BMRB Entry 27683

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27683
MolProbity Validation Chart

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

Title:
Euprosthenops australis major ampullate spidroin 1 N-terminal domain (NTD) mutant at pH7
Deposition date:
2018-11-06
Original release date:
2019-09-04
Authors:
Goretzki, Benedikt; Heiby, Julia; Hellmich, Ute A.; Neuweiler, Hannes
Citation:

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).
PubMed: 31558722

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts513
15N chemical shifts126
1H chemical shifts827

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NTD1

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   GLYSERGLYASNSERHISTHRTHRPROTRP
2   THRASNPROGLYLEUALAGLUASNPHELEU
3   ASNSERPHELEUGLNGLYLEUSERSERMET
4   PROGLYPHETHRALASERGLNLEUASPASP
5   LEUSERTHRILEALAGLNSERLEUVALGLN
6   SERILEGLNSERLEUALAALAGLNGLYARG
7   THRSERPROASNLYSLEUGLNALALEUASN
8   METALAPHEALASERSERLEUALAGLUILE
9   ALAALASERGLUGLUGLYGLYGLYSERLEU
10   SERTHRLYSTHRSERSERILEALASERALA
11   LEUSERASNALAPHELEUGLNTHRTHRGLY
12   VALVALASNGLNPROPHEILEASNGLUILE
13   THRGLNLEUVALSERMETPHEALAGLNALA
14   GLYMETASNASPVALSERALA

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks