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Fluorine in PDB 2q6p: The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein

Protein crystallography data

The structure of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein, PDB code: 2q6p was solved by T.Steiner, P.Hess, J.H.Bae, B.Wiltschi, L.Moroder, N.Budisa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.94 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.168, 62.556, 69.215, 90.00, 90.00, 90.00
R / Rfree (%) 22.7 / 26

Fluorine Binding Sites:

The binding sites of Fluorine atom in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein (pdb code 2q6p). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 10 binding sites of Fluorine where determined in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein, PDB code: 2q6p:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Fluorine binding site 1 out of 10 in 2q6p

Go back to Fluorine Binding Sites List in 2q6p
Fluorine binding site 1 out of 10 in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein


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Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F13

b:22.0
occ:1.00
 FGX A:4FB13 0.0 22.0 1.0
CGX A:4FB13 1.4 15.0 1.0
CDX A:4FB13 2.2 15.7 1.0
CBX A:4FB13 2.4 15.4 1.0
CA A:4FB13 3.0 13.8 1.0
OG1 A:THR118 3.0 13.8 1.0
N A:4FB13 3.1 14.0 1.0
CA A:THR118 3.1 10.2 1.0
O A:ASP117 3.3 9.9 1.0
O A:4FB13 3.3 12.6 1.0
C A:4FB13 3.4 15.6 1.0
N A:THR118 3.5 11.9 1.0
CB A:THR118 3.5 12.5 1.0
C A:ASP117 3.5 11.6 1.0
CG2 A:THR118 3.9 10.5 1.0
CB A:ASP117 4.3 15.2 1.0
C A:THR118 4.4 10.2 1.0
C A:VAL12 4.4 10.0 1.0
N A:ILE14 4.5 13.3 1.0
N A:LEU119 4.6 9.7 1.0
CA A:ASP117 4.6 13.2 1.0
CG1 A:VAL12 4.7 7.2 1.0
O A:HOH261 4.7 25.8 1.0

Fluorine binding site 2 out of 10 in 2q6p

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Fluorine binding site 2 out of 10 in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein


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Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F54

b:22.7
occ:1.00
 FGX A:4FB54 0.0 22.7 1.0
CGX A:4FB54 1.4 17.6 1.0
CDX A:4FB54 2.3 15.4 1.0
CBX A:4FB54 2.4 16.0 1.0
C A:4FB54 2.9 15.6 1.0
CA A:4FB54 3.0 14.6 1.0
CD1 A:PHE27 3.0 10.8 1.0
CE1 A:PHE27 3.1 13.5 1.0
N A:4FB54 3.1 13.0 1.0
N A:VAL55 3.4 9.4 1.0
O A:4FB54 3.6 12.4 1.0
CG1 A:VAL55 3.7 10.5 1.0
CG A:PHE27 3.9 12.4 1.0
CG2 A:VAL55 4.0 12.4 1.0
O A:HIS25 4.0 13.7 1.0
CZ A:PHE27 4.0 11.2 1.0
CB A:VAL55 4.2 10.7 1.0
CB A:HIS25 4.3 12.2 1.0
CB A:VAL22 4.3 9.6 1.0
C A:LEU53 4.4 13.6 1.0
CA A:VAL55 4.4 10.3 1.0
CG2 A:VAL22 4.4 9.2 1.0
CD2 A:PHE27 4.7 8.7 1.0
CB A:PHE27 4.7 10.2 1.0
CE2 A:PHE27 4.7 11.5 1.0
C A:HIS25 4.8 14.8 1.0
O A:HOH301 4.9 15.2 1.0

