1H chemical shift are referenced to internal DSS (present at trace concentrations of 1 to 2 uM).
15N chemical shifts are referenced indirectly by the chemical shift ratio 0.101329118 (IUPAC)
13C chemical shifts are externally referenced to DSS 0 ppm from a natural abundance 13C-1H HSQC spectrum of DSS 20 mM recorded under similar conditions as the protein sample.

(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignments for the 36 proline-containing, full length 29 kDa human chimera-type galectin-3.

Human Gal-3 full-length with (P64H, T98P) mutations and containing an acetylated Ala2 at the N-terminus.

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
-----------------------------------------------------

Important in: cell adhesion, cell activation and chemoattraction, cell growth and differentiation, cell cycle, and apoptosis

Lectin, galactoside-binding, Galectin-3 [Homo sapiens]

X-Ray Crystal Structure Of The Human Galectin-3 Carbohydrate Recognition Domain (Crd) At 2.1 Angstrom Resolution

High Resolution X-Ray Structure Of Human Galectin-3 In Complex With Lacnac

Crystal Structure Of The Human Galectin-3 Crd In Complex With A 3'- Derivative Of N-Acetyllactosamine

Crystal Structure Of Human Galectin-3 Carbohydrate- Recognising Domain At 2.45 Angstrom Resolution

Crystal Structure Of Human Galectin-3 Carbohydrate-Recognition Domain At 1.35 Angstrom Resolution

Crystal Structure Of Human Galectin-3 Carbohydrate-Recognition Domain With Lactose Bound, At 1.35 Angstrom Resolution

Human Galectin-3 In Complex With A Benzamido-N- Acetyllactoseamine Inhibitor

Crystal Structure Of Galectin-3 Crd Domian Complexed With Thomsen- Friedenreich Antigen

Crystal Structure Of Galectin-3 Crd Domian Complexed With Gm1 Pentasaccharide

Crystal Structure Of Galectin-3 Crd Domian Complexed With Tfn

Crystal Structure Of Galectin-3 Crd Domian Complexed With Lactose

Crystal Structure Of Human Galectin-3 In Complex With Methyl 2-o- Acetyl-3-o-toluoyl-beta-d-talopyranoside

Crystal Structure Of Human Galectin-3 Carbohydrate Recognition Domain In Complex With Methyl 3-deoxy-2-o-toluoyl-3-n-toluoyl-be

Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose At 0.86 Angstrom Resolution

Crystal Structure Of Human Galectin-3 Crd With Glycerol Bound At 0.90 Angstrom Resolution

Crystal Structure Of Apo Human Galectin-3 Crd At 1.08 Angstrom Resolution, At Cryogenic Temperature

Crystal Structure Of Apo Human Galectin-3 Crd At 1.25 Angstrom Resolution, At Room Temperature

Galectin-3c In Complex With Bisamido-thiogalactoside Derivate 1

Galectin-3c In Complex With Bisamido-thiogalactoside Derivate 2

Galectin-3c In Complex With Bisamido-thiogalactoside Derivate 3

Galectin-3 Carbohydrate Recognition Domain In Complex With Thiodigalactoside

Galectin-3 Carbohydrate Recognition Domain In Complex With Thioditaloside

Crystal Structure Of Human Galectin-3 Crd K176l Mutant In Complex With Lnt

Crystal Structure Of Human Galectin-3 Crd K176l Mutant In Complex With Lnnt

Crystal Structure Of Human Galectin-3 Crd K176l Mutant In Complex With A-gm3

Crystal Structure Of Human Galectin-3 Crd In Complex With Lnt

Crystal Structure Of Human Galectin-3 Crd In Complex With Lnnt

Crystal Structure Of Human Galectin-3 Crd In Complex With A-gm3

Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose (ph 7.0, Peg4000)

Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose (ph 7.0, Peg 6000)

Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose (ph 7.5, Peg6000)

Crystal Structure Of Human Galectin-3 Crd In Complex With Lactose (ph 7.9, Peg6000)

Crystal Structure Of Human Galectin-3 Crd In Complex With Type 1 N- Acetyllactosamine

lectin, galactoside-binding, soluble, 3 [synthetic construct]

galactose-specific lectin [Homo sapiens]

carbohydrate binding protein 35 [Homo sapiens]

RecName: Full=Galectin-3; Short=Gal-3; AltName: Full=35 kDa lectin; AltName: Full=Carbohydrate-binding protein 35; Short=CBP 35

Gal-3 protein with P64H and T98P mutations has been sequenced from human patients with progressive cancer.

Backbone and side chain resonance assignments for apo human Galectin-3:
full-length (2-250) with natural occurring P64H & T98P point mutations and
containing an acetylated-Ala2 modification at the N-terminus.

1H, 13C, 15N chemical shift assignments of full-length apo human Galectin-3 (2-250).

NMR data collected on apo human Gal-3 using standard sample conditions (20 mM KPi, 8 mM DTT, 0.1 mM EDTA, pH 6.8) at 30 deg Celsius.

Bruker Avance 900 MHz
with 13C,15N,1H cryoprobe

Bruker Avance 700 MHz
with 13C,15N,1H cryoprobe

Bruker Avance HD 700 MHz
with 13C,15N,1H cryoprobe

Assignment of 1H, 15N and 13C resonances of the carbohydrate recognition domain of human galectin-3 with lactose bound

High resolution X-ray structure (0.86 A) of Gal-3 CRD domain in complex with lactose

High resolution X-ray structure (1.08 A) of apo Gal-3 CRD domain at cryogenic temperature

High resolution X-ray structure (1.23 A) of apo Gal-3 CRD domain at room temperature

Analysis and averaging of deposited chemical shifts

PACES: Protein sequential assignment by computer-assisted exhaustive search.
Coggins and Zhou, J Biomol NMR. (2003), 26(2):93-111.