BMRB Entry 25995

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25995
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:
Protein complex
Deposition date:
2016-03-12
Original release date:
2016-07-18
Authors:
Chen, Xiang; Walters, Kylie
Citation:

Citation: Chen, Xiang; Randles, Leah; Shi, Ke; Tarasov, Sergey; Aihara, Hideki; Walters, Kylie. "Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome"  Structure 24, 1257-1270 (2016).
PubMed: 27396824

Assembly members:

Assembly members:
entity_1, polymer, 150 residues, Formula weight is not available
entity_2, polymer, 78 residues, 8764.290 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: pRSET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MTTSGALFPSLVPGSRGASN KYLVEFRAGKMSLKGTTVTP DKRKGLVYIQQTDDSLIHFC WKDRTSGNVEDDLIIFPDDC EFKRVPQCPSGRVYVLKFKA GSKRLFFWMQEPKTDQDEEH CRKVNEYLNNPPMPGALGAS GSSGHELSAL
entity_2: APAEPKIIKVTVKTPKEKEE FAVPENSSVQQFKEAISKRF KSQTDQLVLIFAGKILKDQD TLIQHGIHDGLTVHLVIK

Data sets:
Data typeCount
13C chemical shifts581
15N chemical shifts149
1H chemical shifts915

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 150 residues - Formula weight is not available

1   METTHRTHRSERGLYALALEUPHEPROSER
2   LEUVALPROGLYSERARGGLYALASERASN
3   LYSTYRLEUVALGLUPHEARGALAGLYLYS
4   METSERLEULYSGLYTHRTHRVALTHRPRO
5   ASPLYSARGLYSGLYLEUVALTYRILEGLN
6   GLNTHRASPASPSERLEUILEHISPHECYS
7   TRPLYSASPARGTHRSERGLYASNVALGLU
8   ASPASPLEUILEILEPHEPROASPASPCYS
9   GLUPHELYSARGVALPROGLNCYSPROSER
10   GLYARGVALTYRVALLEULYSPHELYSALA
11   GLYSERLYSARGLEUPHEPHETRPMETGLN
12   GLUPROLYSTHRASPGLNASPGLUGLUHIS
13   CYSARGLYSVALASNGLUTYRLEUASNASN
14   PROPROMETPROGLYALALEUGLYALASER
15   GLYSERSERGLYHISGLULEUSERALALEU

Entity 2, entity_2 78 residues - 8764.290 Da.

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

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N; U-70% 2H], 0.7 mM; entity_2 0.7 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%; H2O 95%; D2O, [U-2H], 5%

sample_2: entity_1, [U-100% 15N], 0.7 mM; entity_2 0.7 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%; H2O 95%; D2O, [U-2H], 5%

sample_3: entity_1, [U-100% 13C], 0.7 mM; entity_2 0.7 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%; D2O, [U-2H], 100%

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 HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

XEASY, Bartels et al. - data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 850 MHz
  • Bruker Avance 600 MHz

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