HEADER SIGNALING PROTEIN, TRANSFERASE/INHIBITOR23-JAN-18 6C7Y
TITLE CRYSTAL STRUCTURE OF INHIBITORY PROTEIN SOCS1 IN COMPLEX WITH JAK1
TITLE 2 KINASE DOMAIN
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TYROSINE-PROTEIN KINASE JAK1;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 869-1153);
COMPND 5 SYNONYM: JANUS KINASE 1, JAK-1;
COMPND 6 EC: 2.7.10.2;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: SUPPRESSOR OF CYTOKINE SIGNALING 1;
COMPND 10 CHAIN: B;
COMPND 11 FRAGMENT: UNP RESIDUES 48-164;
COMPND 12 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;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: GALLUS GALLUS;
SOURCE 11 ORGANISM_COMMON: CHICKEN;
SOURCE 12 ORGANISM_TAXID: 9031;
SOURCE 13 GENE: SOCS1;
SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 15 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS KINASE, KINASE INHIBITOR, SIGNALING PROTEIN, TRANSFERASE-INHIBITOR
KEYWDS 2 COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR N.P.D.LIAU,A.LAKTYUSHIN,I.S.LUCET,J.M.MURPHY,S.YAO,K.CALLAGHAN,
AUTHOR 2 N.A.NICOLA,N.J.KERSHAW,J.J.BABON
REVDAT 5 15-NOV-23 6C7Y 1 REMARK
REVDAT 4 04-OCT-23 6C7Y 1 LINK
REVDAT 3 08-JAN-20 6C7Y 1 REMARK
REVDAT 2 20-FEB-19 6C7Y 1 REMARK
REVDAT 1 02-MAY-18 6C7Y 0
JRNL AUTH N.P.D.LIAU,A.LAKTYUSHIN,I.S.LUCET,J.M.MURPHY,S.YAO,
JRNL AUTH 2 E.WHITLOCK,K.CALLAGHAN,N.A.NICOLA,N.J.KERSHAW,J.J.BABON
JRNL TITL THE MOLECULAR BASIS OF JAK/STAT INHIBITION BY SOCS1.
JRNL REF NAT COMMUN V. 9 1558 2018
JRNL REFN ESSN 2041-1723
JRNL PMID 29674694
JRNL DOI 10.1038/S41467-018-04013-1
REMARK 2
REMARK 2 RESOLUTION. 2.50 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 : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 40.61
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 20702
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.210
REMARK 3 R VALUE (WORKING SET) : 0.207
REMARK 3 FREE R VALUE : 0.241
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 9.640
REMARK 3 FREE R VALUE TEST SET COUNT : 1995
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 40.6187 - 6.0174 1.00 1468 158 0.1831 0.2191
REMARK 3 2 6.0174 - 4.7786 1.00 1386 147 0.1880 0.2066
REMARK 3 3 4.7786 - 4.1752 1.00 1363 144 0.1607 0.1957
REMARK 3 4 4.1752 - 3.7938 1.00 1344 143 0.1781 0.2078
REMARK 3 5 3.7938 - 3.5221 1.00 1327 142 0.2055 0.2538
REMARK 3 6 3.5221 - 3.3145 1.00 1337 143 0.2108 0.2498
REMARK 3 7 3.3145 - 3.1486 1.00 1318 141 0.2454 0.2599
REMARK 3 8 3.1486 - 3.0116 1.00 1319 140 0.2463 0.2959
REMARK 3 9 3.0116 - 2.8957 1.00 1303 140 0.2687 0.2927
REMARK 3 10 2.8957 - 2.7958 1.00 1319 140 0.2704 0.3023
REMARK 3 11 2.7958 - 2.7084 1.00 1294 138 0.2619 0.3245
REMARK 3 12 2.7084 - 2.6310 1.00 1314 140 0.2764 0.3266
REMARK 3 13 2.6310 - 2.5617 1.00 1316 141 0.2969 0.3316
REMARK 3 14 2.5617 - 2.4992 1.00 1299 138 0.3061 0.3474
