NOS1_RAT
ID NOS1_RAT Reviewed; 1429 AA.
AC P29476; P70594;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=Nitric oxide synthase, brain;
DE EC=1.14.13.39;
DE AltName: Full=BNOS;
DE AltName: Full=Constitutive NOS;
DE AltName: Full=NC-NOS;
DE AltName: Full=NOS type I;
DE AltName: Full=Neuronal NOS;
DE Short=N-NOS;
DE Short=nNOS;
DE AltName: Full=Peptidyl-cysteine S-nitrosylase NOS1;
GN Name=Nos1; Synonyms=Bnos;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Brain;
RX PubMed=1712077; DOI=10.1038/351714a0;
RA Bredt D.S., Hwang P.M., Glatt C.L., Lowenstein C., Reed R.R., Snyder S.H.;
RT "Cloned and expressed nitric oxide synthase structurally resembles
RT cytochrome P-450 reductase.";
RL Nature 351:714-718(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PNNOS).
RC STRAIN=Fischer 344; TISSUE=Penis;
RX PubMed=8806605; DOI=10.1006/bbrc.1996.1324;
RA Magee T., Fuentes A.M., Garban H., Rajavashisth T., Marquez D.,
RA Rodriguez J.A., Rajfer J., Gonzalez-Cadavid N.F.;
RT "Cloning of a novel neuronal nitric oxide synthase expressed in penis and
RT lower urinary tract.";
RL Biochem. Biophys. Res. Commun. 226:145-151(1996).
RN [3]
RP PROTEIN SEQUENCE OF 119-129; 132-142; 144-156; 189-200; 264-276; 305-310;
RP 360-369; 376-379; 381-385; 387-396; 779-785; 953-963 AND 1131-1139, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Colon;
RX PubMed=7520037; DOI=10.1093/oxfordjournals.jbchem.a124382;
RA Seo H.G., Tatsumi H., Fujii J., Nishikawa A., Suzuki K., Kangawa K.,
RA Taniguchi N.;
RT "Nitric oxide synthase from rat colorectum: purification, peptide
RT sequencing, partial PCR cloning, and immunohistochemistry.";
RL J. Biochem. 115:602-607(1994).
RN [4]
RP IDENTIFICATION OF TETRAHYDROBIOPTERIN-BINDING DOMAIN.
RX PubMed=7530005; DOI=10.1006/bbrc.1995.1104;
RA Uvarov V.Y., Lyashenko A.A.;
RT "The identification of the pterin-binding domain in the nitric oxide
RT synthase's sequence.";
RL Biochem. Biophys. Res. Commun. 206:736-741(1995).
RN [5]
RP MUTAGENESIS OF TYR-588.
RX PubMed=11237702; DOI=10.1006/bbrc.2001.4356;
RA Sato Y., Sagami I., Matsui T., Shimizu T.;
RT "Unusual role of Tyr588 of neuronal nitric oxide synthase in controlling
RT substrate specificity and electron transfer.";
RL Biochem. Biophys. Res. Commun. 281:621-626(2001).
RN [6]
RP INTERACTION WITH CAPON AND RASD1.
RX PubMed=11086993; DOI=10.1016/s0896-6273(00)00095-7;
RA Fang M., Jaffrey S.R., Sawa A., Ye K., Luo X., Snyder S.H.;
RT "Dexras1: a G protein specifically coupled to neuronal nitric oxide
RT synthase via CAPON.";
RL Neuron 28:183-193(2000).
RN [7]
RP INTERACTION WITH CAPON AND SYN1.
RX PubMed=11867766; DOI=10.1073/pnas.261705799;
RA Jaffrey S.R., Benfenati F., Snowman A.M., Czernik A.J., Snyder S.H.;
RT "Neuronal nitric-oxide synthase localization mediated by a ternary complex
RT with synapsin and CAPON.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:3199-3204(2002).
RN [8]
RP INTERACTION WITH ZDHHC23.
RX PubMed=15105416; DOI=10.1074/jbc.m401471200;
RA Saitoh F., Tian Q.B., Okano A., Sakagami H., Kondo H., Suzuki T.;
RT "NIDD, a novel DHHC-containing protein, targets neuronal nitric-oxide
RT synthase (nNOS) to the synaptic membrane through a PDZ-dependent
RT interaction and regulates nNOS activity.";
RL J. Biol. Chem. 279:29461-29468(2004).
RN [9]
RP UBIQUITINATION.
RX PubMed=15466472; DOI=10.1074/jbc.m406926200;
RA Peng H.M., Morishima Y., Jenkins G.J., Dunbar A.Y., Lau M., Patterson C.,
RA Pratt W.B., Osawa Y.;
RT "Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-
RT dependent E3 ligase.";
RL J. Biol. Chem. 279:52970-52977(2004).
RN [10]
RP INTERACTION WITH NOSIP, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
RX PubMed=15548660; DOI=10.1523/jneurosci.2265-04.2004;
RA Dreyer J., Schleicher M., Tappe A., Schilling K., Kuner T.,
RA Kusumawidijaja G., Mueller-Esterl W., Oess S., Kuner R.;
RT "Nitric oxide synthase (NOS)-interacting protein interacts with neuronal
RT NOS and regulates its distribution and activity.";
RL J. Neurosci. 24:10454-10465(2004).
RN [11]
RP INTERACTION WITH VAC14, AND DOMAIN.
RX PubMed=17161399; DOI=10.1016/j.febslet.2006.11.061;
RA Lemaire J.F., McPherson P.S.;
RT "Binding of Vac14 to neuronal nitric oxide synthase: Characterisation of a
RT new internal PDZ-recognition motif.";
RL FEBS Lett. 580:6948-6954(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-847 AND SER-858, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [13]
RP INTERACTION WITH DLG4.
RX PubMed=23300088; DOI=10.1074/jbc.m112.412478;
RA Akama K.T., Thompson L.I., Milner T.A., McEwen B.S.;
RT "Post-synaptic density-95 (PSD-95) binding capacity of G-protein-coupled
RT receptor 30 (GPR30), an estrogen receptor that can be identified in
RT hippocampal dendritic spines.";
RL J. Biol. Chem. 288:6438-6450(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 14-125.
RX PubMed=10221915; DOI=10.1126/science.284.5415.812;
RA Hillier B.J., Christopherson K.S., Prehoda K.E., Bredt D.S., Lim W.A.;
RT "Unexpected modes of PDZ domain scaffolding revealed by structure of nNOS-
RT syntrophin complex.";
RL Science 284:812-815(1999).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 963-1397.
RX PubMed=11473123; DOI=10.1074/jbc.m105503200;
RA Zhang J., Martasek P., Paschke R., Shea T., Masters B.S.S., Kim J.-J.P.;
RT "Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-
RT oxide synthase. Comparisons with nadph-cytochrome p450 oxidoreductase.";
RL J. Biol. Chem. 276:37506-37513(2001).
CC -!- FUNCTION: Produces nitric oxide (NO) which is a messenger molecule with
CC diverse functions throughout the body. In the brain and peripheral
CC nervous system, NO displays many properties of a neurotransmitter.
CC Inhibitory transmitter for non-adrenergic and non-cholinergic nerves in
CC the colorectum. Probably has nitrosylase activity and mediates cysteine
CC S-nitrosylation of cytoplasmic target proteins such SRR. Inhibitory
CC transmitter for non-adrenergic and non-cholinergic nerves in the
CC colorectum.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + 2 L-arginine + 3 NADPH + 4 O2 = 4 H2O + 2 L-citrulline
CC + 3 NADP(+) + 2 nitric oxide; Xref=Rhea:RHEA:19897,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16480, ChEBI:CHEBI:32682, ChEBI:CHEBI:57743,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.39;
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC Note=Binds 1 FMN. {ECO:0000250};
CC -!- COFACTOR:
CC Name=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin;
CC Xref=ChEBI:CHEBI:59560; Evidence={ECO:0000250};
CC Note=Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the
CC enzyme. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Stimulated by calcium/calmodulin. Inhibited by n-
CC Nos-inhibiting protein (PIN) which may prevent the dimerization of the
CC protein (By similarity). Inhibited by NOSIP. {ECO:0000250,
CC ECO:0000269|PubMed:15548660}.
CC -!- SUBUNIT: Homodimer. Interacts with DLG4; the interaction possibly being
CC prevented by the association between NOS1 and CAPON (PubMed:23300088).
CC Forms a ternary complex with CAPON and RASD1 (PubMed:11086993). Forms a
CC ternary complex with CAPON and SYN1 (PubMed:11867766). Interacts with
CC ZDHHC23 (PubMed:15105416). Interacts with NOSIP; which may impair its
CC synaptic location (PubMed:15548660). Interacts with HTR4 (By
CC similarity). Interacts with SLC6A4. Interacts with VAC14
CC (PubMed:17161399). Interacts (via N-terminal domain) with DLG4 (via N-
CC terminal tandem pair of PDZ domains) (By similarity). Interacts with
CC SLC6A4 (By similarity). Forms a complex with ASL, ASS1 and SLC7A1; the
CC complex regulates cell-autonomous L-arginine synthesis and citrulline
CC recycling while channeling extracellular L-arginine to nitric oxide
CC synthesis pathway (By similarity). {ECO:0000250|UniProtKB:Q9Z0J4,
CC ECO:0000269|PubMed:11086993, ECO:0000269|PubMed:11867766,
CC ECO:0000269|PubMed:15105416, ECO:0000269|PubMed:15548660,
CC ECO:0000269|PubMed:17161399, ECO:0000269|PubMed:23300088}.
CC -!- INTERACTION:
CC P29476; O08701: Arg2; NbExp=2; IntAct=EBI-349460, EBI-15573788;
CC P29476; P62157: CALM; Xeno; NbExp=2; IntAct=EBI-349460, EBI-397403;
CC -!- SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Cell projection, dendritic
CC spine {ECO:0000250}. Note=In skeletal muscle, it is localized beneath
CC the sarcolemma of fast-twitch muscle fiber by associating with the
CC dystrophin glycoprotein complex (By similarity). In neurons, enriched
CC in dendritic spines. {ECO:0000250, ECO:0000269|PubMed:15548660}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=N-NOS-1;
CC IsoId=P29476-1; Sequence=Displayed;
CC Name=N-NOS-2;
CC IsoId=P29476-2; Sequence=VSP_003580;
CC Name=PNNOS;
CC IsoId=P29476-3; Sequence=VSP_003581;
CC -!- TISSUE SPECIFICITY: Isoform N-NOS-1 is expressed in brain and
CC colorectum. Found in the Auerbach's plexus of the enteric nervous
CC system. Isoform PNNOS is expressed in the penis, urethra, prostate, and
CC skeletal muscle, and coexists with the cerebellar nnos in the pelvic
CC plexus, bladder and liver, and is detectable in the cerebellum.
CC {ECO:0000269|PubMed:7520037}.
CC -!- DOMAIN: The PDZ domain in the N-terminal part of the neuronal isoform
CC participates in protein-protein interaction, and is responsible for
CC targeting nNos to synaptic membranes in muscles (By similarity).
CC Mediates interaction with VAC14. {ECO:0000250,
CC ECO:0000269|PubMed:17161399}.
CC -!- PTM: Ubiquitinated; mediated by STUB1/CHIP in the presence of Hsp70 and
CC Hsp40 (in vitro). {ECO:0000269|PubMed:15466472}.
CC -!- SIMILARITY: Belongs to the NOS family. {ECO:0000305}.
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DR EMBL; X59949; CAA42574.1; -; mRNA.
DR EMBL; U67309; AAC52782.1; -; mRNA.
DR PIR; S16233; S16233.
DR RefSeq; NP_434686.1; NM_052799.1.
DR PDB; 1B8Q; NMR; -; A=11-133.
DR PDB; 1CMI; X-ray; 2.50 A; C/D=225-237.
DR PDB; 1F20; X-ray; 1.90 A; A=963-1397.
DR PDB; 1K2R; X-ray; 2.15 A; A/B=299-717.
DR PDB; 1K2S; X-ray; 2.55 A; A/B=299-717.
DR PDB; 1K2T; X-ray; 2.20 A; A/B=299-717.
DR PDB; 1K2U; X-ray; 2.20 A; A/B=299-717.
DR PDB; 1LZX; X-ray; 2.00 A; A/B=299-717.
DR PDB; 1LZZ; X-ray; 2.05 A; A/B=299-717.
DR PDB; 1M00; X-ray; 2.05 A; A/B=299-717.
DR PDB; 1MMV; X-ray; 2.00 A; A/B=299-717.
DR PDB; 1MMW; X-ray; 2.00 A; A/B=299-717.
DR PDB; 1OM4; X-ray; 1.75 A; A/B=297-718.
DR PDB; 1OM5; X-ray; 2.30 A; A/B=297-717.
DR PDB; 1P6H; X-ray; 1.98 A; A/B=297-717.
DR PDB; 1P6I; X-ray; 1.90 A; A/B=297-717.
DR PDB; 1P6J; X-ray; 2.00 A; A/B=297-717.
DR PDB; 1P6K; X-ray; 1.78 A; A/B=297-717.
DR PDB; 1QAU; X-ray; 1.25 A; A=14-125.
DR PDB; 1QAV; X-ray; 1.90 A; B=12-126.
DR PDB; 1QW6; X-ray; 2.10 A; A=298-716.
DR PDB; 1QWC; X-ray; 2.30 A; A=298-716.
DR PDB; 1RS6; X-ray; 1.95 A; A/B=297-717.
DR PDB; 1RS7; X-ray; 1.95 A; A/B=297-717.
DR PDB; 1TLL; X-ray; 2.30 A; A/B=742-1429.
DR PDB; 1VAG; X-ray; 2.00 A; A=298-716.
DR PDB; 1ZVI; X-ray; 2.00 A; A=298-716.
DR PDB; 1ZVL; X-ray; 2.50 A; A/B=298-716.
DR PDB; 1ZZQ; X-ray; 1.90 A; A/B=299-718.
DR PDB; 1ZZR; X-ray; 2.05 A; A/B=299-718.
DR PDB; 1ZZU; X-ray; 1.90 A; A/B=299-718.
DR PDB; 2G6H; X-ray; 2.00 A; A/B=299-718.
DR PDB; 2G6I; X-ray; 1.90 A; A/B=299-718.
DR PDB; 2G6J; X-ray; 2.30 A; A/B=299-718.
DR PDB; 2G6K; X-ray; 2.00 A; A/B=299-718.
DR PDB; 2G6L; X-ray; 2.05 A; A/B=299-718.
DR PDB; 2G6M; X-ray; 1.85 A; A/B=299-718.
DR PDB; 2G6N; X-ray; 1.90 A; A/B=299-718.
DR PDB; 2HX3; X-ray; 2.00 A; A/B=297-718.
DR PDB; 2HX4; X-ray; 2.15 A; A/B=297-718.
DR PDB; 3B3M; X-ray; 1.95 A; A/B=297-718.
DR PDB; 3B3N; X-ray; 1.98 A; A/B=297-718.
DR PDB; 3B3O; X-ray; 2.05 A; A/B=297-718.
DR PDB; 3B3P; X-ray; 2.45 A; A/B=297-718.
DR PDB; 3DQR; X-ray; 2.40 A; A/B=297-718.
DR PDB; 3FC5; X-ray; 2.59 A; A/B=297-718.
DR PDB; 3HSN; X-ray; 1.91 A; A/B=297-718.
DR PDB; 3HSO; X-ray; 2.02 A; A/B=297-718.
DR PDB; 3HSP; X-ray; 2.20 A; A/B=297-718.
DR PDB; 3JT3; X-ray; 2.15 A; A/B=297-718.
DR PDB; 3JT4; X-ray; 1.80 A; A/B=297-718.
DR PDB; 3JT5; X-ray; 2.10 A; A/B=297-718.
DR PDB; 3JT6; X-ray; 2.20 A; A/B=297-718.
DR PDB; 3JT7; X-ray; 2.10 A; A/B=297-718.
DR PDB; 3JT8; X-ray; 1.95 A; A/B=297-718.
DR PDB; 3JT9; X-ray; 2.10 A; A/B=297-718.
DR PDB; 3JTA; X-ray; 2.18 A; A/B=297-718.
DR PDB; 3JWS; X-ray; 1.95 A; A/B=297-718.
DR PDB; 3JWT; X-ray; 2.01 A; A/B=297-718.
DR PDB; 3JWU; X-ray; 1.93 A; A/B=297-718.
DR PDB; 3JWV; X-ray; 1.98 A; A/B=297-718.
DR PDB; 3JX0; X-ray; 2.20 A; A/B=297-718.
DR PDB; 3JX1; X-ray; 2.00 A; A/B=297-718.
DR PDB; 3JX2; X-ray; 2.10 A; A/B=297-718.
DR PDB; 3JX3; X-ray; 1.95 A; A/B=297-718.
DR PDB; 3JX4; X-ray; 2.26 A; A/B=297-718.
DR PDB; 3JX5; X-ray; 2.15 A; A/B=297-718.
DR PDB; 3JX6; X-ray; 2.35 A; A/B=297-718.
DR PDB; 3N2R; X-ray; 1.90 A; A/B=297-718.
DR PDB; 3N5V; X-ray; 2.30 A; A/B=297-718.
DR PDB; 3N5W; X-ray; 1.73 A; A/B=297-718.
DR PDB; 3N5X; X-ray; 1.80 A; A/B=297-718.
DR PDB; 3N5Y; X-ray; 2.05 A; A/B=297-718.
DR PDB; 3N5Z; X-ray; 2.18 A; A/B=297-718.
DR PDB; 3N60; X-ray; 1.98 A; A/B=297-718.
DR PDB; 3N61; X-ray; 1.95 A; A/B=297-718.
DR PDB; 3N62; X-ray; 1.95 A; A/B=297-718.
DR PDB; 3N63; X-ray; 2.00 A; A/B=297-718.
DR PDB; 3N64; X-ray; 1.95 A; A/B=297-718.
DR PDB; 3N65; X-ray; 1.80 A; A/B=297-718.
DR PDB; 3N66; X-ray; 1.78 A; A/B=297-718.
DR PDB; 3N67; X-ray; 2.09 A; A/B=298-711.
DR PDB; 3N68; X-ray; 2.53 A; A/B=298-711.
DR PDB; 3N69; X-ray; 2.65 A; A/B=298-711.
DR PDB; 3N6A; X-ray; 2.49 A; A/B=298-711.
DR PDB; 3N6B; X-ray; 3.10 A; A/B=298-711.
DR PDB; 3N6C; X-ray; 3.06 A; A/B=298-711.
DR PDB; 3N6D; X-ray; 3.05 A; A/B=298-711.
DR PDB; 3N6E; X-ray; 2.20 A; A/B=298-711.
DR PDB; 3N6F; X-ray; 2.18 A; A/B=298-711.
DR PDB; 3N6G; X-ray; 2.21 A; A/B=298-711.
DR PDB; 3NLJ; X-ray; 2.20 A; A/B=297-718.
DR PDB; 3NLK; X-ray; 2.02 A; A/B=297-718.
DR PDB; 3NLM; X-ray; 1.85 A; A/B=297-718.
DR PDB; 3NLN; X-ray; 2.00 A; A/B=297-718.
DR PDB; 3NLO; X-ray; 2.30 A; A/B=297-718.
DR PDB; 3NLP; X-ray; 2.02 A; A/B=297-718.
DR PDB; 3NLQ; X-ray; 2.15 A; A/B=297-718.
DR PDB; 3NLR; X-ray; 2.10 A; A/B=297-718.
DR PDB; 3NLV; X-ray; 2.10 A; A/B=297-718.
DR PDB; 3NLW; X-ray; 2.10 A; A/B=297-718.
DR PDB; 3NLX; X-ray; 1.87 A; A/B=297-718.
DR PDB; 3NLY; X-ray; 1.99 A; A/B=297-718.
DR PDB; 3NLZ; X-ray; 1.92 A; A/B=297-718.
DR PDB; 3NM0; X-ray; 1.81 A; A/B=297-718.
DR PDB; 3NNY; X-ray; 2.10 A; A/B=297-718.
DR PDB; 3NNZ; X-ray; 1.97 A; A/B=297-718.
DR PDB; 3PNE; X-ray; 1.97 A; A/B=297-718.
DR PDB; 3PNF; X-ray; 1.94 A; A/B=297-718.
DR PDB; 3PNG; X-ray; 1.88 A; A/B=297-718.
DR PDB; 3Q99; X-ray; 2.15 A; A/B=297-718.
DR PDB; 3Q9A; X-ray; 2.24 A; A/B=297-718.
DR PDB; 3RQJ; X-ray; 1.84 A; A/B=297-718.
DR PDB; 3RQK; X-ray; 2.21 A; A/B=297-718.
DR PDB; 3RQL; X-ray; 1.93 A; A/B=297-718.
DR PDB; 3RQM; X-ray; 1.95 A; A/B=297-718.
DR PDB; 3RQN; X-ray; 1.95 A; A/B=297-718.
DR PDB; 3SVP; X-ray; 2.05 A; A/B=297-718.
DR PDB; 3SVQ; X-ray; 2.18 A; A/B=297-718.
DR PDB; 3TYL; X-ray; 1.90 A; A/B=297-718.
DR PDB; 3TYM; X-ray; 2.00 A; A/B=297-718.
DR PDB; 3TYN; X-ray; 1.97 A; A/B=297-718.
DR PDB; 3TYO; X-ray; 1.93 A; A/B=297-718.
DR PDB; 3UFO; X-ray; 2.17 A; A/B=297-718.
DR PDB; 3UFP; X-ray; 2.10 A; A/B=297-718.
DR PDB; 3UFQ; X-ray; 2.06 A; A/B=297-718.
DR PDB; 3UFR; X-ray; 2.10 A; A/B=297-718.
DR PDB; 3UFS; X-ray; 1.97 A; A/B=297-718.
DR PDB; 3UFT; X-ray; 2.08 A; A/B=297-718.
DR PDB; 3UFU; X-ray; 1.89 A; A/B=297-718.
DR PDB; 3UFV; X-ray; 2.08 A; A/B=297-718.
DR PDB; 3UFW; X-ray; 2.00 A; A/B=297-718.
DR PDB; 4C39; X-ray; 1.98 A; A/B=297-718.
DR PDB; 4CAM; X-ray; 1.83 A; A/B=297-718.
DR PDB; 4CAN; X-ray; 1.91 A; A/B=297-718.
DR PDB; 4CAO; X-ray; 1.98 A; A/B=297-718.
DR PDB; 4CAP; X-ray; 2.06 A; A/B=297-718.
DR PDB; 4CAQ; X-ray; 1.95 A; A/B=297-718.
DR PDB; 4CDT; X-ray; 2.00 A; A/B=297-718.
DR PDB; 4CTP; X-ray; 2.05 A; A/B=297-718.
DR PDB; 4CTQ; X-ray; 2.00 A; A/B=297-718.
DR PDB; 4CTR; X-ray; 2.20 A; A/B=297-718.
DR PDB; 4CTT; X-ray; 2.30 A; A/B=297-718.
DR PDB; 4CTU; X-ray; 2.16 A; A/B=297-718.
DR PDB; 4CTV; X-ray; 1.78 A; A/B=297-718.
DR PDB; 4CTW; X-ray; 1.90 A; A/B=297-718.
DR PDB; 4CTX; X-ray; 1.82 A; A/B=297-718.
DR PDB; 4CX3; X-ray; 1.97 A; A/B=297-718.
DR PDB; 4CX4; X-ray; 1.98 A; A/B=297-718.
DR PDB; 4CX5; X-ray; 1.80 A; A/B=297-718.
DR PDB; 4CX6; X-ray; 1.90 A; A/B=297-718.
DR PDB; 4D2Y; X-ray; 1.98 A; A/B=297-718.
DR PDB; 4D2Z; X-ray; 1.89 A; A/B=297-718.
DR PDB; 4D30; X-ray; 1.96 A; A/B=297-718.
DR PDB; 4D31; X-ray; 1.95 A; A/B=297-718.
DR PDB; 4D32; X-ray; 2.10 A; A/B=297-718.
DR PDB; 4D3B; X-ray; 1.80 A; A/B=297-718.
DR PDB; 4D7O; X-ray; 1.78 A; A/B=297-718.
DR PDB; 4EUX; X-ray; 2.14 A; A/B=297-718.
DR PDB; 4FVW; X-ray; 1.81 A; A/B=297-718.
DR PDB; 4FVX; X-ray; 2.00 A; A/B=297-718.
DR PDB; 4FVY; X-ray; 1.70 A; A/B=297-718.
DR PDB; 4FVZ; X-ray; 1.99 A; A/B=297-718.
DR PDB; 4FW0; X-ray; 1.95 A; A/B=297-718.
DR PDB; 4GQE; X-ray; 1.80 A; A/B=297-718.
DR PDB; 4HOP; X-ray; 2.29 A; B/D/F=4-126.
DR PDB; 4IMS; X-ray; 2.15 A; A/B=297-718.
DR PDB; 4IMT; X-ray; 2.20 A; A/B=297-718.
DR PDB; 4IMU; X-ray; 2.03 A; A/B=297-718.
DR PDB; 4IMW; X-ray; 2.20 A; A/B=297-718.
DR PDB; 4JSE; X-ray; 1.97 A; A/B=297-718.
DR PDB; 4JSF; X-ray; 2.05 A; A/B=297-718.
DR PDB; 4JSG; X-ray; 1.94 A; A/B=297-718.
DR PDB; 4JSH; X-ray; 2.35 A; A/B=297-718.
DR PDB; 4JSI; X-ray; 2.09 A; A/B=297-718.
DR PDB; 4JSJ; X-ray; 1.92 A; A/B=297-718.
DR PDB; 4K5D; X-ray; 2.10 A; A/B=297-718.
DR PDB; 4K5E; X-ray; 1.89 A; A/B=297-718.
DR PDB; 4K5F; X-ray; 2.20 A; A/B=297-718.
DR PDB; 4K5G; X-ray; 1.85 A; A/B=297-718.
DR PDB; 4KCH; X-ray; 2.15 A; A/B=297-718.
DR PDB; 4KCI; X-ray; 2.27 A; A/B=297-718.
DR PDB; 4KCJ; X-ray; 2.05 A; A/B=297-718.
DR PDB; 4KCK; X-ray; 2.10 A; A/B=297-718.
DR PDB; 4KCL; X-ray; 1.93 A; A/B=297-718.
DR PDB; 4KCM; X-ray; 2.07 A; A/B=297-718.
DR PDB; 4KCN; X-ray; 1.85 A; A/B=297-718.
DR PDB; 4KCO; X-ray; 1.86 A; A/B=297-718.
DR PDB; 4LUX; X-ray; 1.86 A; A/B=297-718.
DR PDB; 4UGZ; X-ray; 2.08 A; A/B=297-718.
DR PDB; 4UH0; X-ray; 2.04 A; A/B=297-718.
DR PDB; 4UH1; X-ray; 1.80 A; A/B=297-718.
DR PDB; 4UH2; X-ray; 1.99 A; A/B=297-718.
DR PDB; 4UH3; X-ray; 2.03 A; A/B=297-718.
DR PDB; 4UH4; X-ray; 1.95 A; A/B=297-718.
DR PDB; 4UPM; X-ray; 1.90 A; A/B=297-718.
DR PDB; 4UPN; X-ray; 2.09 A; A/B=297-718.
DR PDB; 4UPO; X-ray; 1.95 A; A/B=297-718.
DR PDB; 4UPP; X-ray; 1.91 A; A/B=297-718.
DR PDB; 4V3V; X-ray; 2.06 A; A/B=297-718.
DR PDB; 4V3W; X-ray; 2.13 A; A/B=297-718.
DR PDB; 4V3X; X-ray; 1.99 A; A/B=297-718.
DR PDB; 4V3Y; X-ray; 1.96 A; A/B=297-718.
DR PDB; 4V3Z; X-ray; 2.05 A; A/B=297-718.
DR PDB; 5AD4; X-ray; 1.98 A; A/B=297-718.
DR PDB; 5AD5; X-ray; 1.90 A; A/B=297-718.
DR PDB; 5AD6; X-ray; 2.00 A; A/B=297-718.
DR PDB; 5AD7; X-ray; 1.95 A; A/B=297-718.
DR PDB; 5AD8; X-ray; 1.91 A; A/B=297-718.
DR PDB; 5AD9; X-ray; 2.30 A; A/B=297-718.
DR PDB; 5ADA; X-ray; 1.98 A; A/B=297-718.
DR PDB; 5ADB; X-ray; 2.05 A; A/B=297-718.
DR PDB; 5ADC; X-ray; 2.10 A; A/B=297-718.
DR PDB; 5ADD; X-ray; 2.10 A; A/B=297-718.
DR PDB; 5ADE; X-ray; 2.10 A; A/B=297-718.
DR PDB; 5AGK; X-ray; 2.00 A; A/B=297-718.
DR PDB; 5AGL; X-ray; 1.94 A; A/B=297-718.
DR PDB; 5AGM; X-ray; 1.84 A; A/B=297-718.
DR PDB; 5AGN; X-ray; 1.95 A; A/B=297-718.
DR PDB; 5AGO; X-ray; 1.90 A; A/B=297-718.
DR PDB; 5AGP; X-ray; 2.10 A; A/B=297-718.
DR PDB; 5FVO; X-ray; 2.12 A; A=297-718.
DR PDB; 5FVP; X-ray; 2.10 A; A/B=297-718.
DR PDB; 5FVQ; X-ray; 1.95 A; A/B=297-718.
DR PDB; 5FVR; X-ray; 1.84 A; A/B=297-718.
DR PDB; 5FVS; X-ray; 1.95 A; A/B=297-718.
DR PDB; 5FVT; X-ray; 1.83 A; A/B=297-718.
DR PDB; 5FW0; X-ray; 1.80 A; A/B=297-718.
DR PDB; 5G0N; X-ray; 1.94 A; A/B=297-718.
DR PDB; 5G0O; X-ray; 1.85 A; A/B=297-718.
DR PDB; 5G0P; X-ray; 2.10 A; A/B=297-718.
DR PDB; 5UNR; X-ray; 1.95 A; A/B=297-718.
DR PDB; 5UNS; X-ray; 1.90 A; A/B=297-718.
DR PDB; 5UNT; X-ray; 2.05 A; A/B=297-718.
DR PDB; 5UNU; X-ray; 2.05 A; A/B=297-718.
DR PDB; 5UNV; X-ray; 2.00 A; A/B=297-718.
DR PDB; 5UNW; X-ray; 2.04 A; A/B=297-718.
DR PDB; 5UNX; X-ray; 2.03 A; A/B=297-718.
DR PDB; 5UNY; X-ray; 1.82 A; A/B=297-718.
DR PDB; 5UNZ; X-ray; 1.95 A; A/B=297-718.
DR PDB; 5UO0; X-ray; 1.97 A; A/B=297-718.
DR PDB; 5VUI; X-ray; 2.06 A; A/B=297-718.
DR PDB; 5VUJ; X-ray; 1.95 A; A/B=297-718.
DR PDB; 5VUK; X-ray; 1.95 A; A/B=297-718.
DR PDB; 5VUL; X-ray; 2.00 A; A/B=297-718.
DR PDB; 5VUM; X-ray; 2.10 A; A/B=297-718.
DR PDB; 5VUN; X-ray; 1.75 A; A/B=297-718.
DR PDB; 5VUO; X-ray; 1.80 A; A/B=297-718.
DR PDB; 5VUP; X-ray; 1.94 A; A/B=297-718.
DR PDB; 5VUQ; X-ray; 2.00 A; A/B=297-718.
DR PDB; 5VUR; X-ray; 1.97 A; A/B=297-718.
DR PDB; 5VUS; X-ray; 1.95 A; A/B=297-718.
DR PDB; 5VUT; X-ray; 2.00 A; A/B=297-718.
DR PDB; 5VUU; X-ray; 1.96 A; A/B=297-718.
DR PDB; 6AUQ; X-ray; 1.95 A; A/B=297-718.
DR PDB; 6AUR; X-ray; 1.75 A; A/B=297-718.
