BMRB Entry 30231

Name: Solution structure of the oxidized iron-sulfur protein adrenodoxin from Encephalitozoon cuniculi. Seattle Structural Genomics Center for Infectious Disease target EncuA.00705.a
Published: 2017-01-26

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PDB ID: 5uj5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30231
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:

Solution structure of the oxidized iron-sulfur protein adrenodoxin from Encephalitozoon cuniculi. Seattle Structural Genomics Center for Infectious Disease target EncuA.00705.a

Deposition date:

2017-01-17

Original release date:

2017-01-26

Authors:

Buchko, G.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID

Citation:

Citation: Shaheen, Shareef; Barrett, Kayleigh; Subramanian, Sandhya; Arnold, Samuel; Laureanti, Joseph; Myler, Peter; Van Voorhis, Wesley; Buchko, Garry. "Solution structure of the oxidized iron-sulfur protein andrenodoxin from Encephalitozoon cuniculi." Protein Sci. 29, 809-817 (2020).
PubMed: 31912584

Assembly members:

Assembly members:
entity_1, polymer, 132 residues, 14377.485 Da.
entity_FES, non-polymer, 175.820 Da.

Natural source:

Natural source: Common Name: Microsporidian parasite Taxonomy ID: 6035 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Encephalitozoon cuniculi

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: AVA0421

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPGSMDMFSAPDRIPEQIRI FFKTMKQVVPAKAVCGSTVL DVAHKNGVDLEGACEGNLAC STCHVILEEPLYRKLGEPSD KEYDLIDQAFGATGTSRLGC QLRVDKSFENAVFTVPRATK NMAVDGFKPKPH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	443
15N chemical shifts	107
1H chemical shifts	591

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	2

Entities:

Entity 1, entity_1 132 residues - 14377.485 Da.

1

GLY

PRO

GLY

SER

MET

ASP

MET

PHE

SER

ALA

2

PRO

ASP

ARG

ILE

PRO

GLU

GLN

ILE

ARG

ILE

3

PHE

LYS

THR

MET

LYS

GLN

VAL

PRO

4

ALA

LYS

ALA

VAL

CYS

GLY

SER

THR

VAL

LEU

5

ASP

VAL

ALA

HIS

LYS

ASN

GLY

VAL

ASP

LEU

6

GLU

GLY

ALA

CYS

GLU

GLY

ASN

LEU

ALA

CYS

7

SER

THR

CYS

HIS

VAL

ILE

LEU

GLU

PRO

8

LEU

TYR

ARG

LYS

LEU

GLY

GLU

PRO

SER

ASP

9

LYS

GLU

TYR

ASP

LEU

ILE

ASP

GLN

ALA

PHE

10

GLY

ALA

THR

GLY

THR

SER

ARG

LEU

GLY

CYS

11

GLN

LEU

ARG

VAL

ASP

LYS

SER

PHE

GLU

ASN

12

ALA

VAL

PHE

THR

VAL

PRO

ARG

ALA

THR

LYS

13

ASN

MET

ALA

VAL

ASP

GLY

PHE

LYS

PRO

LYS

14

PRO

HIS

Entity 2, entity_2 - Fe2 S2 - 175.820 Da.

1

FES

Samples:

sample_1: DTT 1 ± 0.1 mM; E5, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM; TRIS 20 ± 0.2 mM; sodium chloride 100 ± 2 mM

sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aliphatic	sample_1	anisotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	anisotropic	sample_conditions_1
3D HNCACB	sample_1	anisotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	anisotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	anisotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	anisotropic	sample_conditions_1
3D HNCO	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	anisotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	anisotropic	sample_conditions_1
deuterium exchange	sample_1	anisotropic	sample_conditions_1
3D C(CO)NH	sample_1	anisotropic	sample_conditions_1
3D H(CCO)NH	sample_1	anisotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	anisotropic	sample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation

Felix v2007, Accelrys Software Inc. - processing

PSVS v1.5, Bhattacharya and Montelione - data analysis

SPARKY v3.115, Goddard - data analysis, peak picking

NMR spectrometers:

Varian INOVA 600 MHz
Varian VXRS 750 MHz

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