DMS_index,DMS_id,DMS_filename,UniProt_ID,taxon,source_organism,target_seq,seq_len,DMS_total_number_mutants,DMS_binarization_cutoff,DMS_binarization_method,first_author,title,year,jo,molecule_name,selection_assay,selection_type,MSA_filename,MSA_start,MSA_end,MSA_len,MSA_bitscore,MSA_theta,MSA_num_seqs,MSA_perc_cov,MSA_num_cov,MSA_N_eff,MSA_Neff_L,MSA_Neff_L_category,MSA_num_significant,MSA_num_significant_L,raw_DMS_filename,raw_DMS_phenotype_name,raw_DMS_directionality,raw_DMS_mutant_column,weight_file_name,ProteinGym_version,coarse_selection_type
DMS_ind_0,A4_HUMAN_Seuma_2022_indels,A4_HUMAN_Seuma_2022_indels.csv,A4_HUMAN,Human,Homo sapiens,MLPGLALLLLAAWTARALEVPTDGNAGLLAEPQIAMFCGRLNMHMNVQNGKWDSDPSGTKTCIDTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHPHFVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDNVDSADAEEDDSDVWWGGADTDYADGSEDKVVEVAEEEEVAEVEEEEADDDEDDEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFFYGGCGGNRNNFDTEEYCMAVCGSAMSQSLLKTTQEPLARDPVKLPTTAASTPDAVDKYLETPGDENEHAHFQKAKERLEAKHRERMSQVMREWEEAERQAKNLPKADKKAVIQHFQEKVESLEQEAANERQQLVETHMARVEAMLNDRRRLALENYITALQAVPPRPRHVFNMLKKYVRAEQKDRQHTLKHFEHVRMVDPKKAAQIRSQVMTHLRVIYERMNQSLSLLYNVPAVAEEIQDEVDELLQKEQNYSDDVLANMISEPRISYGNDALMPSLTETKTTVELLPVNGEFSLDDLQPWHSFGADSVPANTENEVEPVDARPAADRGLTTRPGSGLTNIKTEEISEVKMDAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIATVIVITLVMLKKKQYTSIHHGVVEVDAAVTPEERHLSKMQQNGYENPTYKFFEQMQN,770,2346,-2.319333116,median,Seuma,"An atlas of amyloid aggregation: the impact of substitutions, insertions, deletions and truncations on amyloid beta fibril nucleation",2022,10.1038/s41467-022-34742-3,APP,aggregation,survival assessment assay,A4_HUMAN_2023-08-07_b01.a2m,1,770,770,0.1,0.2,5272,0.987,760,99.3,0.1306578947,Low,0,0,,nscore_c,1,mutated_sequence,A4_HUMAN_theta0.2_2023-08-07_b01.npy,1,Stability
DMS_ind_1,AMFR_HUMAN_Tsuboyama_2023_4G3O_indels,AMFR_HUMAN_Tsuboyama_2023_4G3O_indels.csv,AMFR_HUMAN,Human,Homo sapiens,YFQGQLNAMAHQIQEMFPQVPYHLVLQDLQLTRSVEITTDNILEGRI,47,117,-1.504736022,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,E3 ubiquitin-protein ligase AMFR,Stability,cDNA display proteolysis,AMFR_HUMAN_2023-08-07_b04.a2m,1,47,47,0.4,0.2,17787,0.872,41,1166.9,28.46097561,Medium,12,0.2926829268,,ddG_ML_float,1,aa_seq,AMFR_HUMAN_theta0.2_2023-08-07_b04.npy,1,Stability
DMS_ind_2,ARGR_ECOLI_Tsuboyama_2023_1AOY_indels,ARGR_ECOLI_Tsuboyama_2023_1AOY_indels.csv,ARGR_ECOLI,Prokaryote,Escherichia coli,QEELVKAFKALLKEEKFSSQGEIVAALQEQGFDNINQSKVSRMLTKFGAVRTRNAKMEMVYCLPAELGV,69,181,-0.4541373765,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Arginine repressor,Stability,cDNA display proteolysis,ARGR_ECOLI_2023-08-07_b04.a2m,1,69,69,0.4,0.2,21443,0.913,63,3719.2,59.03492063,Medium,29,0.4603174603,,ddG_ML_float,1,aa_seq,ARGR_ECOLI_theta0.2_2023-08-07_b04.npy,1,Stability
DMS_ind_3,B1LPA6_ECOSM_Russ_2020_indels,B1LPA6_ECOSM_Russ_2020_indels.csv,B1LPA6_ECOSM,Prokaryote,Escherichia coli,MTSENPLLALREKISALDEKLLALLAERRELAVEVGKAKLLSHRPVRDIDRERDLLERLITLGKAHHLDAHYITRLFQLIIEDSVLTQQALLQQHLNKINPHSARIAFLGPKGSYSHLAARQYAARHFEQFIESGCAKFADIFNQVETGQADYAVVPIENTSSGAINDVYDLLQHTSLSIVGEMTLTIDHCLLVSGTTDLSTINTVYSHPQPFQQCSKFLNRYPHWKIEYTESTSAAMEKVAQAKSPHVAALGSEAGGTLYGLQVLERIEANQRQNFTRFVVLARKAINVSDQVPAKTTLLMATGQQAGALVEALLVLRNHSLIMTRLESRPIHGNPWEEMFYLDIQANLESAEMQKALKELGEITRSMKVLGCYPSENVVPVDPT,386,3074,0.4,manual,Russ,An evolution-based model for designing chorismate mutase enzymes,2020,10.1126/science.aba3304,chorismate mutase,enzyme activity,enzyme activity,B1LPA6_ECOSM_full_04-30-2022_b05.a2m,1,386,386,0.5,0.2,33872,0.699,270,6160,22.81481481,Medium,341,1.262962963,B1LPA6_ECOSM_Russ_2020.csv,activity,1,mutant,B1LPA6_ECOSM_theta_0.2.npy,0.1,Activity
DMS_ind_4,BBC1_YEAST_Tsuboyama_2023_1TG0_indels,BBC1_YEAST_Tsuboyama_2023_1TG0_indels.csv,BBC1_YEAST,Eukaryote,Saccharomyces cerevisiae,EVPFKVVAQFPYKSDYEDDLNFEKDQEIIVTSVEDAEWYFGEYQDSNGDVIEGIFPKSFVAVQG,64,134,-1.271998543,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Myosin tail region-interacting protein MTI1,Stability,cDNA display proteolysis,BBC1_YEAST_2023-08-07_b05.a2m,1,64,64,0.5,0.2,604824,0.844,54,17529.2,324.6148148,High,55,1.018518519,,ddG_ML_float,1,aa_seq,BBC1_YEAST_theta0.2_2023-08-07_b05.npy,1,Stability
DMS_ind_5,BCHB_CHLTE_Tsuboyama_2023_2KRU_indels,BCHB_CHLTE_Tsuboyama_2023_2KRU_indels.csv,BCHB_CHLTE,Prokaryote,Chlorobaculum tepidum,ELSWTAEAEKMLGKVPFFVRKKVRKNTDNYAREIGEPVVTADVFRKAKEHLG,52,82,-0.9540616602,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Light-independent protochlorophyllide reductase subunit B,Stability,cDNA display proteolysis,BCHB_CHLTE_2023-08-07_b04.a2m,1,52,52,0.4,0.2,12079,0.923,48,2630.8,54.80833333,Medium,18,0.375,,ddG_ML_float,1,aa_seq,BCHB_CHLTE_theta0.2_2023-08-07_b04.npy,1,Stability
