BMRB Entry 26740

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26740

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Title:
1H, 13C, and 15N Chemical Shift Assignments for C-terminal intrinsically disordered cytosolic fragment of ErbB2
Deposition date:
2016-02-02
Original release date:
2018-06-27
Authors:
Van Heijenoort, Carine; Wang, Ying Hui; Guerlesquin, Francoise; Badache, Ali; Lescop, Ewen; Assrir, Nadine; Pinet, Louise
Citation:

Citation: Wang, YingHui; Pinet, Louise; Assrir, Nadine; Elantak, Latifa; Guerlesquin, Francoise; Badache, Ali; Lescop, Ewen; van Heijenoort, Carine. "."  Biomol. NMR Assign. 12, 23-26 (2018).
PubMed: 28905237

Assembly members:

Assembly members:
Cterbb2, polymer, 272 residues, 28711.5 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: YP304

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Cterbb2: GSHMVIQNEDLGPASPLDST FYRSLLEDDDMGDLVDAEEY LVPQQGFFCPDPAPGAGGMV HHRHRSSSTRSGGGDLTLGL EPSEEEAPRSPLAPSEGAGS DVFDGDLGMGAAKGLQSLPT HDPSPLQRYSEDPTVPLPSE TDGYVAPLTCSPQPEYVNQP DVRPQPPSPREGPLPAARPA GATLERPKTLSPGKNGVVKD VFAFGGAVENPEYLTPQGGA APQPHPPPAFSPAFDNLYYW DQDPPERGAPPSTFKGTPTA ENPEYLGLDVPV

Data sets:
Data typeCount
13C chemical shifts994
15N chemical shifts267
1H chemical shifts1433

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CtErbB21

Entities:

Entity 1, CtErbB2 272 residues - 28711.5 Da.

Residues 1-4 represent a non-native affinity tag

1   GLYSERHISMETVALILEGLNASNGLUASP
2   LEUGLYPROALASERPROLEUASPSERTHR
3   PHETYRARGSERLEULEUGLUASPASPASP
4   METGLYASPLEUVALASPALAGLUGLUTYR
5   LEUVALPROGLNGLNGLYPHEPHECYSPRO
6   ASPPROALAPROGLYALAGLYGLYMETVAL
7   HISHISARGHISARGSERSERSERTHRARG
8   SERGLYGLYGLYASPLEUTHRLEUGLYLEU
9   GLUPROSERGLUGLUGLUALAPROARGSER
10   PROLEUALAPROSERGLUGLYALAGLYSER
11   ASPVALPHEASPGLYASPLEUGLYMETGLY
12   ALAALALYSGLYLEUGLNSERLEUPROTHR
13   HISASPPROSERPROLEUGLNARGTYRSER
14   GLUASPPROTHRVALPROLEUPROSERGLU
15   THRASPGLYTYRVALALAPROLEUTHRCYS
16   SERPROGLNPROGLUTYRVALASNGLNPRO
17   ASPVALARGPROGLNPROPROSERPROARG
18   GLUGLYPROLEUPROALAALAARGPROALA
19   GLYALATHRLEUGLUARGPROLYSTHRLEU
20   SERPROGLYLYSASNGLYVALVALLYSASP
21   VALPHEALAPHEGLYGLYALAVALGLUASN
22   PROGLUTYRLEUTHRPROGLNGLYGLYALA
23   ALAPROGLNPROHISPROPROPROALAPHE
24   SERPROALAPHEASPASNLEUTYRTYRTRP
25   ASPGLNASPPROPROGLUARGGLYALAPRO
26   PROSERTHRPHELYSGLYTHRPROTHRALA
27   GLUASNPROGLUTYRLEUGLYLEUASPVAL
28   PROVAL

Samples:

sample_1: Cterbb2, [U-100% 13C; U-100% 15N], 325 uM; TCEP 2 mM; MES 40 mM; sodium chloride 200 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 5.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCANHsample_1isotropicsample_conditions_1
3D HN(CO)CANHsample_1isotropicsample_conditions_1
3D HCANsample_1isotropicsample_conditions_1
3D HACA(CO)Nsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3.1, Bruker Biospin - processing

CCPNMR v2.4, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 950 MHz

Related Database Links:

UNP P04626
AlphaFold X5D2V5

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