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
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) : 0.310
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.350
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 54.94
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.25
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 : 0.001 3165
REMARK 3 ANGLE : 0.478 4283
REMARK 3 CHIRALITY : 0.038 474
REMARK 3 PLANARITY : 0.003 542
REMARK 3 DIHEDRAL : 10.054 1881
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: (CHAIN A AND RESID 869:921)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0016 23.4682 -8.4362
REMARK 3 T TENSOR
REMARK 3 T11: 1.6711 T22: 0.9861
REMARK 3 T33: 1.1545 T12: 0.4580
REMARK 3 T13: 0.2675 T23: 0.0587
REMARK 3 L TENSOR
REMARK 3 L11: 7.3466 L22: 8.6072
REMARK 3 L33: 5.6607 L12: -1.3265
REMARK 3 L13: 0.7133 L23: 5.3808
REMARK 3 S TENSOR
REMARK 3 S11: -0.0156 S12: 0.3028 S13: -1.3322
REMARK 3 S21: -2.1436 S22: 0.2763 S23: -1.1251
REMARK 3 S31: 0.6144 S32: 1.4286 S33: -0.2302
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: (CHAIN A AND RESID 922:1030)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.4177 28.5703 -2.0270
REMARK 3 T TENSOR
REMARK 3 T11: 1.1864 T22: 0.4599
REMARK 3 T33: 1.0039 T12: 0.1823
REMARK 3 T13: 0.0180 T23: 0.1079
REMARK 3 L TENSOR
REMARK 3 L11: 3.9333 L22: 3.6539
REMARK 3 L33: 3.6970 L12: 0.4625
REMARK 3 L13: -1.0078 L23: 0.1557
REMARK 3 S TENSOR
REMARK 3 S11: -0.1606 S12: -0.0966 S13: -1.7508
REMARK 3 S21: -0.6226 S22: 0.1886 S23: -0.0782
REMARK 3 S31: 1.5664 S32: 0.4520 S33: -0.1450
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: (CHAIN A AND RESID 1031:1153)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4754 45.7901 -2.7854
REMARK 3 T TENSOR
REMARK 3 T11: 0.4419 T22: 0.3164
REMARK 3 T33: 0.3491 T12: 0.0115
REMARK 3 T13: -0.0310 T23: 0.0402
REMARK 3 L TENSOR
REMARK 3 L11: 3.5070 L22: 4.6465
REMARK 3 L33: 5.4773 L12: 0.1134
REMARK 3 L13: 0.2093 L23: -1.3854
REMARK 3 S TENSOR
REMARK 3 S11: 0.0945 S12: -0.1179 S13: -0.4156
REMARK 3 S21: -0.7725 S22: -0.0173 S23: 0.2685
REMARK 3 S31: 0.6627 S32: -0.0372 S33: -0.0552
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: (CHAIN B AND RESID 52:168)
REMARK 3 ORIGIN FOR THE GROUP (A): -1.1893 66.7876 -9.8764
REMARK 3 T TENSOR
REMARK 3 T11: 1.0289 T22: 0.8288
REMARK 3 T33: 0.7413 T12: -0.3052
REMARK 3 T13: 0.4366 T23: -0.1528
REMARK 3 L TENSOR
REMARK 3 L11: 2.5576 L22: 2.7306
REMARK 3 L33: 6.9051 L12: 1.0173
REMARK 3 L13: -2.7797 L23: -2.7031
REMARK 3 S TENSOR
REMARK 3 S11: 0.7604 S12: -0.4761 S13: 0.3518
REMARK 3 S21: 0.0435 S22: -0.0206 S23: -0.6851
REMARK 3 S31: -1.7113 S32: 1.3348 S33: -0.3490
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 6C7Y COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-18.
REMARK 100 THE DEPOSITION ID IS D_1000231332.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-15
REMARK 200 TEMPERATURE (KELVIN) : 77
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9537
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20768
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.500
REMARK 200 RESOLUTION RANGE LOW (A) : 40.613
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 8.268
REMARK 200 R MERGE (I) : 0.11300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.7700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 8.42
REMARK 200 R MERGE FOR SHELL (I) : 1.70100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.660
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHENIX
REMARK 200 STARTING MODEL: PDB ENTRIES 6C5X & 3EYH
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 60.17
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES PH 7.0, 14% (W/V) PEG8000,
REMARK 280 100MM MAGNESIUM ACETATE, 2MM TCEP, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 281K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
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 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 80.71900
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 41.96300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 41.96300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 40.35950
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 41.96300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 41.96300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 121.07850
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 41.96300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 41.96300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 40.35950
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 41.96300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 41.96300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 121.07850
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 80.71900
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 17780 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 ASP A 895
REMARK 465 PRO A 896
REMARK 465 GLU A 897
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 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 GLU A 871 CG CD OE1 OE2
REMARK 470 LYS A 872 CG CD CE NZ
REMARK 470 ARG A 873 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 874 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LEU A 875 CG CD1 CD2
REMARK 470 LYS A 876 CG CD CE NZ
REMARK 470 ARG A 877 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 888 CD CE NZ
REMARK 470 ARG A 893 CG CD NE CZ NH1 NH2
REMARK 470 TYR A 894 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 THR A 901 OG1 CG2
REMARK 470 GLU A 903 CG CD OE1 OE2
REMARK 470 VAL A 905 CG1 CG2
REMARK 470 LYS A 911 CG CD CE NZ
REMARK 470 LYS A 923 CD CE NZ
REMARK 470 GLU A 927 CD OE1 OE2
REMARK 470 ARG A 930 CG CD NE CZ NH1 NH2
REMARK 470 ILE A 943 CG1 CG2 CD1
REMARK 470 LYS A 978 CD CE NZ
REMARK 470 LYS A 982 CG CD CE NZ
REMARK 470 GLU B 142 CG CD OE1 OE2
REMARK 470 LYS B 149 CG CD CE NZ
REMARK 470 GLU B 152 CG CD OE1 OE2
REMARK 470 ARG B 159 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 160 CG CD CE NZ
REMARK 470 LEU B 162 CG CD1 CD2
REMARK 470 LYS B 168 CG CD CE NZ
