Chlorine in PDB 7ln9: X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 1

All present enzymatic activity of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 1:
3.2.1.17;

The structure of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 1, PDB code: 7ln9 was solved by F.Yabukarski, T.Doukov, D.Herschlag, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.55 / 1.13
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	77.258, 77.258, 37.31, 90, 90, 90
R / Rfree (%)	13.6 / 15.6

The structure of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 1 also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Chlorine atom in the X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 1 (pdb code 7ln9). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 1, PDB code: 7ln9:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:19.1 occ:0.53 CL A:CL202 0.0 19.1 0.5 CL A:CL202 1.1 23.9 0.5 HH A:TYR23 2.0 15.2 0.3 HH A:TYR23 2.3 14.6 0.3 HH A:TYR23 2.5 15.7 0.3 OH A:TYR23 2.6 12.7 0.3 OH A:TYR23 2.9 12.1 0.3 HE1 A:TYR23 3.1 15.4 0.3 OH A:TYR23 3.1 13.1 0.3 O A:HOH317 3.2 19.0 0.6 HE2 A:TYR23 3.3 14.9 0.3 HE1 A:TYR23 3.3 11.9 0.3 HA3 A:GLY104 3.4 14.8 0.4 CZ A:TYR23 3.4 10.8 0.3 HA3 A:GLY104 3.5 17.2 0.1 CE1 A:TYR23 3.6 12.8 0.3 HA3 A:GLY104 3.6 17.1 0.5 CE2 A:TYR23 3.6 12.4 0.3 CZ A:TYR23 3.6 10.9 0.3 CZ A:TYR23 3.7 10.4 0.3 O A:HOH315 3.8 21.6 0.4 CE1 A:TYR23 3.8 9.9 0.3 HA2 A:GLY104 4.0 17.2 0.1 HA2 A:GLY104 4.1 14.8 0.4 CA A:GLY104 4.1 12.3 0.4 O A:HOH317 4.2 18.4 0.4 CA A:GLY104 4.2 14.3 0.1 HA2 A:GLY104 4.4 17.1 0.5 CA A:GLY104 4.4 14.3 0.5 O A:ARG21 4.4 16.5 0.3 CE1 A:TYR23 4.5 10.7 0.3 HH12 A:ARG21 4.7 29.0 0.3 N A:GLY104 4.7 12.5 0.4 HE1 A:TYR23 4.7 12.8 0.3 O A:ARG21 4.7 15.7 0.3 O A:ARG21 4.7 16.9 0.3 H A:MET105 4.7 12.2 0.1 H A:MET105 4.8 12.3 0.5 H A:MET105 4.8 14.0 0.4 CD1 A:TYR23 4.8 11.1 0.3 CD2 A:TYR23 4.8 12.1 0.3 CE2 A:TYR23 4.8 9.7 0.3 H A:GLY104 4.9 15.1 0.2 N A:GLY104 4.9 15.3 0.1 CE2 A:TYR23 4.9 14.0 0.3 HB3 A:ARG21 4.9 24.1 0.3 HB3 A:ARG21 5.0 19.5 0.3 CD1 A:TYR23 5.0 11.4 0.3

Chlorine binding site 2 out of 2 in the X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of X-Ray Radiation Damage Series on Lysozyme at 277K, Multi-Conformer Model, Dataset 1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:23.9 occ:0.47 CL A:CL202 0.0 23.9 0.5 CL A:CL202 1.1 19.1 0.5 HH A:TYR23 1.9 15.2 0.3 HH A:TYR23 2.2 14.6 0.3 HH A:TYR23 2.5 15.7 0.3 OH A:TYR23 2.7 12.7 0.3 HA3 A:GLY104 2.7 14.8 0.4 O A:HOH315 2.7 21.6 0.4 HA3 A:GLY104 2.8 17.2 0.1 HE1 A:TYR23 2.9 15.4 0.3 HA3 A:GLY104 2.9 17.1 0.5 HE2 A:TYR23 2.9 14.9 0.3 OH A:TYR23 3.0 12.1 0.3 HA2 A:GLY104 3.0 17.2 0.1 HE1 A:TYR23 3.1 11.9 0.3 HA2 A:GLY104 3.1 14.8 0.4 OH A:TYR23 3.3 13.1 0.3 CA A:GLY104 3.3 12.3 0.4 CA A:GLY104 3.3 14.3 0.1 HA2 A:GLY104 3.4 17.1 0.5 CZ A:TYR23 3.4 10.8 0.3 CE2 A:TYR23 3.5 12.4 0.3 CA A:GLY104 3.6 14.3 0.5 CE1 A:TYR23 3.6 12.8 0.3 CE1 A:TYR23 3.7 9.9 0.3 N A:GLY104 3.7 12.5 0.4 CZ A:TYR23 3.8 10.9 0.3 H A:GLY104 3.8 15.1 0.2 CZ A:TYR23 3.9 10.4 0.3 O A:HOH317 4.0 19.0 0.6 N A:GLY104 4.0 15.3 0.1 O A:HOH315 4.2 21.7 0.6 N A:GLY104 4.2 15.2 0.5 HH12 A:ARG21 4.2 29.0 0.3 H A:GLY104 4.2 18.3 0.2 H A:GLY104 4.4 18.3 0.3 H A:MET105 4.4 12.3 0.5 H A:MET105 4.4 12.2 0.1 HB3 A:ARG21 4.4 24.1 0.3 H A:MET105 4.5 14.0 0.4 NH1 A:ARG21 4.5 24.1 0.3 C A:ASN103 4.5 13.5 0.2 O A:ARG21 4.5 16.5 0.3 C A:GLY104 4.6 12.9 0.1 C A:ASN103 4.6 13.4 0.3 C A:GLY104 4.6 12.2 0.4 HB3 A:ARG21 4.6 23.9 0.3 HH11 A:ARG21 4.6 29.0 0.3 HB3 A:ARG21 4.6 19.5 0.3 O A:ASN103 4.7 12.8 0.3 CE1 A:TYR23 4.7 10.7 0.3 C A:ASN103 4.7 12.7 0.2 CD2 A:TYR23 4.7 12.1 0.3 HG22 A:VAL99 4.7 17.7 0.4 O A:ARG21 4.8 16.9 0.3 O A:ASN103 4.8 13.4 0.2 C A:GLY104 4.8 12.1 0.5 CD1 A:TYR23 4.8 11.1 0.3 N A:MET105 4.8 10.2 0.3 HG22 A:VAL99 4.8 16.8 0.2 C A:ASN103 4.9 13.0 0.3 O A:VAL99 4.9 13.5 0.4 N A:MET105 4.9 11.7 0.4 N A:MET105 4.9 10.3 0.3 O A:VAL99 4.9 16.5 0.2 O A:GLY102 4.9 21.7 0.5 O A:VAL99 4.9 16.2 0.4 O A:ARG21 4.9 15.7 0.3

F.Yabukarski, T.Doukov, D.A.Mokhtari, S.Du, D.Herschlag. Evaluating the Impact of X-Ray Damage on Conformational Heterogeneity in Room-Temperature (277 K) and Cryo-Cooled Protein Crystals. Acta Crystallogr D Struct V. 78 945 2022BIOL.
ISSN: ISSN 2059-7983
PubMed: 35916220
DOI: 10.1107/S2059798322005939