BMRB Entry 16267

Title:
Solution NMR structure of tungsten formylmethanofuran dehydrogenase subunit D from Archaeoglobus fulgidus, Northeast Structural Genomics Consortium target AtT7
Deposition date:
2009-04-28
Original release date:
2009-04-28
Authors:
Eletsky, Alexander; Wu, Yibing; Yee, Adelinda; Fares, Christophe; Lee, Hsiau-Wei; Prestegard, James; Arrowsmith, Cheryl; Szyperski, Thomas
Citation:

Citation: Eletsky, Alexander; Wu, Yibing; Yee, Adelinda; Fares, Christophe; Lee, Hsiau-Wei; Prestegard, James; Arrowsmith, Cheryl; Szyperski, Thomas. "Solution NMR structure of tungsten formylmethanofuran dehydrogenase subunit D from Archaeoglobus fulgidus"  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
AtT7_protein, polymer, 146 residues, 16169.288 Da.

Natural source:

Natural source:   Common Name: Archaeoglobus fulgidus   Taxonomy ID: 2234   Superkingdom: Archaea   Kingdom: not available   Genus/species: Archaeoglobus fulgidus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: p15Tv lic

Data sets:
Data typeCount
13C chemical shifts604
15N chemical shifts142
1H chemical shifts965

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AtT7_protein1

Entities:

Entity 1, AtT7_protein 146 residues - 16169.288 Da.

Residues 1-23 and 145-146 represent non-native affinity tags

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYARGGLUASNLEUTYRPHEGLN
3   GLYHISMETLEUGLUVALGLUVALILESER
4   GLYARGTHRLEUASNGLNGLYALATHRVAL
5   GLUGLULYSLEUTHRGLUGLUTYRPHEASN
6   ALAVALASNTYRALAGLUILEASNGLUGLU
7   ASPTRPASNALALEUGLYLEUGLNGLUGLY
8   ASPARGVALLYSVALLYSTHRGLUPHEGLY
9   GLUVALVALVALPHEALALYSLYSGLYASP
10   VALPROLYSGLYMETILEPHEILEPROMET
11   GLYPROTYRALAASNMETVALILEASPPRO
12   SERTHRASPGLYTHRGLYMETPROGLNPHE
13   LYSGLYVALLYSGLYTHRVALGLULYSTHR
14   ASPGLULYSVALLEUSERVALLYSGLULEU
15   LEUGLUALAILEGLYSER

Samples:

NC: AtT7 protein, [U-100% 13C; U-100% 15N], 0.6 mM; TRIS 10 mM; sodium chloride 300 mM; benzamidine 1 mM; H2O 90%; D2O 10%

NC5: AtT7 protein, [U-7% 13C; U-100% 15N], 0.6 mM; TRIS 10 mM; sodium chloride 300 mM; benzamidine 1 mM; H2O 90%; D2O 10%

NC5_phage: AtT7 protein, [U-7% 13C; U-100% 15N], 0.4 mM; TRIS 6.6 mM; sodium chloride 200 mM; benzamidine 0.7 mM; Pf1 phage 13.25 g/l; H2O 86%; D2O 14%

sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

phage: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aliphaticNCisotropicsample_conditions_1
3D HCCH-TOCSY aliphaticNCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aromaticNCisotropicsample_conditions_1
3D 1H-15N,13C NOESYNCisotropicsample_conditions_1
3D 1H-13C NOESYNCisotropicsample_conditions_1
2D MEXICONCisotropicsample_conditions_1
2D CLEANEXNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC methylNC5isotropicsample_conditions_1
2D 1H-15N HSQCNC5isotropicsample_conditions_1
2D 1H-15N TROSYNC5isotropicsample_conditions_1
2D 1H-15N HSQCNC5_phageisotropicphage
2D 1H-15N TROSYNC5_phageisotropicphage

Software:

VNMRJ v2.1B, Varian - collection

TOPSPIN, Bruker Biospin - collection, processing

PROSA v6.0.2, Guntert - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CSI v2.0, Wishart and Sykes - data analysis

TALOS v2007.068.09.07, Shen, Cornilescu, Delaglio and Bax - data analysis

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure validation

PSVS v1.3, Bhattacharya and Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
GB AAB89327 AIG98923
REF WP_010879421

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