BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 52384

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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/BMR52384
MolProbity Validation Chart

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Title: Chemical shift assignments of a de novo designed 12 stranded transmembrane beta barrel   PubMed: 39024453

Deposition date: 2024-04-02 Original release date: 2024-07-22

Authors: Muntener, Thomas; Hiller, Sebastian

Citation: Berhanu, Samuel; Majumder, Sagardip; Muntener, Thomas; Whitehouse, James; Berner, Carolin; Bera, Asim; Kang, Alex; Liang, Binyong; Khan, G Nasir; Sankaran, Banumathi; Tamm, Lukas; Brockwell, David; Hiller, Sebastian; Radford, Sheena; Baker, David; Vorobieva, Anastassia. "Sculpting conducting nanopore size and shape through de novo protein design"  Science 385, 282-288 (2024).

Assembly members:
entity_1, polymer, 179 residues, Formula weight is not available

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET29b

Entity Sequences (FASTA):
entity_1: QDKPGSAKAGGWTTYNTDNT FKGGSYAKYVLSPNLALKGE YEWNNSSLNSFKAGAEYVAT PYLKTEVMTEYNTDNTFRVT VVTEGRYPVDPNLELFPGGW YTWNNSSLNKGAPYTRAEYK LTPDLKLLSQVVYNTDNTFK FDTGLEYKLSPNLKVKFEYG WNNSSLNEFTVQFEYDLSS

Data sets:
Data typeCount
13C chemical shifts194
15N chemical shifts103
1H chemical shifts181

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1TMB1121

Entities:

Entity 1, TMB112 179 residues - Formula weight is not available

1   GLNASPLYSPROGLYSERALALYSALAGLY
2   GLYTRPTHRTHRTYRASNTHRASPASNTHR
3   PHELYSGLYGLYSERTYRALALYSTYRVAL
4   LEUSERPROASNLEUALALEULYSGLYGLU
5   TYRGLUTRPASNASNSERSERLEUASNSER
6   PHELYSALAGLYALAGLUTYRVALALATHR
7   PROTYRLEULYSTHRGLUVALMETTHRGLU
8   TYRASNTHRASPASNTHRPHEARGVALTHR
9   VALVALTHRGLUGLYARGTYRPROVALASP
10   PROASNLEUGLULEUPHEPROGLYGLYTRP
11   TYRTHRTRPASNASNSERSERLEUASNLYS
12   GLYALAPROTYRTHRARGALAGLUTYRLYS
13   LEUTHRPROASPLEULYSLEULEUSERGLN
14   VALVALTYRASNTHRASPASNTHRPHELYS
15   PHEASPTHRGLYLEUGLUTYRLYSLEUSER
16   PROASNLEULYSVALLYSPHEGLUTYRGLY
17   TRPASNASNSERSERLEUASNGLUPHETHR
18   VALGLNPHEGLUTYRASPLEUSERSER

Samples:

sample_1: TMB12, [U-13C; U-15N; U-2H], 600 uM; D2O 7.5%; sodium phosphate 20 mM; EDTA 1 mM; LDAO 15 mM

sample_2: TMB12, [U-15N; U-2H; 99% 1HD-Ile,Leu; 99% 1HG-Val; 99% Ala; 99% Met], 600 uM; D2O 7.5%; sodium phosphate 20 mM; EDTA 1 mM; LDAO, [U-2H], 15 mM

sample_conditions_1: ionic strength: 20 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1

Software:

CcpNMR v3.2.1 - chemical shift assignment

TOPSPIN v3.6.2 - collection

NMRPipe - processing

NMR spectrometers:

  • Bruker AVANCE NEO 800 MHz
  • Bruker AVANCE III 700 MHz

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