BMRB Entry 34481

Name: Solution NMR structure of the S0_2.126 designed protein
Published: 2020-04-13

Click here to enlarge.

PDB ID: 6xwi
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34481
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution NMR structure of the S0_2.126 designed protein

Deposition date:

2020-01-23

Original release date:

2020-04-13

Authors:

Abriata, L.

Citation:

Citation: Sesterhenn, Fabian; Yang, Che; Bonet, Jaume; Cramer, Johannes; Wen, Xiaolin; Wang, Yimeng; Chiang, Chi-I; Abriata, Luciano; Kucharska, Iga; Castoro, Giacomo; Vollers, Sabrina; Galloux, Marie; Dheilly, Elie; Rosset, Stephane; Corthesy, Patricia; Georgeon, Sandrine; Villard, Melanie; Richard, Charles-Adrien; Descamps, Delphyne; Delgado, Teresa; Oricchio, Elisa; Rameix-Welti, Marie-Anne; Mas, Vicente; Ervin, Sean; Eleouet, Jean-Francois; Riffault, Sabine; Bates, John; Julien, Jean-Philippe; Li, Yuxing; Jardetzky, Theodore; Krey, Thomas; Correia, Bruno. "De novo protein design enables precise induction of RSV neutralizing antibodies" Science 368, .-. (2020).
PubMed: 32409444

Assembly members:

Assembly members:
entity_1, polymer, 71 residues, 8209.471 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: ASPCDKQKNYIDKQLLPIVN KAGCSRPEEVEERIRRALKK MGDTSCFDEILKGLKEIKCG GSWLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	207
15N chemical shifts	61
1H chemical shifts	313

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 71 residues - 8209.471 Da.

1

ALA

SER

PRO

CYS

ASP

LYS

GLN

LYS

ASN

TYR

2

ILE

ASP

LYS

GLN

LEU

PRO

ILE

VAL

ASN

3

LYS

ALA

GLY

CYS

SER

ARG

PRO

GLU

VAL

4

GLU

ARG

ILE

ARG

ALA

LEU

LYS

5

MET

GLY

ASP

THR

SER

CYS

PHE

ASP

GLU

ILE

6

LEU

LYS

GLY

LEU

LYS

GLU

ILE

LYS

CYS

GLY

7

GLY

SER

TRP

LEU

GLU

HIS

8

HIS

Samples:

sample_1: protein 3hb_126543, natural anundance, 500 uM; sodium phosphate, natural anundance, 20 mM

sample_2: protein 3hb_126543, [U-99% 15N], 500 uM; sodium phosphate, natural anundance, 20 mM

sample_3: protein 3hb_126543, [U-99% 13C; U-99% 15N], 400 uM; sodium phosphate, natural anundance, 20 mM

sample_4: protein 3hb_126543, natural anundance, 500 uM; sodium phosphate, natural anundance, 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_3	isotropic	sample_conditions_1
3D HNHA	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
3D HN(CA)CO	sample_3	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_4	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_4	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

UNIO, T. Herrmann - structure calculation

TopSpin, Bruker Biospin - collection

NMR spectrometers:

Bruker AVANCE II 800 MHz

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