ID   CAH2_HUMAN              Reviewed;         260 AA.
AC   P00918; B2R7G8; Q6FI12; Q96ET9;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   02-SEP-2026, entry version 279.
DE   RecName: Full=Carbonic anhydrase 2;
DE            EC=4.2.1.1 {ECO:0000269|PubMed:12171926, ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:1910042, ECO:0000269|PubMed:4994926, ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:9398308};
DE   AltName: Full=Carbonate dehydratase II;
DE   AltName: Full=Carbonic anhydrase C;
DE            Short=CAC;
DE   AltName: Full=Carbonic anhydrase II;
DE            Short=CA-II;
DE   AltName: Full=Cyanamide hydratase CA2 {ECO:0000305};
DE            EC=4.2.1.69 {ECO:0000269|PubMed:10550681};
GN   Name=CA2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3108857; DOI=10.1093/nar/15.11.4687;
RA   Montgomery J.C., Venta P.J., Tashian R.E., Hewett-Emmett D.;
RT   "Nucleotide sequence of human liver carbonic anhydrase II cDNA.";
RL   Nucleic Acids Res. 15:4687-4687(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3121496; DOI=10.1016/0888-7543(87)90008-5;
RA   Murakami H., Marelich G.P., Grubb J.H., Kyle J.W., Sly W.S.;
RT   "Cloning, expression, and sequence homologies of cDNA for human carbonic
RT   anhydrase II.";
RL   Genomics 1:159-166(1987).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA   Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA   LaBaer J.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Urinary bladder;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-260, CLEAVAGE OF INITIATOR METHIONINE, AND
RP   ACETYLATION AT SER-2.
RX   PubMed=4207120; DOI=10.1016/s0021-9258(19)42734-8;
RA   Lin K.-T.D., Deutsch H.F.;
RT   "Human carbonic anhydrases. XII. The complete primary structure of the C
RT   isozyme.";
RL   J. Biol. Chem. 249:2329-2337(1974).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-260.
RX   PubMed=823150; DOI=10.1016/s0021-9258(17)33081-8;
RA   Henderson L.E., Henriksson D., Nyman P.O.;
RT   "Primary structure of human carbonic anhydrase C.";
RL   J. Biol. Chem. 251:5457-5463(1976).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RX   PubMed=3000449; DOI=10.1016/0167-4781(85)90006-5;
RA   Venta P.J., Montgomery J.C., Hewett-Emmett D., Tashian R.E.;
RT   "Comparison of the 5' regions of human and mouse carbonic anhydrase II
RT   genes and identification of possible regulatory elements.";
RL   Biochim. Biophys. Acta 826:195-201(1985).
RN   [10]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=4994926; DOI=10.1016/s0021-9258(18)62326-9;
RA   Khalifah R.G.;
RT   "The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow
RT   kinetic studies on the native human isoenzymes B and C.";
RL   J. Biol. Chem. 246:2561-2573(1971).
RN   [11]
RP   INTERACTION WITH SLC4A4.
RX   PubMed=14567693; DOI=10.1021/bi0353124;
RA   Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.;
RT   "Direct extracellular interaction between carbonic anhydrase IV and the
RT   human NBC1 sodium/bicarbonate co-transporter.";
RL   Biochemistry 42:12321-12329(2003).
RN   [12]
RP   INTERACTION WITH SLC4A7.
RX   PubMed=14736710; DOI=10.1152/ajpcell.00382.2003;
RA   Loiselle F.B., Morgan P.E., Alvarez B.V., Casey J.R.;
RT   "Regulation of the human NBC3 Na+/HCO3- cotransporter by carbonic anhydrase
RT   II and PKA.";
RL   Am. J. Physiol. 286:C1423-C1433(2004).
RN   [13]
RP   INTERACTION WITH SLC4A4.
RX   PubMed=15218065; DOI=10.1113/jphysiol.2004.065110;
RA   Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I.,
RA   Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I.;
RT   "Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal
RT   tubule cells.";
RL   J. Physiol. (Lond.) 559:55-65(2004).
RN   [14]
RP   FUNCTION, INTERACTION WITH SLC26A6, AND SUBCELLULAR LOCATION.
RX   PubMed=15990874; DOI=10.1038/sj.emboj.7600736;
RA   Alvarez B.V., Vilas G.L., Casey J.R.;
RT   "Metabolon disruption: a mechanism that regulates bicarbonate transport.";
RL   EMBO J. 24:2499-2511(2005).
RN   [15]
RP   ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17314045; DOI=10.1016/j.bmcl.2007.01.113;
RA   Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S.,
RA   Supuran C.T.;
RT   "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray
RT   crystal structure of the antiviral drug foscarnet complexed to human
RT   carbonic anhydrase I.";
RL   Bioorg. Med. Chem. Lett. 17:2210-2215(2007).
RN   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-172, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=4621826; DOI=10.1038/newbio235131a0;
RA   Liljas A., Kannan K.K., Bergsten P.-C., Waara I., Fridborg K.,
RA   Strandberg B., Carlbom U., Jaerup L., Loevgren S., Petef M.;
RT   "Crystal structure of human carbonic anhydrase C.";
RL   Nature New Biol. 235:131-137(1972).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ZINC ION.
RX   PubMed=3151019; DOI=10.1002/prot.340040406;
RA   Eriksson A.E., Jones T.A., Liljas A.;
RT   "Refined structure of human carbonic anhydrase II at 2.0-A resolution.";
RL   Proteins 4:274-282(1988).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP   INHIBITORS.
RX   PubMed=3151020; DOI=10.1002/prot.340040407;
RA   Eriksson A.E., Kylsten P.M., Jones T.A., Liljas A.;
RT   "Crystallographic studies of inhibitor binding sites in human carbonic
RT   anhydrase II: a pentacoordinated binding of the SCN-ion to the zinc at high
RT   pH.";
RL   Proteins 4:283-293(1988).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT SER-199 IN COMPLEX WITH
RP   ZINC ION, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF THR-199, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=1909891; DOI=10.1021/bi00102a005;
RA   Krebs J.F., Fierke C.A., Alexander R.S., Christianson D.W.;
RT   "Conformational mobility of His-64 in the Thr-200TO: human carbonic
RT   anhydrase II.";
RL   Biochemistry 30:9153-9160(1991).
RN   [22]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANTS PHE-142; TYR-142 AND
RP   HIS-142 IN COMPLEX WITH INHIBITORS, AND MUTAGENESIS OF VAL-142.
RX   PubMed=1932029; DOI=10.1021/bi00110a008;
RA   Alexander R.S., Nair S.K., Christianson D.W.;
RT   "Engineering the hydrophobic pocket of carbonic anhydrase II.";
RL   Biochemistry 30:11064-11072(1991).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT ALA-121, FUNCTION,
RP   CATALYTIC ACTIVITY, MUTAGENESIS OF VAL-121, AND ACTIVITY REGULATION.
RX   PubMed=1910042; DOI=10.1016/s0021-9258(19)47376-6;
RA   Nair S.K., Calderone T.L., Christianson D.W., Fierke C.A.;
RT   "Altering the mouth of a hydrophobic pocket. Structure and kinetics of
RT   human carbonic anhydrase II mutants at residue Val-121.";
RL   J. Biol. Chem. 266:17320-17325(1991).
RN   [24]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP   INHIBITORS, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=1336460; DOI=10.1111/j.1432-1033.1992.tb17490.x;
RA   Mangani S., Haakansson K.;
RT   "Crystallographic studies of the binding of protonated and unprotonated
RT   inhibitors to carbonic anhydrase using hydrogen sulphide and nitrate
RT   anions.";
RL   Eur. J. Biochem. 210:867-871(1992).
RN   [25]
RP   X-RAY CRYSTALLOGRAPHY (1.54 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP   INHIBITORS.
RX   PubMed=1433293; DOI=10.1016/0022-2836(92)90531-n;
RA   Haakansson K., Carlsson M., Svensson L.A., Liljas A.;
RT   "Structure of native and apo carbonic anhydrase II and structure of some of
RT   its anion-ligand complexes.";
RL   J. Mol. Biol. 227:1192-1204(1992).
RN   [26]
RP   X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) IN COMPLEX WITH COBALT ION AND
RP   BICARBONATE.
RX   PubMed=1474587; DOI=10.1016/0022-2836(92)90327-g;
RA   Haakansson K., Wehnert A.;
RT   "Structure of cobalt carbonic anhydrase complexed with bicarbonate.";
RL   J. Mol. Biol. 228:1212-1218(1992).
RN   [27]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF MUTANT CYS-94 IN COMPLEX WITH
RP   ZINC ION, AND MUTAGENESIS OF HIS-94.
RX   PubMed=8431430; DOI=10.1021/bi00057a015;
RA   Alexander R.S., Kiefer L.L., Fierke C.A., Christianson D.W.;
RT   "Engineering the zinc binding site of human carbonic anhydrase II:
RT   structure of the His-94-->Cys apoenzyme in a new crystalline form.";
RL   Biochemistry 32:1510-1518(1993).
RN   [28]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF MUTANT ALA-197; GLU-197; HIS-197
RP   AND ARG-197, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LEU-197.
RX   PubMed=8485129; DOI=10.1021/bi00068a005;
RA   Nair S.K., Christianson D.W.;
RT   "Structural consequences of hydrophilic amino acid substitutions in the
RT   hydrophobic pocket of human carbonic anhydrase II.";
RL   Biochemistry 32:4506-4514(1993).
RN   [29]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF MUTANT CYS-198 IN COMPLEX WITH
RP   ZINC ION, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF THR-198.
RX   PubMed=8399159; DOI=10.1021/bi00089a005;
RA   Ippolito J.A., Christianson D.W.;
RT   "Structure of an engineered His3Cys zinc binding site in human carbonic
RT   anhydrase II.";
RL   Biochemistry 32:9901-9905(1993).
RN   [30]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT ALA-201 IN COMPLEX WITH
RP   ZINC ION, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF PRO-201.
RX   PubMed=8218160; DOI=10.1021/bi00092a003;
RA   Tweedy N.B., Nair S.K., Paterno S.A., Fierke C.A., Christianson D.W.;
RT   "Structure and energetics of a non-proline cis-peptidyl linkage in a
RT   proline-202-->alanine carbonic anhydrase II variant.";
RL   Biochemistry 32:10944-10949(1993).
RN   [31]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH ZINC ION AND
RP   INHIBITORS.
RX   PubMed=8482389; DOI=10.1016/0014-5793(93)81565-h;
RA   Joensson B.M., Haakansson K., Liljas A.;
RT   "The structure of human carbonic anhydrase II in complex with bromide and
RT   azide.";
RL   FEBS Lett. 322:186-190(1993).
RN   [32]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF MUTANT VAL-198 IN COMPLEX WITH
RP   ZINC ION AND INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF
RP   THR-198, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=8262987; DOI=10.1016/s0021-9258(19)74269-0;
RA   Krebs J.F., Ippolito J.A., Christianson D.W., Fierke C.A.;
RT   "Structural and functional importance of a conserved hydrogen bond network
RT   in human carbonic anhydrase II.";
RL   J. Biol. Chem. 268:27458-27466(1993).
RN   [33]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR AND ZINC
RP   ION.
RX   PubMed=8331673; DOI=10.1006/jmbi.1993.1365;
RA   Mangani S., Liljas A.;
RT   "Crystal structure of the complex between human carbonic anhydrase II and
RT   the aromatic inhibitor 1,2,4-triazole.";
RL   J. Mol. Biol. 232:9-14(1993).
RN   [34]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANT HIS-199 IN COMPLEX WITH
RP   BICARBONATE AND ZINC ION, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP   THR-199.
RX   PubMed=8451242; DOI=10.1002/prot.340150110;
RA   Xue Y., Vidgren J., Svensson L.A., Liljas A., Jonsson B.H., Lindskog S.;
RT   "Crystallographic analysis of Thr-200-->His human carbonic anhydrase II and
RT   its complex with the substrate, HCO3-.";
RL   Proteins 15:80-87(1993).
RN   [35]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANTS IN COMPLEX WITH
RP   BICARBONATE AND ZINC ION, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP   GLU-106 AND THR-198.
RX   PubMed=7901850; DOI=10.1002/prot.340170112;
RA   Xue Y., Liljas A., Jonsson B.H., Lindskog S.;
RT   "Structural analysis of the zinc hydroxide-Thr-199-Glu-106 hydrogen-bond
RT   network in human carbonic anhydrase II.";
RL   Proteins 17:93-106(1993).
RN   [36]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH COBALT; COPPER;
RP   NICKEL AND MANGANESE IONS.
RX   PubMed=15299481; DOI=10.1107/s0907444993008790;
RA   Haakansson K., Wehnert A., Liljas A.;
RT   "X-ray analysis of metal-substituted human carbonic anhydrase II
RT   derivatives.";
RL   Acta Crystallogr. D 50:93-100(1994).
RN   [37]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) MUTANT GLN-106 IN COMPLEX WITH THE
RP   INHIBITOR ACETATE, AND MUTAGENESIS OF GLU-106.
RX   PubMed=15299482; DOI=10.1107/s0907444993009667;
RA   Haakansson K., Briand C., Zaitsev V., Xue Y., Liljas A.;
RT   "Wild-type and E106Q mutant carbonic anhydrase complexed with acetate.";
RL   Acta Crystallogr. D 50:101-104(1994).
RN   [38]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-259 OF MUTANTS ALA-94; CYS-94;
RP   CYS-96; CYS-119 AND ASP-119 IN COMPLEX WITH ZINC ION.
RX   PubMed=7803386; DOI=10.1021/bi00255a004;
RA   Ippolito J.A., Christianson D.W.;
RT   "Structural consequences of redesigning a protein-zinc binding site.";
RL   Biochemistry 33:15241-15249(1994).
RN   [39]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
RP   TRIFLUOROMETHANE SULFONAMIDE.
RX   PubMed=8070585; DOI=10.1016/0014-5793(94)00798-5;
RA   Haakansson K., Liljas A.;
RT   "The structure of a complex between carbonic anhydrase II and a new
RT   inhibitor, trifluoromethane sulphonamide.";
RL   FEBS Lett. 350:319-322(1994).
RN   [40]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=8142888; DOI=10.1002/pro.5560030115;
RA   Smith G.M., Alexander R.S., Christianson D.W., McKeever B.M.,
RA   Ponticello G.S., Springer J.P., Randall W.C., Baldwin J.J., Habecker C.N.;
RT   "Positions of His-64 and a bound water in human carbonic anhydrase II upon
RT   binding three structurally related inhibitors.";
RL   Protein Sci. 3:118-125(1994).
RN   [41]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS ARG-197; ASP-197 AND
RP   PHE-197 IN COMPLEX WITH THE INHIBITOR ACETAZOLAMIDE.
RX   PubMed=7696263; DOI=10.1021/bi00012a016;
RA   Nair S.K., Krebs J.F., Christianson D.W., Fierke C.A.;
RT   "Structural basis of inhibitor affinity to variants of human carbonic
RT   anhydrase II.";
RL   Biochemistry 34:3981-3989(1995).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=7608893; DOI=10.1021/jm00013a004;
RA   Boriack P.A., Christianson D.W., Kingery-Wood J., Whitesides G.M.;
RT   "Secondary interactions significantly removed from the sulfonamide binding
RT   pocket of carbonic anhydrase II influence inhibitor binding constants.";
RL   J. Med. Chem. 38:2286-2291(1995).
RN   [43]
RP   X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF MUTANTS ASP-198; GLU-198 AND
RP   HIS-198 IN COMPLEX WITH ZINC ION, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS
RP   OF THR-198, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=7761440; DOI=10.1073/pnas.92.11.5017;
RA   Ippolito J.A., Baird T.T. Jr., McGee S.A., Christianson D.W., Fierke C.A.;
RT   "Structure-assisted redesign of a protein-zinc-binding site with femtomolar
RT   affinity.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:5017-5021(1995).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF THE MUTANT GLN-117 IN COMPLEX
RP   WITH ZINC ION AND THE INHIBITOR ACETAZOLAMIDE, FUNCTION, CATALYTIC
RP   ACTIVITY, AND MUTAGENESIS OF GLU-117.
RX   PubMed=8639494; DOI=10.1021/bi9526692;
RA   Huang C.C., Lesburg C.A., Kiefer L.L., Fierke C.A., Christianson D.W.;
RT   "Reversal of the hydrogen bond to zinc ligand histidine-119 dramatically
RT   diminishes catalysis and enhances metal equilibration kinetics in carbonic
RT   anhydrase II.";
RL   Biochemistry 35:3439-3446(1996).
RN   [45]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF MUTANTS GLY-65; HIS-65; LEU-65;
RP   PHE-65; SER-65 AND THR-65 IN COMPLEX WITH ZINC ION.
RX   PubMed=8987974; DOI=10.1021/bi9617872;
RA   Scolnick L.R., Christianson D.W.;
RT   "X-ray crystallographic studies of alanine-65 variants of carbonic
RT   anhydrase II reveal the structural basis of compromised proton transfer in
RT   catalysis.";
RL   Biochemistry 35:16429-16434(1996).
RN   [46]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
RP   DANSYLAMIDE.
RX   PubMed=8557623; DOI=10.1074/jbc.271.2.1003;
RA   Nair S.K., Elbaum D., Christianson D.W.;
RT   "Unexpected binding mode of the sulfonamide fluorophore 5-dimethylamino-1-
RT   naphthalene sulfonamide to human carbonic anhydrase II. Implications for
RT   the development of a zinc biosensor.";
RL   J. Biol. Chem. 271:1003-1007(1996).
RN   [47]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH THE ACTIVATOR
RP   HISTAMINE, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=9265618; DOI=10.1021/bi970760v;
RA   Briganti F., Mangani S., Orioli P., Scozzafava A., Vernaglione G.,
RA   Supuran C.T.;
RT   "Carbonic anhydrase activators: X-ray crystallographic and spectroscopic
RT   investigations for the interaction of isozymes I and II with histamine.";
RL   Biochemistry 36:10384-10392(1997).
RN   [48]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANTS ASN-94; ASN-119 AND
RP   GLN-119 IN COMPLEX WITH ZINC ION, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS
RP   OF HIS-94 AND HIS-119, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9398308; DOI=10.1021/bi971296x;
RA   Lesburg C.A., Huang C., Christianson D.W., Fierke C.A.;
RT   "Histidine --> carboxamide ligand substitutions in the zinc binding site of
RT   carbonic anhydrase II alter metal coordination geometry but retain
RT   catalytic activity.";
RL   Biochemistry 36:15780-15791(1997).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR
RP   BRINZOLAMIDE.
RX   PubMed=9541386; DOI=10.1002/pro.5560070303;
RA   Stams T., Chen Y., Boriack-Sjodin P.A., Hurt J.D., Liao J., May J.A.,
RA   Dean T., Laipis P., Silverman D.N., Christianson D.W.;
RT   "Structures of murine carbonic anhydrase IV and human carbonic anhydrase II
RT   complexed with brinzolamide: molecular basis of isozyme-drug
RT   discrimination.";
RL   Protein Sci. 7:556-563(1998).
RN   [50]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH SULFONAMIDE
RP   INHIBITORS AND ZINC ION.
RX   PubMed=9865942; DOI=10.1002/pro.5560071201;
RA   Boriack-Sjodin P.A., Zeitlin S., Chen H.H., Crenshaw L., Gross S.,
RA   Dantanarayana A., Delgado P., May J.A., Dean T., Christianson D.W.;
RT   "Structural analysis of inhibitor binding to human carbonic anhydrase II.";
RL   Protein Sci. 7:2483-2489(1998).
RN   [51]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CYANAMIDE AND
RP   SUBSTRATE, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=10550681; DOI=10.1007/s007750050375;
RA   Briganti F., Mangani S., Scozzafava A., Vernaglione G., Supuran C.T.;
RT   "Carbonic anhydrase catalyzes cyanamide hydration to urea: is it mimicking
RT   the physiological reaction?";
RL   J. Biol. Inorg. Chem. 4:528-536(1999).
RN   [52]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH CYANAMIDE, FUNCTION,
RP   AND CATALYTIC ACTIVITY.
RX   PubMed=11015219; DOI=10.1021/bi000937c;
RA   Guerri A., Briganti F., Scozzafava A., Supuran C.T., Mangani S.;
RT   "Mechanism of cyanamide hydration catalyzed by carbonic anhydrase II
RT   suggested by cryogenic X-ray diffraction.";
RL   Biochemistry 39:12391-12397(2000).
RN   [53]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF MUTANTS ILE-93/MET-95/VAL-97 AND
RP   SER-93/LEU-95/MET-97 IN COMPLEX WITH COBALT; COPPER AND ZINC IONS.
RX   PubMed=11076507; DOI=10.1021/bi001649j;
RA   Cox J.D., Hunt J.A., Compher K.M., Fierke C.A., Christianson D.W.;
RT   "Structural influence of hydrophobic core residues on metal binding and
RT   specificity in carbonic anhydrase II.";
RL   Biochemistry 39:13687-13694(2000).
RN   [54]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX WITH
RP   4-METHYLIMIDAZOLE, FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-64.
RX   PubMed=11327835; DOI=10.1021/bi002295z;
RA   Duda D., Tu C., Qian M., Laipis P., Agbandje-McKenna M., Silverman D.N.,
RA   McKenna R.;
RT   "Structural and kinetic analysis of the chemical rescue of the proton
RT   transfer function of carbonic anhydrase II.";
RL   Biochemistry 40:1741-1748(2001).
RN   [55]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF MUTANT VAL-130 IN COMPLEX WITH
RP   FLUOROAROMATIC INHIBITORS.
RX   PubMed=11572683; DOI=10.1021/ja011034p;
RA   Kim C.Y., Chandra P.P., Jain A., Christianson D.W.;
RT   "Fluoroaromatic-fluoroaromatic interactions between inhibitors bound in the
RT   crystal lattice of human carbonic anhydrase II.";
RL   J. Am. Chem. Soc. 123:9620-9627(2001).
RN   [56]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH THE INHIBITOR SUGAR
RP   SULFAMATE RWJ-37497, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11802772; DOI=10.1042/0264-6021:3610437;
RA   Recacha R., Costanzo M.J., Maryanoff B.E., Chattopadhyay D.;
RT   "Crystal structure of human carbonic anhydrase II complexed with an anti-
RT   convulsant sugar sulphamate.";
RL   Biochem. J. 361:437-441(2002).
RN   [57]
RP   X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF THE MUTANT PRO-198/SER-205 IN
RP   COMPLEX WITH BICARBONATE AND INHIBITORS, FUNCTION, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF THR-198.
RX   PubMed=12056894; DOI=10.1021/bi020053o;
RA   Huang S., Sjoeblom B., Sauer-Eriksson A.E., Jonsson B.H.;
RT   "Organization of an efficient carbonic anhydrase: implications for the
RT   mechanism based on structure-function studies of a T199P/C206S mutant.";
RL   Biochemistry 41:7628-7635(2002).
RN   [58]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF THE MUTANT HIS-7, FUNCTION,
RP   CATALYTIC ACTIVITY, AND MUTAGENESIS OF TYR-7.
RX   PubMed=12171926; DOI=10.1074/jbc.m205791200;
RA   Tu C., Qian M., An H., Wadhwa N.R., Duda D., Yoshioka C., Pathak Y.,
RA   McKenna R., Laipis P.J., Silverman D.N.;
RT   "Kinetic analysis of multiple proton shuttles in the active site of human
RT   carbonic anhydrase.";
RL   J. Biol. Chem. 277:38870-38876(2002).
RN   [59]
RP   X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH INHIBITORS,
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=11831900; DOI=10.1021/jm010163d;
RA   Kim C.Y., Whittington D.A., Chang J.S., Liao J., May J.A.,
RA   Christianson D.W.;
RT   "Structural aspects of isozyme selectivity in the binding of inhibitors to
RT   carbonic anhydrases II and IV.";
RL   J. Med. Chem. 45:888-893(2002).
RN   [60]
RP   X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=12166932; DOI=10.1021/jm011112j;
RA   Grueneberg S., Stubbs M.T., Klebe G.;
RT   "Successful virtual screening for novel inhibitors of human carbonic
RT   anhydrase: strategy and experimental confirmation.";
RL   J. Med. Chem. 45:3588-3602(2002).
RN   [61]
RP   X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=11818565; DOI=10.1073/pnas.032673399;
RA   Grzybowski B.A., Ishchenko A.V., Kim C.Y., Topalov G., Chapman R.,
RA   Christianson D.W., Whitesides G.M., Shakhnovich E.I.;
RT   "Combinatorial computational method gives new picomolar ligands for a known
RT   enzyme.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:1270-1273(2002).
RN   [62]
RP   X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF THE MUTANT ALA-64 IN COMPLEX WITH
RP   THE INHIBITOR 4-METHYLIMIDAZOLE AND ZINC ION.
RX   PubMed=12499545; DOI=10.1107/s0907444902019455;
RA   Duda D., Govindasamy L., Agbandje-McKenna M., Tu C., Silverman D.N.,
RA   McKenna R.;
RT   "The refined atomic structure of carbonic anhydrase II at 1.05 A
RT   resolution: implications of chemical rescue of proton transfer.";
RL   Acta Crystallogr. D 59:93-104(2003).
RN   [63]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ACTIVITY
RP   REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=14736236; DOI=10.1021/jm030912m;
RA   Weber A., Casini A., Heine A., Kuhn D., Supuran C.T., Scozzafava A.,
RA   Klebe G.;
RT   "Unexpected nanomolar inhibition of carbonic anhydrase by COX-2-selective
RT   celecoxib: new pharmacological opportunities due to related binding site
RT   recognition.";
RL   J. Med. Chem. 47:550-557(2004).
RN   [64]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THE ANTI-CANCER
RP   AGENT 667-COUMATE, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15453828; DOI=10.1042/bj20041037;
RA   Lloyd M.D., Pederick R.L., Natesh R., Woo L.W., Purohit A., Reed M.J.,
RA   Acharya K.R., Potter B.V.;
RT   "Crystal structure of human carbonic anhydrase II at 1.95 A resolution in
RT   complex with 667-coumate, a novel anti-cancer agent.";
RL   Biochem. J. 385:715-720(2005).
RN   [65]
RP   X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS), MUTAGENESIS OF ASN-62; HIS-64 AND
RP   ASN-67, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=15667203; DOI=10.1021/bi0480279;
RA   Fisher Z., Hernandez Prada J.A., Tu C., Duda D., Yoshioka C., An H.,
RA   Govindasamy L., Silverman D.N., McKenna R.;
RT   "Structural and kinetic characterization of active-site histidine as a
RT   proton shuttle in catalysis by human carbonic anhydrase II.";
RL   Biochemistry 44:1097-1105(2005).
RN   [66]
RP   X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH DUAL
RP   AROMATASE-STEROID SULFATASE INHIBITORS, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15865431; DOI=10.1021/bi047692e;
RA   Lloyd M.D., Thiyagarajan N., Ho Y.T., Woo L.W., Sutcliffe O.B., Purohit A.,
RA   Reed M.J., Acharya K.R., Potter B.V.;
RT   "First crystal structures of human carbonic anhydrase II in complex with
RT   dual aromatase-steroid sulfatase inhibitors.";
RL   Biochemistry 44:6858-6866(2005).
RN   [67]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ACTIVATOR
RP   L-HISTIDINE, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX   PubMed=16214338; DOI=10.1016/j.bmcl.2005.08.069;
RA   Temperini C., Scozzafava A., Puccetti L., Supuran C.T.;
RT   "Carbonic anhydrase activators: X-ray crystal structure of the adduct of
RT   human isozyme II with L-histidine as a platform for the design of stronger
RT   activators.";
RL   Bioorg. Med. Chem. Lett. 15:5136-5141(2005).
RN   [68]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX   PubMed=16134940; DOI=10.1021/jm050333c;
RA   Menchise V., De Simone G., Alterio V., Di Fiore A., Pedone C.,
RA   Scozzafava A., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors: stacking with Phe131 determines active site
RT   binding region of inhibitors as exemplified by the X-ray crystal structure
RT   of a membrane-impermeant antitumor sulfonamide complexed with isozyme II.";
RL   J. Med. Chem. 48:5721-5727(2005).
RN   [69]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, AND
RP   MUTAGENESIS OF HIS-64 AND THR-199.
RX   PubMed=16106378; DOI=10.1002/prot.20615;
RA   Bhatt D., Tu C., Fisher S.Z., Hernandez Prada J.A., McKenna R.,
RA   Silverman D.N.;
RT   "Proton transfer in a Thr200His mutant of human carbonic anhydrase II.";
RL   Proteins 61:239-245(2005).
RN   [70]
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RX   PubMed=16511248; DOI=10.1107/s1744309105038248;
RA   Budayova-Spano M., Fisher S.Z., Dauvergne M.T., Agbandje-McKenna M.,
RA   Silverman D.N., Myles D.A., McKenna R.;
RT   "Production and X-ray crystallographic analysis of fully deuterated human
RT   carbonic anhydrase II.";
RL   Acta Crystallogr. F 62:6-9(2006).
RN   [71]
RP   X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=16820676; DOI=10.1107/s1744309106020446;
RA   Fisher S.Z., Govindasamy L., Boyle N., Agbandje-McKenna M., Silverman D.N.,
RA   Blackburn G.M., McKenna R.;
RT   "X-ray crystallographic studies reveal that the incorporation of spacer
RT   groups in carbonic anhydrase inhibitors causes alternate binding modes.";
RL   Acta Crystallogr. F 62:618-622(2006).
RN   [72]
RP   X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS
RP   VALDECOXIB AND CELECOXIB, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=16290146; DOI=10.1016/j.bmcl.2005.09.040;
RA   Di Fiore A., Pedone C., D'Ambrosio K., Scozzafava A., De Simone G.,
RA   Supuran C.T.;
RT   "Carbonic anhydrase inhibitors: Valdecoxib binds to a different active site
RT   region of the human isoform II as compared to the structurally related
RT   cyclooxygenase II 'selective' inhibitor celecoxib.";
RL   Bioorg. Med. Chem. Lett. 16:437-442(2006).
RN   [73]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH N-HYDROXYUREA,
RP   ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16759856; DOI=10.1016/j.bmcl.2006.05.068;
RA   Temperini C., Innocenti A., Scozzafava A., Supuran C.T.;
RT   "N-hydroxyurea -- a versatile zinc binding function in the design of
RT   metalloenzyme inhibitors.";
RL   Bioorg. Med. Chem. Lett. 16:4316-4320(2006).
