BMRB Entry 51038

Name: Hsp104_NTD
Published: 2022-04-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51038

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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:

Hsp104_NTD

Deposition date:

2021-07-29

Original release date:

2022-04-13

Authors:

Harari, Anna; Zoltsman, Guy; Rosenzweig, Rina

Citation:

Citation: Harari, Anna; Zoltsman, Guy; Levin, Tal; Rosenzweig, Rina. "Hsp104 N-terminal domain interaction with substrates plays a regulatory role in protein disaggregation" FEBS J. 289, 5359-5377 (2022).
PubMed: 35305079

Assembly members:

Assembly members:
entity_1, polymer, 151 residues, Formula weight is not available

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MNDQTQFTERALTILTLAQK LASDHQHPQLQPIHILAAFI ETPEDGSVPYLQNLIEKGRY DYDLFKKVVNRNLVRIPQQQ PAPAEITPSYALGKVLQDAA KIQKQQKDSFIAQDHILFAL FNDSSIQQIFKEAQVDIEAI KQQALELRGNT

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	357
15N chemical shifts	132
1H chemical shifts	132

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Hsp104_NTD	1

Entities:

Entity 1, Hsp104_NTD 151 residues - Formula weight is not available

1

MET

ASN

ASP

GLN

THR

GLN

PHE

THR

GLU

ARG

2

ALA

LEU

THR

ILE

LEU

THR

LEU

ALA

GLN

LYS

3

LEU

ALA

SER

ASP

HIS

GLN

HIS

PRO

GLN

LEU

4

GLN

PRO

ILE

HIS

ILE

LEU

ALA

PHE

ILE

5

GLU

THR

PRO

GLU

ASP

GLY

SER

VAL

PRO

TYR

6

LEU

GLN

ASN

LEU

ILE

GLU

LYS

GLY

ARG

TYR

7

ASP

TYR

ASP

LEU

PHE

LYS

VAL

ASN

8

ARG

ASN

LEU

VAL

ARG

ILE

PRO

GLN

9

PRO

ALA

PRO

ALA

GLU

ILE

THR

PRO

SER

TYR

10

ALA

LEU

GLY

LYS

VAL

LEU

GLN

ASP

ALA

11

LYS

ILE

GLN

LYS

GLN

LYS

ASP

SER

PHE

12

ILE

ALA

GLN

ASP

HIS

ILE

LEU

PHE

ALA

LEU

13

PHE

ASN

ASP

SER

ILE

GLN

ILE

PHE

14

LYS

GLU

ALA

GLN

VAL

ASP

ILE

GLU

ALA

ILE

15

LYS

GLN

ALA

LEU

GLU

LEU

ARG

GLY

ASN

16

THR

Samples:

sample_1: Hsp104_NTD, [U-99% 13C; U-99% 15N], 3.6 mM; sodium azide 0.03%; HEPES 50 mM; potassium chloride 50 mM; DTT 2 mM

sample_conditions_1: pH: 7.5; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.4.2 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 800 MHz

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