HEADER TRANSFERASE 03-MAY-18 6DBM
TITLE TYK2 WITH COMPOUND 23
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NON-RECEPTOR TYROSINE-PROTEIN KINASE TYK2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN;
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;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: SF21
KEYWDS KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR F.F.VAJDOS
REVDAT 2 07-NOV-18 6DBM 1 JRNL
REVDAT 1 29-AUG-18 6DBM 0
JRNL AUTH A.FENSOME,C.M.AMBLER,E.ARNOLD,M.E.BANKER,M.F.BROWN,
JRNL AUTH 2 J.CHRENCIK,J.D.CLARK,M.E.DOWTY,I.V.EFREMOV,A.FLICK,
JRNL AUTH 3 B.S.GERSTENBERGER,A.GOPALSAMY,M.M.HAYWARD,M.HEGEN,
JRNL AUTH 4 B.D.HOLLINGSHEAD,J.JUSSIF,J.D.KNAFELS,D.C.LIMBURG,D.LIN,
JRNL AUTH 5 T.H.LIN,B.S.PIERCE,E.SAIAH,R.SHARMA,P.T.SYMANOWICZ,
JRNL AUTH 6 J.B.TELLIEZ,J.I.TRUJILLO,F.F.VAJDOS,F.VINCENT,Z.K.WAN,
JRNL AUTH 7 L.XING,X.YANG,X.YANG,L.ZHANG
JRNL TITL DUAL INHIBITION OF TYK2 AND JAK1 FOR THE TREATMENT OF
JRNL TITL 2 AUTOIMMUNE DISEASES: DISCOVERY OF ((
JRNL TITL 3 S)-2,2-DIFLUOROCYCLOPROPYL)((1 R,5 S)-3-(2-((1-METHYL-1
JRNL TITL 4 H-PYRAZOL-4-YL)AMINO)PYRIMIDIN-4-YL)-3,
JRNL TITL 5 8-DIAZABICYCLO[3.2.1]OCTAN-8-YL)METHANONE (PF-06700841).
JRNL REF J. MED. CHEM. V. 61 8597 2018
JRNL REFN ISSN 1520-4804
JRNL PMID 30113844
JRNL DOI 10.1021/ACS.JMEDCHEM.8B00917
REMARK 2
REMARK 2 RESOLUTION. 2.37 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.37
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.6
REMARK 3 NUMBER OF REFLECTIONS : 10695
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.201
REMARK 3 FREE R VALUE : 0.264
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.090
REMARK 3 FREE R VALUE TEST SET COUNT : 544
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 50.6235 - 3.7581 1.00 2870 151 0.1733 0.2135
REMARK 3 2 3.7581 - 2.9830 1.00 2709 155 0.1960 0.2876
REMARK 3 3 2.9830 - 2.6060 0.90 2423 121 0.2442 0.2896
REMARK 3 4 2.6060 - 2.3677 0.80 2149 117 0.2542 0.3532
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.11
REMARK 3 SHRINKAGE RADIUS : 0.90
REMARK 3 K_SOL : NULL
REMARK 3 B_SOL : NULL
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.360
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 28.69
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.002 2330
REMARK 3 ANGLE : 0.641 3160
REMARK 3 CHIRALITY : 0.030 336
REMARK 3 PLANARITY : 0.002 409
REMARK 3 DIHEDRAL : 14.618 882
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 6DBM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-MAY-18.
REMARK 100 THE DEPOSITION ID IS D_1000234334.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
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) : 1.00
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10734
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.368
REMARK 200 RESOLUTION RANGE LOW (A) : 101.224
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.9
REMARK 200 DATA REDUNDANCY : 5.100
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.37
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.50
REMARK 200 COMPLETENESS FOR SHELL (%) : 76.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.80
REMARK 200 R MERGE FOR SHELL (I) : 0.32100
REMARK 200 R SYM FOR SHELL (I) : 0.32100
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.400
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 33.42
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.85
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS PH 5.5, 0.25 M NACL, 10
REMARK 280 MM TCEP, 27-33% PEG-3350, PH 8.0, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 298K
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 18.11900
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 50.61200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.65850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 50.61200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 18.11900
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.65850
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 865
REMARK 465 ALA A 866
REMARK 465 HIS A 867
REMARK 465 HIS A 868
REMARK 465 HIS A 869
REMARK 465 HIS A 870
REMARK 465 HIS A 871
REMARK 465 HIS A 872
REMARK 465 HIS A 873
REMARK 465 HIS A 874
REMARK 465 HIS A 875
REMARK 465 HIS A 876
REMARK 465 GLY A 877
REMARK 465 ALA A 878
REMARK 465 LEU A 879
REMARK 465 GLU A 880
REMARK 465 VAL A 881
REMARK 465 LEU A 882
REMARK 465 PHE A 883
REMARK 465 GLN A 884
REMARK 465 GLY A 885
REMARK 465 PRO A 886
REMARK 465 GLY A 887
REMARK 465 ASP A 888
REMARK 465 ASP A 917
REMARK 465 PRO A 918
REMARK 465 THR A 919
REMARK 465 ASN A 920
REMARK 465 ASP A 921
REMARK 465 GLY A 922
REMARK 465 THR A 923
REMARK 465 GLY A 924
REMARK 465 ALA A 934
REMARK 465 ASP A 935
REMARK 465 ALA A 936
REMARK 465 GLY A 937
REMARK 465 PRO A 938
REMARK 465 VAL A 1057
REMARK 465 ARG A 1058
REMARK 465 GLU A 1059
REMARK 465 GLN A 1179
REMARK 465 ALA A 1180
REMARK 465 PRO A 1181
REMARK 465 SER A 1182
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 PHE A 908 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 910 CG CD CE NZ
REMARK 470 GLN A 939 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 O HOH A 4159 O HOH A 4191 1.81
REMARK 500 O HOH A 4174 O HOH A 4188 1.96
REMARK 500 NE2 GLN A 1116 O HOH A 4101 2.08
REMARK 500 OE2 GLU A 947 O HOH A 4102 2.10
REMARK 500 O HOH A 4189 O HOH A 4195 2.13
REMARK 500 OE2 GLU A 1009 O HOH A 4103 2.14
REMARK 500 O HOH A 4171 O HOH A 4184 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 O HOH A 4108 O HOH A 4130 3555 1.88
REMARK 500 O HOH A 4184 O HOH A 4186 3555 2.08
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 LYS A 894 4.38 -61.96
REMARK 500 HIS A 907 -102.94 50.79
REMARK 500 ALA A 971 47.18 -168.10
REMARK 500 ALA A 972 37.10 36.79
REMARK 500 SER A 973 -148.51 -167.23
REMARK 500 ASP A1023 36.65 -157.55
REMARK 500 GLN A1177 34.91 -77.06
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 A4200 DISTANCE = 6.14 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue G4J A 4000
DBREF 6DBM A 888 1182 UNP P29597 TYK2_HUMAN 888 1182
SEQADV 6DBM MET A 865 UNP P29597 EXPRESSION TAG
SEQADV 6DBM ALA A 866 UNP P29597 EXPRESSION TAG
SEQADV 6DBM HIS A 867 UNP P29597 EXPRESSION TAG
SEQADV 6DBM HIS A 868 UNP P29597 EXPRESSION TAG
SEQADV 6DBM HIS A 869 UNP P29597 EXPRESSION TAG
SEQADV 6DBM HIS A 870 UNP P29597 EXPRESSION TAG
SEQADV 6DBM HIS A 871 UNP P29597 EXPRESSION TAG
SEQADV 6DBM HIS A 872 UNP P29597 EXPRESSION TAG
SEQADV 6DBM HIS A 873 UNP P29597 EXPRESSION TAG
SEQADV 6DBM HIS A 874 UNP P29597 EXPRESSION TAG
SEQADV 6DBM HIS A 875 UNP P29597 EXPRESSION TAG
SEQADV 6DBM HIS A 876 UNP P29597 EXPRESSION TAG
SEQADV 6DBM GLY A 877 UNP P29597 EXPRESSION TAG
SEQADV 6DBM ALA A 878 UNP P29597 EXPRESSION TAG
SEQADV 6DBM LEU A 879 UNP P29597 EXPRESSION TAG
SEQADV 6DBM GLU A 880 UNP P29597 EXPRESSION TAG
SEQADV 6DBM VAL A 881 UNP P29597 EXPRESSION TAG
SEQADV 6DBM LEU A 882 UNP P29597 EXPRESSION TAG
SEQADV 6DBM PHE A 883 UNP P29597 EXPRESSION TAG
SEQADV 6DBM GLN A 884 UNP P29597 EXPRESSION TAG
SEQADV 6DBM GLY A 885 UNP P29597 EXPRESSION TAG
SEQADV 6DBM PRO A 886 UNP P29597 EXPRESSION TAG
SEQADV 6DBM GLY A 887 UNP P29597 EXPRESSION TAG
SEQADV 6DBM ALA A 936 UNP P29597 CYS 936 ENGINEERED MUTATION
SEQADV 6DBM ALA A 969 UNP P29597 GLN 969 ENGINEERED MUTATION
SEQADV 6DBM ALA A 971 UNP P29597 GLU 971 ENGINEERED MUTATION
SEQADV 6DBM ALA A 972 UNP P29597 LYS 972 ENGINEERED MUTATION
SEQADV 6DBM SER A 1016 UNP P29597 ALA 1016 CONFLICT
SEQADV 6DBM ALA A 1142 UNP P29597 CYS 1142 ENGINEERED MUTATION
SEQRES 1 A 318 MET ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS HIS GLY
SEQRES 2 A 318 ALA LEU GLU VAL LEU PHE GLN GLY PRO GLY ASP PRO THR
SEQRES 3 A 318 VAL PHE HIS LYS ARG TYR LEU LYS LYS ILE ARG ASP LEU
SEQRES 4 A 318 GLY GLU GLY HIS PHE GLY LYS VAL SER LEU TYR CYS TYR
SEQRES 5 A 318 ASP PRO THR ASN ASP GLY THR GLY GLU MET VAL ALA VAL
SEQRES 6 A 318 LYS ALA LEU LYS ALA ASP ALA GLY PRO GLN HIS ARG SER
SEQRES 7 A 318 GLY TRP LYS GLN GLU ILE ASP ILE LEU ARG THR LEU TYR
SEQRES 8 A 318 HIS GLU HIS ILE ILE LYS TYR LYS GLY CYS CYS GLU ASP
SEQRES 9 A 318 ALA GLY ALA ALA SER LEU GLN LEU VAL MET GLU TYR VAL
SEQRES 10 A 318 PRO LEU GLY SER LEU ARG ASP TYR LEU PRO ARG HIS SER
SEQRES 11 A 318 ILE GLY LEU ALA GLN LEU LEU LEU PHE ALA GLN GLN ILE
SEQRES 12 A 318 CYS GLU GLY MET ALA TYR LEU HIS SER GLN HIS TYR ILE
SEQRES 13 A 318 HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU LEU ASP ASN
SEQRES 14 A 318 ASP ARG LEU VAL LYS ILE GLY ASP PHE GLY LEU ALA LYS
