Fluorine in PDB 2a9n: A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex

The structure of A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex, PDB code: 2a9n was solved by C.Cambillau, S.Spinelli, A.Honegger, A.Pluckthun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.00 / 3.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	81.382, 100.460, 61.749, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 26.6

The binding sites of Fluorine atom in the A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex (pdb code 2a9n). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex, PDB code: 2a9n:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex within 5.0Å range: probe atom residue distance (Å) B Occ H:F149 b:36.5 occ:1.00 F2 H:ORE149 0.0 36.5 1.0 C7 H:ORE149 1.3 35.1 1.0 C8 H:ORE149 2.3 35.0 1.0 C6 H:ORE149 2.4 34.7 1.0 O3 H:ORE149 2.7 34.2 1.0 CA H:GLY57 3.2 33.7 1.0 C H:GLY57 3.3 33.7 1.0 ND1 H:HIS69 3.5 37.7 1.0 O H:GLY57 3.7 33.1 1.0 C9 H:ORE149 3.7 34.6 1.0 N H:LEU58 3.7 34.2 1.0 C5 H:ORE149 3.7 35.0 1.0 CG H:HIS69 3.8 36.5 1.0 N H:GLY57 3.8 33.6 1.0 CZ2 H:TRP54 4.0 33.1 1.0 CE1 H:HIS69 4.0 38.0 1.0 NH1 H:ARG109 4.0 35.5 1.0 CB H:HIS69 4.1 35.6 1.0 C4 H:ORE149 4.2 33.9 1.0 CD2 H:HIS69 4.4 36.8 1.0 N H:HIS69 4.4 35.1 1.0 NE2 H:HIS69 4.5 38.0 1.0 O H:HIS69 4.5 34.8 1.0 NH2 H:ARG109 4.6 35.1 1.0 CA H:LEU58 4.6 34.7 1.0 C H:ALA56 4.7 33.4 1.0 CZ H:ARG109 4.7 34.6 1.0 C H:LEU58 4.7 35.0 1.0 CA H:HIS69 4.8 35.3 1.0 C10 H:ORE149 4.8 35.0 1.0 CE2 H:TRP54 4.8 33.1 1.0 O4 H:ORE149 4.8 34.2 1.0 O H:MET41 4.8 32.6 1.0 CH2 H:TRP54 4.8 33.9 1.0 NE1 H:TRP54 4.9 32.9 1.0 O H:LEU58 4.9 35.0 1.0 CZ3 L:TRP109 4.9 33.3 1.0 CH2 L:TRP109 5.0 33.2 1.0 C14 H:ORE149 5.0 34.4 1.0

Fluorine binding site 2 out of 4 in the A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex within 5.0Å range: probe atom residue distance (Å) B Occ H:F149 b:36.1 occ:1.00 F1 H:ORE149 0.0 36.1 1.0 C13 H:ORE149 1.3 35.6 1.0 C12 H:ORE149 2.3 35.0 1.0 C1 H:ORE149 2.5 36.0 1.0 O1 H:ORE149 2.8 36.7 1.0 O H:GLY130 3.2 35.0 1.0 C11 H:ORE149 3.6 34.7 1.0 C2 H:ORE149 3.7 35.0 1.0 CA H:HIS131 3.8 35.1 1.0 ND1 H:HIS131 3.8 34.0 1.0 CG H:HIS131 3.9 34.7 1.0 C H:GLY130 4.1 35.5 1.0 CE1 H:HIS131 4.1 34.5 1.0 C3 H:ORE149 4.1 34.3 1.0 CB H:HIS131 4.2 35.1 1.0 CD2 H:HIS131 4.2 35.0 1.0 OD1 L:ASN39 4.3 35.8 1.0 NE2 H:HIS131 4.4 34.6 1.0 N H:HIS131 4.4 35.4 1.0 CB L:TRP109 4.5 34.2 1.0 CG L:TRP109 4.7 34.0 1.0 CD1 L:TRP109 4.7 33.7 1.0 C H:HIS131 4.8 35.0 1.0 C10 H:ORE149 4.8 35.0 1.0

