HEADER TRANSFERASE 14-JAN-17 5UIT
TITLE CRYSTAL STRUCTURE OF IRAK4 IN COMPLEX WITH COMPOUND 14
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 IRAK4, KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR S.HAN,J.S.CHANG
REVDAT 2 26-JUL-17 5UIT 1 JRNL
REVDAT 1 24-MAY-17 5UIT 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. 1.84 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.9.6
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) : 1.84
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 59.29
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.7
REMARK 3 NUMBER OF REFLECTIONS : 59027
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.218
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100
REMARK 3 FREE R VALUE TEST SET COUNT : 3010
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) : 1.84
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.89
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 89.73
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 692
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2374
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 655
REMARK 3 BIN R VALUE (WORKING SET) : 0.2367
REMARK 3 BIN FREE R VALUE : 0.2502
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.35
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 37
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 : 4502
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 454
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 31.51
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.71
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.43550
REMARK 3 B22 (A**2) : -3.66390
REMARK 3 B33 (A**2) : 4.09940
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) : 0.245
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.129
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.123
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.124
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.121
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 : 0.955
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.941
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4672 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6344 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1660 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 133 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 699 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4672 ; 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 : 604 ; 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 : 43 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.02
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.94
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.05
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): -27.7729 -31.9794 14.9603
REMARK 3 T TENSOR
REMARK 3 T11: -0.1009 T22: -0.0557
REMARK 3 T33: -0.1295 T12: -0.0372
REMARK 3 T13: 0.0234 T23: 0.0022
REMARK 3 L TENSOR
REMARK 3 L11: 1.7604 L22: 3.0590
REMARK 3 L33: 1.2170 L12: 1.2812
REMARK 3 L13: -0.0041 L23: 0.4836
REMARK 3 S TENSOR
REMARK 3 S11: 0.2457 S12: -0.2188 S13: -0.0411
REMARK 3 S21: 0.3773 S22: -0.2721 S23: 0.1966
REMARK 3 S31: 0.0303 S32: -0.1433 S33: 0.0264
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): -12.0115 -25.1071 -16.0182
REMARK 3 T TENSOR
REMARK 3 T11: -0.0658 T22: -0.0590
REMARK 3 T33: -0.1518 T12: 0.0187
REMARK 3 T13: -0.0198 T23: -0.0091
REMARK 3 L TENSOR
REMARK 3 L11: 1.5231 L22: 2.2039
REMARK 3 L33: 1.4019 L12: -0.6437
REMARK 3 L13: -0.0963 L23: 0.2653
REMARK 3 S TENSOR
REMARK 3 S11: 0.2005 S12: 0.1756 S13: -0.0247
REMARK 3 S21: -0.2806 S22: -0.1508 S23: 0.1245
REMARK 3 S31: -0.0559 S32: -0.0800 S33: -0.0496
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5UIT 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_1000225939.
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 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 59046
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.840
REMARK 200 RESOLUTION RANGE LOW (A) : 90.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.2
REMARK 200 DATA REDUNDANCY : 5.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.8000
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 (%): 52.39
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6-1.8 M 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 45.57000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 59.29000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 69.81500
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.57000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 59.29000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.81500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.57000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 59.29000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.81500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.57000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 59.29000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 69.81500
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 ALA A 216
REMARK 465 ALA A 217
REMARK 465 MET A 218
REMARK 465 VAL A 219
REMARK 465 ASP A 220
REMARK 465 ILE A 221
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 ALA B 217
REMARK 465 MET B 218
REMARK 465 VAL B 219
REMARK 465 ASP B 220
REMARK 465 ILE B 221
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: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 OE2 GLU B 402 OH TYR B 413 2.07
REMARK 500 O HOH A 637 O HOH A 763 2.09
REMARK 500 O HOH A 617 O HOH A 685 2.14
REMARK 500 O HOH B 688 O HOH B 797 2.15
REMARK 500 O HOH A 704 O HOH A 770 2.17
REMARK 500 O HOH A 670 O HOH A 735 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 OE2 GLU B 172 OE2 GLU B 172 4555 1.50
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 THR A 223 -96.13 81.67
REMARK 500 ARG A 310 -8.98 75.95
REMARK 500 ASP A 311 48.90 -140.97
REMARK 500 ASP A 329 85.43 65.21
REMARK 500 HIS A 390 10.34 -67.67
REMARK 500 LYS A 417 41.40 -86.35
REMARK 500 ASN B 206 -101.44 61.39
