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Database: PDB
Entry: 4XT3
LinkDB: 4XT3
Original site: 4XT3 
HEADER    VIRAL PROTEIN/SIGNALLING PROTEIN        22-JAN-15   4XT3              
TITLE     STRUCTURE OF A VIRAL GPCR BOUND TO HUMAN CHEMOKINE CX3CL1             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: G-PROTEIN COUPLED RECEPTOR HOMOLOG US28;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HHRF3;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: FRACTALKINE;                                               
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: UNP RESIDUES 25-101;                                       
COMPND  10 SYNONYM: C-X3-C MOTIF CHEMOKINE 1,CX3C MEMBRANE-ANCHORED CHEMOKINE,  
COMPND  11 NEUROTACTIN,SMALL-INDUCIBLE CYTOKINE D1;                             
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CYTOMEGALOVIRUS;                                
SOURCE   3 ORGANISM_TAXID: 10358;                                               
SOURCE   4 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   5 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;                          
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: CX3CL1, FKN, NTT, SCYD1, A-152E5.2;                            
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-                           
KEYWDS    GPCR, CHEMOKINE, MEMBRANE PROTEIN, COMPLEX, VIRAL PROTEIN-CYTOKINE    
KEYWDS   2 COMPLEX, VIRAL PROTEIN-SIGNALLING PROTEIN COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.BURG,K.M.JUDE,D.WAGHRAY,K.C.GARCIA                                
REVDAT   3   29-JUL-20 4XT3    1       COMPND SOURCE KEYWDS JRNL                
REVDAT   3 2                   1       REMARK SEQRES HETNAM LINK                
REVDAT   3 3                   1       SITE   ATOM                              
REVDAT   2   18-MAR-15 4XT3    1       JRNL                                     
REVDAT   1   04-MAR-15 4XT3    0                                                
JRNL        AUTH   J.S.BURG,J.R.INGRAM,A.J.VENKATAKRISHNAN,K.M.JUDE,            
JRNL        AUTH 2 A.DUKKIPATI,E.N.FEINBERG,A.ANGELINI,D.WAGHRAY,R.O.DROR,      
JRNL        AUTH 3 H.L.PLOEGH,K.C.GARCIA                                        
JRNL        TITL   STRUCTURAL BIOLOGY. STRUCTURAL BASIS FOR CHEMOKINE           
JRNL        TITL 2 RECOGNITION AND ACTIVATION OF A VIRAL G PROTEIN-COUPLED      
JRNL        TITL 3 RECEPTOR.                                                    
JRNL        REF    SCIENCE                       V. 347  1113 2015              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   25745166                                                     
JRNL        DOI    10.1126/SCIENCE.AAA5026                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1839)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.92                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 4827                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.288                           
REMARK   3   R VALUE            (WORKING SET) : 0.284                           
REMARK   3   FREE R VALUE                     : 0.322                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.030                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 484                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.9243 -  5.4798    0.96     1693   190  0.2636 0.2914        
REMARK   3     2  5.4798 -  4.3503    0.94     1571   174  0.3054 0.3458        
REMARK   3     3  4.3503 -  3.8006    0.64     1079   120  0.3013 0.3654        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.660            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.580           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           2851                                  
REMARK   3   ANGLE     :  0.874           3912                                  
REMARK   3   CHIRALITY :  0.031            483                                  
REMARK   3   PLANARITY :  0.005            468                                  
REMARK   3   DIHEDRAL  : 11.365            942                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4XT3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206266.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 26                                 
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.033                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PILATUS3 6M                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 4834                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.0                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.27500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 55.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4MBS, 1F2L, 3ONA                                     
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 300, HEPES, AMMONIUM PHOSPHATE, PH   
REMARK 280  7.4, LIPIDIC CUBIC PHASE, TEMPERATURE 293K                          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       47.20000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.20000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       29.95000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       96.35000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       29.95000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       96.35000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       47.20000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       29.95000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       96.35000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       47.20000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       29.95000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       96.35000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 P    PO4 A 402  LIES ON A SPECIAL POSITION.                          
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 A    -7                                                      
REMARK 465     TYR A    -6                                                      
REMARK 465     LYS A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     THR A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     THR A    11                                                      
REMARK 465     THR A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     PHE A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     TYR A    16                                                      
REMARK 465     ASP A    17                                                      
REMARK 465     ASN A    97                                                      
REMARK 465     SER A    98                                                      
REMARK 465     LEU A    99                                                      
REMARK 465     PHE A   309                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     GLN A   311                                                      
REMARK 465     ARG A   312                                                      
REMARK 465     LEU A   313                                                      
REMARK 465     PHE A   314                                                      
REMARK 465     SER A   315                                                      
REMARK 465     ARG A   316                                                      
REMARK 465     ASP A   317                                                      
REMARK 465     VAL A   318                                                      
REMARK 465     SER A   319                                                      
REMARK 465     TRP A   320                                                      
REMARK 465     TYR A   321                                                      
REMARK 465     HIS A   322                                                      
REMARK 465     SER A   323                                                      
REMARK 465     MET A   324                                                      
REMARK 465     SER A   325                                                      
REMARK 465     PHE A   326                                                      
REMARK 465     SER A   327                                                      
REMARK 465     ARG A   328                                                      
REMARK 465     ARG A   329                                                      
REMARK 465     SER A   330                                                      
REMARK 465     SER A   331                                                      
REMARK 465     PRO A   332                                                      
REMARK 465     SER A   333                                                      
REMARK 465     ARG A   334                                                      
REMARK 465     ARG A   335                                                      
REMARK 465     GLU A   336                                                      
REMARK 465     THR A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     SER A   339                                                      
REMARK 465     ASP A   340                                                      
REMARK 465     THR A   341                                                      
REMARK 465     LEU A   342                                                      
REMARK 465     SER A   343                                                      
REMARK 465     ASP A   344                                                      
REMARK 465     GLU A   345                                                      
REMARK 465     VAL A   346                                                      
REMARK 465     CYS A   347                                                      
REMARK 465     ARG A   348                                                      
REMARK 465     VAL A   349                                                      
REMARK 465     SER A   350                                                      
REMARK 465     GLN A   351                                                      
REMARK 465     ILE A   352                                                      
REMARK 465     ILE A   353                                                      
REMARK 465     PRO A   354                                                      
REMARK 465     ALA B    70                                                      
REMARK 465     ALA B    71                                                      
REMARK 465     LEU B    72                                                      
REMARK 465     THR B    73                                                      
REMARK 465     ARG B    74                                                      
REMARK 465     ASN B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     SER B    78                                                      
REMARK 465     GLY B    79                                                      
REMARK 465     SER B    80                                                      
REMARK 465     GLY B    81                                                      
REMARK 465     SER B    82                                                      
REMARK 465     ALA B    83                                                      
REMARK 465     ALA B    84                                                      
REMARK 465     ALA B    85                                                      
REMARK 465     LEU B    86                                                      
REMARK 465     GLU B    87                                                      
REMARK 465     VAL B    88                                                      
REMARK 465     LEU B    89                                                      
REMARK 465     PHE B    90                                                      
REMARK 465     GLN B    91                                                      
