BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18811

Title: Structural Characterization of Minor Ampullate Spidroin Domains and their Distinct Roles in Fibroin Solubility and Fiber Formation   PubMed: 23418525

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

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).

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts313
15N chemical shifts112
1H chemical shifts678

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Spidroin_11
2Spidroin_21

Entities:

Entity 1, Spidroin_1 107 residues - 10505.787 Da.

1   VALGLYTHRTHRVALALASERTHRTHRSER
2   ARGLEUSERTHRALAGLUALASERSERARG
3   ILESERTHRALAALASERTHRLEUVALSER
4   GLYGLYTYRLEUASNTHRALAALALEUPRO
5   SERVALILEALAASPLEUPHEALAGLNVAL
6   GLYALASERSERPROGLYVALSERASPSER
7   GLUVALLEUILEGLNVALLEULEUGLUILE
8   VALSERSERLEUILEHISILELEUSERSER
9   SERSERVALGLYGLNVALASPPHESERSER
10   VALGLYSERSERALAALAALAVALGLYGLN
11   SERMETGLNVALVALMETGLY

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D MQ-CCH-TOCSYsample_1isotropicsample_conditions_1
4D 13C, 15N-edited NOESYsample_1isotropicsample_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

Related Database Links:

PDB
GB AAC14589 ABC72645