BMRB Entry 17131

Name: NMR resonance assignment of the N-terminal domain of Latrodectus hesperus (black widow) major ampullate spider silk fibroin 1
Published: 2010-11-10

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17131

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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:

NMR resonance assignment of the N-terminal domain of Latrodectus hesperus (black widow) major ampullate spider silk fibroin 1

Deposition date:

2010-08-16

Original release date:

2010-11-10

Authors:

Kessler, Horst; Hagn, Franz

Citation:

Citation: Hagn, Franz; Thamm, Christopher; Scheibel, Thomas; Kessler, Horst. "pH-dependent dimerization and salt-dependent stabilization of the N-terminal domain of spider dragline silk--implications for fiber formation." Angew. Chem. Int. Ed. Engl. 50, 310-313 (2011).

Assembly members:

Assembly members:
N1, polymer, 132 residues, Formula weight is not available

Natural source:

Natural source: Common Name: black widow spider Taxonomy ID: 256737 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Latrodectus hesperus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N1: MGQANTPWSSKANADAFINS FISAASNTGSFSQDQMEDMS LIGNTLMAAMDNMGGRITPS KLQALDMAFASSVAEIAASE GGDLGVTTNAIADALTSAFY QTTGVVNSRFISEIRSLIGM FAQASANDVYAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	458
15N chemical shifts	131
1H chemical shifts	496

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N1	1

Entities:

Entity 1, N1 132 residues - Formula weight is not available

1

MET

GLY

GLN

ALA

ASN

THR

PRO

TRP

SER

2

LYS

ALA

ASN

ALA

ASP

ALA

PHE

ILE

ASN

SER

3

PHE

ILE

SER

ALA

SER

ASN

THR

GLY

SER

4

PHE

SER

GLN

ASP

GLN

MET

GLU

ASP

MET

SER

5

LEU

ILE

GLY

ASN

THR

LEU

MET

ALA

MET

6

ASP

ASN

MET

GLY

ARG

ILE

THR

PRO

SER

7

LYS

LEU

GLN

ALA

LEU

ASP

MET

ALA

PHE

ALA

8

SER

VAL

ALA

GLU

ILE

ALA

SER

GLU

9

GLY

ASP

LEU

GLY

VAL

THR

ASN

ALA

10

ILE

ALA

ASP

ALA

LEU

THR

SER

ALA

PHE

TYR

11

GLN

THR

GLY

VAL

ASN

SER

ARG

PHE

12

ILE

SER

GLU

ILE

ARG

SER

LEU

ILE

GLY

MET

13

PHE

ALA

GLN

ALA

SER

ALA

ASN

ASP

VAL

TYR

14

ALA

SER

Samples:

sample_1: sodium phosphate 10 mM; sodium chloride 300 mM; H2O 95%; D2O 5%; N1, [U-99% 13C; U-99% 15N], 0.85 mM

sample_conditions_1: ionic strength: 0.32 M; pH: 7.2; 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	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection, processing

SPARKY v3.115, Goddard - chemical shift assignment, data analysis

PASTA v1.1, Kessler and Gemmercker - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz