BMRB Entry 25912

Name: Backbone 1H, 13C, and 15N Chemical Shift of bacterial IscA protein
Published: 2016-01-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25912

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone 1H, 13C, and 15N Chemical Shift of bacterial IscA protein

Deposition date:

2015-12-01

Original release date:

2016-01-19

Authors:

Pastore, Annalisa; Popovic, Matija; Kelly, Geoff

Citation:

Citation: Popovic, Matija; Kelly, Geoff; Pastore, Annalisa. "Chemical shift assignment of the difficult protein IscA" Biomol. NMR Assign. 10, 227-231 (2016).
PubMed: 26887894

Assembly members:

Assembly members:
IscA, polymer, 107 residues, Formula weight is not available

Natural source:

Natural source: Common Name: enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: Eubacteria Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
IscA: MSITLSDSAAARVNTFLANR GKGFGLRLGVRTSGCSGMAY VLEFVDEPTPEDIVFEDKGV KVVVDGKSLQFLDGTQLDFV KEGLNEGFKFTNPNVKDECG CGESFHV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	270
15N chemical shifts	91
1H chemical shifts	166

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IscA, 1	1
2	IscA, 2	1

Entities:

Entity 1, IscA, 1 107 residues - Formula weight is not available

1

MET

SER

ILE

THR

LEU

SER

ASP

SER

ALA

2

ALA

ARG

VAL

ASN

THR

PHE

LEU

ALA

ASN

ARG

3

GLY

LYS

GLY

PHE

GLY

LEU

ARG

LEU

GLY

VAL

4

ARG

THR

SER

GLY

CYS

SER

GLY

MET

ALA

TYR

5

VAL

LEU

GLU

PHE

VAL

ASP

GLU

PRO

THR

PRO

6

GLU

ASP

ILE

VAL

PHE

GLU

ASP

LYS

GLY

VAL

7

LYS

VAL

ASP

GLY

LYS

SER

LEU

GLN

8

PHE

LEU

ASP

GLY

THR

GLN

LEU

ASP

PHE

VAL

9

LYS

GLU

GLY

LEU

ASN

GLU

GLY

PHE

LYS

PHE

10

THR

ASN

PRO

ASN

VAL

LYS

ASP

GLU

CYS

GLY

11

CYS

GLY

GLU

SER

PHE

HIS

VAL

Samples:

sample_1: IscA, [U-99% 13C; U-99% 15N], 50 – 400 uM; Tris-HCl 20 mM; NaCl 150 mM; TCEP 5 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.150 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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