BMRB Entry 18362

Name: The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(S107A)
Published: 2012-09-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18362

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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: The chemical shifts and T1, T2, and 1H-15N NOE data for apo-IscU(S107A) PubMed: 22734684

Deposition date: 2012-03-29 Original release date: 2012-09-14

Authors: Kim, Jin Hae; Tonelli, Marco; Markley, John

Citation: Kim, Jin Hae; Tonelli, Marco; Kim, Taewook; Markley, John. "Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli." Biochemistry 51, 5557-5563 (2012).

Assembly members:
IscU(S107A), polymer, 128 residues, Formula weight is not available

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
IscU(S107A): MAYSEKVIDHYENPRNVGSF DNNDENVGSGMVGAPACGDV MKLQIKVNDEGIIEDARFKT YGCGSAIASSSLVTEWVKGK SLDEAQAIKNTDIAEELELP PVKIHCAILAEDAIKAAIAD YKSKREAK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1
heteronucl_T1_relaxation
- heteronuclear_T1_list_1
heteronucl_T2_relaxation
- heteronuclear_T2_list_1

Data type	Count
13C chemical shifts	263
15N chemical shifts	90
1H chemical shifts	92
T1 relaxation values	81
T2 relaxation values	81
heteronuclear NOE values	80

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IscU(S107A)	1

Entities:

Entity 1, IscU(S107A) 128 residues - Formula weight is not available

1

MET

ALA

TYR

SER

GLU

LYS

VAL

ILE

ASP

HIS

2

TYR

GLU

ASN

PRO

ARG

ASN

VAL

GLY

SER

PHE

3

ASP

ASN

ASP

GLU

ASN

VAL

GLY

SER

GLY

4

MET

VAL

GLY

ALA

PRO

ALA

CYS

GLY

ASP

VAL

5

MET

LYS

LEU

GLN

ILE

LYS

VAL

ASN

ASP

GLU

6

GLY

ILE

GLU

ASP

ALA

ARG

PHE

LYS

THR

7

TYR

GLY

CYS

GLY

SER

ALA

ILE

ALA

SER

8

SER

LEU

VAL

THR

GLU

TRP

VAL

LYS

GLY

LYS

9

SER

LEU

ASP

GLU

ALA

GLN

ALA

ILE

LYS

ASN

10

THR

ASP

ILE

ALA

GLU

LEU

GLU

LEU

PRO

11

PRO

VAL

LYS

ILE

HIS

CYS

ALA

ILE

LEU

ALA

12

GLU

ASP

ALA

ILE

LYS

ALA

ILE

ALA

ASP

13

TYR

LYS

SER

LYS

ARG

GLU

ALA

LYS

Samples:

sample_1: IscU(S107A), [U-13C; U-15N], 1.5 – 2 mM; TRIS 20 mM; DTT 5 mM; EDTA 0.5 mM; sodium chloride 150 mM; DSS 0.7 mM; D2O, [U-99% 2H], 7%; sodium azide 0.02%; H2O, [U-99% 2H], 93%

sample_conditions_1: ionic strength: 0.15 M; pH: 8; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

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

VNMRJ, Varian - collection

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Varian VNMRS 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts