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Database: PDB
Entry: 6IDF
LinkDB: 6IDF
Original site: 6IDF 
HEADER    MEMBRANE PROTEIN                        09-SEP-18   6IDF              
TITLE     CRYO-EM STRUCTURE OF GAMMA SECRETASE IN COMPLEX WITH A NOTCH FRAGMENT 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NICASTRIN;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: PRESENILIN-1;                                              
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: PS-1;                                                       
COMPND   9 EC: 3.4.23.-;                                                        
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: GAMMA-SECRETASE SUBUNIT APH-1A;                            
COMPND  13 CHAIN: C;                                                            
COMPND  14 SYNONYM: APH-1A;                                                     
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: GAMMA-SECRETASE SUBUNIT PEN-2;                             
COMPND  18 CHAIN: D;                                                            
COMPND  19 SYNONYM: PRESENILIN ENHANCER PROTEIN 2;                              
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: NOTCH1;                                                    
COMPND  23 CHAIN: E;                                                            
COMPND  24 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: NCSTN;                                                         
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: PS1;                                                           
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: APH1A;                                                         
SOURCE  20 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  24 ORGANISM_COMMON: HUMAN;                                              
SOURCE  25 ORGANISM_TAXID: 9606;                                                
SOURCE  26 GENE: PEN2;                                                          
SOURCE  27 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  28 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  29 MOL_ID: 5;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  31 ORGANISM_TAXID: 9606;                                                
SOURCE  32 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    COMPLEX, MEMBRANE PROTEIN                                             
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    G.YANG,R.ZHOU,Q.ZHOU,X.GUO,C.YAN,M.KE,J.LEI,Y.SHI                     
REVDAT   3   23-JAN-19 6IDF    1       JRNL                                     
REVDAT   2   16-JAN-19 6IDF    1       JRNL                                     
REVDAT   1   26-DEC-18 6IDF    0                                                
JRNL        AUTH   G.YANG,R.ZHOU,Q.ZHOU,X.GUO,C.YAN,M.KE,J.LEI,Y.SHI            
JRNL        TITL   STRUCTURAL BASIS OF NOTCH RECOGNITION BY HUMAN               
JRNL        TITL 2 GAMMA-SECRETASE                                              
JRNL        REF    NATURE                        V. 565   192 2019              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   30598546                                                     
JRNL        DOI    10.1038/S41586-018-0813-8                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 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)  : 2.700                          
REMARK   3   NUMBER OF PARTICLES               : 476853                         
REMARK   3   CTF CORRECTION METHOD             : NONE                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6IDF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300009019.                                   
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                 : GAMMA-SECRETASE                   
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                             : 7.40                              
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 K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 1.56                           
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: PENTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     ARG A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     ARG A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     SER A    22                                                      
REMARK 465     PHE A    23                                                      
REMARK 465     CYS A    24                                                      
REMARK 465     VAL A    25                                                      
REMARK 465     LEU A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     ALA A    28                                                      
REMARK 465     GLY A    29                                                      
REMARK 465     LEU A    30                                                      
REMARK 465     CYS A    31                                                      
REMARK 465     ARG A    32                                                      
REMARK 465     GLY A    33                                                      
REMARK 465     PRO A   701                                                      
REMARK 465     ARG A   702                                                      
REMARK 465     GLU A   703                                                      
REMARK 465     PRO A   704                                                      
REMARK 465     GLY A   705                                                      
REMARK 465     ALA A   706                                                      
REMARK 465     VAL A   707                                                      
REMARK 465     SER A   708                                                      
REMARK 465     TYR A   709                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     GLU B     3                                                      
REMARK 465     LEU B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     PRO B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     TYR B    10                                                      
REMARK 465     PHE B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     ASN B    13                                                      
REMARK 465     ALA B    14                                                      
REMARK 465     GLN B    15                                                      
REMARK 465     MET B    16                                                      
REMARK 465     SER B    17                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     ASP B    19                                                      
REMARK 465     ASN B    20                                                      
REMARK 465     HIS B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     SER B    23                                                      
REMARK 465     ASN B    24                                                      
REMARK 465     THR B    25                                                      
REMARK 465     VAL B    26                                                      
REMARK 465     ARG B    27                                                      
REMARK 465     SER B    28                                                      
REMARK 465     GLN B    29                                                      
REMARK 465     ASN B    30                                                      
REMARK 465     ASP B    31                                                      
REMARK 465     ASN B    32                                                      
REMARK 465     ARG B    33                                                      
REMARK 465     GLU B    34                                                      
REMARK 465     ARG B    35                                                      
REMARK 465     GLN B    36                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     HIS B    38                                                      
REMARK 465     ASN B    39                                                      
REMARK 465     ASP B    40                                                      
REMARK 465     ARG B    41                                                      
REMARK 465     ARG B    42                                                      
REMARK 465     SER B    43                                                      
REMARK 465     LEU B    44                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     HIS B    46                                                      
REMARK 465     PRO B    47                                                      
REMARK 465     GLU B    48                                                      
REMARK 465     PRO B    49                                                      
REMARK 465     LEU B    50                                                      
REMARK 465     SER B    51                                                      
REMARK 465     ASN B    52                                                      
REMARK 465     GLY B    53                                                      
REMARK 465     ARG B    54                                                      
REMARK 465     PRO B    55                                                      
REMARK 465     GLN B    56                                                      
REMARK 465     GLY B    57                                                      
REMARK 465     ASN B    58                                                      
REMARK 465     SER B    59                                                      
REMARK 465     ARG B    60                                                      
REMARK 465     GLN B    61                                                      
REMARK 465     VAL B    62                                                      
REMARK 465     VAL B    63                                                      
REMARK 465     GLU B    64                                                      
REMARK 465     GLN B    65                                                      
REMARK 465     ASP B    66                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     GLU B    68                                                      
REMARK 465     GLU B    69                                                      
REMARK 465     ASP B    70                                                      
REMARK 465     GLU B    71                                                      
REMARK 465     GLU B    72                                                      
REMARK 465     VAL B   293                                                      
REMARK 465     TRP B   294                                                      
REMARK 465     LEU B   295                                                      
REMARK 465     VAL B   296                                                      
REMARK 465     ASN B   297                                                      
REMARK 465     MET B   298                                                      
REMARK 465     ALA B   299                                                      
REMARK 465     GLU B   300                                                      
REMARK 465     GLY B   301                                                      
REMARK 465     ASP B   302                                                      
REMARK 465     PRO B   303                                                      
REMARK 465     GLU B   304                                                      
REMARK 465     ALA B   305                                                      
REMARK 465     GLN B   306                                                      
REMARK 465     ARG B   307                                                      
REMARK 465     ARG B   308                                                      
REMARK 465     VAL B   309                                                      
REMARK 465     SER B   310                                                      
REMARK 465     LYS B   311                                                      
REMARK 465     ASN B   312                                                      
REMARK 465     SER B   313                                                      
REMARK 465     LYS B   314                                                      
REMARK 465     TYR B   315                                                      
REMARK 465     ASN B   316                                                      
REMARK 465     ALA B   317                                                      
REMARK 465     GLU B   318                                                      
REMARK 465     SER B   319                                                      
REMARK 465     THR B   320                                                      
REMARK 465     GLU B   321                                                      
REMARK 465     ARG B   322                                                      
REMARK 465     GLU B   323                                                      
REMARK 465     SER B   324                                                      
REMARK 465     GLN B   325                                                      
REMARK 465     ASP B   326                                                      
REMARK 465     THR B   327                                                      
REMARK 465     VAL B   328                                                      
REMARK 465     ALA B   329                                                      
REMARK 465     GLU B   330                                                      
REMARK 465     ASN B   331                                                      
REMARK 465     ASP B   332                                                      
REMARK 465     ASP B   333                                                      
REMARK 465     GLY B   334                                                      
REMARK 465     GLY B   335                                                      
REMARK 465     PHE B   336                                                      
REMARK 465     SER B   337                                                      
REMARK 465     GLU B   338                                                      
REMARK 465     GLU B   339                                                      
REMARK 465     TRP B   340                                                      
REMARK 465     GLU B   341                                                      
REMARK 465     ALA B   342                                                      
REMARK 465     GLN B   343                                                      
REMARK 465     ARG B   344                                                      
REMARK 465     ASP B   345                                                      
REMARK 465     SER B   346                                                      
REMARK 465     HIS B   347                                                      
REMARK 465     LEU B   348                                                      
REMARK 465     GLY B   349                                                      
REMARK 465     PRO B   350                                                      
REMARK 465     HIS B   351                                                      
REMARK 465     ARG B   352                                                      
REMARK 465     SER B   353                                                      
REMARK 465     THR B   354                                                      
REMARK 465     PRO B   355                                                      
REMARK 465     GLU B   356                                                      
REMARK 465     SER B   357                                                      
REMARK 465     ARG B   358                                                      
REMARK 465     ALA B   359                                                      
REMARK 465     ALA B   360                                                      
REMARK 465     VAL B   361                                                      
REMARK 465     GLN B   362                                                      
REMARK 465     GLU B   363                                                      
REMARK 465     LEU B   364                                                      
REMARK 465     SER B   365                                                      
REMARK 465     SER B   366                                                      
REMARK 465     SER B   367                                                      
REMARK 465     ILE B   368                                                      
REMARK 465     LEU B   369                                                      
REMARK 465     ALA B   370                                                      
REMARK 465     GLY B   371                                                      
REMARK 465     GLU B   372                                                      
REMARK 465     ASP B   373                                                      
REMARK 465     PRO B   374                                                      
REMARK 465     GLU B   375                                                      
REMARK 465     MET C     1                                                      
REMARK 465     CYS C   245                                                      
REMARK 465     ARG C   246                                                      
REMARK 465     ARG C   247                                                      
REMARK 465     GLN C   248                                                      
REMARK 465     GLU C   249                                                      
REMARK 465     ASP C   250                                                      
REMARK 465     SER C   251                                                      
REMARK 465     ARG C   252                                                      
REMARK 465     VAL C   253                                                      
REMARK 465     MET C   254                                                      
REMARK 465     VAL C   255                                                      
REMARK 465     TYR C   256                                                      
REMARK 465     SER C   257                                                      
REMARK 465     ALA C   258                                                      
REMARK 465     LEU C   259                                                      
REMARK 465     ARG C   260                                                      
REMARK 465     ILE C   261                                                      
REMARK 465     PRO C   262                                                      
REMARK 465     PRO C   263                                                      
REMARK 465     GLU C   264                                                      
REMARK 465     ASP C   265                                                      
REMARK 465     MET D     1                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ARG E    43                                                      
REMARK 465     GLN E    44                                                      
REMARK 465     HIS E    45                                                      
REMARK 465     GLY E    46                                                      
REMARK 465     GLN E    47                                                      
REMARK 465     LEU E    48                                                      
REMARK 465     TRP E    49                                                      
REMARK 465     PHE E    50                                                      
REMARK 465     PRO E    51                                                      
REMARK 465     GLU E    52                                                      
REMARK 465     GLY E    53                                                      
REMARK 465     PHE E    54                                                      
REMARK 465     LYS E    55                                                      
REMARK 465     VAL E    56                                                      
REMARK 465     SER E    57                                                      
REMARK 465     GLU E    58                                                      
REMARK 465     ALA E    59                                                      
REMARK 465     SER E    60                                                      
REMARK 465     LYS E    61                                                      
REMARK 465     LYS E    62                                                      
REMARK 465     LYS E    63                                                      
REMARK 465     ARG E    64                                                      
REMARK 465     ARG E    65                                                      
REMARK 465     GLU E    66                                                      
REMARK 465     PRO E    67                                                      
REMARK 465     LEU E    68                                                      
REMARK 465     GLY E    69                                                      
REMARK 465     GLU E    70                                                      
REMARK 465     ASP E    71                                                      
REMARK 465     SER E    72                                                      
REMARK 465     VAL E    73                                                      
REMARK 465     GLY E    74                                                      
REMARK 465     LEU E    75                                                      
