BMRB Entry 25710

Name: Structure of high-density lipoprotein particles
Published: 2016-12-15

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PDB ID: 2n5e
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25710
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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: Structure of high-density lipoprotein particles PubMed: 28024148

Deposition date: 2015-07-15 Original release date: 2016-12-15

Authors: Bibow, Stefan; Polyhach, Yevhen; Eichmann, Cedric; Chi, Celestine; Kowal, Julia; Stahlberg, Henning; Jeschke, Gunnar; Guentert, Peter; Riek, Roland

Citation: Bibow, Stefan; Polyhach, Yevhen; Eichmann, Cedric; Chi, Celestine; Kowal, Julia; Albiez, Stefan; McLeod, Robert; Stahlberg, Henning; Jeschke, Gunnar; Guntert, Peter; Riek, Roland. "Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I" Nat. Struct. Mol. Biol. 24, 187-193 (2017).

Assembly members:
entity, polymer, 167 residues, 19462.148 Da.

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

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

Entity Sequences (FASTA):
entity: STFSKLREQLGPVTQEFWDN LEKETEGLRQEMSKDLEEVK AKVQPYLDDFQKKWQEEMEL YRQKVEPLGEEMRDRARAHV DALRTHLAPYSDELRQRLAA RLEALKENGGARLAEYHAKA TEHLSTLSEKAKPALEDLRQ GLLPVLESFKVSFLSALEEY TKKLNTQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	391
15N chemical shifts	149
1H chemical shifts	149

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	1

Entities:

Entity 1, entity_1 167 residues - 19462.148 Da.

1

SER

THR

PHE

SER

LYS

LEU

ARG

GLU

GLN

LEU

2

GLY

PRO

VAL

THR

GLN

GLU

PHE

TRP

ASP

ASN

3

LEU

GLU

LYS

GLU

THR

GLU

GLY

LEU

ARG

GLN

4

GLU

MET

SER

LYS

ASP

LEU

GLU

VAL

LYS

5

ALA

LYS

VAL

GLN

PRO

TYR

LEU

ASP

PHE

6

GLN

LYS

TRP

GLN

GLU

MET

GLU

LEU

7

TYR

ARG

GLN

LYS

VAL

GLU

PRO

LEU

GLY

GLU

8

GLU

MET

ARG

ASP

ARG

ALA

ARG

ALA

HIS

VAL

9

ASP

ALA

LEU

ARG

THR

HIS

LEU

ALA

PRO

TYR

10

SER

ASP

GLU

LEU

ARG

GLN

ARG

LEU

ALA

11

ARG

LEU

GLU

ALA

LEU

LYS

GLU

ASN

GLY

12

ALA

ARG

LEU

ALA

GLU

TYR

HIS

ALA

LYS

ALA

13

THR

GLU

HIS

LEU

SER

THR

LEU

SER

GLU

LYS

14

ALA

LYS

PRO

ALA

LEU

GLU

ASP

LEU

ARG

GLN

15

GLY

LEU

PRO

VAL

LEU

GLU

SER

PHE

LYS

16

VAL

SER

PHE

LEU

SER

ALA

LEU

GLU

TYR

17

THR

LYS

LEU

ASN

THR

GLN

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 0.75 mM; entity, stereospecific Methyl-labeling, 1 mM; entity, selective unlabeling, 1 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 316 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

Cyana, Guntert, Braun and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 700 MHz
Bruker Avance 600 MHz

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