RN   [74]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=17000110; DOI=10.1016/j.bmcl.2006.09.022;
RA   Menchise V., De Simone G., Di Fiore A., Scozzafava A., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors: X-ray crystallographic studies for the
RT   binding of 5-amino-1,3,4-thiadiazole-2-sulfonamide and 5-(4-amino-3-chloro-
RT   5-fluorophenylsulfonamido)-1,3,4-thiadiazole-2-sulfonamide to human isoform
RT   II.";
RL   Bioorg. Med. Chem. Lett. 16:6204-6208(2006).
RN   [75]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH L- AND D-HISTIDINE,
RP   ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16807956; DOI=10.1002/chem.200600159;
RA   Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
RT   "Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII,
RT   and XIV with l- and d-histidine and crystallographic analysis of their
RT   adducts with isoform II: engineering proton-transfer processes within the
RT   active site of an enzyme.";
RL   Chemistry 12:7057-7066(2006).
RN   [76]
RP   X-RAY CRYSTALLOGRAPHY (0.99 ANGSTROMS) IN COMPLEX WITH TWO-PRONG
RP   INHIBITORS.
RX   PubMed=16506782; DOI=10.1021/ja057257n;
RA   Jude K.M., Banerjee A.L., Haldar M.K., Manokaran S., Roy B., Mallik S.,
RA   Srivastava D.K., Christianson D.W.;
RT   "Ultrahigh resolution crystal structures of human carbonic anhydrases I and
RT   II complexed with 'two-prong' inhibitors reveal the molecular basis of high
RT   affinity.";
RL   J. Am. Chem. Soc. 128:3011-3018(2006).
RN   [77]
RP   X-RAY CRYSTALLOGRAPHY (1.71 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX   PubMed=16787097; DOI=10.1021/ja061574s;
RA   Alterio V., Vitale R.M., Monti S.M., Pedone C., Scozzafava A., Cecchi A.,
RA   De Simone G., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors: X-ray and molecular modeling study for the
RT   interaction of a fluorescent antitumor sulfonamide with isozyme II and
RT   IX.";
RL   J. Am. Chem. Soc. 128:8329-8335(2006).
RN   [78]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH L- AND
RP   D-PHENYLALANINE, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16686544; DOI=10.1021/jm0603320;
RA   Temperini C., Scozzafava A., Vullo D., Supuran C.T.;
RT   "Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII,
RT   and XIV with L- and D-phenylalanine and crystallographic analysis of their
RT   adducts with isozyme II: stereospecific recognition within the active site
RT   of an enzyme and its consequences for the drug design.";
RL   J. Med. Chem. 49:3019-3027(2006).
RN   [79]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX   PubMed=16942027; DOI=10.1021/jm060531j;
RA   De Simone G., Vitale R.M., Di Fiore A., Pedone C., Scozzafava A.,
RA   Montero J.-L., Winum J.-Y., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors: Hypoxia-activatable sulfonamides
RT   incorporating disulfide bonds that target the tumor-associated isoform
RT   IX.";
RL   J. Med. Chem. 49:5544-5551(2006).
RN   [80]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITOR.
RX   PubMed=17125255; DOI=10.1021/jm060807n;
RA   Winum J.Y., Temperini C., El Cheikh K., Innocenti A., Vullo D.,
RA   Ciattini S., Montero J.-L., Scozzafava A., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors: clash with Ala65 as a means for designing
RT   inhibitors with low affinity for the ubiquitous isozyme II, exemplified by
RT   the crystal structure of the topiramate sulfamide analogue.";
RL   J. Med. Chem. 49:7024-7031(2006).
RN   [81]
RP   X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=17181151; DOI=10.1021/jm060705x;
RA   Leese M.P., Leblond B., Smith A., Newman S.P., Di Fiore A., De Simone G.,
RA   Supuran C.T., Purohit A., Reed M.J., Potter B.V.;
RT   "2-substituted estradiol bis-sulfamates, multitargeted antitumor agents:
RT   synthesis, in vitro SAR, protein crystallography, and in vivo activity.";
RL   J. Med. Chem. 49:7683-7696(2006).
RN   [82]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH SACCHARIN, ACTIVITY
RP   REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17705204; DOI=10.1002/anie.200701189;
RA   Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A.,
RA   Supuran C.T., Klebe G.;
RT   "Saccharin inhibits carbonic anhydrases: possible explanation for its
RT   unpleasant metallic aftertaste.";
RL   Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007).
RN   [83]
RP   X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS).
RX   PubMed=17319692; DOI=10.1021/bi062066y;
RA   Fisher S.Z., Maupin C.M., Budayova-Spano M., Govindasamy L., Tu C.,
RA   Agbandje-McKenna M., Silverman D.N., Voth G.A., McKenna R.;
RT   "Atomic crystal and molecular dynamics simulation structures of human
RT   carbonic anhydrase II: insights into the proton transfer mechanism.";
RL   Biochemistry 46:2930-2937(2007).
RN   [84]
RP   X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS), MUTAGENESIS OF TYR-7; ASN-62 AND
RP   ASN-67, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17330962; DOI=10.1021/bi602620k;
RA   Fisher S.Z., Tu C., Bhatt D., Govindasamy L., Agbandje-McKenna M.,
RA   McKenna R., Silverman D.N.;
RT   "Speeding up proton transfer in a fast enzyme: kinetic and crystallographic
RT   studies on the effect of hydrophobic amino acid substitutions in the active
RT   site of human carbonic anhydrase II.";
RL   Biochemistry 46:3803-3813(2007).
RN   [85]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ACTIVATOR
RP   L-ADRENALINE, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17127057; DOI=10.1016/j.bmcl.2006.11.027;
RA   Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.;
RT   "Carbonic anhydrase activators: L-Adrenaline plugs the active site entrance
RT   of isozyme II, activating better isoforms I, IV, VA, VII, and XIV.";
RL   Bioorg. Med. Chem. Lett. 17:628-635(2007).
RN   [86]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) IN COMPLEX WITH INHIBITOR, FUNCTION,
RP   AND CATALYTIC ACTIVITY.
RX   PubMed=17251017; DOI=10.1016/j.bmcl.2006.12.099;
RA   Di Fiore A., Scozzafava A., Winum J.-Y., Montero J.-L., Pedone C.,
RA   Supuran C.T., De Simone G.;
RT   "Carbonic anhydrase inhibitors: binding of an antiglaucoma glycosyl-
RT   sulfanilamide derivative to human isoform II and its consequences for the
RT   drug design of enzyme inhibitors incorporating sugar moieties.";
RL   Bioorg. Med. Chem. Lett. 17:1726-1731(2007).
RN   [87]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP   N-HYDROXYSULFAMIDE, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17346964; DOI=10.1016/j.bmcl.2007.02.068;
RA   Temperini C., Winum J.Y., Montero J.L., Scozzafava A., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors: the X-ray crystal structure of the adduct
RT   of N-hydroxysulfamide with isozyme II explains why this new zinc binding
RT   function is effective in the design of potent inhibitors.";
RL   Bioorg. Med. Chem. Lett. 17:2795-2801(2007).
RN   [88]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ACTIVITY
RP   REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17540563; DOI=10.1016/j.bmcl.2007.05.045;
RA   Alterio V., De Simone G., Monti S.M., Scozzafava A., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors: inhibition of human, bacterial, and
RT   archaeal isozymes with benzene-1,3-disulfonamides -- solution and
RT   crystallographic studies.";
RL   Bioorg. Med. Chem. Lett. 17:4201-4207(2007).
RN   [89]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ACTIVITY
RP   REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17588751; DOI=10.1016/j.bmcl.2007.06.044;
RA   Temperini C., Innocenti A., Mastrolorenzo A., Scozzafava A., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors. Interaction of the antiepileptic drug
RT   sulthiame with twelve mammalian isoforms: kinetic and X-ray
RT   crystallographic studies.";
RL   Bioorg. Med. Chem. Lett. 17:4866-4872(2007).
RN   [90]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH 4-METHYLIMIDAZOLE,
RP   AND MUTAGENESIS OF TRP-5 AND HIS-64.
RX   PubMed=17071654; DOI=10.1529/biophysj.106.093203;
RA   Bhatt D., Fisher S.Z., Tu C., McKenna R., Silverman D.N.;
RT   "Location of binding sites in small molecule rescue of human carbonic
RT   anhydrase II.";
RL   Biophys. J. 92:562-570(2007).
RN   [91]
RP   X-RAY CRYSTALLOGRAPHY (1.01 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=17407288; DOI=10.1021/ja068359w;
RA   Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S.,
RA   Kooren J., Mallik S., Christianson D.W.;
RT   "Structural analysis of charge discrimination in the binding of inhibitors
RT   to human carbonic anhydrases I and II.";
RL   J. Am. Chem. Soc. 129:5528-5537(2007).
RN   [92]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH INHIBITOR
RP   THIOXOLONE, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18266323; DOI=10.1021/bi702385k;
RA   Barrese A.A. III, Genis C., Fisher S.Z., Orwenyo J.N., Kumara M.T.,
RA   Dutta S.K., Phillips E., Kiddle J.J., Tu C., Silverman D.N.,
RA   Govindasamy L., Agbandje-McKenna M., McKenna R., Tripp B.C.;
RT   "Inhibition of carbonic anhydrase II by thioxolone: a mechanistic and
RT   structural study.";
RL   Biochemistry 47:3174-3184(2008).
RN   [93]
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF MUTANTS, MUTAGENESIS OF ASN-62,
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18942852; DOI=10.1021/bi801473w;
RA   Zheng J., Avvaru B.S., Tu C., McKenna R., Silverman D.N.;
RT   "Role of hydrophilic residues in proton transfer during catalysis by human
RT   carbonic anhydrase II.";
RL   Biochemistry 47:12028-12036(2008).
RN   [94]
RP   X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ACTIVITY
RP   REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18024029; DOI=10.1016/j.bmcl.2007.10.110;
RA   Guezel O., Temperini C., Innocenti A., Scozzafava A., Salman A.,
RA   Supuran C.T.;
RT   "Carbonic anhydrase inhibitors. Interaction of 2-(hydrazinocarbonyl)-3-
RT   phenyl-1H-indole-5-sulfonamide with 12 mammalian isoforms: kinetic and X-
RT   ray crystallographic studies.";
RL   Bioorg. Med. Chem. Lett. 18:152-158(2008).
RN   [95]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ACTIVITY
RP   REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18162396; DOI=10.1016/j.bmcl.2007.12.022;
RA   Temperini C., Cecchi A., Boyle N.A., Scozzafava A., Cabeza J.E.,
RA   Wentworth P. Jr., Blackburn G.M., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors. Interaction of 2-N,N-dimethylamino-1,3,4-
RT   thiadiazole-5-methanesulfonamide with 12 mammalian isoforms: kinetic and X-
RT   ray crystallographic studies.";
RL   Bioorg. Med. Chem. Lett. 18:999-1005(2008).
RN   [96]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ACTIVITY
RP   REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18374572; DOI=10.1016/j.bmcl.2008.03.051;
RA   Temperini C., Cecchi A., Scozzafava A., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors. Interaction of indapamide and related
RT   diuretics with 12 mammalian isozymes and X-ray crystallographic studies for
RT   the indapamide-isozyme II adduct.";
RL   Bioorg. Med. Chem. Lett. 18:2567-2573(2008).
RN   [97]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=18359629; DOI=10.1016/j.bmcl.2008.03.023;
RA   Di Fiore A., Pedone C., Antel J., Waldeck H., Witte A., Wurl M.,
RA   Scozzafava A., Supuran C.T., De Simone G.;
RT   "Carbonic anhydrase inhibitors: the X-ray crystal structure of
RT   ethoxzolamide complexed to human isoform II reveals the importance of
RT   thr200 and gln92 for obtaining tight-binding inhibitors.";
RL   Bioorg. Med. Chem. Lett. 18:2669-2674(2008).
RN   [98]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ACTIVITY
RP   REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18640037; DOI=10.1016/j.bmcl.2008.06.105;
RA   Temperini C., Innocenti A., Scozzafava A., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors. Interaction of the antitumor sulfamate EMD
RT   486019 with twelve mammalian carbonic anhydrase isoforms: Kinetic and X-ray
RT   crystallographic studies.";
RL   Bioorg. Med. Chem. Lett. 18:4282-4286(2008).
RN   [99]
RP   X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH INHIBITORS
RP   INDANESULFONAMIDES.
RX   PubMed=18161740; DOI=10.1002/cmdc.200700274;
RA   D'Ambrosio K., Masereel B., Thiry A., Scozzafava A., Supuran C.T.,
RA   De Simone G.;
RT   "Carbonic anhydrase inhibitors: binding of indanesulfonamides to the human
RT   isoform II.";
RL   ChemMedChem 3:473-477(2008).
RN   [100]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH (129)XE-CRYPTOPHANE
RP   BIOSENSOR.
RX   PubMed=18461940; DOI=10.1021/ja802214x;
RA   Aaron J.A., Chambers J.M., Jude K.M., Di Costanzo L., Dmochowski I.J.,
RA   Christianson D.W.;
RT   "Structure of a (129)Xe-cryptophane biosensor complexed with human carbonic
RT   anhydrase II.";
RL   J. Am. Chem. Soc. 130:6942-6943(2008).
RN   [101]
RP   X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH CO2.
RX   PubMed=18768466; DOI=10.1074/jbc.m805353200;
RA   Domsic J.F., Avvaru B.S., Kim C.U., Gruner S.M., Agbandje-McKenna M.,
RA   Silverman D.N., McKenna R.;
RT   "Entrapment of carbon dioxide in the active site of carbonic anhydrase
RT   II.";
RL   J. Biol. Chem. 283:30766-30771(2008).
RN   [102]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=18260615; DOI=10.1021/jm701319c;
RA   Leese M.P., Jourdan F.L., Gaukroger K., Mahon M.F., Newman S.P.,
RA   Foster P.A., Stengel C., Regis-Lydi S., Ferrandis E., Di Fiore A.,
RA   De Simone G., Supuran C.T., Purohit A., Reed M.J., Potter B.V.;
RT   "Structure-activity relationships of C-17 cyano-substituted estratrienes as
RT   anticancer agents.";
RL   J. Med. Chem. 51:1295-1308(2008).
RN   [103]
RP   X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ACTIVITY
RP   REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=18481843; DOI=10.1021/jm800121c;
RA   D'Ambrosio K., Vitale R.-M., Dogne J.-M., Masereel B., Innocenti A.,
RA   Scozzafava A., De Simone G., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors: bioreductive nitro-containing sulfonamides
RT   with selectivity for targeting the tumor associated isoforms IX and XII.";
RL   J. Med. Chem. 51:3230-3237(2008).
RN   [104]
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=18723489; DOI=10.1158/1535-7163.mct-08-0195;
RA   Woo L.W.L., Fischer D.S., Sharland C.M., Trusselle M., Foster P.A.,
RA   Chander S.K., Di Fiore A., Supuran C.T., De Simone G., Purohit A.,
RA   Reed M.J., Potter B.V.L.;
RT   "Anticancer steroid sulfatase inhibitors: synthesis of a potent fluorinated
RT   second-generation agent, in vitro and in vivo activities, molecular
RT   modeling, and protein crystallography.";
RL   Mol. Cancer Ther. 7:2435-2444(2008).
RN   [105]
RP   X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH INHIBITORS, ACTIVITY
RP   REGULATION, MUTAGENESIS OF ALA-65 AND ASN-67, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=19170619; DOI=10.1021/bi802035f;
RA   Genis C., Sippel K.H., Case N., Cao W., Avvaru B.S., Tartaglia L.J.,
RA   Govindasamy L., Tu C., Agbandje-McKenna M., Silverman D.N., Rosser C.J.,
RA   McKenna R.;
RT   "Design of a carbonic anhydrase IX active-site mimic to screen inhibitors
RT   for possible anticancer properties.";
RL   Biochemistry 48:1322-1331(2009).
RN   [106]
RP   X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) FREE AND IN COMPLEX WITH ZINC ION,
RP   AND COFACTOR.
RX   PubMed=19583303; DOI=10.1021/bi9007512;
RA   Avvaru B.S., Busby S.A., Chalmers M.J., Griffin P.R., Venkatakrishnan B.,
RA   Agbandje-McKenna M., Silverman D.N., McKenna R.;
RT   "Apo-human carbonic anhydrase II revisited: implications of the loss of a
RT   metal in protein structure, stability, and solvent network.";
RL   Biochemistry 48:7365-7372(2009).
RN   [107]
RP   X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITOR
RP   THIABENDAZOLE-5-SULFONAMIDE, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC
RP   ACTIVITY.
RX   PubMed=19186056; DOI=10.1016/j.bmcl.2009.01.038;
RA   Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A.,
RA   Muehlschlegel F.A., Supuran C.T.;
RT   "A thiabendazole sulfonamide shows potent inhibitory activity against
RT   mammalian and nematode alpha-carbonic anhydrases.";
RL   Bioorg. Med. Chem. Lett. 19:1371-1375(2009).
RN   [108]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-260 IN COMPLEX WITH COUMARIN
RP   INHIBITORS, ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=19206230; DOI=10.1021/ja809683v;
RA   Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A.,
RA   Quinn R.J., Supuran C.T.;
RT   "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new
RT   class of suicide inhibitors.";
RL   J. Am. Chem. Soc. 131:3057-3062(2009).
RN   [109]
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=19115843; DOI=10.1021/jm801386n;
RA   Temperini C., Cecchi A., Scozzafava A., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors. Comparison of chlorthalidone and indapamide
RT   X-ray crystal structures in adducts with isozyme II: when three water
RT   molecules and the keto-enol tautomerism make the difference.";
RL   J. Med. Chem. 52:322-328(2009).
RN   [110]
RP   X-RAY CRYSTALLOGRAPHY (1.41 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX   PubMed=19731956; DOI=10.1021/jm900641r;
RA   Vitale R.M., Alterio V., Innocenti A., Winum J.-Y., Monti S.M.,
RA   De Simone G., Supuran C.T.;
RT   "Carbonic anhydrase inhibitors. Comparison of aliphatic sulfamate/bis-
RT   sulfamate adducts with isozymes II and IX as a platform for designing
RT   tight-binding, more isoform-selective inhibitors.";
RL   J. Med. Chem. 52:5990-5998(2009).
RN   [111]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITORS.
RX   PubMed=19827837; DOI=10.1021/jm900914e;
RA   Lopez M., Paul B., Hofmann A., Morizzi J., Wu Q.K., Charman S.A.,
RA   Innocenti A., Vullo D., Supuran C.T., Poulsen S.-A.;
RT   "S-glycosyl primary sulfonamides--a new structural class for selective
RT   inhibition of cancer-associated carbonic anhydrases.";
RL   J. Med. Chem. 52:6421-6432(2009).
RN   [112]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-260 IN COMPLEX WITH INHIBITORS,
RP   ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=19778001; DOI=10.1021/jp906593c;
RA   Ciani L., Cecchi A., Temperini C., Supuran C.T., Ristori S.;
RT   "Dissecting the inhibition mechanism of cytosolic versus transmembrane
RT   carbonic anhydrases by ESR.";
RL   J. Phys. Chem. B 113:13998-14005(2009).
RN   [113]
RP   X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, ACTIVITY
RP   REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=19520834; DOI=10.1073/pnas.0904184106;
RA   Sjoeblom B., Polentarutti M., Djinovic-Carugo K.;
RT   "Structural study of X-ray induced activation of carbonic anhydrase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:10609-10613(2009).
RN   [114]
RP   VARIANT JOGJAKARTA GLU-18.
RX   PubMed=6817747; DOI=10.1007/bf00484072;
RA   Jones G.L., Sofro A.S.M., Shaw D.C.;
RT   "Chemical and enzymological characterization of an Indonesian variant of
RT   human erythrocyte carbonic anhydrase II, CAII Jogjakarta (17 Lys leads to
RT   Glu).";
RL   Biochem. Genet. 20:979-1000(1982).
RN   [115]
RP   VARIANT MELBOURNE HIS-236.
RX   PubMed=6407977; DOI=10.1007/bf00274768;
RA   Jones G.L., Shaw D.C.;
RT   "A chemical and enzymological comparison of the common major human
RT   erythrocyte carbonic anhydrase II, its minor component, and a new genetic
RT   variant, CA II Melbourne (237 Pro leads to His).";
RL   Hum. Genet. 63:392-399(1983).
RN   [116]
RP   VARIANT OPTB3 TYR-107.
RX   PubMed=1928091;
RA   Venta P.J., Welty R.J., Johnson T.M., Sly W.S., Tashian R.E.;
RT   "Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by
RT   a point mutation at an invariant histidine residue (107 His-->Tyr):
RT   complete structure of the normal human CA II gene.";
RL   Am. J. Hum. Genet. 49:1082-1090(1991).
RN   [117]
RP   VARIANT OPTB3 TYR-107.
RX   PubMed=1542674; DOI=10.1073/pnas.89.5.1804;
RA   Roth D.E., Venta P.J., Tashian R.E., Sly W.S.;
RT   "Molecular basis of human carbonic anhydrase II deficiency.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:1804-1808(1992).
RN   [118]
RP   VARIANT OPTB3 TYR-107.
RX   PubMed=8834238; DOI=10.1007/bf02267062;
RA   Soda H., Yukizane S., Yoshida I., Koga Y., Aramaki S., Kato H.;
RT   "A point mutation in exon 3 (His 107-->Tyr) in two unrelated Japanese
RT   patients with carbonic anhydrase II deficiency with central nervous system
RT   involvement.";
RL   Hum. Genet. 97:435-437(1996).
RN   [119]
RP   VARIANT OPTB3 PRO-92.
RX   PubMed=9143915;
RX   DOI=10.1002/(sici)1098-1004(1997)9:5<383::aid-humu1>3.0.co;2-5;
RA   Hu P.Y., Lim E.J., Ciccolella J., Strisciuglio P., Sly W.S.;
RT   "Seven novel mutations in carbonic anhydrase II deficiency syndrome
RT   identified by SSCP and direct sequencing analysis.";
RL   Hum. Mutat. 9:383-387(1997).
RN   [120]
RP   VARIANTS OPTB3 PRO-92; TYR-94; TYR-107 AND ARG-144, FUNCTION, CATALYTIC
RP   ACTIVITY, AND CHARACTERIZATION OF VARIANTS TYR-94 AND ARG-144.
RX   PubMed=15300855; DOI=10.1002/humu.9266;
RA   Shah G.N., Bonapace G., Hu P.Y., Strisciuglio P., Sly W.S.;
RT   "Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal
RT   tubular acidosis and brain calcification): novel mutations in CA2
RT   identified by direct sequencing expand the opportunity for genotype-
RT   phenotype correlation.";
RL   Hum. Mutat. 24:272-272(2004).
CC   -!- FUNCTION: Catalyzes the reversible hydration of carbon dioxide
CC       (PubMed:11327835, PubMed:11802772, PubMed:11831900, PubMed:12056894,
CC       PubMed:12171926, PubMed:1336460, PubMed:14736236, PubMed:15300855,
CC       PubMed:15453828, PubMed:15667203, PubMed:15865431, PubMed:16106378,
CC       PubMed:16214338, PubMed:16290146, PubMed:16686544, PubMed:16759856,
CC       PubMed:16807956, PubMed:17127057, PubMed:17251017, PubMed:17314045,
CC       PubMed:17330962, PubMed:17346964, PubMed:17540563, PubMed:17588751,
CC       PubMed:17705204, PubMed:18024029, PubMed:18162396, PubMed:18266323,
CC       PubMed:18374572, PubMed:18481843, PubMed:18640037, PubMed:18942852,
CC       PubMed:1909891, PubMed:1910042, PubMed:19170619, PubMed:19186056,
CC       PubMed:19206230, PubMed:19520834, PubMed:19778001, PubMed:7761440,
CC       PubMed:7901850, PubMed:8218160, PubMed:8262987, PubMed:8399159,
CC       PubMed:8451242, PubMed:8485129, PubMed:8639494, PubMed:9265618,
CC       PubMed:9398308, PubMed:4994926). Can also hydrate cyanamide to urea
CC       (PubMed:10550681, PubMed:11015219). Stimulates the chloride-bicarbonate
CC       exchange activity of SLC26A6 (PubMed:15990874). Essential for bone
CC       resorption and osteoclast differentiation (PubMed:15300855). Involved
CC       in the regulation of fluid secretion into the anterior chamber of the
CC       eye. Contributes to intracellular pH regulation in the duodenal upper
CC       villous epithelium during proton-coupled peptide absorption.
CC       {ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:11015219,
CC       ECO:0000269|PubMed:11327835, ECO:0000269|PubMed:11802772,
CC       ECO:0000269|PubMed:11831900, ECO:0000269|PubMed:12056894,
CC       ECO:0000269|PubMed:12171926, ECO:0000269|PubMed:1336460,
CC       ECO:0000269|PubMed:14736236, ECO:0000269|PubMed:15300855,
CC       ECO:0000269|PubMed:15453828, ECO:0000269|PubMed:15667203,
CC       ECO:0000269|PubMed:15865431, ECO:0000269|PubMed:15990874,
CC       ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:16214338,
CC       ECO:0000269|PubMed:16290146, ECO:0000269|PubMed:16686544,
CC       ECO:0000269|PubMed:16759856, ECO:0000269|PubMed:16807956,
CC       ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17251017,
CC       ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17330962,
CC       ECO:0000269|PubMed:17346964, ECO:0000269|PubMed:17540563,
CC       ECO:0000269|PubMed:17588751, ECO:0000269|PubMed:17705204,
CC       ECO:0000269|PubMed:18024029, ECO:0000269|PubMed:18162396,
CC       ECO:0000269|PubMed:18266323, ECO:0000269|PubMed:18374572,
CC       ECO:0000269|PubMed:18481843, ECO:0000269|PubMed:18640037,
CC       ECO:0000269|PubMed:18942852, ECO:0000269|PubMed:1909891,
CC       ECO:0000269|PubMed:1910042, ECO:0000269|PubMed:19170619,
CC       ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230,
CC       ECO:0000269|PubMed:19520834, ECO:0000269|PubMed:19778001,
CC       ECO:0000269|PubMed:4994926, ECO:0000269|PubMed:7761440,
CC       ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160,
CC       ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159,
CC       ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8485129,
CC       ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:9265618,
CC       ECO:0000269|PubMed:9398308}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogencarbonate + H(+) = CO2 + H2O; Xref=Rhea:RHEA:10748,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000269|PubMed:11327835,
CC         ECO:0000269|PubMed:11802772, ECO:0000269|PubMed:11831900,
CC         ECO:0000269|PubMed:12056894, ECO:0000269|PubMed:12171926,
CC         ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:14736236,
CC         ECO:0000269|PubMed:15300855, ECO:0000269|PubMed:15453828,
CC         ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:15865431,
CC         ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:16214338,
CC         ECO:0000269|PubMed:16290146, ECO:0000269|PubMed:16686544,
CC         ECO:0000269|PubMed:16759856, ECO:0000269|PubMed:16807956,
CC         ECO:0000269|PubMed:17127057, ECO:0000269|PubMed:17251017,
CC         ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17330962,
CC         ECO:0000269|PubMed:17346964, ECO:0000269|PubMed:17540563,
CC         ECO:0000269|PubMed:17588751, ECO:0000269|PubMed:17705204,
CC         ECO:0000269|PubMed:18024029, ECO:0000269|PubMed:18162396,
CC         ECO:0000269|PubMed:18266323, ECO:0000269|PubMed:18374572,
CC         ECO:0000269|PubMed:18481843, ECO:0000269|PubMed:18640037,
CC         ECO:0000269|PubMed:18942852, ECO:0000269|PubMed:1909891,
CC         ECO:0000269|PubMed:1910042, ECO:0000269|PubMed:19170619,
CC         ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230,
CC         ECO:0000269|PubMed:19520834, ECO:0000269|PubMed:19778001,
CC         ECO:0000269|PubMed:4994926, ECO:0000269|PubMed:7761440,
CC         ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160,
CC         ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159,
CC         ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8485129,
CC         ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:9265618,
CC         ECO:0000269|PubMed:9398308};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=urea = cyanamide + H2O; Xref=Rhea:RHEA:23056,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:16698; EC=4.2.1.69;
CC         Evidence={ECO:0000269|PubMed:10550681, ECO:0000269|PubMed:11015219};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:11076507, ECO:0000269|PubMed:12499545,
CC         ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:1433293,
CC         ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:19583303,
CC         ECO:0000269|PubMed:3151019, ECO:0000269|PubMed:3151020,
CC         ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386,
CC         ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160,
CC         ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673,
CC         ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430,
CC         ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389,
CC         ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974,
CC         ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:19583303};
CC       Note=Zinc. Can also use cobalt(II) with lower efficiency, but not
CC       copper(II), nickel(II) and manganese(II).
CC       {ECO:0000269|PubMed:19583303};
CC   -!- ACTIVITY REGULATION: Activated by X-ray, histamine, L-adrenaline,
CC       L- and D-phenylalanine, L- and D-histidine, L-His-OMe and beta-Ala-His
CC       (carnosine). Competitively inhibited by saccharin, thioxolone,
CC       coumarins, 667-coumate, celecoxib (Celebrex), valdecoxib (Bextra), SC-
CC       125, SC-560, diclofenac, acetate, azide, bromide, sulfonamide
CC       derivatives such as acetazolamide (AZA), methazolamide (MZA),
CC       ethoxzolamide (EZA), dichlorophenamide (DCP), brinzolamide,
CC       dansylamide, thiabendazole-5-sulfonamide, trifluoromethane sulfonamide
CC       and N-hydroxysulfamide, fructose-based sugar sulfamate RWJ-37497, and
CC       Foscarnet (phosphonoformate trisodium salt). Repressed strongly by
CC       hydrogen sulfide(HS) and weakly by nitrate (NO(3)). Esterase activity
CC       weakly reduced by cyanamide. N-hydroxyurea interferes with zinc binding
CC       and inhibit activity. {ECO:0000269|PubMed:11802772,
CC       ECO:0000269|PubMed:1336460, ECO:0000269|PubMed:14736236,
CC       ECO:0000269|PubMed:16214338, ECO:0000269|PubMed:16290146,
CC       ECO:0000269|PubMed:16686544, ECO:0000269|PubMed:16759856,
CC       ECO:0000269|PubMed:16807956, ECO:0000269|PubMed:17127057,
CC       ECO:0000269|PubMed:17314045, ECO:0000269|PubMed:17540563,
CC       ECO:0000269|PubMed:17588751, ECO:0000269|PubMed:17705204,
CC       ECO:0000269|PubMed:18024029, ECO:0000269|PubMed:18162396,
CC       ECO:0000269|PubMed:18266323, ECO:0000269|PubMed:18374572,
CC       ECO:0000269|PubMed:18481843, ECO:0000269|PubMed:18640037,
CC       ECO:0000269|PubMed:1910042, ECO:0000269|PubMed:19170619,
CC       ECO:0000269|PubMed:19186056, ECO:0000269|PubMed:19206230,
CC       ECO:0000269|PubMed:19520834, ECO:0000269|PubMed:19778001,
CC       ECO:0000269|PubMed:9265618}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9.3 mM for CO(2) {ECO:0000269|PubMed:4994926,
CC         ECO:0000269|PubMed:7761440};
CC         KM=11 mM for CO(2) {ECO:0000269|PubMed:1909891};
CC         KM=8.2 mM for CO(2) {ECO:0000269|PubMed:9398308};
CC         KM=82 mM for H(2)CO(3) {ECO:0000269|PubMed:8262987};
CC         KM=2.9 mM for 4-nitrophenyl acetate {ECO:0000269|PubMed:10550681};
CC       pH dependence:
CC         Optimum pH is 6-8. {ECO:0000269|PubMed:15667203,
CC         ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:18942852,
CC         ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:9398308};
CC   -!- SUBUNIT: Interacts with SLC4A4 (PubMed:14567693, PubMed:15218065).
