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Database: PDB
Entry: 5NAN
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HEADER    CYTOKINE                                28-FEB-17   5NAN              
TITLE     CRYSTAL STRUCTURE OF HUMAN IL-17AF IN COMPLEX WITH HUMAN IL-17RA      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-17A;                                           
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 SYNONYM: IL-17A,CYTOTOXIC T-LYMPHOCYTE-ASSOCIATED ANTIGEN 8,CTLA-8;  
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: INTERLEUKIN-17 RECEPTOR A;                                 
COMPND   8 CHAIN: B, C;                                                         
COMPND   9 SYNONYM: IL-17RA,CDW217;                                             
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: INTERLEUKIN-17F;                                           
COMPND  13 CHAIN: E, F;                                                         
COMPND  14 SYNONYM: IL-17F,CYTOKINE ML-1;                                       
COMPND  15 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: IL17A, CTLA8, IL17;                                            
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S;                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PCI;                                      
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: IL17RA, IL17R;                                                 
SOURCE  16 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-;                          
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PRS5;                                     
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: IL17F;                                                         
SOURCE  26 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  28 EXPRESSION_SYSTEM_CELL_LINE: HEK293S;                                
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PCI                                       
KEYWDS    CYSTINE-KNOT, FIBRONECTIN TYPE III, CYTOKINE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-M.RONDEAU,A.GOEPFERT                                               
REVDAT   5   29-JUL-20 5NAN    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE   ATOM                              
REVDAT   4   24-JAN-18 5NAN    1       SOURCE                                   
REVDAT   3   20-SEP-17 5NAN    1       JRNL                                     
REVDAT   2   13-SEP-17 5NAN    1       AUTHOR                                   
REVDAT   1   06-SEP-17 5NAN    0                                                
JRNL        AUTH   A.GOEPFERT,S.LEHMANN,E.WIRTH,J.M.RONDEAU                     
JRNL        TITL   THE HUMAN IL-17A/F HETERODIMER: A TWO-FACED CYTOKINE WITH    
JRNL        TITL 2 UNIQUE RECEPTOR RECOGNITION PROPERTIES.                      
JRNL        REF    SCI REP                       V.   7  8906 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   28827714                                                     
JRNL        DOI    10.1038/S41598-017-08360-9                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.6                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 66.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 20143                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.189                          
REMARK   3   R VALUE            (WORKING SET)  : 0.186                          
REMARK   3   FREE R VALUE                      : 0.243                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.010                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1009                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : 0.000                          
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 10                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.48                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 84.22                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2520                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2580                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2391                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2570                   
REMARK   3   BIN FREE R VALUE                        : 0.2730                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.12                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 129                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7814                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 109                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 145.2                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 169.1                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 36.36560                                             
REMARK   3    B22 (A**2) : -38.01060                                            
REMARK   3    B33 (A**2) : 1.64500                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 24.96160                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.540               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.491               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.929                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.911                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8161   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11144  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2811   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 204    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1175   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8161   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1086   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 8618   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.34                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.31                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 23.18                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   13.7063   -6.9679   32.9451           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3280 T22:    0.0609                                    
REMARK   3     T33:   -0.0762 T12:   -0.2959                                    
REMARK   3     T13:   -0.3045 T23:    0.2017                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.3224 L22:    4.6297                                    
REMARK   3     L33:    4.6022 L12:    1.0286                                    
REMARK   3     L13:    1.2179 L23:    2.9340                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0524 S12:   -0.1333 S13:    0.0814                     
REMARK   3     S21:    0.1011 S22:    0.1675 S23:   -0.4891                     
REMARK   3     S31:    0.1785 S32:    0.4678 S33:   -0.1151                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    2.6648   -7.6755   13.9743           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3400 T22:    0.0965                                    
REMARK   3     T33:   -0.2962 T12:   -0.2828                                    
REMARK   3     T13:   -0.0326 T23:    0.2705                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.2094 L22:    6.0817                                    
REMARK   3     L33:    1.2505 L12:   -1.9235                                    
REMARK   3     L13:   -0.2790 L23:    0.8484                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0759 S12:    0.4988 S13:    0.1658                     
REMARK   3     S21:   -0.0698 S22:   -0.0286 S23:   -0.6275                     
REMARK   3     S31:   -0.1884 S32:    0.5083 S33:   -0.0473                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -52.2768   -1.3293   37.9313           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2487 T22:   -0.2464                                    
REMARK   3     T33:   -0.3559 T12:    0.0835                                    
REMARK   3     T13:   -0.0384 T23:   -0.1952                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.3527 L22:    2.9901                                    
REMARK   3     L33:    3.1540 L12:    2.4113                                    
REMARK   3     L13:   -0.0635 L23:   -1.6920                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1520 S12:   -0.4282 S13:    0.0208                     
REMARK   3     S21:   -0.0577 S22:    0.0086 S23:    0.0175                     
REMARK   3     S31:   -0.1168 S32:   -0.6126 S33:   -0.1606                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -62.8902    0.0797   18.6009           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3472 T22:    0.3402                                    
REMARK   3     T33:   -0.3017 T12:   -0.1152                                    
REMARK   3     T13:   -0.2459 T23:    0.0260                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.7166 L22:    6.0816                                    
REMARK   3     L33:    2.9619 L12:    1.3524                                    
REMARK   3     L13:   -1.4580 L23:   -3.0229                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0397 S12:    0.6630 S13:    0.3233                     
REMARK   3     S21:   -0.1554 S22:    0.1161 S23:    0.2577                     
REMARK   3     S31:    0.2141 S32:   -1.0776 S33:   -0.1557                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { E|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -51.5893   -0.1132   17.0697           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2656 T22:    0.1423                                    
REMARK   3     T33:   -0.3936 T12:   -0.0825                                    
REMARK   3     T13:   -0.0403 T23:   -0.0966                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.7259 L22:    9.5049                                    
REMARK   3     L33:    4.7337 L12:    4.0968                                    
REMARK   3     L13:   -0.5791 L23:   -2.2164                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1749 S12:    0.9060 S13:   -0.0595                     
REMARK   3     S21:   -0.4672 S22:   -0.3274 S23:   -0.3342                     
REMARK   3     S31:    0.3029 S32:   -0.0372 S33:    0.5023                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { F|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):    1.7399   -4.7051   34.3514           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1475 T22:    0.0356                                    
REMARK   3     T33:   -0.3535 T12:   -0.2391                                    
REMARK   3     T13:   -0.1419 T23:    0.2568                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.1933 L22:    6.8610                                    
REMARK   3     L33:    2.0530 L12:   -2.0655                                    
REMARK   3     L13:   -0.0759 L23:   -0.1282                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0766 S12:   -0.4665 S13:   -0.0804                     
REMARK   3     S21:    0.4334 S22:    0.0226 S23:   -0.1239                     
REMARK   3     S31:   -0.0099 S32:   -0.0862 S33:    0.0539                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5NAN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 28-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003780.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-FEB-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.999920                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 20621                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 66.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.368                              
REMARK 200  R MERGE                    (I) : 0.14900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.34                               
REMARK 200  R MERGE FOR SHELL          (I) : 3.48300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.320                              
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: PDBID 4HSA                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES, 15% PEG MME 5,000, 0.05M     
REMARK 280  AMMONIUM ACETATE, PH 7.5, VAPOR DIFFUSION, TEMPERATURE 293K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-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        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 23410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, F, G                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10850 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 23830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E                               
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     GLY A    24                                                      
REMARK 465     ILE A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     ILE A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     ARG A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     GLY A    32                                                      
REMARK 465     CYS A    33                                                      
REMARK 465     PRO A    34                                                      
REMARK 465     ASN A    35                                                      
REMARK 465     SER A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     ASP A    38                                                      
REMARK 465     LYS A    39                                                      
REMARK 465     ASN A    40                                                      
