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Green fluorescent protein

 GFP_AEQVI               Reviewed;         238 AA.
P42212; Q17104; Q27903; Q93125;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
22-NOV-2017, entry version 145.
RecName: Full=Green fluorescent protein;
Name=GFP;
Aequorea victoria (Jellyfish).
Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Leptothecata;
Aequoreidae; Aequorea.
NCBI_TaxID=6100;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANTS
TYR-100; SER-108; MET-141 AND ILE-219.
PubMed=1347277; DOI=10.1016/0378-1119(92)90691-H;
Prasher D.C., Eckenrode V.K., Ward W.W., Prendergast F.G.,
Cormier M.J.;
"Primary structure of the Aequorea victoria green-fluorescent
protein.";
Gene 111:229-233(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8137953; DOI=10.1016/0014-5793(94)80472-9;
Inouye S., Tsuji F.I.;
"Aequorea green fluorescent protein. Expression of the gene and
fluorescence characteristics of the recombinant protein.";
FEBS Lett. 341:277-280(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES, AND
BIOTECHNOLOGY.
PubMed=9154981; DOI=10.1023/A:1005740823703;
Rouwendal G.J.A., Mendes O., Wolbert E.J.H., de Boer A.D.;
"Enhanced expression in tobacco of the gene encoding green fluorescent
protein by modification of its codon usage.";
Plant Mol. Biol. 33:989-999(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], BIOTECHNOLOGY, AND MUTAGENESIS OF
PHE-64; SER-65; VAL-68 AND SER-72.
PubMed=8707053; DOI=10.1016/0378-1119(95)00685-0;
Cormack B.P., Valdivia R.H., Falkow S.;
"FACS-optimized mutants of the green fluorescent protein (GFP).";
Gene 173:33-38(1996).
[5]
CHROMOPHORE, AND DEHYDROGENATION AT TYR-66.
PubMed=8448132; DOI=10.1021/bi00056a003;
Cody C.W., Prasher D.C., Westler W.M., Prendergast F.G., Ward W.W.;
"Chemical structure of the hexapeptide chromophore of the Aequorea
green-fluorescent protein.";
Biochemistry 32:1212-1218(1993).
[6]
MUTAGENESIS OF TYR-66; ILE-167; SER-202 AND THR-203.
PubMed=7809066; DOI=10.1073/pnas.91.26.12501;
Heim R., Prasher D.C., Tsien R.Y.;
"Wavelength mutations and posttranslational autoxidation of green
fluorescent protein.";
Proc. Natl. Acad. Sci. U.S.A. 91:12501-12504(1994).
[7]
MUTAGENESIS OF PHE-64; SER-65 AND GLN-69.
PubMed=9634755; DOI=10.1038/nbt0295-151;
Delagrave S., Hawtin R.E., Silva C.M., Yang M.M., Youvan D.C.;
"Red-shifted excitation mutants of the green fluorescent protein.";
Biotechnology (N.Y.) 13:151-154(1995).
[8]
MUTAGENESIS OF THR-203 AND GLU-222.
PubMed=7796912; DOI=10.1016/0014-5793(95)00557-P;
Ehrig T., O'Kane D.J., Prendergast F.G.;
"Green-fluorescent protein mutants with altered fluorescence
excitation spectra.";
FEBS Lett. 367:163-166(1995).
[9]
MUTAGENESIS OF TYR-66, AND BIOTECHNOLOGY.
PubMed=8578587; DOI=10.1016/S0968-0004(00)89099-4;
Cubitt A.B., Heim R., Adams S.R., Boyd A.E., Gross L.A., Tsien R.Y.;
"Understanding, improving and using green fluorescent proteins.";
Trends Biochem. Sci. 20:448-455(1995).
[10]
MUTAGENESIS OF VAL-163 AND SER-175.
PubMed=8994830; DOI=10.1016/S0960-9822(02)70789-6;
Siemering K.R., Golbik R., Sever R., Haseloff J.;
"Mutations that suppress the thermosensitivity of green fluorescent
protein.";
Curr. Biol. 6:1653-1663(1996).
[11]
MUTAGENESIS OF PHE-99; MET-153 AND VAL-163.
PubMed=9630892; DOI=10.1038/nbt0396-315;
Crameri A., Whitehorn E.A., Tate E., Stemmer W.P.;
"Improved green fluorescent protein by molecular evolution using DNA
shuffling.";
Nat. Biotechnol. 14:315-319(1996).
[12]
MUTAGENESIS OF PHE-99; MET-153 AND VAL-163.
PubMed=9631088; DOI=10.1038/nbt1096-1252;
Yokoe H., Meyer T.;
"Spatial dynamics of GFP-tagged proteins investigated by local
fluorescence enhancement.";
Nat. Biotechnol. 14:1252-1256(1996).
[13]
MUTAGENESIS OF SER-147.
PubMed=9125154; DOI=10.1006/bbrc.1997.6235;
Kimata Y., Iwaki M., Lim C.R., Kohno K.;
"A novel mutation which enhances the fluorescence of green fluorescent
protein at high temperatures.";
Biochem. Biophys. Res. Commun. 232:69-73(1997).
[14]
MUTAGENESIS OF PHE-64; SER-65; TYR-66; PHE-99; MET-153 AND VAL-163.
PubMed=9370472; DOI=10.1016/S0006-3495(97)78307-3;
Patterson G.H., Knobel S.M., Sharif W.D., Kain S.R., Piston D.W.;
"Use of the green fluorescent protein and its mutants in quantitative
fluorescence microscopy.";
Biophys. J. 73:2782-2790(1997).
[15]
REVIEW ON MUTAGENESIS, AND BIOTECHNOLOGY.
PubMed=9759496; DOI=10.1146/annurev.biochem.67.1.509;
Tsien R.Y.;
"The green fluorescent protein.";
Annu. Rev. Biochem. 67:509-544(1998).
[16]
MUTAGENESIS OF SER-65; VAL-68; SER-72; ASN-146; MET-153; VAL-163 AND
THR-203.
PubMed=11299042; DOI=10.1186/1471-213X-1-4;
Srinivas S., Watanabe T., Lin C.S., William C.M., Tanabe Y.,
Jessell T.M., Costantini F.;
"Cre reporter strains produced by targeted insertion of EYFP and ECFP
into the ROSA26 locus.";
BMC Dev. Biol. 1:4-4(2001).
[17]
MUTAGENESIS OF PHE-64 AND SER-65.
PubMed=11776264;
Baumstark-Khan C., Hellweg C.E., Palm M., Horneck G.;
"Enhanced green fluorescent protein (EGFP) for space radiation
research using mammalian cells in the International Space Station.";
Phys. Med. 17:210-214(2001).
[18]
MUTAGENESIS OF SER-72; TYR-145 AND THR-203.
PubMed=12769828; DOI=10.1186/1472-6750-3-5;
Zapata-Hommer O., Griesbeck O.;
"Efficiently folding and circularly permuted variants of the Sapphire
mutant of GFP.";
BMC Biotechnol. 3:5-5(2003).
[19]
MUTAGENESIS OF PHE-64; SER-65; TYR-66; ASN-146; MET-153 AND VAL-163.
PubMed=15065907; DOI=10.1117/1.1646416;
Wang Z., Shah J.V., Chen Z., Sun C.H., Berns M.W.;
"Fluorescence correlation spectroscopy investigation of a GFP mutant-
enhanced cyan fluorescent protein and its tubulin fusion in living
cells with two-photon excitation.";
J. Biomed. Opt. 9:395-403(2004).
[20]
MUTAGENESIS OF PHE-64; SER-65; TYR-66; SER-72; TYR-145; ASN-146;
HIS-148; MET-153 AND VAL-163.
PubMed=14990965; DOI=10.1038/nbt945;
Rizzo M.A., Springer G.H., Granada B., Piston D.W.;
"An improved cyan fluorescent protein variant useful for FRET.";
Nat. Biotechnol. 22:445-449(2004).
[21]
MUTAGENESIS OF SER-30; PHE-46; GLN-69; ASP-103; TYR-145; VAL-176;
VAL-193 AND ASN-198.
PubMed=16201762; DOI=10.1021/bi050550f;
Scruggs A.W., Flores C.L., Wachter R., Woodbury N.W.;
"Development and characterization of green fluorescent protein mutants
with altered lifetimes.";
Biochemistry 44:13377-13384(2005).
[22]
MUTAGENESIS OF ALA-206.
PubMed=16739159; DOI=10.1002/cphc.200600057;
Grailhe R., Merola F., Ridard J., Couvignou S., Le Poupon C.,
Changeux J.P., Laguitton-Pasquier H.;
"Monitoring protein interactions in the living cell through the
fluorescence decays of the cyan fluorescent protein.";
ChemPhysChem 7:1442-1454(2006).
[23]
MUTAGENESIS OF PHE-64; SER-65; SER-72; ASN-149; MET-153 AND ILE-167.
PubMed=17658219; DOI=10.1016/j.bbagen.2007.06.005;
Teerawanichpan P., Hoffman T., Ashe P., Datla R., Selvaraj G.;
"Investigations of combinations of mutations in the jellyfish green
fluorescent protein (GFP) that afford brighter fluorescence, and use
of a version (VisGreen) in plant, bacterial, and animal cells.";
Biochim. Biophys. Acta 1770:1360-1368(2007).
[24]
BIOTECHNOLOGY.
PubMed=17685514; DOI=10.1021/ja0715905;
Wong F.H., Banks D.S., Abu-Arish A., Fradin C.;
"A molecular thermometer based on fluorescent protein blinking.";
J. Am. Chem. Soc. 129:10302-10303(2007).
[25]
MUTAGENESIS OF PHE-46; PHE-64; VAL-68; LYS-162; VAL-163; ILE-167 AND
ILE-171.
PubMed=18366185; DOI=10.1021/bi702130s;
Mishin A.S., Subach F.V., Yampolsky I.V., King W., Lukyanov K.A.,
Verkhusha V.V.;
"The first mutant of the Aequorea victoria green fluorescent protein
that forms a red chromophore.";
Biochemistry 47:4666-4673(2008).
[26]
MUTAGENESIS OF SER-30; TYR-39; TYR-66; SER-72; GLN-80; ASN-105;
ILE-128; TYR-145; VAL-150; ASP-155; ILE-171; ASN-198; ALA-206 AND
VAL-224.
PubMed=22891786; DOI=10.1021/jp306257t;
Park J.W., Rhee Y.M.;
"Interpolated mechanics-molecular mechanics study of internal rotation
dynamics of the chromophore unit in blue fluorescent protein and its
variants.";
J. Phys. Chem. B 116:11137-11147(2012).
[27]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed=9631087; DOI=10.1038/nbt1096-1246;
Yang F., Moss L.G., Phillips G.N. Jr.;
"The molecular structure of green fluorescent protein.";
Nat. Biotechnol. 14:1246-1251(1996).
[28] {ECO:0000244|PDB:1EMA}
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND MUTAGENESIS OF SER-65 AND
THR-203.
PubMed=8703075; DOI=10.1126/science.273.5280.1392;
Ormo M., Cubitt A.B., Kallio K., Gross L.A., Tsien R.Y.,
Remington S.J.;
"Crystal structure of the Aequorea victoria green fluorescent
protein.";
Science 273:1392-1395(1996).
[29] {ECO:0000244|PDB:1EMC, ECO:0000244|PDB:1EME, ECO:0000244|PDB:1EMF, ECO:0000244|PDB:1EMK, ECO:0000244|PDB:1EML, ECO:0000244|PDB:1EMM, ECO:0000244|PDB:2EMD, ECO:0000244|PDB:2EMN, ECO:0000244|PDB:2EMO}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), MUTAGENESIS OF PHE-64; TYR-66;
SER-72; ASN-149; MET-153 AND ILE-167, BIOPHYSICOCHEMICAL PROPERTIES,
AND BIOTECHNOLOGY.
PubMed=9145105; DOI=10.1038/nsb0597-361;
Palm G.J., Zdanov A., Gaitanaris G.A., Stauber R., Pavlakis G.N.,
Wlodawer A.;
"The structural basis for spectral variations in green fluorescent
protein.";
Nat. Struct. Biol. 4:361-365(1997).
[30] {ECO:0000244|PDB:1YFP, ECO:0000244|PDB:2YFP}
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF YELLOW EMISSION MUTANT
TYR-203/GLY-65/LEU-68/ALA-72, MUTAGENESIS OF SER-65; VAL-68; SER-72
AND THR-203, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY, AND
SUBUNIT.
PubMed=9782051; DOI=10.1016/S0969-2126(98)00127-0;
Wachter R.M., Elsliger M.-A., Kallio K., Hanson G.T., Remington S.J.;
"Structural basis of spectral shifts in the yellow-emission variants
of green fluorescent protein.";
Structure 6:1267-1277(1998).
[31]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=10220315; DOI=10.1021/bi9902182;
Elsliger M.-A., Wachter R.M., Hanson G.T., Kallio K., Remington S.J.;
"Structural and spectral response of green fluorescent protein
variants to changes in pH.";
Biochemistry 38:5296-5301(1999).
[32] {ECO:0000244|PDB:1HUY}
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-238 OF MUTANT CITRININE,
AND MUTAGENESIS OF VAL-68; GLN-69; SER-72 AND THR-203.
PubMed=11387331; DOI=10.1074/jbc.M102815200;
Griesbeck O., Baird G.S., Campbell R.E., Zacharias D.A., Tsien R.Y.;
"Reducing the environmental sensitivity of yellow fluorescent protein.
Mechanism and applications.";
J. Biol. Chem. 276:29188-29194(2001).
[33] {ECO:0000244|PDB:1MYW}
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-238 OF VENUS, AND
MUTAGENESIS OF PHE-46; PHE-64; SER-65; VAL-68; SER-72; MET-153;
VAL-163; SER-175 AND THR-203.
PubMed=12370172; DOI=10.1074/jbc.M209524200;
Rekas A., Alattia J.R., Nagai T., Miyawaki A., Ikura M.;
"Crystal structure of venus, a yellow fluorescent protein with
improved maturation and reduced environmental sensitivity.";
J. Biol. Chem. 277:50573-50578(2002).
[34] {ECO:0000244|PDB:2Q57}
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), MUTAGENESIS OF 65-SER-TYR-66,
BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
PubMed=17685554; DOI=10.1021/bi602664c;
Malo G.D., Pouwels L.J., Wang M., Weichsel A., Montfort W.R.,
Rizzo M.A., Piston D.W., Wachter R.M.;
"X-ray structure of Cerulean GFP: a tryptophan-based chromophore
useful for fluorescence lifetime imaging.";
Biochemistry 46:9865-9873(2007).
-!- FUNCTION: Energy-transfer acceptor. Its role is to transduce the
blue chemiluminescence of the protein aequorin into green
fluorescent light by energy transfer. Fluoresces in vivo upon
receiving energy from the Ca(2+)-activated photoprotein aequorin.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=395 nm;
Note=Exhibits a smaller absorbance peak at 470 nm. The
fluorescence emission spectrum peaks at 507-510 nm with a
shoulder at 545 nm (PubMed:8137953, PubMed:9154981). The exact
value of the emission maximum depends on the environment of the
chromophore (PubMed:10220315). As a consequence, mutant versions
have been designed that have substantially shifted emission
spectra, including yellow-emission variants (YFP), blue and
cerulean fluorescing proteins (PubMed:9145105, PubMed:9782051,
PubMed:17685554). {ECO:0000269|PubMed:10220315,
ECO:0000269|PubMed:17685554, ECO:0000269|PubMed:8137953,
ECO:0000269|PubMed:9145105, ECO:0000269|PubMed:9154981,
ECO:0000269|PubMed:9782051};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9782051}.
-!- TISSUE SPECIFICITY: Photocytes.
-!- PTM: Contains a chromophore consisting of modified amino acid
residues. The chromophore is formed by autocatalytic backbone
condensation between Ser-65 and Gly-67, and oxidation of Tyr-66 to
didehydrotyrosine. Maturation of the chromophore requires nothing
other than molecular oxygen. {ECO:0000269|PubMed:8448132}.
-!- BIOTECHNOLOGY: Green fluorescent protein has been engineered to
produce a vast number of variously colored mutants, fusion
proteins, and biosensors. Green fluorescent protein can be mutated
to emit at different wavelengths such as blue for BFP (when Tyr-66
is replaced by His), cyan for CFP (when Tyr-66 is replaced by
Trp), and yellow for YFP (when THR-203 is replaced by Tyr).
Further generation of mutants led to more stable proteins (at 37
degrees Celsius for example) with brighter fluorescence and longer
fluorescence lifetimes. Fluorescent proteins and their mutated
allelic forms have become a useful and ubiquitous tool for making
chimeric proteins, where they function as a fluorescent protein
tag. Typically they tolerate N- and C-terminal fusion to a broad
variety of proteins. They have been expressed in most known cell
types and are used as a noninvasive fluorescent marker in living
cells and organisms. They enable a wide range of applications
where they have functioned as a cell lineage tracer, reporter of
gene expression, or as a measure of protein-protein interactions.
{ECO:0000269|PubMed:17685514, ECO:0000269|PubMed:17685554,
ECO:0000269|PubMed:8578587, ECO:0000269|PubMed:8707053,
ECO:0000269|PubMed:9145105, ECO:0000269|PubMed:9154981,
ECO:0000269|PubMed:9759496, ECO:0000269|PubMed:9782051}.
-!- BIOTECHNOLOGY: Can also be used as a molecular thermometer,
allowing accurate temperature measurements in fluids. The
measurement process relies on the detection of the blinking of GFP
using fluorescence correlation spectroscopy.
{ECO:0000269|PubMed:17685514}.
-!- SIMILARITY: Belongs to the GFP family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The greenest of us all
- Issue 11 of June 2001;
URL="https://web.expasy.org/spotlight/back_issues/011";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Paint my thoughts
- Issue 108 of August 2009;
URL="https://web.expasy.org/spotlight/back_issues/108";
-!- WEB RESOURCE: Name=Wikipedia; Note=Green fluorescent protein
entry;
URL="https://en.wikipedia.org/wiki/Green_fluorescent_protein";
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Paint my thoughts
- Issue 108 of November 2007;
URL="https://web.expasy.org/spotlight/back_issues/108/";
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EMBL; M62654; AAA27722.1; -; mRNA.
EMBL; M62653; AAA27721.1; -; mRNA.
EMBL; L29345; AAA58246.1; -; mRNA.
EMBL; X96418; CAA65278.1; -; mRNA.
EMBL; U73901; AAB18957.1; -; Genomic_DNA.
PIR; JS0692; JQ1514.
PDB; 1B9C; X-ray; 2.40 A; A/B/C/D=1-238.
PDB; 1BFP; X-ray; 2.10 A; A=1-238.
PDB; 1C4F; X-ray; 2.25 A; A=1-238.
PDB; 1CV7; X-ray; 2.50 A; A=1-228.
PDB; 1EMA; X-ray; 1.90 A; A=1-238.
PDB; 1EMB; X-ray; 2.13 A; A=1-238.
PDB; 1EMC; X-ray; 2.30 A; A/B/C/D=2-237.
PDB; 1EME; X-ray; 2.50 A; A=2-237.
PDB; 1EMF; X-ray; 2.40 A; A=2-238.
PDB; 1EMG; X-ray; 2.00 A; A=1-229.
PDB; 1EMK; X-ray; 2.10 A; A=2-237.
PDB; 1EML; X-ray; 2.30 A; A=2-237.
PDB; 1EMM; X-ray; 2.30 A; A=2-238.
PDB; 1F09; X-ray; 2.14 A; A=1-238.
PDB; 1F0B; X-ray; 2.10 A; A=1-238.
PDB; 1GFL; X-ray; 1.90 A; A/B=2-238.
PDB; 1H6R; X-ray; 1.50 A; A/B/C=1-238.
PDB; 1HCJ; X-ray; 1.80 A; A/B/C/D=1-238.
PDB; 1HUY; X-ray; 2.20 A; A=2-238.
PDB; 1JBY; X-ray; 1.80 A; A=1-238.
PDB; 1JBZ; X-ray; 1.50 A; A=1-238.
PDB; 1JC0; X-ray; 2.00 A; A/B/C=1-238.
PDB; 1JC1; X-ray; 1.90 A; A/B/C=1-238.
PDB; 1KP5; X-ray; 2.60 A; A/B=1-238.
PDB; 1KYP; X-ray; 1.35 A; A=2-238.
PDB; 1KYR; X-ray; 1.50 A; A=2-238.
PDB; 1KYS; X-ray; 1.44 A; A=2-238.
PDB; 1MYW; X-ray; 2.20 A; A=2-238.
PDB; 1Q4A; X-ray; 1.45 A; A=1-238.
PDB; 1Q4B; X-ray; 1.48 A; A=1-238.
PDB; 1Q4C; X-ray; 1.55 A; A=1-238.
PDB; 1Q4D; X-ray; 1.58 A; A=1-238.
PDB; 1Q4E; X-ray; 1.38 A; A=1-238.
PDB; 1Q73; X-ray; 1.60 A; A=1-238.
PDB; 1QXT; X-ray; 2.00 A; A=2-229.
PDB; 1QY3; X-ray; 2.00 A; A=1-229.
PDB; 1QYF; X-ray; 1.50 A; A=1-227.
PDB; 1QYO; X-ray; 1.80 A; A=1-238.
PDB; 1QYQ; X-ray; 1.80 A; A=2-238.
PDB; 1RM9; X-ray; 2.90 A; A=2-236.
PDB; 1RMM; X-ray; 1.90 A; A=2-227.
PDB; 1RMO; X-ray; 1.80 A; A=2-236.
PDB; 1RMP; X-ray; 3.00 A; A=2-229.
PDB; 1RRX; X-ray; 2.10 A; A=2-227.
PDB; 1S6Z; X-ray; 1.50 A; A=1-238.
PDB; 1W7S; X-ray; 1.85 A; A/B/C/D=1-238.
PDB; 1W7T; X-ray; 1.85 A; A/B/C/D=1-238.
PDB; 1W7U; X-ray; 1.85 A; A/B/C/D=1-238.
PDB; 1YFP; X-ray; 2.50 A; A/B=3-229.
PDB; 1YHG; X-ray; 2.50 A; A/B=2-238.
PDB; 1YHH; X-ray; 1.50 A; A=2-238.
PDB; 1YHI; X-ray; 1.90 A; A=2-238.
PDB; 1YJ2; X-ray; 1.50 A; A=2-238.
PDB; 1YJF; X-ray; 1.35 A; A=2-238.
PDB; 1Z1P; X-ray; 2.00 A; A=1-238.
PDB; 1Z1Q; X-ray; 1.50 A; A=1-238.
PDB; 2AH8; X-ray; 2.24 A; A/B=1-238.
PDB; 2AHA; X-ray; 1.98 A; A/B=1-238.
PDB; 2AWJ; X-ray; 1.60 A; A=2-229.
PDB; 2AWK; X-ray; 1.15 A; A=1-229.
PDB; 2AWL; X-ray; 1.85 A; A=1-229.
PDB; 2AWM; X-ray; 1.70 A; A=1-229.
PDB; 2B3P; X-ray; 1.40 A; A=1-238.
PDB; 2B3Q; X-ray; 2.30 A; A/B/C/D=1-238.
PDB; 2DUE; X-ray; 1.24 A; A=1-238.
PDB; 2DUF; X-ray; 1.50 A; A=1-238.
PDB; 2DUG; X-ray; 1.40 A; A=1-238.
PDB; 2DUH; X-ray; 1.20 A; A=1-238.
PDB; 2DUI; X-ray; 1.36 A; A=1-238.
PDB; 2EMD; X-ray; 2.00 A; A=1-238.
PDB; 2EMN; X-ray; 2.30 A; A=1-238.
PDB; 2EMO; X-ray; 2.60 A; A=1-238.
PDB; 2FWQ; X-ray; 1.40 A; A=2-238.
PDB; 2FZU; X-ray; 1.25 A; A=2-238.
PDB; 2G16; X-ray; 2.00 A; A=2-64, B=67-238.
PDB; 2G2S; X-ray; 1.20 A; A=2-63, B=66-238.
PDB; 2G3D; X-ray; 1.35 A; A=2-63, B=66-238.
PDB; 2G5Z; X-ray; 1.80 A; A=2-65, B=66-238.
PDB; 2G6E; X-ray; 1.30 A; A=2-238.
PDB; 2H6V; X-ray; 1.47 A; A=2-238.
PDB; 2H9W; X-ray; 1.82 A; A=2-237.
PDB; 2HCG; X-ray; 1.35 A; A=2-238.
PDB; 2HFC; X-ray; 1.20 A; A=2-238.
PDB; 2HGD; X-ray; 1.60 A; A=2-238.
PDB; 2HGY; X-ray; 2.05 A; A=2-238.
PDB; 2HJO; X-ray; 1.25 A; A=1-238.
PDB; 2HQZ; X-ray; 1.20 A; A=1-238.
PDB; 2HRS; X-ray; 1.40 A; A=1-238.
PDB; 2JAD; X-ray; 2.70 A; A=1-238.
PDB; 2O24; X-ray; 1.45 A; A=2-238.
PDB; 2O29; X-ray; 1.80 A; A=2-238.
PDB; 2O2B; X-ray; 1.94 A; A=2-238.
PDB; 2OKW; X-ray; 1.90 A; A/B/C/D/E/F=1-238.
PDB; 2OKY; X-ray; 2.40 A; A/B=1-238.
PDB; 2Q57; X-ray; 2.00 A; A=1-238.
PDB; 2Q6P; X-ray; 2.10 A; A=1-238.
PDB; 2QRF; X-ray; 1.50 A; A=1-230.
PDB; 2QT2; X-ray; 1.31 A; A=1-238.
PDB; 2QU1; X-ray; 1.70 A; A=1-238.
PDB; 2QZ0; X-ray; 1.20 A; A=2-229.
PDB; 2WSN; X-ray; 1.37 A; A=2-238.
PDB; 2WSO; X-ray; 1.15 A; A=2-238.
PDB; 2WUR; X-ray; 0.90 A; A=1-237.
PDB; 2Y0G; X-ray; 1.50 A; A=2-238.
PDB; 2YDZ; X-ray; 1.59 A; A=2-238.
PDB; 2YE0; X-ray; 1.47 A; A=2-238.
PDB; 2YE1; X-ray; 1.63 A; A=2-238.
PDB; 2YFP; X-ray; 2.60 A; A=1-238.
PDB; 3AI4; X-ray; 1.60 A; A=1-230.
PDB; 3CB9; X-ray; 1.31 A; A=2-238.
PDB; 3CBE; X-ray; 1.49 A; A=2-238.
PDB; 3CD1; X-ray; 1.31 A; A=2-238.
PDB; 3CD9; X-ray; 1.50 A; A=2-238.
PDB; 3DPW; X-ray; 1.59 A; A=2-238.
PDB; 3DPX; X-ray; 1.50 A; A=2-238.
PDB; 3DPZ; X-ray; 1.70 A; A=2-238.
PDB; 3DQ1; X-ray; 1.70 A; A=2-238.
PDB; 3DQ2; X-ray; 1.60 A; A=2-238.
PDB; 3DQ3; X-ray; 1.70 A; A=2-238.
PDB; 3DQ4; X-ray; 1.47 A; A=2-238.
PDB; 3DQ5; X-ray; 1.50 A; A=2-238.
PDB; 3DQ6; X-ray; 1.60 A; A=2-238.
PDB; 3DQ7; X-ray; 1.23 A; A=2-238.
PDB; 3DQ8; X-ray; 1.51 A; A=2-238.
PDB; 3DQ9; X-ray; 1.40 A; A=2-238.
PDB; 3DQA; X-ray; 1.44 A; A=2-238.
PDB; 3DQC; X-ray; 1.49 A; A=2-238.
PDB; 3DQD; X-ray; 1.40 A; A=2-238.
PDB; 3DQE; X-ray; 1.43 A; A=2-238.
PDB; 3DQF; X-ray; 1.46 A; A=2-238.
PDB; 3DQH; X-ray; 1.45 A; A=2-238.
PDB; 3DQI; X-ray; 1.42 A; A=2-238.
PDB; 3DQJ; X-ray; 1.51 A; A=2-238.
PDB; 3DQK; X-ray; 1.40 A; A=2-238.
PDB; 3DQL; X-ray; 1.47 A; A=2-238.
PDB; 3DQM; X-ray; 1.44 A; A=2-238.
PDB; 3DQN; X-ray; 1.44 A; A=2-238.
PDB; 3DQO; X-ray; 1.50 A; A=2-238.
PDB; 3DQU; X-ray; 1.42 A; A=2-238.
PDB; 3ED8; X-ray; 2.70 A; A/B/C/D/E=2-238.
PDB; 3EK4; X-ray; 2.65 A; A=2-238.
PDB; 3EK7; X-ray; 1.85 A; A=2-238.
PDB; 3EK8; X-ray; 2.80 A; A=2-238.
PDB; 3EKH; X-ray; 2.00 A; A=2-238.
PDB; 3EKJ; X-ray; 2.80 A; A=2-238.
PDB; 3EVP; X-ray; 1.45 A; A=2-144.
PDB; 3EVR; X-ray; 2.00 A; A=2-144.
PDB; 3EVU; X-ray; 1.75 A; A=2-144.
PDB; 3EVV; X-ray; 2.60 A; A=2-238.
PDB; 3G9A; X-ray; 1.61 A; A=1-238.
PDB; 3GEX; X-ray; 1.60 A; A=1-238.
PDB; 3GJ1; X-ray; 1.80 A; A/B/C/D=1-230.
PDB; 3GJ2; X-ray; 1.90 A; A/B/C/D=1-230.
PDB; 3I19; X-ray; 1.36 A; A=1-238.
PDB; 3K1K; X-ray; 2.15 A; A/B=1-238.
PDB; 3LA1; X-ray; 1.29 A; A=1-238.
PDB; 3O77; X-ray; 2.35 A; A=2-238.
PDB; 3O78; X-ray; 2.60 A; A/B=2-237.
PDB; 3OGO; X-ray; 2.80 A; A/B/C/D=1-238.
PDB; 3OSQ; X-ray; 1.90 A; A=2-238.
PDB; 3OSR; X-ray; 2.00 A; A/B=2-238.
PDB; 3P28; X-ray; 1.80 A; A=3-229.
PDB; 3SG2; X-ray; 2.00 A; A=2-238.
PDB; 3SG3; X-ray; 2.10 A; A=2-238.
PDB; 3SG4; X-ray; 2.40 A; A=2-238.
PDB; 3SG5; X-ray; 1.90 A; A=2-238.
PDB; 3SG6; X-ray; 1.70 A; A=2-238.
PDB; 3SG7; X-ray; 1.90 A; A=2-238.
PDB; 3SRY; X-ray; 1.16 A; A=2-238.
PDB; 3SS0; X-ray; 1.49 A; A=2-238.
PDB; 3SSH; X-ray; 1.28 A; A=2-238.
PDB; 3SSK; X-ray; 1.36 A; A=2-238.
PDB; 3SSL; X-ray; 1.45 A; A=2-238.
PDB; 3SSP; X-ray; 1.63 A; A=2-238.
PDB; 3SST; X-ray; 1.40 A; A=2-238.
PDB; 3SSV; X-ray; 1.86 A; A=2-238.
PDB; 3SSY; X-ray; 1.77 A; A=2-238.