Fluorine binding site 3 out of 10 in 2q6p

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Fluorine binding site 3 out of 10 in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F56

b:23.4
occ:1.00
 FGX A:4FB56 0.0 23.4 1.0
CGX A:4FB56 1.4 14.7 1.0
CDX A:4FB56 2.4 13.8 1.0
CBX A:4FB56 2.4 14.1 1.0
CD1 A:LEU141 3.1 10.4 1.0
O A:ASN135 3.1 7.6 1.0
CG A:LEU141 3.2 10.1 1.0
O A:HOH256 3.4 13.1 1.0
CB A:LEU141 3.5 10.9 1.0
CA A:ILE136 3.6 9.2 1.0
N A:4FB56 3.6 11.5 1.0
O A:ILE136 3.6 9.6 1.0
CA A:4FB56 3.6 11.7 1.0
N A:LEU141 3.9 12.1 1.0
C A:ASN135 4.0 9.8 1.0
CG2 A:THR59 4.0 8.7 1.0
C A:ILE136 4.1 9.3 1.0
CA A:HIS139 4.1 12.6 1.0
N A:LYS140 4.2 13.7 1.0
N A:ILE136 4.2 9.0 1.0
CA A:LEU141 4.3 9.6 1.0
FGX A:4FB58 4.4 17.2 1.0
CB A:ILE136 4.5 8.4 1.0
C A:HIS139 4.5 13.1 1.0
CG2 A:ILE136 4.6 7.0 1.0
CD2 A:LEU141 4.6 6.3 1.0
CG1 A:ILE136 4.6 8.1 1.0
N A:HIS139 4.6 13.6 1.0
C A:4FB56 4.8 10.6 1.0
C A:VAL55 4.8 10.3 1.0
O A:HOH272 4.9 12.4 1.0
C A:LYS140 5.0 12.3 1.0

Fluorine binding site 4 out of 10 in 2q6p

Go back to Fluorine Binding Sites List in 2q6p
Fluorine binding site 4 out of 10 in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F58

b:17.2
occ:1.00
 FGX A:4FB58 0.0 17.2 1.0
CGX A:4FB58 1.4 12.1 1.0
CBX A:4FB58 2.4 11.2 1.0
CDX A:4FB58 2.4 9.3 1.0
N A:4FB58 3.0 10.1 1.0
CA A:4FB58 3.0 10.4 1.0
N A:THR59 3.2 8.3 1.0
CBX A:4FB56 3.2 14.1 1.0
C A:4FB58 3.4 11.6 1.0
CG2 A:THR59 3.8 8.7 1.0
CB A:LEU141 3.8 10.9 1.0
CD1 A:LEU141 3.9 10.4 1.0
C A:4FB56 3.9 10.6 1.0
O A:4FB56 4.0 8.6 1.0
C A:TRP57 4.1 10.1 1.0
O A:HOH271 4.1 15.0 1.0
CA A:4FB56 4.2 11.7 1.0
O A:GLU142 4.2 8.9 1.0
N A:TRP57 4.2 8.4 1.0
CA A:THR59 4.3 6.1 1.0
O A:HOH312 4.3 17.7 1.0
O A:4FB58 4.4 11.2 1.0
CGX A:4FB56 4.4 14.7 1.0
FGX A:4FB56 4.4 23.4 1.0
ND1 A:HIS169 4.4 3.7 1.0
CG A:LEU141 4.5 10.1 1.0
CB A:THR59 4.6 9.5 1.0
O A:HOH244 4.6 5.1 1.0
CE1 A:HIS169 4.7 5.1 1.0
CA A:TRP57 4.8 8.2 1.0
O A:LEU141 4.9 9.5 1.0
O A:TRP57 4.9 9.7 1.0
C A:LEU141 4.9 11.1 1.0
CG A:HIS169 5.0 4.9 1.0

