Chlorine in PDB 1vq0: Crystal Structure of 33 kDa Chaperonin (Heat Shock Protein 33 Homolog) (HSP33) (TM1394) From Thermotoga Maritima at 2.20 A Resolution

The structure of Crystal Structure of 33 kDa Chaperonin (Heat Shock Protein 33 Homolog) (HSP33) (TM1394) From Thermotoga Maritima at 2.20 A Resolution, PDB code: 1vq0 was solved by Joint Center For Structural Genomics (Jcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.62 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	76.213, 101.673, 113.686, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 24.1

The structure of Crystal Structure of 33 kDa Chaperonin (Heat Shock Protein 33 Homolog) (HSP33) (TM1394) From Thermotoga Maritima at 2.20 A Resolution also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Chlorine atom in the Crystal Structure of 33 kDa Chaperonin (Heat Shock Protein 33 Homolog) (HSP33) (TM1394) From Thermotoga Maritima at 2.20 A Resolution (pdb code 1vq0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of 33 kDa Chaperonin (Heat Shock Protein 33 Homolog) (HSP33) (TM1394) From Thermotoga Maritima at 2.20 A Resolution, PDB code: 1vq0:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Crystal Structure of 33 kDa Chaperonin (Heat Shock Protein 33 Homolog) (HSP33) (TM1394) From Thermotoga Maritima at 2.20 A Resolution


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 33 kDa Chaperonin (Heat Shock Protein 33 Homolog) (HSP33) (TM1394) From Thermotoga Maritima at 2.20 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl301 b:41.6 occ:1.00 N A:ALA168 3.3 33.8 1.0 NH1 A:ARG18 3.4 54.0 1.0 O A:ALA168 3.5 34.7 1.0 CD A:ARG18 3.5 47.2 1.0 N A:MET19 3.7 27.5 1.0 C A:ALA168 3.7 35.4 1.0 N A:ARG20 3.7 33.3 1.0 CA A:ILE167 3.8 34.7 1.0 CB A:ARG18 3.9 32.3 1.0 CA A:ARG18 3.9 31.6 1.0 CB A:ARG20 3.9 36.9 1.0 C A:ILE167 4.0 33.9 1.0 C A:ARG18 4.1 30.1 1.0 CA A:ALA168 4.1 33.5 1.0 CZ A:ARG18 4.2 56.7 1.0 CG2 A:ILE167 4.2 33.1 1.0 NE A:ARG18 4.2 52.6 1.0 N A:GLY169 4.3 35.3 1.0 CG A:ARG18 4.3 39.5 1.0 CA A:ARG20 4.4 36.0 1.0 CG A:ARG20 4.4 41.0 1.0 CB A:ILE167 4.5 34.2 1.0 ND1 A:HIS-1 4.5 58.0 1.0 C A:MET19 4.6 31.0 1.0 CA A:GLY169 4.6 35.5 1.0 CA A:MET19 4.7 30.0 1.0 O A:LYS166 4.7 34.2 1.0 CD2 A:PHE202 4.7 39.0 1.0 CB A:ALA168 4.8 34.2 1.0 CG1 A:ILE167 4.9 37.1 1.0 N A:ILE167 4.9 33.5 1.0 CD A:ARG20 5.0 41.5 1.0

Chlorine binding site 2 out of 2 in the Crystal Structure of 33 kDa Chaperonin (Heat Shock Protein 33 Homolog) (HSP33) (TM1394) From Thermotoga Maritima at 2.20 A Resolution


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 33 kDa Chaperonin (Heat Shock Protein 33 Homolog) (HSP33) (TM1394) From Thermotoga Maritima at 2.20 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl301 b:40.8 occ:1.00 N B:ALA168 3.3 33.5 1.0 NH1 B:ARG18 3.4 54.8 1.0 O B:ALA168 3.4 35.1 1.0 CD B:ARG18 3.6 47.4 1.0 N B:MET19 3.7 28.4 1.0 N B:ARG20 3.7 33.3 1.0 C B:ALA168 3.8 35.0 1.0 CB B:ARG20 3.8 35.6 1.0 CA B:ILE167 3.9 34.7 1.0 CA B:ARG18 3.9 31.4 1.0 CB B:ARG18 3.9 32.1 1.0 C B:ARG18 4.1 29.9 1.0 C B:ILE167 4.1 34.5 1.0 CA B:ALA168 4.2 33.6 1.0 CZ B:ARG18 4.2 57.4 1.0 CG2 B:ILE167 4.2 35.5 1.0 NE B:ARG18 4.3 52.6 1.0 CG B:ARG18 4.3 39.4 1.0 CA B:ARG20 4.3 34.9 1.0 CG B:ARG20 4.4 40.2 1.0 N B:GLY169 4.4 35.5 1.0 ND1 B:HIS-1 4.4 58.7 1.0 CB B:ILE167 4.5 35.3 1.0 C B:MET19 4.6 30.9 1.0 O B:LYS166 4.7 33.3 1.0 CA B:MET19 4.7 29.8 1.0 CA B:GLY169 4.7 36.0 1.0 CD2 B:PHE202 4.8 38.1 1.0 CG1 B:ILE167 4.8 36.9 1.0 CD B:ARG20 4.8 41.4 1.0 N B:ILE167 5.0 33.5 1.0 CB B:ALA168 5.0 34.3 1.0

L.Jaroszewski, R.Schwarzenbacher, D.Mcmullan, P.Abdubek, S.Agarwalla, E.Ambing, H.Axelrod, T.Biorac, J.M.Canaves, H.J.Chiu, A.M.Deacon, M.Didonato, M.A.Elsliger, A.Godzik, C.Grittini, S.K.Grzechnik, J.Hale, E.Hampton, G.W.Han, J.Haugen, M.Hornsby, H.E.Klock, E.Koesema, A.Kreusch, P.Kuhn, S.A.Lesley, M.D.Miller, K.Moy, E.Nigoghossian, J.Paulsen, K.Quijano, R.Reyes, C.Rife, G.Spraggon, R.C.Stevens, H.Van Den Bedem, J.Velasquez, J.Vincent, A.White, G.Wolf, Q.Xu, K.O.Hodgson, J.Wooley, I.A.Wilson. Crystal Structure of HSP33 Chaperone (TM1394) From Thermotoga Maritima at 2.20 A Resolution. Proteins V. 61 669 2005.
ISSN: ISSN 0887-3585
PubMed: 16167343
DOI: 10.1002/PROT.20542