BMRB Entry 17465

Name: Structural Characterisation of Apoflavodoxin shows that the Location of the Stable Nucleus Differs Among Proteins with a Flavodoxin-like Topology
Published: 2016-06-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17465

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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:

Structural Characterisation of Apoflavodoxin shows that the Location of the Stable Nucleus Differs Among Proteins with a Flavodoxin-like Topology

Deposition date:

2011-02-11

Original release date:

2016-06-09

Authors:

Steensma, Elles; van Mierlo, Carlo

Citation:

Citation: Steensma, Elles; van Mierlo, Carlo. "Structural Characterisation of Apoflavodoxin shows that the Location of the Stable Nucleus Differs Among Proteins with a Flavodoxin-like Topology" J. Mol. Biol. 282, 653-666 (1998).

Assembly members:

Assembly members:
aII, polymer, 179 residues, Formula weight is not available

Natural source:

Natural source: Common Name: A. vinelandii Taxonomy ID: 354 Superkingdom: Bacteria Kingdom: not available Genus/species: Azotobacter vinelandii

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
aII: AKIGLFFGSNTGKTRKVAKS IKKRFDDETMSDALNVNRVS AEDFAQYQFLILGTPTLGEG ELPGLSSDAENESWEEFLPK IEGLDFSGKTVALFGLGDQV GYPENYLDALGELYSFFKDR GAKIVGSWSTDGYEFESSEA VVDGKFVGLALDLDNQSGKT DERVAAWLAQIAPEFGLSL

Data sets:

chemical_rates
- Chemical_rate_list

Data type

Count

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	aII	1

Entities:

Entity 1, aII 179 residues - Formula weight is not available

1

ALA

LYS

ILE

GLY

LEU

PHE

GLY

SER

ASN

2

THR

GLY

LYS

THR

ARG

LYS

VAL

ALA

LYS

SER

3

ILE

LYS

ARG

PHE

ASP

GLU

THR

MET

4

SER

ASP

ALA

LEU

ASN

VAL

ASN

ARG

VAL

SER

5

ALA

GLU

ASP

PHE

ALA

GLN

TYR

GLN

PHE

LEU

6

ILE

LEU

GLY

THR

PRO

THR

LEU

GLY

GLU

GLY

7

GLU

LEU

PRO

GLY

LEU

SER

ASP

ALA

GLU

8

ASN

GLU

SER

TRP

GLU

PHE

LEU

PRO

LYS

9

ILE

GLU

GLY

LEU

ASP

PHE

SER

GLY

LYS

THR

10

VAL

ALA

LEU

PHE

GLY

LEU

GLY

ASP

GLN

VAL

11

GLY

TYR

PRO

GLU

ASN

TYR

LEU

ASP

ALA

LEU

12

GLY

GLU

LEU

TYR

SER

PHE

LYS

ASP

ARG

13

GLY

ALA

LYS

ILE

VAL

GLY

SER

TRP

SER

THR

14

ASP

GLY

TYR

GLU

PHE

GLU

SER

GLU

ALA

15

VAL

ASP

GLY

LYS

PHE

VAL

GLY

LEU

ALA

16

LEU

ASP

LEU

ASP

ASN

GLN

SER

GLY

LYS

THR

17

ASP

GLU

ARG

VAL

ALA

TRP

LEU

ALA

GLN

18

ILE

ALA

PRO

GLU

PHE

GLY

LEU

SER

LEU

Samples:

sample_1: aII, [U-15N], 2 mM; potassium pyrophosphate 150 mM; D2O 100%

sample_conditions_1: pH*: 6.2; pressure: 1 atm; temperature: 303 K

Experiments:

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

Software:

FELIX v2.5, Accelrys Software Inc. - processing

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker AMX 500 MHz