BMRB Entry 25829

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25829
MolProbity Validation Chart

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All files associated with the entry

Title:
p75NTR DD:RhoGDI
Deposition date:
2015-09-30
Original release date:
2015-12-21
Authors:
Lin, Zhi; Ibanez, Carlos
Citation:

Citation: Lin, Zhi; Tann, Jason; Goh, Eddy; Kelly, Claire; Lim, Kim; Gao, Jian; Ibanez, Carlos. "Structural basis of death domain signaling in the p75 neurotrophin receptor"  Elife 4, 11692-11692 (2015).
PubMed: 26646181

Assembly members:

Assembly members:
entity_1, polymer, 94 residues, 10172.424 Da.
entity_2, polymer, 174 residues, 19884.719 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: pET32a-derived

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GLYSSLPPAKREEVEKLLNG SAGDTWRHLAGELGYQPEHI DSFTHEACPVRALLASWATQ DSATLDALLAALRRIQRADL VESLCSESTATSPV
entity_2: AQKSIQEIQELDKDDESLRK YKEALLGRVAVSADPNVPNV VVTGLTLVCSSAPGPLELDL TGDLESFKKQSFVLKEGVEY RIKISFRVNREIVSGMKYIQ HTYRKGVKIDKTDYMVGSYG PRAEEYEFLTPVEEAPKGML ARGSYSIKSRFTDDDKTDHL SWEWNLTIKKDWKD

Data sets:
Data typeCount
13C chemical shifts878
15N chemical shifts257
1H chemical shifts1713

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 94 residues - 10172.424 Da.

1   GLYLEUTYRSERSERLEUPROPROALALYS
2   ARGGLUGLUVALGLULYSLEULEUASNGLY
3   SERALAGLYASPTHRTRPARGHISLEUALA
4   GLYGLULEUGLYTYRGLNPROGLUHISILE
5   ASPSERPHETHRHISGLUALACYSPROVAL
6   ARGALALEULEUALASERTRPALATHRGLN
7   ASPSERALATHRLEUASPALALEULEUALA
8   ALALEUARGARGILEGLNARGALAASPLEU
9   VALGLUSERLEUCYSSERGLUSERTHRALA
10   THRSERPROVAL

Entity 2, entity_2 174 residues - 19884.719 Da.

1   ALAGLNLYSSERILEGLNGLUILEGLNGLU
2   LEUASPLYSASPASPGLUSERLEUARGLYS
3   TYRLYSGLUALALEULEUGLYARGVALALA
4   VALSERALAASPPROASNVALPROASNVAL
5   VALVALTHRGLYLEUTHRLEUVALCYSSER
6   SERALAPROGLYPROLEUGLULEUASPLEU
7   THRGLYASPLEUGLUSERPHELYSLYSGLN
8   SERPHEVALLEULYSGLUGLYVALGLUTYR
9   ARGILELYSILESERPHEARGVALASNARG
10   GLUILEVALSERGLYMETLYSTYRILEGLN
11   HISTHRTYRARGLYSGLYVALLYSILEASP
12   LYSTHRASPTYRMETVALGLYSERTYRGLY
13   PROARGALAGLUGLUTYRGLUPHELEUTHR
14   PROVALGLUGLUALAPROLYSGLYMETLEU
15   ALAARGGLYSERTYRSERILELYSSERARG
16   PHETHRASPASPASPLYSTHRASPHISLEU
17   SERTRPGLUTRPASNLEUTHRILELYSLYS
18   ASPTRPLYSASP

Samples:

sample_1: p75NTR DD, [U-99% 13C; U-99% 15N], 0.5 mM; DTT, [U-98% 2H], 1 mM; HEPES, [U-98% 2H], 10 mM; EDTA 1 mM; sodium azide 1 mM; RhoGDI 2 mM

sample_2: RhoGDI, [U-99% 13C; U-99% 15N], 0.5 mM; p75NTR DD 2 mM; DTT, [U-98% 2H], 1 mM; HEPES, [U-98% 2H], 10 mM; EDTA 1 mM; sodium azide 1 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.9; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 13C,15N-filtered NOESYsample_1isotropicsample_conditions_1
4D 13C, 15N-edited NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 13C,15N-filtered NOESYsample_2isotropicsample_conditions_1
4D 13C, 15N-edited NOESYsample_2isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

CYANA, Guntert, Braun and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz

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