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Database: PDB
Entry: 4HSA
LinkDB: 4HSA
Original site: 4HSA 
HEADER    IMMUNE SYSTEM/PROTEIN BINDING           29-OCT-12   4HSA              
TITLE     STRUCTURE OF INTERLEUKIN 17A IN COMPLEX WITH IL17RA RECEPTOR          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-17A;                                           
COMPND   3 CHAIN: A, B, D, E;                                                   
COMPND   4 SYNONYM: IL-17, IL-17A, CYTOTOXIC T-LYMPHOCYTE-ASSOCIATED ANTIGEN 8, 
COMPND   5 CTLA-8;                                                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTERLEUKIN-17 RECEPTOR A;                                 
COMPND  10 CHAIN: C, F;                                                         
COMPND  11 SYNONYM: IL-17 RECEPTOR A, IL-17RA, CDW217;                          
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MUTATION: 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_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_COMMON: HUMAN;                                              
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 GENE: IL17RA, IL17R;                                                 
SOURCE  15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    CYTOKINE RECEPTOR, GLYCOSYLATION, IMMUNE SYSTEM-PROTEIN BINDING       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LIU                                                                 
REVDAT   4   29-JUL-20 4HSA    1       COMPND REMARK SEQADV HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   19-JUN-13 4HSA    1       JRNL                                     
REVDAT   2   05-JUN-13 4HSA    1       JRNL                                     
REVDAT   1   22-MAY-13 4HSA    0                                                
JRNL        AUTH   S.LIU,X.SONG,B.A.CHRUNYK,S.SHANKER,L.R.HOTH,E.S.MARR,        
JRNL        AUTH 2 M.C.GRIFFOR                                                  
JRNL        TITL   CRYSTAL STRUCTURES OF INTERLEUKIN 17A AND ITS COMPLEX WITH   
JRNL        TITL 2 IL-17 RECEPTOR A.                                            
JRNL        REF    NAT COMMUN                    V.   4  1888 2013              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   23695682                                                     
JRNL        DOI    10.1038/NCOMMS2880                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.15 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.2                                        
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) : 3.15                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 32406                          
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)  : 0.187                          
REMARK   3   FREE R VALUE                      : 0.232                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.070                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1774                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 18                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.15                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.24                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.94                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2816                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2366                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2662                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2323                   
REMARK   3   BIN FREE R VALUE                        : 0.3115                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.47                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 154                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7830                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 196                                     
REMARK   3   SOLVENT ATOMS            : 5                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 97.66                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 106.3                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -11.27640                                            
REMARK   3    B22 (A**2) : -11.27640                                            
REMARK   3    B33 (A**2) : 22.55270                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.674               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
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      : 0.921                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.888                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8289   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11345  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2842   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 201    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1186   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8289   ; 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   : 1125   ; 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   : 8885   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.31                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.19                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 24.00                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: A 17 A 131                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -58.3734   42.9358  -33.2586           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3285 T22:   -0.0678                                    
REMARK   3     T33:   -0.3920 T12:   -0.1260                                    
REMARK   3     T13:   -0.0210 T23:    0.0041                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8096 L22:    2.6276                                    
