BMRB Entry 34423

Name: NMR structure of MLP124017
Published: 2019-12-13

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34423

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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: NMR structure of MLP124017 PubMed: 31792250

Deposition date: 2019-08-05 Original release date: 2019-12-13

Authors: Barthe, P.; de Guillen, K.; Padilla, A.; Hecker, A.

Citation: de Guillen, K.; Lorrain, C.; Tsan, P.; Barthe, P.; Petre, B.; Saveleva, N.; Rouhier, N.; Duplessis, S.; Padilla, A.; Hecker, A.. "Structural genomics applied to the rust fungus Melampsora larici-populina reveals two candidate effector proteins adopting cystine knot and NTF2-like protein folds." Sci. Rep. 9, 18084-18084 (2019).

Assembly members:
entity_1, polymer, 157 residues, 18200.594 Da.

Natural source: Common Name: Poplar leaf rust fungus Taxonomy ID: 203908 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Melampsora larici-populina

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

Entity Sequences (FASTA):
entity_1: MELPESFEFILTEDMVTDLD VKGLGYDFIDLVTKSPDSVN SEHELAHFLGPHDPEIYVNG KIQTTTAFLQFFRQGLFKKL KDAEFAINVSGKVKEGEGYK LVWKSAAQRSHDQKIRWDEA EAYIWRRKDGSCWLHSVKFI MSKAAPYVAIDHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	344
15N chemical shifts	127
1H chemical shifts	852

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 157 residues - 18200.594 Da.

1

MET

GLU

LEU

PRO

GLU

SER

PHE

GLU

PHE

ILE

2

LEU

THR

GLU

ASP

MET

VAL

THR

ASP

LEU

ASP

3

VAL

LYS

GLY

LEU

GLY

TYR

ASP

PHE

ILE

ASP

4

LEU

VAL

THR

LYS

SER

PRO

ASP

SER

VAL

ASN

5

SER

GLU

HIS

GLU

LEU

ALA

HIS

PHE

LEU

GLY

6

PRO

HIS

ASP

PRO

GLU

ILE

TYR

VAL

ASN

GLY

7

LYS

ILE

GLN

THR

ALA

PHE

LEU

GLN

8

PHE

ARG

GLN

GLY

LEU

PHE

LYS

LEU

9

LYS

ASP

ALA

GLU

PHE

ALA

ILE

ASN

VAL

SER

10

GLY

LYS

VAL

LYS

GLU

GLY

GLU

GLY

TYR

LYS

11

LEU

VAL

TRP

LYS

SER

ALA

GLN

ARG

SER

12

HIS

ASP

GLN

LYS

ILE

ARG

TRP

ASP

GLU

ALA

13

GLU

ALA

TYR

ILE

TRP

ARG

LYS

ASP

GLY

14

SER

CYS

TRP

LEU

HIS

SER

VAL

LYS

PHE

ILE

15

MET

SER

LYS

ALA

PRO

TYR

VAL

ALA

ILE

16

ASP

HIS

Samples:

sample_1: MLP124017, [U-15N], 1 mM

sample_2: MLP124017, [U-13C; U-15N], 0.6 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCACO	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CINDY, Padilla - chemical shift assignment

Gifa, Delsuc - peak picking

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker AVANCE III 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts