BMRB Entry 30824

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30824
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Protein complex
Deposition date:
2020-12-03
Original release date:
2021-12-10
Authors:
Lu, X.; Walters, K.
Citation:

Citation: Lu, Xiuxiu; Sabbasani, Venkata; Osei-Amponsa, Vasty; Evans, Christine; King, Julianna; Tarasov, Sergey; Dyba, Marzena; Das, Sudipto; Chan, King; Schwieters, Charles; Choudhari, Sulbha; Fromont, Caroline; Zhao, Yongmei; Tran, Bao; Chen, Xiang; Matsuo, Hiroshi; Andresson, Thorkell; Chari, Raj; Swenson, Rolf; Tarasova, Nadya; Walters, Kylie. "Structure-guided bifunctional molecules hit a DEUBAD-lacking hRpn13 species upregulated in multiple myeloma"  Nat. Commun. 12, 7318-7318 (2021).
PubMed: 34916494

Assembly members:

Assembly members:
entity_1, polymer, 154 residues, 17040.340 Da.
entity_XAY, non-polymer, 427.452 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSMTTSGALFPSLVPGSR GASNKYLVEFRAGKMSLKGT TVTPDKRKGLVYIQQTDDSL IHFCWKDRTSGNVEDDLIIF PDDCEFKRVPQCPSGRVYVL KFKAGSKRLFFWMQEPKTDQ DEEHCRKVNEYLNNPPMPGA LGASGSSGHELSAL

Data sets:
Data typeCount
13C chemical shifts189
15N chemical shifts109
1H chemical shifts643

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 154 residues - 17040.340 Da.

1   GLYPROGLYSERMETTHRTHRSERGLYALA
2   LEUPHEPROSERLEUVALPROGLYSERARG
3   GLYALASERASNLYSTYRLEUVALGLUPHE
4   ARGALAGLYLYSMETSERLEULYSGLYTHR
5   THRVALTHRPROASPLYSARGLYSGLYLEU
6   VALTYRILEGLNGLNTHRASPASPSERLEU
7   ILEHISPHECYSTRPLYSASPARGTHRSER
8   GLYASNVALGLUASPASPLEUILEILEPHE
9   PROASPASPCYSGLUPHELYSARGVALPRO
10   GLNCYSPROSERGLYARGVALTYRVALLEU
11   LYSPHELYSALAGLYSERLYSARGLEUPHE
12   PHETRPMETGLNGLUPROLYSTHRASPGLN
13   ASPGLUGLUHISCYSARGLYSVALASNGLU
14   TYRLEUASNASNPROPROMETPROGLYALA
15   LEUGLYALASERGLYSERSERGLYHISGLU
16   LEUSERALALEU

Entity 2, unit_2 - C25 H21 N3 O4 - 427.452 Da.

1   XAY

Samples:

sample_1: 13C_protein, [U-13C], 0.4 mM; ligand 0.48 mM

sample_2: 13C_protein, [U-13C], 0.25 mM; ligand 0.5 mM

sample_3: ligand, [U-13C], 0.5 mM; protein 0.5 mM

sample_4: ligand, [U-13C], 0.4 mM; protein 0.4 mM

sample_5: ligand 0.5 mM; protein, [U-15N], 0.25 mM

sample_conditions_1: ionic strength: 0.11 M; pH: 6.5; pressure: 1 atm; temperature: 283.15 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_5isotropicsample_conditions_1
3D 1H-13C half-filtered NOESYsample_2isotropicsample_conditions_1
2D 1H-13C half-filtered NOESYsample_3isotropicsample_conditions_1
3D 1H-13C half-filtered NOESYsample_4isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

XEASY, Bartels et al. - chemical shift assignment

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

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

NMR spectrometers:

  • Bruker AVANCE III 850 MHz

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