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