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Database: PDB
Entry: 6MEO
LinkDB: 6MEO
Original site: 6MEO 
HEADER    MEMBRANE PROTEIN                        06-SEP-18   6MEO              
TITLE     STRUCTURAL BASIS OF CORECEPTOR RECOGNITION BY HIV-1 ENVELOPE SPIKE    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENVELOPE GLYCOPROTEIN GP160;                               
COMPND   3 CHAIN: G;                                                            
COMPND   4 FRAGMENT: GP120 DOMAIN RESIDUES 29-489;                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: T-CELL SURFACE GLYCOPROTEIN CD4;                           
COMPND   8 CHAIN: A;                                                            
COMPND   9 FRAGMENT: IG-LIKE V-TYPE AND IG-LIKE C2-TYPE 1 DOMAINS, RESIDUES 26- 
COMPND  10 201;                                                                 
COMPND  11 SYNONYM: T-CELL SURFACE ANTIGEN T4/LEU-3;                            
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: C-C CHEMOKINE RECEPTOR TYPE 5;                             
COMPND  15 CHAIN: B;                                                            
COMPND  16 FRAGMENT: RESIDUES 1-313;                                            
COMPND  17 SYNONYM: CCR5,CHEMR13,HIV-1 FUSION CORECEPTOR;                       
COMPND  18 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 GENE: ENV;                                                           
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: 293T;                                   
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: CD4;                                                           
SOURCE  14 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  15 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  17 EXPRESSION_SYSTEM_CELL_LINE: 293T;                                   
SOURCE  18 MOL_ID: 3;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  20 ORGANISM_COMMON: HUMAN;                                              
SOURCE  21 ORGANISM_TAXID: 9606;                                                
SOURCE  22 GENE: CCR5, CMKBR5;                                                  
SOURCE  23 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  24 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  26 EXPRESSION_SYSTEM_CELL_LINE: 293T                                    
KEYWDS    HIV CORECEPTOR, MEMBRANE PROTEIN                                      
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    M.M.SHAIK,B.CHEN                                                      
REVDAT   5   29-JUL-20 6MEO    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE   ATOM                              
REVDAT   4   18-DEC-19 6MEO    1       REMARK                                   
REVDAT   3   16-JAN-19 6MEO    1       JRNL                                     
REVDAT   2   26-DEC-18 6MEO    1       JRNL                                     
REVDAT   1   12-DEC-18 6MEO    0                                                
JRNL        AUTH   M.M.SHAIK,H.PENG,J.LU,S.RITS-VOLLOCH,C.XU,M.LIAO,B.CHEN      
JRNL        TITL   STRUCTURAL BASIS OF CORECEPTOR RECOGNITION BY HIV-1 ENVELOPE 
JRNL        TITL 2 SPIKE.                                                       
JRNL        REF    NATURE                        V. 565   318 2018              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   30542158                                                     
JRNL        DOI    10.1038/S41586-018-0804-9                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : SERIALEM, CTFFIND, UCSF CHIMERA,          
REMARK   3                            RELION, PHENIX                            
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 5UIW                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : 200.000                             
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.900                          
REMARK   3   NUMBER OF PARTICLES               : 307346                         
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6MEO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000236675.                                   
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                 : C-C CHEMOKINE RECEPTOR TYPE 5     
REMARK 245                                    (CCR5) IN COMPLEX WITH T-CELL     
REMARK 245                                    SURFACE GLYCOPROTEIN CD4 AND      
REMARK 245                                    HIV1 ENVELOPE GLYCOPROTEIN        
REMARK 245                                    GP120; ENVELOPE GLYCOPROTEIN      
REMARK 245                                    GP160; T-CELL SURFACE             
REMARK 245                                    GLYCOPROTEIN CD4; C-C CHEMOKINE   
REMARK 245                                    RECEPTOR TYPE 5                   
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 1.00                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN 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                        : 2.70                           
REMARK 245   IMAGING MODE                      : OTHER                          
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 46.00                          
REMARK 245   ILLUMINATION MODE                 : OTHER                          
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, A, B, C, D, E, F, H, I, J,         
REMARK 350                    AND CHAINS: K, L                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ASP G   132                                                      
REMARK 465     LEU G   133                                                      
REMARK 465     ASN G   134                                                      
REMARK 465     ASN G   135                                                      
REMARK 465     SER G   136                                                      
REMARK 465     THR G   137                                                      
REMARK 465     ASN G   138                                                      
REMARK 465     ASN G   139                                                      
REMARK 465     ASN G   140                                                      
REMARK 465     ASN G   141                                                      
REMARK 465     SER G   142                                                      
REMARK 465     SER G   143                                                      
REMARK 465     GLY G   144                                                      
REMARK 465     VAL G   145                                                      
REMARK 465     LYS G   146                                                      
REMARK 465     THR G   147                                                      
REMARK 465     GLY G   148                                                      
REMARK 465     ILE G   149                                                      
REMARK 465     ASP G   150                                                      
REMARK 465     LYS G   151                                                      
REMARK 465     GLY G   152                                                      
REMARK 465     GLU G   153                                                      
REMARK 465     ILE G   154                                                      
REMARK 465     LYS G   155                                                      
REMARK 465     ASN G   156                                                      
REMARK 465     CYS G   157                                                      
REMARK 465     SER G   158                                                      
REMARK 465     PHE G   159                                                      
REMARK 465     ASN G   160                                                      
REMARK 465     THR G   161                                                      
REMARK 465     THR G   162                                                      
REMARK 465     THR G   163                                                      
REMARK 465     SER G   164                                                      
REMARK 465     VAL G   165                                                      
REMARK 465     LYS G   166                                                      
REMARK 465     ASP G   167                                                      
REMARK 465     LYS G   168                                                      
REMARK 465     GLU G   169                                                      
REMARK 465     LYS G   170                                                      
REMARK 465     LYS G   171                                                      
