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A report on the crystal structure of a lectin isolated from Canavalia …


Biology Articles » Mycology » Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules » Tables

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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