BMRB Entry 51899

Name: cytosolic abundant heat soluble protein motif 1 and 2
Published: 2023-04-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51899

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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:

cytosolic abundant heat soluble protein motif 1 and 2

Deposition date:

2023-04-06

Original release date:

2023-04-11

Authors:

Kang, Donguk; Park, Chin-Ju

Citation:

Citation: Kang, Donguk; Park, Chin-Ju. "CAHS motif 1 and 2" .

Assembly members:

Assembly members:
entity_1, polymer, 82 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Tardigrade Taxonomy ID: 42241 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: not available not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MKSSHHHHHHENLYFQSNAT EAYRKQQEVEADKIRKELEK QHLRDVEFRKDIVEMAIENQ KKMIDVESRYAKKDMDRERV KV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	192
15N chemical shifts	63
1H chemical shifts	63

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CAHS	1

Entities:

Entity 1, CAHS 82 residues - Formula weight is not available

1

MET

LYS

SER

HIS

2

GLU

ASN

LEU

TYR

PHE

GLN

SER

ASN

ALA

THR

3

GLU

ALA

TYR

ARG

LYS

GLN

GLU

VAL

GLU

4

ALA

ASP

LYS

ILE

ARG

LYS

GLU

LEU

GLU

LYS

5

GLN

HIS

LEU

ARG

ASP

VAL

GLU

PHE

ARG

LYS

6

ASP

ILE

VAL

GLU

MET

ALA

ILE

GLU

ASN

GLN

7

LYS

MET

ILE

ASP

VAL

GLU

SER

ARG

TYR

8

ALA

LYS

ASP

MET

ASP

ARG

GLU

ARG

VAL

9

LYS

VAL

Samples:

sample_1: CAHS motif 1 and 2, [U-99% 13C; U-99% 15N], 300 uM; MES 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

SPARKY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 900 MHz

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