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Database: PDB
Entry: 5HI5
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HEADER    IMMUNE SYSTEM/INHIBITOR                 11-JAN-16   5HI5              
TITLE     BINDING SITE ELUCIDATION AND STRUCTURE GUIDED DESIGN OF MACROCYCLIC   
TITLE    2 IL-17A ANTAGONISTS                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-17A;                                           
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 24-155;                                       
COMPND   5 SYNONYM: IL-17A,CYTOTOXIC T-LYMPHOCYTE-ASSOCIATED ANTIGEN 8,CTLA-8;  
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CAT-2000 FAB HEAVY CHAIN;                                  
COMPND   9 CHAIN: C, H;                                                         
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: CAT-2000 LIGHT CHAIN;                                      
COMPND  13 CHAIN: D, L;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: SYNTHETIC IL-17A INHIBITOR;                                
COMPND  17 CHAIN: I;                                                            
COMPND  18 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: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PPPARG4;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_TAXID: 9606;                                                
SOURCE  19 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  21 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  22 MOL_ID: 4;                                                           
SOURCE  23 SYNTHETIC: YES;                                                      
SOURCE  24 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  25 ORGANISM_TAXID: 32630                                                
KEYWDS    IL-17A, PSORIASIS, MD SIMULATION, SULFONYL FLUORIDE, INHIBITOR,       
KEYWDS   2 MACROCYCLE, IMMUNE SYSTEM-INHIBITOR COMPLEX                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.LIU                                                                 
REVDAT   3   06-MAR-24 5HI5    1       REMARK                                   
REVDAT   2   22-NOV-17 5HI5    1       REMARK                                   
REVDAT   1   31-AUG-16 5HI5    0                                                
JRNL        AUTH   S.LIU,L.A.DAKIN,L.XING,J.M.WITHKA,P.V.SAHASRABUDHE,W.LI,     
JRNL        AUTH 2 M.E.BANKER,P.BALBO,S.SHANKER,B.A.CHRUNYK,Z.GUO,J.M.CHEN,     
JRNL        AUTH 3 J.A.YOUNG,G.BAI,J.T.STARR,S.W.WRIGHT,J.BUSSENIUS,S.TAN,      
JRNL        AUTH 4 A.GOPALSAMY,B.A.LEFKER,F.VINCENT,L.H.JONES,H.XU,L.R.HOTH,    
JRNL        AUTH 5 K.F.GEOGHEGAN,X.QIU,M.E.BUNNAGE,A.THORARENSEN                
JRNL        TITL   BINDING SITE ELUCIDATION AND STRUCTURE GUIDED DESIGN OF      
JRNL        TITL 2 MACROCYCLIC IL-17A ANTAGONISTS.                              
JRNL        REF    SCI REP                       V.   6 30859 2016              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   27527709                                                     
JRNL        DOI    10.1038/SREP30859                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 91.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 110571                         
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)  : 0.202                          
REMARK   3   R VALUE            (WORKING SET)  : 0.201                          
REMARK   3   FREE R VALUE                      : 0.219                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.020                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 5555                           
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               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.80                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.85                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 89.63                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 7637                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2694                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 7239                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2676                   
REMARK   3   BIN FREE R VALUE                        : 0.3028                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.21                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 398                      
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            : 8028                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 319                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.38                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.82                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.09230                                             
REMARK   3    B22 (A**2) : -2.33260                                             
REMARK   3    B33 (A**2) : 3.42480                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.90180                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.259               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.118               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.108               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.121               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.110               