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 ILE A 878 -73.52 -71.61
REMARK 500 LYS A 911 77.54 55.72
REMARK 500 TYR A 933 87.09 -153.19
REMARK 500 LYS A 941 -73.05 -112.40
REMARK 500 ASP A1003 37.47 -157.91
REMARK 500 ASP A1021 84.96 58.49
REMARK 500 PHE B 112 -69.54 -90.41
REMARK 500 THR B 119 -162.82 -105.35
REMARK 500 VAL B 163 -47.62 -141.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASN A1008 OD1
REMARK 620 2 ASP A1021 OD2 84.0
REMARK 620 3 ADP A1201 O3B 171.3 88.8
REMARK 620 4 ADP A1201 O1A 77.7 82.9 96.7
REMARK 620 5 HOH A1302 O 72.0 155.2 114.6 86.1
REMARK 620 6 HOH A1317 O 113.2 92.2 71.8 167.7 102.5
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A1203 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A1021 OD1
REMARK 620 2 ASP A1021 OD2 59.9
REMARK 620 3 ADP A1201 O2B 75.0 82.1
REMARK 620 4 ADP A1201 O3B 120.3 79.2 56.7
REMARK 620 5 HOH A1325 O 102.3 161.9 96.4 115.1
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6C5X RELATED DB: PDB
REMARK 900 SOCS1 IN COMPLEX WITH ELONGIN B AND ELONGIN C
DBREF 6C7Y A 869 1153 UNP P23458 JAK1_HUMAN 869 1153
DBREF 6C7Y B 52 168 UNP B6RCQ2 B6RCQ2_CHICK 48 164
SEQADV 6C7Y ALA A 868 UNP P23458 EXPRESSION TAG
SEQRES 1 A 286 ALA HIS PHE GLU LYS ARG PHE LEU LYS ARG ILE ARG ASP
SEQRES 2 A 286 LEU GLY GLU GLY HIS PHE GLY LYS VAL GLU LEU CYS ARG
SEQRES 3 A 286 TYR ASP PRO GLU GLY ASP ASN THR GLY GLU GLN VAL ALA
SEQRES 4 A 286 VAL LYS SER LEU LYS PRO GLU SER GLY GLY ASN HIS ILE
SEQRES 5 A 286 ALA ASP LEU LYS LYS GLU ILE GLU ILE LEU ARG ASN LEU
SEQRES 6 A 286 TYR HIS GLU ASN ILE VAL LYS TYR LYS GLY ILE CYS THR
SEQRES 7 A 286 GLU ASP GLY GLY ASN GLY ILE LYS LEU ILE MET GLU PHE
SEQRES 8 A 286 LEU PRO SER GLY SER LEU LYS GLU TYR LEU PRO LYS ASN
SEQRES 9 A 286 LYS ASN LYS ILE ASN LEU LYS GLN GLN LEU LYS TYR ALA
SEQRES 10 A 286 VAL GLN ILE CYS LYS GLY MET ASP TYR LEU GLY SER ARG
SEQRES 11 A 286 GLN TYR VAL HIS ARG ASP LEU ALA ALA ARG ASN VAL LEU
SEQRES 12 A 286 VAL GLU SER GLU HIS GLN VAL LYS ILE GLY ASP PHE GLY
SEQRES 13 A 286 LEU THR LYS ALA ILE GLU THR ASP LYS GLU TYR PTR THR
SEQRES 14 A 286 VAL LYS ASP ASP ARG ASP SER PRO VAL PHE TRP TYR ALA
SEQRES 15 A 286 PRO GLU CYS LEU MET GLN SER LYS PHE TYR ILE ALA SER
SEQRES 16 A 286 ASP VAL TRP SER PHE GLY VAL THR LEU HIS GLU LEU LEU
SEQRES 17 A 286 THR TYR CYS ASP SER ASP SER SER PRO MET ALA LEU PHE
SEQRES 18 A 286 LEU LYS MET ILE GLY PRO THR HIS GLY GLN MET THR VAL
SEQRES 19 A 286 THR ARG LEU VAL ASN THR LEU LYS GLU GLY LYS ARG LEU
SEQRES 20 A 286 PRO CYS PRO PRO ASN CYS PRO ASP GLU VAL TYR GLN LEU
SEQRES 21 A 286 MET ARG LYS CYS TRP GLU PHE GLN PRO SER ASN ARG THR
SEQRES 22 A 286 SER PHE GLN ASN LEU ILE GLU GLY PHE GLU ALA LEU LEU
SEQRES 1 B 117 SER THR HIS PHE ARG THR PHE ARG SER GLN ALA ASP PHE
SEQRES 2 B 117 SER SER ILE THR ARG ALA SER SER LEU LEU ASP ALA CYS
SEQRES 3 B 117 GLY PHE TYR TRP GLY PRO LEU THR VAL SER ALA ALA HIS
SEQRES 4 B 117 GLU LYS LEU LYS SER GLU PRO GLU GLY THR PHE LEU ILE
SEQRES 5 B 117 ARG ASP SER THR GLN LYS ASN CYS PHE PHE ALA ILE SER
SEQRES 6 B 117 VAL LYS THR ALA THR GLY PRO THR SER ILE ARG ILE ASN
SEQRES 7 B 117 PHE GLN THR GLY ARG PHE SER LEU ASP GLY SER LYS GLU
SEQRES 8 B 117 THR PHE ASP CYS LEU PHE LYS LEU LEU GLU HIS TYR LEU
SEQRES 9 B 117 SER SER PRO ARG LYS VAL LEU VAL THR PRO LEU ARG LYS
MODRES 6C7Y PTR A 1035 TYR MODIFIED RESIDUE
