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Chlorine in PDB 4auv: Crystal Structure of the BRMS1 N-Terminal Region

Protein crystallography data

The structure of Crystal Structure of the BRMS1 N-Terminal Region, PDB code: 4auv was solved by M.Spinola-Amilibia, J.Rivera, M.Ortiz-Lombardia, A.Romero, J.L.Neira, J.Bravo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 95.64 / 2.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 42.636, 191.274, 71.940, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 25.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the BRMS1 N-Terminal Region (pdb code 4auv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the BRMS1 N-Terminal Region, PDB code: 4auv:

Chlorine binding site 1 out of 1 in 4auv

Go back to Chlorine Binding Sites List in 4auv
Chlorine binding site 1 out of 1 in the Crystal Structure of the BRMS1 N-Terminal Region


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 the BRMS1 N-Terminal Region within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1085

b:61.8
occ:1.00
NH2 A:ARG55 2.9 72.3 1.0
N A:ASP52 3.4 31.9 1.0
O A:HOH2001 3.8 48.7 1.0
CD A:ARG56 3.9 43.2 1.0
NH1 A:ARG56 3.9 69.9 1.0
CA A:GLU51 4.0 35.2 1.0
CB A:ASP52 4.1 28.9 1.0
CZ A:ARG55 4.1 92.6 1.0
C A:GLU51 4.2 37.5 1.0
CA A:ASP52 4.3 29.2 1.0
CG A:GLU51 4.5 28.3 1.0
O A:SER50 4.5 38.5 1.0
CG A:ARG56 4.7 37.8 1.0
CB A:GLU51 4.8 29.9 1.0
NE A:ARG55 4.8 89.0 1.0
NE A:ARG56 4.9 48.5 1.0
CZ A:ARG56 4.9 70.4 1.0
C A:ASP52 4.9 32.7 1.0
O A:ASP52 4.9 31.5 1.0

Reference:

M.Spinola-Amilibia, J.Rivera, M.Ortiz-Lombardia, A.Romero, J.L.Neira, J.Bravo. BRMS151-98 and BRMS151-84 Are Crystal Oligomeric Coiled Coils with Different Oligomerization States, Which Behave As Disordered Protein Fragments in Solution. J.Mol.Biol. V. 425 2147 2013.
ISSN: ISSN 0022-2836
PubMed: 23500495
DOI: 10.1016/J.JMB.2013.03.005
Page generated: Sun Jul 21 09:27:34 2024

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