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      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 8328   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 11394  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 2711   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 163    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1258   ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 8328   ; 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   : 1105   ; 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   : 8988   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.08                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.70                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.10                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   74.3911  -30.8624  -42.3863           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0594 T22:   -0.0401                                    
REMARK   3     T33:   -0.0787 T12:    0.0053                                    
REMARK   3     T13:    0.0803 T23:   -0.0884                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6130 L22:    0.8434                                    
REMARK   3     L33:    4.4690 L12:    0.3765                                    
REMARK   3     L13:   -0.3250 L23:   -0.3272                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0157 S12:    0.0360 S13:   -0.1959                     
REMARK   3     S21:    0.1366 S22:    0.0172 S23:   -0.2139                     
REMARK   3     S31:    0.4074 S32:    0.5821 S33:   -0.0328                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   66.5804  -39.0838  -49.2691           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1188 T22:   -0.1043                                    
REMARK   3     T33:   -0.1105 T12:   -0.0187                                    
REMARK   3     T13:    0.0948 T23:   -0.1636                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.3869 L22:    1.5031                                    
REMARK   3     L33:    3.6372 L12:    0.3469                                    
REMARK   3     L13:   -0.3727 L23:    0.3156                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0744 S12:    0.3946 S13:   -0.4962                     
REMARK   3     S21:   -0.2097 S22:    0.0719 S23:   -0.2621                     
REMARK   3     S31:    0.9610 S32:    0.0629 S33:    0.0026                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: { C|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   81.8338  -23.4446  -84.9169           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0549 T22:   -0.0482                                    
REMARK   3     T33:   -0.0091 T12:   -0.0297                                    
REMARK   3     T13:    0.0095 T23:   -0.0364                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8427 L22:    0.7297                                    
REMARK   3     L33:    0.6967 L12:    0.2789                                    
REMARK   3     L13:   -0.5129 L23:   -0.5150                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0080 S12:   -0.1794 S13:    0.0696                     
REMARK   3     S21:    0.1331 S22:   -0.0661 S23:   -0.0131                     
REMARK   3     S31:   -0.0585 S32:   -0.0329 S33:    0.0582                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: { D|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   75.7568   -7.1456  -87.9848           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0838 T22:   -0.1916                                    
REMARK   3     T33:   -0.0154 T12:    0.0172                                    
REMARK   3     T13:    0.0956 T23:   -0.0601                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9450 L22:    1.1705                                    
REMARK   3     L33:    1.9188 L12:    0.9678                                    
REMARK   3     L13:   -0.6780 L23:   -1.5922                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.2834 S12:   -0.1183 S13:    0.3135                     
REMARK   3     S21:    0.3340 S22:    0.0462 S23:    0.3672                     
REMARK   3     S31:   -0.3584 S32:   -0.1553 S33:   -0.3296                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: { H|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   50.5398  -30.0499   -8.1449           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0981 T22:   -0.0555                                    
REMARK   3     T33:   -0.0004 T12:   -0.0146                                    
REMARK   3     T13:   -0.0110 T23:   -0.0211                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9510 L22:    0.5683                                    
REMARK   3     L33:    0.7979 L12:    0.0289                                    
REMARK   3     L13:   -0.8246 L23:   -0.1865                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0358 S12:   -0.0073 S13:   -0.0858                     
REMARK   3     S21:   -0.1578 S22:   -0.0103 S23:    0.0709                     
REMARK   3     S31:    0.0403 S32:    0.0524 S33:    0.0461                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: { I|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   76.8378  -60.7559  -40.1141           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1330 T22:   -0.2317                                    
REMARK   3     T33:    0.0359 T12:    0.1708                                    
REMARK   3     T13:    0.0008 T23:    0.0113                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -0.0258 L22:    1.2275                                    
REMARK   3     L33:    0.0349 L12:   -1.4821                                    
REMARK   3     L13:    1.1390 L23:    0.9790                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0019 S12:   -0.1141 S13:   -0.0817                     
REMARK   3     S21:   -0.0265 S22:   -0.0255 S23:   -0.0362                     
REMARK   3     S31:    0.0354 S32:    0.0735 S33:    0.0274                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: { L|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   40.8842  -15.5391   -9.6956           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0740 T22:   -0.0589                                    
REMARK   3     T33:   -0.0236 T12:    0.0104                                    
REMARK   3     T13:    0.0082 T23:    0.0057                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5433 L22:    0.4127                                    
REMARK   3     L33:    1.3204 L12:   -0.0006                                    
REMARK   3     L13:   -0.5335 L23:   -0.0892                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0295 S12:    0.0602 S13:    0.0001                     
REMARK   3     S21:   -0.0119 S22:    0.0209 S23:   -0.0275                     
REMARK   3     S31:   -0.1337 S32:   -0.1069 S33:   -0.0505                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5HI5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217070.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-SEP-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : AUTOPROC, AIMLESS                  
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 113034                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 91.310                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.03700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% 2-PROPANOL, 20-24% PEG 6K, 0.1 M     
REMARK 280  SODIUM ACETATE PH=4.0-5.0, PH 4.5, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       34.34000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEPTAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, H, I, L                   
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     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     CYS A    10                                                      
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    17                                                      
REMARK 465     PHE A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     ARG A    20                                                      
REMARK 465     THR A    21                                                      
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     ARG A   101                                                      
REMARK 465     GLU A   102                                                      
REMARK 465     PRO A   103                                                      
REMARK 465     PRO A   104                                                      
REMARK 465     HIS A   105                                                      
REMARK 465     CYS A   106                                                      
REMARK 465     PRO A   107                                                      
REMARK 465     ASN A   108                                                      
REMARK 465     SER A   109                                                      
REMARK 465     HIS A   130                                                      
REMARK 465     VAL A   131                                                      
REMARK 465     ALA A   132                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     ILE B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     PRO B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     CYS B    10                                                      
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     PRO B    19                                                      
REMARK 465     ARG B    20                                                      
REMARK 465     THR B    21                                                      
REMARK 465     VAL B    22                                                      
REMARK 465     MET B    23                                                      
REMARK 465     VAL B    24                                                      
REMARK 465     ASN B    25                                                      
REMARK 465     LEU B    26                                                      
REMARK 465     ASN B    27                                                      
REMARK 465     ILE B    28                                                      
REMARK 465     HIS B    29                                                      
REMARK 465     ASN B    30                                                      
REMARK 465     ARG B    31                                                      
REMARK 465     ASN B    32                                                      
REMARK 465     THR B    33                                                      
