BMRB Entry 31022

Title:
Solution NMR structure of 8-residue Rosetta-designed cyclic peptide D8.21 in 50% d6-DMSO and 50% water with cis/trans switching (CC conformation, 50%)
Deposition date:
2022-05-17
Original release date:
2022-09-08
Authors:
Ramelot, T.; Tejero, R.; Montelione, G.
Citation:

Citation: Bhardwaj, G.; O'Connor, J.; Rettie, S.; Huang, Y.; Ramelot, T.; Mulligan, V.; Alpkilic, G.; Palmer, J.; Bera, A.; Bick, M.; Di Piazza, M.; Li, X.; Hosseinzadeh, P.; Craven, T.; Tejero, R.; Lauko, A.; Choi, R.; Glynn, C.; Dong, L.; Griffin, R.; van Voorhis, W.; Rodriguez, J.; Stewart, L.; Montelione, G.; Craik, D.; Baker, D.. "Accurate de novo design of membrane-traversing macrocycles"  Cell 185, 3520-3532 (2022).
PubMed: 36041435

Assembly members:

Assembly members:
entity_1, polymer, 8 residues, 891.190 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 32630   Superkingdom: not available   Kingdom: not available   Genus/species: synthetic construct

Experimental source:

Experimental source:   Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: XXXLXXXL

Data sets:
Data typeCount
13C chemical shifts20
15N chemical shifts2
1H chemical shifts30

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 8 residues - 891.190 Da.

1   DVAMLEDPRLEUDVAMLEDPRLEU

Samples:

sample_1: peptide 6 ± 2 mg/L; TMS 0.03 ± 0.003 %

sample_2: peptide 6 ± 2 mg/L; TMS 0.03 ± 0.003 %

sample_conditions_1: pH: 0.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
1D 1Hsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H COSYsample_2isotropicsample_conditions_1
2D 1H-1H ROESYsample_2isotropicsample_conditions_1
2D 1H-15N SOFASTsample_1isotropicsample_conditions_1
1H-13C HSQC-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
1H-13C HMBCsample_1isotropicsample_conditions_1

Software:

CYANA v3.98.13, Guntert , Mumenthaler, and Wuthrich - refinement, structure calculation

NMRFAM-SPARKY v1.370, Lee, Tonelli, Markley - peak picking

NMRPipe v10.9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PdbStat v5.21.6, modified for non-standard amino acids and cyclic peptide analysis - data analysis

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE II 600 MHz

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