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BMRB Entry 19491 BMRB - Biological Magnetic Resonance Bank

BMRB Entry 19491

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR19491

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Title:
1H, 13C, 15N chemical shift assignments of full-length apo human Galectin-3 (2-250).
Deposition date:
2013-09-11
Original release date:
2014-02-12
Authors:
Ippel, Hans; Andre, Sabine; Suijlen, Dennis; Hackeng, Tilman; Weber, Christian; Gabius, Hans-Joachim; Mayo, Kevin
Citation:

Citation: Ippel, Hans; Miller, Michelle; Berbis, Manuel Alvaro; Suylen, Dennis; Andre, Sabine; Hackeng, Tilman; Canada, F. Javier; Weber, Christian; Gabius, Hans-Joachim; Jimenez-Barbero, Jesus; Mayo, Kevin. "(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignments for the 36 proline-containing, full length 29kDa human chimera-type galectin-3."  Biomol. NMR Assignments ., .-. (2014).
PubMed: 24504927

Assembly members:

Assembly members:
Galectin-3, polymer, 250 residues, 26150 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: prCBP35s

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Galectin-3: MADNFSLHDALSGSGNPNPQ GWPGAWGNQPAGAGGYPGAS YPGAYPGQAPPGAYPGQAPP GAYHGAPGAYPGAPAPGVYP GPPSGPGAYPSSGQPSAPGA YPATGPYGAPAGPLIVPYNL PLPGGVVPRMLITILGTVKP NANRIALDFQRGNDVAFHFN PRFNENNRRVIVCNTKLDNN WGREERQSVFPFESGKPFKI QVLVEPDHFKVAVNDAHLLQ YNHRVKKLNEISKLGISGDI DLTSASYTMI

Data sets:
Data typeCount
13C chemical shifts1260
15N chemical shifts336
1H chemical shifts1751

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Galectin-3, trans form, 1 (major form)1
2Galectin-3, cis form, 1 (b)1
3Galectin-3, cis form, 2 (c)1
4Galectin-3, cis form, 3 (d)1
5Galectin-3, cis form, 4 (e)1

Entities:

Entity 1, Galectin-3, trans form, 1 (major form) 250 residues - 26150 Da.

Backbone and side chain resonance assignments for apo full-length human Galectin-3 (2-250) with natural occurring P64H & T98P point mutations. The original N-terminal Met1 amino acid is truncated from the amino acid sequence during protein expression (>70% processed), and substituted by an acetylated-Ala2 modification similarly as found in native Gal-3. The DNA sequence of the mutant Gal-3 is derived from human patients having cancer and cloned into a E.Coli plasmid vector for study of the protein. Multiple conformational states of the protein are present in solution caused by slow cis-trans isomerization of multiple prolines in the primary amino acid sequence. Set 1 correspond to the main set of peaks contributed to the major ensemble containing mostly trans-prolines. Exceptions on this rule are: P117 where no trans-proline state can be observed next to the major cis form, and P46/G47 where multiple cis-Pro peaks are observed in the spectra, with no obvious major trans-Pro peaks. Assignments of minor cis proline induced peaks in the NMR spectra are listed in conformer sets 2, 3, 4, and 5 (or resp. b, c,d and e in related figure plots) following set 1. Isomer set 2 represent resonance peaks of associated with the most abundant cis-Pro isomer (5-40%) affecting one particular local region, whereas sets c, d, and e represent minor forms induced by two (nearby) cis-prolines. Note that more than four discrete peaks per resonance signal can exist when multiple prolines are closely located within each other, e.g. at PxP or PxxxP junctions. Galectin-3 contains an N-acetyl alanine (Ala2) at position 2 (according to the original sequence numbering). HAC and CAC atoms of Ac-Ala2 in the BMRB entry represent the CH3 methyl proton and carbon atom of the acetyl group. Chemical shifts are: ----------------------------------------------------- 2 A CAC 13C 24.524 0.062 2 2 A HAC 1H 2.012 0.000 1 -----------------------------------------------------

