BMRB Entry 17204

Name: the 1H, 13C and 15N resonance assignment of ubiquitin-like small archaeal modifier protein from Haloferax volcanii
Published: 2014-03-04

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17204

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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 1H, 13C and 15N resonance assignment of ubiquitin-like small archaeal modifier protein from Haloferax volcanii

Deposition date:

2010-09-24

Original release date:

2014-03-04

Authors:

Zhang, Wen; Fan, Kai; Zhang, Jiahai; Tu, Xiaoming

Citation:

Citation: Liao, Shanhui; Zhang, Wen; Fan, Kai; Ye, Kaiqin; Zhang, Xuecheng; Zhang, Jiahai; Xu, Chao; Tu, Xiaoming. "Ionic strength-dependent conformations of a ubiquitin-like small archaeal modifier protein (SAMP2) from Haloferax volcanii." Sci. Rep. 3, 2136-2136 (2013).
PubMed: 23823798

Assembly members:

Assembly members:
ubiquitin-like_small_archaeal_modifier_protein, polymer, 74 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Haloferax volcanii Taxonomy ID: 2246 Superkingdom: Archaea Kingdom: not available Genus/species: Haloferax volcanii

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet22

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ubiquitin-like_small_archaeal_modifier_protein: MNVTVEVVGEETSEVAVDDD GTYADLVRAVDLSPHEVTVL VDGRPVPEDQSVEVDRVKVL RLIKGGLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	179
15N chemical shifts	61
1H chemical shifts	367

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ubiquitin-like small archaeal modifier protein	1

Entities:

Entity 1, ubiquitin-like small archaeal modifier protein 74 residues - Formula weight is not available

1

MET

ASN

VAL

THR

VAL

GLU

VAL

GLY

GLU

2

GLU

THR

SER

GLU

VAL

ALA

VAL

ASP

3

GLY

THR

TYR

ALA

ASP

LEU

VAL

ARG

ALA

VAL

4

ASP

LEU

SER

PRO

HIS

GLU

VAL

THR

VAL

LEU

5

VAL

ASP

GLY

ARG

PRO

VAL

PRO

GLU

ASP

GLN

6

SER

VAL

GLU

VAL

ASP

ARG

VAL

LYS

VAL

LEU

7

ARG

LEU

ILE

LYS

GLY

LEU

GLU

HIS

8

HIS

Samples:

sample_1: submit 2, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 25 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.125 M; pH: 6.7; pressure: 1 atm; temperature: 293 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment, collection

NMR spectrometers:

Bruker DMX 500 MHz

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