REMARK 465     ASN B    34                                                      
REMARK 465     THR B    35                                                      
REMARK 465     ARG B   101                                                      
REMARK 465     GLU B   102                                                      
REMARK 465     PRO B   103                                                      
REMARK 465     PRO B   104                                                      
REMARK 465     HIS B   105                                                      
REMARK 465     CYS B   106                                                      
REMARK 465     PRO B   107                                                      
REMARK 465     HIS B   130                                                      
REMARK 465     VAL B   131                                                      
REMARK 465     ALA B   132                                                      
REMARK 465     GLY C   -16                                                      
REMARK 465     SER C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     HIS C    -9                                                      
REMARK 465     GLY C    -8                                                      
REMARK 465     SER C    -7                                                      
REMARK 465     GLU C    -6                                                      
REMARK 465     ASN C    -5                                                      
REMARK 465     LEU C    -4                                                      
REMARK 465     TYR C    -3                                                      
REMARK 465     PHE C    -2                                                      
REMARK 465     GLN C    -1                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     GLU D   211                                                      
REMARK 465     GLY H   -16                                                      
REMARK 465     SER H   -15                                                      
REMARK 465     HIS H   -14                                                      
REMARK 465     HIS H   -13                                                      
REMARK 465     HIS H   -12                                                      
REMARK 465     HIS H   -11                                                      
REMARK 465     HIS H   -10                                                      
REMARK 465     HIS H    -9                                                      
REMARK 465     GLY H    -8                                                      
REMARK 465     SER H    -7                                                      
REMARK 465     GLU H    -6                                                      
REMARK 465     ASN H    -5                                                      
REMARK 465     LEU H    -4                                                      
REMARK 465     TYR H    -3                                                      
REMARK 465     PHE H    -2                                                      
REMARK 465     GLN H    -1                                                      
REMARK 465     GLY H     0                                                      
REMARK 465     ACE I     0                                                      
REMARK 465     LYS I    15                                                      
REMARK 465     GLU L   211                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 113    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 111    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 113    CG   CD   OE1  OE2                                  
REMARK 470     ASN D   1    CG   OD1  ND2                                       
REMARK 470     ASN L   1    CG   OD1  ND2                                       
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    MET A  23       97.46    -69.81                                   
REMARK 500    ASN A  25       62.20   -108.80                                   
REMARK 500    THR C 191      -50.76   -128.18                                   
REMARK 500    ASN D  51      -48.40     72.36                                   
REMARK 500    ASN D  52       11.10   -145.09                                   
REMARK 500    ALA D  84     -179.60    176.52                                   
REMARK 500    PRO D 142     -177.21    -68.97                                   
REMARK 500    ASP D 152     -110.86     61.67                                   
REMARK 500    ASN D 171       -8.67     77.05                                   
REMARK 500    ASN L  51      -48.48     72.09                                   
REMARK 500    ASN L  52       11.30   -145.58                                   
REMARK 500    ALA L  84     -179.19    177.49                                   
REMARK 500    ASP L 152     -109.86     60.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 63Q B 4000                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HHV   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HHX   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HI3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HI4   RELATED DB: PDB                                   
DBREF  5HI5 A    1   132  UNP    Q16552   IL17_HUMAN      24    155             
DBREF  5HI5 B    1   132  UNP    Q16552   IL17_HUMAN      24    155             