PDB; 3ST0; X-ray; 1.19 A; A=2-238.
PDB; 3SV5; X-ray; 1.53 A; A=2-238.
PDB; 3SVB; X-ray; 1.30 A; A=2-238.
PDB; 3SVC; X-ray; 1.31 A; A=2-238.
PDB; 3SVD; X-ray; 1.78 A; A=2-238.
PDB; 3SVE; X-ray; 1.49 A; A=2-238.
PDB; 3U8P; X-ray; 2.75 A; A/B/C=2-238.
PDB; 3UFZ; X-ray; 1.85 A; A=2-229.
PDB; 3UG0; X-ray; 2.09 A; A=2-229.
PDB; 3V3D; X-ray; 1.95 A; A=2-238.
PDB; 3VHT; X-ray; 2.40 A; A=1-230.
PDB; 3W1C; X-ray; 1.30 A; A=2-238.
PDB; 3W1D; X-ray; 1.50 A; A=2-238.
PDB; 3WLC; X-ray; 2.49 A; A=2-238.
PDB; 3WLD; X-ray; 2.70 A; A=2-144.
PDB; 3ZTF; X-ray; 1.31 A; A=2-238.
PDB; 4ANJ; X-ray; 2.60 A; A=1-238.
PDB; 4AR7; X-ray; 1.23 A; A=2-238.
PDB; 4AS8; X-ray; 1.02 A; A=2-238.
PDB; 4B5Y; X-ray; 1.45 A; A=2-238.
PDB; 4BDU; X-ray; 3.00 A; A/B/C/D=1-230.
PDB; 4EN1; X-ray; 1.62 A; A/B=2-238.
PDB; 4EUL; X-ray; 1.35 A; A=2-238.
PDB; 4GES; X-ray; 1.23 A; B=1-238.
PDB; 4GF6; X-ray; 1.10 A; B=1-237.
PDB; 4H47; X-ray; 1.90 A; A=1-238.
PDB; 4H48; X-ray; 1.45 A; A=1-238.
PDB; 4IK1; X-ray; 2.00 A; A=2-144.
PDB; 4IK3; X-ray; 2.01 A; A=149-238, A=2-142.
PDB; 4IK4; X-ray; 2.01 A; A=2-142, A=149-238.
PDB; 4IK5; X-ray; 2.50 A; A=2-142, A=149-238.
PDB; 4IK8; X-ray; 1.55 A; A=2-144, A=149-238.
PDB; 4IK9; X-ray; 1.80 A; A=2-144.
PDB; 4J88; X-ray; 2.08 A; A/B=2-238.
PDB; 4J89; X-ray; 2.10 A; A/B=2-238.
PDB; 4J8A; X-ray; 1.26 A; A=2-238.
PDB; 4JFG; X-ray; 3.00 A; A/B/C/D/E/F/G/H=1-238.
PDB; 4JRB; X-ray; 2.41 A; A=1-229.
PDB; 4KA9; X-ray; 1.58 A; A=5-238.
PDB; 4KAG; X-ray; 1.12 A; A=1-238.
PDB; 4KEX; X-ray; 1.60 A; A=1-238.
PDB; 4KF5; X-ray; 2.60 A; A/B=1-196.
PDB; 4KW4; X-ray; 1.75 A; A=2-238.
PDB; 4KW8; X-ray; 2.46 A; A=2-238.
PDB; 4KW9; X-ray; 1.80 A; A=2-238.
PDB; 4L12; X-ray; 1.78 A; A=2-230.
PDB; 4L13; X-ray; 1.66 A; A=2-230.
PDB; 4L1I; X-ray; 1.20 A; A=2-230.
PDB; 4LQT; X-ray; 1.10 A; A=2-238.
PDB; 4LQU; X-ray; 1.60 A; A/B/C/D=2-238.
PDB; 4LW5; X-ray; 2.55 A; A/B/C/D/E=2-238.
PDB; 4N3D; X-ray; 1.34 A; A/B=1-230.
PDB; 4NDJ; X-ray; 1.85 A; A=2-238.
PDB; 4NDK; X-ray; 2.30 A; A/B=2-238.
PDB; 4OGS; X-ray; 2.21 A; A/B=1-238.
PDB; 4ORN; X-ray; 1.71 A; A/B=2-238.
PDB; 4P1Q; X-ray; 1.50 A; A=3-231.
PDB; 4P7H; X-ray; 3.20 A; A/B=5-238.
PDB; 4PA0; X-ray; 2.25 A; A/B=5-234.
PDB; 4PFE; X-ray; 2.60 A; A/B=2-229.
PDB; 4U2V; X-ray; 2.30 A; A/B/C/D=1-230.
PDB; 4XBI; X-ray; 2.01 A; A/B=2-230.
PDB; 4XGY; X-ray; 1.49 A; A=2-238.
PDB; 4XL5; X-ray; 2.00 A; A=2-238.
PDB; 4XOV; X-ray; 1.20 A; A=2-238.
PDB; 4XOW; X-ray; 1.25 A; A=2-238.
PDB; 4XVP; X-ray; 3.40 A; A/B/C=2-238.
PDB; 4Z4K; X-ray; 2.80 A; A/B=1-230.
PDB; 4Z4M; X-ray; 2.15 A; A/B=1-230.
PDB; 4ZF3; X-ray; 1.90 A; A/B=51-236.
PDB; 4ZF4; X-ray; 1.82 A; A/B=4-237.
PDB; 4ZF5; X-ray; 1.70 A; A/B=4-237.
PDB; 5AQB; X-ray; 1.37 A; B=2-231.
PDB; 5B61; X-ray; 3.12 A; A/B/C/D/E/F=1-238.
PDB; 5DPG; X-ray; 1.85 A; A=2-238.
PDB; 5DPH; X-ray; 1.42 A; A/B=2-238.
PDB; 5DPI; X-ray; 2.54 A; A/B/C/D/E/F=2-238.
PDB; 5DPJ; X-ray; 2.50 A; A/B/C/D=2-238.
PDB; 5DQB; X-ray; 1.25 A; A=2-238.
PDB; 5DQM; X-ray; 1.30 A; A=2-238.
PDB; 5DRF; X-ray; 1.14 A; A=2-238.
PDB; 5DRG; X-ray; 1.14 A; A=2-238.
PDB; 5DTX; X-ray; 1.45 A; A=1-63, A=65-238.
PDB; 5DTY; X-ray; 1.50 A; A=1-63, A=65-238.
PDB; 5DTZ; X-ray; 1.50 A; A/B/C/D=2-238.
PDB; 5DU0; X-ray; 2.35 A; A/B/C/D=2-238.
PDB; 5EHU; X-ray; 1.45 A; A/B=2-238.
PDB; 5F9G; X-ray; 2.77 A; A=2-144.
PDB; 5FGU; X-ray; 1.90 A; A=1-229.
PDB; 5HBD; X-ray; 1.65 A; A=1-238.
PDB; 5HGE; X-ray; 1.86 A; A=1-238.
PDB; 5HW9; X-ray; 3.00 A; A=1-238.
PDB; 5HZO; X-ray; 2.49 A; A/B=1-235.
PDB; 5J2O; X-ray; 1.50 A; A=2-238.
PDB; 5J3N; X-ray; 2.45 A; A/B=2-238.
PDB; 5KTG; X-ray; 2.80 A; A/B=1-230.
PDB; 5LEM; X-ray; 2.98 A; C=2-238.
PDB; 5T3I; X-ray; 1.60 A; A=2-238.
PDBsum; 1B9C; -.
PDBsum; 1BFP; -.
PDBsum; 1C4F; -.
PDBsum; 1CV7; -.
PDBsum; 1EMA; -.
PDBsum; 1EMB; -.
PDBsum; 1EMC; -.
PDBsum; 1EME; -.
PDBsum; 1EMF; -.
PDBsum; 1EMG; -.
PDBsum; 1EMK; -.
PDBsum; 1EML; -.
PDBsum; 1EMM; -.
PDBsum; 1F09; -.
PDBsum; 1F0B; -.
PDBsum; 1GFL; -.
PDBsum; 1H6R; -.
PDBsum; 1HCJ; -.
PDBsum; 1HUY; -.
PDBsum; 1JBY; -.
PDBsum; 1JBZ; -.
PDBsum; 1JC0; -.
PDBsum; 1JC1; -.
PDBsum; 1KP5; -.
PDBsum; 1KYP; -.
PDBsum; 1KYR; -.
PDBsum; 1KYS; -.
PDBsum; 1MYW; -.
PDBsum; 1Q4A; -.
PDBsum; 1Q4B; -.
PDBsum; 1Q4C; -.
PDBsum; 1Q4D; -.
PDBsum; 1Q4E; -.
PDBsum; 1Q73; -.
PDBsum; 1QXT; -.
PDBsum; 1QY3; -.
PDBsum; 1QYF; -.
PDBsum; 1QYO; -.
PDBsum; 1QYQ; -.
PDBsum; 1RM9; -.
PDBsum; 1RMM; -.
PDBsum; 1RMO; -.
PDBsum; 1RMP; -.
PDBsum; 1RRX; -.
PDBsum; 1S6Z; -.
PDBsum; 1W7S; -.
PDBsum; 1W7T; -.
PDBsum; 1W7U; -.
PDBsum; 1YFP; -.
PDBsum; 1YHG; -.
PDBsum; 1YHH; -.
PDBsum; 1YHI; -.
PDBsum; 1YJ2; -.
PDBsum; 1YJF; -.
PDBsum; 1Z1P; -.
PDBsum; 1Z1Q; -.
PDBsum; 2AH8; -.
PDBsum; 2AHA; -.
PDBsum; 2AWJ; -.
PDBsum; 2AWK; -.
PDBsum; 2AWL; -.
PDBsum; 2AWM; -.
PDBsum; 2B3P; -.
PDBsum; 2B3Q; -.
PDBsum; 2DUE; -.
PDBsum; 2DUF; -.
PDBsum; 2DUG; -.
PDBsum; 2DUH; -.
PDBsum; 2DUI; -.
PDBsum; 2EMD; -.
PDBsum; 2EMN; -.
PDBsum; 2EMO; -.
PDBsum; 2FWQ; -.
PDBsum; 2FZU; -.
PDBsum; 2G16; -.
PDBsum; 2G2S; -.
PDBsum; 2G3D; -.
PDBsum; 2G5Z; -.
PDBsum; 2G6E; -.
PDBsum; 2H6V; -.
PDBsum; 2H9W; -.
PDBsum; 2HCG; -.
PDBsum; 2HFC; -.
PDBsum; 2HGD; -.
PDBsum; 2HGY; -.
PDBsum; 2HJO; -.
PDBsum; 2HQZ; -.
PDBsum; 2HRS; -.
PDBsum; 2JAD; -.
PDBsum; 2O24; -.
PDBsum; 2O29; -.
PDBsum; 2O2B; -.
PDBsum; 2OKW; -.
PDBsum; 2OKY; -.
PDBsum; 2Q57; -.
PDBsum; 2Q6P; -.
PDBsum; 2QRF; -.
PDBsum; 2QT2; -.
PDBsum; 2QU1; -.
PDBsum; 2QZ0; -.
PDBsum; 2WSN; -.
PDBsum; 2WSO; -.
PDBsum; 2WUR; -.
PDBsum; 2Y0G; -.
PDBsum; 2YDZ; -.
PDBsum; 2YE0; -.
PDBsum; 2YE1; -.
PDBsum; 2YFP; -.
PDBsum; 3AI4; -.
PDBsum; 3CB9; -.
PDBsum; 3CBE; -.
PDBsum; 3CD1; -.
PDBsum; 3CD9; -.
PDBsum; 3DPW; -.
PDBsum; 3DPX; -.
PDBsum; 3DPZ; -.
PDBsum; 3DQ1; -.
PDBsum; 3DQ2; -.
PDBsum; 3DQ3; -.
PDBsum; 3DQ4; -.
PDBsum; 3DQ5; -.
PDBsum; 3DQ6; -.
PDBsum; 3DQ7; -.
PDBsum; 3DQ8; -.
PDBsum; 3DQ9; -.
PDBsum; 3DQA; -.
PDBsum; 3DQC; -.
PDBsum; 3DQD; -.
PDBsum; 3DQE; -.
PDBsum; 3DQF; -.
PDBsum; 3DQH; -.
PDBsum; 3DQI; -.
PDBsum; 3DQJ; -.
PDBsum; 3DQK; -.
PDBsum; 3DQL; -.
PDBsum; 3DQM; -.
PDBsum; 3DQN; -.
PDBsum; 3DQO; -.
PDBsum; 3DQU; -.
PDBsum; 3ED8; -.
PDBsum; 3EK4; -.
PDBsum; 3EK7; -.
PDBsum; 3EK8; -.
PDBsum; 3EKH; -.
PDBsum; 3EKJ; -.
PDBsum; 3EVP; -.
PDBsum; 3EVR; -.
PDBsum; 3EVU; -.
PDBsum; 3EVV; -.
PDBsum; 3G9A; -.
PDBsum; 3GEX; -.
PDBsum; 3GJ1; -.
PDBsum; 3GJ2; -.
PDBsum; 3I19; -.
PDBsum; 3K1K; -.
PDBsum; 3LA1; -.
PDBsum; 3O77; -.
PDBsum; 3O78; -.
PDBsum; 3OGO; -.
PDBsum; 3OSQ; -.
PDBsum; 3OSR; -.
PDBsum; 3P28; -.
PDBsum; 3SG2; -.
PDBsum; 3SG3; -.
PDBsum; 3SG4; -.
PDBsum; 3SG5; -.
PDBsum; 3SG6; -.
PDBsum; 3SG7; -.
PDBsum; 3SRY; -.
PDBsum; 3SS0; -.
PDBsum; 3SSH; -.
PDBsum; 3SSK; -.
PDBsum; 3SSL; -.
PDBsum; 3SSP; -.
PDBsum; 3SST; -.
PDBsum; 3SSV; -.
PDBsum; 3SSY; -.
PDBsum; 3ST0; -.
PDBsum; 3SV5; -.
PDBsum; 3SVB; -.
PDBsum; 3SVC; -.
PDBsum; 3SVD; -.
PDBsum; 3SVE; -.
PDBsum; 3U8P; -.
PDBsum; 3UFZ; -.
PDBsum; 3UG0; -.
PDBsum; 3V3D; -.
PDBsum; 3VHT; -.
PDBsum; 3W1C; -.
PDBsum; 3W1D; -.
PDBsum; 3WLC; -.
PDBsum; 3WLD; -.
PDBsum; 3ZTF; -.
PDBsum; 4ANJ; -.
PDBsum; 4AR7; -.
PDBsum; 4AS8; -.
PDBsum; 4B5Y; -.
PDBsum; 4BDU; -.
PDBsum; 4EN1; -.
PDBsum; 4EUL; -.
PDBsum; 4GES; -.
PDBsum; 4GF6; -.
PDBsum; 4H47; -.
PDBsum; 4H48; -.
PDBsum; 4IK1; -.
PDBsum; 4IK3; -.
PDBsum; 4IK4; -.
PDBsum; 4IK5; -.
PDBsum; 4IK8; -.
PDBsum; 4IK9; -.
PDBsum; 4J88; -.
PDBsum; 4J89; -.
PDBsum; 4J8A; -.
PDBsum; 4JFG; -.
PDBsum; 4JRB; -.
PDBsum; 4KA9; -.
PDBsum; 4KAG; -.
PDBsum; 4KEX; -.
PDBsum; 4KF5; -.
PDBsum; 4KW4; -.
PDBsum; 4KW8; -.
PDBsum; 4KW9; -.
PDBsum; 4L12; -.
PDBsum; 4L13; -.
PDBsum; 4L1I; -.
PDBsum; 4LQT; -.
PDBsum; 4LQU; -.
PDBsum; 4LW5; -.
PDBsum; 4N3D; -.
PDBsum; 4NDJ; -.
PDBsum; 4NDK; -.
PDBsum; 4OGS; -.
PDBsum; 4ORN; -.
PDBsum; 4P1Q; -.
PDBsum; 4P7H; -.
PDBsum; 4PA0; -.
PDBsum; 4PFE; -.
PDBsum; 4U2V; -.
PDBsum; 4XBI; -.
PDBsum; 4XGY; -.
PDBsum; 4XL5; -.
PDBsum; 4XOV; -.
PDBsum; 4XOW; -.
PDBsum; 4XVP; -.
PDBsum; 4Z4K; -.
PDBsum; 4Z4M; -.
PDBsum; 4ZF3; -.
PDBsum; 4ZF4; -.
PDBsum; 4ZF5; -.
PDBsum; 5AQB; -.
PDBsum; 5B61; -.
PDBsum; 5DPG; -.
PDBsum; 5DPH; -.
PDBsum; 5DPI; -.
PDBsum; 5DPJ; -.
PDBsum; 5DQB; -.
PDBsum; 5DQM; -.
PDBsum; 5DRF; -.
PDBsum; 5DRG; -.
PDBsum; 5DTX; -.
PDBsum; 5DTY; -.
PDBsum; 5DTZ; -.
PDBsum; 5DU0; -.
PDBsum; 5EHU; -.
PDBsum; 5F9G; -.
PDBsum; 5FGU; -.
PDBsum; 5HBD; -.
PDBsum; 5HGE; -.
PDBsum; 5HW9; -.
PDBsum; 5HZO; -.
PDBsum; 5J2O; -.
PDBsum; 5J3N; -.
PDBsum; 5KTG; -.
PDBsum; 5LEM; -.
PDBsum; 5T3I; -.
ProteinModelPortal; P42212; -.
SMR; P42212; -.
IntAct; P42212; 1.
PRIDE; P42212; -.
EvolutionaryTrace; P42212; -.
GO; GO:0008218; P:bioluminescence; TAS:UniProtKB.
GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:UniProtKB.
GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
InterPro; IPR009017; GFP.
InterPro; IPR011584; GFP-related.
InterPro; IPR000786; Green_fluorescent_prot.
Pfam; PF01353; GFP; 1.
PRINTS; PR01229; GFLUORESCENT.
SUPFAM; SSF54511; SSF54511; 1.
1: Evidence at protein level;
3D-structure; Chromophore; Direct protein sequencing; Luminescence;
Photoprotein.
CHAIN 1 238 Green fluorescent protein.
/FTId=PRO_0000192576.
MOD_RES 66 66 (Z)-2,3-didehydrotyrosine.
{ECO:0000269|PubMed:8448132}.
CROSSLNK 65 67 5-imidazolinone (Ser-Gly).
{ECO:0000269|PubMed:8448132}.
VARIANT 100 100 F -> Y. {ECO:0000269|PubMed:1347277}.
VARIANT 108 108 T -> S. {ECO:0000269|PubMed:1347277}.
VARIANT 141 141 L -> M. {ECO:0000269|PubMed:1347277}.
VARIANT 219 219 V -> I. {ECO:0000269|PubMed:1347277}.
MUTAGEN 30 30 S->R: In mut1.28; shifts fluorescence
lifetime from 3.03 to 2.76 ns; when
associated with H-145. In mut2.2; shifts
fluorescence lifetime from 3.03 to 1.94
ns; when associated with H-69 and H-145.
In mut3.3; shifts fluorescence lifetime
from 3.03 to 1.88 ns; when associated
with L-46; H-69 and H-145. In EBFP1.2;
shifts the excitation and emission
spectra to shorter wavelengths and
increases quantum yields compared to BFP;
when associated with N-39; H-66; A-72; T-
105; F-145; V-171; S-198 and V-206. In
EBFP2.0; shifts the excitation and
emission spectra to shorter wavelengths
and increases quantum yields compared to
BFP; when associated with N-39; H-66; A-
72; T-105; V-128; F-145; I-150; V-155; V-
171; S-198; V-206 and V-224.
{ECO:0000269|PubMed:16201762,
ECO:0000269|PubMed:22891786}.
MUTAGEN 39 39 Y->N: In EBFP1.2; shifts the excitation
and emission spectra to shorter
wavelengths and increases quantum yields
compared to BFP; when associated with R-
30; H-66; A-72; T-105; F-145; V-171; S-
198 and V-206. In EBFP2.0; shifts the
excitation and emission spectra to
shorter wavelengths and increases quantum
yields compared to BFP; when associated
with R-30; H-66; A-72; T-105; V-128; F-
145; I-150; V-155; V-171; S-198; V-206
and V-224. {ECO:0000269|PubMed:22891786}.
MUTAGEN 46 46 F->L: In mut3.3; shifts fluorescence
lifetime from 3.03 to 1.88 ns; when
associated with R-30; H-69 and H-145. In
R10-3; matures to the red-emitting state
with excitation and emission maxima at
555 and 585 nm, respectively; when
associated with L-64; N-68; Q-162; A-163;
V-167 and L-171. In Venus; leads to
yellow fluorescence, improved maturation
and reduced environmental sensitivity;
when associated with L-64; G-65; L-68; A-
72; T-153; A-163; G-175 and Y-203.
{ECO:0000269|PubMed:12370172,
ECO:0000269|PubMed:16201762,
ECO:0000269|PubMed:18366185}.
