BMRB Entry 34026

Name: NMR solution structure of human FNIII domain 2 of NCAM
Published: 2016-09-09

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PDB ID: 5lkn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34026
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR solution structure of human FNIII domain 2 of NCAM PubMed: 27535221

Deposition date: 2016-07-22 Original release date: 2016-09-09

Authors: Slapsak, U.; Salzano, G.; Amin, L.; Abskharon, R.; Ilc, G.; Zupancic, B.; Biljan, I.; Plavec, J.; Giachin, G.; Legname, G.

Citation: Slapsak, U.; Salzano, G.; Amin, L.; Abskharon, R.; Ilc, G.; Zupancic, B.; Biljan, I.; Plavec, J.; Giachin, G.; Legname, G.. "The N Terminus of the Prion Protein Mediates Functional Interactions with the Neuronal Cell Adhesion Molecule (NCAM) Fibronectin Domain" J. Biol. Chem. 291, 21857-21868 (2016).

Assembly members:
Neural cell adhesion molecule 1, polymer, 103 residues, 11858.316 Da.

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
Neural cell adhesion molecule 1: MQPVREPSAPKLEGQMGEDG NSIKVNLIKQDDGGSPIRHY LVRYRALSSEWKPEIRLPSG SDHVMLKSLDWNAEYEVYVV AENQQGKSKAAHFVFRTHHH HHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	331
15N chemical shifts	101
1H chemical shifts	674

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_1 103 residues - 11858.316 Da.

1

MET

GLN

PRO

VAL

ARG

GLU

PRO

SER

ALA

PRO

2

LYS

LEU

GLU

GLY

GLN

MET

GLY

GLU

ASP

GLY

3

ASN

SER

ILE

LYS

VAL

ASN

LEU

ILE

LYS

GLN

4

ASP

GLY

SER

PRO

ILE

ARG

HIS

TYR

5

LEU

VAL

ARG

TYR

ARG

ALA

LEU

SER

GLU

6

TRP

LYS

PRO

GLU

ILE

ARG

LEU

PRO

SER

GLY

7

SER

ASP

HIS

VAL

MET

LEU

LYS

SER

LEU

ASP

8

TRP

ASN

ALA

GLU

TYR

GLU

VAL

TYR

VAL

9

ALA

GLU

ASN

GLN

GLY

LYS

SER

LYS

ALA

10

ALA

HIS

PHE

VAL

PHE

ARG

THR

HIS

11

HIS

Samples:

sample_1: fibronectin type III domain 2, [U-99% 13C; U-99% 15N], 0.9 mM; D2O, [U-2H], 10%; H2O 90%; TBS 20 mM; sodium chloride 150 mM

sample_conditions_1: ionic strength: 150 mM; pH: 7.45; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

Software:

CARA vv1.8.42, Keller and Wuthrich - chemical shift assignment

CING, Doreleijers JF - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

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

PSVS, Bhattacharya and Montelione - data analysis

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Thornton - data analysis

SPARKY, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMR, Varian - collection

YASARA, Elmar Krieger and Gert Vriend - refinement

NMR spectrometers:

Varian VNMRS 800 MHz

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