BMRB Entry 15573

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15573
MolProbity Validation Chart

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Title:
SOLUTION STRUCTURE OF 50S RIBOSOMAL PROTEIN LX FROM Methanobacterium thermoautotrophicum, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET TR80
Deposition date:
2007-11-29
Original release date:
2009-04-16
Authors:
LIU, GAOHUA; WANG, DONGYAN; NWOSU, CHIOMA; OWENS, LEAH; XIAO, RONG; LIU, JINFENG; BARAN, MICHAEL; SWAPNA, G.V.T; ACTON, THOMAS; ROST, BURKHARD; MONTELIONE, GAETANO
Citation:

Citation: Liu, Gaohua; Xiao, Rong; Montelione, Gaetano. "SOLUTION STRUCTURE OF 50S RIBOSOMAL PROTEIN LX FROM Methanobacterium thermoautotrophicum, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET TR80"  .

Assembly members:

Assembly members:
Protein LX, polymer, 86 residues, 10373.190 Da.

Natural source:

Natural source:   Common Name: Methanobacterium thermoautotrophicum   Taxonomy ID: 145262   Superkingdom: Archaea   Kingdom: not available   Genus/species: Methanobacterium thermoautotrophicum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Protein LX: MKMKTKIFRVKGKFLMGDKL QPFTKELNAIREEEIYERLY SEFGSKHRVPRSKVKIEEIE EISPEEVQDPVVKALVQRLE HHHHHH

Data sets:
Data typeCount
13C chemical shifts291
15N chemical shifts79
1H chemical shifts607

Time Domain Data

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Protein LX1

Entities:

Entity 1, Protein LX 86 residues - 10373.190 Da.

1   METLYSMETLYSTHRLYSILEPHEARGVAL
2   LYSGLYLYSPHELEUMETGLYASPLYSLEU
3   GLNPROPHETHRLYSGLULEUASNALAILE
4   ARGGLUGLUGLUILETYRGLUARGLEUTYR
5   SERGLUPHEGLYSERLYSHISARGVALPRO
6   ARGSERLYSVALLYSILEGLUGLUILEGLU
7   GLUILESERPROGLUGLUVALGLNASPPRO
8   VALVALLYSALALEUVALGLNARGLEUGLU
9   HISHISHISHISHISHIS

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1.07 mM

sample_2: entity, [U-10% 13C; U-100% 15N], 1.1 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D SIMULTANEOUS CN-NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
4,3D GFT CABCACONHNsample_1isotropicsample_conditions_1
4,3D GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D GFT HCCHsample_1isotropicsample_conditions_1
4,3D GFT HABCABCONHNsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - data analysis, structure solution

AutoStruct v2.0.0, Huang, Tejero, Powers and Montelione - data analysis

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

XEASY, Bartels et al. - chemical shift assignment, data analysis

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR, Varian - collection

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAM70717
GB AAB86083
REF WP_048061100 WP_048176133
SP O27647
AlphaFold O27647

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks