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 30574

Title: NMR ensemble of computationally designed protein XAA

Deposition date: 2019-02-16 Original release date: 2020-04-17

Authors: Wei, K.; Moschidi, D.; Nerli, S.; Sgourakis, N.; Baker, D.

Citation: Wei, K.; Moschidi, D.; Bick, M.; Nerli, S.; McShan, A.; Carter, L.; Huang, P.; Fletcher, D.; Sgourakis, N.; Boyken, S.; Baker, D.. "NMR ensemble of computationally designed protein XAA"  . ., .-..

Assembly members:
entity_1, polymer, 98 residues, 11094.648 Da.

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

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

Entity Sequences (FASTA):
entity_1: GSHMGTEDLKYSLERLREIL ERLEENPSEKQIVEAIRAIV ENNAQIVEAIRAIVENNAQI VENNRAIIEALEAIGGGTKI LEEMKKQLKDLKRSLERG

Data sets:
Data typeCount
13C chemical shifts864
15N chemical shifts261
1H chemical shifts558

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21
3entity_1, 31

Entities:

Entity 1, entity_1, 1 98 residues - 11094.648 Da.

1   GLYSERHISMETGLYTHRGLUASPLEULYS
2   TYRSERLEUGLUARGLEUARGGLUILELEU
3   GLUARGLEUGLUGLUASNPROSERGLULYS
4   GLNILEVALGLUALAILEARGALAILEVAL
5   GLUASNASNALAGLNILEVALGLUALAILE
6   ARGALAILEVALGLUASNASNALAGLNILE
7   VALGLUASNASNARGALAILEILEGLUALA
8   LEUGLUALAILEGLYGLYGLYTHRLYSILE
9   LEUGLUGLUMETLYSLYSGLNLEULYSASP
10   LEULYSARGSERLEUGLUARGGLY

Samples:

sample_1: XAA_MAI(LV)proS, U-[15N, 12C, 2H] 13Ce Met 13Cb Ala 13Cd1 Ile 13Cd2 Leu 13Cg2 Val, 440 uM; NaCl 100 mM

sample_2: XAA_ILVstar, U-[15N, 13C, 2H], 500 uM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.2; pressure: 1 atm; temperature: 310.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CM-CMHM NOESYsample_1isotropicsample_conditions_1
3D CM-NHN NOESYsample_1isotropicsample_conditions_1
3D HNHa-CMHM NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1

Software:

Rosetta, Rohl CA, Strauss CE, Misura KM, Baker D - refinement, structure calculation

SPARKY, Goddard - chemical shift assignment, data analysis

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

NMR spectrometers:

  • Bruker Avance III 800 MHz

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