Fluorine binding site 5 out of 10 in 2q6p

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Fluorine binding site 5 out of 10 in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F75

b:35.0
occ:1.00
 FGX A:4FB75 0.0 35.0 1.0
CGX A:4FB75 1.4 26.4 1.0
CDX A:4FB75 2.4 24.9 1.0
CBX A:4FB75 2.5 24.4 1.0
CG A:MET78 2.6 25.0 1.0
CB A:MET78 2.7 24.1 1.0
SD A:MET78 2.9 27.0 1.0
CA A:4FB75 3.0 22.1 1.0
CE1 A:HIS77 3.1 19.4 1.0
N A:4FB75 3.2 22.0 1.0
C A:4FB75 3.2 18.5 1.0
ND1 A:HIS77 3.3 20.8 1.0
N A:MET78 3.3 23.8 1.0
O A:4FB75 3.4 16.0 1.0
NE2 A:HIS77 3.5 18.5 1.0
CA A:MET78 3.6 23.4 1.0
CG A:HIS77 3.8 20.4 1.0
CD2 A:HIS77 3.9 19.2 1.0
C A:HIS77 3.9 21.9 1.0
N A:HIS77 4.2 21.3 1.0
C A:TYR74 4.2 14.1 1.0
N A:ASP76 4.2 23.3 1.0
CA A:HIS77 4.4 22.4 1.0
CE A:MET78 4.6 19.7 1.0
O A:HIS77 4.6 22.3 1.0
C A:MET78 4.6 23.7 1.0
C A:ASP76 4.7 21.8 1.0
CB A:HIS77 4.7 22.3 1.0
O A:ALA226 4.8 16.3 1.0
CA A:TYR74 4.9 12.0 1.0
O A:TYR74 4.9 15.6 1.0

Fluorine binding site 6 out of 10 in 2q6p

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Fluorine binding site 6 out of 10 in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F89

b:18.9
occ:1.00
 FGX A:4FB89 0.0 18.9 1.0
CGX A:4FB89 1.4 15.2 1.0
CBX A:4FB89 2.5 13.2 1.0
CDX A:4FB89 2.5 15.4 1.0
N A:GLU90 2.9 16.8 1.0
CA A:4FB89 3.0 12.7 1.0
C A:4FB89 3.0 13.2 1.0
N A:4FB89 3.1 10.2 1.0
OE2 A:GLU90 3.3 33.2 1.0
O A:HOH327 3.3 22.8 1.0
CD A:GLU90 3.5 27.3 1.0
O A:4FB89 3.8 14.2 1.0
CA A:GLU90 3.9 17.1 1.0
OE1 A:GLU90 3.9 27.6 1.0
CG A:GLU90 4.0 24.7 1.0
C A:MET88 4.4 10.0 1.0
O A:HOH286 4.4 27.1 1.0
CB A:GLU90 4.5 19.4 1.0
O A:MET88 4.9 10.4 1.0

Fluorine binding site 7 out of 10 in 2q6p

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Fluorine binding site 7 out of 10 in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F187

b:24.6
occ:1.00
 FGX A:4FB187 0.0 24.6 1.0
CGX A:4FB187 1.4 24.6 1.0
CDX A:4FB187 2.5 22.7 1.0
CBX A:4FB187 2.5 23.1 1.0
O A:4FB187 2.9 16.2 1.0
CA A:4FB187 3.0 22.1 1.0
N A:4FB187 3.1 22.0 1.0
C A:4FB187 3.2 20.3 1.0
O A:HOH282 3.4 20.7 1.0
O A:GLY189 3.5 18.9 1.0
ND2 A:ASN159 3.8 27.4 1.0
C A:THR186 4.2 16.6 1.0
N A:ILE188 4.2 14.7 1.0
O A:ASN159 4.4 25.6 1.0
C A:GLY189 4.7 21.4 1.0
CG A:ASN159 4.8 25.7 1.0
CA A:THR186 4.9 17.4 1.0
CB A:THR186 4.9 18.9 1.0
O A:THR186 5.0 14.2 1.0
CB A:ASN159 5.0 27.3 1.0

Fluorine binding site 8 out of 10 in 2q6p

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Fluorine binding site 8 out of 10 in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F192

b:24.1
occ:1.00
 FGX A:4FB192 0.0 24.1 1.0
CGX A:4FB192 1.4 20.5 1.0
CBX A:4FB192 2.5 18.7 1.0
CDX A:4FB192 2.5 20.5 1.0
O A:4FB192 2.9 13.9 1.0
O A:HOH354 3.0 26.5 1.0
CA A:4FB192 3.0 18.1 1.0
N A:4FB192 3.1 20.2 1.0
C A:4FB192 3.2 16.0 1.0
C A:GLY191 4.2 19.7 1.0
N A:VAL193 4.2 17.4 1.0
CA A:GLY191 4.9 19.8 1.0
O A:GLY191 5.0 18.0 1.0

Fluorine binding site 9 out of 10 in 2q6p

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Fluorine binding site 9 out of 10 in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F196

b:26.6
occ:1.00
 FGX A:4FB196 0.0 26.6 1.0
CGX A:4FB196 1.4 25.9 1.0
CBX A:4FB196 2.5 24.3 1.0
CDX A:4FB196 2.6 25.6 1.0
O A:4FB196 2.9 24.8 1.0
CA A:4FB196 3.1 24.8 1.0
C A:4FB196 3.1 24.6 1.0
N A:4FB196 3.2 24.4 1.0
N A:ALA154 3.4 27.4 1.0
C A:MET153 3.6 26.9 1.0
CG2 A:ILE152 3.6 14.4 1.0
CG2 A:ILE161 3.7 10.0 1.0
CA A:ALA154 3.7 27.7 1.0
O A:ASP197 3.7 24.9 1.0
CB A:ALA154 3.8 28.0 1.0
O A:MET153 4.0 24.4 1.0
CA A:MET153 4.2 26.6 1.0
N A:ASP197 4.2 26.1 1.0
O A:HOH335 4.2 19.5 1.0
CE1 A:HIS199 4.3 15.3 1.0
C A:LEU195 4.3 22.5 1.0
N A:MET153 4.3 24.1 1.0
C A:ASP197 4.5 26.6 1.0
ND1 A:HIS199 4.5 18.0 1.0
C A:ILE152 4.6 21.4 1.0
CB A:ILE161 4.6 11.0 1.0
O A:HOH239 4.6 3.8 1.0
O A:ILE152 4.7 20.9 1.0
CB A:ILE152 4.9 17.4 1.0
CA A:LEU195 4.9 22.4 1.0
CA A:ASP197 4.9 26.4 1.0

Fluorine binding site 10 out of 10 in 2q6p

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Fluorine binding site 10 out of 10 in the The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 10 of The Chemical Control of Protein Folding: Engineering A Superfolder Green Fluorescent Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F211

b:28.2
occ:1.00
 FGX A:4FB211 0.0 28.2 1.0
CGX A:4FB211 1.4 26.0 1.0
CDX A:4FB211 2.3 23.7 1.0
CBX A:4FB211 2.5 24.7 1.0
CA A:4FB211 3.1 25.4 1.0
OD1 A:ASN212 3.1 32.5 1.0
N A:4FB211 3.1 21.8 1.0
C A:4FB211 3.2 26.5 1.0
N A:ASN212 3.4 25.6 1.0
CG A:ASN212 3.5 30.4 1.0
OD1 A:ASP210 3.8 14.9 1.0
ND2 A:ASN212 3.9 30.6 1.0
O A:4FB211 4.0 27.8 1.0
C A:ASP210 4.2 18.1 1.0
CB A:ASN212 4.3 27.3 1.0
CA A:ASN212 4.4 24.1 1.0
CA A:ASP210 5.0 17.3 1.0
O A:ASP210 5.0 16.7 1.0

Reference:

T.Steiner, P.Hess, J.H.Bae, B.Wiltschi, L.Moroder, N.Budisa. Synthetic Biology of Proteins: Tuning Gfps Folding and Stability with Fluoroproline. Plos One V. 3 E1680 2008.
ISSN: ESSN 1932-6203
PubMed: 18301757
DOI: 10.1371/JOURNAL.PONE.0001680
Page generated: Wed Jul 31 15:44:15 2024

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