BMRB Entry 25942

Name: Full-length WT SOD1 in DPC MICELLE
Published: 2016-12-08

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PDB ID: 2nam
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25942
MolProbity Validation Chart

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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:

Full-length WT SOD1 in DPC MICELLE

Deposition date:

2016-01-06

Original release date:

2016-12-08

Authors:

Lim, Liangzhong; Song, Jianxing

Citation:

Citation: Lim, Liangzhong; Song, Jianxing. "SALS-linked WT-SOD1 adopts a highly similar helical conformation as FALS-causing L126Z-SOD1 in a membrane environment" Biochim. Biophys. Acta 1858, 2223-2230 (2016).
PubMed: 27378311

Assembly members:

Assembly members:
entity, polymer, 161 residues, 15827.688 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MGHHHHHHATKAVCVLKGDG PVQGIINFEQKESNGPVKVW GSIKGLTEGLHGFHVHEFGD NTAGCTSAGPHFNPLSRKHG GPKDEERHVGDLGNVTADKD GVADVSIEDSVISLSGDHCI IGRTLVVHEKADDLGKGGNE ESTKTGNAGSRLACGVIGIA Q

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	279
15N chemical shifts	158
1H chemical shifts	721

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 161 residues - 15827.688 Da.

Residue 1-8 are the non-native affinity 6xHis-tag of full-length SOD1

1

MET

GLY

HIS

ALA

THR

2

LYS

ALA

VAL

CYS

VAL

LEU

LYS

GLY

ASP

GLY

3

PRO

VAL

GLN

GLY

ILE

ASN

PHE

GLU

GLN

4

LYS

GLU

SER

ASN

GLY

PRO

VAL

LYS

VAL

TRP

5

GLY

SER

ILE

LYS

GLY

LEU

THR

GLU

GLY

LEU

6

HIS

GLY

PHE

HIS

VAL

HIS

GLU

PHE

GLY

ASP

7

ASN

THR

ALA

GLY

CYS

THR

SER

ALA

GLY

PRO

8

HIS

PHE

ASN

PRO

LEU

SER

ARG

LYS

HIS

GLY

9

GLY

PRO

LYS

ASP

GLU

ARG

HIS

VAL

GLY

10

ASP

LEU

GLY

ASN

VAL

THR

ALA

ASP

LYS

ASP

11

GLY

VAL

ALA

ASP

VAL

SER

ILE

GLU

ASP

SER

12

VAL

ILE

SER

LEU

SER

GLY

ASP

HIS

CYS

ILE

13

ILE

GLY

ARG

THR

LEU

VAL

HIS

GLU

LYS

14

ALA

ASP

LEU

GLY

LYS

GLY

ASN

GLU

15

GLU

SER

THR

LYS

THR

GLY

ASN

ALA

GLY

SER

16

ARG

LEU

ALA

CYS

GLY

VAL

ILE

GLY

ILE

ALA

17

GLN

Samples:

sample_1: DPC 20 mM; entity, [U-13C; U-15N], 0.4 mM

sample_conditions_1: ionic strength: 0 M; pH: 4; pressure: 1 atm; temperature: 313 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	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
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

Gromacs v4.5.3, David van der Spoel, and Erik Lindahl - refinement

Cyana v2, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 800 MHz

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