HEADER TRANSFERASE/TRANSFERASE INHIBITOR 14-FEB-17 5UT0
TITLE JAK2 JH2 IN COMPLEX WITH AT9283
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK2;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: JANUS KINASE 2,JAK-2;
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: JAK2;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS PSEUDOKINASE DOMAIN, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.E.PULEO,J.SCHLESSINGER
REVDAT 6 04-OCT-23 5UT0 1 REMARK
REVDAT 5 01-JAN-20 5UT0 1 REMARK
REVDAT 4 27-SEP-17 5UT0 1 REMARK
REVDAT 3 13-SEP-17 5UT0 1 REMARK
REVDAT 2 05-JUL-17 5UT0 1 JRNL
REVDAT 1 07-JUN-17 5UT0 0
JRNL AUTH D.E.PULEO,K.KUCERA,H.M.HAMMAREN,D.UNGUREANU,A.S.NEWTON,
JRNL AUTH 2 O.SILVENNOINEN,W.L.JORGENSEN,J.SCHLESSINGER
JRNL TITL IDENTIFICATION AND CHARACTERIZATION OF JAK2 PSEUDOKINASE
JRNL TITL 2 DOMAIN SMALL MOLECULE BINDERS.
JRNL REF ACS MED CHEM LETT V. 8 618 2017
JRNL REFN ISSN 1948-5875
JRNL PMID 28626521
JRNL DOI 10.1021/ACSMEDCHEMLETT.7B00153
REMARK 2
REMARK 2 RESOLUTION. 2.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.49
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 16704
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.171
REMARK 3 R VALUE (WORKING SET) : 0.168
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.050
REMARK 3 FREE R VALUE TEST SET COUNT : 843
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 41.4943 - 3.8183 1.00 2702 150 0.1490 0.1699
REMARK 3 2 3.8183 - 3.0309 1.00 2650 141 0.1511 0.2546
REMARK 3 3 3.0309 - 2.6479 1.00 2654 149 0.1834 0.2322
REMARK 3 4 2.6479 - 2.4058 1.00 2623 142 0.1846 0.2412
REMARK 3 5 2.4058 - 2.2334 1.00 2646 136 0.1891 0.2703
REMARK 3 6 2.2334 - 2.1017 0.98 2586 125 0.1904 0.2677
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.200
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.370
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
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 : 0.003 2201
REMARK 3 ANGLE : 0.604 2995
REMARK 3 CHIRALITY : 0.044 334
REMARK 3 PLANARITY : 0.004 389
REMARK 3 DIHEDRAL : 15.098 1303
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 537 THROUGH 556 )
REMARK 3 ORIGIN FOR THE GROUP (A): -2.8116 22.1510 27.4939
REMARK 3 T TENSOR
REMARK 3 T11: 0.1995 T22: 0.1610
REMARK 3 T33: 0.1073 T12: -0.0056
REMARK 3 T13: -0.0122 T23: -0.0635
REMARK 3 L TENSOR
REMARK 3 L11: 3.7444 L22: 3.3886
REMARK 3 L33: 2.8877 L12: -1.2392
REMARK 3 L13: -0.4520 L23: -0.2934
REMARK 3 S TENSOR
REMARK 3 S11: 0.0529 S12: -0.0418 S13: 0.3509
REMARK 3 S21: 0.3561 S22: 0.0935 S23: -0.2410
REMARK 3 S31: -0.2191 S32: 0.2686 S33: -0.1191
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 557 THROUGH 603 )
REMARK 3 ORIGIN FOR THE GROUP (A): -0.3609 21.5610 23.2335
REMARK 3 T TENSOR
REMARK 3 T11: 0.1524 T22: 0.1194
REMARK 3 T33: 0.0944 T12: -0.0383
REMARK 3 T13: -0.0459 T23: -0.0678
REMARK 3 L TENSOR
REMARK 3 L11: 1.6345 L22: 5.0995
REMARK 3 L33: 1.7206 L12: -1.1960
REMARK 3 L13: -0.5869 L23: -1.5534
REMARK 3 S TENSOR
REMARK 3 S11: -0.1310 S12: -0.1134 S13: 0.0994
REMARK 3 S21: 0.3073 S22: 0.1468 S23: -0.0597
REMARK 3 S31: -0.1975 S32: 0.1424 S33: -0.0097
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 604 THROUGH 697 )
REMARK 3 ORIGIN FOR THE GROUP (A): -6.8442 12.6395 11.2508
REMARK 3 T TENSOR
REMARK 3 T11: 0.0843 T22: 0.0869
REMARK 3 T33: 0.1085 T12: 0.0272
REMARK 3 T13: 0.0045 T23: 0.0120
REMARK 3 L TENSOR
REMARK 3 L11: 1.7426 L22: 2.3905
REMARK 3 L33: 2.0693 L12: -0.0725
REMARK 3 L13: -0.3202 L23: 0.6136
REMARK 3 S TENSOR
REMARK 3 S11: 0.0099 S12: 0.0252 S13: 0.0590
REMARK 3 S21: -0.0218 S22: -0.0571 S23: 0.2146
REMARK 3 S31: -0.0860 S32: -0.2450 S33: 0.0266
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 698 THROUGH 748 )
REMARK 3 ORIGIN FOR THE GROUP (A): 3.6811 -0.6870 15.5506
REMARK 3 T TENSOR
REMARK 3 T11: 0.0863 T22: 0.0918
REMARK 3 T33: 0.0834 T12: 0.0135
REMARK 3 T13: -0.0007 T23: 0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 2.4929 L22: 2.7923
REMARK 3 L33: 2.6820 L12: -0.3597
REMARK 3 L13: 1.0675 L23: 0.2171
REMARK 3 S TENSOR
REMARK 3 S11: 0.0821 S12: -0.1027 S13: -0.0783
REMARK 3 S21: 0.2073 S22: -0.0110 S23: -0.1696
REMARK 3 S31: 0.2327 S32: 0.1819 S33: -0.0405
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 749 THROUGH 808 )
REMARK 3 ORIGIN FOR THE GROUP (A): -1.8950 -7.1150 8.1371
REMARK 3 T TENSOR
REMARK 3 T11: 0.1467 T22: 0.0340
REMARK 3 T33: 0.1012 T12: 0.0101
REMARK 3 T13: 0.0273 T23: -0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 2.0025 L22: 2.9507
REMARK 3 L33: 3.6496 L12: -0.1035
REMARK 3 L13: -0.7862 L23: -0.8683
REMARK 3 S TENSOR
REMARK 3 S11: 0.0152 S12: 0.0763 S13: -0.1612
REMARK 3 S21: 0.0142 S22: -0.0913 S23: 0.1685
REMARK 3 S31: 0.0719 S32: 0.1173 S33: 0.0368
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 5UT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-FEB-17.
REMARK 100 THE DEPOSITION ID IS D_1000226414.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-MAR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5-8.5
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 MICROMAX-007 HF
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.54
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 200K
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 16717
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100
REMARK 200 RESOLUTION RANGE LOW (A) : 41.486
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 3.600
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.11000
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.9000
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 (%) : 99.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.32300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.900
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: 4FVP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.0 0.2M SODIUM ACETATE
REMARK 280 12-20% PEG 4,000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 28.84050
REMARK 290 SMTRY3 2 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 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 VAL A 536
REMARK 465 PHE A 809
REMARK 465 THR A 810
REMARK 465 PRO A 811
REMARK 465 ASP A 812
REMARK 465 LEU A 813
REMARK 465 VAL A 814
REMARK 465 PRO A 815
REMARK 465 ARG A 816
REMARK 465 GLY A 817
REMARK 465 SER A 818
REMARK 465 HIS A 819
REMARK 465 HIS A 820
REMARK 465 HIS A 821
REMARK 465 HIS A 822
