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Database: PDB
Entry: 5UIU
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Original site: 5UIU 
HEADER    TRANSFERASE                             14-JAN-17   5UIU              
TITLE     CRYSTAL STRUCTURE OF IRAK4 IN COMPLEX WITH COMPOUND 30                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTERLEUKIN-1 RECEPTOR-ASSOCIATED KINASE 4;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 154-460;                                      
COMPND   5 SYNONYM: IRAK-4,RENAL CARCINOMA ANTIGEN NY-REN-64;                   
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: IRAK4;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    TRANSFERASE, IRAK4, KINASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.HAN,J.S.CHANG                                                       
REVDAT   2   26-JUL-17 5UIU    1       JRNL                                     
REVDAT   1   24-MAY-17 5UIU    0                                                
JRNL        AUTH   K.L.LEE,C.M.AMBLER,D.R.ANDERSON,B.P.BOSCOE,A.G.BREE,         
JRNL        AUTH 2 J.I.BRODFUEHRER,J.S.CHANG,C.CHOI,S.CHUNG,K.J.CURRAN,J.E.DAY, 
JRNL        AUTH 3 C.M.DEHNHARDT,K.DOWER,S.E.DROZDA,R.K.FRISBIE,L.K.GAVRIN,     
JRNL        AUTH 4 J.A.GOLDBERG,S.HAN,M.HEGEN,D.HEPWORTH,H.R.HOPE,S.KAMTEKAR,   
JRNL        AUTH 5 I.C.KILTY,A.LEE,L.L.LIN,F.E.LOVERING,M.D.LOWE,J.P.MATHIAS,   
JRNL        AUTH 6 H.M.MORGAN,E.A.MURPHY,N.PAPAIOANNOU,A.PATNY,B.S.PIERCE,      
JRNL        AUTH 7 V.R.RAO,E.SAIAH,I.J.SAMARDJIEV,B.M.SAMAS,M.W.H.SHEN,         
JRNL        AUTH 8 J.H.SHIN,H.H.SOUTTER,J.W.STROHBACH,P.T.SYMANOWICZ,           
JRNL        AUTH 9 J.R.THOMASON,J.D.TRZUPEK,R.VARGAS,F.VINCENT,J.YAN,C.W.ZAPF,  
JRNL        AUTH10 S.W.WRIGHT                                                   
JRNL        TITL   DISCOVERY OF CLINICAL CANDIDATE                              
JRNL        TITL 2 1-{[(2S,3S,4S)                                               
JRNL        TITL 3 -3-ETHYL-4-FLUORO-5-OXOPYRROLIDIN-2-YL]METHOXY}-7-METHOXYISO 
JRNL        TITL 4 QUINOLINE-6-CARBOXAMIDE (PF-06650833), A POTENT, SELECTIVE   
JRNL        TITL 5 INHIBITOR OF INTERLEUKIN-1 RECEPTOR ASSOCIATED KINASE 4      
JRNL        TITL 6 (IRAK4), BY FRAGMENT-BASED DRUG DESIGN.                      
