BMRB Entry 27683

Name: Euprosthenops australis major ampullate spidroin 1 N-terminal domain (NTD) mutant at pH7
Published: 2019-09-04

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27683

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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: Euprosthenops australis major ampullate spidroin 1 N-terminal domain (NTD) mutant at pH7 PubMed: 31558722

Deposition date: 2018-11-06 Original release date: 2019-09-04

Authors: Goretzki, Benedikt; Heiby, Julia; Hellmich, Ute A.; Neuweiler, Hannes

Citation: Heiby, Julia; Goretzki, Benedikt; Johnson, Christopher; Hellmich, Ute; Neuweiler, Hannes. "Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk" Nat. Commun. 10, 4378-4378 (2019).

Assembly members:
MaSp1_L6-NTD, polymer, 137 residues, 14071.6 Da.

Natural source: Common Name: Euprosthenops australis Taxonomy ID: 332052 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Euprosthenops australis

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

Entity Sequences (FASTA):
MaSp1_L6-NTD: GSGNSHTTPWTNPGLAENFL NSFLQGLSSMPGFTASQLDD LSTIAQSLVQSIQSLAAQGR TSPNKLQALNMAFASSLAEI AASEEGGGSLSTKTSSIASA LSNAFLQTTGVVNQPFINEI TQLVSMFAQAGMNDVSA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	513
15N chemical shifts	126
1H chemical shifts	827

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NTD	1

Entities:

Entity 1, NTD 137 residues - 14071.6 Da.

The first two amino acids in the protein sequence (GS) are remains of a thrombin cleavage site.

1

GLY

SER

GLY

ASN

SER

HIS

THR

PRO

TRP

2

THR

ASN

PRO

GLY

LEU

ALA

GLU

ASN

PHE

LEU

3

ASN

SER

PHE

LEU

GLN

GLY

LEU

SER

MET

4

PRO

GLY

PHE

THR

ALA

SER

GLN

LEU

ASP

5

LEU

SER

THR

ILE

ALA

GLN

SER

LEU

VAL

GLN

6

SER

ILE

GLN

SER

LEU

ALA

GLN

GLY

ARG

7

THR

SER

PRO

ASN

LYS

LEU

GLN

ALA

LEU

ASN

8

MET

ALA

PHE

ALA

SER

LEU

ALA

GLU

ILE

9

ALA

SER

GLU

GLY

SER

LEU

10

SER

THR

LYS

THR

SER

ILE

ALA

SER

ALA

11

LEU

SER

ASN

ALA

PHE

LEU

GLN

THR

GLY

12

VAL

ASN

GLN

PRO

PHE

ILE

ASN

GLU

ILE

13

THR

GLN

LEU

VAL

SER

MET

PHE

ALA

GLN

ALA

14

GLY

MET

ASN

ASP

VAL

SER

ALA

Samples:

sample_1: MaSp1 L6-NTD, [U-13C; U-15N], 300 uM; potassium phosphate 20 mM; sodium chloride 200 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 7.0; pressure: 1.0 atm; temperature: 298 K

Experiments:

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

Software:

CCPNMR v2.4.2, CCPN - chemical shift assignment, peak picking

TOPSPIN v3.2, Bruker - processing

CARA_NMR, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts