BMRB Entry 19916

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp with dT7
Published: 2014-08-25

Click here to enlarge.

PDB ID: 2mo1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19916
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp with dT7

Deposition date:

2014-04-17

Original release date:

2014-08-25

Authors:

Jin, Bonghwan; Jeong, Ki-woong; Kim, Yangmee

Citation:

Citation: Jin, Bonghwan; Jeong, Ki-Woong; Kim, Yangmee. "Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus." Biochem. Biophys. Res. Commun. 451, 402-407 (2014).
PubMed: 25101648

Assembly members:

Assembly members:
entity, polymer, 68 residues, 7692.736 Da.
6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide, non-polymer, 272.321 Da.

Natural source:

Natural source: Common Name: thermophilic bacteria Taxonomy ID: 271 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus aquaticus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MKKGTVKWFNAEKGYGFIQQ EEGPDVFVHFTAIEADGFRT LNEGEHVEFEVEPGRGGKGP QAKKVRRI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	380
13C chemical shifts	155
15N chemical shifts	66

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1
2	entity_DT7	2

Entities:

Entity 1, entity 68 residues - 7692.736 Da.

1

MET

LYS

GLY

THR

VAL

LYS

TRP

PHE

ASN

2

ALA

GLU

LYS

GLY

TYR

GLY

PHE

ILE

GLN

3

GLU

GLY

PRO

ASP

VAL

PHE

VAL

HIS

PHE

4

THR

ALA

ILE

GLU

ALA

ASP

GLY

PHE

ARG

THR

5

LEU

ASN

GLU

GLY

GLU

HIS

VAL

GLU

PHE

GLU

6

VAL

GLU

PRO

GLY

ARG

GLY

LYS

GLY

PRO

7

GLN

ALA

LYS

VAL

ARG

ILE

Entity 2, entity_DT7 - C11 H16 N2 O4 S - 272.321 Da.

1

DT7

Samples:

tacspcom: potassium phosphate 50 mM; KCl 100 mM; EDTA 0.1 mM; thermus aquaticus cold shock protein, [U-99% 13C; U-99% 15N], 0.8 mM; heptathymidine 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	tacspcom	isotropic	sample_conditions_1
3D HN(CA)CO	tacspcom	isotropic	sample_conditions_1
3D CBCA(CO)NH	tacspcom	isotropic	sample_conditions_1
3D HN(CO)CA	tacspcom	isotropic	sample_conditions_1
3D HBHA(CO)NH	tacspcom	isotropic	sample_conditions_1
3D HNHA	tacspcom	isotropic	sample_conditions_1
3D HCCH-TOCSY	tacspcom	isotropic	sample_conditions_1
3D 1H-15N NOESY	tacspcom	isotropic	sample_conditions_1
3D 1H-13C NOESY	tacspcom	isotropic	sample_conditions_1
2D 1H-15N HSQC	tacspcom	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift calculation

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 500 MHz

BMRB	19915
PDB	2MO0 2MO1
GB	ALJ89896 EED09135 KOX89549
REF	WP_003049060 WP_018110812 WP_022797725 WP_053768577