MUTAGEN 64 64 F->L: In EGFP; increases fluoresence at
warmer temperatures such as 37 degrees
Celsius; when associated with T-65. In
EBFP; gives rise to variants with blue
fluorescence; when associated with T-65
and H-66. In ECFP; leads to cyan
fluorescence, folds faster and more
efficiently at 37 degrees Celsius and has
superior solubility and brightness; when
associated with T-65; W-66; I-146; T-153
and A-163. In Cerulean; leads to improved
quantum yield, a higher extinction
coefficient and is 2.5-fold brighterH
than ECFP; when associated with T-65; W-
66; A-72; A-145; I-146; D-148; T-153 and
A-163. In R10-3; matures to the red-
emitting state with excitation and
emission maxima at 555 and 585 nm,
respectively; when associated with L-46;
N-68; Q-162; A-163; V-167 and L-171. In
GFPmut 1; red-shifts by about 100 nm the
excitation maxima, permitting efficient
excitation at 488 nm and increases
fluorescence; when associated with T-65.
In VisGreen; leads to brighter
fluorescence; when associated with T-65;
A-72; K-149 and T-167. In Venus; leads to
yellow fluorescence, improved maturation
and reduced environmental sensitivity;
when associated with L-46; G-65; L-68; A-
72; T-153; A-163; G-175 and Y-203.
{ECO:0000269|PubMed:11299042,
ECO:0000269|PubMed:11776264,
ECO:0000269|PubMed:12370172,
ECO:0000269|PubMed:14990965,
ECO:0000269|PubMed:15065907,
ECO:0000269|PubMed:17658219,
ECO:0000269|PubMed:18366185,
ECO:0000269|PubMed:8707053,
ECO:0000269|PubMed:9145105,
ECO:0000269|PubMed:9370472}.
MUTAGEN 64 64 F->M: In RSGFP4; increases fluorescence
and shifts the major exitation peak to
489-490 nm; when associated with G-65 and
L-69. {ECO:0000269|PubMed:9634755}.
MUTAGEN 65 66 SY->TW: Gives rise to variants with
cerulean fluorsecence.
{ECO:0000269|PubMed:17685554}.
MUTAGEN 65 65 S->A: In GFPmut 2; red-shifts by about
100 nm the excitation maxima, permitting
efficient excitation at 488 nm and
increases fluorescence; when associated
with L-68 and A-72.
{ECO:0000269|PubMed:8707053}.
MUTAGEN 65 65 S->G: In EYFP; leads to yellow
fluorescence, folds faster and more
efficiently at 37 degrees Celsius and has
superior solubility and brightness; when
associated with L-68; A-72 and Y-203. In
GFPmut 3; highly fluorescent mutant when
excited at 488 nm; when associated with
A-72. Highly fluorescent; when associated
with Y-203; L-68 and A-72. In RSGFP4;
increases fluoresence and shifts the
major exitation peak to 489-490 nm; when
associated with M-64 and L-69. In YFP
10C; shifts the major emission and
exitation peak up to 20 nm; when
associated with L-68; A-72 and Y-203. In
Topaz; shifts the major emission and
exitation peak up to 20 nm; when
associated with A-72; R-79 and Y-203. In
Venus; leads to yellow fluorescence,
improved maturation and reduced
environmental sensitivity; when
associated with L-46; L-64; L-68; A-72;
T-153; A-163; G-175 and Y-203.
{ECO:0000269|PubMed:11299042,
ECO:0000269|PubMed:12370172,
ECO:0000269|PubMed:8707053,
ECO:0000269|PubMed:9634755,
ECO:0000269|PubMed:9759496,
ECO:0000269|PubMed:9782051}.
MUTAGEN 65 65 S->T: Increases fluoresence,
photostability and shifts the major
exitation peak to 488 nm. In EGFP;
increases fluoresence at warmer
temperatures such as 37 degrees Celsius;
when associated with L-64. In EBFP; gives
rise to variants with blue fluorescence;
when associated with L-64 and H-66. In
GFPmut 1; red-shifts by about 100 nm the
excitation maxima, permitting efficient
excitation at 488 nm and increases
fluorescence; when associated with T-65.
In ECFP; leads to cyan fluorescence,
folds faster and more efficiently at 37
degrees Celsius and has superior
solubility and brightness; when
associated with L-64; W-66; I-146; T-153
and A-163. In Cerulean; leads to improved
quantum yield, a higher extinction
coefficient and is 2.5-fold brighter than
ECFP; when associated with L-64; W-66; A-
72; A-145; I-146; D-148; T-153 and A-163.
In Esmerald; leads to brighter
fluorescence; when associated with A-72;
K-149; T-153 and T-167. In VisGreen;
leads to brighter fluorescence; when
associated with L-64; A-72; K-149 and T-
167. {ECO:0000269|PubMed:11299042,
ECO:0000269|PubMed:11776264,
ECO:0000269|PubMed:14990965,
ECO:0000269|PubMed:15065907,
ECO:0000269|PubMed:17658219,
ECO:0000269|PubMed:8703075,
ECO:0000269|PubMed:8707053,
ECO:0000269|PubMed:9370472}.
MUTAGEN 66 66 Y->H: In BFP; shifts the excitation and
emission spectra to shorter wavelengths.
In EBFP; gives rise to variants with blue
fluorescence; when associated with L-64
and T-65. In Azurite; shifts the
excitation and emission spectra to
shorter wavelengths and increases quantum
yields compared to BFP; when associated
with R-80; F-145; I-150 and R-224. In
EBFP1.2; shifts the excitation and
emission spectra to shorter wavelengths
and increases quantum yields compared to
BFP; when associated with R-30; N-39; A-
72; T-105; F-145; V-171; S-198 and V-206.
In EBFP2.0; shifts the excitation and
emission spectra to shorter wavelengths
and increases quantum yields compared to
BFP; when associated with R-30; N-39; A-
72; T-105; V-128; F-145; I-150; V-155; V-
171; S-198; V-206 and V-224.
{ECO:0000269|PubMed:22891786,
ECO:0000269|PubMed:8578587,
ECO:0000269|PubMed:9145105,
ECO:0000269|PubMed:9370472}.
MUTAGEN 66 66 Y->T,F: Shifts the excitation and
emission spectra to shorter wavelengths.
{ECO:0000269|PubMed:8578587}.
MUTAGEN 66 66 Y->W: In W; leads to excitation and
emission wavelengths intermediate between
tyrosine and histidine but is only weakly
fluorescent. In ECFP; leads to cyan
fluorescence, folds faster and more
efficiently at 37 degrees Celsius and has
superior solubility and brightness; when
associated with L-64; T-65; I-146; T-153
and A-163. In Cerulean; leads to improved
quantum yield, a higher extinction
coefficient and is 2.5-fold brighter than
ECFP; when associated with L-64; T-65; A-
72; A-145; I-146; D-148; T-153 and A-163.
{ECO:0000269|PubMed:11299042,
ECO:0000269|PubMed:14990965,
ECO:0000269|PubMed:15065907,
ECO:0000269|PubMed:7809066}.
MUTAGEN 68 68 V->L: In EYFP; leads to yellow
fluorescence, folds faster and more
efficiently at 37 degrees Celsius and has
superior solubility and brightness; when
associated with G-65; A-72 and Y-203. In
GFPmut 2; red-shifts by about 100 nm the
excitation maxima, permitting efficient
excitation at 488 nm and increases
fluorescence; when associated with A-65
and A-72. In Citrinine; leads to
excitation and emission peaks of 516 and
529 nm, respectively; when associated
with M-69; A-72 and Y-203. In YFP 10C;
shifts the major emission and exitation
peak up to 20 nm; when associated with G-
65; A-72 and Y-203. In Venus; leads to
yellow fluorescence, improved maturation
and reduced environmental sensitivity;
when associated with L-46; L-64; G-65; A-
72; T-153; A-163; G-175 and Y-203.
{ECO:0000269|PubMed:11299042,
ECO:0000269|PubMed:11387331,
ECO:0000269|PubMed:12370172,
ECO:0000269|PubMed:8707053,
ECO:0000269|PubMed:9759496,
ECO:0000269|PubMed:9782051}.
MUTAGEN 68 68 V->N: In R10-3; matures to the red-
emitting state with excitation and
emission maxima at 555 and 585 nm,
respectively; when associated with L-46;
L-64; Q-162; A-163; V-167 and L-171.
{ECO:0000269|PubMed:18366185}.
MUTAGEN 69 69 Q->H: In P4; leads to no detectable
fluorescence. In mut2.2; shifts
fluorescence lifetime from 3.03 to 1.94
ns; when associated with R-30 and H-145.
In mut3.3; shifts fluorescence lifetime
from 3.03 to 1.88 ns; when associated
with R-30; L-46 and H-145.
{ECO:0000269|PubMed:16201762,
ECO:0000269|PubMed:7809066}.
MUTAGEN 69 69 Q->L: In RSGFP4; increases fluorescence
and shifts the major exitation peak to
489-490 nm; when associated with M-64 and
G-65. {ECO:0000269|PubMed:9634755}.
MUTAGEN 69 69 Q->M: In Citrinine; leads to excitation
and emission peaks of 516 and 529 nm,
respectively; when associated with L-68;
A-72 and Y-203.
{ECO:0000269|PubMed:11387331}.
MUTAGEN 72 72 S->A: Increases fluoresence at warmer
temperatures such as 37 degrees Celsius.
In GFPmut 3; highly fluorescent mutant
when excited at 488 nm; when associated
with G-65. In EYFP; leads to yellow
fluorescence, folds faster and more
efficiently at 37 degrees Celsius and has
superior solubility and brightness; when
associated with G-65; L-68 and Y-203. In
GFPmut 2; red-shifts by about 100 nm the
excitation maxima, permitting efficient
excitation at 488 nm and increases
fluorescence; when associated with A-65
and L-68. In Citrinine; leads to
excitation and emission peaks of 516 and
529 nm, respectively; when associated
with L-68; M-69 and Y-203. In YFP 10C;
shifts the major emission and exitation
peak up to 20 nm; when associated with G-
65; L-68; and Y-203. In Topaz; shifts the
major emission and exitation peak up to
20 nm; when associated with G-65; R-79
and Y-203. In Cerulean; leads to improved
quantum yield, a higher extinction
coefficient and is 2.5-fold brighter than
ECFP; when associated with L-64; T-65; W-
66; A-145; I-146; D-148; T-153 and A-163.