1   METALAASPASNPHESERLEUHISASPALA
2   LEUSERGLYSERGLYASNPROASNPROGLN
3   GLYTRPPROGLYALATRPGLYASNGLNPRO
4   ALAGLYALAGLYGLYTYRPROGLYALASER
5   TYRPROGLYALATYRPROGLYGLNALAPRO
6   PROGLYALATYRPROGLYGLNALAPROPRO
7   GLYALATYRHISGLYALAPROGLYALATYR
8   PROGLYALAPROALAPROGLYVALTYRPRO
9   GLYPROPROSERGLYPROGLYALATYRPRO
10   SERSERGLYGLNPROSERALAPROGLYALA
11   TYRPROALATHRGLYPROTYRGLYALAPRO
12   ALAGLYPROLEUILEVALPROTYRASNLEU
13   PROLEUPROGLYGLYVALVALPROARGMET
14   LEUILETHRILELEUGLYTHRVALLYSPRO
15   ASNALAASNARGILEALALEUASPPHEGLN
16   ARGGLYASNASPVALALAPHEHISPHEASN
17   PROARGPHEASNGLUASNASNARGARGVAL
18   ILEVALCYSASNTHRLYSLEUASPASNASN
19   TRPGLYARGGLUGLUARGGLNSERVALPHE
20   PROPHEGLUSERGLYLYSPROPHELYSILE
21   GLNVALLEUVALGLUPROASPHISPHELYS
22   VALALAVALASNASPALAHISLEULEUGLN
23   TYRASNHISARGVALLYSLYSLEUASNGLU
24   ILESERLYSLEUGLYILESERGLYASPILE
25   ASPLEUTHRSERALASERTYRTHRMETILE

Samples:

sample_1: Galectin-3, [U-98% 15N], 0.4 mM; DSS 2 uM; potassium phosphate 20 mM; DTT 8 mM; EDTA 0.1 mM

sample_2: Galectin-3, [U-98% 15N], 40 uM; DSS 1 uM; potassium phosphate 20 mM; DTT 8 mM; EDTA 0.1 mM

sample_3: Galectin-3, [U-98% 15N], 20 uM; DSS 1 uM; potassium phosphate 20 mM; DTT 8 mM; EDTA 0.1 mM

sample_4: Galectin-3, [U-98% 13C; U-98% 15N], 0.4 mM; DSS 2 uM; potassium phosphate 20 mM; DTT 8 mM; EDTA 0.1 mM

sample_5: Galectin-3, [U-98% 13C; U-98% 15N], 40 uM; DSS 1 uM; potassium phosphate 20 mM; DTT 8 mM; EDTA 0.1 mM

sample_6: Galectin-3, [U-98% 13C; U-98% 15N], 0.27 mM; DSS 2 uM; potassium phosphate 20 mM; DTT 11 mM; EDTA 0.1 mM; sodium azide 1 mM

sample_conditions_1: ionic strength: 25 mM; pH: 6.8; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_4isotropicsample_conditions_1
2D 1H-13C HSQCsample_5isotropicsample_conditions_1
2D 1H-13C HSQCsample_6isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D HNCAsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_5isotropicsample_conditions_1
3D HNCACBsample_4isotropicsample_conditions_1
3D CC(CO)NHsample_4isotropicsample_conditions_1
3D HN(CA)COsample_4isotropicsample_conditions_1
3D HBHA(CO)NHsample_4isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_4isotropicsample_conditions_1
3D HcCH DIPSIsample_4isotropicsample_conditions_1
3D HcCH DIPSIsample_6isotropicsample_conditions_1
3D hCCH DIPSIsample_6isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D C_CONsample_1isotropicsample_conditions_1
2D C_CACOsample_1isotropicsample_conditions_1
2D C_CANsample_1isotropicsample_conditions_1

Software:

SPARKY v3.114, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN v3.2, Bruker Biospin - collection, processing

PACES, Coggins and Zhou - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 700 MHz

Related Database Links:

GB AAH53667.1 AAA35607 AAA36163 AAA88086 AAB26229 AAB86584
BMRB 15705
PDB
DBJ BAA22164 BAD92628 BAG37435 BAI46476
EMBL CAG33178 CAG46894
REF NP_001170859 NP_002297 XP_001148424 XP_002824813 XP_003831735
SP P17931
AlphaFold P17931

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