BMRB Entry 34515

Name: NMR solution structure of unbound recombinant human Nerve Growth Factor (rhNGF)
Published: 2021-05-07

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PDB ID: 6yw8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34515
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:

NMR solution structure of unbound recombinant human Nerve Growth Factor (rhNGF)

Deposition date:

2020-04-29

Original release date:

2021-05-07

Authors:

Golic Grdadolnik, S.; Paoletti, F.

Citation:

Citation: Paoletti, Francesca; Merzel, Franci; Cassetta, Alberto; Ogris, Iza; Covaceuszach, Sonia; Grdadolnik, Joze; Lamba, Doriano; Golic Grdadolnik, Simona. "Endogenous modulators of neurotrophin signaling: Landscape of the transient ATP-NGF interactions" Comput. Struct. Biotechnol. J. 19, 2938-2949 (2021).
PubMed: 34136093

Assembly members:

Assembly members:
entity_1, polymer, 118 residues, 13287.139 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SSSHPIFHRGEFSVCDSVSV WVGDKTTATDIKGKEVMVLG EVNINNSVFKQYFFETKCRD PNPVDSGCRGIDSKHWNSYC TTTHTFVKALTMDGKQAAWR FIRIDTACVCVLSRKAVR

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	658
15N chemical shifts	228
1H chemical shifts	1530

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	1

Entities:

Entity 1, unit_1 118 residues - 13287.139 Da.

1

SER

HIS

PRO

ILE

PHE

HIS

ARG

GLY

2

GLU

PHE

SER

VAL

CYS

ASP

SER

VAL

SER

VAL

3

TRP

VAL

GLY

ASP

LYS

THR

ALA

THR

ASP

4

ILE

LYS

GLY

LYS

GLU

VAL

MET

VAL

LEU

GLY

5

GLU

VAL

ASN

ILE

ASN

SER

VAL

PHE

LYS

6

GLN

TYR

PHE

GLU

THR

LYS

CYS

ARG

ASP

7

PRO

ASN

PRO

VAL

ASP

SER

GLY

CYS

ARG

GLY

8

ILE

ASP

SER

LYS

HIS

TRP

ASN

SER

TYR

CYS

9

THR

HIS

THR

PHE

VAL

LYS

ALA

LEU

10

THR

MET

ASP

GLY

LYS

GLN

ALA

TRP

ARG

11

PHE

ILE

ARG

ILE

ASP

THR

ALA

CYS

VAL

CYS

12

VAL

LEU

SER

ARG

LYS

ALA

VAL

ARG

Samples:

sample_1: Nerve Growth Factor, [U-99% 15N], 0.1 mM; HEPES 50 mM

sample_2: Nerve Growth Factor, [U-99% 13C; U-99% 15N], 0.1 mM; HEPES 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1

Software:

ARIA v2.3.2, Rieping W., Habeck M., Bardiaux B., Bernard A., Malliavin T.E., Nilges M. - refinement, structure calculation

CARA, Keller and Wuthrich - data analysis, peak picking

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

NMR spectrometers:

Agilent VNMRS 800 MHz

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