In Sapphire/H9-40; exhibits a huge
Stoke's shift, with an excitation peak at
399 nm and an emission peak at 511 nm;
when associated with F-145 and I-203. In
EBFP1.2; shifts the excitation and
emission spectra to shorter wavelengths
and increases quantum yields compared to
BFP; when associated with R-30; N-39; H-
66; T-105; F-145; V-171; S-198 and V-206.
In EBFP2.0; shifts the excitation and
emission spectra to shorter wavelengths
and increases quantum yields compared to
BFP; when associated with R-30; N-39; H-
66; T-105; V-128; F-145; I-150; V-155; V-
171; S-198; V-206 and V-224. In Esmerald;
leads to brighter fluorescence; when
associated with T-65; K-149; T-153 and T-
167. In VisGreen; leads to brighter
fluorescence; when associated with L-64;
T-65; K-149 and T-167. In Venus; leads to
yellow fluorescence, improved maturation
and reduced environmental sensitivity;
when associated with L-46; L-64; G-65; L-
68; T-153; A-163; G-175 and Y-203.
{ECO:0000269|PubMed:11299042,
ECO:0000269|PubMed:11387331,
ECO:0000269|PubMed:12370172,
ECO:0000269|PubMed:12769828,
ECO:0000269|PubMed:14990965,
ECO:0000269|PubMed:17658219,
ECO:0000269|PubMed:22891786,
ECO:0000269|PubMed:8707053,
ECO:0000269|PubMed:9145105,
ECO:0000269|PubMed:9759496,
ECO:0000269|PubMed:9782051}.
MUTAGEN 79 79 K->R: In Topaz; shifts the major emission
and exitation peak up to 20 nm; when
associated with G-65; A-72 and Y-203.
{ECO:0000269|PubMed:9759496}.
MUTAGEN 80 80 Q->R: In Azurite; shifts the excitation
and emission spectra to shorter
wavelengths and increases quantum yields
compared to BFP; when associated with H-
66; F-145; I-150 and R-224.
{ECO:0000269|PubMed:22891786}.
MUTAGEN 99 99 F->S: In alphaGFP/cycle 3 GFP; improves
folding at 37 degrees Celsius, reduces
aggregation at high concentrations, and
increases the diffusibility of the
protein inside cells; when associated
with T-153 and A-163.
{ECO:0000269|PubMed:9370472,
ECO:0000269|PubMed:9630892,
ECO:0000269|PubMed:9631088}.
MUTAGEN 103 103 D->E: In mut1.27; shifts fluorescence
lifetime from 3.03 to 2.85 ns; when
associated with H-145.
{ECO:0000269|PubMed:16201762}.
MUTAGEN 105 105 N->T: In EBFP1.2; shifts the excitation
and emission spectra to shorter
wavelengths and increases quantum yields
compared to BFP; when associated with R-
30; N-39; H-66; A-72; F-145; V-171; S-198
and V-206. In EBFP2.0; shifts the
excitation and emission spectra to
shorter wavelengths and increases quantum
yields compared to BFP; when associated
with R-30; N-39; H-66; A-72; V-128; F-
145; I-150; V-155; V-171; S-198; V-206
and V-224. {ECO:0000269|PubMed:22891786}.
MUTAGEN 128 128 I->V: In EBFP2.0; shifts the excitation
and emission spectra to shorter
wavelengths and increases quantum yields
compared to BFP; when associated with R-
30; N-39; H-66; A-72; T-105; F-145; I-
150; V-155; V-171; S-198; V-206 and V-
224. {ECO:0000269|PubMed:22891786}.
MUTAGEN 145 145 Y->A: In Cerulean; leads to improved
quantum yield, a higher extinction
coefficient and is 2.5-fold brighter than
ECFP; when associated with L-64; T-65; W-
66; A-72; I-146; D-148; T-153 and A-163.
{ECO:0000269|PubMed:14990965}.
MUTAGEN 145 145 Y->C: In mut1.9; shifts fluorescence
lifetime from 3.03 to 2.74 ns.
{ECO:0000269|PubMed:16201762}.
MUTAGEN 145 145 Y->F: In Sapphire/H9-40; exhibits a huge
Stoke's shift, with an excitation peak at
399 nm and an emission peak at 511 nm;
when associated with A-72 and I-203. In
Azurite; shifts the excitation and
emission spectra to shorter wavelengths
and increases quantum yields compared to
BFP; when associated with H-66; R-80; I-
150 and R-224. In EBFP1.2; shifts the
excitation and emission spectra to
shorter wavelengths and increases quantum
yields compared to BFP; when associated
with R-30; N-39; H-66; A-72; T-105; V-
171; S-198 and V-206. In EBFP2.0; shifts
the excitation and emission spectra to
shorter wavelengths and increases quantum
yields compared to BFP; when associated
with R-30; N-39; H-66; A-72; T-105; V-
128; I-150; V-155; V-171; S-198; V-206
and V-224. {ECO:0000269|PubMed:12769828,
ECO:0000269|PubMed:22891786}.
MUTAGEN 145 145 Y->H: In mut1.3; shifts fluorescence
lifetime from 3.03 to 2.78 ns. In mut1.5;
shifts fluorescence lifetime from 3.03 to
2.72 ns; when associated with A-193. In
mut1.27; shifts fluorescence lifetime
from 3.03 to 2.85 ns; when associated
with E-103. In mut1.28; shifts
fluorescence lifetime from 3.03 to 2.76
ns; when associated with R-30. In mut2.1;
shifts fluorescence lifetime from 3.03 to
2.50 ns; when associated with A-176 and
I-198. In mut2.2; shifts fluorescence
lifetime from 3.03 to 1.94 ns; when
associated with R-30 and H-69. In mut3.3;
shifts fluorescence lifetime from 3.03 to
1.88 ns; when associated with R-30; L-46
and H-69. {ECO:0000269|PubMed:16201762}.
MUTAGEN 146 146 N->I: In ECFP; leads to cyan
fluorescence, folds faster and more
efficiently at 37 degrees Celsius and has
superior solubility and brightness; when
associated with L-64; T-65; W-66; T-153
and A-163. In Cerulean; leads to improved
quantum yield, a higher extinction
coefficient and is 2.5-fold brighter than
ECFP; when associated with L-64; T-65; W-
66; A-72; A-145; D-148; T-153 and A-163.
{ECO:0000269|PubMed:11299042,
ECO:0000269|PubMed:14990965,
ECO:0000269|PubMed:15065907}.
MUTAGEN 147 147 S->P: Increases fluorescence at warmer
temperatures such as 37 degrees Celsius.
{ECO:0000269|PubMed:9125154}.
MUTAGEN 148 148 H->D: In Cerulean; leads to improved
quantum yield, a higher extinction
coefficient and is 2.5-fold brighter than
ECFP; when associated with L-64; T-65; W-
66; A-72; A-145; I-146; T-153 and A-163.
{ECO:0000269|PubMed:14990965}.
MUTAGEN 149 149 N->K: Increases fluorescence at warmer
temperatures such as 37 degrees Celsius.
In Esmerald; leads to brighter
fluorescence; when associated with T-65;
A-72; T-153 and T-167. In VisGreen; leads
to brighter fluorescence; when associated
with L-64; T-65; A-72 and T-167.
{ECO:0000269|PubMed:17658219,
ECO:0000269|PubMed:9145105}.
MUTAGEN 150 150 V->I: In Azurite; shifts the excitation
and emission spectra to shorter
wavelengths and increases quantum yields
compared to BFP; when associated with H-
66; R-80; F-145 and R-224. In EBFP2.0;
shifts the excitation and emission
spectra to shorter wavelengths and
increases quantum yields compared to BFP;
when associated with R-30; N-39; H-66; A-
72; T-105; V-128; F-145; V-155; V-171; S-
198; V-206 and V-224.
{ECO:0000269|PubMed:22891786}.
MUTAGEN 153 153 M->T: Increases fluorescence at warmer
temperatures such as 37 degrees Celsius.
In alphaGFP/cycle 3 GFP; improves folding
at 37 degrees Celsius, reduces
aggregation at high concentrations, and
increases the diffusibility of the
protein inside cells; when associated
with S-99 and A-163. In ECFP; leads to
cyan fluorescence, folds faster and more
efficiently at 37 degrees Celsius and has
superior solubility and brightness; when
associated with L-64; T-65; W-66; I-146
and A-163. In Cerulean; leads to improved
quantum yield, a higher extinction
coefficient and is 2.5-fold brighter than
ECFP; when associated with L-64; T-65; W-
66; A-72; A-145; I-146; D-148 and A-163.
In Esmerald; leads to brighter
fluorescence; when associated with T-65;
A-72; K-149 and T-167. In Venus; leads to
yellow fluorescence, improved maturation
and reduced environmental sensitivity;
when associated with L-46; L-64; G-65; L-
68; A-72; A-163; G-175 and Y-203.
{ECO:0000269|PubMed:11299042,
ECO:0000269|PubMed:12370172,
ECO:0000269|PubMed:14990965,
ECO:0000269|PubMed:15065907,
ECO:0000269|PubMed:17658219,
ECO:0000269|PubMed:9145105,
ECO:0000269|PubMed:9370472,
ECO:0000269|PubMed:9630892,
ECO:0000269|PubMed:9631088}.
MUTAGEN 155 155 D->V: In EBFP2.0; shifts the excitation
and emission spectra to shorter
wavelengths and increases quantum yields
compared to BFP; when associated with R-
30; N-39; H-66; A-72; T-105; V-128; F-
145; I-150; V-171; S-198; V-206 and V-
224. {ECO:0000269|PubMed:22891786}.
MUTAGEN 162 162 K->Q: In R10-3; matures to the red-
emitting state with excitation and
emission maxima at 555 and 585 nm,
respectively; when associated with L-46;
L-64; N-68; A-163; V-167 and L-171.
{ECO:0000269|PubMed:18366185}.
MUTAGEN 163 163 V->A: In GFPB; leads to enhanced
fluorescence at 37 degrees Celsius. In
GFPA; leads to even higher fluorescence
at 37 degrees Celsius than GFPA;
whenassociated with G-175. In
alphaGFP/cycle 3 GFP; improves folding at
37 degrees Celsius, reduces aggregation
at high concentrations, and increases the
diffusibility of the protein inside
cells; when associated with S-99 and T-
153. In R10-3; matures to the red-
emitting state with excitation and
emission maxima at 555 and 585 nm,
respectively; when associated with L-46;
L-64; N-68; Q-162; V-167 and L-171. In
ECFP; leads to cyan fluorescence, folds
faster and more efficiently at 37 degrees
Celsius and has superior solubility and
brightness; when associated with L-64; T-
65; W-66; I-146 and T-153. In Cerulean;
leads to improved quantum yield, a higher
extinction coefficient and is 2.5-fold
brighter than ECFP; when associated with
L-64; T-65; W-66; A-72; A-145; I-146; D-
148 and T-153. In Venus; leads to yellow
fluorescence, improved maturation and
reduced environmental sensitivity; when
associated with L-46; L-64; G-65; L-68;
A-72; T-153; G-175 and Y-203.