DR PDB; 6AUS; X-ray; 1.70 A; A/B=297-718.
DR PDB; 6AUT; X-ray; 1.90 A; A/B=297-718.
DR PDB; 6AUU; X-ray; 1.85 A; A/B=297-718.
DR PDB; 6AUV; X-ray; 1.76 A; A/B=297-718.
DR PDB; 6AUW; X-ray; 1.70 A; A/B=297-718.
DR PDB; 6AUX; X-ray; 1.90 A; A/B=297-718.
DR PDB; 6NGJ; X-ray; 1.76 A; A/B=297-718.
DR PDB; 6NGK; X-ray; 1.83 A; A/B=297-718.
DR PDB; 6NGL; X-ray; 1.83 A; A/B=297-718.
DR PDB; 6NGM; X-ray; 1.69 A; A/B=297-718.
DR PDB; 6NGN; X-ray; 1.90 A; A/B=297-718.
DR PDB; 6NGP; X-ray; 1.98 A; A/B=297-718.
DR PDB; 6NGQ; X-ray; 1.95 A; A/B=297-718.
DR PDB; 6NGR; X-ray; 1.82 A; A/B=297-718.
DR PDB; 6NGS; X-ray; 1.90 A; A/B=297-718.
DR PDB; 6NGT; X-ray; 1.94 A; A/B=297-718.
DR PDB; 6NGU; X-ray; 2.00 A; A/B=297-718.
DR PDB; 6NGV; X-ray; 1.83 A; A/B=297-718.
DR PDB; 6NGW; X-ray; 1.86 A; A/B=297-718.
DR PDB; 6NGX; X-ray; 1.77 A; A/B=297-718.
DR PDB; 6NGY; X-ray; 1.93 A; A/B=297-718.
DR PDB; 6NGZ; X-ray; 2.00 A; A/B=297-718.
DR PDB; 6NH0; X-ray; 1.90 A; A/B=297-718.
DR PDB; 6NHD; X-ray; 2.10 A; A/B=297-718.
DR PDB; 6NHE; X-ray; 2.00 A; A/B=297-718.
DR PDB; 6PMV; X-ray; 1.80 A; A/B=297-718.
DR PDB; 6PMW; X-ray; 1.75 A; A/B=297-718.
DR PDB; 6PMX; X-ray; 2.05 A; A/B=297-718.
DR PDB; 6PMY; X-ray; 1.95 A; A/B=297-718.
DR PDB; 6PMZ; X-ray; 2.10 A; A/B=297-718.
DR PDB; 6PN0; X-ray; 2.23 A; A/B=297-718.
DR PDB; 6PN1; X-ray; 2.20 A; A/B=297-718.
DR PDB; 6PN2; X-ray; 1.88 A; A/B=297-718.
DR PDB; 6PN3; X-ray; 1.80 A; A/B=297-718.
DR PDB; 6PN4; X-ray; 1.90 A; A/B=297-718.
DR PDB; 6PN5; X-ray; 1.70 A; A/B=297-718.
DR PDB; 6PN6; X-ray; 1.84 A; A/B=297-718.
DR PDB; 6PN7; X-ray; 1.88 A; A/B=297-718.
DR PDB; 6PN8; X-ray; 1.84 A; A/B=297-718.
DR PDB; 6PN9; X-ray; 1.84 A; A/B=297-718.
DR PDBsum; 1B8Q; -.
DR PDBsum; 1CMI; -.
DR PDBsum; 1F20; -.
DR PDBsum; 1K2R; -.
DR PDBsum; 1K2S; -.
DR PDBsum; 1K2T; -.
DR PDBsum; 1K2U; -.
DR PDBsum; 1LZX; -.
DR PDBsum; 1LZZ; -.
DR PDBsum; 1M00; -.
DR PDBsum; 1MMV; -.
DR PDBsum; 1MMW; -.
DR PDBsum; 1OM4; -.
DR PDBsum; 1OM5; -.
DR PDBsum; 1P6H; -.
DR PDBsum; 1P6I; -.
DR PDBsum; 1P6J; -.
DR PDBsum; 1P6K; -.
DR PDBsum; 1QAU; -.
DR PDBsum; 1QAV; -.
DR PDBsum; 1QW6; -.
DR PDBsum; 1QWC; -.
DR PDBsum; 1RS6; -.
DR PDBsum; 1RS7; -.
DR PDBsum; 1TLL; -.
DR PDBsum; 1VAG; -.
DR PDBsum; 1ZVI; -.
DR PDBsum; 1ZVL; -.
DR PDBsum; 1ZZQ; -.
DR PDBsum; 1ZZR; -.
DR PDBsum; 1ZZU; -.
DR PDBsum; 2G6H; -.
DR PDBsum; 2G6I; -.
DR PDBsum; 2G6J; -.
DR PDBsum; 2G6K; -.
DR PDBsum; 2G6L; -.
DR PDBsum; 2G6M; -.
DR PDBsum; 2G6N; -.
DR PDBsum; 2HX3; -.
DR PDBsum; 2HX4; -.
DR PDBsum; 3B3M; -.
DR PDBsum; 3B3N; -.
DR PDBsum; 3B3O; -.
DR PDBsum; 3B3P; -.
DR PDBsum; 3DQR; -.
DR PDBsum; 3FC5; -.
DR PDBsum; 3HSN; -.
DR PDBsum; 3HSO; -.
DR PDBsum; 3HSP; -.
DR PDBsum; 3JT3; -.
DR PDBsum; 3JT4; -.
DR PDBsum; 3JT5; -.
DR PDBsum; 3JT6; -.
DR PDBsum; 3JT7; -.
DR PDBsum; 3JT8; -.
DR PDBsum; 3JT9; -.
DR PDBsum; 3JTA; -.
DR PDBsum; 3JWS; -.
DR PDBsum; 3JWT; -.
DR PDBsum; 3JWU; -.
DR PDBsum; 3JWV; -.
DR PDBsum; 3JX0; -.
DR PDBsum; 3JX1; -.
DR PDBsum; 3JX2; -.
DR PDBsum; 3JX3; -.
DR PDBsum; 3JX4; -.
DR PDBsum; 3JX5; -.
DR PDBsum; 3JX6; -.
DR PDBsum; 3N2R; -.
DR PDBsum; 3N5V; -.
DR PDBsum; 3N5W; -.
DR PDBsum; 3N5X; -.
DR PDBsum; 3N5Y; -.
DR PDBsum; 3N5Z; -.
DR PDBsum; 3N60; -.
DR PDBsum; 3N61; -.
DR PDBsum; 3N62; -.
DR PDBsum; 3N63; -.
DR PDBsum; 3N64; -.
DR PDBsum; 3N65; -.
DR PDBsum; 3N66; -.
DR PDBsum; 3N67; -.
DR PDBsum; 3N68; -.
DR PDBsum; 3N69; -.
DR PDBsum; 3N6A; -.
DR PDBsum; 3N6B; -.
DR PDBsum; 3N6C; -.
DR PDBsum; 3N6D; -.
DR PDBsum; 3N6E; -.
DR PDBsum; 3N6F; -.
DR PDBsum; 3N6G; -.
DR PDBsum; 3NLJ; -.
DR PDBsum; 3NLK; -.
DR PDBsum; 3NLM; -.
DR PDBsum; 3NLN; -.
DR PDBsum; 3NLO; -.
DR PDBsum; 3NLP; -.
DR PDBsum; 3NLQ; -.
DR PDBsum; 3NLR; -.
DR PDBsum; 3NLV; -.
DR PDBsum; 3NLW; -.
DR PDBsum; 3NLX; -.
DR PDBsum; 3NLY; -.
DR PDBsum; 3NLZ; -.
DR PDBsum; 3NM0; -.
DR PDBsum; 3NNY; -.
DR PDBsum; 3NNZ; -.
DR PDBsum; 3PNE; -.
DR PDBsum; 3PNF; -.
DR PDBsum; 3PNG; -.
DR PDBsum; 3Q99; -.
DR PDBsum; 3Q9A; -.
DR PDBsum; 3RQJ; -.
DR PDBsum; 3RQK; -.
DR PDBsum; 3RQL; -.