DMS_ind_6,BLAT_ECOLX_Gonzalez_2019_indels,BLAT_ECOLX_Gonzalez_2019_indels.csv,BLAT_ECOLX,Prokaryote,Escherichia coli,MSIQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRPEERFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVRELCSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTMPAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGSRGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW,286,4751,0.015686274,median,Gonzalez,Fitness Effects of Single Amino Acid Insertions and Deletions in TEM-1 β-Lactamase,2019,10.1016/j.jmb.2019.04.030,Beta-lactamase TEM,"antibiotic resistance, MIC",Amp resistance,BLAT_ECOLX_full_11-26-2021_b02.a2m,1,286,286,0.2,0.2,209644,0.752,215,47605,221.4186047,High,446,2.074418605,BLAT_ECOLX_Gonzalez_indels_2019.csv,DMS_score,1,sequence,BLAT_ECOLX_theta_0.2.npy,0.1,OrganismalFitness
DMS_ind_7,CAPSD_AAV2S_Sinai_2021_designed_indels,CAPSD_AAV2S_Sinai_2021_designed_indels.csv,CAPSD_AAV2S,Virus,Adeno-associated virus 2 (isolate Srivastava/1982) (AAV-2),MAADGYLPDWLEDTLSEGIRQWWKLKPGPPPPKPAERHKDDSRGLVLPGYKYLGPFNGLDKGEPVNEADAAALEHDKAYDRQLDSGDNPYLKYNHADAEFQERLKEDTSFGGNLGRAVFQAKKRVLEPLGLVEEPVKTAPGKKRPVEHSPVEPDSSSGTGKAGQQPARKRLNFGQTGDADSVPDPQPLGQPPAAPSGLGTNTMATGSGAPMADNNEGADGVGNSSGNWHCDSTWMGDRVITTSTRTWALPTYNNHLYKQISSQSGASNDNHYFGYSTPWGYFDFNRFHCHFSPRDWQRLINNNWGFRPKRLNFKLFNIQVKEVTQNDGTTTIANNLTSTVQVFTDSEYQLPYVLGSAHQGCLPPFPADVFMVPQYGYLTLNNGSQAVGRSSFYCLEYFPSQMLRTGNNFTFSYTFEDVPFHSSYAHSQSLDRLMNPLIDQYLYYLSRTNTPSGTTTQSRLQFSQAGASDIRDQSRNWLPGPCYRQQRVSKTSADNNNSEYSWTGATKYHLNGRDSLVNPGPAMASHKDDEEKFFPQSGVLIFGKQGSEKTNVDIEKVMITDEEEIRTTNPVATEQYGSVSTNLQRGNRQAATADVNTQGVLPGMVWQDRDVYLQGPIWAKIPHTDGHFHPSPLMGGFGLKHPPPQILIKNTPVPANPSTTFSAAKFASFITQYSTGQVSVEIEWELQKENSKRWNPEIQYTSNYNKSVNVDFTVDTNGVYSEPRPIGTRYLTRNL,735,225998,-2.18477642,median,Sinai,Generative AAV capsid diversification by latent interpolation,2021,10.1101/2021.04.16.440236,AAV,viability for AAV capsid production,,CAPSD_AAV2S_uniprot_t099_msc70_mcc70_b0.8.a2m,1,735,735,0.8,0.01,604,0.782,575,213.8,0.371826087,Low,1943,3.379130435,CAPSD_AAV2S_Sinai_indels_2021.csv,label,1,mutated_sequence,CAPSD_AAV2S_theta_0.01.npy,0.1,OrganismalFitness
DMS_ind_8,CAPSD_AAV2S_Sinai_2021_library_indels,CAPSD_AAV2S_Sinai_2021_library_indels.csv,CAPSD_AAV2S,Virus,Adeno-associated virus 2 (isolate Srivastava/1982) (AAV-2),MAADGYLPDWLEDTLSEGIRQWWKLKPGPPPPKPAERHKDDSRGLVLPGYKYLGPFNGLDKGEPVNEADAAALEHDKAYDRQLDSGDNPYLKYNHADAEFQERLKEDTSFGGNLGRAVFQAKKRVLEPLGLVEEPVKTAPGKKRPVEHSPVEPDSSSGTGKAGQQPARKRLNFGQTGDADSVPDPQPLGQPPAAPSGLGTNTMATGSGAPMADNNEGADGVGNSSGNWHCDSTWMGDRVITTSTRTWALPTYNNHLYKQISSQSGASNDNHYFGYSTPWGYFDFNRFHCHFSPRDWQRLINNNWGFRPKRLNFKLFNIQVKEVTQNDGTTTIANNLTSTVQVFTDSEYQLPYVLGSAHQGCLPPFPADVFMVPQYGYLTLNNGSQAVGRSSFYCLEYFPSQMLRTGNNFTFSYTFEDVPFHSSYAHSQSLDRLMNPLIDQYLYYLSRTNTPSGTTTQSRLQFSQAGASDIRDQSRNWLPGPCYRQQRVSKTSADNNNSEYSWTGATKYHLNGRDSLVNPGPAMASHKDDEEKFFPQSGVLIFGKQGSEKTNVDIEKVMITDEEEIRTTNPVATEQYGSVSTNLQRGNRQAATADVNTQGVLPGMVWQDRDVYLQGPIWAKIPHTDGHFHPSPLMGGFGLKHPPPQILIKNTPVPANPSTTFSAAKFASFITQYSTGQVSVEIEWELQKENSKRWNPEIQYTSNYNKSVNVDFTVDTNGVYSEPRPIGTRYLTRNL,735,24908,-2.18477642,median,Sinai,Generative AAV capsid diversification by latent interpolation,2021,10.1101/2021.04.16.440236,AAV,viability for AAV capsid production,,CAPSD_AAV2S_uniprot_t099_msc70_mcc70_b0.8.a2m,1,735,735,0.8,0.01,604,0.782,575,213.8,0.371826087,Low,1943,3.379130435,CAPSD_AAV2S_Sinai_indels_2021.csv,label,1,mutated_sequence,CAPSD_AAV2S_theta_0.01.npy,0.1,OrganismalFitness
DMS_ind_9,CATR_CHLRE_Tsuboyama_2023_2AMI_indels,CATR_CHLRE_Tsuboyama_2023_2AMI_indels.csv,CATR_CHLRE,Eukaryote,Chlamydomonas reinhardtii,GLTEEQKQEIREAFDLFDTDGSGTIDAKELKVAMRALGFEPKKEEIKKMISEIDKDGSGTIDFEEFLTMMTA,72,197,-0.5681612987,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Caltractin,Stability,cDNA display proteolysis,CATR_CHLRE_2023-08-07_b03.a2m,1,72,72,0.3,0.2,551057,0.903,65,75596.9,1163.029231,High,57,0.8769230769,,ddG_ML_float,1,aa_seq,CATR_CHLRE_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_10,CBPA2_HUMAN_Tsuboyama_2023_1O6X_indels,CBPA2_HUMAN_Tsuboyama_2023_1O6X_indels.csv,CBPA2_HUMAN,Human,Homo sapiens,VGDQVLEIVPSNEEQIKNLLQLEAQEHLQLDFWKSPTTPGETAHVRVPFVNVQAVKVFLESQGIAYSIMIED,72,205,-1.221174658,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Carboxypeptidase A2,Stability,cDNA display proteolysis,CBPA2_HUMAN_2023-08-07_b03.a2m,1,72,72,0.3,0.2,12711,0.986,71,3086.5,43.47183099,Medium,34,0.4788732394,,ddG_ML_float,1,aa_seq,CBPA2_HUMAN_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_11,CBX4_HUMAN_Tsuboyama_2023_2K28_indels,CBX4_HUMAN_Tsuboyama_2023_2K28_indels.csv,CBX4_HUMAN,Human,Homo sapiens,AVESIEKKRIRKGRVEYLVKWRGWSPKYNTWEPEENILDPRLLIAFQNRE,50,129,-1.635037732,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,E3 SUMO-protein ligase CBX4,Stability,cDNA display proteolysis,CBX4_HUMAN_2023-08-07_b03.a2m,1,50,50,0.3,0.2,108263,0.96,48,13404.4,279.2583333,High,23,0.4791666667,,ddG_ML_float,1,aa_seq,CBX4_HUMAN_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_12,CSN4_MOUSE_Tsuboyama_2023_1UFM_indels,CSN4_MOUSE_Tsuboyama_2023_1UFM_indels.csv,CSN4_MOUSE,Eukaryote,Mus musculus,SSGGSSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFETR,72,195,-0.7,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,COP9 signalosome complex subunit 4,Stability,cDNA display proteolysis,CSN4_MOUSE_2023-08-07_b03.a2m,1,72,72,0.3,0.2,39217,0.889,64,3492.9,54.5765625,Medium,9,0.140625,,ddG_ML_float,1,aa_seq,CSN4_MOUSE_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_13,CUE1_YEAST_Tsuboyama_2023_2MYX_indels,CUE1_YEAST_Tsuboyama_2023_2MYX_indels.csv,CUE1_YEAST,Eukaryote,Saccharomyces cerevisiae,GGHPVTTQMVETVQNLAPNLHPEQIRYSLENTGSVEETVERYLRGDEFSFPP,52,140,-1.319713733,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Coupling of ubiquitin conjugation to ER degradation protein 1,Stability,cDNA display proteolysis,CUE1_YEAST_2023-08-07_b08.a2m,1,52,52,0.8,0.2,3213,0.923,48,387.1,8.064583333,Medium,10,0.2083333333,,ddG_ML_float,1,aa_seq,CUE1_YEAST_theta0.2_2023-08-07_b08.npy,1,Stability
DMS_ind_14,DN7A_SACS2_Tsuboyama_2023_1JIC_indels,DN7A_SACS2_Tsuboyama_2023_1JIC_indels.csv,DN7A_SACS2,Prokaryote,Saccharolobus solfataricus,TVKFKYKGEEKQVDISKIKKVWRVGKMISFTYDEGGGKTGRGAVSEKDAPKELLQ,55,136,-0.472754253,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,DNA-binding protein 7a,Stability,cDNA display proteolysis,DN7A_SACS2_2023-08-07_b02.a2m,1,55,55,0.2,0.2,42895,0.764,42,1248.1,29.71666667,Medium,13,0.3095238095,,ddG_ML_float,1,aa_seq,DN7A_SACS2_theta0.2_2023-08-07_b02.npy,1,Stability
DMS_ind_15,DNJA1_HUMAN_Tsuboyama_2023_2LO1_indels,DNJA1_HUMAN_Tsuboyama_2023_2LO1_indels.csv,DNJA1_HUMAN,Human,Homo sapiens,TTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLSDAKKRELYDKGGE,65,174,-2.239788161,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,DnaJ homolog subfamily A member 1,Stability,cDNA display proteolysis,DNJA1_HUMAN_2023-08-07_b07.a2m,1,65,65,0.7,0.2,280284,0.969,63,35361.9,561.3,High,52,0.8253968254,,ddG_ML_float,1,aa_seq,DNJA1_HUMAN_theta0.2_2023-08-07_b07.npy,1,Stability
DMS_ind_16,DOCK1_MOUSE_Tsuboyama_2023_2M0Y_indels,DOCK1_MOUSE_Tsuboyama_2023_2M0Y_indels.csv,DOCK1_MOUSE,Eukaryote,Mus musculus,WVPTKREEKYGVAFYNYDARGADELSLQIGDTVHILETYEGWYRGYTLRKKSKKGIFPASYIHLKE,66,154,-1.104437518,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Dedicator of cytokinesis protein 1,Stability,cDNA display proteolysis,DOCK1_MOUSE_2023-08-07_b03.a2m,1,66,66,0.3,0.2,705447,0.848,56,22172.3,395.9339286,High,55,0.9821428571,,ddG_ML_float,1,aa_seq,DOCK1_MOUSE_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_17,EPHB2_HUMAN_Tsuboyama_2023_1F0M_indels,EPHB2_HUMAN_Tsuboyama_2023_1F0M_indels.csv,EPHB2_HUMAN,Human,Homo sapiens,SFNTVDEWLEAIKMGQYKESFANAGFTSFDVVSQMMMEDILRVGVTLAGHQKKILNSIQVMRAQMN,66,185,-1.932053964,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Ephrin type-B receptor 2,Stability,cDNA display proteolysis,EPHB2_HUMAN_2023-08-07_b04.a2m,1,66,66,0.4,0.2,212234,0.894,59,8426.3,142.8186441,High,29,0.4915254237,,ddG_ML_float,1,aa_seq,EPHB2_HUMAN_theta0.2_2023-08-07_b04.npy,1,Stability
DMS_ind_18,FECA_ECOLI_Tsuboyama_2023_2D1U_indels,FECA_ECOLI_Tsuboyama_2023_2D1U_indels.csv,FECA_ECOLI,Eukaryote,Escherichia coli,QVNIAPGSLDKALNQYAAHSGFTLSVDASLTRGKQSNGLHGDYDVESGLQQLLDGSGLQVKPLGNNSWTLEP,72,193,-0.813576222,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Fe(3+) dicitrate transport protein FecA,Stability,cDNA display proteolysis,FECA_ECOLI_2023-08-07_b06.a2m,1,72,72,0.6,0.2,74248,0.986,71,9949.9,140.1394366,High,63,0.8873239437,,ddG_ML_float,1,aa_seq,FECA_ECOLI_theta0.2_2023-08-07_b06.npy,1,Stability
DMS_ind_19,HCP_LAMBD_Tsuboyama_2023_2L6Q_indels,HCP_LAMBD_Tsuboyama_2023_2L6Q_indels.csv,HCP_LAMBD,Virus,Escherichia phage lambda (Bacteriophage lambda),VRQEELAAARAALHDLMTGKRVATVQKDGRRVEFTATSVSDLKKYIAELEVQTGM,55,148,-0.350614016,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Head completion protein,Stability,cDNA display proteolysis,HCP_LAMBD_2023-08-07_b05.a2m,1,55,55,0.5,0.2,2128,0.945,52,606.5,11.66346154,Medium,15,0.2884615385,,ddG_ML_float,1,aa_seq,HCP_LAMBD_theta0.2_2023-08-07_b05.npy,1,Stability
DMS_ind_20,HECD1_HUMAN_Tsuboyama_2023_3DKM_indels,HECD1_HUMAN_Tsuboyama_2023_3DKM_indels.csv,HECD1_HUMAN,Human,Homo sapiens,NLYFQGLKYMVPGARVTRGLDWKWRDQDGSPQGEGTVTGELHNGWIDVTWDAGGSNSYRMGAEGKFDLKLAP,72,154,-0.7,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,E3 ubiquitin-protein ligase HECTD1,Stability,cDNA display proteolysis,HECD1_HUMAN_2023-08-07_b03.a2m,1,72,72,0.3,0.2,18660,0.903,65,1192.3,18.34307692,Medium,24,0.3692307692,,ddG_ML_float,1,aa_seq,HECD1_HUMAN_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_21,HIS7_YEAST_Pokusaeva_2019_indels,HIS7_YEAST_Pokusaeva_2019_indels.csv,HIS7_YEAST,Eukaryote,Saccharomyces cerevisiae,MTEQKALVKRITNETKIQIAISLKGGPLAIEHSIFPEKEAEAVAEQATQSQVINVHTGIGFLDHMIHALAKHSGWSLIVECIGDLHIDDHHTTEDCGIALGQAFKEALGAVRGVKRFGSGFAPLDEALSRAVVDLSNRPYAVVELGLQREKVGDLSCEMIPHFLESFAEASRITLHVDCLRGKNDHHRSESAFKALAVAIREATSPNGTNDVPSTKGVLM,220,6102,0.25,manual,Pokusaeva,An experimental assay of the interactions of amino acids from orthologous sequences shaping a complex fitness landscape,2019,10.1371/journal.pgen.1008079,IGP dehydratase (HIS3),Growth,Growth,HIS7_YEAST_full_11-26-2021_b09.a2m,1,220,220,0.9,0.2,40154,0.873,192,5191.3,27.03802083,Medium,318,1.65625,HIS7_YEAST_Pokusaeva_indels_2019.csv,DMS_score,1,sequence,HIS7_YEAST_theta_0.2.npy,0.1,OrganismalFitness
