BMRB Entry 18811

Name: Structural Characterization of Minor Ampullate Spidroin Domains and their Distinct Roles in Fibroin Solubility and Fiber Formation
Published: 2013-02-21

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PDB ID: 2m0m
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18811
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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:

Structural Characterization of Minor Ampullate Spidroin Domains and their Distinct Roles in Fibroin Solubility and Fiber Formation

Deposition date:

2012-10-30

Original release date:

2013-02-21

Authors:

Yang, Daiwen; Gao, Zhenwei; Lin, Zhi; Huang, Weidong; Lai, Chong Cheong; Fan, Jing-song

Citation:

Citation: Gao, Zhenwei; Lin, Zhi; Huang, Weidong; Lai, Chong Cheong; Fan, Jing-Song; Yang, Daiwen. "Structural characterization of minor ampullate spidroin domains and their distinct roles in fibroin solubility and fiber formation." PLoS ONE 8, e56142-e56142 (2013).
PubMed: 23418525

Assembly members:

Assembly members:
Spidroin, polymer, 107 residues, 10505.787 Da.

Natural source:

Natural source: Common Name: Spiders Taxonomy ID: 171624 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Nephila antipodiana

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-32a derived

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Spidroin: VGTTVASTTSRLSTAEASSR ISTAASTLVSGGYLNTAALP SVIADLFAQVGASSPGVSDS EVLIQVLLEIVSSLIHILSS SSVGQVDFSSVGSSAAAVGQ SMQVVMG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	313
15N chemical shifts	112
1H chemical shifts	678

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Spidroin_1	1
2	Spidroin_2	1

Entities:

Entity 1, Spidroin_1 107 residues - 10505.787 Da.

1

VAL

GLY

THR

VAL

ALA

SER

THR

SER

2

ARG

LEU

SER

THR

ALA

GLU

ALA

SER

ARG

3

ILE

SER

THR

ALA

SER

THR

LEU

VAL

SER

4

GLY

TYR

LEU

ASN

THR

ALA

LEU

PRO

5

SER

VAL

ILE

ALA

ASP

LEU

PHE

ALA

GLN

VAL

6

GLY

ALA

SER

PRO

GLY

VAL

SER

ASP

SER

7

GLU

VAL

LEU

ILE

GLN

VAL

LEU

GLU

ILE

8

VAL

SER

LEU

ILE

HIS

ILE

LEU

SER

9

SER

VAL

GLY

GLN

VAL

ASP

PHE

SER

10

VAL

GLY

SER

ALA

VAL

GLY

GLN

11

SER

MET

GLN

VAL

MET

GLY

Samples:

sample_1: CTD, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM; sodium azide 0.01%; EDTA 5 mM; sodium chloride 50 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.06 M; pH: 6.8; pressure: 1 atm; temperature: 307 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D MQ-CCH-TOCSY	sample_1	isotropic	sample_conditions_1
4D 13C, 15N-edited NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TALOS, Cornilescu, Delaglio and Bax - processing

NMRspy, Daiwen Yang, Yu Zheng - chemical shift assignment, NOE assignment, peak picking

NMR spectrometers:

Bruker Avance 800 MHz

PDB	2M0M
GB	AAC14589 ABC72645