,,,,,Present dataset,,,,,,,,,,,,,AG dataset,,,,,,
No.,"Protein
short name",PDB,Class,Fold,Lpdb,L,pH,"Temp
(°C)","Folding
type",ln(kf),"ln(kf)
(25°C)",,ln(kI),ln(ku),"ln(ku)
(25°C)",,βT,pH,"Temp
(°C)","Folding
type",ln(kf),Comments,,
1,Apomyoglobin (Whale) [1],1A6N,α,Globin-like,151,153,6.2,5,N2S,1.1 ,4.5 ,,NA,-3.8 ,5.5 ,,0.72 ,—,—,—,—,,,
2,Pit1 [2],1AU7 (103–160),α,DNA/RNA-binding 3-helical bundle,58,63,5.5,25.0,N2S,9.7 ,,,12.6 ,5.5 ,,,0.74 ,—,—,—,—,,,
3,4-helix bundle protein FRB [3],1AUE (Chain B: 2022–2115),α,Four-helical up-and-down bundle ,94,95,7.5,10,N2S,5.4 ,6.7 ,,NA,-5.2 ,-1.0 ,,0.83 ,"—
 —","—
 —",—,"—
 6.0","Both the AG and our datasets adopted the same reference [3]. The ACPro and our datasets reported the same ln(kf) value, but the Garbuzynskiy dataset reported a different value.",,
4,IM7 [4],1AYI (1–86),α,HIV-1 gp41 fragments ,86,86,7.0,10,N2S,5.7 ,6.9 ,,8.0 ,-0.84 ,3.0 ,,0.90 ,—,25,2S,7.2,"The ln(kf) value reported in the AG dataset was based on the 2S model [5]. However, the N2S nature of this protein is well established [4], so that our reported value is based on the N2S model.",,
5,Apomyoglobin (Horse) [6],1DWR (1–152),α,Globin-like,152,153,6.0,26,N2S,2.9 ,2.9 ,,5.3 ,NA,,,NA,NA,Na,NA,NA,The value of ln(kI) was taken from the rate constant of the fast phase of the bi-phasic refolding kinetics reported.,,
6,Engrailed Homeodomain [7],1ENH,α,DNA/RNA-binding 3-helical bundle,54,54,5.7,25.0,N2S,10.6 ,,,NA,7.6 ,,,0.83 ,—,—,—,—,,,
7,FF domain from human HYPA/FBP11 [8],1UZC (3–71),α,3-Helical bundle,69,71,5.7,25,N2S,8.0 ,,,9.9 ,3.4 ,,,0.91 ,"—
 —","—
 10",—,"—
 7.6","The same experimental group reported the ln(kf) values at 25°C [8] and at 10°C [9]. The ACPro and our datasets reported the value at 25°C, but the Garbuzynskiy dataset reported the value at 10°C.",,
8,ACBP (Bovine) [10],1NTI,α,Acyl-CoA binding protein-like ,86,86,5.3,26,N2S,6.5 ,6.4 ,,9.3 ,-2.7 ,-2.9 ,,0.70 ,—,25,2S,6.96,"The ln(kf) value reported in the AG dataset was based on the 2S model [5]. However, the N2S nature of this protein is well established [10], so that our reported value is based on the N2S model.",,
9,Phage 434 Cro [11],2CRO (1–65),α,Lambda repressor-like DNA-binding domains ,65,71,6.0,20,N2S,3.7 ,4.0 ,,NA,-0.39 ,,,0.91 ,"—
 —","—
 —",—,"5.35
 —","Both the AG and our datasets adopted the same reference [11]. The Garbuzynskiy and our datasets reported the same ln(kf) value, but the ACPro dataset reported a different value.",,
10,X domain of Measles Virus protein [12],1OKS,α,Immunoglobulin/albumin-binding domain-like ,49,49,7.2,25,N2S,6.2 ,,,8.6 ,4.5 ,,,0.84 ,NA,NA,NA,NA,,,
11,Barstar [13],1BTA,α/β,Barstar-like,89,90,7,25,N2S,3.5 ,,,NA,-2.3 ,,,NA,8,—,—,3.47,"We have adopted the data from reference [13], which is more updated than reference [14] adopted by the AG dataset.",,
12,Apoflavodoxin (Anabaena) [15],1FTG (2–169),α/β,Flavodoxin-like,168,169,7.0,25.0,N2S,2.3 ,,,3.4 ,-3.0 ,,,0.55 ,"—
 —","—
 —",2S,"—