REMARK   3     L33:    4.0812 L12:    0.1365                                    
REMARK   3     L13:   -0.5991 L23:    1.1713                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2538 S12:   -0.0419 S13:   -0.3603                     
REMARK   3     S21:    0.3029 S22:   -0.1844 S23:    0.2801                     
REMARK   3     S31:    0.5105 S32:   -0.3158 S33:   -0.0694                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: B 19 B 127                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -52.9465   52.3940  -35.6823           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4174 T22:   -0.0732                                    
REMARK   3     T33:   -0.4290 T12:    0.0068                                    
REMARK   3     T13:    0.0675 T23:    0.0155                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5627 L22:    3.4587                                    
REMARK   3     L33:    5.1166 L12:    1.0102                                    
REMARK   3     L13:    1.0226 L23:    2.0587                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3121 S12:    0.1821 S13:   -0.0394                     
REMARK   3     S21:   -0.1338 S22:   -0.1596 S23:    0.1450                     
REMARK   3     S31:   -0.1462 S32:   -0.3417 S33:   -0.1525                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: C 2 C 273                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -36.2146   42.0479  -34.7152           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.5408 T22:   -0.2621                                    
REMARK   3     T33:   -0.5712 T12:    0.1002                                    
REMARK   3     T13:   -0.1562 T23:   -0.0530                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.1056 L22:    3.1603                                    
REMARK   3     L33:    2.6969 L12:    0.7928                                    
REMARK   3     L13:    0.6193 L23:    1.5409                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3565 S12:    0.0243 S13:   -0.4265                     
REMARK   3     S21:    0.4523 S22:    0.0003 S23:   -0.4526                     
REMARK   3     S31:    0.5770 S32:    0.3635 S33:   -0.3568                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: D 20 D 131                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -80.7792   58.7090  -64.8682           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3121 T22:    0.1584                                    
REMARK   3     T33:    0.1288 T12:    0.0504                                    
REMARK   3     T13:    0.0528 T23:    0.1652                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.0365 L22:    3.2158                                    
REMARK   3     L33:    7.4173 L12:    0.4268                                    
REMARK   3     L13:   -0.0829 L23:    0.2785                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0946 S12:   -0.3019 S13:    0.0430                     
REMARK   3     S21:    0.1284 S22:    0.1583 S23:    0.7358                     
REMARK   3     S31:    0.0695 S32:   -1.1046 S33:   -0.0637                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: E 19 E 127                                             
REMARK   3    ORIGIN FOR THE GROUP (A):  -70.4000   58.3355  -68.9809           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3554 T22:   -0.1332                                    
REMARK   3     T33:   -0.0691 T12:    0.0102                                    
REMARK   3     T13:   -0.0124 T23:    0.0563                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.7884 L22:    2.3805                                    
REMARK   3     L33:    7.3898 L12:   -0.1431                                    
REMARK   3     L13:   -0.5004 L23:   -0.5475                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1568 S12:   -0.1552 S13:    0.1213                     
REMARK   3     S21:    0.0139 S22:    0.3376 S23:    0.2509                     
REMARK   3     S31:    0.1031 S32:   -0.1988 S33:   -0.4944                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: F 2 F 272                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -70.2374   78.0096  -68.0738           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.4365 T22:   -0.7139                                    
REMARK   3     T33:   -0.3677 T12:    0.1540                                    
REMARK   3     T13:    0.1656 T23:    0.0422                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.5155 L22:    1.6543                                    
REMARK   3     L33:    5.1270 L12:    0.1594                                    
REMARK   3     L13:   -1.4875 L23:   -0.6678                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.3642 S12:   -0.1461 S13:    0.9642                     
REMARK   3     S21:    0.3903 S22:    0.2907 S23:    0.4405                     
REMARK   3     S31:   -1.2441 S32:   -0.3766 S33:   -0.6549                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HSA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000075857.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34990                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.150                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.7                               
REMARK 200  DATA REDUNDANCY                : 14.60                              
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                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.83                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       59.69667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      119.39333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      119.39333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       59.69667            
