BMRB Entry 51108

Name: 1H,15N and 13C backbone chemical shift assignment of Spy1-124
Published: 2022-04-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51108

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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 Spy1-124 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, 124 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-spy1-124

Entity Sequences (FASTA):
entity_1: ADTTTAAPADAKPMMHHKGK FGPHQDMMFKDLNLTDAQKQ QIREIMKGQRDQMKRPPLEE RRAMHDIIASDTFDKVKAEA QIAKMEEQRKANMLAHMETQ NKIYNILTPEQKKQFNANFE KRLT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	323
15N chemical shifts	103
1H chemical shifts	103

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	spy1-124	1

Entities:

Entity 1, spy1-124 124 residues - Formula weight is not available

1

ALA

ASP

THR

ALA

PRO

ALA

ASP

2

ALA

LYS

PRO

MET

HIS

LYS

GLY

LYS

3

PHE

GLY

PRO

HIS

GLN

ASP

MET

PHE

LYS

4

ASP

LEU

ASN

LEU

THR

ASP

ALA

GLN

LYS

GLN

5

GLN

ILE

ARG

GLU

ILE

MET

LYS

GLY

GLN

ARG

6

ASP

GLN

MET

LYS

ARG

PRO

LEU

GLU

7

ARG

ALA

MET

HIS

ASP

ILE

ALA

SER

8

ASP

THR

PHE

ASP

LYS

VAL

LYS

ALA

GLU

ALA

9

GLN

ILE

ALA

LYS

MET

GLU

GLN

ARG

LYS

10

ALA

ASN

MET

LEU

ALA

HIS

MET

GLU

THR

GLN

11

ASN

LYS

ILE

TYR

ASN

ILE

LEU

THR

PRO

GLU

12

GLN

LYS

GLN

PHE

ASN

ALA

ASN

PHE

GLU

13

LYS

ARG

LEU

THR

Samples:

sample_1: spy1-124, [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