JRNL        REF    J. MED. CHEM.                 V.  60  5521 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   28498658                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B00231                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.02 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) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 75.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 48890                          
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)  : 0.186                          
REMARK   3   R VALUE            (WORKING SET)  : 0.185                          
REMARK   3   FREE R VALUE                      : 0.204                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.060                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2472                           
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) : 2.02                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.07                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 99.91                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3606                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1958                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 3435                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1954                   
REMARK   3   BIN FREE R VALUE                        : 0.2034                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.74                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 171                      
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            : 4561                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 52                                      
REMARK   3   SOLVENT ATOMS            : 393                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 37.41                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 46.34                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.06480                                             
REMARK   3    B22 (A**2) : -6.60630                                             
REMARK   3    B33 (A**2) : 8.67110                                              
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) : 0.247               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.163               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.134               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.156               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.132               
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      : 0.944                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.932                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4750   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6460   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1685   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 134    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 719    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4750   ; 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   : 619    ; 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   : 5683   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.09                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.88                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.44                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -27.5264  -31.9028   14.5714           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2818 T22:   -0.2233                                    
REMARK   3     T33:   -0.2729 T12:    0.0410                                    
REMARK   3     T13:    0.0143 T23:    0.0184                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1165 L22:    1.2706                                    
REMARK   3     L33:    1.4566 L12:    0.6795                                    
REMARK   3     L13:   -0.2323 L23:   -0.1086                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0774 S12:   -0.0515 S13:   -0.1334                     
REMARK   3     S21:    0.1050 S22:   -0.0446 S23:    0.1331                     
REMARK   3     S31:    0.0063 S32:   -0.1807 S33:   -0.0329                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -11.8731  -24.8002  -15.5647           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2174 T22:   -0.2764                                    
REMARK   3     T33:   -0.2806 T12:   -0.0296                                    
REMARK   3     T13:   -0.0381 T23:    0.0156                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.5240 L22:    1.0055                                    
REMARK   3     L33:    2.2045 L12:   -0.2281                                    
REMARK   3     L13:    0.6991 L23:    0.2373                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0896 S12:    0.1040 S13:    0.0750                     
REMARK   3     S21:   -0.1204 S22:   -0.0247 S23:    0.0816                     
REMARK   3     S31:   -0.2943 S32:   -0.0243 S33:    0.1143                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UIU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000225940.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 173                                
REMARK 200  PH                             : NULL                               
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 PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49042                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 75.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.4000                            
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: 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   (%): 51.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6-1.8M AMMONIUM CITRATE, PH7.0,        
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       44.97000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       59.23000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       69.42000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       44.97000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       59.23000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       69.42000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       44.97000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       59.23000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       69.42000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       44.97000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       59.23000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       69.42000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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     MET A   138                                                      
REMARK 465     HIS A   139                                                      
REMARK 465     HIS A   140                                                      
REMARK 465     HIS A   141                                                      
REMARK 465     HIS A   142                                                      
REMARK 465     HIS A   143                                                      
REMARK 465     HIS A   144                                                      
REMARK 465     GLY A   145                                                      
REMARK 465     GLY A   146                                                      
REMARK 465     GLU A   147                                                      
REMARK 465     ASN A   148                                                      
REMARK 465     LEU A   149                                                      
REMARK 465     TYR A   150                                                      
REMARK 465     PHE A   151                                                      
REMARK 465     GLN A   152                                                      
REMARK 465     GLY A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     ASN A   155                                                      
REMARK 465     LYS A   156                                                      
REMARK 465     SER A   157                                                      
REMARK 465     LEU A   158                                                      
REMARK 465     GLU A   159                                                      
REMARK 465     VAL A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     ASP A   162                                                      
REMARK 465     THR A   163                                                      
REMARK 465     ARG A   164                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     LYS A   338                                                      
REMARK 465     PHE A   339                                                      
REMARK 465     ALA A   340                                                      
REMARK 465     GLN A   341                                                      
REMARK 465     ALA A   459                                                      
REMARK 465     SER A   460                                                      
REMARK 465     MET B   138                                                      
REMARK 465     HIS B   139                                                      
REMARK 465     HIS B   140                                                      
REMARK 465     HIS B   141                                                      
REMARK 465     HIS B   142                                                      
REMARK 465     HIS B   143                                                      
REMARK 465     HIS B   144                                                      
REMARK 465     GLY B   145                                                      
REMARK 465     GLY B   146                                                      
REMARK 465     GLU B   147                                                      
REMARK 465     ASN B   148                                                      
REMARK 465     LEU B   149                                                      
REMARK 465     TYR B   150                                                      
REMARK 465     PHE B   151                                                      
REMARK 465     GLN B   152                                                      
REMARK 465     GLY B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     ASN B   155                                                      
REMARK 465     LYS B   156                                                      
REMARK 465     SER B   157                                                      
REMARK 465     LEU B   158                                                      
REMARK 465     GLU B   159                                                      
REMARK 465     VAL B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     ASP B   162                                                      
REMARK 465     THR B   163                                                      
REMARK 465     GLU B   337                                                      
REMARK 465     LYS B   338                                                      
