BMRB Entry 27147

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27147

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Title:
1H, 13C and 15N chemical shift assignments for the repetitive domain of E. australis major ampullate spidroin 1
Deposition date:
2017-06-19
Original release date:
2017-11-16
Authors:
Otikovs, Martins; Andersson, Marlene; Jia, Quipin; Nordling, Kerstin; Meng, Qing; Andreas, Loren; Pintacuda, Guido; Johansson, Jan; Rising, Anna; Jaudzems, Kristaps
Citation:

Citation: Otikovs, Martins; Andersson, Marlene; Jia, Qiupin; Nordling, Kerstin; Meng, Qing; Andreas, Loren; Pintacuda, Guido; Johansson, Jan; Rising, Anna; Jaudzems, Kristaps. "Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy."  Angew. Chem. Int. Ed. Engl. 56, 12571-12575 (2017).
PubMed: 28791761

Assembly members:

Assembly members:
NT-2Rep-CT, polymer, 346 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pT7

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NT-2Rep-CT: MGHHHHHHMSHTTPWTNPGL AENFMNSFMQGLSSMPGFTA SQLDDMSTIAQSMVQSIQSL AAQGRTSPNKLQALNMAFAS SMAEIAASEEGGGSLSTKTS SIASAMSNAFLQTTGVVNQP FINEITQLVSMFAQAGMNDV SAGNSGRGQGGYGQGSGGNA AAAAAAAAAAAAAAGQGGQG GYGRQSQGAGSAAAAAAAAA AAAAAGSGQGGYGGQGQGGY GQSGNSVTSGGYGYGTSAAA GAGVAAGSYAGAVNRLSSAE AASRVSSNIAAIASGGASAL PSVISNIYSGVVASGVSSNE ALIQALLELLSALVHVLSSA SIGNVSSVGVDSTLNVVQDS VGQYVG

Data sets:
Data typeCount
13C chemical shifts246
15N chemical shifts92
1H chemical shifts92

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Dimer of NT-2Rep-CT1

Entities:

Entity 1, Dimer of NT-2Rep-CT 346 residues - Formula weight is not available

Residues 145-223 represent the Rep domain.

1   METGLYHISHISHISHISHISHISMETSER
2   HISTHRTHRPROTRPTHRASNPROGLYLEU
3   ALAGLUASNPHEMETASNSERPHEMETGLN
4   GLYLEUSERSERMETPROGLYPHETHRALA
5   SERGLNLEUASPASPMETSERTHRILEALA
6   GLNSERMETVALGLNSERILEGLNSERLEU
7   ALAALAGLNGLYARGTHRSERPROASNLYS
8   LEUGLNALALEUASNMETALAPHEALASER
9   SERMETALAGLUILEALAALASERGLUGLU
10   GLYGLYGLYSERLEUSERTHRLYSTHRSER
11   SERILEALASERALAMETSERASNALAPHE
12   LEUGLNTHRTHRGLYVALVALASNGLNPRO
13   PHEILEASNGLUILETHRGLNLEUVALSER
14   METPHEALAGLNALAGLYMETASNASPVAL
15   SERALAGLYASNSERGLYARGGLYGLNGLY
16   GLYTYRGLYGLNGLYSERGLYGLYASNALA
17   ALAALAALAALAALAALAALAALAALAALA
18   ALAALAALAALAGLYGLNGLYGLYGLNGLY
19   GLYTYRGLYARGGLNSERGLNGLYALAGLY
20   SERALAALAALAALAALAALAALAALAALA
21   ALAALAALAALAALAGLYSERGLYGLNGLY
22   GLYTYRGLYGLYGLNGLYGLNGLYGLYTYR
23   GLYGLNSERGLYASNSERVALTHRSERGLY
24   GLYTYRGLYTYRGLYTHRSERALAALAALA
25   GLYALAGLYVALALAALAGLYSERTYRALA
26   GLYALAVALASNARGLEUSERSERALAGLU
27   ALAALASERARGVALSERSERASNILEALA
28   ALAILEALASERGLYGLYALASERALALEU
29   PROSERVALILESERASNILETYRSERGLY
30   VALVALALASERGLYVALSERSERASNGLU
31   ALALEUILEGLNALALEULEUGLULEULEU
32   SERALALEUVALHISVALLEUSERSERALA
33   SERILEGLYASNVALSERSERVALGLYVAL
34   ASPSERTHRLEUASNVALVALGLNASPSER
35   VALGLYGLNTYRVALGLY

Samples:

sample_1: NT-2Rep-CT, [U-99% 13C; U-99% 15N], 0.4 mM; H2O 95 % v/v; D2O, [U-2H], 5 % v/v; sodium chloride 20 mM; sodium phosphate 20 mM; sodium azide 0.02 % w/v

sample_conditions_1: ionic strength: 0.0585 M; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CA)NHsample_1isotropicsample_conditions_1
3D HN(CO)Nsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1

Software:

CARA v1.9.0, Keller and Wuthrich - chemical shift assignment

TOPSPIN v3.2, Bruker Biospin - collection, processing

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

VNMRJ v2.1b, Varian - collection

NMR spectrometers:

  • Varian INOVA 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