BMRB Entry 30528

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30528
MolProbity Validation Chart

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NMR-STAR v3 text file.
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Title:
Shuttle proteins complex
Deposition date:
2018-10-23
Original release date:
2019-08-30
Authors:
Chen, X.; Walters, K.
Citation:

Citation: Chen, Xiang; Ebelle, Danielle; Wright, Brandon; Sridharan, Vinidhra; Hooper, Evan; Walters, Kylie. "Structure of hRpn10 Bound to UBQLN2 UBL Illustrates Basis for Complementarity between Shuttle Factors and Substrates at the Proteasome"  J. Mol. Biol. 431, 939-955 (2019).
PubMed: 30664872

Assembly members:

Assembly members:
entity_1, polymer, 111 residues, 11826.878 Da.
entity_2, polymer, 78 residues, 8764.189 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: MLGLGASDFEFGVDPSADPE LALALRVSMEEQRQRQEEEA RRAAAASAAEAGIATTGTED SDDALLKMTISQQEFGRTGL PDLSSMTEEEQIAYAMQMSL QGAEFGQAESA
entity_2: APAEPKIIKVTVKTPKEKEE FAVPENSSVQQFKEAISKRF KSQTDQLVLIFAGKILKDQD TLIQHGIHDGLTVHLVIK

Data sets:
Data typeCount
13C chemical shifts851
15N chemical shifts279
1H chemical shifts1924

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_2, 12
3entity_2, 22

Entities:

Entity 1, entity_1 111 residues - 11826.878 Da.

1   METLEUGLYLEUGLYALASERASPPHEGLU
2   PHEGLYVALASPPROSERALAASPPROGLU
3   LEUALALEUALALEUARGVALSERMETGLU
4   GLUGLNARGGLNARGGLNGLUGLUGLUALA
5   ARGARGALAALAALAALASERALAALAGLU
6   ALAGLYILEALATHRTHRGLYTHRGLUASP
7   SERASPASPALALEULEULYSMETTHRILE
8   SERGLNGLNGLUPHEGLYARGTHRGLYLEU
9   PROASPLEUSERSERMETTHRGLUGLUGLU
10   GLNILEALATYRALAMETGLNMETSERLEU
11   GLNGLYALAGLUPHEGLYGLNALAGLUSER
12   ALA

Entity 2, entity_2, 1 78 residues - 8764.189 Da.

1   ALAPROALAGLUPROLYSILEILELYSVAL
2   THRVALLYSTHRPROLYSGLULYSGLUGLU
3   PHEALAVALPROGLUASNSERSERVALGLN
4   GLNPHELYSGLUALAILESERLYSARGPHE
5   LYSSERGLNTHRASPGLNLEUVALLEUILE
6   PHEALAGLYLYSILELEULYSASPGLNASP
7   THRLEUILEGLNHISGLYILEHISASPGLY
8   LEUTHRVALHISLEUVALILELYS

Samples:

sample_1: hRpn10 196-306, [U-100% 15N], 0.6 mM; UBQLN2 UBL 1.38 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%

sample_2: hRpn10 196-306, [U-100% 13C], 0.6 mM; UBQLN2 UBL 1.38 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%

sample_3: hRpn10 196-306, [U-100% 15N; U-100% 2H], 0.6 mM; UBQLN2 UBL 1.38 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%

sample_4: hRpn10 196-306 0.6 mM; UBQLN2 UBL, [U-100% 13C; U-100% 15N], 0.6 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%

sample_5: hRpn10 196-306 0.6 mM; UBQLN2 UBL, [U-100% 13C; U-100% 15N], 0.6 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%

sample_6: UBQLN2 UBL, [U-100% 13C; U-100% 15N], 0.6 mM; NaPO4 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_5isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D 1H-13C half-filter NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_6isotropicsample_conditions_1
3D 1H-13C half-filter NOESYsample_5isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_5isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_5isotropicsample_conditions_1
3D 1H-13C half-filter NOESYsample_6isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_5isotropicsample_conditions_1
3D HCCH-TOCSYsample_5isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz

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