Tables
- Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules

Table 1

Statistics of data collection, refinement and quality of the structure

	CGL	CGL-αMM

Data collection
Total number of observations	238,197	483,177
Total number of unique observations	57,503	61,808
Rmerge (%)	8.8 (34.4)	7.3 (35.4)
Resolution limit (Å)	42.64-2.3	51.99-2.31
Completeness (%)	97.87 (98.2)	99.1 (94.5)
Multiplicity	3.9	4.5
(I)/σ	7.2 (2.2)	8.9 (2.0)
Wavelength (Å)	1.431	1.431
Space group	C2221	C2221
Cell parameters (Å)	a = 100.90	a = 100.91
	b = 115.35	b = 115.75
	c = 241.08	c = 241.62

Refinement
Resolution range (Å)	10-2.3	9.99-2.31
Rfactor (%)	18.38	16.87
Rfree (%)	23.28	22.31
Number amino acid residues in biological assembly	948	948
Number of water molecules	432	448
RMS deviations from ideal values
Bond lengths (Å)	0.021	0.026
Bond angles (degrees)	2.019	2.223
Temperature factors
Average B value for whole protein chain (Å ²)	20.6	20.1
Ramachandran plot
Residues in most favored regions	84.0	86.2
Residues in additional allowed regions	15.3	13.2
Residues in generously allowed regions	0.7	0.6

*Values in parenthesis represent the high resolution shell.

Table 2

Amino acids of Abu hydrophobic pocket, showing the conservation in lectins isolated from seeds of leguminous from various tribes.

Lectin	Abu hydrophobic pocket

CGL	Asn 124	Ala 125	Leu 126	Gln 137	Asp 139	Val 179
ConA	Asn 124	Ala 125	Leu 126	Gln 137	Asp 139	Val 179
BMA	Asn 126	Ser 127	Val 128	Gln 139	Asp 141	Val 181
Dlab	Gln 10	Ser 11	Leu 12	Gln 23	Asp 25	Leu 64
GML	Gln 32	Tre 33	Val 34	Gln 45	Asp 47	Leu 100
SBA	Glu 02	Tre 03	Val 04	Gln 15	Asp 17	Ile 57

Bold letters means identical amino acids; and unbolded letters are conservative modifications when compared with CGL.

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