HEADER TRANSFERASE/TRANSFERASE INHIBITOR 01-AUG-17 5WNJ
TITLE CRYSTAL STRUCTURE OF MURINE RECEPTOR-INTERACTING PROTEIN KINASE 4
TITLE 2 (RIPK4) D143N IN COMPLEX WITH LESTAURTINIB
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-INTERACTING SERINE/THREONINE-PROTEIN KINASE 4;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 1-342;
COMPND 5 SYNONYM: ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 3,PKC-ASSOCIATED
COMPND 6 PROTEIN KINASE,PKC-REGULATED PROTEIN KINASE;
COMPND 7 EC: 2.7.11.1;
COMPND 8 ENGINEERED: YES;
COMPND 9 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: RIPK4, ANKRD3, PKK;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE, INHIBITOR, COMPLEX, TRANSFERASE, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.S.HUANG,S.G.HYMOWITZ
REVDAT 3 07-DEC-22 5WNJ 1 COMPND FORMUL
REVDAT 2 16-MAY-18 5WNJ 1 JRNL
REVDAT 1 09-MAY-18 5WNJ 0
JRNL AUTH C.S.HUANG,N.OBERBECK,Y.C.HSIAO,P.LIU,A.R.JOHNSON,V.M.DIXIT,
JRNL AUTH 2 S.G.HYMOWITZ
JRNL TITL CRYSTAL STRUCTURE OF RIPK4 REVEALS DIMERIZATION-DEPENDENT
JRNL TITL 2 KINASE ACTIVITY.
JRNL REF STRUCTURE V. 26 767 2018
JRNL REFN ISSN 1878-4186
JRNL PMID 29706531
JRNL DOI 10.1016/J.STR.2018.04.002
REMARK 2
REMARK 2 RESOLUTION. 2.55 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0158
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.01
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 17877
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) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.220
REMARK 3 FREE R VALUE : 0.252
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.900
REMARK 3 FREE R VALUE TEST SET COUNT : 912
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.55
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.62
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1253
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.22
REMARK 3 BIN R VALUE (WORKING SET) : 0.3070
REMARK 3 BIN FREE R VALUE SET COUNT : 69
REMARK 3 BIN FREE R VALUE : 0.3180
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2042
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 34
REMARK 3 SOLVENT ATOMS : 24
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 63.23
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.98000
REMARK 3 B22 (A**2) : 1.05000
REMARK 3 B33 (A**2) : -4.03000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.269
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.225
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.170
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.865
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.940
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2137 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 1942 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2917 ; 1.232 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 4481 ; 0.907 ; 2.988
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 261 ; 5.643 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 84 ;32.958 ;22.857
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 336 ;12.721 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 13 ;18.582 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 320 ; 0.068 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2361 ; 0.006 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 440 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1053 ; 3.195 ; 6.662
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1052 ; 3.176 ; 6.658
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1311 ; 5.122 ; 9.967
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 1312 ; 5.120 ; 9.973
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1084 ; 2.999 ; 6.579
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1085 ; 2.998 ; 6.579
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 1607 ; 4.816 ; 9.770
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 2343 ; 7.139 ;73.874
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 2344 ; 7.137 ;73.857
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5WNJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-AUG-17.
