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 50972

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50972

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Title: 1H,13C, 15N chemical shift assignment of NTD MaSp1 from Triconephila clavipes   PubMed: 36990448

Deposition date: 2021-06-13 Original release date: 2023-03-02

Authors: Oktaviani, Nur Alia; Malay, Ali; Matsugami, Akimasa; Oktaviani, Fumiaki; Numata, Keiji

Citation: Oktaviani, Nur Alia; Malay, Ali; Matsugami, Akimasa; Hayashi, Fumiaki; Numata, Keiji. "Unusual p Ka Values Mediate the Self-Assembly of Spider Dragline Silk Proteins"  Biomacromolecules 24, 1604-1616 (2023).

Assembly members:
entity_1, polymer, 137 residues, Formula weight is not available

Natural source:   Common Name: Triconephila clavipes   Taxonomy ID: 2585209   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Triconephila clavipes

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):
entity_1: GSHMGQNTPWSSTELADAFI NAFMNEAGRTGAFTADQLDD MSTIGDTIKTAMDKMARSNK SSKGKLQALNMAFASSMAEI AAVEQGGLSVDAKTNAIADS LNSAFYQTTGAANPQFVNEI RSLINMFAQSSANEVSY

Data sets:
Data typeCount
13C chemical shifts527
15N chemical shifts143
1H chemical shifts882

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N-terminal domain of major ampullate spidroin 1 from Triconephila clavipes1

Entities:

Entity 1, N-terminal domain of major ampullate spidroin 1 from Triconephila clavipes 137 residues - Formula weight is not available

1   GLYSERHISMETGLYGLNASNTHRPROTRP
2   SERSERTHRGLULEUALAASPALAPHEILE
3   ASNALAPHEMETASNGLUALAGLYARGTHR
4   GLYALAPHETHRALAASPGLNLEUASPASP
5   METSERTHRILEGLYASPTHRILELYSTHR
6   ALAMETASPLYSMETALAARGSERASNLYS
7   SERSERLYSGLYLYSLEUGLNALALEUASN
8   METALAPHEALASERSERMETALAGLUILE
9   ALAALAVALGLUGLNGLYGLYLEUSERVAL
10   ASPALALYSTHRASNALAILEALAASPSER
11   LEUASNSERALAPHETYRGLNTHRTHRGLY
12   ALAALAASNPROGLNPHEVALASNGLUILE
13   ARGSERLEUILEASNMETPHEALAGLNSER
14   SERALAASNGLUVALSERTYR

Samples:

sample_1: N-terminal domain of major ampullate spidroin 1 from Triconephila clavipes, [U-99% 13C; U-99% 15N], 0.75 mM; DSS 0.1 mM; D2O, [U-99% 2H], 10%; NaCl 300 mM; sodium phosphate 10 mM

sample_conditions_1: ionic strength: 0.3 M; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D (H)C(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D H(C)CH-TOCSYsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
2D HB(CBCG)CD(HD)sample_1isotropicsample_conditions_1
2D HB(CBCGCD)CE(HE)sample_1isotropicsample_conditions_1
3D 15N-separated NOESYsample_1isotropicsample_conditions_1
3D 13C-separated NOESYsample_1isotropicsample_conditions_1
2D HB(CB)CG(HG) asp/glusample_1isotropicsample_conditions_1

Software:

MddNMR - processing non uniform sampling NMR data

NMRPipe - processing NMR data

NMRFAM-SPARKY - chemical shift assignment

MAGRO - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 700 MHz

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