BMRB Entry 25773

Name: 1H, 13C, 15N assignments of Trappin-2
Published: 2016-03-03

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25773

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H, 13C, 15N assignments of Trappin-2

Deposition date:

2015-08-26

Original release date:

2016-03-03

Authors:

LOTH, Karine; Abou Ibrahim Alami, Soha; Habes, Chahrazed; Zani, Marie-Louise; Delmas, Agnes; Moreau, Thierry; Landon, Celine

Citation:

Citation: Loth, Karine; Abou Ibrahim Alami, Soha; Habes, Chahrazed; Zani, Marie-Louise; Delmas, Agnes; Moreau, Thierry; Landon, Celine. "Complete assignment of 15N, 13C Trappin-2 and 1H assignment of its two domains, Elafin and Cementoin." Biomol. NMR Assign. 10, 223-226 (2016).
PubMed: 26878852

Assembly members:

Assembly members:
Trappin-2, polymer, 95 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: Pichia pastoris Vector: pPIC9

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Trappin-2: AVTGVPVKGQDTVKGRVPFN GQDPVKGQVSVKGQDKVKAQ EPVKGPVSTKPGSCPIILIR CAMLNPPNRCLKDTDCPGIK KCCEGSCGMACFVPQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	401
15N chemical shifts	95
1H chemical shifts	652

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Trappin-2	1

Entities:

Entity 1, Trappin-2 95 residues - Formula weight is not available

1

ALA

VAL

THR

GLY

VAL

PRO

VAL

LYS

GLY

GLN

2

ASP

THR

VAL

LYS

GLY

ARG

VAL

PRO

PHE

ASN

3

GLY

GLN

ASP

PRO

VAL

LYS

GLY

GLN

VAL

SER

4

VAL

LYS

GLY

GLN

ASP

LYS

VAL

LYS

ALA

GLN

5

GLU

PRO

VAL

LYS

GLY

PRO

VAL

SER

THR

LYS

6

PRO

GLY

SER

CYS

PRO

ILE

LEU

ILE

ARG

7

CYS

ALA

MET

LEU

ASN

PRO

ASN

ARG

CYS

8

LEU

LYS

ASP

THR

ASP

CYS

PRO

GLY

ILE

LYS

9

LYS

CYS

GLU

GLY

SER

CYS

GLY

MET

ALA

10

CYS

PHE

VAL

PRO

GLN

Samples:

sample_1: Trappin-2, [U-100% 13C; U-100% 15N], 0.3 mM; sodium phosphate 25 mM; sodium chloride 300 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 6.1; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNHAHB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

Ccpnmr, CCPN - chemical shift assignment

NMR spectrometers:

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