Header list of 1rq6.pdb file
Complete list - r 2 2 Bytes
HEADER TRANSLATION 04-DEC-03 1RQ6
TITLE SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN S17E FROM METHANOBACTERIUM
TITLE 2 THERMOAUTOTROPHICUM, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET
TITLE 3 TT802 / ONTARIO CENTER FOR STRUCTURAL PROTEOMICS TARGET MTH0803
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 30S RIBOSOMAL PROTEIN S17E;
COMPND 3 CHAIN: A;
COMPND 4 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: METHANOTHERMOBACTER THERMAUTOTROPHICUS;
SOURCE 3 ORGANISM_TAXID: 145262;
SOURCE 4 GENE: RPS17E, MTH803;
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: PET15B
KEYWDS ALPHA PROTEIN, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE,
KEYWDS 2 PSI, NESG, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM, TRANSLATION
EXPDTA SOLUTION NMR
NUMMDL 15
AUTHOR B.WU,A.YEE,Y.J.HUANG,T.A.RAMELOT,A.SEMESI,J.W.JUNG,A.EDWARD,W.LEE,
AUTHOR 2 M.A.KENNEDY,G.T.MONTELIONE,C.H.ARROWSMITH,NORTHEAST STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (NESG)
REVDAT 4 02-MAR-22 1RQ6 1 REMARK
REVDAT 3 30-DEC-08 1RQ6 1 JRNL VERSN
REVDAT 2 25-JAN-05 1RQ6 1 AUTHOR REMARK
REVDAT 1 14-DEC-04 1RQ6 0
JRNL AUTH B.WU,A.YEE,Y.J.HUANG,T.A.RAMELOT,J.R.CORT,A.SEMESI,J.W.JUNG,
JRNL AUTH 2 W.LEE,G.T.MONTELIONE,M.A.KENNEDY,C.H.ARROWSMITH
JRNL TITL THE SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN S17E FROM
JRNL TITL 2 METHANOBACTERIUM THERMOAUTOTROPHICUM: A STRUCTURAL HOMOLOG
JRNL TITL 3 OF THE FF DOMAIN.
JRNL REF PROTEIN SCI. V. 17 583 2008
JRNL REFN ISSN 0961-8368
JRNL PMID 18218711
JRNL DOI 10.1110/PS.073272208
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NMRPIPE 2.1, DYANA 1.5, CNS 1.0
REMARK 3 AUTHORS : DELAGLIO,F. (NMRPIPE), GUNTER,P. (DYANA), BRUNGER,
REMARK 3 A.T. ET AL. (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: 1143 NOE-DERIVED DISTANCE CONSTRAINTS
REMARK 3 AND 159 ANGLE CONSTRAINTS (PHI AND PSI)
REMARK 4
REMARK 4 1RQ6 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-DEC-03.
REMARK 100 THE DEPOSITION ID IS D_1000020944.
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 : 450 MM NACL, 25 MM PHOSPHATE
REMARK 210 BUFFER
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM MTH0803, U-15N,13C; 450 MM
REMARK 210 NACL, 25 MM NA2PO4, 1MM
REMARK 210 BENZAMIDINE, 1XINHIBITOR
REMARK 210 COOKTAIL, 0.01% NAN3, 95% H2O, 5%
REMARK 210 D2O
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 3D_13C
REMARK 210 -SEPARATED_NOESY; 4D_13C-
REMARK 210 SEPARATED_NOESY; HNHA
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : INOVA
REMARK 210 SPECTROMETER MANUFACTURER : VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : AUTOSTRUCTURE 2.0
REMARK 210 METHOD USED : TORSION ANGLE DYANMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 112
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 15
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS,TARGET
REMARK 210 FUNCTION
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: 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
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 ARG A 5 88.61 58.43
REMARK 500 1 THR A 6 -26.09 -164.73
REMARK 500 1 PRO A 21 25.83 -67.70
REMARK 500 1 PHE A 38 -80.47 -113.83
REMARK 500 1 SER A 39 103.49 63.84
REMARK 500 1 THR A 43 107.53 72.38
REMARK 500 2 THR A 6 -19.30 -164.48
REMARK 500 2 LYS A 23 -158.39 62.32
REMARK 500 2 PHE A 24 -72.70 -158.76
REMARK 500 2 PHE A 38 -52.14 -124.79
REMARK 500 2 SER A 42 108.25 -47.65
REMARK 500 2 LYS A 44 -83.14 -24.19
REMARK 500 3 ILE A 4 -62.06 -98.12
REMARK 500 3 THR A 6 -39.30 -170.18
REMARK 500 3 LYS A 23 -71.42 -145.76
REMARK 500 3 PHE A 24 28.63 42.50
REMARK 500 3 PHE A 38 -157.79 -97.92
REMARK 500 4 ARG A 5 112.78 68.19
REMARK 500 4 THR A 6 30.21 -163.21
REMARK 500 4 GLU A 18 -59.39 73.84
REMARK 500 4 PHE A 38 -73.63 -85.55
REMARK 500 4 VAL A 41 104.54 61.76
REMARK 500 4 HIS A 45 21.33 -154.86
REMARK 500 5 ASN A 3 -144.74 62.55
REMARK 500 5 ILE A 4 -155.56 48.04
REMARK 500 5 ARG A 5 -158.92 71.97
REMARK 500 5 THR A 6 21.83 -161.47
REMARK 500 5 THR A 19 -54.50 76.62
REMARK 500 5 LYS A 23 92.28 60.28
REMARK 500 5 GLU A 37 53.51 -156.68
REMARK 500 5 PHE A 38 -89.05 -148.55
REMARK 500 5 THR A 43 47.92 -89.95
REMARK 500 5 LYS A 44 -75.40 -60.96
REMARK 500 6 ARG A 5 -176.32 64.29
REMARK 500 6 THR A 6 20.11 -161.41
REMARK 500 6 THR A 19 -57.37 72.53
REMARK 500 6 PHE A 24 -70.47 -94.67
REMARK 500 6 PHE A 38 -141.94 -110.99
REMARK 500 6 SER A 39 174.02 71.40
REMARK 500 6 THR A 40 -81.17 -112.48
REMARK 500 7 ASN A 3 -53.34 73.38
REMARK 500 7 THR A 6 -42.66 -164.66
REMARK 500 7 PRO A 21 42.91 -76.84
REMARK 500 7 LYS A 44 -78.04 -85.62
REMARK 500 8 ILE A 4 27.49 45.87
REMARK 500 8 THR A 6 -27.24 -160.59
REMARK 500 8 GLU A 18 -86.37 61.94
REMARK 500 8 THR A 19 11.96 -153.04
REMARK 500 8 LYS A 23 -51.89 -129.67
REMARK 500 8 PHE A 24 81.63 64.56
REMARK 500
REMARK 500 THIS ENTRY HAS 106 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 6028 RELATED DB: BMRB
REMARK 900 RELATED ID: TT802 RELATED DB: TARGETDB
DBREF 1RQ6 A 1 62 UNP O26894 RS17E_METTH 1 62
SEQRES 1 A 62 MET GLY ASN ILE ARG THR SER PHE VAL LYS ARG ILE ALA
SEQRES 2 A 62 LYS GLU MET ILE GLU THR HIS PRO GLY LYS PHE THR ASP
SEQRES 3 A 62 ASP PHE ASP THR ASN LYS LYS LEU VAL GLU GLU PHE SER
SEQRES 4 A 62 THR VAL SER THR LYS HIS LEU ARG ASN LYS ILE ALA GLY
SEQRES 5 A 62 TYR ILE THR ARG ILE ILE SER GLN GLN LYS
HELIX 1 1 THR A 6 GLU A 18 1 13
HELIX 2 2 ASP A 27 GLU A 37 1 11
HELIX 3 3 HIS A 45 LYS A 62 1 18
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