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Database: PDB
Entry: 3JVF
LinkDB: 3JVF
Original site: 3JVF 
HEADER    SIGNALING PROTEIN / CYTOKINE            16-SEP-09   3JVF              
TITLE     CRYSTAL STRUCTURE OF AN INTERLEUKIN-17 RECEPTOR COMPLEX               
CAVEAT     3JVF    NAG C 302 HAS WRONG CHIRALITY AT ATOM C1 NAG C 304 HAS WRONG 
CAVEAT   2 3JVF    CHIRALITY AT ATOM C1                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-17F;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: IL-17F, INTERLEUKIN-24, IL-24, CYTOKINE ML-1;               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: INTERLEUKIN-17 RECEPTOR A;                                 
COMPND   8 CHAIN: C;                                                            
COMPND   9 FRAGMENT: EXTRACELLULAR DOMAIN;                                      
COMPND  10 SYNONYM: IL-17 RECEPTOR, CDW217;                                     
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IL17F, IL24;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS;                                
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: IL17RA, IL17R;                                                 
SOURCE  14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  16 EXPRESSION_SYSTEM_CELL: BACMAM 293 CELLS;                            
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS                                 
KEYWDS    CYTOKINE, INTERLEUKIN, CYSTEINE-KNOT GROWTH FACTOR, RECEPTOR-CYTOKINE 
KEYWDS   2 COMPLEX, DISULFIDE BOND, GLYCOPROTEIN, SECRETED, MEMBRANE, RECEPTOR, 
KEYWDS   3 TRANSMEMBRANE, SIGNALING PROTEIN, SIGNALING PROTEIN - CYTOKINE       
KEYWDS   4 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.K.ELY,K.C.GARCIA                                                    
REVDAT   4   29-JUL-20 3JVF    1       CAVEAT COMPND REMARK HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   13-JUL-11 3JVF    1       VERSN                                    
REVDAT   2   29-DEC-09 3JVF    1       JRNL                                     
REVDAT   1   20-OCT-09 3JVF    0                                                
JRNL        AUTH   L.K.ELY,S.FISCHER,K.C.GARCIA                                 
JRNL        TITL   STRUCTURAL BASIS OF RECEPTOR SHARING BY INTERLEUKIN 17       
JRNL        TITL 2 CYTOKINES.                                                   
JRNL        REF    NAT.IMMUNOL.                  V.  10  1245 2009              
JRNL        REFN                   ISSN 1529-2908                               
JRNL        PMID   19838198                                                     
JRNL        DOI    10.1038/NI.1813                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 18479                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.231                           
REMARK   3   R VALUE            (WORKING SET) : 0.229                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 948                             
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 39.8235 -  6.3061    0.95     2581   116  0.2358 0.2251        
REMARK   3     2  6.3061 -  5.0085    0.99     2547   129  0.2094 0.2236        
REMARK   3     3  5.0085 -  4.3763    0.99     2509   129  0.1863 0.2309        
REMARK   3     4  4.3763 -  3.9766    0.99     2492   147  0.2180 0.2611        
REMARK   3     5  3.9766 -  3.6918    0.99     2481   124  0.2430 0.3054        
REMARK   3     6  3.6918 -  3.4742    0.99     2456   152  0.2715 0.3233        
REMARK   3     7  3.4742 -  3.3003    1.00     2465   151  0.2999 0.3336        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 72.06                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.680           
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      :  0.009           3987                                  
REMARK   3   ANGLE     :  1.333           5428                                  
REMARK   3   CHIRALITY :  0.079            631                                  
REMARK   3   PLANARITY :  0.005            695                                  
REMARK   3   DIHEDRAL  : 19.892           1456                                  
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 3JVF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-OCT-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000055208.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-APR-08; 16-APR-09; 17-JUL-08;   
REMARK 200                                   10-DEC-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100; 100; 100                 
REMARK 200  PH                             : 9.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 4                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y; Y; Y                         
REMARK 200  RADIATION SOURCE               : SSRL; SSRL; SSRL; APS              
REMARK 200  BEAMLINE                       : BL9-2; BL11-1; BL11-1; 23-ID-D     
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL; NULL; NULL             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL; NULL; NULL                
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00; 1.07; 0.978; 1.03            
REMARK 200  MONOCHROMATOR                  : NULL; NULL; NULL; NULL             
REMARK 200  OPTICS                         : NULL; NULL; NULL; NULL             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL; NULL; NULL; NULL             
REMARK 200  DETECTOR MANUFACTURER          : NULL; NULL; NULL; NULL             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18749                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL; NULL; NULL            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
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   (%): 74.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG6000, 0.1M CAPSO, CALCIUM CHLORIDE,   
REMARK 280  PH 9.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       40.95000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       85.36500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       85.36500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       20.47500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       85.36500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       85.36500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       61.42500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       85.36500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       85.36500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       20.47500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       85.36500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       85.36500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       61.42500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       40.95000            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 23710 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL                        
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     ARG A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     LYS A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     HIS A     8                                                      
REMARK 465     THR A     9                                                      
REMARK 465     PHE A    10                                                      
REMARK 465     PHE A    11                                                      
REMARK 465     GLN A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     GLU A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     CYS A    17                                                      
REMARK 465     PRO A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     PRO A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     GLN A   105                                                      
REMARK 465     GLY A   106                                                      
REMARK 465     CYS A   107                                                      
REMARK 465     SER A   108                                                      
REMARK 465     VAL A   109                                                      
REMARK 465     GLN A   133                                                      
REMARK 465     ARG B     1                                                      
REMARK 465     LYS B     2                                                      
REMARK 465     ILE B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     LYS B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     HIS B     8                                                      
REMARK 465     THR B     9                                                      
REMARK 465     PHE B    10                                                      
REMARK 465     PHE B    11                                                      
REMARK 465     GLN B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     GLU B    15                                                      
