HEADER TRANSFERASE 14-AUG-09 3IOK
TITLE 2-AMINOPYRAZOLO[1,5-A]PYRIMIDINES AS POTENT AND SELECTIVE INHIBITORS
TITLE 2 OF JAK2
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK2;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: JAK2 KINASE DOMAIN (UNP RESIDUES 842-1132);
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: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBEV1
KEYWDS KINASE, INHIBITOR, JAK2, JANUS KINASE, ATP-BINDING, DISEASE MUTATION,
KEYWDS 2 MEMBRANE, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN, PROTO-ONCOGENE, SH2
KEYWDS 3 DOMAIN, TRANSFERASE, TYROSINE-PROTEIN KINASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.J.ZUCCOLA,M.W.LEDEBOER,A.C.PIERCE
REVDAT 3 03-APR-13 3IOK 1 REMARK VERSN
REVDAT 2 17-NOV-09 3IOK 1 JRNL
REVDAT 1 10-NOV-09 3IOK 0
JRNL AUTH M.W.LEDEBOER,A.C.PIERCE,J.P.DUFFY,H.GAO,D.MESSERSMITH,
JRNL AUTH 2 F.G.SALITURO,S.NANTHAKUMAR,J.COME,H.J.ZUCCOLA,L.SWENSON,
JRNL AUTH 3 D.SHLYAKTER,S.MAHAJAN,T.HOOCK,B.FAN,W.J.TSAI,E.KOLACZKOWSKI,
JRNL AUTH 4 S.CARRIER,J.K.HOGAN,R.ZESSIS,S.PAZHANISAMY,Y.L.BENNANI
JRNL TITL 2-AMINOPYRAZOLO[1,5-A]PYRIMIDINES AS POTENT AND SELECTIVE
JRNL TITL 2 INHIBITORS OF JAK2.
JRNL REF BIOORG.MED.CHEM.LETT. V. 19 6529 2009
JRNL REFN ISSN 0960-894X
JRNL PMID 19857967
JRNL DOI 10.1016/J.BMCL.2009.10.053
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 19286
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) : 0.228
REMARK 3 R VALUE (WORKING SET) : 0.224
REMARK 3 FREE R VALUE : 0.270
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 7.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1509
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) : 2.10
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.15
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1285
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 100.00
REMARK 3 BIN R VALUE (WORKING SET) : 0.2580
REMARK 3 BIN FREE R VALUE SET COUNT : 96
REMARK 3 BIN FREE R VALUE : 0.3500
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 2382
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 26
REMARK 3 SOLVENT ATOMS : 78
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 32.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.72000
REMARK 3 B22 (A**2) : 2.36000
REMARK 3 B33 (A**2) : -0.64000
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): 0.276
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.162
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.054
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.929
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2487 ; 0.008 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3350 ; 1.116 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 285 ; 5.178 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 126 ;39.630 ;24.048
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 479 ;15.782 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 19 ;16.565 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 351 ; 0.079 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1884 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1130 ; 0.180 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1684 ; 0.302 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 110 ; 0.141 ; 0.200
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): 51 ; 0.134 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 9 ; 0.156 ; 0.200
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): 1492 ; 0.718 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2332 ; 1.231 ; 2.000
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1148 ; 1.520 ; 3.000
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1018 ; 2.482 ; 4.500
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 3IOK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-09.
REMARK 100 THE RCSB ID CODE IS RCSB054668.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-OCT-06
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) : 1.00
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : D*TREK
REMARK 200 DATA SCALING SOFTWARE : D*TREK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19316
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 46.760
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 4.730
REMARK 200 R MERGE (I) : 0.07300
REMARK 200 R SYM (I) : 0.08300
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.1000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.18
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 4.81
REMARK 200 R MERGE FOR SHELL (I) : 0.29600
REMARK 200 R SYM FOR SHELL (I) : 0.33400
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS
REMARK 200 SOFTWARE USED: REFMAC
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.03
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.1 - 1.5 D-L MALIC ACID, VAPOR
REMARK 280 DIFFUSION, TEMPERATURE 298K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
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 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 33.80100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 33.80100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 46.75600
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 51.27300
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.75600
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 51.27300
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 33.80100
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.75600
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 51.27300
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 33.80100
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.75600
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 51.27300
REMARK 290 SMTRY3 8 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A1369 LIES ON A SPECIAL POSITION.
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 820
REMARK 465 GLY A 821
REMARK 465 SER A 822
REMARK 465 SER A 823
REMARK 465 HIS A 824
REMARK 465 HIS A 825
REMARK 465 HIS A 826
REMARK 465 HIS A 827
REMARK 465 HIS A 828
REMARK 465 HIS A 829
REMARK 465 SER A 830
REMARK 465 SER A 831
REMARK 465 GLY A 832
REMARK 465 LEU A 833
REMARK 465 VAL A 834
REMARK 465 PRO A 835
REMARK 465 ARG A 836
REMARK 465 GLY A 837
REMARK 465 SER A 838
REMARK 465 HIS A 839
REMARK 465 ASN A 840
REMARK 465 MET A 841
REMARK 465 ASN A 859
REMARK 465 PHE A 860
REMARK 465 ALA A 1131
REMARK 465 GLY A 1132
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 945 -118.56 19.98
REMARK 500 ARG A 975 -14.13 73.01
REMARK 500 TRP A1106 44.63 -90.33
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 1P6 A 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3IO7 RELATED DB: PDB
DBREF 3IOK A 842 1132 UNP O60674 JAK2_HUMAN 842 1132
SEQADV 3IOK MET A 820 UNP O60674 EXPRESSION TAG
SEQADV 3IOK GLY A 821 UNP O60674 EXPRESSION TAG
SEQADV 3IOK SER A 822 UNP O60674 EXPRESSION TAG
SEQADV 3IOK SER A 823 UNP O60674 EXPRESSION TAG
SEQADV 3IOK HIS A 824 UNP O60674 EXPRESSION TAG
SEQADV 3IOK HIS A 825 UNP O60674 EXPRESSION TAG
SEQADV 3IOK HIS A 826 UNP O60674 EXPRESSION TAG
SEQADV 3IOK HIS A 827 UNP O60674 EXPRESSION TAG
SEQADV 3IOK HIS A 828 UNP O60674 EXPRESSION TAG
SEQADV 3IOK HIS A 829 UNP O60674 EXPRESSION TAG
SEQADV 3IOK SER A 830 UNP O60674 EXPRESSION TAG
SEQADV 3IOK SER A 831 UNP O60674 EXPRESSION TAG
SEQADV 3IOK GLY A 832 UNP O60674 EXPRESSION TAG
SEQADV 3IOK LEU A 833 UNP O60674 EXPRESSION TAG
SEQADV 3IOK VAL A 834 UNP O60674 EXPRESSION TAG
SEQADV 3IOK PRO A 835 UNP O60674 EXPRESSION TAG
SEQADV 3IOK ARG A 836 UNP O60674 EXPRESSION TAG
SEQADV 3IOK GLY A 837 UNP O60674 EXPRESSION TAG
SEQADV 3IOK SER A 838 UNP O60674 EXPRESSION TAG
SEQADV 3IOK HIS A 839 UNP O60674 EXPRESSION TAG
SEQADV 3IOK ASN A 840 UNP O60674 EXPRESSION TAG
SEQADV 3IOK MET A 841 UNP O60674 EXPRESSION TAG
SEQRES 1 A 313 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 313 LEU VAL PRO ARG GLY SER HIS ASN MET THR GLN PHE GLU
SEQRES 3 A 313 GLU ARG HIS LEU LYS PHE LEU GLN GLN LEU GLY LYS GLY
SEQRES 4 A 313 ASN PHE GLY SER VAL GLU MET CYS ARG TYR ASP PRO LEU
SEQRES 5 A 313 GLN ASP ASN THR GLY GLU VAL VAL ALA VAL LYS LYS LEU
SEQRES 6 A 313 GLN HIS SER THR GLU GLU HIS LEU ARG ASP PHE GLU ARG
SEQRES 7 A 313 GLU ILE GLU ILE LEU LYS SER LEU GLN HIS ASP ASN ILE
SEQRES 8 A 313 VAL LYS TYR LYS GLY VAL CYS TYR SER ALA GLY ARG ARG
SEQRES 9 A 313 ASN LEU LYS LEU ILE MET GLU TYR LEU PRO TYR GLY SER
SEQRES 10 A 313 LEU ARG ASP TYR LEU GLN LYS HIS LYS GLU ARG ILE ASP
SEQRES 11 A 313 HIS ILE LYS LEU LEU GLN TYR THR SER GLN ILE CYS LYS
SEQRES 12 A 313 GLY MET GLU TYR LEU GLY THR LYS ARG TYR ILE HIS ARG
SEQRES 13 A 313 ASP LEU ALA THR ARG ASN ILE LEU VAL GLU ASN GLU ASN
