BMRB Entry 52448

Name: Streptococcal Protein G antibody-binding domain C2 - variant 3
Published: 2024-09-26

Click here to enlarge.

PDB ID: 9fa8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52448
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:

Streptococcal Protein G antibody-binding domain C2 - variant 3

Deposition date:

2024-05-08

Original release date:

2024-09-26

Authors:

Mushtaq, Ameeq Ul; Nagy, Tamas Milan; Wolf-Watz, Magnus

Citation:

Citation: Jonsson, Malin; Mushtaq, Ameeq Ul; Nagy, Tamas Milan; von Witting, Emma; Lofblom, John; Nam, Kwangho; Wolf-Watz, Magnus; Hober, Sophia. "Cooperative Folding as a Molecular Switch in an Evolved Antibody Binder" J. Biol. Chem. 300, 107795-107795 (2024).
PubMed: 39305954

Assembly members:

Assembly members:
entity_1, polymer, 65 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pBad2.2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: HTTYKLVINGKTLKGETTTE PPDTNRDGRVDYKDAEKVFK QYANDNGVDGEWTYDDATKT FTVTE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	177
15N chemical shifts	60
1H chemical shifts	124

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C2 variant3	1

Entities:

Entity 1, C2 variant3 65 residues - Formula weight is not available

1

HIS

THR

TYR

LYS

LEU

VAL

ILE

ASN

GLY

2

LYS

THR

LEU

LYS

GLY

GLU

THR

GLU

3

PRO

ASP

THR

ASN

ARG

ASP

GLY

ARG

VAL

4

ASP

TYR

LYS

ASP

ALA

GLU

LYS

VAL

PHE

LYS

5

GLN

TYR

ALA

ASN

ASP

ASN

GLY

VAL

ASP

GLY

6

GLU

TRP

THR

TYR

ASP

ALA

THR

LYS

THR

7

PHE

THR

VAL

THR

GLU

Samples:

sample_1: C2 variant3, [U-100% 13C; U-100% 15N], 0.55 mM; MES 30 mM; calcium chloride 3 mM

sample_conditions_1: pH: 6; temperature: 293 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMR spectrometers:

Bruker Avance 850 MHz

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