REMARK 465     LYS E    76                                                      
REMARK 465     PRO E    77                                                      
REMARK 465     LEU E    78                                                      
REMARK 465     LYS E    79                                                      
REMARK 465     ASN E    80                                                      
REMARK 465     ALA E    81                                                      
REMARK 465     SER E    82                                                      
REMARK 465     ASP E    83                                                      
REMARK 465     GLY E    84                                                      
REMARK 465     ALA E    85                                                      
REMARK 465     LEU E    86                                                      
REMARK 465     MET E    87                                                      
REMARK 465     ASP E    88                                                      
REMARK 465     ASP E    89                                                      
REMARK 465     ASN E    90                                                      
REMARK 465     GLN E    91                                                      
REMARK 465     ASN E    92                                                      
REMARK 465     GLU E    93                                                      
REMARK 465     TRP E    94                                                      
REMARK 465     GLY E    95                                                      
REMARK 465     ASP E    96                                                      
REMARK 465     GLU E    97                                                      
REMARK 465     ASP E    98                                                      
REMARK 465     LEU E    99                                                      
REMARK 465     GLU E   100                                                      
REMARK 465     THR E   101                                                      
REMARK 465     GLU E   102                                                      
REMARK 465     GLN E   103                                                      
REMARK 465     LYS E   104                                                      
REMARK 465     LEU E   105                                                      
REMARK 465     ILE E   106                                                      
REMARK 465     SER E   107                                                      
REMARK 465     GLU E   108                                                      
REMARK 465     GLU E   109                                                      
REMARK 465     ASP E   110                                                      
REMARK 465     LEU E   111                                                      
REMARK 465     LEU E   112                                                      
REMARK 465     GLU E   113                                                      
REMARK 465     SER E   114                                                      
REMARK 465     ASP E   115                                                      
REMARK 465     GLU E   116                                                      
REMARK 465     VAL E   117                                                      
REMARK 465     ASP E   118                                                      
REMARK 465     ALA E   119                                                      
REMARK 465     ILE E   120                                                      
REMARK 465     GLU E   121                                                      
REMARK 465     HIS E   122                                                      
REMARK 465     HIS E   123                                                      
REMARK 465     HIS E   124                                                      
REMARK 465     HIS E   125                                                      
REMARK 465     HIS E   126                                                      
REMARK 465     HIS E   127                                                      
REMARK 465     HIS E   128                                                      
REMARK 465     HIS E   129                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU B  73    CG   CD1  CD2                                       
REMARK 470     LYS B  76    CG   CD   CE   NZ                                   
REMARK 470     LYS B 109    CG   CD   CE   NZ                                   
REMARK 470     ASP B 110    CG   OD1  OD2                                       
REMARK 470     LEU B 113    CG   CD1  CD2                                       
REMARK 470     TYR B 115    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR B 116    OG1  CG2                                            
REMARK 470     PRO B 117    CG   CD                                             
REMARK 470     PHE B 118    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR B 119    OG1  CG2                                            
REMARK 470     GLU B 120    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 121    CG   OD1  OD2                                       
REMARK 470     THR B 122    OG1  CG2                                            
REMARK 470     GLU B 123    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 279    CG   OD1  ND2                                       
REMARK 470     GLU B 280    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 376    CG   CD   OE1  OE2                                  
REMARK 470     PRO E  10    CG   CD                                             
REMARK 470     PRO E  11    CG   CD                                             
REMARK 470     PRO E  12    CG   CD                                             
REMARK 470     GLN E  14    CG   CD   OE1  NE2                                  
REMARK 470     LEU E  15    CG   CD1  CD2                                       
REMARK 470     HIS E  16    CG   ND1  CD2  CE1  NE2                             
REMARK 470     PHE E  17    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET E  18    CG   SD   CE                                        
REMARK 470     TYR E  19    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE E  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS E  40    CG   CD   CE   NZ                                   
REMARK 470     ARG E  41    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E  42    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 117   N   -  CA  -  CB  ANGL. DEV. =   7.7 DEGREES          
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    PHE A 210       53.91   -110.23                                   
REMARK 500    ASN A 243       73.71     57.52                                   
REMARK 500    THR A 265       -6.94     72.27                                   
REMARK 500    SER A 284     -169.35   -161.00                                   
REMARK 500    ALA A 292       80.12   -158.72                                   
REMARK 500    ASP A 317       69.33   -101.21                                   
REMARK 500    THR A 320       53.68    -93.86                                   
REMARK 500    PHE A 335     -159.39    -96.76                                   
REMARK 500    TYR A 337       70.28     53.78                                   
REMARK 500    LYS A 351       33.21    -93.10                                   
REMARK 500    GLN A 367       71.48     58.34                                   
REMARK 500    ARG A 371       73.38     58.22                                   
REMARK 500    ALA A 433      -30.38   -132.33                                   
REMARK 500    THR A 459     -168.57   -101.77                                   
REMARK 500    THR A 505       15.36     56.78                                   
REMARK 500    PHE A 507       52.31    -98.13                                   
REMARK 500    LEU A 617       79.52   -116.89                                   
REMARK 500    ARG A 626     -169.33   -128.73                                   
REMARK 500    LYS A 693       32.62    -96.73                                   
REMARK 500    LEU B 113     -158.04   -147.47                                   
REMARK 500    THR B 122      -70.96    -62.67                                   
REMARK 500    LYS B 155     -157.59   -147.70                                   
REMARK 500    ALA B 164       27.83   -140.59                                   
REMARK 500    LYS B 265       47.93    -91.75                                   
REMARK 500    LEU B 286       -4.91     67.59                                   
REMARK 500    TYR C 155       34.93    -96.86                                   
REMARK 500    SER C 235     -158.15   -148.49                                   
REMARK 500    ALA D  24       51.50    -92.28                                   
REMARK 500    VAL E  35      -53.73   -129.24                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASN A   91     PRO A   92                 -148.97                    
REMARK 500 PHE A  210     PRO A  211                  137.02                    
REMARK 500 LEU C  206     ASN C  207                 -147.88                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PC1 B  501                                                       
REMARK 610     PC1 B  502                                                       
REMARK 610     PC1 C  301                                                       
REMARK 610     PC1 D  201                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NAG A 821                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR C 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PC1 D 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  801 through NAG A 802 bound to ASN A 45                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  803 through BMA A 807 bound to ASN A 55                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 820 bound   
REMARK 800  to ASN A 187                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 819 bound   
REMARK 800  to ASN A 264                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 810 bound   
REMARK 800  to ASN A 387                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  808 through NAG A 809 bound to ASN A 435                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 817 bound   
REMARK 800  to ASN A 464                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 818 bound   
REMARK 800  to ASN A 506                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  813 through NAG A 814 bound to ASN A 530                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  815 through NAG A 816 bound to ASN A 562                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  811 through NAG A 812 bound to ASN A 573                            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-3061   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-3237   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-3238   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-3239   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-3240   RELATED DB: EMDB                              
REMARK 900 RELATED ID: EMD-9648   RELATED DB: EMDB                              
REMARK 900 CRYO-EM STRUCTURE OF GAMMA SECRETASE IN COMPLEX WITH A NOTCH         
REMARK 900 FRAGMENT                                                             
DBREF  6IDF A    1   709  UNP    Q92542   NICA_HUMAN       1    709             
DBREF  6IDF B    1   467  UNP    P49768   PSN1_HUMAN       1    467             
DBREF  6IDF C    1   265  UNP    Q96BI3   APH1A_HUMAN      1    265             
DBREF  6IDF D    1   101  UNP    Q9NZ42   PEN2_HUMAN       1    101             
DBREF  6IDF E    1   129  PDB    6IDF     6IDF             1    129             
SEQADV 6IDF CYS B  112  UNP  P49768    GLN   112 ENGINEERED MUTATION            
SEQADV 6IDF ALA B  385  UNP  P49768    ASP   385 ENGINEERED MUTATION            
SEQRES   1 A  709  MET ALA THR ALA GLY GLY GLY SER GLY ALA ASP PRO GLY          
SEQRES   2 A  709  SER ARG GLY LEU LEU ARG LEU LEU SER PHE CYS VAL LEU          
SEQRES   3 A  709  LEU ALA GLY LEU CYS ARG GLY ASN SER VAL GLU ARG LYS          
SEQRES   4 A  709  ILE TYR ILE PRO LEU ASN LYS THR ALA PRO CYS VAL ARG          
SEQRES   5 A  709  LEU LEU ASN ALA THR HIS GLN ILE GLY CYS GLN SER SER          
SEQRES   6 A  709  ILE SER GLY ASP THR GLY VAL ILE HIS VAL VAL GLU LYS          
SEQRES   7 A  709  GLU GLU ASP LEU GLN TRP VAL LEU THR ASP GLY PRO ASN          
SEQRES   8 A  709  PRO PRO TYR MET VAL LEU LEU GLU SER LYS HIS PHE THR          
SEQRES   9 A  709  ARG ASP LEU MET GLU LYS LEU LYS GLY ARG THR SER ARG          
SEQRES  10 A  709  ILE ALA GLY LEU ALA VAL SER LEU THR LYS PRO SER PRO          
SEQRES  11 A  709  ALA SER GLY PHE SER PRO SER VAL GLN CYS PRO ASN ASP          
SEQRES  12 A  709  GLY PHE GLY VAL TYR SER ASN SER TYR GLY PRO GLU PHE          
SEQRES  13 A  709  ALA HIS CYS ARG GLU ILE GLN TRP ASN SER LEU GLY ASN          
SEQRES  14 A  709  GLY LEU ALA TYR GLU ASP PHE SER PHE PRO ILE PHE LEU          
SEQRES  15 A  709  LEU GLU ASP GLU ASN GLU THR LYS VAL ILE LYS GLN CYS          
SEQRES  16 A  709  TYR GLN ASP HIS ASN LEU SER GLN ASN GLY SER ALA PRO          
SEQRES  17 A  709  THR PHE PRO LEU CYS ALA MET GLN LEU PHE SER HIS MET          
SEQRES  18 A  709  HIS ALA VAL ILE SER THR ALA THR CYS MET ARG ARG SER          
SEQRES  19 A  709  SER ILE GLN SER THR PHE SER ILE ASN PRO GLU ILE VAL          
SEQRES  20 A  709  CYS ASP PRO LEU SER ASP TYR ASN VAL TRP SER MET LEU          
SEQRES  21 A  709  LYS PRO ILE ASN THR THR GLY THR LEU LYS PRO ASP ASP          
SEQRES  22 A  709  ARG VAL VAL VAL ALA ALA THR ARG LEU ASP SER ARG SER          
SEQRES  23 A  709  PHE PHE TRP ASN VAL ALA PRO GLY ALA GLU SER ALA VAL          
SEQRES  24 A  709  ALA SER PHE VAL THR GLN LEU ALA ALA ALA GLU ALA LEU          
SEQRES  25 A  709  GLN LYS ALA PRO ASP VAL THR THR LEU PRO ARG ASN VAL          
SEQRES  26 A  709  MET PHE VAL PHE PHE GLN GLY GLU THR PHE ASP TYR ILE          
SEQRES  27 A  709  GLY SER SER ARG MET VAL TYR ASP MET GLU LYS GLY LYS          
SEQRES  28 A  709  PHE PRO VAL GLN LEU GLU ASN VAL ASP SER PHE VAL GLU          
SEQRES  29 A  709  LEU GLY GLN VAL ALA LEU ARG THR SER LEU GLU LEU TRP          
SEQRES  30 A  709  MET HIS THR ASP PRO VAL SER GLN LYS ASN GLU SER VAL          
SEQRES  31 A  709  ARG ASN GLN VAL GLU ASP LEU LEU ALA THR LEU GLU LYS          
SEQRES  32 A  709  SER GLY ALA GLY VAL PRO ALA VAL ILE LEU ARG ARG PRO          
SEQRES  33 A  709  ASN GLN SER GLN PRO LEU PRO PRO SER SER LEU GLN ARG          
SEQRES  34 A  709  PHE LEU ARG ALA ARG ASN ILE SER GLY VAL VAL LEU ALA          
SEQRES  35 A  709  ASP HIS SER GLY ALA PHE HIS ASN LYS TYR TYR GLN SER          
SEQRES  36 A  709  ILE TYR ASP THR ALA GLU ASN ILE ASN VAL SER TYR PRO          
SEQRES  37 A  709  GLU TRP LEU SER PRO GLU GLU ASP LEU ASN PHE VAL THR          
SEQRES  38 A  709  ASP THR ALA LYS ALA LEU ALA ASP VAL ALA THR VAL LEU          
SEQRES  39 A  709  GLY ARG ALA LEU TYR GLU LEU ALA GLY GLY THR ASN PHE          
SEQRES  40 A  709  SER ASP THR VAL GLN ALA ASP PRO GLN THR VAL THR ARG          
SEQRES  41 A  709  LEU LEU TYR GLY PHE LEU ILE LYS ALA ASN ASN SER TRP          
SEQRES  42 A  709  PHE GLN SER ILE LEU ARG GLN ASP LEU ARG SER TYR LEU          
SEQRES  43 A  709  GLY ASP GLY PRO LEU GLN HIS TYR ILE ALA VAL SER SER          
SEQRES  44 A  709  PRO THR ASN THR THR TYR VAL VAL GLN TYR ALA LEU ALA          
SEQRES  45 A  709  ASN LEU THR GLY THR VAL VAL ASN LEU THR ARG GLU GLN          
SEQRES  46 A  709  CYS GLN ASP PRO SER LYS VAL PRO SER GLU ASN LYS ASP          
SEQRES  47 A  709  LEU TYR GLU TYR SER TRP VAL GLN GLY PRO LEU HIS SER          
SEQRES  48 A  709  ASN GLU THR ASP ARG LEU PRO ARG CYS VAL ARG SER THR          
SEQRES  49 A  709  ALA ARG LEU ALA ARG ALA LEU SER PRO ALA PHE GLU LEU          
SEQRES  50 A  709  SER GLN TRP SER SER THR GLU TYR SER THR TRP THR GLU          
SEQRES  51 A  709  SER ARG TRP LYS ASP ILE ARG ALA ARG ILE PHE LEU ILE          
SEQRES  52 A  709  ALA SER LYS GLU LEU GLU LEU ILE THR LEU THR VAL GLY          
SEQRES  53 A  709  PHE GLY ILE LEU ILE PHE SER LEU ILE VAL THR TYR CYS          
SEQRES  54 A  709  ILE ASN ALA LYS ALA ASP VAL LEU PHE ILE ALA PRO ARG          
SEQRES  55 A  709  GLU PRO GLY ALA VAL SER TYR                                  
SEQRES   1 B  467  MET THR GLU LEU PRO ALA PRO LEU SER TYR PHE GLN ASN          
SEQRES   2 B  467  ALA GLN MET SER GLU ASP ASN HIS LEU SER ASN THR VAL          
SEQRES   3 B  467  ARG SER GLN ASN ASP ASN ARG GLU ARG GLN GLU HIS ASN          
SEQRES   4 B  467  ASP ARG ARG SER LEU GLY HIS PRO GLU PRO LEU SER ASN          
SEQRES   5 B  467  GLY ARG PRO GLN GLY ASN SER ARG GLN VAL VAL GLU GLN          
SEQRES   6 B  467  ASP GLU GLU GLU ASP GLU GLU LEU THR LEU LYS TYR GLY          
SEQRES   7 B  467  ALA LYS HIS VAL ILE MET LEU PHE VAL PRO VAL THR LEU          
SEQRES   8 B  467  CYS MET VAL VAL VAL VAL ALA THR ILE LYS SER VAL SER          
SEQRES   9 B  467  PHE TYR THR ARG LYS ASP GLY CYS LEU ILE TYR THR PRO          
SEQRES  10 B  467  PHE THR GLU ASP THR GLU THR VAL GLY GLN ARG ALA LEU          
SEQRES  11 B  467  HIS SER ILE LEU ASN ALA ALA ILE MET ILE SER VAL ILE          
SEQRES  12 B  467  VAL VAL MET THR ILE LEU LEU VAL VAL LEU TYR LYS TYR          
SEQRES  13 B  467  ARG CYS TYR LYS VAL ILE HIS ALA TRP LEU ILE ILE SER          
SEQRES  14 B  467  SER LEU LEU LEU LEU PHE PHE PHE SER PHE ILE TYR LEU          
SEQRES  15 B  467  GLY GLU VAL PHE LYS THR TYR ASN VAL ALA VAL ASP TYR          
SEQRES  16 B  467  ILE THR VAL ALA LEU LEU ILE TRP ASN PHE GLY VAL VAL          
SEQRES  17 B  467  GLY MET ILE SER ILE HIS TRP LYS GLY PRO LEU ARG LEU          
SEQRES  18 B  467  GLN GLN ALA TYR LEU ILE MET ILE SER ALA LEU MET ALA          
SEQRES  19 B  467  LEU VAL PHE ILE LYS TYR LEU PRO GLU TRP THR ALA TRP          
SEQRES  20 B  467  LEU ILE LEU ALA VAL ILE SER VAL TYR ASP LEU VAL ALA          
SEQRES  21 B  467  VAL LEU CYS PRO LYS GLY PRO LEU ARG MET LEU VAL GLU          
SEQRES  22 B  467  THR ALA GLN GLU ARG ASN GLU THR LEU PHE PRO ALA LEU          
SEQRES  23 B  467  ILE TYR SER SER THR MET VAL TRP LEU VAL ASN MET ALA          
SEQRES  24 B  467  GLU GLY ASP PRO GLU ALA GLN ARG ARG VAL SER LYS ASN          
SEQRES  25 B  467  SER LYS TYR ASN ALA GLU SER THR GLU ARG GLU SER GLN          
SEQRES  26 B  467  ASP THR VAL ALA GLU ASN ASP ASP GLY GLY PHE SER GLU          
SEQRES  27 B  467  GLU TRP GLU ALA GLN ARG ASP SER HIS LEU GLY PRO HIS          
SEQRES  28 B  467  ARG SER THR PRO GLU SER ARG ALA ALA VAL GLN GLU LEU          
SEQRES  29 B  467  SER SER SER ILE LEU ALA GLY GLU ASP PRO GLU GLU ARG          
SEQRES  30 B  467  GLY VAL LYS LEU GLY LEU GLY ALA PHE ILE PHE TYR SER          
SEQRES  31 B  467  VAL LEU VAL GLY LYS ALA SER ALA THR ALA SER GLY ASP          
SEQRES  32 B  467  TRP ASN THR THR ILE ALA CYS PHE VAL ALA ILE LEU ILE          
SEQRES  33 B  467  GLY LEU CYS LEU THR LEU LEU LEU LEU ALA ILE PHE LYS          
SEQRES  34 B  467  LYS ALA LEU PRO ALA LEU PRO ILE SER ILE THR PHE GLY          
SEQRES  35 B  467  LEU VAL PHE TYR PHE ALA THR ASP TYR LEU VAL GLN PRO          
SEQRES  36 B  467  PHE MET ASP GLN LEU ALA PHE HIS GLN PHE TYR ILE              
SEQRES   1 C  265  MET GLY ALA ALA VAL PHE PHE GLY CYS THR PHE VAL ALA          
SEQRES   2 C  265  PHE GLY PRO ALA PHE ALA LEU PHE LEU ILE THR VAL ALA          
SEQRES   3 C  265  GLY ASP PRO LEU ARG VAL ILE ILE LEU VAL ALA GLY ALA          
SEQRES   4 C  265  PHE PHE TRP LEU VAL SER LEU LEU LEU ALA SER VAL VAL          
SEQRES   5 C  265  TRP PHE ILE LEU VAL HIS VAL THR ASP ARG SER ASP ALA          
SEQRES   6 C  265  ARG LEU GLN TYR GLY LEU LEU ILE PHE GLY ALA ALA VAL          
SEQRES   7 C  265  SER VAL LEU LEU GLN GLU VAL PHE ARG PHE ALA TYR TYR          
SEQRES   8 C  265  LYS LEU LEU LYS LYS ALA ASP GLU GLY LEU ALA SER LEU          
SEQRES   9 C  265  SER GLU ASP GLY ARG SER PRO ILE SER ILE ARG GLN MET          
SEQRES  10 C  265  ALA TYR VAL SER GLY LEU SER PHE GLY ILE ILE SER GLY          
SEQRES  11 C  265  VAL PHE SER VAL ILE ASN ILE LEU ALA ASP ALA LEU GLY          
SEQRES  12 C  265  PRO GLY VAL VAL GLY ILE HIS GLY ASP SER PRO TYR TYR          
SEQRES  13 C  265  PHE LEU THR SER ALA PHE LEU THR ALA ALA ILE ILE LEU          
SEQRES  14 C  265  LEU HIS THR PHE TRP GLY VAL VAL PHE PHE ASP ALA CYS          
SEQRES  15 C  265  GLU ARG ARG ARG TYR TRP ALA LEU GLY LEU VAL VAL GLY          
SEQRES  16 C  265  SER HIS LEU LEU THR SER GLY LEU THR PHE LEU ASN PRO          
SEQRES  17 C  265  TRP TYR GLU ALA SER LEU LEU PRO ILE TYR ALA VAL THR          
SEQRES  18 C  265  VAL SER MET GLY LEU TRP ALA PHE ILE THR ALA GLY GLY          
SEQRES  19 C  265  SER LEU ARG SER ILE GLN ARG SER LEU LEU CYS ARG ARG          
SEQRES  20 C  265  GLN GLU ASP SER ARG VAL MET VAL TYR SER ALA LEU ARG          
SEQRES  21 C  265  ILE PRO PRO GLU ASP                                          
SEQRES   1 D  101  MET ASN LEU GLU ARG VAL SER ASN GLU GLU LYS LEU ASN          
SEQRES   2 D  101  LEU CYS ARG LYS TYR TYR LEU GLY GLY PHE ALA PHE LEU          
SEQRES   3 D  101  PRO PHE LEU TRP LEU VAL ASN ILE PHE TRP PHE PHE ARG          
SEQRES   4 D  101  GLU ALA PHE LEU VAL PRO ALA TYR THR GLU GLN SER GLN          
SEQRES   5 D  101  ILE LYS GLY TYR VAL TRP ARG SER ALA VAL GLY PHE LEU          
SEQRES   6 D  101  PHE TRP VAL ILE VAL LEU THR SER TRP ILE THR ILE PHE          
SEQRES   7 D  101  GLN ILE TYR ARG PRO ARG TRP GLY ALA LEU GLY ASP TYR          
SEQRES   8 D  101  LEU SER PHE THR ILE PRO LEU GLY THR PRO                      
SEQRES   1 E  129  MET VAL GLN SER GLU THR VAL GLU CYS PRO PRO PRO ALA          
SEQRES   2 E  129  GLN LEU HIS PHE MET TYR VAL ALA ALA ALA ALA PHE VAL          
