BMRB Entry 25219

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25219
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution Structure of the UBM1 domain of human HUWE1/ARF-BP1
Deposition date:
2014-09-12
Original release date:
2015-09-14
Authors:
Farhadi, Sahar; Khatun, Rahima; Lemak, Alexander; Kaustov, Lilia; Ramabadran, Raghav; Hunter, Howard; Sheng, Yi
Citation:

Citation: Khatun, Rahima; Sheng, Yi. "Solution structure of Ubiquitin Binding Motif of human Arf-bp1"  .

Assembly members:

Assembly members:
entity, polymer, 53 residues, 5663.236 Da.

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: pGEX2TK

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: TSSEEEDPLAGISLPEGVDP SFLAALPDDIRREVLQNQLG IRPPTRTAPSTNS

Data sets:
Data typeCount
13C chemical shifts195
15N chemical shifts45
1H chemical shifts325

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 53 residues - 5663.236 Da.

1   THRSERSERGLUGLUGLUASPPROLEUALA
2   GLYILESERLEUPROGLUGLYVALASPPRO
3   SERPHELEUALAALALEUPROASPASPILE
4   ARGARGGLUVALLEUGLNASNGLNLEUGLY
5   ILEARGPROPROTHRARGTHRALAPROSER
6   THRASNSER

Samples:

sample_1: entity, [U-13C; U-15N], 0.4 mM; sodium chloride 300 mM; potassium chloride 2.7 mM; sodium phosphate 10 mM; potassium phosphate 2 mM; CHAPS 0.05 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

FMCGUI, Lemak A., Gutmanas A., Chitayat S., Karra M., Far s C., Sunnerhagen M., and Arrowsmith CH - chemical shift assignment, refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAA20771 BAC06833
EMBL CAI39580 CAI39581 CAI42354 CAI42654 CAI42656
GB AAF28950 AAV90838 AAX24125 AAY98258 EAW93160
REF NP_001103474 NP_001253681 NP_113584 XP_001914766 XP_002831735
SP Q7Z6Z7
TPG DAA12802
AlphaFold Q7Z6Z7

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