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11520 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 24560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 1.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, H, I                      
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10570 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 23840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F, J                            
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     PRO A    11                                                      
REMARK 465     ASN A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     ARG A    31                                                      
REMARK 465     ASN A    32                                                      
REMARK 465     THR A    33                                                      
REMARK 465     ASN A    34                                                      
REMARK 465     THR A    35                                                      
REMARK 465     ASN A    36                                                      
REMARK 465     PRO A    37                                                      
REMARK 465     LYS A    38                                                      
REMARK 465     ARG A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     ALA A   132                                                      
REMARK 465     PRO B    11                                                      
REMARK 465     ASN B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     ASP B    15                                                      
REMARK 465     LYS B    16                                                      
REMARK 465     ASN B    17                                                      
REMARK 465     PHE B    18                                                      
REMARK 465     VAL B   128                                                      
REMARK 465     HIS B   129                                                      
REMARK 465     HIS B   130                                                      
REMARK 465     VAL B   131                                                      
REMARK 465     ALA B   132                                                      
REMARK 465     SER C     1                                                      
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 465     LEU C   287                                                      
REMARK 465     VAL C   288                                                      
REMARK 465     PRO C   289                                                      
REMARK 465     ARG C   290                                                      
REMARK 465     GLY C   291                                                      
REMARK 465     SER C   292                                                      
REMARK 465     ASP C   293                                                      
REMARK 465     TYR C   294                                                      
REMARK 465     LYS C   295                                                      
REMARK 465     ASP C   296                                                      
REMARK 465     ASP C   297                                                      
REMARK 465     ASP C   298                                                      
REMARK 465     ASP C   299                                                      
REMARK 465     LYS C   300                                                      
REMARK 465     GLY C   301                                                      
REMARK 465     PRO D    11                                                      
REMARK 465     ASN D    12                                                      
REMARK 465     SER D    13                                                      
REMARK 465     GLU D    14                                                      
REMARK 465     ASP D    15                                                      
REMARK 465     LYS D    16                                                      
REMARK 465     ASN D    17                                                      
REMARK 465     PHE D    18                                                      
REMARK 465     PRO D    19                                                      
REMARK 465     ASN D    30                                                      
REMARK 465     ARG D    31                                                      
REMARK 465     ASN D    32                                                      
REMARK 465     THR D    33                                                      
REMARK 465     ASN D    34                                                      
REMARK 465     THR D    35                                                      
REMARK 465     ASN D    36                                                      
REMARK 465     PRO D    37                                                      
REMARK 465     LYS D    38                                                      
REMARK 465     ARG D    39                                                      
REMARK 465     SER D    40                                                      
REMARK 465     SER D    41                                                      
REMARK 465     ALA D   132                                                      
REMARK 465     PRO E    11                                                      
REMARK 465     ASN E    12                                                      
REMARK 465     SER E    13                                                      
REMARK 465     GLU E    14                                                      
REMARK 465     ASP E    15                                                      
REMARK 465     LYS E    16                                                      
REMARK 465     ASN E    17                                                      
REMARK 465     PHE E    18                                                      
REMARK 465     VAL E   128                                                      
REMARK 465     HIS E   129                                                      
REMARK 465     HIS E   130                                                      
REMARK 465     VAL E   131                                                      
REMARK 465     ALA E   132                                                      
REMARK 465     SER F     1                                                      
REMARK 465     PRO F   273                                                      
REMARK 465     GLU F   274                                                      
REMARK 465     MET F   275                                                      
REMARK 465     PRO F   276                                                      
REMARK 465     ASP F   277                                                      
REMARK 465     THR F   278                                                      
REMARK 465     PRO F   279                                                      
REMARK 465     GLU F   280                                                      
REMARK 465     PRO F   281                                                      
REMARK 465     ILE F   282                                                      
REMARK 465     PRO F   283                                                      
REMARK 465     ASP F   284                                                      
REMARK 465     TYR F   285                                                      
REMARK 465     MET F   286                                                      
REMARK 465     LEU F   287                                                      
REMARK 465     VAL F   288                                                      
REMARK 465     PRO F   289                                                      
REMARK 465     ARG F   290                                                      
REMARK 465     GLY F   291                                                      
REMARK 465     SER F   292                                                      
REMARK 465     ASP F   293                                                      
REMARK 465     TYR F   294                                                      
REMARK 465     LYS F   295                                                      
REMARK 465     ASP F   296                                                      
REMARK 465     ASP F   297                                                      
REMARK 465     ASP F   298                                                      
REMARK 465     ASP F   299                                                      
REMARK 465     LYS F   300                                                      
REMARK 465     GLY F   301                                                      
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     ASP C  29    CG   OD1  OD2                                       
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     ASP F  29    CG   OD1  OD2                                       
REMARK 470     LEU F 101    CG   CD1  CD2                                       
REMARK 470     VAL F 178    CG1  CG2                                            
REMARK 470     SER F 189    OG                                                  
REMARK 470     GLN F 231    CG   CD   OE1  NE2                                  
REMARK 470     LYS F 243    CG   CD   CE   NZ                                   
REMARK 470     SER F 267    OG                                                  
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    PRO E 103   CA  -  C   -  N   ANGL. DEV. =  16.8 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  42     -152.90   -171.14                                   
REMARK 500    TYR A  43      -45.16     70.55                                   
REMARK 500    SER A  49       73.60   -111.44                                   
REMARK 500    HIS A 105       -6.00     77.22                                   
REMARK 500    SER B  40      140.14     56.73                                   
REMARK 500    SER B  49       69.31   -111.77                                   
REMARK 500    PRO B 103     -102.63      7.10                                   
REMARK 500    HIS B 105      147.42    141.39                                   
REMARK 500    SER B 106       78.33     60.75                                   
REMARK 500    ASN C  91       47.31    -95.48                                   
REMARK 500    ALA C 183       86.29     51.25                                   
REMARK 500    HIS C 184       46.20     36.62                                   
REMARK 500    SER C 196       49.84    -86.04                                   
REMARK 500    ASN C 211       40.45    -91.94                                   
REMARK 500    HIS C 230       -3.27     64.98                                   
REMARK 500    LEU C 242      103.21   -164.25                                   
REMARK 500    LEU C 260     -115.24     57.03                                   
REMARK 500    ASP C 262       34.03    -86.46                                   
REMARK 500    SER C 271     -151.00    -86.20                                   
REMARK 500    CYS C 272      -77.32   -133.59                                   
REMARK 500    SER D  49       70.30   -115.01                                   
REMARK 500    SER E  40      128.13     42.82                                   
REMARK 500    PRO E 103      -99.48     10.43                                   
REMARK 500    HIS E 105      129.16    160.40                                   
REMARK 500    SER E 106      154.34     71.16                                   