REMARK 465 HIS A 823
REMARK 465 HIS A 824
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 539 CG CD CE NZ
REMARK 470 LYS A 558 CG CD CE NZ
REMARK 470 ARG A 565 CG CD NE CZ NH1 NH2
REMARK 470 GLN A 572 CG CD OE1 NE2
REMARK 470 LYS A 585 CG CD CE NZ
REMARK 470 GLU A 592 CG CD OE1 OE2
REMARK 470 MET A 600 CG SD CE
REMARK 470 LYS A 603 CG CD CE NZ
REMARK 470 LYS A 639 CG CD CE NZ
REMARK 470 LYS A 640 CG CD CE NZ
REMARK 470 ASN A 643 CG OD1 ND2
REMARK 470 LYS A 677 CG CD CE NZ
REMARK 470 ARG A 687 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 688 CG CD CE NZ
REMARK 470 LYS A 709 CG CD CE NZ
REMARK 470 LYS A 728 CG CD CE NZ
REMARK 470 GLN A 760 CG CD OE1 NE2
REMARK 470 ARG A 769 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 776 CG CD CE NZ
REMARK 470 ARG A 803 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 808 CG CD1 CD2
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 1140 O HOH A 1194 2.09
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 ASN A 548 -140.50 -116.77
REMARK 500 TYR A 570 16.90 59.62
REMARK 500 ASN A 673 62.30 -152.95
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 GOL A 901
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 902
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 35R A 903
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 904
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 905
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5USY RELATED DB: PDB
REMARK 900 RELATED ID: 5USZ RELATED DB: PDB
REMARK 900 RELATED ID: 5UT1 RELATED DB: PDB
REMARK 900 RELATED ID: 5UT2 RELATED DB: PDB
REMARK 900 RELATED ID: 5UT3 RELATED DB: PDB
REMARK 900 RELATED ID: 5UT4 RELATED DB: PDB
REMARK 900 RELATED ID: 5UT5 RELATED DB: PDB
REMARK 900 RELATED ID: 5UT6 RELATED DB: PDB
DBREF 5UT0 A 536 812 UNP O60674 JAK2_HUMAN 536 812
SEQADV 5UT0 ALA A 659 UNP O60674 TRP 659 ENGINEERED MUTATION
SEQADV 5UT0 ALA A 777 UNP O60674 TRP 777 ENGINEERED MUTATION
SEQADV 5UT0 HIS A 794 UNP O60674 PHE 794 ENGINEERED MUTATION
SEQADV 5UT0 LEU A 813 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 VAL A 814 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 PRO A 815 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 ARG A 816 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 GLY A 817 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 SER A 818 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 HIS A 819 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 HIS A 820 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 HIS A 821 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 HIS A 822 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 HIS A 823 UNP O60674 EXPRESSION TAG
SEQADV 5UT0 HIS A 824 UNP O60674 EXPRESSION TAG
SEQRES 1 A 289 VAL PHE HIS LYS ILE ARG ASN GLU ASP LEU ILE PHE ASN
SEQRES 2 A 289 GLU SER LEU GLY GLN GLY THR PHE THR LYS ILE PHE LYS
SEQRES 3 A 289 GLY VAL ARG ARG GLU VAL GLY ASP TYR GLY GLN LEU HIS
SEQRES 4 A 289 GLU THR GLU VAL LEU LEU LYS VAL LEU ASP LYS ALA HIS
SEQRES 5 A 289 ARG ASN TYR SER GLU SER PHE PHE GLU ALA ALA SER MET
SEQRES 6 A 289 MET SER LYS LEU SER HIS LYS HIS LEU VAL LEU ASN TYR
SEQRES 7 A 289 GLY VAL CYS VAL CYS GLY ASP GLU ASN ILE LEU VAL GLN
SEQRES 8 A 289 GLU PHE VAL LYS PHE GLY SER LEU ASP THR TYR LEU LYS
SEQRES 9 A 289 LYS ASN LYS ASN CYS ILE ASN ILE LEU TRP LYS LEU GLU
SEQRES 10 A 289 VAL ALA LYS GLN LEU ALA ALA ALA MET HIS PHE LEU GLU
SEQRES 11 A 289 GLU ASN THR LEU ILE HIS GLY ASN VAL CYS ALA LYS ASN
SEQRES 12 A 289 ILE LEU LEU ILE ARG GLU GLU ASP ARG LYS THR GLY ASN
SEQRES 13 A 289 PRO PRO PHE ILE LYS LEU SER ASP PRO GLY ILE SER ILE
SEQRES 14 A 289 THR VAL LEU PRO LYS ASP ILE LEU GLN GLU ARG ILE PRO
SEQRES 15 A 289 TRP VAL PRO PRO GLU CYS ILE GLU ASN PRO LYS ASN LEU
SEQRES 16 A 289 ASN LEU ALA THR ASP LYS TRP SER PHE GLY THR THR LEU
SEQRES 17 A 289 TRP GLU ILE CYS SER GLY GLY ASP LYS PRO LEU SER ALA
SEQRES 18 A 289 LEU ASP SER GLN ARG LYS LEU GLN PHE TYR GLU ASP ARG
SEQRES 19 A 289 HIS GLN LEU PRO ALA PRO LYS ALA ALA GLU LEU ALA ASN
SEQRES 20 A 289 LEU ILE ASN ASN CYS MET ASP TYR GLU PRO ASP HIS ARG
SEQRES 21 A 289 PRO SER PHE ARG ALA ILE ILE ARG ASP LEU ASN SER LEU
SEQRES 22 A 289 PHE THR PRO ASP LEU VAL PRO ARG GLY SER HIS HIS HIS
SEQRES 23 A 289 HIS HIS HIS
HET GOL A 901 6
HET GOL A 902 6
HET 35R A 903 28
HET ACT A 904 4
HET DMS A 905 4
HETNAM GOL GLYCEROL
HETNAM 35R 1-CYCLOPROPYL-3-{3-[5-(MORPHOLIN-4-YLMETHYL)-1H-
HETNAM 2 35R BENZIMIDAZOL-2-YL]-1H-PYRAZOL-4-YL}UREA
HETNAM ACT ACETATE ION
HETNAM DMS DIMETHYL SULFOXIDE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 2 GOL 2(C3 H8 O3)
FORMUL 4 35R C19 H23 N7 O2
FORMUL 5 ACT C2 H3 O2 1-
FORMUL 6 DMS C2 H6 O S
FORMUL 7 HOH *246(H2 O)
HELIX 1 AA1 ARG A 541 GLU A 543 5 3
HELIX 2 AA2 ASP A 569 GLY A 571 5 3
HELIX 3 AA3 LYS A 585 ASN A 589 5 5
HELIX 4 AA4 TYR A 590 LEU A 604 1 15
HELIX 5 AA5 SER A 633 LYS A 642 1 10
HELIX 6 AA6 ASN A 643 ILE A 645 5 3
HELIX 7 AA7 ASN A 646 ASN A 667 1 22
HELIX 8 AA8 CYS A 675 LYS A 677 5 3
HELIX 9 AA9 ASP A 686 GLY A 690 5 5
HELIX 10 AB1 PRO A 708 ARG A 715 1 8
HELIX 11 AB2 PRO A 720 ASN A 726 1 7
HELIX 12 AB3 PRO A 727 LEU A 730 5 4
HELIX 13 AB4 ASN A 731 SER A 748 1 18
HELIX 14 AB5 ASP A 758 ASP A 768 1 11
HELIX 15 AB6 LEU A 780 MET A 788 1 9
HELIX 16 AB7 GLU A 791 ARG A 795 5 5
HELIX 17 AB8 SER A 797 LEU A 808 1 12
SHEET 1 AA1 5 LEU A 545 GLY A 554 0
SHEET 2 AA1 5 THR A 557 VAL A 567 -1 O LYS A 561 N ASN A 548
SHEET 3 AA1 5 LEU A 573 LEU A 583 -1 O VAL A 582 N LYS A 558
SHEET 4 AA1 5 ILE A 623 GLU A 627 -1 O GLN A 626 N LEU A 579
SHEET 5 AA1 5 ASN A 612 CYS A 616 -1 N GLY A 614 O VAL A 625
SHEET 1 AA2 2 ILE A 679 ARG A 683 0
SHEET 2 AA2 2 PHE A 694 LEU A 697 -1 O LYS A 696 N LEU A 680
CISPEP 1 ILE A 716 PRO A 717 0 4.60
SITE 1 AC1 4 ASN A 673 CYS A 675 ARG A 715 TRP A 718
SITE 1 AC2 4 PHE A 694 HOH A1036 HOH A1101 HOH A1107
SITE 1 AC3 13 LEU A 551 LEU A 579 GLU A 627 PHE A 628
SITE 2 AC3 13 VAL A 629 LYS A 630 PHE A 631 GLY A 632
SITE 3 AC3 13 LEU A 680 HOH A1009 HOH A1021 HOH A1077
SITE 4 AC3 13 HOH A1158
SITE 1 AC4 3 GLY A 619 ASP A 620 ASN A 622
SITE 1 AC5 1 ASN A 782
CRYST1 44.135 57.681 60.443 90.00 109.95 90.00 P 1 21 1 2
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 0.022658 0.000000 0.008225 0.00000
SCALE2 0.000000 0.017337 0.000000 0.00000
SCALE3 0.000000 0.000000 0.017601 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