REMARK 465     PHE B   339                                                      
REMARK 465     ALA B   340                                                      
REMARK 465     GLN B   341                                                      
REMARK 465     ALA B   459                                                      
REMARK 465     SER B   460                                                      
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     GLN A 228    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 228    CG   CD   OE1  NE2                                  
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    THR B 222   C   -  N   -  CA  ANGL. DEV. =  17.4 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 181       98.43    -60.70                                   
REMARK 500    ASN A 206       56.53     38.67                                   
REMARK 500    ASP A 220      104.60    -33.24                                   
REMARK 500    ARG A 310       -5.91     79.76                                   
REMARK 500    ASP A 311       45.53   -144.52                                   
REMARK 500    ASP A 329       86.68     57.40                                   
REMARK 500    GLU A 406       15.57     56.54                                   
REMARK 500    LYS A 417       38.05    -83.86                                   
REMARK 500    ASP B 181       97.80    -59.55                                   
REMARK 500    ASN B 206     -118.25     64.40                                   
REMARK 500    ASP B 256      -19.57     77.26                                   
REMARK 500    ARG B 310       -3.57     78.72                                   
REMARK 500    ASP B 311       45.54   -146.08                                   
REMARK 500    ASP B 329       85.65     66.57                                   
REMARK 500    GLU B 406       14.94     56.85                                   
REMARK 500    LYS B 417       38.34    -83.76                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A4289        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH A4290        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A4291        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH A4292        DISTANCE =  6.94 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8CG A 4000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8CG B 4000                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UIQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UIR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UIS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UIT   RELATED DB: PDB                                   
DBREF  5UIU A  154   460  UNP    Q9NWZ3   IRAK4_HUMAN    154    460             
DBREF  5UIU B  154   460  UNP    Q9NWZ3   IRAK4_HUMAN    154    460             
SEQADV 5UIU MET A  138  UNP  Q9NWZ3              INITIATING METHIONINE          
SEQADV 5UIU HIS A  139  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU HIS A  140  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU HIS A  141  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU HIS A  142  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU HIS A  143  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU HIS A  144  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU GLY A  145  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU GLY A  146  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU GLU A  147  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU ASN A  148  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU LEU A  149  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU TYR A  150  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU PHE A  151  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU GLN A  152  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU GLY A  153  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU MET B  138  UNP  Q9NWZ3              INITIATING METHIONINE          
SEQADV 5UIU HIS B  139  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU HIS B  140  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU HIS B  141  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU HIS B  142  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU HIS B  143  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU HIS B  144  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU GLY B  145  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU GLY B  146  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU GLU B  147  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU ASN B  148  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU LEU B  149  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU TYR B  150  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU PHE B  151  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU GLN B  152  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQADV 5UIU GLY B  153  UNP  Q9NWZ3              EXPRESSION TAG                 
SEQRES   1 A  323  MET HIS HIS HIS HIS HIS HIS GLY GLY GLU ASN LEU TYR          
SEQRES   2 A  323  PHE GLN GLY GLU ASN LYS SER LEU GLU VAL SER ASP THR          
SEQRES   3 A  323  ARG PHE HIS SER PHE SER PHE TYR GLU LEU LYS ASN VAL          
SEQRES   4 A  323  THR ASN ASN PHE ASP GLU ARG PRO ILE SER VAL GLY GLY          
SEQRES   5 A  323  ASN LYS MET GLY GLU GLY GLY PHE GLY VAL VAL TYR LYS          
SEQRES   6 A  323  GLY TYR VAL ASN ASN THR THR VAL ALA VAL LYS LYS LEU          
SEQRES   7 A  323  ALA ALA MET VAL ASP ILE THR THR GLU GLU LEU LYS GLN          
SEQRES   8 A  323  GLN PHE ASP GLN GLU ILE LYS VAL MET ALA LYS CYS GLN          
SEQRES   9 A  323  HIS GLU ASN LEU VAL GLU LEU LEU GLY PHE SER SER ASP          
SEQRES  10 A  323  GLY ASP ASP LEU CYS LEU VAL TYR VAL TYR MET PRO ASN          
SEQRES  11 A  323  GLY SER LEU LEU ASP ARG LEU SER CYS LEU ASP GLY THR          
SEQRES  12 A  323  PRO PRO LEU SER TRP HIS MET ARG CYS LYS ILE ALA GLN          
SEQRES  13 A  323  GLY ALA ALA ASN GLY ILE ASN PHE LEU HIS GLU ASN HIS          
SEQRES  14 A  323  HIS ILE HIS ARG ASP ILE LYS SER ALA ASN ILE LEU LEU          
SEQRES  15 A  323  ASP GLU ALA PHE THR ALA LYS ILE SER ASP PHE GLY LEU          
SEQRES  16 A  323  ALA ARG ALA SER GLU LYS PHE ALA GLN TPO VAL MET TPO          
SEQRES  17 A  323  SEP ARG ILE VAL GLY THR THR ALA TYR MET ALA PRO GLU          
SEQRES  18 A  323  ALA LEU ARG GLY GLU ILE THR PRO LYS SER ASP ILE TYR          
SEQRES  19 A  323  SER PHE GLY VAL VAL LEU LEU GLU ILE ILE THR GLY LEU          
SEQRES  20 A  323  PRO ALA VAL ASP GLU HIS ARG GLU PRO GLN LEU LEU LEU          
SEQRES  21 A  323  ASP ILE LYS GLU GLU ILE GLU ASP GLU GLU LYS THR ILE          
SEQRES  22 A  323  GLU ASP TYR ILE ASP LYS LYS MET ASN ASP ALA ASP SER          
SEQRES  23 A  323  THR SER VAL GLU ALA MET TYR SER VAL ALA SER GLN CYS          
SEQRES  24 A  323  LEU HIS GLU LYS LYS ASN LYS ARG PRO ASP ILE LYS LYS          
SEQRES  25 A  323  VAL GLN GLN LEU LEU GLN GLU MET THR ALA SER                  
SEQRES   1 B  323  MET HIS HIS HIS HIS HIS HIS GLY GLY GLU ASN LEU TYR          
SEQRES   2 B  323  PHE GLN GLY GLU ASN LYS SER LEU GLU VAL SER ASP THR          
SEQRES   3 B  323  ARG PHE HIS SER PHE SER PHE TYR GLU LEU LYS ASN VAL          
SEQRES   4 B  323  THR ASN ASN PHE ASP GLU ARG PRO ILE SER VAL GLY GLY          
SEQRES   5 B  323  ASN LYS MET GLY GLU GLY GLY PHE GLY VAL VAL TYR LYS          
SEQRES   6 B  323  GLY TYR VAL ASN ASN THR THR VAL ALA VAL LYS LYS LEU          
SEQRES   7 B  323  ALA ALA MET VAL ASP ILE THR THR GLU GLU LEU LYS GLN          
SEQRES   8 B  323  GLN PHE ASP GLN GLU ILE LYS VAL MET ALA LYS CYS GLN          
SEQRES   9 B  323  HIS GLU ASN LEU VAL GLU LEU LEU GLY PHE SER SER ASP          
SEQRES  10 B  323  GLY ASP ASP LEU CYS LEU VAL TYR VAL TYR MET PRO ASN          
SEQRES  11 B  323  GLY SER LEU LEU ASP ARG LEU SER CYS LEU ASP GLY THR          
SEQRES  12 B  323  PRO PRO LEU SER TRP HIS MET ARG CYS LYS ILE ALA GLN          
SEQRES  13 B  323  GLY ALA ALA ASN GLY ILE ASN PHE LEU HIS GLU ASN HIS          
SEQRES  14 B  323  HIS ILE HIS ARG ASP ILE LYS SER ALA ASN ILE LEU LEU          
SEQRES  15 B  323  ASP GLU ALA PHE THR ALA LYS ILE SER ASP PHE GLY LEU          
SEQRES  16 B  323  ALA ARG ALA SER GLU LYS PHE ALA GLN TPO VAL MET TPO          
SEQRES  17 B  323  SEP ARG ILE VAL GLY THR THR ALA TYR MET ALA PRO GLU          
SEQRES  18 B  323  ALA LEU ARG GLY GLU ILE THR PRO LYS SER ASP ILE TYR          
SEQRES  19 B  323  SER PHE GLY VAL VAL LEU LEU GLU ILE ILE THR GLY LEU          
SEQRES  20 B  323  PRO ALA VAL ASP GLU HIS ARG GLU PRO GLN LEU LEU LEU          
SEQRES  21 B  323  ASP ILE LYS GLU GLU ILE GLU ASP GLU GLU LYS THR ILE          
SEQRES  22 B  323  GLU ASP TYR ILE ASP LYS LYS MET ASN ASP ALA ASP SER          
SEQRES  23 B  323  THR SER VAL GLU ALA MET TYR SER VAL ALA SER GLN CYS          
SEQRES  24 B  323  LEU HIS GLU LYS LYS ASN LYS ARG PRO ASP ILE LYS LYS          
SEQRES  25 B  323  VAL GLN GLN LEU LEU GLN GLU MET THR ALA SER                  
MODRES 5UIU TPO A  342  THR  MODIFIED RESIDUE                                   
MODRES 5UIU TPO A  345  THR  MODIFIED RESIDUE                                   
MODRES 5UIU SEP A  346  SER  MODIFIED RESIDUE                                   
MODRES 5UIU TPO B  342  THR  MODIFIED RESIDUE                                   
MODRES 5UIU TPO B  345  THR  MODIFIED RESIDUE                                   
MODRES 5UIU SEP B  346  SER  MODIFIED RESIDUE                                   
HET    TPO  A 342      11                                                       
HET    TPO  A 345      11                                                       
HET    SEP  A 346      10                                                       
HET    TPO  B 342      11                                                       
HET    TPO  B 345      11                                                       
HET    SEP  B 346      10                                                       
HET    8CG  A4000      46                                                       
HET    8CG  B4000      46                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     8CG 1-{[(2S,3S,4S)-3-ETHYL-4-FLUORO-5-OXOPYRROLIDIN-2-               
HETNAM   2 8CG  YL]METHOXY}-7-METHOXYISOQUINOLINE-6-CARBOXAMIDE                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   1  TPO    4(C4 H10 N O6 P)                                             
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  8CG    2(C18 H20 F N3 O4)                                           
FORMUL   5  HOH   *393(H2 O)                                                    
HELIX    1 AA1 SER A  169  THR A  177  1                                   9    
HELIX    2 AA2 PRO A  184  GLY A  188  5                                   5    
HELIX    3 AA3 THR A  222  CYS A  240  1                                  19    
HELIX    4 AA4 SER A  269  CYS A  276  1                                   8    
HELIX    5 AA5 LEU A  277  THR A  280  5                                   4    
HELIX    6 AA6 SER A  284  ASN A  305  1                                  22    
HELIX    7 AA7 LYS A  313  ALA A  315  5                                   3    
HELIX    8 AA8 ALA A  356  ARG A  361  1                                   6    
HELIX    9 AA9 PRO A  366  GLY A  383  1                                  18    