REMARK 465     GLU G   172                                                      
REMARK 465     TYR G   173                                                      
REMARK 465     ALA G   174                                                      
REMARK 465     LEU G   175                                                      
REMARK 465     PHE G   176                                                      
REMARK 465     TYR G   177                                                      
REMARK 465     ASN G   178                                                      
REMARK 465     LEU G   179                                                      
REMARK 465     ASP G   180                                                      
REMARK 465     VAL G   181                                                      
REMARK 465     VAL G   182                                                      
REMARK 465     GLN G   183                                                      
REMARK 465     ILE G   184                                                      
REMARK 465     GLY G   185                                                      
REMARK 465     ASN G   186                                                      
REMARK 465     GLY G   399                                                      
REMARK 465     THR G   400                                                      
REMARK 465     SER G   401                                                      
REMARK 465     ASN G   402                                                      
REMARK 465     THR G   403                                                      
REMARK 465     THR G   404                                                      
REMARK 465     GLY G   405                                                      
REMARK 465     ASN G   406                                                      
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     ILE G 131    CG1  CG2  CD1                                       
REMARK 470     ASP G 187    CG   OD1  OD2                                       
REMARK 470     ASN G 188    CG   OD1  ND2                                       
REMARK 470     THR G 189    OG1  CG2                                            
REMARK 470     SER G 190    OG                                                  
REMARK 470     TYR G 191    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG G 192    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER B     7     C1   A2G B   401              1.81            
REMARK 500   O6   BMA E     3     C1   BMA G   612              1.92            
REMARK 500   CG2  THR G   209     O4   MAN E     4              1.98            
REMARK 500   ND2  ASN G   384     O5   NAG K     1              2.15            
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    CYS G  73      161.73    178.70                                   
REMARK 500    VAL G 126      -73.91   -116.56                                   
REMARK 500    THR G 127      118.03   -173.10                                   
REMARK 500    PHE G 233       -9.87     68.69                                   
REMARK 500    ASN G 234       -8.89     62.38                                   
REMARK 500    THR G 236       32.02    -94.88                                   
REMARK 500    GLN G 258      -11.89     70.38                                   
REMARK 500    LEU G 261     -156.52    -80.98                                   
REMARK 500    ASN G 262      126.28    -34.80                                   
REMARK 500    THR G 278       -7.40     75.27                                   
REMARK 500    ALA G 281      -36.65   -143.71                                   
REMARK 500    HIS G 308       56.86    -91.07                                   
REMARK 500    ALA G 317      160.33    -48.46                                   
REMARK 500    GLU G 353       61.94     62.37                                   
REMARK 500    ASN G 354       62.34     62.84                                   
REMARK 500    GLN G 387       44.86    -86.79                                   
REMARK 500    LEU G 388      -18.29   -141.80                                   
REMARK 500    GLU G 424     -161.19     70.24                                   
REMARK 500    TYR G 430     -169.20   -105.56                                   
REMARK 500    LEU G 479       34.35    -97.26                                   
REMARK 500    ILE A  36      -54.61   -121.71                                   
REMARK 500    GLU A 150     -169.89   -124.82                                   
REMARK 500    ARG B  60       10.35     90.76                                   
REMARK 500    LEU B  61       40.81     37.39                                   
REMARK 500    LYS B  62        4.19    -66.81                                   
REMARK 500    ALA B  92      -81.06   -126.36                                   
REMARK 500    GLN B  93     -156.61   -160.92                                   
REMARK 500    ASN B  98      -26.43   -145.13                                   
REMARK 500    CYS B 178       78.49   -107.09                                   
REMARK 500    HIS B 181       79.62   -104.77                                   
REMARK 500    LEU B 203      -50.58   -121.54                                   
REMARK 500    GLU B 262     -159.96    -85.51                                   
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     BMA G  612                                                       
REMARK 610     A2G B  401                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-9108   RELATED DB: EMDB                              
REMARK 900 STRUCTURAL BASIS OF CORECEPTOR RECOGNITION BY HIV-1 ENVELOPE SPIKE   
DBREF  6MEO G   31   491  UNP    Q70145   Q70145_9HIV1    29    489             
DBREF  6MEO A    1   176  UNP    P01730   CD4_HUMAN       26    201             
DBREF  6MEO B    1   313  UNP    P51681   CCR5_HUMAN       1    313             
SEQRES   1 G  461  ASP ASN LEU TRP VAL THR VAL TYR TYR GLY VAL PRO VAL          
SEQRES   2 G  461  TRP LYS GLU ALA THR THR THR LEU PHE CYS ALA SER ASP          
SEQRES   3 G  461  ALA LYS ALA TYR LYS ALA GLU VAL HIS ASN VAL TRP ALA          
SEQRES   4 G  461  THR HIS ALA CYS VAL PRO THR ASP PRO ASN PRO GLN GLU          
SEQRES   5 G  461  ILE VAL LEU GLU ASN VAL THR GLU ASN PHE ASN MET TRP          
SEQRES   6 G  461  LYS ASN ASN MET VAL GLU GLN MET HIS GLU ASP ILE ILE          
SEQRES   7 G  461  SER LEU TRP ASP GLN SER LEU LYS PRO CYS VAL LYS LEU          
SEQRES   8 G  461  THR PRO LEU CYS VAL THR LEU ASN CYS ILE ASP LEU ASN          
SEQRES   9 G  461  ASN SER THR ASN ASN ASN ASN SER SER GLY VAL LYS THR          
SEQRES  10 G  461  GLY ILE ASP LYS GLY GLU ILE LYS ASN CYS SER PHE ASN          
SEQRES  11 G  461  THR THR THR SER VAL LYS ASP LYS GLU LYS LYS GLU TYR          
SEQRES  12 G  461  ALA LEU PHE TYR ASN LEU ASP VAL VAL GLN ILE GLY ASN          
SEQRES  13 G  461  ASP ASN THR SER TYR ARG LEU THR SER CYS ASN THR SER          
SEQRES  14 G  461  VAL ILE THR GLN ALA CYS PRO LYS VAL THR PHE GLU PRO          
SEQRES  15 G  461  ILE PRO ILE HIS TYR CYS THR PRO ALA GLY TYR ALA ILE          
SEQRES  16 G  461  LEU LYS CYS ASN GLY LYS LYS PHE ASN GLY THR GLY PRO          
SEQRES  17 G  461  CYS THR ASN VAL SER THR VAL GLN CYS THR HIS GLY ILE          
SEQRES  18 G  461  LYS PRO VAL VAL SER THR GLN LEU LEU LEU ASN GLY SER          
SEQRES  19 G  461  LEU ALA GLU GLU ASP ILE VAL ILE ARG SER GLU ASN LEU          
SEQRES  20 G  461  THR ASN ASN ALA LYS THR ILE ILE VAL GLN LEU LYS ASP          
SEQRES  21 G  461  PRO VAL ASP ILE ASN CYS THR ARG PRO ASN ASN ASN THR          
SEQRES  22 G  461  ARG LYS SER ILE HIS ILE GLY PRO GLY ARG ALA PHE TYR          
SEQRES  23 G  461  ALA THR GLY ASP ILE ILE GLY ASP ILE ARG GLN ALA HIS          
SEQRES  24 G  461  CYS ASN LEU SER ARG ALA GLN TRP ASN ASP THR LEU SER          
SEQRES  25 G  461  LYS ILE VAL THR LYS LEU ARG GLU GLN PHE GLU ASN LYS          
SEQRES  26 G  461  THR ILE LYS PHE GLN PRO PRO SER GLY GLY ASP PRO GLU          
SEQRES  27 G  461  ILE VAL PHE HIS SER PHE ASN CYS GLY GLY GLU PHE PHE          
SEQRES  28 G  461  TYR CYS ASN THR THR GLN LEU PHE ASN SER THR TRP THR          
SEQRES  29 G  461  ASN ASN THR GLU GLY THR SER ASN THR THR GLY ASN ASP          
SEQRES  30 G  461  THR ILE THR LEU PRO CYS ARG ILE LYS GLN ILE VAL ASN          
SEQRES  31 G  461  MET TRP GLN GLU VAL GLY LYS ALA MET TYR ALA PRO PRO          
SEQRES  32 G  461  ILE LYS GLY LYS ILE LYS CYS SER SER ASN ILE THR GLY          
SEQRES  33 G  461  LEU LEU LEU THR ARG ASP GLY GLY ASN ASN GLU MET ASN          
SEQRES  34 G  461  THR THR GLU ILE PHE ARG PRO GLY GLY GLY ASP MET ARG          
SEQRES  35 G  461  ASP ASN TRP ARG SER GLU LEU TYR LYS TYR LYS VAL VAL          
SEQRES  36 G  461  ARG ILE GLU PRO LEU GLY                                      
SEQRES   1 A  176  LYS LYS VAL VAL LEU GLY LYS LYS GLY ASP THR VAL GLU          
SEQRES   2 A  176  LEU THR CYS THR ALA SER GLN LYS LYS SER ILE GLN PHE          
SEQRES   3 A  176  HIS TRP LYS ASN SER ASN GLN ILE LYS ILE LEU GLY ASN          
SEQRES   4 A  176  GLN GLY SER PHE LEU THR LYS GLY PRO SER LYS LEU ASN          
SEQRES   5 A  176  ASP ARG ALA ASP SER ARG ARG SER LEU TRP ASP GLN GLY          
SEQRES   6 A  176  ASN PHE PRO LEU ILE ILE LYS ASN LEU LYS ILE GLU ASP          
SEQRES   7 A  176  SER ASP THR TYR ILE CYS GLU VAL GLU ASP GLN LYS GLU          
SEQRES   8 A  176  GLU VAL GLN LEU LEU VAL PHE GLY LEU THR ALA ASN SER          
SEQRES   9 A  176  ASP THR HIS LEU LEU GLN GLY GLN SER LEU THR LEU THR          
SEQRES  10 A  176  LEU GLU SER PRO PRO GLY SER SER PRO SER VAL GLN CYS          
SEQRES  11 A  176  ARG SER PRO ARG GLY LYS ASN ILE GLN GLY GLY LYS THR          
SEQRES  12 A  176  LEU SER VAL SER GLN LEU GLU LEU GLN ASP SER GLY THR          
SEQRES  13 A  176  TRP THR CYS THR VAL LEU GLN ASN GLN LYS LYS VAL GLU          
SEQRES  14 A  176  PHE LYS ILE ASP ILE VAL VAL                                  
SEQRES   1 B  313  MET ASP TYR GLN VAL SER SER PRO ILE TYS ASP ILE ASN          
SEQRES   2 B  313  TYS TYR THR SER GLU PRO CYS GLN LYS ILE ASN VAL LYS          
SEQRES   3 B  313  GLN ILE ALA ALA ARG LEU LEU PRO PRO LEU TYR SER LEU          
SEQRES   4 B  313  VAL PHE ILE PHE GLY PHE VAL GLY ASN MET LEU VAL ILE          
SEQRES   5 B  313  LEU ILE LEU ILE ASN CYS LYS ARG LEU LYS SER MET THR          
SEQRES   6 B  313  ASP ILE TYR LEU LEU ASN LEU ALA ILE SER ASP LEU PHE          
SEQRES   7 B  313  PHE LEU LEU THR VAL PRO PHE TRP ALA HIS TYR ALA ALA          
SEQRES   8 B  313  ALA GLN TRP ASP PHE GLY ASN THR MET CYS GLN LEU LEU          
SEQRES   9 B  313  THR GLY LEU TYR PHE ILE GLY PHE PHE SER GLY ILE PHE          
SEQRES  10 B  313  PHE ILE ILE LEU LEU THR ILE ASP ARG TYR LEU ALA VAL          
SEQRES  11 B  313  VAL HIS ALA VAL PHE ALA LEU LYS ALA ARG THR VAL THR          
SEQRES  12 B  313  PHE GLY VAL VAL THR SER VAL ILE THR TRP VAL VAL ALA          
SEQRES  13 B  313  VAL PHE ALA SER LEU PRO GLY ILE ILE PHE THR ARG SER          
SEQRES  14 B  313  GLN LYS GLU GLY LEU HIS TYR THR CYS SER SER HIS PHE          
SEQRES  15 B  313  PRO TYR SER GLN TYR GLN PHE TRP LYS ASN PHE GLN THR          
SEQRES  16 B  313  LEU LYS ILE VAL ILE LEU GLY LEU VAL LEU PRO LEU LEU          
SEQRES  17 B  313  VAL MET VAL ILE CYS TYR SER GLY ILE LEU LYS THR LEU          
SEQRES  18 B  313  LEU ARG CYS ARG ASN GLU LYS LYS ARG HIS ARG ALA VAL          
SEQRES  19 B  313  ARG LEU ILE PHE THR ILE MET ILE VAL TYR PHE LEU PHE          
SEQRES  20 B  313  TRP ALA PRO TYR ASN ILE VAL LEU LEU LEU ASN THR PHE          
SEQRES  21 B  313  GLN GLU PHE PHE GLY LEU ASN ASN CYS SER SER SER ASN          
SEQRES  22 B  313  ARG LEU ASP GLN ALA MET GLN VAL THR GLU THR LEU GLY          
SEQRES  23 B  313  MET THR HIS CYS CYS ILE ASN PRO ILE ILE TYR ALA PHE          
SEQRES  24 B  313  VAL GLY GLU LYS PHE ARG ASN TYR LEU LEU VAL PHE PHE          
SEQRES  25 B  313  GLN                                                          
MODRES 6MEO TYS B   10  TYR  MODIFIED RESIDUE                                   
MODRES 6MEO TYS B   14  TYR  MODIFIED RESIDUE                                   
HET    TYS  B  10      16                                                       
HET    TYS  B  14      16                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    BMA  D   3      11                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    MAN  E   4      11                                                       
HET    MAN  E   5      11                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    BMA  J   3      11                                                       
HET    NAG  K   1      14                                                       
HET    NAG  K   2      14                                                       
HET    NAG  L   1      14                                                       
HET    NAG  L   2      14                                                       
HET    NAG  G 601      14                                                       
HET    BMA  G 612      11                                                       
HET    NAG  G 619      14                                                       
HET    NAG  G 620      14                                                       
HET    NAG  G 626      14                                                       
HET    NAG  G 627      14                                                       
HET    NAG  G 628      14                                                       
