Header list of 1qu6.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSFERASE 08-JUL-99 1QU6
TITLE STRUCTURE OF THE DOUBLE-STRANDED RNA-BINDING DOMAIN OF THE PROTEIN
TITLE 2 KINASE PKR REVEALS THE MOLECULAR BASIS OF ITS DSRNA-MEDIATED
TITLE 3 ACTIVATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN KINASE PKR;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: DSRNA-BINDING N-TERMINAL DOMAIN;
COMPND 5 EC: 2.7.1.-;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PET-15B
KEYWDS DSRNA-BINDING DOMAIN, PKR, SOLUTION STRUCTURE, PROTEIN KINASE,
KEYWDS 2 TRANSFERASE
EXPDTA SOLUTION NMR
NUMMDL 21
MDLTYP MINIMIZED AVERAGE
AUTHOR S.NANDURI,B.W.CARPICK,Y.YANG,B.R.G.WILLIAMS,J.QIN
REVDAT 4 02-MAR-22 1QU6 1 REMARK
REVDAT 3 24-FEB-09 1QU6 1 VERSN
REVDAT 2 01-APR-03 1QU6 1 JRNL
REVDAT 1 23-DEC-99 1QU6 0
JRNL AUTH S.NANDURI,B.W.CARPICK,Y.YANG,B.R.WILLIAMS,J.QIN
JRNL TITL STRUCTURE OF THE DOUBLE-STRANDED RNA-BINDING DOMAIN OF THE
JRNL TITL 2 PROTEIN KINASE PKR REVEALS THE MOLECULAR BASIS OF ITS
JRNL TITL 3 DSRNA-MEDIATED ACTIVATION.
JRNL REF EMBO J. V. 17 5458 1998
JRNL REFN ISSN 0261-4189
JRNL PMID 9736623
JRNL DOI 10.1093/EMBOJ/17.18.5458
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : X-PLOR
REMARK 3 AUTHORS : BRUNGER, A. T.
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1QU6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JUL-99.
REMARK 100 THE DEPOSITION ID IS D_1000001217.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 298
REMARK 210 PH : 6.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D HNCACB; 3D CBCA(CO)NH; 3D
REMARK 210 H(CCO)NH; 3D HCCH-TOCSY; 4D_15N;
REMARK 210 13C_EDITED_NOESY; 4D_13C; 2D_15N
REMARK 210 HOHAHA; 3D_15N; 3D HNHA; 3D HNHB;
REMARK 210 2D-ARO-(HB)CB(CGCD)HD; 2D-ARO_
REMARK 210 (HB)CB(CGCDCE)HE
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ
REMARK 210 SPECTROMETER MODEL : UNITY INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE, PIPP
REMARK 210 METHOD USED : MODIFIED DG/SA PROTOCOL IN XPLOR
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 90
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 21
REMARK 210 CONFORMERS, SELECTION CRITERIA : NULL
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 21
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: CLOSE CONTACTS
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 HG1 THR A 154 H GLU A 157 1.23
REMARK 500 H1 GLY A 1 H SER A 2 1.32
REMARK 500 H VAL A 29 O ILE A 52 1.45
REMARK 500 O ASP A 43 H ARG A 45 1.47
REMARK 500 O PRO A 40 H HIS A 42 1.48
REMARK 500 O MET A 16 H ASN A 20 1.49
REMARK 500 O ASN A 70 H LYS A 74 1.57
REMARK 500 O ALA A 163 H TYR A 167 1.59
REMARK 500 O VAL A 29 O ILE A 52 2.18
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 1 HIS A 3 -79.92 -162.77
REMARK 500 1 GLU A 5 22.18 -147.77
REMARK 500 1 ALA A 7 -129.04 -75.31
REMARK 500 1 LEU A 10 3.69 -156.71
REMARK 500 1 ALA A 12 -121.32 94.67
REMARK 500 1 PHE A 14 -97.00 -170.76
REMARK 500 1 VAL A 28 -162.29 -104.45
REMARK 500 1 ASN A 37 97.61 34.39
REMARK 500 1 SER A 38 -13.81 -143.18
REMARK 500 1 PRO A 41 55.14 -63.00
REMARK 500 1 HIS A 42 18.29 42.98
REMARK 500 1 ARG A 44 58.46 -63.73
REMARK 500 1 ASP A 53 -64.91 -120.41
REMARK 500 1 ARG A 55 -18.63 -148.08
REMARK 500 1 PHE A 57 47.40 -157.03
REMARK 500 1 ARG A 63 -178.46 86.28
REMARK 500 1 LYS A 65 -173.40 169.17
REMARK 500 1 LYS A 82 -144.88 -80.38
REMARK 500 1 GLU A 83 -5.42 52.97
REMARK 500 1 PRO A 89 -150.11 -59.34
REMARK 500 1 LEU A 90 -88.51 -86.56
REMARK 500 1 THR A 93 58.24 -115.47
REMARK 500 1 THR A 95 35.11 -95.58
REMARK 500 1 ASN A 96 -86.76 -150.52
REMARK 500 1 SER A 97 -148.36 52.77
REMARK 500 1 SER A 98 174.13 -54.19
REMARK 500 1 LEU A 101 2.08 55.50
REMARK 500 1 SER A 102 -161.73 45.11
REMARK 500 1 TYR A 106 -52.61 -171.08
REMARK 500 1 ALA A 114 -70.22 -60.62
REMARK 500 1 LYS A 117 36.47 -98.77
REMARK 500 1 ARG A 118 103.23 31.85
REMARK 500 1 GLN A 125 142.14 -177.01
REMARK 500 1 VAL A 130 -79.30 -61.50
REMARK 500 1 PRO A 133 1.59 -62.85
REMARK 500 1 GLU A 134 -92.57 -59.97
REMARK 500 1 LYS A 145 41.84 -148.55
REMARK 500 1 SER A 148 74.89 -67.47
REMARK 500 2 SER A 2 -160.26 46.71
REMARK 500 2 HIS A 3 -68.40 -160.74
REMARK 500 2 MET A 4 -125.38 -58.79
REMARK 500 2 GLU A 5 38.53 -153.40
REMARK 500 2 LEU A 10 3.07 -155.91
REMARK 500 2 SER A 11 28.45 -157.59
REMARK 500 2 PHE A 14 -78.17 -129.34
REMARK 500 2 VAL A 28 -166.57 -110.31
REMARK 500 2 ASN A 37 90.99 39.77
REMARK 500 2 PRO A 41 55.79 -65.24
REMARK 500 2 HIS A 42 20.09 40.96
REMARK 500 2 ARG A 44 65.37 -62.33
REMARK 500
REMARK 500 THIS ENTRY HAS 794 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
DBREF 1QU6 A 6 175 UNP P19525 E2AK2_HUMAN 1 170
SEQRES 1 A 179 GLY SER HIS MET GLU MET ALA GLY ASP LEU SER ALA GLY
SEQRES 2 A 179 PHE PHE MET GLU GLU LEU ASN THR TYR ARG GLN LYS GLN
SEQRES 3 A 179 GLY VAL VAL LEU LYS TYR GLN GLU LEU PRO ASN SER GLY
SEQRES 4 A 179 PRO PRO HIS ASP ARG ARG PHE THR PHE GLN VAL ILE ILE
SEQRES 5 A 179 ASP GLY ARG GLU PHE PRO GLU GLY GLU GLY ARG SER LYS
SEQRES 6 A 179 LYS GLU ALA LYS ASN ALA ALA ALA LYS LEU ALA VAL GLU
SEQRES 7 A 179 ILE LEU ASN LYS GLU LYS LYS ALA VAL SER PRO LEU LEU
SEQRES 8 A 179 LEU THR THR THR ASN SER SER GLU GLY LEU SER MET GLY
SEQRES 9 A 179 ASN TYR ILE GLY LEU ILE ASN ARG ILE ALA GLN LYS LYS
SEQRES 10 A 179 ARG LEU THR VAL ASN TYR GLU GLN CYS ALA SER GLY VAL
SEQRES 11 A 179 HIS GLY PRO GLU GLY PHE HIS TYR LYS CYS LYS MET GLY
SEQRES 12 A 179 GLN LYS GLU TYR SER ILE GLY THR GLY SER THR LYS GLN
SEQRES 13 A 179 GLU ALA LYS GLN LEU ALA ALA LYS LEU ALA TYR LEU GLN
SEQRES 14 A 179 ILE LEU SER GLU GLU THR GLY SER GLY CYS
HELIX 1 1 PHE A 14 GLY A 27 1 14
HELIX 2 2 LYS A 65 LYS A 82 1 18
HELIX 3 3 TYR A 106 LYS A 117 1 12
HELIX 4 4 THR A 154 GLU A 173 1 20
SHEET 1 A 3 LYS A 31 PRO A 36 0
SHEET 2 A 3 PHE A 46 ILE A 51 -1 O THR A 47 N LEU A 35
SHEET 3 A 3 GLU A 59 GLU A 61 -1 O GLY A 60 N PHE A 48
SHEET 1 B 3 THR A 120 SER A 128 0
SHEET 2 B 3 GLY A 135 GLY A 143 -1 N GLY A 135 O SER A 128
SHEET 3 B 3 ILE A 149 GLY A 152 -1 O GLY A 150 N TYR A 138
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
Complete list - r 2 2 Bytes