REMARK 100 THE DEPOSITION ID IS D_1000229188.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-JUN-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : NULL
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18791
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550
REMARK 200 RESOLUTION RANGE LOW (A) : 50.010
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.08300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 19.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 66.24
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.64
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 0.2M MAGNESIUM
REMARK 280 CHLORIDE, 10% 2-PROPANOL, 15% ETHYLENE GLYCOL, 10% PEG4000,
REMARK 280 MICROBATCH, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z+1/2
REMARK 290 6555 -X,-Y+1/2,Z
REMARK 290 7555 -X+1/2,Y,-Z
REMARK 290 8555 X,-Y,-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 35.41250
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 72.76800
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.12350
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 72.76800
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 35.41250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.12350
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 35.41250
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 55.12350
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 72.76800
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 55.12350
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 35.41250
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 72.76800
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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL
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 BIOMT1 2 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 -72.76800
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 1
REMARK 465 GLU A 2
REMARK 465 GLY A 3
REMARK 465 GLU A 4
REMARK 465 GLY A 5
REMARK 465 ARG A 6
REMARK 465 GLY A 7
REMARK 465 ARG A 8
REMARK 465 TRP A 9
REMARK 465 GLY A 31
REMARK 465 GLY A 32
REMARK 465 ASN A 168
REMARK 465 GLY A 169
REMARK 465 MET A 170
REMARK 465 SER A 171
REMARK 465 HIS A 172
REMARK 465 SER A 173
REMARK 465 HIS A 174
REMARK 465 ASP A 175
REMARK 465 LEU A 176
REMARK 465 SER A 177
REMARK 465 MET A 178
REMARK 465 ASP A 179
REMARK 465 GLY A 180
REMARK 465 LEU A 181
REMARK 465 PRO A 290
REMARK 465 ASP A 291
REMARK 465 GLU A 292
REMARK 465 GLU A 293
REMARK 465 VAL A 294
REMARK 465 LYS A 295
REMARK 465 ASP A 296
REMARK 465 LEU A 297
REMARK 465 ALA A 298
REMARK 465 HIS A 299
REMARK 465 GLU A 300
REMARK 465 PRO A 301
REMARK 465 GLY A 302
REMARK 465 GLU A 303
REMARK 465 LYS A 304
REMARK 465 SER A 305
REMARK 465 SER A 306
REMARK 465 LEU A 307
REMARK 465 GLU A 308
REMARK 465 SER A 309
REMARK 465 LYS A 310
REMARK 465 SER A 311
REMARK 465 GLU A 312
REMARK 465 ALA A 313
REMARK 465 ARG A 314
REMARK 465 PRO A 315
REMARK 465 GLU A 316
REMARK 465 SER A 317
REMARK 465 SER A 318
REMARK 465 ARG A 319
REMARK 465 LEU A 320
REMARK 465 LYS A 321
REMARK 465 ARG A 322
REMARK 465 ALA A 323
REMARK 465 SER A 324
REMARK 465 ALA A 325
REMARK 465 PRO A 326
REMARK 465 PRO A 327
REMARK 465 PHE A 328
REMARK 465 ASP A 329
REMARK 465 ASN A 330
REMARK 465 ASP A 331
REMARK 465 CYS A 332
REMARK 465 SER A 333
REMARK 465 LEU A 334
REMARK 465 SER A 335
REMARK 465 GLU A 336
REMARK 465 LEU A 337
REMARK 465 LEU A 338
REMARK 465 SER A 339
REMARK 465 GLN A 340
REMARK 465 LEU A 341
REMARK 465 ASP A 342
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 LEU A 11 CG CD1 CD2
REMARK 470 LYS A 27 CD CE NZ
REMARK 470 PHE A 33 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 GLN A 35 CG CD OE1 NE2
REMARK 470 LEU A 56 CG CD1 CD2
REMARK 470 HIS A 57 CG ND1 CD2 CE1 NE2
REMARK 470 VAL A 58 CG1 CG2
REMARK 470 ARG A 61 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 63 CG CD NE CZ NH1 NH2
REMARK 470 MET A 64 CE
REMARK 470 GLU A 68 CG CD OE1 OE2
REMARK 470 LYS A 71 CD CE NZ
REMARK 470 GLU A 74 CD OE1 OE2
REMARK 470 LYS A 77 CD CE NZ
REMARK 470 GLU A 90 CG CD OE1 OE2
REMARK 470 LYS A 106 CE NZ
REMARK 470 SER A 136 OG
REMARK 470 LYS A 145 NZ
REMARK 470 PHE A 182 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ILE A 185 CG1 CG2 CD1
REMARK 470 LYS A 196 CG CD CE NZ
REMARK 470 LYS A 227 CG CD CE NZ
REMARK 470 ILE A 229 CG1 CG2 CD1
REMARK 470 MET A 233 CG SD CE
REMARK 470 LYS A 235 CG CD CE NZ
REMARK 470 ARG A 253 CZ NH1 NH2
REMARK 470 GLU A 288 CG CD OE1 OE2
REMARK 470 LYS A 289 CG CD CE NZ
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 GLU A 90 -72.69 -54.07
REMARK 500 ASP A 161 84.85 60.62
REMARK 500 SER A 197 76.87 39.99
REMARK 500 LYS A 227 -75.26 -73.98
REMARK 500 GLU A 288 77.85 -68.95
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLU A 90 PRO A 91 146.81
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 2V9 A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5WNI RELATED DB: PDB
REMARK 900 RELATED ID: 5WNK RELATED DB: PDB
REMARK 900 RELATED ID: 5WNL RELATED DB: PDB
REMARK 900 RELATED ID: 5WNM RELATED DB: PDB
DBREF 5WNJ A 1 342 UNP Q9ERK0 RIPK4_MOUSE 1 342
SEQADV 5WNJ ASN A 143 UNP Q9ERK0 ASP 143 ENGINEERED MUTATION
SEQRES 1 A 342 MET GLU GLY GLU GLY ARG GLY ARG TRP ALA LEU GLY LEU
SEQRES 2 A 342 LEU ARG THR PHE ASP ALA GLY GLU PHE ALA GLY TRP GLU
SEQRES 3 A 342 LYS VAL GLY SER GLY GLY PHE GLY GLN VAL TYR LYS VAL
SEQRES 4 A 342 ARG HIS VAL HIS TRP LYS THR TRP LEU ALA ILE LYS CYS
SEQRES 5 A 342 SER PRO SER LEU HIS VAL ASP ASP ARG GLU ARG MET GLU
SEQRES 6 A 342 LEU LEU GLU GLU ALA LYS LYS MET GLU MET ALA LYS PHE
SEQRES 7 A 342 ARG TYR ILE LEU PRO VAL TYR GLY ILE CYS GLN GLU PRO
SEQRES 8 A 342 VAL GLY LEU VAL MET GLU TYR MET GLU THR GLY SER LEU
SEQRES 9 A 342 GLU LYS LEU LEU ALA SER GLU PRO LEU PRO TRP ASP LEU
SEQRES 10 A 342 ARG PHE ARG ILE VAL HIS GLU THR ALA VAL GLY MET ASN
