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 30185

Title: NMR structure of apo-PS1   PubMed: 29168496

Deposition date: 2016-09-28 Original release date: 2017-08-03

Authors: Polizzi, N.; Wu, Y.

Citation: Polizzi, Nicholas; Wu, Yibing; Lemmin, Thomas; Maxwell, Alison; Zhang, Shao-Qing; Rawson, Jeff; Beratan, David; Therien, Michael; DeGrado, William. "De novo design of a hyperstable non-natural protein-ligand complex with sub-angstrom accuracy."  Nat. Chem. 9, 1157-1164 (2017).

Assembly members:
PS1, polymer, 109 residues, 12965.262 Da.

Natural source:   Common Name: enterobacteria   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
PS1: SEFEKLRQTGDELVQAFQRL REIFDKGDDDSLEQVLEEIE ELIQKHRQLFDNRQEAADTE AAKQGDQWVQLFQRFREAID KGDKDSLEQLLEELEQALQK IRELAEKKN

Data sets:
Data typeCount
13C chemical shifts363
15N chemical shifts108
1H chemical shifts784

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 109 residues - 12965.262 Da.

1   SERGLUPHEGLULYSLEUARGGLNTHRGLY
2   ASPGLULEUVALGLNALAPHEGLNARGLEU
3   ARGGLUILEPHEASPLYSGLYASPASPASP
4   SERLEUGLUGLNVALLEUGLUGLUILEGLU
5   GLULEUILEGLNLYSHISARGGLNLEUPHE
6   ASPASNARGGLNGLUALAALAASPTHRGLU
7   ALAALALYSGLNGLYASPGLNTRPVALGLN
8   LEUPHEGLNARGPHEARGGLUALAILEASP
9   LYSGLYASPLYSASPSERLEUGLUGLNLEU
10   LEUGLUGLULEUGLUGLNALALEUGLNLYS
11   ILEARGGLULEUALAGLULYSLYSASN

Samples:

sample_1: apo-PS1, [U-100% 13C; U-100% 15N], 780 uM; NaPi 100 mM; NaCl 50 mM; H2O 95%; D2O 5%

sample_2: apo-PS1, U-100% 15N; 10% 13C], 780 uM; NaPi 100 mM; NaCl 50 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CO(CA)NHsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 15N-13Caliphatic-13Caromatic-resolved [1H-1H]-NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D simultaneous NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

XEASY, Bartels et al. - peak picking

NMR spectrometers:

  • Bruker AvanceII 600 MHz

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