{ECO:0000269|PubMed:11299042,
ECO:0000269|PubMed:12370172,
ECO:0000269|PubMed:14990965,
ECO:0000269|PubMed:15065907,
ECO:0000269|PubMed:18366185,
ECO:0000269|PubMed:8994830,
ECO:0000269|PubMed:9370472,
ECO:0000269|PubMed:9630892,
ECO:0000269|PubMed:9631088}.
MUTAGEN 167 167 I->T: In P11; increases fluorescence at
475 nm excitation and at warmer
temperatures such as 37 degrees Celsius.
In Esmerald; leads to brighter
fluorescence; when associated with T-65;
A-72; K-149 and T-153. In VisGreen; leads
to brighter fluorescence; when associated
with L-64; T-65; A-72 and K-149.
{ECO:0000269|PubMed:17658219,
ECO:0000269|PubMed:7809066,
ECO:0000269|PubMed:9145105}.
MUTAGEN 167 167 I->V: In P9; increases fluorescence at
475 nm excitation. In R10-3; matures to
the red-emitting state with excitation
and emission maxima at 555 and 585 nm,
respectively; when associated with L-46;
L-64; N-68; Q-162; A-163 and L-171.
{ECO:0000269|PubMed:18366185,
ECO:0000269|PubMed:7809066}.
MUTAGEN 171 171 I->L: In R10-3; matures to the red-
emitting state with excitation and
emission maxima at 555 and 585 nm,
respectively; when associated with L-46;
L-64; N-68; Q-162; A-163 and V-167.
{ECO:0000269|PubMed:18366185}.
MUTAGEN 171 171 I->V: In EBFP1.2; shifts the excitation
and emission spectra to shorter
wavelengths and increases quantum yields
compared to BFP; when associated with R-
30; N-39; H-66; A-72; T-105; F-145; S-198
and V-206. In EBFP2.0; shifts the
excitation and emission spectra to
shorter wavelengths and increases quantum
yields compared to BFP; when associated
with R-30; N-39; H-66; A-72; T-105; V-
128; F-145; I-150; V-155; S-198; V-206
and V-224. {ECO:0000269|PubMed:22891786}.
MUTAGEN 175 175 S->G: In GFPA; leads to enhanced
fluorescence at 37 degrees Celsius; when
associated with A-163. In Venus; leads to
yellow fluorescence, improved maturation
and reduced environmental sensitivity;
when associated with L-46; L-64; G-65; L-
68; A-72; T-153; A-163 and Y-203.
{ECO:0000269|PubMed:12370172,
ECO:0000269|PubMed:8994830}.
MUTAGEN 176 176 V->A: In mut2.1; shifts fluorescence
lifetime from 3.03 to 2.50 ns; when
associated with H-145 and I-198.
{ECO:0000269|PubMed:16201762}.
MUTAGEN 193 193 V->A: In mut1.5; shifts fluorescence
lifetime from 3.03 to 2.72 ns; when
associated with H-145.
{ECO:0000269|PubMed:16201762}.
MUTAGEN 198 198 N->I: In mut2.1; shifts fluorescence
lifetime from 3.03 to 2.50 ns; when
associated with H-145 and A-176.
{ECO:0000269|PubMed:16201762}.
MUTAGEN 198 198 N->S: In EBFP1.2; shifts the excitation
and emission spectra to shorter
wavelengths and increases quantum yields
compared to BFP; when associated with R-
30; N-39; H-66; A-72; T-105; F-145; V-171
and V-206. In EBFP2.0; shifts the
excitation and emission spectra to
shorter wavelengths and increases quantum
yields compared to BFP; when associated
with R-30; N-39; H-66; A-72; T-105; V-
128; F-145; I-150; V-155; V-171; S-198
and V-224. {ECO:0000269|PubMed:22891786}.
MUTAGEN 202 202 S->F: In H9; increases fluorescence at
395 nm excitation; when associated with
I-203. {ECO:0000269|PubMed:7809066}.
MUTAGEN 203 203 T->H,W,F: Results in significantly red-
shifted excitation and emission maxima.
{ECO:0000269|PubMed:8703075}.
MUTAGEN 203 203 T->I: Suppresses the 475 nm excitation
peak, leaving only the shorter wavelength
peak at 399 nm. In H9; increases
fluorescence at 395 nm excitation; when
associated with I-203. In Sapphire/H9-40;
exhibits a huge Stoke's shift, with an
excitation peak at 399 nm and an emission
peak at 511 nm; when associated with A-72
and F-145. {ECO:0000269|PubMed:12769828,
ECO:0000269|PubMed:7796912,
ECO:0000269|PubMed:7809066}.
MUTAGEN 203 203 T->Y: Gives rise to yellow-emission
variants. In EYFP; leads to yellow
fluorescence, folds faster and more
efficiently at 37 degrees Celsius and has
superior solubility and brightness; when
associated with G-65; L-68 and A-72. In
Citrinine; leads to excitation and
emission peaks of 516 and 529 nm,
respectively; when associated with L-68;
M-69 and A-72. In YFP 10C; shifts the
major emission and exitation peak up to
20 nm; when associated with G-65; L-68
and A-72. In Topaz; shifts the major
emission and exitation peak up to 20 nm;
when associated with G-65; A-72 and R-79.
In Venus; leads to yellow fluorescence,
improved maturation and reduced
environmental sensitivity; when
associated with L-46; L-64; G-65; L-68;
A-72; T-153; A-163 and G-175.
{ECO:0000269|PubMed:11299042,
ECO:0000269|PubMed:11387331,
ECO:0000269|PubMed:12370172,
ECO:0000269|PubMed:9759496,
ECO:0000269|PubMed:9782051}.
MUTAGEN 206 206 A->K: Abolishes the tendency to dimerize
and leads to monomeric fluorescent
proteins. {ECO:0000269|PubMed:16739159}.
MUTAGEN 206 206 A->V: In EBFP1.2; shifts the excitation
and emission spectra to shorter
wavelengths and increases quantum yields
compared to BFP; when associated with R-
30; N-39; H-66; A-72; T-105; F-145; V-171
and S-198. In EBFP2.0; shifts the
excitation and emission spectra to
shorter wavelengths and increases quantum
yields compared to BFP; when associated
with R-30; N-39; H-66; A-72; T-105; V-
128; F-145; I-150; V-155; V-171; S-198
and V-206.
MUTAGEN 222 222 E->G: Suppresses the 399 nm excitation
peak, leaving only the longer wavelength
peak at 475 nm.
{ECO:0000269|PubMed:7796912}.
MUTAGEN 224 224 V->R: In Azurite; shifts the excitation
and emission spectra to shorter
wavelengths and increases quantum yields
compared to BFP; when associated with H-
66; R-80; F-145 and I-150. In EBFP2.0;
shifts the excitation and emission
spectra to shorter wavelengths and
increases quantum yields compared to BFP;
when associated with R-30; N-39; H-66; A-
72; T-105; V-128; F-145; I-150; V-155; V-
171; S-198 and V-206.
{ECO:0000269|PubMed:22891786}.
CONFLICT 2 2 S -> G (in Ref. 3; CAA65278).
{ECO:0000305}.
CONFLICT 25 25 H -> Q (in Ref. 3; CAA65278).
{ECO:0000305}.
CONFLICT 80 80 Q -> R (in Ref. 3; CAA65278).
{ECO:0000305}.
CONFLICT 157 157 Q -> P (in Ref. 2; AAA58246).
{ECO:0000305}.
CONFLICT 172 172 E -> K (in Ref. 2; AAA58246).
{ECO:0000305}.
HELIX 4 8 {ECO:0000244|PDB:2WUR}.
STRAND 12 22 {ECO:0000244|PDB:2WUR}.
STRAND 25 36 {ECO:0000244|PDB:2WUR}.
HELIX 37 39 {ECO:0000244|PDB:2WUR}.
STRAND 41 48 {ECO:0000244|PDB:2WUR}.
HELIX 57 60 {ECO:0000244|PDB:2WUR}.
HELIX 61 64 {ECO:0000244|PDB:2WUR}.
TURN 65 67 {ECO:0000244|PDB:1QYO}.
HELIX 69 71 {ECO:0000244|PDB:2WUR}.
HELIX 73 75 {ECO:0000244|PDB:3EVV}.
HELIX 76 81 {ECO:0000244|PDB:2WUR}.
HELIX 83 86 {ECO:0000244|PDB:2WUR}.
TURN 87 90 {ECO:0000244|PDB:2WUR}.
STRAND 92 100 {ECO:0000244|PDB:2WUR}.
STRAND 105 115 {ECO:0000244|PDB:2WUR}.
STRAND 118 128 {ECO:0000244|PDB:2WUR}.
STRAND 132 134 {ECO:0000244|PDB:1EMK}.
TURN 135 139 {ECO:0000244|PDB:2WUR}.
STRAND 143 145 {ECO:0000244|PDB:3OSQ}.
STRAND 146 148 {ECO:0000244|PDB:4IK8}.
STRAND 149 155 {ECO:0000244|PDB:2WUR}.
HELIX 156 158 {ECO:0000244|PDB:2WUR}.
STRAND 160 171 {ECO:0000244|PDB:2WUR}.
TURN 172 174 {ECO:0000244|PDB:4OGS}.
STRAND 176 191 {ECO:0000244|PDB:2WUR}.
STRAND 198 208 {ECO:0000244|PDB:2WUR}.
HELIX 209 213 {ECO:0000244|PDB:4IK8}.
STRAND 217 227 {ECO:0000244|PDB:2WUR}.
HELIX 233 236 {ECO:0000244|PDB:4GF6}.
SEQUENCE 238 AA; 26886 MW; EA5A6F21FBFB6E05 CRC64;
MSKGEELFTG VVPILVELDG DVNGHKFSVS GEGEGDATYG KLTLKFICTT GKLPVPWPTL
VTTFSYGVQC FSRYPDHMKQ HDFFKSAMPE GYVQERTIFF KDDGNYKTRA EVKFEGDTLV
NRIELKGIDF KEDGNILGHK LEYNYNSHNV YIMADKQKNG IKVNFKIRHN IEDGSVQLAD
HYQQNTPIGD GPVLLPDNHY LSTQSALSKD PNEKRDHMVL LEFVTAAGIT HGMDELYK


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