HEADER TRANSFERASE/TRANSFERASE INHIBITOR 09-AUG-12 4GJ2
TITLE TYK2 (JH1) IN COMPLEX WITH 2,6-DICHLORO-N-[2-({[(1R,2R)-2-
TITLE 2 FLUOROCYCLOPROPYL]CARBONYL}AMINO)PYRIDIN-4-YL]BENZAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-RECEPTOR TYROSINE-PROTEIN KINASE TYK2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN, UNP RESIDUES 696-1022;
COMPND 5 EC: 2.7.10.2;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TYK2 GENE;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE, ATP BINDING, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR M.H.ULTSCH
REVDAT 3 13-SEP-23 4GJ2 1 REMARK SEQADV
REVDAT 2 26-JUN-13 4GJ2 1 JRNL
REVDAT 1 29-MAY-13 4GJ2 0
JRNL AUTH J.LIANG,A.VAN ABBEMA,M.BALAZS,K.BARRETT,L.BEREZHKOVSKY,
JRNL AUTH 2 W.BLAIR,C.CHANG,D.DELAROSA,J.DEVOSS,J.DRISCOLL,C.EIGENBROT,
JRNL AUTH 3 N.GHILARDI,P.GIBBONS,J.HALLADAY,A.JOHNSON,P.B.KOHLI,Y.LAI,
JRNL AUTH 4 Y.LIU,J.LYSSIKATOS,P.MANTIK,K.MENGHRAJANI,J.MURRAY,I.PENG,
JRNL AUTH 5 A.SAMBRONE,S.SHIA,Y.SHIN,J.SMITH,S.SOHN,V.TSUI,M.ULTSCH,
JRNL AUTH 6 L.C.WU,Y.XIAO,W.YANG,J.YOUNG,B.ZHANG,B.Y.ZHU,S.MAGNUSON
JRNL TITL LEAD OPTIMIZATION OF A 4-AMINOPYRIDINE BENZAMIDE SCAFFOLD TO
JRNL TITL 2 IDENTIFY POTENT, SELECTIVE, AND ORALLY BIOAVAILABLE TYK2
JRNL TITL 3 INHIBITORS.
JRNL REF J.MED.CHEM. V. 56 4521 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23668484
JRNL DOI 10.1021/JM400266T
REMARK 2
REMARK 2 RESOLUTION. 2.40 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) : 2.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.04
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 11448
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) : 0.198
REMARK 3 R VALUE (WORKING SET) : 0.195
REMARK 3 FREE R VALUE : 0.237
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 8.050
REMARK 3 FREE R VALUE TEST SET COUNT : 596
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 : 6
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.63
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.86
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2603
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2212
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2416
REMARK 3 BIN R VALUE (WORKING SET) : 0.2188
REMARK 3 BIN FREE R VALUE : 0.2526
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 7.18
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 187
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 : 2335
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 24
REMARK 3 SOLVENT ATOMS : 94
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 47.22
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 42.82
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.94540
REMARK 3 B22 (A**2) : 1.33740
REMARK 3 B33 (A**2) : -2.28280
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) : 0.313
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.576
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.888
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 2425 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 3288 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 835 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 53 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 353 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 2425 ; 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 : 295 ; 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 : 2762 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.007
REMARK 3 BOND ANGLES (DEGREES) : 1.00
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.41
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.94
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|890 - A|916 }
REMARK 3 ORIGIN FOR THE GROUP (A): -4.5871 -16.2749 -8.6795
REMARK 3 T TENSOR
REMARK 3 T11: -0.0236 T22: -0.1207
REMARK 3 T33: -0.1248 T12: 0.0508
REMARK 3 T13: -0.0002 T23: 0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 3.8716 L22: 0.7797
REMARK 3 L33: 4.6384 L12: -0.6337
REMARK 3 L13: 1.1497 L23: -0.2404
REMARK 3 S TENSOR
REMARK 3 S11: 0.0312 S12: -0.2396 S13: 0.0546
REMARK 3 S21: 0.0762 S22: 0.0937 S23: -0.1224
REMARK 3 S31: 0.0252 S32: 0.0045 S33: -0.1248
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|917 - A|1017 }
REMARK 3 ORIGIN FOR THE GROUP (A): -11.8296 -7.2120 -11.5627
REMARK 3 T TENSOR
REMARK 3 T11: -0.0494 T22: -0.0982
REMARK 3 T33: -0.0826 T12: -0.0358
REMARK 3 T13: -0.0066 T23: 0.0281
REMARK 3 L TENSOR
REMARK 3 L11: 1.1374 L22: 2.3333
REMARK 3 L33: 1.9899 L12: -0.9690
REMARK 3 L13: 0.3662 L23: -0.5481
REMARK 3 S TENSOR
REMARK 3 S11: 0.0134 S12: -0.2191 S13: -0.0494
REMARK 3 S21: 0.3277 S22: 0.1217 S23: 0.0898
REMARK 3 S31: 0.1671 S32: 0.0819 S33: -0.1352
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|1018 - A|1076 }
REMARK 3 ORIGIN FOR THE GROUP (A): -10.5446 7.1988 -11.9761
REMARK 3 T TENSOR
REMARK 3 T11: -0.0756 T22: -0.0219
REMARK 3 T33: -0.0847 T12: 0.0143
REMARK 3 T13: -0.0065 T23: 0.0190
REMARK 3 L TENSOR
REMARK 3 L11: 1.9569 L22: 5.0894
REMARK 3 L33: 1.1752 L12: 0.5150
REMARK 3 L13: -0.7268 L23: 0.0932
REMARK 3 S TENSOR
REMARK 3 S11: 0.0010 S12: -0.1880 S13: 0.1631
REMARK 3 S21: 0.3091 S22: -0.0004 S23: 0.0443
REMARK 3 S31: -0.1066 S32: 0.0958 S33: -0.0006
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|1077 - A|1177 }
REMARK 3 ORIGIN FOR THE GROUP (A): -12.9656 12.7102 -24.7836
REMARK 3 T TENSOR
REMARK 3 T11: -0.0548 T22: -0.0631
REMARK 3 T33: -0.0573 T12: 0.0083
REMARK 3 T13: 0.0158 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 1.8555 L22: 1.0437
REMARK 3 L33: 0.3777 L12: -0.3016
REMARK 3 L13: 0.4207 L23: -0.0824
REMARK 3 S TENSOR
REMARK 3 S11: 0.0197 S12: 0.0796 S13: 0.1124
REMARK 3 S21: -0.0493 S22: -0.0691 S23: 0.1009
REMARK 3 S31: -0.0227 S32: 0.0145 S33: 0.0494
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4GJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-AUG-12.
REMARK 100 THE DEPOSITION ID IS D_1000074245.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-APR-12
REMARK 200 TEMPERATURE (KELVIN) : 173
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97
REMARK 200 MONOCHROMATOR : SIDE SCATTERING BENT CUBE-ROOT I
REMARK 200 -BEAM SINGLE CRYSTAL; ASYMMETRIC
REMARK 200 CUT 4.965 DEGS
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 11482
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 37.040
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.8
REMARK 200 DATA REDUNDANCY : 4.000
REMARK 200 R MERGE (I) : 0.09000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 13.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.53
REMARK 200 COMPLETENESS FOR SHELL (%) : 98.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.10
REMARK 200 R MERGE FOR SHELL (I) : 0.48900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: 3NZ0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 39.77
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-25%(W/V) PEG3350 AND 0.2M MG
REMARK 280 SULFATE, 0.1M MES PH6.5, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K
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 18.07450
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 53.00450
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.03850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 53.00450
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.07450
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.03850
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: 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 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 882
REMARK 465 GLY A 883
REMARK 465 SER A 884
REMARK 465 PRO A 885
REMARK 465 ALA A 886
REMARK 465 SER A 887
REMARK 465 ASP A 888
REMARK 465 PRO A 889
REMARK 465 HIS A 1178
REMARK 465 HIS A 1179
REMARK 465 HIS A 1180
REMARK 465 HIS A 1181
REMARK 465 HIS A 1182
REMARK 465 HIS A 1183
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 ALA A 971 -10.52 68.84
REMARK 500 SER A 994 95.49 -68.09
REMARK 500 ASN A1023 46.95 -159.32
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 0XH A 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4GIH RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CMP 46
REMARK 900 RELATED ID: 4GII RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CMP 19
REMARK 900 RELATED ID: 4GI3 RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH CMP 35
REMARK 900 RELATED ID: 4GVJ RELATED DB: PDB
REMARK 900 THE SAME PROTEIN COMPLEXED WITH ADENOSINE DI-PHOSPHATE
DBREF 4GJ2 A 885 1176 UNP P29597 TYK2_HUMAN 885 1176
SEQADV 4GJ2 MET A 882 UNP P29597 EXPRESSION TAG
SEQADV 4GJ2 GLY A 883 UNP P29597 EXPRESSION TAG
SEQADV 4GJ2 SER A 884 UNP P29597 EXPRESSION TAG
SEQADV 4GJ2 ALA A 936 UNP P29597 CYS 936 ENGINEERED MUTATION
SEQADV 4GJ2 ALA A 969 UNP P29597 GLN 969 ENGINEERED MUTATION
SEQADV 4GJ2 ALA A 971 UNP P29597 GLU 971 ENGINEERED MUTATION
SEQADV 4GJ2 ALA A 972 UNP P29597 LYS 972 ENGINEERED MUTATION
SEQADV 4GJ2 ASN A 1023 UNP P29597 ASP 1023 ENGINEERED MUTATION
SEQADV 4GJ2 ALA A 1142 UNP P29597 CYS 1142 ENGINEERED MUTATION
SEQADV 4GJ2 ARG A 1177 UNP P29597 EXPRESSION TAG
SEQADV 4GJ2 HIS A 1178 UNP P29597 EXPRESSION TAG
SEQADV 4GJ2 HIS A 1179 UNP P29597 EXPRESSION TAG
SEQADV 4GJ2 HIS A 1180 UNP P29597 EXPRESSION TAG
SEQADV 4GJ2 HIS A 1181 UNP P29597 EXPRESSION TAG
SEQADV 4GJ2 HIS A 1182 UNP P29597 EXPRESSION TAG
SEQADV 4GJ2 HIS A 1183 UNP P29597 EXPRESSION TAG
SEQRES 1 A 302 MET GLY SER PRO ALA SER ASP PRO THR VAL PHE HIS LYS
SEQRES 2 A 302 ARG TYR LEU LYS LYS ILE ARG ASP LEU GLY GLU GLY HIS
SEQRES 3 A 302 PHE GLY LYS VAL SER LEU TYR CYS TYR ASP PRO THR ASN
