GenomeNet

Database: PDB
Entry: 4UIS
LinkDB: 4UIS
Original site: 4UIS 
HEADER    HYDROLASE                               03-APR-15   4UIS              
TITLE     THE CRYOEM STRUCTURE OF HUMAN GAMMA-SECRETASE COMPLEX                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GAMMA-SECRETASE;                                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: GAMMA-SECRETASE;                                           
COMPND   7 CHAIN: B;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: GAMMA-SECRETASE;                                           
COMPND  11 CHAIN: C;                                                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: GAMMA-SECRETASE;                                           
COMPND  15 CHAIN: D;                                                            
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 MOL_ID: 5;                                                           
COMPND  18 MOLECULE: LYSOZYME;                                                  
COMPND  19 CHAIN: G;                                                            
COMPND  20 EC: 3.2.1.17;                                                        
COMPND  21 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293S;                               
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: HEK 293S;                               
SOURCE  17 MOL_ID: 3;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  22 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  24 EXPRESSION_SYSTEM_CELL_LINE: HEK 293S;                               
SOURCE  25 MOL_ID: 4;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  27 ORGANISM_COMMON: HUMAN;                                              
SOURCE  28 ORGANISM_TAXID: 9606;                                                
SOURCE  29 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  30 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  31 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  32 EXPRESSION_SYSTEM_CELL_LINE: HEK 293S;                               
SOURCE  33 MOL_ID: 5;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  35 ORGANISM_COMMON: HUMAN;                                              
SOURCE  36 ORGANISM_TAXID: 9606;                                                
SOURCE  37 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  38 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  39 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  40 EXPRESSION_SYSTEM_CELL_LINE: HEK 293S                                
KEYWDS    HYDROLASE, GAMMA-SECRETASE                                            
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    L.SUN,L.ZHAO,G.YANG,C.YAN,R.ZHOU,X.ZHOU,T.XIE,Y.ZHAO,S.WU,X.LI,Y.SHI  
REVDAT   2   02-AUG-17 4UIS    1                                                
REVDAT   1   10-JUN-15 4UIS    0                                                
JRNL        AUTH   L.SUN,L.ZHAO,G.YANG,C.YAN,R.ZHOU,X.ZHOU,T.XIE,Y.ZHAO,S.WU,   
JRNL        AUTH 2 X.LI,Y.SHI                                                   
JRNL        TITL   STRUCTURAL BASIS OF HUMAN GAMMA-SECRETASE ASSEMBLY.          
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 112  6003 2015              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   25918421                                                     
JRNL        DOI    10.1073/PNAS.1506242112                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : UCSF CHIMERA, RELION                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 4R12                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : METHOD--FLEXIBLE                                 
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 1.320                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 4.400                          
REMARK   3   NUMBER OF PARTICLES               : 177207                         
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD   
REMARK   3  -2974. (DEPOSITION ID: 13293                                        
REMARK   4                                                                      
REMARK   4 4UIS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1290063530.                                   
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                 : T4-LYSOZYME FUSION GAMMA-         
REMARK 245                                    SECRETASE                         
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 4.20                              
REMARK 245   SAMPLE SUPPORT DETAILS         : HOLEY CARBON                      
REMARK 245   SAMPLE VITRIFICATION DETAILS   : VITRIFICATION 1 -- CRYOGEN-       
REMARK 245                                    ETHANE, HUMIDITY- 100,            
REMARK 245                                    TEMPERATURE- 277, INSTRUMENT-     
REMARK 245                                    FEI VITROBOT MARK IV, METHOD-     
REMARK 245                                    BLOT FOR 3 SECONDS BEFORE         
REMARK 245                                    PLUNGING,                         
REMARK 245   SAMPLE BUFFER                  : 0.1% DIGITONIN, 25 MM HEPES, PH   
REMARK 245                                    7.4, AND 150 MM NACL.             
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 22-DEC-14                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : DIRECT ELECTRON DE-12 (4K X    
REMARK 245                                       3K)                            
REMARK 245   MINIMUM DEFOCUS (NM)              : 1500.00                        
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                        : 1.40                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 4.50                           
REMARK 245   ILLUMINATION MODE                 : SPOT SCAN                      
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, G                         
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 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     LYS A 351    CG   CD   CE   NZ                                   
REMARK 470     PHE A 352    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     THR A 372    OG1  CG2                                            
REMARK 470     SER A 373    OG                                                  
REMARK 470     LEU A 374    CG   CD1  CD2                                       
REMARK 470     GLU A 375    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 528    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    UNK D    42     N    UNK D    44              1.55            
REMARK 500   OE2  GLU G    11     NH1  ARG G   145              1.84            
REMARK 500   CB   CYS A   230     SG   CYS A   248              1.87            
REMARK 500   O    GLN A   516     CD   ARG A   520              1.87            
REMARK 500   CB   SER A   219     CG2  ILE A   656              1.91            
REMARK 500   OD2  ASP G    10     ND2  ASN G   101              2.01            
REMARK 500   OD2  ASP B   257     OD1  ASP B   385              2.02            
REMARK 500   OD1  ASP A   317     OG1  THR A   320              2.12            
REMARK 500   CE2  TYR A   467     CE2  TYR A   523              2.14            
REMARK 500   OG   SER A   100     OH   TYR A   457              2.16            
REMARK 500   CB   CYS A    50     SG   CYS A    62              2.17            
REMARK 500   O    SER A   226     OG1  THR A   229              2.17            
REMARK 500   O    ILE B   227     OG   SER B   230              2.18            
REMARK 500   O    TYR A   337     OG   SER A   340              2.19            
REMARK 500   O    GLU A   186     OG1  THR A   189              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 A  90   C   -  N   -  CA  ANGL. DEV. =  -9.7 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    ASN A  45      -98.73    -82.42                                   
REMARK 500    SER A  67      -71.80     65.25                                   
REMARK 500    ASP A  88      -78.39    -63.88                                   
REMARK 500    PRO A  93       67.13    -65.09                                   
REMARK 500    ARG A 117     -165.96     62.04                                   
REMARK 500    CYS A 159     -123.70     39.07                                   
REMARK 500    ASP A 185      128.01     64.13                                   
REMARK 500    GLN A 197      -70.03    -49.20                                   
REMARK 500    ASN A 200      -39.56   -137.35                                   
REMARK 500    SER A 202       -2.77     58.02                                   
REMARK 500    ASN A 204      -50.06   -179.05                                   
REMARK 500    LEU A 212     -176.76   -178.44                                   
REMARK 500    SER A 219       68.41   -172.98                                   
REMARK 500    HIS A 222       55.02   -114.70                                   
REMARK 500    ILE A 225      -82.58     66.55                                   
REMARK 500    ASP A 253     -119.82   -173.58                                   
REMARK 500    VAL A 256     -157.91   -103.34                                   
REMARK 500    SER A 258      137.62   -170.99                                   
REMARK 500    ASP A 274       46.95   -160.19                                   
REMARK 500    ASP A 283      -93.80   -101.90                                   
REMARK 500    SER A 284       99.01     56.35                                   
