BMRB Entry 15714

Name: Backbone chemical shift assignements for monomeric apoSOD1 - variant D90A
Published: 2009-10-01

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15714

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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:

Backbone chemical shift assignements for monomeric apoSOD1 - variant D90A

Deposition date:

2008-04-03

Original release date:

2009-10-01

Authors:

Teilum, Kaare; Akke, Mikael

Citation:

Citation: Teilum, Kaare; Smith, Melanie; Schulz, Eike; Christensen, Lea; Solomentsev, Gleb; Oliveberg, Mikael; Akke, Mikael. "Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization." Proc. Natl. Acad. Sci. U.S.A. 106, 18273-18278 (2009).
PubMed: 19828437

Assembly members:

Assembly members:
SOD1, polymer, 153 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: N/A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SOD1: ATKAVAVLKGDGPVQGIINF EQKESNGPVKVWGSIKGLTE GLHGFHVHEEEDNTAGCTSA GPHFNPLSRKHGGPKDEERH VGDLGNVTAAKDGVADVSIE DSVISLSGDHAIIGRTLVVH EKADDLGKGGNEESTKTGNA GSRLACGVIGIAQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	154
15N chemical shifts	146
1H chemical shifts	146

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	chain 1, proline cis conformer	1
2	chain 2, proline trans conformer	1

Entities:

Entity 1, chain 1, proline cis conformer 153 residues - Formula weight is not available

1

ALA

THR

LYS

ALA

VAL

ALA

VAL

LEU

LYS

GLY

2

ASP

GLY

PRO

VAL

GLN

GLY

ILE

ASN

PHE

3

GLU

GLN

LYS

GLU

SER

ASN

GLY

PRO

VAL

LYS

4

VAL

TRP

GLY

SER

ILE

LYS

GLY

LEU

THR

GLU

5

GLY

LEU

HIS

GLY

PHE

HIS

VAL

HIS

GLU

6

GLU

ASP

ASN

THR

ALA

GLY

CYS

THR

SER

ALA

7

GLY

PRO

HIS

PHE

ASN

PRO

LEU

SER

ARG

LYS

8

HIS

GLY

PRO

LYS

ASP

GLU

ARG

HIS

9

VAL

GLY

ASP

LEU

GLY

ASN

VAL

THR

ALA

10

LYS

ASP

GLY

VAL

ALA

ASP

VAL

SER

ILE

GLU

11

ASP

SER

VAL

ILE

SER

LEU

SER

GLY

ASP

HIS

12

ALA

ILE

GLY

ARG

THR

LEU

VAL

HIS

13

GLU

LYS

ALA

ASP

LEU

GLY

LYS

GLY

14

ASN

GLU

SER

THR

LYS

THR

GLY

ASN

ALA

15

GLY

SER

ARG

LEU

ALA

CYS

GLY

VAL

ILE

GLY

16

ILE

ALA

GLN

Samples:

sample_1: SOD1, [U-100% 13C; U-100% 15N], 1 mM; MES 10 mM; EDTA 1 mM; D2O 10%

sample_conditions_1: ionic strength: 0.01 M; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	15711 15712 15713 18509 18708 18968 26570 4202
PDB	1BA9 1DSW 1KMG 1L3N 1MFM 1N18 1RK7 1SOS 2AF2 2GBT 2LU5 2XJK 2XJL 4BCY
GB	AAA72747 AAA80237