BMRB Entry 30185

Name: NMR structure of apo-PS1
Published: 2017-08-03

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PDB ID: 5tgw
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30185
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of apo-PS1

Deposition date:

2016-09-28

Original release date:

2017-08-03

Authors:

Polizzi, N.; Wu, Y.

Citation:

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).
PubMed: 29168496

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	363
15N chemical shifts	108
1H chemical shifts	784

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 109 residues - 12965.262 Da.

1

SER

GLU

PHE

GLU

LYS

LEU

ARG

GLN

THR

GLY

2

ASP

GLU

LEU

VAL

GLN

ALA

PHE

GLN

ARG

LEU

3

ARG

GLU

ILE

PHE

ASP

LYS

GLY

ASP

4

SER

LEU

GLU

GLN

VAL

LEU

GLU

ILE

GLU

5

GLU

LEU

ILE

GLN

LYS

HIS

ARG

GLN

LEU

PHE

6

ASP

ASN

ARG

GLN

GLU

ALA

ASP

THR

GLU

7

ALA

LYS

GLN

GLY

ASP

GLN

TRP

VAL

GLN

8

LEU

PHE

GLN

ARG

PHE

ARG

GLU

ALA

ILE

ASP

9

LYS

GLY

ASP

LYS

ASP

SER

LEU

GLU

GLN

LEU

10

LEU

GLU

LEU

GLU

GLN

ALA

LEU

GLN

LYS

11

ILE

ARG

GLU

LEU

ALA

GLU

LYS

ASN

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:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CO(CA)NH	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 15N-13Caliphatic-13Caromatic-resolved [1H-1H]-NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D simultaneous NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks