BMRB Entry 18298

Click here to enlarge.

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/BMR18298
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Domain interaction in Thermotoga maritima NusG
Deposition date:
2012-02-27
Original release date:
2013-01-22
Authors:
Droegemueller, Johanna; Stegmann, Christian; Burmann, Bjoern; Roesch, Paul; Wahl, Markus; Schweimer, Kristian
Citation:

Citation: Drogemuller, Johanna; Stegmann, Christian; Mandal, Angshuman; Steiner, Thomas; Burmann, Bjorn; Gottesman, Max; Wohrl, Birgitta; Rosch, Paul; Wahl, Markus; Schweimer, Kristian. "An autoinhibited state in the structure of Thermotoga maritima NusG."  Structure 21, 365-375 (2013).
PubMed: 23415559

Assembly members:

Assembly members:
entity, polymer, 177 residues, 20178.822 Da.

Natural source:

Natural source:   Common Name: Thermotoga maritima   Taxonomy ID: 2336   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermotoga maritima

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-M11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAMKKKWYIVLTMSGYEEKV KENIEKKVEATGIKNLVGRI VIPIRGGQRRKSEKLFPGYV FVEMIMNDEAYNFVRSVPYV MGFVSSGGQPVPVKDREMRP ILRLAGLEEYEEKKKPVKVE LGFKVGDMVKIISGPFEDFA GVIKEIDPERQELKVNVTIF GRETPVVLHVSEVEKIE

Data sets:
Data typeCount
13C chemical shifts549
15N chemical shifts147
1H chemical shifts1199

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1NusG1

Entities:

Entity 1, NusG 177 residues - 20178.822 Da.

1   GLYALAMETLYSLYSLYSTRPTYRILEVAL
2   LEUTHRMETSERGLYTYRGLUGLULYSVAL
3   LYSGLUASNILEGLULYSLYSVALGLUALA
4   THRGLYILELYSASNLEUVALGLYARGILE
5   VALILEPROILEARGGLYGLYGLNARGARG
6   LYSSERGLULYSLEUPHEPROGLYTYRVAL
7   PHEVALGLUMETILEMETASNASPGLUALA
8   TYRASNPHEVALARGSERVALPROTYRVAL
9   METGLYPHEVALSERSERGLYGLYGLNPRO
10   VALPROVALLYSASPARGGLUMETARGPRO
11   ILELEUARGLEUALAGLYLEUGLUGLUTYR
12   GLUGLULYSLYSLYSPROVALLYSVALGLU
13   LEUGLYPHELYSVALGLYASPMETVALLYS
14   ILEILESERGLYPROPHEGLUASPPHEALA
15   GLYVALILELYSGLUILEASPPROGLUARG
16   GLNGLULEULYSVALASNVALTHRILEPHE
17   GLYARGGLUTHRPROVALVALLEUHISVAL
18   SERGLUVALGLULYSILEGLU

Samples:

sample_1: NusG, [U-95% 13C; U-95% 15N], 0.4 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.4; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB

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