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 19404

Title: Solution NMR Structure of DE NOVO DESIGNED Top7 Fold Protein Top7m13, Northeast Structural Genomics Consortium (NESG) Target OR33

Deposition date: 2013-08-02 Original release date: 2013-11-26

Authors: Liu, Gaohua; Zanghellini, Alexandre; Chan, Kui; Xiao, Rong; Janjua, Haleema; Kogan, Sam; Maglaqui, Melissa; Ciccosanti, Colleen; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano

Citation: Liu, Gaohua; Zanghellini, Alexandre; Chan, Kui; Xiao, Rong; Janjua, Haleema; Kogan, Sam; Maglaqui, Melissa; Ciccosanti, Colleen; Acton, Thomas; Kornhaber, Gregory; Everett, John; Baker, David; Montelione, Gaetano. "Solution NMR Structure of DE NOVO DESIGNED Top7 Fold Protein Top7m13, Northeast Structural Genomics Consortium (NESG) Target OR33"  To be published ., .-..

Assembly members:
OR33, polymer, 120 residues, 13888.051 Da.

Natural source:   Common Name: not available   Taxonomy ID: not available   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):
OR33: MSGKKVEVQVKITCNGKTYE RTYQLYAVRDEELKEKLKKV LNERMDPIKKLGCKRVRISI RVKHSDAAEEKKEAKKFAAI LNKVFAELGYNDSNVTWDGD TVTVEGQLEGVDLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts504
15N chemical shifts110
1H chemical shifts826
residual dipolar couplings83

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OR331

Entities:

Entity 1, OR33 120 residues - 13888.051 Da.

1   METSERGLYLYSLYSVALGLUVALGLNVAL
2   LYSILETHRCYSASNGLYLYSTHRTYRGLU
3   ARGTHRTYRGLNLEUTYRALAVALARGASP
4   GLUGLULEULYSGLULYSLEULYSLYSVAL
5   LEUASNGLUARGMETASPPROILELYSLYS
6   LEUGLYCYSLYSARGVALARGILESERILE
7   ARGVALLYSHISSERASPALAALAGLUGLU
8   LYSLYSGLUALALYSLYSPHEALAALAILE
9   LEUASNLYSVALPHEALAGLULEUGLYTYR
10   ASNASPSERASNVALTHRTRPASPGLYASP
11   THRVALTHRVALGLUGLYGLNLEUGLUGLY
12   VALASPLEUGLUHISHISHISHISHISHIS

Samples:

sample_NC: OR33, [U-100% 13C; U-100% 15N], 0.69 mM; NaN3 0.02%; NaCl 100 mM; Tris-HCl 10 mM

sample_NC5: OR33, [U-100% 13C; U-100% 15N], 0.69 mM; NaN3 0.02%; NaCl 100 mM; Tris-HCl 10 mM

sample_NC5_RDC: OR33, [U-100% 13C; U-100% 15N], 0.69 mM; NaN3 0.02%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_NCisotropicsample_conditions_1
2D 1H-13C HSQCsample_NCisotropicsample_conditions_1
3D HNCOsample_NCisotropicsample_conditions_1
3D CBCA(CO)NHsample_NCisotropicsample_conditions_1
3D HNCACBsample_NCisotropicsample_conditions_1
3D 1H-13C arom NOESYsample_NCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_NCisotropicsample_conditions_1
3D HCCH-TOCSYsample_NCisotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_NC5isotropicsample_conditions_1
2D 1H-15N HSQCsample_NC5_RDCisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

REDCAT, Valafar, Prestegard - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB

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