DMS_ind_22,ILF3_HUMAN_Tsuboyama_2023_2L33_indels,ILF3_HUMAN_Tsuboyama_2023_2L33_indels.csv,ILF3_HUMAN,Human,Homo sapiens,MLTKHGKNPVMELNEKRRGLKYELISETGGSHDKRFVMEVEVDGQKFQGAGSNKKVAKAYAALAALEKLFP,71,193,-0.4,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Interleukin enhancer-binding factor 3,Stability,cDNA display proteolysis,ILF3_HUMAN_2023-08-07_b03.a2m,1,71,71,0.3,0.2,145438,0.915,65,21228,326.5846154,High,57,0.8769230769,,ddG_ML_float,1,aa_seq,ILF3_HUMAN_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_23,KCNJ2_MOUSE_Macdonald_2022_indels,KCNJ2_MOUSE_Macdonald_2022_indels.csv,KCNJ2_MOUSE,Eukaryote,Mus Musculus,MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFINVGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDTSKVSKACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVMAKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEGEYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEGMVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARDLAEKKYILSNANSFCYENEVALTSKEEEEDSENGVPESTSTDSPPGIDLHNQASVPLEPRPLRRESEI,428,10501,-2,manual,Macdonald,"DIMPLE: deep insertion, deletion, and missense mutation libraries for exploring protein variation in evolution, disease, and biology",2022,10.1186/s13059-023-02880-6,Kir2.1,surface trafficking,FACS,KCNJ2_MOUSE_b01.a2m,1,428,428,0.1,0.2,20953,0.743,318,2154.5,6.77515723,Medium,160,0.50314465,KCNJ2_MOUSE_Macdonald_2022_indels_noflag.csv,score,1,mutated_sequence_no_flag,KCNJ2_MOUSE_b01_theta_0.2.npy,1,Expression
DMS_ind_24,MAFG_MOUSE_Tsuboyama_2023_1K1V_indels,MAFG_MOUSE_Tsuboyama_2023_1K1V_indels.csv,MAFG_MOUSE,Eukaryote,Mus musculus,LTDEELVTMSVRELNQHLRGLSKEEIIQLKQRRRTLKNRGY,41,115,-0.5,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Transcription factor MafG,Stability,cDNA display proteolysis,MAFG_MOUSE_2023-08-07_b07.a2m,1,41,41,0.7,0.2,6178,1,41,156.7,3.82195122,Medium,4,0.09756097561,,ddG_ML_float,1,aa_seq,MAFG_MOUSE_theta0.2_2023-08-07_b07.npy,1,Stability
DMS_ind_25,MBD11_ARATH_Tsuboyama_2023_6ACV_indels,MBD11_ARATH_Tsuboyama_2023_6ACV_indels.csv,MBD11_ARATH,Eukaryote,Arabidopsis thaliana,VSVELPAPSSWKKLFYPNKVGSVKKTEVVFVAPTGEEISNRKQLEQYLKSHPGNPAIAEFDWTTSG,66,131,-1.578921171,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Methyl-CpG-binding domain-containing protein 11,Stability,cDNA display proteolysis,MBD11_ARATH_2023-08-07_b03.a2m,1,66,66,0.3,0.2,26035,0.909,60,1510.5,25.175,Medium,11,0.1833333333,,ddG_ML_float,1,aa_seq,MBD11_ARATH_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_26,MYO3_YEAST_Tsuboyama_2023_2BTT_indels,MYO3_YEAST_Tsuboyama_2023_2BTT_indels.csv,MYO3_YEAST,Eukaryote,Saccharomyces cerevisiae,KDPKFEAAYDFPGSGSSSELPLKKGDIVFISRDEPSGWSLAKLLDGSKEGWVPTAYMTPYK,61,80,-1,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Myosin-3,Stability,cDNA display proteolysis,MYO3_YEAST_2023-08-07_b07.a2m,1,61,61,0.7,0.2,442941,0.885,54,12893.2,238.762963,High,51,0.9444444444,,ddG_ML_float,1,aa_seq,MYO3_YEAST_theta0.2_2023-08-07_b07.npy,1,Stability
DMS_ind_27,NKX31_HUMAN_Tsuboyama_2023_2L9R_indels,NKX31_HUMAN_Tsuboyama_2023_2L9R_indels.csv,NKX31_HUMAN,Human,Homo sapiens,HSHMSHTQVIELERKFSHQKYLSAPERAHLAKNLKLTETQVKIWFQNRRYKTKRKQLSSEL,61,178,-0.3,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Homeobox protein Nkx-3.1,Stability,cDNA display proteolysis,NKX31_HUMAN_2023-08-07_b04.a2m,1,61,61,0.4,0.2,319273,0.902,55,8440.8,153.4690909,High,27,0.4909090909,,ddG_ML_float,1,aa_seq,NKX31_HUMAN_theta0.2_2023-08-07_b04.npy,1,Stability
DMS_ind_28,NUSA_ECOLI_Tsuboyama_2023_1WCL_indels,NUSA_ECOLI_Tsuboyama_2023_1WCL_indels.csv,NUSA_ECOLI,Prokaryote,Escherichia coli,EAHAAIDTFTKYLDIDEDFATVLVEEGFSTLEELAYVPMKELLEIEGLDEPTVEALRERAKNALATIAQ,69,191,-1.318069467,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Transcription termination/antitermination protein NusA,Stability,cDNA display proteolysis,NUSA_ECOLI_2023-08-07_b03.a2m,1,69,69,0.3,0.2,205612,0.812,56,39002.5,696.4732143,High,38,0.6785714286,,ddG_ML_float,1,aa_seq,NUSA_ECOLI_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_29,NUSG_MYCTU_Tsuboyama_2023_2MI6_indels,NUSG_MYCTU_Tsuboyama_2023_2MI6_indels.csv,NUSG_MYCTU,Prokaryote,Mycobacterium tuberculosis,DYEVGESVTVMDGPFATLPATISEVNAEQQKLKVLVSIFGRETPVELTFGQVSKI,55,157,-0.5,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Transcription termination/antitermination protein NusG,Stability,cDNA display proteolysis,NUSG_MYCTU_2023-08-07_b03.a2m,1,55,55,0.3,0.2,102004,0.964,53,16625.7,313.6924528,High,41,0.7735849057,,ddG_ML_float,1,aa_seq,NUSG_MYCTU_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_30,OBSCN_HUMAN_Tsuboyama_2023_1V1C_indels,OBSCN_HUMAN_Tsuboyama_2023_1V1C_indels.csv,OBSCN_HUMAN,Human,Homo sapiens,FDIYVVTADYLPLGAEQDAITLREGQYVEVLDAAHPLRWLVRTKPTKSSPSRQGWVSPAYLDRRL,65,169,-1,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Obscurin,Stability,cDNA display proteolysis,OBSCN_HUMAN_2023-08-07_b02.a2m,1,65,65,0.2,0.2,718751,0.815,53,23710.7,447.3716981,High,54,1.018867925,,ddG_ML_float,1,aa_seq,OBSCN_HUMAN_theta0.2_2023-08-07_b02.npy,1,Stability