REMARK 465     SER B    16                                                      
REMARK 465     CYS B    17                                                      
REMARK 465     PRO B    18                                                      
REMARK 465     PRO B    19                                                      
REMARK 465     VAL B    20                                                      
REMARK 465     PRO B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     SER B    24                                                      
REMARK 465     ILE B   129                                                      
REMARK 465     HIS B   130                                                      
REMARK 465     HIS B   131                                                      
REMARK 465     VAL B   132                                                      
REMARK 465     GLN B   133                                                      
REMARK 465     SER C     1                                                      
REMARK 465     PRO C   273                                                      
REMARK 465     GLU C   274                                                      
REMARK 465     MET C   275                                                      
REMARK 465     PRO C   276                                                      
REMARK 465     ASP C   277                                                      
REMARK 465     THR C   278                                                      
REMARK 465     PRO C   279                                                      
REMARK 465     GLU C   280                                                      
REMARK 465     PRO C   281                                                      
REMARK 465     ILE C   282                                                      
REMARK 465     PRO C   283                                                      
REMARK 465     ASP C   284                                                      
REMARK 465     TYR C   285                                                      
REMARK 465     MET C   286                                                      
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     SER A  24    OG                                                  
REMARK 470     LYS A  26    CG   CD   CE   NZ                                   
REMARK 470     GLU A  34    CG   CD   OE1  OE2                                  
REMARK 470     ASN A  35    CG   OD1  ND2                                       
REMARK 470     ARG A  37    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A  41    OG                                                  
REMARK 470     LYS A 103    CG   CD   CE   NZ                                   
REMARK 470     HIS A 104    CG   ND1  CD2  CE1  NE2                             
REMARK 470     SER A 110    OG                                                  
REMARK 470     GLU B  34    CG   CD   OE1  OE2                                  
REMARK 470     ASN B  35    CG   OD1  ND2                                       
REMARK 470     SER B  41    OG                                                  
REMARK 470     LYS B 103    CG   CD   CE   NZ                                   
REMARK 470     GLN B 105    CG   CD   OE1  NE2                                  
REMARK 470     CYS B 107    SG                                                  
REMARK 470     SER B 108    OG                                                  
REMARK 470     LYS B 115    CG   CD   CE   NZ                                   
REMARK 470     VAL B 128    CG1  CG2                                            
REMARK 470     ASP C  29    CG   OD1  OD2                                       
REMARK 470     SER C  30    OG                                                  
REMARK 470     LEU C 101    CG   CD1  CD2                                       
REMARK 470     VAL C 178    CG1  CG2                                            
REMARK 470     SER C 189    OG                                                  
REMARK 470     GLN C 231    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 243    CG   CD   CE   NZ                                   
REMARK 470     SER C 267    OG                                                  
REMARK 470     CYS C 272    SG                                                  
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   ND2  ASN A    53     C2   NAG D     1              2.15            
