Table 2. NMR structure determination statistics of CCL2 in the free form and in complex with the fucosylated chitobiose (GlcNAcβ1,4[Fucα1,3]GlcNAc-spacer, the spacer [CH₂]₅COOH was truncated in the structure calculations to a methyl group.).

		CCL2–carbohydrate complex
	CCL2 free	CCL2	carbohydrate
NMR distance and dihedral constraints
Distance restraints
Total NOE	2514	2054	42
Intra-residue	482	446	23
Inter-residue	2032	1608	19
Sequential (|i−j| = 1)	593	489	9
Nonsequential (|i−j|>1 )	1439	1119	10
Hydrogen bonds	46	49	–
Protein–carbohydrate intermolecular		82
Total dihedral angle restraints	186	178
Protein
φ	91*	85*
ψ	95	91
Carbohydrate
HN-CO peptide bonds of acetamido			2
Structure statistics
Violations (mean and s.d.)
Number of distance constraint violations >0.2 Å	0.42±0.64	0.45±0.61
Number of dihedral angle violations >5°	0.05±0.22	4.75±1.48
Max. dihedral angle violation (°)	2.6±3.4	17.4±8.5
Max. distance constraint violation (Å)	0.24±0.07	0.20±0.04
Deviations from idealized geometry
Bond lengths (Å)	0.010	0.010
Bond angles (°)	2.29	2.38
Average pairwise r.m.s. deviation** (Å)
Protein (residues G22-V153)
Heavy	0.98±0.14	1.18±0.15
Backbone	0.45±0.10	0.71±0.13
carbohydrate
All glycan heavy			0.47±0.21
Complex
Protein and carbohydrate heavy		1.17±0.15

^*Phi values for prolines were omitted.

^**Pairwise r.m.s. deviation was calculated among 20 refined structures.