Addiction to nicotine, and possibly other tobacco constituents, is a major factor that contributes to the difficulties smokers face when attempting to quit smoking. Amongst the various subtypes of nicotinic acetylcholine receptors (nAChRs), the
α4
β2 subtype plays an important role in mediating the addiction process. The characterization of human
α4
β2-ligand binding interactions provides a molecular framework for understanding ligand-receptor interactions, rendering insights into mechanisms of nicotine addiction and may furnish a tool for efficiently identifying ligands that can bind the nicotine receptor. Therefore, we constructed a homology model of human
α4
β2 nAChR and performed molecular docking and molecular dynamics (MD) simulations to elucidate the potential human
α4
β2-ligand binding modes for eleven compounds known to bind to this receptor. Residues V96, L97 and F151 of the
α4 subunit and L111, F119 and F121 of the
β2 subunit were found to be involved in hydrophobic interactions while residues S153 and W154 of the α4 subunit were involved in the formation of hydrogen bonds between the receptor and respective ligands. The homology model and its eleven ligand-bound structures will be used to develop a virtual screening program for identifying tobacco constituents that are potentially addictive.
Nicotinic Acetylcholine Receptors Homology Model Ligand-Receptor Interactions1. Introduction
Most smokers continue tobacco use because of their nicotine addiction despite of the well-known adverse health consequences. Of the more than 40 million smokers in the United States, more than 70% of smokers express a desire to quit smoking [1] . Only 3% of smokers who made a quit attempt in the past year were successful [2] [3] .
Nicotine from inhaled smoke rapidly moves into the brain to exert its actions by binding to neuronal nicotinic acetylcholine receptors (nAChRs), which are members of the Cys-loop family of ligand-gated ion channels [4] . To date, 12 neuronal-type nAChR subunits (α2-α10, β2-β4) which can assemble into functional heteromeric or homomeric (α-subunit only) pentamers have been identified [4] - [6] . In the mammalian brain, the α4β2 subtypeisone of the most commonly found nAChRs [7] [8] . It plays important roles in mediating the nicotine reward and addiction process and has been targeted for nicotine addiction treatment [9] . The pocket of α4β2 nAChR, to which various ligands can bind, is situated at the interface of the primary α4 subunit and the complementary β2 subunit [10] [11] . Understanding the molecular interactions between α4β2 nAChR and its ligands could assist development of virtual screening of tobacco constituents with addiction potential through human α4β2 nAChR binding. The three-dimensional (3D) structure of the receptor and its dynamic molecular properties are the key for elucidation of the molecular interactions [12] . However, the 3D structure of a human α4β2 nAChR has yet to be experimentally determined. On the other hand, the 3D crystal structures of acetylcholine binding proteins (AChBPs) from Lymnaea stagnalis (Ls) [13] , Aplysia californica (Ac) [14] , and annelid Capitella teleta (Ct) have been experimentally determined [15] [16] . These AChBPs are structurally similar to the extracellular ligand-binding domain (LBD) of human AChRs and thus serve as an important surrogate for the study of nAChRs. Based on the template of these AChBP X-ray structures, homology structures of the human α4β2 receptor have previously been constructed using the 3D crystal structure data for the AChBPs [11] [17] [18] , although this information has not been made available to the scientific community.
In this study, we constructed a 3D homology model of the extracellular domain of the human α4β2 nAChR (hereafter referred to as human α4β2 nAChR) using the X-ray crystal structure of Ct-AChBP that was determined at a high resolution [19] . The homology structure of human α4β2 nAChR was then further optimized using molecular dynamics (MD) simulations through the exploration of the accessible structural space for the complex [20] [21] . We used the eleven compounds (including compounds contained in tobacco products such as nicotine) that were co-crystalized with nAChRs or AChBPs to elucidate the ligand binding interactions because there are α4β2 binding data for these eleven compounds. These eleven α4β2-ligand complex structures were obtained from molecular docking and further optimized by MD simulations. Examining the binding modes of these compounds in the α4β2 nAChR homology model revealed that hydrophobic interactions between ligands and V96, L97 and F151 of the α4 subunit and L111, F119 and F121 of the β2 subunit and the hydrogen bonds with S153 and W154 of the α4 subunit played key roles for the ligand binding.
The 3D structures of our human α4β2 nAChR homology model, its eleven ligand-bound complexes (supplementary materials which were made publically available), and the elucidated key interactions of these ligands in the α4β2binding pocket, could be used to develop a model for rapid screening of tobacco constituents with addiction potential through human α4β2 nAChR binding.
2. Material and Methods2.1. Study Design and Workflow
The study design and workflow were shown in Figure 1. Briefly, the human α4β2 nAChR (target) sequences were first searched in the PDB using BLAST to select a highly homologous protein (template). The 3D structure of human α4β2 nAChR was then built using homology modeling. After docking the ligand co-crystalized with the template protein, the initial α4β2-ligand complex was then optimized with MD simulations. After MD optimization, the ligand was removed from the complex. The remaining optimized 3D structure of human α4β2
Study design and overall workflow. BLAST was used to search the human α4β2 nAChR sequence against PDB to select a template sequence for homology modeling. The initial homology model was then optimized using MD simulations. Eleven structurally diverse ligands PDB were docked into the optimizedα4β2 and followed by MD simulations
nAChR was used to define a binding grid for subsequent docking analyses. Eleven structurally diverse α4β2 ligands were selected from PDB database and their 3D structures were built and optimized. The optimized ligands were then docked into the α4β2 binding pocket. The α4β2-ligand complexes obtained from docking were further optimized through MD simulations. Finally, the protein-ligand interactions were analyzed by examining the trajectory of MD simulations.
2.2. Homology Modeling
The tertiary structure of a protein is better conserved than its amino acid sequence [22] [23] . Homology modeling is widely used to construct atomic-resolution models for proteins without experimentally determined structures from their amino acid sequences and experimental 3D structures of related homologous proteins [12] [24] . The homology model of human α4β2 nAChR was built using Maestro 9.6 in the Schrödinger Suite [25] . The extracellular ligand-binding domain sequences of the human α4and β2 nAChR subunits were downloaded from UniProt database [26] (α4: P43681(29-242), ACHA4_HUMAN and β2: P17787(26-233), ACHB2_HUMAN). The 3D structure of Ct-AChBPs (UniprotID: I6L8L2) was downloaded from PDB (PDB ID: 4AFH) [19] as the template structure. The template sequence was identified through searching the target human α4β2 sequences in PDB using the BLAST homology searching with default parameters in the Prime 3.4. The target and the template sequences were aligned using the ClustralW method employed in Prime 3.4. The hetero-multimer model was used to predict the secondary structure of human α4β2 dimer. The ligand co-crystalized with the template protein was removed before homology modeling.
2.3. Molecular Docking
There are many structure-activity relationship techniques such as pharmacophore modeling [27] - [29] , comparative molecular field analysis [30] [31] , machine learning methods [32] such as classification tree model [33] and Decision Forest models [34] - [41] based on molecular descriptors [42] that are calculated using the algorithm developed for the expert systems of structure elucidation [43] - [49] , and molecular docking [15] [50] [51] . Molecular docking was used in our previous studies of interactions between ligands and estrogen receptors [52] [53] for prediction of estrogenic activity [54] and endocrine disruptions [53] [55] . A similar docking protocol was adopted in this study. The 3D structure of α4β2 nAChR obtained from homology modeling followed by MD optimizations was prepared using the “protein preparation” tool in the Schrödinger suite [25] . The protein structures were optimized to reach the converged RMSD of 0.3 angstrom (Å) under OPLS_2005 force field. The grid box was defined using “receptor Grid Generation” tool also in the Schrödinger suite. The grid was set as a 15 × 15 × 15 (x × y × z, Å) cubic box around the ligand thus comprising the entire binding pocket.
The two-dimensional (2D) structures of the eleven compounds co-crystalized with AChBPs in PDB are shown in Figure 2. Hereafter, the 3-letter symbols given in Figure 2 will be used to indicate the ligands for simplicity; their names and experimental activity data are also given in Supplementary Table S1. Their 3D structures of the ligands were obtained from the corresponding PDB files of the bound AChBP complexes and further optimized usingLigPrep2.8 tool and OPLS_2005 force field in Schrödinger suite. Epik 2.6 tool of Schrödinger suite was used to generate the ligands ionization states at pH 7.0 ± 2.0. The optimized ligands were docked into the docking grid in the 3D structure of α4β2 using Glide 6.1 tool in the Schrödinger suite with standard precision (SP). The binding poses with the top glide scores were selected and the corresponding complexes were output for subsequent MD simulations.
2.4. MD Simulations
The 3D structure of the human α4β2 homology model and the elevenα4β2-ligand complexes output from molecular docking were optimized using MD simulations. The MD simulations were carried out through AMBER11 [56] using the Amber ff99SB force field [57] and general Amber force field (GAFF) [58] for the receptor and ligands, respectively. AM1-BCC charges [59] were added for the ligands using Antechamber. The topology and parameters of the complexes were constructed by LEAP program [56] . Each complex was solvated with TIP3P water molecules with a 10.0 Å truncated octahedron periodic box. Sodium ions were added to maintain charge neutrality of the systems. The SHAKE algorithm [60] was used to constrain the bonds involving hydrogen. The Particle-mesh Ewald (PME) algorithm [61] was used to deal with the long-range interactions with a 8.0 Å non-bonded interactions cutoff. Prior to MD production simulations, a total of 10,000 steps of minimizations were applied to the entire model system including solvent molecules, followed by 2000 steps of steepest-descent, and subsequently 8000 steps of conjugated gradient minimizations. Two hundred ps (picoseconds) of equilibrations were applied to the system to reach the stable state. The molecular systems were heated in NVT ensemble from 0 to 300 K gradually over 200 ps with weak harmonic potential solutes restrained. After equilibration, 50 and 10 ns (nanoseconds) NPT ensemble MD simulations were performed for the α4β2 homology model and its eleven ligand-bound complexes, respectively, at 1 atm pressure, temperature of 300 K and a time step of 2 fs (fem to seconds). The coordinates of the systems were saved every 10 ps for subsequent trajectory analyses.
Chemical structures of the eleven compounds in the AChBPs complexes collected from PDB and their names used in this paper
3. Results and Discussion3.1. Optimized 3D Structure of Human α4β2 nAChR Homology Model
The sequences of the α4 and β2 subunits of the human nAChRs were queried using the BLAST algorithm to select a template structure in the protein data bank (PDB) to be used for the homology modeling of the human α4β2 nAChR. The α4 subunit sequence was aligned with 811 sequences in PDB (see Supplementary Table S2). The β2 subunit sequence was aligned with 765 sequences in PDB (see Supplementary Table S3). Recent studies have demonstrated that 3D structures can be constructed using homology modeling based on template structures of proteins with 25% or higher sequence identity to the target proteins [62] [63] . The 3D structure of marine annelid Ct-AChBP with PDB ID 4B5D at a resolution of 2.2 Å has been successfully used previously as the template for the homology modeling of α4β2 nAChR to study the structural determinants of ligand recognition inhuman α4β2nAChR [11] . The crystal structure of Ct-AChBP with a higher resolution of 1.88 Å had been determined recently and deposited in PDB (ID: 4AFH). The α4 and β2 subunit sequences were found to have 31% and 28% sequence identities, respectively, with the 4AFH structure. Therefore, this was used as the template to construct the homology model of the human α4β2 nAChR.
The final alignment between the template and the target with the secondary structure prediction is shown in Figure 3 (the first three residues of α4 subunit were not included in the homology modeling because they could not be aligned to the template sequence).Most of the secondary structures including the disulphide bridges aligned well between the template and the target. The core residues located at the dimer interface, include residues Y98, W154 and Y195from the α4 subunit and residues W57, V111, F119 and L121 from theβ2 subunit. These core residues played key roles in α4β2-ligand interactions, which is consistent with the interactions between the human α4β2 nAChR and the nicotine addiction treatment drug varenicline derived from analysis using the structure-guided mutagenesis [19] .
The 3D structure of the human α4β2 dimer shown in Figure 4(a) was constructed by homology modeling using the structure of Ct-AChBP (Figure 4(b)) as the template. The homology model superimposed well with the template structure as depicted in Figure 4(c). Consistent with our expectation, the α helices and β sheets in both the template and target structures were more conserved compared to the loops. Our homology model was
Sequence alignment result between the human α4β2 nAChR and the template Ct-AChBP. The predicted secondary structure from Ct-AChBP is also shown: the tube represents the helix; arrows indicate strands; and dotted lines depict loops. The identical residues are highlighted in colors according to the property of the corresponding query residue in the alignment to depict the location of charged (purple: positive charge; red: negative charge), aromatics (brown), polar (cyan), hydrophobic (green) and special (yellow: cysteine; grey: proline) query residues. The residues that interact with the ligands are marked with black boxes
Homology model of the human α4β2 nAChR. Template structure Ct-AChBP color coded in red (a) and the homology model is shown in solid blue ribbons for α4 and green ribbons for β2 (b). Superimposition of the homology model with the template is depicted in (c).
compared with the homology model constructed using a template structure of the same protein with a slightly lower resolution [11] . The overall structure and key structural features were similar.
More often than not, initial 3D structures from homology modeling were further optimized using MD simulations [64] . MD simulations are a technique widely applied to study protein folding, protein dynamics and protein-ligand interactions [20] [21] [65] - [69] . Considering the ligand impact on the residues conformations in the binding pocket [20] of the α4β2 homology model, MD simulations were performed in the presence of the ligand (LOB) (co-crystallized in the Ct-AChBP template protein). The root mean square deviation (RMSD) values of the optimized human α4β2-LOB complex structure were calculated to characterize the dynamic property of the molecular system during the MD simulations and were plotted in Figure 5(a). The molecular system reached stable states during the 50 ns simulations. The RSMD value of human α4β2 backbone atoms was stabilized at 3.5 Å after 30 ns simulations and the ligand fluctuated stably from 43 ns with a RMSD of 2.0 Å. The optimized human α4β2 homology model is available upon request.
The root-mean-square fluctuations (RMSF) of residues of the human α4β2 homology model during the MD simulations were calculated to characterize the mobility of the individual residues and plotted in Figure 5(b). As expected, the N-terminal alpha helix and the 10 beta strands are more rigid than the loops and, thus, had smaller RMSF values. The peaks in Figure 5(b) indicated larger RMSF values for the residues in the loops: 130 - 140, 170 - 180, 260 - 270, 280 - 290, 340 - 350 and 400 - 410.
The Ramachandran plot (Figure 5(c)) showed that 99.3% of the residues in the optimized α4β2 structure were in the favorable regions-higher than the percentage of residues (96.2%, see Figure 5(d)) in the initial homology model without MD simulations―thus indicating that the homology model of human α4β2 was optimized to an energy stable state.
To examine the structural changes of the α4β2 homology model following the MD simulations, the structures before and after the optimization were superimposed together and depicted in Figure 5(e). The two structures superimposed well with each other, especially for the β-sandwich cores, providing evidence that the homology model is a reasonably stable structure. On the other hand, much larger changes in the loop regions (some near the ligand binding site) were observed during the simulations points towards a better characterized ligand binding pocket for the α4β2. This indicates that optimization using MD simulations is a necessary step for the structural refinement of the human α4β2 homology model.
To examine the binding interactions between the human α4β2 homology model and the cognate ligand in the template, LOB, the zoomed-in view of the receptor ligand binding pocket is shown in Figure 5(f). The tertiary amine of LOB was stabilized through the π-cation interactions with the conserved aromatic residues W154 and Y195. The benzene ring of LOB also interacted with the piperidine ring of residue W154through π-π interactions. The receptor-ligand hydrophobic interactions mainly involved residues V96 and L97 from the α4 subunit and V111, F119 and L121 from the β2 subunit. The binding interactions observed for the human α4β2 homology model were similar to those between LOB and Ct-AChBP elucidated from the X-ray structure [19] .
3.2. Ligands Docking
Site Map [70] was used to generate the potential ligand binding site of the extracellular domains of human
Optimization of the homology model by MD simulations. The RMSD values (y-axis) for atoms of protein backbone (blue line) and ligand (red line) during the optimization (x-axis) were plotted in (a). The RMSF values (y-axis) of individual residues (x-axis) were given in (b). Ramachandran plots of the optimized and initial homology models were given in (c) and (d), respectively. The homology models before (blue ribbon) and after (red ribbon) the MD simulations were superimposed (e). The binding pocket was illustrated by a zoomed surface representation (f). The core residues were color coded in blue. The arrows indicated the hydrophobic moment (residues colored in red). The red lines depicted the π-π interaction and the purple lines for the π-cation interaction.
α4β2n AChR homology model. The eleven ligands shown in Figure 2 were docked in the receptor model. For each ligand, the lowest docking score and its corresponding docking pose in the receptor were selected and output for subsequent analysis. The docking poses of all eleven ligands in the human α4β2 nAChR homology model are shown in Figure 6 and Supplementary Figure S1. The ligand binding site composed of the α4 subunit residues V96, L97, Y98, S153, W154, Y195 and Y202 and the β2 subunit residues W57, V111, F119, L121 and F157. The orientations of the eleven ligands were similar i.e. the hydrophobic parts of all the ligands extended into the major surface of the binding pocket. Aromatic and hydrophobic interactions were the major contributions to the binding.
3.3. Ligand Binding Interactions
To elucidate the binding modes of the eleven ligands in the human α4β2 receptor, the complexes of α4β2 bound with the ligands resulting from the molecular docking were again optimized using MD simulations [71] [72] . MD simulations were carried out on the eleven human α4β2-ligand complexes obtained from molecular docking and the results were given in Figure 7. The RMSD values generated by the MD simulations for the proteins (Figure 7(a)) and the ligands (Figure 7(b)) indicated the complexes reached relatively stable states. In more detail, for the structures of α4β2 homology model bound with IM4, 09O, 09R, LOB and QMR ligands, the irreceptor RMSD values stabilized around 2.0 Å after 6 ns MD simulations. On the other hand, the structures of α4β2 homology model bound with NCT, 09P, 09Q, 09S, SW4 and C5E continued to show small fluctuations of the receptor (RMSD values of ~2.5 Å) after 6 ns MD simulations. Furthermore, as expected, the rigid ligands (C5E and QMR) remained highly stable as evidenced by a low RMSD of 0.3 Å during the whole simulations; the ligands with one rotatable bond (NCT and 09R) had slightly larger fluctuations of ~1 Å RMSD; the ligands with multiple rotatable bonds (e.g. 09Q, 09S, and SW4) had larger fluctuations in the simulations. In other words, the more rotatable bonds in a ligand, the larger the RMSD. Interestingly, LOB has six rotatable bonds but its conformation only changed slightly with RMSD values of about 0.5 Å during the simulations. This indicates that the fluctuation of a ligand in simulations depends not only on the ligand structure but also on its binding environment [73] [74] .
To elucidate the binding interactions of the eleven ligands, the corresponding receptor-ligand complexes from the final frame of the MD simulations were examined. The binding mode of NCT was shown in Figure 8(a). On the α4 subunit side, NCT had extensive binding with residues Y98, S153, W154 and Y202 through hydrogen bond, π-π and π-cation interactions. It also bound with the hydrophobic residues V96, L97 and F151 through hydrophobic interactions. On the β2 subunit side, the ligand bound with W57 and L121 through π-sigma interactions and hydrophobic interactions. The receptor-ligand interactions observed for the human α4β2 nAChR are consistent with the ones found in AChBP crystal complex of the same ligand [72] .
The binding interactions between α4β2 and IM4 were shown in Figure 8(b). The pyridine ring of IM4 interacted with α4β2 through the π-π interactions with residue Y195 of the α4 subunit and the hydrophobic interact-
Docking poses of the eleven ligands in the binding site of human α4β2
Trajectory analyses of MD simulations. The RMSD values of the protein backbones (a) and the ligands (b) were plotted again the time. The complexes are indicated by the ligand abbreviations using different colors shown in the legends.
tions with residues L111, L119 and F172 of the β2 subunit. The binding mode of IM4 in the human α4β2 elucidated in this study was similar to the one observed in the crystal structure of the Ls-AChBP complex bound with IM4 [74] .
Ligands 09O, 09P, 09Q, 09R and 09S share a structural fragment in which a diazepane and a pyridine are connected by a single bond. Their binding interactions with the human α4β2 homology model are depicted in Figures 8(c)-(g), respectively. Although the binding modes of these ligands in the receptor were not the same due to the structural elements attached to the common fragment, the binding interactions formed were similar. These interactions were hydrogen bond, hydrophobic, π-π and π-cation interactions. The π-π and π-cation interactions mainly occurred between the diazepane and pyridine of the ligands and the residues W154, Y195, Y202, V96, L97 and Y98 of the α4 subunit and the residues W57, L121, F172 and F119 of the β2 subunit. These binding interactions as elucidated from our MD simulations are consistent with the ones identified in the AChBP X-ray complex structures bound with the respective ligands [75] .
The ligand binding mode ofSW4is illustrated in Figure 8(h). SW4 forms a hydrogen bond with residue Y196 of the α4 subunit and had π-cation and hydrophobic interactions with residues V111, F119 and F121 of the β2 subunit. These binding interactions were observed in the x-ray crystal structure of the Ct-AChBP bound with SW4 [11] .
Ligands binding modes. Binding pocket surfaces are colored in the interpolated charge. The core residues are in cyan and the arrows indicated the hydrophobic moments (residues were labelled in red).The red lines depicted the π-π interaction and the purple lines for the π-cation interaction. The ligands in the complexes: NCT (a); IM4 (b); 09O (c); 09P (d); 09Q (e); 09R (f); 09S (g); LOB (h); QMR (i); SW4 (j) and C5E (k)
Figure 8(i) depicts the binding mode ofC5E.The ligand bound with the human α4β2 through hydrogen bonds, π-cation interactions, π-sigma interactions and hydrophobic interactions with the residues V96, L97, F151, S153, W154 and Y202 of the α4 subunit. It also has π-π interactions and hydrophobic interactions with the residues W57 and L121 of the β2 subunit. The binding interaction was confirmed in the x-ray structure of Ac-AChBP complex bound with C5E [76] .
The binding mode of QMR is shown in Figure 8(j). This highly rigid ligand bound to the binding pocket through π-π interactions, π-cation interactions, π-sigma interactions and hydrophobic interactions with residues V96, L97, F151, Y195 and Y202 of the α4 subunit and the side chains of residues W57, F119 and F121 of the β2 subunit. These binding interactions were in a good agreement with the Ac-AChBP complex bound with the same ligand [76] .
The binding mode of LOB is given in Figure 8(k). LOB interacted with α4β2 through π-cation interactions with residues W154, Y195 and Y202 and π-π interactions with W154 of the α4 subunit. It also had hydrophobic interactions with residues V96, L97 and F151 of the α4 subunit and residues V111, F119 and L121of the β2 subunit. These molecular interactions were similar to those observed in x-ray structure of LOB-CtAChBP complex [19] .
The binding interactions between the human α4β2 homology model and the eleven ligands were summarized in the Table 1. In general, the hydrophobic interactions mainly involved residues V96, L97 and F151 of the α4 subunit and residues L111, F119 and F121 of the β2 subunit. The π-π, π-cation, and π-sigma interactions were mainly from residues Y98, W154, Y195 and Y202 of the α4 subunit and from residue W57 of the β2 subunit.
The hydrogen bonds were formed between the ligands and residues S153 and W154 of theα4 subunit. It is worth noting that residues W154 and W57 interacted with most of the eleven ligands and played key roles in the binding as confirmed in the X-ray structures of the AChBPs bound with the respective ligands [19] [77] . It is worth noting that in this study, we focus on the binding of these ligands to the human α4β2 nAChR i.e. the pre-requisite step for chemicals to elicit subsequent pharmacological actions on the body-indeed, the ligands considered in this study display different pharmacology (various degree of activation and desensitization) upon binding to the human α4β2 nAChR. However, this aspect is out of the scope of our study.
4. Conclusion
The human α4β2 nAChR plays an important role in nicotine addiction and could be used for screening tobacco constituents with addiction potential. Determining the 3D structure of the human α4β2 nAChR and elucidating its ligand binding interactions would help with screening for tobacco constituents with nicotine receptor binding activity and addictive properties. This type of screening will result in a rank order of tobacco constituents that have addiction potential and may inform regulation of tobacco products. As there are no 3D structures of human α4β2 nAChR either alone or bound with ligands available to researchers today, we constructed a homology model of the human α4β2 nAChR based on the X-ray structure of the Ct-AChBP complex bound with LOB as an alternative approach for gaining insights into ligand binding characteristics of the human α4β2 nAChR. Based on the homology model of the human α4β2 nAChR, we further characterized the ligand binding interactions of human α4β2 nAChR by docking eleven ligands to the receptor followed by MD simulations. Our results provide molecular details into the ligand binding interactions with human α4β2 nAChR homology model and a modeling method for identifying nicotine receptor binding compounds that are potentially addictive.
Acknowledgements
This project was funded by the Center for Tobacco Products at the U.S. Food and Drug Administration. This research was supported in part by an appointment to the Research Participation Program at the National Center for Toxicological Research (Hui Wen Ng and Hao Ye) administered by the Oak Ridge Institute for Science and Education through an interagency agreement between the U.S. Department of Energy and the U.S. Food and Drug Administration. This publication represents the views of the author(s) and does not represent CTP position or policy.
Author Contributions
H.H. and M.O. conceived and designed the experiments; M.S. and H.W.N. performed the experiments; M.S., H.W.N., H.L., H.Y. and W.G. analyzed the data; M.S., M.S., W.T. and H.H. wrote the paper.
Conflicts of Interest
The authors declare no conflict of interest.
Cite this paper
Shu Mao,Hui Wen Ng,Michael Orr,Heng Luo,Hao Ye,Weigong Ge,Weida Tong,Huixiao Hong, (2016) Homology Model and Ligand Binding Interactions of the Extracellular Domain of the Human α4β2 Nicotinic Acetylcholine Receptor. Journal of Biomedical Science and Engineering,09,41-100. doi: 10.4236/jbise.2016.91005
Results of search a4 subunit on the PDB. ID consists of PDB ID (the first 4 letters) and the subunit (the last letter)
ID
Score
Expect
Identity
Positives
Gaps
Resolution
2WN9_A
87.8
1.20E−20
28%
43%
2%
1.75
2WN9_B
87.8
1.20E−20
28%
43%
2%
1.75
2WN9_C
87.8
1.20E−20
28%
43%
2%
1.75
2WN9_D
87.8
1.20E−20
28%
43%
2%
1.75
2WN9_E
87.8
1.20E−20
28%
43%
2%
1.75
2PGZ_A
87.8
1.10E−20
28%
43%
2%
1.76
2PGZ_B
87.8
1.10E−20
28%
43%
2%
1.76
2PGZ_C
87.8
1.10E−20
28%
43%
2%
1.76
2PGZ_D
87.8
1.10E−20
28%
43%
2%
1.76
2PGZ_E
87.8
1.10E−20
28%
43%
2%
1.76
2WNJ_A
87.8
1.20E−20
28%
43%
2%
1.8
2WNJ_B
87.8
1.20E−20
28%
43%
2%
1.8
2WNJ_C
87.8
1.20E−20
28%
43%
2%
1.8
2WNJ_D
87.8
1.20E−20
28%
43%
2%
1.8
2WNJ_E
87.8
1.20E−20
28%
43%
2%
1.8
4AFH_A
99.8
6.30E−25
31%
48%
7%
1.88
4AFH_B
99.8
6.30E−25
31%
48%
7%
1.88
4AFH_C
99.8
6.30E−25
31%
48%
7%
1.88
4AFH_D
99.8
6.30E−25
31%
48%
7%
1.88
4AFH_E
99.8
6.30E−25
31%
48%
7%
1.88
2Y7Y_A
89.4
3.00E−21
29%
43%
2%
1.9
2Y7Y_B
89.4
3.00E−21
29%
43%
2%
1.9
2Y7Y_C
89.4
3.00E−21
29%
43%
2%
1.9
2Y7Y_D
89.4
3.00E−21
29%
43%
2%
1.9
2Y7Y_E
89.4
3.00E−21
29%
43%
2%
1.9
2XYS_A
89.4
3.00E−21
29%
43%
2%
1.909
2XYS_B
89.4
3.00E−21
29%
43%
2%
1.909
2XYS_C
89.4
3.00E−21
29%
43%
2%
1.909
2XYS_D
89.4
3.00E−21
29%
43%
2%
1.909
2XYS_E
89.4
3.00E−21
29%
43%
2%
1.909
3C84_A
87.8
1.00E−20
28%
43%
2%
1.94
3C84_B
87.8
1.00E−20
28%
43%
2%
1.94
3C84_C
87.8
1.00E−20
28%
43%
2%
1.94
3C84_D
87.8
1.00E−20
28%
43%
2%
1.94
3C84_E
87.8
1.00E−20
28%
43%
2%
1.94
2QC1_B
217.6
1.90E−70
52%
66%
0%
1.94
2YMD_A
90.1
1.30E−21
28%
42%
2%
1.96
2YMD_B
90.1
1.30E−21
28%
42%
2%
1.96
2YMD_C
90.1
1.30E−21
28%
42%
2%
1.96
2YMD_D
90.1
1.30E−21
28%
42%
2%
1.96
2YMD_E
90.1
1.30E−21
28%
42%
2%
1.96
2YMD_F
90.1
1.30E−21
28%
42%
2%
1.96
2YMD_G
90.1
1.30E−21
28%
42%
2%
1.96
2YMD_H
90.1
1.30E−21
28%
42%
2%
1.96
2YMD_I
90.1
1.30E−21
28%
42%
2%
1.96
2YMD_J
90.1
1.30E−21
28%
42%
2%
1.96
2BJ0_A
60.5
2.50E−11
22%
43%
3%
2
2BJ0_B
60.5
2.50E−11
22%
43%
3%
2
2BJ0_C
60.5
2.50E−11
22%
43%
3%
2
2BJ0_D
60.5
2.50E−11
22%
43%
3%
2
2BJ0_E
60.5
2.50E−11
22%
43%
3%
2
1A05_A
30.4
1.2
26%
43%
21%
2
1A05_B
30.4
1.2
26%
43%
21%
2
4AFG_A
99.8
6.30E−25
31%
48%
7%
2
4AFG_B
99.8
6.30E−25
31%
48%
7%
2
4AFG_C
99.8
6.30E−25
31%
48%
7%
2
4AFG_D
99.8
6.30E−25
31%
48%
7%
2
4AFG_E
99.8
6.30E−25
31%
48%
7%
2
2BYN_A
87.8
1.00E−20
28%
43%
2%
2.02
2BYN_B
87.8
1.00E−20
28%
43%
2%
2.02
2BYN_C
87.8
1.00E−20
28%
43%
2%
2.02
2BYN_D
87.8
1.00E−20
28%
43%
2%
2.02
2BYN_E
87.8
1.00E−20
28%
43%
2%
2.02
2BYS_A
87.8
1.00E−20
28%
43%
2%
2.05
2BYS_B
87.8
1.00E−20
28%
43%
2%
2.05
2BYS_C
87.8
1.00E−20
28%
43%
2%
2.05
2BYS_D
87.8
1.00E−20
28%
43%
2%
2.05
2BYS_E
87.8
1.00E−20
28%
43%
2%
2.05
2BYS_F
87.8
1.00E−20
28%
43%
2%
2.05
2BYS_G
87.8
1.00E−20
28%
43%
2%
2.05
2BYS_H
87.8
1.00E−20
28%
43%
2%
2.05
2BYS_I
87.8
1.00E−20
28%
43%
2%
2.05
2BYS_J
87.8
1.00E−20
28%
43%
2%
2.05
2XYT_A
89.4
3.00E−21
29%
43%
2%
2.05
2XYT_B
89.4
3.00E−21
29%
43%
2%
2.05
2XYT_C
89.4
3.00E−21
29%
43%
2%
2.05
2XYT_D
89.4
3.00E−21
29%
43%
2%
2.05
2XYT_E
89.4
3.00E−21
29%
43%
2%
2.05
2XYT_F
89.4
3.00E−21
29%
43%
2%
2.05
2XYT_G
89.4
3.00E−21
29%
43%
2%
2.05
2XYT_H
89.4
3.00E−21
29%
43%
2%
2.05
2XYT_I
89.4
3.00E−21
29%
43%
2%
2.05
2XYT_J
89.4
3.00E−21
29%
43%
2%
2.05
2BYP_A
88.2
6.80E−21
28%
43%
2%
2.07
2BYP_B
88.2
6.80E−21
28%
43%
2%
2.07
2BYP_C
88.2
6.80E−21
28%
43%
2%
2.07
2BYP_D
88.2
6.80E−21
28%
43%
2%
2.07
2BYP_E
88.2
6.80E−21
28%
43%
2%
2.07
3PEO_A
87.8
1.20E−20
28%
43%
2%
2.1
3PEO_B
87.8
1.20E−20
28%
43%
2%
2.1
3PEO_C
87.8
1.20E−20
28%
43%
2%
2.1
3PEO_D
87.8
1.20E−20
28%
43%
2%
2.1
3PEO_E
87.8
1.20E−20
28%
43%
2%
2.1
3PEO_F
87.8
1.20E−20
28%
43%
2%
2.1
3PEO_G
87.8
1.20E−20
28%
43%
2%
2.1
3PEO_H
87.8
1.20E−20
28%
43%
2%
2.1
3PEO_I
87.8
1.20E−20
28%
43%
2%
2.1
3PEO_J
87.8
1.20E−20
28%
43%
2%
2.1
1UW6_A
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_B
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_C
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_D
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_E
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_F
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_G
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_H
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_I
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_J
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_K
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_L
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_M
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_N
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_O
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_P
63.5
2.20E−12
26%
41%
7%
2.2
1UW6_Q
63.5
2.20E−12
26%
41%
7%
2.2
1UX2_A
63.5
2.40E−12
26%
41%
7%
2.2
1UX2_B
63.5
2.40E−12
26%
41%
7%
2.2
1UX2_C
63.5
2.40E−12
26%
41%
7%
2.2
1UX2_D
63.5
2.40E−12
26%
41%
7%
2.2
1UX2_E
63.5
2.40E−12
26%
41%
7%
2.2
1UX2_F
63.5
2.40E−12
26%
41%
7%
2.2
1UX2_G
63.5
2.40E−12
26%
41%
7%
2.2
1UX2_H
63.5
2.40E−12
26%
41%
7%
2.2
1UX2_I
63.5
2.40E−12
26%
41%
7%
2.2
1UX2_J
63.5
2.40E−12
26%
41%
7%
2.2
2WNC_A
87.8
1.00E−20
28%
43%
2%
2.2
2WNC_B
87.8
1.00E−20
28%
43%
2%
2.2
2WNC_C
87.8
1.00E−20
28%
43%
2%
2.2
2WNC_D
87.8
1.00E−20
28%
43%
2%
2.2
2WNC_E
87.8
1.00E−20
28%
43%
2%
2.2
4B5D_A
99.8
6.30E−25
31%
48%
7%
2.2
4B5D_B
99.8
6.30E−25
31%
48%
7%
2.2
4B5D_C
99.8
6.30E−25
31%
48%
7%
2.2
4B5D_D
99.8
6.30E−25
31%
48%
7%
2.2
4B5D_E
99.8
6.30E−25
31%
48%
7%
2.2
2C9T_A
89.4
3.00E−21
29%
43%
2%
2.25
2C9T_B
89.4
3.00E−21
29%
43%
2%
2.25
2C9T_C
89.4
3.00E−21
29%
43%
2%
2.25
2C9T_D
89.4
3.00E−21
29%
43%
2%
2.25
2C9T_E
89.4
3.00E−21
29%
43%
2%
2.25
2C9T_F
89.4
3.00E−21
29%
43%
2%
2.25
2C9T_G
89.4
3.00E−21
29%
43%
2%
2.25
2C9T_H
89.4
3.00E−21
29%
43%
2%
2.25
2C9T_I
89.4
3.00E−21
29%
43%
2%
2.25
2C9T_J
89.4
3.00E−21
29%
43%
2%
2.25
3IGQ_A
31.6
0.3
25%
45%
9%
2.3
3IGQ_B
31.6
0.3
25%
45%
9%
2.3
3IGQ_C
31.6
0.3
25%
45%
9%
2.3
3IGQ_D
31.6
0.3
25%
45%
9%
2.3
3IGQ_E
31.6
0.3
25%
45%
9%
2.3
3IGQ_F
31.6
0.3
25%
45%
9%
2.3
4ALX_A
63.5
2.80E−12
25%
41%
7%
2.3
4ALX_B
63.5
2.80E−12
25%
41%
7%
2.3
4ALX_C
63.5
2.80E−12
25%
41%
7%
2.3
4ALX_D
63.5
2.80E−12
25%
41%
7%
2.3
4ALX_E
63.5
2.80E−12
25%
41%
7%
2.3
4ALX_F
63.5
2.80E−12
25%
41%
7%
2.3
4ALX_G
63.5
2.80E−12
25%
41%
7%
2.3
4ALX_H
63.5
2.80E−12
25%
41%
7%
2.3
4ALX_I
63.5
2.80E−12
25%
41%
7%
2.3
4ALX_J
63.5
2.80E−12
25%
41%
7%
2.3
4DBM_A
87.8
1.10E−20
28%
43%
2%
2.3
4DBM_B
87.8
1.10E−20
28%
43%
2%
2.3
4DBM_C
87.8
1.10E−20
28%
43%
2%
2.3
4DBM_D
87.8
1.10E−20
28%
43%
2%
2.3
4DBM_E
87.8
1.10E−20
28%
43%
2%
2.3
3U8L_A
63.5
2.00E−12
26%
41%
7%
2.32
3U8L_B
63.5
2.00E−12
26%
41%
7%
2.32
3U8L_C
63.5
2.00E−12
26%
41%
7%
2.32
3U8L_D
63.5
2.00E−12
26%
41%
7%
2.32
3U8L_E
63.5
2.00E−12
26%
41%
7%
2.32
3U8L_F
63.5
2.00E−12
26%
41%
7%
2.32
3U8L_G
63.5
2.00E−12
26%
41%
7%
2.32
3U8L_H
63.5
2.00E−12
26%
41%
7%
2.32
3U8L_I
63.5
2.00E−12
26%
41%
7%
2.32
3U8L_J
63.5
2.00E−12
26%
41%
7%
2.32
3SIO_A
85.9
4.80E−20
28%
42%
2%
2.32
3SIO_B
85.9
4.80E−20
28%
42%
2%
2.32
3SIO_C
85.9
4.80E−20
28%
42%
2%
2.32
3SIO_D
85.9
4.80E−20
28%
42%
2%
2.32
3SIO_E
85.9
4.80E−20
28%
42%
2%
2.32
3SIO_F
85.9
4.80E−20
28%
42%
2%
2.32
3SIO_G
85.9
4.80E−20
28%
42%
2%
2.32