REMARK 500    ARG A 285     -147.09    -72.95                                   
REMARK 500    TRP A 289      105.35     19.87                                   
REMARK 500    VAL A 291     -131.39    -84.18                                   
REMARK 500    ALA A 295     -106.73   -123.84                                   
REMARK 500    ALA A 298      -53.38   -156.13                                   
REMARK 500    GLN A 305      -74.60    -54.97                                   
REMARK 500    PHE A 335     -101.01    -72.75                                   
REMARK 500    ASP A 336     -119.42    -75.20                                   
REMARK 500    ILE A 338     -122.27     36.15                                   
REMARK 500    PRO A 353       46.50    -70.09                                   
REMARK 500    ASN A 358     -152.51    -75.62                                   
REMARK 500    VAL A 359      139.46     69.89                                   
REMARK 500    ASP A 360      -58.25   -122.82                                   
REMARK 500    ALA A 369      -49.39   -161.70                                   
REMARK 500    ARG A 371     -158.50     45.35                                   
REMARK 500    THR A 372       38.93   -162.12                                   
REMARK 500    LEU A 374       78.76   -173.06                                   
REMARK 500    LEU A 376      146.17     72.95                                   
REMARK 500    THR A 380     -156.20   -129.34                                   
REMARK 500    PRO A 409     -156.86    -65.73                                   
REMARK 500    ALA A 410       84.65     51.93                                   
REMARK 500    ILE A 436      151.49     62.78                                   
REMARK 500    SER A 437     -140.50    -70.31                                   
REMARK 500    VAL A 439      117.31     67.03                                   
REMARK 500    LYS A 451      -81.29     57.04                                   
REMARK 500    GLN A 454       39.62     33.94                                   
REMARK 500    ASN A 464       70.39     62.21                                   
REMARK 500    PRO A 473     -105.65    -70.60                                   
REMARK 500    THR A 481     -142.86     51.85                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      97 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-2974   RELATED DB: EMDB                              
DBREF  4UIS A   42   688  PDB    4UIS     4UIS            42    688             
DBREF  4UIS B   69   465  PDB    4UIS     4UIS            69    465             
DBREF  4UIS C    1   222  PDB    4UIS     4UIS             1    222             
DBREF  4UIS D    5    75  PDB    4UIS     4UIS             5     75             
DBREF1 4UIS G    1   162  UNP                  A0A097J809_BPT4                  
DBREF2 4UIS G     A0A097J809                          1         162             
SEQRES   1 A  588  ILE PRO LEU ASN LYS THR ALA PRO CYS VAL ARG LEU LEU          
SEQRES   2 A  588  ASN ALA THR HIS GLN ILE GLY CYS GLN SER SER ILE SER          
SEQRES   3 A  588  GLY ASP THR GLY VAL ILE HIS VAL VAL GLU LYS GLU GLU          
SEQRES   4 A  588  ASP LEU GLN TRP VAL LEU THR ASP GLY PRO ASN PRO PRO          
SEQRES   5 A  588  TYR MET VAL LEU LEU GLU SER LYS HIS PHE THR ARG ASP          
SEQRES   6 A  588  LEU MET GLU LYS LEU LYS GLY ARG THR SER ARG ILE ALA          
SEQRES   7 A  588  GLY LEU ALA VAL SER LEU THR LYS PRO SER PRO ALA SER          
SEQRES   8 A  588  GLY PHE SER PRO SER VAL GLN CYS PRO ASN ASP GLY PHE          
SEQRES   9 A  588  GLY VAL TYR HIS CYS ARG GLU ILE GLN TRP ASN SER LEU          
SEQRES  10 A  588  GLY ASN GLY LEU ALA TYR GLU ASP PHE SER PHE PRO ILE          
SEQRES  11 A  588  PHE LEU LEU GLU ASP GLU ASN GLU THR LYS VAL ILE LYS          
SEQRES  12 A  588  GLN CYS TYR GLN ASP HIS ASN LEU SER GLN ASN GLY SER          
SEQRES  13 A  588  ALA PRO THR PHE PRO LEU CYS ALA MET GLN LEU PHE SER          
SEQRES  14 A  588  HIS MET HIS ALA VAL ILE SER THR ALA THR CYS MET ARG          
SEQRES  15 A  588  ARG SER SER ILE ALA ALA VAL CYS ASP PRO LEU SER ASP          
SEQRES  16 A  588  TYR ASN VAL TRP SER MET LEU LYS PRO ILE ALA ASP ASP          
SEQRES  17 A  588  VAL VAL VAL ALA ALA THR ARG LEU ASP SER ARG SER PHE          