DBREF  5HI5 C  -16   215  PDB    5HI5     5HI5           -16    215             
DBREF  5HI5 D    1   211  PDB    5HI5     5HI5             1    211             
DBREF  5HI5 H  -16   215  PDB    5HI5     5HI5           -16    215             
DBREF  5HI5 I    0    15  PDB    5HI5     5HI5             0     15             
DBREF  5HI5 L    1   211  PDB    5HI5     5HI5             1    211             
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  132  GLY ILE THR ILE PRO ARG ASN PRO GLY CYS PRO ASN SER          
SEQRES   2 B  132  GLU ASP LYS ASN PHE PRO ARG THR VAL MET VAL ASN LEU          
SEQRES   3 B  132  ASN ILE HIS ASN ARG ASN THR ASN THR ASN PRO LYS ARG          
SEQRES   4 B  132  SER SER ASP TYR TYR ASN ARG SER THR SER PRO TRP ASN          
SEQRES   5 B  132  LEU HIS ARG ASN GLU ASP PRO GLU ARG TYR PRO SER VAL          
SEQRES   6 B  132  ILE TRP GLU ALA LYS CYS ARG HIS LEU GLY CYS ILE ASN          
SEQRES   7 B  132  ALA ASP GLY ASN VAL ASP TYR HIS MET ASN SER VAL PRO          
SEQRES   8 B  132  ILE GLN GLN GLU ILE LEU VAL LEU ARG ARG GLU PRO PRO          
SEQRES   9 B  132  HIS CYS PRO ASN SER PHE ARG LEU GLU LYS ILE LEU VAL          
SEQRES  10 B  132  SER VAL GLY CYS THR CYS VAL THR PRO ILE VAL HIS HIS          
SEQRES  11 B  132  VAL ALA                                                      
SEQRES   1 C  237  GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLU ASN LEU          
SEQRES   2 C  237  TYR PHE GLN GLY GLU VAL GLN LEU LEU GLU SER GLY GLY          
SEQRES   3 C  237  GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS          
SEQRES   4 C  237  ALA ALA SER GLY PHE THR PHE SER SER TYR ALA MET SER          
SEQRES   5 C  237  TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL          
SEQRES   6 C  237  SER ALA ILE SER GLY SER GLY GLY SER THR TYR TYR ALA          
SEQRES   7 C  237  ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN          
SEQRES   8 C  237  SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG          
SEQRES   9 C  237  ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG ASP LEU          
SEQRES  10 C  237  ILE HIS GLY VAL THR ARG ASN TRP GLY GLN GLY THR LEU          
SEQRES  11 C  237  VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL          
SEQRES  12 C  237  PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY          
SEQRES  13 C  237  THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO          
SEQRES  14 C  237  GLN PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR          
SEQRES  15 C  237  SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER          
SEQRES  16 C  237  GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER          
SEQRES  17 C  237  SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN          
SEQRES  18 C  237  HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU          
SEQRES  19 C  237  PRO LYS SER                                                  
SEQRES   1 D  214  ASN PHE MET LEU THR GLN PRO HIS SER VAL SER GLU SER          
SEQRES   2 D  214  PRO GLY LYS THR VAL THR ILE SER CYS THR ARG SER SER          
SEQRES   3 D  214  GLY SER LEU ALA ASN TYR TYR VAL GLN TRP TYR GLN GLN          
SEQRES   4 D  214  ARG PRO GLY SER SER PRO THR ILE VAL ILE PHE ALA ASN          
SEQRES   5 D  214  ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY          
SEQRES   6 D  214  SER ILE ASP SER SER SER ASN SER ALA SER LEU THR ILE          
SEQRES   7 D  214  SER GLY LEU LYS THR GLU ASP GLU ALA ASP TYR TYR CYS          
SEQRES   8 D  214  GLN THR TYR ASP PRO TYR SER VAL VAL PHE GLY GLY GLY          
SEQRES   9 D  214  THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO          
SEQRES  10 D  214  SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN          
SEQRES  11 D  214  ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE          
SEQRES  12 D  214  TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER          
SEQRES  13 D  214  SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER          
SEQRES  14 D  214  LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU          
SEQRES  15 D  214  SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR          
SEQRES  16 D  214  SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS          
SEQRES  17 D  214  THR VAL ALA PRO THR GLU                                      
SEQRES   1 H  237  GLY SER HIS HIS HIS HIS HIS HIS GLY SER GLU ASN LEU          
SEQRES   2 H  237  TYR PHE GLN GLY GLU VAL GLN LEU LEU GLU SER GLY GLY          
SEQRES   3 H  237  GLY LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS          
SEQRES   4 H  237  ALA ALA SER GLY PHE THR PHE SER SER TYR ALA MET SER          
SEQRES   5 H  237  TRP VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL          
SEQRES   6 H  237  SER ALA ILE SER GLY SER GLY GLY SER THR TYR TYR ALA          
SEQRES   7 H  237  ASP SER VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN          
SEQRES   8 H  237  SER LYS ASN THR LEU TYR LEU GLN MET ASN SER LEU ARG          
SEQRES   9 H  237  ALA GLU ASP THR ALA VAL TYR TYR CYS ALA ARG ASP LEU          
SEQRES  10 H  237  ILE HIS GLY VAL THR ARG ASN TRP GLY GLN GLY THR LEU          
SEQRES  11 H  237  VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL          
SEQRES  12 H  237  PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY          
SEQRES  13 H  237  THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO          
