HEADER HYDROLASE/HYDROLASE INHIBITOR 15-JUN-17 5W5J
TITLE IDENTIFICATION OF POTENT AND SELECTIVE RIPK2 INHIBITORS FOR THE
TITLE 2 TREATMENT OF INFLAMMATORY DISEASES
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: RECEPTOR-INTERACTING SERINE/THREONINE-PROTEIN KINASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: CARD-CONTAINING INTERLEUKIN-1 BETA-CONVERTING ENZYME-
COMPND 5 ASSOCIATED KINASE,CARD-CONTAINING IL-1 BETA ICE-KINASE,RIP-LIKE-
COMPND 6 INTERACTING CLARP KINASE,RECEPTOR-INTERACTING PROTEIN 2,RIP-2,
COMPND 7 TYROSINE-PROTEIN KINASE RIPK2;
COMPND 8 EC: 2.7.10.2;
COMPND 9 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: RIPK2, CARDIAK, RICK, RIP2, UNQ277/PRO314/PRO34092;
SOURCE 6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10469;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF9
KEYWDS INHIBITOR, COMPLEX, KINASE, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR A.KREUSCH,G.SPRAGGON
REVDAT 4 03-APR-24 5W5J 1 REMARK
REVDAT 3 13-MAR-24 5W5J 1 REMARK
REVDAT 2 08-NOV-17 5W5J 1 JRNL
REVDAT 1 25-OCT-17 5W5J 0
JRNL AUTH X.HE,S.DA ROS,J.NELSON,X.ZHU,T.JIANG,B.OKRAM,S.JIANG,
JRNL AUTH 2 P.Y.MICHELLYS,M.ISKANDAR,S.ESPINOLA,Y.JIA,B.BURSULAYA,
JRNL AUTH 3 A.KREUSCH,M.Y.GAO,G.SPRAGGON,J.BAATEN,L.CLEMMER,S.MEEUSEN,
JRNL AUTH 4 D.HUANG,R.HILL,V.NGUYEN-TRAN,J.FATHMAN,B.LIU,T.TUNTLAND,
JRNL AUTH 5 P.GORDON,T.HOLLENBECK,K.NG,J.SHI,L.BORDONE,H.LIU
JRNL TITL IDENTIFICATION OF POTENT AND SELECTIVE RIPK2 INHIBITORS FOR
JRNL TITL 2 THE TREATMENT OF INFLAMMATORY DISEASES.
JRNL REF ACS MED CHEM LETT V. 8 1048 2017
JRNL REFN ISSN 1948-5875
JRNL PMID 29057049
JRNL DOI 10.1021/ACSMEDCHEMLETT.7B00258
REMARK 2
REMARK 2 RESOLUTION. 2.85 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) : 2.85
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 46.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 16533
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) : 0.220
REMARK 3 R VALUE (WORKING SET) : 0.217
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.910
REMARK 3 FREE R VALUE TEST SET COUNT : 812
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 : 8
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.05
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.94
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2951
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2333
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2803
REMARK 3 BIN R VALUE (WORKING SET) : 0.2276
REMARK 3 BIN FREE R VALUE : 0.3421
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.02
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 148
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 : 3990
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 53
REMARK 3 SOLVENT ATOMS : 25
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 83.54
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 72.48
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.11060
REMARK 3 B22 (A**2) : -15.80790
REMARK 3 B33 (A**2) : 13.69730
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) : 0.366
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 3.171
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.373
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.379
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 : 0.913
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.869
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4156 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 5678 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1334 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 83 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 601 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4156 ; 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 : 558 ; 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 : 4622 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.16
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.65
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 20.86
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5W5J COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUN-17.
REMARK 100 THE DEPOSITION ID IS D_1000228479.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-AUG-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.0-5.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9765
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16533
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.850
REMARK 200 RESOLUTION RANGE LOW (A) : 46.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : 0.10000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.65000
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: MOLREP
REMARK 200 STARTING MODEL: UNPUBLISHED IN-HOUSE STRUCTURE
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.46
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6M AMMONIUM SULFATE, 0.1M CITRIC
REMARK 280 ACID PH 5.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 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
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 29.10650
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 63.31500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.13200
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 63.31500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 29.10650
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.13200
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3540 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23110 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 ASN A 2
REMARK 465 GLY A 3
REMARK 465 GLU A 4
REMARK 465 ALA A 5
REMARK 465 ILE A 6
REMARK 465 CYS A 7
REMARK 465 SER A 8
REMARK 465 LEU A 49
REMARK 465 HIS A 50
REMARK 465 ILE A 51
REMARK 465 HIS A 52
REMARK 465 THR A 53
REMARK 465 PRO A 54
REMARK 465 LEU A 55
REMARK 465 LEU A 56
REMARK 465 ASP A 57
REMARK 465 SER A 58
REMARK 465 GLU A 59
REMARK 465 ARG A 60
REMARK 465 LYS A 61
REMARK 465 ASP A 62
REMARK 465 VAL A 63
REMARK 465 LEU A 64
REMARK 465 ARG A 65
REMARK 465 GLU A 66
REMARK 465 ALA A 67
REMARK 465 GLU A 68
REMARK 465 GLU A 89
REMARK 465 GLY A 166
REMARK 465 LEU A 167
REMARK 465 SER A 168
REMARK 465 LYS A 169
REMARK 465 TRP A 170
REMARK 465 ARG A 171
REMARK 465 MET A 172
REMARK 465 MET A 173
REMARK 465 SER A 174
REMARK 465 LEU A 175
REMARK 465 SER A 176
REMARK 465 GLN A 177
REMARK 465 SER A 178
REMARK 465 ARG A 179
REMARK 465 SER A 180
REMARK 465 SER A 181
REMARK 465 LYS A 182
REMARK 465 SER A 183
REMARK 465 ALA A 184
REMARK 465 PRO A 185
REMARK 465 GLU A 186
REMARK 465 GLY A 187
REMARK 465 GLY A 188
REMARK 465 GLY A 201
REMARK 465 GLN A 202
REMARK 465 LYS A 203
REMARK 465 SER A 204
REMARK 465 ARG A 205
REMARK 465 ALA A 206
REMARK 465 SER A 207
REMARK 465 LYS A 311
REMARK 465 ASN B 2
REMARK 465 GLY B 3
REMARK 465 GLU B 4
REMARK 465 ALA B 5
REMARK 465 ILE B 6
REMARK 465 CYS B 7
REMARK 465 SER B 8
REMARK 465 ALA B 9
REMARK 465 GLY B 27
REMARK 465 ILE B 51
REMARK 465 HIS B 52
REMARK 465 THR B 53
REMARK 465 PRO B 54
REMARK 465 LEU B 55
REMARK 465 LEU B 56
REMARK 465 ASP B 57
REMARK 465 SER B 58
REMARK 465 GLU B 59
REMARK 465 ARG B 60
REMARK 465 LYS B 61
REMARK 465 LEU B 142
REMARK 465 LEU B 143
REMARK 465 GLY B 166
REMARK 465 LEU B 167
REMARK 465 SER B 168
REMARK 465 LYS B 169
REMARK 465 TRP B 170
REMARK 465 ARG B 171
REMARK 465 MET B 172
REMARK 465 MET B 173
REMARK 465 SER B 174
REMARK 465 LEU B 175
REMARK 465 SER B 176
REMARK 465 GLN B 177
REMARK 465 SER B 178
REMARK 465 ARG B 179
REMARK 465 SER B 180
REMARK 465 SER B 181
REMARK 465 LYS B 182
REMARK 465 SER B 183
REMARK 465 ALA B 184
REMARK 465 PRO B 185
REMARK 465 GLU B 186
REMARK 465 GLY B 187
REMARK 465 GLY B 188
REMARK 465 PRO B 200
REMARK 465 GLY B 201
REMARK 465 GLN B 202
REMARK 465 LYS B 203
REMARK 465 SER B 204
REMARK 465 ARG B 205
REMARK 465 ALA B 206
REMARK 465 SER B 207
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 10 CG CD1 CD2
REMARK 470 ARG A 22 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 26 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 69 CG1 CG2 CD1
REMARK 470 LEU A 70 CG CD1 CD2
REMARK 470 HIS A 71 CG ND1 CD2 CE1 NE2
REMARK 470 LYS A 72 CG CD CE NZ
REMARK 470 GLU A 87 CG CD OE1 OE2
REMARK 470 PHE A 90 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 91 CG CD1 CD2
REMARK 470 GLU A 96 CG CD OE1 OE2
REMARK 470 LEU A 142 CG CD1 CD2
REMARK 470 LEU A 143 CG CD1 CD2
REMARK 470 HIS A 144 CG ND1 CD2 CE1 NE2
REMARK 470 HIS A 145 CG ND1 CD2 CE1 NE2
REMARK 470 ASP A 146 CG OD1 OD2
REMARK 470 GLU A 230 CG CD OE1 OE2
REMARK 470 GLU A 252 CG CD OE1 OE2
REMARK 470 GLU A 253 CG CD OE1 OE2
REMARK 470 ARG A 264 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 21 CG CD1 CD2
REMARK 470 ARG B 26 CG CD NE CZ NH1 NH2
REMARK 470 SER B 29 OG
REMARK 470 HIS B 50 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 62 CG OD1 OD2
REMARK 470 LEU B 64 CG CD1 CD2
REMARK 470 ARG B 65 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 66 CG CD OE1 OE2
REMARK 470 GLU B 68 CG CD OE1 OE2
REMARK 470 LYS B 72 CG CD CE NZ
REMARK 470 ARG B 74 CG CD NE CZ NH1 NH2
REMARK 470 GLU B 89 CG CD OE1 OE2
REMARK 470 HIS B 144 CG ND1 CD2 CE1 NE2
REMARK 470 MET B 193 CG SD CE
REMARK 470 ILE B 208 CG1 CG2 CD1
REMARK 470 LYS B 209 CG CD CE NZ
REMARK 470 HIS B 210 CG ND1 CD2 CE1 NE2
REMARK 470 LYS B 226 CG CD CE NZ
REMARK 470 GLU B 230 CG CD OE1 OE2
REMARK 470 ASP B 231 CG OD1 OD2
REMARK 470 THR B 233 OG1 CG2
REMARK 470 GLU B 252 CG CD OE1 OE2
REMARK 470 GLU B 279 CG CD OE1 OE2
REMARK 470 LEU B 284 CG CD1 CD2
REMARK 470 GLU B 299 CG CD OE1 OE2
REMARK 470 LYS B 310 CG CD CE NZ
REMARK 470 LYS B 311 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 LEU A 21 96.75 -60.65
REMARK 500 ARG A 26 103.90 -167.13
REMARK 500 ALA A 73 93.88 -69.42
REMARK 500 LEU A 142 69.45 -100.51
REMARK 500 HIS A 144 33.51 -76.29
REMARK 500 ALA A 163 58.24 -119.10
REMARK 500 ASP A 164 48.17 -81.72
REMARK 500 LYS A 209 35.31 -86.11
REMARK 500 LEU A 309 27.94 -79.54
REMARK 500 LEU B 21 85.75 -60.99
REMARK 500 ALA B 73 93.33 -68.40
REMARK 500 HIS B 145 -61.78 -106.07
REMARK 500 TYR B 198 -21.58 -144.37
REMARK 500 LYS B 209 34.10 -88.15
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 9WS A 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 9WS B 401
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5W5W RELATED DB: PDB
DBREF 5W5J A 2 311 UNP O43353 RIPK2_HUMAN 2 311
DBREF 5W5J B 2 311 UNP O43353 RIPK2_HUMAN 2 311
SEQRES 1 A 310 ASN GLY GLU ALA ILE CYS SER ALA LEU PRO THR ILE PRO
SEQRES 2 A 310 TYR HIS LYS LEU ALA ASP LEU ARG TYR LEU SER ARG GLY
SEQRES 3 A 310 ALA SER GLY THR VAL SER SER ALA ARG HIS ALA ASP TRP
SEQRES 4 A 310 ARG VAL GLN VAL ALA VAL LYS HIS LEU HIS ILE HIS THR
SEQRES 5 A 310 PRO LEU LEU ASP SER GLU ARG LYS ASP VAL LEU ARG GLU
SEQRES 6 A 310 ALA GLU ILE LEU HIS LYS ALA ARG PHE SER TYR ILE LEU
SEQRES 7 A 310 PRO ILE LEU GLY ILE CYS ASN GLU PRO GLU PHE LEU GLY
SEQRES 8 A 310 ILE VAL THR GLU TYR MET PRO ASN GLY SER LEU ASN GLU
SEQRES 9 A 310 LEU LEU HIS ARG LYS THR GLU TYR PRO ASP VAL ALA TRP
SEQRES 10 A 310 PRO LEU ARG PHE ARG ILE LEU HIS GLU ILE ALA LEU GLY
SEQRES 11 A 310 VAL ASN TYR LEU HIS ASN MET THR PRO PRO LEU LEU HIS
SEQRES 12 A 310 HIS ASP LEU LYS THR GLN ASN ILE LEU LEU ASP ASN GLU
SEQRES 13 A 310 PHE HIS VAL LYS ILE ALA ASP PHE GLY LEU SER LYS TRP
SEQRES 14 A 310 ARG MET MET SER LEU SER GLN SER ARG SER SER LYS SER
SEQRES 15 A 310 ALA PRO GLU GLY GLY THR ILE ILE TYR MET PRO PRO GLU
SEQRES 16 A 310 ASN TYR GLU PRO GLY GLN LYS SER ARG ALA SER ILE LYS
SEQRES 17 A 310 HIS ASP ILE TYR SER TYR ALA VAL ILE THR TRP GLU VAL
SEQRES 18 A 310 LEU SER ARG LYS GLN PRO PHE GLU ASP VAL THR ASN PRO
SEQRES 19 A 310 LEU GLN ILE MET TYR SER VAL SER GLN GLY HIS ARG PRO
SEQRES 20 A 310 VAL ILE ASN GLU GLU SER LEU PRO TYR ASP ILE PRO HIS
SEQRES 21 A 310 ARG ALA ARG MET ILE SER LEU ILE GLU SER GLY TRP ALA
SEQRES 22 A 310 GLN ASN PRO ASP GLU ARG PRO SER PHE LEU LYS CYS LEU
SEQRES 23 A 310 ILE GLU LEU GLU PRO VAL LEU ARG THR PHE GLU GLU ILE
SEQRES 24 A 310 THR PHE LEU GLU ALA VAL ILE GLN LEU LYS LYS
SEQRES 1 B 310 ASN GLY GLU ALA ILE CYS SER ALA LEU PRO THR ILE PRO
SEQRES 2 B 310 TYR HIS LYS LEU ALA ASP LEU ARG TYR LEU SER ARG GLY
SEQRES 3 B 310 ALA SER GLY THR VAL SER SER ALA ARG HIS ALA ASP TRP
SEQRES 4 B 310 ARG VAL GLN VAL ALA VAL LYS HIS LEU HIS ILE HIS THR
SEQRES 5 B 310 PRO LEU LEU ASP SER GLU ARG LYS ASP VAL LEU ARG GLU
SEQRES 6 B 310 ALA GLU ILE LEU HIS LYS ALA ARG PHE SER TYR ILE LEU
SEQRES 7 B 310 PRO ILE LEU GLY ILE CYS ASN GLU PRO GLU PHE LEU GLY
SEQRES 8 B 310 ILE VAL THR GLU TYR MET PRO ASN GLY SER LEU ASN GLU
SEQRES 9 B 310 LEU LEU HIS ARG LYS THR GLU TYR PRO ASP VAL ALA TRP
SEQRES 10 B 310 PRO LEU ARG PHE ARG ILE LEU HIS GLU ILE ALA LEU GLY
SEQRES 11 B 310 VAL ASN TYR LEU HIS ASN MET THR PRO PRO LEU LEU HIS
SEQRES 12 B 310 HIS ASP LEU LYS THR GLN ASN ILE LEU LEU ASP ASN GLU
SEQRES 13 B 310 PHE HIS VAL LYS ILE ALA ASP PHE GLY LEU SER LYS TRP
SEQRES 14 B 310 ARG MET MET SER LEU SER GLN SER ARG SER SER LYS SER
SEQRES 15 B 310 ALA PRO GLU GLY GLY THR ILE ILE TYR MET PRO PRO GLU
SEQRES 16 B 310 ASN TYR GLU PRO GLY GLN LYS SER ARG ALA SER ILE LYS
SEQRES 17 B 310 HIS ASP ILE TYR SER TYR ALA VAL ILE THR TRP GLU VAL
SEQRES 18 B 310 LEU SER ARG LYS GLN PRO PHE GLU ASP VAL THR ASN PRO