SEQRES   3 E  129  LEU LEU PHE PHE VAL GLY CYS GLY VAL LEU LEU SER ARG          
SEQRES   4 E  129  LYS ARG ARG ARG GLN HIS GLY GLN LEU TRP PHE PRO GLU          
SEQRES   5 E  129  GLY PHE LYS VAL SER GLU ALA SER LYS LYS LYS ARG ARG          
SEQRES   6 E  129  GLU PRO LEU GLY GLU ASP SER VAL GLY LEU LYS PRO LEU          
SEQRES   7 E  129  LYS ASN ALA SER ASP GLY ALA LEU MET ASP ASP ASN GLN          
SEQRES   8 E  129  ASN GLU TRP GLY ASP GLU ASP LEU GLU THR GLU GLN LYS          
SEQRES   9 E  129  LEU ILE SER GLU GLU ASP LEU LEU GLU SER ASP GLU VAL          
SEQRES  10 E  129  ASP ALA ILE GLU HIS HIS HIS HIS HIS HIS HIS HIS              
HET    NAG  A 801      14                                                       
HET    NAG  A 802      14                                                       
HET    NAG  A 803      14                                                       
HET    NAG  A 804      14                                                       
HET    BMA  A 805      11                                                       
HET    BMA  A 806      11                                                       
HET    BMA  A 807      11                                                       
HET    NAG  A 808      14                                                       
HET    NAG  A 809      14                                                       
HET    NAG  A 810      14                                                       
HET    NAG  A 811      14                                                       
HET    NAG  A 812      14                                                       
HET    NAG  A 813      14                                                       
HET    NAG  A 814      14                                                       
HET    NAG  A 815      14                                                       
HET    NAG  A 816      14                                                       
HET    NAG  A 817      14                                                       
HET    NAG  A 818      14                                                       
HET    NAG  A 819      14                                                       
HET    NAG  A 820      14                                                       
HET    NAG  A 821      15                                                       
HET    PC1  B 501      52                                                       
HET    PC1  B 502      43                                                       
HET    PC1  C 301      50                                                       
HET    CLR  C 302      28                                                       
HET    CLR  C 303      28                                                       
HET    CLR  C 304      28                                                       
HET    PC1  D 201      39                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     PC1 1,2-DIACYL-SN-GLYCERO-3-PHOSPHOCHOLINE                           
HETNAM     CLR CHOLESTEROL                                                      
HETSYN     PC1 3-SN-PHOSPHATIDYLCHOLINE                                         
FORMUL   6  NAG    18(C8 H15 N O6)                                              
FORMUL   7  BMA    3(C6 H12 O6)                                                 
FORMUL  18  PC1    4(C44 H88 N O8 P)                                            
FORMUL  21  CLR    3(C27 H46 O)                                                 
HELIX    1 AA1 VAL A   36  ILE A   40  5                                   5    
HELIX    2 AA2 GLU A   80  ASP A   88  1                                   9    
HELIX    3 AA3 THR A  104  ARG A  114  1                                  11    
HELIX    4 AA4 ASN A  142  GLY A  146  5                                   5    
HELIX    5 AA5 GLY A  170  GLU A  174  5                                   5    
HELIX    6 AA6 ASP A  185  ASN A  200  1                                  16    
HELIX    7 AA7 SER A  226  GLN A  237  1                                  12    
HELIX    8 AA8 ALA A  298  LYS A  314  1                                  17    
HELIX    9 AA9 TYR A  337  GLY A  350  1                                  14    
HELIX   10 AB1 VAL A  383  LYS A  386  5                                   4    
HELIX   11 AB2 ASN A  387  GLY A  405  1                                  19    
HELIX   12 AB3 SER A  426  LEU A  431  1                                   6    
HELIX   13 AB4 THR A  483  GLY A  503  1                                  21    
HELIX   14 AB5 ASP A  514  ILE A  527  1                                  14    
HELIX   15 AB6 TRP A  533  ILE A  537  5                                   5    
HELIX   16 AB7 ARG A  539  LEU A  546  5                                   8    
HELIX   17 AB8 THR A  561  GLY A  576  1                                  16    
HELIX   18 AB9 THR A  582  ASP A  588  1                                   7    
HELIX   19 AC1 SER A  632  GLU A  636  5                                   5    
HELIX   20 AC2 SER A  665  LYS A  693  1                                  29    
HELIX   21 AC3 LYS A  693  PHE A  698  1                                   6    
HELIX   22 AC4 THR B   74  VAL B  103  1                                  30    
HELIX   23 AC5 THR B  124  TYR B  154  1                                  31    
HELIX   24 AC6 CYS B  158  LEU B  166  1                                   9    
HELIX   25 AC7 ILE B  167  PHE B  175  1                                   9    
HELIX   26 AC8 PHE B  176  TYR B  189  1                                  14    
HELIX   27 AC9 TYR B  195  HIS B  214  1                                  20    
HELIX   28 AD1 PRO B  218  TYR B  240  1                                  23    
HELIX   29 AD2 PRO B  242  CYS B  263  1                                  22    
HELIX   30 AD3 GLY B  266  ARG B  278  1                                  13    
HELIX   31 AD4 LEU B  383  THR B  399  1                                  17    
HELIX   32 AD5 TRP B  404  LYS B  429  1                                  26    
HELIX   33 AD6 ALA B  434  ASP B  450  1                                  17    
HELIX   34 AD7 VAL B  453  GLN B  464  1                                  12    
HELIX   35 AD8 ALA C    3  PHE C   14  1                                  12    
HELIX   36 AD9 GLY C   15  VAL C   25  1                                  11    
HELIX   37 AE1 ASP C   28  THR C   60  1                                  33    
HELIX   38 AE2 LEU C   67  ASP C  107  1                                  41    
HELIX   39 AE3 SER C  113  ALA C  139  1                                  27    
HELIX   40 AE4 ASP C  140  LEU C  142  5                                   3    
HELIX   41 AE5 TYR C  155  ARG C  185  1                                  31    
HELIX   42 AE6 TRP C  188  LEU C  203  1                                  16    
HELIX   43 AE7 THR C  204  ASN C  207  5                                   4    
HELIX   44 AE8 TRP C  209  SER C  213  5                                   5    
HELIX   45 AE9 LEU C  214  ALA C  232  1                                  19    
HELIX   46 AF1 SER C  235  LEU C  243  1                                   9    
HELIX   47 AF2 SER D    7  GLY D   21  1                                  15    
HELIX   48 AF3 GLY D   22  ALA D   24  5                                   3    
HELIX   49 AF4 LEU D   26  PHE D   42  1                                  17    
HELIX   50 AF5 GLN D   52  ARG D   59  1                                   8    
HELIX   51 AF6 ARG D   59  TYR D   81  1                                  23    
HELIX   52 AF7 ALA D   87  LEU D   92  1                                   6    
HELIX   53 AF8 GLN E    3  GLU E    8  5                                   6    
HELIX   54 AF9 HIS E   16  ALA E   23  1                                   8    
HELIX   55 AG1 ALA E   23  LEU E   28  1                                   6    
SHEET    1 AA1 8 ILE A  42  LEU A  44  0                                        
SHEET    2 AA1 8 ARG A 657  ILE A 663 -1  O  ALA A 658   N  LEU A  44           
SHEET    3 AA1 8 LEU A 212  PHE A 218 -1  N  ALA A 214   O  PHE A 661           
SHEET    4 AA1 8 ASP A  69  VAL A  76 -1  N  GLY A  71   O  MET A 215           
SHEET    5 AA1 8 TYR A  94  GLU A  99  1  O  LEU A  97   N  VAL A  76           
SHEET    6 AA1 8 ILE A 118  SER A 124  1  O  ALA A 119   N  TYR A  94           
SHEET    7 AA1 8 ILE A 180  LEU A 183  1  O  LEU A 183   N  VAL A 123           
SHEET    8 AA1 8 THR A  47  PRO A  49 -1  N  ALA A  48   O  LEU A 182           
SHEET    1 AA2 3 GLN A  59  ILE A  60  0                                        
SHEET    2 AA2 3 LEU A  53  LEU A  54 -1  N  LEU A  53   O  ILE A  60           
SHEET    3 AA2 3 THR A 649  GLU A 650 -1  O  THR A 649   N  LEU A  54           
SHEET    1 AA3 2 MET A 221  HIS A 222  0                                        
SHEET    2 AA3 2 ARG A 652  TRP A 653 -1  O  ARG A 652   N  HIS A 222           
SHEET    1 AA4 8 ILE A 412  ARG A 414  0                                        
SHEET    2 AA4 8 GLU A 375  HIS A 379  1  N  LEU A 376   O  ILE A 412           
SHEET    3 AA4 8 GLY A 438  ALA A 442 -1  O  VAL A 440   N  HIS A 379           
SHEET    4 AA4 8 VAL A 359  LEU A 365  1  N  GLU A 364   O  LEU A 441           
SHEET    5 AA4 8 VAL A 275  ARG A 281  1  N  VAL A 275   O  ASP A 360           
SHEET    6 AA4 8 ASN A 324  PHE A 330  1  O  MET A 326   N  ALA A 278           
SHEET    7 AA4 8 ASP A 253  MET A 259 -1  N  SER A 258   O  PHE A 327           
SHEET    8 AA4 8 ARG A 626  ALA A 630 -1  O  ALA A 628   N  ASN A 255           
SHEET    1 AA5 3 THR A 577  VAL A 579  0                                        
SHEET    2 AA5 3 ARG A 619  SER A 623 -1  O  ARG A 622   N  THR A 577           
SHEET    3 AA5 3 GLU A 601  VAL A 605 -1  N  VAL A 605   O  ARG A 619           
SHEET    1 AA6 2 VAL B 193  ASP B 194  0                                        
SHEET    2 AA6 2 SER D  93  THR D  95 -1  O  PHE D  94   N  VAL B 193           
SHEET    1 AA7 4 ILE B 287  SER B 289  0                                        
SHEET    2 AA7 4 ARG B 377  GLY B 382 -1  O  LEU B 381   N  TYR B 288           
SHEET    3 AA7 4 LEU E  36  ARG E  41 -1  O  LYS E  40   N  GLY B 378           
SHEET    4 AA7 4 LEU B 432  PRO B 433 -1  N  LEU B 432   O  LEU E  37           
SSBOND   1 CYS A   50    CYS A   62                          1555   1555  2.04  
SSBOND   2 CYS A  140    CYS A  159                          1555   1555  2.03  
SSBOND   3 CYS A  230    CYS A  248                          1555   1555  2.02  
SSBOND   4 CYS A  586    CYS A  620                          1555   1555  2.03  
SSBOND   5 CYS B  112    CYS E    9                          1555   1555  2.03  
LINK         ND2 ASN A  45                 C1  NAG A 801     1555   1555  1.44  
LINK         ND2 ASN A  55                 C1  NAG A 803     1555   1555  1.44  
LINK         ND2 ASN A 187                 C1  NAG A 820     1555   1555  1.44  
LINK         ND2 ASN A 264                 C1  NAG A 819     1555   1555  1.46  
LINK         ND2 ASN A 387                 C1  NAG A 810     1555   1555  1.44  
LINK         ND2 ASN A 435                 C1  NAG A 808     1555   1555  1.43  
LINK         ND2 ASN A 464                 C1  NAG A 817     1555   1555  1.46  
LINK         ND2 ASN A 506                 C1  NAG A 818     1555   1555  1.45  
LINK         ND2 ASN A 530                 C1  NAG A 813     1555   1555  1.44  
LINK         ND2 ASN A 562                 C1  NAG A 815     1555   1555  1.44  
LINK         ND2 ASN A 573                 C1  NAG A 811     1555   1555  1.46  
LINK         O   GLY C 202                 C19 CLR C 302     1555   1555  1.38  
LINK         O4  NAG A 801                 C1  NAG A 802     1555   1555  1.44  
LINK         O4  NAG A 803                 C1  NAG A 804     1555   1555  1.44  
LINK         O4  NAG A 804                 C1  BMA A 805     1555   1555  1.45  
LINK         O3  BMA A 805                 C1  BMA A 807     1555   1555  1.45  
LINK         O6  BMA A 805                 C1  BMA A 806     1555   1555  1.45  
LINK         O4  NAG A 808                 C1  NAG A 809     1555   1555  1.45  
LINK         O4  NAG A 811                 C1  NAG A 812     1555   1555  1.48  
LINK         O4  NAG A 813                 C1  NAG A 814     1555   1555  1.45  
LINK         O4  NAG A 815                 C1  NAG A 816     1555   1555  1.44  
SITE     1 AC1  1 ASN A 580                                                     
SITE     1 AC2  3 LYS B 101  TRP B 404  LEU C 142                               
SITE     1 AC3  3 ARG B 128  TRP B 244  TYR B 451                               
SITE     1 AC4  7 PHE A 698  SER C 113  GLN C 116  TYR C 119                    
SITE     2 AC4  7 VAL C 176  GLY C 225  ALA C 232                               
SITE     1 AC5  4 GLY C 202  LEU C 203  PHE C 205  LEU C 206                    
SITE     1 AC6  4 TRP C 188  LEU C 192  SER C 223  TRP C 227                    
SITE     1 AC7  3 TYR C 155  PHE C 162  LEU C 214                               
SITE     1 AC8  6 PRO B 218  ARG B 220  LEU D   3  PHE D  28                    
SITE     2 AC8  6 PHE D  35  TRP D  36                                          
SITE     1 AC9  3 PRO A  43  ASN A  45  HIS C 150                               
SITE     1 AD1  5 ASN A  55  HIS A  58  PHE A 145  TYR A 173                    
SITE     2 AD1  5 GLU A 174                                                     
SITE     1 AD2  1 ASN A 187                                                     
SITE     1 AD3  4 ASN A 264  THR A 266  ASN A 596  ASP A 598                    
SITE     1 AD4  1 ASN A 387                                                     
SITE     1 AD5  5 TYR A 152  VAL A 383  LYS A 386  ALA A 433                    
SITE     2 AD5  5 ASN A 435                                                     
SITE     1 AD6  1 ASN A 464                                                     
SITE     1 AD7  3 GLY A 504  THR A 505  ASN A 506                               
SITE     1 AD8  2 ASN A 530  GLN A 535                                          
SITE     1 AD9  5 SER A 544  TYR A 545  GLY A 547  PRO A 550                    
SITE     2 AD9  5 ASN A 562                                                     
SITE     1 AE1  4 TRP A 533  ASN A 573  ARG A 619  VAL A 621                    
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      0.002864  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002864  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002864        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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