BMRB Entry 51107

Name: 1H,15N and 13C backbone chemical shift assignment of Spy29-124
Published: 2022-04-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51107

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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: 1H,15N and 13C backbone chemical shift assignment of Spy29-124 PubMed: 35595811

Deposition date: 2021-09-28 Original release date: 2022-04-08

Authors: He, Wei; Li, Xinming; Xue, Hongjuan; Yang, Yuanyuan; Mencius, Jun; Bai, Ling; Zhang, Jiayin; Wu, Bin; Xue, Yi; Quan, Shu

Citation: He, Wei; Li, Xinming; Xue, Hongjuan; Yang, Yuanyuan; Mencius, Jun; Bai, Ling; Zhang, Jiayin; Xu, Jianhe; Wu, Bin; Xue, Yi; Quan, Shu. "Insights into the client protein release mechanism of the ATP-independent chaperone Spy" Nat. commun. 13, 2818-2818 (2022).

Assembly members:
entity_1, polymer, 96 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 BL21(DE3) Vector: pET28b(+)-HisSUMO-spy29-124

Entity Sequences (FASTA):
entity_1: FKDLNLTDAQKQQIREIMKG QRDQMKRPPLEERRAMHDII ASDTFDKVKAEAQIAKMEEQ RKANMLAHMETQNKIYNILT PEQKKQFNANFEKRLT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	271
15N chemical shifts	88
1H chemical shifts	88

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	spy29-124	1

Entities:

Entity 1, spy29-124 96 residues - Formula weight is not available

1

PHE

LYS

ASP

LEU

ASN

LEU

THR

ASP

ALA

GLN

2

LYS

GLN

ILE

ARG

GLU

ILE

MET

LYS

GLY

3

GLN

ARG

ASP

GLN

MET

LYS

ARG

PRO

LEU

4

GLU

ARG

ALA

MET

HIS

ASP

ILE

5

ALA

SER

ASP

THR

PHE

ASP

LYS

VAL

LYS

ALA

6

GLU

ALA

GLN

ILE

ALA

LYS

MET

GLU

GLN

7

ARG

LYS

ALA

ASN

MET

LEU

ALA

HIS

MET

GLU

8

THR

GLN

ASN

LYS

ILE

TYR

ASN

ILE

LEU

THR

9

PRO

GLU

GLN

LYS

GLN

PHE

ASN

ALA

ASN

10

PHE

GLU

LYS

ARG

LEU

THR

Samples:

sample_1: spy29-124, [U-13C; U-15N; U-2H], 0.4 mM; HEPES 40 mM; NaCl 150 mM; DTT 3 mM; PMSF 1 mM; NaN3 0.03%; inhibitor cocktail 100 x

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D trHNCO	sample_1	isotropic	sample_conditions_1
3D trHNCACO	sample_1	isotropic	sample_conditions_1
3D trHNCOCA	sample_1	isotropic	sample_conditions_1
3D trHNCA	sample_1	isotropic	sample_conditions_1
3D trHN(CA)CB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe v9.7 - processing

NMRFAM-SPARKY v1.2 - data analysis

qMDD v1.2 - data processing

NMR spectrometers:

Agilent DD2 800 MHz
Agilent DD2 600 MHz

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