BMRB Entry 25634

Name: Fusion to a Highly Stable Consensus Albumin Binding Domain Allows for Tunable Pharmacokinetics
Published: 2015-08-31

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PDB ID: 2n35
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25634
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Fusion to a Highly Stable Consensus Albumin Binding Domain Allows for Tunable Pharmacokinetics PubMed: 26275855

Deposition date: 2015-05-21 Original release date: 2015-08-31

Authors: Gibbs, Alan; Jacobs, Steven

Citation: Jacobs, Steven; Gibbs, Alan; Conk, Michelle; Yi, Fang; Maguire, Diane; O'Neil, Karyn. "Fusion to a highly stable consensus albumin binding domain allows for tunable pharmacokinetics" Protein Eng. Des. Sel. 28, 385-393 (2015).

Assembly members:
ABD, polymer, 52 residues, 5863.789 Da.

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

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

Entity Sequences (FASTA):
ABD: GTIDEWLLKEAKEKAIEELK KAGITSDYYFDLINKAKTVE GVNALKDEILKA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1

Data type	Count
13C chemical shifts	214
15N chemical shifts	53
1H chemical shifts	375

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ABD	1

Entities:

Entity 1, ABD 52 residues - 5863.789 Da.

1

GLY

THR

ILE

ASP

GLU

TRP

LEU

LYS

GLU

2

ALA

LYS

GLU

LYS

ALA

ILE

GLU

LEU

LYS

3

LYS

ALA

GLY

ILE

THR

SER

ASP

TYR

PHE

4

ASP

LEU

ILE

ASN

LYS

ALA

LYS

THR

VAL

GLU

5

GLY

VAL

ASN

ALA

LEU

LYS

ASP

GLU

ILE

LEU

6

LYS

ALA

Samples:

sample_1: ABD, [U-100% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 90%

sample_2: ABD, [U-10% 13C; U-100% 15N], 0.8 mM; H2O 90%; D2O 90%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CS-Rosetta, Yang Shen, Oliver Lange, Frank Delaglio, et al. - refinement

NMR spectrometers:

Bruker Avance 500 MHz
Varian INOVA 600 MHz
Bruker Avance 800 MHz

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