SEQRES  14 H  237  GLN PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR          
SEQRES  15 H  237  SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER          
SEQRES  16 H  237  GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER          
SEQRES  17 H  237  SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN          
SEQRES  18 H  237  HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU          
SEQRES  19 H  237  PRO LYS SER                                                  
SEQRES   1 I   16  ACE ILE HIS VAL THR ILE PRO ALA ASP LEU TRP ASP TRP          
SEQRES   2 I   16  ILE ASN LYS                                                  
SEQRES   1 L  214  ASN PHE MET LEU THR GLN PRO HIS SER VAL SER GLU SER          
SEQRES   2 L  214  PRO GLY LYS THR VAL THR ILE SER CYS THR ARG SER SER          
SEQRES   3 L  214  GLY SER LEU ALA ASN TYR TYR VAL GLN TRP TYR GLN GLN          
SEQRES   4 L  214  ARG PRO GLY SER SER PRO THR ILE VAL ILE PHE ALA ASN          
SEQRES   5 L  214  ASN GLN ARG PRO SER GLY VAL PRO ASP ARG PHE SER GLY          
SEQRES   6 L  214  SER ILE ASP SER SER SER ASN SER ALA SER LEU THR ILE          
SEQRES   7 L  214  SER GLY LEU LYS THR GLU ASP GLU ALA ASP TYR TYR CYS          
SEQRES   8 L  214  GLN THR TYR ASP PRO TYR SER VAL VAL PHE GLY GLY GLY          
SEQRES   9 L  214  THR LYS LEU THR VAL LEU GLY GLN PRO LYS ALA ALA PRO          
SEQRES  10 L  214  SER VAL THR LEU PHE PRO PRO SER SER GLU GLU LEU GLN          
SEQRES  11 L  214  ALA ASN LYS ALA THR LEU VAL CYS LEU ILE SER ASP PHE          
SEQRES  12 L  214  TYR PRO GLY ALA VAL THR VAL ALA TRP LYS ALA ASP SER          
SEQRES  13 L  214  SER PRO VAL LYS ALA GLY VAL GLU THR THR THR PRO SER          
SEQRES  14 L  214  LYS GLN SER ASN ASN LYS TYR ALA ALA SER SER TYR LEU          
SEQRES  15 L  214  SER LEU THR PRO GLU GLN TRP LYS SER HIS ARG SER TYR          
SEQRES  16 L  214  SER CYS GLN VAL THR HIS GLU GLY SER THR VAL GLU LYS          
SEQRES  17 L  214  THR VAL ALA PRO THR GLU                                      
HET    63Q  B4000      77                                                       
HETNAM     63Q (4S,20R)-7-CHLORO-N-METHYL-4-{[(1-METHYL-1H-PYRAZOL-5-           
HETNAM   2 63Q  YL)CARBONYL]AMINO}-3,18-DIOXO-2,19-                             
HETNAM   3 63Q  DIAZATETRACYCLO[20.2.2.1~6,10~.1~11,15~]OCTACOSA-               
HETNAM   4 63Q  1(24),6(28),7,9,11(27),12,14,22,25-NONAENE-20-                  
HETNAM   5 63Q  CARBOXAMIDE                                                     
FORMUL   8  63Q    C33 H33 CL N6 O4                                             
FORMUL   9  HOH   *319(H2 O)                                                    
HELIX    1 AA1 ASN A   36  SER A   40  5                                   5    
HELIX    2 AA2 ASP A   42  SER A   47  1                                   6    
HELIX    3 AA3 ASN B   36  SER B   40  5                                   5    
HELIX    4 AA4 ASP B   42  SER B   47  1                                   6    
HELIX    5 AA5 THR C   28  TYR C   32  5                                   5    
HELIX    6 AA6 ASP C   61  LYS C   64  5                                   4    
HELIX    7 AA7 ARG C   83  THR C   87  5                                   5    
HELIX    8 AA8 SER C  156  ALA C  158  5                                   3    
HELIX    9 AA9 SER C  187  LEU C  189  5                                   3    
HELIX   10 AB1 LYS C  201  ASN C  204  5                                   4    
HELIX   11 AB2 SER D   27B TYR D   31  5                                   5    
HELIX   12 AB3 LYS D   79  GLU D   83  5                                   5    
HELIX   13 AB4 SER D  122  ALA D  128  1                                   7    
HELIX   14 AB5 THR D  182  HIS D  189  1                                   8    
HELIX   15 AB6 THR H   28  TYR H   32  5                                   5    
HELIX   16 AB7 ASP H   61  LYS H   64  5                                   4    
HELIX   17 AB8 ARG H   83  THR H   87  5                                   5    
HELIX   18 AB9 SER H  127  LYS H  129  5                                   3    
HELIX   19 AC1 SER H  156  ALA H  158  5                                   3    
HELIX   20 AC2 SER H  187  LEU H  189  5                                   3    
HELIX   21 AC3 LYS H  201  ASN H  204  5                                   4    
HELIX   22 AC4 ALA I    7  ASN I   14  1                                   8    
HELIX   23 AC5 SER L   27B TYR L   31  5                                   5    
HELIX   24 AC6 LYS L   79  GLU L   83  5                                   5    
HELIX   25 AC7 SER L  122  ALA L  128  1                                   7    
HELIX   26 AC8 THR L  182  HIS L  189  1                                   8    
SHEET    1 AA1 4 ASN A  27  HIS A  29  0                                        
SHEET    2 AA1 4 HIS I   2  PRO I   6  1  O  ILE I   5   N  ASN A  27           
SHEET    3 AA1 4 SER B 109  VAL B 124  1  N  PHE B 110   O  THR I   4           
SHEET    4 AA1 4 ASN B  88  ARG B 100 -1  N  ILE B  96   O  ILE B 115           
SHEET    1 AA2 2 TRP A  51  GLU A  57  0                                        
SHEET    2 AA2 2 VAL A  65  CYS A  71 -1  O  GLU A  68   N  HIS A  54           
SHEET    1 AA3 2 CYS A  76  ILE A  77  0                                        
SHEET    2 AA3 2 VAL A  83  ASP A  84 -1  O  ASP A  84   N  CYS A  76           
