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LongText Report for: 7e87-pdb

Name Class
7e87-pdb
HEADER    MEMBRANE PROTEIN                        01-MAR-21   7E87              
TITLE     CRYOEM STRUCTURE OF THE HUMAN KV4.2-DPP6S COMPLEX, TRANSMEMBRANE AND  
TITLE    2 INTRACELLULAR REGION                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 2;      
COMPND   3 CHAIN: B, C;                                                         
COMPND   4 SYNONYM: VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT KV4.2;              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY D MEMBER 2;      
COMPND   8 CHAIN: A, D;                                                         
COMPND   9 SYNONYM: VOLTAGE-GATED POTASSIUM CHANNEL SUBUNIT KV4.2;              
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: DIPEPTIDYL AMINOPEPTIDASE-LIKE PROTEIN 6;                  
COMPND  13 CHAIN: J, I, E, F;                                                   
COMPND  14 SYNONYM: DPPX,DIPEPTIDYL AMINOPEPTIDASE-RELATED PROTEIN,DIPEPTIDYL   
COMPND  15 PEPTIDASE 6,DIPEPTIDYL PEPTIDASE IV-LIKE PROTEIN,DIPEPTIDYL PEPTIDASE
COMPND  16 VI,DPP VI;                                                           
COMPND  17 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KCND2, KIAA1044;                                               
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: KCND2, KIAA1044;                                               
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  17 ORGANISM_COMMON: HUMAN;                                              
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 GENE: DPP6;                                                          
SOURCE  20 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    MEMBRANE PROTEIN                                                      
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    Y.KISE,O.NUREKI                                                       
REVDAT   1   13-OCT-21 7E87    0                                                
JRNL        AUTH   Y.KISE,G.KASUYA,H.H.OKAMOTO,D.YAMANOUCHI,K.KOBAYASHI,        
JRNL        AUTH 2 T.KUSAKIZAKO,T.NISHIZAWA,K.NAKAJO,O.NUREKI                   
JRNL        TITL   STRUCTURAL BASIS OF GATING MODULATION OF KV4 CHANNEL         
JRNL        TITL 2 COMPLEXES.                                                   
JRNL        REF    NATURE                                     2021              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   34552243                                                     
JRNL        DOI    10.1038/S41586-021-03935-Z                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
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)  : 3.400                          
REMARK   3   NUMBER OF PARTICLES               : 91974                          
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 7E87 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-MAR-21.                  
REMARK 100 THE DEPOSITION ID IS D_1300020957.                                   
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                 : HUMAN KV4.2-DPP6S COMPLEX         
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                             : 8.00                              
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 KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K3 BIOQUANTUM (6K X      
REMARK 245                                       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)  : 4800.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A, J, I, C, D, E, F                
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     ALA B   161                                                      
REMARK 465     LEU B   162                                                      
REMARK 465     PRO B   163                                                      
REMARK 465     THR B   164                                                      
REMARK 465     MET B   165                                                      
REMARK 465     THR B   166                                                      
REMARK 465     PRO B   220                                                      
REMARK 465     CYS B   221                                                      
REMARK 465     GLY B   222                                                      
REMARK 465     GLU B   223                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     SER A   160                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     LEU A   162                                                      
REMARK 465     PRO A   163                                                      
REMARK 465     PRO A   220                                                      
REMARK 465     CYS A   221                                                      
REMARK 465     GLY A   222                                                      
REMARK 465     GLU A   223                                                      
REMARK 465     ALA C   161                                                      
REMARK 465     LEU C   162                                                      