Fluorine binding site 3 out of 4 in the A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex within 5.0Å range: probe atom residue distance (Å) B Occ I:F149 b:32.5 occ:1.00 F2 I:ORE149 0.0 32.5 1.0 C7 I:ORE149 1.3 32.2 1.0 C8 I:ORE149 2.3 32.1 1.0 C6 I:ORE149 2.4 32.3 1.0 O3 I:ORE149 2.8 33.4 1.0 ND1 I:HIS131 3.0 34.0 1.0 O I:GLY130 3.5 34.4 1.0 CG I:HIS131 3.5 33.7 1.0 C9 I:ORE149 3.6 31.7 1.0 CE1 I:HIS131 3.7 33.1 1.0 CA I:HIS131 3.7 34.2 1.0 C5 I:ORE149 3.7 31.6 1.0 CB I:HIS131 3.8 34.0 1.0 C4 I:ORE149 4.1 31.5 1.0 C I:GLY130 4.4 34.7 1.0 CD2 I:HIS131 4.4 32.9 1.0 NE2 I:HIS131 4.4 33.2 1.0 N I:HIS131 4.5 34.6 1.0 CB M:TRP109 4.5 32.6 1.0 OD1 M:ASN39 4.5 34.9 1.0 CG M:TRP109 4.7 32.2 1.0 C10 I:ORE149 4.8 32.1 1.0 CD1 M:TRP109 4.8 32.2 1.0 C I:HIS131 4.8 34.0 1.0

Fluorine binding site 4 out of 4 in the A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex within 5.0Å range: probe atom residue distance (Å) B Occ I:F149 b:29.4 occ:1.00 F1 I:ORE149 0.0 29.4 1.0 C13 I:ORE149 1.3 31.2 1.0 C1 I:ORE149 2.4 32.0 1.0 C12 I:ORE149 2.4 31.9 1.0 O1 I:ORE149 2.7 32.0 1.0 CA I:GLY57 3.1 32.8 1.0 C I:GLY57 3.3 32.8 1.0 CB I:HIS69 3.6 35.1 1.0 N I:GLY57 3.6 32.7 1.0 C2 I:ORE149 3.7 32.9 1.0 C11 I:ORE149 3.7 31.9 1.0 NH1 I:ARG109 3.8 33.7 1.0 N I:LEU58 3.8 32.9 1.0 O I:GLY57 3.8 32.7 1.0 CD2 I:HIS69 3.9 36.0 1.0 CZ2 I:TRP54 3.9 33.2 1.0 CG I:HIS69 4.0 36.0 1.0 C3 I:ORE149 4.2 32.4 1.0 NE1 I:TRP54 4.4 32.6 1.0 C I:ALA56 4.5 32.9 1.0 O I:LEU58 4.5 33.4 1.0 CE2 I:TRP54 4.6 33.2 1.0 CZ I:ARG109 4.6 33.6 1.0 O I:HIS69 4.6 34.9 1.0 NH2 I:ARG109 4.6 33.5 1.0 C I:LEU58 4.7 33.4 1.0 CA I:LEU58 4.7 33.2 1.0 CA I:HIS69 4.7 34.9 1.0 N I:HIS69 4.8 34.9 1.0 O5 I:ORE149 4.8 34.1 1.0 O I:ALA56 4.8 32.6 1.0 O I:MET41 4.8 32.4 1.0 C10 I:ORE149 5.0 32.1 1.0 CH2 I:TRP54 5.0 33.8 1.0

A.Honegger, S.Spinelli, C.Cambillau, A.Pluckthun. A Mutation Designed to Alter Crystal Packing Permits Structural Analysis of A Tight-Binding Fluorescein-Scfv Complex. Protein Sci. V. 14 2537 2005.
ISSN: ISSN 0961-8368
PubMed: 16195545
DOI: 10.1110/PS.051520605