BMRB Entry 15819

Title:
Solution NMR Structure of the replication Factor A Related Protein from Methanobacterium thermoautotrophicum. Northeast Structural Genomics Target TR91A.
Deposition date:
2008-06-23
Original release date:
2008-08-08
Authors:
Rossi, Paolo; Xiao, Rong; Maglaqui, Melissa; Foote, Erica; Ciccosanti, Coleen; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Everett, John; Montelione, Gaetano
Citation:

Citation: Rossi, Paolo; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Solution NMR Structure of the replication Factor A Related Protein from Methanobacterium thermoautotrophicum. Northeast Structural Genomics Target TR91A."  .

Assembly members:

Assembly members:
TR91A, polymer, 110 residues, 12479.563 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

Data sets:
Data typeCount
13C chemical shifts475
15N chemical shifts103
1H chemical shifts761

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TR91A1

Entities:

Entity 1, TR91A 110 residues - 12479.563 Da.

1   METLYSPROGLUHISARGMETASPTHRILE
2   SERLYSLEUGLUGLUGLYALAGLUTHRPRO
3   VALTHRGLYARGVALMETLYSILESERSER
4   PROARGTHRPHETHRTHRARGLYSGLYARG
5   GLUGLYLYSLEUALAASNVALILEILEALA
6   ASPASPTHRGLYGLULEUARGALAVALPHE
7   TRPTHRGLUASNILELYSLEULEULYSLYS
8   PHEARGGLUGLYASPVALILEARGILELYS
9   ASPVALASNILEARGGLYGLYPHEGLYGLY
10   ARGLYSGLUALAHISLEUMETPROARGSER
11   THRVALGLUVALLEUASPPROLEUGLUHIS

Samples:

sample_1: TR91A, [U-100% 13C; U-100% 15N], 1.25 mM; MES 20 mM; sodium chloride 100 mM; DTT 100 mM; Calcium Chloride 5 mM; sodium azide 0.02%

sample_2: TR91A, [U-100% 15N; 5% 13C], 1.33 mM; MES 20 mM; sodium chloride 100 mM; DTT 100 mM; Calcium Chloride 5 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC (arom)sample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY (aliph)sample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D HET NOEsample_2isotropicsample_conditions_1
Pseudo 2D T1sample_2isotropicsample_conditions_1
Pseudo 2D T2 (CPMG)sample_2isotropicsample_conditions_1
3D 1H-13C NOESY (arom)sample_1isotropicsample_conditions_1
2D 1H-13C HSQC (aliph)sample_1isotropicsample_conditions_1
2D 1H-13C HSQC (stereomethyl)sample_1isotropicsample_conditions_1

Software:

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

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

SPARKY v3.113, Goddard - data analysis

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

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

TOPSPIN v2.1, Bruker Biospin - collection

PSVS, Bhattacharya and Montelione - validation

RPF(AutoStructure), Huang, Tejero, Powers and Montelione - validation

Molmol, Koradi, Billeter and Wuthrich - visualization

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - validation

MolProbity, Richardson - validation

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 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