REMARK 465     PRO C   163                                                      
REMARK 465     THR C   164                                                      
REMARK 465     MET C   165                                                      
REMARK 465     THR C   166                                                      
REMARK 465     PRO C   220                                                      
REMARK 465     CYS C   221                                                      
REMARK 465     GLY C   222                                                      
REMARK 465     GLU C   223                                                      
REMARK 465     GLU D   159                                                      
REMARK 465     SER D   160                                                      
REMARK 465     ALA D   161                                                      
REMARK 465     LEU D   162                                                      
REMARK 465     PRO D   163                                                      
REMARK 465     PRO D   220                                                      
REMARK 465     CYS D   221                                                      
REMARK 465     GLY D   222                                                      
REMARK 465     GLU D   223                                                      
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   OG   SER A    69     OE1  GLU A    71              2.11            
REMARK 500   OG   SER D    69     OE1  GLU D    71              2.11            
REMARK 500   OD1  ASN B    97     NH1  ARG B   100              2.15            
REMARK 500   OD1  ASN C    97     NH1  ARG C   100              2.15            
REMARK 500   O    MET A   238     OG1  THR A   241              2.17            
REMARK 500   O    MET D   238     OG1  THR D   241              2.18            
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    PRO B  89       41.93    -86.42                                   
REMARK 500    CYS B 111     -164.43     51.80                                   
REMARK 500    THR B 156     -121.24     57.79                                   
REMARK 500    PRO B 208       -7.63    -58.79                                   
REMARK 500    ASN B 282       57.42    -92.47                                   
REMARK 500    GLU B 283     -134.85     59.21                                   
REMARK 500    PHE B 303        1.13    -69.21                                   
REMARK 500    HIS B 306       49.60    -85.33                                   
REMARK 500    GLU A 127       30.87    -93.35                                   
REMARK 500    ALA A 167     -168.61   -167.64                                   
REMARK 500    PRO A 178       46.56    -83.97                                   
REMARK 500    HIS A 179       10.83   -142.08                                   
REMARK 500    GLU A 205        7.19    -66.71                                   
REMARK 500    PRO A 208       43.51    -81.34                                   
REMARK 500    ALA A 228       -7.97    -56.61                                   
REMARK 500    ASN A 282       40.07   -104.35                                   
REMARK 500    GLU A 283      172.93     68.32                                   
REMARK 500    ALA A 288       -7.08    -56.67                                   
REMARK 500    HIS A 306       48.94    -91.14                                   
REMARK 500    LEU A 371      -60.52    -93.30                                   
REMARK 500    LYS J  32       -5.44     72.22                                   
REMARK 500    PRO C  89       41.94    -86.37                                   
REMARK 500    CYS C 111     -164.41     51.71                                   
REMARK 500    THR C 156     -121.22     57.87                                   
REMARK 500    PRO C 208       -7.50    -58.90                                   
REMARK 500    ASN C 282       57.43    -92.51                                   
REMARK 500    GLU C 283     -134.88     59.24                                   
REMARK 500    PHE C 303        1.04    -69.13                                   
REMARK 500    HIS C 306       49.68    -85.38                                   
REMARK 500    GLU D 127       30.93    -93.34                                   
REMARK 500    ALA D 167     -168.56   -167.64                                   
REMARK 500    PRO D 178       46.63    -84.03                                   
REMARK 500    HIS D 179       10.78   -142.09                                   
REMARK 500    GLU D 205        7.18    -66.64                                   
REMARK 500    PRO D 208       43.50    -81.34                                   
REMARK 500    ALA D 228       -8.00    -56.54                                   
REMARK 500    ASN D 282       40.09   -104.39                                   
REMARK 500    GLU D 283      172.90     68.35                                   
REMARK 500    ALA D 288       -7.15    -56.63                                   
REMARK 500    HIS D 306       48.96    -91.20                                   
REMARK 500    LEU D 371      -60.54    -93.30                                   
REMARK 500    LYS E  32       -5.45     72.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-31011   RELATED DB: EMDB                             
REMARK 900 TRANSMEMBRANE PROTEIN                                                
DBREF  7E87 B   40   437  UNP    Q9NZV8   KCND2_HUMAN     40    437             
DBREF  7E87 A   40   436  UNP    Q9NZV8   KCND2_HUMAN     40    436             
DBREF  7E87 J   31    58  UNP    P42658   DPP6_HUMAN      93    120             
DBREF  7E87 I   31    58  UNP    P42658   DPP6_HUMAN      93    120             
DBREF  7E87 C   40   437  UNP    Q9NZV8   KCND2_HUMAN     40    437             
DBREF  7E87 D   40   436  UNP    Q9NZV8   KCND2_HUMAN     40    436             
DBREF  7E87 E   31    58  UNP    P42658   DPP6_HUMAN      93    120             
DBREF  7E87 F   31    58  UNP    P42658   DPP6_HUMAN      93    120             
SEQRES   1 B  398  ASP ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE          
SEQRES   2 B  398  GLN THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR          
SEQRES   3 B  398  LEU LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO          
SEQRES   4 B  398  GLU THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE          
SEQRES   5 B  398  PHE ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU          
SEQRES   6 B  398  HIS TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU          
SEQRES   7 B  398  GLU LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY          
SEQRES   8 B  398  ASP CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU          
SEQRES   9 B  398  ASN ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR          
SEQRES  10 B  398  ALA GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN          
SEQRES  11 B  398  ARG VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR          
SEQRES  12 B  398  MET ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE          
SEQRES  13 B  398  ALA VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO          
SEQRES  14 B  398  CYS GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS          
SEQRES  15 B  398  GLY GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR          
SEQRES  16 B  398  ALA CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG          
SEQRES  17 B  398  LEU ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER          
SEQRES  18 B  398  VAL MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR          
SEQRES  19 B  398  TYR ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER          
SEQRES  20 B  398  GLY ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG          
SEQRES  21 B  398  ILE PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE          
SEQRES  22 B  398  LEU GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY          
SEQRES  23 B  398  PHE LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE          
SEQRES  24 B  398  ALA THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA          
SEQRES  25 B  398  SER LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR          
SEQRES  26 B  398  ILE VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL          
SEQRES  27 B  398  PRO LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS          
SEQRES  28 B  398  SER LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO          
SEQRES  29 B  398  VAL ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN          
SEQRES  30 B  398  GLN ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG          
SEQRES  31 B  398  LEU ALA ARG ILE ARG ALA ALA LYS                              
SEQRES   1 A  397  ASP ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE          
SEQRES   2 A  397  GLN THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR          
SEQRES   3 A  397  LEU LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO          
SEQRES   4 A  397  GLU THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE          
SEQRES   5 A  397  PHE ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU          
SEQRES   6 A  397  HIS TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU          
SEQRES   7 A  397  GLU LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY          
SEQRES   8 A  397  ASP CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU          
SEQRES   9 A  397  ASN ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR          
SEQRES  10 A  397  ALA GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN          
SEQRES  11 A  397  ARG VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR          
SEQRES  12 A  397  MET ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE          
SEQRES  13 A  397  ALA VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO          
SEQRES  14 A  397  CYS GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS          
SEQRES  15 A  397  GLY GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR          
SEQRES  16 A  397  ALA CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG          
SEQRES  17 A  397  LEU ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER          