DR PDBsum; 3RQM; -.
DR PDBsum; 3RQN; -.
DR PDBsum; 3SVP; -.
DR PDBsum; 3SVQ; -.
DR PDBsum; 3TYL; -.
DR PDBsum; 3TYM; -.
DR PDBsum; 3TYN; -.
DR PDBsum; 3TYO; -.
DR PDBsum; 3UFO; -.
DR PDBsum; 3UFP; -.
DR PDBsum; 3UFQ; -.
DR PDBsum; 3UFR; -.
DR PDBsum; 3UFS; -.
DR PDBsum; 3UFT; -.
DR PDBsum; 3UFU; -.
DR PDBsum; 3UFV; -.
DR PDBsum; 3UFW; -.
DR PDBsum; 4C39; -.
DR PDBsum; 4CAM; -.
DR PDBsum; 4CAN; -.
DR PDBsum; 4CAO; -.
DR PDBsum; 4CAP; -.
DR PDBsum; 4CAQ; -.
DR PDBsum; 4CDT; -.
DR PDBsum; 4CTP; -.
DR PDBsum; 4CTQ; -.
DR PDBsum; 4CTR; -.
DR PDBsum; 4CTT; -.
DR PDBsum; 4CTU; -.
DR PDBsum; 4CTV; -.
DR PDBsum; 4CTW; -.
DR PDBsum; 4CTX; -.
DR PDBsum; 4CX3; -.
DR PDBsum; 4CX4; -.
DR PDBsum; 4CX5; -.
DR PDBsum; 4CX6; -.
DR PDBsum; 4D2Y; -.
DR PDBsum; 4D2Z; -.
DR PDBsum; 4D30; -.
DR PDBsum; 4D31; -.
DR PDBsum; 4D32; -.
DR PDBsum; 4D3B; -.
DR PDBsum; 4D7O; -.
DR PDBsum; 4EUX; -.
DR PDBsum; 4FVW; -.
DR PDBsum; 4FVX; -.
DR PDBsum; 4FVY; -.
DR PDBsum; 4FVZ; -.
DR PDBsum; 4FW0; -.
DR PDBsum; 4GQE; -.
DR PDBsum; 4HOP; -.
DR PDBsum; 4IMS; -.
DR PDBsum; 4IMT; -.
DR PDBsum; 4IMU; -.
DR PDBsum; 4IMW; -.
DR PDBsum; 4JSE; -.
DR PDBsum; 4JSF; -.
DR PDBsum; 4JSG; -.
DR PDBsum; 4JSH; -.
DR PDBsum; 4JSI; -.
DR PDBsum; 4JSJ; -.
DR PDBsum; 4K5D; -.
DR PDBsum; 4K5E; -.
DR PDBsum; 4K5F; -.
DR PDBsum; 4K5G; -.
DR PDBsum; 4KCH; -.
DR PDBsum; 4KCI; -.
DR PDBsum; 4KCJ; -.
DR PDBsum; 4KCK; -.
DR PDBsum; 4KCL; -.
DR PDBsum; 4KCM; -.
DR PDBsum; 4KCN; -.
DR PDBsum; 4KCO; -.
DR PDBsum; 4LUX; -.
DR PDBsum; 4UGZ; -.
DR PDBsum; 4UH0; -.
DR PDBsum; 4UH1; -.
DR PDBsum; 4UH2; -.
DR PDBsum; 4UH3; -.
DR PDBsum; 4UH4; -.
DR PDBsum; 4UPM; -.
DR PDBsum; 4UPN; -.
DR PDBsum; 4UPO; -.
DR PDBsum; 4UPP; -.
DR PDBsum; 4V3V; -.
DR PDBsum; 4V3W; -.
DR PDBsum; 4V3X; -.
DR PDBsum; 4V3Y; -.
DR PDBsum; 4V3Z; -.
DR PDBsum; 5AD4; -.
DR PDBsum; 5AD5; -.
DR PDBsum; 5AD6; -.
DR PDBsum; 5AD7; -.
DR PDBsum; 5AD8; -.
DR PDBsum; 5AD9; -.
DR PDBsum; 5ADA; -.
DR PDBsum; 5ADB; -.
DR PDBsum; 5ADC; -.
DR PDBsum; 5ADD; -.
DR PDBsum; 5ADE; -.
DR PDBsum; 5AGK; -.
DR PDBsum; 5AGL; -.
DR PDBsum; 5AGM; -.
DR PDBsum; 5AGN; -.
DR PDBsum; 5AGO; -.
DR PDBsum; 5AGP; -.
DR PDBsum; 5FVO; -.
DR PDBsum; 5FVP; -.
DR PDBsum; 5FVQ; -.
DR PDBsum; 5FVR; -.
DR PDBsum; 5FVS; -.
DR PDBsum; 5FVT; -.
DR PDBsum; 5FW0; -.
DR PDBsum; 5G0N; -.
DR PDBsum; 5G0O; -.
DR PDBsum; 5G0P; -.
DR PDBsum; 5UNR; -.
DR PDBsum; 5UNS; -.
DR PDBsum; 5UNT; -.
DR PDBsum; 5UNU; -.
DR PDBsum; 5UNV; -.
DR PDBsum; 5UNW; -.
DR PDBsum; 5UNX; -.
DR PDBsum; 5UNY; -.
DR PDBsum; 5UNZ; -.
DR PDBsum; 5UO0; -.
DR PDBsum; 5VUI; -.
DR PDBsum; 5VUJ; -.
DR PDBsum; 5VUK; -.
DR PDBsum; 5VUL; -.
DR PDBsum; 5VUM; -.
DR PDBsum; 5VUN; -.
DR PDBsum; 5VUO; -.
DR PDBsum; 5VUP; -.
DR PDBsum; 5VUQ; -.
DR PDBsum; 5VUR; -.
DR PDBsum; 5VUS; -.
DR PDBsum; 5VUT; -.
DR PDBsum; 5VUU; -.
DR PDBsum; 6AUQ; -.
DR PDBsum; 6AUR; -.
DR PDBsum; 6AUS; -.
DR PDBsum; 6AUT; -.
DR PDBsum; 6AUU; -.
DR PDBsum; 6AUV; -.
DR PDBsum; 6AUW; -.
DR PDBsum; 6AUX; -.
DR PDBsum; 6NGJ; -.
DR PDBsum; 6NGK; -.
DR PDBsum; 6NGL; -.
DR PDBsum; 6NGM; -.
DR PDBsum; 6NGN; -.
DR PDBsum; 6NGP; -.
DR PDBsum; 6NGQ; -.
DR PDBsum; 6NGR; -.
DR PDBsum; 6NGS; -.
DR PDBsum; 6NGT; -.
DR PDBsum; 6NGU; -.
DR PDBsum; 6NGV; -.
DR PDBsum; 6NGW; -.
DR PDBsum; 6NGX; -.
DR PDBsum; 6NGY; -.
DR PDBsum; 6NGZ; -.
DR PDBsum; 6NH0; -.
DR PDBsum; 6NHD; -.
DR PDBsum; 6NHE; -.
DR PDBsum; 6PMV; -.
DR PDBsum; 6PMW; -.
DR PDBsum; 6PMX; -.
DR PDBsum; 6PMY; -.
DR PDBsum; 6PMZ; -.
DR PDBsum; 6PN0; -.
DR PDBsum; 6PN1; -.
DR PDBsum; 6PN2; -.
DR PDBsum; 6PN3; -.
DR PDBsum; 6PN4; -.
DR PDBsum; 6PN5; -.
DR PDBsum; 6PN6; -.
DR PDBsum; 6PN7; -.
DR PDBsum; 6PN8; -.
DR PDBsum; 6PN9; -.
DR AlphaFoldDB; P29476; -.
DR BMRB; P29476; -.
DR SMR; P29476; -.
DR BioGRID; 246738; 17.
DR CORUM; P29476; -.
DR DIP; DIP-33272N; -.
DR ELM; P29476; -.
DR IntAct; P29476; 9.
DR MINT; P29476; -.
DR STRING; 10116.ENSRNOP00000062735; -.
DR BindingDB; P29476; -.
DR ChEMBL; CHEMBL3048; -.
DR DrugCentral; P29476; -.
DR GuidetoPHARMACOLOGY; 1251; -.
DR CarbonylDB; P29476; -.
DR iPTMnet; P29476; -.
DR PhosphoSitePlus; P29476; -.
DR PaxDb; P29476; -.
DR PRIDE; P29476; -.
DR ABCD; P29476; 2 sequenced antibodies.
DR DNASU; 24598; -.
DR GeneID; 24598; -.
DR KEGG; rno:24598; -.
DR UCSC; RGD:3184; rat. [P29476-1]
DR CTD; 4842; -.
DR RGD; 3184; Nos1.
DR eggNOG; KOG1158; Eukaryota.
DR InParanoid; P29476; -.
DR PhylomeDB; P29476; -.
DR BRENDA; 1.14.13.39; 5301.
DR Reactome; R-RNO-1222556; ROS and RNS production in phagocytes.
DR Reactome; R-RNO-392154; Nitric oxide stimulates guanylate cyclase.
DR Reactome; R-RNO-5578775; Ion homeostasis.
DR SABIO-RK; P29476; -.
DR EvolutionaryTrace; P29476; -.
DR PRO; PR:P29476; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042582; C:azurophil granule; IDA:RGD.
DR GO; GO:0044305; C:calyx of Held; ISO:RGD.
DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005856; C:cytoskeleton; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; ISO:RGD.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:RGD.
DR GO; GO:0005739; C:mitochondrion; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0001917; C:photoreceptor inner segment; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:SynGO.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; IDA:SynGO.
DR GO; GO:0099091; C:postsynaptic specialization, intracellular component; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; IDA:BHF-UCL.
DR GO; GO:0042383; C:sarcolemma; IDA:BHF-UCL.
DR GO; GO:0016529; C:sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; ISO:RGD.
DR GO; GO:0030141; C:secretory granule; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0030315; C:T-tubule; ISO:RGD.
DR GO; GO:0012506; C:vesicle membrane; IDA:RGD.
DR GO; GO:0030018; C:Z disc; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0046870; F:cadmium ion binding; IDA:BHF-UCL.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:ARUK-UCL.
DR GO; GO:0005516; F:calmodulin binding; IDA:RGD.
DR GO; GO:0019899; F:enzyme binding; IPI:RGD.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:BHF-UCL.
DR GO; GO:0010181; F:FMN binding; IDA:BHF-UCL.
DR GO; GO:0020037; F:heme binding; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0050661; F:NADP binding; IDA:BHF-UCL.
DR GO; GO:0070402; F:NADPH binding; IDA:RGD.
DR GO; GO:0004517; F:nitric-oxide synthase activity; IDA:BHF-UCL.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0051219; F:phosphoprotein binding; IPI:CAFA.
DR GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
DR GO; GO:0017080; F:sodium channel regulator activity; IMP:BHF-UCL.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; IDA:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006527; P:arginine catabolic process; IDA:BHF-UCL.
DR GO; GO:0048148; P:behavioral response to cocaine; IMP:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; IMP:BHF-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:RGD.
DR GO; GO:0045184; P:establishment of protein localization; IDA:CAFA.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0033555; P:multicellular organismal response to stress; ISO:RGD.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0045822; P:negative regulation of heart contraction; IMP:RGD.
DR GO; GO:0061875; P:negative regulation of hepatic stellate cell contraction; IDA:RGD.
DR GO; GO:0051346; P:negative regulation of hydrolase activity; ISO:RGD.
DR GO; GO:0046676; P:negative regulation of insulin secretion; IMP:RGD.
DR GO; GO:0034760; P:negative regulation of iron ion transmembrane transport; IMP:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR GO; GO:0043267; P:negative regulation of potassium ion transport; ISO:RGD.
DR GO; GO:0051612; P:negative regulation of serotonin uptake; ISO:RGD.
DR GO; GO:0045906; P:negative regulation of vasoconstriction; IMP:RGD.
DR GO; GO:0006809; P:nitric oxide biosynthetic process; IDA:BHF-UCL.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; IMP:BHF-UCL.
DR GO; GO:0018119; P:peptidyl-cysteine S-nitrosylation; IDA:BHF-UCL.
DR GO; GO:0140196; P:positive regulation of adenylate cyclase-activating adrenergic receptor signaling pathway involved in heart process; ISO:RGD.
DR GO; GO:0031284; P:positive regulation of guanylate cyclase activity; IBA:GO_Central.
DR GO; GO:0035066; P:positive regulation of histone acetylation; ISO:RGD.
DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IMP:RGD.
DR GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:1902307; P:positive regulation of sodium ion transmembrane transport; IMP:BHF-UCL.
DR GO; GO:0098735; P:positive regulation of the force of heart contraction; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0008016; P:regulation of heart contraction; IMP:RGD.
DR GO; GO:0050767; P:regulation of neurogenesis; ISO:RGD.
DR GO; GO:0051930; P:regulation of sensory perception of pain; IMP:RGD.
DR GO; GO:0002028; P:regulation of sodium ion transport; ISO:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0043627; P:response to estrogen; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0009408; P:response to heat; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IBA:GO_Central.
DR GO; GO:0001666; P:response to hypoxia; IEP:BHF-UCL.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0035094; P:response to nicotine; IEP:RGD.
DR GO; GO:0071731; P:response to nitric oxide; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IMP:RGD.
DR GO; GO:0033197; P:response to vitamin E; IEP:RGD.
DR GO; GO:0098924; P:retrograde trans-synaptic signaling by nitric oxide; ISO:RGD.
DR GO; GO:0006941; P:striated muscle contraction; ISO:RGD.
DR GO; GO:0099163; P:synaptic signaling by nitric oxide; ISO:RGD.
DR GO; GO:0042311; P:vasodilation; IMP:RGD.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:RGD.
DR Gene3D; 1.20.990.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR Gene3D; 3.90.1230.10; -; 1.
DR Gene3D; 3.90.340.10; -; 1.
DR Gene3D; 3.90.440.10; -; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR044943; NOS_dom_1.
DR InterPro; IPR044940; NOS_dom_2.
DR InterPro; IPR044944; NOS_dom_3.
DR InterPro; IPR012144; NOS_euk.
DR InterPro; IPR004030; NOS_N.
DR InterPro; IPR036119; NOS_N_sf.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF02898; NO_synthase; 1.
DR Pfam; PF00595; PDZ; 1.
DR PIRSF; PIRSF000333; NOS; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52218; SSF52218; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF56512; SSF56512; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
DR PROSITE; PS60001; NOS; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calmodulin-binding; Cell membrane;
KW Cell projection; Direct protein sequencing; FAD; Flavoprotein; FMN; Heme;
KW Iron; Membrane; Metal-binding; NADP; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Synapse; Ubl conjugation.
FT CHAIN 1..1429
FT /note="Nitric oxide synthase, brain"
FT /id="PRO_0000170924"
FT DOMAIN 17..99
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 755..935
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT DOMAIN 990..1237
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT REGION 1..200
FT /note="Interaction with NOSIP"
FT /evidence="ECO:0000269|PubMed:15548660"
FT REGION 152..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..240
FT /note="PIN (nNOS-inhibiting protein) binding"
FT /evidence="ECO:0000250"
FT REGION 214..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..745
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000255"
FT COMPBIAS 230..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 334
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 415
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 478
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 587
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 588
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 592
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 677
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 678
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 691
FT /ligand="(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin"
FT /ligand_id="ChEBI:CHEBI:59560"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 706
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /evidence="ECO:0000250|UniProtKB:P29475"
FT BINDING 881..912
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00088"
FT BINDING 1027..1038
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1170..1180
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 1245..1263
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT BINDING 1343..1358
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0J4"
FT MOD_RES 847
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Z0J4"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 504..608
FT /note="Missing (in isoform N-NOS-2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003580"
FT VAR_SEQ 839
FT /note="K -> KYPEPLRFFPRKGPSLSHVDSEAHSLVAARDSQHR (in isoform
FT PNNOS)"
FT /evidence="ECO:0000303|PubMed:8806605"
FT /id="VSP_003581"
FT MUTAGEN 588
FT /note="Y->F: No decrease in activity."
FT /evidence="ECO:0000269|PubMed:11237702"
FT MUTAGEN 588
FT /note="Y->H: 50% decrease of activity."
FT /evidence="ECO:0000269|PubMed:11237702"
FT MUTAGEN 588
FT /note="Y->S: 30% decrease of activity."
FT /evidence="ECO:0000269|PubMed:11237702"
FT CONFLICT 269
FT /note="I -> V (in Ref. 2; AAC52782 and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 953
FT /note="P -> A (in Ref. 2; AAC52782 and 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="F -> S (in Ref. 2; AAC52782)"
FT /evidence="ECO:0000305"
FT CONFLICT 1311
FT /note="A -> V (in Ref. 2; AAC52782)"
FT /evidence="ECO:0000305"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:4HOP"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:1QAU"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1QAU"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:1QAU"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1QAU"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1QAU"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:1QAU"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:1B8Q"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1QAU"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1B8Q"
FT HELIX 77..86
FT /evidence="ECO:0007829|PDB:1QAU"
FT STRAND 89..98
FT /evidence="ECO:0007829|PDB:1QAU"
FT STRAND 103..111
FT /evidence="ECO:0007829|PDB:1QAU"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1QAV"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:1QAU"
FT STRAND 228..236
FT /evidence="ECO:0007829|PDB:1CMI"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:6NGM"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 311..314
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:3N5V"
FT HELIX 339..341
FT /evidence="ECO:0007829|PDB:6NGV"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:1VAG"
FT HELIX 351..368
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:1K2U"
FT HELIX 375..391
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 398..410
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 435..450
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 476..480
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 488..494
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 496..498
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 499..506
FT /evidence="ECO:0007829|PDB:6NGM"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 515..517
FT /evidence="ECO:0007829|PDB:3N5W"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:3N6D"
FT STRAND 532..534
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 538..540
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 577..580
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 590..594
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 596..599
FT /evidence="ECO:0007829|PDB:6NGM"
FT TURN 601..604
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 607..614
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 621..623
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 625..643
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 651..668
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 676..679
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 685..687
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 689..692
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 696..698
FT /evidence="ECO:0007829|PDB:3N6D"
FT STRAND 701..705
FT /evidence="ECO:0007829|PDB:6NGM"
FT HELIX 710..713
FT /evidence="ECO:0007829|PDB:6NGM"
FT STRAND 754..760
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 762..764
FT /evidence="ECO:0007829|PDB:1TLL"
FT HELIX 765..777
FT /evidence="ECO:0007829|PDB:1TLL"
FT TURN 778..780
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 781..787
FT /evidence="ECO:0007829|PDB:1TLL"
FT TURN 788..790
FT /evidence="ECO:0007829|PDB:1TLL"
FT HELIX 796..798
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 800..806
FT /evidence="ECO:0007829|PDB:1TLL"
FT TURN 810..812
FT /evidence="ECO:0007829|PDB:1TLL"
FT HELIX 816..818
FT /evidence="ECO:0007829|PDB:1TLL"
FT HELIX 819..828
FT /evidence="ECO:0007829|PDB:1TLL"
FT HELIX 841..844
FT /evidence="ECO:0007829|PDB:1TLL"
FT TURN 873..876
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 878..885
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 889..891
FT /evidence="ECO:0007829|PDB:1TLL"
FT HELIX 894..905
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 909..912
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 915..918
FT /evidence="ECO:0007829|PDB:1TLL"
FT TURN 919..922
FT /evidence="ECO:0007829|PDB:1TLL"
FT HELIX 923..942
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 946..948
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 961..963
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 968..973
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 980..988
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 993..1002
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1012..1018
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1023..1025
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1032..1035
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1041..1048
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1051..1053
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1061..1072
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1076..1081
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1090..1096
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1106..1113
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1119..1128
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1133..1142
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1146..1152
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1160..1166
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1173..1176
FT /evidence="ECO:0007829|PDB:1F20"
FT TURN 1181..1183
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1187..1193
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1196..1198
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1200..1202
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1206..1208
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1210..1215
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1223..1229
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1232..1234
FT /evidence="ECO:0007829|PDB:1TLL"
FT STRAND 1244..1247
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1250..1253
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1254..1270
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1277..1284
FT /evidence="ECO:0007829|PDB:1F20"
FT TURN 1286..1288
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1293..1301
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1304..1314
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1323..1330
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1332..1340
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1345..1350
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1352..1369
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1374..1386
FT /evidence="ECO:0007829|PDB:1F20"
FT STRAND 1390..1394
FT /evidence="ECO:0007829|PDB:1F20"
FT HELIX 1401..1411
FT /evidence="ECO:0007829|PDB:1TLL"
SQ SEQUENCE 1429 AA; 160559 MW; 7255C5AE165200F5 CRC64;
MEENTFGVQQ IQPNVISVRL FKRKVGGLGF LVKERVSKPP VIISDLIRGG AAEQSGLIQA
GDIILAVNDR PLVDLSYDSA LEVLRGIASE THVVLILRGP EGFTTHLETT FTGDGTPKTI
RVTQPLGPPT KAVDLSHQPS ASKDQSLAVD RVTGLGNGPQ HAQGHGQGAG SVSQANGVAI
DPTMKSTKAN LQDIGEHDEL LKEIEPVLSI LNSGSKATNR GGPAKAEMKD TGIQVDRDLD
GKSHKAPPLG GDNDRVFNDL WGKDNVPVIL NNPYSEKEQS PTSGKQSPTK NGSPSRCPRF
LKVKNWETDV VLTDTLHLKS TLETGCTEHI CMGSIMLPSQ HTRKPEDVRT KDQLFPLAKE
FLDQYYSSIK RFGSKAHMDR LEEVNKEIES TSTYQLKDTE LIYGAKHAWR NASRCVGRIQ
WSKLQVFDAR DCTTAHGMFN YICNHVKYAT NKGNLRSAIT IFPQRTDGKH DFRVWNSQLI
RYAGYKQPDG STLGDPANVQ FTEICIQQGW KAPRGRFDVL PLLLQANGND PELFQIPPEL
VLEVPIRHPK FDWFKDLGLK WYGLPAVSNM LLEIGGLEFS ACPFSGWYMG TEIGVRDYCD
NSRYNILEEV AKKMDLDMRK TSSLWKDQAL VEINIAVLYS FQSDKVTIVD HHSATESFIK
HMENEYRCRG GCPADWVWIV PPMSGSITPV FHQEMLNYRL TPSFEYQPDP WNTHVWKGTN
GTPTKRRAIG FKKLAEAVKF SAKLMGQAMA KRVKATILYA TETGKSQAYA KTLCEIFKHA
FDAKAMSMEE YDIVHLEHEA LVLVVTSTFG NGDPPENGEK FGCALMEMRH PNSVQEERKS
YKVRFNSVSS YSDSRKSSGD GPDLRDNFES TGPLANVRFS VFGLGSRAYP HFCAFGHAVD
TLLEELGGER ILKMREGDEL CGQEEAFRTW AKKVFKAACD VFCVGDDVNI EKPNNSLISN
DRSWKRNKFR LTYVAEAPDL TQGLSNVHKK RVSAARLLSR QNLQSPKFSR STIFVRLHTN
GNQELQYQPG DHLGVFPGNH EDLVNALIER LEDAPPANHV VKVEMLEERN TALGVISNWK
DESRLPPCTI FQAFKYYLDI TTPPTPLQLQ QFASLATNEK EKQRLLVLSK GLQEYEEWKW
GKNPTMVEVL EEFPSIQMPA TLLLTQLSLL QPRYYSISSS PDMYPDEVHL TVAIVSYHTR
DGEGPVHHGV CSSWLNRIQA DDVVPCFVRG APSFHLPRNP QVPCILVGPG TGIAPFRSFW
QQRQFDIQHK GMNPCPMVLV FGCRQSKIDH IYREETLQAK NKGVFRELYT AYSREPDRPK
KYVQDVLQEQ LAESVYRALK EQGGHIYVCG DVTMAADVLK AIQRIMTQQG KLSEEDAGVF
ISRLRDDNRY HEDIFGVTLR TYEVTNRLRS ESIAFIEESK KDADEVFSS