SEQRES  18 A  588  ALA TRP ASN VAL ALA PRO GLY ALA GLU SER ALA VAL ALA          
SEQRES  19 A  588  SER PHE VAL THR GLN LEU ALA ALA ALA GLU ALA LEU GLN          
SEQRES  20 A  588  LYS ALA PRO ASP VAL THR THR LEU PRO ARG ASN VAL MET          
SEQRES  21 A  588  PHE VAL PHE PHE GLN GLY GLU THR PHE ASP TYR ILE GLY          
SEQRES  22 A  588  SER SER ARG MET VAL TYR ASP MET GLU LYS GLY LYS PHE          
SEQRES  23 A  588  PRO VAL GLN LEU GLU ASN VAL ASP SER PHE VAL GLU LEU          
SEQRES  24 A  588  GLY GLN VAL ALA LEU ARG THR SER LEU GLU LEU TRP MET          
SEQRES  25 A  588  HIS THR ASP PRO VAL GLN LYS ASN GLU SER VAL ARG ASN          
SEQRES  26 A  588  GLN VAL GLU ASP LEU GLY ALA GLY VAL PRO ALA VAL ILE          
SEQRES  27 A  588  LEU ARG SER GLY VAL PRO LEU PRO PRO SER SER LEU GLN          
SEQRES  28 A  588  ARG PHE LEU ARG ALA ARG ASN ILE SER GLY VAL VAL LEU          
SEQRES  29 A  588  ALA ASP HIS SER GLY ALA PHE HIS ASN LYS TYR TYR GLN          
SEQRES  30 A  588  SER ILE TYR ASP THR ALA GLU ASN ILE ASN VAL SER TYR          
SEQRES  31 A  588  PRO GLU TRP LEU ALA PRO GLU GLU ASP LEU ASN PHE VAL          
SEQRES  32 A  588  THR ASP THR ALA LYS ALA LEU ALA ASP VAL ALA THR VAL          
SEQRES  33 A  588  LEU GLY ARG ALA LEU TYR GLU LEU ALA GLY GLY ASP THR          
SEQRES  34 A  588  VAL GLN ALA ASP PRO GLN THR VAL THR ARG LEU LEU TYR          
SEQRES  35 A  588  GLY PHE LEU ILE LYS LEU ARG GLN ASP LEU ARG SER TYR          
SEQRES  36 A  588  LEU GLY ASP GLY PRO LEU GLN HIS TYR ILE ALA VAL SER          
SEQRES  37 A  588  SER PRO THR ASN THR THR TYR VAL VAL GLN TYR ALA LEU          
SEQRES  38 A  588  ALA ASN LEU THR GLY THR VAL VAL UNK UNK UNK UNK UNK          
SEQRES  39 A  588  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  40 A  588  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  41 A  588  UNK UNK UNK UNK UNK UNK UNK THR ALA ARG LEU ALA ARG          
SEQRES  42 A  588  ALA LEU SER PRO ALA GLN TRP SER SER THR GLU TYR SER          
SEQRES  43 A  588  THR TRP THR GLU SER ARG TRP LYS ALA ILE ARG ALA ARG          
SEQRES  44 A  588  ILE PHE LEU ILE ALA SER UNK UNK UNK UNK UNK UNK UNK          
SEQRES  45 A  588  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  46 A  588  UNK UNK UNK                                                  
SEQRES   1 B  241  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK HIS          
SEQRES   2 B  241  VAL ILE MET LEU PHE VAL PRO VAL THR LEU CYS MET VAL          
SEQRES   3 B  241  VAL VAL VAL ALA THR ILE UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 B  241  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 B  241  UNK UNK UNK UNK UNK UNK UNK LEU LEU LEU PHE PHE PHE          
SEQRES   6 B  241  SER PHE ILE TYR LEU GLY GLU VAL PHE LYS THR TYR UNK          
SEQRES   7 B  241  UNK UNK UNK UNK UNK UNK UNK UNK UNK LEU ILE TRP ASN          
SEQRES   8 B  241  PHE GLY UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   9 B  241  UNK UNK ARG LEU GLN GLN ALA TYR LEU ILE MET ILE SER          
SEQRES  10 B  241  ALA LEU MET UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  11 B  241  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK ASP UNK UNK          
SEQRES  12 B  241  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  13 B  241  UNK UNK UNK UNK UNK ASP UNK UNK UNK UNK UNK UNK UNK          
SEQRES  14 B  241  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK TRP ASN          
SEQRES  15 B  241  THR THR ILE ALA CYS PHE VAL ALA ILE LEU ILE GLY LEU          
SEQRES  16 B  241  CYS LEU THR LEU LEU UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  17 B  241  UNK UNK UNK UNK UNK UNK UNK UNK UNK GLY LEU VAL PHE          
SEQRES  18 B  241  TYR PHE ALA THR ASP TYR LEU VAL GLN PRO PHE ALA ASP          
SEQRES  19 B  241  GLN LEU ALA PHE HIS UNK UNK                                  
SEQRES   1 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   6 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   7 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   8 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   9 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  10 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  11 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  12 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  13 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  14 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  15 C  196  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES  16 C  196  UNK                                                          