SEQRES 19 B 310 LEU GLN ILE MET TYR SER VAL SER GLN GLY HIS ARG PRO
SEQRES 20 B 310 VAL ILE ASN GLU GLU SER LEU PRO TYR ASP ILE PRO HIS
SEQRES 21 B 310 ARG ALA ARG MET ILE SER LEU ILE GLU SER GLY TRP ALA
SEQRES 22 B 310 GLN ASN PRO ASP GLU ARG PRO SER PHE LEU LYS CYS LEU
SEQRES 23 B 310 ILE GLU LEU GLU PRO VAL LEU ARG THR PHE GLU GLU ILE
SEQRES 24 B 310 THR PHE LEU GLU ALA VAL ILE GLN LEU LYS LYS
HET 9WS A 401 19
HET SO4 A 402 5
HET SO4 A 403 5
HET 9WS B 401 19
HET SO4 B 402 5
HETNAM 9WS N-(2-CHLOROPHENYL)PYRAZOLO[1,5-A]PYRIDINE-3-CARBOXAMIDE
HETNAM SO4 SULFATE ION
FORMUL 3 9WS 2(C14 H10 CL N3 O)
FORMUL 4 SO4 3(O4 S 2-)
FORMUL 8 HOH *25(H2 O)
HELIX 1 AA1 PRO A 14 HIS A 16 5 3
HELIX 2 AA2 SER A 102 ARG A 109 1 8
HELIX 3 AA3 ALA A 117 MET A 138 1 22
HELIX 4 AA4 THR A 189 MET A 193 5 5
HELIX 5 AA5 PRO A 194 TYR A 198 5 5
HELIX 6 AA6 LYS A 209 ARG A 225 1 17
HELIX 7 AA7 ASN A 234 GLN A 244 1 11
HELIX 8 AA8 HIS A 261 TRP A 273 1 13
HELIX 9 AA9 ASN A 276 ARG A 280 5 5
HELIX 10 AB1 SER A 282 THR A 296 1 15
HELIX 11 AB2 GLU A 298 LEU A 309 1 12
HELIX 12 AB3 PRO B 14 HIS B 16 5 3
HELIX 13 AB4 VAL B 63 ALA B 73 1 11
HELIX 14 AB5 SER B 102 ARG B 109 1 8
HELIX 15 AB6 ALA B 117 MET B 138 1 22
HELIX 16 AB7 THR B 189 MET B 193 5 5
HELIX 17 AB8 PRO B 194 TYR B 198 5 5
HELIX 18 AB9 LYS B 209 ARG B 225 1 17
HELIX 19 AC1 ASN B 234 GLN B 244 1 11
HELIX 20 AC2 HIS B 261 TRP B 273 1 13
HELIX 21 AC3 ASN B 276 ARG B 280 5 5
HELIX 22 AC4 SER B 282 THR B 296 1 15
HELIX 23 AC5 GLU B 298 GLN B 308 1 11
SHEET 1 AA1 5 LEU A 18 SER A 25 0
SHEET 2 AA1 5 VAL A 32 HIS A 37 -1 O ARG A 36 N ALA A 19
SHEET 3 AA1 5 VAL A 42 LYS A 47 -1 O VAL A 44 N ALA A 35
SHEET 4 AA1 5 ILE A 93 GLU A 96 -1 O THR A 95 N ALA A 45
SHEET 5 AA1 5 ILE A 81 ILE A 84 -1 N GLY A 83 O VAL A 94
SHEET 1 AA2 2 ILE A 152 LEU A 154 0
SHEET 2 AA2 2 VAL A 160 ILE A 162 -1 O LYS A 161 N LEU A 153
SHEET 1 AA3 5 LEU B 18 SER B 25 0
SHEET 2 AA3 5 VAL B 32 HIS B 37 -1 O SER B 34 N ARG B 22
SHEET 3 AA3 5 GLN B 43 HIS B 48 -1 O VAL B 44 N ALA B 35
SHEET 4 AA3 5 LEU B 91 GLU B 96 -1 O THR B 95 N ALA B 45
SHEET 5 AA3 5 ILE B 81 ASN B 86 -1 N CYS B 85 O GLY B 92
SHEET 1 AA4 2 ILE B 152 LEU B 154 0
SHEET 2 AA4 2 VAL B 160 ILE B 162 -1 O LYS B 161 N LEU B 153
CISPEP 1 ARG A 26 GLY A 27 0 6.60
CISPEP 2 THR A 139 PRO A 140 0 1.49
CISPEP 3 LEU B 10 PRO B 11 0 1.68
CISPEP 4 THR B 139 PRO B 140 0 1.18
SITE 1 AC1 9 ALA A 45 VAL A 46 LYS A 47 LEU A 79
SITE 2 AC1 9 ILE A 93 THR A 95 GLU A 96 MET A 98
SITE 3 AC1 9 LEU A 153
SITE 1 AC2 3 LYS A 110 PRO A 114 ARG A 225
SITE 1 AC3 3 HIS A 136 SER A 282 PHE A 283
SITE 1 AC4 11 LEU B 24 VAL B 32 ALA B 45 VAL B 46
SITE 2 AC4 11 LYS B 47 LEU B 79 ILE B 93 THR B 95
SITE 3 AC4 11 GLU B 96 MET B 98 LEU B 153
SITE 1 AC5 3 HIS B 136 SER B 282 PHE B 283
CRYST1 58.213 92.264 126.630 90.00 90.00 90.00 P 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 0.017178 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010838 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007897 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
