{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_H_R1_R2.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_D.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_EDC_R1_R2_R3_R4.xlsx","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_M_R1_R2.xlsx"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_EDC_R4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_M_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_D.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_EDC_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_H_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_EDC_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_H_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_M_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_EDC_R2.raw"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_M_R2.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_H_R2.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_EDC_R1_R2_R3_R4.mgf.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_D.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_H_R1.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Zou_Rappsilber_JP_Mis18_BP1_SDA_M_R1.mgf"],"Fasta":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Mis18.fasta","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2024/05/PXD047345/Mis18_BP1.fasta"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["juri.rappsilber@ed.ac.uk"],"submitter":["Juan Zou"],"technology_type":["Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"software":[""],"submitter_keywords":["Centromere","Mis18 complex","Cenp-a"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD047345"],"sample_protocol":["Cross-linking was performed on gel filtered complexes dialysed into PBS. 16 μg EDC and 35.2 μg sulpho-NHS were used to cross-link 10 μg of Mis18a/b with Mis18BP120-130 (Mis18core) for 1.5 h at RT. The reactions were quenched with final concentration 100 mM Tris–HCl before separation on Bolt™ 4–12% Bis-Tris Plus gels (Invitrogen). Sulfo-SDA (sulfosuccinimidyl 4,4’- azipentanoate) (Thermo Scientific Pierce) cross-linking reaction was a two-step process. First, sulfo-SDA mixed with Mis18a/b (0.39 μg/μl) at different ratio (w/w) of 1:0.07, 1:0.13, 1:0.19, 1:0.38, 1:0.5, 1:0.75, 1:1 and 1:1.4 (Mis18a/b:Sulfo-SDA) was allowed to incubate 30 min at room temperature to initiate incomplete lysine reaction with the sulfo-NHS ester component of the cross-linker. The diazirine group was then photoactivated for 20 mins using UV 26 irradiation from a UVP CL-1000 UV Cross-linker (UVP Inc.) at 365 nm (40 W). The reactions were quenched with 2 μl of 2.7 M ammonium bicarbonate before loading on Bolt™ 4–12% Bis-Tris Plus gels (Invitrogen) for separation. Following previously established protocol [38], either the whole sample or specific bands were excised, and proteins were digested with 13 ng/μl trypsin (Pierce) overnight at 37°C after being reduced and alkylated. The digested peptides were loaded onto C18-Stage-tips [39] for LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["LC-MS/MS analysis was performed using an Orbitrap Fusion Lumos (Thermo Fisher Scientific) coupled on-line with an Ultimate 3000 RSLCnano system (Thermo Fisher Scientific) with a “high/high” acquisition strategy. The peptide separation was carried out on a 50cm EASY-Spray column (Thermo Fisher Scientific). Mobile phase A consisted of water and 0.1% v/v formic acid. Mobile phase B consisted of 80% v/v acetonitrile and 0.1% v/v formic acid. Peptides were loaded at a flow rate of 0.3 μl/min and eluted at 0.2 μl/min or 0.25 μl/min using a linear gradient going from 2% mobile phase B to 40% mobile phase B over 109 or 79 min, followed by a linear increase from 40% to 95% mobile phase B in 11 min. The eluted peptides were directly introduced into the mass spectrometer. MS data were acquired in the data- dependent mode with a 3 s acquisition cycle. Precursor spectra were recorded in the Orbitrap with a resolution of 120,000. The ions with a precursor charge state between 3+ and 8+ were isolated with a window size of 1.6 m/z and fragmented using high-energy collision dissociation (HCD) with a collision energy of 30. The fragmentation spectra were recorded in the Orbitrap with a resolution of 15,000. Dynamic exclusion was enabled with single repeat count and 60 s exclusion duration. The mass spectrometric raw files were processed into peak lists using ProteoWizard (version 3.0.20388), and cross-linked peptides were matched to spectra using Xi software (version 1.7.6.3) with in-search assignment of monoisotopic peaks. Search parameters were MS accuracy, 3 ppm; MS/MS accuracy, 10ppm; enzyme, trypsin; cross-linker, EDC; max missed cleavages, 4; missing mono-isotopic peaks, 2. For EDC search cross-linker, EDC; fixed modification, carbamidomethylation on cysteine; variable modifications, oxidation on methionine. For sulfo- SDA search: fixed modifications, none; variable modifications, carbamidomethylation on cysteine, oxidation on methionine, SDA-loop SDA cross-link within a peptide that is also cross- linked to a separate peptide. Fragments b and y type ions (HCD) or b, c, y, and z type ions (EThcD) with loss of H2O, NH3 and CH3SOH. 5% on link level False discovery rate (FDR) was estimated based on the number of decoy identification using XiFDR (Fischer and Rappsilber, 2017)"],"omics_type":["Proteomics"],"labhead":["Prof. Juri Rappsilber"],"instrument_platform":[""],"labhead_affiliation":["Michael Swann Building Max Born Crescent The University of Edinburgh Edinburgh EH9 3BF"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["jzou@ed.ac.uk"],"submitter_affiliation":["The University of Edinburgh"],"submitter_country":["United Kingdom"],"description_synonyms":["CENP-A loading, hMIS18beta, RGD1305846, INSDC_feature:centromere, CenH3-containing nucleosome assembly at centromere, B28, conformation, Gm975, Cid[Mel], LINT-25, neurotubule, Hominini, composed of, CENP-A containing nucleosome assembly, CENP-A, 6430706D22Rik, CENP-C, protrusion, FASP1, CenpA, C330011F01Rik, Apes, Histone H2b, Histone H2a, Polynucleosome, MIS18 complex, Mfleg1, Knl2, KNL2, Homo, Cycle, Hominids, AA959943, CT86, URLC9, Separated, microtubulus, pericentric region, Histone H3.3, 5730547N13Rik, CenH3[Cid], CG13329, CenH3[CID], Cell Division Cycles, Cycles, HSA242977, Centromeres., Divorced, BcDNA:RE21270, MIS18alpha, Centromeres, Cell Division Cycle, cell-division cycle, DmelCG13329, Pongidae, composition, Cell Division, Divorces, RGD1310778, Maintenances, Acts, Hominins, centromere, centric region, Hominin, Cell Cycles, Cenp-A, Histone H5, Histone H4, Histone H7, site, microtubuli, relational structural quality, Histone H1, Hominid, Histone H3, Acta-2, 6720403H11, anatomical protrusion, 2610039C10Rik, hMis18alpha, CENP-A containing chromatin organization, Actsk-1, A730008H23Rik, cenH3, FAKTS, hFLEG1, function, CENP-A deposition, compositionality, RGD1305497, Homininus, Histone, Cell, results, Division Cycles, Cid, CID, Centromere protein A, centromere specific nucleosome exchange, Nucleosome, centromeric chromatin organization, Polynucleosomes, Microtubule, region, cenpA, Dinucleosome, C79407, Separation, CenH3, CenH3/CID, CENP-A/Cid, CENP-A/CID, Division Cycle, CENPA, mKIAA1903, content, Separations, Centromere autoantigen A, Histone H1(s), Dinucleosomes, M18BP1, MIS18beta, chromosome, spine, structure, 2810018N07Rik, MIS18B, C21orf46, C21orf45, Ape, CenpA/CID, C14orf106, humans, CID/CENP-A"],"sample_synonyms":["Methane, liquid chromatography tandem mass spectroscopy, B28, Lysine Hydrochloride, determination, SDA, CTRCT40, 15Z)-Octadecatetraenoic acid, CG3629, 12, Polypeptides, Lysine Acetate, peptido, Gm48, Chloride(1-), GRP1, Grp1, B1, DGS, 2, Min, 6, 9, DmelCG42273, L Lysine, Art, Divorced, LCMSMS, peptides, K, PTPSTEP, weight-weight percentage, hypoplasia, min, epsilon-diaminocaproic acid, chemical analysis., mAPC, IBP, Divorces, Xcat, 12Z, RGD1310778, EG:196F3.2, Ba, AI047805, reaction, set, cataract, LYS, DmelCG1106, 3-propanediol, l(2)k08110, Lysin, sample, D1, stage, Bladder pain syndrome, CXN, GPH, LC-MS2, anatomical protrusion, dl, BZRP, Ester, LC-MS/MS, Dmel_CG7826, incomplete, SCML1, Thermo Scientific, PBS, PBR, abolished, l(2)01092, Dm1, DmelCG3629, 3.1.3.48, lysine, BcDNA:LP01770, CG14784, Dmel_CG7835, CG14783, Mnb, MNB, absence of, esters, Cl-, DLL, Painful Bladder Syndrome, Step, CG11628, Xylella fastidiosa str. Temecula1, cataract-dental syndrome, Striatum-enriched protein-tyrosine phosphatase, alpha, AW124434, study protocol, beta Trypsin, E(Arp), En(Arp), CG1106, w/w, dll, Painful bladder syndrome, STEP, spine, liquid chromatography-tandem mass spectroscopy, 2810018N07Rik, 2-(bis(2-hydroxyethyl)amino)-2(hydroxymethyl)-1, Polypeptide, C21orf46, C21orf45, DmelCG32810, Bladder Pain Syndrome, Gruppe, BPBS, CHLORIDE ION, diazo-, X-linked, GRP1/cytohesin 1, (6Z, developmental stage, Pierce, Gene, abdominal muscles, CG7826, LC-MS-MS, FASP1, protrusion, CG11633, cytohesin/GRP1, method, l(2)387, reduced, method used in an experiment, LC-MSMS, CG7835, Gene Products, CG42273, Lysine, tiny, cataract X-linked with Hutchinsonian teeth, Separated, 9Z, MIS18alpha, gel, Mesiodens cataract syndrome, beta-Trypsin, l(2)SH2 0323, pk18, MBR, Nhs1, cataract dental syndrome, Xylella fastidiosa (strain Temecula1 / ATCC 700964), Mesiodens-cataract syndrome, Neural-specific protein-tyrosine phosphatase, grupos, PTBR, peptidos, bis(2-hydroxyethyl)imino-tris(hydroxymethyl)methane, stearidonic acid, Cl(-), 2.7, PTHB1, small, DYRK1, mass percentage, 2610039C10Rik, grupo, DBI, hMis18alpha, Proteins, stepk, sulfo-NHS, Peptide, group, LC/MS/MS, Temperatures, PKBS, Acetate, C18, Protein, with Hutchinsonian teeth, Chloride ion, Gm389, Dyrk1, eagle-Barrett syndrome, l(2)SH0323, L-Lysine, 15-Octadecatetraenoic acid, CYH1, AU020952, Separation, with urinary tract Abnormality and cryptorchidism, PRSS, Diazirine, ensemble, underdeveloped, Separations, CC1, Bis-Tris, Rest, Tripcellim, NHS, mDRC, sample population, DmelCG11628, ME-IV, plan specification, Protein Gene Products, Gene Proteins, Trypure, concentration, Chlorine anion, liquid chromatography tandem