BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 30802

Title: Solution NMR Structure of DE NOVO DESIGNED Rossmann 3x3 Fold Protein r3x3_bp3, Northeast Structural Genomics Consortium (NESG) Target OR689

Deposition date: 2020-10-02 Original release date: 2021-05-14

Authors: Liu, G.; Montelione, G.; Northeast Structural Genomics Consortium (NESG), NESG

Citation: Koga, N.; Koga, R.; Liu, G.; Castellanos, J.; Montelione, G.; Baker, D.. "Role of backbone strain in de novo design of complex alpha/beta protein structures Accurate de novo design of asymetric alpha/beta proteins with ten or more secondary structure elements requires consideration of backbone strain Design principle proposed from designed larger alpha/beta-proteins not folded as designed: Consistency between local, non-local, and global structures"  .

Assembly members:
entity_1, polymer, 135 residues, 15823.438 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: MRIIVIIVTDEQKIEDMWEI LKEIGVDRIVIITSNKQLAE RAKELGVDRIFLLTDDELIA EIVKKLGADIVFSENRDIAK KIIRKLKNIIILSNDEQLVK ELQKEASDARVFNVQTKQDF KDLIEKILEHHHHHH

Data sets:
Data typeCount
13C chemical shifts467
15N chemical shifts126
1H chemical shifts1021

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 135 residues - 15823.438 Da.

1   METARGILEILEVALILEILEVALTHRASP
2   GLUGLNLYSILEGLUASPMETTRPGLUILE
3   LEULYSGLUILEGLYVALASPARGILEVAL
4   ILEILETHRSERASNLYSGLNLEUALAGLU
5   ARGALALYSGLULEUGLYVALASPARGILE
6   PHELEULEUTHRASPASPGLULEUILEALA
7   GLUILEVALLYSLYSLEUGLYALAASPILE
8   VALPHESERGLUASNARGASPILEALALYS
9   LYSILEILEARGLYSLEULYSASNILEILE
10   ILELEUSERASNASPGLUGLNLEUVALLYS
11   GLULEUGLNLYSGLUALASERASPALAARG
12   VALPHEASNVALGLNTHRLYSGLNASPPHE
13   LYSASPLEUILEGLULYSILELEUGLUHIS
14   HISHISHISHISHIS

Samples:

sample_1: OR689, [U-100% 13C; U-100% 15N], 0.6 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; 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 HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D SIMUTANEOUS 1H, 15N, 13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

XEASY, Bartels et al. - peak picking

ASDP, Huang, Montelione - structure calculation

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