REMARK 500 THR B 223 -102.03 91.26
REMARK 500 ASP B 256 -155.98 84.71
REMARK 500 ARG B 310 -4.01 75.87
REMARK 500 ASP B 311 48.65 -147.81
REMARK 500 ASP B 329 83.22 70.00
REMARK 500 ASP B 405 31.09 -89.09
REMARK 500 GLU B 406 -175.28 38.67
REMARK 500 GLU B 407 -27.29 111.84
REMARK 500 LYS B 417 41.14 -85.16
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 A 833 DISTANCE = 6.54 ANGSTROMS
REMARK 525 HOH A 834 DISTANCE = 6.70 ANGSTROMS
REMARK 525 HOH B 819 DISTANCE = 6.01 ANGSTROMS
REMARK 525 HOH B 820 DISTANCE = 6.54 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8CD A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 8CD B 501
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: 5UIU RELATED DB: PDB
DBREF 5UIT A 154 460 UNP Q9NWZ3 IRAK4_HUMAN 154 460
DBREF 5UIT B 154 460 UNP Q9NWZ3 IRAK4_HUMAN 154 460
SEQADV 5UIT MET A 138 UNP Q9NWZ3 INITIATING METHIONINE
SEQADV 5UIT HIS A 139 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT HIS A 140 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT HIS A 141 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT HIS A 142 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT HIS A 143 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT HIS A 144 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT GLY A 145 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT GLY A 146 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT GLU A 147 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT ASN A 148 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT LEU A 149 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT TYR A 150 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT PHE A 151 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT GLN A 152 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT GLY A 153 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT MET B 138 UNP Q9NWZ3 INITIATING METHIONINE
SEQADV 5UIT HIS B 139 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT HIS B 140 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT HIS B 141 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT HIS B 142 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT HIS B 143 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT HIS B 144 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT GLY B 145 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT GLY B 146 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT GLU B 147 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT ASN B 148 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT LEU B 149 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT TYR B 150 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT PHE B 151 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT GLN B 152 UNP Q9NWZ3 EXPRESSION TAG
SEQADV 5UIT 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 THR 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 THR 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 5UIT TPO A 345 THR MODIFIED RESIDUE
MODRES 5UIT SEP A 346 SER MODIFIED RESIDUE
MODRES 5UIT TPO B 345 THR MODIFIED RESIDUE
MODRES 5UIT SEP B 346 SER MODIFIED RESIDUE
HET TPO A 345 11
HET SEP A 346 10
HET TPO B 345 11
HET SEP B 346 10
HET 8CD A 501 46
HET 8CD B 501 46
HETNAM TPO PHOSPHOTHREONINE
HETNAM SEP PHOSPHOSERINE
HETNAM 8CD 1-{[(2S)-5-OXOPYRROLIDIN-2-YL]METHOXY}-7-[(PROPAN-2-
HETNAM 2 8CD YL)OXY]ISOQUINOLINE-6-CARBOXAMIDE
HETSYN TPO PHOSPHONOTHREONINE
HETSYN SEP PHOSPHONOSERINE
FORMUL 1 TPO 2(C4 H10 N O6 P)
FORMUL 1 SEP 2(C3 H8 N O6 P)
FORMUL 3 8CD 2(C18 H21 N3 O4)
FORMUL 5 HOH *454(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 223 CYS A 240 1 18
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 THR A 351 MET A 355 5 5
HELIX 9 AA9 ALA A 356 ARG A 361 1 6
HELIX 10 AB1 PRO A 366 GLY A 383 1 18
HELIX 11 AB2 LEU A 395 LEU A 397 5 3
HELIX 12 AB3 ASP A 398 ASP A 405 1 8
HELIX 13 AB4 THR A 409 ILE A 414 1 6
HELIX 14 AB5 ASP A 422 LEU A 437 1 16
HELIX 15 AB6 LYS A 440 ARG A 444 5 5
HELIX 16 AB7 ASP A 446 THR A 458 1 13
HELIX 17 AB8 SER B 169 THR B 177 1 9
HELIX 18 AB9 PRO B 184 GLY B 188 5 5
HELIX 19 AC1 THR B 223 CYS B 240 1 18
HELIX 20 AC2 SER B 269 CYS B 276 1 8
HELIX 21 AC3 LEU B 277 THR B 280 5 4
HELIX 22 AC4 SER B 284 ASN B 305 1 22
HELIX 23 AC5 LYS B 313 ALA B 315 5 3
HELIX 24 AC6 THR B 351 MET B 355 5 5
HELIX 25 AC7 ALA B 356 ARG B 361 1 6
HELIX 26 AC8 THR B 365 GLY B 383 1 19
HELIX 27 AC9 LEU B 395 LEU B 397 5 3
HELIX 28 AD1 ASP B 398 ASP B 405 1 8
HELIX 29 AD2 THR B 409 ILE B 414 1 6
HELIX 30 AD3 ASP B 422 LEU B 437 1 16
HELIX 31 AD4 LYS B 440 ARG B 444 5 5
HELIX 32 AD5 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 LYS A 214 -1 N LYS A 213 O LEU A 260
SHEET 5 AA1 6 VAL A 199 VAL A 205 -1 N TYR A 201 O VAL A 212
SHEET 6 AA1 6 LYS A 191 GLU A 194 -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 SER B 253 1 O LEU B 249 N HIS B 166
SHEET 3 AA5 6 LEU B 258 VAL B 263 -1 O VAL B 261 N LEU B 249
SHEET 4 AA5 6 THR B 208 LEU B 215 -1 N LYS B 213 O LEU B 260
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 GLU B 194 -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 MET A 344 N TPO A 345 1555 1555 1.33
LINK C TPO A 345 N SEP A 346 1555 1555 1.34
LINK C SEP A 346 N ARG A 347 1555 1555 1.34
LINK C MET B 344 N TPO B 345 1555 1555 1.33
LINK C TPO B 345 N SEP B 346 1555 1555 1.34
LINK C SEP B 346 N ARG B 347 1555 1555 1.35
CISPEP 1 GLU A 392 PRO A 393 0 -2.69
CISPEP 2 GLU B 392 PRO B 393 0 -2.26
SITE 1 AC1 13 MET A 192 GLU A 194 ALA A 211 TYR A 262
SITE 2 AC1 13 VAL A 263 TYR A 264 MET A 265 ALA A 315
SITE 3 AC1 13 ASN A 316 LEU A 318 SER A 328 HOH A 629
SITE 4 AC1 13 HOH A 675
SITE 1 AC2 13 MET B 192 GLU B 194 ALA B 211 TYR B 262
SITE 2 AC2 13 VAL B 263 TYR B 264 MET B 265 ALA B 315
SITE 3 AC2 13 ASN B 316 LEU B 318 SER B 328 HOH B 612
SITE 4 AC2 13 HOH B 643
CRYST1 91.140 118.580 139.630 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 0.010972 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008433 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007162 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