SEQRES   1 D   62  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 D   62  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 D   62  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   4 D   62  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   5 D   62  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK                      
SEQRES   1 G  162  MET ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU          
SEQRES   2 G  162  ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR          
SEQRES   3 G  162  ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU          
SEQRES   4 G  162  ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG          
SEQRES   5 G  162  ASN CYS ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS          
SEQRES   6 G  162  LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE          
SEQRES   7 G  162  LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU          
SEQRES   8 G  162  ASP ALA VAL ARG ARG CYS ALA LEU ILE ASN MET VAL PHE          
SEQRES   9 G  162  GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER          
SEQRES  10 G  162  LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA          
SEQRES  11 G  162  VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO          
SEQRES  12 G  162  ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY          
SEQRES  13 G  162  THR TRP ASP ALA TYR LYS                                      
HELIX    1   1 LYS A   78  THR A   87  1                                  10    
HELIX    2   2 THR A  104  GLY A  113  1                                  10    
HELIX    3   3 ASP A  185  LEU A  201  1                                  17    
HELIX    4   4 SER A  226  ARG A  233  1                                   8    
HELIX    5   5 ALA A  298  LYS A  314  1                                  17    
HELIX    6   6 ALA A  315  THR A  320  5                                   6    
HELIX    7   7 TYR A  337  LYS A  349  1                                  13    
HELIX    8   8 GLN A  392  VAL A  408  1                                  17    
HELIX    9   9 SER A  426  ARG A  432  1                                   7    
HELIX   10  10 THR A  459  ASN A  464  1                                   6    
HELIX   11  11 PRO A  473  ASN A  478  1                                   6    
HELIX   12  12 THR A  483  GLY A  503  1                                  21    
HELIX   13  13 ASP A  514  ILE A  527  1                                  14    
HELIX   14  14 LEU A  538  LEU A  542  5                                   5    
HELIX   15  15 THR A  561  THR A  575  1                                  15    
HELIX   16  16 UNK A  588  UNK A  595  1                                   8    
HELIX   17  17 SER A  665  UNK A  687  1                                  23    
HELIX   18  18 UNK B   69  UNK B  101  1                                  33    
HELIX   19  19 UNK B  137  UNK B  155  1                                  19    
HELIX   20  20 UNK B  167  UNK B  190  1                                  24    
HELIX   21  21 UNK B  194  UNK B  216  1                                  23    
HELIX   22  22 UNK B  218  UNK B  241  1                                  24    
HELIX   23  23 UNK B  246  UNK B  271  1                                  26    
HELIX   24  24 UNK B  382  UNK B  400  1                                  19    
HELIX   25  25 TRP B  404  UNK B  427  1                                  24    
HELIX   26  26 UNK B  434  LEU B  452  1                                  19    
HELIX   27  27 LEU B  452  HIS B  463  1                                  12    
HELIX   28  28 UNK C    2  UNK C   22  1                                  21    
HELIX   29  29 UNK C   25  UNK C   34  1                                  10    
HELIX   30  30 UNK C   36  UNK C   56  1                                  21    
HELIX   31  31 UNK C   72  UNK C  102  1                                  31    
HELIX   32  32 UNK C  109  UNK C  122  1                                  14    
HELIX   33  33 UNK C  123  UNK C  135  1                                  13    
HELIX   34  34 UNK C  152  UNK C  178  1                                  27    
HELIX   35  35 UNK C  179  UNK C  184  1                                   6    
HELIX   36  36 UNK C  184  UNK C  198  1                                  15    
HELIX   37  37 UNK C  204  UNK C  220  1                                  17    
HELIX   38  38 UNK D    7  UNK D   17  1                                  11    
HELIX   39  39 UNK D   18  UNK D   20  5                                   3    
HELIX   40  40 UNK D   21  UNK D   31  1                                  11    
HELIX   41  41 UNK D   43  UNK D   72  1                                  30    
HELIX   42  42 UNK D   73  UNK D   75  5                                   3    
HELIX   43  43 MET G    6  GLY G   12  1                                   7    
HELIX   44  44 SER G   38  GLY G   51  1                                  14    
HELIX   45  45 THR G   59  VAL G   75  1                                  17    
HELIX   46  46 GLY G   77  ASN G   81  5                                   5    
HELIX   47  47 LYS G   83  LEU G   91  1                                   9    
HELIX   48  48 ASP G   92  MET G  106  1                                  15    
HELIX   49  49 GLY G  107  GLY G  113  1                                   7    
HELIX   50  50 PHE G  114  GLN G  123  1                                  10    
HELIX   51  51 ARG G  125  ALA G  134  1                                  10    
HELIX   52  52 THR G  142  GLY G  156  1                                  15    
HELIX   53  53 TRP G  158  LYS G  162  5                                   5    
SHEET    1  AA 3 THR A  47  ALA A  48  0                                        
SHEET    2  AA 3 ILE A 180  LEU A 183 -1  O  LEU A 182   N  ALA A  48           
SHEET    3  AA 3 LEU A 121  SER A 124  1  O  LEU A 121   N  PHE A 181           
SHEET    1  AB 2 LEU A  53  LEU A  54  0                                        
SHEET    2  AB 2 GLN A  59  ILE A  60 -1  O  ILE A  60   N  LEU A  53           
SHEET    1  AC 4 TYR A  94  MET A  95  0                                        
SHEET    2  AC 4 ASP A  69  ILE A  73  1  O  VAL A  72   N  MET A  95           
SHEET    3  AC 4 CYS A 213  PHE A 218 -1  O  CYS A 213   N  ILE A  73           
SHEET    4  AC 4 ARG A 657  LEU A 662 -1  O  ARG A 657   N  PHE A 218           
SHEET    1  AD 2 CYS A 248  PRO A 250  0                                        
SHEET    2  AD 2 THR A 649  SER A 651 -1  O  GLU A 650   N  ASP A 249           
SHEET    1  AE 2 ASP A 253  ASN A 255  0                                        
SHEET    2  AE 2 ARG A 629  ALA A 631 -1  O  ARG A 629   N  ASN A 255           
SHEET    1  AF 2 VAL A 275  VAL A 277  0                                        
SHEET    2  AF 2 ASN A 324  MET A 326  1  O  ASN A 324   N  VAL A 276           
SHEET    1  AG 2 THR A 280  ARG A 281  0                                        
SHEET    2  AG 2 PHE A 329  PHE A 330  1  N  PHE A 330   O  THR A 280           
SHEET    1  AH 2 LEU A 365  GLY A 366  0                                        
SHEET    2  AH 2 LEU A 441  ALA A 442  1  O  LEU A 441   N  GLY A 366           
SHEET    1  AI 2 UNK A 605  UNK A 606  0                                        
SHEET    2  AI 2 UNK A 621  UNK A 622 -1  O  UNK A 622   N  UNK A 605           
SHEET    1  GA 3 ILE G  17  LYS G  19  0                                        
SHEET    2  GA 3 TYR G  25  ILE G  27 -1  O  THR G  26   N  TYR G  18           
SHEET    3  GA 3 HIS G  31  THR G  34 -1  O  HIS G  31   N  ILE G  27           
SSBOND   1 CYS A   50    CYS A   62                          1555   1555  2.04  
SSBOND   2 CYS A  195    CYS A  213                          1555   1555  2.03  
SSBOND   3 CYS A  230    CYS A  248                          1555   1555  2.04  
CISPEP   1 HIS A  158    CYS A  159          0       -10.37                     
CISPEP   2 ASN A  204    GLY A  205          0        10.30                     
CISPEP   3 GLY A  205    SER A  206          0         3.37                     
CISPEP   4 ALA A  207    PRO A  208          0       -23.66                     
CISPEP   5 UNK C  139    UNK C  140          0         4.99                     
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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