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 51687

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51687

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Title: Backbone and CB chemical shifts of HPy1 repetitive unit from Argiope argentata   PubMed: 36802452

Deposition date: 2022-11-05 Original release date: 2023-03-14

Authors: Simmons, Jeffrey; Rainey, Jan

Citation: Simmons, Jeffrey; Gasmi-Seabrook, Genevieve; Rainey, Jan. "Structural Features, Intrinsic Disorder, and Modularity of a Pyriform Spidroin 1 Core Repetitive Domain"  Biochem. Cell Biol. 101, 271-283 (2023).

Assembly members:
entity_1, polymer, 243 residues, 24509.6595 Da.

Natural source:   Common Name: Argiope argentata   Taxonomy ID: 233271   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Argiope argentata

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET32

Entity Sequences (FASTA):
entity_1: MGHHHHHHSSAQENSFTQSS VAQQSAVAQQSSVSQQSSAA QQSSVAQSQQTSYSAATNAG SSVSQSQAIVSSAPVYFNSQ TLTNNLASSLQSLNALNYVS NGQLSSSDVASTVARAVAQS LGLSQGSVQNIMSQQLSSIG SGASTSSLSQAIANAVSSAV QGSQAAAPGQEQSIAQRVNS AISSAFAQLISQRTAPAPAP RPRPAPLPAPAPRPRPAPAP RPAPVYAPAPVASQFQASAS SQS

Data sets:
Data typeCount
13C chemical shifts569
15N chemical shifts190
1H chemical shifts185

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HPy1 v21

Entities:

Entity 1, HPy1 v2 243 residues - 24509.6595 Da.

1   METGLYHISHISHISHISHISHISSERSER
2   ALAGLNGLUASNSERPHETHRGLNSERSER
3   VALALAGLNGLNSERALAVALALAGLNGLN
4   SERSERVALSERGLNGLNSERSERALAALA
5   GLNGLNSERSERVALALAGLNSERGLNGLN
6   THRSERTYRSERALAALATHRASNALAGLY
7   SERSERVALSERGLNSERGLNALAILEVAL
8   SERSERALAPROVALTYRPHEASNSERGLN
9   THRLEUTHRASNASNLEUALASERSERLEU
10   GLNSERLEUASNALALEUASNTYRVALSER
11   ASNGLYGLNLEUSERSERSERASPVALALA
12   SERTHRVALALAARGALAVALALAGLNSER
13   LEUGLYLEUSERGLNGLYSERVALGLNASN
14   ILEMETSERGLNGLNLEUSERSERILEGLY
15   SERGLYALASERTHRSERSERLEUSERGLN
16   ALAILEALAASNALAVALSERSERALAVAL
17   GLNGLYSERGLNALAALAALAPROGLYGLN
18   GLUGLNSERILEALAGLNARGVALASNSER
19   ALAILESERSERALAPHEALAGLNLEUILE
20   SERGLNARGTHRALAPROALAPROALAPRO
21   ARGPROARGPROALAPROLEUPROALAPRO
22   ALAPROARGPROARGPROALAPROALAPRO
23   ARGPROALAPROVALTYRALAPROALAPRO
24   VALALASERGLNPHEGLNALASERALASER
25   SERGLNSER

Samples:

sample_1: 1 mM DSS 1.0 mM; 1 mM NaN3 1.0 mM; HPy1_v2, [U-100% 13C; U-100% 15N], 0.5 mM

sample_conditions_1: ionic strength: 0.050 M; pH: 6.000; pressure: 1.000 atm; temperature: 313.150 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
HNcaCO (HNcaCO)sample_1isotropicsample_conditions_1
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1
CBCAcoNH (H[N[co[{CA|ca[C]}]]])sample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
hcanco (hCANCO)sample_1isotropicsample_conditions_1
hcacon (h{CA|Cca}CO[N])sample_1isotropicsample_conditions_1
hcaco (haCACO)sample_1isotropicsample_conditions_1
con v3 (CO[N])sample_1isotropicsample_conditions_1
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis v2.4 - chemical shift assignment, data analysis

DANGLE v1.1 - data analysis

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

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