CC       Interaction with SLC4A7 regulates SLC4A7 transporter activity
CC       (PubMed:14736710). Interacts with SLC26A6 isoform 4 (via C-terminus
CC       cytoplasmic domain) (PubMed:15990874). {ECO:0000269|PubMed:14567693,
CC       ECO:0000269|PubMed:14736710, ECO:0000269|PubMed:15218065,
CC       ECO:0000269|PubMed:15990874}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15990874}. Cell
CC       membrane {ECO:0000269|PubMed:15990874}. Note=Colocalized with SLC26A6
CC       at the surface of the cell membrane in order to form a bicarbonate
CC       transport metabolon. Displaced from the cytosolic surface of the cell
CC       membrane by PKC in phorbol myristate acetate (PMA)-induced cells.
CC       {ECO:0000269|PubMed:15990874}.
CC   -!- DISEASE: Osteopetrosis, autosomal recessive 3 (OPTB3) [MIM:259730]: A
CC       rare genetic disease characterized by abnormally dense bone, due to
CC       defective resorption of immature bone. Osteopetrosis occurs in two
CC       forms: a severe autosomal recessive form occurring in utero, infancy,
CC       or childhood, and a benign autosomal dominant form occurring in
CC       adolescence or adulthood. Recessive osteopetrosis commonly manifests in
CC       early infancy with macrocephaly, feeding difficulties, evolving
CC       blindness and deafness, bone marrow failure, severe anemia, and
CC       hepatosplenomegaly. Deafness and blindness are generally thought to
CC       represent effects of pressure on nerves. OPTB3 is associated with renal
CC       tubular acidosis, cerebral calcification (marble brain disease) and in
CC       some cases with intellectual disability. {ECO:0000269|PubMed:15300855,
CC       ECO:0000269|PubMed:1542674, ECO:0000269|PubMed:1928091,
CC       ECO:0000269|PubMed:8834238, ECO:0000269|PubMed:9143915}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- MISCELLANEOUS: Target of drugs used in treatments against glaucoma
CC       disorder and breast cancer. {ECO:0000269|PubMed:17251017}.
CC   -!- SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
CC       {ECO:0000305}.
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DR   EMBL; M77181; AAA51909.1; -; Genomic_DNA.
DR   EMBL; M77176; AAA51909.1; JOINED; Genomic_DNA.
DR   EMBL; M77177; AAA51909.1; JOINED; Genomic_DNA.
DR   EMBL; M77178; AAA51909.1; JOINED; Genomic_DNA.
DR   EMBL; M77179; AAA51909.1; JOINED; Genomic_DNA.
DR   EMBL; M77180; AAA51909.1; JOINED; Genomic_DNA.
DR   EMBL; Y00339; CAA68426.1; -; mRNA.
DR   EMBL; X03251; CAA27012.1; -; Genomic_DNA.
DR   EMBL; J03037; AAA51908.1; -; mRNA.
DR   EMBL; CR536526; CAG38763.1; -; mRNA.
DR   EMBL; CR541875; CAG46673.1; -; mRNA.
DR   EMBL; AK312978; BAG35815.1; -; mRNA.
DR   EMBL; CH471068; EAW87136.1; -; Genomic_DNA.
DR   EMBL; BC011949; AAH11949.1; -; mRNA.
DR   EMBL; M36532; AAA51911.1; -; mRNA.
DR   CCDS; CCDS6239.1; -.
DR   PIR; A27175; CRHU2.
DR   RefSeq; NP_000058.1; NM_000067.3.
DR   PDB; 12CA; X-ray; 2.40 A; A=1-260.
DR   PDB; 1A42; X-ray; 2.25 A; A=2-260.
DR   PDB; 1AM6; X-ray; 2.00 A; A=2-260.
DR   PDB; 1AVN; X-ray; 2.00 A; A=2-260.
DR   PDB; 1BCD; X-ray; 1.90 A; A=2-260.
DR   PDB; 1BIC; X-ray; 1.90 A; A=2-260.
DR   PDB; 1BN1; X-ray; 2.10 A; A=2-260.
DR   PDB; 1BN3; X-ray; 2.20 A; A=2-260.
DR   PDB; 1BN4; X-ray; 2.10 A; A=2-260.
DR   PDB; 1BNM; X-ray; 2.60 A; A=2-260.
DR   PDB; 1BNN; X-ray; 2.30 A; A=2-260.
DR   PDB; 1BNQ; X-ray; 2.40 A; A=2-260.
DR   PDB; 1BNT; X-ray; 2.15 A; A=2-260.
DR   PDB; 1BNU; X-ray; 2.15 A; A=2-260.
DR   PDB; 1BNV; X-ray; 2.40 A; A=2-260.
DR   PDB; 1BNW; X-ray; 2.25 A; A=2-260.
DR   PDB; 1BV3; X-ray; 1.85 A; A=2-260.
DR   PDB; 1CA2; X-ray; 2.00 A; A=2-260.
DR   PDB; 1CA3; X-ray; 2.30 A; A=1-260.
DR   PDB; 1CAH; X-ray; 1.88 A; A=2-260.
DR   PDB; 1CAI; X-ray; 1.80 A; A=2-260.
DR   PDB; 1CAJ; X-ray; 1.90 A; A=2-260.
DR   PDB; 1CAK; X-ray; 1.90 A; A=2-260.
DR   PDB; 1CAL; X-ray; 2.20 A; A=2-260.
DR   PDB; 1CAM; X-ray; 1.70 A; A=2-260.
DR   PDB; 1CAN; X-ray; 1.90 A; A=2-260.
DR   PDB; 1CAO; X-ray; 1.90 A; A=2-260.
DR   PDB; 1CAY; X-ray; 2.10 A; A=2-260.
DR   PDB; 1CAZ; X-ray; 1.90 A; A=2-260.
DR   PDB; 1CCS; X-ray; 2.35 A; A=2-260.
DR   PDB; 1CCT; X-ray; 2.20 A; A=2-260.
DR   PDB; 1CCU; X-ray; 2.25 A; A=2-260.
DR   PDB; 1CIL; X-ray; 1.60 A; A=2-260.
DR   PDB; 1CIM; X-ray; 2.10 A; A=2-260.
DR   PDB; 1CIN; X-ray; 2.10 A; A=2-260.
DR   PDB; 1CNB; X-ray; 2.35 A; A=2-260.
DR   PDB; 1CNC; X-ray; 2.20 A; A=2-260.
DR   PDB; 1CNG; X-ray; 1.90 A; A=2-260.
DR   PDB; 1CNH; X-ray; 2.05 A; A=2-260.
DR   PDB; 1CNI; X-ray; 1.80 A; A=2-260.
DR   PDB; 1CNJ; X-ray; 1.80 A; A=2-260.
DR   PDB; 1CNK; X-ray; 2.15 A; A=2-260.
DR   PDB; 1CNW; X-ray; 2.00 A; A=1-260.
DR   PDB; 1CNX; X-ray; 1.90 A; A=1-260.
DR   PDB; 1CNY; X-ray; 2.30 A; A=1-260.
DR   PDB; 1CRA; X-ray; 1.90 A; A=2-260.
DR   PDB; 1CVA; X-ray; 2.25 A; A=2-260.
DR   PDB; 1CVB; X-ray; 2.40 A; A=2-260.
DR   PDB; 1CVC; X-ray; 2.30 A; A=2-260.
DR   PDB; 1CVD; X-ray; 2.20 A; A=5-259.
DR   PDB; 1CVE; X-ray; 2.25 A; A=2-260.
DR   PDB; 1CVF; X-ray; 2.25 A; A=2-260.
DR   PDB; 1CVH; X-ray; 2.30 A; A=5-259.
DR   PDB; 1DCA; X-ray; 2.20 A; A=1-260.
DR   PDB; 1DCB; X-ray; 2.10 A; A=1-260.
DR   PDB; 1EOU; X-ray; 2.10 A; A=1-260.
DR   PDB; 1F2W; X-ray; 1.90 A; A=2-260.
DR   PDB; 1FQL; X-ray; 2.00 A; A=1-260.
DR   PDB; 1FQM; X-ray; 2.00 A; A=1-260.
DR   PDB; 1FQN; X-ray; 2.00 A; A=1-260.
DR   PDB; 1FQR; X-ray; 2.00 A; A=1-260.
DR   PDB; 1FR4; X-ray; 1.60 A; A=1-260.
DR   PDB; 1FR7; X-ray; 1.50 A; A/B=1-260.
DR   PDB; 1FSN; X-ray; 2.00 A; A/B=1-260.
DR   PDB; 1FSQ; X-ray; 2.00 A; A/B=1-260.
DR   PDB; 1FSR; X-ray; 2.00 A; A/B=1-260.
DR   PDB; 1G0E; X-ray; 1.60 A; A=1-260.
DR   PDB; 1G0F; X-ray; 1.60 A; A=1-260.
DR   PDB; 1G1D; X-ray; 2.04 A; A=2-260.
DR   PDB; 1G3Z; X-ray; 1.86 A; A=2-260.
DR   PDB; 1G45; X-ray; 1.83 A; A=2-260.
DR   PDB; 1G46; X-ray; 1.84 A; A=2-260.
DR   PDB; 1G48; X-ray; 1.86 A; A=2-260.
DR   PDB; 1G4J; X-ray; 1.84 A; A=2-260.
DR   PDB; 1G4O; X-ray; 1.96 A; A=2-260.
DR   PDB; 1G52; X-ray; 1.80 A; A=2-260.
DR   PDB; 1G53; X-ray; 1.94 A; A=2-260.
DR   PDB; 1G54; X-ray; 1.86 A; A=2-260.
DR   PDB; 1H4N; X-ray; 2.00 A; A=2-260.
DR   PDB; 1H9N; X-ray; 1.85 A; A=2-260.
DR   PDB; 1H9Q; X-ray; 2.20 A; A=2-260.
DR   PDB; 1HCA; X-ray; 2.30 A; A=1-260.
DR   PDB; 1HEA; X-ray; 2.00 A; A=1-260.
DR   PDB; 1HEB; X-ray; 2.00 A; A=1-260.
DR   PDB; 1HEC; X-ray; 2.00 A; A=1-260.
DR   PDB; 1HED; X-ray; 2.00 A; A=1-260.
DR   PDB; 1HVA; X-ray; 2.30 A; A=1-260.
DR   PDB; 1I8Z; X-ray; 1.93 A; A=2-260.
DR   PDB; 1I90; X-ray; 2.00 A; A=2-260.
DR   PDB; 1I91; X-ray; 2.00 A; A=2-260.
DR   PDB; 1I9L; X-ray; 1.93 A; A=2-260.
DR   PDB; 1I9M; X-ray; 1.84 A; A=2-260.
DR   PDB; 1I9N; X-ray; 1.86 A; A=2-260.
DR   PDB; 1I9O; X-ray; 1.86 A; A=2-260.
DR   PDB; 1I9P; X-ray; 1.92 A; A=2-260.
DR   PDB; 1I9Q; X-ray; 1.80 A; A=2-260.
DR   PDB; 1IF4; X-ray; 1.93 A; A=2-260.
DR   PDB; 1IF5; X-ray; 2.00 A; A=2-260.
DR   PDB; 1IF6; X-ray; 2.09 A; A=2-260.
DR   PDB; 1IF7; X-ray; 1.98 A; A=2-260.
DR   PDB; 1IF8; X-ray; 1.94 A; A=2-260.
DR   PDB; 1IF9; X-ray; 2.00 A; A=2-260.
DR   PDB; 1KWQ; X-ray; 2.60 A; A=1-260.
DR   PDB; 1KWR; X-ray; 2.25 A; A=1-260.
DR   PDB; 1LG5; X-ray; 1.75 A; A=1-260.
DR   PDB; 1LG6; X-ray; 2.20 A; A=1-260.
DR   PDB; 1LGD; X-ray; 1.90 A; A=1-260.
DR   PDB; 1LUG; X-ray; 0.95 A; A=2-260.
DR   PDB; 1LZV; X-ray; 2.30 A; A=1-260.
DR   PDB; 1MOO; X-ray; 1.05 A; A=1-260.
DR   PDB; 1MUA; X-ray; 1.70 A; A=4-259.
DR   PDB; 1OKL; X-ray; 2.10 A; A=2-260.
DR   PDB; 1OKM; X-ray; 2.20 A; A=2-260.
DR   PDB; 1OKN; X-ray; 2.40 A; A=2-260.
DR   PDB; 1OQ5; X-ray; 1.50 A; A=2-260.
DR   PDB; 1RAY; X-ray; 1.80 A; A=2-260.
DR   PDB; 1RAZ; X-ray; 1.90 A; A=2-260.
DR   PDB; 1RZA; X-ray; 1.90 A; A=2-260.
DR   PDB; 1RZB; X-ray; 1.80 A; A=2-260.
DR   PDB; 1RZC; X-ray; 1.90 A; A=2-260.
DR   PDB; 1RZD; X-ray; 1.90 A; A=2-260.
DR   PDB; 1RZE; X-ray; 1.90 A; A=2-260.
DR   PDB; 1T9N; X-ray; 2.00 A; A=1-260.
DR   PDB; 1TB0; X-ray; 2.00 A; X=1-260.
DR   PDB; 1TBT; X-ray; 2.00 A; X=1-260.
DR   PDB; 1TE3; X-ray; 2.00 A; X=1-260.
DR   PDB; 1TEQ; X-ray; 2.00 A; X=1-260.
DR   PDB; 1TEU; X-ray; 2.00 A; X=1-260.
DR   PDB; 1TG3; X-ray; 1.80 A; A=1-260.
DR   PDB; 1TG9; X-ray; 1.90 A; A=1-260.
DR   PDB; 1TH9; X-ray; 1.63 A; A=1-260.
DR   PDB; 1THK; X-ray; 1.80 A; A=1-260.
DR   PDB; 1TTM; X-ray; 1.95 A; A=2-260.
DR   PDB; 1UGA; X-ray; 2.00 A; A=3-260.
DR   PDB; 1UGB; X-ray; 2.00 A; A=3-260.
DR   PDB; 1UGC; X-ray; 2.00 A; A=3-260.
DR   PDB; 1UGD; X-ray; 2.00 A; A=3-260.
DR   PDB; 1UGE; X-ray; 1.90 A; A=3-260.
DR   PDB; 1UGF; X-ray; 2.00 A; A=3-260.
DR   PDB; 1UGG; X-ray; 2.20 A; A=3-260.
DR   PDB; 1XEG; X-ray; 1.81 A; A=1-260.
DR   PDB; 1XEV; X-ray; 2.20 A; A/B/C/D=1-260.
DR   PDB; 1XPZ; X-ray; 2.02 A; A=3-260.
DR   PDB; 1XQ0; X-ray; 1.76 A; A=2-260.
DR   PDB; 1YDA; X-ray; 2.10 A; A=2-260.
DR   PDB; 1YDB; X-ray; 1.90 A; A=2-260.
DR   PDB; 1YDC; X-ray; 1.95 A; A=2-260.
DR   PDB; 1YDD; X-ray; 2.10 A; A=2-260.
DR   PDB; 1YO0; X-ray; 1.80 A; A=1-260.
DR   PDB; 1YO1; X-ray; 1.70 A; A=1-260.
DR   PDB; 1YO2; X-ray; 1.80 A; A=1-260.
DR   PDB; 1Z9Y; X-ray; 1.66 A; A=2-260.
DR   PDB; 1ZE8; X-ray; 2.00 A; A=2-260.
DR   PDB; 1ZFK; X-ray; 1.56 A; A=2-260.
DR   PDB; 1ZFQ; X-ray; 1.55 A; A=2-260.
DR   PDB; 1ZGE; X-ray; 1.65 A; A=2-260.
DR   PDB; 1ZGF; X-ray; 1.75 A; A=2-260.
DR   PDB; 1ZH9; X-ray; 1.70 A; A=2-260.
DR   PDB; 1ZSA; X-ray; 2.50 A; A=2-260.
DR   PDB; 1ZSB; X-ray; 2.00 A; A=2-260.
DR   PDB; 1ZSC; X-ray; 1.80 A; A=2-260.
DR   PDB; 2ABE; X-ray; 2.00 A; A=2-260.
DR   PDB; 2AW1; X-ray; 1.46 A; A=2-260.
DR   PDB; 2AX2; X-ray; 1.50 A; A=1-260.
DR   PDB; 2CA2; X-ray; 1.90 A; A=2-260.
DR   PDB; 2CBA; X-ray; 1.54 A; A=2-260.
DR   PDB; 2CBB; X-ray; 1.67 A; A=2-260.
DR   PDB; 2CBC; X-ray; 1.88 A; A=2-260.
DR   PDB; 2CBD; X-ray; 1.67 A; A=2-260.
DR   PDB; 2CBE; X-ray; 1.82 A; A=2-260.
DR   PDB; 2EU2; X-ray; 1.15 A; A=1-260.
DR   PDB; 2EU3; X-ray; 1.60 A; A=1-260.
DR   PDB; 2EZ7; X-ray; 2.00 A; A=1-260.
DR   PDB; 2F14; X-ray; 1.71 A; A=2-260.
DR   PDB; 2FMG; X-ray; 1.60 A; A=1-260.
DR   PDB; 2FMZ; X-ray; 1.60 A; A=1-260.
DR   PDB; 2FNK; X-ray; 1.80 A; A=1-260.
DR   PDB; 2FNM; X-ray; 1.80 A; A=1-260.
DR   PDB; 2FNN; X-ray; 1.80 A; A=1-260.
DR   PDB; 2FOQ; X-ray; 1.25 A; A=1-260.
DR   PDB; 2FOS; X-ray; 1.10 A; A=1-260.
DR   PDB; 2FOU; X-ray; 0.99 A; A=1-260.
DR   PDB; 2FOV; X-ray; 1.15 A; A=1-260.
DR   PDB; 2GD8; X-ray; 1.46 A; A=2-260.
DR   PDB; 2GEH; X-ray; 2.00 A; A=1-260.
DR   PDB; 2H15; X-ray; 1.90 A; A=1-260.
DR   PDB; 2H4N; X-ray; 1.90 A; A=2-260.
DR   PDB; 2HD6; X-ray; 1.80 A; A=2-260.
DR   PDB; 2HKK; X-ray; 1.90 A; A=1-260.
DR   PDB; 2HL4; X-ray; 1.55 A; A=2-260.
DR   PDB; 2HNC; X-ray; 1.55 A; A=2-260.
DR   PDB; 2HOC; X-ray; 2.10 A; A=2-260.
DR   PDB; 2ILI; X-ray; 1.05 A; A=2-260.
DR   PDB; 2NNG; X-ray; 1.20 A; A=2-260.
DR   PDB; 2NNO; X-ray; 1.01 A; A=2-260.
DR   PDB; 2NNS; X-ray; 1.03 A; A=2-260.
DR   PDB; 2NNV; X-ray; 1.10 A; A=2-260.
DR   PDB; 2NWO; X-ray; 1.70 A; A=1-260.
DR   PDB; 2NWP; X-ray; 1.80 A; A=1-260.
DR   PDB; 2NWY; X-ray; 1.65 A; A=1-260.
DR   PDB; 2NWZ; X-ray; 1.80 A; A=1-260.
DR   PDB; 2NXR; X-ray; 1.70 A; A=1-260.
DR   PDB; 2NXS; X-ray; 1.80 A; A=1-260.
DR   PDB; 2NXT; X-ray; 1.15 A; A=1-260.
DR   PDB; 2O4Z; X-ray; 2.10 A; A=1-260.
DR   PDB; 2OSF; X-ray; 1.60 A; A=2-260.
DR   PDB; 2OSM; X-ray; 1.60 A; A=2-260.
DR   PDB; 2POU; X-ray; 1.60 A; A=1-260.
DR   PDB; 2POV; X-ray; 1.60 A; A=1-259.
DR   PDB; 2POW; X-ray; 1.75 A; A=1-260.
DR   PDB; 2Q1B; X-ray; 1.70 A; A=1-260.
DR   PDB; 2Q1Q; X-ray; 1.90 A; A=1-260.
DR   PDB; 2Q38; X-ray; 1.95 A; A=1-260.
DR   PDB; 2QO8; X-ray; 1.40 A; A=2-260.
DR   PDB; 2QOA; X-ray; 1.60 A; A=2-260.
DR   PDB; 2QP6; X-ray; 1.45 A; A=2-260.
DR   PDB; 2VVA; X-ray; 1.56 A; X=1-260.
DR   PDB; 2VVB; X-ray; 1.66 A; X=1-260.
DR   PDB; 2WD2; X-ray; 1.49 A; A=2-260.
DR   PDB; 2WD3; X-ray; 1.80 A; A=2-260.
DR   PDB; 2WEG; X-ray; 1.10 A; A=2-260.
DR   PDB; 2WEH; X-ray; 2.09 A; A=2-260.
DR   PDB; 2WEJ; X-ray; 1.45 A; A=2-260.
DR   PDB; 2WEO; X-ray; 1.40 A; A=2-260.
DR   PDB; 2X7S; X-ray; 1.64 A; A=2-260.
DR   PDB; 2X7T; X-ray; 1.89 A; A=2-260.
DR   PDB; 2X7U; X-ray; 2.12 A; A=2-260.
DR   PDB; 3B4F; X-ray; 1.89 A; A=1-260.
DR   PDB; 3BET; X-ray; 1.85 A; A=2-260.
DR   PDB; 3BL0; X-ray; 1.90 A; A=1-260.
DR   PDB; 3BL1; X-ray; 2.10 A; A=1-260.
DR   PDB; 3C7P; X-ray; 1.70 A; A=1-260.
DR   PDB; 3CA2; X-ray; 2.00 A; A=2-260.
DR   PDB; 3CAJ; X-ray; 1.80 A; A=1-260.
DR   PDB; 3CYU; X-ray; 1.70 A; A=1-260.
DR   PDB; 3D8W; X-ray; 1.70 A; A=1-260.
DR   PDB; 3D92; X-ray; 1.10 A; A=1-260.
DR   PDB; 3D93; X-ray; 1.10 A; A=1-260.
DR   PDB; 3D9Z; X-ray; 1.65 A; A=1-260.
DR   PDB; 3DAZ; X-ray; 1.60 A; A=1-260.
DR   PDB; 3DBU; X-ray; 1.70 A; A=1-260.
DR   PDB; 3DC3; X-ray; 1.70 A; A=1-260.
DR   PDB; 3DC9; X-ray; 1.60 A; A=1-260.
DR   PDB; 3DCC; X-ray; 1.60 A; A=1-260.
DR   PDB; 3DCS; X-ray; 1.80 A; A=1-260.
DR   PDB; 3DCW; X-ray; 1.50 A; A=1-260.
DR   PDB; 3DD0; X-ray; 1.48 A; A=1-260.
DR   PDB; 3DD8; X-ray; 1.90 A; A=1-260.
DR   PDB; 3DV7; X-ray; 1.70 A; A=2-260.
DR   PDB; 3DVB; X-ray; 1.70 A; A=2-260.
DR   PDB; 3DVC; X-ray; 1.60 A; A=2-260.
DR   PDB; 3DVD; X-ray; 1.60 A; A=2-260.
DR   PDB; 3EFI; X-ray; 1.75 A; A=1-260.
DR   PDB; 3EFT; X-ray; 1.85 A; A=1-260.
DR   PDB; 3F4X; X-ray; 1.90 A; A=1-260.
DR   PDB; 3F8E; X-ray; 2.00 A; A=1-260.
DR   PDB; 3FFP; X-ray; 1.81 A; X=1-260.
DR   PDB; 3GZ0; X-ray; 1.26 A; A=2-260.
DR   PDB; 3HFP; X-ray; 2.10 A; A=1-260.
DR   PDB; 3HKN; X-ray; 1.80 A; A=1-260.
DR   PDB; 3HKQ; X-ray; 1.70 A; A=1-260.
DR   PDB; 3HKT; X-ray; 2.36 A; A=1-260.
DR   PDB; 3HKU; X-ray; 1.80 A; A=1-260.
DR   PDB; 3HLJ; X-ray; 1.44 A; A=1-260.
DR   PDB; 3HS4; X-ray; 1.10 A; A=1-260.
DR   PDB; 3IBI; X-ray; 1.93 A; A=2-260.
DR   PDB; 3IBL; X-ray; 1.55 A; A=2-260.
DR   PDB; 3IBN; X-ray; 2.20 A; A=2-260.
DR   PDB; 3IBU; X-ray; 1.41 A; A=2-260.
DR   PDB; 3IEO; X-ray; 2.00 A; A=1-260.
DR   PDB; 3IGP; X-ray; 1.65 A; A=1-260.
DR   PDB; 3K2F; X-ray; 1.98 A; A=1-260.
DR   PDB; 3K34; X-ray; 0.90 A; A=1-260.
DR   PDB; 3K7K; X-ray; 1.90 A; A=1-260.
DR   PDB; 3KIG; X-ray; 1.39 A; A=1-260.
DR   PDB; 3KKX; Neutron; 2.00 A; A=1-260.
DR   PDB; 3KNE; X-ray; 1.35 A; A=1-260.
DR   PDB; 3KOI; X-ray; 1.64 A; A=1-260.
DR   PDB; 3KOK; X-ray; 1.50 A; A=1-260.
DR   PDB; 3KON; X-ray; 1.50 A; A=1-260.
DR   PDB; 3KS3; X-ray; 0.90 A; A=1-260.
DR   PDB; 3KWA; X-ray; 2.00 A; A=1-260.
DR   PDB; 3L14; X-ray; 1.22 A; A=1-260.
DR   PDB; 3M04; X-ray; 1.40 A; A=1-260.
DR   PDB; 3M14; X-ray; 1.38 A; A=1-260.
DR   PDB; 3M1J; X-ray; 1.80 A; A=1-260.
DR   PDB; 3M1K; X-ray; 1.35 A; A=1-260.
DR   PDB; 3M1Q; X-ray; 1.69 A; A=1-260.
DR   PDB; 3M1W; X-ray; 1.38 A; A=1-260.
DR   PDB; 3M2N; X-ray; 1.65 A; A=1-260.
DR   PDB; 3M2X; X-ray; 1.87 A; A=1-260.
DR   PDB; 3M2Y; X-ray; 1.17 A; A=1-260.
DR   PDB; 3M2Z; X-ray; 1.70 A; A=1-260.
DR   PDB; 3M3X; X-ray; 1.68 A; A=1-260.
DR   PDB; 3M40; X-ray; 1.60 A; A=1-260.
DR   PDB; 3M5E; X-ray; 1.70 A; A=1-260.
DR   PDB; 3M5S; X-ray; 1.40 A; A=1-260.
DR   PDB; 3M5T; X-ray; 1.95 A; A=1-260.
DR   PDB; 3M67; X-ray; 1.80 A; A=1-260.
DR   PDB; 3M96; X-ray; 1.40 A; A=1-260.
DR   PDB; 3M98; X-ray; 1.50 A; A=1-260.
DR   PDB; 3MHC; X-ray; 1.70 A; A=1-260.
DR   PDB; 3MHI; X-ray; 1.70 A; A=1-260.
DR   PDB; 3MHL; X-ray; 1.90 A; A=1-260.
DR   PDB; 3MHM; X-ray; 1.50 A; A=1-260.
DR   PDB; 3MHO; X-ray; 1.15 A; A=1-260.
DR   PDB; 3ML2; X-ray; 1.80 A; A=1-260.
DR   PDB; 3MMF; X-ray; 1.50 A; A=1-260.
DR   PDB; 3MNA; X-ray; 1.50 A; A=1-260.
DR   PDB; 3MNH; X-ray; 1.65 A; A=1-260.
DR   PDB; 3MNI; X-ray; 1.75 A; A=1-260.
DR   PDB; 3MNJ; X-ray; 1.75 A; A=1-260.
DR   PDB; 3MNK; X-ray; 1.75 A; A=1-260.
DR   PDB; 3MNU; X-ray; 1.80 A; A=2-260.
DR   PDB; 3MWO; X-ray; 1.40 A; A/B=1-260.
DR   PDB; 3MYQ; X-ray; 1.35 A; A=1-260.
DR   PDB; 3MZC; X-ray; 1.50 A; A=1-260.
DR   PDB; 3N0N; X-ray; 1.50 A; A=1-260.
DR   PDB; 3N2P; X-ray; 1.65 A; A=1-260.
DR   PDB; 3N3J; X-ray; 1.50 A; A=1-260.
DR   PDB; 3N4B; X-ray; 1.60 A; A=1-260.
DR   PDB; 3NB5; X-ray; 1.80 A; A=1-260.
DR   PDB; 3NI5; X-ray; 2.10 A; A=1-260.
DR   PDB; 3NJ9; X-ray; 2.00 A; A=1-260.
DR   PDB; 3OIK; X-ray; 1.50 A; A=1-260.
DR   PDB; 3OIL; X-ray; 1.50 A; A=1-260.
DR   PDB; 3OIM; X-ray; 1.45 A; A=1-260.
DR   PDB; 3OKU; X-ray; 1.45 A; A=1-260.
DR   PDB; 3OKV; X-ray; 1.45 A; A=1-260.
DR   PDB; 3OY0; X-ray; 1.60 A; A=1-260.
DR   PDB; 3OYQ; X-ray; 1.47 A; A=1-260.
DR   PDB; 3OYS; X-ray; 1.54 A; A=1-260.
DR   PDB; 3P3H; X-ray; 1.50 A; A=1-260.
DR   PDB; 3P3J; X-ray; 1.60 A; A=1-260.
DR   PDB; 3P44; X-ray; 2.20 A; A=1-260.
DR   PDB; 3P4V; X-ray; 2.00 A; A=1-260.
DR   PDB; 3P55; X-ray; 2.00 A; A=1-260.
DR   PDB; 3P58; X-ray; 1.49 A; A=1-260.
DR   PDB; 3P5A; X-ray; 1.49 A; A=1-260.
DR   PDB; 3P5L; X-ray; 1.50 A; A=1-260.
DR   PDB; 3PJJ; X-ray; 1.80 A; A=2-260.
DR   PDB; 3PO6; X-ray; 1.47 A; A=2-260.
DR   PDB; 3PYK; X-ray; 1.30 A; A=1-260.
DR   PDB; 3QYK; X-ray; 1.47 A; A=1-260.
DR   PDB; 3R16; X-ray; 1.60 A; A=4-260.
DR   PDB; 3R17; X-ray; 1.70 A; B=4-260.
DR   PDB; 3RG3; X-ray; 1.90 A; A=1-260.
DR   PDB; 3RG4; X-ray; 1.50 A; A=1-260.
DR   PDB; 3RGE; X-ray; 2.10 A; A=1-260.
DR   PDB; 3RJ7; X-ray; 1.20 A; A=3-260.
DR   PDB; 3RLD; X-ray; 1.50 A; A=1-260.
DR   PDB; 3RYJ; X-ray; 1.39 A; B=2-260.
DR   PDB; 3RYV; X-ray; 1.20 A; B=2-260.
DR   PDB; 3RYX; X-ray; 1.60 A; B=2-260.
DR   PDB; 3RYY; X-ray; 1.16 A; A=2-260.
DR   PDB; 3RYZ; X-ray; 1.37 A; A=2-260.
DR   PDB; 3RZ0; X-ray; 1.80 A; B=2-260.
DR   PDB; 3RZ1; X-ray; 1.51 A; B=2-260.
DR   PDB; 3RZ5; X-ray; 1.65 A; A=2-260.
DR   PDB; 3RZ7; X-ray; 1.80 A; A=2-260.
DR   PDB; 3RZ8; X-ray; 1.70 A; A=2-260.
DR   PDB; 3S71; X-ray; 1.25 A; B=3-260.
DR   PDB; 3S72; X-ray; 1.60 A; B=3-260.
DR   PDB; 3S73; X-ray; 1.75 A; B=3-260.
DR   PDB; 3S74; X-ray; 1.40 A; B=3-260.
DR   PDB; 3S75; X-ray; 1.50 A; B=3-260.
DR   PDB; 3S76; X-ray; 1.60 A; A=3-260.
DR   PDB; 3S77; X-ray; 1.86 A; B=3-260.
DR   PDB; 3S78; X-ray; 1.98 A; B=3-260.
DR   PDB; 3S8X; X-ray; 1.30 A; A=1-260.
DR   PDB; 3S9T; X-ray; 1.30 A; A=1-260.
DR   PDB; 3SAP; X-ray; 1.75 A; A=1-260.
DR   PDB; 3SAX; X-ray; 1.10 A; A=1-260.
DR   PDB; 3SBH; X-ray; 1.65 A; A=1-260.
DR   PDB; 3SBI; X-ray; 1.40 A; A=1-260.
DR   PDB; 3T5U; X-ray; 1.75 A; A=2-260.
DR   PDB; 3T5Z; X-ray; 1.65 A; A=2-260.
DR   PDB; 3T82; X-ray; 2.00 A; A=1-260.
DR   PDB; 3T83; X-ray; 1.80 A; A=1-260.
DR   PDB; 3T84; X-ray; 2.00 A; A=1-260.
DR   PDB; 3T85; X-ray; 2.40 A; A=1-260.
DR   PDB; 3TMJ; Other; 2.00 A; A=3-260.
DR   PDB; 3TVN; X-ray; 1.50 A; X=3-260.
DR   PDB; 3TVO; X-ray; 1.60 A; X=3-260.
DR   PDB; 3U3A; X-ray; 1.55 A; X=1-260.
DR   PDB; 3U45; X-ray; 1.70 A; X=1-260.
DR   PDB; 3U47; X-ray; 1.60 A; A=1-260.
DR   PDB; 3U7C; X-ray; 0.93 A; A=1-260.
DR   PDB; 3V2J; X-ray; 1.70 A; A=1-260.
DR   PDB; 3V2M; X-ray; 1.47 A; A=1-260.
DR   PDB; 3V3F; X-ray; 2.00 A; A=1-260.
DR   PDB; 3V3G; X-ray; 1.56 A; B=1-260.
DR   PDB; 3V3H; X-ray; 1.85 A; B=1-260.
DR   PDB; 3V3I; X-ray; 1.73 A; B=1-260.
DR   PDB; 3V3J; X-ray; 1.63 A; A=1-260.
DR   PDB; 3V5G; X-ray; 1.50 A; A=1-260.
DR   PDB; 3V7X; X-ray; 1.03 A; A=2-260.
DR   PDB; 3VBD; X-ray; 1.05 A; A=2-260.
DR   PDB; 3ZP9; X-ray; 1.31 A; A=1-260.
DR   PDB; 4BCW; X-ray; 1.50 A; A=4-260.
DR   PDB; 4BF1; X-ray; 1.35 A; A=2-260.
DR   PDB; 4BF6; X-ray; 1.82 A; A=2-260.
DR   PDB; 4CA2; X-ray; 2.10 A; A=1-260.
DR   PDB; 4CAC; X-ray; 2.20 A; A=2-260.
DR   PDB; 4CQ0; X-ray; 1.45 A; A=1-260.
DR   PDB; 4DZ7; X-ray; 1.49 A; A=1-260.
DR   PDB; 4DZ9; X-ray; 1.49 A; A=1-260.
DR   PDB; 4E3D; X-ray; 1.60 A; A=1-260.
DR   PDB; 4E3F; X-ray; 1.50 A; A=1-260.
DR   PDB; 4E3G; X-ray; 1.55 A; A=1-260.
DR   PDB; 4E3H; X-ray; 1.50 A; A=1-260.
DR   PDB; 4E49; X-ray; 1.45 A; A=1-260.
DR   PDB; 4E4A; X-ray; 1.45 A; A=1-260.
DR   PDB; 4E5Q; X-ray; 1.70 A; A=1-260.
DR   PDB; 4FIK; X-ray; 1.20 A; A=1-260.
DR   PDB; 4FL7; X-ray; 1.85 A; A=2-260.
DR   PDB; 4FPT; X-ray; 0.98 A; A=1-260.
DR   PDB; 4FRC; X-ray; 0.98 A; A=1-260.
DR   PDB; 4FU5; X-ray; 0.98 A; A=1-260.
DR   PDB; 4FVN; X-ray; 1.05 A; A=1-260.
DR   PDB; 4FVO; X-ray; 1.05 A; A=1-260.
DR   PDB; 4G0C; Neutron; 2.00 A; A=4-260.
DR   PDB; 4GL1; X-ray; 1.50 A; X=1-260.
DR   PDB; 4HBA; X-ray; 1.76 A; A=1-260.
DR   PDB; 4HEW; X-ray; 1.70 A; A=1-260.
DR   PDB; 4HEY; X-ray; 1.45 A; A=1-260.
DR   PDB; 4HEZ; X-ray; 1.34 A; A=1-260.
DR   PDB; 4HF3; X-ray; 1.15 A; A=1-260.
DR   PDB; 4HT0; X-ray; 1.60 A; A=1-260.
DR   PDB; 4IDR; X-ray; 1.60 A; X=3-260.
DR   PDB; 4ILX; X-ray; 1.60 A; A=4-260.
DR   PDB; 4ITO; X-ray; 1.16 A; A=1-260.
DR   PDB; 4ITP; X-ray; 1.70 A; A=4-260.
DR   PDB; 4IWZ; X-ray; 1.60 A; A=4-260.
DR   PDB; 4JS6; X-ray; 1.55 A; A=1-260.
DR   PDB; 4JSA; X-ray; 1.50 A; A=1-260.
DR   PDB; 4JSS; X-ray; 1.50 A; A=1-260.
DR   PDB; 4JSW; X-ray; 1.90 A; A=1-260.
DR   PDB; 4JSZ; X-ray; 1.90 A; A=1-260.
DR   PDB; 4K0S; X-ray; 1.80 A; A=4-260.
DR   PDB; 4K0T; X-ray; 1.78 A; A=4-260.
DR   PDB; 4K0Z; X-ray; 1.80 A; A=3-260.
DR   PDB; 4K13; X-ray; 1.60 A; A=4-260.
DR   PDB; 4K1Q; X-ray; 1.70 A; A=3-260.
DR   PDB; 4KAP; X-ray; 1.45 A; A=5-260.
DR   PDB; 4KNI; X-ray; 1.80 A; A=1-260.
DR   PDB; 4KNJ; X-ray; 2.00 A; A=1-260.
DR   PDB; 4KUV; X-ray; 1.35 A; A=5-260.
DR   PDB; 4KUW; X-ray; 1.55 A; A=4-260.
DR   PDB; 4KUY; X-ray; 1.65 A; A=4-260.
DR   PDB; 4KV0; X-ray; 1.55 A; A=4-260.
DR   PDB; 4L5U; X-ray; 2.05 A; A=1-260.
DR   PDB; 4L5V; X-ray; 1.63 A; A=1-260.
DR   PDB; 4L5W; X-ray; 1.70 A; A=1-260.
DR   PDB; 4LHI; X-ray; 1.60 A; A=1-260.
DR   PDB; 4LP6; X-ray; 2.15 A; A/B=1-260.
DR   PDB; 4M2R; X-ray; 1.99 A; A=4-260.
DR   PDB; 4M2U; X-ray; 2.00 A; A=4-260.
DR   PDB; 4M2V; X-ray; 1.72 A; A=4-260.
DR   PDB; 4M2W; X-ray; 1.66 A; A=4-260.
DR   PDB; 4MDG; X-ray; 1.35 A; A=3-260.
DR   PDB; 4MDL; X-ray; 1.52 A; A=3-260.
DR   PDB; 4MDM; X-ray; 1.55 A; A=3-260.
DR   PDB; 4MLT; X-ray; 2.00 A; A=1-260.
DR   PDB; 4MLX; X-ray; 1.65 A; A=1-260.
DR   PDB; 4MO8; X-ray; 1.85 A; A=1-260.
DR   PDB; 4MTY; X-ray; 1.00 A; A=1-260.
DR   PDB; 4N0X; X-ray; 1.63 A; B=1-260.
DR   PDB; 4N16; X-ray; 1.54 A; A=1-260.
DR   PDB; 4PQ7; X-ray; 1.85 A; A=1-260.
DR   PDB; 4PXX; X-ray; 1.85 A; A=1-260.
DR   PDB; 4PYX; X-ray; 1.80 A; A=1-260.
DR   PDB; 4PYY; X-ray; 1.75 A; A=1-260.
DR   PDB; 4PZH; X-ray; 1.06 A; A=1-260.
DR   PDB; 4Q06; X-ray; 1.15 A; A=1-260.
DR   PDB; 4Q07; X-ray; 1.15 A; A=1-260.
DR   PDB; 4Q08; X-ray; 1.07 A; A=1-260.
DR   PDB; 4Q09; X-ray; 1.20 A; A=1-260.
DR   PDB; 4Q49; Neutron; 1.80 A; A=1-260.
DR   PDB; 4Q6D; X-ray; 1.12 A; A=1-260.
DR   PDB; 4Q6E; X-ray; 1.12 A; A=1-260.
DR   PDB; 4Q78; X-ray; 1.00 A; A=3-260.
DR   PDB; 4Q7P; X-ray; 1.65 A; A=1-260.
DR   PDB; 4Q7S; X-ray; 1.80 A; A=1-260.
DR   PDB; 4Q7V; X-ray; 1.60 A; A=1-260.
DR   PDB; 4Q7W; X-ray; 1.45 A; A=1-260.
DR   PDB; 4Q81; X-ray; 1.55 A; A=1-260.
DR   PDB; 4Q83; X-ray; 1.55 A; A=1-260.
DR   PDB; 4Q87; X-ray; 1.55 A; A=1-260.
DR   PDB; 4Q8X; X-ray; 1.55 A; A=1-260.
DR   PDB; 4Q8Y; X-ray; 1.45 A; A=1-260.
DR   PDB; 4Q8Z; X-ray; 1.50 A; A=1-260.
DR   PDB; 4Q90; X-ray; 1.54 A; A=1-260.
DR   PDB; 4Q99; X-ray; 1.50 A; A=1-260.
DR   PDB; 4Q9Y; X-ray; 1.55 A; A=1-260.
DR   PDB; 4QEF; X-ray; 1.47 A; A=1-260.
DR   PDB; 4QIY; X-ray; 1.30 A; A/B/C/D=1-260.
DR   PDB; 4QJM; X-ray; 1.75 A; A=1-260.
DR   PDB; 4QK1; X-ray; 1.60 A; A=1-260.
DR   PDB; 4QK2; X-ray; 1.52 A; A=1-260.
DR   PDB; 4QK3; X-ray; 1.34 A; A=1-260.
DR   PDB; 4QSA; X-ray; 1.50 A; A=1-260.
DR   PDB; 4QSB; X-ray; 1.40 A; A=1-260.
DR   PDB; 4QSI; X-ray; 1.95 A; A=1-260.
DR   PDB; 4QTL; X-ray; 1.80 A; A=1-260.
DR   PDB; 4QY3; X-ray; 1.50 A; A=2-260.
DR   PDB; 4R59; X-ray; 1.65 A; A=1-260.
DR   PDB; 4R5A; X-ray; 1.64 A; A=1-260.
DR   PDB; 4R5B; X-ray; 1.50 A; A=1-260.
DR   PDB; 4RFC; X-ray; 1.65 A; A=1-260.
DR   PDB; 4RFD; X-ray; 1.63 A; A=1-260.
DR   PDB; 4RH2; X-ray; 1.30 A; A=1-260.
DR   PDB; 4RIU; X-ray; 1.65 A; A=1-260.
DR   PDB; 4RIV; X-ray; 1.63 A; A=1-260.
DR   PDB; 4RN4; X-ray; 1.53 A; A=1-260.
DR   PDB; 4RUX; X-ray; 1.14 A; A=1-260.
DR   PDB; 4RUY; X-ray; 1.14 A; A=1-260.
DR   PDB; 4RUZ; X-ray; 1.63 A; A=1-260.
DR   PDB; 4WL4; X-ray; 1.10 A; A=1-260.
DR   PDB; 4WW6; X-ray; 1.06 A; A=1-260.
DR   PDB; 4XE1; X-ray; 1.80 A; A=1-260.
DR   PDB; 4Y0J; Neutron; 2.00 A; A=3-260.
DR   PDB; 4YGJ; X-ray; 1.10 A; A=3-260.
DR   PDB; 4YGK; X-ray; 1.50 A; A=3-260.
DR   PDB; 4YGL; X-ray; 1.51 A; A=3-260.
DR   PDB; 4YGN; X-ray; 1.23 A; A=3-260.
DR   PDB; 4YVY; X-ray; 1.45 A; A=2-260.
DR   PDB; 4YWP; X-ray; 1.45 A; A=4-260.
DR   PDB; 4YX4; X-ray; 1.01 A; A=1-260.
DR   PDB; 4YXI; X-ray; 0.96 A; A=1-260.
DR   PDB; 4YXO; X-ray; 1.06 A; A=1-260.
DR   PDB; 4YXU; X-ray; 1.08 A; A=1-260.
DR   PDB; 4YYT; X-ray; 1.07 A; A=1-260.
DR   PDB; 4Z0Q; X-ray; 1.45 A; A=3-260.
DR   PDB; 4Z1E; X-ray; 2.01 A; A=2-260.
DR   PDB; 4Z1J; X-ray; 1.27 A; A=3-260.
DR   PDB; 4Z1K; X-ray; 1.35 A; A=4-260.
DR   PDB; 4Z1N; X-ray; 1.47 A; A=3-260.
DR   PDB; 4ZAO; X-ray; 1.80 A; A=1-257.
DR   PDB; 4ZWI; X-ray; 1.60 A; A=4-260.
DR   PDB; 4ZWX; X-ray; 1.70 A; A=4-260.
DR   PDB; 4ZWY; X-ray; 1.50 A; A=4-260.
DR   PDB; 4ZWZ; X-ray; 1.62 A; A=4-260.
DR   PDB; 4ZX0; X-ray; 1.60 A; A=4-260.
DR   PDB; 4ZX1; X-ray; 1.50 A; A=4-260.
DR   PDB; 5A6H; X-ray; 1.57 A; A=1-260.
DR   PDB; 5AMD; X-ray; 1.50 A; A=2-260.
DR   PDB; 5AMG; X-ray; 1.55 A; A=2-260.
DR   PDB; 5AML; X-ray; 1.36 A; A=2-260.
DR   PDB; 5BNL; X-ray; 2.00 A; A=4-260.
DR   PDB; 5BRU; X-ray; 1.60 A; A=3-260.
DR   PDB; 5BRV; X-ray; 1.60 A; A=3-260.
DR   PDB; 5BRW; X-ray; 1.40 A; A=1-260.
DR   PDB; 5BYI; X-ray; 1.15 A; A=1-260.
DR   PDB; 5C8I; Other; 1.56 A; A=1-260.
DR   PDB; 5CA2; X-ray; 2.10 A; A=1-260.
DR   PDB; 5CAC; X-ray; 2.20 A; A=2-260.
DR   PDB; 5CLU; X-ray; 1.55 A; A=4-260.
DR   PDB; 5DOG; X-ray; 1.70 A; A=1-260.
DR   PDB; 5DOH; X-ray; 1.05 A; A/B=1-260.
DR   PDB; 5DRS; X-ray; 1.10 A; A=1-260.
DR   PDB; 5DSK; X-ray; 1.30 A; A=1-260.
DR   PDB; 5DSL; X-ray; 1.45 A; A=1-260.
DR   PDB; 5DSM; X-ray; 1.30 A; A=1-260.
DR   PDB; 5DSO; X-ray; 1.40 A; A=1-260.
DR   PDB; 5DSP; X-ray; 1.40 A; A=1-260.
DR   PDB; 5DSQ; X-ray; 1.50 A; A=1-260.
DR   PDB; 5DSR; X-ray; 1.30 A; A=1-260.
DR   PDB; 5E28; X-ray; 1.30 A; A=4-260.
DR   PDB; 5E2K; X-ray; 1.40 A; A=4-260.
DR   PDB; 5E2R; X-ray; 1.60 A; A=1-260.
DR   PDB; 5E2S; X-ray; 1.50 A; A=3-260.
DR   PDB; 5EH5; X-ray; 1.21 A; A=1-260.
DR   PDB; 5EH7; X-ray; 1.43 A; A=1-260.
DR   PDB; 5EH8; X-ray; 1.38 A; A=1-260.
DR   PDB; 5EHE; X-ray; 1.50 A; A=1-260.
DR   PDB; 5EHV; X-ray; 1.21 A; A=1-260.
DR   PDB; 5EHW; X-ray; 1.39 A; A=1-260.
DR   PDB; 5EIJ; X-ray; 1.99 A; A=4-260.
DR   PDB; 5EKH; X-ray; 1.34 A; A=1-260.
DR   PDB; 5EKJ; X-ray; 1.13 A; A=1-260.
DR   PDB; 5EKM; X-ray; 1.33 A; A=1-260.
DR   PDB; 5EOI; X-ray; 1.80 A; A=3-260.
DR   PDB; 5FDC; X-ray; 1.75 A; A=1-260.
DR   PDB; 5FDI; X-ray; 1.85 A; A=1-260.
DR   PDB; 5FLO; X-ray; 1.66 A; A=1-260.
DR   PDB; 5FLP; X-ray; 1.71 A; A=1-260.
DR   PDB; 5FLQ; X-ray; 1.70 A; A=1-260.
DR   PDB; 5FLR; X-ray; 1.68 A; A=1-260.
DR   PDB; 5FLS; X-ray; 1.67 A; A=1-260.
DR   PDB; 5FLT; X-ray; 1.67 A; A=1-260.
DR   PDB; 5FNG; X-ray; 2.05 A; A=1-260.
DR   PDB; 5FNH; X-ray; 1.66 A; A=1-260.
DR   PDB; 5FNI; X-ray; 1.60 A; A=1-260.
DR   PDB; 5FNJ; X-ray; 1.67 A; A=1-260.
DR   PDB; 5FNK; X-ray; 1.59 A; A=1-260.
DR   PDB; 5FNL; X-ray; 1.59 A; A=1-260.
DR   PDB; 5FNM; X-ray; 1.59 A; A=1-260.
DR   PDB; 5G01; X-ray; 1.40 A; A=1-260.
DR   PDB; 5G03; X-ray; 1.35 A; A=1-260.
DR   PDB; 5G0B; X-ray; 1.55 A; A=1-260.
DR   PDB; 5G0C; X-ray; 1.28 A; A=1-260.
DR   PDB; 5GMN; X-ray; 1.80 A; A=1-260.
DR   PDB; 5J8Z; X-ray; 1.70 A; A=1-260.
DR   PDB; 5JDV; X-ray; 1.34 A; B=3-260.
DR   PDB; 5JE7; X-ray; 1.15 A; B=4-260.
DR   PDB; 5JEG; X-ray; 1.19 A; B=3-260.
DR   PDB; 5JEH; X-ray; 1.13 A; B=3-260.
DR   PDB; 5JEP; X-ray; 1.19 A; B=3-260.
DR   PDB; 5JES; X-ray; 1.21 A; B=3-260.
DR   PDB; 5JG3; X-ray; 1.21 A; B=3-260.
DR   PDB; 5JG5; X-ray; 1.19 A; B=3-260.
DR   PDB; 5JGS; X-ray; 1.11 A; B=4-260.
DR   PDB; 5JGT; X-ray; 1.10 A; B=3-260.
DR   PDB; 5JMZ; X-ray; 1.90 A; A=4-260.
DR   PDB; 5JN3; X-ray; 1.60 A; A=4-260.
DR   PDB; 5JN7; X-ray; 1.52 A; A=4-260.
DR   PDB; 5JQ0; X-ray; 1.40 A; A=1-260.
DR   PDB; 5JQT; X-ray; 1.36 A; A=1-260.
DR   PDB; 5L3O; X-ray; 1.98 A; A/B=1-260.
DR   PDB; 5L6K; X-ray; 1.70 A; A/B=1-260.
DR   PDB; 5L6T; X-ray; 2.65 A; A/B=1-260.
DR   PDB; 5L70; X-ray; 2.20 A; A/B=1-260.
DR   PDB; 5L9E; X-ray; 2.90 A; A/B/C/D=1-260.
DR   PDB; 5LJQ; X-ray; 1.05 A; A=3-260.
DR   PDB; 5LJT; X-ray; 1.00 A; A=3-260.
DR   PDB; 5LL4; X-ray; 1.12 A; A/B=1-260.
DR   PDB; 5LL8; X-ray; 1.03 A; A=1-260.
DR   PDB; 5LLC; X-ray; 1.10 A; A=1-260.
DR   PDB; 5LLE; X-ray; 1.90 A; A=1-260.
DR   PDB; 5LLG; X-ray; 1.12 A; A=1-260.
DR   PDB; 5LLH; X-ray; 1.90 A; A=1-260.
DR   PDB; 5LMD; X-ray; 1.70 A; A=1-260.
DR   PDB; 5LVS; X-ray; 1.42 A; A/B=2-260.
DR   PDB; 5M78; X-ray; 1.08 A; A=1-260.
DR   PDB; 5MJN; X-ray; 1.17 A; A=2-260.
DR   PDB; 5N0D; X-ray; 1.70 A; A=1-260.
DR   PDB; 5N0E; X-ray; 1.75 A; A=1-260.
DR   PDB; 5N1R; X-ray; 1.30 A; A=1-260.
DR   PDB; 5N1S; X-ray; 1.30 A; A=1-260.
DR   PDB; 5N24; X-ray; 1.50 A; A=1-260.
DR   PDB; 5N25; X-ray; 1.40 A; A=1-260.
DR   PDB; 5NEA; X-ray; 1.30 A; A=1-260.
DR   PDB; 5NEE; X-ray; 1.70 A; A=1-260.
DR   PDB; 5NXG; X-ray; 1.20 A; A=4-260.
DR   PDB; 5NXI; X-ray; 1.16 A; A=2-260.
DR   PDB; 5NXM; X-ray; 1.25 A; A=3-260.
DR   PDB; 5NXO; X-ray; 1.20 A; A=3-260.
DR   PDB; 5NXP; X-ray; 1.25 A; A=3-260.
DR   PDB; 5NXV; X-ray; 1.10 A; A=3-260.
DR   PDB; 5NXW; X-ray; 1.10 A; A=4-260.
DR   PDB; 5NY1; X-ray; 1.10 A; A=4-260.
DR   PDB; 5NY3; X-ray; 1.40 A; A=3-260.
DR   PDB; 5NY6; X-ray; 1.10 A; A=3-260.
DR   PDB; 5NYA; X-ray; 1.20 A; A=4-260.
DR   PDB; 5O07; X-ray; 1.80 A; A=1-260.
DR   PDB; 5OGN; X-ray; 1.10 A; A/B=3-260.
DR   PDB; 5OGO; X-ray; 0.99 A; A=1-260.
DR   PDB; 5OGP; X-ray; 1.10 A; A=2-260.
DR   PDB; 5SZ0; X-ray; 1.63 A; A=4-260.
DR   PDB; 5SZ1; X-ray; 1.55 A; A=4-260.
DR   PDB; 5SZ2; X-ray; 1.63 A; A=4-260.
DR   PDB; 5SZ3; X-ray; 1.69 A; A=4-260.
DR   PDB; 5SZ4; X-ray; 1.60 A; A=4-260.
DR   PDB; 5SZ5; X-ray; 1.27 A; A=4-260.
DR   PDB; 5SZ6; X-ray; 1.15 A; A=4-260.
DR   PDB; 5SZ7; X-ray; 1.78 A; A=4-260.
DR   PDB; 5T71; X-ray; 1.30 A; A=1-260.
DR   PDB; 5T72; X-ray; 1.30 A; A=1-260.
DR   PDB; 5T74; X-ray; 1.20 A; A=1-260.
DR   PDB; 5T75; X-ray; 1.50 A; A=1-260.
DR   PDB; 5TFX; X-ray; 1.50 A; A=1-260.
DR   PDB; 5TH4; X-ray; 1.47 A; A=1-260.
DR   PDB; 5THI; X-ray; 1.50 A; A=1-260.
DR   PDB; 5THJ; X-ray; 1.50 A; A=1-260.
DR   PDB; 5THN; X-ray; 1.33 A; A=1-260.
DR   PDB; 5TI0; X-ray; 1.42 A; A=1-260.
DR   PDB; 5TXY; X-ray; 1.21 A; A=1-260.
DR   PDB; 5TY1; X-ray; 1.60 A; A=1-260.
DR   PDB; 5TY8; X-ray; 1.45 A; A=1-260.
DR   PDB; 5TY9; X-ray; 1.53 A; A=1-260.
DR   PDB; 5TYA; X-ray; 1.50 A; A=1-260.
DR   PDB; 5U0D; X-ray; 1.59 A; A=1-260.
DR   PDB; 5U0E; X-ray; 1.27 A; A=1-260.
DR   PDB; 5U0F; X-ray; 1.21 A; A=1-260.
DR   PDB; 5U0G; X-ray; 1.54 A; A=1-260.
DR   PDB; 5ULN; X-ray; 1.35 A; A=1-260.
DR   PDB; 5UMC; X-ray; 2.15 A; A=1-260.
DR   PDB; 5VGY; X-ray; 1.39 A; A=1-260.
DR   PDB; 5W8B; X-ray; 1.60 A; A=4-260.
DR   PDB; 5WEX; X-ray; 1.26 A; A=1-260.
DR   PDB; 5WG7; X-ray; 1.45 A; A=4-260.
DR   PDB; 5WGP; X-ray; 1.53 A; A=4-260.
DR   PDB; 5WLR; X-ray; 1.49 A; A=4-260.
DR   PDB; 5WLT; X-ray; 1.57 A; A=4-260.
DR   PDB; 5WLU; X-ray; 1.39 A; A=4-260.
DR   PDB; 5WLV; X-ray; 1.40 A; A=4-260.
DR   PDB; 5Y2R; X-ray; 1.00 A; A=1-260.
DR   PDB; 5Y2S; X-ray; 0.90 A; A=1-260.
DR   PDB; 5YUI; X-ray; 1.20 A; A=1-260.
DR   PDB; 5YUJ; X-ray; 1.25 A; A=1-260.
DR   PDB; 5YUK; X-ray; 1.45 A; A=1-260.
DR   PDB; 5ZXW; X-ray; 1.32 A; A=5-260.
DR   PDB; 6B00; X-ray; 0.90 A; A=3-260.
DR   PDB; 6B4D; X-ray; 1.20 A; A=4-260.
DR   PDB; 6B59; X-ray; 1.64 A; A=4-260.
DR   PDB; 6B5A; X-ray; 1.62 A; A=4-260.
DR   PDB; 6BBS; Other; 2.00 A; A=1-260.
DR   PDB; 6BC9; Other; 1.80 A; A=1-260.
DR   PDB; 6BCC; Other; 1.80 A; A=1-260.
DR   PDB; 6C7W; X-ray; 1.28 A; A=1-260.
DR   PDB; 6C7X; X-ray; 1.50 A; A=1-260.
DR   PDB; 6CA2; X-ray; 2.50 A; A=1-260.
DR   PDB; 6CEH; X-ray; 1.43 A; A=2-260.
DR   PDB; 6CJV; X-ray; 1.55 A; A=4-260.
DR   PDB; 6D1L; X-ray; 1.40 A; A=1-260.
DR   PDB; 6D1M; X-ray; 1.21 A; A=1-260.
DR   PDB; 6E8P; X-ray; 1.90 A; A=4-260.
DR   PDB; 6E8X; X-ray; 1.60 A; A=4-260.
DR   PDB; 6E91; X-ray; 1.80 A; A=4-260.
DR   PDB; 6E92; X-ray; 1.77 A; A=4-260.
DR   PDB; 6EBE; X-ray; 1.88 A; A=4-260.
DR   PDB; 6ECZ; X-ray; 2.21 A; A=4-260.
DR   PDB; 6EDA; X-ray; 1.88 A; A=4-260.
DR   PDB; 6EEA; X-ray; 1.63 A; A=4-260.
DR   PDB; 6EEH; X-ray; 1.63 A; A=4-260.
DR   PDB; 6EEO; X-ray; 1.72 A; A=4-260.
DR   PDB; 6EQU; X-ray; 1.65 A; A=1-260.
DR   PDB; 6FJI; Other; 1.60 A; A=1-260.
DR   PDB; 6FJJ; Other; 1.50 A; A=1-260.
DR   PDB; 6G3Q; X-ray; 1.01 A; A=1-260.
DR   PDB; 6G6T; X-ray; 1.12 A; A=1-260.
DR   PDB; 6GCY; Other; 1.30 A; A=1-260.
DR   PDB; 6GDC; X-ray; 1.08 A; A=1-260.
DR   PDB; 6GM9; X-ray; 1.09 A; A=1-260.
DR   PDB; 6GOT; X-ray; 1.56 A; A=1-260.
DR   PDB; 6GXB; X-ray; 1.35 A; A=4-260.
DR   PDB; 6GXE; X-ray; 1.30 A; A=4-260.
DR   PDB; 6H29; X-ray; 1.46 A; A=1-260.
DR   PDB; 6H2Z; X-ray; 1.94 A; A=1-260.
DR   PDB; 6H33; X-ray; 1.58 A; A=1-260.
DR   PDB; 6H34; X-ray; 1.55 A; A=1-260.
DR   PDB; 6H3Q; X-ray; 1.31 A; A=1-260.
DR   PDB; 6H6S; X-ray; 1.45 A; A/B=2-260.
DR   PDB; 6HD2; NMR; -; A=1-260.
DR   PDB; 6HQX; X-ray; 1.10 A; A=1-260.
DR   PDB; 6HR3; X-ray; 1.02 A; A=1-260.
DR   PDB; 6HX5; X-ray; 1.44 A; A=1-260.
DR   PDB; 6HXD; X-ray; 1.12 A; A=1-260.
DR   PDB; 6HZX; X-ray; 2.91 A; A/B=4-260.
DR   PDB; 6I0W; X-ray; 1.04 A; A=1-260.
DR   PDB; 6I1U; X-ray; 1.08 A; A=1-260.
DR   PDB; 6I2F; X-ray; 1.20 A; A=1-260.
DR   PDB; 6I3E; X-ray; 1.07 A; A=1-260.
DR   PDB; 6IC2; X-ray; 1.15 A; A=1-260.
DR   PDB; 6KLZ; X-ray; 0.90 A; A=1-260.
DR   PDB; 6KM0; X-ray; 0.93 A; A=1-260.
DR   PDB; 6KM1; X-ray; 1.05 A; A=1-260.
DR   PDB; 6KM2; X-ray; 0.90 A; A=1-260.
DR   PDB; 6KM3; X-ray; 1.15 A; A=1-260.
DR   PDB; 6KM4; X-ray; 1.15 A; A=1-260.
DR   PDB; 6KM5; X-ray; 1.15 A; A=1-260.
DR   PDB; 6KM6; X-ray; 1.15 A; A=1-260.
DR   PDB; 6LUU; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LUV; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LUW; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LUX; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LUY; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LUZ; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LV1; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LV2; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LV3; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LV4; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LV5; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LV6; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LV7; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LV8; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LV9; X-ray; 1.20 A; A=1-260.
DR   PDB; 6LVA; X-ray; 1.20 A; A=1-260.
DR   PDB; 6MBV; X-ray; 1.70 A; A=4-260.
DR   PDB; 6MBY; X-ray; 1.50 A; A=4-260.
DR   PDB; 6NJ2; X-ray; 1.50 A; A/B=3-260.
DR   PDB; 6NJ3; X-ray; 1.01 A; A=3-260.
DR   PDB; 6NJ4; X-ray; 1.30 A; A=3-260.
DR   PDB; 6NJ5; X-ray; 1.25 A; A=3-260.
DR   PDB; 6NJ6; X-ray; 1.60 A; A/B=3-260.
DR   PDB; 6NLV; X-ray; 1.79 A; A=4-260.
DR   PDB; 6NM0; X-ray; 1.44 A; A=4-260.
DR   PDB; 6ODZ; X-ray; 1.30 A; A=1-260.
DR   PDB; 6OE0; X-ray; 1.30 A; A=1-260.
DR   PDB; 6OE1; X-ray; 1.45 A; A=1-260.
DR   PDB; 6OTI; X-ray; 2.00 A; A=4-260.
DR   PDB; 6OTK; X-ray; 1.12 A; A=4-260.
DR   PDB; 6OTM; X-ray; 1.31 A; A=4-260.
DR   PDB; 6OTO; X-ray; 1.50 A; A=1-260.
DR   PDB; 6OTP; X-ray; 1.47 A; A=4-260.
DR   PDB; 6OTQ; X-ray; 1.47 A; A=4-260.
DR   PDB; 6OUB; X-ray; 1.42 A; A=4-260.
DR   PDB; 6OUD; X-ray; 1.26 A; A=4-260.
DR   PDB; 6OUE; X-ray; 1.42 A; A=4-260.
DR   PDB; 6OUF; X-ray; 1.36 A; A=4-260.
DR   PDB; 6OUH; X-ray; 1.45 A; A=4-260.
DR   PDB; 6OUI; X-ray; 1.53 A; A=4-260.
DR   PDB; 6OUJ; X-ray; 1.47 A; A=4-260.
DR   PDB; 6OUK; X-ray; 1.50 A; A=4-260.
DR   PDB; 6OUM; X-ray; 1.56 A; A=4-260.
DR   PDB; 6PDV; X-ray; 1.23 A; A=1-260.
DR   PDB; 6PEA; X-ray; 1.36 A; A=1-260.
DR   PDB; 6PGX; X-ray; 1.36 A; A=1-260.
DR   PDB; 6Q3O; X-ray; 2.23 A; A/B/C/D=2-260.
DR   PDB; 6Q9T; X-ray; 2.68 A; A=2-260.
DR   PDB; 6QEB; NMR; -; A=1-260.
DR   PDB; 6QFU; X-ray; 1.80 A; A=3-260.
DR   PDB; 6QFV; X-ray; 1.45 A; A=3-260.
DR   PDB; 6QFW; X-ray; 1.20 A; A=3-260.
DR   PDB; 6QFX; X-ray; 1.32 A; A=3-260.
DR   PDB; 6QL1; X-ray; 1.42 A; A=1-260.
DR   PDB; 6QL2; X-ray; 1.30 A; A=1-260.
DR   PDB; 6QL3; X-ray; 1.35 A; A=1-260.
DR   PDB; 6R6F; X-ray; 1.20 A; A=1-260.
DR   PDB; 6R6J; X-ray; 1.55 A; A=1-260.
DR   PDB; 6RFH; X-ray; 0.97 A; A=1-260.
DR   PDB; 6RG3; X-ray; 1.32 A; A=1-260.
DR   PDB; 6RG4; X-ray; 1.25 A; A=1-260.
DR   PDB; 6RG5; X-ray; 1.09 A; A=1-260.
DR   PDB; 6RH4; X-ray; 0.95 A; A=1-260.
DR   PDB; 6RHJ; X-ray; 1.44 A; A=1-260.
DR   PDB; 6RHK; X-ray; 1.44 A; A=1-260.
DR   PDB; 6RIG; X-ray; 1.00 A; A=1-260.
DR   PDB; 6RIT; X-ray; 1.01 A; A=1-260.
DR   PDB; 6RJJ; X-ray; 1.06 A; A=1-260.
DR   PDB; 6RKN; X-ray; 0.96 A; A=1-260.
DR   PDB; 6RL9; X-ray; 1.00 A; A=1-260.
DR   PDB; 6RM1; X-ray; 1.68 A; A=1-260.
DR   PDB; 6RMP; X-ray; 1.22 A; A=1-260.
DR   PDB; 6RMX; X-ray; 1.60 A; A=4-260.
DR   PDB; 6RMY; X-ray; 1.50 A; A=1-260.
DR   PDB; 6RNP; X-ray; 1.07 A; A=1-260.
DR   PDB; 6ROB; X-ray; 0.93 A; A=1-260.
DR   PDB; 6ROE; X-ray; 0.94 A; A=1-260.
DR   PDB; 6ROF; X-ray; 1.50 A; A=1-260.
DR   PDB; 6RQI; X-ray; 0.95 A; A=1-260.
DR   PDB; 6RRG; X-ray; 1.13 A; A=1-260.
DR   PDB; 6RRI; X-ray; 1.10 A; A=1-260.
DR   PDB; 6RS5; X-ray; 1.07 A; A=1-260.
DR   PDB; 6RSZ; X-ray; 1.09 A; A=1-260.
DR   PDB; 6RVF; X-ray; 2.07 A; A=1-260.
DR   PDB; 6RVK; X-ray; 1.58 A; A=1-260.
DR   PDB; 6RVL; X-ray; 1.72 A; A=1-260.
DR   PDB; 6RW1; X-ray; 1.70 A; A=1-260.
DR   PDB; 6RZX; X-ray; 1.00 A; A=1-260.
DR   PDB; 6S03; X-ray; 1.38 A; A=1-260.
DR   PDB; 6S9G; X-ray; 1.14 A; A=1-260.
DR   PDB; 6S9Z; X-ray; 0.95 A; A=1-260.
DR   PDB; 6SAC; X-ray; 1.02 A; A=1-260.
DR   PDB; 6SAS; X-ray; 1.10 A; A=1-260.
DR   PDB; 6SAY; X-ray; 0.95 A; A=1-260.
DR   PDB; 6SB7; X-ray; 1.09 A; A=1-260.
DR   PDB; 6SBH; X-ray; 0.95 A; A=1-260.
DR   PDB; 6SBL; X-ray; 0.94 A; A=1-260.
DR   PDB; 6SBM; X-ray; 0.95 A; A=1-260.
DR   PDB; 6SD7; X-ray; 1.05 A; A=1-260.
DR   PDB; 6SDH; X-ray; 1.04 A; A=1-260.
DR   PDB; 6SDI; X-ray; 1.03 A; A=1-260.
DR   PDB; 6SDJ; X-ray; 1.02 A; A=1-260.
DR   PDB; 6SDL; X-ray; 1.08 A; A=1-260.
DR   PDB; 6SDS; X-ray; 1.26 A; A=1-260.
DR   PDB; 6SEY; X-ray; 1.23 A; A=1-260.
DR   PDB; 6SFQ; X-ray; 1.00 A; A=1-260.
DR   PDB; 6SFU; X-ray; 1.04 A; A=1-260.
DR   PDB; 6SG0; X-ray; 1.13 A; A=1-260.
DR   PDB; 6SG6; X-ray; 0.98 A; A=1-260.
DR   PDB; 6SX9; X-ray; 1.43 A; A=1-260.
DR   PDB; 6SYB; X-ray; 1.60 A; A=1-260.
DR   PDB; 6SYS; X-ray; 1.30 A; A=1-260.
DR   PDB; 6T4N; X-ray; 1.40 A; A=1-260.
DR   PDB; 6T4O; X-ray; 1.13 A; A=1-260.
DR   PDB; 6T4P; X-ray; 1.75 A; A=1-260.
DR   PDB; 6T5C; X-ray; 1.22 A; A=1-260.
DR   PDB; 6T7U; X-ray; 1.20 A; A=1-260.
DR   PDB; 6T81; X-ray; 0.98 A; A=1-260.
DR   PDB; 6T9Z; X-ray; 1.12 A; A=1-260.
DR   PDB; 6U4Q; X-ray; 1.31 A; A=4-260.
DR   PDB; 6U4T; X-ray; 1.36 A; A=4-260.
DR   PDB; 6UFB; X-ray; 1.67 A; A=1-260.
DR   PDB; 6UFC; X-ray; 1.32 A; A=1-260.
DR   PDB; 6UFD; X-ray; 1.48 A; A=1-260.
DR   PDB; 6UGN; X-ray; 1.41 A; A=4-260.
DR   PDB; 6UGO; X-ray; 1.46 A; A=4-260.
DR   PDB; 6UGP; X-ray; 1.31 A; A=4-260.
DR   PDB; 6UGQ; X-ray; 1.30 A; A=4-260.
DR   PDB; 6UGR; X-ray; 1.31 A; A=4-260.
DR   PDB; 6UGZ; X-ray; 1.31 A; A=4-260.
DR   PDB; 6UH0; X-ray; 1.31 A; A=4-260.
DR   PDB; 6UX1; X-ray; 1.36 A; A=1-260.
DR   PDB; 6UZU; X-ray; 1.50 A; A=4-260.
DR   PDB; 6VJ3; X-ray; 1.35 A; A=3-260.
DR   PDB; 6VKG; X-ray; 1.37 A; A=1-260.
DR   PDB; 6WKA; X-ray; 1.34 A; A=1-260.
DR   PDB; 6WQ4; X-ray; 1.35 A; A=1-260.
DR   PDB; 6WQ5; X-ray; 1.30 A; A=1-260.
DR   PDB; 6WQ7; X-ray; 1.30 A; A=1-260.
DR   PDB; 6WQ8; X-ray; 1.41 A; A=1-260.
DR   PDB; 6WQ9; X-ray; 1.30 A; A=1-260.
DR   PDB; 6XVH; X-ray; 1.80 A; A=4-260.
DR   PDB; 6XWZ; X-ray; 1.38 A; AAA=1-260.
DR   PDB; 6XXT; X-ray; 1.05 A; X=1-260.
DR   PDB; 6YH4; X-ray; 1.30 A; A=1-260.
DR   PDB; 6YH5; X-ray; 1.20 A; A=1-260.
DR   PDB; 6YH6; X-ray; 1.40 A; A=1-260.
DR   PDB; 6YH7; X-ray; 1.12 A; A=1-260.
DR   PDB; 6YH8; X-ray; 1.20 A; A=1-260.
DR   PDB; 6YH9; X-ray; 1.55 A; A=1-260.
DR   PDB; 6YHA; X-ray; 1.25 A; A=1-260.
DR   PDB; 6YHB; X-ray; 1.65 A; A=1-260.
DR   PDB; 6YHC; X-ray; 1.28 A; A=1-260.
DR   PDB; 6YJ3; X-ray; 1.55 A; A=1-260.
DR   PDB; 6YKC; X-ray; 1.20 A; A=1-260.
DR   PDB; 6YKH; X-ray; 1.10 A; A=1-260.
DR   PDB; 6YMA; EM; 2.50 A; A=1-260.
DR   PDB; 6YMB; EM; 2.50 A; A=1-260.
DR   PDB; 6YO2; X-ray; 1.20 A; A=1-260.
DR   PDB; 6YO4; X-ray; 1.70 A; A=1-260.
DR   PDB; 6YO7; X-ray; 1.17 A; A=1-260.
DR   PDB; 6YOI; X-ray; 1.20 A; A=1-260.
DR   PDB; 6YOK; X-ray; 1.25 A; A=1-260.
DR   PDB; 6YOL; X-ray; 1.15 A; A=1-260.
DR   PDB; 6YPW; X-ray; 1.10 A; A=1-260.
DR   PDB; 6YQT; X-ray; 1.50 A; A=1-260.
DR   PDB; 6YQU; X-ray; 1.48 A; A=1-260.
DR   PDB; 6YRI; X-ray; 1.60 A; A=1-260.
DR   PDB; 6YZJ; X-ray; 1.20 A; A=1-260.
DR   PDB; 6YZK; X-ray; 0.99 A; A=1-260.
DR   PDB; 6YZL; X-ray; 1.20 A; A=1-260.
DR   PDB; 6YZM; X-ray; 1.50 A; A=1-260.
DR   PDB; 6YZN; X-ray; 0.95 A; A=1-260.
DR   PDB; 6YZO; X-ray; 1.50 A; A=1-260.
DR   PDB; 6YZP; X-ray; 1.35 A; A=1-260.
DR   PDB; 6YZQ; X-ray; 1.04 A; A=1-260.
DR   PDB; 6YZR; X-ray; 1.20 A; A=1-260.
DR   PDB; 6YZS; X-ray; 1.05 A; A=1-260.
DR   PDB; 6YZT; X-ray; 1.05 A; A=1-260.
DR   PDB; 6YZU; X-ray; 1.00 A; A=1-260.
DR   PDB; 6YZV; X-ray; 1.65 A; A=1-260.
DR   PDB; 6YZW; X-ray; 1.03 A; A=1-260.
DR   PDB; 6YZX; X-ray; 1.10 A; A=1-260.
DR   PDB; 6Z04; X-ray; 1.05 A; A=1-260.
DR   PDB; 6ZR8; X-ray; 1.79 A; A=1-260.
DR   PDB; 7A6V; X-ray; 2.00 A; A=3-260.
DR   PDB; 7AEQ; X-ray; 1.50 A; A=1-260.
DR   PDB; 7AES; X-ray; 1.40 A; A=1-260.
DR   PDB; 7AGN; X-ray; 1.15 A; A/B/C/D=1-260.
DR   PDB; 7ASJ; X-ray; 1.43 A; A=1-260.
DR   PDB; 7BFA; X-ray; 1.60 A; AAA=1-260.
DR   PDB; 7BG5; X-ray; 1.43 A; AAA=1-260.
DR   PDB; 7BHH; X-ray; 1.40 A; A=1-260.
DR   PDB; 7BI5; X-ray; 1.74 A; A=1-260.
DR   PDB; 7CA2; X-ray; 2.40 A; A=1-260.
DR   PDB; 7JNR; X-ray; 1.44 A; A=1-260.
DR   PDB; 7JNV; X-ray; 1.49 A; A=1-260.
DR   PDB; 7JNW; X-ray; 1.29 A; A=1-260.
DR   PDB; 7JNX; X-ray; 1.29 A; A=1-260.
DR   PDB; 7JNZ; X-ray; 1.29 A; A=1-260.
DR   PDB; 7JO0; X-ray; 1.61 A; A=1-257.
DR   PDB; 7JO1; X-ray; 1.50 A; A=1-257.
DR   PDB; 7JO2; X-ray; 1.31 A; A=1-257.
DR   PDB; 7JO3; X-ray; 1.45 A; A=1-257.
DR   PDB; 7JOB; X-ray; 1.38 A; A=1-257.
DR   PDB; 7JOC; X-ray; 1.39 A; A=1-257.
DR   PDB; 7K6I; X-ray; 1.41 A; A=1-260.
DR   PDB; 7K6J; X-ray; 1.75 A; A=1-260.
DR   PDB; 7K6K; X-ray; 1.31 A; A=1-260.
DR   PDB; 7K6L; X-ray; 1.66 A; A=1-260.
DR   PDB; 7K6T; X-ray; 1.76 A; A=1-257.
DR   PDB; 7K6U; X-ray; 1.60 A; A=1-257.
DR   PDB; 7K6X; X-ray; 1.76 A; A=1-257.
DR   PDB; 7K6Z; X-ray; 1.66 A; A=1-257.
DR   PDB; 7M23; X-ray; 1.30 A; A=3-260.
DR   PDB; 7M24; X-ray; 1.30 A; A=3-260.
DR   PDB; 7M26; X-ray; 1.30 A; A=3-260.
DR   PDB; 7MU3; X-ray; 1.35 A; A=1-260.
DR   PDB; 7NH6; X-ray; 1.28 A; AAA=1-260.
DR   PDB; 7NH8; X-ray; 1.37 A; AAA=1-260.
DR   PDB; 7NTB; X-ray; 1.70 A; A=2-260.
DR   PDB; 7NZR; X-ray; 1.28 A; A=1-260.
DR   PDB; 7NZS; X-ray; 1.50 A; A=1-260.
DR   PDB; 7NZT; X-ray; 1.35 A; A=1-260.
DR   PDB; 7NZU; X-ray; 1.24 A; A=1-260.
DR   PDB; 7NZW; X-ray; 1.45 A; A=1-260.
DR   PDB; 7NZX; X-ray; 1.33 A; A=1-260.
DR   PDB; 7OK8; X-ray; 1.43 A; AAA=1-260.
DR   PDB; 7ONM; X-ray; 1.77 A; A=3-260.
DR   PDB; 7ONP; X-ray; 1.41 A; AAA=3-260.
DR   PDB; 7ONQ; X-ray; 1.65 A; A=3-260.
DR   PDB; 7ONV; X-ray; 1.04 A; A=3-260.
DR   PDB; 7ORP; X-ray; 1.43 A; AAA=1-260.
DR   PDB; 7ORQ; X-ray; 1.43 A; AAA=1-260.
DR   PDB; 7OYM; X-ray; 0.98 A; A=1-260.
DR   PDB; 7OYN; X-ray; 0.98 A; A=1-260.
DR   PDB; 7OYO; X-ray; 1.03 A; A=1-260.
DR   PDB; 7OYP; X-ray; 1.05 A; A=1-260.
DR   PDB; 7OYQ; X-ray; 1.15 A; A=1-260.
DR   PDB; 7OYR; X-ray; 1.15 A; A=1-260.
DR   PDB; 7Q0C; X-ray; 1.12 A; A/B=1-260.
DR   PDB; 7Q0E; X-ray; 1.30 A; A=3-260.
DR   PDB; 7QBH; X-ray; 1.22 A; AAA=1-260.
DR   PDB; 7QGX; X-ray; 1.19 A; A=1-260.
DR   PDB; 7QGY; X-ray; 1.50 A; A=1-260.
DR   PDB; 7QGZ; X-ray; 1.13 A; A=1-260.
DR   PDB; 7QNV; X-ray; 1.28 A; AAA=1-260.
DR   PDB; 7QRK; X-ray; 1.43 A; AAA=1-260.
DR   PDB; 7QSE; X-ray; 1.43 A; AAA=1-260.
DR   PDB; 7QSI; X-ray; 1.30 A; AAA=1-260.
DR   PDB; 7QZX; X-ray; 1.24 A; AAA=1-260.
DR   PDB; 7R1X; X-ray; 1.35 A; AAA=1-260.
DR   PDB; 7RNY; X-ray; 1.29 A; A=1-260.
DR   PDB; 7RNZ; X-ray; 1.30 A; A=1-260.
DR   PDB; 7RRE; X-ray; 1.44 A; A=1-260.
DR   PDB; 7RRF; X-ray; 1.45 A; A=4-260.
DR   PDB; 7SUW; X-ray; 1.46 A; A=4-260.
DR   PDB; 7SUY; X-ray; 1.41 A; A=4-260.
DR   PDB; 7SV1; X-ray; 1.56 A; A=4-260.
DR   PDB; 7SV8; X-ray; 1.39 A; A=4-260.
DR   PDB; 7U5W; X-ray; 1.13 A; A=3-260.
DR   PDB; 7U5X; X-ray; 1.04 A; A=3-260.
DR   PDB; 7Y2A; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2C; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2E; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2F; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2G; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2H; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2I; X-ray; 1.40 A; A=1-260.
DR   PDB; 7Y2J; X-ray; 1.25 A; A=1-260.
DR   PDB; 7Y2K; X-ray; 1.25 A; A=1-260.
DR   PDB; 7Y2L; X-ray; 1.25 A; A=1-260.
DR   PDB; 7Y2M; X-ray; 1.25 A; A=1-260.
DR   PDB; 7Y2N; X-ray; 1.25 A; A=1-260.
DR   PDB; 7Y2O; X-ray; 1.25 A; A=1-260.
DR   PDB; 7Y2Q; X-ray; 1.35 A; A=1-260.
DR   PDB; 7Y2R; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2S; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2T; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2U; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2V; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2W; X-ray; 1.20 A; A=1-260.
DR   PDB; 7Y2X; X-ray; 1.50 A; A=1-260.
DR   PDB; 7YWT; X-ray; 1.11 A; AAA=1-260.
DR   PDB; 7ZL6; X-ray; 1.38 A; AAA=1-260.
DR   PDB; 7ZWB; X-ray; 1.48 A; AAA=1-260.
DR   PDB; 8AA6; X-ray; 1.15 A; A=1-260.
DR   PDB; 8AAE; X-ray; 1.15 A; A=1-260.
DR   PDB; 8B29; X-ray; 1.70 A; A=3-260.
DR   PDB; 8BJX; X-ray; 1.28 A; AAA=1-260.
DR   PDB; 8BOE; X-ray; 1.55 A; AAA=1-260.
DR   PDB; 8BZZ; X-ray; 1.07 A; AAA=1-260.
DR   PDB; 8C0Q; X-ray; 1.67 A; A=1-260.
DR   PDB; 8C0R; X-ray; 1.56 A; A=1-260.
DR   PDB; 8CA2; X-ray; 2.40 A; A=1-260.
DR   PDB; 8CR0; X-ray; 1.22 A; X=1-260.
DR   PDB; 8DJ9; X-ray; 1.54 A; A=1-260.
DR   PDB; 8EM3; X-ray; 1.62 A; A=1-260.
DR   PDB; 8EMU; X-ray; 1.13 A; A=1-260.
DR   PDB; 8EXC; X-ray; 1.90 A; A=1-260.
DR   PDB; 8EXG; X-ray; 1.99 A; A=1-260.
DR   PDB; 8EYL; X-ray; 1.18 A; A=1-260.
DR   PDB; 8FAL; X-ray; 1.37 A; A=1-260.
DR   PDB; 8FAU; X-ray; 1.44 A; A=1-260.
DR   PDB; 8FQX; X-ray; 1.50 A; A=1-260.
DR   PDB; 8FQY; X-ray; 1.47 A; A=1-260.
DR   PDB; 8FQZ; X-ray; 1.47 A; A=1-260.
DR   PDB; 8FR1; X-ray; 2.00 A; A=4-260.
DR   PDB; 8FR2; X-ray; 1.31 A; A=4-260.
DR   PDB; 8FR4; X-ray; 1.12 A; A=4-260.
DR   PDB; 8IGF; X-ray; 2.60 A; A=4-260.
DR   PDB; 8J2O; X-ray; 2.60 A; A=1-260.
DR   PDB; 8JEE; X-ray; 2.96 A; A=4-260.
DR   PDB; 8OGD; X-ray; 1.75 A; A=1-260.
DR   PDB; 8OGE; X-ray; 1.46 A; A=1-260.
DR   PDB; 8OGF; X-ray; 1.32 A; AAA=1-260.
DR   PDB; 8OKE; X-ray; 1.05 A; A=1-260.
DR   PDB; 8OKG; X-ray; 1.45 A; A=1-260.
DR   PDB; 8OKJ; X-ray; 1.40 A; A=1-260.
DR   PDB; 8OKO; X-ray; 1.25 A; A=1-260.
DR   PDB; 8OKP; X-ray; 1.25 A; A=1-260.
DR   PDB; 8OKQ; X-ray; 1.00 A; A=1-260.
DR   PDB; 8OKT; X-ray; 1.50 A; A=1-260.
DR   PDB; 8OLA; X-ray; 1.40 A; A=1-260.
DR   PDB; 8OLF; X-ray; 1.45 A; A=1-260.
DR   PDB; 8OLI; X-ray; 1.40 A; A=1-260.
DR   PDB; 8OLK; X-ray; 1.27 A; A=1-260.
DR   PDB; 8OLM; X-ray; 1.50 A; A=1-260.
DR   PDB; 8OMB; X-ray; 1.35 A; A=1-260.
DR   PDB; 8OMH; X-ray; 1.45 A; A=1-260.
DR   PDB; 8OMN; X-ray; 1.40 A; A=1-260.
DR   PDB; 8OMP; X-ray; 1.41 A; A=1-260.
DR   PDB; 8OO8; X-ray; 1.40 A; A=2-260.
DR   PDB; 8OTP; X-ray; 1.40 A; AAA=1-260.
DR   PDB; 8OUB; X-ray; 1.18 A; AAA=1-260.
DR   PDB; 8P6U; X-ray; 1.30 A; A=3-260.
DR   PDB; 8PHL; X-ray; 1.30 A; A=3-260.
DR   PDB; 8PHM; X-ray; 1.45 A; A=5-260.
DR   PDB; 8Q0C; X-ray; 1.30 A; A=3-260.
DR   PDB; 8QF7; X-ray; 1.23 A; AAA=1-260.
DR   PDB; 8QF9; X-ray; 1.28 A; AAA=1-260.
DR   PDB; 8QFK; X-ray; 1.11 A; AAA=1-260.
DR   PDB; 8QH8; X-ray; 1.04 A; A=1-260.
DR   PDB; 8QHG; X-ray; 1.91 A; A=1-260.
DR   PDB; 8QHJ; X-ray; 1.62 A; A=1-260.
DR   PDB; 8QHO; X-ray; 1.43 A; AAA=1-260.
DR   PDB; 8QKZ; X-ray; 1.34 A; AAA=1-260.
DR   PDB; 8QQA; X-ray; 1.35 A; AAA=1-260.
DR   PDB; 8QUF; X-ray; 1.14 A; AAA=1-260.
DR   PDB; 8R1I; X-ray; 1.46 A; A=1-260.
DR   PDB; 8R2F; X-ray; 1.25 A; AAA=1-260.
DR   PDB; 8R2K; X-ray; 1.60 A; AAA=1-260.
DR   PDB; 8RAR; X-ray; 1.15 A; A=1-260.
DR   PDB; 8RBP; X-ray; 1.15 A; A=1-260.
DR   PDB; 8RJ2; X-ray; 1.12 A; A=1-260.
DR   PDB; 8RLP; X-ray; 1.34 A; AAA=1-260.
DR   PDB; 8RLQ; X-ray; 1.50 A; AAA=1-260.
DR   PDB; 8RNS; X-ray; 1.14 A; A=1-260.
DR   PDB; 8ROU; X-ray; 1.08 A; A=1-260.
DR   PDB; 8ROW; X-ray; 1.05 A; A=1-260.
DR   PDB; 8SAF; X-ray; 1.23 A; A=1-260.
DR   PDB; 8SAG; X-ray; 1.52 A; A=1-260.
DR   PDB; 8SD1; X-ray; 1.30 A; A=1-260.
DR   PDB; 8SD6; X-ray; 1.40 A; A=1-260.
DR   PDB; 8SD7; X-ray; 1.70 A; A=1-260.
