BMRB Entry 27668

Name: Backbone 1H and 15N Chemical Shift Assignments for bovine BLG A at pH 2.65, 3.2, and 4.0
Published: 2018-11-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27668

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:

Backbone 1H and 15N Chemical Shift Assignments for bovine BLG A at pH 2.65, 3.2, and 4.0

Deposition date:

2018-10-30

Original release date:

2018-11-14

Authors:

Birch, Johnny; Nielsen, Lau; Stender, Emil; Svensson, Birte; Kragelund, Birthe

Citation:

Citation: Stender, Emil; Birch, Johnny; Kjeldsen, Christian; Nielsen, Lau; Duus, Jens; Kragelund, Birthe; Svensson, Birte. "Alginate Trisaccharide Binding Sites on the Surface of beta-Lactoglobulin Identified by NMR Spectroscopy: Implications for Molecular Network Formation" ACS Omega 4, 6165-6174 (2019).
PubMed: 31459761

Assembly members:

Assembly members:
BLG_A, polymer, 162 residues, Formula weight is not available

Natural source:

Natural source: Common Name: cow Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Pichia pastoris Vector: pPICZ A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BLG_A: AYVTQTMKGLDIQKVAGTWY SLAMAASDISLLDAQSAPLR VYVEELKPTPEGDLEILLQK WENDECAQKKIIAEKTKIPA VFKIDALNENKVLVLDTDYK KYLLFCMENSAEPEQSLVCQ CLVRTPEVDDEALEKFDKAL KALPMHIRLSFNPTQLEEQC HI

Data sets:

assigned_chemical_shifts

Data type	Count
15N chemical shifts	419
1H chemical shifts	419

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BLG A	1

Entities:

Entity 1, BLG A 162 residues - Formula weight is not available

1

ALA

TYR

VAL

THR

GLN

THR

MET

LYS

GLY

LEU

2

ASP

ILE

GLN

LYS

VAL

ALA

GLY

THR

TRP

TYR

3

SER

LEU

ALA

MET

ALA

SER

ASP

ILE

SER

4

LEU

ASP

ALA

GLN

SER

ALA

PRO

LEU

ARG

5

VAL

TYR

VAL

GLU

LEU

LYS

PRO

THR

PRO

6

GLU

GLY

ASP

LEU

GLU

ILE

LEU

GLN

LYS

7

TRP

GLU

ASN

ASP

GLU

CYS

ALA

GLN

LYS

8

ILE

ALA

GLU

LYS

THR

LYS

ILE

PRO

ALA

9

VAL

PHE

LYS

ILE

ASP

ALA

LEU

ASN

GLU

ASN

10

LYS

VAL

LEU

VAL

LEU

ASP

THR

ASP

TYR

LYS

11

LYS

TYR

LEU

PHE

CYS

MET

GLU

ASN

SER

12

ALA

GLU

PRO

GLU

GLN

SER

LEU

VAL

CYS

GLN

13

CYS

LEU

VAL

ARG

THR

PRO

GLU

VAL

ASP

14

GLU

ALA

LEU

GLU

LYS

PHE

ASP

LYS

ALA

LEU

15

LYS

ALA

LEU

PRO

MET

HIS

ILE

ARG

LEU

SER

16

PHE

ASN

PRO

THR

GLN

LEU

GLU

GLN

CYS

17

HIS

ILE

Samples:

sample_1: BLG A dimer, [1H, 15N], 400 uM; potassium phosphate 50 mM; ammonium sulfate, [U-99% 15N], 1%; DSS 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 2.65; pressure: 1 atm; temperature: 273 K

sample_conditions_2: ionic strength: 50 mM; pH: 3.2; pressure: 1 atm; temperature: 273 K

sample_conditions_3: ionic strength: 50 mM; pH: 4.0; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_2
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_3

Software:

TOPSPIN, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz