BMRB Entry 50320

Name: ABD3
Published: 2020-07-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50320

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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:

ABD3

Deposition date:

2020-06-10

Original release date:

2020-07-09

Authors:

Wang, Conan

Citation:

Citation: Wang, Conan; Amiss, Anna; Weidmann, Joachim; Craik, David. "Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery" J. Biol. Chem. 295, 12143-12152 (2020).
PubMed: 32647013

Assembly members:

Assembly members:
entity_1, polymer, 17 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: TVEEVNALKNEILKAHA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
1H chemical shifts	17

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ABD3 monomer	1

Entities:

Entity 1, ABD3 monomer 17 residues - Formula weight is not available

1

THR

VAL

GLU

VAL

ASN

ALA

LEU

LYS

ASN

2

GLU

ILE

LEU

LYS

ALA

HIS

ALA

Samples:

sample_1: ABD3 0.75 mM

sample_conditions_1: ionic strength: 0 M; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis - chemical shift assignment

NMR spectrometers:

Bruker ARX 500 MHz