REMARK 500    ASN E 108     -157.89    -99.72                                   
REMARK 500    ASN F  91       47.11    -95.88                                   
REMARK 500    ALA F 183       86.09     51.67                                   
REMARK 500    HIS F 184       46.14     36.43                                   
REMARK 500    ASN F 211       36.13    -89.12                                   
REMARK 500    HIS F 230       -3.16     65.50                                   
REMARK 500    LEU F 260     -116.79     63.03                                   
REMARK 500    ASP F 262       34.00    -84.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4HR9   RELATED DB: PDB                                   
REMARK 900 UNBOUND IL17A                                                        
DBREF  4HSA A   11   132  UNP    Q16552   IL17_HUMAN      34    155             
DBREF  4HSA B   11   132  UNP    Q16552   IL17_HUMAN      34    155             
DBREF  4HSA C    1   286  UNP    Q96F46   I17RA_HUMAN     32    317             
DBREF  4HSA D   11   132  UNP    Q16552   IL17_HUMAN      34    155             
DBREF  4HSA E   11   132  UNP    Q16552   IL17_HUMAN      34    155             
DBREF  4HSA F    1   286  UNP    Q96F46   I17RA_HUMAN     32    317             
SEQADV 4HSA ASP A   45  UNP  Q16552    ASN    68 ENGINEERED MUTATION            
SEQADV 4HSA SER A  106  UNP  Q16552    CYS   129 ENGINEERED MUTATION            
SEQADV 4HSA ASP B   45  UNP  Q16552    ASN    68 ENGINEERED MUTATION            
SEQADV 4HSA SER B  106  UNP  Q16552    CYS   129 ENGINEERED MUTATION            
SEQADV 4HSA ASP C  175  UNP  Q96F46    ASN   206 ENGINEERED MUTATION            
SEQADV 4HSA ASP C  234  UNP  Q96F46    ASN   265 ENGINEERED MUTATION            
SEQADV 4HSA LEU C  287  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA VAL C  288  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA PRO C  289  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ARG C  290  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA GLY C  291  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA SER C  292  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP C  293  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA TYR C  294  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA LYS C  295  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP C  296  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP C  297  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP C  298  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP C  299  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA LYS C  300  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA GLY C  301  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP D   45  UNP  Q16552    ASN    68 ENGINEERED MUTATION            
SEQADV 4HSA SER D  106  UNP  Q16552    CYS   129 ENGINEERED MUTATION            
SEQADV 4HSA ASP E   45  UNP  Q16552    ASN    68 ENGINEERED MUTATION            
SEQADV 4HSA SER E  106  UNP  Q16552    CYS   129 ENGINEERED MUTATION            
SEQADV 4HSA ASP F  175  UNP  Q96F46    ASN   206 ENGINEERED MUTATION            
SEQADV 4HSA ASP F  234  UNP  Q96F46    ASN   265 ENGINEERED MUTATION            
SEQADV 4HSA LEU F  287  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA VAL F  288  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA PRO F  289  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ARG F  290  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA GLY F  291  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA SER F  292  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP F  293  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA TYR F  294  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA LYS F  295  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP F  296  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP F  297  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP F  298  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA ASP F  299  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA LYS F  300  UNP  Q96F46              EXPRESSION TAG                 
SEQADV 4HSA GLY F  301  UNP  Q96F46              EXPRESSION TAG                 
SEQRES   1 A  122  PRO ASN SER GLU ASP LYS ASN PHE PRO ARG THR VAL MET          
SEQRES   2 A  122  VAL ASN LEU ASN ILE HIS ASN ARG ASN THR ASN THR ASN          
SEQRES   3 A  122  PRO LYS ARG SER SER ASP TYR TYR ASP ARG SER THR SER          
SEQRES   4 A  122  PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR          
SEQRES   5 A  122  PRO SER VAL ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY          
SEQRES   6 A  122  CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR HIS MET ASN          
SEQRES   7 A  122  SER VAL PRO ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG          
SEQRES   8 A  122  GLU PRO PRO HIS SER PRO ASN SER PHE ARG LEU GLU LYS          
SEQRES   9 A  122  ILE LEU VAL SER VAL GLY CYS THR CYS VAL THR PRO ILE          
SEQRES  10 A  122  VAL HIS HIS VAL ALA                                          
SEQRES   1 B  122  PRO ASN SER GLU ASP LYS ASN PHE PRO ARG THR VAL MET          
SEQRES   2 B  122  VAL ASN LEU ASN ILE HIS ASN ARG ASN THR ASN THR ASN          
SEQRES   3 B  122  PRO LYS ARG SER SER ASP TYR TYR ASP ARG SER THR SER          
SEQRES   4 B  122  PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR          
SEQRES   5 B  122  PRO SER VAL ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY          
SEQRES   6 B  122  CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR HIS MET ASN          
SEQRES   7 B  122  SER VAL PRO ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG          
SEQRES   8 B  122  GLU PRO PRO HIS SER PRO ASN SER PHE ARG LEU GLU LYS          
SEQRES   9 B  122  ILE LEU VAL SER VAL GLY CYS THR CYS VAL THR PRO ILE          
SEQRES  10 B  122  VAL HIS HIS VAL ALA                                          
