BMRB Entry 26929

Name: 1H and 15N resonance assignment of the first fibronectin type III module of the neural cell adhesion molecule (NCAM FN1)
Published: 2017-04-26

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26929

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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:

1H and 15N resonance assignment of the first fibronectin type III module of the neural cell adhesion molecule (NCAM FN1)

Deposition date:

2016-10-28

Original release date:

2017-04-26

Authors:

Bhide, Gaurang; Prehna, Gerd; Ramirez, Benjamin; Colley, Karen

Citation:

Citation: Bhide, Gaurang; Prehna, Gerd; Ramirez, Benjamin; Colley, Karen. "The Polybasic Region of the Polysialyltransferase ST8Sia-IV Binds Directly to the Neural Cell Adhesion Molecule, NCAM" Biochemistry 56, 1504-1517 (2017).
PubMed: 28233978

Assembly members:

Assembly members:
NCAM_FN1, polymer, 127 residues, Formula weight is not available

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 Vector: pET14(b)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NCAM_FN1: MGSSHHHHHHSSGLVPRGSH MQADTPSSPSIDQVEPYSST AQVQFDEPEATGGVPILKYK AEWRAVGEEVWHSKWYDAKE ASMEGIVTIVGLKPETTYAV RLAALNGKGLGEISAASEFK TQPVQGE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	308
15N chemical shifts	98
1H chemical shifts	98

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NCAM FN1	1

Entities:

Entity 1, NCAM FN1 127 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

GLN

ALA

ASP

THR

PRO

SER

PRO

SER

4

ILE

ASP

GLN

VAL

GLU

PRO

TYR

SER

THR

5

ALA

GLN

VAL

GLN

PHE

ASP

GLU

PRO

GLU

ALA

6

THR

GLY

VAL

PRO

ILE

LEU

LYS

TYR

LYS

7

ALA

GLU

TRP

ARG

ALA

VAL

GLY

GLU

VAL

8

TRP

HIS

SER

LYS

TRP

TYR

ASP

ALA

LYS

GLU

9

ALA

SER

MET

GLU

GLY

ILE

VAL

THR

ILE

VAL

10

GLY

LEU

LYS

PRO

GLU

THR

TYR

ALA

VAL

11

ARG

LEU

ALA

LEU

ASN

GLY

LYS

GLY

LEU

12

GLY

GLU

ILE

SER

ALA

SER

GLU

PHE

LYS

13

THR

GLN

PRO

VAL

GLN

GLY

GLU

Samples:

sample_1: NCAM FN1, [U-99% 13C; U-99% 15N], 500 mM; potassium phosphate 20 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.3 M; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1

Software:

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

TOPSPIN, Bruker Biospin - collection

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

Bruker DRX 600 MHz

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