REMARK 465     PHE A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     ARG A    43                                                      
REMARK 465     ASN A    53                                                      
REMARK 465     ARG A    54                                                      
REMARK 465     ASN A    55                                                      
REMARK 465     THR A    56                                                      
REMARK 465     ASN A    57                                                      
REMARK 465     THR A    58                                                      
REMARK 465     ASN A    59                                                      
REMARK 465     PRO A    60                                                      
REMARK 465     LYS A    61                                                      
REMARK 465     ARG A    62                                                      
REMARK 465     SER A    63                                                      
REMARK 465     ALA A   155                                                      
REMARK 465     PRO B   304                                                      
REMARK 465     GLU B   305                                                      
REMARK 465     MET B   306                                                      
REMARK 465     PRO B   307                                                      
REMARK 465     ASP B   308                                                      
REMARK 465     THR B   309                                                      
REMARK 465     PRO B   310                                                      
REMARK 465     GLU B   311                                                      
REMARK 465     PRO B   312                                                      
REMARK 465     ILE B   313                                                      
REMARK 465     PRO B   314                                                      
REMARK 465     ASP B   315                                                      
REMARK 465     TYR B   316                                                      
REMARK 465     MET B   317                                                      
REMARK 465     PRO B   318                                                      
REMARK 465     LEU B   319                                                      
REMARK 465     TRP B   320                                                      
REMARK 465     GLU B   321                                                      
REMARK 465     PHE B   322                                                      
REMARK 465     ARG B   323                                                      
REMARK 465     HIS B   324                                                      
REMARK 465     ASP B   325                                                      
REMARK 465     SER B   326                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     GLY B   328                                                      
REMARK 465     GLY B   329                                                      
REMARK 465     LEU B   330                                                      
REMARK 465     ASN B   331                                                      
REMARK 465     ASP B   332                                                      
REMARK 465     ILE B   333                                                      
REMARK 465     PHE B   334                                                      
REMARK 465     GLU B   335                                                      
REMARK 465     ALA B   336                                                      
REMARK 465     GLN B   337                                                      
REMARK 465     LYS B   338                                                      
REMARK 465     ILE B   339                                                      
REMARK 465     GLU B   340                                                      
REMARK 465     TRP B   341                                                      
REMARK 465     HIS B   342                                                      
REMARK 465     GLU B   343                                                      
REMARK 465     PRO C   304                                                      
REMARK 465     GLU C   305                                                      
REMARK 465     MET C   306                                                      
REMARK 465     PRO C   307                                                      
REMARK 465     ASP C   308                                                      
REMARK 465     THR C   309                                                      
REMARK 465     PRO C   310                                                      
REMARK 465     GLU C   311                                                      
REMARK 465     PRO C   312                                                      
REMARK 465     ILE C   313                                                      
REMARK 465     PRO C   314                                                      
REMARK 465     ASP C   315                                                      
REMARK 465     TYR C   316                                                      
REMARK 465     MET C   317                                                      
REMARK 465     PRO C   318                                                      
REMARK 465     LEU C   319                                                      
REMARK 465     TRP C   320                                                      
REMARK 465     GLU C   321                                                      
REMARK 465     PHE C   322                                                      
REMARK 465     ARG C   323                                                      
REMARK 465     HIS C   324                                                      
REMARK 465     ASP C   325                                                      
REMARK 465     SER C   326                                                      
REMARK 465     GLY C   327                                                      
REMARK 465     GLY C   328                                                      
REMARK 465     GLY C   329                                                      
REMARK 465     LEU C   330                                                      
REMARK 465     ASN C   331                                                      
REMARK 465     ASP C   332                                                      
REMARK 465     ILE C   333                                                      
REMARK 465     PHE C   334                                                      
REMARK 465     GLU C   335                                                      
REMARK 465     ALA C   336                                                      
REMARK 465     GLN C   337                                                      
REMARK 465     LYS C   338                                                      
REMARK 465     ILE C   339                                                      
REMARK 465     GLU C   340                                                      
REMARK 465     TRP C   341                                                      
REMARK 465     HIS C   342                                                      
REMARK 465     GLU C   343                                                      
REMARK 465     GLY D    24                                                      
REMARK 465     ILE D    25                                                      
REMARK 465     THR D    26                                                      
REMARK 465     ILE D    27                                                      
REMARK 465     PRO D    28                                                      
REMARK 465     ARG D    29                                                      
REMARK 465     ASN D    30                                                      
REMARK 465     PRO D    31                                                      
REMARK 465     GLY D    32                                                      
REMARK 465     CYS D    33                                                      
REMARK 465     PRO D    34                                                      
REMARK 465     ASN D    35                                                      
REMARK 465     SER D    36                                                      
REMARK 465     GLU D    37                                                      
REMARK 465     ASP D    38                                                      
REMARK 465     LYS D    39                                                      
REMARK 465     ASN D    40                                                      
REMARK 465     PHE D    41                                                      
REMARK 465     PRO D    42                                                      
REMARK 465     THR D    56                                                      
REMARK 465     ASN D    57                                                      
REMARK 465     THR D    58                                                      
REMARK 465     ASN D    59                                                      
REMARK 465     PRO D    60                                                      
REMARK 465     LYS D    61                                                      
REMARK 465     ARG D    62                                                      
REMARK 465     SER D    63                                                      
REMARK 465     ALA D   155                                                      
REMARK 465     GLU E    25                                                      
REMARK 465     PHE E    26                                                      
REMARK 465     ARG E    27                                                      
REMARK 465     HIS E    28                                                      
REMARK 465     ASP E    29                                                      
REMARK 465     SER E    30                                                      
REMARK 465     ARG E    31                                                      
REMARK 465     LYS E    32                                                      
REMARK 465     ILE E    33                                                      
REMARK 465     PRO E    34                                                      
REMARK 465     LYS E    35                                                      
REMARK 465     VAL E    36                                                      
REMARK 465     GLY E    37                                                      
REMARK 465     HIS E    38                                                      
REMARK 465     THR E    39                                                      
REMARK 465     PHE E    40                                                      
REMARK 465     PHE E    41                                                      
REMARK 465     GLN E    42                                                      
REMARK 465     LYS E    43                                                      
REMARK 465     PRO E    44                                                      
REMARK 465     GLU E    45                                                      
REMARK 465     ILE E   159                                                      
REMARK 465     HIS E   160                                                      
REMARK 465     HIS E   161                                                      
REMARK 465     VAL E   162                                                      
REMARK 465     GLN E   163                                                      
REMARK 465     GLU F    25                                                      
REMARK 465     PHE F    26                                                      
REMARK 465     ARG F    27                                                      
REMARK 465     HIS F    28                                                      
REMARK 465     ASP F    29                                                      
REMARK 465     SER F    30                                                      
REMARK 465     ARG F    31                                                      
REMARK 465     LYS F    32                                                      
REMARK 465     ILE F    33                                                      
REMARK 465     PRO F    34                                                      
REMARK 465     LYS F    35                                                      
REMARK 465     VAL F    36                                                      
REMARK 465     GLY F    37                                                      
REMARK 465     HIS F    38                                                      
REMARK 465     THR F    39                                                      
REMARK 465     PHE F    40                                                      
REMARK 465     PHE F    41                                                      
REMARK 465     GLN F    42                                                      
REMARK 465     LYS F    43                                                      
REMARK 465     PRO F    44                                                      
REMARK 465     GLU F    45                                                      
REMARK 465     ILE F   159                                                      
REMARK 465     HIS F   160                                                      
REMARK 465     HIS F   161                                                      
REMARK 465     VAL F   162                                                      
