BMRB Entry 18968

Name: Diffuse binding of Zn2+ to the denatured ensemble of Cu/Zn superoxide dismutase 1
Published: 2015-07-29

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18968

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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:

Diffuse binding of Zn2+ to the denatured ensemble of Cu/Zn superoxide dismutase 1

Deposition date:

2013-01-22

Original release date:

2015-07-29

Authors:

Szpryngiel, Scarlett; Oliveberg, Mikael; Maler, Lena

Citation:

Citation: Szpryngiel, Scarlett; Oliveberg, Mikael; Maler, Lena. "Diffuse binding of Zn2+ to the denatured ensemble of Cu/Zn superoxide dismutase 1" .

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: pSOD1

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	299
15N chemical shifts	148
1H chemical shifts	146

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SOD1	1

Entities:

Entity 1, SOD1 153 residues - Formula weight is not available

SOD1

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

ASP

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], 0.2-0.5 mM; D2O, [U-99% 2H], 10%; urea 9 M; bis-Tris 10 mM; H2O 90%

sample_conditions_1: ionic strength: 10 mM; 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1
3D CANCO	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

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 600 MHz

BMRB	15711 15712 15713 15714 18509 18708 26570 4202
PDB	1BA9 1DSW 1FUN 1HL4 1HL5 1KMG 1L3N 1MFM 1N18 1N19 1PTZ 1PU0 1RK7 1SOS 1SPD 2AF2 2C9S 2C9U 2C9V 2GBT 2GBU 2GBV 2LU5 2V0A 2XJK 2XJL 3ECU 3HFF 3KH3 3KH4 3RE0 3T5W 4B3E 4BCY 4FF9 4OH2
DBJ	BAA14373 BAC20345 BAG35052 BAG73767
EMBL	CAA26182 CAG29351 CAG46542
GB	AAA72747 AAA80237 AAB05661 AAD42179 AAH01034
REF	NP_000445 NP_001009025 XP_003813274 XP_008976454
SP	P00441 P60052
AlphaFold	P00441 P60052