HEADER TRANSFERASE/TRANSFERASE INHIBITOR 28-APR-15 4ZIM
TITLE CRYSTAL STRUCTURE OF JANUS KINASE 2 IN COMPLEX WITH A 9H-CARBAZOLE-1-
TITLE 2 CARBOXAMIDE INHIBITOR
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, UNP RESIDUES 839-1132;
COMPND 5 SYNONYM: JANUS KINASE 2,JAK-2;
COMPND 6 EC: 2.7.10.2;
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: JAK2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS KINASE, TRANSFERASE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.SACK
REVDAT 4 22-NOV-17 4ZIM 1 REMARK
REVDAT 3 20-JUL-16 4ZIM 1 REMARK
REVDAT 2 17-JUN-15 4ZIM 1 JRNL
REVDAT 1 03-JUN-15 4ZIM 0
JRNL AUTH K.ZIMMERMANN,X.SANG,H.A.MASTALERZ,W.L.JOHNSON,G.ZHANG,Q.LIU,
JRNL AUTH 2 D.BATT,L.J.LOMBARDO,D.VYAS,G.L.TRAINOR,J.S.TOKARSKI,
JRNL AUTH 3 M.V.LORENZI,D.YOU,M.M.GOTTARDIS,J.LIPPY,J.KHAN,J.S.SACK,
JRNL AUTH 4 A.V.PURANDARE
JRNL TITL 9H-CARBAZOLE-1-CARBOXAMIDES AS POTENT AND SELECTIVE JAK2
JRNL TITL 2 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 25 2809 2015
JRNL REFN ESSN 1464-3405
JRNL PMID 25987372
JRNL DOI 10.1016/J.BMCL.2015.04.101
REMARK 2
REMARK 2 RESOLUTION. 2.65 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.11.6
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) : 2.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 37.46
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 25761
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.202
REMARK 3 FREE R VALUE : 0.274
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 2.550
REMARK 3 FREE R VALUE TEST SET COUNT : 656
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 : 13
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.65
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.76
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.68
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2873
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2955
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2782
REMARK 3 BIN R VALUE (WORKING SET) : 0.2930
REMARK 3 BIN FREE R VALUE : 0.3677
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 3.17
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 91
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 : 4786
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 64
REMARK 3 SOLVENT ATOMS : 262
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 62.43
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.00
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.20050
REMARK 3 B22 (A**2) : -2.20050
REMARK 3 B33 (A**2) : 4.40100
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) : 0.372
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.542
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.321
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.526
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.323
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 : 0.928
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.877
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4971 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6721 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1776 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 140 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 768 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4971 ; 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 : 601 ; 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 : 5704 ; 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) : 2.96
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 19.88
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 4ZIM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-APR-15.
