HEADER TRANSFERASE 29-SEP-15 5E1E
TITLE HUMAN JAK1 KINASE IN COMPLEX WITH COMPOUND 30 AT 2.30 ANGSTROMS
TITLE 2 RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PROTEIN KINASE 2 DOMAIN RESIDUES 865-1154;
COMPND 5 SYNONYM: JANUS KINASE 1,JAK-1;
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: JAK1, JAK1A, JAK1B;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.D.FERGUSON
REVDAT 3 30-DEC-15 5E1E 1 JRNL
REVDAT 2 16-DEC-15 5E1E 1 JRNL
REVDAT 1 25-NOV-15 5E1E 0
JRNL AUTH M.M.VASBINDER,M.ALIMZHANOV,M.AUGUSTIN,G.BEBERNITZ,K.BELL,
JRNL AUTH 2 C.CHUAQUI,T.DEEGAN,A.D.FERGUSON,K.GOODWIN,D.HUSZAR,
JRNL AUTH 3 A.KAWATKAR,S.KAWATKAR,J.READ,J.SHI,S.STEINBACHER,H.STEUBER,
JRNL AUTH 4 Q.SU,D.TOADER,H.WANG,R.WOESSNER,A.WU,M.YE,M.ZINDA
JRNL TITL IDENTIFICATION OF AZABENZIMIDAZOLES AS POTENT JAK1 SELECTIVE
JRNL TITL 2 INHIBITORS.
JRNL REF BIOORG.MED.CHEM.LETT. V. 26 60 2016
JRNL REFN ESSN 1464-3405
JRNL PMID 26614408
JRNL DOI 10.1016/J.BMCL.2015.11.031
REMARK 2
REMARK 2 RESOLUTION. 2.30 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) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.73
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 30693
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) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.225
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.270
REMARK 3 FREE R VALUE TEST SET COUNT : 1312
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 : 15
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.38
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.23
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2950
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2384
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2823
REMARK 3 BIN R VALUE (WORKING SET) : 0.2355
REMARK 3 BIN FREE R VALUE : 0.3053
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.31
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 127
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 : 4591
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 65
REMARK 3 SOLVENT ATOMS : 227
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 44.93
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 43.37
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 2.99270
REMARK 3 B22 (A**2) : -0.31510
REMARK 3 B33 (A**2) : -2.67760
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) : 0.325
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.370
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.250
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.347
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.247
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 : 0.937
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 4827 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 6513 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 1745 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 123 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 728 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 4827 ; 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 : 587 ; 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 : 5524 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.18
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.57
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|867 - A|959 }
REMARK 3 ORIGIN FOR THE GROUP (A): -5.9740 -19.4140 15.0570
REMARK 3 T TENSOR
REMARK 3 T11: -0.0313 T22: 0.0868
REMARK 3 T33: -0.0313 T12: -0.0170
REMARK 3 T13: -0.0288 T23: -0.0201
REMARK 3 L TENSOR
REMARK 3 L11: 2.7456 L22: 3.8336
REMARK 3 L33: 1.2851 L12: 0.9631
REMARK 3 L13: -0.6017 L23: -0.8177
REMARK 3 S TENSOR
REMARK 3 S11: 0.0861 S12: -0.3458 S13: 0.1309
REMARK 3 S21: 0.2585 S22: -0.1475 S23: -0.0875
REMARK 3 S31: -0.2010 S32: 0.1450 S33: 0.0614
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|961 - A|1154 }
REMARK 3 ORIGIN FOR THE GROUP (A): -22.2400 -37.7960 23.4880
REMARK 3 T TENSOR
REMARK 3 T11: 0.0013 T22: 0.1495
REMARK 3 T33: 0.0134 T12: -0.0212
REMARK 3 T13: -0.0265 T23: 0.0681
REMARK 3 L TENSOR
REMARK 3 L11: 3.3834 L22: 0.7403
REMARK 3 L33: 1.5177 L12: 0.0979
REMARK 3 L13: 0.6399 L23: -0.3185
REMARK 3 S TENSOR
REMARK 3 S11: 0.0772 S12: -0.5779 S13: -0.4077
REMARK 3 S21: 0.0837 S22: -0.0755 S23: -0.0274
REMARK 3 S31: 0.1179 S32: -0.1654 S33: -0.0016
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { B|867 - B|959 }
REMARK 3 ORIGIN FOR THE GROUP (A): -9.4120 24.5780 15.2320
REMARK 3 T TENSOR
REMARK 3 T11: -0.0168 T22: 0.1036
REMARK 3 T33: -0.0437 T12: -0.0157
REMARK 3 T13: -0.0254 T23: -0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 1.7162 L22: 3.1789
REMARK 3 L33: 1.0996 L12: 0.4941
REMARK 3 L13: -0.7192 L23: -0.7138
REMARK 3 S TENSOR
REMARK 3 S11: 0.0581 S12: -0.1811 S13: 0.1468
REMARK 3 S21: 0.1491 S22: -0.0570 S23: -0.1515
REMARK 3 S31: -0.2519 S32: 0.2717 S33: -0.0011
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { B|961 - B|1154 }
REMARK 3 ORIGIN FOR THE GROUP (A): -25.9230 6.3090 23.3770
REMARK 3 T TENSOR
REMARK 3 T11: 0.0403 T22: 0.1110
REMARK 3 T33: -0.0122 T12: -0.0092
REMARK 3 T13: -0.0249 T23: 0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 3.1254 L22: 0.8529
REMARK 3 L33: 1.1440 L12: 0.0792
REMARK 3 L13: 0.4627 L23: -0.1817
REMARK 3 S TENSOR
REMARK 3 S11: 0.0319 S12: -0.4217 S13: -0.2304
REMARK 3 S21: 0.0684 S22: -0.0830 S23: -0.0198
REMARK 3 S31: 0.1499 S32: -0.1608 S33: 0.0511
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5E1E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-OCT-15.
REMARK 100 THE DEPOSITION ID IS D_1000214170.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 16-AUG-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9999
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30744
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 87.460
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.11000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.45
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.5
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.67800
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.72
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% (M/V) PEG6000, 0.1 M MES/NAOH PH
REMARK 280 6.0 AND 5 MM DTT, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
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 21.54750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 87.46400
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.35400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 87.46400
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.54750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.35400
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 PRO A 912
REMARK 465 GLU A 913
REMARK 465 SER A 914
REMARK 465 GLY A 915
REMARK 465 GLY A 916
REMARK 465 GLU A 946
REMARK 465 ASP A 947
REMARK 465 GLY A 948
REMARK 465 GLY A 949
REMARK 465 PRO B 912
REMARK 465 GLU B 913
REMARK 465 SER B 914
REMARK 465 GLY B 915
REMARK 465 GLY B 916
REMARK 465 ASP B 947
REMARK 465 GLY B 948
REMARK 465 GLY B 949
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 ASP A 895 71.26 -118.90
REMARK 500 GLN A 998 46.93 70.31
REMARK 500 ARG A1002 -0.01 64.83
REMARK 500 ASP A1003 34.11 -140.69
REMARK 500 ASP A1021 87.79 50.16
REMARK 500 ASP A1042 41.30 -107.99
REMARK 500 ILE B 878 -62.38 -103.38
REMARK 500 ILE B 878 -67.91 -103.38
REMARK 500 ASP B 895 71.62 -118.70
REMARK 500 ASP B1003 33.88 -141.01
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 PEG A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5JG A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 5JG B 1201