3SIO_H
85.9
4.80E−20
28%
42%
2%
2.32
3SIO_I
85.9
4.80E−20
28%
42%
2%
2.32
3SIO_J
85.9
4.80E−20
28%
42%
2%
2.32
3U8J_A
63.5
2.00E−12
26%
41%
7%
2.35
3U8J_B
63.5
2.00E−12
26%
41%
7%
2.35
3U8J_C
63.5
2.00E−12
26%
41%
7%
2.35
3U8J_D
63.5
2.00E−12
26%
41%
7%
2.35
3U8J_E
63.5
2.00E−12
26%
41%
7%
2.35
3U8J_F
63.5
2.00E−12
26%
41%
7%
2.35
3U8J_G
63.5
2.00E−12
26%
41%
7%
2.35
3U8J_H
63.5
2.00E−12
26%
41%
7%
2.35
3U8J_I
63.5
2.00E−12
26%
41%
7%
2.35
3U8J_J
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_A
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_B
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_C
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_D
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_E
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_F
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_G
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_H
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_I
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_J
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_K
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_L
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_M
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_N
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_O
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_P
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_Q
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_R
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_S
63.5
2.00E−12
26%
41%
7%
2.35
3U8N_T
63.5
2.00E−12
26%
41%
7%
2.35
2X00_A
87.8
1.20E−20
28%
43%
2%
2.4
2X00_B
87.8
1.20E−20
28%
43%
2%
2.4
2X00_C
87.8
1.20E−20
28%
43%
2%
2.4
2X00_D
87.8
9.60E−21
28%
43%
2%
2.4
2X00_E
87.8
1.20E−20
28%
43%
2%
2.4
2BR8_A
89.4
3.00E−21
29%
43%
2%
2.4
2BR8_B
89.4
3.00E−21
29%
43%
2%
2.4
2BR8_C
89.4
3.00E−21
29%
43%
2%
2.4
2BR8_D
89.4
3.00E−21
29%
43%
2%
2.4
2BR8_E
89.4
3.00E−21
29%
43%
2%
2.4
2UZ6_A
89.4
3.00E−21
29%
43%
2%
2.4
2UZ6_B
89.4
3.00E−21
29%
43%
2%
2.4
2UZ6_C
89.4
3.00E−21
29%
43%
2%
2.4
2UZ6_D
89.4
3.00E−21
29%
43%
2%
2.4
2UZ6_E
89.4
3.00E−21
29%
43%
2%
2.4
2UZ6_F
89.4
3.00E−21
29%
43%
2%
2.4
2UZ6_G
89.4
3.00E−21
29%
43%
2%
2.4
2UZ6_H
89.4
3.00E−21
29%
43%
2%
2.4
2UZ6_I
89.4
3.00E−21
29%
43%
2%
2.4
2UZ6_J
89.4
3.00E−21
29%
43%
2%
2.4
2YME_A
92.4
2.00E−22
29%
43%
2%
2.4
2YME_B
92.4
2.00E−22
29%
43%
2%
2.4
2YME_C
92.4
2.00E−22
29%
43%
2%
2.4
2YME_D
92.4
2.00E−22
29%
43%
2%
2.4
2YME_E
92.4
2.00E−22
29%
43%
2%
2.4
2YME_F
92.4
2.00E−22
29%
43%
2%
2.4
2YME_G
92.4
2.00E−22
29%
43%
2%
2.4
2YME_H
92.4
2.00E−22
29%
43%
2%
2.4
2YME_I
92.4
2.00E−22
29%
43%
2%
2.4
2YME_J
92.4
2.00E−22
29%
43%
2%
2.4
2XNV_A
90.9
9.90E−22
27%
44%
2%
2.44
2XNV_B
90.9
9.90E−22
27%
44%
2%
2.44
2XNV_C
90.9
9.90E−22
27%
44%
2%
2.44
2XNV_D
90.9
9.90E−22
27%
44%
2%
2.44
2XNV_E
90.9
9.90E−22
27%
44%
2%
2.44
2XNV_F
90.9
9.90E−22
27%
44%
2%
2.44
2XNV_G
90.9
9.90E−22
27%
44%
2%
2.44
2XNV_H
90.9
9.90E−22
27%
44%
2%
2.44
2XNV_I
90.9
9.90E−22
27%
44%
2%
2.44
2XNV_J
90.9
9.90E−22
27%
44%
2%
2.44
3PMZ_A
87.8
1.00E−20
28%
43%
2%
2.44
3PMZ_B
87.8
1.00E−20
28%
43%
2%
2.44
3PMZ_C
87.8
1.00E−20
28%
43%
2%
2.44
3PMZ_D
87.8
1.00E−20
28%
43%
2%
2.44
3PMZ_E
87.8
1.00E−20
28%
43%
2%
2.44
3PMZ_F
87.8
1.00E−20
28%
43%
2%
2.44
3PMZ_G
87.8
1.00E−20
28%
43%
2%
2.44
3PMZ_H
87.8
1.00E−20
28%
43%
2%
2.44
3PMZ_I
87.8
1.00E−20
28%
43%
2%
2.44
3PMZ_J
87.8
1.00E−20
28%
43%
2%
2.44
2BYR_A
87.8
1.00E−20
28%
43%
2%
2.45
2BYR_B
87.8
1.00E−20
28%
43%
2%
2.45
2BYR_C
87.8
1.00E−20
28%
43%
2%
2.45
2BYR_D
87.8
1.00E−20
28%
43%
2%
2.45
2BYR_E
87.8
1.00E−20
28%
43%
2%
2.45
2BYR_F
87.8
1.00E−20
28%
43%
2%
2.45
2BYR_G
87.8
1.00E−20
28%
43%
2%
2.45
2BYR_H
87.8
1.00E−20
28%
43%
2%
2.45
2BYR_I
87.8
1.00E−20
28%
43%
2%
2.45
2BYR_J
87.8
1.00E−20
28%
43%
2%
2.45
3U8K_A
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_B
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_C
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_D
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_E
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_F
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_G
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_H
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_I
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_J
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_K
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_L
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_M
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_N
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_O
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_P
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_Q
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_R
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_S
63.5
2.00E−12
26%
41%
7%
2.47
3U8K_T
63.5
2.00E−12
26%
41%
7%
2.47
3C79_A
87.8
1.00E−20
28%
43%
2%
2.48
3C79_B
87.8
1.00E−20
28%
43%
2%
2.48
3C79_C
87.8
1.00E−20
28%
43%
2%
2.48
3C79_D
87.8
1.00E−20
28%
43%
2%
2.48
3C79_E
87.8
1.00E−20
28%
43%
2%
2.48
1UV6_A
63.5
2.00E−12
26%
41%
7%
2.5
1UV6_B
63.5
2.00E−12
26%
41%
7%
2.5
1UV6_C
63.5
2.00E−12
26%
41%
7%
2.5
1UV6_D
63.5
2.00E−12
26%
41%
7%
2.5
1UV6_E
63.5
2.00E−12
26%
41%
7%
2.5
1UV6_F
63.5
2.00E−12
26%
41%
7%
2.5
1UV6_G
63.5
2.00E−12
26%
41%
7%
2.5
1UV6_H
63.5
2.00E−12
26%
41%
7%
2.5
1UV6_I
63.5
2.00E−12
26%
41%
7%
2.5
1UV6_J
63.5
2.00E−12
26%
41%
7%
2.5
3C75_L
27.7
5.3
27%
41%
11%
2.5
3C75_M
27.7
5.3
27%
41%
11%
2.5
2WZY_A
87.8
1.20E−20
28%
43%
2%
2.51
2WZY_B
87.8
1.20E−20
28%
43%
2%
2.51
2WZY_C
87.8
1.20E−20
28%
43%
2%
2.51
2WZY_D
87.8
1.20E−20
28%
43%
2%
2.51
2WZY_E
87.8
1.20E−20
28%
43%
2%
2.51
2WZY_F
87.8
1.20E−20
28%
43%
2%
2.51
2WZY_G
87.8
1.20E−20
28%
43%
2%
2.51
2WZY_H
87.8
1.20E−20
28%
43%
2%
2.51
2WZY_I
87.8
1.20E−20
28%
43%
2%
2.51
2WZY_J
87.8
1.20E−20
28%
43%
2%
2.51
2XNU_A
90.9
9.90E−22
27%
44%
2%
2.55
2XNU_B
90.9
9.90E−22
27%
44%
2%
2.55
2XNU_C
90.9
9.90E−22
27%
44%
2%
2.55
2XNU_D
90.9
9.90E−22
27%
44%
2%
2.55
2XNU_E
90.9
9.90E−22
27%
44%
2%
2.55
2ZJU_A
65.5
5.50E−13
26%
41%
7%
2.58
2ZJU_B
65.5
5.50E−13
26%
41%
7%
2.58
2ZJU_C
65.5
5.50E−13
26%
41%
7%
2.58
2ZJU_D
65.5
5.50E−13
26%
41%
7%
2.58
2ZJU_E
65.5
5.50E−13
26%
41%
7%
2.58
3TLW_A
33.1
0.12
24%
43%
13%
2.6
3TLW_B
33.1
0.12
24%
43%
13%
2.6
3TLW_C
33.1
0.12
24%
43%
13%
2.6
3TLW_D
33.1
0.12
24%
43%
13%
2.6
3TLW_E
33.1
0.12
24%
43%
13%
2.6
2W8G_A
89.4
3.00E−21
29%
43%
2%
2.6
2W8G_B
89.4
3.00E−21
29%
43%
2%
2.6
2W8G_C
89.4
3.00E−21
29%
43%
2%
2.6
2W8G_D
89.4
3.00E−21
29%
43%
2%
2.6
2W8G_E
89.4
3.00E−21
29%
43%
2%
2.6
1I9B_A
63.5
2.30E−12
26%
41%
7%
2.7
1I9B_B
63.5
2.30E−12
26%
41%
7%
2.7
1I9B_C
63.5
2.30E−12
26%
41%
7%
2.7
1I9B_D
63.5
2.30E−12
26%
41%
7%
2.7
1I9B_E
63.5
2.30E−12
26%
41%
7%
2.7
2ZJV_A
65.5
5.50E−13
26%
41%
7%
2.7
2ZJV_B
65.5
5.50E−13
26%
41%
7%
2.7
2ZJV_C
65.5
5.50E−13
26%
41%
7%
2.7
2ZJV_D
65.5
5.50E−13
26%
41%
7%
2.7
2ZJV_E
65.5
5.50E−13
26%
41%
7%
2.7
3U8M_A
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_B
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_C
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_D
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_E
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_F
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_G
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_H
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_I
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_J
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_K
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_L
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_M
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_N
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_O
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_P
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_Q
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_R
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_S
63.5
2.00E−12
26%
41%
7%
2.7
3U8M_T
63.5
2.00E−12
26%
41%
7%
2.7
2WNL_A
87.8
1.00E−20
28%
43%
2%
2.7
2WNL_B
87.8
1.00E−20
28%
43%
2%
2.7
2WNL_C
87.8
1.00E−20
28%
43%
2%
2.7
2WNL_D
87.8
1.00E−20
28%
43%
2%
2.7
2WNL_E
87.8
1.00E−20
28%
43%
2%
2.7
2WNL_F
87.8
1.00E−20
28%
43%
2%
2.7
2WNL_G
87.8
1.00E−20
28%
43%
2%
2.7
2WNL_H
87.8
1.00E−20
28%
43%
2%
2.7
2WNL_I
87.8
1.00E−20
28%
43%
2%
2.7
2WNL_J
87.8
1.00E−20
28%
43%
2%
2.7
2W8F_A
89.4
3.00E−21
29%
43%
2%
2.7
2W8F_B
89.4
3.00E−21
29%
43%
2%
2.7
2W8F_C
89.4
3.00E−21
29%
43%
2%
2.7
2W8F_D
89.4
3.00E−21
29%
43%
2%
2.7
2W8F_E
89.4
3.00E−21
29%
43%
2%
2.7
2W8F_F
89.4
3.00E−21
29%
43%
2%
2.7
2W8F_G
89.4
3.00E−21
29%
43%
2%
2.7
2W8F_H
89.4
3.00E−21
29%
43%
2%
2.7
2W8F_I
89.4
3.00E−21
29%
43%
2%
2.7
2W8F_J
89.4
3.00E−21
29%
43%
2%
2.7
2XZ5_A
87.8
1.10E−20
29%
43%
2%
2.8
2XZ5_B
87.8
1.10E−20
29%
43%
2%
2.8
2XZ5_C
87.8
1.10E−20
29%
43%
2%
2.8
2XZ5_D
87.8
1.10E−20
29%
43%
2%
2.8
2XZ5_E
87.8
1.10E−20
29%
43%
2%
2.8
3SQ6_A
104.4
6.40E−27
31%
48%
3%
2.8
3SQ6_B
104.4
6.40E−27
31%
48%
3%
2.8
3SQ6_C
104.4
6.40E−27
31%
48%
3%
2.8
3SQ6_D
104.4
6.40E−27
31%
48%
3%
2.8
3SQ6_E
104.4
6.40E−27
31%
48%
3%
2.8
3SQ6_F
104.4
6.40E−27
31%
48%
3%
2.8
3SQ6_G
104.4
6.40E−27
31%
48%
3%
2.8
3SQ6_H
104.4
6.40E−27
31%
48%
3%
2.8
3SQ6_I
104.4
6.40E−27
31%
48%
3%
2.8
3SQ6_J
104.4
6.40E−27
31%
48%
3%
2.8
1IQP_A
30.4
1.1
38%
48%
0%
2.8
1IQP_B
30.4
1.1
38%
48%
0%
2.8
1IQP_C
30.4
1.1
38%
48%
0%
2.8
1IQP_D
30.4
1.1
38%
48%
0%
2.8
1IQP_E
30.4
1.1
38%
48%
0%
2.8
1IQP_F
30.4
1.1
38%
48%
0%
2.8
3TLU_A
33.1
0.12
24%
43%
13%
2.85
3TLU_B
33.1
0.12
24%
43%
13%
2.85
3TLU_C
33.1
0.12
24%
43%
13%
2.85
3TLU_D
33.1
0.12
24%
43%
13%
2.85
3TLU_E
33.1
0.12
24%
43%
13%
2.85
2PH9_A
87.8
1.10E−20
28%
43%
2%
2.88
2PH9_B
87.8
1.10E−20
28%
43%
2%
2.88
2PH9_C
87.8
1.10E−20
28%
43%
2%
2.88
2PH9_D
87.8
1.10E−20
28%
43%
2%
2.88
2PH9_E
87.8
1.10E−20
28%
43%
2%
2.88
3TLV_A
33.5
0.11
24%
43%
13%
2.9
3TLV_B
33.5
0.11
24%
43%
13%
2.9
3TLV_C
33.5
0.11
24%
43%
13%
2.9
3TLV_D
33.5
0.11
24%
43%
13%
2.9
3TLV_E
33.5
0.11
24%
43%
13%
2.9
3UU5_A
33.5
0.12
24%
43%
13%
2.9
3UU5_B
33.5
0.12
24%
43%
13%
2.9
3UU5_C
33.5
0.12
24%
43%
13%
2.9
3UU5_D
33.5
0.12
24%
43%
13%
2.9
3UU5_E
33.5
0.12
24%
43%
13%
2.9
3UUB_A
33.1
0.12
24%
43%
13%
2.9
3UUB_B
33.1
0.12
24%
43%
13%
2.9
3UUB_C
33.1
0.12
24%
43%
13%
2.9
3UUB_D
33.1
0.12
24%
43%
13%
2.9
3UUB_E
33.1
0.12
24%
43%
13%
2.9
3UUB_F
33.1
0.12
24%
43%
13%
2.9
3UUB_G
33.1
0.12
24%
43%
13%
2.9
3UUB_H
33.1
0.12
24%
43%
13%
2.9
3UUB_I
33.1
0.12
24%
43%
13%
2.9
3UUB_J
33.1
0.12
24%
43%
13%
2.9
3EAM_A
36.6
0.0088
25%
44%
13%
2.9
3EAM_B
36.6
0.0088
25%
44%
13%
2.9
3EAM_C
36.6
0.0088
25%
44%
13%
2.9
3EAM_D
36.6
0.0088
25%
44%
13%
2.9
3EAM_E
36.6
0.0088
25%
44%
13%
2.9
3SH1_A
93.2
1.40E−22
30%
44%
2%
2.9
3SH1_B
93.2
1.40E−22
30%
44%
2%
2.9
3SH1_C
93.2
1.40E−22
30%
44%
2%
2.9
3SH1_D
93.2
1.40E−22
30%
44%
2%
2.9
3SH1_E
93.2
1.40E−22
30%
44%
2%
2.9
3SH1_F
93.2
1.40E−22
30%
44%
2%
2.9
3SH1_G
93.2
1.40E−22
30%
44%
2%
2.9
3SH1_H
93.2
1.40E−22
30%
44%
2%
2.9
3SH1_I
93.2
1.40E−22
30%
44%
2%
2.9
3SH1_J
93.2
1.40E−22
30%
44%
2%
2.9
3RQW_A
42.4
0.00013
22%
41%
5%
2.91
3RQW_B
42.4
0.00013
22%
41%
5%
2.91
3RQW_C
42.4
0.00013
22%
41%
5%
2.91
3RQW_D
42.4
0.00013
22%
41%
5%
2.91
3RQW_E
42.4
0.00013
22%
41%
5%
2.91
3RQW_F
42.4
0.00013
22%
41%
5%
2.91
3RQW_G
42.4
0.00013
22%
41%
5%
2.91
3RQW_H
42.4
0.00013
22%
41%
5%
2.91
3RQW_I
42.4
0.00013
22%
41%
5%
2.91
3RQW_J
42.4
0.00013
22%
41%
5%
2.91
3UU6_A
33.5
0.11
24%
43%
13%
2.98
3UU6_B
33.5
0.11
24%
43%
13%
2.98
3UU6_C
33.5
0.11
24%
43%
13%
2.98
3UU6_D
33.5
0.11
24%
43%
13%
2.98
3UU6_E
33.5
0.11
24%
43%
13%
2.98
4F8H_A
37.7
0.0046
24%
42%
11%
2.99
4F8H_B
37.7
0.0046
24%
42%
11%
2.99
4F8H_C
37.7
0.0046
24%
42%
11%
2.99
4F8H_D
37.7
0.0046
24%
42%
11%
2.99
4F8H_E
37.7
0.0046
24%
42%
11%
2.99
2BR7_A
89.4
3.00E−21
29%
43%
2%
3
2BR7_B
89.4
3.00E−21
29%
43%
2%
3
2BR7_C
89.4
3.00E−21
29%
43%
2%
3
2BR7_D
89.4
3.00E−21
29%
43%
2%
3
2BR7_E
89.4
3.00E−21
29%
43%
2%
3
3T4M_A
102.1
8.20E−26
31%
45%
2%
3
3T4M_B
102.1
8.20E−26
31%
45%
2%
3
3T4M_C
102.1
8.20E−26
31%
45%
2%
3
3T4M_D
102.1
8.20E−26
31%
45%
2%
3
3T4M_E
102.1
8.20E−26
31%
45%
2%
3
3T4M_F
102.1
8.20E−26
31%
45%
2%
3
3T4M_G
102.1
8.20E−26
31%
45%
2%
3
3T4M_H
102.1
8.20E−26
31%
45%
2%
3
3T4M_I
102.1
8.20E−26
31%
45%
2%
3
3T4M_J
102.1
8.20E−26
31%
45%
2%
3
3UU4_A
33.1
0.12
24%
43%
13%
3.05
3UU4_B
33.1
0.12
24%
43%
13%
3.05
3UU4_C
33.1
0.12
24%
43%
13%
3.05
3UU4_D
33.1
0.12
24%
43%
13%
3.05
3UU4_E
33.1
0.12
24%
43%
13%
3.05
3RQU_A
42.4
0.00013
22%
41%
5%
3.09
3RQU_B
42.4
0.00013
22%
41%
5%
3.09
3RQU_C
42.4
0.00013
22%
41%
5%
3.09
3RQU_D
42.4
0.00013
22%
41%
5%
3.09
3RQU_E
42.4
0.00013
22%
41%
5%
3.09
3RQU_F
42.4
0.00013
22%
41%
5%
3.09
3RQU_G
42.4
0.00013
22%
41%
5%
3.09
3RQU_H
42.4
0.00013
22%
41%
5%
3.09
3RQU_I
42.4
0.00013
22%
41%
5%
3.09
3RQU_J
42.4
0.00013
22%
41%
5%
3.09
3EHZ_A
37.7
0.0046
24%
42%
11%
3.1
3EHZ_B
37.7
0.0046
24%
42%
11%
3.1
3EHZ_C
37.7
0.0046
24%
42%
11%
3.1
3EHZ_D
37.7
0.0046
24%
42%
11%
3.1
3EHZ_E
37.7
0.0046
24%
42%
11%
3.1
3GUA_A
87.8
9.10E−21
28%
43%
2%
3.1
3GUA_B
87.8
9.10E−21
28%
43%
2%
3.1
3GUA_C
87.8
9.10E−21
28%
43%
2%
3.1
3GUA_D
87.8
9.10E−21
28%
43%
2%
3.1
3GUA_E
87.8
9.10E−21
28%
43%
2%
3.1
3GUA_F
87.8
9.10E−21
28%
43%
2%
3.1
3GUA_G
87.8
9.10E−21
28%
43%
2%
3.1
3GUA_H
87.8
9.10E−21
28%
43%
2%
3.1
3GUA_I
87.8
9.10E−21
28%
43%
2%
3.1
3GUA_J
87.8
9.10E−21
28%
43%
2%
3.1
3SQ9_A
104.4
6.40E−27
31%
48%
3%
3.1
3SQ9_B
104.4
6.40E−27
31%
48%
3%
3.1
3SQ9_C
104.4
6.40E−27
31%
48%
3%
3.1
3SQ9_D
104.4
6.40E−27
31%
48%
3%
3.1
3SQ9_E
104.4
6.40E−27
31%
48%
3%
3.1
3SQ9_F
104.4
6.40E−27
31%
48%
3%
3.1
3SQ9_G
104.4
6.40E−27
31%
48%
3%
3.1
3SQ9_H
104.4
6.40E−27
31%
48%
3%
3.1
3SQ9_I
104.4
6.40E−27
31%
48%
3%
3.1
3SQ9_J
104.4
6.40E−27
31%
48%
3%
3.1
2XZ6_A
87.8
9.30E−21
29%
43%
2%
3.137
2XZ6_B
87.8
9.30E−21
29%
43%
2%
3.137
2XZ6_C
87.8
9.30E−21
29%
43%
2%
3.137
2XZ6_D
87.8
9.30E−21
29%
43%
2%
3.137
2XZ6_E
87.8
9.30E−21
29%
43%
2%
3.137
2XZ6_F
87.8
9.30E−21
29%
43%
2%
3.137
2XZ6_G
87.8
9.30E−21
29%
43%
2%
3.137
2XZ6_H
87.8
9.30E−21
29%
43%
2%
3.137
2XZ6_I
87.8
9.30E−21
29%
43%
2%
3.137
2XZ6_J
87.8
9.30E−21
29%
43%
2%
3.137
3UU3_A
33.5
0.12
24%
43%
13%
3.15
3UU3_B
33.5
0.12
24%
43%
13%
3.15
3UU3_C
33.5
0.12
24%
43%
13%
3.15
3UU3_D
33.5
0.12
24%
43%
13%
3.15
3UU3_E
33.5
0.12
24%
43%
13%
3.15
3LSV_A
36.6
0.0093
25%
44%
13%
3.15
3LSV_B
36.6
0.0093
25%
44%
13%
3.15
3LSV_C
36.6
0.0093
25%
44%
13%
3.15
3LSV_D
36.6
0.0093
25%
44%
13%
3.15
3LSV_E
36.6
0.0093
25%
44%
13%
3.15
2XQ9_A
37.7
0.0045
24%
42%
11%
3.2
2XQ9_B
37.7
0.0045
24%
42%
11%
3.2
2XQ9_C
37.7
0.0045
24%
42%
11%
3.2
2XQ9_D
37.7
0.0045
24%
42%
11%
3.2
2XQ9_E
37.7
0.0045
24%
42%
11%
3.2
3P4W_A
36.6
0.0089
25%
44%
13%
3.2
3P4W_B
36.6
0.0089
25%
44%
13%
3.2
3P4W_C
36.6
0.0089
25%
44%
13%
3.2
3P4W_D
36.6
0.0089
25%
44%
13%
3.2
3P4W_E
36.6
0.0089
25%
44%
13%
3.2
3TLS_A
36.6
0.0094
25%
44%
13%
3.2
3TLS_B
36.6
0.0094
25%
44%
13%
3.2
3TLS_C
36.6
0.0094
25%
44%
13%
3.2
3TLS_D
36.6
0.0094
25%
44%
13%
3.2
3TLS_E
36.6
0.0094
25%
44%
13%
3.2
4AFT_A
89.4
3.00E−21
29%
43%
2%
3.2
4AFT_B
89.4
3.00E−21
29%
43%
2%
3.2
4AFT_C
89.4
3.00E−21
29%
43%
2%
3.2
4AFT_D
89.4
3.00E−21
29%
43%
2%
3.2
4AFT_E
89.4
3.00E−21
29%
43%
2%
3.2
2XNT_A
90.9
9.90E−22
27%
44%
2%
3.21
2XNT_B
90.9
9.90E−22
27%
44%
2%
3.21
2XNT_C
90.9
9.90E−22
27%
44%
2%
3.21
2XNT_D
90.9
9.90E−22
27%
44%
2%
3.21
2XNT_E
90.9
9.90E−22
27%
44%
2%
3.21
2XNT_F
90.9
9.90E−22
27%
44%
2%
3.21
2XNT_G
90.9
9.90E−22
27%
44%
2%
3.21
2XNT_H
90.9
9.90E−22
27%
44%
2%
3.21
2XNT_I
90.9
9.90E−22
27%
44%
2%
3.21
2XNT_J
90.9
9.90E−22
27%
44%
2%
3.21
3UU8_A
33.1
0.12
24%
43%
13%
3.25
3UU8_B
33.1
0.12
24%
43%
13%
3.25
3UU8_C
33.1
0.12
24%
43%
13%
3.25
3UU8_D
33.1
0.12
24%
43%
13%
3.25
3UU8_E
33.1
0.12
24%
43%
13%
3.25
2Y58_A
89.4
3.00E−21
29%
43%
2%
3.25
2Y58_B
89.4
3.00E−21
29%
43%
2%
3.25
2Y58_C
89.4
3.00E−21
29%
43%
2%
3.25
2Y58_D
89.4
3.00E−21
29%
43%
2%
3.25
2Y58_E
89.4
3.00E−21
29%
43%
2%
3.25
3RHW_A
45.1
1.70E−05
23%
42%
8%
3.26
3RHW_B
45.1
1.70E−05
23%
42%
8%
3.26
3RHW_C
45.1
1.70E−05
23%
42%
8%
3.26
3RHW_D
45.1
1.70E−05
23%
42%
8%
3.26
3RHW_E
45.1
1.70E−05
23%
42%
8%
3.26
2VL0_A
43.9
3.60E−05
22%
41%
4%
3.3
2VL0_B
43.9
3.60E−05
22%
41%
4%
3.3
2VL0_C
43.9
3.60E−05
22%
41%
4%
3.3
2VL0_D
43.9
3.60E−05
22%
41%
4%
3.3
2VL0_E
43.9
3.60E−05
22%
41%
4%
3.3
2VL0_F
43.9
3.60E−05
22%
41%
4%
3.3
2VL0_G
43.9
3.60E−05
22%
41%
4%
3.3
2VL0_H
43.9
3.60E−05
22%
41%
4%
3.3
2VL0_I
43.9
3.60E−05
22%
41%
4%
3.3
2VL0_J
43.9
3.60E−05
22%
41%
4%
3.3
2YKS_A
43.9
3.60E−05
22%
41%
4%
3.3
2YKS_B
43.9
3.60E−05
22%
41%
4%
3.3
2YKS_C
43.9
3.60E−05
22%
41%
4%
3.3
2YKS_D
43.9
3.60E−05
22%
41%
4%
3.3
2YKS_E
43.9
3.60E−05
22%
41%
4%
3.3
2YKS_F
43.9
3.60E−05
22%
41%
4%
3.3
2YKS_G
43.9
3.60E−05
22%
41%
4%
3.3
2YKS_H
43.9
3.60E−05
22%
41%
4%
3.3
2YKS_I
43.9
3.60E−05
22%
41%
4%
3.3
2YKS_J
43.9
3.60E−05
22%
41%
4%
3.3
3P50_A
36.6
0.0089
25%
44%
13%
3.3
3P50_B
36.6
0.0089
25%
44%
13%
3.3
3P50_C
36.6
0.0089
25%
44%
13%
3.3
3P50_D
36.6
0.0089
25%
44%
13%
3.3
3P50_E
36.6
0.0089
25%
44%
13%
3.3
3TLT_A
37
0.0083
25%
44%
13%
3.3
3TLT_B
37
0.0083
25%
44%
13%
3.3
3TLT_C
37
0.0083
25%
44%
13%
3.3
3TLT_D
37
0.0083
25%
44%
13%
3.3
3TLT_E
37
0.0083
25%
44%
13%
3.3
2Y57_A
89.4
3.00E−21
29%
43%
2%
3.3
2Y57_B
89.4
3.00E−21
29%
43%
2%
3.3
2Y57_C
89.4
3.00E−21
29%
43%
2%
3.3
2Y57_D
89.4
3.00E−21
29%
43%
2%
3.3
2Y57_E
89.4
3.00E−21
29%
43%
2%
3.3
2YN6_A
42.4
0.00013
22%
41%
5%
3.31
2YN6_B
42.4
0.00013
22%
41%
5%
3.31
2YN6_C
42.4
0.00013
22%
41%
5%
3.31
2YN6_D
42.4
0.00013
22%
41%
5%
3.31
2YN6_E
42.4
0.00013
22%
41%
5%
3.31
4A97_A
41.2
0.00027
21%
41%
4%
3.34
4A97_B
41.2
0.00027
21%
41%
4%
3.34
4A97_C
41.2
0.00027
21%
41%
4%
3.34
4A97_D
41.2
0.00027
21%
41%
4%
3.34
4A97_E
41.2
0.00027
21%
41%
4%
3.34
4A97_F
41.2
0.00027
21%
41%
4%
3.34
4A97_G
41.2
0.00027
21%
41%
4%
3.34
4A97_H
41.2
0.00027
21%
41%
4%
3.34
4A97_I
41.2
0.00027
21%
41%
4%
3.34
4A97_J
41.2
0.00027
21%
41%
4%
3.34
3RIF_A
45.1
1.70E−05
23%
42%
8%
3.35
3RIF_B
45.1
1.70E−05
23%
42%
8%
3.35
3RIF_C
45.1
1.70E−05
23%
42%
8%
3.35
3RIF_D
45.1
1.70E−05
23%
42%
8%
3.35
3RIF_E
45.1
1.70E−05
23%
42%
8%
3.35
3RI5_A
45.1
1.70E−05
23%
42%
8%
3.4
3RI5_B
45.1
1.70E−05
23%
42%
8%
3.4
3RI5_C
45.1
1.70E−05
23%
42%
8%
3.4
3RI5_D
45.1
1.70E−05
23%
42%
8%
3.4
3RI5_E
45.1
1.70E−05
23%
42%
8%
3.4
2XQ7_A
37.7
0.0046
24%
42%
11%
3.4
2XQ7_B
37.7
0.0046
24%
42%
11%
3.4
2XQ7_C
37.7
0.0046
24%
42%
11%
3.4
2XQ7_D
37.7
0.0046
24%
42%
11%
3.4
2XQ7_E
37.7
0.0046
24%
42%
11%
3.4
2BYQ_A
87.8
1.00E−20
28%
43%
2%
3.4
2BYQ_B
87.8
1.00E−20
28%
43%
2%
3.4
2BYQ_C
87.8
1.00E−20
28%
43%
2%
3.4
2BYQ_D
87.8
1.00E−20
28%
43%
2%
3.4
2BYQ_E
87.8
1.00E−20
28%
43%
2%
3.4
3UQ4_A
43.1
6.30E−05
22%
41%
5%
3.5
3UQ4_B
43.1
6.30E−05
22%
41%
5%
3.5
3UQ4_C
43.1
6.30E−05
22%
41%
5%
3.5
3UQ4_D
43.1
6.30E−05
22%
41%
5%
3.5
3UQ4_E
43.1
6.30E−05
22%
41%
5%
3.5
3UQ4_F
43.1
6.30E−05
22%
41%
5%
3.5
3UQ4_G
43.1
6.30E−05
22%
41%
5%
3.5
3UQ4_H
43.1
6.30E−05
22%
41%
5%
3.5
3UQ4_I
43.1
6.30E−05
22%
41%
5%
3.5
3UQ4_J
43.1
6.30E−05
22%
41%
5%
3.5
2XQ3_A
37.7
0.0046
24%
42%
11%
3.5
2XQ3_B
37.7
0.0046
24%
42%
11%
3.5
2XQ3_C
37.7
0.0046
24%
42%
11%
3.5
2XQ3_D
37.7
0.0046
24%
42%
11%
3.5
2XQ3_E
37.7
0.0046
24%
42%
11%
3.5
2XQ5_A
37.7
0.0046
24%
42%
11%
3.5
2XQ5_B
37.7
0.0046
24%
42%
11%
3.5
2XQ5_C
37.7
0.0046
24%
42%
11%
3.5
2XQ5_D
37.7
0.0046
24%
42%
11%
3.5
2XQ5_E
37.7
0.0046
24%
42%
11%
3.5
3EI0_A
37.7
0.0048
24%
42%
11%
3.5
3EI0_B
37.7
0.0048
24%
42%
11%
3.5
3EI0_C
37.7
0.0048
24%
42%
11%
3.5
3EI0_D
37.7
0.0048
24%
42%
11%
3.5
3EI0_E
37.7
0.0048
24%
42%
11%
3.5
2Y56_A
89.4
3.00E−21
29%
43%
2%
3.59
2Y56_B
89.4
3.00E−21
29%
43%
2%
3.59
2Y56_C
89.4
3.00E−21
29%
43%
2%
3.59
2Y56_D
89.4
3.00E−21
29%
43%
2%
3.59
2Y56_E
89.4
3.00E−21
29%
43%
2%
3.59
2XQ4_A
37.7
0.0046
24%
42%
11%
3.6
2XQ4_B
37.7
0.0046
24%
42%
11%
3.6
2XQ4_C
37.7
0.0046
24%
42%
11%
3.6
2XQ4_D
37.7
0.0046
24%
42%
11%
3.6
2XQ4_E
37.7
0.0046
24%
42%
11%
3.6
2XQ8_A
37.7
0.0046
24%
42%
11%
3.6
2XQ8_B
37.7
0.0046
24%
42%
11%
3.6
2XQ8_C
37.7
0.0046
24%
42%
11%
3.6
2XQ8_D
37.7
0.0046
24%
42%
11%
3.6
2XQ8_E
37.7
0.0046
24%
42%
11%
3.6
4A98_A
41.2
0.00027
21%
41%
4%
3.61
4A98_B
41.2
0.00027
21%
41%
4%
3.61
4A98_C
41.2
0.00027
21%
41%
4%
3.61
4A98_D
41.2
0.00027
21%
41%
4%
3.61
4A98_E
41.2
0.00027
21%
41%
4%
3.61
4A98_F
41.2
0.00027
21%
41%
4%
3.61
4A98_G
41.2
0.00027
21%
41%
4%
3.61
4A98_H
41.2
0.00027
21%
41%
4%
3.61
4A98_I
41.2
0.00027
21%
41%
4%
3.61
4A98_J
41.2
0.00027
21%
41%
4%
3.61
3ZKR_A
41.2
0.00027
21%
41%
4%
3.65
3ZKR_B
41.2
0.00027
21%
41%
4%
3.65
3ZKR_C
41.2
0.00027
21%
41%
4%
3.65
3ZKR_D
41.2
0.00027
21%
41%
4%
3.65
3ZKR_E
41.2
0.00027
21%
41%
4%
3.65
3ZKR_F
41.2
0.00027
21%
41%
4%
3.65
3ZKR_G
41.2
0.00027
21%
41%
4%
3.65
3ZKR_H
41.2
0.00027
21%
41%
4%
3.65
3ZKR_I
41.2
0.00027
21%
41%
4%
3.65
3ZKR_J
41.2
0.00027
21%
41%
4%
3.65
2Y54_A
89.4
3.00E−21
29%
43%
2%
3.65
2Y54_B
89.4
3.00E−21
29%
43%
2%
3.65
2Y54_C
89.4
3.00E−21
29%
43%
2%
3.65
2Y54_D
89.4
3.00E−21
29%
43%
2%
3.65
2Y54_E
89.4
3.00E−21
29%
43%
2%
3.65
2XQ6_A
37.7
0.0046
24%
42%
11%
3.7
2XQ6_B
37.7
0.0046
24%
42%
11%
3.7
2XQ6_C
37.7
0.0046
24%
42%
11%
3.7
2XQ6_D
37.7
0.0046
24%
42%
11%
3.7
2XQ6_E
37.7
0.0046
24%
42%
11%
3.7
2XQA_A
37.7
0.0046
24%
42%
11%
3.7
2XQA_B
37.7
0.0046
24%
42%
11%
3.7
2XQA_C
37.7
0.0046
24%
42%
11%
3.7
2XQA_D
37.7
0.0046
24%
42%
11%
3.7
2XQA_E
37.7
0.0046
24%
42%
11%
3.7
3UQ7_A
43.1
6.50E−05
22%
41%
5%
3.8
3UQ7_B
43.1
6.50E−05
22%
41%
5%
3.8
3UQ7_C
43.1
6.50E−05
22%
41%
5%
3.8
3UQ7_D
43.1
6.50E−05
22%
41%
5%
3.8
3UQ7_E
43.1
6.50E−05
22%
41%
5%
3.8
3UQ7_F
43.1
6.50E−05
22%
41%
5%
3.8
3UQ7_G
43.1
6.50E−05
22%
41%
5%
3.8
3UQ7_H
43.1
6.50E−05
22%
41%
5%
3.8
3UQ7_I
43.1
6.50E−05
22%
41%
5%
3.8
3UQ7_J
43.1
6.50E−05
22%
41%
5%
3.8
3RIA_A
45.1
1.70E−05
23%
42%
8%
3.8
3RIA_B
45.1
1.70E−05
23%
42%
8%
3.8
3RIA_C
45.1
1.70E−05
23%
42%
8%
3.8
3RIA_D
45.1
1.70E−05
23%
42%
8%
3.8
3RIA_E
45.1
1.70E−05
23%
42%
8%
3.8
4AR2_A
34.7
0.056
25%
47%
16%
3.8
2YOE_A
41.2
0.00027
21%
41%
4%
3.9
2YOE_B
41.2
0.00027
21%
41%
4%
3.9
2YOE_C
41.2
0.00027
21%
41%
4%
3.9
2YOE_D
41.2
0.00027
21%
41%
4%
3.9
2YOE_E
41.2
0.00027
21%
41%
4%
3.9
2YOE_F
41.2
0.00027
21%
41%
4%
3.9
2YOE_G
41.2
0.00027
21%
41%
4%
3.9
2YOE_H
41.2
0.00027
21%
41%
4%
3.9
2YOE_I
41.2
0.00027
21%
41%
4%
3.9
2YOE_J
41.2
0.00027
21%
41%
4%
3.9
2BG9_C
158.3
9.40E−46
38%
59%
3%
4
2BG9_B
176.8
1.10E−52
43%
62%
1%
4
2BG9_E
174.5
8.60E−52
43%
67%
0%
4
2BG9_A
222.6
2.60E−70
51%
67%