DR   PDB; 8SD8; X-ray; 1.79 A; A=1-260.
DR   PDB; 8SD9; X-ray; 1.90 A; A=1-260.
DR   PDB; 8SF1; X-ray; 1.70 A; A=1-260.
DR   PDB; 8TTR; X-ray; 1.45 A; A=1-260.
DR   PDB; 8UFW; X-ray; 1.22 A; A=1-260.
DR   PDB; 8UFX; X-ray; 1.21 A; A=1-260.
DR   PDB; 8VQ5; X-ray; 1.50 A; A=1-259.
DR   PDB; 8VQ6; X-ray; 1.45 A; A=1-260.
DR   PDB; 8VQ7; X-ray; 1.41 A; A=1-260.
DR   PDB; 8VZG; X-ray; 1.79 A; A=1-260.
DR   PDB; 8WEP; X-ray; 1.20 A; A=1-260.
DR   PDB; 8WER; X-ray; 1.42 A; A=1-260.
DR   PDB; 8WES; X-ray; 1.45 A; A=1-260.
DR   PDB; 8ZWV; X-ray; 1.50 A; A=1-260.
DR   PDB; 9CA2; X-ray; 2.80 A; A=1-260.
DR   PDB; 9EN8; X-ray; 1.10 A; A=1-260.
DR   PDB; 9EN9; X-ray; 2.02 A; A=1-260.
DR   PDB; 9F15; X-ray; 1.93 A; A=1-260.
DR   PDB; 9F2E; X-ray; 2.02 A; A=1-260.
DR   PDB; 9F2F; X-ray; 1.52 A; A/B/C/D=1-260.
DR   PDB; 9FAI; X-ray; 1.27 A; AAA=1-260.
DR   PDB; 9FAO; X-ray; 1.21 A; AAA=1-260.
DR   PDB; 9FJQ; X-ray; 1.10 A; A=1-260.
DR   PDB; 9FJV; X-ray; 1.20 A; A=1-260.
DR   PDB; 9FPQ; X-ray; 1.50 A; A=1-260.
DR   PDB; 9FPR; X-ray; 1.46 A; A=1-260.
DR   PDB; 9FPS; X-ray; 1.39 A; A=1-260.
DR   PDB; 9FPT; X-ray; 1.18 A; A=1-260.
DR   PDB; 9FPU; X-ray; 1.12 A; A=1-260.
DR   PDB; 9G38; X-ray; 1.20 A; A=1-260.
DR   PDB; 9GAJ; X-ray; 1.64 A; A=1-260.
DR   PDB; 9GAK; X-ray; 2.11 A; A=1-260.
DR   PDB; 9GAM; X-ray; 1.40 A; A=1-260.
DR   PDB; 9GFV; X-ray; 1.14 A; A=1-260.
DR   PDB; 9GFW; X-ray; 1.07 A; A=1-260.
DR   PDB; 9GFX; X-ray; 1.35 A; A=1-260.
DR   PDB; 9GOO; X-ray; 1.40 A; AAA=1-260.
DR   PDB; 9GU7; X-ray; 1.35 A; AAA=1-260.
DR   PDB; 9GUM; X-ray; 1.70 A; AAA=1-260.
DR   PDB; 9GUO; X-ray; 1.65 A; AAA=1-260.
DR   PDB; 9H0V; X-ray; 1.40 A; A=1-260.
DR   PDB; 9H0W; X-ray; 1.44 A; A=1-260.
DR   PDB; 9H3H; X-ray; 1.80 A; A=4-260.
DR   PDB; 9HD6; X-ray; 1.60 A; AAA=1-260.
DR   PDB; 9HGP; X-ray; 2.05 A; A=3-260.
DR   PDB; 9HNX; X-ray; 1.35 A; AAA=1-260.
DR   PDB; 9HQ3; X-ray; 1.50 A; AAA=1-260.
DR   PDB; 9HQG; X-ray; 1.32 A; AAA=1-260.
DR   PDB; 9HWM; X-ray; 1.15 A; A=1-260.
DR   PDB; 9HXZ; X-ray; 1.32 A; AAA=1-260.
DR   PDB; 9I29; X-ray; 1.62 A; AAA=1-260.
DR   PDB; 9JWE; X-ray; 1.29 A; A=1-260.
DR   PDB; 9JWU; X-ray; 1.23 A; A=1-260.
DR   PDB; 9JWW; X-ray; 1.25 A; A=1-260.
DR   PDB; 9KH8; X-ray; 1.20 A; A=1-260.
DR   PDB; 9L2X; X-ray; 1.14 A; A=1-260.
DR   PDB; 9L2Y; X-ray; 1.20 A; A=1-260.
DR   PDB; 9L2Z; X-ray; 1.20 A; A=1-260.
DR   PDB; 9L30; X-ray; 1.20 A; A=1-260.
DR   PDB; 9L31; X-ray; 1.20 A; A=1-260.
DR   PDB; 9L32; X-ray; 1.20 A; A=1-260.
DR   PDB; 9L33; X-ray; 1.35 A; A=1-260.
DR   PDB; 9LDO; X-ray; 1.14 A; A=1-260.
DR   PDB; 9LDP; X-ray; 1.14 A; A=1-260.
DR   PDB; 9LR6; X-ray; 1.25 A; A=1-260.
DR   PDB; 9O8X; X-ray; 1.40 A; A=1-260.
DR   PDB; 9OAF; X-ray; 1.40 A; A=1-260.
DR   PDB; 9OAM; X-ray; 1.40 A; A=1-260.
DR   PDB; 9OBJ; X-ray; 1.40 A; A=1-260.
DR   PDB; 9P0W; X-ray; 1.88 A; A=1-260.
DR   PDB; 9RAY; X-ray; 1.31 A; AAA=1-260.
DR   PDB; 9U5B; X-ray; 1.25 A; A=1-260.
DR   AlphaFoldDB; P00918; -.
DR   MDposit; P00918; -.
DR   MDRepo; P00918; -.
DR   SMR; P00918; -.
DR   BioGRID; 107215; 77.
DR   FunCoup; P00918; 607.
DR   IntAct; P00918; 28.
DR   MINT; P00918; -.
DR   NDEx; IQUERY-CP-CA2; 3 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000285379; -.
DR   BindingDB; P00918; -.
DR   ChEMBL; CHEMBL205; -.
DR   DrugBank; DB07596; (17beta)-17-(cyanomethyl)-2-methoxyestra-1(10),2,4-trien-3-yl sulfamate.
DR   DrugBank; DB03333; (4-sulfamoyl-phenyl)-thiocarbamic acid O-(2-thiophen-3-yl-ethyl) ester.
DR   DrugBank; DB08418; (4aS,4bR,10bS,12aS)-12a-methyl-1,3-dioxo-2-(pyridin-3-ylmethyl)-1,2,3,4,4a,4b,5,6,10b,11,12,12a-dodecahydronaphtho[2,1-f]isoquinolin-8-yl sulfamate.
DR   DrugBank; DB04081; (4s-Trans)-4-(Methylamino)-5,6-Dihydro-6-Methyl-4h-Thieno(2,3-B)Thiopyran-2-Sulfonamide-7,7-Dioxide.
DR   DrugBank; DB08416; (9BETA,13ALPHA,14BETA,17ALPHA)-2-METHOXYESTRA-1,3,5(10)-TRIENE-3,17-DIYL DISULFAMATE.
DR   DrugBank; DB02479; (R)-N-(3-Indol-1-Yl-2-Methyl-Propyl)-4-Sulfamoyl-Benzamide.
DR   DrugBank; DB07467; (S)-Indapamide.
DR   DrugBank; DB03950; (S)-N-(3-Indol-1-Yl-2-Methyl-Propyl)-4-Sulfamoyl-Benzamide.
DR   DrugBank; DB03594; 1,2,4-Triazole.
DR   DrugBank; DB02232; 1,2-Dihydroxybenzene.
DR   DrugBank; DB03294; 1-Methyl-3-Oxo-1,3-Dihydro-Benzo[C]Isothiazole-5-Sulfonic Acid Amide.
DR   DrugBank; DB04763; 1-N-(4-SULFAMOYLPHENYL-ETHYL)-2,4,6-TRIMETHYLPYRIDINIUM.
DR   DrugBank; DB03270; 2,6-Difluorobenzenesulfonamide.
DR   DrugBank; DB08083; 2-(1,3-thiazol-4-yl)-1H-benzimidazole-5-sulfonamide.
DR   DrugBank; DB06954; 2-(cycloheptylmethyl)-1,1-dioxido-1-benzothiophen-6-yl sulfamate.
DR   DrugBank; DB08659; 2-(hydrazinocarbonyl)-3-phenyl-1H-indole-5-sulfonamide.
DR   DrugBank; DB08046; 2-chloro-5-[(1S)-1-hydroxy-3-oxo-2H-isoindol-1-yl]benzenesulfonamide.
DR   DrugBank; DB02087; 3,5-Difluorobenzenesulfonamide.
DR   DrugBank; DB08156; 3-[4-(AMINOSULFONYL)PHENYL]PROPANOIC ACID.
DR   DrugBank; DB04203; 3-Mercuri-4-Aminobenzenesulfonamide.
DR   DrugBank; DB04394; 3-Nitro-4-(2-Oxo-Pyrrolidin-1-Yl)-Benzenesulfonamide.
DR   DrugBank; DB08782; 4-(2-AMINOETHYL)BENZENESULFONAMIDE.
DR   DrugBank; DB04549; 4-(Aminosulfonyl)-N-[(2,3,4-Trifluorophenyl)Methyl]-Benzamide.
DR   DrugBank; DB02221; 4-(Aminosulfonyl)-N-[(2,4,6-Trifluorophenyl)Methyl]-Benzamide.
DR   DrugBank; DB04180; 4-(Aminosulfonyl)-N-[(2,4-Difluorophenyl)Methyl]-Benzamide.
DR   DrugBank; DB03039; 4-(Aminosulfonyl)-N-[(2,5-Difluorophenyl)Methyl]-Benzamide.
DR   DrugBank; DB02861; 4-(Aminosulfonyl)-N-[(3,4,5-Trifluorophenyl)Methyl]-Benzamide.
DR   DrugBank; DB02429; 4-(Aminosulfonyl)-N-[(4-Fluorophenyl)Methyl]-Benzamide.
DR   DrugBank; DB08202; 4-({[(4-METHYLPIPERAZIN-1-YL)AMINO]CARBONOTHIOYL}AMINO)BENZENESULFONAMIDE.
DR   DrugBank; DB04600; 4-[(3-BROMO-4-O-SULFAMOYLBENZYL)(4-CYANOPHENYL)AMINO]-4H-[1,2,4]-TRIAZOLE.
DR   DrugBank; DB04601; 4-[(4-O-SULFAMOYLBENZYL)(4-CYANOPHENYL)AMINO]-4H-[1,2,4]-TRIAZOLE.
DR   DrugBank; DB01784; 4-Flourobenzenesulfonamide.
DR   DrugBank; DB03385; 4-Methylimidazole.
DR   DrugBank; DB04214; 4-Nitrophenyl Phosphate.
DR   DrugBank; DB03697; 4-Sulfonamide-[1-(4-Aminobutane)]Benzamide.
DR   DrugBank; DB04002; 4-Sulfonamide-[4-(Thiomethylaminobutane)]Benzamide.
DR   DrugBank; DB07632; 5-(2-chlorophenyl)-1,3,4-thiadiazole-2-sulfonamide.
DR   DrugBank; DB12348; 5-amino-1,3,4-thiadiazole-2-thiol.
DR   DrugBank; DB06891; 5-{[(4-AMINO-3-CHLORO-5-FLUOROPHENYL)SULFONYL]AMINO}-1,3,4-THIADIAZOLE-2-SULFONAMIDE.
DR   DrugBank; DB08645; 6-CHLORO-3-(DICHLOROMETHYL)-3,4-DIHYDRO-2H-1,2,4-BENZOTHIADIAZINE-7-SULFONAMIDE 1,1-DIOXIDE.
DR   DrugBank; DB08765; 6-HYDROXY-1,3-BENZOTHIAZOLE-2-SULFONAMIDE.
DR   DrugBank; DB14511; Acetate.
DR   DrugBank; DB00819; Acetazolamide.
DR   DrugBank; DB03877; AL-4623.
DR   DrugBank; DB03262; Al-6619, [2h-Thieno[3,2-E]-1,2-Thiazine-6-Sulfonamide,2-(3-Hydroxyphenyl)-3-(4-Morpholinyl)-, 1,1-Dioxide].
DR   DrugBank; DB03598; Al-6629, [2h-Thieno[3,2-E]-1,2-Thiazine-6-Sulfonamide,2-(3-Methoxyphenyl)-3-(4-Morpholinyl)-, 1,1-Dioxide].
DR   DrugBank; DB04089; AL5300.
DR   DrugBank; DB01964; AL5424.
DR   DrugBank; DB03526; AL5927.
DR   DrugBank; DB04371; AL6528.
DR   DrugBank; DB02220; AL7089A.
DR   DrugBank; DB03221; AL7099A.
DR   DrugBank; DB02602; AL7182.
DR   DrugBank; DB02535; Aminodi(Ethyloxy)Ethylaminocarbonylbenzenesulfonamide.
DR   DrugBank; DB00436; Bendroflumethiazide.
DR   DrugBank; DB07050; Benzolamide.
DR   DrugBank; DB00562; Benzthiazide.
DR   DrugBank; DB01194; Brinzolamide.
DR   DrugBank; DB16863; Butylated hydroxytoluene.
DR   DrugBank; DB03854; Cadaverine.
DR   DrugBank; DB19764; Carzenide.
DR   DrugBank; DB00482; Celecoxib.
DR   DrugBank; DB07556; CGS-27023.
DR   DrugBank; DB00880; Chlorothiazide.
DR   DrugBank; DB14086; Cianidanol.
DR   DrugBank; DB04665; Coumarin.
DR   DrugBank; DB11672; Curcumin.
DR   DrugBank; DB02679; Cyanamide.
DR   DrugBank; DB00606; Cyclothiazide.
DR   DrugBank; DB02866; Dansylamide.
DR   DrugBank; DB01144; Diclofenamide.
DR   DrugBank; DB00869; Dorzolamide.
DR   DrugBank; DB08846; Ellagic acid.
DR   DrugBank; DB01031; Ethinamate.
DR   DrugBank; DB00311; Ethoxzolamide.
DR   DrugBank; DB08157; ETHYL 3-[4-(AMINOSULFONYL)PHENYL]PROPANOATE.
DR   DrugBank; DB07767; Ferulic acid.
DR   DrugBank; DB01942; Formic acid.
DR   DrugBank; DB00695; Furosemide.
DR   DrugBank; DB11359; Guaiacol.
DR   DrugBank; DB00774; Hydroflumethiazide.
DR   DrugBank; DB08165; indane-5-sulfonamide.
DR   DrugBank; DB12754; Iodide.
DR   DrugBank; DB02292; Irosustat.
DR   DrugBank; DB06795; Mafenide.
DR   DrugBank; DB03345; Mercaptoethanol.
DR   DrugBank; DB03975; Mercuribenzoic Acid.
DR   DrugBank; DB00703; Methazolamide.
DR   DrugBank; DB00232; Methyclothiazide.
DR   DrugBank; DB02610; N-(2,3,4,5,6-Pentaflouro-Benzyl)-4-Sulfamoyl-Benzamide.
DR   DrugBank; DB07742; N-(2,3-DIFLUORO-BENZYL)-4-SULFAMOYL-BENZAMIDE.
DR   DrugBank; DB03844; N-(2,6-Diflouro-Benzyl)-4-Sulfamoyl-Benzamide.
DR   DrugBank; DB02069; N-(2-Flouro-Benzyl)-4-Sulfamoyl-Benzamide.
DR   DrugBank; DB02986; N-(2-Thienylmethyl)-2,5-Thiophenedisulfonamide.
DR   DrugBank; DB08301; N-({[4-(AMINOSULFONYL)PHENYL]AMINO}CARBONYL)-4-METHYLBENZENESULFONAMIDE.
DR   DrugBank; DB07048; N-[(2R)-5-(aminosulfonyl)-2,3-dihydro-1H-inden-2-yl]-2-propylpentanamide.
DR   DrugBank; DB03596; N-[2-(1h-Indol-5-Yl)-Butyl]-4-Sulfamoyl-Benzamide.
DR   DrugBank; DB07476; N-[4-(AMINOSULFONYL)PHENYL]-2-MERCAPTOBENZAMIDE.
DR   DrugBank; DB01748; N-Benzyl-4-Sulfamoyl-Benzamide.
DR   DrugBank; DB08155; N-{2-[4-(AMINOSULFONYL)PHENYL]ETHYL}ACETAMIDE.
DR   DrugBank; DB14049; Nitrate.
DR   DrugBank; DB04066; p-Coumaric acid.
DR   DrugBank; DB01671; p-Hydroxymercuribenzoic acid.
DR   DrugBank; DB17299; p-Toluenesulfonamide.
DR   DrugBank; DB13495; Paraoxon.
DR   DrugBank; DB03255; Phenol.
DR   DrugBank; DB07710; PHENYLALANYLAMINODI(ETHYLOXY)ETHYL BENZENESULFONAMIDEAMINOCARBONYLBENZENESULFONAMIDE.
DR   DrugBank; DB01795; Phenylboronic acid.
DR   DrugBank; DB01963; Phenylethane Boronic Acid.
DR   DrugBank; DB12399; Polmacoxib.
DR   DrugBank; DB01325; Quinethazone.
DR   DrugBank; DB11085; Resorcinol.
DR   DrugBank; DB12418; Saccharin.
DR   DrugBank; DB00936; Salicylic acid.
DR   DrugBank; DB09460; Sodium carbonate.
DR   DrugBank; DB09472; Sodium sulfate.
DR   DrugBank; DB02894; Sulfamic Acid 2,3-O-(1-Methylethylidene)-4,5-O-Sulfonyl-Beta-Fructopyranose Ester.
DR   DrugBank; DB00391; Sulpiride.
DR   DrugBank; DB08329; Sulthiame.
DR   DrugBank; DB07363; THIOPHENE-2,5-DISULFONIC ACID 2-AMIDE-5-(4-METHYL-BENZYLAMIDE).
DR   DrugBank; DB13343; Tioxolone.
DR   DrugBank; DB00273; Topiramate.
DR   DrugBank; DB01650; trans-2-hydroxycinnamic acid.
DR   DrugBank; DB19785; Trecadrine.
DR   DrugBank; DB01021; Trichlormethiazide.
DR   DrugBank; DB03904; Urea.
DR   DrugBank; DB00580; Valdecoxib.
DR   DrugBank; DB14533; Zinc chloride.
DR   DrugBank; DB14548; Zinc sulfate, unspecified form.
DR   DrugBank; DB00909; Zonisamide.
DR   DrugCentral; P00918; -.
DR   GuidetoPHARMACOLOGY; 3092; -.
DR   GlyGen; P00918; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P00918; -.
DR   PhosphoSitePlus; P00918; -.
DR   BioMuta; CA2; -.
DR   OGP; P00918; -.
DR   REPRODUCTION-2DPAGE; IPI00218414; -.
DR   REPRODUCTION-2DPAGE; P00918; -.
DR   CPTAC; CPTAC-177; -.
DR   CPTAC; CPTAC-178; -.
DR   jPOST; P00918; -.
DR   MassIVE; P00918; -.
DR   PaxDb; 9606-ENSP00000285379; -.
DR   PeptideAtlas; P00918; -.
DR   ProteomicsDB; 51292; -.
DR   Pumba; P00918; -.
DR   Antibodypedia; 677; 719 antibodies from 46 providers.
DR   DNASU; 760; -.
DR   Ensembl; ENST00000285379.10; ENSP00000285379.4; ENSG00000104267.11.
DR   GeneID; 760; -.
DR   KEGG; hsa:760; -.
DR   MANE-Select; ENST00000285379.10; ENSP00000285379.4; NM_000067.3; NP_000058.1.
DR   AGR; HGNC:1373; -.
DR   ClinPGx; PA25989; -.
DR   CTD; 760; -.
DR   DisGeNET; 760; -.
DR   GeneCards; CA2; -.
DR   HGNC; HGNC:1373; CA2.
DR   HPA; ENSG00000104267; Tissue enhanced (choroid plexus, intestine, stomach).
DR   MalaCards; CA2; -.
DR   MIM; 259730; phenotype.
DR   MIM; 611492; gene.
DR   OpenTargets; ENSG00000104267; -.
DR   Orphanet; 2785; Osteopetrosis with renal tubular acidosis.
DR   VEuPathDB; HostDB:ENSG00000104267; -.
DR   eggNOG; KOG0382; Eukaryota.
DR   GeneTree; ENSGT00940000160385; -.
DR   HOGENOM; CLU_039326_2_1_1; -.
DR   InParanoid; P00918; -.
DR   OMA; INPHWKV; -.
DR   OrthoDB; 429145at2759; -.
DR   PAN-GO; P00918; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; P00918; -.
DR   BRENDA; 4.2.1.1; 2681.
DR   PathwayCommons; P00918; -.
DR   Reactome; R-HSA-1237044; Erythrocytes take up carbon dioxide and release oxygen.
DR   Reactome; R-HSA-1247673; Erythrocytes take up oxygen and release carbon dioxide.
DR   Reactome; R-HSA-1475029; Reversible hydration of carbon dioxide.
DR   Reactome; R-HSA-9925563; Developmental Lineage of Pancreatic Ductal Cells.
DR   SABIO-RK; P00918; -.
DR   SignaLink; P00918; -.
DR   Agora; ENSG00000104267; -.
DR   BioGRID-ORCS; 760; 14 hits in 1166 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; CA2; human.
DR   EvolutionaryTrace; P00918; -.
DR   GeneWiki; Carbonic_anhydrase_II; -.
DR   GenomeRNAi; 760; -.
DR   Pharos; P00918; Tclin.
DR   PRO; PR:P00918; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; P00918; protein.
DR   Bgee; ENSG00000104267; Expressed in colonic mucosa and 191 other cell types or tissues.
DR   ExpressionAtlas; P00918; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0004064; F:arylesterase activity; IMP:CACAO.
DR   GO; GO:0004089; F:carbonate dehydratase activity; IDA:UniProtKB.
DR   GO; GO:0018820; F:cyanamide hydratase activity; EXP:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0038166; P:angiotensin-activated signaling pathway; IDA:UniProtKB.
DR   GO; GO:2001150; P:positive regulation of dipeptide transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0051453; P:regulation of intracellular pH; ISS:UniProtKB.
DR   GO; GO:0044070; P:regulation of monoatomic anion transport; IDA:UniProtKB.
DR   CDD; cd03119; alpha_CA_I_II_III_XIII; 1.
DR   FunFam; 3.10.200.10:FF:000001; Carbonic anhydrase 2; 1.
DR   Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR   InterPro; IPR001148; CA_dom.
DR   InterPro; IPR036398; CA_dom_sf.
DR   InterPro; IPR023561; Carbonic_anhydrase_a-class.
DR   InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR   PANTHER; PTHR18952; CARBONIC ANHYDRASE; 1.
DR   PANTHER; PTHR18952:SF120; CARBONIC ANHYDRASE 2; 1.
DR   Pfam; PF00194; Carb_anhydrase; 1.
DR   SMART; SM01057; Carb_anhydrase; 1.
DR   SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR   PROSITE; PS00162; ALPHA_CA_1; 1.
DR   PROSITE; PS51144; ALPHA_CA_2; 1.
DR   PDBsum; 12CA; -.
DR   PDBsum; 1A42; -.
DR   PDBsum; 1AM6; -.
DR   PDBsum; 1AVN; -.
DR   PDBsum; 1BCD; -.
DR   PDBsum; 1BIC; -.
DR   PDBsum; 1BN1; -.
DR   PDBsum; 1BN3; -.
DR   PDBsum; 1BN4; -.
DR   PDBsum; 1BNM; -.
DR   PDBsum; 1BNN; -.
DR   PDBsum; 1BNQ; -.
DR   PDBsum; 1BNT; -.
DR   PDBsum; 1BNU; -.
DR   PDBsum; 1BNV; -.
DR   PDBsum; 1BNW; -.
DR   PDBsum; 1BV3; -.
DR   PDBsum; 1CA2; -.
DR   PDBsum; 1CA3; -.
DR   PDBsum; 1CAH; -.
DR   PDBsum; 1CAI; -.
DR   PDBsum; 1CAJ; -.
DR   PDBsum; 1CAK; -.
DR   PDBsum; 1CAL; -.
DR   PDBsum; 1CAM; -.
DR   PDBsum; 1CAN; -.
DR   PDBsum; 1CAO; -.
DR   PDBsum; 1CAY; -.
DR   PDBsum; 1CAZ; -.
DR   PDBsum; 1CCS; -.
DR   PDBsum; 1CCT; -.
DR   PDBsum; 1CCU; -.
DR   PDBsum; 1CIL; -.
DR   PDBsum; 1CIM; -.
DR   PDBsum; 1CIN; -.
DR   PDBsum; 1CNB; -.
DR   PDBsum; 1CNC; -.
DR   PDBsum; 1CNG; -.
DR   PDBsum; 1CNH; -.
DR   PDBsum; 1CNI; -.
DR   PDBsum; 1CNJ; -.
DR   PDBsum; 1CNK; -.
DR   PDBsum; 1CNW; -.
DR   PDBsum; 1CNX; -.
DR   PDBsum; 1CNY; -.
DR   PDBsum; 1CRA; -.
DR   PDBsum; 1CVA; -.
DR   PDBsum; 1CVB; -.
DR   PDBsum; 1CVC; -.
DR   PDBsum; 1CVD; -.
DR   PDBsum; 1CVE; -.
DR   PDBsum; 1CVF; -.
DR   PDBsum; 1CVH; -.
DR   PDBsum; 1DCA; -.
DR   PDBsum; 1DCB; -.
DR   PDBsum; 1EOU; -.
DR   PDBsum; 1F2W; -.
DR   PDBsum; 1FQL; -.
DR   PDBsum; 1FQM; -.
DR   PDBsum; 1FQN; -.
DR   PDBsum; 1FQR; -.
DR   PDBsum; 1FR4; -.
DR   PDBsum; 1FR7; -.
DR   PDBsum; 1FSN; -.
DR   PDBsum; 1FSQ; -.
DR   PDBsum; 1FSR; -.
DR   PDBsum; 1G0E; -.
DR   PDBsum; 1G0F; -.
DR   PDBsum; 1G1D; -.
DR   PDBsum; 1G3Z; -.
DR   PDBsum; 1G45; -.
DR   PDBsum; 1G46; -.
DR   PDBsum; 1G48; -.
DR   PDBsum; 1G4J; -.
DR   PDBsum; 1G4O; -.
DR   PDBsum; 1G52; -.
DR   PDBsum; 1G53; -.
DR   PDBsum; 1G54; -.
DR   PDBsum; 1H4N; -.
DR   PDBsum; 1H9N; -.
DR   PDBsum; 1H9Q; -.
DR   PDBsum; 1HCA; -.
DR   PDBsum; 1HEA; -.
DR   PDBsum; 1HEB; -.
DR   PDBsum; 1HEC; -.
DR   PDBsum; 1HED; -.
DR   PDBsum; 1HVA; -.
DR   PDBsum; 1I8Z; -.
DR   PDBsum; 1I90; -.
DR   PDBsum; 1I91; -.
DR   PDBsum; 1I9L; -.
DR   PDBsum; 1I9M; -.
DR   PDBsum; 1I9N; -.
DR   PDBsum; 1I9O; -.
DR   PDBsum; 1I9P; -.
DR   PDBsum; 1I9Q; -.
DR   PDBsum; 1IF4; -.
DR   PDBsum; 1IF5; -.
DR   PDBsum; 1IF6; -.
DR   PDBsum; 1IF7; -.
DR   PDBsum; 1IF8; -.
DR   PDBsum; 1IF9; -.
DR   PDBsum; 1KWQ; -.
DR   PDBsum; 1KWR; -.
DR   PDBsum; 1LG5; -.
DR   PDBsum; 1LG6; -.
DR   PDBsum; 1LGD; -.
DR   PDBsum; 1LUG; -.
DR   PDBsum; 1LZV; -.
DR   PDBsum; 1MOO; -.
DR   PDBsum; 1MUA; -.
DR   PDBsum; 1OKL; -.
DR   PDBsum; 1OKM; -.
DR   PDBsum; 1OKN; -.
DR   PDBsum; 1OQ5; -.
DR   PDBsum; 1RAY; -.
DR   PDBsum; 1RAZ; -.
DR   PDBsum; 1RZA; -.
DR   PDBsum; 1RZB; -.
DR   PDBsum; 1RZC; -.
DR   PDBsum; 1RZD; -.
DR   PDBsum; 1RZE; -.
DR   PDBsum; 1T9N; -.
DR   PDBsum; 1TB0; -.
DR   PDBsum; 1TBT; -.
DR   PDBsum; 1TE3; -.
DR   PDBsum; 1TEQ; -.
DR   PDBsum; 1TEU; -.
DR   PDBsum; 1TG3; -.
DR   PDBsum; 1TG9; -.
DR   PDBsum; 1TH9; -.
DR   PDBsum; 1THK; -.
DR   PDBsum; 1TTM; -.
DR   PDBsum; 1UGA; -.
DR   PDBsum; 1UGB; -.
DR   PDBsum; 1UGC; -.
DR   PDBsum; 1UGD; -.
DR   PDBsum; 1UGE; -.
DR   PDBsum; 1UGF; -.
DR   PDBsum; 1UGG; -.
DR   PDBsum; 1XEG; -.
DR   PDBsum; 1XEV; -.
DR   PDBsum; 1XPZ; -.
DR   PDBsum; 1XQ0; -.
DR   PDBsum; 1YDA; -.
DR   PDBsum; 1YDB; -.
DR   PDBsum; 1YDC; -.
DR   PDBsum; 1YDD; -.
DR   PDBsum; 1YO0; -.
DR   PDBsum; 1YO1; -.
DR   PDBsum; 1YO2; -.
DR   PDBsum; 1Z9Y; -.
DR   PDBsum; 1ZE8; -.
DR   PDBsum; 1ZFK; -.
DR   PDBsum; 1ZFQ; -.
DR   PDBsum; 1ZGE; -.
DR   PDBsum; 1ZGF; -.
DR   PDBsum; 1ZH9; -.
DR   PDBsum; 1ZSA; -.
DR   PDBsum; 1ZSB; -.
