HEADER TRANSFERASE/TRANSFERASE INHIBITOR 13-MAR-12 4E4N
TITLE JAK1 KINASE (JH1 DOMAIN) IN COMPLEX WITH COMPOUND 49
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: PROTEIN KINASE DOMAIN JH1, 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_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS O-PHOSPHOTYROSINE, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR C.EIGENBROT
REVDAT 4 06-DEC-23 4E4N 1 REMARK
REVDAT 3 13-SEP-23 4E4N 1 REMARK SEQADV LINK
REVDAT 2 11-JUL-12 4E4N 1 JRNL
REVDAT 1 30-MAY-12 4E4N 0
JRNL AUTH J.J.KULAGOWSKI,W.BLAIR,R.J.BULL,C.CHANG,G.DESHMUKH,H.J.DYKE,
JRNL AUTH 2 C.EIGENBROT,N.GHILARDI,P.GIBBONS,T.K.HARRISON,P.R.HEWITT,
JRNL AUTH 3 M.LIIMATTA,C.A.HURLEY,A.JOHNSON,T.JOHNSON,J.R.KENNY,
JRNL AUTH 4 P.BIR KOHLI,R.J.MAXEY,R.MENDONCA,K.MORTARA,J.MURRAY,
JRNL AUTH 5 R.NARUKULLA,S.SHIA,M.STEFFEK,S.UBHAYAKAR,M.ULTSCH,
JRNL AUTH 6 A.VAN ABBEMA,S.I.WARD,B.WASZKOWYCZ,M.ZAK
JRNL TITL IDENTIFICATION OF IMIDAZO-PYRROLOPYRIDINES AS NOVEL AND
JRNL TITL 2 POTENT JAK1 INHIBITORS.
JRNL REF J.MED.CHEM. V. 55 5901 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22591402
JRNL DOI 10.1021/JM300438J
REMARK 2
REMARK 2 RESOLUTION. 1.90 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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.0
REMARK 3 NUMBER OF REFLECTIONS : 47965
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) : 0.183
REMARK 3 R VALUE (WORKING SET) : 0.181
REMARK 3 FREE R VALUE : 0.226
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.600
REMARK 3 FREE R VALUE TEST SET COUNT : 2336
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00
REMARK 3 REFLECTION IN BIN (WORKING SET) : 6615
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.67
REMARK 3 BIN R VALUE (WORKING SET) : 0.2310
REMARK 3 BIN FREE R VALUE SET COUNT : 322
REMARK 3 BIN FREE R VALUE : 0.2700
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4677
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 50
REMARK 3 SOLVENT ATOMS : 294
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 27.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 32.84
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.69000
REMARK 3 B22 (A**2) : -0.02000
REMARK 3 B33 (A**2) : 0.73000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.15000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.149
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.141
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.098
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.468
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.959
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.944
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4834 ; 0.010 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3367 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 6526 ; 1.171 ; 1.993
REMARK 3 BOND ANGLES OTHERS (DEGREES): 8226 ; 0.833 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 569 ; 5.579 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 222 ;38.598 ;24.414
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 896 ;12.104 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 26 ;17.198 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 697 ; 0.064 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 5230 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 932 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 944 ; 0.199 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 3417 ; 0.187 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 2314 ; 0.176 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2361 ; 0.082 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 225 ; 0.132 ; 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): 15 ; 0.157 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 52 ; 0.304 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 14 ; 0.147 ; 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): 3017 ; 3.096 ; 2.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1154 ; 0.630 ; 2.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4636 ; 3.997 ; 5.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 2144 ; 3.074 ; 2.500
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1890 ; 4.595 ; 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 853 A 1160 4
REMARK 3 1 B 853 B 1160 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 3924 ; 0.30 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 3924 ; 0.64 ; 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): -6.1864 60.1146 -3.4821
REMARK 3 T TENSOR
REMARK 3 T11: -0.0159 T22: -0.0500
REMARK 3 T33: 0.0305 T12: -0.0226
REMARK 3 T13: -0.0076 T23: -0.0426
REMARK 3 L TENSOR
REMARK 3 L11: 1.3272 L22: 0.2886
REMARK 3 L33: 1.8674 L12: -0.4945
REMARK 3 L13: 1.2592 L23: -0.7341
REMARK 3 S TENSOR
REMARK 3 S11: 0.0363 S12: -0.0101 S13: -0.2162
REMARK 3 S21: -0.0881 S22: -0.0071 S23: 0.0925
REMARK 3 S31: 0.0926 S32: 0.0200 S33: -0.0292
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 1154
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9712 51.2062 16.4574
REMARK 3 T TENSOR
REMARK 3 T11: -0.0374 T22: -0.0530
REMARK 3 T33: -0.0006 T12: -0.0217
REMARK 3 T13: 0.0096 T23: -0.0065
REMARK 3 L TENSOR
REMARK 3 L11: 1.5236 L22: 0.8482
REMARK 3 L33: 0.7313 L12: 0.1970
REMARK 3 L13: 0.2270 L23: -0.2403
REMARK 3 S TENSOR
REMARK 3 S11: 0.0170 S12: -0.0210 S13: -0.1769
REMARK 3 S21: 0.0825 S22: 0.0623 S23: -0.0044
REMARK 3 S31: 0.0059 S32: 0.0000 S33: -0.0794
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 865 B 959
REMARK 3 ORIGIN FOR THE GROUP (A): 24.3482 2.8760 -2.9411
REMARK 3 T TENSOR
REMARK 3 T11: -0.0100 T22: -0.0354
REMARK 3 T33: -0.0423 T12: 0.0011
REMARK 3 T13: 0.0166 T23: -0.0111
REMARK 3 L TENSOR
REMARK 3 L11: 1.3817 L22: 0.9435
REMARK 3 L33: 1.8214 L12: -0.4006
REMARK 3 L13: -0.3599 L23: 0.0155
REMARK 3 S TENSOR
REMARK 3 S11: 0.0795 S12: 0.0228 S13: 0.0154
REMARK 3 S21: -0.2136 S22: -0.0337 S23: -0.1768
REMARK 3 S31: 0.0298 S32: 0.0988 S33: -0.0458
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 1154
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3374 10.2211 15.9851
REMARK 3 T TENSOR
REMARK 3 T11: -0.0384 T22: -0.0294
REMARK 3 T33: -0.0332 T12: -0.0083
REMARK 3 T13: 0.0020 T23: -0.0224
REMARK 3 L TENSOR
REMARK 3 L11: 1.3778 L22: 1.2130
REMARK 3 L33: 0.8178 L12: 0.5997
REMARK 3 L13: -0.1776 L23: 0.1585
REMARK 3 S TENSOR
REMARK 3 S11: 0.0562 S12: -0.1213 S13: 0.2052
REMARK 3 S21: 0.0778 S22: 0.0255 S23: 0.1846
REMARK 3 S31: -0.0268 S32: 0.0376 S33: -0.0817
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 4E4N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071163.
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) : 100
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 : DOUBLE-CRYSTAL 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 : 50322
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
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 (%) : 99.6
REMARK 200 DATA REDUNDANCY : 3.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06800
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.91
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.1
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.48900
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.200
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: 2B7A
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.20
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 86.61950
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 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 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: 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 ALA A 862 96.39 -66.51
REMARK 500 ASP A1003 31.63 -148.92
REMARK 500 ASP A1042 48.80 -96.76
REMARK 500 ASP B1003 33.16 -146.89
REMARK 500 ASP B1042 49.17 -107.54
REMARK 500 THR B1095 51.93 -114.94
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 HOH A 1408
REMARK 615 HOH B 1389
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0NL A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0NL B 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4E4L RELATED DB: PDB
REMARK 900 RELATED ID: 4E4M RELATED DB: PDB
REMARK 900 RELATED ID: 4E5W RELATED DB: PDB
REMARK 900 RELATED ID: 4E6D RELATED DB: PDB
REMARK 900 RELATED ID: 4E6Q RELATED DB: PDB
DBREF 4E4N A 854 1154 UNP P23458 JAK1_HUMAN 854 1154
DBREF 4E4N B 854 1154 UNP P23458 JAK1_HUMAN 854 1154
SEQADV 4E4N GLY A 853 UNP P23458 EXPRESSION TAG
SEQADV 4E4N 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 4E4N PTR A 1034 TYR O-PHOSPHOTYROSINE
MODRES 4E4N PTR A 1035 TYR O-PHOSPHOTYROSINE
MODRES 4E4N PTR B 1034 TYR O-PHOSPHOTYROSINE
MODRES 4E4N PTR B 1035 TYR O-PHOSPHOTYROSINE
HET PTR A1034 16
HET PTR A1035 16
HET PTR B1034 16
HET PTR B1035 16
HET 0NL A1201 25
HET 0NL B1201 25
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM 0NL TERT-BUTYL [(1R,3R)-3-(IMIDAZO[4,5-D]PYRROLO[2,3-
HETNAM 2 0NL B]PYRIDIN-1(6H)-YL)CYCLOPENTYL]CARBAMATE
HETSYN PTR PHOSPHONOTYROSINE
FORMUL 1 PTR 4(C9 H12 N O6 P)
FORMUL 3 0NL 2(C18 H23 N5 O2)
FORMUL 5 HOH *294(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 ILE A 1060 THR A 1076 1 17
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 CYS A 1131 1 11
HELIX 14 14 GLN A 1135 ARG A 1139 5 5
HELIX 15 15 SER A 1141 LYS A 1154 1 14
HELIX 16 16 GLU B 871 ARG B 873 5 3
HELIX 17 17 HIS B 918 ASN B 931 1 14
HELIX 18 18 SER B 963 ASN B 971 1 9
HELIX 19 19 ASN B 976 ARG B 997 1 22
HELIX 20 20 ALA B 1005 ARG B 1007 5 3
HELIX 21 21 PRO B 1044 TYR B 1048 5 5
HELIX 22 22 ALA B 1049 SER B 1056 1 8
HELIX 23 23 ILE B 1060 THR B 1076 1 17
HELIX 24 24 ASP B 1079 SER B 1082 5 4
HELIX 25 25 SER B 1083 GLY B 1093 1 11
HELIX 26 26 HIS B 1096 GLN B 1098 5 3
HELIX 27 27 MET B 1099 GLU B 1110 1 12
HELIX 28 28 PRO B 1121 CYS B 1131 1 11
HELIX 29 29 GLN B 1135 ARG B 1139 5 5
HELIX 30 30 SER B 1141 LYS B 1154 1 14
SHEET 1 A 5 LEU A 875 GLU A 883 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 GLU A 903 N TYR A 894
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 A1034 THR A1036 0
SHEET 2 D 2 LYS A1057 TYR A1059 -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 ILE B 878
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 1.34
SITE 1 AC1 16 GLY A 882 GLU A 883 GLY A 887 LYS A 888
SITE 2 AC1 16 VAL A 889 ALA A 906 LYS A 908 MET A 956
SITE 3 AC1 16 GLU A 957 PHE A 958 LEU A 959 ASN A1008
SITE 4 AC1 16 LEU A1010 GLY A1020 ASP A1021 HOH A1393
SITE 1 AC2 15 GLY B 882 GLU B 883 GLY B 884 GLY B 887
SITE 2 AC2 15 VAL B 889 ALA B 906 LYS B 908 GLU B 957
SITE 3 AC2 15 PHE B 958 LEU B 959 ASN B1008 LEU B1010
SITE 4 AC2 15 ASP B1021 HOH B1315 HOH B1447
CRYST1 42.640 173.239 44.799 90.00 94.22 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 0.023452 0.000000 0.001730 0.00000
SCALE2 0.000000 0.005772 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022383 0.00000
(ATOM LINES ARE NOT SHOWN.)
END