BMRB Entry 52367

Name: The backbone assignment of disordered protein D131D
Published: 2024-07-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52367

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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 backbone assignment of disordered protein D131D

Deposition date:

2024-03-26

Original release date:

2024-07-22

Authors:

Qu, Xiaozhan

Citation:

Citation: Qu, Xiaozhan; Zhao, Shuo; Wan, Chanjuan; Zhu, Lei; Ji, Tuo; Rossi, Paolo; Wang, Junfeng; Kalodimos, Charalampos; Wang, Chao; Xu, Weiya; Huang, Chengdong. "Structural basis for the dynamic chaperoning of disordered clients by Hsp90" Nat. Struct. Mol. Biol. ., .-. (2024).
PubMed: 38890550

Assembly members:

Assembly members:
entity_1, polymer, 131 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET16a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ATSTLIKAIDGDTVKLMYKG QPMTFRLLLVDTPETKHPKK GVEKYGPEASAFTKKMVENA KKIEVEFDKGQRTDKYGRGL AYIYADGKMVNEALVRQGLA KVAYVYKPNNTHEQHLRKSE AQAKKEKLNIW

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	243
15N chemical shifts	116
1H chemical shifts	115

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	disordered protein D131D	1

Entities:

Entity 1, disordered protein D131D 131 residues - Formula weight is not available

1

ALA

THR

SER

THR

LEU

ILE

LYS

ALA

ILE

ASP

2

GLY

ASP

THR

VAL

LYS

LEU

MET

TYR

LYS

GLY

3

GLN

PRO

MET

THR

PHE

ARG

LEU

VAL

4

ASP

THR

PRO

GLU

THR

LYS

HIS

PRO

LYS

5

GLY

VAL

GLU

LYS

TYR

GLY

PRO

GLU

ALA

SER

6

ALA

PHE

THR

LYS

MET

VAL

GLU

ASN

ALA

7

LYS

ILE

GLU

VAL

GLU

PHE

ASP

LYS

GLY

8

GLN

ARG

THR

ASP

LYS

TYR

GLY

ARG

GLY

LEU

9

ALA

TYR

ILE

TYR

ALA

ASP

GLY

LYS

MET

VAL

10

ASN

GLU

ALA

LEU

VAL

ARG

GLN

GLY

LEU

ALA

11

LYS

VAL

ALA

TYR

VAL

TYR

LYS

PRO

ASN

12

THR

HIS

GLU

GLN

HIS

LEU

ARG

LYS

SER

GLU

13

ALA

GLN

ALA

LYS

GLU

LYS

LEU

ASN

ILE

14

TRP

Samples:

sample_1: disordered protein D131D, [U-99% 13C; U-99% 15N], 500 uM; MES monohydrate 25 mM; KCl 75 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 283 K

Experiments:

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

Software:

SPARKY - data analysis

NMRViewJ - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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