 RELATED ID: EMD-2971   RELATED DB: EMDB                              
REMARK 900 RELATED ID: 25561   RELATED DB: BMRB                                 
DBREF  2N1F A    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F B    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F C    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F D    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F E    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F F    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F G    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F H    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F I    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F J    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F K    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F L    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F M    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F N    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
DBREF  2N1F O    2    90  UNP    Q9EPB4   ASC_MOUSE        2     90             
SEQRES   1 A   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 A   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 A   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 A   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 A   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 A   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 A   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 B   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 B   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 B   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 B   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 B   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 B   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 B   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 C   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 C   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 C   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 C   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 C   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 C   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 C   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 D   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 D   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 D   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 D   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 D   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 D   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 D   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 E   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 E   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 E   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 E   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 E   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 E   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 E   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 F   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 F   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 F   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 F   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 F   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 F   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 F   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 G   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 G   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 G   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 G   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 G   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 G   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 G   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 H   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 H   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 H   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 H   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 H   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 H   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 H   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 I   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 I   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 I   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 I   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 I   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 I   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 I   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 J   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 J   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 J   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 J   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 J   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 J   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 J   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 K   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 K   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 K   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 K   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 K   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 K   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 K   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 L   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 L   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 L   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 L   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 L   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 L   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 L   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 M   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 M   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 M   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 M   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 M   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 M   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 M   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 N   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 N   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 N   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 N   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 N   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 N   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 N   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
SEQRES   1 O   89  GLY ARG ALA ARG ASP ALA ILE LEU ASP ALA LEU GLU ASN          
SEQRES   2 O   89  LEU SER GLY ASP GLU LEU LYS LYS PHE LYS MET LYS LEU          
SEQRES   3 O   89  LEU THR VAL GLN LEU ARG GLU GLY TYR GLY ARG ILE PRO          
SEQRES   4 O   89  ARG GLY ALA LEU LEU GLN MET ASP ALA ILE ASP LEU THR          
SEQRES   5 O   89  ASP LYS LEU VAL SER TYR TYR LEU GLU SER TYR GLY LEU          
SEQRES   6 O   89  GLU LEU THR MET THR VAL LEU ARG ASP MET GLY LEU GLN          
SEQRES   7 O   89  GLU LEU ALA GLU GLN LEU GLN THR THR LYS GLU                  
HELIX    1   1 GLY A    2  GLU A   13  1                                  12    
HELIX    2   2 SER A   16  VAL A   30  1                                  15    
HELIX    3   3 PRO A   40  MET A   47  1                                   8    
HELIX    4   4 ASP A   48  TYR A   60  1                                  13    
HELIX    5   5 LEU A   61  MET A   76  1                                  16    
HELIX    6   6 GLN A   79  GLU A   90  1                                  12    
HELIX    7   7 ARG B    3  GLU B   13  1                                  11    
HELIX    8   8 SER B   16  VAL B   30  1                                  15    
HELIX    9   9 PRO B   40  MET B   47  1                                   8    
HELIX   10  10 ASP B   48  TYR B   60  1                                  13    
HELIX   11  11 LEU B   61  MET B   76  1                                  16    
HELIX   12  12 GLN B   79  GLU B   90  1                                  12    
HELIX   13  13 ARG C    3  GLU C   13  1                                  11    
HELIX   14  14 SER C   16  VAL C   30  1                                  15    
HELIX   15  15 PRO C   40  MET C   47  1                                   8    
HELIX   16  16 ASP C   48  TYR C   60  1                                  13    
HELIX   17  17 LEU C   61  MET C   76  1                                  16    
HELIX   18  18 GLN C   79  GLU C   90  1                                  12    
HELIX   19  19 ARG D    3  GLU D   13  1                                  11    
HELIX   20  20 SER D   16  VAL D   30  1                                  15    
HELIX   21  21 PRO D   40  MET D   47  1                                   8    
HELIX   22  22 ASP D   48  TYR D   60  1                                  13    
HELIX   23  23 LEU D   61  MET D   76  1                                  16    
HELIX   24  24 GLN D   79  GLU D   90  1                                  12    
HELIX   25  25 ARG E    3  GLU E   13  1                                  11    
HELIX   26  26 SER E   16  VAL E   30  1                                  15    
HELIX   27  27 PRO E   40  MET E   47  1                                   8    
HELIX   28  28 ASP E   48  TYR E   60  1                                  13    
HELIX   29  29 LEU E   61  MET E   76  1                                  16    
HELIX   30  30 GLN E   79  GLU E   90  1                                  12    
HELIX   31  31 ARG F    3  GLU F   13  1                                  11    
HELIX   32  32 SER F   16  VAL F   30  1                                  15    
HELIX   33  33 PRO F   40  MET F   47  1                                   8    
HELIX   34  34 ASP F   48  TYR F   60  1                                  13    
HELIX   35  35 LEU F   61  MET F   76  1                                  16    
HELIX   36  36 GLN F   79  GLU F   90  1                                  12    
HELIX   37  37 ARG G    3  GLU G   13  1                                  11    
HELIX   38  38 SER G   16  VAL G   30  1                                  15    
HELIX   39  39 PRO G   40  MET G   47  1                                   8    
HELIX   40  40 ASP G   48  TYR G   60  1                                  13    
HELIX   41  41 LEU G   61  MET G   76  1                                  16    
HELIX   42  42 GLN G   79  GLU G   90  1                                  12    
HELIX   43  43 ARG H    3  GLU H   13  1                                  11    
HELIX   44  44 SER H   16  VAL H   30  1                                  15    
HELIX   45  45 PRO H   40  MET H   47  1                                   8    
HELIX   46  46 ASP H   48  TYR H   60  1                                  13    
HELIX   47  47 LEU H   61  MET H   76  1                                  16    
HELIX   48  48 GLN H   79  GLU H   90  1                                  12    
HELIX   49  49 ARG I    3  GLU I   13  1                                  11    
HELIX   50  50 SER I   16  VAL I   30  1                                  15    
HELIX   51  51 PRO I   40  MET I   47  1                                   8    
HELIX   52  52 ASP I   48  TYR I   60  1                                  13    
HELIX   53  53 LEU I   61  MET I   76  1                                  16    
HELIX   54  54 GLN I   79  GLU I   90  1                                  12    
HELIX   55  55 ARG J    3  GLU J   13  1                                  11    
HELIX   56  56 SER J   16  VAL J   30  1                                  15    
HELIX   57  57 PRO J   40  MET J   47  1                                   8    
HELIX   58  58 ASP J   48  TYR J   60  1                                  13    
HELIX   59  59 LEU J   61  MET J   76  1                                  16    
HELIX   60  60 GLN J   79  GLU J   90  1                                  12    
HELIX   61  61 ARG K    3  GLU K   13  1                                  11    
HELIX   62  62 SER K   16  VAL K   30  1                                  15    
HELIX   63  63 PRO K   40  MET K   47  1                                   8    
HELIX   64  64 ASP K   48  TYR K   60  1                                  13    
HELIX   65  65 LEU K   61  MET K   76  1                                  16    
HELIX   66  66 GLN K   79  GLU K   90  1                                  12    
HELIX   67  67 ARG L    3  GLU L   13  1                                  11    
HELIX   68  68 SER L   16  VAL L   30  1                                  15    
HELIX   69  69 PRO L   40  MET L   47  1                                   8    
HELIX   70  70 ASP L   48  TYR L   60  1                                  13    
HELIX   71  71 LEU L   61  MET L   76  1                                  16    
HELIX   72  72 GLN L   79  GLU L   90  1                                  12    
HELIX   73  73 ARG M    3  GLU M   13  1                                  11    
HELIX   74  74 SER M   16  VAL M   30  1                                  15    
HELIX   75  75 PRO M   40  MET M   47  1                                   8    
HELIX   76  76 ASP M   48  TYR M   60  1                                  13    
HELIX   77  77 LEU M   61  MET M   76  1                                  16    
HELIX   78  78 GLN M   79  GLU M   90  1                                  12    
HELIX   79  79 ARG N    3  GLU N   13  1                                  11    
HELIX   80  80 SER N   16  VAL N   30  1                                  15    
HELIX   81  81 PRO N   40  MET N   47  1                                   8    
HELIX   82  82 ASP N   48  TYR N   60  1                                  13    
HELIX   83  83 LEU N   61  MET N   76  1                                  16    
HELIX   84  84 GLN N   79  GLU N   90  1                                  12    
HELIX   85  85 ARG O    3  GLU O   13  1                                  11    
HELIX   86  86 SER O   16  VAL O   30  1                                  15    
HELIX   87  87 PRO O   40  MET O   47  1                                   8    
HELIX   88  88 ASP O   48  TYR O   60  1                                  13    
HELIX   89  89 LEU O   61  MET O   76  1                                  16    
HELIX   90  90 GLN O   79  GLU O   90  1                                  12    
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                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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