REMARK 100 THE DEPOSITION ID IS D_1000209367.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-08
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : RIGAKU RU200
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : MICROMAX CONFOCAL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO (DENZO), HKL-2000 (DENZO)
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK (SCALEPACK), HKL-2000
REMARK 200 (SCALEPACK)
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 25927
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.650
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.500
REMARK 200 R MERGE (I) : 0.12200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.74
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 7.40
REMARK 200 R MERGE FOR SHELL (I) : 0.61600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.600
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 (%): 58.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES BUFFER, 100MM NACL, 28%
REMARK 280 (W/V) PEG3350, 2MM DTT AND 200MM TRI-SODIUM CITRATE, PH 6.5,
REMARK 280 VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y,X,Z+1/4
REMARK 290 4555 Y,-X,Z+3/4
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 35.40500
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 17.70250
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 53.10750
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 818
REMARK 465 GLY A 819
REMARK 465 SER A 820
REMARK 465 SER A 821
REMARK 465 HIS A 822
REMARK 465 HIS A 823
REMARK 465 HIS A 824
REMARK 465 HIS A 825
REMARK 465 HIS A 826
REMARK 465 HIS A 827
REMARK 465 SER A 828
REMARK 465 SER A 829
REMARK 465 GLY A 830
REMARK 465 LEU A 831
REMARK 465 VAL A 832
REMARK 465 PRO A 833
REMARK 465 ARG A 834
REMARK 465 GLY A 835
REMARK 465 SER A 836
REMARK 465 HIS A 837
REMARK 465 MET A 838
REMARK 465 ARG A 839
REMARK 465 ASP A 840
REMARK 465 PRO A 841
REMARK 465 ALA A 920
REMARK 465 GLY A 921
REMARK 465 ARG A 922
REMARK 465 GLY A 1132
REMARK 465 HIS A 1133
REMARK 465 HIS A 1134
REMARK 465 HIS A 1135
REMARK 465 HIS A 1136
REMARK 465 HIS A 1137
REMARK 465 HIS A 1138
REMARK 465 MET B 818
REMARK 465 GLY B 819
REMARK 465 SER B 820
REMARK 465 SER B 821
REMARK 465 HIS B 822
REMARK 465 HIS B 823
REMARK 465 HIS B 824
REMARK 465 HIS B 825
REMARK 465 HIS B 826
REMARK 465 HIS B 827
REMARK 465 SER B 828
REMARK 465 SER B 829
REMARK 465 GLY B 830
REMARK 465 LEU B 831
REMARK 465 VAL B 832
REMARK 465 PRO B 833
REMARK 465 ARG B 834
REMARK 465 GLY B 835
REMARK 465 SER B 836
REMARK 465 HIS B 1133
REMARK 465 HIS B 1134
REMARK 465 HIS B 1135
REMARK 465 HIS B 1136
REMARK 465 HIS B 1137
REMARK 465 HIS B 1138
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 LYS A 857 CG CD CE NZ
REMARK 470 LYS A1053 CG CD CE NZ
REMARK 470 GLN A1070 CG CD OE1 NE2
REMARK 470 MET A1100 CE
REMARK 470 MET B 838 CG SD CE
REMARK 470 ARG B 839 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 857 CG CD CE NZ
REMARK 470 ARG B 922 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 923 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 943 CG CD CE NZ
REMARK 470 LYS B1011 CG CD CE NZ
REMARK 470 GLU B1015 CG CD OE1 OE2
REMARK 470 GLN B1070 CG CD OE1 NE2
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 GLN A 843 120.52 62.14
REMARK 500 LEU A 852 -61.42 -106.13
REMARK 500 SER A 862 127.46 172.30
REMARK 500 GLN A 872 14.72 56.60
REMARK 500 ASP A 976 49.22 -162.21
REMARK 500 TRP A1106 38.40 -86.95
REMARK 500 LEU B 852 -61.51 -106.05
REMARK 500 ASP B 869 79.60 -115.14
REMARK 500 GLN B 872 15.27 58.71
REMARK 500 SER B 919 -27.42 -179.59
REMARK 500 ARG B 922 78.95 63.15
REMARK 500 ARG B 923 -42.62 -173.02
REMARK 500 ASP B 976 47.48 -163.16
REMARK 500 PRO B1013 -84.87 -71.85
REMARK 500 GLU B1015 96.70 -69.16
REMARK 500 GLN B1070 -110.05 -42.68
REMARK 500 TRP B1106 38.69 -88.05
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 A1434 DISTANCE = 7.04 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4OK A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 4OK B 1201
DBREF 4ZIM A 839 1132 UNP O60674 JAK2_HUMAN 839 1132
DBREF 4ZIM B 839 1132 UNP O60674 JAK2_HUMAN 839 1132
SEQADV 4ZIM MET A 818 UNP O60674 INITIATING METHIONINE
SEQADV 4ZIM GLY A 819 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM SER A 820 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM SER A 821 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 822 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 823 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 824 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 825 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 826 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 827 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM SER A 828 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM SER A 829 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM GLY A 830 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM LEU A 831 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM VAL A 832 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM PRO A 833 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM ARG A 834 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM GLY A 835 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM SER A 836 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 837 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM MET A 838 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 1133 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 1134 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 1135 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 1136 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 1137 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS A 1138 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM MET B 818 UNP O60674 INITIATING METHIONINE
SEQADV 4ZIM GLY B 819 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM SER B 820 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM SER B 821 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 822 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 823 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 824 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 825 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 826 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 827 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM SER B 828 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM SER B 829 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM GLY B 830 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM LEU B 831 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM VAL B 832 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM PRO B 833 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM ARG B 834 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM GLY B 835 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM SER B 836 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 837 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM MET B 838 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 1133 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 1134 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 1135 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 1136 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 1137 UNP O60674 EXPRESSION TAG
SEQADV 4ZIM HIS B 1138 UNP O60674 EXPRESSION TAG
SEQRES 1 A 321 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 321 LEU VAL PRO ARG GLY SER HIS MET ARG ASP PRO THR GLN
SEQRES 3 A 321 PHE GLU GLU ARG HIS LEU LYS PHE LEU GLN GLN LEU GLY
SEQRES 4 A 321 LYS GLY ASN PHE GLY SER VAL GLU MET CYS ARG TYR ASP
SEQRES 5 A 321 PRO LEU GLN ASP ASN THR GLY GLU VAL VAL ALA VAL LYS
SEQRES 6 A 321 LYS LEU GLN HIS SER THR GLU GLU HIS LEU ARG ASP PHE
SEQRES 7 A 321 GLU ARG GLU ILE GLU ILE LEU LYS SER LEU GLN HIS ASP
SEQRES 8 A 321 ASN ILE VAL LYS TYR LYS GLY VAL CYS TYR SER ALA GLY
SEQRES 9 A 321 ARG ARG ASN LEU LYS LEU ILE MET GLU TYR LEU PRO TYR
SEQRES 10 A 321 GLY SER LEU ARG ASP TYR LEU GLN LYS HIS LYS GLU ARG
SEQRES 11 A 321 ILE ASP HIS ILE LYS LEU LEU GLN TYR THR SER GLN ILE
SEQRES 12 A 321 CYS LYS GLY MET GLU TYR LEU GLY THR LYS ARG TYR ILE
SEQRES 13 A 321 HIS ARG ASP LEU ALA THR ARG ASN ILE LEU VAL GLU ASN
SEQRES 14 A 321 GLU ASN ARG VAL LYS ILE GLY ASP PHE GLY LEU THR LYS
SEQRES 15 A 321 VAL LEU PRO GLN ASP LYS GLU PTR PTR LYS VAL LYS GLU
SEQRES 16 A 321 PRO GLY GLU SER PRO ILE PHE TRP TYR ALA PRO GLU SER
SEQRES 17 A 321 LEU THR GLU SER LYS PHE SER VAL ALA SER ASP VAL TRP
SEQRES 18 A 321 SER PHE GLY VAL VAL LEU TYR GLU LEU PHE THR TYR ILE
SEQRES 19 A 321 GLU LYS SER LYS SER PRO PRO ALA GLU PHE MET ARG MET
SEQRES 20 A 321 ILE GLY ASN ASP LYS GLN GLY GLN MET ILE VAL PHE HIS
SEQRES 21 A 321 LEU ILE GLU LEU LEU LYS ASN ASN GLY ARG LEU PRO ARG
SEQRES 22 A 321 PRO ASP GLY CYS PRO ASP GLU ILE TYR MET ILE MET THR
SEQRES 23 A 321 GLU CYS TRP ASN ASN ASN VAL ASN GLN ARG PRO SER PHE
SEQRES 24 A 321 ARG ASP LEU ALA LEU ARG VAL ASP GLN ILE ARG ASP ASN
SEQRES 25 A 321 MET ALA GLY HIS HIS HIS HIS HIS HIS
SEQRES 1 B 321 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 321 LEU VAL PRO ARG GLY SER HIS MET ARG ASP PRO THR GLN
SEQRES 3 B 321 PHE GLU GLU ARG HIS LEU LYS PHE LEU GLN GLN LEU GLY
SEQRES 4 B 321 LYS GLY ASN PHE GLY SER VAL GLU MET CYS ARG TYR ASP
SEQRES 5 B 321 PRO LEU GLN ASP ASN THR GLY GLU VAL VAL ALA VAL LYS
SEQRES 6 B 321 LYS LEU GLN HIS SER THR GLU GLU HIS LEU ARG ASP PHE
SEQRES 7 B 321 GLU ARG GLU ILE GLU ILE LEU LYS SER LEU GLN HIS ASP
SEQRES 8 B 321 ASN ILE VAL LYS TYR LYS GLY VAL CYS TYR SER ALA GLY
SEQRES 9 B 321 ARG ARG ASN LEU LYS LEU ILE MET GLU TYR LEU PRO TYR
SEQRES 10 B 321 GLY SER LEU ARG ASP TYR LEU GLN LYS HIS LYS GLU ARG
SEQRES 11 B 321 ILE ASP HIS ILE LYS LEU LEU GLN TYR THR SER GLN ILE
SEQRES 12 B 321 CYS LYS GLY MET GLU TYR LEU GLY THR LYS ARG TYR ILE
SEQRES 13 B 321 HIS ARG ASP LEU ALA THR ARG ASN ILE LEU VAL GLU ASN
SEQRES 14 B 321 GLU ASN ARG VAL LYS ILE GLY ASP PHE GLY LEU THR LYS
SEQRES 15 B 321 VAL LEU PRO GLN ASP LYS GLU PTR PTR LYS VAL LYS GLU
SEQRES 16 B 321 PRO GLY GLU SER PRO ILE PHE TRP TYR ALA PRO GLU SER
SEQRES 17 B 321 LEU THR GLU SER LYS PHE SER VAL ALA SER ASP VAL TRP
SEQRES 18 B 321 SER PHE GLY VAL VAL LEU TYR GLU LEU PHE THR TYR ILE
SEQRES 19 B 321 GLU LYS SER LYS SER PRO PRO ALA GLU PHE MET ARG MET
SEQRES 20 B 321 ILE GLY ASN ASP LYS GLN GLY GLN MET ILE VAL PHE HIS
SEQRES 21 B 321 LEU ILE GLU LEU LEU LYS ASN ASN GLY ARG LEU PRO ARG
SEQRES 22 B 321 PRO ASP GLY CYS PRO ASP GLU ILE TYR MET ILE MET THR
SEQRES 23 B 321 GLU CYS TRP ASN ASN ASN VAL ASN GLN ARG PRO SER PHE
SEQRES 24 B 321 ARG ASP LEU ALA LEU ARG VAL ASP GLN ILE ARG ASP ASN
SEQRES 25 B 321 MET ALA GLY HIS HIS HIS HIS HIS HIS
MODRES 4ZIM PTR A 1007 TYR MODIFIED RESIDUE
MODRES 4ZIM PTR A 1008 TYR MODIFIED RESIDUE
MODRES 4ZIM PTR B 1007 TYR MODIFIED RESIDUE
MODRES 4ZIM PTR B 1008 TYR MODIFIED RESIDUE
HET PTR A1007 16
HET PTR A1008 16
HET PTR B1007 16
HET PTR B1008 16
HET 4OK A1201 32
HET 4OK B1201 32
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM 4OK 3-(3,4-DICHLOROPHENYL)-6-(MORPHOLIN-4-YLCARBONYL)-9H-
HETNAM 2 4OK CARBAZOLE-1-CARBOXAMIDE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR 4(C9 H12 N O6 P)
FORMUL 3 4OK 2(C24 H19 CL2 N3 O3)
FORMUL 5 HOH *262(H2 O)
HELIX 1 AA1 GLU A 845 ARG A 847 5 3
HELIX 2 AA2 THR A 888 SER A 904 1 17
HELIX 3 AA3 SER A 936 HIS A 944 1 9
HELIX 4 AA4 LYS A 945 ILE A 948 5 4
HELIX 5 AA5 ASP A 949 LYS A 970 1 22
HELIX 6 AA6 ALA A 978 ARG A 980 5 3
HELIX 7 AA7 ALA A 1022 SER A 1029 1 8
HELIX 8 AA8 SER A 1032 THR A 1049 1 18
HELIX 9 AA9 GLU A 1052 LYS A 1055 5 4
HELIX 10 AB1 SER A 1056 GLY A 1066 1 11
HELIX 11 AB2 GLN A 1072 ASN A 1084 1 13
HELIX 12 AB3 PRO A 1095 TRP A 1106 1 12
HELIX 13 AB4 ASN A 1109 ARG A 1113 5 5
HELIX 14 AB5 SER A 1115 ALA A 1131 1 17
HELIX 15 AB6 GLU B 845 ARG B 847 5 3
HELIX 16 AB7 THR B 888 SER B 904 1 17
HELIX 17 AB8 SER B 936 HIS B 944 1 9
HELIX 18 AB9 LYS B 945 ILE B 948 5 4
HELIX 19 AC1 ASP B 949 LYS B 970 1 22
HELIX 20 AC2 ALA B 978 ARG B 980 5 3
HELIX 21 AC3 PRO B 1017 TYR B 1021 5 5
HELIX 22 AC4 ALA B 1022 SER B 1029 1 8
HELIX 23 AC5 SER B 1032 THR B 1049 1 18
HELIX 24 AC6 GLU B 1052 LYS B 1055 5 4
HELIX 25 AC7 SER B 1056 GLY B 1066 1 11
HELIX 26 AC8 GLY B 1071 ASN B 1084 1 14
HELIX 27 AC9 PRO B 1095 TRP B 1106 1 12
HELIX 28 AD1 ASN B 1109 ARG B 1113 5 5
HELIX 29 AD2 SER B 1115 GLY B 1132 1 18
SHEET 1 AA1 5 LEU A 849 LYS A 857 0
SHEET 2 AA1 5 SER A 862 TYR A 868 -1 O MET A 865 N GLN A 853
SHEET 3 AA1 5 GLU A 877 LYS A 883 -1 O GLU A 877 N TYR A 868
SHEET 4 AA1 5 LYS A 926 GLU A 930 -1 O MET A 929 N ALA A 880
SHEET 5 AA1 5 TYR A 913 CYS A 917 -1 N LYS A 914 O ILE A 928
SHEET 1 AA2 2 TYR A 972 ILE A 973 0
SHEET 2 AA2 2 LYS A 999 VAL A1000 -1 O LYS A 999 N ILE A 973
SHEET 1 AA3 2 ILE A 982 ASN A 986 0
SHEET 2 AA3 2 ARG A 989 ILE A 992 -1 O LYS A 991 N LEU A 983
SHEET 1 AA4 2 PTR A1008 LYS A1009 0
SHEET 2 AA4 2 LYS A1030 PHE A1031 -1 O PHE A1031 N PTR A1008
SHEET 1 AA5 6 GLN B 843 PHE B 844 0
SHEET 2 AA5 6 TYR B 913 CYS B 917 1 O VAL B 916 N PHE B 844
SHEET 3 AA5 6 LYS B 926 GLU B 930 -1 O ILE B 928 N GLY B 915
SHEET 4 AA5 6 GLU B 877 LEU B 884 -1 N LYS B 882 O LEU B 927
SHEET 5 AA5 6 GLY B 861 TYR B 868 -1 N TYR B 868 O GLU B 877
SHEET 6 AA5 6 LEU B 849 LYS B 857 -1 N GLN B 853 O MET B 865
SHEET 1 AA6 2 TYR B 972 ILE B 973 0
SHEET 2 AA6 2 LYS B 999 VAL B1000 -1 O LYS B 999 N ILE B 973
SHEET 1 AA7 2 ILE B 982 VAL B 984 0
SHEET 2 AA7 2 VAL B 990 ILE B 992 -1 O LYS B 991 N LEU B 983
SHEET 1 AA8 2 PTR B1008 LYS B1009 0
SHEET 2 AA8 2 LYS B1030 PHE B1031 -1 O PHE B1031 N PTR B1008
LINK C GLU A1006 N PTR A1007 1555 1555 1.33
LINK C PTR A1007 N PTR A1008 1555 1555 1.33
LINK C PTR A1008 N LYS A1009 1555 1555 1.35
LINK C GLU B1006 N PTR B1007 1555 1555 1.34
LINK C PTR B1007 N PTR B1008 1555 1555 1.33
LINK C PTR B1008 N LYS B1009 1555 1555 1.35
SITE 1 AC1 16 GLN A 853 LEU A 855 GLY A 856 LYS A 857
SITE 2 AC1 16 VAL A 863 ALA A 880 GLU A 930 TYR A 931
SITE 3 AC1 16 LEU A 932 GLY A 935 LEU A 983 ASP A 994
SITE 4 AC1 16 HOH A1305 HOH A1306 HOH A1333 GLU B 987
SITE 1 AC2 17 HIS A 886 GLN B 853 GLN B 854 LEU B 855
SITE 2 AC2 17 GLY B 856 LYS B 857 VAL B 863 ALA B 880
SITE 3 AC2 17 GLU B 930 TYR B 931 LEU B 932 PRO B 933
SITE 4 AC2 17 GLY B 935 LEU B 983 ASP B 994 HOH B1302
SITE 5 AC2 17 HOH B1342
CRYST1 112.390 112.390 70.810 90.00 90.00 90.00 P 41 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 0.008898 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008898 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014122 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