DMS_ind_31,ODP2_GEOSE_Tsuboyama_2023_1W4G_indels,ODP2_GEOSE_Tsuboyama_2023_1W4G_indels.csv,ODP2_GEOSE,Prokaryote,Geobacillus stearothermophilus,NRRVIAMPSVRKWAREKGVDIRLVQGTGKNGRVLKEDIDAFLAG,44,47,-0.4168227551,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex,Stability,cDNA display proteolysis,ODP2_GEOSE_2023-08-07_b07.a2m,1,44,44,0.7,0.2,163835,0.909,40,14834.6,370.865,High,21,0.525,,ddG_ML_float,1,aa_seq,ODP2_GEOSE_theta0.2_2023-08-07_b07.npy,1,Stability
DMS_ind_32,OTU7A_HUMAN_Tsuboyama_2023_2L2D_indels,OTU7A_HUMAN_Tsuboyama_2023_2L2D_indels.csv,OTU7A_HUMAN,Human,Homo sapiens,TLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDLTAALSDYEQ,42,84,-1,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,OTU domain-containing protein 7A,Stability,cDNA display proteolysis,OTU7A_HUMAN_2023-08-07_b02.a2m,1,42,42,0.2,0.2,1359071,0.881,37,514715.2,13911.22162,High,28,0.7567567568,,ddG_ML_float,1,aa_seq,OTU7A_HUMAN_theta0.2_2023-08-07_b02.npy,1,Stability
DMS_ind_33,P53_HUMAN_Kotler_2018_indels,P53_HUMAN_Kotler_2018_indels.csv,P53_HUMAN,Human,Homo sapiens,MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD,393,341,0.206718584,median,Kotler,A Systematic p53 Mutation Library Links Differential Functional Impact to Cancer Mutation Pattern and Evolutionary Conservation,2018,10.1016/j.molcel.2018.06.012,p53,growth,Growth,P53_HUMAN_full_11-26-2021_b09.a2m,1,393,393,0.9,0.2,4129,0.863,339,148,0.4365781711,Low,15,0.04424778761,P53_HUMAN_Kotler_deletions_2018.csv,RFS_H1299,-1,sequence,P53_HUMAN_Kotler_theta_0.2.npy,0.1,OrganismalFitness
DMS_ind_34,PIN1_HUMAN_Tsuboyama_2023_1I6C_indels,PIN1_HUMAN_Tsuboyama_2023_1I6C_indels.csv,PIN1_HUMAN,Human,Homo sapiens,KLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNSSSG,39,106,-0.6844420472,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1,Stability,cDNA display proteolysis,PIN1_HUMAN_2023-08-07_b02.a2m,1,39,39,0.2,0.2,248269,0.821,32,10833.2,338.5375,High,13,0.40625,,ddG_ML_float,1,aa_seq,PIN1_HUMAN_theta0.2_2023-08-07_b02.npy,1,Stability
DMS_ind_35,PITX2_HUMAN_Tsuboyama_2023_2L7M_indels,PITX2_HUMAN_Tsuboyama_2023_2L7M_indels.csv,PITX2_HUMAN,Human,Homo sapiens,THFTSQQLQELEATFQRNHYPDMSTREEIAVWTNLTEARVRVWFKNRRAKWR,52,117,-1.201366007,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Pituitary homeobox 2,Stability,cDNA display proteolysis,PITX2_HUMAN_2023-08-07_b04.a2m,1,52,52,0.4,0.2,344174,1,52,9819.6,188.8384615,High,25,0.4807692308,,ddG_ML_float,1,aa_seq,PITX2_HUMAN_theta0.2_2023-08-07_b04.npy,1,Stability
DMS_ind_36,PKN1_HUMAN_Tsuboyama_2023_1URF_indels,PKN1_HUMAN_Tsuboyama_2023_1URF_indels.csv,PKN1_HUMAN,Human,Homo sapiens,GIPATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQ,71,187,-0.5,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Serine/threonine-protein kinase N1,Stability,cDNA display proteolysis,PKN1_HUMAN_2023-08-07_b01.a2m,1,71,71,0.1,0.2,187829,0.845,60,53755.8,895.93,High,13,0.2166666667,,ddG_ML_float,1,aa_seq,PKN1_HUMAN_theta0.2_2023-08-07_b01.npy,1,Stability
DMS_ind_37,POLG_PESV_Tsuboyama_2023_2MXD_indels,POLG_PESV_Tsuboyama_2023_2MXD_indels.csv,POLG_PESV,Virus,Porcine enteric sapovirus (isolate Swine/United States/Cowden/1980),ALRDDEYDEWQDIIRDWRKEMTVQQFLDLKERALSGASDPDSQRYNAWLELRA,53,149,-1.7,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Genome polyprotein,Stability,cDNA display proteolysis,POLG_PESV_2023-08-07_b03.a2m,1,53,53,0.3,0.2,20190,0.887,47,3718.4,79.11489362,Medium,12,0.2553191489,,ddG_ML_float,1,aa_seq,POLG_PESV_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_38,PR40A_HUMAN_Tsuboyama_2023_1UZC_indels,PR40A_HUMAN_Tsuboyama_2023_1UZC_indels.csv,PR40A_HUMAN,Human,Homo sapiens,TYTWNTKEEAKQAFKELLKEKRVPSNASWEQAMKMIINDPRYSALAKLSEKKQAFNAYKVQTE,63,168,-1.362579422,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Pre-mRNA-processing factor 40 homolog A,Stability,cDNA display proteolysis,PR40A_HUMAN_2023-08-07_b03.a2m,1,63,63,0.3,0.2,63560,0.857,54,3663.8,67.84814815,Medium,16,0.2962962963,,ddG_ML_float,1,aa_seq,PR40A_HUMAN_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_39,PSAE_PICP2_Tsuboyama_2023_1PSE_indels,PSAE_PICP2_Tsuboyama_2023_1PSE_indels.csv,PSAE_PICP2,Prokaryote,Synechococcus sp,AIERGSKVKILRKESYWYGDVGTVASIDKSGIIYPVIVRFNKVNYNGFSGSAGGLNTNNFAEHELEVV,68,175,-0.7,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Photosystem I reaction center subunit IV,Stability,cDNA display proteolysis,PSAE_PICP2_2023-08-07_b09.a2m,1,68,68,0.9,0.2,1785,0.868,59,130.7,2.215254237,Medium,9,0.1525423729,,ddG_ML_float,1,aa_seq,PSAE_PICP2_theta0.2_2023-08-07_b09.npy,1,Stability
DMS_ind_40,PTEN_HUMAN_Mighell_2018_indels,PTEN_HUMAN_Mighell_2018_indels.csv,PTEN_HUMAN,Human,Homo sapiens,MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHTQITKV,403,314,-2.020820613,median,Mighell,A Saturation Mutagenesis Approach to Understanding PTEN Lipid Phosphatase Activity and Genotype-Phenotype Relationships,2018,10.1016/j.ajhg.2018.03.018,PTEN,"growth (surrogate for enzymatic activity/hydrolysis of lipid phosphates to restore PIP2, which affects proliferation rate)",lipid phosphatase activity,PTEN_HUMAN_full_11-26-2021_b01.a2m,1,403,403,0.1,0.2,19058,0.752,303,1425.3,4.703960396,Medium,52,0.1716171617,PTEN_HUMAN_Mighell_deletions_2018.csv,DMS_score,1,sequence,PTEN_HUMAN_theta_0.2.npy,0.1,Activity
DMS_ind_41,Q8EG35_SHEON_Campbell_2022_indels,Q8EG35_SHEON_Campbell_2022_indels.csv,Q8EG35_SHEON,Prokaryote,Shewanella oneidensis,MKNCLKMKNLLPALTITMAMSAVMALVVTPNAYASKWDEKMTPEQVEATLDKKFAEGNYSPKGADSCLMCHKKSEKVMDLFKGVHGAIDSSKSPMAGLQCEACHGPLGQHNKGGNEPMITFGKQSTLSADKQNSVCMSCHQDDKRMSWNGGHHDNADVACASCHQVHVAKDPVLSKNTEMEVCTSCHTKQKADMNKRSSHPLKWAQMTCSDCHNPHGSMTDSDLNKPSVNDTCYSCHAEKRGPKLWEHAPVTENCVTCHNPHGSVNDGMLKTRAPQLCQQCHASDGHASNAYLGNTGLGSNVGDNAFTGGRSCLNCHSQVHGSNHPSGKLLQR,333,331,0.003035782214,median,Campbell,Determinants of Multiheme Cytochrome Extracellular Electron Transfer Uncovered by Systematic Peptide Insertion,2022,10.1021/acs.biochem.2c00148,MtrA,extracellular electron transfer,survival assessment assay,Q8EG35_SHEON_b03.a2m,1,333,333,0.3,0.2,2866,0.778,259,1289.1,4.97722008,Medium,89,0.34362934,Q8EG35_SHEON_Campbell_2023.csv,selected_avg,1,mutated_sequence,Q8EG35_SHEON_b03_theta_0.2.npy,1,OrganismalFitness
DMS_ind_42,RAD_ANTMA_Tsuboyama_2023_2CJJ_indels,RAD_ANTMA_Tsuboyama_2023_2CJJ_indels.csv,RAD_ANTMA,Eukaryote,Antirrhinum majus,PWSAKENKAFERALAVYDKDTPDRWANVARAVEGRTPEEVKKHYEILVEDIKYI,54,97,-0.3943851731,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Transcription factor RADIALIS,Stability,cDNA display proteolysis,RAD_ANTMA_2023-08-07_b01.a2m,1,54,54,0.1,0.2,423275,0.833,45,38133.9,847.42,High,27,0.6,,ddG_ML_float,1,aa_seq,RAD_ANTMA_theta0.2_2023-08-07_b01.npy,1,Stability
DMS_ind_43,RCD1_ARATH_Tsuboyama_2023_5OAO_indels,RCD1_ARATH_Tsuboyama_2023_5OAO_indels.csv,RCD1_ARATH,Eukaryote,Arabidopsis thaliana,PTLFAAISHKVAENDMLLINADYQQLRDKKMTRAEFVRKLRVIVGDDLLRSTITTLQ,57,124,-0.3828831078,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Inactive poly [ADP-ribose] polymerase RCD1,Stability,cDNA display proteolysis,RCD1_ARATH_2023-08-07_b02.a2m,1,57,57,0.2,0.2,6525,0.93,53,1578.5,29.78301887,Medium,2,0.03773584906,,ddG_ML_float,1,aa_seq,RCD1_ARATH_theta0.2_2023-08-07_b02.npy,1,Stability
DMS_ind_44,RD23A_HUMAN_Tsuboyama_2023_1IFY_indels,RD23A_HUMAN_Tsuboyama_2023_1IFY_indels.csv,RD23A_HUMAN,Human,Homo sapiens,SEYETMLTEIMSMGYERERVVAALRASYNNPHRAVEYLLTGIPG,44,120,-0.7285205281,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,UV excision repair protein RAD23 homolog A,Stability,cDNA display proteolysis,RD23A_HUMAN_2023-08-07_b04.a2m,1,44,44,0.4,0.2,100991,0.864,38,7912.9,208.2342105,High,21,0.5526315789,,ddG_ML_float,1,aa_seq,RD23A_HUMAN_theta0.2_2023-08-07_b04.npy,1,Stability
DMS_ind_45,RPC1_BP434_Tsuboyama_2023_1R69_indels,RPC1_BP434_Tsuboyama_2023_1R69_indels.csv,RPC1_BP434,Virus,Enterobacteria phage 434 (Bacteriophage 434),SISSRVKSKRIQLGLNQAELAQKVGTTQQSIEQLENGKTKRPRFLPELASALGVSVDWLLN,61,164,-1.349855239,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Repressor protein CI,Stability,cDNA display proteolysis,RPC1_BP434_2023-08-07_b05.a2m,1,61,61,0.5,0.2,820224,0.951,58,192520.2,3319.313793,High,73,1.25862069,,ddG_ML_float,1,aa_seq,RPC1_BP434_theta0.2_2023-08-07_b05.npy,1,Stability
DMS_ind_46,RS15_GEOSE_Tsuboyama_2023_1A32_indels,RS15_GEOSE_Tsuboyama_2023_1A32_indels.csv,RS15_GEOSE,Prokaryote,Geobacillus stearothermophilus,SPEVQIAILTEQINNLNEHLRVHKKDHHSRRGLLKMVGKRRRLLAYLRNKDVARYREIVEKLG,63,176,-0.1292928041,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Small ribosomal subunit protein uS15,Stability,cDNA display proteolysis,RS15_GEOSE_2023-08-07_b06.a2m,1,63,63,0.6,0.2,44428,1,63,4519.5,71.73809524,Medium,35,0.5555555556,,ddG_ML_float,1,aa_seq,RS15_GEOSE_theta0.2_2023-08-07_b06.npy,1,Stability
DMS_ind_47,S22A1_HUMAN_Yee_2023_abundance_indels,S22A1_HUMAN_Yee_2023_abundance_indels.csv,S22A1_HUMAN,Human,Homo sapiens,PTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAELSQRCGWSPAEELNYTVPGLGPAGEAFLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLGPCQDGWVYDTPGSSIVTEFNLVCADSWKLDLFQSCLNAGFLFGSLGVGYFADRFGRKLCLLGTVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIMYQMAFTVGLVALTGLAYALPHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKMLSLEEDVTEKLSPSFADLFRTPRLRKRTFILMYLWFTDSVLYQGLILHMGATSGNLYLDFLYSALVEIPGAFIALITIDRVGRIYPMAMSNLLAGAACLVMIFISPDLHWLNIIIMCVGRMGITIAIQMICLVNAELYPTFVRNLGVMVCSSLCDIGGIITPFIVFRLREVWQALPLILFAVLGLLAAGVTLLLPETKGVALPETMKDAENLGRKAKPKENTIYLKVQTSEPSGT,553,430,-0.75,manual,Yee,The full spectrum of OCT1 (SLC22A1) mutations bridges transporter biophysics to drug pharmacogenomics,2023,10.1101/2023.06.06.543963,Oct1,abundance,FACS,S22A1_HUMAN_2023-08-07_b02.a2m,1,553,553,0.2,0.2,198790,0.807,446,32557.5,72.99887892,Medium,485,1.087443946,543963_file04.xlsx,GFP_score,1,mutated_sequence,S22A1_HUMAN_theta0.2_2023-08-07_b02.npy,1,Expression
DMS_ind_48,S22A1_HUMAN_Yee_2023_activity_indels,S22A1_HUMAN_Yee_2023_activity_indels.csv,S22A1_HUMAN,Human,Homo sapiens,PTVDDILEQVGESGWFQKQAFLILCLLSAAFAPICVGIVFLGFTPDHHCQSPGVAELSQRCGWSPAEELNYTVPGLGPAGEAFLGQCRRYEVDWNQSALSCVDPLASLATNRSHLPLGPCQDGWVYDTPGSSIVTEFNLVCADSWKLDLFQSCLNAGFLFGSLGVGYFADRFGRKLCLLGTVLVNAVSGVLMAFSPNYMSMLLFRLLQGLVSKGNWMAGYTLITEFVGSGSRRTVAIMYQMAFTVGLVALTGLAYALPHWRWLQLAVSLPTFLFLLYYWCVPESPRWLLSQKRNTEAIKIMDHIAQKNGKLPPADLKMLSLEEDVTEKLSPSFADLFRTPRLRKRTFILMYLWFTDSVLYQGLILHMGATSGNLYLDFLYSALVEIPGAFIALITIDRVGRIYPMAMSNLLAGAACLVMIFISPDLHWLNIIIMCVGRMGITIAIQMICLVNAELYPTFVRNLGVMVCSSLCDIGGIITPFIVFRLREVWQALPLILFAVLGLLAAGVTLLLPETKGVALPETMKDAENLGRKAKPKENTIYLKVQTSEPSGT,553,490,1,manual,Yee,The full spectrum of OCT1 (SLC22A1) mutations bridges transporter biophysics to drug pharmacogenomics,2023,10.1101/2023.06.06.543963,Oct1,uptake of cytotoxic substrate,Growth,S22A1_HUMAN_2023-08-07_b02.a2m,1,553,553,0.2,0.2,198790,0.807,446,32557.5,72.99887892,Medium,485,1.087443946,543963_file04.xlsx,SM73_1_score,-1,mutated_sequence,S22A1_HUMAN_theta0.2_2023-08-07_b02.npy,1,Activity
DMS_ind_49,SAV1_MOUSE_Tsuboyama_2023_2YSB_indels,SAV1_MOUSE_Tsuboyama_2023_2YSB_indels.csv,SAV1_MOUSE,Eukaryote,Mus musculus,GEDLPLPPGWSVDWTMRGRKYYIDHNTNTTHWSHPLESGPSSG,43,86,-0.6280556038,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Protein salvador homolog 1,Stability,cDNA display proteolysis,SAV1_MOUSE_2023-08-07_b06.a2m,1,43,43,0.6,0.2,177542,0.791,34,4627.6,136.1058824,High,14,0.4117647059,,ddG_ML_float,1,aa_seq,SAV1_MOUSE_theta0.2_2023-08-07_b06.npy,1,Stability
DMS_ind_50,SDA_BACSU_Tsuboyama_2023_1PV0_indels,SDA_BACSU_Tsuboyama_2023_1PV0_indels.csv,SDA_BACSU,Prokaryote,Bacillus subtilis,MRKLSDELLIESYFKATEMNLNRDFIELIENEIKRRSLGHIISV,44,127,-1,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Sporulation inhibitor sda,Stability,cDNA display proteolysis,SDA_BACSU_2023-08-07_b05.a2m,1,44,44,0.5,0.2,1953,0.886,39,876.8,22.48205128,Medium,4,0.1025641026,,ddG_ML_float,1,aa_seq,SDA_BACSU_theta0.2_2023-08-07_b05.npy,1,Stability
DMS_ind_51,SOX30_HUMAN_Tsuboyama_2023_7JJK_indels,SOX30_HUMAN_Tsuboyama_2023_7JJK_indels.csv,SOX30_HUMAN,Human,Homo sapiens,RPMNAFMVWARIHRPALAKANPAANNAEISVQLGLEWNKLSEEQKKPYYDEAQKIKE,57,109,-0.3216404755,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Transcription factor SOX-30,Stability,cDNA display proteolysis,SOX30_HUMAN_2023-08-07_b03.a2m,1,57,57,0.3,0.2,158104,0.982,56,14909.6,266.2428571,High,36,0.6428571429,,ddG_ML_float,1,aa_seq,SOX30_HUMAN_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_52,SPG2_STRSG_Tsuboyama_2023_5UBS_indels,SPG2_STRSG_Tsuboyama_2023_5UBS_indels.csv,SPG2_STRSG,Prokaryote,Streptococcus sp. group G,MTFKLIINGKTLKGETTTEAVDAATAEKVFKQYFNDNGIDGEWTYDDATKTFTITE,56,148,-1.000627629,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Immunoglobulin G-binding protein G,Stability,cDNA display proteolysis,SPG2_STRSG_2023-08-07_b03.a2m,1,56,56,0.3,0.2,39899,0.75,42,2567.6,61.13333333,Medium,6,0.1428571429,,ddG_ML_float,1,aa_seq,SPG2_STRSG_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_53,SPTN1_CHICK_Tsuboyama_2023_1TUD_indels,SPTN1_CHICK_Tsuboyama_2023_1TUD_indels.csv,SPTN1_CHICK,Eukaryote,Gallus gallus,RQGFVPAAYVKKLDSGTGKELVLALYDYQEKSPREVTMKKGDILTLLNSTNKDWWKVEVN,60,129,-2.360476078,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,"Spectrin alpha chain, non-erythrocytic 1",Stability,cDNA display proteolysis,SPTN1_CHICK_2023-08-07_b03.a2m,1,60,60,0.3,0.2,420793,0.933,56,15051.5,268.7767857,High,47,0.8392857143,,ddG_ML_float,1,aa_seq,SPTN1_CHICK_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_54,SQSTM_MOUSE_Tsuboyama_2023_2RRU_indels,SQSTM_MOUSE_Tsuboyama_2023_2RRU_indels.csv,SQSTM_MOUSE,Eukaryote,Mus musculus,RLIESLSQMLSMGFSDEGGWLTRLLQTKNYDIGAALDTIQ,40,111,-0.8554856463,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Sequestosome-1,Stability,cDNA display proteolysis,SQSTM_MOUSE_2023-08-07_b05.a2m,1,40,40,0.5,0.2,34660,0.925,37,3244.5,87.68918919,Medium,13,0.3513513514,,ddG_ML_float,1,aa_seq,SQSTM_MOUSE_theta0.2_2023-08-07_b05.npy,1,Stability
DMS_ind_55,SR43C_ARATH_Tsuboyama_2023_2N88_indels,SR43C_ARATH_Tsuboyama_2023_2N88_indels.csv,SR43C_ARATH,Eukaryote,Arabidopsis thaliana,AVAESVIGKRVGDDGKTIEYLVKWTDMSDATWEPQDNVDSTLVLLYQQ,48,135,-1.591761235,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,"Signal recognition particle 43 kDa protein, chloroplastic",Stability,cDNA display proteolysis,SR43C_ARATH_2023-08-07_b02.a2m,1,48,48,0.2,0.2,101118,0.917,44,12180.6,276.8318182,High,26,0.5909090909,,ddG_ML_float,1,aa_seq,SR43C_ARATH_theta0.2_2023-08-07_b02.npy,1,Stability
DMS_ind_56,SRBS1_HUMAN_Tsuboyama_2023_2O2W_indels,SRBS1_HUMAN_Tsuboyama_2023_2O2W_indels.csv,SRBS1_HUMAN,Human,Homo sapiens,GIDPFTGEAIAKFNFNGDTQVEMSFRKGERITLLRQVDENWYEGRIPGTSRQGIFPITYVDVIKRPL,67,154,-1.169019411,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Sorbin and SH3 domain-containing protein 1,Stability,cDNA display proteolysis,SRBS1_HUMAN_2023-08-07_b03.a2m,1,67,67,0.3,0.2,708655,0.836,56,22689,405.1607143,High,60,1.071428571,,ddG_ML_float,1,aa_seq,SRBS1_HUMAN_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_57,TCRG1_MOUSE_Tsuboyama_2023_1E0L_indels,TCRG1_MOUSE_Tsuboyama_2023_1E0L_indels.csv,TCRG1_MOUSE,Eukaryote,Mus musculus,GATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQELK,37,99,-1.2,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Transcription elongation regulator 1,Stability,cDNA display proteolysis,TCRG1_MOUSE_2023-08-07_b08.a2m,1,37,37,0.8,0.2,43363,0.865,32,2819.7,88.115625,Medium,14,0.4375,,ddG_ML_float,1,aa_seq,TCRG1_MOUSE_theta0.2_2023-08-07_b08.npy,1,Stability
DMS_ind_58,THO1_YEAST_Tsuboyama_2023_2WQG_indels,THO1_YEAST_Tsuboyama_2023_2WQG_indels.csv,THO1_YEAST,Eukaryote,Saccharomyces cerevisiae,SADYSSLTVVQLKDLLTKRNLSVGGLKNEWVQRLIKDDEES,41,82,-0.7,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Protein THO1,Stability,cDNA display proteolysis,THO1_YEAST_2023-08-07_b05.a2m,1,41,41,0.5,0.2,54877,0.805,33,8516.7,258.0818182,High,15,0.4545454545,,ddG_ML_float,1,aa_seq,THO1_YEAST_theta0.2_2023-08-07_b05.npy,1,Stability
DMS_ind_59,TNKS2_HUMAN_Tsuboyama_2023_5JRT_indels,TNKS2_HUMAN_Tsuboyama_2023_5JRT_indels.csv,TNKS2_HUMAN,Human,Homo sapiens,FSITQFVRNLGLEHLMDIFEREQITLRVLVEMGHKELKEIGINAYGHREKLIKGVERLI,59,171,-0.9451205822,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Poly [ADP-ribose] polymerase tankyrase-2,Stability,cDNA display proteolysis,TNKS2_HUMAN_2023-08-07_b03.a2m,1,59,59,0.3,0.2,270654,0.949,56,11206,200.1071429,High,26,0.4642857143,,ddG_ML_float,1,aa_seq,TNKS2_HUMAN_theta0.2_2023-08-07_b03.npy,1,Stability
DMS_ind_60,UBE4B_HUMAN_Tsuboyama_2023_3L1X_indels,UBE4B_HUMAN_Tsuboyama_2023_3L1X_indels.csv,UBE4B_HUMAN,Human,Homo sapiens,DAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAWMR,69,147,-1,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Ubiquitin conjugation factor E4 B,Stability,cDNA display proteolysis,UBE4B_HUMAN_2023-08-07_b04.a2m,1,69,69,0.4,0.2,310943,0.928,64,34185.4,534.146875,High,52,0.8125,,ddG_ML_float,1,aa_seq,UBE4B_HUMAN_theta0.2_2023-08-07_b04.npy,1,Stability
DMS_ind_61,UBR5_HUMAN_Tsuboyama_2023_1I2T_indels,UBR5_HUMAN_Tsuboyama_2023_1I2T_indels.csv,UBR5_HUMAN,Human,Homo sapiens,HRQALGERLYPRVQAMQPAFASKITGMLLELSPAQLLLLLASEDSLRARVDEAMELII,58,156,-0.4460165437,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,E3 ubiquitin-protein ligase UBR5,Stability,cDNA display proteolysis,UBR5_HUMAN_2023-08-07_b05.a2m,1,58,58,0.5,0.2,17888,0.966,56,1031.7,18.42321429,Medium,14,0.25,,ddG_ML_float,1,aa_seq,UBR5_HUMAN_theta0.2_2023-08-07_b05.npy,1,Stability
DMS_ind_62,VG08_BPP22_Tsuboyama_2023_2GP8_indels,VG08_BPP22_Tsuboyama_2023_2GP8_indels.csv,VG08_BPP22,Virus,Salmonella phage P22 (Bacteriophage P22),ITGDVSAANKDAIRKQMDAAASKGDVETYRKLKAKLKGIR,40,101,-0.2013306011,median,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Scaffolding protein,Stability,cDNA display proteolysis,VG08_BPP22_2023-08-07_b05.a2m,1,40,40,0.5,0.2,102464,0.875,35,12963.6,370.3885714,High,13,0.3714285714,,ddG_ML_float,1,aa_seq,VG08_BPP22_theta0.2_2023-08-07_b05.npy,1,Stability
DMS_ind_63,VILI_CHICK_Tsuboyama_2023_1YU5_indels,VILI_CHICK_Tsuboyama_2023_1YU5_indels.csv,VILI_CHICK,Eukaryote,Gallus gallus,KLETFPLDVLVNTAAEDLPRGVDPSRKENHLSDEDFKAVFGMTRSAFANLPLWKQQNLKKEKGLF,65,156,-0.7,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Villin-1,Stability,cDNA display proteolysis,VILI_CHICK_2023-08-07_b01.a2m,1,65,65,0.1,0.2,254210,0.769,50,46507.8,930.156,High,19,0.38,,ddG_ML_float,1,aa_seq,VILI_CHICK_theta0.2_2023-08-07_b01.npy,1,Stability
DMS_ind_64,VRPI_BPT7_Tsuboyama_2023_2WNM_indels,VRPI_BPT7_Tsuboyama_2023_2WNM_indels.csv,VRPI_BPT7,Virus,Escherichia phage T7 (Bacteriophage T7),SLSVDNKKFWATVESSEHSFEVPIYAETLDEALELAEWQYVPAGFEVTRVRPCVAP,56,154,-1.1,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,Bacterial RNA polymerase inhibitor,Stability,cDNA display proteolysis,VRPI_BPT7_2023-08-07_b02.a2m,1,56,56,0.2,0.2,6266,0.875,49,1555.8,31.75102041,Medium,3,0.0612244898,,ddG_ML_float,1,aa_seq,VRPI_BPT7_theta0.2_2023-08-07_b02.npy,1,Stability
DMS_ind_65,YNZC_BACSU_Tsuboyama_2023_2JVD_indels,YNZC_BACSU_Tsuboyama_2023_2JVD_indels.csv,YNZC_BACSU,Prokaryote,Bacillus subtilis,MISNAKIARINELAAKAKAGVITEEEKAEQQKLRQEYLK,39,104,-1,manual,Tsuboyama,Mega-scale experimental analysis of protein folding stability in biology and design,2023,10.1038/s41586-023-06328-69,UPF0291 protein YnzC,Stability,cDNA display proteolysis,YNZC_BACSU_2023-08-07_b07.a2m,1,39,39,0.7,0.2,7116,0.974,38,1588.3,41.79736842,Medium,13,0.3421052632,,ddG_ML_float,1,aa_seq,YNZC_BACSU_theta0.2_2023-08-07_b07.npy,1,Stability