BMRB Entry 50592

Name: Slow disulfide bridge formation in the folded CH2 domain
Published: 2021-06-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50592

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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: Slow disulfide bridge formation in the folded CH2 domain PubMed: 34107549

Deposition date: 2020-11-22 Original release date: 2021-06-30

Authors: Ishima, Rieko; Persons, John; Xi, Zhaoyong

Citation: Xi, Zhaoyong; Liu, Xianglei; Lin, Rui; Persons, John; Ilina, Tatiana; Li, Wei; Dimitrov, Dimiter; Ishima, Rieko. "The reduced form of the antibody CH2 domain." Protein Sci. 30, 1895-1903 (2021).

Assembly members:
entity_1, polymer, 106 residues, Formula weight is not available

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

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):
entity_1: SGGPSVFLFPPKPKDTLMIS RTPEVTCVVVDVSHEDPEVK FNWYVDGVEVHNAKTKPREE QYNSTYRVVSVLTVLHQDWL NGKEYKCKVSNKALPAPIEK TISKAK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	176
15N chemical shifts	85
1H chemical shifts	85

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CH2	1

Entities:

Entity 1, CH2 106 residues - Formula weight is not available

1

SER

GLY

PRO

SER

VAL

PHE

LEU

PHE

PRO

2

PRO

LYS

PRO

LYS

ASP

THR

LEU

MET

ILE

SER

3

ARG

THR

PRO

GLU

VAL

THR

CYS

VAL

4

ASP

VAL

SER

HIS

GLU

ASP

PRO

GLU

VAL

LYS

5

PHE

ASN

TRP

TYR

VAL

ASP

GLY

VAL

GLU

VAL

6

HIS

ASN

ALA

LYS

THR

LYS

PRO

ARG

GLU

7

GLN

TYR

ASN

SER

THR

TYR

ARG

VAL

SER

8

VAL

LEU

THR

VAL

LEU

HIS

GLN

ASP

TRP

LEU

9

ASN

GLY

LYS

GLU

TYR

LYS

CYS

LYS

VAL

SER

10

ASN

LYS

ALA

LEU

PRO

ALA

PRO

ILE

GLU

LYS

11

THR

ILE

SER

LYS

ALA

LYS

Samples:

sample_1: CH2, [U-99% 13C; U-99% 15N], 0.25 mM; sodium phosphate 25 mM; sodium chloride 100 mM; sodium azide 0.02%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

ANALYSIS v2.4.2 - chemical shift assignment, data analysis

NMRPipe - processing

TOPSPIN - collection

NMRDraw - processing

NMR spectrometers:

Bruker Avance 900 MHz

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