HELIX   10 AB1 LEU A  397  ASP A  405  1                                   9    
HELIX   11 AB2 THR A  409  TYR A  413  5                                   5    
HELIX   12 AB3 ASP A  422  LEU A  437  1                                  16    
HELIX   13 AB4 LYS A  440  ARG A  444  5                                   5    
HELIX   14 AB5 ASP A  446  THR A  458  1                                  13    
HELIX   15 AB6 SER B  169  THR B  177  1                                   9    
HELIX   16 AB7 PRO B  184  GLY B  188  5                                   5    
HELIX   17 AB8 THR B  222  CYS B  240  1                                  19    
HELIX   18 AB9 SER B  269  CYS B  276  1                                   8    
HELIX   19 AC1 LEU B  277  THR B  280  5                                   4    
HELIX   20 AC2 SER B  284  ASN B  305  1                                  22    
HELIX   21 AC3 LYS B  313  ALA B  315  5                                   3    
HELIX   22 AC4 THR B  351  MET B  355  5                                   5    
HELIX   23 AC5 ALA B  356  ARG B  361  1                                   6    
HELIX   24 AC6 THR B  365  GLY B  383  1                                  19    
HELIX   25 AC7 LEU B  395  LEU B  397  5                                   3    
HELIX   26 AC8 ASP B  398  ASP B  405  1                                   8    
HELIX   27 AC9 THR B  409  TYR B  413  5                                   5    
HELIX   28 AD1 ASP B  422  LEU B  437  1                                  16    
HELIX   29 AD2 LYS B  440  ARG B  444  5                                   5    
HELIX   30 AD3 ASP B  446  THR B  458  1                                  13    
SHEET    1 AA1 6 HIS A 166  SER A 167  0                                        
SHEET    2 AA1 6 LEU A 248  SER A 252  1  O  LEU A 249   N  HIS A 166           
SHEET    3 AA1 6 CYS A 259  VAL A 263 -1  O  VAL A 261   N  LEU A 249           
SHEET    4 AA1 6 THR A 208  LEU A 215 -1  N  LYS A 213   O  LEU A 260           
SHEET    5 AA1 6 GLY A 198  VAL A 205 -1  N  TYR A 201   O  VAL A 212           
SHEET    6 AA1 6 LYS A 191  GLY A 195 -1  N  MET A 192   O  VAL A 200           
SHEET    1 AA2 2 HIS A 307  ILE A 308  0                                        
SHEET    2 AA2 2 ARG A 334  ALA A 335 -1  O  ARG A 334   N  ILE A 308           
SHEET    1 AA3 2 ILE A 317  LEU A 319  0                                        
SHEET    2 AA3 2 ALA A 325  ILE A 327 -1  O  LYS A 326   N  LEU A 318           
SHEET    1 AA4 2 VAL A 343  MET A 344  0                                        
SHEET    2 AA4 2 GLU A 363  ILE A 364 -1  O  ILE A 364   N  VAL A 343           
SHEET    1 AA5 6 HIS B 166  SER B 167  0                                        
SHEET    2 AA5 6 LEU B 248  ASP B 254  1  O  LEU B 249   N  HIS B 166           
SHEET    3 AA5 6 ASP B 257  VAL B 263 -1  O  VAL B 261   N  GLY B 250           
SHEET    4 AA5 6 THR B 208  LEU B 215 -1  N  LEU B 215   O  LEU B 258           
SHEET    5 AA5 6 GLY B 198  VAL B 205 -1  N  TYR B 201   O  VAL B 212           
SHEET    6 AA5 6 LYS B 191  GLY B 195 -1  N  MET B 192   O  VAL B 200           
SHEET    1 AA6 2 HIS B 307  ILE B 308  0                                        
SHEET    2 AA6 2 ARG B 334  ALA B 335 -1  O  ARG B 334   N  ILE B 308           
SHEET    1 AA7 2 ILE B 317  LEU B 319  0                                        
SHEET    2 AA7 2 ALA B 325  ILE B 327 -1  O  LYS B 326   N  LEU B 318           
SHEET    1 AA8 2 VAL B 343  MET B 344  0                                        
SHEET    2 AA8 2 GLU B 363  ILE B 364 -1  O  ILE B 364   N  VAL B 343           
LINK         C   TPO A 342                 N   VAL A 343     1555   1555  1.35  
LINK         C   MET A 344                 N   TPO A 345     1555   1555  1.33  
LINK         C   TPO A 345                 N   SEP A 346     1555   1555  1.33  
LINK         C   SEP A 346                 N   ARG A 347     1555   1555  1.35  
LINK         C   TPO B 342                 N   VAL B 343     1555   1555  1.34  
LINK         C   MET B 344                 N   TPO B 345     1555   1555  1.34  
LINK         C   TPO B 345                 N   SEP B 346     1555   1555  1.33  
LINK         C   SEP B 346                 N   ARG B 347     1555   1555  1.35  
CISPEP   1 GLU A  392    PRO A  393          0         1.86                     
CISPEP   2 ILE B  221    THR B  222          0        -7.19                     
CISPEP   3 GLU B  392    PRO B  393          0         1.00                     
SITE     1 AC1 19 MET A 192  GLU A 194  GLY A 195  GLY A 198                    
SITE     2 AC1 19 VAL A 200  ALA A 211  LYS A 213  TYR A 262                    
SITE     3 AC1 19 VAL A 263  TYR A 264  MET A 265  GLY A 268                    
SITE     4 AC1 19 ALA A 315  ASN A 316  LEU A 318  SER A 328                    
SITE     5 AC1 19 ASP A 329  HOH A4129  HOH A4149                               
SITE     1 AC2 19 MET B 192  GLU B 194  GLY B 195  GLY B 198                    
SITE     2 AC2 19 VAL B 200  ALA B 211  LYS B 213  TYR B 262                    
SITE     3 AC2 19 VAL B 263  TYR B 264  MET B 265  GLY B 268                    
SITE     4 AC2 19 ALA B 315  ASN B 316  LEU B 318  SER B 328                    
SITE     5 AC2 19 ASP B 329  HOH B4113  HOH B4175                               
CRYST1   89.940  118.460  138.840  90.00  90.00  90.00 I 2 2 2      16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011119  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008442  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007203        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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