mass spectrometry, Peptid, assay, 6-diaminohexanoic acid, Enisyl, groupe, CG32810"],"name_synonyms":["FASP1, 2810018N07Rik, C21orf46, MIS18alpha, C21orf45, 2610039C10Rik, B28, core., hMis18alpha, RGD1310778"],"data_synonyms":["Water, sodium salt, ammonium formate, 13C-labeled, cadmium salt, MeCN, dmMOF, ion, Raw, PLXN4, odd(Oz), PLXN3, fond, H(2)O, SDA, A4, BOUND WATER, magnesium formate, CycEI, 15Z)-Octadecatetraenoic acid, oxidane, zinc salt, heavy chain disease, WATER, HOH, DmelCG9648, Polypeptides, cobalt(II) formate dihydrate, CH3-C#N, dMOF, ten-m, Software Engineering, 2-amino-3-mercaptopropanoic acid, 6, 9, R-717, WMS, gamma sarcoglycan, ammoniac, C, Divorced, l(3)rP126, M, Divorces, BcDNA:AT25108, AI047805, glandular fever, column, spirit of hartshorn, EThcD, Gammaherpesviral mononucleosis, Half Cystine, z, 6.3, nickel salt, SGS, LC-MS2, cobalt (+2) salt, Zinc Cysteinate, CG5723, Cyc E, not genetically inherited, Software Tools, ACMICD, bHLHd7, bHLHd6, bHLHd9, Computer Applications, bHLHd8, H2O, sodium (4:1:1) salt, bHLHd5, bHLHd4, BG:DS07108.3, count, magnesium salt, Dm1, Computer Applications Software, Methionin, sarcoglycan, Hmet, l(2)05206, (2R)-2-amino-3-sulfanylpropanoic acid, Hydrogen Oxide, Software Applications, Source Software, formate, cromium (+3), beta Trypsin, Applications, liquid chromatography-tandem mass spectroscopy, 35kD dystrophin-associated glycoprotein, ammonium (4:1) salt, 2017, methyl cyanide, lead (+2) salt, Liquimeth, Computer Software Applications, 2-amino-4-(methylsulfanyl)butanoic acid, 5301, nickel formate dihydrate, cycline, lead formate, Biocatalysts, (6Z, fractured, DmcyclinE, aluminum salt, number, L-Zystein, introduced into, precursor, thomson, CG7826, agua, mass-to-charge ratio, cdi7, Odz, DmelCG3025, cyclinE, LC-MSMS, CG7835, Cdi7, CDI7, CG42273, Half-Cystine, MAM, gamma-SG, Application, Open Source Softwares, odz, MAX, anatomical systems, thallium (+1) salt, Software Application, L Cysteine, E-920, rubidium salt, beta-Trypsin, inserted, Open Source Software, Hcys, methanoic acid, DmcycE, ions, l(3)rJ307, Computer Software Application, l(3)05301, Enzyme, max, 2-amino-4-(methylthio)butanoic acid, Tools, CYSTEINE, Pfeiffer's disease, FREE CYSTEINE, peptidos, (2R)-2-amino-3-mercaptopropanoic acid, metionina, Ten-mc., 1-(14)C-labeled, 35 kDa dystrophin-associated glycoprotein, Ammoniak, CG3025, split, potassium formate, copper (+2) salt, acetonitrile, L-Isomer, SGCG, Tool, Ten79E, polypeptide, l(2)k02514, DmCycE, cupric formate, chemical analysis, hemorrhaged, MFS1, Kissing disease, NH3, aluminum formate, [NH3], Met, AU020952, torn, lithium formate, l(2)k02602, Col4a-1, CT16449, DMDA1, Separations, Glandular Fever, (R)-2-amino-3-mercaptopropanoic acid, ethanenitrile, 2-Amino-3-mercaptopropionic acid, ME-IV, Computer Programs, D-CycE, Applications Softwares, Monocytic angina, liquid chromatography tandem mass spectrometry, E920, ten(m), [OH2], CG11452, liquid chromatography tandem mass spectroscopy, MGC130048, Bru, E 920, NCMe, determination, zinc formate, lead salt, Mononucleosis, 12, peptide, L-Isomer Methionine, DmelCG5723, ammonium tetraformate, Methionine, peptido, Ccne, Min, Cystein, Computer Program, DmelCG42273, Svc, LCMSMS, peptides, l(3)rL201, cisteina, dMax, Open, min, Computer Programs and Programming, ten-m/odz, mAPC, mononucleosis, copper, 12Z, ten[m], AMMONIA, lithium