HET PTR A1035 25
HET ADP A1201 27
HET MG A1202 1
HET MG A1203 1
HET EDO A1204 4
HET EDO A1205 4
HET EDO B 201 4
HET ACT B 202 4
HETNAM PTR O-PHOSPHOTYROSINE
HETNAM ADP ADENOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ACT ACETATE ION
HETSYN PTR PHOSPHONOTYROSINE
HETSYN EDO ETHYLENE GLYCOL
FORMUL 1 PTR C9 H12 N O6 P
FORMUL 3 ADP C10 H15 N5 O10 P2
FORMUL 4 MG 2(MG 2+)
FORMUL 6 EDO 3(C2 H6 O2)
FORMUL 9 ACT C2 H3 O2 1-
FORMUL 10 HOH *35(H2 O)
HELIX 1 AA1 GLU A 871 LEU A 875 5 5
HELIX 2 AA2 ILE A 919 LEU A 932 1 14
HELIX 3 AA3 SER A 963 LEU A 968 1 6
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 SER A 1056 1 8
HELIX 8 AA8 TYR A 1059 THR A 1076 1 18
HELIX 9 AA9 SER A 1083 GLY A 1093 1 11
HELIX 10 AB1 GLN A 1098 GLU A 1110 1 13
HELIX 11 AB2 PRO A 1121 CYS A 1131 1 11
HELIX 12 AB3 GLN A 1135 ARG A 1139 5 5
HELIX 13 AB4 SER A 1141 ALA A 1151 1 11
HELIX 14 AB5 SER B 60 CYS B 77 1 18
HELIX 15 AB6 THR B 85 LYS B 94 1 10
HELIX 16 AB7 CYS B 146 LEU B 155 1 10
SHEET 1 AA1 5 ARG A 879 GLU A 883 0
SHEET 2 AA1 5 LYS A 888 TYR A 894 -1 O VAL A 889 N LEU A 881
SHEET 3 AA1 5 GLU A 903 SER A 909 -1 O VAL A 907 N GLU A 890
SHEET 4 AA1 5 LYS A 953 GLU A 957 -1 O LEU A 954 N LYS A 908
SHEET 5 AA1 5 TYR A 940 CYS A 944 -1 N CYS A 944 O LYS A 953
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 VAL A1011 0
SHEET 2 AA3 2 VAL A1017 ILE A1019 -1 O LYS A1018 N LEU A1010
SHEET 1 AA4 2 PTR A1035 THR A1036 0
SHEET 2 AA4 2 LYS A1057 PHE A1058 -1 O PHE A1058 N PTR A1035
SHEET 1 AA5 5 ARG B 134 LEU B 137 0
SHEET 2 AA5 5 GLY B 122 GLN B 131 -1 N ASN B 129 O SER B 136
SHEET 3 AA5 5 PHE B 113 THR B 119 -1 N VAL B 117 O THR B 124
SHEET 4 AA5 5 THR B 100 ASP B 105 -1 N ARG B 104 O ALA B 114
SHEET 5 AA5 5 THR B 164 PRO B 165 1 O THR B 164 N PHE B 101
LINK C TYR A1034 N PTR A1035 1555 1555 1.33
LINK C PTR A1035 N THR A1036 1555 1555 1.33
LINK OD1 ASN A1008 MG MG A1202 1555 1555 2.18
LINK OD2 ASP A1021 MG MG A1202 1555 1555 2.05
LINK OD1 ASP A1021 MG MG A1203 1555 1555 2.03
LINK OD2 ASP A1021 MG MG A1203 1555 1555 2.33
LINK O3B ADP A1201 MG MG A1202 1555 1555 2.64
LINK O1A ADP A1201 MG MG A1202 1555 1555 2.36
LINK O2B ADP A1201 MG MG A1203 1555 1555 2.47
LINK O3B ADP A1201 MG MG A1203 1555 1555 2.83
LINK MG MG A1202 O HOH A1302 1555 1555 2.27
LINK MG MG A1202 O HOH A1317 1555 1555 2.65
LINK MG MG A1203 O HOH A1325 1555 1555 2.48
SITE 1 AC1 19 GLY A 882 GLY A 884 HIS A 885 PHE A 886
SITE 2 AC1 19 GLY A 887 VAL A 889 ALA A 906 LYS A 908
SITE 3 AC1 19 MET A 956 GLU A 957 LEU A 959 SER A 963
SITE 4 AC1 19 GLU A 966 ARG A1007 ASN A1008 LEU A1010
SITE 5 AC1 19 ASP A1021 MG A1202 MG A1203
SITE 1 AC2 6 ASN A1008 ASP A1021 ADP A1201 MG A1203
SITE 2 AC2 6 HOH A1302 HOH A1317
SITE 1 AC3 5 ASP A1003 ASP A1021 ADP A1201 MG A1202
SITE 2 AC3 5 HOH A1325
SITE 1 AC4 5 LEU A1108 LYS A1109 GLY A1111 ARG A1113
SITE 2 AC4 5 PHE A1134
SITE 1 AC5 6 GLN A1055 LYS A1057 HOH A1316 ARG B 59
SITE 2 AC5 6 SER B 60 GLN B 61
SITE 1 AC6 3 GLN A1098 ARG B 59 ASP B 63
SITE 1 AC7 4 VAL B 86 ARG B 104 SER B 106 THR B 107
CRYST1 83.926 83.926 161.438 90.00 90.00 90.00 P 41 21 2 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 0.011915 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011915 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006194 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