DR   PDBsum; 1ZSC; -.
DR   PDBsum; 2ABE; -.
DR   PDBsum; 2AW1; -.
DR   PDBsum; 2AX2; -.
DR   PDBsum; 2CA2; -.
DR   PDBsum; 2CBA; -.
DR   PDBsum; 2CBB; -.
DR   PDBsum; 2CBC; -.
DR   PDBsum; 2CBD; -.
DR   PDBsum; 2CBE; -.
DR   PDBsum; 2EU2; -.
DR   PDBsum; 2EU3; -.
DR   PDBsum; 2EZ7; -.
DR   PDBsum; 2F14; -.
DR   PDBsum; 2FMG; -.
DR   PDBsum; 2FMZ; -.
DR   PDBsum; 2FNK; -.
DR   PDBsum; 2FNM; -.
DR   PDBsum; 2FNN; -.
DR   PDBsum; 2FOQ; -.
DR   PDBsum; 2FOS; -.
DR   PDBsum; 2FOU; -.
DR   PDBsum; 2FOV; -.
DR   PDBsum; 2GD8; -.
DR   PDBsum; 2GEH; -.
DR   PDBsum; 2H15; -.
DR   PDBsum; 2H4N; -.
DR   PDBsum; 2HD6; -.
DR   PDBsum; 2HKK; -.
DR   PDBsum; 2HL4; -.
DR   PDBsum; 2HNC; -.
DR   PDBsum; 2HOC; -.
DR   PDBsum; 2ILI; -.
DR   PDBsum; 2NNG; -.
DR   PDBsum; 2NNO; -.
DR   PDBsum; 2NNS; -.
DR   PDBsum; 2NNV; -.
DR   PDBsum; 2NWO; -.
DR   PDBsum; 2NWP; -.
DR   PDBsum; 2NWY; -.
DR   PDBsum; 2NWZ; -.
DR   PDBsum; 2NXR; -.
DR   PDBsum; 2NXS; -.
DR   PDBsum; 2NXT; -.
DR   PDBsum; 2O4Z; -.
DR   PDBsum; 2OSF; -.
DR   PDBsum; 2OSM; -.
DR   PDBsum; 2POU; -.
DR   PDBsum; 2POV; -.
DR   PDBsum; 2POW; -.
DR   PDBsum; 2Q1B; -.
DR   PDBsum; 2Q1Q; -.
DR   PDBsum; 2Q38; -.
DR   PDBsum; 2QO8; -.
DR   PDBsum; 2QOA; -.
DR   PDBsum; 2QP6; -.
DR   PDBsum; 2VVA; -.
DR   PDBsum; 2VVB; -.
DR   PDBsum; 2WD2; -.
DR   PDBsum; 2WD3; -.
DR   PDBsum; 2WEG; -.
DR   PDBsum; 2WEH; -.
DR   PDBsum; 2WEJ; -.
DR   PDBsum; 2WEO; -.
DR   PDBsum; 2X7S; -.
DR   PDBsum; 2X7T; -.
DR   PDBsum; 2X7U; -.
DR   PDBsum; 3B4F; -.
DR   PDBsum; 3BET; -.
DR   PDBsum; 3BL0; -.
DR   PDBsum; 3BL1; -.
DR   PDBsum; 3C7P; -.
DR   PDBsum; 3CA2; -.
DR   PDBsum; 3CAJ; -.
DR   PDBsum; 3CYU; -.
DR   PDBsum; 3D8W; -.
DR   PDBsum; 3D92; -.
DR   PDBsum; 3D93; -.
DR   PDBsum; 3D9Z; -.
DR   PDBsum; 3DAZ; -.
DR   PDBsum; 3DBU; -.
DR   PDBsum; 3DC3; -.
DR   PDBsum; 3DC9; -.
DR   PDBsum; 3DCC; -.
DR   PDBsum; 3DCS; -.
DR   PDBsum; 3DCW; -.
DR   PDBsum; 3DD0; -.
DR   PDBsum; 3DD8; -.
DR   PDBsum; 3DV7; -.
DR   PDBsum; 3DVB; -.
DR   PDBsum; 3DVC; -.
DR   PDBsum; 3DVD; -.
DR   PDBsum; 3EFI; -.
DR   PDBsum; 3EFT; -.
DR   PDBsum; 3F4X; -.
DR   PDBsum; 3F8E; -.
DR   PDBsum; 3FFP; -.
DR   PDBsum; 3GZ0; -.
DR   PDBsum; 3HFP; -.
DR   PDBsum; 3HKN; -.
DR   PDBsum; 3HKQ; -.
DR   PDBsum; 3HKT; -.
DR   PDBsum; 3HKU; -.
DR   PDBsum; 3HLJ; -.
DR   PDBsum; 3HS4; -.
DR   PDBsum; 3IBI; -.
DR   PDBsum; 3IBL; -.
DR   PDBsum; 3IBN; -.
DR   PDBsum; 3IBU; -.
DR   PDBsum; 3IEO; -.
DR   PDBsum; 3IGP; -.
DR   PDBsum; 3K2F; -.
DR   PDBsum; 3K34; -.
DR   PDBsum; 3K7K; -.
DR   PDBsum; 3KIG; -.
DR   PDBsum; 3KKX; -.
DR   PDBsum; 3KNE; -.
DR   PDBsum; 3KOI; -.
DR   PDBsum; 3KOK; -.
DR   PDBsum; 3KON; -.
DR   PDBsum; 3KS3; -.
DR   PDBsum; 3KWA; -.
DR   PDBsum; 3L14; -.
DR   PDBsum; 3M04; -.
DR   PDBsum; 3M14; -.
DR   PDBsum; 3M1J; -.
DR   PDBsum; 3M1K; -.
DR   PDBsum; 3M1Q; -.
DR   PDBsum; 3M1W; -.
DR   PDBsum; 3M2N; -.
DR   PDBsum; 3M2X; -.
DR   PDBsum; 3M2Y; -.
DR   PDBsum; 3M2Z; -.
DR   PDBsum; 3M3X; -.
DR   PDBsum; 3M40; -.
DR   PDBsum; 3M5E; -.
DR   PDBsum; 3M5S; -.
DR   PDBsum; 3M5T; -.
DR   PDBsum; 3M67; -.
DR   PDBsum; 3M96; -.
DR   PDBsum; 3M98; -.
DR   PDBsum; 3MHC; -.
DR   PDBsum; 3MHI; -.
DR   PDBsum; 3MHL; -.
DR   PDBsum; 3MHM; -.
DR   PDBsum; 3MHO; -.
DR   PDBsum; 3ML2; -.
DR   PDBsum; 3MMF; -.
DR   PDBsum; 3MNA; -.
DR   PDBsum; 3MNH; -.
DR   PDBsum; 3MNI; -.
DR   PDBsum; 3MNJ; -.
DR   PDBsum; 3MNK; -.
DR   PDBsum; 3MNU; -.
DR   PDBsum; 3MWO; -.
DR   PDBsum; 3MYQ; -.
DR   PDBsum; 3MZC; -.
DR   PDBsum; 3N0N; -.
DR   PDBsum; 3N2P; -.
DR   PDBsum; 3N3J; -.
DR   PDBsum; 3N4B; -.
DR   PDBsum; 3NB5; -.
DR   PDBsum; 3NI5; -.
DR   PDBsum; 3NJ9; -.
DR   PDBsum; 3OIK; -.
DR   PDBsum; 3OIL; -.
DR   PDBsum; 3OIM; -.
DR   PDBsum; 3OKU; -.
DR   PDBsum; 3OKV; -.
DR   PDBsum; 3OY0; -.
DR   PDBsum; 3OYQ; -.
DR   PDBsum; 3OYS; -.
DR   PDBsum; 3P3H; -.
DR   PDBsum; 3P3J; -.
DR   PDBsum; 3P44; -.
DR   PDBsum; 3P4V; -.
DR   PDBsum; 3P55; -.
DR   PDBsum; 3P58; -.
DR   PDBsum; 3P5A; -.
DR   PDBsum; 3P5L; -.
DR   PDBsum; 3PJJ; -.
DR   PDBsum; 3PO6; -.
DR   PDBsum; 3PYK; -.
DR   PDBsum; 3QYK; -.
DR   PDBsum; 3R16; -.
DR   PDBsum; 3R17; -.
DR   PDBsum; 3RG3; -.
DR   PDBsum; 3RG4; -.
DR   PDBsum; 3RGE; -.
DR   PDBsum; 3RJ7; -.
DR   PDBsum; 3RLD; -.
DR   PDBsum; 3RYJ; -.
DR   PDBsum; 3RYV; -.
DR   PDBsum; 3RYX; -.
DR   PDBsum; 3RYY; -.
DR   PDBsum; 3RYZ; -.
DR   PDBsum; 3RZ0; -.
DR   PDBsum; 3RZ1; -.
DR   PDBsum; 3RZ5; -.
DR   PDBsum; 3RZ7; -.
DR   PDBsum; 3RZ8; -.
DR   PDBsum; 3S71; -.
DR   PDBsum; 3S72; -.
DR   PDBsum; 3S73; -.
DR   PDBsum; 3S74; -.
DR   PDBsum; 3S75; -.
DR   PDBsum; 3S76; -.
DR   PDBsum; 3S77; -.
DR   PDBsum; 3S78; -.
DR   PDBsum; 3S8X; -.
DR   PDBsum; 3S9T; -.
DR   PDBsum; 3SAP; -.
DR   PDBsum; 3SAX; -.
DR   PDBsum; 3SBH; -.
DR   PDBsum; 3SBI; -.
DR   PDBsum; 3T5U; -.
DR   PDBsum; 3T5Z; -.
DR   PDBsum; 3T82; -.
DR   PDBsum; 3T83; -.
DR   PDBsum; 3T84; -.
DR   PDBsum; 3T85; -.
DR   PDBsum; 3TMJ; -.
DR   PDBsum; 3TVN; -.
DR   PDBsum; 3TVO; -.
DR   PDBsum; 3U3A; -.
DR   PDBsum; 3U45; -.
DR   PDBsum; 3U47; -.
DR   PDBsum; 3U7C; -.
DR   PDBsum; 3V2J; -.
DR   PDBsum; 3V2M; -.
DR   PDBsum; 3V3F; -.
DR   PDBsum; 3V3G; -.
DR   PDBsum; 3V3H; -.
DR   PDBsum; 3V3I; -.
DR   PDBsum; 3V3J; -.
DR   PDBsum; 3V5G; -.
DR   PDBsum; 3V7X; -.
DR   PDBsum; 3VBD; -.
DR   PDBsum; 3ZP9; -.
DR   PDBsum; 4BCW; -.
DR   PDBsum; 4BF1; -.
DR   PDBsum; 4BF6; -.
DR   PDBsum; 4CA2; -.
DR   PDBsum; 4CAC; -.
DR   PDBsum; 4CQ0; -.
DR   PDBsum; 4DZ7; -.
DR   PDBsum; 4DZ9; -.
DR   PDBsum; 4E3D; -.
DR   PDBsum; 4E3F; -.
DR   PDBsum; 4E3G; -.
DR   PDBsum; 4E3H; -.
DR   PDBsum; 4E49; -.
DR   PDBsum; 4E4A; -.
DR   PDBsum; 4E5Q; -.
DR   PDBsum; 4FIK; -.
DR   PDBsum; 4FL7; -.
DR   PDBsum; 4FPT; -.
DR   PDBsum; 4FRC; -.
DR   PDBsum; 4FU5; -.
DR   PDBsum; 4FVN; -.
DR   PDBsum; 4FVO; -.
DR   PDBsum; 4G0C; -.
DR   PDBsum; 4GL1; -.
DR   PDBsum; 4HBA; -.
DR   PDBsum; 4HEW; -.
DR   PDBsum; 4HEY; -.
DR   PDBsum; 4HEZ; -.
DR   PDBsum; 4HF3; -.
DR   PDBsum; 4HT0; -.
DR   PDBsum; 4IDR; -.
DR   PDBsum; 4ILX; -.
DR   PDBsum; 4ITO; -.
DR   PDBsum; 4ITP; -.
DR   PDBsum; 4IWZ; -.
DR   PDBsum; 4JS6; -.
DR   PDBsum; 4JSA; -.
DR   PDBsum; 4JSS; -.
DR   PDBsum; 4JSW; -.
DR   PDBsum; 4JSZ; -.
DR   PDBsum; 4K0S; -.
DR   PDBsum; 4K0T; -.
DR   PDBsum; 4K0Z; -.
DR   PDBsum; 4K13; -.
DR   PDBsum; 4K1Q; -.
DR   PDBsum; 4KAP; -.
DR   PDBsum; 4KNI; -.
DR   PDBsum; 4KNJ; -.
DR   PDBsum; 4KUV; -.
DR   PDBsum; 4KUW; -.
DR   PDBsum; 4KUY; -.
DR   PDBsum; 4KV0; -.
DR   PDBsum; 4L5U; -.
DR   PDBsum; 4L5V; -.
DR   PDBsum; 4L5W; -.
DR   PDBsum; 4LHI; -.
DR   PDBsum; 4LP6; -.
DR   PDBsum; 4M2R; -.
DR   PDBsum; 4M2U; -.
DR   PDBsum; 4M2V; -.
DR   PDBsum; 4M2W; -.
DR   PDBsum; 4MDG; -.
DR   PDBsum; 4MDL; -.
DR   PDBsum; 4MDM; -.
DR   PDBsum; 4MLT; -.
DR   PDBsum; 4MLX; -.
DR   PDBsum; 4MO8; -.
DR   PDBsum; 4MTY; -.
DR   PDBsum; 4N0X; -.
DR   PDBsum; 4N16; -.
DR   PDBsum; 4PQ7; -.
DR   PDBsum; 4PXX; -.
DR   PDBsum; 4PYX; -.
DR   PDBsum; 4PYY; -.
DR   PDBsum; 4PZH; -.
DR   PDBsum; 4Q06; -.
DR   PDBsum; 4Q07; -.
DR   PDBsum; 4Q08; -.
DR   PDBsum; 4Q09; -.
DR   PDBsum; 4Q49; -.
DR   PDBsum; 4Q6D; -.
DR   PDBsum; 4Q6E; -.
DR   PDBsum; 4Q78; -.
DR   PDBsum; 4Q7P; -.
DR   PDBsum; 4Q7S; -.
DR   PDBsum; 4Q7V; -.
DR   PDBsum; 4Q7W; -.
DR   PDBsum; 4Q81; -.
DR   PDBsum; 4Q83; -.
DR   PDBsum; 4Q87; -.
DR   PDBsum; 4Q8X; -.
DR   PDBsum; 4Q8Y; -.
DR   PDBsum; 4Q8Z; -.
DR   PDBsum; 4Q90; -.
DR   PDBsum; 4Q99; -.
DR   PDBsum; 4Q9Y; -.
DR   PDBsum; 4QEF; -.
DR   PDBsum; 4QIY; -.
DR   PDBsum; 4QJM; -.
DR   PDBsum; 4QK1; -.
DR   PDBsum; 4QK2; -.
DR   PDBsum; 4QK3; -.
DR   PDBsum; 4QSA; -.
DR   PDBsum; 4QSB; -.
DR   PDBsum; 4QSI; -.
DR   PDBsum; 4QTL; -.
DR   PDBsum; 4QY3; -.
DR   PDBsum; 4R59; -.
DR   PDBsum; 4R5A; -.
DR   PDBsum; 4R5B; -.
DR   PDBsum; 4RFC; -.
DR   PDBsum; 4RFD; -.
DR   PDBsum; 4RH2; -.
DR   PDBsum; 4RIU; -.
DR   PDBsum; 4RIV; -.
DR   PDBsum; 4RN4; -.
DR   PDBsum; 4RUX; -.
DR   PDBsum; 4RUY; -.
DR   PDBsum; 4RUZ; -.
DR   PDBsum; 4WL4; -.
DR   PDBsum; 4WW6; -.
DR   PDBsum; 4XE1; -.
DR   PDBsum; 4Y0J; -.
DR   PDBsum; 4YGJ; -.
DR   PDBsum; 4YGK; -.
DR   PDBsum; 4YGL; -.
DR   PDBsum; 4YGN; -.
DR   PDBsum; 4YVY; -.
DR   PDBsum; 4YWP; -.
DR   PDBsum; 4YX4; -.
DR   PDBsum; 4YXI; -.
DR   PDBsum; 4YXO; -.
DR   PDBsum; 4YXU; -.
DR   PDBsum; 4YYT; -.
DR   PDBsum; 4Z0Q; -.
DR   PDBsum; 4Z1E; -.
DR   PDBsum; 4Z1J; -.
DR   PDBsum; 4Z1K; -.
DR   PDBsum; 4Z1N; -.
DR   PDBsum; 4ZAO; -.
DR   PDBsum; 4ZWI; -.
DR   PDBsum; 4ZWX; -.
DR   PDBsum; 4ZWY; -.
DR   PDBsum; 4ZWZ; -.
DR   PDBsum; 4ZX0; -.
DR   PDBsum; 4ZX1; -.
DR   PDBsum; 5A6H; -.
DR   PDBsum; 5AMD; -.
DR   PDBsum; 5AMG; -.
DR   PDBsum; 5AML; -.
DR   PDBsum; 5BNL; -.
DR   PDBsum; 5BRU; -.
DR   PDBsum; 5BRV; -.
DR   PDBsum; 5BRW; -.
DR   PDBsum; 5BYI; -.
DR   PDBsum; 5C8I; -.
DR   PDBsum; 5CA2; -.
DR   PDBsum; 5CAC; -.
DR   PDBsum; 5CLU; -.
DR   PDBsum; 5DOG; -.
DR   PDBsum; 5DOH; -.
DR   PDBsum; 5DRS; -.
DR   PDBsum; 5DSK; -.
DR   PDBsum; 5DSL; -.
DR   PDBsum; 5DSM; -.
DR   PDBsum; 5DSO; -.
DR   PDBsum; 5DSP; -.
DR   PDBsum; 5DSQ; -.
DR   PDBsum; 5DSR; -.
DR   PDBsum; 5E28; -.
DR   PDBsum; 5E2K; -.
DR   PDBsum; 5E2R; -.
DR   PDBsum; 5E2S; -.
DR   PDBsum; 5EH5; -.
DR   PDBsum; 5EH7; -.
DR   PDBsum; 5EH8; -.
DR   PDBsum; 5EHE; -.
DR   PDBsum; 5EHV; -.
DR   PDBsum; 5EHW; -.
DR   PDBsum; 5EIJ; -.
DR   PDBsum; 5EKH; -.
DR   PDBsum; 5EKJ; -.
DR   PDBsum; 5EKM; -.
DR   PDBsum; 5EOI; -.
DR   PDBsum; 5FDC; -.
DR   PDBsum; 5FDI; -.
DR   PDBsum; 5FLO; -.
DR   PDBsum; 5FLP; -.
DR   PDBsum; 5FLQ; -.
DR   PDBsum; 5FLR; -.
DR   PDBsum; 5FLS; -.
DR   PDBsum; 5FLT; -.
DR   PDBsum; 5FNG; -.
DR   PDBsum; 5FNH; -.
DR   PDBsum; 5FNI; -.
DR   PDBsum; 5FNJ; -.
DR   PDBsum; 5FNK; -.
DR   PDBsum; 5FNL; -.
DR   PDBsum; 5FNM; -.
DR   PDBsum; 5G01; -.
DR   PDBsum; 5G03; -.
DR   PDBsum; 5G0B; -.
DR   PDBsum; 5G0C; -.
DR   PDBsum; 5GMN; -.
DR   PDBsum; 5J8Z; -.
DR   PDBsum; 5JDV; -.
DR   PDBsum; 5JE7; -.
DR   PDBsum; 5JEG; -.
DR   PDBsum; 5JEH; -.
DR   PDBsum; 5JEP; -.
DR   PDBsum; 5JES; -.
DR   PDBsum; 5JG3; -.
DR   PDBsum; 5JG5; -.
DR   PDBsum; 5JGS; -.
DR   PDBsum; 5JGT; -.
DR   PDBsum; 5JMZ; -.
DR   PDBsum; 5JN3; -.
DR   PDBsum; 5JN7; -.
DR   PDBsum; 5JQ0; -.
DR   PDBsum; 5JQT; -.
DR   PDBsum; 5L3O; -.
DR   PDBsum; 5L6K; -.
DR   PDBsum; 5L6T; -.
DR   PDBsum; 5L70; -.
DR   PDBsum; 5L9E; -.
DR   PDBsum; 5LJQ; -.
DR   PDBsum; 5LJT; -.
DR   PDBsum; 5LL4; -.
DR   PDBsum; 5LL8; -.
DR   PDBsum; 5LLC; -.
DR   PDBsum; 5LLE; -.
DR   PDBsum; 5LLG; -.
DR   PDBsum; 5LLH; -.
DR   PDBsum; 5LMD; -.
DR   PDBsum; 5LVS; -.
DR   PDBsum; 5M78; -.
DR   PDBsum; 5MJN; -.
DR   PDBsum; 5N0D; -.
DR   PDBsum; 5N0E; -.
DR   PDBsum; 5N1R; -.
DR   PDBsum; 5N1S; -.
DR   PDBsum; 5N24; -.
DR   PDBsum; 5N25; -.
DR   PDBsum; 5NEA; -.
DR   PDBsum; 5NEE; -.
DR   PDBsum; 5NXG; -.
DR   PDBsum; 5NXI; -.
DR   PDBsum; 5NXM; -.
DR   PDBsum; 5NXO; -.
DR   PDBsum; 5NXP; -.
DR   PDBsum; 5NXV; -.
DR   PDBsum; 5NXW; -.
DR   PDBsum; 5NY1; -.
DR   PDBsum; 5NY3; -.
DR   PDBsum; 5NY6; -.
DR   PDBsum; 5NYA; -.
DR   PDBsum; 5O07; -.
DR   PDBsum; 5OGN; -.
DR   PDBsum; 5OGO; -.
DR   PDBsum; 5OGP; -.
DR   PDBsum; 5SZ0; -.
DR   PDBsum; 5SZ1; -.
DR   PDBsum; 5SZ2; -.
DR   PDBsum; 5SZ3; -.
DR   PDBsum; 5SZ4; -.
DR   PDBsum; 5SZ5; -.
DR   PDBsum; 5SZ6; -.
DR   PDBsum; 5SZ7; -.
DR   PDBsum; 5T71; -.
DR   PDBsum; 5T72; -.
DR   PDBsum; 5T74; -.
DR   PDBsum; 5T75; -.
DR   PDBsum; 5TFX; -.
DR   PDBsum; 5TH4; -.
DR   PDBsum; 5THI; -.
DR   PDBsum; 5THJ; -.
DR   PDBsum; 5THN; -.
DR   PDBsum; 5TI0; -.
DR   PDBsum; 5TXY; -.
DR   PDBsum; 5TY1; -.
DR   PDBsum; 5TY8; -.
DR   PDBsum; 5TY9; -.
DR   PDBsum; 5TYA; -.
DR   PDBsum; 5U0D; -.
DR   PDBsum; 5U0E; -.
DR   PDBsum; 5U0F; -.
DR   PDBsum; 5U0G; -.
DR   PDBsum; 5ULN; -.
DR   PDBsum; 5UMC; -.
DR   PDBsum; 5VGY; -.
DR   PDBsum; 5W8B; -.
DR   PDBsum; 5WEX; -.
DR   PDBsum; 5WG7; -.
DR   PDBsum; 5WGP; -.
DR   PDBsum; 5WLR; -.
DR   PDBsum; 5WLT; -.
DR   PDBsum; 5WLU; -.
DR   PDBsum; 5WLV; -.
DR   PDBsum; 5Y2R; -.
DR   PDBsum; 5Y2S; -.
DR   PDBsum; 5YUI; -.
DR   PDBsum; 5YUJ; -.
DR   PDBsum; 5YUK; -.
DR   PDBsum; 5ZXW; -.
DR   PDBsum; 6B00; -.
DR   PDBsum; 6B4D; -.
DR   PDBsum; 6B59; -.
DR   PDBsum; 6B5A; -.
DR   PDBsum; 6BBS; -.
DR   PDBsum; 6BC9; -.
DR   PDBsum; 6BCC; -.
DR   PDBsum; 6C7W; -.
DR   PDBsum; 6C7X; -.
DR   PDBsum; 6CA2; -.
DR   PDBsum; 6CEH; -.
DR   PDBsum; 6CJV; -.
DR   PDBsum; 6D1L; -.
DR   PDBsum; 6D1M; -.
DR   PDBsum; 6E8P; -.
DR   PDBsum; 6E8X; -.
DR   PDBsum; 6E91; -.
DR   PDBsum; 6E92; -.
DR   PDBsum; 6EBE; -.
DR   PDBsum; 6ECZ; -.
DR   PDBsum; 6EDA; -.
DR   PDBsum; 6EEA; -.
DR   PDBsum; 6EEH; -.
DR   PDBsum; 6EEO; -.
DR   PDBsum; 6EQU; -.
DR   PDBsum; 6FJI; -.
DR   PDBsum; 6FJJ; -.
DR   PDBsum; 6G3Q; -.
DR   PDBsum; 6G6T; -.
DR   PDBsum; 6GCY; -.
DR   PDBsum; 6GDC; -.
DR   PDBsum; 6GM9; -.
DR   PDBsum; 6GOT; -.
DR   PDBsum; 6GXB; -.
DR   PDBsum; 6GXE; -.
DR   PDBsum; 6H29; -.
DR   PDBsum; 6H2Z; -.
DR   PDBsum; 6H33; -.
DR   PDBsum; 6H34; -.
DR   PDBsum; 6H3Q; -.
DR   PDBsum; 6H6S; -.
DR   PDBsum; 6HD2; -.
DR   PDBsum; 6HQX; -.
DR   PDBsum; 6HR3; -.
DR   PDBsum; 6HX5; -.
DR   PDBsum; 6HXD; -.
DR   PDBsum; 6HZX; -.
DR   PDBsum; 6I0W; -.
DR   PDBsum; 6I1U; -.
DR   PDBsum; 6I2F; -.
DR   PDBsum; 6I3E; -.
DR   PDBsum; 6IC2; -.
DR   PDBsum; 6KLZ; -.
DR   PDBsum; 6KM0; -.
DR   PDBsum; 6KM1; -.
DR   PDBsum; 6KM2; -.
DR   PDBsum; 6KM3; -.
DR   PDBsum; 6KM4; -.
DR   PDBsum; 6KM5; -.
DR   PDBsum; 6KM6; -.
DR   PDBsum; 6LUU; -.
DR   PDBsum; 6LUV; -.
DR   PDBsum; 6LUW; -.
DR   PDBsum; 6LUX; -.
DR   PDBsum; 6LUY; -.
DR   PDBsum; 6LUZ; -.
DR   PDBsum; 6LV1; -.
DR   PDBsum; 6LV2; -.
DR   PDBsum; 6LV3; -.
DR   PDBsum; 6LV4; -.
DR   PDBsum; 6LV5; -.
DR   PDBsum; 6LV6; -.
DR   PDBsum; 6LV7; -.
DR   PDBsum; 6LV8; -.
DR   PDBsum; 6LV9; -.
DR   PDBsum; 6LVA; -.
DR   PDBsum; 6MBV; -.
DR   PDBsum; 6MBY; -.
DR   PDBsum; 6NJ2; -.
DR   PDBsum; 6NJ3; -.
DR   PDBsum; 6NJ4; -.
DR   PDBsum; 6NJ5; -.
DR   PDBsum; 6NJ6; -.
DR   PDBsum; 6NLV; -.
DR   PDBsum; 6NM0; -.
DR   PDBsum; 6ODZ; -.
DR   PDBsum; 6OE0; -.
DR   PDBsum; 6OE1; -.
DR   PDBsum; 6OTI; -.
DR   PDBsum; 6OTK; -.
DR   PDBsum; 6OTM; -.
DR   PDBsum; 6OTO; -.
DR   PDBsum; 6OTP; -.
DR   PDBsum; 6OTQ; -.
DR   PDBsum; 6OUB; -.
DR   PDBsum; 6OUD; -.
DR   PDBsum; 6OUE; -.
DR   PDBsum; 6OUF; -.
DR   PDBsum; 6OUH; -.
DR   PDBsum; 6OUI; -.
DR   PDBsum; 6OUJ; -.
DR   PDBsum; 6OUK; -.
DR   PDBsum; 6OUM; -.
DR   PDBsum; 6PDV; -.
DR   PDBsum; 6PEA; -.
DR   PDBsum; 6PGX; -.
DR   PDBsum; 6Q3O; -.
DR   PDBsum; 6Q9T; -.
DR   PDBsum; 6QEB; -.
DR   PDBsum; 6QFU; -.
DR   PDBsum; 6QFV; -.
DR   PDBsum; 6QFW; -.
DR   PDBsum; 6QFX; -.
DR   PDBsum; 6QL1; -.
DR   PDBsum; 6QL2; -.
DR   PDBsum; 6QL3; -.
DR   PDBsum; 6R6F; -.
DR   PDBsum; 6R6J; -.
DR   PDBsum; 6RFH; -.
DR   PDBsum; 6RG3; -.
DR   PDBsum; 6RG4; -.
DR   PDBsum; 6RG5; -.
DR   PDBsum; 6RH4; -.
DR   PDBsum; 6RHJ; -.
DR   PDBsum; 6RHK; -.
DR   PDBsum; 6RIG; -.
DR   PDBsum; 6RIT; -.
DR   PDBsum; 6RJJ; -.
DR   PDBsum; 6RKN; -.
DR   PDBsum; 6RL9; -.
DR   PDBsum; 6RM1; -.
DR   PDBsum; 6RMP; -.
DR   PDBsum; 6RMX; -.
DR   PDBsum; 6RMY; -.
DR   PDBsum; 6RNP; -.
DR   PDBsum; 6ROB; -.
DR   PDBsum; 6ROE; -.
DR   PDBsum; 6ROF; -.
DR   PDBsum; 6RQI; -.
DR   PDBsum; 6RRG; -.
DR   PDBsum; 6RRI; -.
DR   PDBsum; 6RS5; -.
DR   PDBsum; 6RSZ; -.
DR   PDBsum; 6RVF; -.
DR   PDBsum; 6RVK; -.
DR   PDBsum; 6RVL; -.
DR   PDBsum; 6RW1; -.
DR   PDBsum; 6RZX; -.
DR   PDBsum; 6S03; -.
DR   PDBsum; 6S9G; -.
DR   PDBsum; 6S9Z; -.
