BMRB Entry 27609

Name: Sequence-specific 1H, 13C, and 15N backbone assignment of Fibronectin type III 13
Published: 2018-10-01

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27609

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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:

Sequence-specific 1H, 13C, and 15N backbone assignment of Fibronectin type III 13

Deposition date:

2018-09-13

Original release date:

2018-10-01

Authors:

Zhong, Xueyin; Arnolds, Oliver; Krenczyk, Oktavian; Gajewski, Jana; Puetz, Stefanie; Herrmann, Christian; Stoll, Raphael

Citation:

Citation: Zhong, Xueyin; Arnolds, Oliver; Krenczyk, Oktavian; Gajewski, Jana; Puetz, Stefanie; Herrmann, Christian; Stoll, Raphael. "Structure in solution of fibronectin type III-domain 14 reveals its synergistic heparin binding site" Biochemistry 57, 6045-6049 (2018).
PubMed: 30260627

Assembly members:

Assembly members:
FNIII13, polymer, 111 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: pET-19

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FNIII13: MGHHHHHHAENLYFQGHMLE NVSPPRRARVTDATETTITI SWRTKTETITGFQVDAVPAN GQTPIQRTIKPDVRSYTITG LQPGTDYKIYLYTLNDNARS SPVVIDASTAI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	230
15N chemical shifts	81
1H chemical shifts	84

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FNIII13	1

Entities:

Entity 1, FNIII13 111 residues - Formula weight is not available

1

MET

GLY

HIS

ALA

GLU

2

ASN

LEU

TYR

PHE

GLN

GLY

HIS

MET

LEU

GLU

3

ASN

VAL

SER

PRO

ARG

ALA

ARG

VAL

4

THR

ASP

ALA

THR

GLU

THR

ILE

THR

ILE

5

SER

TRP

ARG

THR

LYS

THR

GLU

THR

ILE

THR

6

GLY

PHE

GLN

VAL

ASP

ALA

VAL

PRO

ALA

ASN

7

GLY

GLN

THR

PRO

ILE

GLN

ARG

THR

ILE

LYS

8

PRO

ASP

VAL

ARG

SER

TYR

THR

ILE

THR

GLY

9

LEU

GLN

PRO

GLY

THR

ASP

TYR

LYS

ILE

TYR

10

LEU

TYR

THR

LEU

ASN

ASP

ASN

ALA

ARG

SER

11

SER

PRO

VAL

ILE

ASP

ALA

SER

THR

ALA

12

ILE

Samples:

sample_1: FNIII13, [U-13C; U-15N], 1 mM; NaCl 137 mM; KCl 2.7 mM; Na2HPO4 10 mM; KH2PO4 1.4 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 0.163 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR, Bruker Biospin, CCPN - chemical shift assignment, processing

NMR spectrometers:

Bruker DRX 600 MHz
Bruker Avance 700 MHz

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