BMRB Entry 36250

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36250
MolProbity Validation Chart

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Title:
Solution structure of camelid nanobody Nb11 against aflatoxin B1
Deposition date:
2019-05-14
Original release date:
2025-09-27
Authors:
Nie, Y.; Li, S.; He, T.; Zhu, J.; Yang, Y.
Citation:

Citation: Nie, Y.; Li, S.; He, T.; Zhu, J.; Yang, Y.. "Solution structure of camelid nanobody Nb11 against aflatoxin B1"  .

Assembly members:

Assembly members:
camelid nanobody Nb11, polymer, 131 residues, 14481.106 Da.

Natural source:

Natural source:   Common Name: alpaca   Taxonomy ID: 30538   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Vicugna pacos

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
camelid nanobody Nb11: MQLQLVESGGGLVQAGGSLR LSCVASGRTFRSNAMGWFRQ APGKEREFVAAIRWSGGSTY YADSVKGRFTISRDNAKNTV YLQMNSLKPEDTAVYLCAAG VWRSSGWDTPDYWGQGTQVT VSSLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts478
15N chemical shifts130
1H chemical shifts750

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 131 residues - 14481.106 Da.

1   METGLNLEUGLNLEUVALGLUSERGLYGLY
2   GLYLEUVALGLNALAGLYGLYSERLEUARG
3   LEUSERCYSVALALASERGLYARGTHRPHE
4   ARGSERASNALAMETGLYTRPPHEARGGLN
5   ALAPROGLYLYSGLUARGGLUPHEVALALA
6   ALAILEARGTRPSERGLYGLYSERTHRTYR
7   TYRALAASPSERVALLYSGLYARGPHETHR
8   ILESERARGASPASNALALYSASNTHRVAL
9   TYRLEUGLNMETASNSERLEULYSPROGLU
10   ASPTHRALAVALTYRLEUCYSALAALAGLY
11   VALTRPARGSERSERGLYTRPASPTHRPRO
12   ASPTYRTRPGLYGLNGLYTHRGLNVALTHR
13   VALSERSERLEUGLUHISHISHISHISHIS
14   HIS

Samples:

13C_15N: camelid nanobody 11, [U-100% 13C; U-100% 15N], 0.6 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.15 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC13C_15Nisotropicsample_conditions_1
2D 1H-13C HSQC13C_15Nisotropicsample_conditions_1
3D HNCO13C_15Nisotropicsample_conditions_1
3D HN(CA)CO13C_15Nisotropicsample_conditions_1
3D HNCA13C_15Nisotropicsample_conditions_1
2D 1H-13C HSQC aromatic13C_15Nisotropicsample_conditions_1
3D HN(CO)CA13C_15Nisotropicsample_conditions_1
3D CBCA(CO)NH13C_15Nisotropicsample_conditions_1
3D HNCACB13C_15Nisotropicsample_conditions_1
3D HBHA(CO)NH13C_15Nisotropicsample_conditions_1
3D C(CO)NH13C_15Nisotropicsample_conditions_1
3D H(CCO)NH13C_15Nisotropicsample_conditions_1
3D HCCH-TOCSY13C_15Nisotropicsample_conditions_1
3D 1H-15N NOESY13C_15Nisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic13C_15Nisotropicsample_conditions_1
3D 1H-13C NOESY aromatic13C_15Nisotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment

Sparky, Goddard - peak picking

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 850 MHz

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