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     ARG A  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  62    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A  63    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A  65    CG   CD   OE1  NE2                                  
REMARK 470     GLN A  91    CG   CD   OE1  NE2                                  
REMARK 470     ASP A  95    CG   OD1  OD2                                       
REMARK 470     HIS A  96    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 137    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG A 139    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 168    CG   CD   CE   NZ                                   
REMARK 470     LEU A 180    CG   CD1  CD2                                       
REMARK 470     GLU A 264    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 267    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 270    CG   CD   CE   NZ                                   
REMARK 470     ARG A 271    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 296    OG1  CG2                                            
REMARK 470     LYS A 297    CG   CD   CE   NZ                                   
REMARK 470     PHE A 298    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 299    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 300    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 301    CG   CD   OE1  OE2                                  
REMARK 470     CYS A 304    SG                                                  
REMARK 470     LEU A 305    CG   CD1  CD2                                       
REMARK 470     LEU A 306    CG   CD1  CD2                                       
REMARK 470     GLU A 308    CG   CD   OE1  OE2                                  
REMARK 470     LYS B   7    CG   CD   CE   NZ                                   
REMARK 470     LYS B  14    CG   CD   CE   NZ                                   
REMARK 470     LYS B  18    CG   CD   CE   NZ                                   
REMARK 470     ILE B  19    CG1  CG2  CD1                                       
REMARK 470     LEU B  23    CG   CD1  CD2                                       
REMARK 470     HIS B  26    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B  36    CG   CD   CE   NZ                                   
REMARK 470     ARG B  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  44    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  47    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  54    CG   CD   CE   NZ                                   
REMARK 470     LYS B  59    CG   CD   CE   NZ                                   
REMARK 470     MET B  62    CG   SD   CE                                        
REMARK 470     GLN B  63    CG   CD   OE1  NE2                                  
REMARK 470     HIS B  64    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B  66    CG   OD1  OD2                                       
REMARK 470     ARG B  67    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  68    CG   CD   OE1  NE2                                  
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    ALA A  20       21.41    -79.71                                   
REMARK 500    LEU A  45      -75.44    -54.79                                   
REMARK 500    ASP A 176       97.02    -64.86                                   
REMARK 500    TYR A 291      -50.53   -129.51                                   
REMARK 500    ALA A 307       47.76    -81.45                                   
REMARK 500    LYS B  18      -39.94   -146.93                                   
REMARK 500    GLN B  68      -70.13    -73.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4XT1   RELATED DB: PDB                                   
DBREF  4XT3 A    1   354  UNP    P69332   US28_HCMVA       1    354             
DBREF  4XT3 B    1    77  UNP    P78423   X3CL1_HUMAN     25    101             
SEQADV 4XT3 ASP A   -7  UNP  P69332              EXPRESSION TAG                 
SEQADV 4XT3 TYR A   -6  UNP  P69332              EXPRESSION TAG                 
SEQADV 4XT3 LYS A   -5  UNP  P69332              EXPRESSION TAG                 
SEQADV 4XT3 ASP A   -4  UNP  P69332              EXPRESSION TAG                 
SEQADV 4XT3 ASP A   -3  UNP  P69332              EXPRESSION TAG                 
SEQADV 4XT3 ASP A   -2  UNP  P69332              EXPRESSION TAG                 
SEQADV 4XT3 ASP A   -1  UNP  P69332              EXPRESSION TAG                 
SEQADV 4XT3 ALA A    0  UNP  P69332              EXPRESSION TAG                 
SEQADV 4XT3 SER B   78  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 GLY B   79  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 SER B   80  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 GLY B   81  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 SER B   82  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 ALA B   83  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 ALA B   84  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 ALA B   85  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 LEU B   86  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 GLU B   87  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 VAL B   88  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 LEU B   89  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 PHE B   90  UNP  P78423              EXPRESSION TAG                 
SEQADV 4XT3 GLN B   91  UNP  P78423              EXPRESSION TAG                 
SEQRES   1 A  362  ASP TYR LYS ASP ASP ASP ASP ALA MET THR PRO THR THR          
SEQRES   2 A  362  THR THR ALA GLU LEU THR THR GLU PHE ASP TYR ASP GLU          
SEQRES   3 A  362  ASP ALA THR PRO CYS VAL PHE THR ASP VAL LEU ASN GLN          
SEQRES   4 A  362  SER LYS PRO VAL THR LEU PHE LEU TYR GLY VAL VAL PHE          
SEQRES   5 A  362  LEU PHE GLY SER ILE GLY ASN PHE LEU VAL ILE PHE THR          
SEQRES   6 A  362  ILE THR TRP ARG ARG ARG ILE GLN CYS SER GLY ASP VAL          
SEQRES   7 A  362  TYR PHE ILE ASN LEU ALA ALA ALA ASP LEU LEU PHE VAL          