REMARK 465     GLN F   163                                                      
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     ASN E  65    CG   OD1  ND2                                       
REMARK 470     ASN F  65    CG   OD1  ND2                                       
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    ASN B  54   C   -  N   -  CA  ANGL. DEV. =  15.3 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    ASP A  65       25.19    175.77                                   
REMARK 500    CYS A 129      155.52    -44.31                                   
REMARK 500    LEU B  36      -74.46    -78.61                                   
REMARK 500    LYS B  53      171.37    165.62                                   
REMARK 500    ASN B  54      136.19    -25.02                                   
REMARK 500    SER B  72      154.15    -45.56                                   
REMARK 500    GLN B  77      112.53   -160.62                                   
REMARK 500    ASP B 103      158.33    -44.75                                   
REMARK 500    HIS B 138       14.43   -159.01                                   
REMARK 500    ASP B 154       79.29     71.16                                   
REMARK 500    ILE B 168      154.92    -49.66                                   
REMARK 500    PRO B 173      -68.15     -3.59                                   
REMARK 500    ASN B 174       -4.58     65.39                                   
REMARK 500    CYS B 185        4.81    -67.09                                   
REMARK 500    LYS B 191        1.89    -66.56                                   
REMARK 500    ASN B 206       22.44     48.96                                   
REMARK 500    ILE B 207      124.11    -32.01                                   
REMARK 500    ALA B 214       42.17    -67.90                                   
REMARK 500    ASN B 225       39.69    -80.16                                   
REMARK 500    PRO B 238     -166.13    -68.41                                   
REMARK 500    HIS B 261       -2.50     66.37                                   
REMARK 500    LEU B 291      -93.96     68.71                                   
REMARK 500    ASP B 293        5.65    -53.31                                   
REMARK 500    LEU C  36      -96.35    -65.89                                   
REMARK 500    GLN C  77      112.64   -160.05                                   
REMARK 500    ASP C 103      156.62    -47.52                                   
REMARK 500    HIS C 137     -168.53   -110.44                                   
REMARK 500    HIS C 138       -7.07   -150.70                                   
REMARK 500    ILE C 168      155.61    -49.83                                   
REMARK 500    PRO C 169      130.05    -39.67                                   
REMARK 500    PRO C 173      -76.62     -5.82                                   
REMARK 500    ILE C 207      124.68    -32.15                                   
REMARK 500    ALA C 214       42.95    -68.18                                   
REMARK 500    ASN C 225       39.46    -85.72                                   
REMARK 500    PRO C 238     -165.84    -68.16                                   
REMARK 500    HIS C 261       -2.46     66.78                                   
REMARK 500    LEU C 291      -99.49     51.98                                   
REMARK 500    ASP C 293        8.48    -55.39                                   
REMARK 500    ASP D  65       26.33    176.19                                   
REMARK 500    CYS D 129      150.91    -43.82                                   
REMARK 500    ILE E  61      100.75     -1.44                                   
REMARK 500    ARG E  67      -93.96      9.22                                   
REMARK 500    MET E  70      108.15    -41.13                                   
REMARK 500    SER E  80       77.05   -111.97                                   
REMARK 500    PRO E 157     -177.24    -62.79                                   
REMARK 500    ILE F  61      101.09     -0.02                                   
REMARK 500    ARG F  67      -89.72     -0.61                                   
REMARK 500    MET F  70      107.82    -40.31                                   
REMARK 500    SER F  80       79.92   -117.30                                   
REMARK 500    PRO F 157     -178.96    -65.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5N92   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN IL-17AF                                   
REMARK 900 RELATED ID: 5N9B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF UNLIGANDED HUMAN IL-17RA                        
DBREF  5NAN A   24   155  UNP    Q16552   IL17_HUMAN      24    155             
DBREF  5NAN B   33   320  UNP    Q96F46   I17RA_HUMAN     33    320             
DBREF  5NAN C   33   320  UNP    Q96F46   I17RA_HUMAN     33    320             
DBREF  5NAN D   24   155  UNP    Q16552   IL17_HUMAN      24    155             
DBREF  5NAN E   31   163  UNP    Q96PD4   IL17F_HUMAN     31    163             
DBREF  5NAN F   31   163  UNP    Q96PD4   IL17F_HUMAN     31    163             
SEQADV 5NAN GLU B  321  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN PHE B  322  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ARG B  323  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN HIS B  324  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ASP B  325  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN SER B  326  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLY B  327  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLY B  328  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLY B  329  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN LEU B  330  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ASN B  331  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ASP B  332  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ILE B  333  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN PHE B  334  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLU B  335  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ALA B  336  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLN B  337  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN LYS B  338  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ILE B  339  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLU B  340  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN TRP B  341  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN HIS B  342  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLU B  343  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLU C  321  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN PHE C  322  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ARG C  323  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN HIS C  324  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ASP C  325  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN SER C  326  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLY C  327  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLY C  328  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLY C  329  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN LEU C  330  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ASN C  331  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ASP C  332  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ILE C  333  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN PHE C  334  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLU C  335  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ALA C  336  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLN C  337  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN LYS C  338  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN ILE C  339  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLU C  340  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN TRP C  341  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN HIS C  342  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLU C  343  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 5NAN GLU E   25  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN PHE E   26  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN ARG E   27  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN HIS E   28  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN ASP E   29  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN SER E   30  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN GLU F   25  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN PHE F   26  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN ARG F   27  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN HIS F   28  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN ASP F   29  UNP  Q96PD4              EXPRESSION TAG                 
SEQADV 5NAN SER F   30  UNP  Q96PD4              EXPRESSION TAG                 
SEQRES   1 A  132  GLY ILE THR ILE PRO ARG ASN PRO GLY CYS PRO ASN SER          
SEQRES   2 A  132  GLU ASP LYS ASN PHE PRO ARG THR VAL MET VAL ASN LEU          
SEQRES   3 A  132  ASN ILE HIS ASN ARG ASN THR ASN THR ASN PRO LYS ARG          
SEQRES   4 A  132  SER SER ASP TYR TYR ASN ARG SER THR SER PRO TRP ASN          
SEQRES   5 A  132  LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR PRO SER VAL          
SEQRES   6 A  132  ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY CYS ILE ASN          
SEQRES   7 A  132  ALA ASP GLY ASN VAL ASP TYR HIS MET ASN SER VAL PRO          
SEQRES   8 A  132  ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG GLU PRO PRO          
SEQRES   9 A  132  HIS CYS PRO ASN SER PHE ARG LEU GLU LYS ILE LEU VAL          
SEQRES  10 A  132  SER VAL GLY CYS THR CYS VAL THR PRO ILE VAL HIS HIS          
SEQRES  11 A  132  VAL ALA                                                      
SEQRES   1 B  311  LEU ARG LEU LEU ASP HIS ARG ALA LEU VAL CYS SER GLN          
SEQRES   2 B  311  PRO GLY LEU ASN CYS THR VAL LYS ASN SER THR CYS LEU          
SEQRES   3 B  311  ASP ASP SER TRP ILE HIS PRO ARG ASN LEU THR PRO SER          
SEQRES   4 B  311  SER PRO LYS ASP LEU GLN ILE GLN LEU HIS PHE ALA HIS          
SEQRES   5 B  311  THR GLN GLN GLY ASP LEU PHE PRO VAL ALA HIS ILE GLU          
SEQRES   6 B  311  TRP THR LEU GLN THR ASP ALA SER ILE LEU TYR LEU GLU          
SEQRES   7 B  311  GLY ALA GLU LEU SER VAL LEU GLN LEU ASN THR ASN GLU          
SEQRES   8 B  311  ARG LEU CYS VAL ARG PHE GLU PHE LEU SER LYS LEU ARG          
SEQRES   9 B  311  HIS HIS HIS ARG ARG TRP ARG PHE THR PHE SER HIS PHE          
SEQRES  10 B  311  VAL VAL ASP PRO ASP GLN GLU TYR GLU VAL THR VAL HIS          
SEQRES  11 B  311  HIS LEU PRO LYS PRO ILE PRO ASP GLY ASP PRO ASN HIS          
SEQRES  12 B  311  GLN SER LYS ASN PHE LEU VAL PRO ASP CYS GLU HIS ALA          
SEQRES  13 B  311  ARG MET LYS VAL THR THR PRO CYS MET SER SER GLY SER          
SEQRES  14 B  311  LEU TRP ASP PRO ASN ILE THR VAL GLU THR LEU GLU ALA          
SEQRES  15 B  311  HIS GLN LEU ARG VAL SER PHE THR LEU TRP ASN GLU SER          
SEQRES  16 B  311  THR HIS TYR GLN ILE LEU LEU THR SER PHE PRO HIS MET          
SEQRES  17 B  311  GLU ASN HIS SER CYS PHE GLU HIS MET HIS HIS ILE PRO          
SEQRES  18 B  311  ALA PRO ARG PRO GLU GLU PHE HIS GLN ARG SER ASN VAL          
SEQRES  19 B  311  THR LEU THR LEU ARG ASN LEU LYS GLY CYS CYS ARG HIS          
SEQRES  20 B  311  GLN VAL GLN ILE GLN PRO PHE PHE SER SER CYS LEU ASN          
SEQRES  21 B  311  ASP CYS LEU ARG HIS SER ALA THR VAL SER CYS PRO GLU          
SEQRES  22 B  311  MET PRO ASP THR PRO GLU PRO ILE PRO ASP TYR MET PRO          
SEQRES  23 B  311  LEU TRP GLU PHE ARG HIS ASP SER GLY GLY GLY LEU ASN          
SEQRES  24 B  311  ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU              
SEQRES   1 C  311  LEU ARG LEU LEU ASP HIS ARG ALA LEU VAL CYS SER GLN          
SEQRES   2 C  311  PRO GLY LEU ASN CYS THR VAL LYS ASN SER THR CYS LEU          
SEQRES   3 C  311  ASP ASP SER TRP ILE HIS PRO ARG ASN LEU THR PRO SER          
SEQRES   4 C  311  SER PRO LYS ASP LEU GLN ILE GLN LEU HIS PHE ALA HIS          
SEQRES   5 C  311  THR GLN GLN GLY ASP LEU PHE PRO VAL ALA HIS ILE GLU          
SEQRES   6 C  311  TRP THR LEU GLN THR ASP ALA SER ILE LEU TYR LEU GLU          
SEQRES   7 C  311  GLY ALA GLU LEU SER VAL LEU GLN LEU ASN THR ASN GLU          
SEQRES   8 C  311  ARG LEU CYS VAL ARG PHE GLU PHE LEU SER LYS LEU ARG          
SEQRES   9 C  311  HIS HIS HIS ARG ARG TRP ARG PHE THR PHE SER HIS PHE          
SEQRES  10 C  311  VAL VAL ASP PRO ASP GLN GLU TYR GLU VAL THR VAL HIS          
SEQRES  11 C  311  HIS LEU PRO LYS PRO ILE PRO ASP GLY ASP PRO ASN HIS          
SEQRES  12 C  311  GLN SER LYS ASN PHE LEU VAL PRO ASP CYS GLU HIS ALA          
SEQRES  13 C  311  ARG MET LYS VAL THR THR PRO CYS MET SER SER GLY SER          
SEQRES  14 C  311  LEU TRP ASP PRO ASN ILE THR VAL GLU THR LEU GLU ALA          
SEQRES  15 C  311  HIS GLN LEU ARG VAL SER PHE THR LEU TRP ASN GLU SER          
SEQRES  16 C  311  THR HIS TYR GLN ILE LEU LEU THR SER PHE PRO HIS MET          
SEQRES  17 C  311  GLU ASN HIS SER CYS PHE GLU HIS MET HIS HIS ILE PRO          
SEQRES  18 C  311  ALA PRO ARG PRO GLU GLU PHE HIS GLN ARG SER ASN VAL          
SEQRES  19 C  311  THR LEU THR LEU ARG ASN LEU LYS GLY CYS CYS ARG HIS          
SEQRES  20 C  311  GLN VAL GLN ILE GLN PRO PHE PHE SER SER CYS LEU ASN          
SEQRES  21 C  311  ASP CYS LEU ARG HIS SER ALA THR VAL SER CYS PRO GLU          
SEQRES  22 C  311  MET PRO ASP THR PRO GLU PRO ILE PRO ASP TYR MET PRO          
SEQRES  23 C  311  LEU TRP GLU PHE ARG HIS ASP SER GLY GLY GLY LEU ASN          
SEQRES  24 C  311  ASP ILE PHE GLU ALA GLN LYS ILE GLU TRP HIS GLU              
SEQRES   1 D  132  GLY ILE THR ILE PRO ARG ASN PRO GLY CYS PRO ASN SER          
SEQRES   2 D  132  GLU ASP LYS ASN PHE PRO ARG THR VAL MET VAL ASN LEU          
SEQRES   3 D  132  ASN ILE HIS ASN ARG ASN THR ASN THR ASN PRO LYS ARG          
SEQRES   4 D  132  SER SER ASP TYR TYR ASN ARG SER THR SER PRO TRP ASN          
SEQRES   5 D  132  LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR PRO SER VAL          
SEQRES   6 D  132  ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY CYS ILE ASN          
SEQRES   7 D  132  ALA ASP GLY ASN VAL ASP TYR HIS MET ASN SER VAL PRO          
SEQRES   8 D  132  ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG GLU PRO PRO          
SEQRES   9 D  132  HIS CYS PRO ASN SER PHE ARG LEU GLU LYS ILE LEU VAL          
SEQRES  10 D  132  SER VAL GLY CYS THR CYS VAL THR PRO ILE VAL HIS HIS          
SEQRES  11 D  132  VAL ALA                                                      
SEQRES   1 E  139  GLU PHE ARG HIS ASP SER ARG LYS ILE PRO LYS VAL GLY          
SEQRES   2 E  139  HIS THR PHE PHE GLN LYS PRO GLU SER CYS PRO PRO VAL          
SEQRES   3 E  139  PRO GLY GLY SER MET LYS LEU ASP ILE GLY ILE ILE ASN          
SEQRES   4 E  139  GLU ASN GLN ARG VAL SER MET SER ARG ASN ILE GLU SER          
SEQRES   5 E  139  ARG SER THR SER PRO TRP ASN TYR THR VAL THR TRP ASP          
SEQRES   6 E  139  PRO ASN ARG TYR PRO SER GLU VAL VAL GLN ALA GLN CYS          
SEQRES   7 E  139  ARG ASN LEU GLY CYS ILE ASN ALA GLN GLY LYS GLU ASP          
SEQRES   8 E  139  ILE SER MET ASN SER VAL PRO ILE GLN GLN GLU THR LEU          
SEQRES   9 E  139  VAL VAL ARG ARG LYS HIS GLN GLY CYS SER VAL SER PHE          
SEQRES  10 E  139  GLN LEU GLU LYS VAL LEU VAL THR VAL GLY CYS THR CYS          
SEQRES  11 E  139  VAL THR PRO VAL ILE HIS HIS VAL GLN                          
SEQRES   1 F  139  GLU PHE ARG HIS ASP SER ARG LYS ILE PRO LYS VAL GLY          
SEQRES   2 F  139  HIS THR PHE PHE GLN LYS PRO GLU SER CYS PRO PRO VAL          
SEQRES   3 F  139  PRO GLY GLY SER MET LYS LEU ASP ILE GLY ILE ILE ASN          
SEQRES   4 F  139  GLU ASN GLN ARG VAL SER MET SER ARG ASN ILE GLU SER          
SEQRES   5 F  139  ARG SER THR SER PRO TRP ASN TYR THR VAL THR TRP ASP          
SEQRES   6 F  139  PRO ASN ARG TYR PRO SER GLU VAL VAL GLN ALA GLN CYS          
SEQRES   7 F  139  ARG ASN LEU GLY CYS ILE ASN ALA GLN GLY LYS GLU ASP          
SEQRES   8 F  139  ILE SER MET ASN SER VAL PRO ILE GLN GLN GLU THR LEU          
SEQRES   9 F  139  VAL VAL ARG ARG LYS HIS GLN GLY CYS SER VAL SER PHE          
SEQRES  10 F  139  GLN LEU GLU LYS VAL LEU VAL THR VAL GLY CYS THR CYS          
SEQRES  11 F  139  VAL THR PRO VAL ILE HIS HIS VAL GLN                          
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    GAL  G   3      11                                                       
HET    NAG  B 401      14                                                       
HET    NAG  C 401      14                                                       
HET    NAG  C 402      14                                                       
HET    NAG  C 403      14                                                       
HET    NAG  E 201      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     GAL BETA-D-GALACTOPYRANOSE                                           
FORMUL   7  NAG    7(C8 H15 N O6)                                               
FORMUL   7  GAL    C6 H12 O6                                                    
HELIX    1 AA1 ASP A   65  SER A   70  1                                   6    
HELIX    2 AA2 ASP B   59  HIS B   64  1                                   6    
HELIX    3 AA3 ASP B  103  LEU B  109  5                                   7    
HELIX    4 AA4 THR B  193  SER B  199  1                                   7    
HELIX    5 AA5 ASP C   59  HIS C   64  1                                   6    
HELIX    6 AA6 ASP C  103  LEU C  109  5                                   7    
HELIX    7 AA7 HIS C  187  VAL C  192  1                                   6    
HELIX    8 AA8 THR C  193  SER C  199  1                                   7    
HELIX    9 AA9 ASP D   65  SER D   70  1                                   6    
HELIX   10 AB1 ASN E   73  SER E   78  1                                   6    
SHEET    1 AA1 8 ARG A  84  TYR A  85  0                                        
SHEET    2 AA1 8 ASN A 111  ARG A 124 -1  O  LEU A 122   N  TYR A  85           
SHEET    3 AA1 8 SER A 132  VAL A 147 -1  O  GLU A 136   N  VAL A 121           
SHEET    4 AA1 8 SER F  54  ASN F  63  1  O  LYS F  56   N  PHE A 133           
SHEET    5 AA1 8 VAL A  45  HIS A  52 -1  N  VAL A  45   O  LEU F  57           
SHEET    6 AA1 8 VAL F 139  VAL F 155  1  O  LYS F 145   N  HIS A  52           
SHEET    7 AA1 8 GLU F 114  HIS F 134 -1  N  THR F 127   O  VAL F 146           
SHEET    8 AA1 8 ARG F  92  TYR F  93 -1  N  TYR F  93   O  VAL F 130           
SHEET    1 AA2 8 ARG A  84  TYR A  85  0                                        
SHEET    2 AA2 8 ASN A 111  ARG A 124 -1  O  LEU A 122   N  TYR A  85           
SHEET    3 AA2 8 SER A 132  VAL A 147 -1  O  GLU A 136   N  VAL A 121           
SHEET    4 AA2 8 SER F  54  ASN F  63  1  O  LYS F  56   N  PHE A 133           
SHEET    5 AA2 8 VAL A  45  HIS A  52 -1  N  VAL A  45   O  LEU F  57           
SHEET    6 AA2 8 VAL F 139  VAL F 155  1  O  LYS F 145   N  HIS A  52           
SHEET    7 AA2 8 GLU F 114  HIS F 134 -1  N  THR F 127   O  VAL F 146           
SHEET    8 AA2 8 GLY F 106  ILE F 108 -1  N  CYS F 107   O  ASP F 115           
SHEET    1 AA3 2 TRP A  74  GLU A  80  0                                        
SHEET    2 AA3 2 VAL A  88  CYS A  94 -1  O  LYS A  93   N  ASN A  75           
SHEET    1 AA4 2 CYS A  99  ILE A 100  0                                        
SHEET    2 AA4 2 VAL A 106  ASP A 107 -1  O  ASP A 107   N  CYS A  99           
SHEET    1 AA5 5 VAL A 151  HIS A 152  0                                        
SHEET    2 AA5 5 ARG B 296  VAL B 301  1  O  ARG B 296   N  HIS A 152           
SHEET    3 AA5 5 HIS B 279  PRO B 285 -1  N  VAL B 281   O  ALA B 299           
SHEET    4 AA5 5 TYR B 230  SER B 236 -1  N  GLN B 231   O  GLN B 284           
SHEET    5 AA5 5 PHE B 246  ILE B 252 -1  O  HIS B 250   N  ILE B 232           
SHEET    1 AA6 4 ARG B  34  LEU B  35  0                                        
SHEET    2 AA6 4 ARG B 143  VAL B 150 -1  O  VAL B 150   N  ARG B  34           
SHEET    3 AA6 4 LEU B  90  THR B  99 -1  N  TRP B  98   O  PHE B 144           
SHEET    4 AA6 4 LYS B  74  HIS B  84 -1  N  LYS B  74   O  THR B  99           
SHEET    1 AA7 5 CYS B  50  SER B  55  0                                        
SHEET    2 AA7 5 ARG B 124  PHE B 131 -1  O  GLU B 130   N  THR B  51           
SHEET    3 AA7 5 GLY B 111  GLN B 118 -1  N  LEU B 114   O  VAL B 127           
SHEET    4 AA7 5 GLN B 155  LEU B 164 -1  O  HIS B 162   N  GLU B 113           
SHEET    5 AA7 5 HIS B 175  VAL B 182 -1  O  GLN B 176   N  VAL B 161           
SHEET    1 AA8 3 THR B 208  LEU B 212  0                                        
SHEET    2 AA8 3 GLN B 216  PHE B 221 -1  O  SER B 220   N  THR B 208           
SHEET    3 AA8 3 SER B 264  THR B 269 -1  O  LEU B 268   N  LEU B 217           
SHEET    1 AA9 4 ARG C  34  LEU C  35  0                                        
SHEET    2 AA9 4 ARG C 143  VAL C 150 -1  O  VAL C 150   N  ARG C  34           
SHEET    3 AA9 4 LEU C  90  THR C  99 -1  N  TRP C  98   O  PHE C 144           
SHEET    4 AA9 4 LYS C  74  HIS C  84 -1  N  LYS C  74   O  THR C  99           
SHEET    1 AB1 5 CYS C  50  SER C  55  0                                        
SHEET    2 AB1 5 ARG C 124  PHE C 131 -1  O  GLU C 130   N  THR C  51           
SHEET    3 AB1 5 GLY C 111  GLN C 118 -1  N  LEU C 114   O  VAL C 127           
SHEET    4 AB1 5 GLN C 155  LEU C 164 -1  O  HIS C 162   N  GLU C 113           
SHEET    5 AB1 5 HIS C 175  VAL C 182 -1  O  GLN C 176   N  VAL C 161           
SHEET    1 AB2 3 THR C 208  LEU C 212  0                                        
SHEET    2 AB2 3 GLN C 216  PHE C 221 -1  O  SER C 220   N  THR C 208           
SHEET    3 AB2 3 SER C 264  THR C 269 -1  O  LEU C 268   N  LEU C 217           
SHEET    1 AB3 5 PHE C 246  ILE C 252  0                                        
SHEET    2 AB3 5 TYR C 230  SER C 236 -1  N  ILE C 232   O  HIS C 250           
SHEET    3 AB3 5 HIS C 279  PRO C 285 -1  O  GLN C 284   N  GLN C 231           
SHEET    4 AB3 5 ARG C 296  VAL C 301 -1  O  ALA C 299   N  VAL C 281           
SHEET    5 AB3 5 VAL D 151  HIS D 153  1  O  HIS D 152   N  ARG C 296           
SHEET    1 AB4 5 THR D  44  ASN D  48  0                                        
SHEET    2 AB4 5 SER E  54  ASN E  63 -1  O  MET E  55   N  VAL D  47           
SHEET    3 AB4 5 SER D 132  VAL D 147  1  N  PHE D 133   O  LYS E  56           
SHEET    4 AB4 5 ASN D 111  ARG D 124 -1  N  VAL D 121   O  GLU D 136           
SHEET    5 AB4 5 ARG D  84  TYR D  85 -1  N  TYR D  85   O  LEU D 122           
SHEET    1 AB5 4 HIS D  52  ASN D  53  0                                        
SHEET    2 AB5 4 VAL E 139  VAL E 155  1  O  LYS E 145   N  HIS D  52           
SHEET    3 AB5 4 GLU E 114  HIS E 134 -1  N  THR E 127   O  VAL E 146           
SHEET    4 AB5 4 ARG E  92  TYR E  93 -1  N  TYR E  93   O  VAL E 130           
SHEET    1 AB6 4 HIS D  52  ASN D  53  0                                        
SHEET    2 AB6 4 VAL E 139  VAL E 155  1  O  LYS E 145   N  HIS D  52           
SHEET    3 AB6 4 GLU E 114  HIS E 134 -1  N  THR E 127   O  VAL E 146           
SHEET    4 AB6 4 GLY E 106  ILE E 108 -1  N  CYS E 107   O  ASP E 115           
SHEET    1 AB7 2 TRP D  74  GLU D  80  0                                        
SHEET    2 AB7 2 VAL D  88  CYS D  94 -1  O  LYS D  93   N  ASN D  75           
SHEET    1 AB8 2 CYS D  99  ILE D 100  0                                        
SHEET    2 AB8 2 VAL D 106  ASP D 107 -1  O  ASP D 107   N  CYS D  99           
SHEET    1 AB9 2 TRP E  82  TRP E  88  0                                        
SHEET    2 AB9 2 GLU E  96  CYS E 102 -1  O  GLN E  99   N  THR E  85           
SHEET    1 AC1 2 TRP F  82  TRP F  88  0                                        
SHEET    2 AC1 2 GLU F  96  CYS F 102 -1  O  GLN F  99   N  THR F  85           
SSBOND   1 CYS A   94    CYS A  144                          1555   1555  2.06  
SSBOND   2 CYS A   99    CYS A  146                          1555   1555  2.04  
SSBOND   3 CYS A  129    CYS F   47                          1555   1555  2.03  
SSBOND   4 CYS B   43    CYS B   50                          1555   1555  2.03  
SSBOND   5 CYS B   57    CYS B  126                          1555   1555  2.05  
SSBOND   6 CYS B  185    CYS B  196                          1555   1555  2.04  
SSBOND   7 CYS B  245    CYS B  276                          1555   1555  2.04  
SSBOND   8 CYS B  277    CYS B  303                          1555   1555  2.05  
SSBOND   9 CYS B  290    CYS B  294                          1555   1555  2.05  
SSBOND  10 CYS C   43    CYS C   50                          1555   1555  2.05  
SSBOND  11 CYS C   57    CYS C  126                          1555   1555  2.05  
SSBOND  12 CYS C  185    CYS C  196                          1555   1555  2.04  
SSBOND  13 CYS C  245    CYS C  276                          1555   1555  2.04  
SSBOND  14 CYS C  277    CYS C  303                          1555   1555  2.04  
SSBOND  15 CYS C  290    CYS C  294                          1555   1555  2.06  
SSBOND  16 CYS D   94    CYS D  144                          1555   1555  2.06  
SSBOND  17 CYS D   99    CYS D  146                          1555   1555  2.03  
SSBOND  18 CYS D  129    CYS E   47                          1555   1555  2.05  
SSBOND  19 CYS E  102    CYS E  152                          1555   1555  2.05  
SSBOND  20 CYS E  107    CYS E  154                          1555   1555  2.03  
SSBOND  21 CYS F  102    CYS F  152                          1555   1555  2.05  
SSBOND  22 CYS F  107    CYS F  154                          1555   1555  2.03  
LINK         ND2 ASN B 225                 C1  NAG B 401     1555   1555  1.43  
LINK         ND2 ASN C  54                 C1  NAG C 401     1555   1555  1.44  
LINK         ND2 ASN C 225                 C1  NAG C 402     1555   1555  1.43  
LINK         ND2 ASN C 265                 C1  NAG C 403     1555   1555  1.44  
LINK         ND2 ASN E  83                 C1  NAG E 201     1555   1555  1.44  
LINK         ND2 ASN F  83                 C1  NAG G   1     1555   1555  1.43  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.42  
LINK         O6  NAG G   1                 C1  GAL G   3     1555   1555  1.42  
CISPEP   1 TYR A   85    PRO A   86          0        -4.26                     
CISPEP   2 GLU A  125    PRO A  126          0         1.94                     
CISPEP   3 LEU B  164    PRO B  165          0         0.88                     
CISPEP   4 LEU C  164    PRO C  165          0         0.02                     
CISPEP   5 TYR D   85    PRO D   86          0        -4.51                     
CISPEP   6 GLU D  125    PRO D  126          0         1.97                     
CISPEP   7 TYR E   93    PRO E   94          0        -0.04                     
CISPEP   8 TYR F   93    PRO F   94          0        -0.81                     
CRYST1  100.002   66.103  104.119  90.00  90.13  90.00 P 1 2 1       4          
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      0.010000  0.000000  0.000023        0.00000                         
SCALE2      0.000000  0.015128  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009604        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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