SHEET    1 AA4 2 ASN A  88  LEU A  99  0                                        
SHEET    2 AA4 2 LEU A 112  VAL A 124 -1  O  GLY A 120   N  ILE A  92           
SHEET    1 AA5 2 TRP B  51  GLU B  57  0                                        
SHEET    2 AA5 2 VAL B  65  CYS B  71 -1  O  GLU B  68   N  HIS B  54           
SHEET    1 AA6 2 CYS B  76  ILE B  77  0                                        
SHEET    2 AA6 2 VAL B  83  ASP B  84 -1  O  ASP B  84   N  CYS B  76           
SHEET    1 AA7 4 GLN C   3  SER C   7  0                                        
SHEET    2 AA7 4 LEU C  18  SER C  25 -1  O  ALA C  23   N  LEU C   5           
SHEET    3 AA7 4 THR C  77  MET C  82 -1  O  LEU C  80   N  LEU C  20           
SHEET    4 AA7 4 PHE C  67  ASP C  72 -1  N  SER C  70   O  TYR C  79           
SHEET    1 AA8 6 GLY C  10  VAL C  12  0                                        
SHEET    2 AA8 6 THR C 107  VAL C 111  1  O  THR C 110   N  VAL C  12           
SHEET    3 AA8 6 ALA C  88  ASP C  95 -1  N  TYR C  90   O  THR C 107           
SHEET    4 AA8 6 ALA C  33  GLN C  39 -1  N  VAL C  37   O  TYR C  91           
SHEET    5 AA8 6 LEU C  45  ILE C  51 -1  O  GLU C  46   N  ARG C  38           
SHEET    6 AA8 6 THR C  57  TYR C  59 -1  O  TYR C  58   N  ALA C  50           
SHEET    1 AA9 4 GLY C  10  VAL C  12  0                                        
SHEET    2 AA9 4 THR C 107  VAL C 111  1  O  THR C 110   N  VAL C  12           
SHEET    3 AA9 4 ALA C  88  ASP C  95 -1  N  TYR C  90   O  THR C 107           
SHEET    4 AA9 4 THR C 100A TRP C 103 -1  O  ARG C 101   N  ARG C  94           
SHEET    1 AB1 4 SER C 120  LEU C 124  0                                        
SHEET    2 AB1 4 THR C 135  TYR C 145 -1  O  GLY C 139   N  LEU C 124           
SHEET    3 AB1 4 TYR C 176  PRO C 185 -1  O  LEU C 178   N  VAL C 142           
SHEET    4 AB1 4 VAL C 163  THR C 165 -1  N  HIS C 164   O  VAL C 181           
SHEET    1 AB2 4 THR C 131  SER C 132  0                                        
SHEET    2 AB2 4 THR C 135  TYR C 145 -1  O  THR C 135   N  SER C 132           
SHEET    3 AB2 4 TYR C 176  PRO C 185 -1  O  LEU C 178   N  VAL C 142           
SHEET    4 AB2 4 VAL C 169  LEU C 170 -1  N  VAL C 169   O  SER C 177           
SHEET    1 AB3 3 THR C 151  TRP C 154  0                                        
SHEET    2 AB3 3 TYR C 194  HIS C 200 -1  O  ASN C 197   N  SER C 153           
SHEET    3 AB3 3 THR C 205  VAL C 211 -1  O  VAL C 207   N  VAL C 198           
SHEET    1 AB4 4 LEU D   4  THR D   5  0                                        
SHEET    2 AB4 4 VAL D  19  ARG D  25 -1  O  THR D  24   N  THR D   5           
SHEET    3 AB4 4 SER D  70  ILE D  75 -1  O  ILE D  75   N  VAL D  19           
SHEET    4 AB4 4 PHE D  62  ASP D  67 -1  N  ASP D  67   O  SER D  70           
SHEET    1 AB5 5 SER D   9  GLU D  13  0                                        
SHEET    2 AB5 5 THR D 102  VAL D 106  1  O  THR D 105   N  VAL D  11           
SHEET    3 AB5 5 ALA D  84  TYR D  91 -1  N  ALA D  84   O  LEU D 104           
SHEET    4 AB5 5 GLN D  34  GLN D  38 -1  N  GLN D  34   O  GLN D  89           
SHEET    5 AB5 5 THR D  45  ILE D  48 -1  O  ILE D  48   N  TRP D  35           
SHEET    1 AB6 4 SER D   9  GLU D  13  0                                        
SHEET    2 AB6 4 THR D 102  VAL D 106  1  O  THR D 105   N  VAL D  11           
SHEET    3 AB6 4 ALA D  84  TYR D  91 -1  N  ALA D  84   O  LEU D 104           
SHEET    4 AB6 4 VAL D  96  PHE D  98 -1  O  VAL D  97   N  THR D  90           
SHEET    1 AB7 4 SER D 115  PHE D 119  0                                        
SHEET    2 AB7 4 ALA D 131  PHE D 140 -1  O  LEU D 136   N  THR D 117           
SHEET    3 AB7 4 TYR D 173  LEU D 181 -1  O  SER D 177   N  CYS D 135           
SHEET    4 AB7 4 VAL D 160  THR D 162 -1  N  GLU D 161   O  TYR D 178           
SHEET    1 AB8 4 SER D 115  PHE D 119  0                                        
SHEET    2 AB8 4 ALA D 131  PHE D 140 -1  O  LEU D 136   N  THR D 117           
SHEET    3 AB8 4 TYR D 173  LEU D 181 -1  O  SER D 177   N  CYS D 135           
SHEET    4 AB8 4 SER D 166  LYS D 167 -1  N  SER D 166   O  ALA D 174           
SHEET    1 AB9 4 SER D 154  VAL D 156  0                                        
SHEET    2 AB9 4 THR D 146  ALA D 151 -1  N  ALA D 151   O  SER D 154           
SHEET    3 AB9 4 TYR D 192  HIS D 198 -1  O  GLN D 195   N  ALA D 148           
SHEET    4 AB9 4 SER D 201  VAL D 207 -1  O  VAL D 203   N  VAL D 196           
SHEET    1 AC1 4 GLN H   3  SER H   7  0                                        
SHEET    2 AC1 4 LEU H  18  SER H  25 -1  O  ALA H  23   N  LEU H   5           
SHEET    3 AC1 4 THR H  77  MET H  82 -1  O  MET H  82   N  LEU H  18           
SHEET    4 AC1 4 PHE H  67  ASP H  72 -1  N  SER H  70   O  TYR H  79           
SHEET    1 AC2 6 LEU H  11  VAL H  12  0                                        
SHEET    2 AC2 6 THR H 107  VAL H 111  1  O  THR H 110   N  VAL H  12           
SHEET    3 AC2 6 ALA H  88  ASP H  95 -1  N  TYR H  90   O  THR H 107           
SHEET    4 AC2 6 ALA H  33  GLN H  39 -1  N  VAL H  37   O  TYR H  91           
SHEET    5 AC2 6 LEU H  45  ILE H  51 -1  O  GLU H  46   N  ARG H  38           
SHEET    6 AC2 6 THR H  57  TYR H  59 -1  O  TYR H  58   N  ALA H  50           
SHEET    1 AC3 4 LEU H  11  VAL H  12  0                                        
