HEADER TRANSFERASE/TRANSFERASE INHIBITOR 04-APR-12 4EI4
TITLE JAK1 KINASE (JH1 DOMAIN) IN COMPLEX WITH COMPOUND 20
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: JH1 (KINASE) DOMAIN (UNP RESIDUES 854-1154);
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_TAXID: 7108
KEYWDS PROTEIN KINASE, PHOSPHO-TRANSFER CATALYST, TRANSFERASE-TRANSFERASE
KEYWDS 2 INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.EIGENBROT,M.STEFFEK
REVDAT 6 06-DEC-23 4EI4 1 REMARK
REVDAT 5 13-SEP-23 4EI4 1 REMARK SEQADV LINK
REVDAT 4 15-NOV-17 4EI4 1 REMARK
REVDAT 3 23-JAN-13 4EI4 1 JRNL
REVDAT 2 02-JAN-13 4EI4 1 JRNL
REVDAT 1 04-JUL-12 4EI4 0
JRNL AUTH M.ZAK,R.MENDONCA,M.BALAZS,K.BARRETT,P.BERGERON,W.S.BLAIR,
JRNL AUTH 2 C.CHANG,G.DESHMUKH,J.DEVOSS,P.S.DRAGOVICH,C.EIGENBROT,
JRNL AUTH 3 N.GHILARDI,P.GIBBONS,S.GRADL,C.HAMMAN,E.J.HANAN,E.HARSTAD,
JRNL AUTH 4 P.R.HEWITT,C.A.HURLEY,T.JIN,A.JOHNSON,T.JOHNSON,J.R.KENNY,
JRNL AUTH 5 M.F.KOEHLER,P.BIR KOHLI,J.J.KULAGOWSKI,S.LABADIE,J.LIAO,
JRNL AUTH 6 M.LIIMATTA,Z.LIN,P.J.LUPARDUS,R.J.MAXEY,J.M.MURRAY,R.PULK,
JRNL AUTH 7 M.RODRIGUEZ,S.SAVAGE,S.SHIA,M.STEFFEK,S.UBHAYAKAR,M.ULTSCH,
JRNL AUTH 8 A.VAN ABBEMA,S.I.WARD,L.XIAO,Y.XIAO
JRNL TITL DISCOVERY AND OPTIMIZATION OF C-2 METHYL
JRNL TITL 2 IMIDAZOPYRROLOPYRIDINES AS POTENT AND ORALLY BIOAVAILABLE
JRNL TITL 3 JAK1 INHIBITORS WITH SELECTIVITY OVER JAK2.
JRNL REF J.MED.CHEM. V. 55 6176 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22698084
JRNL DOI 10.1021/JM300628C
REMARK 2
REMARK 2 RESOLUTION. 2.22 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.22
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 3 NUMBER OF REFLECTIONS : 30234
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) : 0.202
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.239
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.800
REMARK 3 FREE R VALUE TEST SET COUNT : 1513
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 10
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.22
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.34
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4394
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.91
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE SET COUNT : 233
REMARK 3 BIN FREE R VALUE : 0.2670
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4661
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 40
REMARK 3 SOLVENT ATOMS : 116
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 40.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.27
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.96000
REMARK 3 B22 (A**2) : 0.74000
REMARK 3 B33 (A**2) : 0.13000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -0.53000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.300
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.216
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.167
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.363
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.947
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.931
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4807 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3354 ; 0.006 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6486 ; 1.135 ; 1.990
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8193 ; 0.829 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 567 ; 5.693 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 221 ;37.659 ;24.389
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 894 ;12.443 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;15.769 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 691 ; 0.061 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5203 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 931 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 914 ; 0.195 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3360 ; 0.189 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2290 ; 0.175 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2355 ; 0.081 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 128 ; 0.155 ; 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): 12 ; 0.184 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 43 ; 0.222 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 11 ; 0.208 ; 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): 2997 ; 3.109 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1151 ; 0.785 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4617 ; 3.947 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2141 ; 3.197 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1869 ; 4.481 ; 5.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : 1
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 850 A 1160 4
REMARK 3 1 B 850 B 1160 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3910 ; 0.35 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3910 ; 0.70 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 853 A 959
REMARK 3 ORIGIN FOR THE GROUP (A): -6.4283 60.5524 -3.4399
REMARK 3 T TENSOR
REMARK 3 T11: -0.0451 T22: -0.0224
REMARK 3 T33: 0.0373 T12: -0.0337
REMARK 3 T13: -0.0103 T23: -0.0563
REMARK 3 L TENSOR
REMARK 3 L11: 1.4564 L22: 0.4368
REMARK 3 L33: 2.1202 L12: -0.0616
REMARK 3 L13: 0.8141 L23: -0.7439
REMARK 3 S TENSOR
REMARK 3 S11: -0.0001 S12: 0.0653 S13: -0.2324
REMARK 3 S21: -0.0642 S22: 0.0599 S23: 0.1263
REMARK 3 S31: 0.1249 S32: -0.0025 S33: -0.0598
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 960 A 2000
REMARK 3 ORIGIN FOR THE GROUP (A): 12.8804 51.1830 16.0977
REMARK 3 T TENSOR
REMARK 3 T11: -0.0351 T22: -0.0505
REMARK 3 T33: 0.0051 T12: -0.0192
REMARK 3 T13: 0.0119 T23: -0.0102
REMARK 3 L TENSOR
REMARK 3 L11: 1.3540 L22: 0.9536
REMARK 3 L33: 0.5502 L12: -0.0337
REMARK 3 L13: 0.1487 L23: -0.1986
REMARK 3 S TENSOR
REMARK 3 S11: -0.0008 S12: -0.0513 S13: -0.1797
REMARK 3 S21: 0.0825 S22: 0.0535 S23: 0.0429
REMARK 3 S31: -0.0151 S32: -0.0049 S33: -0.0528
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 853 B 959
REMARK 3 ORIGIN FOR THE GROUP (A): 24.6403 2.8254 -3.0362
REMARK 3 T TENSOR
REMARK 3 T11: -0.0390 T22: -0.0358
REMARK 3 T33: -0.0568 T12: 0.0064
REMARK 3 T13: 0.0043 T23: 0.0004
REMARK 3 L TENSOR
REMARK 3 L11: 1.9928 L22: 1.0047
REMARK 3 L33: 1.4683 L12: -0.0943
REMARK 3 L13: -0.1206 L23: 0.1447
REMARK 3 S TENSOR
REMARK 3 S11: 0.0618 S12: 0.0754 S13: 0.0154
REMARK 3 S21: -0.1586 S22: 0.0050 S23: -0.1440
REMARK 3 S31: 0.0226 S32: 0.0513 S33: -0.0668
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 960 B 2000
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3815 10.3688 15.5699
REMARK 3 T TENSOR
REMARK 3 T11: -0.0504 T22: -0.0072
REMARK 3 T33: -0.0622 T12: -0.0150
REMARK 3 T13: -0.0032 T23: -0.0414
REMARK 3 L TENSOR
REMARK 3 L11: 1.5914 L22: 1.2563
REMARK 3 L33: 0.6509 L12: 0.1585
REMARK 3 L13: -0.1137 L23: 0.1753
REMARK 3 S TENSOR
REMARK 3 S11: 0.0316 S12: -0.2237 S13: 0.1996
REMARK 3 S21: 0.0450 S22: 0.0342 S23: 0.1032
REMARK 3 S31: -0.0116 S32: 0.0218 S33: -0.0658
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 4EI4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071646.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-JUN-10
REMARK 200 TEMPERATURE (KELVIN) : 110
REMARK 200 PH : 5.5
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) : 1.0
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32187
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.220
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 200 DATA REDUNDANCY : 3.200
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06900
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.22
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.30
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.38300
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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: PDB ENTRY 2B7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000, PH 5.5, VAPOR DIFFUSION,
REMARK 280 SITTING DROP, TEMPERATURE 300K
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 86.66100
REMARK 290 SMTRY3 2 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 ASN A 917
REMARK 465 GLU A 946
REMARK 465 ASP A 947
REMARK 465 GLY A 948
REMARK 465 GLY A 949
REMARK 465 ASN A 950
REMARK 465 GLY B 853
REMARK 465 ASP B 854
REMARK 465 ILE B 855
REMARK 465 VAL B 856
REMARK 465 SER B 857
REMARK 465 GLU B 858
REMARK 465 LYS B 859
REMARK 465 LYS B 860
REMARK 465 PRO B 861
REMARK 465 ALA B 862
REMARK 465 THR B 863
REMARK 465 GLU B 864
REMARK 465 GLU B 913
REMARK 465 SER B 914
REMARK 465 GLY B 915
REMARK 465 GLY B 916
REMARK 465 GLU B 946
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: 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 GLY A 884 O HOH A 1326 2.15
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 GLU A 883 -177.38 -172.75
REMARK 500 HIS A 885 -77.17 83.34
REMARK 500 ASP A1003 31.87 -152.81
REMARK 500 ASP A1042 42.94 -105.53
REMARK 500 ILE B 878 -64.02 -104.94
REMARK 500 GLN B 998 39.72 70.47
REMARK 500 ASP B1003 31.16 -148.94
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 0Q2 A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0Q2 B 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4EHZ RELATED DB: PDB
REMARK 900 RELATED ID: 4F08 RELATED DB: PDB
REMARK 900 RELATED ID: 4F09 RELATED DB: PDB
DBREF 4EI4 A 854 1154 UNP P23458 JAK1_HUMAN 854 1154
DBREF 4EI4 B 854 1154 UNP P23458 JAK1_HUMAN 854 1154
SEQADV 4EI4 GLY A 853 UNP P23458 EXPRESSION TAG
SEQADV 4EI4 GLY B 853 UNP P23458 EXPRESSION TAG
SEQRES 1 A 302 GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL
SEQRES 2 A 302 ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE
SEQRES 3 A 302 ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU
SEQRES 4 A 302 CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN
SEQRES 5 A 302 VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN
SEQRES 6 A 302 HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG
SEQRES 7 A 302 ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE
SEQRES 8 A 302 CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET
SEQRES 9 A 302 GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO
SEQRES 10 A 302 LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS
SEQRES 11 A 302 TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY
SEQRES 12 A 302 SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN
SEQRES 13 A 302 VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP
SEQRES 14 A 302 PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR
SEQRES 15 A 302 PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP
SEQRES 16 A 302 TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE
SEQRES 17 A 302 ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU
SEQRES 18 A 302 LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA
SEQRES 19 A 302 LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET
SEQRES 20 A 302 THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS
SEQRES 21 A 302 ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR
SEQRES 22 A 302 GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN
SEQRES 23 A 302 ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA
SEQRES 24 A 302 LEU LEU LYS
SEQRES 1 B 302 GLY ASP ILE VAL SER GLU LYS LYS PRO ALA THR GLU VAL
SEQRES 2 B 302 ASP PRO THR HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE
SEQRES 3 B 302 ARG ASP LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU
SEQRES 4 B 302 CYS ARG TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN
SEQRES 5 B 302 VAL ALA VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN
SEQRES 6 B 302 HIS ILE ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG
SEQRES 7 B 302 ASN LEU TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE
SEQRES 8 B 302 CYS THR GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET
SEQRES 9 B 302 GLU PHE LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO
SEQRES 10 B 302 LYS ASN LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS
SEQRES 11 B 302 TYR ALA VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY
SEQRES 12 B 302 SER ARG GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN
SEQRES 13 B 302 VAL LEU VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP
SEQRES 14 B 302 PHE GLY LEU THR LYS ALA ILE GLU THR ASP LYS GLU PTR
SEQRES 15 B 302 PTR THR VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP
SEQRES 16 B 302 TYR ALA PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE
SEQRES 17 B 302 ALA SER ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU
SEQRES 18 B 302 LEU LEU THR TYR CYS ASP SER ASP SER SER PRO MET ALA
SEQRES 19 B 302 LEU PHE LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET
SEQRES 20 B 302 THR VAL THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS
SEQRES 21 B 302 ARG LEU PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR
SEQRES 22 B 302 GLN LEU MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN
SEQRES 23 B 302 ARG THR SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA
SEQRES 24 B 302 LEU LEU LYS
MODRES 4EI4 PTR A 1034 TYR O-PHOSPHOTYROSINE
MODRES 4EI4 PTR A 1035 TYR O-PHOSPHOTYROSINE
MODRES 4EI4 PTR B 1034 TYR O-PHOSPHOTYROSINE
MODRES 4EI4 PTR B 1035 TYR O-PHOSPHOTYROSINE
HET PTR A1034 16
HET PTR A1035 16
HET PTR B1034 16
HET PTR B1035 16
HET 0Q2 A1201 20
HET 0Q2 B1201 20
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM 0Q2 (1R,3R)-3-(2-METHYLIMIDAZO[4,5-D]PYRROLO[2,3-B]PYRIDIN-
HETNAM 2 0Q2 1(8H)-YL)CYCLOHEXANOL
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR 4(C9 H12 N O6 P)
FORMUL 3 0Q2 2(C15 H18 N4 O)
FORMUL 5 HOH *116(H2 O)
HELIX 1 1 GLU A 871 ARG A 873 5 3
HELIX 2 2 ILE A 919 ASN A 931 1 13
HELIX 3 3 SER A 963 ASN A 971 1 9
HELIX 4 4 ASN A 976 ARG A 997 1 22
HELIX 5 5 ALA A 1005 ARG A 1007 5 3
HELIX 6 6 PRO A 1044 TYR A 1048 5 5
HELIX 7 7 ALA A 1049 SER A 1056 1 8
HELIX 8 8 TYR A 1059 THR A 1076 1 18
HELIX 9 9 ASP A 1079 SER A 1082 5 4
HELIX 10 10 SER A 1083 GLY A 1093 1 11
HELIX 11 11 HIS A 1096 GLN A 1098 5 3
HELIX 12 12 MET A 1099 GLU A 1110 1 12
HELIX 13 13 PRO A 1121 LYS A 1130 1 10
HELIX 14 14 CYS A 1131 GLU A 1133 5 3
HELIX 15 15 GLN A 1135 ARG A 1139 5 5
HELIX 16 16 SER A 1141 LYS A 1154 1 14
HELIX 17 17 GLU B 871 ARG B 873 5 3
HELIX 18 18 HIS B 918 ASN B 931 1 14
HELIX 19 19 SER B 963 LYS B 972 1 10
HELIX 20 20 ASN B 976 ARG B 997 1 22
HELIX 21 21 ALA B 1005 ARG B 1007 5 3
HELIX 22 22 PRO B 1044 TYR B 1048 5 5
HELIX 23 23 ALA B 1049 SER B 1056 1 8
HELIX 24 24 ILE B 1060 THR B 1076 1 17
HELIX 25 25 ASP B 1079 SER B 1082 5 4
HELIX 26 26 SER B 1083 GLY B 1093 1 11
HELIX 27 27 HIS B 1096 GLN B 1098 5 3
HELIX 28 28 MET B 1099 GLU B 1110 1 12
HELIX 29 29 PRO B 1121 LYS B 1130 1 10
HELIX 30 30 CYS B 1131 GLU B 1133 5 3
HELIX 31 31 GLN B 1135 ARG B 1139 5 5
HELIX 32 32 SER B 1141 LYS B 1154 1 14
SHEET 1 A 5 LEU A 875 GLY A 884 0
SHEET 2 A 5 GLY A 887 TYR A 894 -1 O LEU A 891 N ARG A 879
SHEET 3 A 5 GLU A 903 LEU A 910 -1 O VAL A 907 N GLU A 890
SHEET 4 A 5 LYS A 953 GLU A 957 -1 O MET A 956 N ALA A 906
SHEET 5 A 5 TYR A 940 CYS A 944 -1 N GLY A 942 O ILE A 955
SHEET 1 B 2 TYR A 999 VAL A1000 0
SHEET 2 B 2 LYS A1026 ALA A1027 -1 O LYS A1026 N VAL A1000
SHEET 1 C 2 VAL A1009 SER A1013 0
SHEET 2 C 2 GLN A1016 ILE A1019 -1 O LYS A1018 N LEU A1010
SHEET 1 D 2 PTR A1035 THR A1036 0
SHEET 2 D 2 LYS A1057 PHE A1058 -1 O PHE A1058 N PTR A1035
SHEET 1 E 5 LEU B 875 GLU B 883 0
SHEET 2 E 5 GLY B 887 TYR B 894 -1 O LEU B 891 N ARG B 879
SHEET 3 E 5 GLU B 903 LEU B 910 -1 O GLU B 903 N TYR B 894
SHEET 4 E 5 LYS B 953 GLU B 957 -1 O MET B 956 N ALA B 906
SHEET 5 E 5 TYR B 940 CYS B 944 -1 N GLY B 942 O ILE B 955
SHEET 1 F 2 TYR B 999 VAL B1000 0
SHEET 2 F 2 LYS B1026 ALA B1027 -1 O LYS B1026 N VAL B1000
SHEET 1 G 2 VAL B1009 SER B1013 0
SHEET 2 G 2 GLN B1016 ILE B1019 -1 O LYS B1018 N LEU B1010
SHEET 1 H 2 PTR B1034 THR B1036 0
SHEET 2 H 2 LYS B1057 TYR B1059 -1 O PHE B1058 N PTR B1035
LINK C GLU A1033 N PTR A1034 1555 1555 1.33
LINK C PTR A1034 N PTR A1035 1555 1555 1.33
LINK C PTR A1035 N THR A1036 1555 1555 1.33
LINK C GLU B1033 N PTR B1034 1555 1555 1.33
LINK C PTR B1034 N PTR B1035 1555 1555 1.33
LINK C PTR B1035 N THR B1036 1555 1555 1.33
SITE 1 AC1 12 LEU A 881 VAL A 889 ALA A 906 GLU A 957
SITE 2 AC1 12 PHE A 958 LEU A 959 GLY A 962 GLU A 966
SITE 3 AC1 12 ARG A1007 ASN A1008 LEU A1010 GLY A1020
SITE 1 AC2 12 LEU B 881 VAL B 889 ALA B 906 GLU B 957
SITE 2 AC2 12 PHE B 958 LEU B 959 GLY B 962 GLU B 966
SITE 3 AC2 12 ARG B1007 ASN B1008 LEU B1010 HOH B1313
CRYST1 42.755 173.322 44.595 90.00 94.27 90.00 P 1 21 1 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 0.023389 0.000000 0.001748 0.00000
SCALE2 0.000000 0.005770 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022487 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
