BMRB Entry 30394

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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/BMR30394
MolProbity Validation Chart

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Title:
Solution structure of a phosphate-loop protein
Deposition date:
2018-01-09
Original release date:
2018-11-13
Authors:
Yang, F.; Yang, W.; Lin, Y.; Romero Romero, M.; Tawfik, D.; Baker, D.; Varani, G.
Citation:

Citation: Romero Romero, Maria Luisa; Yang, Fan; Lin, Yu-Ru; Toth-Petroczy, Agnes; Berezovsky, Igor; Goncearenco, Alexander; Yang, Wen; Wellner, Alon; Kumar-Deshmukh, Fanindra; Sharon, Michal; Baker, David; Varani, Gabriele; Tawfik, Dan. "Simple yet functional phosphate-loop proteins."  Proc. Natl. Acad. Sci. U.S.A. 115, E11943-E11950 (2018).
PubMed: 30504143

Assembly members:

Assembly members:
entity_1, polymer, 115 residues, 12501.373 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: MRVIVVIVGPSGAGKTTLDE LARKAKEEVPDAEIRTVTTK EDAKRVAEEAERRNADIVVI VGPSGSGKSTLAKIVKKIIA RAGAKTIEVTTEEELRKAVA KARGSWSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts461
15N chemical shifts113
1H chemical shifts701

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 115 residues - 12501.373 Da.

1   METARGVALILEVALVALILEVALGLYPRO
2   SERGLYALAGLYLYSTHRTHRLEUASPGLU
3   LEUALAARGLYSALALYSGLUGLUVALPRO
4   ASPALAGLUILEARGTHRVALTHRTHRLYS
5   GLUASPALALYSARGVALALAGLUGLUALA
6   GLUARGARGASNALAASPILEVALVALILE
7   VALGLYPROSERGLYSERGLYLYSSERTHR
8   LEUALALYSILEVALLYSLYSILEILEALA
9   ARGALAGLYALALYSTHRILEGLUVALTHR
10   THRGLUGLUGLULEUARGLYSALAVALALA
11   LYSALAARGGLYSERTRPSERLEUGLUHIS
12   HISHISHISHISHIS

Samples:

sample_1: protein, [U-13C; U-15N], 2.0 mM; sodium phosphate 10 mM; sodium chloride 50 mM

sample_2: protein, [U-100% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 50 mM

sample_3: protein, [U-13C; U-15N], 2 mM; sodium phosphate 10 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

AMBER, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

TOPSPIN, Bruker Biospin - collection

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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