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Database: PDB
Entry: 6SHS
LinkDB: 6SHS
Original site: 6SHS 
HEADER    PROTEIN FIBRIL                          08-AUG-19   6SHS              
TITLE     ABETA FIBRIL (MORPHOLOGY I)                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AMYLOID-BETA PRECURSOR PROTEIN;                            
COMPND   3 CHAIN: A, B, C, H, D, I, E, J, F, K, G, L;                           
COMPND   4 SYNONYM: APP,ABPP,APPI,ALZHEIMER DISEASE AMYLOID PROTEIN,AMYLOID     
COMPND   5 PRECURSOR PROTEIN,AMYLOID-BETA A4 PROTEIN,CEREBRAL VASCULAR AMYLOID  
COMPND   6 PEPTIDE,CVAP,PREA4,PROTEASE NEXIN-II,PN-II                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 ORGAN: BRAIN;                                                        
SOURCE   6 TISSUE: MENINGES                                                     
KEYWDS    FIBRIL, BETA AMYLOID, CRYO-EM, PROTEIN FIBRIL                         
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    M.KOLLMER,M.FANDRICH                                                  
REVDAT   1   06-NOV-19 6SHS    0                                                
JRNL        AUTH   M.KOLLMER,W.CLOSE,L.FUNK,J.RASMUSSEN,A.BSOUL,A.SCHIERHORN,   
JRNL        AUTH 2 M.SCHMIDT,C.J.SIGURDSON,M.JUCKER,M.FANDRICH                  
JRNL        TITL   CRYO-EM STRUCTURE AND POLYMORPHISM OF A BETA AMYLOID FIBRILS 
JRNL        TITL 2 PURIFIED FROM ALZHEIMER'S BRAIN TISSUE.                      
JRNL        REF    NAT COMMUN                    V.  10  4760 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   31664019                                                     
JRNL        DOI    10.1038/S41467-019-12683-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : GCTF, COOT, PHENIX, RELION, RELION,       
REMARK   3                            RELION, RELION, PHENIX                    
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : AB INITIO MODEL                     
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 4.400                          
REMARK   3   NUMBER OF PARTICLES               : 12282                          
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 6SHS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 08-AUG-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292103770.                                   
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                    : HELICAL ARRAY                     
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : MENINGES                          
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                             : 7.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 3027                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : 1000.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 40.90                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 105000                         
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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 36980 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 20920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -147.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, H, D, I, E, J, F, K,         
REMARK 350                    AND CHAINS: G, L                                  
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: 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    GLU A  22      -53.60   -121.03                                   
REMARK 500    ALA A  30      -39.44   -131.07                                   
REMARK 500    GLU B  22      -53.57   -121.04                                   
REMARK 500    ALA B  30      -39.46   -131.08                                   
REMARK 500    GLU C  22      -53.56   -121.07                                   
REMARK 500    ALA C  30      -39.41   -131.07                                   
REMARK 500    GLU H  22      -53.53   -121.02                                   
REMARK 500    ALA H  30      -39.47   -131.07                                   
REMARK 500    GLU D  22      -53.58   -121.05                                   
REMARK 500    ALA D  30      -39.39   -131.09                                   
REMARK 500    GLU I  22      -53.56   -121.07                                   
REMARK 500    ALA I  30      -39.49   -131.10                                   
REMARK 500    GLU E  22      -53.61   -121.04                                   
REMARK 500    ALA E  30      -39.44   -131.08                                   
REMARK 500    GLU J  22      -53.58   -121.04                                   
REMARK 500    ALA J  30      -39.47   -131.06                                   
REMARK 500    GLU F  22      -53.62   -121.06                                   
REMARK 500    ALA F  30      -39.47   -131.11                                   
REMARK 500    GLU K  22      -53.63   -121.06                                   
REMARK 500    ALA K  30      -39.49   -131.06                                   
REMARK 500    GLU G  22      -53.64   -121.05                                   
REMARK 500    ALA G  30      -39.44   -131.09                                   
REMARK 500    GLU L  22      -53.60   -121.04                                   
REMARK 500    ALA L  30      -39.46   -131.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-4864   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-4866   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-10204   RELATED DB: EMDB                             
REMARK 900 ABETA FIBRIL (MORPHOLOGY I)                                          
DBREF  6SHS A    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS B    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS C    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS H    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS D    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS I    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS E    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS J    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS F    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS K    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS G    1    40  UNP    P05067   A4_HUMAN       616    655             
DBREF  6SHS L    1    40  UNP    P05067   A4_HUMAN       616    655             
SEQRES   1 A   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 A   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 A   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 A   40  VAL                                                          
SEQRES   1 B   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 B   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 B   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 B   40  VAL                                                          
SEQRES   1 C   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 C   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 C   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 C   40  VAL                                                          
SEQRES   1 H   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 H   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 H   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 H   40  VAL                                                          
SEQRES   1 D   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 D   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 D   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 D   40  VAL                                                          
SEQRES   1 I   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 I   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 I   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 I   40  VAL                                                          
SEQRES   1 E   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 E   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 E   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 E   40  VAL                                                          
SEQRES   1 J   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 J   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 J   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 J   40  VAL                                                          
SEQRES   1 F   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 F   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 F   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 F   40  VAL                                                          
SEQRES   1 K   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 K   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 K   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 K   40  VAL                                                          
SEQRES   1 G   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 G   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 G   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 G   40  VAL                                                          
SEQRES   1 L   40  ASP ALA GLU PHE ARG HIS ASP SER GLY TYR GLU VAL HIS          
SEQRES   2 L   40  HIS GLN LYS LEU VAL PHE PHE ALA GLU ASP VAL GLY SER          
SEQRES   3 L   40  ASN LYS GLY ALA ILE ILE GLY LEU MET VAL GLY GLY VAL          
SEQRES   4 L   40  VAL                                                          
SHEET    1 AA1 6 ALA D   2  VAL D  12  0                                        
SHEET    2 AA1 6 ALA C   2  VAL C  12  1  N  ASP C   7   O  HIS D   6           
SHEET    3 AA1 6 ALA A   2  VAL A  12  1  N  ASP A   7   O  HIS C   6           
SHEET    4 AA1 6 ALA E   2  VAL E  12  1  O  ASP E   7   N  HIS A   6           
SHEET    5 AA1 6 ALA F   2  VAL F  12  1  O  ASP F   7   N  HIS E   6           
SHEET    6 AA1 6 ALA G   2  VAL G  12  1  O  ASP G   7   N  HIS F   6           
SHEET    1 AA2 6 GLN D  15  PHE D  19  0                                        
SHEET    2 AA2 6 GLN C  15  PHE C  19  1  N  LEU C  17   O  LYS D  16           
SHEET    3 AA2 6 GLN A  15  PHE A  19  1  N  LEU A  17   O  LYS C  16           
SHEET    4 AA2 6 GLN E  15  PHE E  19  1  O  LEU E  17   N  LYS A  16           
SHEET    5 AA2 6 GLN F  15  PHE F  19  1  O  LEU F  17   N  LYS E  16           
SHEET    6 AA2 6 GLN G  15  PHE G  19  1  O  LEU G  17   N  LYS F  16           
SHEET    1 AA3 6 GLY D  33  LEU D  34  0                                        
SHEET    2 AA3 6 GLY C  33  LEU C  34  1  N  GLY C  33   O  LEU D  34           
SHEET    3 AA3 6 GLY A  33  LEU A  34  1  N  GLY A  33   O  LEU C  34           
SHEET    4 AA3 6 GLY E  33  LEU E  34  1  O  GLY E  33   N  LEU A  34           
SHEET    5 AA3 6 GLY F  33  LEU F  34  1  O  GLY F  33   N  LEU E  34           
SHEET    6 AA3 6 GLY G  33  LEU G  34  1  O  GLY G  33   N  LEU F  34           
SHEET    1 AA4 6 GLU I   3  VAL I  12  0                                        
SHEET    2 AA4 6 GLU H   3  VAL H  12  1  N  GLU H   3   O  PHE I   4           
SHEET    3 AA4 6 GLU B   3  VAL B  12  1  N  GLU B   3   O  PHE H   4           
SHEET    4 AA4 6 GLU J   3  VAL J  12  1  O  GLU J   3   N  PHE B   4           
SHEET    5 AA4 6 GLU K   3  VAL K  12  1  O  GLU K   3   N  PHE J   4           
SHEET    6 AA4 6 GLU L   3  VAL L  12  1  O  GLU L   3   N  PHE K   4           
SHEET    1 AA5 6 GLN I  15  PHE I  19  0                                        
SHEET    2 AA5 6 GLN H  15  PHE H  19  1  N  LEU H  17   O  LYS I  16           
SHEET    3 AA5 6 GLN B  15  PHE B  19  1  N  LEU B  17   O  LYS H  16           
SHEET    4 AA5 6 GLN J  15  PHE J  19  1  O  LEU J  17   N  LYS B  16           
SHEET    5 AA5 6 GLN K  15  PHE K  19  1  O  LEU K  17   N  LYS J  16           
SHEET    6 AA5 6 GLN L  15  PHE L  19  1  O  LEU L  17   N  LYS K  16           
SHEET    1 AA6 6 GLY I  33  LEU I  34  0                                        
SHEET    2 AA6 6 GLY H  33  LEU H  34  1  N  GLY H  33   O  LEU I  34           
SHEET    3 AA6 6 GLY B  33  LEU B  34  1  N  GLY B  33   O  LEU H  34           
SHEET    4 AA6 6 GLY J  33  LEU J  34  1  O  GLY J  33   N  LEU B  34           
SHEET    5 AA6 6 GLY K  33  LEU K  34  1  O  GLY K  33   N  LEU J  34           
SHEET    6 AA6 6 GLY L  33  LEU L  34  1  O  GLY L  33   N  LEU K  34           
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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