BMRB Entry 16746

Name: Chemical shift assignment of GmR58A from Geobacter metallireducens. Northeast Structural Genomics Consortium Target GmR58A
Published: 2010-03-31

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PDB ID: 2kut
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16746
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Chemical shift assignment of GmR58A from Geobacter metallireducens. Northeast Structural Genomics Consortium Target GmR58A

Deposition date:

2010-02-28

Original release date:

2010-03-31

Authors:

Lee, Hsiau-Wei; Wang, Huang; Buchwald, William; Janjua, Haleema; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Prestegard, James

Citation:

Citation: Lee, Hsiau-Wei; Montelione, Gaetano; Prestegard, James. "Solution Structure of GmR58A" .

Assembly members:

Assembly members:
GmR58A, polymer, 122 residues, 13133.925 Da.

Natural source:

Natural source: Common Name: Geobacter metallireducens Taxonomy ID: 28232 Superkingdom: Bacteria Kingdom: not available Genus/species: Geobacter metallireducens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Geobacter metallireducens Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
GmR58A: MDLPITLSKETPFEGEEITV SARVTNRGAAEAHNVPVAVY LGNPAQGGVEIGRDTISRIP VGGTGLARVQWKATRKLAGR AANPGVPVYAVVDPDNRVAE SDKANNVFSRIVKVLEHHHH HH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
RDCs

Data type	Count
13C chemical shifts	451
15N chemical shifts	107
1H chemical shifts	717
residual dipolar couplings	155

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GmR58A	1

Entities:

Entity 1, GmR58A 122 residues - 13133.925 Da.

LEHHHHHH are at the C-terminal as part of Hig-Tag

1

MET

ASP

LEU

PRO

ILE

THR

LEU

SER

LYS

GLU

2

THR

PRO

PHE

GLU

GLY

GLU

ILE

THR

VAL

3

SER

ALA

ARG

VAL

THR

ASN

ARG

GLY

ALA

4

GLU

ALA

HIS

ASN

VAL

PRO

VAL

ALA

VAL

TYR

5

LEU

GLY

ASN

PRO

ALA

GLN

GLY

VAL

GLU

6

ILE

GLY

ARG

ASP

THR

ILE

SER

ARG

ILE

PRO

7

VAL

GLY

THR

GLY

LEU

ALA

ARG

VAL

GLN

8

TRP

LYS

ALA

THR

ARG

LYS

LEU

ALA

GLY

ARG

9

ALA

ASN

PRO

GLY

VAL

PRO

VAL

TYR

ALA

10

VAL

ASP

PRO

ASP

ASN

ARG

VAL

ALA

GLU

11

SER

ASP

LYS

ALA

ASN

VAL

PHE

SER

ARG

12

ILE

VAL

LYS

VAL

LEU

GLU

HIS

13

HIS

Samples:

NC_Sample: GmR58A, [U-100% 13C; U-100% 15N], 0.77 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; H2O 95%; D2O 5%

PEG: GmR58A, [U-100% 13C; U-100% 15N], 0.65 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; C12E5 4.2%; H2O 95%; D2O 5%

Negative_Gel: GmR58A, [U-100% 13C; U-100% 15N], 0.65 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; negatively charged compressed polyacrylamide gel 7%; H2O 95%; D2O 5%

Stretch_Gel: GmR58A, [U-100% 13C; U-100% 15N], 0.65 mM; sodium azide 2%; DTT 10 mM; CaCl 5 mM; sodium chloride 200 mM; MES 20 mM; Neutral stretched polyacrylamide gel 5%; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_Sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_Sample	isotropic	sample_conditions_1
3D C(CO)NH	NC_Sample	isotropic	sample_conditions_1
3D HNCO	NC_Sample	isotropic	sample_conditions_1
3D HNCACB	NC_Sample	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_Sample	isotropic	sample_conditions_1
3D H(CCO)NH	NC_Sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_Sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC_Sample	isotropic	sample_conditions_1
3D 1H-13C NOESY	NC_Sample	isotropic	sample_conditions_1
NH J-modulation	PEG	anisotropic	sample_conditions_1
NH J-modulation	Negative_Gel	anisotropic	sample_conditions_1
NH J-modulation	Stretch_Gel	anisotropic	sample_conditions_1

Software:

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

X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - refinement

SPARKY v3.115, Goddard - chemical shift assignment

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

PSVS, Bhattacharya and Montelione - data analysis

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMR spectrometers:

Varian INOVA 600 MHz