HET    NAG  G 631      14                                                       
HET    A2G  B 401      14                                                       
HETNAM     TYS O-SULFO-L-TYROSINE                                               
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     A2G 2-ACETAMIDO-2-DEOXY-ALPHA-D-GALACTOPYRANOSE                      
FORMUL   3  TYS    2(C9 H11 N O6 S)                                             
FORMUL   4  NAG    25(C8 H15 N O6)                                              
FORMUL   5  BMA    4(C6 H12 O6)                                                 
FORMUL   6  MAN    2(C6 H12 O6)                                                 
FORMUL  21  A2G    C8 H15 N O6                                                  
HELIX    1 AA1 GLU G   63  ALA G   72  1                                  10    
HELIX    2 AA2 MET G   99  LEU G  115  1                                  17    
HELIX    3 AA3 ARG G  334  GLU G  353  1                                  20    
HELIX    4 AA4 ASP G  366  PHE G  371  1                                   6    
HELIX    5 AA5 THR G  385  PHE G  389  5                                   5    
HELIX    6 AA6 ASP G  470  SER G  477  1                                   8    
HELIX    7 AA7 ARG A   58  GLN A   64  5                                   7    
HELIX    8 AA8 GLU A  150  SER A  154  5                                   5    
HELIX    9 AA9 LYS B   26  ARG B   31  1                                   6    
HELIX   10 AB1 LEU B   32  CYS B   58  1                                  27    
HELIX   11 AB2 SER B   63  LEU B   81  1                                  19    
HELIX   12 AB3 THR B   82  ALA B   91  1                                  10    
HELIX   13 AB4 MET B  100  VAL B  131  1                                  32    
HELIX   14 AB5 HIS B  132  ARG B  140  1                                   9    
HELIX   15 AB6 THR B  141  ALA B  159  1                                  19    
HELIX   16 AB7 SER B  160  ILE B  165  5                                   6    
HELIX   17 AB8 GLN B  186  LEU B  203  1                                  18    
HELIX   18 AB9 LEU B  203  CYS B  224  1                                  22    
HELIX   19 AC1 GLU B  227  PHE B  260  1                                  34    
HELIX   20 AC2 ASN B  268  THR B  288  1                                  21    
HELIX   21 AC3 CYS B  291  VAL B  300  1                                  10    
HELIX   22 AC4 ARG B  305  GLN B  313  1                                   9    
SHEET    1 AA1 5 LYS G  45  GLU G  46  0                                        
SHEET    2 AA1 5 TYR G 482  ARG G 486 -1  O  ARG G 486   N  LYS G  45           
SHEET    3 AA1 5 TYR G 223  CYS G 228 -1  N  ALA G 224   O  VAL G 485           
SHEET    4 AA1 5 VAL G 242  VAL G 245 -1  O  SER G 243   N  LYS G 227           
SHEET    5 AA1 5 ILE G  83  VAL G  84 -1  N  ILE G  83   O  THR G 244           
SHEET    1 AA2 2 PHE G  52  SER G  55  0                                        
SHEET    2 AA2 2 ILE G 215  CYS G 218 -1  O  CYS G 218   N  PHE G  52           
SHEET    1 AA3 4 CYS G 196  THR G 202  0                                        
SHEET    2 AA3 4 VAL G 119  CYS G 125 -1  N  LEU G 124   O  ASN G 197           
SHEET    3 AA3 4 LYS G 427  MET G 429 -1  O  MET G 429   N  VAL G 119           
SHEET    4 AA3 4 VAL G 419  ASN G 420 -1  N  VAL G 419   O  ALA G 428           
SHEET    1 AA4 3 VAL G 271  ARG G 273  0                                        
SHEET    2 AA4 3 ILE G 284  GLN G 287 -1  O  ILE G 285   N  ARG G 273           
SHEET    3 AA4 3 GLY G 446  LEU G 449 -1  O  LEU G 449   N  ILE G 284           
SHEET    1 AA5 4 THR G 408  ARG G 414  0                                        
SHEET    2 AA5 4 GLN G 327  SER G 333 -1  N  CYS G 330   O  LEU G 411           
SHEET    3 AA5 4 ILE G 294  THR G 297 -1  N  THR G 297   O  HIS G 329           
SHEET    4 AA5 4 LYS G 439  SER G 442 -1  O  CYS G 440   N  CYS G 296           
SHEET    1 AA6 2 ILE G 357  PHE G 359  0                                        
SHEET    2 AA6 2 GLU G 462  PHE G 464  1  O  GLU G 462   N  LYS G 358           
SHEET    1 AA7 2 HIS G 372  CYS G 376  0                                        
SHEET    2 AA7 2 GLU G 379  CYS G 383 -1  O  CYS G 383   N  HIS G 372           
SHEET    1 AA8 2 LEU A   5  GLY A   6  0                                        
SHEET    2 AA8 2 LEU A  96  VAL A  97  1  O  LEU A  96   N  GLY A   6           
SHEET    1 AA9 3 VAL A  12  GLU A  13  0                                        
SHEET    2 AA9 3 ILE A  70  ILE A  71 -1  O  ILE A  71   N  VAL A  12           
SHEET    3 AA9 3 ALA A  55  ASP A  56 -1  N  ASP A  56   O  ILE A  70           
SHEET    1 AB1 4 PHE A  43  LEU A  44  0                                        
SHEET    2 AB1 4 LYS A  35  GLN A  40 -1  N  GLN A  40   O  PHE A  43           
SHEET    3 AB1 4 HIS A  27  ASN A  30 -1  N  TRP A  28   O  ILE A  36           
SHEET    4 AB1 4 TYR A  82  CYS A  84 -1  O  ILE A  83   N  LYS A  29           
SHEET    1 AB2 2 GLY A  99  THR A 101  0                                        
SHEET    2 AB2 2 THR A 117  GLU A 119 -1  O  GLU A 119   N  GLY A  99           
SHEET    1 AB3 2 LEU A 114  THR A 115  0                                        
SHEET    2 AB3 2 SER A 145  VAL A 146 -1  O  VAL A 146   N  LEU A 114           
SHEET    1 AB4 2 VAL A 128  ARG A 131  0                                        
SHEET    2 AB4 2 THR A 158  VAL A 161 -1  O  THR A 160   N  GLN A 129           
SSBOND   1 CYS G   53    CYS G   73                          1555   1555  2.03  
SSBOND   2 CYS G  118    CYS G  205                          1555   1555  2.03  
SSBOND   3 CYS G  125    CYS G  196                          1555   1555  2.03  
SSBOND   4 CYS G  218    CYS G  247                          1555   1555  2.03  
SSBOND   5 CYS G  228    CYS G  239                          1555   1555  2.04  
SSBOND   6 CYS G  296    CYS G  330                          1555   1555  2.03  
SSBOND   7 CYS G  376    CYS G  440                          1555   1555  2.03  
SSBOND   8 CYS G  383    CYS G  413                          1555   1555  2.03  
SSBOND   9 CYS A   16    CYS A   84                          1555   1555  2.04  
SSBOND  10 CYS A  130    CYS A  159                          1555   1555  2.03  
SSBOND  11 CYS B   20    CYS B  269                          1555   1555  2.03  
SSBOND  12 CYS B  101    CYS B  178                          1555   1555  2.03  
LINK         ND2 ASN G  87                 C1  NAG G 601     1555   1555  1.44  
LINK         ND2 ASN G 197                 C1  NAG G 628     1555   1555  1.43  
LINK         ND2 ASN G 234                 C1  NAG C   1     1555   1555  1.44  
LINK         ND2 ASN G 241                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN G 262                 C1  NAG E   1     1555   1555  1.44  
LINK         ND2 ASN G 276                 C1  NAG F   1     1555   1555  1.44  
LINK         ND2 ASN G 295                 C1  NAG H   1     1555   1555  1.44  
LINK         ND2 ASN G 301                 C1  NAG J   1     1555   1555  1.46  
LINK         ND2 ASN G 331                 C1  NAG I   1     1555   1555  1.45  
LINK         ND2 ASN G 338                 C1  NAG G 619     1555   1555  1.44  
LINK         ND2 ASN G 354                 C1  NAG G 620     1555   1555  1.45  
LINK         ND2 ASN G 384                 C1  NAG K   1     1555   1555  1.47  
LINK         ND2 ASN G 390                 C1  NAG G 631     1555   1555  1.44  
LINK         ND2 ASN G 395                 C1  NAG G 626     1555   1555  1.45  
LINK         ND2 ASN G 443                 C1  NAG L   1     1555   1555  1.46  
LINK         ND2 ASN G 459                 C1  NAG G 627     1555   1555  1.44  
LINK         C   ILE B   9                 N   TYS B  10     1555   1555  1.33  
LINK         C   TYS B  10                 N   ASP B  11     1555   1555  1.33  
LINK         C   ASN B  13                 N   TYS B  14     1555   1555  1.33  
LINK         C   TYS B  14                 N   TYR B  15     1555   1555  1.33  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.45  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.44  
LINK         O4  NAG D   2                 C1  BMA D   3     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.44  
LINK         O3  BMA E   3                 C1  MAN E   4     1555   1555  1.45  
LINK         O2  MAN E   4                 C1  MAN E   5     1555   1555  1.44  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.44  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.44  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.44  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.43  
LINK         O4  NAG J   2                 C1  BMA J   3     1555   1555  1.45  
LINK         O4  NAG K   1                 C1  NAG K   2     1555   1555  1.25  
LINK         O4  NAG L   1                 C1  NAG L   2     1555   1555  1.45  
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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