BIOMOLECULE: 1 This entry contains the crystallographic asymmetric unit which consists of 1 chain(s) ...BIOMOLECULE: 1 This entry contains the crystallographic asymmetric unit which consists of 1 chain(s). the biological molecule(s) is expected to be full-length galectin-3 which consists of N-terminal domain and the CRD domain. see remark 350 for information on generating the biological molecule(s) of CRD domain.
The Biological unit is a monomer of the Galectin-3 carbohydrate-recognition domain. The crystallographic asymmetric unit contains one molecule of the galectin-3 carbohydrate-recognition domain
-
Components
#1: Protein
Galectin-3 / Galactose-specific lectin 3 / Mac-2 antigen / IgE-binding protein / 35 kDa lectin / Carbohydrate- ...Galactose-specific lectin 3 / Mac-2 antigen / IgE-binding protein / 35 kDa lectin / Carbohydrate-binding protein 35 / CBP 35 / Laminin-binding protein / Lectin L-29 / L-31 / Galactoside-binding protein / GALBP
Mass: 15701.049 Da / Num. of mol.: 1 / Fragment: Galectin-3 CRD domain, Residues 113-250 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET-3a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 / References: UniProt: P17931
Resolution: 1.35→31.36 Å / Cor.coef. Fo:Fc: 0.963 / Cor.coef. Fo:Fc free: 0.957 / SU B: 0.768 / SU ML: 0.033 / Cross valid method: THROUGHOUT / ESU R: 0.059 / ESU R Free: 0.057 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.18441
1459
5.1 %
RANDOM
Rwork
0.16948
-
-
-
obs
0.17022
27116
97.28 %
-
Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parameters
Biso mean: 12.931 Å2
Baniso -1
Baniso -2
Baniso -3
1-
0.29 Å2
0 Å2
0 Å2
2-
-
-0.19 Å2
0 Å2
3-
-
-
-0.09 Å2
Refinement step
Cycle: LAST / Resolution: 1.35→31.36 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
1108
0
36
170
1314
Refine LS restraints
Refine-ID
Type
Dev ideal
Dev ideal target
Number
X-RAY DIFFRACTION
r_bond_refined_d
0.007
0.022
1235
X-RAY DIFFRACTION
r_bond_other_d
X-RAY DIFFRACTION
r_angle_refined_deg
1.294
1.981
1689
X-RAY DIFFRACTION
r_angle_other_deg
X-RAY DIFFRACTION
r_dihedral_angle_1_deg
6.797
5
155
X-RAY DIFFRACTION
r_dihedral_angle_2_deg
35.369
23.71
62
X-RAY DIFFRACTION
r_dihedral_angle_3_deg
11.046
15
209
X-RAY DIFFRACTION
r_dihedral_angle_4_deg
9.198
15
11
X-RAY DIFFRACTION
r_chiral_restr
0.089
0.2
191
X-RAY DIFFRACTION
r_gen_planes_refined
0.005
0.02
947
X-RAY DIFFRACTION
r_gen_planes_other
X-RAY DIFFRACTION
r_nbd_refined
0.192
0.2
440
X-RAY DIFFRACTION
r_nbd_other
X-RAY DIFFRACTION
r_nbtor_refined
0.31
0.2
826
X-RAY DIFFRACTION
r_nbtor_other
X-RAY DIFFRACTION
r_xyhbond_nbd_refined
0.079
0.2
106
X-RAY DIFFRACTION
r_xyhbond_nbd_other
X-RAY DIFFRACTION
r_metal_ion_refined
X-RAY DIFFRACTION
r_metal_ion_other
X-RAY DIFFRACTION
r_symmetry_vdw_refined
0.169
0.2
38
X-RAY DIFFRACTION
r_symmetry_vdw_other
X-RAY DIFFRACTION
r_symmetry_hbond_refined
0.131
0.2
19
X-RAY DIFFRACTION
r_symmetry_hbond_other
X-RAY DIFFRACTION
r_symmetry_metal_ion_refined
X-RAY DIFFRACTION
r_symmetry_metal_ion_other
X-RAY DIFFRACTION
r_mcbond_it
1.408
2
749
X-RAY DIFFRACTION
r_mcbond_other
X-RAY DIFFRACTION
r_mcangle_it
2.02
3
1196
X-RAY DIFFRACTION
r_scbond_it
2.764
4
535
X-RAY DIFFRACTION
r_scangle_it
4.15
6
486
X-RAY DIFFRACTION
r_rigid_bond_restr
X-RAY DIFFRACTION
r_sphericity_free
X-RAY DIFFRACTION
r_sphericity_bonded
LS refinement shell
Resolution: 1.35→1.385 Å / Total num. of bins used: 20
Rfactor
Num. reflection
% reflection
Rfree
0.246
105
-
Rwork
0.245
1621
-
obs
-
-
81.07 %
+
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