Chlorine in PDB 4i1k: Crystal Structure of VRN1 (Residues 208-341)

The structure of Crystal Structure of VRN1 (Residues 208-341), PDB code: 4i1k was solved by G.King, A.H.Chanson, E.J.Mccallum, M.Ohme-Takagi, K.Byriel, J.M.Hill, J.L.Martin, J.S.Mylne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	106.152, 47.310, 61.413, 90.00, 114.97, 90.00
R / Rfree (%)	12 / 16.6

The binding sites of Chlorine atom in the Crystal Structure of VRN1 (Residues 208-341) (pdb code 4i1k). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Crystal Structure of VRN1 (Residues 208-341), PDB code: 4i1k:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Crystal Structure of VRN1 (Residues 208-341)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of VRN1 (Residues 208-341) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl201 b:17.6 occ:1.00 O B:HOH340 3.1 16.8 1.0 O A:HOH312 3.1 16.5 1.0 NH2 A:ARG42 3.3 14.2 1.0 NH2 B:ARG42 3.3 18.5 1.0 NH1 B:ARG42 3.3 18.9 1.0 NH1 A:ARG42 3.4 15.1 1.0 CZ A:ARG42 3.8 13.8 1.0 CZ B:ARG42 3.8 18.7 1.0 CD1 A:ILE24 4.3 14.8 1.0 CD1 B:ILE24 4.5 14.7 1.0 CD A:ARG20 4.6 19.3 1.0 CG1 B:VAL40 4.7 12.4 1.0 CD B:ARG20 4.8 19.0 1.0 CG1 A:VAL40 4.8 12.8 1.0 NH1 B:ARG20 4.9 20.9 1.0

Chlorine binding site 2 out of 4 in the Crystal Structure of VRN1 (Residues 208-341)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of VRN1 (Residues 208-341) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:17.9 occ:1.00 NH1 A:ARG82 3.1 16.3 1.0 N A:GLY68 3.3 12.7 1.0 CA A:GLY68 3.6 11.3 1.0 CG A:ARG82 3.8 13.2 1.0 CD A:ARG82 3.9 14.9 1.0 O A:HOH407 4.1 45.2 1.0 OG A:SER67 4.1 36.2 1.0 CD1 A:LEU84 4.2 27.7 1.0 CZ A:ARG82 4.3 14.6 1.0 CB A:LEU84 4.3 23.7 1.0 C A:SER67 4.4 17.2 1.0 NE A:ARG82 4.5 13.9 1.0 CD2 A:LEU84 4.6 28.2 1.0 CG A:LEU84 4.6 27.6 1.0 C A:GLY68 4.6 10.8 1.0 CA A:SER67 4.8 23.2 1.0 O A:GLY68 4.8 11.2 1.0 O A:CYS83 5.0 18.1 1.0 CA A:LEU84 5.0 19.3 1.0

Chlorine binding site 3 out of 4 in the Crystal Structure of VRN1 (Residues 208-341)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of VRN1 (Residues 208-341) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl201 b:20.2 occ:1.00 O B:HOH454 2.8 40.8 1.0 O B:HOH463 3.1 46.4 1.0 N B:ARG117 3.3 12.7 1.0 ND2 B:ASN34 3.4 10.6 1.0 CB B:ARG117 3.8 15.6 1.0 CA B:LEU116 4.0 11.6 1.0 CB B:LEU116 4.0 12.2 1.0 CG B:ARG117 4.0 17.2 1.0 CD2 B:LEU116 4.0 13.6 1.0 CA B:ARG117 4.1 13.6 1.0 C B:LEU116 4.1 12.0 1.0 CG B:ASN34 4.2 10.7 1.0 OD1 B:ASN34 4.3 12.3 1.0 CD B:ARG117 4.4 19.4 1.0 CG B:LEU116 4.5 11.7 1.0 C B:ARG117 4.7 18.1 1.0 O B:HOH477 4.7 50.9 1.0 O B:HOH376 4.8 22.1 1.0 O B:ARG117 4.8 22.9 1.0 CD1 B:LEU116 4.9 13.8 1.0

Chlorine binding site 4 out of 4 in the Crystal Structure of VRN1 (Residues 208-341)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Crystal Structure of VRN1 (Residues 208-341) within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl202 b:21.4 occ:1.00 O B:HOH331 3.0 20.0 1.0 N B:GLY95 3.2 10.3 1.0 N B:GLU98 3.3 11.7 1.0 CA B:GLY95 3.4 10.1 1.0 C B:GLY95 3.6 9.1 1.0 CG B:GLU98 3.6 24.4 0.5 N B:TYR97 3.7 9.3 1.0 CB B:GLU98 3.8 17.2 1.0 CB B:TYR97 3.8 13.4 1.0 N B:TRP96 4.0 8.4 1.0 O B:GLY95 4.0 9.6 1.0 CA B:TYR97 4.0 10.9 1.0 CA B:GLU98 4.1 11.1 1.0 C B:TYR97 4.1 11.7 1.0 O B:HOH316 4.2 14.0 1.0 C B:GLN94 4.4 11.2 1.0 NH1 B:ARG48 4.5 41.3 1.0 C B:TRP96 4.5 10.6 1.0 CD2 B:TYR97 4.6 19.1 1.0 CG B:TYR97 4.7 15.9 1.0 O B:HOH434 4.8 32.5 1.0 CD B:GLU98 4.9 31.4 0.5 CA B:GLN94 4.9 10.8 1.0 CA B:TRP96 4.9 10.7 1.0 O B:SER93 4.9 10.1 1.0

G.J.King, A.H.Chanson, E.J.Mccallum, M.Ohme-Takagi, K.Byriel, J.M.Hill, J.L.Martin, J.S.Mylne. The Arabidopsis B3 Domain Protein VERNALIZATION1 (VRN1) Is Involved in Processes Essential For Development, with Structural and Mutational Studies Revealing Its Dna-Binding Surface. J.Biol.Chem. V. 288 3198 2013.
ISSN: ISSN 0021-9258
PubMed: 23255593
DOI: 10.1074/JBC.M112.438572