BMRB Entry 16267

Name: Solution NMR structure of tungsten formylmethanofuran dehydrogenase subunit D from Archaeoglobus fulgidus, Northeast Structural Genomics Consortium target AtT7
Published: 2009-04-28

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PDB ID: 2ki8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16267
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
AtT7_protein: MGSSHHHHHHSSGRENLYFQ GHMLEVEVISGRTLNQGATV EEKLTEEYFNAVNYAEINEE DWNALGLQEGDRVKVKTEFG EVVVFAKKGDVPKGMIFIPM GPYANMVIDPSTDGTGMPQF KGVKGTVEKTDEKVLSVKEL LEAIGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	604
15N chemical shifts	142
1H chemical shifts	965

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	AtT7_protein	1

Entities:

Entity 1, AtT7_protein 146 residues - 16169.288 Da.

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

1

MET

GLY

SER

HIS

2

SER

GLY

ARG

GLU

ASN

LEU

TYR

PHE

GLN

3

GLY

HIS

MET

LEU

GLU

VAL

GLU

VAL

ILE

SER

4

GLY

ARG

THR

LEU

ASN

GLN

GLY

ALA

THR

VAL

5

GLU

LYS

LEU

THR

GLU

TYR

PHE

ASN

6

ALA

VAL

ASN

TYR

ALA

GLU

ILE

ASN

GLU

7

ASP

TRP

ASN

ALA

LEU

GLY

LEU

GLN

GLU

GLY

8

ASP

ARG

VAL

LYS

VAL

LYS

THR

GLU

PHE

GLY

9

GLU

VAL

PHE

ALA

LYS

GLY

ASP

10

VAL

PRO

LYS

GLY

MET

ILE

PHE

ILE

PRO

MET

11

GLY

PRO

TYR

ALA

ASN

MET

VAL

ILE

ASP

PRO

12

SER

THR

ASP

GLY

THR

GLY

MET

PRO

GLN

PHE

13

LYS

GLY

VAL

LYS

GLY

THR

VAL

GLU

LYS

THR

14

ASP

GLU

LYS

VAL

LEU

SER

VAL

LYS

GLU

LEU

15

LEU

GLU

ALA

ILE

GLY

SER

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
3D HN(CA)CO	NC	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC	isotropic	sample_conditions_1
3D HNCACB	NC	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC	isotropic	sample_conditions_1
(4,3)D GFT HCCH-COSY aliphatic	NC	isotropic	sample_conditions_1
3D HCCH-TOCSY aliphatic	NC	isotropic	sample_conditions_1
(4,3)D GFT HCCH-COSY aromatic	NC	isotropic	sample_conditions_1
3D 1H-15N,13C NOESY	NC	isotropic	sample_conditions_1
3D 1H-13C NOESY	NC	isotropic	sample_conditions_1
2D MEXICO	NC	isotropic	sample_conditions_1
2D CLEANEX	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC methyl	NC5	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC5	isotropic	sample_conditions_1
2D 1H-15N TROSY	NC5	isotropic	sample_conditions_1
2D 1H-15N HSQC	NC5_phage	isotropic	phage
2D 1H-15N TROSY	NC5_phage	isotropic	phage

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

PDB	2KI8
GB	AAB89327 AIG98923
REF	WP_010879421

Biological Magnetic Resonance Data Bank