HEADER RNA BINDING PROTEIN 14-MAY-05 1X49
TITLE SOLUTION STRUCTURE OF THE FIRST DSRM DOMAIN IN INTERFERON-INDUCED,
TITLE 2 DOUBLE-STRANDED RNA-ACTIVATED PROTEIN KINASE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: INTERFERON-INDUCED, DOUBLE-STRANDED RNA-ACTIVATED PROTEIN
COMPND 3 KINASE;
COMPND 4 CHAIN: A;
COMPND 5 FRAGMENT: DSRM DOMAIN;
COMPND 6 SYNONYM: INTERFERON-INDUCIBLE RNA-DEPENDENT PROTEIN KINASE, P68
COMPND 7 KINASE, P1/EIF-2A PROTEIN KINASE, SERINE/THREONINE-PROTEIN KINASE
COMPND 8 TIK;
COMPND 9 EC: 2.7.1.-;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 4 ORGANISM_TAXID: 10090;
SOURCE 5 GENE: PRKR, EIF2AK2, PKR, TIK;
SOURCE 6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 7 EXPRESSION_SYSTEM_PLASMID: P040712-15;
SOURCE 8 OTHER_DETAILS: CELL FREE PROTEIN SYNTHESIS
KEYWDS STRUCTURE GENOMICS, DSRM DOMAIN, STRUCTURAL GENOMICS, NPPSFA,
KEYWDS 2 NATIONAL PROJECT ON PROTEIN STRUCTURAL AND FUNCTIONAL ANALYSES,
KEYWDS 3 RIKEN STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE, RSGI, RNA BINDING
KEYWDS 4 PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR F.HE,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA,RIKEN
AUTHOR 2 STRUCTURAL GENOMICS/PROTEOMICS INITIATIVE (RSGI)
REVDAT 3 02-MAR-22 1X49 1 REMARK SEQADV
REVDAT 2 24-FEB-09 1X49 1 VERSN
REVDAT 1 14-NOV-05 1X49 0
JRNL AUTH F.HE,Y.MUTO,M.INOUE,T.KIGAWA,M.SHIROUZU,T.TERADA,S.YOKOYAMA
JRNL TITL SOLUTION STRUCTURE OF THE FIRST DSRM DOMAIN IN
JRNL TITL 2 INTERFERON-INDUCED, DOUBLE-STRANDED RNA-ACTIVATED PROTEIN
JRNL TITL 3 KINASE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CYANA 2.0.17
REMARK 3 AUTHORS : BRUKER (XWINNMR), GUNTERT,P. (CYANA)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1X49 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 16-MAY-05.
REMARK 100 THE DEPOSITION ID IS D_1000024359.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : 120MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 0.8MM U-15,13C; 20MM PHOSPHATE
REMARK 210 BUFFER NA; 100MM NACL; 1MM D-DTT;
REMARK 210 0.02% NAN3
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 800 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 20031121, NMRVIEW 5.0.4,
REMARK 210 KUJIRA 0.863, CYANA 2.0.17
REMARK 210 METHOD USED : TORSION ANGLE DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION, STRUCTURES WITH
REMARK 210 THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: NULL
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 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 1 ASP A 11 49.75 -107.47
REMARK 500 1 PRO A 13 81.32 -69.75
REMARK 500 1 SER A 37 -176.95 -69.71
REMARK 500 1 GLU A 60 173.40 -46.43
REMARK 500 1 ASP A 82 -35.17 -36.62
REMARK 500 1 SER A 95 101.46 -43.78
REMARK 500 2 SER A 6 116.43 -174.94
REMARK 500 2 ASP A 11 43.73 -88.61
REMARK 500 2 GLU A 60 177.88 -48.91
REMARK 500 2 ASP A 82 -35.51 -38.20
REMARK 500 2 LYS A 86 43.02 37.15
REMARK 500 2 ASP A 88 126.92 -39.53
REMARK 500 3 SER A 5 95.54 -68.80
REMARK 500 3 MET A 8 115.46 -34.65
REMARK 500 3 PRO A 13 81.49 -69.81
REMARK 500 3 GLU A 60 178.89 -49.02
REMARK 500 3 ASP A 82 -29.54 -37.25
REMARK 500 3 ASN A 85 42.75 -102.19
REMARK 500 3 LYS A 86 125.36 -37.31
REMARK 500 3 VAL A 87 107.04 -53.71
REMARK 500 3 CYS A 89 102.23 -40.82
REMARK 500 3 PRO A 94 95.57 -69.72
REMARK 500 4 GLU A 60 174.06 -46.83
REMARK 500 4 ASP A 82 -34.01 -35.73
REMARK 500 5 PRO A 13 96.68 -69.80
REMARK 500 5 SER A 37 -174.96 -68.22
REMARK 500 5 GLU A 60 172.31 -45.79
REMARK 500 5 GLU A 68 -39.06 -35.40
REMARK 500 5 ASP A 82 -27.81 -39.64
REMARK 500 5 HIS A 90 164.52 -48.63
REMARK 500 6 GLU A 60 178.86 -49.08
REMARK 500 6 ASN A 85 76.89 -100.79
REMARK 500 6 LYS A 86 124.91 -36.08
REMARK 500 7 ALA A 9 -44.41 -131.97
REMARK 500 7 ASP A 11 32.80 36.68
REMARK 500 7 SER A 37 -177.12 -69.13
REMARK 500 7 GLU A 60 176.75 -48.00
REMARK 500 7 ASP A 82 -30.64 -37.37
REMARK 500 8 SER A 5 98.23 -59.37
REMARK 500 8 MET A 8 41.80 36.88
REMARK 500 8 ALA A 9 118.48 -162.34
REMARK 500 8 PRO A 13 79.99 -69.79
REMARK 500 8 GLU A 60 -178.35 -50.26
REMARK 500 8 GLU A 84 25.22 47.46
REMARK 500 8 VAL A 87 176.56 -59.04
REMARK 500 8 ASP A 88 52.96 -93.50
REMARK 500 9 SER A 3 41.51 -87.82
REMARK 500 9 MET A 8 131.56 -174.79
REMARK 500 9 ASP A 11 32.94 -95.70
REMARK 500 9 PHE A 15 -63.68 -91.19
REMARK 500
REMARK 500 THIS ENTRY HAS 103 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 650
REMARK 650 HELIX
REMARK 650 DETERMINATION METHOD: AUTHOR DETERMINED
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: MMT008000608.2 RELATED DB: TARGETDB
DBREF 1X49 A 8 91 UNP Q03963 E2AK2_MOUSE 1 84
SEQADV 1X49 GLY A 1 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 SER A 2 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 SER A 3 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 GLY A 4 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 SER A 5 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 SER A 6 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 GLY A 7 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 SER A 92 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 GLY A 93 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 PRO A 94 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 SER A 95 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 SER A 96 UNP Q03963 CLONING ARTIFACT
SEQADV 1X49 GLY A 97 UNP Q03963 CLONING ARTIFACT
SEQRES 1 A 97 GLY SER SER GLY SER SER GLY MET ALA SER ASP THR PRO
SEQRES 2 A 97 GLY PHE TYR MET ASP LYS LEU ASN LYS TYR ARG GLN MET
SEQRES 3 A 97 HIS GLY VAL ALA ILE THR TYR LYS GLU LEU SER THR SER
SEQRES 4 A 97 GLY PRO PRO HIS ASP ARG ARG PHE THR PHE GLN VAL LEU
SEQRES 5 A 97 ILE ASP GLU LYS GLU PHE PRO GLU ALA LYS GLY ARG SER
SEQRES 6 A 97 LYS GLN GLU ALA ARG ASN ALA ALA ALA LYS LEU ALA VAL
SEQRES 7 A 97 ASP ILE LEU ASP ASN GLU ASN LYS VAL ASP CYS HIS THR
SEQRES 8 A 97 SER GLY PRO SER SER GLY
HELIX 1 1 PHE A 15 MET A 26 1 12
HELIX 2 2 LYS A 66 LEU A 81 1 16
SHEET 1 A 3 ILE A 31 SER A 39 0
SHEET 2 A 3 ARG A 46 ILE A 53 -1 O ARG A 46 N SER A 39
SHEET 3 A 3 ALA A 61 GLY A 63 -1 O ALA A 61 N PHE A 49
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
(ATOM LINES ARE NOT SHOWN.)
END