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Database: PDB
Entry: 1F2L
LinkDB: 1F2L
Original site: 1F2L 
HEADER    CYTOKINE                                26-MAY-00   1F2L              
TITLE     CRYSTAL STRUCTURE OF CHEMOKINE DOMAIN OF FRACTALKINE                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FRACTALKINE;                                               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: CHEMOKINE DOMAIN;                                          
COMPND   5 SYNONYM: NEUROTACTIN, CX3C MEMBRANE-ANCHORED CHEMOKINE,              
COMPND   6 SMALL INDUCIBLE CYTOKINE D1;                                         
COMPND   7 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: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PAED4                                     
KEYWDS    CHEMOATTRACTANT, X-RAY STRUCTURE, FRACTALKINE, NEUROTACTIN,           
KEYWDS   2 CYTOKINE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.M.HOOVER,L.S.MIZOUE,T.M.HANDEL,J.LUBKOWSKI                          
REVDAT   2   24-FEB-09 1F2L    1       VERSN                                    
REVDAT   1   06-SEP-00 1F2L    0                                                
JRNL        AUTH   D.M.HOOVER,L.S.MIZOUE,T.M.HANDEL,J.LUBKOWSKI                 
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE CHEMOKINE DOMAIN OF             
JRNL        TITL 2 FRACTALKINE SHOWS A NOVEL QUATERNARY ARRANGEMENT.            
JRNL        REF    J.BIOL.CHEM.                  V. 275 23187 2000              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   10770945                                                     
JRNL        DOI    10.1074/JBC.M002584200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.9                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.237                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.237                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.321                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 0.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 2950                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 345321                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.232                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 0.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 2431                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 2105                                          
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 0                                             
REMARK   3   SOLVENT ATOMS      : 264                                           
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 2369.00                 
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 949                     
REMARK   3   NUMBER OF RESTRAINTS                     : 862                     
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.006                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.022                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.023                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.029                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.036                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.010                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.000                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.100                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1F2L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JUN-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB011166.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-99; NULL; NULL; NULL        
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL; NULL; NULL              
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; NULL; NULL; NULL                
REMARK 200  RADIATION SOURCE               : NSLS; NULL; NULL; NULL             
REMARK 200  BEAMLINE                       : X9B; NULL; NULL; NULL              
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL; NULL             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M; M; M                         
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98; NULL; NULL; NULL             
REMARK 200  MONOCHROMATOR                  : NULL; NULL; NULL; NULL             
REMARK 200  OPTICS                         : NULL; NULL; NULL; NULL             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL; NULL; NULL              
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4; NULL; NULL;        
REMARK 200                                   NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 30366                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 15.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 11.400                             
REMARK 200  R MERGE                    (I) : 0.03900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 61.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD; MAD; MAD; MAD                             
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MULTIWAVELENGTH              
REMARK 200  ANOMALOUS DIFFRACTION USING SELENOMETHIONINE (SELENIUM) AS          
REMARK 200  ANOMALOUS SCATTERER                                                 
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM FORMATE, DISODIUM CITRATE,        
REMARK 280  PH 5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       41.33133            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       82.66267            