SHEET    2 AC3 4 THR H 107  VAL H 111  1  O  THR H 110   N  VAL H  12           
SHEET    3 AC3 4 ALA H  88  ASP H  95 -1  N  TYR H  90   O  THR H 107           
SHEET    4 AC3 4 THR H 100A TRP H 103 -1  O  ARG H 101   N  ARG H  94           
SHEET    1 AC4 4 SER H 120  LEU H 124  0                                        
SHEET    2 AC4 4 THR H 135  TYR H 145 -1  O  GLY H 139   N  LEU H 124           
SHEET    3 AC4 4 TYR H 176  PRO H 185 -1  O  LEU H 178   N  VAL H 142           
SHEET    4 AC4 4 VAL H 163  THR H 165 -1  N  HIS H 164   O  VAL H 181           
SHEET    1 AC5 4 THR H 131  SER H 132  0                                        
SHEET    2 AC5 4 THR H 135  TYR H 145 -1  O  THR H 135   N  SER H 132           
SHEET    3 AC5 4 TYR H 176  PRO H 185 -1  O  LEU H 178   N  VAL H 142           
SHEET    4 AC5 4 VAL H 169  LEU H 170 -1  N  VAL H 169   O  SER H 177           
SHEET    1 AC6 3 THR H 151  TRP H 154  0                                        
SHEET    2 AC6 3 ILE H 195  HIS H 200 -1  O  ASN H 197   N  SER H 153           
SHEET    3 AC6 3 THR H 205  LYS H 210 -1  O  VAL H 207   N  VAL H 198           
SHEET    1 AC7 4 LEU L   4  THR L   5  0                                        
SHEET    2 AC7 4 VAL L  19  ARG L  25 -1  O  THR L  24   N  THR L   5           
SHEET    3 AC7 4 SER L  70  ILE L  75 -1  O  ILE L  75   N  VAL L  19           
SHEET    4 AC7 4 PHE L  62  ASP L  67 -1  N  ASP L  67   O  SER L  70           
SHEET    1 AC8 5 SER L   9  GLU L  13  0                                        
SHEET    2 AC8 5 THR L 102  VAL L 106  1  O  THR L 105   N  VAL L  11           
SHEET    3 AC8 5 ALA L  84  TYR L  91 -1  N  ALA L  84   O  LEU L 104           
SHEET    4 AC8 5 GLN L  34  GLN L  38 -1  N  GLN L  34   O  GLN L  89           
SHEET    5 AC8 5 THR L  45  ILE L  48 -1  O  ILE L  48   N  TRP L  35           
SHEET    1 AC9 4 SER L   9  GLU L  13  0                                        
SHEET    2 AC9 4 THR L 102  VAL L 106  1  O  THR L 105   N  VAL L  11           
SHEET    3 AC9 4 ALA L  84  TYR L  91 -1  N  ALA L  84   O  LEU L 104           
SHEET    4 AC9 4 VAL L  96  PHE L  98 -1  O  VAL L  97   N  THR L  90           
SHEET    1 AD1 4 SER L 115  PHE L 119  0                                        
SHEET    2 AD1 4 ALA L 131  PHE L 140 -1  O  LEU L 136   N  THR L 117           
SHEET    3 AD1 4 TYR L 173  LEU L 181 -1  O  TYR L 173   N  PHE L 140           
SHEET    4 AD1 4 VAL L 160  THR L 162 -1  N  GLU L 161   O  TYR L 178           
SHEET    1 AD2 4 SER L 115  PHE L 119  0                                        
SHEET    2 AD2 4 ALA L 131  PHE L 140 -1  O  LEU L 136   N  THR L 117           
SHEET    3 AD2 4 TYR L 173  LEU L 181 -1  O  TYR L 173   N  PHE L 140           
SHEET    4 AD2 4 SER L 166  LYS L 167 -1  N  SER L 166   O  ALA L 174           
SHEET    1 AD3 4 SER L 154  VAL L 156  0                                        
SHEET    2 AD3 4 THR L 146  ALA L 151 -1  N  ALA L 151   O  SER L 154           
SHEET    3 AD3 4 TYR L 192  HIS L 198 -1  O  GLN L 195   N  ALA L 148           
SHEET    4 AD3 4 SER L 201  VAL L 207 -1  O  VAL L 203   N  VAL L 196           
SSBOND   1 CYS A   71    CYS A  121                          1555   1555  2.07  
SSBOND   2 CYS A   76    CYS A  123                          1555   1555  2.05  
SSBOND   3 CYS B   71    CYS B  121                          1555   1555  2.08  
SSBOND   4 CYS B   76    CYS B  123                          1555   1555  2.05  
SSBOND   5 CYS C   22    CYS C   92                          1555   1555  2.03  
SSBOND   6 CYS C  140    CYS C  196                          1555   1555  2.04  
SSBOND   7 CYS D   23    CYS D   88                          1555   1555  2.05  
SSBOND   8 CYS D  135    CYS D  194                          1555   1555  2.05  
SSBOND   9 CYS H   22    CYS H   92                          1555   1555  2.05  
SSBOND  10 CYS H  140    CYS H  196                          1555   1555  2.03  
SSBOND  11 CYS L   23    CYS L   88                          1555   1555  2.06  
SSBOND  12 CYS L  135    CYS L  194                          1555   1555  2.04  
CISPEP   1 TYR A   62    PRO A   63          0         1.55                     
CISPEP   2 TYR B   62    PRO B   63          0         1.94                     
CISPEP   3 PHE C  146    PRO C  147          0        -4.41                     
CISPEP   4 GLN C  148    PRO C  149          0         0.08                     
CISPEP   5 TYR D  141    PRO D  142          0        -2.38                     
CISPEP   6 PHE H  146    PRO H  147          0        -8.32                     
CISPEP   7 GLN H  148    PRO H  149          0         4.76                     
CISPEP   8 TYR L  141    PRO L  142          0        -2.77                     
SITE     1 AC1 13 PRO A  63  GLU A  95  ILE A  96  LEU A  97                    
SITE     2 AC1 13 TYR B  62  PRO B  63  VAL B  65  ILE B  66                    
SITE     3 AC1 13 TRP B  67  GLU B  95  ILE B  96  LEU B  97                    
SITE     4 AC1 13 LEU B 112                                                     
CRYST1   91.320   68.680  100.530  90.00  90.65  90.00 P 1 21 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      0.010951  0.000000  0.000124        0.00000                         
SCALE2      0.000000  0.014560  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009948        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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