SEQRES   1 C  301  SER LEU ARG LEU LEU ASP HIS ARG ALA LEU VAL CYS SER          
SEQRES   2 C  301  GLN PRO GLY LEU ASN CYS THR VAL LYS ASN SER THR CYS          
SEQRES   3 C  301  LEU ASP ASP SER TRP ILE HIS PRO ARG ASN LEU THR PRO          
SEQRES   4 C  301  SER SER PRO LYS ASP LEU GLN ILE GLN LEU HIS PHE ALA          
SEQRES   5 C  301  HIS THR GLN GLN GLY ASP LEU PHE PRO VAL ALA HIS ILE          
SEQRES   6 C  301  GLU TRP THR LEU GLN THR ASP ALA SER ILE LEU TYR LEU          
SEQRES   7 C  301  GLU GLY ALA GLU LEU SER VAL LEU GLN LEU ASN THR ASN          
SEQRES   8 C  301  GLU ARG LEU CYS VAL ARG PHE GLU PHE LEU SER LYS LEU          
SEQRES   9 C  301  ARG HIS HIS HIS ARG ARG TRP ARG PHE THR PHE SER HIS          
SEQRES  10 C  301  PHE VAL VAL ASP PRO ASP GLN GLU TYR GLU VAL THR VAL          
SEQRES  11 C  301  HIS HIS LEU PRO LYS PRO ILE PRO ASP GLY ASP PRO ASN          
SEQRES  12 C  301  HIS GLN SER LYS ASN PHE LEU VAL PRO ASP CYS GLU HIS          
SEQRES  13 C  301  ALA ARG MET LYS VAL THR THR PRO CYS MET SER SER GLY          
SEQRES  14 C  301  SER LEU TRP ASP PRO ASP ILE THR VAL GLU THR LEU GLU          
SEQRES  15 C  301  ALA HIS GLN LEU ARG VAL SER PHE THR LEU TRP ASN GLU          
SEQRES  16 C  301  SER THR HIS TYR GLN ILE LEU LEU THR SER PHE PRO HIS          
SEQRES  17 C  301  MET GLU ASN HIS SER CYS PHE GLU HIS MET HIS HIS ILE          
SEQRES  18 C  301  PRO ALA PRO ARG PRO GLU GLU PHE HIS GLN ARG SER ASP          
SEQRES  19 C  301  VAL THR LEU THR LEU ARG ASN LEU LYS GLY CYS CYS ARG          
SEQRES  20 C  301  HIS GLN VAL GLN ILE GLN PRO PHE PHE SER SER CYS LEU          
SEQRES  21 C  301  ASN ASP CYS LEU ARG HIS SER ALA THR VAL SER CYS PRO          
SEQRES  22 C  301  GLU MET PRO ASP THR PRO GLU PRO ILE PRO ASP TYR MET          
SEQRES  23 C  301  LEU VAL PRO ARG GLY SER ASP TYR LYS ASP ASP ASP ASP          
SEQRES  24 C  301  LYS GLY                                                      
SEQRES   1 D  122  PRO ASN SER GLU ASP LYS ASN PHE PRO ARG THR VAL MET          
SEQRES   2 D  122  VAL ASN LEU ASN ILE HIS ASN ARG ASN THR ASN THR ASN          
SEQRES   3 D  122  PRO LYS ARG SER SER ASP TYR TYR ASP ARG SER THR SER          
SEQRES   4 D  122  PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR          
SEQRES   5 D  122  PRO SER VAL ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY          
SEQRES   6 D  122  CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR HIS MET ASN          
SEQRES   7 D  122  SER VAL PRO ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG          
SEQRES   8 D  122  GLU PRO PRO HIS SER PRO ASN SER PHE ARG LEU GLU LYS          
SEQRES   9 D  122  ILE LEU VAL SER VAL GLY CYS THR CYS VAL THR PRO ILE          
SEQRES  10 D  122  VAL HIS HIS VAL ALA                                          
SEQRES   1 E  122  PRO ASN SER GLU ASP LYS ASN PHE PRO ARG THR VAL MET          
SEQRES   2 E  122  VAL ASN LEU ASN ILE HIS ASN ARG ASN THR ASN THR ASN          
SEQRES   3 E  122  PRO LYS ARG SER SER ASP TYR TYR ASP ARG SER THR SER          
SEQRES   4 E  122  PRO TRP ASN LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR          
SEQRES   5 E  122  PRO SER VAL ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY          
SEQRES   6 E  122  CYS ILE ASN ALA ASP GLY ASN VAL ASP TYR HIS MET ASN          
SEQRES   7 E  122  SER VAL PRO ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG          
SEQRES   8 E  122  GLU PRO PRO HIS SER PRO ASN SER PHE ARG LEU GLU LYS          
SEQRES   9 E  122  ILE LEU VAL SER VAL GLY CYS THR CYS VAL THR PRO ILE          
SEQRES  10 E  122  VAL HIS HIS VAL ALA                                          
SEQRES   1 F  301  SER LEU ARG LEU LEU ASP HIS ARG ALA LEU VAL CYS SER          
SEQRES   2 F  301  GLN PRO GLY LEU ASN CYS THR VAL LYS ASN SER THR CYS          
SEQRES   3 F  301  LEU ASP ASP SER TRP ILE HIS PRO ARG ASN LEU THR PRO          
SEQRES   4 F  301  SER SER PRO LYS ASP LEU GLN ILE GLN LEU HIS PHE ALA          
SEQRES   5 F  301  HIS THR GLN GLN GLY ASP LEU PHE PRO VAL ALA HIS ILE          
SEQRES   6 F  301  GLU TRP THR LEU GLN THR ASP ALA SER ILE LEU TYR LEU          
SEQRES   7 F  301  GLU GLY ALA GLU LEU SER VAL LEU GLN LEU ASN THR ASN          
SEQRES   8 F  301  GLU ARG LEU CYS VAL ARG PHE GLU PHE LEU SER LYS LEU          
SEQRES   9 F  301  ARG HIS HIS HIS ARG ARG TRP ARG PHE THR PHE SER HIS          
SEQRES  10 F  301  PHE VAL VAL ASP PRO ASP GLN GLU TYR GLU VAL THR VAL          
SEQRES  11 F  301  HIS HIS LEU PRO LYS PRO ILE PRO ASP GLY ASP PRO ASN          
SEQRES  12 F  301  HIS GLN SER LYS ASN PHE LEU VAL PRO ASP CYS GLU HIS          
SEQRES  13 F  301  ALA ARG MET LYS VAL THR THR PRO CYS MET SER SER GLY          
SEQRES  14 F  301  SER LEU TRP ASP PRO ASP ILE THR VAL GLU THR LEU GLU          
SEQRES  15 F  301  ALA HIS GLN LEU ARG VAL SER PHE THR LEU TRP ASN GLU          
SEQRES  16 F  301  SER THR HIS TYR GLN ILE LEU LEU THR SER PHE PRO HIS          
SEQRES  17 F  301  MET GLU ASN HIS SER CYS PHE GLU HIS MET HIS HIS ILE          
SEQRES  18 F  301  PRO ALA PRO ARG PRO GLU GLU PHE HIS GLN ARG SER ASP          
SEQRES  19 F  301  VAL THR LEU THR LEU ARG ASN LEU LYS GLY CYS CYS ARG          
SEQRES  20 F  301  HIS GLN VAL GLN ILE GLN PRO PHE PHE SER SER CYS LEU          
SEQRES  21 F  301  ASN ASP CYS LEU ARG HIS SER ALA THR VAL SER CYS PRO          
SEQRES  22 F  301  GLU MET PRO ASP THR PRO GLU PRO ILE PRO ASP TYR MET          
SEQRES  23 F  301  LEU VAL PRO ARG GLY SER ASP TYR LYS ASP ASP ASP ASP          
SEQRES  24 F  301  LYS GLY                                                      
MODRES 4HSA ASN F   23  ASN  GLYCOSYLATION SITE                                 
MODRES 4HSA ASN C  194  ASN  GLYCOSYLATION SITE                                 
MODRES 4HSA ASN F  194  ASN  GLYCOSYLATION SITE                                 
MODRES 4HSA ASN C   23  ASN  GLYCOSYLATION SITE                                 
MODRES 4HSA ASN C   18  ASN  GLYCOSYLATION SITE                                 
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    MAN  G   3      11                                                       
HET    MAN  G   4      11                                                       
HET    FUC  G   5      10                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    FUC  H   3      10                                                       
HET    NAG  I   1      14                                                       
HET    FUC  I   2      10                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    MAN  J   3      11                                                       
HET    MAN  J   4      11                                                       
HET    FUC  J   5      10                                                       
HET    NAG  F 606      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
FORMUL   7  NAG    8(C8 H15 N O6)                                               
FORMUL   7  MAN    4(C6 H12 O6)                                                 
FORMUL   7  FUC    4(C6 H12 O5)                                                 
FORMUL  12  HOH   *5(H2 O)                                                      
HELIX    1   1 ASP C   28  HIS C   33  1                                   6    
HELIX    2   2 ASP C   72  LEU C   78  5                                   7    
HELIX    3   3 ARG C  158  VAL C  161  5                                   4    
HELIX    4   4 THR C  162  SER C  168  1                                   7    
HELIX    5   5 ARG C  225  PHE C  229  5                                   5    
HELIX    6   6 CYS C  259  CYS C  263  5                                   5    
HELIX    7   7 TYR D   43  SER D   47  1                                   5    
HELIX    8   8 ASP F   28  HIS F   33  1                                   6    
HELIX    9   9 ASP F   72  LEU F   78  5                                   7    
HELIX   10  10 ARG F  158  VAL F  161  5                                   4    
HELIX   11  11 THR F  162  SER F  167  1                                   6    
HELIX   12  12 ARG F  225  PHE F  229  5                                   5    
HELIX   13  13 CYS F  259  CYS F  263  5                                   5    
SHEET    1   A 8 ARG A  61  TYR A  62  0                                        
SHEET    2   A 8 ASN A  88  ARG A 101 -1  O  LEU A  99   N  TYR A  62           
SHEET    3   A 8 SER A 109  VAL A 124 -1  O  GLY A 120   N  ILE A  92           
SHEET    4   A 8 THR B  21  ASN B  30  1  O  HIS B  29   N  LEU A 112           
SHEET    5   A 8 THR A  21  LEU A  26 -1  N  VAL A  24   O  VAL B  22           
SHEET    6   A 8 PHE B 110  VAL B 124  1  O  PHE B 110   N  ASN A  25           
SHEET    7   A 8 ASN B  88  ARG B 101 -1  N  ILE B  96   O  ILE B 115           
SHEET    8   A 8 ARG B  61  TYR B  62 -1  N  TYR B  62   O  LEU B  99           
SHEET    1   B 2 TRP A  51  GLU A  57  0                                        
SHEET    2   B 2 VAL A  65  CYS A  71 -1  O  GLU A  68   N  HIS A  54           
SHEET    1   C 2 CYS A  76  ILE A  77  0                                        
SHEET    2   C 2 VAL A  83  ASP A  84 -1  O  ASP A  84   N  CYS A  76           
SHEET    1   D 5 VAL A 128  HIS A 130  0                                        
SHEET    2   D 5 ARG C 265  VAL C 270  1  O  SER C 267   N  HIS A 129           
SHEET    3   D 5 CYS C 245  PRO C 254 -1  N  VAL C 250   O  ALA C 268           
SHEET    4   D 5 TYR C 199  PRO C 207 -1  N  LEU C 202   O  GLN C 251           
SHEET    5   D 5 PHE C 215  ILE C 221 -1  O  PHE C 215   N  SER C 205           
SHEET    1   E 2 TRP B  51  GLU B  57  0                                        
SHEET    2   E 2 VAL B  65  CYS B  71 -1  O  GLU B  68   N  HIS B  54           
SHEET    1   F 2 CYS B  76  ILE B  77  0                                        
SHEET    2   F 2 VAL B  83  ASP B  84 -1  O  ASP B  84   N  CYS B  76           
SHEET    1   G 4 ARG C   3  LEU C   4  0                                        
SHEET    2   G 4 ARG C 112  VAL C 119 -1  O  VAL C 119   N  ARG C   3           
SHEET    3   G 4 LEU C  59  LEU C  69 -1  N  TRP C  67   O  PHE C 113           
SHEET    4   G 4 PRO C  42  HIS C  53 -1  N  LYS C  43   O  THR C  68           
SHEET    1   H 5 CYS C  19  SER C  24  0                                        
SHEET    2   H 5 ARG C  93  PHE C 100 -1  O  ARG C  97   N  LYS C  22           
SHEET    3   H 5 GLY C  80  GLN C  87 -1  N  ALA C  81   O  PHE C  98           
SHEET    4   H 5 GLN C 124  LEU C 133 -1  O  THR C 129   N  SER C  84           
SHEET    5   H 5 HIS C 144  VAL C 151 -1  O  PHE C 149   N  TYR C 126           
SHEET    1   I 3 THR C 177  LEU C 181  0                                        
SHEET    2   I 3 GLN C 185  SER C 189 -1  O  ARG C 187   N  GLU C 179           
SHEET    3   I 3 VAL C 235  THR C 238 -1  O  LEU C 237   N  LEU C 186           
SHEET    1   J 8 ARG D  61  TYR D  62  0                                        
SHEET    2   J 8 ASN D  88  ARG D 101 -1  O  LEU D  99   N  TYR D  62           
SHEET    3   J 8 SER D 109  VAL D 124 -1  O  THR D 122   N  VAL D  90           
SHEET    4   J 8 THR E  21  ASN E  30  1  O  MET E  23   N  PHE D 110           
SHEET    5   J 8 THR D  21  ASN D  25 -1  N  VAL D  24   O  VAL E  22           
SHEET    6   J 8 PHE E 110  VAL E 124  1  O  LEU E 112   N  ASN D  25           
SHEET    7   J 8 ASN E  88  ARG E 101 -1  N  VAL E  90   O  THR E 122           
SHEET    8   J 8 ARG E  61  TYR E  62 -1  N  TYR E  62   O  LEU E  99           
SHEET    1   K 2 TRP D  51  GLU D  57  0                                        
SHEET    2   K 2 VAL D  65  CYS D  71 -1  O  GLU D  68   N  HIS D  54           
SHEET    1   L 2 CYS D  76  ILE D  77  0                                        