SEQRES 4 A 302 ASP GLY THR GLY GLU MET VAL ALA VAL LYS ALA LEU LYS
SEQRES 5 A 302 ALA ASP ALA GLY PRO GLN HIS ARG SER GLY TRP LYS GLN
SEQRES 6 A 302 GLU ILE ASP ILE LEU ARG THR LEU TYR HIS GLU HIS ILE
SEQRES 7 A 302 ILE LYS TYR LYS GLY CYS CYS GLU ASP ALA GLY ALA ALA
SEQRES 8 A 302 SER LEU GLN LEU VAL MET GLU TYR VAL PRO LEU GLY SER
SEQRES 9 A 302 LEU ARG ASP TYR LEU PRO ARG HIS SER ILE GLY LEU ALA
SEQRES 10 A 302 GLN LEU LEU LEU PHE ALA GLN GLN ILE CYS GLU GLY MET
SEQRES 11 A 302 ALA TYR LEU HIS ALA GLN HIS TYR ILE HIS ARG ASN LEU
SEQRES 12 A 302 ALA ALA ARG ASN VAL LEU LEU ASP ASN ASP ARG LEU VAL
SEQRES 13 A 302 LYS ILE GLY ASP PHE GLY LEU ALA LYS ALA VAL PRO GLU
SEQRES 14 A 302 GLY HIS GLU TYR TYR ARG VAL ARG GLU ASP GLY ASP SER
SEQRES 15 A 302 PRO VAL PHE TRP TYR ALA PRO GLU CYS LEU LYS GLU TYR
SEQRES 16 A 302 LYS PHE TYR TYR ALA SER ASP VAL TRP SER PHE GLY VAL
SEQRES 17 A 302 THR LEU TYR GLU LEU LEU THR HIS CYS ASP SER SER GLN
SEQRES 18 A 302 SER PRO PRO THR LYS PHE LEU GLU LEU ILE GLY ILE ALA
SEQRES 19 A 302 GLN GLY GLN MET THR VAL LEU ARG LEU THR GLU LEU LEU
SEQRES 20 A 302 GLU ARG GLY GLU ARG LEU PRO ARG PRO ASP LYS CYS PRO
SEQRES 21 A 302 ALA GLU VAL TYR HIS LEU MET LYS ASN CYS TRP GLU THR
SEQRES 22 A 302 GLU ALA SER PHE ARG PRO THR PHE GLU ASN LEU ILE PRO
SEQRES 23 A 302 ILE LEU LYS THR VAL HIS GLU LYS TYR ARG HIS HIS HIS
SEQRES 24 A 302 HIS HIS HIS
HET 0XH A1201 26
HETNAM 0XH 2,6-DICHLORO-N-[2-({[(1R,2R)-2-
HETNAM 2 0XH FLUOROCYCLOPROPYL]CARBONYL}AMINO)PYRIDIN-4-
HETNAM 3 0XH YL]BENZAMIDE
FORMUL 2 0XH C16 H12 CL2 F N3 O2
FORMUL 3 HOH *94(H2 O)
HELIX 1 1 HIS A 893 ARG A 895 5 3
HELIX 2 2 GLY A 937 THR A 953 1 17
HELIX 3 3 LEU A 986 LEU A 990 1 5
HELIX 4 4 GLY A 996 GLN A 1017 1 22
HELIX 5 5 PRO A 1064 TYR A 1068 5 5
HELIX 6 6 ALA A 1069 LYS A 1074 1 6
HELIX 7 7 TYR A 1080 THR A 1096 1 17
HELIX 8 8 SER A 1103 GLY A 1113 1 11
HELIX 9 9 MET A 1119 ARG A 1130 1 12
HELIX 10 10 PRO A 1141 TRP A 1152 1 12
HELIX 11 11 GLU A 1155 ARG A 1159 5 5
HELIX 12 12 THR A 1161 ARG A 1177 1 17
SHEET 1 A 6 VAL A 891 PHE A 892 0
SHEET 2 A 6 TYR A 962 ASP A 968 1 O CYS A 965 N PHE A 892
SHEET 3 A 6 SER A 973 GLU A 979 -1 O VAL A 977 N LYS A 963
SHEET 4 A 6 GLU A 925 LEU A 932 -1 N LYS A 930 O LEU A 976
SHEET 5 A 6 GLY A 909 TYR A 916 -1 N TYR A 914 O VAL A 927
SHEET 6 A 6 LEU A 897 GLU A 905 -1 N ARG A 901 O LEU A 913
SHEET 1 B 3 GLY A 984 SER A 985 0
SHEET 2 B 3 VAL A1029 ASN A1033 -1 O LEU A1031 N GLY A 984
SHEET 3 B 3 LEU A1036 ILE A1039 -1 O LYS A1038 N LEU A1030
SHEET 1 C 2 TYR A1019 ILE A1020 0
SHEET 2 C 2 LYS A1046 ALA A1047 -1 O LYS A1046 N ILE A1020
SHEET 1 D 2 TYR A1054 ARG A1056 0
SHEET 2 D 2 LYS A1077 TYR A1079 -1 O PHE A1078 N TYR A1055
SITE 1 AC1 16 ARG A 901 LEU A 903 GLY A 904 GLU A 905
SITE 2 AC1 16 VAL A 911 ALA A 928 GLU A 979 TYR A 980
SITE 3 AC1 16 VAL A 981 PRO A 982 GLY A 984 ARG A1027
SITE 4 AC1 16 ASN A1028 LEU A1030 GLY A1040 HOH A1327
CRYST1 36.149 74.077 106.009 90.00 90.00 90.00 P 21 21 21 4
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 0.027663 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013499 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009433 0.00000
(ATOM LINES ARE NOT SHOWN.)
END