DBREF 5E1E A 865 1154 UNP P23458 JAK1_HUMAN 865 1154
DBREF 5E1E B 865 1154 UNP P23458 JAK1_HUMAN 865 1154
SEQRES 1 A 290 VAL ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG
SEQRES 2 A 290 ILE ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU
SEQRES 3 A 290 LEU CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU
SEQRES 4 A 290 GLN VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY
SEQRES 5 A 290 ASN HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU
SEQRES 6 A 290 ARG ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY
SEQRES 7 A 290 ILE CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE
SEQRES 8 A 290 MET GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU
SEQRES 9 A 290 PRO LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU
SEQRES 10 A 290 LYS TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU
SEQRES 11 A 290 GLY SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG
SEQRES 12 A 290 ASN VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY
SEQRES 13 A 290 ASP PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU
SEQRES 14 A 290 PTR PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE
SEQRES 15 A 290 TRP TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR
SEQRES 16 A 290 ILE ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS
SEQRES 17 A 290 GLU LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET
SEQRES 18 A 290 ALA LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN
SEQRES 19 A 290 MET THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY
SEQRES 20 A 290 LYS ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL
SEQRES 21 A 290 TYR GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER
SEQRES 22 A 290 ASN ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU
SEQRES 23 A 290 ALA LEU LEU LYS
SEQRES 1 B 290 VAL ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG
SEQRES 2 B 290 ILE ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU
SEQRES 3 B 290 LEU CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU
SEQRES 4 B 290 GLN VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY
SEQRES 5 B 290 ASN HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU
SEQRES 6 B 290 ARG ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY
SEQRES 7 B 290 ILE CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE
SEQRES 8 B 290 MET GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU
SEQRES 9 B 290 PRO LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU
SEQRES 10 B 290 LYS TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU
SEQRES 11 B 290 GLY SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG
SEQRES 12 B 290 ASN VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY
SEQRES 13 B 290 ASP PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU
SEQRES 14 B 290 PTR PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE
SEQRES 15 B 290 TRP TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR
SEQRES 16 B 290 ILE ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS
SEQRES 17 B 290 GLU LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET
SEQRES 18 B 290 ALA LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN
SEQRES 19 B 290 MET THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY
SEQRES 20 B 290 LYS ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL
SEQRES 21 B 290 TYR GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER
SEQRES 22 B 290 ASN ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU
SEQRES 23 B 290 ALA LEU LEU LYS
MODRES 5E1E PTR A 1034 TYR MODIFIED RESIDUE
MODRES 5E1E PTR A 1035 TYR MODIFIED RESIDUE
MODRES 5E1E PTR B 1034 TYR MODIFIED RESIDUE
MODRES 5E1E PTR B 1035 TYR MODIFIED RESIDUE
HET PTR A1034 16
HET PTR A1035 16
HET PTR B1034 16
HET PTR B1035 16
HET PEG A1201 7
HET 5JG A1202 29
HET 5JG B1201 29
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM 5JG 6-CHLORO-2-(2-FLUORO-4,5-DIMETHOXYPHENYL)-N-(PIPERIDIN-
HETNAM 2 5JG 4-YLMETHYL)-3H-IMIDAZO[4,5-B]PYRIDIN-7-AMINE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR 4(C9 H12 N O6 P)
FORMUL 3 PEG C4 H10 O3
FORMUL 4 5JG 2(C20 H23 CL F N5 O2)
FORMUL 6 HOH *227(H2 O)
HELIX 1 AA1 GLU A 871 ARG A 873 5 3
HELIX 2 AA2 HIS A 918 ASN A 931 1 14
HELIX 3 AA3 SER A 963 ASN A 971 1 9
HELIX 4 AA4 ASN A 976 ARG A 997 1 22
HELIX 5 AA5 ALA A 1005 ARG A 1007 5 3
HELIX 6 AA6 PRO A 1044 TYR A 1048 5 5
HELIX 7 AA7 ALA A 1049 GLN A 1055 1 7
HELIX 8 AA8 ILE A 1060 THR A 1076 1 17
HELIX 9 AA9 ASP A 1079 SER A 1082 5 4
HELIX 10 AB1 SER A 1083 GLY A 1093 1 11
HELIX 11 AB2 HIS A 1096 GLN A 1098 5 3
HELIX 12 AB3 MET A 1099 GLU A 1110 1 12
HELIX 13 AB4 PRO A 1121 LYS A 1130 1 10
HELIX 14 AB5 CYS A 1131 GLU A 1133 5 3
HELIX 15 AB6 GLN A 1135 ARG A 1139 5 5
HELIX 16 AB7 SER A 1141 LYS A 1154 1 14
HELIX 17 AB8 GLU B 871 ARG B 873 5 3
HELIX 18 AB9 HIS B 918 ASN B 931 1 14
HELIX 19 AC1 SER B 963 LEU B 968 1 6
HELIX 20 AC2 PRO B 969 ASN B 971 5 3
HELIX 21 AC3 ASN B 976 ARG B 997 1 22
HELIX 22 AC4 ALA B 1005 ARG B 1007 5 3
HELIX 23 AC5 PRO B 1044 TYR B 1048 5 5
HELIX 24 AC6 ALA B 1049 GLN B 1055 1 7
HELIX 25 AC7 ILE B 1060 THR B 1076 1 17
HELIX 26 AC8 ASP B 1079 SER B 1082 5 4
HELIX 27 AC9 SER B 1083 GLY B 1093 1 11
HELIX 28 AD1 HIS B 1096 GLN B 1098 5 3
HELIX 29 AD2 MET B 1099 GLU B 1110 1 12
HELIX 30 AD3 PRO B 1121 LYS B 1130 1 10
HELIX 31 AD4 CYS B 1131 GLU B 1133 5 3
HELIX 32 AD5 GLN B 1135 ARG B 1139 5 5
HELIX 33 AD6 SER B 1141 LYS B 1154 1 14
SHEET 1 AA1 5 LEU A 875 GLU A 883 0
SHEET 2 AA1 5 GLY A 887 TYR A 894 -1 O LEU A 891 N ILE A 878
SHEET 3 AA1 5 GLU A 903 LEU A 910 -1 O VAL A 907 N GLU A 890
SHEET 4 AA1 5 LYS A 953 GLU A 957 -1 O MET A 956 N ALA A 906
SHEET 5 AA1 5 TYR A 940 CYS A 944 -1 N LYS A 941 O ILE A 955
SHEET 1 AA2 2 TYR A 999 VAL A1000 0
SHEET 2 AA2 2 LYS A1026 ALA A1027 -1 O LYS A1026 N VAL A1000
SHEET 1 AA3 2 VAL A1009 SER A1013 0
SHEET 2 AA3 2 GLN A1016 ILE A1019 -1 O LYS A1018 N LEU A1010
SHEET 1 AA4 2 PTR A1034 THR A1036 0
SHEET 2 AA4 2 LYS A1057 TYR A1059 -1 O PHE A1058 N PTR A1035
SHEET 1 AA5 5 LEU B 875 GLY B 884 0
SHEET 2 AA5 5 GLY B 887 TYR B 894 -1 O LEU B 891 N ARG B 879
SHEET 3 AA5 5 GLU B 903 LEU B 910 -1 O VAL B 907 N GLU B 890
SHEET 4 AA5 5 ILE B 952 GLU B 957 -1 O MET B 956 N ALA B 906
SHEET 5 AA5 5 TYR B 940 THR B 945 -1 N LYS B 941 O ILE B 955
SHEET 1 AA6 2 TYR B 999 VAL B1000 0
SHEET 2 AA6 2 LYS B1026 ALA B1027 -1 O LYS B1026 N VAL B1000
SHEET 1 AA7 2 VAL B1009 SER B1013 0
SHEET 2 AA7 2 GLN B1016 ILE B1019 -1 O LYS B1018 N LEU B1010
SHEET 1 AA8 2 PTR B1034 THR B1036 0
SHEET 2 AA8 2 LYS B1057 TYR B1059 -1 O PHE B1058 N PTR B1035
LINK C GLU A1033 N PTR A1034 1555 1555 1.35
LINK C PTR A1034 N PTR A1035 1555 1555 1.35
LINK C PTR A1035 N THR A1036 1555 1555 1.35
LINK C GLU B1033 N PTR B1034 1555 1555 1.34
LINK C PTR B1034 N PTR B1035 1555 1555 1.35
LINK C PTR B1035 N THR B1036 1555 1555 1.36
SITE 1 AC1 4 ARG A 879 ARG A 893 GLN A 904 HOH A1329
SITE 1 AC2 14 LEU A 881 ALA A 906 MET A 956 GLU A 957
SITE 2 AC2 14 PHE A 958 LEU A 959 PRO A 960 GLY A 962
SITE 3 AC2 14 GLU A 966 ARG A1007 ASN A1008 LEU A1010
SITE 4 AC2 14 ASP A1021 HOH A1391
SITE 1 AC3 14 LEU B 881 ALA B 906 MET B 956 GLU B 957
SITE 2 AC3 14 PHE B 958 LEU B 959 PRO B 960 GLY B 962
SITE 3 AC3 14 GLU B 966 ARG B1007 ASN B1008 LEU B1010
SITE 4 AC3 14 GLY B1020 ASP B1021
CRYST1 43.095 88.708 174.928 90.00 90.00 90.00 P 21 21 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 0.023205 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011273 0.000000 0.00000
SCALE3 0.000000 0.000000 0.005717 0.00000
(ATOM LINES ARE NOT SHOWN.)
END