DR   PDBsum; 6SAC; -.
DR   PDBsum; 6SAS; -.
DR   PDBsum; 6SAY; -.
DR   PDBsum; 6SB7; -.
DR   PDBsum; 6SBH; -.
DR   PDBsum; 6SBL; -.
DR   PDBsum; 6SBM; -.
DR   PDBsum; 6SD7; -.
DR   PDBsum; 6SDH; -.
DR   PDBsum; 6SDI; -.
DR   PDBsum; 6SDJ; -.
DR   PDBsum; 6SDL; -.
DR   PDBsum; 6SDS; -.
DR   PDBsum; 6SEY; -.
DR   PDBsum; 6SFQ; -.
DR   PDBsum; 6SFU; -.
DR   PDBsum; 6SG0; -.
DR   PDBsum; 6SG6; -.
DR   PDBsum; 6SX9; -.
DR   PDBsum; 6SYB; -.
DR   PDBsum; 6SYS; -.
DR   PDBsum; 6T4N; -.
DR   PDBsum; 6T4O; -.
DR   PDBsum; 6T4P; -.
DR   PDBsum; 6T5C; -.
DR   PDBsum; 6T7U; -.
DR   PDBsum; 6T81; -.
DR   PDBsum; 6T9Z; -.
DR   PDBsum; 6U4Q; -.
DR   PDBsum; 6U4T; -.
DR   PDBsum; 6UFB; -.
DR   PDBsum; 6UFC; -.
DR   PDBsum; 6UFD; -.
DR   PDBsum; 6UGN; -.
DR   PDBsum; 6UGO; -.
DR   PDBsum; 6UGP; -.
DR   PDBsum; 6UGQ; -.
DR   PDBsum; 6UGR; -.
DR   PDBsum; 6UGZ; -.
DR   PDBsum; 6UH0; -.
DR   PDBsum; 6UX1; -.
DR   PDBsum; 6UZU; -.
DR   PDBsum; 6VJ3; -.
DR   PDBsum; 6VKG; -.
DR   PDBsum; 6WKA; -.
DR   PDBsum; 6WQ4; -.
DR   PDBsum; 6WQ5; -.
DR   PDBsum; 6WQ7; -.
DR   PDBsum; 6WQ8; -.
DR   PDBsum; 6WQ9; -.
DR   PDBsum; 6XVH; -.
DR   PDBsum; 6XWZ; -.
DR   PDBsum; 6XXT; -.
DR   PDBsum; 6YH4; -.
DR   PDBsum; 6YH5; -.
DR   PDBsum; 6YH6; -.
DR   PDBsum; 6YH7; -.
DR   PDBsum; 6YH8; -.
DR   PDBsum; 6YH9; -.
DR   PDBsum; 6YHA; -.
DR   PDBsum; 6YHB; -.
DR   PDBsum; 6YHC; -.
DR   PDBsum; 6YJ3; -.
DR   PDBsum; 6YKC; -.
DR   PDBsum; 6YKH; -.
DR   PDBsum; 6YMA; -.
DR   PDBsum; 6YMB; -.
DR   PDBsum; 6YO2; -.
DR   PDBsum; 6YO4; -.
DR   PDBsum; 6YO7; -.
DR   PDBsum; 6YOI; -.
DR   PDBsum; 6YOK; -.
DR   PDBsum; 6YOL; -.
DR   PDBsum; 6YPW; -.
DR   PDBsum; 6YQT; -.
DR   PDBsum; 6YQU; -.
DR   PDBsum; 6YRI; -.
DR   PDBsum; 6YZJ; -.
DR   PDBsum; 6YZK; -.
DR   PDBsum; 6YZL; -.
DR   PDBsum; 6YZM; -.
DR   PDBsum; 6YZN; -.
DR   PDBsum; 6YZO; -.
DR   PDBsum; 6YZP; -.
DR   PDBsum; 6YZQ; -.
DR   PDBsum; 6YZR; -.
DR   PDBsum; 6YZS; -.
DR   PDBsum; 6YZT; -.
DR   PDBsum; 6YZU; -.
DR   PDBsum; 6YZV; -.
DR   PDBsum; 6YZW; -.
DR   PDBsum; 6YZX; -.
DR   PDBsum; 6Z04; -.
DR   PDBsum; 6ZR8; -.
DR   PDBsum; 7A6V; -.
DR   PDBsum; 7AEQ; -.
DR   PDBsum; 7AES; -.
DR   PDBsum; 7AGN; -.
DR   PDBsum; 7ASJ; -.
DR   PDBsum; 7BFA; -.
DR   PDBsum; 7BG5; -.
DR   PDBsum; 7BHH; -.
DR   PDBsum; 7BI5; -.
DR   PDBsum; 7CA2; -.
DR   PDBsum; 7JNR; -.
DR   PDBsum; 7JNV; -.
DR   PDBsum; 7JNW; -.
DR   PDBsum; 7JNX; -.
DR   PDBsum; 7JNZ; -.
DR   PDBsum; 7JO0; -.
DR   PDBsum; 7JO1; -.
DR   PDBsum; 7JO2; -.
DR   PDBsum; 7JO3; -.
DR   PDBsum; 7JOB; -.
DR   PDBsum; 7JOC; -.
DR   PDBsum; 7K6I; -.
DR   PDBsum; 7K6J; -.
DR   PDBsum; 7K6K; -.
DR   PDBsum; 7K6L; -.
DR   PDBsum; 7K6T; -.
DR   PDBsum; 7K6U; -.
DR   PDBsum; 7K6X; -.
DR   PDBsum; 7K6Z; -.
DR   PDBsum; 7M23; -.
DR   PDBsum; 7M24; -.
DR   PDBsum; 7M26; -.
DR   PDBsum; 7MU3; -.
DR   PDBsum; 7NH6; -.
DR   PDBsum; 7NH8; -.
DR   PDBsum; 7NTB; -.
DR   PDBsum; 7NZR; -.
DR   PDBsum; 7NZS; -.
DR   PDBsum; 7NZT; -.
DR   PDBsum; 7NZU; -.
DR   PDBsum; 7NZW; -.
DR   PDBsum; 7NZX; -.
DR   PDBsum; 7OK8; -.
DR   PDBsum; 7ONM; -.
DR   PDBsum; 7ONP; -.
DR   PDBsum; 7ONQ; -.
DR   PDBsum; 7ONV; -.
DR   PDBsum; 7ORP; -.
DR   PDBsum; 7ORQ; -.
DR   PDBsum; 7OYM; -.
DR   PDBsum; 7OYN; -.
DR   PDBsum; 7OYO; -.
DR   PDBsum; 7OYP; -.
DR   PDBsum; 7OYQ; -.
DR   PDBsum; 7OYR; -.
DR   PDBsum; 7Q0C; -.
DR   PDBsum; 7Q0E; -.
DR   PDBsum; 7QBH; -.
DR   PDBsum; 7QGX; -.
DR   PDBsum; 7QGY; -.
DR   PDBsum; 7QGZ; -.
DR   PDBsum; 7QNV; -.
DR   PDBsum; 7QRK; -.
DR   PDBsum; 7QSE; -.
DR   PDBsum; 7QSI; -.
DR   PDBsum; 7QZX; -.
DR   PDBsum; 7R1X; -.
DR   PDBsum; 7RNY; -.
DR   PDBsum; 7RNZ; -.
DR   PDBsum; 7RRE; -.
DR   PDBsum; 7RRF; -.
DR   PDBsum; 7SUW; -.
DR   PDBsum; 7SUY; -.
DR   PDBsum; 7SV1; -.
DR   PDBsum; 7SV8; -.
DR   PDBsum; 7U5W; -.
DR   PDBsum; 7U5X; -.
DR   PDBsum; 7Y2A; -.
DR   PDBsum; 7Y2C; -.
DR   PDBsum; 7Y2E; -.
DR   PDBsum; 7Y2F; -.
DR   PDBsum; 7Y2G; -.
DR   PDBsum; 7Y2H; -.
DR   PDBsum; 7Y2I; -.
DR   PDBsum; 7Y2J; -.
DR   PDBsum; 7Y2K; -.
DR   PDBsum; 7Y2L; -.
DR   PDBsum; 7Y2M; -.
DR   PDBsum; 7Y2N; -.
DR   PDBsum; 7Y2O; -.
DR   PDBsum; 7Y2Q; -.
DR   PDBsum; 7Y2R; -.
DR   PDBsum; 7Y2S; -.
DR   PDBsum; 7Y2T; -.
DR   PDBsum; 7Y2U; -.
DR   PDBsum; 7Y2V; -.
DR   PDBsum; 7Y2W; -.
DR   PDBsum; 7Y2X; -.
DR   PDBsum; 7YWT; -.
DR   PDBsum; 7ZL6; -.
DR   PDBsum; 7ZWB; -.
DR   PDBsum; 8AA6; -.
DR   PDBsum; 8AAE; -.
DR   PDBsum; 8B29; -.
DR   PDBsum; 8BJX; -.
DR   PDBsum; 8BOE; -.
DR   PDBsum; 8BZZ; -.
DR   PDBsum; 8C0Q; -.
DR   PDBsum; 8C0R; -.
DR   PDBsum; 8CA2; -.
DR   PDBsum; 8CR0; -.
DR   PDBsum; 8DJ9; -.
DR   PDBsum; 8EM3; -.
DR   PDBsum; 8EMU; -.
DR   PDBsum; 8EXC; -.
DR   PDBsum; 8EXG; -.
DR   PDBsum; 8EYL; -.
DR   PDBsum; 8FAL; -.
DR   PDBsum; 8FAU; -.
DR   PDBsum; 8FQX; -.
DR   PDBsum; 8FQY; -.
DR   PDBsum; 8FQZ; -.
DR   PDBsum; 8FR1; -.
DR   PDBsum; 8FR2; -.
DR   PDBsum; 8FR4; -.
DR   PDBsum; 8IGF; -.
DR   PDBsum; 8J2O; -.
DR   PDBsum; 8JEE; -.
DR   PDBsum; 8OGD; -.
DR   PDBsum; 8OGE; -.
DR   PDBsum; 8OGF; -.
DR   PDBsum; 8OKE; -.
DR   PDBsum; 8OKG; -.
DR   PDBsum; 8OKJ; -.
DR   PDBsum; 8OKO; -.
DR   PDBsum; 8OKP; -.
DR   PDBsum; 8OKQ; -.
DR   PDBsum; 8OKT; -.
DR   PDBsum; 8OLA; -.
DR   PDBsum; 8OLF; -.
DR   PDBsum; 8OLI; -.
DR   PDBsum; 8OLK; -.
DR   PDBsum; 8OLM; -.
DR   PDBsum; 8OMB; -.
DR   PDBsum; 8OMH; -.
DR   PDBsum; 8OMN; -.
DR   PDBsum; 8OMP; -.
DR   PDBsum; 8OO8; -.
DR   PDBsum; 8OTP; -.
DR   PDBsum; 8OUB; -.
DR   PDBsum; 8P6U; -.
DR   PDBsum; 8PHL; -.
DR   PDBsum; 8PHM; -.
DR   PDBsum; 8Q0C; -.
DR   PDBsum; 8QF7; -.
DR   PDBsum; 8QF9; -.
DR   PDBsum; 8QFK; -.
DR   PDBsum; 8QH8; -.
DR   PDBsum; 8QHG; -.
DR   PDBsum; 8QHJ; -.
DR   PDBsum; 8QHO; -.
DR   PDBsum; 8QKZ; -.
DR   PDBsum; 8QQA; -.
DR   PDBsum; 8QUF; -.
DR   PDBsum; 8R1I; -.
DR   PDBsum; 8R2F; -.
DR   PDBsum; 8R2K; -.
DR   PDBsum; 8RAR; -.
DR   PDBsum; 8RBP; -.
DR   PDBsum; 8RJ2; -.
DR   PDBsum; 8RLP; -.
DR   PDBsum; 8RLQ; -.
DR   PDBsum; 8RNS; -.
DR   PDBsum; 8ROU; -.
DR   PDBsum; 8ROW; -.
DR   PDBsum; 8SAF; -.
DR   PDBsum; 8SAG; -.
DR   PDBsum; 8SD1; -.
DR   PDBsum; 8SD6; -.
DR   PDBsum; 8SD7; -.
DR   PDBsum; 8SD8; -.
DR   PDBsum; 8SD9; -.
DR   PDBsum; 8SF1; -.
DR   PDBsum; 8TTR; -.
DR   PDBsum; 8UFW; -.
DR   PDBsum; 8UFX; -.
DR   PDBsum; 8VQ5; -.
DR   PDBsum; 8VQ6; -.
DR   PDBsum; 8VQ7; -.
DR   PDBsum; 8VZG; -.
DR   PDBsum; 8WEP; -.
DR   PDBsum; 8WER; -.
DR   PDBsum; 8WES; -.
DR   PDBsum; 8ZWV; -.
DR   PDBsum; 9CA2; -.
DR   PDBsum; 9EN8; -.
DR   PDBsum; 9EN9; -.
DR   PDBsum; 9F15; -.
DR   PDBsum; 9F2E; -.
DR   PDBsum; 9F2F; -.
DR   PDBsum; 9FAI; -.
DR   PDBsum; 9FAO; -.
DR   PDBsum; 9FJQ; -.
DR   PDBsum; 9FJV; -.
DR   PDBsum; 9FPQ; -.
DR   PDBsum; 9FPR; -.
DR   PDBsum; 9FPS; -.
DR   PDBsum; 9FPT; -.
DR   PDBsum; 9FPU; -.
DR   PDBsum; 9G38; -.
DR   PDBsum; 9GAJ; -.
DR   PDBsum; 9GAK; -.
DR   PDBsum; 9GAM; -.
DR   PDBsum; 9GFV; -.
DR   PDBsum; 9GFW; -.
DR   PDBsum; 9GFX; -.
DR   PDBsum; 9GOO; -.
DR   PDBsum; 9GU7; -.
DR   PDBsum; 9GUM; -.
DR   PDBsum; 9GUO; -.
DR   PDBsum; 9H0V; -.
DR   PDBsum; 9H0W; -.
DR   PDBsum; 9H3H; -.
DR   PDBsum; 9HD6; -.
DR   PDBsum; 9HGP; -.
DR   PDBsum; 9HNX; -.
DR   PDBsum; 9HQ3; -.
DR   PDBsum; 9HQG; -.
DR   PDBsum; 9HWM; -.
DR   PDBsum; 9HXZ; -.
DR   PDBsum; 9I29; -.
DR   PDBsum; 9JWE; -.
DR   PDBsum; 9JWU; -.
DR   PDBsum; 9JWW; -.
DR   PDBsum; 9KH8; -.
DR   PDBsum; 9L2X; -.
DR   PDBsum; 9L2Y; -.
DR   PDBsum; 9L2Z; -.
DR   PDBsum; 9L30; -.
DR   PDBsum; 9L31; -.
DR   PDBsum; 9L32; -.
DR   PDBsum; 9L33; -.
DR   PDBsum; 9LDO; -.
DR   PDBsum; 9LDP; -.
DR   PDBsum; 9LR6; -.
DR   PDBsum; 9O8X; -.
DR   PDBsum; 9OAF; -.
DR   PDBsum; 9OAM; -.
DR   PDBsum; 9OBJ; -.
DR   PDBsum; 9P0W; -.
DR   PDBsum; 9RAY; -.
DR   PDBsum; 9U5B; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cell membrane; Cytoplasm;
KW   Direct protein sequencing; Disease variant; Lyase; Membrane; Metal-binding;
KW   Osteopetrosis; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:4207120,
FT                   ECO:0000269|PubMed:823150"
FT   CHAIN           2..260
FT                   /note="Carbonic anhydrase 2"
FT                   /id="PRO_0000077418"
FT   DOMAIN          3..259
FT                   /note="Alpha-carbonic anhydrase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01134"
FT   ACT_SITE        64
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000305|PubMed:15667203,
FT                   ECO:0000305|PubMed:17330962"
FT   BINDING         94
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:11076507,
FT                   ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460,
FT                   ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891,
FT                   ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019,
FT                   ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:4621826,
FT                   ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7803386,
FT                   ECO:0000269|PubMed:7901850, ECO:0000269|PubMed:8218160,
FT                   ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8331673,
FT                   ECO:0000269|PubMed:8399159, ECO:0000269|PubMed:8431430,
FT                   ECO:0000269|PubMed:8451242, ECO:0000269|PubMed:8482389,
FT                   ECO:0000269|PubMed:8639494, ECO:0000269|PubMed:8987974,
FT                   ECO:0000269|PubMed:9398308, ECO:0000269|PubMed:9865942"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:11076507,
FT                   ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460,
FT                   ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891,
FT                   ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019,
FT                   ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440,
FT                   ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850,
FT                   ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987,
FT                   ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159,
FT                   ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242,
FT                   ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494,
FT                   ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308,
FT                   ECO:0000269|PubMed:9865942"
FT   BINDING         119
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000269|PubMed:11076507,
FT                   ECO:0000269|PubMed:12499545, ECO:0000269|PubMed:1336460,
FT                   ECO:0000269|PubMed:1433293, ECO:0000269|PubMed:1909891,
FT                   ECO:0000269|PubMed:19583303, ECO:0000269|PubMed:3151019,
FT                   ECO:0000269|PubMed:3151020, ECO:0000269|PubMed:7761440,
FT                   ECO:0000269|PubMed:7803386, ECO:0000269|PubMed:7901850,
FT                   ECO:0000269|PubMed:8218160, ECO:0000269|PubMed:8262987,
FT                   ECO:0000269|PubMed:8331673, ECO:0000269|PubMed:8399159,
FT                   ECO:0000269|PubMed:8431430, ECO:0000269|PubMed:8451242,
FT                   ECO:0000269|PubMed:8482389, ECO:0000269|PubMed:8639494,
FT                   ECO:0000269|PubMed:8987974, ECO:0000269|PubMed:9398308,
FT                   ECO:0000269|PubMed:9865942"
FT   BINDING         198..199
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000269|PubMed:10550681,
FT                   ECO:0000269|PubMed:19520834"
FT   SITE            7
FT                   /note="Fine-tunes the proton-transfer properties of H-64"
FT                   /evidence="ECO:0000305|PubMed:17330962"
FT   SITE            62
FT                   /note="Fine-tunes the proton-transfer properties of H-64;
FT                   involved in the binding of some activators, including
FT                   histamine and L-histidine"
FT                   /evidence="ECO:0000269|PubMed:16214338,
FT                   ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962"
FT   SITE            67
FT                   /note="Fine-tunes the proton-transfer properties of H-64;
FT                   involved in the binding of some activators, including
FT                   histamine and L-histidine"
FT                   /evidence="ECO:0000269|PubMed:16214338,
FT                   ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962"
FT   SITE            92
FT                   /note="Involved in the binding of some activators,
FT                   including histamine and L-histidine"
FT                   /evidence="ECO:0000269|PubMed:16214338,
FT                   ECO:0000269|PubMed:9265618, ECO:0000305|PubMed:17330962"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:4207120,
FT                   ECO:0000269|PubMed:823150"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P27139"
FT   MOD_RES         165
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VARIANT         18
FT                   /note="K -> E (in Jogjakarta; dbSNP:rs118203931)"
FT                   /evidence="ECO:0000269|PubMed:6817747"
FT                   /id="VAR_001380"
FT   VARIANT         92
FT                   /note="Q -> P (in OPTB3; in Czechoslovakia;
FT                   dbSNP:rs1304160279)"
FT                   /evidence="ECO:0000269|PubMed:15300855,
FT                   ECO:0000269|PubMed:9143915"
FT                   /id="VAR_001381"
FT   VARIANT         94
FT                   /note="H -> Y (in OPTB3; partial loss of activity)"
FT                   /evidence="ECO:0000269|PubMed:15300855"
FT                   /id="VAR_021009"
FT   VARIANT         107
FT                   /note="H -> Y (in OPTB3; dbSNP:rs118203933)"
FT                   /evidence="ECO:0000269|PubMed:15300855,
FT                   ECO:0000269|PubMed:1542674, ECO:0000269|PubMed:1928091,
FT                   ECO:0000269|PubMed:8834238"
FT                   /id="VAR_001382"
FT   VARIANT         144
FT                   /note="G -> R (in OPTB3; complete loss of activity)"
FT                   /evidence="ECO:0000269|PubMed:15300855"
FT                   /id="VAR_021010"
FT   VARIANT         236
FT                   /note="P -> H (in Melbourne; dbSNP:rs118203932)"
FT                   /evidence="ECO:0000269|PubMed:6407977"
FT                   /id="VAR_001383"
FT   VARIANT         252
FT                   /note="N -> D (in dbSNP:rs2228063)"
FT                   /id="VAR_001384"
FT   MUTAGEN         5
FT                   /note="W->A: Impaired activity, not rescued by
FT                   4-methylimidazole (4-MI); when associated with W-64."
FT                   /evidence="ECO:0000269|PubMed:17071654"
FT   MUTAGEN         7
FT                   /note="Y->F: Enhanced activity."
FT                   /evidence="ECO:0000269|PubMed:12171926,
FT                   ECO:0000269|PubMed:17330962"
FT   MUTAGEN         7
FT                   /note="Y->H: Reduced proton transfer rate."
FT                   /evidence="ECO:0000269|PubMed:12171926,
FT                   ECO:0000269|PubMed:17330962"
FT   MUTAGEN         62
FT                   /note="N->A: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:18942852"
FT   MUTAGEN         62
FT                   /note="N->D: Strongly reduced activity."
FT                   /evidence="ECO:0000269|PubMed:18942852"
FT   MUTAGEN         62
FT                   /note="N->H: Reduced proton transfer; when associated with
FT                   A-64."
FT                   /evidence="ECO:0000269|PubMed:15667203,
FT                   ECO:0000269|PubMed:17330962, ECO:0000269|PubMed:18942852"
FT   MUTAGEN         62
FT                   /note="N->L: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:17330962,
FT                   ECO:0000269|PubMed:18942852"
FT   MUTAGEN         62
FT                   /note="N->T: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:18942852"
FT   MUTAGEN         62
FT                   /note="N->V: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:18942852"
FT   MUTAGEN         64
FT                   /note="H->A: Reduced CO(2) hydrase activity, rescued by
FT                   4-methylimidazole (4-MI). Reduced proton transfer; when
FT                   associated with H-62. Enhanced proton transfer; when
FT                   associated with H-67. Enhanced proton transfer capacity;
FT                   when associated with H-99."
FT                   /evidence="ECO:0000269|PubMed:11327835,
FT                   ECO:0000269|PubMed:15667203, ECO:0000269|PubMed:16106378,
FT                   ECO:0000269|PubMed:17071654"
FT   MUTAGEN         64
FT                   /note="H->G: Impaired activity, not rescued by
FT                   4-methylimidazole (4-MI)."
FT                   /evidence="ECO:0000269|PubMed:11327835,
FT                   ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:17071654"
FT   MUTAGEN         64
FT                   /note="H->W: Impaired activity, rescued by
FT                   4-methylimidazole (4-MI). Impaired activity, not rescued by
FT                   4-methylimidazole (4-MI); when associated with A-5."
FT                   /evidence="ECO:0000269|PubMed:11327835,
FT                   ECO:0000269|PubMed:16106378, ECO:0000269|PubMed:17071654"
FT   MUTAGEN         65
FT                   /note="A->F: Reduced activity."
FT   MUTAGEN         65
FT                   /note="A->S: 2-fold decrease in enzyme efficiency, as
FT                   determined by kcat/KM ratio, and efficiently inhibited by
FT                   chlorzolamide; when associated with Q-67."
FT                   /evidence="ECO:0000269|PubMed:19170619"
FT   MUTAGEN         67
FT                   /note="N->H: Enhanced proton transfer; when associated with
FT                   A-64."
FT                   /evidence="ECO:0000269|PubMed:15667203"
FT   MUTAGEN         67
FT                   /note="N->L: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:17330962"
FT   MUTAGEN         67
FT                   /note="N->Q: 2-fold decrease in enzyme efficiency, as
FT                   determined by kcat/KM ratio, and efficiently inhibited by
FT                   chlorzolamide; when associated with S-65."
FT                   /evidence="ECO:0000269|PubMed:19170619"
FT   MUTAGEN         94
FT                   /note="H->C,D,E,N,Q: Strongly reduced CO(2) hydrase and
FT                   p-nitrophenyl acetate esterase activities, impaired
FT                   stability of zinc binding."
FT                   /evidence="ECO:0000269|PubMed:8431430,
FT                   ECO:0000269|PubMed:9398308"
FT   MUTAGEN         106
FT                   /note="E->A,Q: Strongly reduced CO(2) hydrase activity."
FT                   /evidence="ECO:0000269|PubMed:15299482,
FT                   ECO:0000269|PubMed:7901850"
FT   MUTAGEN         106
FT                   /note="E->D: Normal CO(2) hydrase activity."
FT                   /evidence="ECO:0000269|PubMed:15299482,
FT                   ECO:0000269|PubMed:7901850"
FT   MUTAGEN         117
FT                   /note="E->Q: Strongly reduced activity and sulfonamide
FT                   affinity."
FT                   /evidence="ECO:0000269|PubMed:8639494"
FT   MUTAGEN         119
FT                   /note="H->D,N,Q: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:9398308"
FT   MUTAGEN         119
FT                   /note="H->E: Strongly reduced activity."
FT                   /evidence="ECO:0000269|PubMed:9398308"
FT   MUTAGEN         121
FT                   /note="V->A,G,I,L,S: Reduced CO(2) hydrase and
FT                   p-nitrophenyl acetate esterase activities."
FT                   /evidence="ECO:0000269|PubMed:1910042"
FT   MUTAGEN         121
FT                   /note="V->K,R: Strongly reduced CO(2) hydrase and
FT                   p-nitrophenyl acetate esterase activities."
FT                   /evidence="ECO:0000269|PubMed:1910042"
FT   MUTAGEN         142
FT                   /note="V->F,Y: Strongly impaired activity."
FT                   /evidence="ECO:0000269|PubMed:1932029"
FT   MUTAGEN         142
FT                   /note="V->G: Weakly impaired activity."
FT                   /evidence="ECO:0000269|PubMed:1932029"
FT   MUTAGEN         142
FT                   /note="V->H: Impaired activity."
FT                   /evidence="ECO:0000269|PubMed:1932029"
FT   MUTAGEN         197
FT                   /note="L->A: Reduced CO(2) hydrase activity."
FT                   /evidence="ECO:0000269|PubMed:8485129"
FT   MUTAGEN         197
FT                   /note="L->E,H,R: Strongly reduced CO(2) hydrase activity."
FT                   /evidence="ECO:0000269|PubMed:8485129"
FT   MUTAGEN         197
FT                   /note="L->F: Normal activity."
FT                   /evidence="ECO:0000269|PubMed:8485129"
FT   MUTAGEN         198
FT                   /note="T->A,C,H,P: Strongly reduced activity."
FT                   /evidence="ECO:0000269|PubMed:12056894,
FT                   ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850,
FT                   ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159"
FT   MUTAGEN         198
FT                   /note="T->D,E: Strongly reduced activity, but enhanced zinc
FT                   affinity."
FT                   /evidence="ECO:0000269|PubMed:12056894,
FT                   ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850,
FT                   ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159"
FT   MUTAGEN         198
FT                   /note="T->S,V: Reduced activity."
FT                   /evidence="ECO:0000269|PubMed:12056894,
FT                   ECO:0000269|PubMed:7761440, ECO:0000269|PubMed:7901850,
FT                   ECO:0000269|PubMed:8262987, ECO:0000269|PubMed:8399159"
FT   MUTAGEN         199
FT                   /note="T->H: Higher affinity for bicarbonate. Enhanced
FT                   proton transfer capacity; when associated with A-64."
FT                   /evidence="ECO:0000269|PubMed:16106378,
FT                   ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:8451242"
FT   MUTAGEN         199
FT                   /note="T->S: Enhanced p-nitrophenyl acetate esterase
FT                   activity, but normal CO(2) hydrase activity."
FT                   /evidence="ECO:0000269|PubMed:16106378,
FT                   ECO:0000269|PubMed:1909891, ECO:0000269|PubMed:8451242"
FT   MUTAGEN         201
FT                   /note="P->A: Normal CO(2) hydrase activity, but impaired
FT                   stability."
FT                   /evidence="ECO:0000269|PubMed:8218160"
FT   CONFLICT        179..180
FT                   /note="DP -> AA (in Ref. 6; AAH11949)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..5
FT                   /evidence="ECO:0007829|PDB:9F2F"
FT   STRAND          6..8
FT                   /evidence="ECO:0007829|PDB:5Y2R"
FT   TURN            9..11
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   TURN            13..15
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   HELIX           16..18
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   HELIX           21..24
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          25..27
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:2X7S"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:3KS3"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:3KOI"
FT   STRAND          45..50
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          56..61
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          77..82
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   TURN            83..85
FT                   /evidence="ECO:0007829|PDB:5GMN"
FT   STRAND          88..97
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          99..103
FT                   /evidence="ECO:0007829|PDB:6Q9T"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          115..124
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   HELIX           125..127
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   HELIX           130..133
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          139..151
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   HELIX           157..162
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   HELIX           163..165
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          172..174
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   HELIX           180..183
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          190..195
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          198..202
FT                   /evidence="ECO:0007829|PDB:6QEB"
FT   STRAND          206..213
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          215..217
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   HELIX           219..225
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   TURN            226..228
FT                   /evidence="ECO:0007829|PDB:4QK3"
FT   STRAND          229..231
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   STRAND          233..236
FT                   /evidence="ECO:0007829|PDB:7Q0C"
FT   HELIX           245..247
FT                   /evidence="ECO:0007829|PDB:3K34"
FT   HELIX           253..255
FT                   /evidence="ECO:0007829|PDB:6SAY"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:3K34"
SQ   SEQUENCE   260 AA;  29246 MW;  2EC2BB7548F10558 CRC64;
     MSHHWGYGKH NGPEHWHKDF PIAKGERQSP VDIDTHTAKY DPSLKPLSVS YDQATSLRIL
     NNGHAFNVEF DDSQDKAVLK GGPLDGTYRL IQFHFHWGSL DGQGSEHTVD KKKYAAELHL
     VHWNTKYGDF GKAVQQPDGL AVLGIFLKVG SAKPGLQKVV DVLDSIKTKG KSADFTNFDP
     RGLLPESLDY WTYPGSLTTP PLLECVTWIV LKEPISVSSE QVLKFRKLNF NGEGEPEELM
     VDNWRPAQPL KNRQIKASFK
//