SEQRES   8 A  362  CYS THR LEU PRO LEU TRP MET GLN TYR LEU LEU ASP HIS          
SEQRES   9 A  362  ASN SER LEU ALA SER VAL PRO CYS THR LEU LEU THR ALA          
SEQRES  10 A  362  CYS PHE TYR VAL ALA MET PHE ALA SER LEU CYS PHE ILE          
SEQRES  11 A  362  THR GLU ILE ALA LEU ASP ARG TYR TYR ALA ILE VAL TYR          
SEQRES  12 A  362  MET ARG TYR ARG PRO VAL LYS GLN ALA CYS LEU PHE SER          
SEQRES  13 A  362  ILE PHE TRP TRP ILE PHE ALA VAL ILE ILE ALA ILE PRO          
SEQRES  14 A  362  HIS PHE MET VAL VAL THR LYS LYS ASP ASN GLN CYS MET          
SEQRES  15 A  362  THR ASP TYR ASP TYR LEU GLU VAL SER TYR PRO ILE ILE          
SEQRES  16 A  362  LEU ASN VAL GLU LEU MET LEU GLY ALA PHE VAL ILE PRO          
SEQRES  17 A  362  LEU SER VAL ILE SER TYR CYS TYR TYR ARG ILE SER ARG          
SEQRES  18 A  362  ILE VAL ALA VAL SER GLN SER ARG HIS LYS GLY ARG ILE          
SEQRES  19 A  362  VAL ARG VAL LEU ILE ALA VAL VAL LEU VAL PHE ILE ILE          
SEQRES  20 A  362  PHE TRP LEU PRO TYR HIS LEU THR LEU PHE VAL ASP THR          
SEQRES  21 A  362  LEU LYS LEU LEU LYS TRP ILE SER SER SER CYS GLU PHE          
SEQRES  22 A  362  GLU ARG SER LEU LYS ARG ALA LEU ILE LEU THR GLU SER          
SEQRES  23 A  362  LEU ALA PHE CYS HIS CYS CYS LEU ASN PRO LEU LEU TYR          
SEQRES  24 A  362  VAL PHE VAL GLY THR LYS PHE ARG GLN GLU LEU HIS CYS          
SEQRES  25 A  362  LEU LEU ALA GLU PHE ARG GLN ARG LEU PHE SER ARG ASP          
SEQRES  26 A  362  VAL SER TRP TYR HIS SER MET SER PHE SER ARG ARG SER          
SEQRES  27 A  362  SER PRO SER ARG ARG GLU THR SER SER ASP THR LEU SER          
SEQRES  28 A  362  ASP GLU VAL CYS ARG VAL SER GLN ILE ILE PRO                  
SEQRES   1 B   91  PCA HIS HIS GLY VAL THR LYS CYS ASN ILE THR CYS SER          
SEQRES   2 B   91  LYS MET THR SER LYS ILE PRO VAL ALA LEU LEU ILE HIS          
SEQRES   3 B   91  TYR GLN GLN ASN GLN ALA SER CYS GLY LYS ARG ALA ILE          
SEQRES   4 B   91  ILE LEU GLU THR ARG GLN HIS ARG LEU PHE CYS ALA ASP          
SEQRES   5 B   91  PRO LYS GLU GLN TRP VAL LYS ASP ALA MET GLN HIS LEU          
SEQRES   6 B   91  ASP ARG GLN ALA ALA ALA LEU THR ARG ASN GLY GLY SER          
SEQRES   7 B   91  GLY SER GLY SER ALA ALA ALA LEU GLU VAL LEU PHE GLN          
MODRES 4XT3 PCA B    1  GLN  MODIFIED RESIDUE                                   
HET    PCA  B   1       8                                                       
HET    NAG  C   1      14                                                       
HET    NAG  C   2      14                                                       
HET    NAG  C   3      14                                                       
HET    UNL  A 401       9                                                       
HET    PO4  A 402       5                                                       
HETNAM     PCA PYROGLUTAMIC ACID                                                
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     UNL UNKNOWN LIGAND                                                   
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   2  PCA    C5 H7 N O3                                                   
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   5  PO4    O4 P 3-                                                      
HELIX    1 AA1 PHE A   25  ARG A   62  1                                  38    
HELIX    2 AA2 CYS A   66  CYS A   84  1                                  19    
HELIX    3 AA3 THR A   85  LEU A   94  1                                  10    
HELIX    4 AA4 PRO A  103  VAL A  134  1                                  32    
HELIX    5 AA5 PRO A  140  ILE A  158  1                                  19    
HELIX    6 AA6 ALA A  159  MET A  164  1                                   6    
HELIX    7 AA7 VAL A  182  PHE A  197  1                                  16    
HELIX    8 AA8 PHE A  197  ALA A  216  1                                  20    
HELIX    9 AA9 LYS A  223  LEU A  256  1                                  34    
HELIX   10 AB1 SER A  262  PHE A  281  1                                  20    
HELIX   11 AB2 CYS A  282  VAL A  292  1                                  11    
HELIX   12 AB3 LYS A  297  ALA A  307  1                                  11    
HELIX   13 AB4 GLN B   31  GLY B   35  5                                   5    
HELIX   14 AB5 TRP B   57  ALA B   69  1                                  13    
SHEET    1 AA1 2 CYS A  23  VAL A  24  0                                        
SHEET    2 AA1 2 ILE B  10  THR B  11 -1  O  THR B  11   N  CYS A  23           
SHEET    1 AA2 2 VAL A 166  LYS A 169  0                                        
SHEET    2 AA2 2 GLN A 172  THR A 175 -1  O  MET A 174   N  THR A 167           
SHEET    1 AA3 3 LEU B  24  GLN B  29  0                                        
SHEET    2 AA3 3 ILE B  39  THR B  43 -1  O  ILE B  40   N  GLN B  28           
SHEET    3 AA3 3 LEU B  48  ALA B  51 -1  O  PHE B  49   N  LEU B  41           
SSBOND   1 CYS A   23    CYS A  263                          1555   1555  2.03  
SSBOND   2 CYS A  104    CYS A  173                          1555   1555  2.03  
SSBOND   3 CYS B    8    CYS B   34                          1555   1555  2.03  
SSBOND   4 CYS B   12    CYS B   50                          1555   1555  2.03  
LINK         C   PCA B   1                 N   HIS B   2     1555   1555  1.33  
LINK         ND2 ASN B   9                 C1  NAG C   1     1555   1555  1.44  
LINK         O4  NAG C   1                 C1  NAG C   2     1555   1555  1.43  
LINK         O4  NAG C   2                 C1  NAG C   3     1555   1555  1.44  
CISPEP   1 ILE B   19    PRO B   20          0        -7.26                     
CRYST1   59.900  192.700   94.400  90.00  90.00  90.00 C 2 2 21      8          
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      0.016694  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005189  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010593        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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