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       61.99700            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      103.32833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       20.66567            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       41.33133            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       82.66267            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      103.32833            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       61.99700            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       20.66567            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A DIMER CONSTRUCTED FROM          
REMARK 300 CHAINS A AND D, AND FROM CHAINS B AND C                              
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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     GLN A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     ALA A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     ALA A    71                                                      
REMARK 465     LEU A    72                                                      
REMARK 465     THR A    73                                                      
REMARK 465     ARG A    74                                                      
REMARK 465     ASP A    75                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     GLN B     1                                                      
REMARK 465     HIS B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     ALA B    69                                                      
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     ASP B    75                                                      
REMARK 465     GLY B    76                                                      
REMARK 465     GLN C     1                                                      
REMARK 465     HIS C     2                                                      
REMARK 465     HIS C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     ALA C    69                                                      
REMARK 465     ALA C    70                                                      
REMARK 465     ALA C    71                                                      
REMARK 465     LEU C    72                                                      
REMARK 465     THR C    73                                                      
REMARK 465     ARG C    74                                                      
REMARK 465     ASP C    75                                                      
REMARK 465     GLY C    76                                                      
REMARK 465     GLN D     1                                                      
REMARK 465     HIS D     2                                                      
REMARK 465     HIS D     3                                                      
REMARK 465     GLY D     4                                                      
REMARK 465     ASP D    75                                                      
REMARK 465     GLY D    76                                                      
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    ARG D  37   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ARG D  37   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 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   9      -99.06    -98.64                                   
REMARK 500    SER A  13      -70.45    -97.88                                   
REMARK 500    LYS A  18      103.87    -41.06                                   
REMARK 500    ASN B   9      -75.03   -121.34                                   
REMARK 500    SER B  13      -81.09   -106.46                                   
REMARK 500    THR B  16     -161.88    -66.82                                   
REMARK 500    ASN C   9     -111.35   -106.35                                   
REMARK 500    SER C  13      -17.18   -148.38                                   
REMARK 500    THR C  16     -178.35    -58.83                                   
REMARK 500    ASN D   9      -73.63   -105.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D  86        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH C  93        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH B 109        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH A 114        DISTANCE =  6.56 ANGSTROMS                       
REMARK 525    HOH B 114        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH A 120        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH A 122        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH A 127        DISTANCE =  6.81 ANGSTROMS                       
REMARK 525    HOH D 136        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH D 150        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH D 157        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH D 161        DISTANCE =  7.07 ANGSTROMS                       
REMARK 525    HOH D 162        DISTANCE =  9.49 ANGSTROMS                       
DBREF  1F2L A    1    76  UNP    P78423   X3CL1_HUMAN     25    100             
DBREF  1F2L B    1    76  UNP    P78423   X3CL1_HUMAN     25    100             
DBREF  1F2L C    1    76  UNP    P78423   X3CL1_HUMAN     25    100             
DBREF  1F2L D    1    76  UNP    P78423   X3CL1_HUMAN     25    100             
SEQADV 1F2L ASP A   75  UNP  P78423    ASN    99 CONFLICT                       
SEQADV 1F2L ASP B   75  UNP  P78423    ASN    99 CONFLICT                       
SEQADV 1F2L ASP C   75  UNP  P78423    ASN    99 CONFLICT                       
SEQADV 1F2L ASP D   75  UNP  P78423    ASN    99 CONFLICT                       
SEQRES   1 A   76  GLN HIS HIS GLY VAL THR LYS CYS ASN ILE THR CYS SER          
SEQRES   2 A   76  LYS MET THR SER LYS ILE PRO VAL ALA LEU LEU ILE HIS          
SEQRES   3 A   76  TYR GLN GLN ASN GLN ALA SER CYS GLY LYS ARG ALA ILE          
SEQRES   4 A   76  ILE LEU GLU THR ARG GLN HIS ARG LEU PHE CYS ALA ASP          
SEQRES   5 A   76  PRO LYS GLU GLN TRP VAL LYS ASP ALA MET GLN HIS LEU          
SEQRES   6 A   76  ASP ARG GLN ALA ALA ALA LEU THR ARG ASP GLY                  
SEQRES   1 B   76  GLN HIS HIS GLY VAL THR LYS CYS ASN ILE THR CYS SER          
SEQRES   2 B   76  LYS MET THR SER LYS ILE PRO VAL ALA LEU LEU ILE HIS          
SEQRES   3 B   76  TYR GLN GLN ASN GLN ALA SER CYS GLY LYS ARG ALA ILE          
SEQRES   4 B   76  ILE LEU GLU THR ARG GLN HIS ARG LEU PHE CYS ALA ASP          
SEQRES   5 B   76  PRO LYS GLU GLN TRP VAL LYS ASP ALA MET GLN HIS LEU          
SEQRES   6 B   76  ASP ARG GLN ALA ALA ALA LEU THR ARG ASP GLY                  
SEQRES   1 C   76  GLN HIS HIS GLY VAL THR LYS CYS ASN ILE THR CYS SER          
SEQRES   2 C   76  LYS MET THR SER LYS ILE PRO VAL ALA LEU LEU ILE HIS          
SEQRES   3 C   76  TYR GLN GLN ASN GLN ALA SER CYS GLY LYS ARG ALA ILE          
SEQRES   4 C   76  ILE LEU GLU THR ARG GLN HIS ARG LEU PHE CYS ALA ASP          
SEQRES   5 C   76  PRO LYS GLU GLN TRP VAL LYS ASP ALA MET GLN HIS LEU          
SEQRES   6 C   76  ASP ARG GLN ALA ALA ALA LEU THR ARG ASP GLY                  
SEQRES   1 D   76  GLN HIS HIS GLY VAL THR LYS CYS ASN ILE THR CYS SER          
SEQRES   2 D   76  LYS MET THR SER LYS ILE PRO VAL ALA LEU LEU ILE HIS          
SEQRES   3 D   76  TYR GLN GLN ASN GLN ALA SER CYS GLY LYS ARG ALA ILE          
SEQRES   4 D   76  ILE LEU GLU THR ARG GLN HIS ARG LEU PHE CYS ALA ASP          
SEQRES   5 D   76  PRO LYS GLU GLN TRP VAL LYS ASP ALA MET GLN HIS LEU          
SEQRES   6 D   76  ASP ARG GLN ALA ALA ALA LEU THR ARG ASP GLY                  
FORMUL   5  HOH   *264(H2 O)                                                    
HELIX    1   1 PRO A   20  ALA A   22  5                                   3    
HELIX    2   2 GLN A   31  GLY A   35  5                                   5    
HELIX    3   3 GLU A   55  ARG A   67  1                                  13    
HELIX    4   4 PRO B   20  ALA B   22  5                                   3    
HELIX    5   5 GLN B   31  GLY B   35  5                                   5    
HELIX    6   6 GLU B   55  ARG B   67  1                                  13    
HELIX    7   7 PRO C   20  ALA C   22  5                                   3    
HELIX    8   8 GLN C   31  GLY C   35  5                                   5    
HELIX    9   9 GLU C   55  ARG C   67  1                                  13    
HELIX   10  10 PRO D   20  ALA D   22  5                                   3    
HELIX   11  11 GLN D   31  GLY D   35  5                                   5    
HELIX   12  12 GLU D   55  THR D   73  1                                  19    
SHEET    1   A 2 ILE A  10  CYS A  12  0                                        
SHEET    2   A 2 ILE D  10  CYS D  12 -1  N  THR D  11   O  THR A  11           
SHEET    1   B 3 LEU A  24  GLN A  29  0                                        
SHEET    2   B 3 ILE A  39  THR A  43 -1  N  ILE A  40   O  GLN A  28           
SHEET    3   B 3 LEU A  48  ALA A  51 -1  N  PHE A  49   O  LEU A  41           
SHEET    1   C 2 THR B  11  CYS B  12  0                                        
SHEET    2   C 2 ILE C  10  THR C  11 -1  O  THR C  11   N  THR B  11           
SHEET    1   D 3 LEU B  24  GLN B  29  0                                        
SHEET    2   D 3 ILE B  39  THR B  43 -1  N  ILE B  40   O  GLN B  28           
SHEET    3   D 3 LEU B  48  ALA B  51 -1  O  PHE B  49   N  LEU B  41           
SHEET    1   E 3 LEU C  24  GLN C  29  0                                        
SHEET    2   E 3 ILE C  39  THR C  43 -1  N  ILE C  40   O  GLN C  28           
SHEET    3   E 3 LEU C  48  ALA C  51 -1  O  PHE C  49   N  LEU C  41           
SHEET    1   F 3 LEU D  24  GLN D  29  0                                        
SHEET    2   F 3 ILE D  39  THR D  43 -1  N  ILE D  40   O  GLN D  28           
SHEET    3   F 3 LEU D  48  ALA D  51 -1  O  PHE D  49   N  LEU D  41           
SSBOND   1 CYS A    8    CYS A   34                          1555   1555  2.06  
SSBOND   2 CYS A   12    CYS A   50                          1555   1555  2.03  
SSBOND   3 CYS B    8    CYS B   34                          1555   1555  2.02  
SSBOND   4 CYS B   12    CYS B   50                          1555   1555  2.04  
SSBOND   5 CYS C    8    CYS C   34                          1555   1555  2.06  
SSBOND   6 CYS C   12    CYS C   50                          1555   1555  2.05  
SSBOND   7 CYS D    8    CYS D   34                          1555   1555  2.04  
SSBOND   8 CYS D   12    CYS D   50                          1555   1555  2.04  
CRYST1  110.473  110.473  123.994  90.00  90.00 120.00 P 61 2 2     48          
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      0.009052  0.005226  0.000000        0.00000                         
SCALE2      0.000000  0.010452  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008065        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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