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Chlorine in PDB 1lw9: Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability

Enzymatic activity of Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability

All present enzymatic activity of Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability:
3.2.1.17;

Protein crystallography data

The structure of Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability, PDB code: 1lw9 was solved by N.C.Gassner, W.A.Baase, B.H.M.Mooers, R.D.Busam, L.H.Weaver, J.D.Lindstrom, M.L.Quillin, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.00 / 1.45
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.207, 60.207, 95.375, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 25.4

Other elements in 1lw9:

The structure of Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability also contains other interesting chemical elements:

Potassium (K) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability (pdb code 1lw9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability, PDB code: 1lw9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1lw9

Go back to Chlorine Binding Sites List in 1lw9
Chlorine binding site 1 out of 2 in the Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl173

b:18.3
occ:0.73
 O A:HOH291 2.9 32.0 1.0
O A:HOH209 3.0 15.0 1.0
N A:ARG145 3.2 11.8 1.0
N A:ASN144 3.3 12.5 1.0
C A:THR142 3.4 17.0 1.0
CA A:THR142 3.5 15.1 1.0
CB A:THR142 3.6 15.9 1.0
CB A:ASN144 3.7 15.2 1.0
N A:PRO143 3.7 19.0 1.0
CB A:ARG145 3.7 14.4 1.0
O A:THR142 3.7 15.2 1.0
CA A:ASN144 3.8 14.8 1.0
O A:HOH463 4.0 41.8 1.0
C A:ASN144 4.0 15.0 1.0
CA A:ARG145 4.1 11.9 1.0
C A:PRO143 4.2 13.9 1.0
CD A:PRO143 4.2 17.9 1.0
CG2 A:THR142 4.3 14.5 1.0
CA A:PRO143 4.5 12.5 1.0
CG A:ASN144 4.7 29.8 1.0
O A:HOH230 4.7 18.5 1.0
OG1 A:THR142 4.8 15.1 1.0
N A:THR142 4.9 12.6 1.0

Chlorine binding site 2 out of 2 in 1lw9

Go back to Chlorine Binding Sites List in 1lw9
Chlorine binding site 2 out of 2 in the Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl178

b:16.0
occ:0.73
 O A:HOH182 3.2 16.4 1.0
O A:HOH215 3.3 16.2 1.0
O A:HOH246 3.3 33.5 1.0
O A:HOH200 3.4 20.5 1.0
CE1 A:HIS31 3.8 16.1 1.0
NE2 A:HIS31 4.1 15.3 1.0
CB A:ALA49 4.1 13.9 1.0
O A:HOH282 4.5 48.6 1.0
NE2 A:GLN69 4.5 15.9 1.0
CA A:ALA49 4.5 14.6 1.0
O A:HOH202 4.6 32.4 1.0
CD2 A:LEU66 4.8 20.2 1.0
ND1 A:HIS31 4.9 13.0 1.0

Reference:

N.C.Gassner, W.A.Baase, B.H.Mooers, R.D.Busam, L.H.Weaver, J.D.Lindstrom, M.L.Quillin, B.W.Matthews. Multiple Methionine Substitutions Are Tolerated in T4 Lysozyme and Have Coupled Effects on Folding and Stability. Biophys.Chem. V. 100 325 2003.
ISSN: ISSN 0301-4622
PubMed: 12646375
DOI: 10.1016/S0301-4622(02)00290-9
Page generated: Sat Dec 12 08:42:05 2020

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