BMRB Entry 15372

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15372

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Title:
Solution Structure of the Tick Carboxypeptidase Inhibitor
Deposition date:
2007-07-10
Original release date:
2008-06-25
Authors:
Pantoja-Uceda, David; Blanco, Francisco J
Citation:

Citation: Pantoja-Uceda, David; Arolas, Joan; Garcia, Pascal; Lopez-Hernandez, Eva; Padro, Daniel; Aviles, Francesc; Blanco, Francisco J. "The NMR Structure and Dynamics of the Two-Domain Tick Carboxypeptidase Inhibitor Reveal Flexibility in Its Free Form and Stiffness upon Binding to Human Carboxypeptidase B"  Biochemistry 47, 7066-7078 (2008).
PubMed: 18558717

Assembly members:

Assembly members:
TCI, polymer, 75 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rhipicephalus bursa   Taxonomy ID: 67831   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rhipicephalus bursa

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pBAT-4-OmpA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TCI: NECVSKGFGCLPQSDCPQEA RLSYGGCSTVCCDLSKLTGC KGKGGECNPLDRQCKELQAE SASCGKGQKCCVWLH

Data sets:
Data typeCount
13C chemical shifts258
15N chemical shifts81
1H chemical shifts454

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subnunit 11

Entities:

Entity 1, subnunit 1 75 residues - Formula weight is not available

1   ASNGLUCYSVALSERLYSGLYPHEGLYCYS
2   LEUPROGLNSERASPCYSPROGLNGLUALA
3   ARGLEUSERTYRGLYGLYCYSSERTHRVAL
4   CYSCYSASPLEUSERLYSLEUTHRGLYCYS
5   LYSGLYLYSGLYGLYGLUCYSASNPROLEU
6   ASPARGGLNCYSLYSGLULEUGLNALAGLU
7   SERALASERCYSGLYLYSGLYGLNLYSCYS
8   CYSVALTRPLEUHIS

Samples:

sample_1: TCI 0.76 mM

sample_2: TCI, [U-100% 15N], 0.7 mM

sample_3: TCI, [U-100% 13C; U-100% 15N], 0.1 mM

sample_conditions_1: dielectric constant: 78.4 mM; pH: 5.6; pressure: 1 atm; temperature: 298.0 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-15N TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1

Software:

NMRView v5.0.4, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMRPipe vfebrary 205, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

xwinnmr v3.5, Bruker Biospin - collection

NMRDraw v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

GARANT v1.2, Bartels, Guntert, Billeter and Wuthrich - chemical shift calculation

MARS v1.3, MARS (Young-Sang Jung and Markus Zweckstetter) - chemical shift calculation

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

BMRB 15729 15730 15731
PDB
GB AAW72225
SP Q5EPH2
AlphaFold Q5EPH2

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