SEQRES  18 A  397  VAL MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR          
SEQRES  19 A  397  TYR ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER          
SEQRES  20 A  397  GLY ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG          
SEQRES  21 A  397  ILE PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE          
SEQRES  22 A  397  LEU GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY          
SEQRES  23 A  397  PHE LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE          
SEQRES  24 A  397  ALA THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA          
SEQRES  25 A  397  SER LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR          
SEQRES  26 A  397  ILE VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL          
SEQRES  27 A  397  PRO LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS          
SEQRES  28 A  397  SER LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO          
SEQRES  29 A  397  VAL ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN          
SEQRES  30 A  397  GLN ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG          
SEQRES  31 A  397  LEU ALA ARG ILE ARG ALA ALA                                  
SEQRES   1 J   28  TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL          
SEQRES   2 J   28  ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR          
SEQRES   3 J   28  PRO ALA                                                      
SEQRES   1 I   28  TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL          
SEQRES   2 I   28  ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR          
SEQRES   3 I   28  PRO ALA                                                      
SEQRES   1 C  398  ASP ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE          
SEQRES   2 C  398  GLN THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR          
SEQRES   3 C  398  LEU LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO          
SEQRES   4 C  398  GLU THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE          
SEQRES   5 C  398  PHE ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU          
SEQRES   6 C  398  HIS TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU          
SEQRES   7 C  398  GLU LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY          
SEQRES   8 C  398  ASP CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU          
SEQRES   9 C  398  ASN ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR          
SEQRES  10 C  398  ALA GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN          
SEQRES  11 C  398  ARG VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR          
SEQRES  12 C  398  MET ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE          
SEQRES  13 C  398  ALA VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO          
SEQRES  14 C  398  CYS GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS          
SEQRES  15 C  398  GLY GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR          
SEQRES  16 C  398  ALA CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG          
SEQRES  17 C  398  LEU ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER          
SEQRES  18 C  398  VAL MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR          
SEQRES  19 C  398  TYR ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER          
SEQRES  20 C  398  GLY ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG          
SEQRES  21 C  398  ILE PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE          
SEQRES  22 C  398  LEU GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY          
SEQRES  23 C  398  PHE LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE          
SEQRES  24 C  398  ALA THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA          
SEQRES  25 C  398  SER LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR          
SEQRES  26 C  398  ILE VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL          
SEQRES  27 C  398  PRO LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS          
SEQRES  28 C  398  SER LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO          
SEQRES  29 C  398  VAL ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN          
SEQRES  30 C  398  GLN ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG          
SEQRES  31 C  398  LEU ALA ARG ILE ARG ALA ALA LYS                              
SEQRES   1 D  397  ASP ALA LEU ILE VAL LEU ASN VAL SER GLY THR ARG PHE          
SEQRES   2 D  397  GLN THR TRP GLN ASP THR LEU GLU ARG TYR PRO ASP THR          
SEQRES   3 D  397  LEU LEU GLY SER SER GLU ARG ASP PHE PHE TYR HIS PRO          
SEQRES   4 D  397  GLU THR GLN GLN TYR PHE PHE ASP ARG ASP PRO ASP ILE          
SEQRES   5 D  397  PHE ARG HIS ILE LEU ASN PHE TYR ARG THR GLY LYS LEU          
SEQRES   6 D  397  HIS TYR PRO ARG HIS GLU CYS ILE SER ALA TYR ASP GLU          
SEQRES   7 D  397  GLU LEU ALA PHE PHE GLY LEU ILE PRO GLU ILE ILE GLY          
SEQRES   8 D  397  ASP CYS CYS TYR GLU GLU TYR LYS ASP ARG ARG ARG GLU          
SEQRES   9 D  397  ASN ALA GLU ARG LEU GLN ASP ASP ALA ASP THR ASP THR          
SEQRES  10 D  397  ALA GLY GLU SER ALA LEU PRO THR MET THR ALA ARG GLN          
SEQRES  11 D  397  ARG VAL TRP ARG ALA PHE GLU ASN PRO HIS THR SER THR          
SEQRES  12 D  397  MET ALA LEU VAL PHE TYR TYR VAL THR GLY PHE PHE ILE          
SEQRES  13 D  397  ALA VAL SER VAL ILE ALA ASN VAL VAL GLU THR VAL PRO          
SEQRES  14 D  397  CYS GLY SER SER PRO GLY HIS ILE LYS GLU LEU PRO CYS          
SEQRES  15 D  397  GLY GLU ARG TYR ALA VAL ALA PHE PHE CYS LEU ASP THR          
SEQRES  16 D  397  ALA CYS VAL MET ILE PHE THR VAL GLU TYR LEU LEU ARG          
SEQRES  17 D  397  LEU ALA ALA ALA PRO SER ARG TYR ARG PHE VAL ARG SER          
SEQRES  18 D  397  VAL MET SER ILE ILE ASP VAL VAL ALA ILE LEU PRO TYR          
SEQRES  19 D  397  TYR ILE GLY LEU VAL MET THR ASP ASN GLU ASP VAL SER          
SEQRES  20 D  397  GLY ALA PHE VAL THR LEU ARG VAL PHE ARG VAL PHE ARG          
SEQRES  21 D  397  ILE PHE LYS PHE SER ARG HIS SER GLN GLY LEU ARG ILE          
SEQRES  22 D  397  LEU GLY TYR THR LEU LYS SER CYS ALA SER GLU LEU GLY          
SEQRES  23 D  397  PHE LEU LEU PHE SER LEU THR MET ALA ILE ILE ILE PHE          
SEQRES  24 D  397  ALA THR VAL MET PHE TYR ALA GLU LYS GLY SER SER ALA          
SEQRES  25 D  397  SER LYS PHE THR SER ILE PRO ALA ALA PHE TRP TYR THR          
SEQRES  26 D  397  ILE VAL THR MET THR THR LEU GLY TYR GLY ASP MET VAL          
SEQRES  27 D  397  PRO LYS THR ILE ALA GLY LYS ILE PHE GLY SER ILE CYS          
SEQRES  28 D  397  SER LEU SER GLY VAL LEU VAL ILE ALA LEU PRO VAL PRO          
SEQRES  29 D  397  VAL ILE VAL SER ASN PHE SER ARG ILE TYR HIS GLN ASN          
SEQRES  30 D  397  GLN ARG ALA ASP LYS ARG ARG ALA GLN LYS LYS ALA ARG          
SEQRES  31 D  397  LEU ALA ARG ILE ARG ALA ALA                                  
SEQRES   1 E   28  TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL          
SEQRES   2 E   28  ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR          
SEQRES   3 E   28  PRO ALA                                                      
SEQRES   1 F   28  TRP LYS GLY ILE ALA ILE ALA LEU LEU VAL ILE LEU VAL          
SEQRES   2 F   28  ILE CYS SER LEU ILE VAL THR SER VAL ILE LEU LEU THR          
SEQRES   3 F   28  PRO ALA                                                      
HELIX    1 AA1 GLN B   56  GLU B   60  1                                   5    
HELIX    2 AA2 SER B   70  TYR B   76  1                                   7    
HELIX    3 AA3 ASP B   90  GLY B  102  1                                  13    
HELIX    4 AA4 ALA B  114  PHE B  122  1                                   9    
HELIX    5 AA5 ASP B  131  ARG B  147  1                                  17    
HELIX    6 AA6 GLN B  149  THR B  154  1                                   6    
HELIX    7 AA7 ARG B  168  ASN B  177  1                                  10    
HELIX    8 AA8 SER B  181  GLU B  205  1                                  25    
HELIX    9 AA9 ALA B  228  ALA B  250  1                                  23    
HELIX   10 AB1 SER B  253  ARG B  259  1                                   7    
HELIX   11 AB2 SER B  260  ASN B  282  1                                  23    
HELIX   12 AB3 ALA B  288  ARG B  296  1                                   9    
HELIX   13 AB4 VAL B  297  ARG B  305  5                                   9    
HELIX   14 AB5 GLN B  308  SER B  319  1                                  12    
HELIX   15 AB6 CYS B  320  LYS B  347  1                                  28    
HELIX   16 AB7 SER B  356  THR B  369  1                                  14    
HELIX   17 AB8 THR B  380  LEU B  400  1                                  21    
HELIX   18 AB9 PRO B  401  ARG B  434  1                                  34    
HELIX   19 AC1 TRP A   55  ARG A   61  1                                   7    
HELIX   20 AC2 SER A   70  PHE A   75  1                                   6    
HELIX   21 AC3 ASP A   88  THR A  101  1                                  14    
HELIX   22 AC4 CYS A  111  GLY A  123  1                                  13    
HELIX   23 AC5 ILE A  125  ILE A  129  5                                   5    
HELIX   24 AC6 ASP A  131  ASP A  150  1                                  20    
HELIX   25 AC7 ASP A  151  ASP A  153  5                                   3    
HELIX   26 AC8 ALA A  167  ASN A  177  1                                  11    
HELIX   27 AC9 SER A  181  GLU A  205  1                                  25    
HELIX   28 AD1 ALA A  228  ALA A  250  1                                  23    
HELIX   29 AD2 SER A  253  SER A  260  1                                   8    
HELIX   30 AD3 SER A  260  ASN A  282  1                                  23    
HELIX   31 AD4 ALA A  288  PHE A  295  1                                   8    
HELIX   32 AD5 ARG A  296  ARG A  305  5                                  10    
HELIX   33 AD6 GLN A  308  CYS A  320  1                                  13    
HELIX   34 AD7 CYS A  320  GLU A  346  1                                  27    
HELIX   35 AD8 SER A  356  THR A  369  1                                  14    
HELIX   36 AD9 THR A  380  LEU A  400  1                                  21    
HELIX   37 AE1 PRO A  401  ARG A  434  1                                  34    
HELIX   38 AE2 LYS J   32  THR J   56  1                                  25    
HELIX   39 AE3 LYS I   32  THR I   56  1                                  25    
HELIX   40 AE4 GLN C   56  GLU C   60  1                                   5    
HELIX   41 AE5 SER C   70  TYR C   76  1                                   7    
HELIX   42 AE6 ASP C   90  GLY C  102  1                                  13    
HELIX   43 AE7 ALA C  114  PHE C  122  1                                   9    
HELIX   44 AE8 ASP C  131  ARG C  147  1                                  17    
HELIX   45 AE9 GLN C  149  THR C  154  1                                   6    
HELIX   46 AF1 ARG C  168  ASN C  177  1                                  10    
HELIX   47 AF2 SER C  181  GLU C  205  1                                  25    
HELIX   48 AF3 ALA C  228  ALA C  250  1                                  23    
HELIX   49 AF4 SER C  253  ARG C  259  1                                   7    
HELIX   50 AF5 SER C  260  ASN C  282  1                                  23    
HELIX   51 AF6 ALA C  288  ARG C  296  1                                   9    
HELIX   52 AF7 VAL C  297  ARG C  305  5                                   9    
HELIX   53 AF8 GLN C  308  SER C  319  1                                  12    
HELIX   54 AF9 CYS C  320  LYS C  347  1                                  28    
HELIX   55 AG1 SER C  356  THR C  369  1                                  14    
HELIX   56 AG2 THR C  380  LEU C  400  1                                  21    
HELIX   57 AG3 PRO C  401  ARG C  434  1                                  34    
HELIX   58 AG4 TRP D   55  ARG D   61  1                                   7    
HELIX   59 AG5 SER D   70  PHE D   75  1                                   6    
HELIX   60 AG6 ASP D   88  THR D  101  1                                  14    
HELIX   61 AG7 CYS D  111  GLY D  123  1                                  13    
HELIX   62 AG8 ILE D  125  ILE D  129  5                                   5    
HELIX   63 AG9 ASP D  131  ASP D  150  1                                  20    
HELIX   64 AH1 ASP D  151  ASP D  153  5                                   3    
HELIX   65 AH2 ALA D  167  ASN D  177  1                                  11    
HELIX   66 AH3 SER D  181  GLU D  205  1                                  25    
HELIX   67 AH4 ALA D  228  ALA D  250  1                                  23    
HELIX   68 AH5 SER D  253  SER D  260  1                                   8    
HELIX   69 AH6 SER D  260  ASN D  282  1                                  23    
HELIX   70 AH7 ALA D  288  PHE D  295  1                                   8    
HELIX   71 AH8 ARG D  296  ARG D  305  5                                  10    
HELIX   72 AH9 GLN D  308  CYS D  320  1                                  13    
HELIX   73 AI1 CYS D  320  GLU D  346  1                                  27    
HELIX   74 AI2 SER D  356  THR D  369  1                                  14    
HELIX   75 AI3 THR D  380  LEU D  400  1                                  21    
HELIX   76 AI4 PRO D  401  ARG D  434  1                                  34    
HELIX   77 AI5 LYS E   32  THR E   56  1                                  25    
HELIX   78 AI6 LYS F   32  THR F   56  1                                  25    
SHEET    1 AA1 3 ARG B  51  TRP B  55  0                                        
SHEET    2 AA1 3 LEU B  42  ASN B  46 -1  N  ILE B  43   O  THR B  54           
SHEET    3 AA1 3 TYR B  83  PHE B  84  1  O  TYR B  83   N  ASN B  46           
SHEET    1 AA2 3 ARG A  51  THR A  54  0                                        
SHEET    2 AA2 3 ILE A  43  ASN A  46 -1  N  LEU A  45   O  PHE A  52           
SHEET    3 AA2 3 TYR A  83  PHE A  84  1  O  TYR A  83   N  ASN A  46           
SHEET    1 AA3 3 ARG C  51  TRP C  55  0                                        
SHEET    2 AA3 3 LEU C  42  ASN C  46 -1  N  ILE C  43   O  THR C  54           
SHEET    3 AA3 3 TYR C  83  PHE C  84  1  O  TYR C  83   N  ASN C  46           
SHEET    1 AA4 3 ARG D  51  THR D  54  0                                        
SHEET    2 AA4 3 ILE D  43  ASN D  46 -1  N  LEU D  45   O  PHE D  52           
SHEET    3 AA4 3 TYR D  83  PHE D  84  1  O  TYR D  83   N  ASN D  46           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 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                         
TER    3123      LYS B 437                                                      
TER    6244      ALA A 436                                                      
TER    6450      ALA J  58                                                      
TER    6656      ALA I  58                                                      
TER    9779      LYS C 437                                                      
TER   12900      ALA D 436                                                      
TER   13106      ALA E  58                                                      
TER   13312      ALA F  58                                                      
MASTER      217    0    0   78   12    0    0    613304    8    0  136          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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