SEQRES 11 A 342 PHE LEU HIS CYS MET SER PRO PRO LEU LEU HIS LEU ASN
SEQRES 12 A 342 LEU LYS PRO ALA ASN ILE LEU LEU ASP ALA HIS TYR HIS
SEQRES 13 A 342 VAL LYS ILE SER ASP PHE GLY LEU ALA LYS CYS ASN GLY
SEQRES 14 A 342 MET SER HIS SER HIS ASP LEU SER MET ASP GLY LEU PHE
SEQRES 15 A 342 GLY THR ILE ALA TYR LEU PRO PRO GLU ARG ILE ARG GLU
SEQRES 16 A 342 LYS SER ARG LEU PHE ASP THR LYS HIS ASP VAL TYR SER
SEQRES 17 A 342 PHE ALA ILE VAL ILE TRP GLY VAL LEU THR GLN LYS LYS
SEQRES 18 A 342 PRO PHE ALA ASP GLU LYS ASN ILE LEU HIS ILE MET MET
SEQRES 19 A 342 LYS VAL VAL LYS GLY HIS ARG PRO GLU LEU PRO PRO ILE
SEQRES 20 A 342 CYS ARG PRO ARG PRO ARG ALA CYS ALA SER LEU ILE GLY
SEQRES 21 A 342 LEU MET GLN ARG CYS TRP HIS ALA ASP PRO GLN VAL ARG
SEQRES 22 A 342 PRO THR PHE GLN GLU ILE THR SER GLU THR GLU ASP LEU
SEQRES 23 A 342 CYS GLU LYS PRO ASP GLU GLU VAL LYS ASP LEU ALA HIS
SEQRES 24 A 342 GLU PRO GLY GLU LYS SER SER LEU GLU SER LYS SER GLU
SEQRES 25 A 342 ALA ARG PRO GLU SER SER ARG LEU LYS ARG ALA SER ALA
SEQRES 26 A 342 PRO PRO PHE ASP ASN ASP CYS SER LEU SER GLU LEU LEU
SEQRES 27 A 342 SER GLN LEU ASP
HET 2V9 A 401 33
HET CL A 402 1
HETNAM 2V9 LESTAURTINIB
HETNAM CL CHLORIDE ION
HETSYN 2V9 (5S,6S,8R)-6-HYDROXY-6-(HYDROXYMETHYL)-5-METHYL-5,6,7,
HETSYN 2 2V9 8-TETRAHYDRO-13H-5,8-EPOXY-4B,8A,14-TRIAZADIBENZO[B,
HETSYN 3 2V9 H]CYCLOOCTA[1,2,3,4-JKL]CYCLOPENTA[E]-AS-INDACEN-13-
HETSYN 4 2V9 ONE
FORMUL 2 2V9 C26 H21 N3 O4
FORMUL 3 CL CL 1-
FORMUL 4 HOH *24(H2 O)
HELIX 1 AA1 ASP A 18 GLY A 20 5 3
HELIX 2 AA2 ASP A 59 ALA A 76 1 18
HELIX 3 AA3 LEU A 104 GLU A 111 1 8
HELIX 4 AA4 PRO A 114 MET A 135 1 22
HELIX 5 AA5 LYS A 145 ALA A 147 5 3
HELIX 6 AA6 PHE A 182 LEU A 188 5 7
HELIX 7 AA7 PRO A 189 GLU A 195 1 7
HELIX 8 AA8 ASP A 201 GLN A 219 1 19
HELIX 9 AA9 ASN A 228 LYS A 238 1 11
HELIX 10 AB1 ARG A 251 TRP A 266 1 16
HELIX 11 AB2 ASP A 269 ARG A 273 5 5
HELIX 12 AB3 THR A 275 GLU A 288 1 14
SHEET 1 AA1 6 ARG A 15 PHE A 17 0
SHEET 2 AA1 6 VAL A 84 CYS A 88 1 O ILE A 87 N PHE A 17
SHEET 3 AA1 6 GLY A 93 GLU A 97 -1 O VAL A 95 N GLY A 86
SHEET 4 AA1 6 THR A 46 CYS A 52 -1 N ALA A 49 O MET A 96
SHEET 5 AA1 6 VAL A 36 HIS A 41 -1 N VAL A 39 O LEU A 48
SHEET 6 AA1 6 PHE A 22 LYS A 27 -1 N ALA A 23 O ARG A 40
SHEET 1 AA2 3 GLY A 102 SER A 103 0
SHEET 2 AA2 3 ILE A 149 LEU A 151 -1 O LEU A 151 N GLY A 102
SHEET 3 AA2 3 VAL A 157 ILE A 159 -1 O LYS A 158 N LEU A 150
CISPEP 1 SER A 136 PRO A 137 0 -5.96
SITE 1 AC1 11 VAL A 28 GLY A 29 ALA A 49 LEU A 82
SITE 2 AC1 11 GLU A 97 TYR A 98 MET A 99 GLY A 102
SITE 3 AC1 11 ALA A 147 LEU A 150 SER A 160
SITE 1 AC2 3 ARG A 251 ARG A 253 ALA A 254
CRYST1 70.825 110.247 145.536 90.00 90.00 90.00 I 21 21 21 8
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 0.014119 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009071 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006871 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
