BMRB Entry 51260

Title:
Denatured State Backbone Assignments for Helix 1 from HHR23A Ubiquitin-Associated Domain 1 in Guanidine Hydrochloride Solutions
Deposition date:
2022-01-05
Original release date:
2022-06-08
Authors:
Becht, Dustin; Briknarova, Klara; Bowler, Bruce
Citation:

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).
PubMed: 35430812

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: STLVTGSEYETMLTEIMSMG YE

Data typeCount
13C chemical shifts168
15N chemical shifts84
1H chemical shifts84

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Helix 1 from UBA(1)1

Entities:

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

1   SERTHRLEUVALTHRGLYSERGLUTYRGLU
2   THRMETLEUTHRGLUILEMETSERMETGLY
3   TYRGLU

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
2D 1H-15N HSQCsample_3isotropicsample_conditions_3
3D HNCOsample_3isotropicsample_conditions_3
3D HNCAsample_3isotropicsample_conditions_3
2D 1H-15N HSQCsample_4isotropicsample_conditions_4
3D HNCOsample_4isotropicsample_conditions_4
3D HNCAsample_4isotropicsample_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 peaks
SPARKY: Backbone or all simulated peaks