 2.8","The ln(kf) value reported in the AG dataset was based on the 2S model [16]. However, the N2S nature of this protein is well established [15], so that our reported value is based on the N2S model. Moreover, the intermediate (I) is mostly off-pathway.",,
13,HIV-1 RNase H [17],1HRH (427–556),α/β,Ribonuclease H-like motif ,130,134,5.5,25,N2S,0.88 ,,,NA,-2.5 ,,,0.64 ,NA,NA,NA,NA,,,
14,N-PGK (Bacillus stearothermophilus) [18],1PHP (1–175),α/β,Phosphoglycerate kinase,175,175,7.5,25,N2S,2.3 ,,,NA,-3.5 ,,,0.84 ,—,—,—,—,,,
15,C-PGK (Bacillus stearothermophilus) [19],1PHP (186–394),α/β,Phosphoglycerate kinase,209,209,7.2,25,N2S,-4.0 ,,,NA,-9.3 ,,,0.51 ,"—
 —","—
 —",—,"−3.44
 —","The Garbuzynskiy and our datasets have adopted the data from reference [19], which is more updated than reference [18] adopted by the ACPro dataset.",,
16,DHFR [20],1RA9,α/β,Dihydrofolate reductase-like ,159,159,7.8,15,N2S,-0.37 ,0.86 ,,1.5 ,-5.2 ,-0.29 ,,0.92 ,"—
 —","—
 —",—,"NA
 −3.20","We have adopted the data from reference [20], which is more updated than reference [21] adopted by the AG dataset.",,
17,Trp-synthase α-subunit (Escherichia coli) [22],1WQ5,α/β,TIM β/α-barrel ,268,268,7,25,N2S,-2.1 ,,,NA,-8.9 ,,,NA,—,—,—,—,,,
18,RNase H (Escherichia coli) [23],2RN2,α/β,Ribonuclease H-like motif,155,155,5.5,25,N2S,-0.3 ,,,NA,-11.4 ,,,0.80 ,"—
 —","—
 —",—,"0.0095
 0.1","We have adopted the data from reference [23] although the AG datasets adopted the data from reference [24], because the ln(kf) value reported in reference [24] is not the value in H2O but in D2O.",,
19,CheY [25],3CHY,α/β,Flavodoxin-like,128,129,7.0,25,N2S,1.0 ,,,NA,-4.4 ,,,0.70 ,—,—,—,—,,,
20,Apoflavodoxin (Desulfovibrio desulfuricans) [26],3F6R (2–148),α/β, Flavodoxin-like,147,148,7,20,N2S,3.5 ,4.0 ,,NA,-5.8 ,-3.6 ,,0.88 ,—,—,—,—,,,
21,sIGPS (Sulfolobus solfataricus) [27],1IGS (27–248),α/β,TIM β/α-barrel ,222,222,7.8,25,N2S,-4.5 ,,,NA,-13.9 ,,,0.79 ,"NA
 —","NA
 —","NA
 —","NA
 —",,,
22,RNase H (Chlorobaculum tepidum) [28],3H08,α/β,Ribonuclease H-like motif,146,146,5.5,25,N2S,1.6 ,,,NA,-13.6 ,,,NA,"NA
 —","NA
 —","NA
 —","NA
 —",,,
23,HisF [29],1THF,α/β,TIM β/α-barrel ,253,253,7.5,25,N2S,-3.2 ,,,-1.4 ,-29.7 ,,,NA,NA,NA,NA,NA,,,
24,GFP [30],1B9C (4–230),α+β,GFP-like,227,238,7.5,25.0,N2S,-2.6 ,,,0.78 ,-23.5 ,,,NA,"—
 NA","—
 NA","—
 NA","−1.59
 NA","Although both the ACPro and our datasets adopted the data from the same reference [30], the ln(kf) value reported is different between the two datasets. Because this protein exhibited multiple parallel pathways of folding, we reported the averaged kf value obtained by the equation:",,
25,Barnase [32],1BNI (3–110),α+β,Microbial ribonucleases,108,110,7.5,25,N2S,2.7 ,,,NA,-12.2 ,,,0.64 ,6.3,—,—,2.56,kf = Σfiki,,
26,p16INK4a [34],2A5E (9–156),α+β,β-Hairpin-α-hairpin repeat ,148,148,7.5,25,N2S,3.5 ,,,NA,-0.22 ,,,0.89 ,—,—,—,—,"where fi and ki are the fractional amplitude and the observed rate constant, respectively, of the ith pathway of folding. On the other hand, the ACPro dataset reported the value of the major pathway of folding. The ln(ku) was taken from reference [31].",,
27,N-HypF [35],1GXT (4–91),α+β,Ferredoxin-like,88,91,5.5,28,N2S,4.4 ,4.3 ,,NA,-3.9 ,-4.7 ,,NA,—,—,—,—,"We have adopted the data from reference [32], which is more updated than reference [33] adopted by the AG dataset.",,
28,Monellin [36],1FA3,α+β,β-β-α Zinc fingers,96,97,7,25,N2S,4.1 ,,,NA,-10.8 ,,,0.89 ,NA,NA,NA,NA,,,
29,T4 Lysozyme [24],1L63 (1–162),α+β, Lysozyme-like ,162,164,6.0,25.0,N2S,3.7 ,,,NA,-12.3 ,,,NA,—,—,—,4.1,,,
30,B1 domain of protein G (Streptococcal sp. group G) [37],1PGB,α+β,Ubiquitin-like,56,57,5,20,N2S,6.4 ,6.6 ,,7.7 ,-2.0 ,-1.2 ,,0.85 ,7.5,25,2S,6.3,"Because this protein exhibited multiple parallel pathways of folding, we reported the averaged kf value obtained by the equation shown in the comment of entry number 24.",,
31,p13suc1 [38],1PUC_mod (2–102),α+β,Cell cycle regulatory proteins,101,114,7.5,25,N2S,4.2 ,,,NA,-4.0 ,,,0.80 ,—,—,—,—,"Although the ACPro and our dataset adopted the data from the same reference [24], the ln(kf) value reported is different between the two datasets. The ACPro dataset reported the value based on the 2S model, however, our value is based on N2S model.",,
32,Ubiquitin [40],1UBQ,α+β,Ubiquitin-like,76,76,5.0,25,N2S,5.3 ,,,7.3 ,-6.7 ,,,0.65 ,—,—,2S,7.33,"The ln(kf) value reported in the AG dataset was based on the 2S model [5]. However, the N2S nature of this protein is well established [37], so that our reported value is based on the N2S model. The value was measured in the presence of 0.4 M sodium sulfate [37].",,
33,Villin 14T [42],2VIL,α+β,Gelsolin-like,126,126,5,37,N2S,4.2 ,4.0 ,,NA,-2.4 ,-6.9 ,,0.78 ,"4.1
 4.1","25
 —",—,"11.9
 5.0","1PUC_mod indicates the monomeric form of p13suc1, and its coordinates were kindly given by J. Schymkowitz [39].",,
34,β-Lactamase (Staphylococcus aureus) [44],3BLM,α+β,β-Lactamase/transpeptidase-like,257,257,7.0,25,N2S,-6.6 ,,,NA,-10.8 ,,,0.79 ,NA,NA,NA,NA,"The ln(kf) value reported in the AG dataset was based on the 2S model [5]. However, the N2S nature of this protein is well established [40], so that our reported value is based on the N2S model. ",,
35,ACYP (Sulfolobus solfataricus) [45],2BJD (12–101),α+β,Ferredoxin-like,90,101,5.5,37,N2S,1.7 ,1.6 ,,NA,-12.0 ,-15.2 ,,0.66 ,NA,NA,NA,NA,"Moreover, the ln(ku) was taken from the following reference  [41].",,
36,UCH-L3 [46],1UCH (5–230),α+β,Cysteine proteinases ,226,230,7.6,25,N2S,-2.6 ,,,NA,-6.9 ,,,0.72 ,NA,NA,NA,NA,"We have adopted the data from reference [42], which is more updated than reference [43] adopted by the AG dataset.",,
37,Ubq-UIM [47],2KDI,α+β,NA,114,114,7.4,25,N2S,2.3 ,,,NA,-9.9 ,,,NA,NA,NA,NA,NA,,,
38,Frataxin (Human) [48],1EKG,α+β,N domain of copper amine oxidase-like ,119,130,7.0,25,N2S,3.5 ,,,NA,-8.9 ,,,0.72 ,NA,NA,NA,NA,,,
39,β-Lactamase (Bacillus licheniformis) [49],4BLM (31–291),α+β,β-Lactamase/transpeptidase-like,261,265,7.0,20,N2S,-4.7 ,-3.9 ,,NA,-13.6 ,-9.6 ,,0.73 ,"—
 NA","—
 NA","—
 NA","−1.24
 NA",,,
40,CD2.d1 [50],1HNG (2–98),β,Immunoglobulin-like β-sandwich,97,98,7.0,25,N2S,1.8 ,,,NA,-5.7 ,,,NA,—,—,"2S
 —",—,,,
41,IL-1β [51],1I1B (3–153),β,β-Trefoil,151,153,7.0,25,N2S,-4.0 ,,,1.4 ,-11.1 ,,,0.93 ,"—
 NA","NA
 NA","—
 NA","—
 NA",,,
42,TI I27 [53],1TIT,β, Immunoglobulin-like β-sandwich,89,89,7.4,25,N2S,3.6 ,,,NA,-7.6 ,,,0.94 ,—,—,"—
 2S",—,"Although the ACPro and our dataset adopted the data from the same reference [49], the ln(kf) value reported is different between the two datasets. The ACPro dataset reported the value based on the 2S analysis using the kinetic folding data between 0.6 and 2 M guanidinium chloride, whereas our reported value is based on the N2S analysis using the data below 0.4 M guanidinium chloride.",,
43,10FNIII [54],1TTG,β,Immunoglobulin-like β-sandwich,94,94,5.0,25,N2S,5.5 ,,,NA,-8.4 ,,,NA,—,—,—,—,"Both the AG and our datasets adopted the same reference [50]. The Garbuzynskiy and our datasets classified the folding type as the N2S type according to the reference, but the ACPro dataset classified it as the 2S type.",,
44,CRABPI (Mouse) [56],1CBI,β,Lipocalins,136,137,8.0,25,N2S,-3.2 ,,,2.6 ,-9.2 ,,,0.72 ,"NA
 —","NA
 —","NA
 —","NA
 —",The ln(ku) was taken from reference [52].,,
45,CRBPII (Rat) [56],1OPA (1–133),β,Lipocalins,133,134,8.0,25,N2S,1.4 ,,,7.6 ,-6.3 ,,,0.79 ,"NA
 —","NA
 —","NA
 —","NA
 —","Both the AG and our datasets adopted the same reference [53]. The ACPro and our datasets classified the folding type as the N2S type according to the reference, but the Garbuzynskiy dataset classified it as the 2S type.",,
46,IFABP [57],1IFC,β,Lipocalins,131,131,7.3,20,N2S,4.3 ,4.7 ,,7.6 ,-5.1 ,-3.1 ,,0.69 ,"NA
 8.0","NA
 25",—,"NA
 3.40",The ln(ku) value was obtained by extrapolation to zero denaturant by using the second-order polynomial of the denaturant (GuSCN) activity. The ln(kf) value was based on the linear extrapolation along GuHCl concentration [55].,,
47,Carbonic anhydrase II (Bovine) [58],1V9E,β,Carbonic anhydrase ,259,260,8.0,20,N2S,-4.4 ,-3.6 ,,-2.4 ,-23.6 ,-19.6 ,,NA,—,—,—,—,,,
48,CRABPII (Mouse) [59],2FS6,β,Lipocalins,137,137,8.0,25,N2S,2.3 ,,,4.7 ,-5.7 ,,,0.83 ,NA,NA,NA,NA,,,
49,Pseudoazurin [60],1ADW,β,Cupredoxin-like,123,123,7.0,15,N2S,0.69 ,1.6 ,,NA,-3.5 ,0.2 ,,0.90 ,"—
 NA","—
 NA","—
 NA","—
 NA","We have adopted the data from reference [57], which is more updated than reference [56] adopted by the Garbuzynskiy dataset.",,
50,SNase [61],2PQE,β,OB-fold,149,149,6.0,20.0,N2S,2.2 ,2.7 ,,4.9 ,-6.3 ,-4.0 ,,NA,5.3,15,—,2.34,,,
51,BABP (Human) [64],5L8I (3–127),β,Lipocalins,125,128,8.0,25,N2S,0.64,,,2.7 ,-8.6 ,,,0.70 ,NA,NA,NA,NA,,,
52,IL-33 [65],2KLL,β,NA,160,160,6.5,25,N2S,-1.4 ,,,NA,-12.3 ,,,0.82 ,NA,NA,NA,NA,,,
,,,,,,,,,,,,,,,,,,,,,,,,
,,,,,,,,,,,,,,,,,,,,,,,,
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