BMRB Entry 30128

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30128
MolProbity Validation Chart

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Title:
Solution NMR Structure of Denovo Beta Sheet Design Protein, Northeast Structural Genomics Consortium (NESG) Target OR664
Deposition date:
2016-07-03
Original release date:
2016-09-16
Authors:
Tang, Yuefeng; Liu, G.; Montelione, G.; Northeast Structural Genomics Consortium (NESG), NESG
Citation:

Citation: Marcos, Enrique; Basanta, Benjamin; Chidyausiku, Tamuka; Tang, Yuefeng; Oberdorfer, Gustav; Liu, Gaohua; Swapna, G.; Guan, Rongjin; Silva, Daniel-Adriano; Dou, Jiayi; Pereira, Jose Henrique; Xiao, Rong; Sankaran, Banumathi; Zwart, Peter; Montelione, Gaetano; Baker, David. "Principles for designing proteins with cavities formed by curved beta sheets"  Science 355, 201-206 (2017).
PubMed: 28082595

Assembly members:

Assembly members:
entity_1, polymer, 120 residues, 13593.999 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQDIVEAAKQAAIAIFQLWK NPTDPEAQELLNKILSPDVL DQVREHARELQKQGIHFEVK RVEVTTDGNTVNVTVELEET TGGTTTNTTYELRFEVDGDT IRRVTVTQNGGSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts384
15N chemical shifts121
1H chemical shifts804

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 120 residues - 13593.999 Da.

1   METGLNASPILEVALGLUALAALALYSGLN
2   ALAALAILEALAILEPHEGLNLEUTRPLYS
3   ASNPROTHRASPPROGLUALAGLNGLULEU
4   LEUASNLYSILELEUSERPROASPVALLEU
5   ASPGLNVALARGGLUHISALAARGGLULEU
6   GLNLYSGLNGLYILEHISPHEGLUVALLYS
7   ARGVALGLUVALTHRTHRASPGLYASNTHR
8   VALASNVALTHRVALGLULEUGLUGLUTHR
9   THRGLYGLYTHRTHRTHRASNTHRTHRTYR
10   GLULEUARGPHEGLUVALASPGLYASPTHR
11   ILEARGARGVALTHRVALTHRGLNASNGLY
12   GLYSERLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: OR664, [U-99% 13C; U-99% 15N], 1.27 ± 0.1 mM; NaCl 137 mM; KCl 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.8 mM

sample_conditions_1: ionic strength: 140 mM; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOCACBsample_1isotropicsample_conditions_1
3D SIMUTANEOUS 13C-AROMATIC,13C- ALIPHATIC,15N EDITED 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

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

AutoStructure, Huang, Tejero, Powers and Montelione - structure calculation

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

XEASY, Bartels et al. - peak picking

NMR spectrometers:

  • Bruker AVENCE 800 MHz

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