SEQRES 15 A 318 ALA VAL PRO GLU GLY HIS GLU PTR TYR ARG VAL ARG GLU
SEQRES 16 A 318 ASP GLY ASP SER PRO VAL PHE TRP TYR ALA PRO GLU CYS
SEQRES 17 A 318 LEU LYS GLU TYR LYS PHE TYR TYR ALA SER ASP VAL TRP
SEQRES 18 A 318 SER PHE GLY VAL THR LEU TYR GLU LEU LEU THR HIS CYS
SEQRES 19 A 318 ASP SER SER GLN SER PRO PRO THR LYS PHE LEU GLU LEU
SEQRES 20 A 318 ILE GLY ILE ALA GLN GLY GLN MET THR VAL LEU ARG LEU
SEQRES 21 A 318 THR GLU LEU LEU GLU ARG GLY GLU ARG LEU PRO ARG PRO
SEQRES 22 A 318 ASP LYS CYS PRO ALA GLU VAL TYR HIS LEU MET LYS ASN
SEQRES 23 A 318 CYS TRP GLU THR GLU ALA SER PHE ARG PRO THR PHE GLU
SEQRES 24 A 318 ASN LEU ILE PRO ILE LEU LYS THR VAL HIS GLU LYS TYR
SEQRES 25 A 318 GLN GLY GLN ALA PRO SER
MODRES 6DBM PTR A 1054 TYR MODIFIED RESIDUE
HET PTR A1054 16
HET G4J A4000 49
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM G4J [(1S)-2,2-DIFLUOROCYCLOPROPYL][(1R,5S)-3-{2-[(1-METHYL-
HETNAM 2 G4J 1H-PYRAZOL-4-YL)AMINO]PYRIMIDIN-4-YL}-3,8-
HETNAM 3 G4J DIAZABICYCLO[3.2.1]OCTAN-8-YL]METHANONE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 2 G4J C18 H21 F2 N7 O
FORMUL 3 HOH *100(H2 O)
HELIX 1 AA1 HIS A 940 LEU A 954 1 15
HELIX 2 AA2 ALA A 969 ALA A 972 5 4
HELIX 3 AA3 SER A 985 LEU A 990 1 6
HELIX 4 AA4 GLY A 996 GLN A 1017 1 22
HELIX 5 AA5 ALA A 1025 ARG A 1027 5 3
HELIX 6 AA6 PRO A 1064 TYR A 1068 5 5
HELIX 7 AA7 ALA A 1069 TYR A 1076 1 8
HELIX 8 AA8 TYR A 1080 THR A 1096 1 17
HELIX 9 AA9 ASP A 1099 GLN A 1102 5 4
HELIX 10 AB1 SER A 1103 GLY A 1113 1 11
HELIX 11 AB2 GLN A 1116 GLN A 1118 5 3
HELIX 12 AB3 MET A 1119 GLU A 1129 1 11
HELIX 13 AB4 PRO A 1141 TRP A 1152 1 12
HELIX 14 AB5 GLU A 1155 ARG A 1159 5 5
HELIX 15 AB6 THR A 1161 GLN A 1177 1 17
SHEET 1 AA1 6 VAL A 891 PHE A 892 0
SHEET 2 AA1 6 TYR A 962 ASP A 968 1 O CYS A 965 N PHE A 892
SHEET 3 AA1 6 SER A 973 GLU A 979 -1 O VAL A 977 N GLY A 964
SHEET 4 AA1 6 VAL A 927 LEU A 932 -1 N LYS A 930 O LEU A 976
SHEET 5 AA1 6 GLY A 909 CYS A 915 -1 N TYR A 914 O VAL A 927
SHEET 6 AA1 6 LYS A 898 GLY A 906 -1 N GLY A 904 O VAL A 911
SHEET 1 AA2 2 TYR A1019 ILE A1020 0
SHEET 2 AA2 2 LYS A1046 ALA A1047 -1 O LYS A1046 N ILE A1020
SHEET 1 AA3 2 VAL A1029 ASN A1033 0
SHEET 2 AA3 2 LEU A1036 ILE A1039 -1 O LYS A1038 N LEU A1030
SHEET 1 AA4 2 PTR A1054 TYR A1055 0
SHEET 2 AA4 2 PHE A1078 TYR A1079 -1 O PHE A1078 N TYR A1055
LINK C GLU A1053 N PTR A1054 1555 1555 1.33
LINK C PTR A1054 N TYR A1055 1555 1555 1.33
SITE 1 AC1 18 LEU A 903 GLY A 904 GLU A 905 GLY A 906
SITE 2 AC1 18 GLY A 909 VAL A 911 ALA A 928 LYS A 930
SITE 3 AC1 18 MET A 978 GLU A 979 TYR A 980 VAL A 981
SITE 4 AC1 18 GLY A 984 ARG A1027 LEU A1030 GLY A1040
SITE 5 AC1 18 ASP A1041 HOH A4134
CRYST1 36.238 73.317 101.224 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 0.027595 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013639 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009879 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