SEQRES 14 A 313 ARG VAL LYS ILE GLY ASP PHE GLY LEU THR LYS VAL LEU
SEQRES 15 A 313 PRO GLN ASP LYS GLU PTR PTR LYS VAL LYS GLU PRO GLY
SEQRES 16 A 313 GLU SER PRO ILE PHE TRP TYR ALA PRO GLU SER LEU THR
SEQRES 17 A 313 GLU SER LYS PHE SER VAL ALA SER ASP VAL TRP SER PHE
SEQRES 18 A 313 GLY VAL VAL LEU TYR GLU LEU PHE THR TYR ILE GLU LYS
SEQRES 19 A 313 SER LYS SER PRO PRO ALA GLU PHE MET ARG MET ILE GLY
SEQRES 20 A 313 ASN ASP LYS GLN GLY GLN MET ILE VAL PHE HIS LEU ILE
SEQRES 21 A 313 GLU LEU LEU LYS ASN ASN GLY ARG LEU PRO ARG PRO ASP
SEQRES 22 A 313 GLY CYS PRO ASP GLU ILE TYR MET ILE MET THR GLU CYS
SEQRES 23 A 313 TRP ASN ASN ASN VAL ASN GLN ARG PRO SER PHE ARG ASP
SEQRES 24 A 313 LEU ALA LEU ARG VAL ASP GLN ILE ARG ASP ASN MET ALA
SEQRES 25 A 313 GLY
MODRES 3IOK PTR A 1007 TYR O-PHOSPHOTYROSINE
MODRES 3IOK PTR A 1008 TYR O-PHOSPHOTYROSINE
HET PTR A1007 16
HET PTR A1008 16
HET 1P6 A1201 26
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM 1P6 3-(6-{[(1S)-1-(4-FLUOROPHENYL)ETHYL]AMINO}PYRIMIDIN-4-
HETNAM 2 1P6 YL)PYRAZOLO[1,5-A]PYRIMIDIN-2-AMINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR 2(C9 H12 N O6 P)
FORMUL 2 1P6 C18 H16 F N7
FORMUL 3 HOH *78(H2 O)
HELIX 1 1 GLU A 845 ARG A 847 5 3
HELIX 2 2 THR A 888 SER A 904 1 17
HELIX 3 3 SER A 936 LYS A 945 1 10
HELIX 4 4 GLU A 946 ILE A 948 5 3
HELIX 5 5 ASP A 949 LYS A 970 1 22
HELIX 6 6 ALA A 978 ARG A 980 5 3
HELIX 7 7 PRO A 1017 TYR A 1021 5 5
HELIX 8 8 ALA A 1022 SER A 1029 1 8
HELIX 9 9 SER A 1032 THR A 1049 1 18
HELIX 10 10 GLU A 1052 LYS A 1055 5 4
HELIX 11 11 SER A 1056 GLY A 1066 1 11
HELIX 12 12 GLY A 1071 ASN A 1084 1 14
HELIX 13 13 PRO A 1095 TRP A 1106 1 12
HELIX 14 14 ASN A 1109 ARG A 1113 5 5
HELIX 15 15 SER A 1115 MET A 1130 1 16
SHEET 1 A 5 LEU A 849 GLY A 856 0
SHEET 2 A 5 SER A 862 TYR A 868 -1 O MET A 865 N GLN A 853
SHEET 3 A 5 GLU A 877 LYS A 883 -1 O GLU A 877 N TYR A 868
SHEET 4 A 5 LEU A 925 GLU A 930 -1 O MET A 929 N ALA A 880
SHEET 5 A 5 TYR A 913 TYR A 918 -1 N GLY A 915 O ILE A 928
SHEET 1 B 2 TYR A 972 ILE A 973 0
SHEET 2 B 2 LYS A 999 VAL A1000 -1 O LYS A 999 N ILE A 973
SHEET 1 C 2 ILE A 982 ASN A 986 0
SHEET 2 C 2 ARG A 989 ILE A 992 -1 O LYS A 991 N LEU A 983
SHEET 1 D 2 PTR A1008 LYS A1009 0
SHEET 2 D 2 LYS A1030 PHE A1031 -1 O PHE A1031 N PTR A1008
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 1.33
SITE 1 AC1 14 LEU A 855 GLY A 856 LYS A 857 VAL A 863
SITE 2 AC1 14 ALA A 880 MET A 929 GLU A 930 TYR A 931
SITE 3 AC1 14 LEU A 932 ARG A 980 ASN A 981 LEU A 983
SITE 4 AC1 14 GLY A 993 ASP A 994
CRYST1 93.512 102.546 67.602 90.00 90.00 90.00 C 2 2 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 0.010694 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009752 0.000000 0.00000
SCALE3 0.000000 0.000000 0.014792 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
