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 27277

Title: 1H, 13C and 15N chemical shift assignments for carbohydrate binding module 14 (CBM14)   PubMed: 31891077

Deposition date: 2017-10-10 Original release date: 2020-01-08

Authors: Madland, Eva; Aachmann, Finn

Citation: Madland, Eva; Crasson, Oscar; Vandevenne, Marylene; Sorlie, Morten; Aachmann, Finn. "NMR and Fluorescence Spectroscopies Reveal the Preorganized Binding Site in Family 14 Carbohydrate-Binding Module from Human Chitotriosidase"  ACS Omega 4, 21975-21984 (2019).

Assembly members:
CBM14, polymer, 57 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
CBM14: GSPTFCQGKADGLYPNPRER SSFYSCAAGRLFQQSCPTGL VFSNSCKCCTWNGLVPR

Data sets:
Data typeCount
13C chemical shifts187
15N chemical shifts50
1H chemical shifts317

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CBM141

Entities:

Entity 1, CBM14 57 residues - Formula weight is not available

1   GLYSERPROTHRPHECYSGLNGLYLYSALA
2   ASPGLYLEUTYRPROASNPROARGGLUARG
3   SERSERPHETYRSERCYSALAALAGLYARG
4   LEUPHEGLNGLNSERCYSPROTHRGLYLEU
5   VALPHESERASNSERCYSLYSCYSCYSTHR
6   TRPASNGLYLEUVALPROARG

Samples:

15N_sample: CBM14, [U-98% 15N], 0.15 mM; sodium phosphate 50 mM

13C_15N_sample: CBM14, [U-98% 13C; U-98% 15N], 0.15 mM; sodium phosphate 50 mM

D2O_sample: CBM14 0.15 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 0.11 M; pH: 5.5; pressure: 1 atm; temperature: 298.1 K

sample_conditions_2: ionic strength: 0.11 M; pH: 5.5; pressure: 1 atm; temperature: 298.1 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aliphatic13C_15N_sampleisotropicsample_conditions_1
3D HNCA13C_15N_sampleisotropicsample_conditions_1
3D HNCO13C_15N_sampleisotropicsample_conditions_1
3D CBCA(CO)NH13C_15N_sampleisotropicsample_conditions_1
3D HNCACB13C_15N_sampleisotropicsample_conditions_1
3D HN(CO)CA13C_15N_sampleisotropicsample_conditions_1
3D HCCH-TOCSY13C_15N_sampleisotropicsample_conditions_1
3D H(CCO)NH13C_15N_sampleisotropicsample_conditions_1
3D 1H-15N NOESY13C_15N_sampleisotropicsample_conditions_1
3D 1H-15N TOCSY15N_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aliphatic13C_15N_sampleisotropicsample_conditions_1
2D 1H-1H NOESYD2O_sampleisotropicsample_conditions_2
2D 1H-1H COSYD2O_sampleisotropicsample_conditions_2
2D 1H-1H TOCSYD2O_sampleisotropicsample_conditions_2

Software:

TOPSPIN v3.5, Bruker Biospin - collection

CARA v1.5, Keller and Wuthrich - chemical shift assignment

XEASY, Bartels et al. - chemical shift assignment

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - structure solution

YASARA, YASARA - geometry optimization

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP Q13231.1

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