BMRB Entry 27610

Name: Sequence-specific 1H, 13C, and 15N backbone assignment of Fibronectin type III 14
Published: 2018-10-01

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PDB ID: 6hnf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27610
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:

Sequence-specific 1H, 13C, and 15N backbone assignment of Fibronectin type III 14

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:
FNIII14, polymer, 91 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):
FNIII14: GHMDAPSNLRFLATTPNSLL VSWQPPRARITGYIIKYEKP GSPPREVVPRPRPGVTEATI TGLEPGTEYTIYVIALKNNQ KSEPLIGRKKT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	389
15N chemical shifts	80
1H chemical shifts	624

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	FNIII14	1

Entities:

Entity 1, FNIII14 91 residues - Formula weight is not available

1

GLY

HIS

MET

ASP

ALA

PRO

SER

ASN

LEU

ARG

2

PHE

LEU

ALA

THR

PRO

ASN

SER

LEU

3

VAL

SER

TRP

GLN

PRO

ARG

ALA

ARG

ILE

4

THR

GLY

TYR

ILE

LYS

TYR

GLU

LYS

PRO

5

GLY

SER

PRO

ARG

GLU

VAL

PRO

ARG

6

PRO

ARG

PRO

GLY

VAL

THR

GLU

ALA

THR

ILE

7

THR

GLY

LEU

GLU

PRO

GLY

THR

GLU

TYR

THR

8

ILE

TYR

VAL

ILE

ALA

LEU

LYS

ASN

GLN

9

LYS

SER

GLU

PRO

LEU

ILE

GLY

ARG

LYS

10

THR

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
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 27610

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: