BMRB Entry 51169

Name: Solution NMR resonance assignment of PD-L1
Published: 2022-06-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51169

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 resonance assignment of PD-L1

Deposition date:

2021-11-05

Original release date:

2022-06-08

Authors:

Rizzo, Domenico; Cerofolini, Linda; Giuntini, Stefano; Iozzino, Luisa; Pergola, Carlo; Sacco, Francesca; Palmese, Angelo; Ravera, Enrico; Luchinat, Claudio; Baroni, Fabio; Fragai, Marco

Citation:

Citation: Rizzo, Domenico; Cerofolini, Linda; Giuntini, Stefano; Iozzino, Luisa; Pergola, Carlo; Sacco, Francesca; Palmese, Angelo; Ravera, Enrico; Luchinat, Claudio; Baroni, Fabio; Fragai, Marco. "Epitope Mapping and Binding Assessment by Solid-State NMR Provide a Way for the Development of Biologics under the Quality by Design Paradigm" J. Am. Chem. Soc. 144, 10006-10016 (2022).
PubMed: 35617699

Assembly members:

Assembly members:
entity_1, polymer, 118 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-21a (+) plasmid

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAFTVTVPKDLYVVEYGSNM TIECKFPVEKQLDLAALIVY WEMEDKNIIQFVHGEEDLKV QHSSYRQRARLLKDQLSLGN AALQITDVKLQDAGVYRCMI SYGGADYKRITVKVNAPY

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	323
15N chemical shifts	111
1H chemical shifts	111

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PD-L1	1

Entities:

Entity 1, PD-L1 118 residues - Formula weight is not available

1

MET

ALA

PHE

THR

VAL

THR

VAL

PRO

LYS

ASP

2

LEU

TYR

VAL

GLU

TYR

GLY

SER

ASN

MET

3

THR

ILE

GLU

CYS

LYS

PHE

PRO

VAL

GLU

LYS

4

GLN

LEU

ASP

LEU

ALA

LEU

ILE

VAL

TYR

5

TRP

GLU

MET

GLU

ASP

LYS

ASN

ILE

GLN

6

PHE

VAL

HIS

GLY

GLU

ASP

LEU

LYS

VAL

7

GLN

HIS

SER

TYR

ARG

GLN

ARG

ALA

ARG

8

LEU

LYS

ASP

GLN

LEU

SER

LEU

GLY

ASN

9

ALA

LEU

GLN

ILE

THR

ASP

VAL

LYS

LEU

10

GLN

ASP

ALA

GLY

VAL

TYR

ARG

CYS

MET

ILE

11

SER

TYR

GLY

ALA

ASP

TYR

LYS

ARG

ILE

12

THR

VAL

LYS

VAL

ASN

ALA

PRO

TYR

Samples:

sample_1: PD-L1, [U-100% 13C; U-100% 15N], 150 uM; TRIS 10 mM; NaCl 20 mM; NaN3 0.1%

sample_2: PD-L1, [U-100% 13C; U-100% 15N], 150 uM; HEPES 20 mM; NaCl 20 mM; NaN3 0.1%

sample_3: PD-L1, [U-100% 13C; U-100% 15N], 50 uM; HEPES 100 mM; NaCl 20 mM; NaN3 0.1%

sample_conditions_1: ionic strength: 0.04 M; pH: 8; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.04 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1D 1H	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_2
2D CON	sample_3	isotropic	sample_conditions_2
2D CACO	sample_3	isotropic	sample_conditions_2
2D CBCACO	sample_3	isotropic	sample_conditions_2

Software:

CARA v1.8 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 950 MHz
Bruker AVANCE NEO 700 MHz

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