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Bromine in PDB 4fbs: Structure of Monomeric Nt From Euprosthenops Australis Major Ampullate Spidroin 1 (MASP1)

Protein crystallography data

The structure of Structure of Monomeric Nt From Euprosthenops Australis Major Ampullate Spidroin 1 (MASP1), PDB code: 4fbs was solved by G.Askarieh, M.Hedhammar, A.Rising, J.Johansson, S.D.Knight, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.44 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.650, 33.244, 44.752, 90.00, 115.37, 90.00
R / Rfree (%) 14.2 / 19.6

Bromine Binding Sites:

The binding sites of Bromine atom in the Structure of Monomeric Nt From Euprosthenops Australis Major Ampullate Spidroin 1 (MASP1) (pdb code 4fbs). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Structure of Monomeric Nt From Euprosthenops Australis Major Ampullate Spidroin 1 (MASP1), PDB code: 4fbs:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in 4fbs

Go back to Bromine Binding Sites List in 4fbs
Bromine binding site 1 out of 2 in the Structure of Monomeric Nt From Euprosthenops Australis Major Ampullate Spidroin 1 (MASP1)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of Monomeric Nt From Euprosthenops Australis Major Ampullate Spidroin 1 (MASP1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br201

b:17.4
occ:0.50
O A:HOH410 3.0 38.9 1.0

Bromine binding site 2 out of 2 in 4fbs

Go back to Bromine Binding Sites List in 4fbs
Bromine binding site 2 out of 2 in the Structure of Monomeric Nt From Euprosthenops Australis Major Ampullate Spidroin 1 (MASP1)


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Structure of Monomeric Nt From Euprosthenops Australis Major Ampullate Spidroin 1 (MASP1) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br202

b:17.9
occ:0.50
O A:HOH317 3.0 18.2 1.0
HA2 A:GLY26 3.2 13.6 1.0
O A:HOH322 3.2 26.1 1.0
HE22 A:GLN107 3.4 29.8 0.4
HB3 A:GLN25 3.6 14.7 1.0
CA A:GLY26 3.9 11.3 1.0
NE2 A:GLN107 3.9 24.8 0.4
HE21 A:GLN107 3.9 29.8 0.4
N A:GLY26 4.0 9.0 1.0
HB2 A:GLN25 4.0 14.7 1.0
O A:HOH314 4.0 19.3 1.0
HA3 A:GLY26 4.1 13.6 1.0
C A:GLN25 4.1 9.4 1.0
O A:HOH391 4.2 33.7 1.0
CB A:GLN25 4.2 12.2 1.0
H A:GLY26 4.2 10.8 1.0
O A:GLN25 4.3 9.5 1.0
O A:HOH312 4.5 17.4 1.0
O A:HOH313 4.7 14.0 1.0
HG A:SER22 4.7 9.8 0.7
O A:HOH301 4.8 8.8 1.0
CA A:GLN25 4.8 9.3 1.0
OE1 A:GLN25 4.9 26.9 1.0
O A:SER22 4.9 7.4 1.0

Reference:

K.Jaudzems, G.Askarieh, M.Landreh, K.Nordling, M.Hedhammar, H.Jornvall, A.Rising, S.D.Knight, J.Johansson. pH-Dependent Dimerization of Spider Silk N-Terminal Domain Requires Relocation of A Wedged Tryptophan Side Chain J.Mol.Biol. 2012.
ISSN: ESSN 1089-8638
PubMed: 22706024
DOI: 10.1016/J.JMB.2012.06.004
Page generated: Wed Jul 10 21:14:26 2024

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