SHEET    2   L 2 VAL D  83  ASP D  84 -1  O  ASP D  84   N  CYS D  76           
SHEET    1   M 5 VAL D 128  HIS D 130  0                                        
SHEET    2   M 5 ARG F 265  VAL F 270  1  O  SER F 267   N  HIS D 129           
SHEET    3   M 5 CYS F 245  PRO F 254 -1  N  VAL F 250   O  ALA F 268           
SHEET    4   M 5 TYR F 199  PRO F 207 -1  N  THR F 204   O  GLN F 249           
SHEET    5   M 5 PHE F 215  ILE F 221 -1  O  PHE F 215   N  SER F 205           
SHEET    1   N 2 TRP E  51  GLU E  57  0                                        
SHEET    2   N 2 VAL E  65  CYS E  71 -1  O  GLU E  68   N  HIS E  54           
SHEET    1   O 2 CYS E  76  ILE E  77  0                                        
SHEET    2   O 2 VAL E  83  ASP E  84 -1  O  ASP E  84   N  CYS E  76           
SHEET    1   P 4 ARG F   3  LEU F   4  0                                        
SHEET    2   P 4 ARG F 112  VAL F 119 -1  O  VAL F 119   N  ARG F   3           
SHEET    3   P 4 LEU F  59  LEU F  69 -1  N  TRP F  67   O  PHE F 113           
SHEET    4   P 4 PRO F  42  HIS F  53 -1  N  ALA F  52   O  PHE F  60           
SHEET    1   Q 5 CYS F  19  SER F  24  0                                        
SHEET    2   Q 5 ARG F  93  PHE F 100 -1  O  ARG F  97   N  LYS F  22           
SHEET    3   Q 5 GLY F  80  GLN F  87 -1  N  ALA F  81   O  PHE F  98           
SHEET    4   Q 5 GLN F 124  LEU F 133 -1  O  THR F 129   N  SER F  84           
SHEET    5   Q 5 HIS F 144  VAL F 151 -1  O  VAL F 151   N  GLN F 124           
SHEET    1   R 3 THR F 177  LEU F 181  0                                        
SHEET    2   R 3 GLN F 185  SER F 189 -1  O  ARG F 187   N  GLU F 179           
SHEET    3   R 3 VAL F 235  THR F 238 -1  O  LEU F 237   N  LEU F 186           
SSBOND   1 CYS A   71    CYS A  121                          1555   1555  2.06  
SSBOND   2 CYS A   76    CYS A  123                          1555   1555  2.04  
SSBOND   3 CYS B   71    CYS B  121                          1555   1555  2.07  
SSBOND   4 CYS B   76    CYS B  123                          1555   1555  2.04  
SSBOND   5 CYS C   12    CYS C   19                          1555   1555  2.04  
SSBOND   6 CYS C   26    CYS C   95                          1555   1555  2.05  
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  246    CYS C  272                          1555   1555  2.05  
SSBOND  10 CYS C  259    CYS C  263                          1555   1555  2.05  
SSBOND  11 CYS D   71    CYS D  121                          1555   1555  2.06  
SSBOND  12 CYS D   76    CYS D  123                          1555   1555  2.04  
SSBOND  13 CYS E   71    CYS E  121                          1555   1555  2.05  
SSBOND  14 CYS E   76    CYS E  123                          1555   1555  2.05  
SSBOND  15 CYS F   12    CYS F   19                          1555   1555  2.05  
SSBOND  16 CYS F   26    CYS F   95                          1555   1555  2.06  
SSBOND  17 CYS F  154    CYS F  165                          1555   1555  2.04  
SSBOND  18 CYS F  214    CYS F  245                          1555   1555  2.04  
SSBOND  19 CYS F  246    CYS F  272                          1555   1555  2.04  
SSBOND  20 CYS F  259    CYS F  263                          1555   1555  2.03  
LINK         ND2 ASN C  18                 C1  NAG I   1     1555   1555  1.44  
LINK         ND2 ASN C  23                 C1  NAG H   1     1555   1555  1.43  
LINK         ND2 ASN C 194                 C1  NAG G   1     1555   1555  1.43  
LINK         ND2 ASN F  23                 C1  NAG F 606     1555   1555  1.43  
LINK         ND2 ASN F 194                 C1  NAG J   1     1555   1555  1.43  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.42  
LINK         O6  NAG G   1                 C1  FUC G   5     1555   1555  1.40  
LINK         O4  NAG G   2                 C1  MAN G   3     1555   1555  1.43  
LINK         O3  MAN G   3                 C1  MAN G   4     1555   1555  1.43  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.43  
LINK         O6  NAG H   1                 C1  FUC H   3     1555   1555  1.41  
LINK         O6  NAG I   1                 C1  FUC I   2     1555   1555  1.41  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.42  
LINK         O6  NAG J   1                 C1  FUC J   5     1555   1555  1.40  
LINK         O4  NAG J   2                 C1  MAN J   3     1555   1555  1.43  
LINK         O3  MAN J   3                 C1  MAN J   4     1555   1555  1.43  
CISPEP   1 ASN A   17    PHE A   18          0         4.61                     
CISPEP   2 TYR A   62    PRO A   63          0        -3.29                     
CISPEP   3 GLU A  102    PRO A  103          0        -4.38                     
CISPEP   4 TYR B   62    PRO B   63          0        -1.16                     
CISPEP   5 PRO B  103    PRO B  104          0        14.36                     
CISPEP   6 PRO B  107    ASN B  108          0         7.71                     
CISPEP   7 LEU C  133    PRO C  134          0         2.39                     
CISPEP   8 TYR D   62    PRO D   63          0        -0.58                     
CISPEP   9 GLU D  102    PRO D  103          0         4.19                     
CISPEP  10 TYR E   62    PRO E   63          0        -1.23                     
CISPEP  11 PRO E  103    PRO E  104          0        18.96                     
CISPEP  12 PRO E  107    ASN E  108          0         5.01                     
CISPEP  13 LEU F  133    PRO F  134          0         2.76                     
CRYST1  138.710  138.710  179.090  90.00  90.00 120.00 P 31 2 1     24          
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      0.007209  0.004162  0.000000        0.00000                         
SCALE2      0.000000  0.008325  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005584        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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