REMARK 500   ND2  ASN C    18     C2   NAG C   303              2.15            
REMARK 500   ND2  ASN C   234     O5   NAG C   304              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  96   CG    GLU A  96   CD      0.105                       
REMARK 500    GLU A  96   CD    GLU A  96   OE1     0.101                       
REMARK 500    GLU A  96   CD    GLU A  96   OE2     0.080                       
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 B  77     -177.26    -64.70                                   
REMARK 500    ASN B  79     -176.86    -68.78                                   
REMARK 500    PRO C  15      108.35    -46.37                                   
REMARK 500    HIS C  33       63.00     61.48                                   
REMARK 500    SER C  41      159.22    -43.13                                   
REMARK 500    THR C  54     -169.65    -78.51                                   
REMARK 500    ASN C  89      -83.40    -39.51                                   
REMARK 500    ASN C  91       47.97    -77.75                                   
REMARK 500    GLN C 145      109.50   -161.61                                   
REMARK 500    LYS C 147      111.30   -163.07                                   
REMARK 500    ASP C 153      176.85    -58.69                                   
REMARK 500    CYS C 154       40.16    -79.02                                   
REMARK 500    LEU C 181     -140.55     56.56                                   
REMARK 500    ASN C 194       39.68    -95.47                                   
REMARK 500    HIS C 198     -179.78    -66.82                                   
REMARK 500    CYS C 245       45.14    -89.74                                   
REMARK 500    LEU C 260      122.55    -35.66                                   
REMARK 500    ASN C 261      -28.73     89.68                                   
REMARK 500    CYS C 263      155.67    -47.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 134  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  43   OD1                                                    
REMARK 620 2 ASN B  43   ND2  61.3                                              
REMARK 620 3 GLU B  45   OE1  97.0  65.7                                        
REMARK 620 4 GLU B  45   OE2  62.9  76.9  46.2                                  
REMARK 620 N                    1     2     3                                   
DBREF  3JVF A    1   133  UNP    Q96PD4   IL17F_HUMAN     31    163             
DBREF  3JVF B    1   133  UNP    Q96PD4   IL17F_HUMAN     31    163             
DBREF  3JVF C    1   286  UNP    Q96F46   I17RA_HUMAN     32    317             
SEQRES   1 A  133  ARG LYS ILE PRO LYS VAL GLY HIS THR PHE PHE GLN LYS          
SEQRES   2 A  133  PRO GLU SER CYS PRO PRO VAL PRO GLY GLY SER MET LYS          
SEQRES   3 A  133  LEU ASP ILE GLY ILE ILE ASN GLU ASN GLN ARG VAL SER          
SEQRES   4 A  133  MET SER ARG ASN ILE GLU SER ARG SER THR SER PRO TRP          
SEQRES   5 A  133  ASN TYR THR VAL THR TRP ASP PRO ASN ARG TYR PRO SER          
SEQRES   6 A  133  GLU VAL VAL GLN ALA GLN CYS ARG ASN LEU GLY CYS ILE          
SEQRES   7 A  133  ASN ALA GLN GLY LYS GLU ASP ILE SER MET ASN SER VAL          
SEQRES   8 A  133  PRO ILE GLN GLN GLU THR LEU VAL VAL ARG ARG LYS HIS          
SEQRES   9 A  133  GLN GLY CYS SER VAL SER PHE GLN LEU GLU LYS VAL LEU          
SEQRES  10 A  133  VAL THR VAL GLY CYS THR CYS VAL THR PRO VAL ILE HIS          
SEQRES  11 A  133  HIS VAL GLN                                                  
SEQRES   1 B  133  ARG LYS ILE PRO LYS VAL GLY HIS THR PHE PHE GLN LYS          
SEQRES   2 B  133  PRO GLU SER CYS PRO PRO VAL PRO GLY GLY SER MET LYS          
SEQRES   3 B  133  LEU ASP ILE GLY ILE ILE ASN GLU ASN GLN ARG VAL SER          
SEQRES   4 B  133  MET SER ARG ASN ILE GLU SER ARG SER THR SER PRO TRP          
SEQRES   5 B  133  ASN TYR THR VAL THR TRP ASP PRO ASN ARG TYR PRO SER          
SEQRES   6 B  133  GLU VAL VAL GLN ALA GLN CYS ARG ASN LEU GLY CYS ILE          
SEQRES   7 B  133  ASN ALA GLN GLY LYS GLU ASP ILE SER MET ASN SER VAL          
SEQRES   8 B  133  PRO ILE GLN GLN GLU THR LEU VAL VAL ARG ARG LYS HIS          
SEQRES   9 B  133  GLN GLY CYS SER VAL SER PHE GLN LEU GLU LYS VAL LEU          
SEQRES  10 B  133  VAL THR VAL GLY CYS THR CYS VAL THR PRO VAL ILE HIS          
SEQRES  11 B  133  HIS VAL GLN                                                  
SEQRES   1 C  286  SER LEU ARG LEU LEU ASP HIS ARG ALA LEU VAL CYS SER          
SEQRES   2 C  286  GLN PRO GLY LEU ASN CYS THR VAL LYS ASN SER THR CYS          
SEQRES   3 C  286  LEU ASP ASP SER TRP ILE HIS PRO ARG ASN LEU THR PRO          
SEQRES   4 C  286  SER SER PRO MLY ASP LEU GLN ILE GLN LEU HIS PHE ALA          
SEQRES   5 C  286  HIS THR GLN GLN GLY ASP LEU PHE PRO VAL ALA HIS ILE          
SEQRES   6 C  286  GLU TRP THR LEU GLN THR ASP ALA SER ILE LEU TYR LEU          
SEQRES   7 C  286  GLU GLY ALA GLU LEU SER VAL LEU GLN LEU ASN THR ASN          
SEQRES   8 C  286  GLU ARG LEU CYS VAL ARG PHE GLU PHE LEU SER LYS LEU          
SEQRES   9 C  286  ARG HIS HIS HIS ARG ARG TRP ARG PHE THR PHE SER HIS          
SEQRES  10 C  286  PHE VAL VAL ASP PRO ASP GLN GLU TYR GLU VAL THR VAL          
SEQRES  11 C  286  HIS HIS LEU PRO LYS PRO ILE PRO ASP GLY ASP PRO ASN          
SEQRES  12 C  286  HIS GLN SER LYS ASN PHE LEU VAL PRO ASP CYS GLU HIS          
SEQRES  13 C  286  ALA ARG MET LYS VAL THR THR PRO CYS MET SER SER GLY          
SEQRES  14 C  286  SER LEU TRP ASP PRO ASN ILE THR VAL GLU THR LEU GLU          
SEQRES  15 C  286  ALA HIS GLN LEU ARG VAL SER PHE THR LEU TRP ASN GLU          
SEQRES  16 C  286  SER THR HIS TYR GLN ILE LEU LEU THR SER PHE PRO HIS          
SEQRES  17 C  286  MET GLU ASN HIS SER CYS PHE GLU HIS MET HIS HIS ILE          
SEQRES  18 C  286  PRO ALA PRO ARG PRO GLU GLU PHE HIS GLN ARG SER ASN          
SEQRES  19 C  286  VAL THR LEU THR LEU ARG ASN LEU LYS GLY CYS CYS ARG          
SEQRES  20 C  286  HIS GLN VAL GLN ILE GLN PRO PHE PHE SER SER CYS LEU          
SEQRES  21 C  286  ASN ASP CYS LEU ARG HIS SER ALA THR VAL SER CYS PRO          
SEQRES  22 C  286  GLU MET PRO ASP THR PRO GLU PRO ILE PRO ASP TYR MET          
MODRES 3JVF ASN A   53  ASN  GLYCOSYLATION SITE                                 
MODRES 3JVF ASN C   18  ASN  GLYCOSYLATION SITE                                 
MODRES 3JVF ASN C   23  ASN  GLYCOSYLATION SITE                                 
MODRES 3JVF ASN C   36  ASN  GLYCOSYLATION SITE                                 
MODRES 3JVF ASN C  194  ASN  GLYCOSYLATION SITE                                 
MODRES 3JVF ASN C  234  ASN  GLYCOSYLATION SITE                                 
MODRES 3JVF MLY C   43  LYS  N-DIMETHYL-LYSINE                                  
HET    MLY  C  43      11                                                       
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET     CA  B 134       1                                                       
HET    NAG  C 301      14                                                       
HET    NAG  C 302      14                                                       
HET    NAG  C 303      14                                                       
HET    NAG  C 304      14                                                       
HET    NAG  C 305      14                                                       
HETNAM     MLY N-DIMETHYL-LYSINE                                                
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM      CA CALCIUM ION                                                      
FORMUL   3  MLY    C8 H18 N2 O2                                                 
FORMUL   4  NAG    7(C8 H15 N O6)                                               
FORMUL   5   CA    CA 2+                                                        
HELIX    1   1 ASN A   43  SER A   48  1                                   6    
HELIX    2   2 ASN B   43  SER B   48  1                                   6    
HELIX    3   3 ASP C   72  LEU C   76  5                                   5    
HELIX    4   4 THR C  162  SER C  167  1                                   6    
SHEET    1   A 5 MET A  25  LYS A  26  0                                        
SHEET    2   A 5 LYS B  26  ASP B  28 -1  O  LEU B  27   N  MET A  25           
SHEET    3   A 5 PHE A 111  VAL A 125  1  N  PHE A 111   O  ASP B  28           
SHEET    4   A 5 ASN A  89  ARG A 102 -1  N  VAL A  99   O  GLU A 114           
SHEET    5   A 5 ARG A  62  TYR A  63 -1  N  TYR A  63   O  VAL A 100           
SHEET    1   B 2 TRP A  52  TRP A  58  0                                        
SHEET    2   B 2 GLU A  66  CYS A  72 -1  O  VAL A  67   N  THR A  57           
SHEET    1   C 2 CYS A  77  ILE A  78  0                                        
SHEET    2   C 2 GLU A  84  ASP A  85 -1  O  ASP A  85   N  CYS A  77           
SHEET    1   D 5 ILE A 129  HIS A 131  0                                        
SHEET    2   D 5 ARG C 265  VAL C 270  1  O  ARG C 265   N  HIS A 130           
SHEET    3   D 5 ARG C 247  PRO C 254 -1  N  HIS C 248   O  VAL C 270           
SHEET    4   D 5 TYR C 199  PHE C 206 -1  N  THR C 204   O  GLN C 249           
SHEET    5   D 5 PHE C 215  ILE C 221 -1  O  HIS C 217   N  LEU C 203           
SHEET    1   E 2 TRP B  52  TRP B  58  0                                        
SHEET    2   E 2 GLU B  66  CYS B  72 -1  O  GLN B  69   N  THR B  55           
SHEET    1   F 3 ARG B  62  TYR B  63  0                                        
SHEET    2   F 3 GLU B  84  LYS B 103 -1  O  VAL B 100   N  TYR B  63           
SHEET    3   F 3 GLY B  76  ILE B  78 -1  N  CYS B  77   O  MET B  88           
SHEET    1   G 3 ARG B  62  TYR B  63  0                                        
SHEET    2   G 3 GLU B  84  LYS B 103 -1  O  VAL B 100   N  TYR B  63           
SHEET    3   G 3 SER B 110  VAL B 125 -1  O  SER B 110   N  LYS B 103           
SHEET    1   H 4 CYS C  19  VAL C  21  0                                        
SHEET    2   H 4 PHE C  98  PHE C 100 -1  O  GLU C  99   N  THR C  20           
SHEET    3   H 4 GLY C  80  GLN C  87 -1  N  ALA C  81   O  PHE C  98           
SHEET    4   H 4 GLU C  92  CYS C  95 -1  O  GLU C  92   N  GLN C  87           
SHEET    1   I 5 CYS C  19  VAL C  21  0                                        
SHEET    2   I 5 PHE C  98  PHE C 100 -1  O  GLU C  99   N  THR C  20           
SHEET    3   I 5 GLY C  80  GLN C  87 -1  N  ALA C  81   O  PHE C  98           
SHEET    4   I 5 GLU C 125  LEU C 133 -1  O  LEU C 133   N  GLY C  80           
SHEET    5   I 5 SER C 146  LEU C 150 -1  O  PHE C 149   N  TYR C 126           
SHEET    1   J 3 PRO C  42  HIS C  53  0                                        
SHEET    2   J 3 LEU C  59  LEU C  69 -1  O  VAL C  62   N  HIS C  50           
SHEET    3   J 3 ARG C 112  VAL C 119 -1  O  PHE C 113   N  TRP C  67           
SHEET    1   K 3 THR C 177  GLU C 179  0                                        
SHEET    2   K 3 LEU C 186  PHE C 190 -1  O  SER C 189   N  THR C 177           
SHEET    3   K 3 SER C 233  LEU C 237 -1  O  LEU C 237   N  LEU C 186           
SSBOND   1 CYS A   72    CYS A  122                          1555   1555  2.04  
SSBOND   2 CYS A   77    CYS A  124                          1555   1555  2.05  
SSBOND   3 CYS B   72    CYS B  122                          1555   1555  2.04  
SSBOND   4 CYS B   77    CYS B  124                          1555   1555  2.03  
SSBOND   5 CYS C   12    CYS C   19                          1555   1555  2.03  
SSBOND   6 CYS C   26    CYS C   95                          1555   1555  2.03  
SSBOND   7 CYS C  154    CYS C  165                          1555   1555  2.04  
SSBOND   8 CYS C  214    CYS C  245                          1555   1555  2.04  
SSBOND   9 CYS C  259    CYS C  263                          1555   1555  2.05  
LINK         ND2 ASN A  53                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN C  18                 C1  NAG C 303     1555   1555  1.45  
LINK         ND2 ASN C  23                 C1  NAG C 305     1555   1555  1.44  
LINK         ND2 ASN C  36                 C1  NAG C 302     1555   1555  1.45  
LINK         C   PRO C  42                 N   MLY C  43     1555   1555  1.32  
LINK         C   MLY C  43                 N   ASP C  44     1555   1555  1.33  
LINK         ND2 ASN C 194                 C1  NAG C 301     1555   1555  1.44  
LINK         ND2 ASN C 234                 C1  NAG C 304     1555   1555  1.45  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.43  
LINK         OD1 ASN B  43                CA    CA B 134     1555   1555  2.02  
LINK         ND2 ASN B  43                CA    CA B 134     1555   1555  2.38  
LINK         OE1 GLU B  45                CA    CA B 134     1555   1555  2.69  
LINK         OE2 GLU B  45                CA    CA B 134     1555   1555  2.90  
CISPEP   1 TYR A   63    PRO A   64          0         2.41                     
CISPEP   2 TYR B   63    PRO B   64          0         4.47                     
CISPEP   3 LEU C  133    PRO C  134          0         4.74                     
CRYST1  170.730  170.730   81.900  90.00  90.00  90.00 P 41 21 2    16          
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      0.005857  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005857  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012210        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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