BMRB Entry 51260

Name: Denatured State Backbone Assignments for Helix 1 from HHR23A Ubiquitin-Associated Domain 1 in Guanidine Hydrochloride Solutions
Published: 2022-06-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51260

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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: Denatured State Backbone Assignments for Helix 1 from HHR23A Ubiquitin-Associated Domain 1 in Guanidine Hydrochloride Solutions PubMed: 35430812

Deposition date: 2022-01-05 Original release date: 2022-06-08

Authors: Becht, Dustin; Briknarova, Klara; Bowler, Bruce

Citation: Becht, Dustin; Leavens, Moses; Zeng, Baisen; Rothfuss, Michael; Briknarova, Klara; Bowler, Bruce. "Residual Structure in the Denatured State of the Fast-Folding UBA(1) Domain from the Human DNA Excision Repair Protein HHR23A" Biochemistry 61, 767-784 (2022).

Assembly members:
entity_1, polymer, 22 residues, Formula weight is not available

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-2T(TEV)

Entity Sequences (FASTA):
entity_1: STLVTGSEYETMLTEIMSMG YE

Data sets:

assigned_chemical_shifts

Data type	Count
13C chemical shifts	168
15N chemical shifts	84
1H chemical shifts	84

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Helix 1 from UBA(1)	1

Entities:

Entity 1, Helix 1 from UBA(1) 22 residues - Formula weight is not available

1

SER

THR

LEU

VAL

THR

GLY

SER

GLU

TYR

GLU

2

THR

MET

LEU

THR

GLU

ILE

MET

SER

MET

GLY

3

TYR

GLU

Samples:

sample_1: Helix 1 from HHR23A ubiquitin-associated domain 1, [U-13C; U-15N], 0.21 mM; sodium phosphate 50 mM; NaCl 100 mM; guanidine hydrochloride 4 M

sample_2: Helix 1 from HHR23A ubiquitin-associated domain 1, [U-13C; U-15N], 0.21 mM; sodium phosphate 50 mM; NaCl 100 mM; guanidine hydrochloride 5 M

sample_3: Helix 1 from HHR23A ubiquitin-associated domain 1, [U-13C; U-15N], 0.21 mM; sodium phosphate 50 mM; NaCl 100 mM; guanidine hydrochloride 6 M

sample_4: Helix 1 from HHR23A ubiquitin-associated domain 1, [U-13C; U-15N], 0.21 mM; sodium phosphate 50 mM; NaCl 100 mM; guanidine hydrochloride 7 M

sample_conditions_1: ionic strength: 4 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 5 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_3: ionic strength: 6 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_4: ionic strength: 7 M; pH: 6.5; 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 HNCA	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_3
3D HNCO	sample_3	isotropic	sample_conditions_3
3D HNCA	sample_3	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_4
3D HNCO	sample_4	isotropic	sample_conditions_4
3D HNCA	sample_4	isotropic	sample_conditions_4

Software:

VNMRj - collection

NMRPipe - processing

CcpNMR - chemical shift assignment

NMR spectrometers:

Varian VNMRS 600 MHz

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