salt, ppm, HSSEXGENE, dihydridooxygen, gamma-sarcoglycan, dihydrogen oxide, GPHYSD2, Racemethionine, ammonium (2:1) salt, XAP-6, T5E21.12, LC-MS/MS, aqua, 2-Amino-4-(methylthio)butyric acid, SG-gamma, Dmel_CG7826, CG9648, Th, br37, l(3)05309, fragmented, Cys, Source Softwares, Programs, Program, HCD, Ionen, dmax, Computer Applications Softwares, Softwares, nickel (+2) salt, fixed, Dmel_CG7835, T5E21_12, Mnb, MNB, parent ion, ammonium salt, MS/MS, cracked, hydrogen hydroxide, cobaltous formate, L-Cysteine, MASS, AW124434, gamma (35kDa dystrophin-associated glycoprotein), acqua, L-Cystein, infectious mononucleosis, loss of, MOF, Mof, DMDA, l35Dd, precursor ion, copper salt, Biocatalyst, Filatov's disease, Ammonia, Polypeptide, Wasser, Pfeiffer's disease (disorder), Cysteine Hydrochloride, SGCG_HUMAN, ammonia, amoniaco, cesium salt, L Isomer, FBN, cycE, Ten[m], Computer, l(2)br37, TYPE, LC-MS-MS, CYCLE, formic acid, DAGA4, potassium salt, Mono, ECTOL1, 14C-labeled, 35DAG, L-Methionine, Del(8)44H, Separated, SCG3, Pedameth, Gammaherpesviral mononucleosis (disorder), 9Z, CYCE, DmelCG3938, iones, MS2, CyclE, 3938, eau, calcium formate, OCTD, l(2)k05007, dm-cycE, 10^[-6], Infectious Mononucleosis, odz/ten-m, azane, cromium (+3) salt, stearidonic acid, sodium formate, Applications Software, Open Source, DYRK1, Computer Software, nickel formate, 3H-labeled, DL-Methionine, strontium formate, strontium salt, Peptide, LGMD2C, AI875693, LC/MS/MS, Software Tool, water, Dyrk1, CyeE, Software, ACETONITRILE, tandem MS, Zystein, cyanomethane, WMS2, 15-Octadecatetraenoic acid, Separation, PRSS, 2-amino-3-sulfanylpropanoic acid, CC1, l(2)35Dd, Engineering, Tripcellim, L-2-Amino-3-mercaptopropionic acid, chromic formate, Trypure, Ion, SSKS, AA960152, SCARMD2, cardinality, calcium salt, alpha-amino-gamma-methylmercaptobutyric acid, monocytic angina, Peptid, assay, Glandular fever, variable, CG3938, l(3)00844"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis for the assembly of Mis18a/b core modules","description":"The centromere, defined by the enrichment of CENP-A (a Histone H3 variant) containing nucleosomes, is a specialised chromosomal locus that acts as a microtubule attachment site. To preserve centromere identity, CENP-A levels must be maintained through active CENP-A loading during the cell cycle. A central player mediating this process is the Mis18 complex (Mis18a, Mis18b and Mis18BP1), which recruits the CENP-A specific chaperone HJURP to centromeres for CENP-A deposition. Here, using a multi-pronged approach, we characterise the structure of the Mis18 complex and show that multiple hetero- and homo-oligomeric interfaces facilitate the hetero-octameric Mis18 complex assembly composed of 4 Mis18a, 2 Mis18b and 2 Mis18BP1. Evaluation of structure-guided/separation-of-function mutants reveals structural determinants essential for Mis18 complex assembly and centromere maintenance. Our results provide new mechanistic insights on centromere maintenance, highlighting that while Mis18a can associate with centromeres and deposit CENP-A independently of Mis18b, the latter is indispensable for the optimal level of CENP-A loading required for preserving the centromere identity.","dates":{"publication":"2024-05-15","submission":"2023-11-28"},"accession":"PXD047345","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063"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