0%
4
2BG9_D
222.6
2.60E−70
51%
67%
0%
4
3UQ5_A
43.1
6.20E−05
22%
41%
5%
4.2
3UQ5_B
43.1
6.20E−05
22%
41%
5%
4.2
3UQ5_C
43.1
6.20E−05
22%
41%
5%
4.2
3UQ5_D
43.1
6.20E−05
22%
41%
5%
4.2
3UQ5_E
43.1
6.20E−05
22%
41%
5%
4.2
3UQ5_F
43.1
6.20E−05
22%
41%
5%
4.2
3UQ5_G
43.1
6.20E−05
22%
41%
5%
4.2
3UQ5_H
43.1
6.20E−05
22%
41%
5%
4.2
3UQ5_I
43.1
6.20E−05
22%
41%
5%
4.2
3UQ5_J
43.1
6.20E−05
22%
41%
5%
4.2
1YI5_A
63.5
2.00E−12
26%
41%
7%
4.2
1YI5_B
63.5
2.00E−12
26%
41%
7%
4.2
1YI5_C
63.5
2.00E−12
26%
41%
7%
4.2
1YI5_D
63.5
2.00E−12
26%
41%
7%
4.2
1YI5_E
63.5
2.00E−12
26%
41%
7%
4.2
4AQQ_A
34.7
0.056
25%
47%
16%
4.75
4AOE_A
73.9
5.40E−16
24%
44%
3%
5.8
4AOE_B
73.9
5.40E−16
24%
44%
3%
5.8
4AOE_C
73.9
5.40E−16
24%
44%
3%
5.8
4AOE_D
73.9
5.40E−16
24%
44%
3%
5.8
4AOE_E
73.9
5.40E−16
24%
44%
3%
5.8
4AOD_A
75.1
2.10E−16
24%
46%
3%
6
4AOD_B
75.1
2.10E−16
24%
46%
3%
6
4AOD_C
75.1
2.10E−16
24%
46%
3%
6
4AOD_D
75.1
2.10E−16
24%
46%
3%
6
4AOD_E
75.1
2.10E−16
24%
46%
3%
6
4AQ5_C
156.4
5.40E−44
36%
57%
7%
6.2
4AQ9_C
156.4
5.40E−44
36%
57%
7%
6.2
4AQ5_B
171
1.60E−49
41%
58%
6%
6.2
4AQ9_B
171
1.60E−49
41%
58%
6%
6.2
4AQ5_E
168.7
9.40E−49
42%
64%
4%
6.2
4AQ9_E
168.7
9.40E−49
42%
64%
4%
6.2
4AQ5_A
222.2
2.80E−69
51%
67%
0%
6.2
4AQ5_D
222.2
2.80E−69
51%
67%
0%
6.2
4AQ9_A
222.2
2.80E−69
51%
67%
0%
6.2
4AQ9_D
222.2
2.80E−69
51%
67%
0%
6.2
Results of search b2 subunit on the PDB. ID consists of PDB ID (the first 4 letters) and the subunit (the last letter)
ID
Score
Expect
Identity
Positives
Gaps
Resolution
2R31_A
28.1
4.5
53%
69%
0%
1
2RB8_A
26.6
7.6
27%
39%
19%
1.45
2WN9_A
63.5
2.20E−12
24%
44%
4%
1.75
2WN9_B
63.5
2.20E−12
24%
44%
4%
1.75
2WN9_C
63.5
2.20E−12
24%
44%
4%
1.75
2WN9_D
63.5
2.20E−12
24%
44%
4%
1.75
2WN9_E
63.5
2.20E−12
24%
44%
4%
1.75
2PGZ_A
63.5
2.30E−12
24%
44%
4%
1.76
2PGZ_B
63.5
2.30E−12
24%
44%
4%
1.76
2PGZ_C
63.5
2.30E−12
24%
44%
4%
1.76
2PGZ_D
63.5
2.30E−12
24%
44%
4%
1.76
2PGZ_E
63.5
2.30E−12
24%
44%
4%
1.76
2WNJ_A
63.5
2.20E−12
24%
44%
4%
1.8
2WNJ_B
63.5
2.20E−12
24%
44%
4%
1.8
2WNJ_C
63.5
2.20E−12
24%
44%
4%
1.8
2WNJ_D
63.5
2.20E−12
24%
44%
4%
1.8
2WNJ_E
63.5
2.20E−12
24%
44%
4%
1.8
2ZD2_A
28.1
4.3
53%
69%
0%
1.8
2ZD2_B
28.1
4.3
53%
69%
0%
1.8
4AFH_A
70.1
1.30E−14
28%
46%
8%
1.88
4AFH_B
70.1
1.30E−14
28%
46%
8%
1.88
4AFH_C
70.1
1.30E−14
28%
46%
8%
1.88
4AFH_D
70.1
1.30E−14
28%
46%
8%
1.88
4AFH_E
70.1
1.30E−14
28%
46%
8%
1.88
2Y7Y_A
63.9
1.50E−12
25%
45%
4%
1.9
2Y7Y_B
63.9
1.50E−12
25%
45%
4%
1.9
2Y7Y_C
63.9
1.50E−12
25%
45%
4%
1.9
2Y7Y_D
63.9
1.50E−12
25%
45%
4%
1.9
2Y7Y_E
63.9
1.50E−12
25%
45%
4%
1.9
2P4X_A
28.1
4.5
53%
69%
0%
1.9
2P4X_B
28.1
4.5
53%
69%
0%
1.9
2XYS_A
63.9
1.50E−12
25%
45%
4%
1.909
2XYS_B
63.9
1.50E−12
25%
45%
4%
1.909
2XYS_C
63.9
1.50E−12
25%
45%
4%
1.909
2XYS_D
63.9
1.50E−12
25%
45%
4%
1.909
2XYS_E
63.9
1.50E−12
25%
45%
4%
1.909
3C84_A
63.5
2.60E−12
24%
44%
4%
1.94
3C84_B
63.5
2.60E−12
24%
44%
4%
1.94
3C84_C
63.5
2.60E−12
24%
44%
4%
1.94
3C84_D
63.5
2.60E−12
24%
44%
4%
1.94
3C84_E
63.5
2.60E−12
24%
44%
4%
1.94
2QC1_B
176.4
2.10E−54
42%
63%
2%
1.94
1OSP_L
28.1
4.8
23%
42%
7%
1.95
2YMD_A
64.7
8.20E−13
25%
42%
1%
1.96
2YMD_B
64.7
8.20E−13
25%
42%
1%
1.96
2YMD_C
64.7
8.20E−13
25%
42%
1%
1.96
2YMD_D
64.7
8.20E−13
25%
42%
1%
1.96
2YMD_E
64.7
8.20E−13
25%
42%
1%
1.96
2YMD_F
64.7
8.20E−13
25%
42%
1%
1.96
2YMD_G
64.7
8.20E−13
25%
42%
1%
1.96
2YMD_H
64.7
8.20E−13
25%
42%
1%
1.96
2YMD_I
64.7
8.20E−13
25%
42%
1%
1.96
2YMD_J
64.7
8.20E−13
25%
42%
1%
1.96
2BJ0_A
51.6
4.10E−08
28%
48%
5%
2
2BJ0_B
51.6
4.10E−08
28%
48%
5%
2
2BJ0_C
51.6
4.10E−08
28%
48%
5%
2
2BJ0_D
51.6
4.10E−08
28%
48%
5%
2
2BJ0_E
51.6
4.10E−08
28%
48%
5%
2
4AFG_A
70.1
1.30E−14
28%
46%
8%
2
4AFG_B
70.1
1.30E−14
28%
46%
8%
2
4AFG_C
70.1
1.30E−14
28%
46%
8%
2
4AFG_D
70.1
1.30E−14
28%
46%
8%
2
4AFG_E
70.1
1.30E−14
28%
46%
8%
2
2BYN_A
63.5
2.60E−12
24%
44%
4%
2.02
2BYN_B
63.5
2.60E−12
24%
44%
4%
2.02
2BYN_C
63.5
2.60E−12
24%
44%
4%
2.02
2BYN_D
63.5
2.60E−12
24%
44%
4%
2.02
2BYN_E
63.5
2.60E−12
24%
44%
4%
2.02
2BYS_A
63.5
2.60E−12
24%
44%
4%
2.05
2BYS_B
63.5
2.60E−12
24%
44%
4%
2.05
2BYS_C
63.5
2.60E−12
24%
44%
4%
2.05
2BYS_D
63.5
2.60E−12
24%
44%
4%
2.05
2BYS_E
63.5
2.60E−12
24%
44%
4%
2.05
2BYS_F
63.5
2.60E−12
24%
44%
4%
2.05
2BYS_G
63.5
2.60E−12
24%
44%
4%
2.05
2BYS_H
63.5
2.60E−12
24%
44%
4%
2.05
2BYS_I
63.5
2.60E−12
24%
44%
4%
2.05
2BYS_J
63.5
2.60E−12
24%
44%
4%
2.05
2XYT_A
63.9
1.50E−12
25%
45%
4%
2.05
2XYT_B
63.9
1.50E−12
25%
45%
4%
2.05
2XYT_C
63.9
1.50E−12
25%
45%
4%
2.05
2XYT_D
63.9
1.50E−12
25%
45%
4%
2.05
2XYT_E
63.9
1.50E−12
25%
45%
4%
2.05
2XYT_F
63.9
1.50E−12
25%
45%
4%
2.05
2XYT_G
63.9
1.50E−12
25%
45%
4%
2.05
2XYT_H
63.9
1.50E−12
25%
45%
4%
2.05
2XYT_I
63.9
1.50E−12
25%
45%
4%
2.05
2XYT_J
63.9
1.50E−12
25%
45%
4%
2.05
2BYP_A
63.5
2.20E−12
24%
43%
1%
2.07
2BYP_B
63.5
2.20E−12
24%
43%
1%
2.07
2BYP_C
63.5
2.20E−12
24%
43%
1%
2.07
2BYP_D
63.5
2.20E−12
24%
43%
1%
2.07
2BYP_E
63.5
2.20E−12
24%
43%
1%
2.07
3PEO_A
63.5
2.20E−12
24%
44%
4%
2.1
3PEO_B
63.5
2.20E−12
24%
44%
4%
2.1
3PEO_C
63.5
2.20E−12
24%
44%
4%
2.1
3PEO_D
63.5
2.20E−12
24%
44%
4%
2.1
3PEO_E
63.5
2.20E−12
24%
44%
4%
2.1
3PEO_F
63.5
2.20E−12
24%
44%
4%
2.1
3PEO_G
63.5
2.20E−12
24%
44%
4%
2.1
3PEO_H
63.5
2.20E−12
24%
44%
4%
2.1
3PEO_I
63.5
2.20E−12
24%
44%
4%
2.1
3PEO_J
63.5
2.20E−12
24%
44%
4%
2.1
1UW6_A
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_B
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_C
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_D
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_E
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_F
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_G
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_H
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_I
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_J
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_K
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_L
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_M
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_N
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_O
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_P
44.3
2.20E−05
24%
40%
3%
2.2
1UW6_Q
44.3
2.20E−05
24%
40%
3%
2.2
1UX2_A
43.9
2.40E−05
24%
40%
3%
2.2
1UX2_B
43.9
2.40E−05
24%
40%
3%
2.2
1UX2_C
43.9
2.40E−05
24%
40%
3%
2.2
1UX2_D
43.9
2.40E−05
24%
40%
3%
2.2
1UX2_E
43.9
2.40E−05
24%
40%
3%
2.2
1UX2_F
43.9
2.40E−05
24%
40%
3%
2.2
1UX2_G
43.9
2.40E−05
24%
40%
3%
2.2
1UX2_H
43.9
2.40E−05
24%
40%
3%
2.2
1UX2_I
43.9
2.40E−05
24%
40%
3%
2.2
1UX2_J
43.9
2.40E−05
24%
40%
3%
2.2
2WNC_A
63.5
2.60E−12
24%
44%
4%
2.2
2WNC_B
63.5
2.60E−12
24%
44%
4%
2.2
2WNC_C
63.5
2.60E−12
24%
44%
4%
2.2
2WNC_D
63.5
2.60E−12
24%
44%
4%
2.2
2WNC_E
63.5
2.60E−12
24%
44%
4%
2.2
4B5D_A
70.1
1.30E−14
28%
46%
8%
2.2
4B5D_B
70.1
1.30E−14
28%
46%
8%
2.2
4B5D_C
70.1
1.30E−14
28%
46%
8%
2.2
4B5D_D
70.1
1.30E−14
28%
46%
8%
2.2
4B5D_E
70.1
1.30E−14
28%
46%
8%
2.2
2C9T_A
63.9
1.50E−12
25%
45%
4%
2.25
2C9T_B
63.9
1.50E−12
25%
45%
4%
2.25
2C9T_C
63.9
1.50E−12
25%
45%
4%
2.25
2C9T_D
63.9
1.50E−12
25%
45%
4%
2.25
2C9T_E
63.9
1.50E−12
25%
45%
4%
2.25
2C9T_F
63.9
1.50E−12
25%
45%
4%
2.25
2C9T_G
63.9
1.50E−12
25%
45%
4%
2.25
2C9T_H
63.9
1.50E−12
25%
45%
4%
2.25
2C9T_I
63.9
1.50E−12
25%
45%
4%
2.25
2C9T_J
63.9
1.50E−12
25%
45%
4%
2.25
4ALX_A
43.9
3.40E−05
24%
40%
3%
2.3
4ALX_B
43.9
3.40E−05
24%
40%
3%
2.3
4ALX_C
43.9
3.40E−05
24%
40%
3%
2.3
4ALX_D
43.9
3.40E−05
24%
40%
3%
2.3
4ALX_E
43.9
3.40E−05
24%
40%
3%
2.3
4ALX_F
43.9
3.40E−05
24%
40%
3%
2.3
4ALX_G
43.9
3.40E−05
24%
40%
3%
2.3
4ALX_H
43.9
3.40E−05
24%
40%
3%
2.3
4ALX_I
43.9
3.40E−05
24%
40%
3%
2.3
4ALX_J
43.9
3.40E−05
24%
40%
3%
2.3
4DBM_A
63.5
2.30E−12
24%
44%
4%
2.3
4DBM_B
63.5
2.30E−12
24%
44%
4%
2.3
4DBM_C
63.5
2.30E−12
24%
44%
4%
2.3
4DBM_D
63.5
2.30E−12
24%
44%
4%
2.3
4DBM_E
63.5
2.30E−12
24%
44%
4%
2.3
3U8L_A
44.3
2.20E−05
24%
40%
3%
2.32
3U8L_B
44.3
2.20E−05
24%
40%
3%
2.32
3U8L_C
44.3
2.20E−05
24%
40%
3%
2.32
3U8L_D
44.3
2.20E−05
24%
40%
3%
2.32
3U8L_E
44.3
2.20E−05
24%
40%
3%
2.32
3U8L_F
44.3
2.20E−05
24%
40%
3%
2.32
3U8L_G
44.3
2.20E−05
24%
40%
3%
2.32
3U8L_H
44.3
2.20E−05
24%
40%
3%
2.32
3U8L_I
44.3
2.20E−05
24%
40%
3%
2.32
3U8L_J
44.3
2.20E−05
24%
40%
3%
2.32
3SIO_A
63.5
3.00E−12
25%
43%
1%
2.32
3SIO_B
63.5
3.00E−12
25%
43%
1%
2.32
3SIO_C
63.5
3.00E−12
25%
43%
1%
2.32
3SIO_D
63.5
3.00E−12
25%
43%
1%
2.32
3SIO_E
63.5
3.00E−12
25%
43%
1%
2.32
3SIO_F
63.5
3.00E−12
25%
43%
1%
2.32
3SIO_G
63.5
3.00E−12
25%
43%
1%
2.32
3SIO_H
63.5
3.00E−12
25%
43%
1%
2.32
3SIO_I
63.5
3.00E−12
25%
43%
1%
2.32
3SIO_J
63.5
3.00E−12
25%
43%
1%
2.32
3U8J_A
44.3
2.20E−05
24%
40%
3%
2.35
3U8J_B
44.3
2.20E−05
24%
40%
3%
2.35
3U8J_C
44.3
2.20E−05
24%
40%
3%
2.35
3U8J_D
44.3
2.20E−05
24%
40%
3%
2.35
3U8J_E
44.3
2.20E−05
24%
40%
3%
2.35
3U8J_F
44.3
2.20E−05
24%
40%
3%
2.35
3U8J_G
44.3
2.20E−05
24%
40%
3%
2.35
3U8J_H
44.3
2.20E−05
24%
40%
3%
2.35
3U8J_I
44.3
2.20E−05
24%
40%
3%
2.35
3U8J_J
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_A
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_B
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_C
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_D
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_E
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_F
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_G
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_H
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_I
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_J
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_K
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_L
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_M
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_N
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_O
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_P
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_Q
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_R
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_S
44.3
2.20E−05
24%
40%
3%
2.35
3U8N_T
44.3
2.20E−05
24%
40%
3%
2.35
2X00_A
63.5
2.20E−12
24%
44%
4%
2.4
2X00_B
63.5
2.20E−12
24%
44%
4%
2.4
2X00_C
63.5
2.20E−12
24%
44%
4%
2.4
2X00_D
63.5
2.20E−12
24%
44%
4%
2.4
2X00_E
63.5
2.20E−12
24%
44%
4%
2.4
2BR8_A
63.9
1.50E−12
25%
45%
4%
2.4
2BR8_B
63.9
1.50E−12
25%
45%
4%
2.4
2BR8_C
63.9
1.50E−12
25%
45%
4%
2.4
2BR8_D
63.9
1.50E−12
25%
45%
4%
2.4
2BR8_E
63.9
1.50E−12
25%
45%
4%
2.4
2UZ6_A
63.9
1.50E−12
25%
45%
4%
2.4
2UZ6_B
63.9
1.50E−12
25%
45%
4%
2.4
2UZ6_C
63.9
1.50E−12
25%
45%
4%
2.4
2UZ6_D
63.9
1.50E−12
25%
45%
4%
2.4
2UZ6_E
63.9
1.50E−12
25%
45%
4%
2.4
2UZ6_F
63.9
1.50E−12
25%
45%
4%
2.4
2UZ6_G
63.9
1.50E−12
25%
45%
4%
2.4
2UZ6_H
63.9
1.50E−12
25%
45%
4%
2.4
2UZ6_I
63.9
1.50E−12
25%
45%
4%
2.4
2UZ6_J
63.9
1.50E−12
25%
45%
4%
2.4
2YME_A
66.6
1.60E−13
25%
43%
1%
2.4
2YME_B
66.6
1.60E−13
25%
43%
1%
2.4
2YME_C
66.6
1.60E−13
25%
43%
1%
2.4
2YME_D
66.6
1.60E−13
25%
43%
1%
2.4
2YME_E
66.6
1.60E−13
25%
43%
1%
2.4
2YME_F
66.6
1.60E−13
25%
43%
1%
2.4
2YME_G
66.6
1.60E−13
25%
43%
1%
2.4
2YME_H
66.6
1.60E−13
25%
43%
1%
2.4
2YME_I
66.6
1.60E−13
25%
43%
1%
2.4
2YME_J
66.6
1.60E−13
25%
43%
1%
2.4
2XNV_A
63.5
2.80E−12
24%
44%
4%
2.44
2XNV_B
63.5
2.80E−12
24%
44%
4%
2.44
2XNV_C
63.5
2.80E−12
24%
44%
4%
2.44
2XNV_D
63.5
2.80E−12
24%
44%
4%
2.44
2XNV_E
63.5
2.80E−12
24%
44%
4%
2.44
2XNV_F
63.5
2.80E−12
24%
44%
4%
2.44
2XNV_G
63.5
2.80E−12
24%
44%
4%
2.44
2XNV_H
63.5
2.80E−12
24%
44%
4%
2.44
2XNV_I
63.5
2.80E−12
24%
44%
4%
2.44
2XNV_J
63.5
2.80E−12
24%
44%
4%
2.44
3PMZ_A
63.5
2.60E−12
24%
44%
4%
2.44
3PMZ_B
63.5
2.60E−12
24%
44%
4%
2.44
3PMZ_C
63.5
2.60E−12
24%
44%
4%
2.44
3PMZ_D
63.5
2.60E−12
24%
44%
4%
2.44
3PMZ_E
63.5
2.60E−12
24%
44%
4%
2.44
3PMZ_F
63.5
2.60E−12
24%
44%
4%
2.44
3PMZ_G
63.5
2.60E−12
24%
44%
4%
2.44
3PMZ_H
63.5
2.60E−12
24%
44%
4%
2.44
3PMZ_I
63.5
2.60E−12
24%
44%
4%
2.44
3PMZ_J
63.5
2.60E−12
24%
44%
4%
2.44
2BYR_A
63.5
2.60E−12
24%
44%
4%
2.45
2BYR_B
63.5
2.60E−12
24%
44%
4%
2.45
2BYR_C
63.5
2.60E−12
24%
44%
4%
2.45
2BYR_D
63.5
2.60E−12
24%
44%
4%
2.45
2BYR_E
63.5
2.60E−12
24%
44%
4%
2.45
2BYR_F
63.5
2.60E−12
24%
44%
4%
2.45
2BYR_G
63.5
2.60E−12
24%
44%
4%
2.45
2BYR_H
63.5
2.60E−12
24%
44%
4%
2.45
2BYR_I
63.5
2.60E−12
24%
44%
4%
2.45
2BYR_J
63.5
2.60E−12
24%
44%
4%
2.45
3U8K_A
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_B
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_C
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_D
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_E
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_F
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_G
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_H
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_I
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_J
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_K
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_L
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_M
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_N
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_O
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_P
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_Q
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_R
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_S
44.3
2.20E−05
24%
40%
3%
2.47
3U8K_T
44.3
2.20E−05
24%
40%
3%
2.47
3C79_A
63.5
2.60E−12
24%
44%
4%
2.48
3C79_B
63.5
2.60E−12
24%
44%
4%
2.48
3C79_C
63.5
2.60E−12
24%
44%
4%
2.48
3C79_D
63.5
2.60E−12
24%
44%
4%
2.48
3C79_E
63.5
2.60E−12
24%
44%
4%
2.48
1UV6_A
44.3
2.20E−05
24%
40%
3%
2.5
1UV6_B
44.3
2.20E−05
24%
40%
3%
2.5
1UV6_C
44.3
2.20E−05
24%
40%
3%
2.5
1UV6_D
44.3
2.20E−05
24%
40%
3%
2.5
1UV6_E
44.3
2.20E−05
24%
40%
3%
2.5
1UV6_F
44.3
2.20E−05
24%
40%
3%
2.5
1UV6_G
44.3
2.20E−05
24%
40%
3%
2.5
1UV6_H
44.3
2.20E−05
24%
40%
3%
2.5
1UV6_I
44.3
2.20E−05
24%
40%
3%
2.5
1UV6_J
44.3
2.20E−05
24%
40%
3%
2.5
3C75_L
29.6
1.4
29%
43%
0%
2.5
3C75_M
29.6
1.4
29%
43%
0%
2.5
2WZY_A
63.5
2.20E−12
24%
44%
4%
2.51
2WZY_B
63.5
2.20E−12
24%
44%
4%
2.51
2WZY_C
63.5
2.20E−12
24%
44%
4%
2.51
2WZY_D
63.5
2.20E−12
24%
44%
4%
2.51
2WZY_E
63.5
2.20E−12
24%
44%
4%
2.51
2WZY_F
63.5
2.20E−12
24%
44%
4%
2.51
2WZY_G
63.5
2.20E−12
24%
44%
4%
2.51
2WZY_H
63.5
2.20E−12
24%
44%
4%
2.51
2WZY_I
63.5
2.20E−12
24%
44%
4%
2.51
2WZY_J
63.5
2.20E−12
24%
44%
4%
2.51
2XNU_A
63.5
2.80E−12
24%
44%
4%
2.55
2XNU_B
63.5
2.80E−12
24%
44%
4%
2.55
2XNU_C
63.5
2.80E−12
24%
44%
4%
2.55
2XNU_D
63.5
2.80E−12
24%
44%
4%
2.55
2XNU_E
63.5
2.80E−12
24%
44%
4%
2.55
2ZJU_A
43.9
2.90E−05
24%
41%
3%
2.58
2ZJU_B
43.9
2.90E−05
24%
41%
3%
2.58
2ZJU_C
43.9
2.90E−05
24%
41%
3%
2.58
2ZJU_D
43.9
2.90E−05
24%
41%
3%
2.58
2ZJU_E
43.9
2.90E−05
24%
41%
3%
2.58
3TLW_A
40
0.00074
24%
42%
7%
2.6
3TLW_B
40
0.00074
24%
42%
7%
2.6
3TLW_C
40
0.00074
24%
42%
7%
2.6
3TLW_D
40
0.00074
24%
42%
7%
2.6
3TLW_E
40
0.00074
24%
42%
7%
2.6
2W8G_A
63.9
1.50E−12
25%
45%
4%
2.6
2W8G_B
63.9
1.50E−12
25%
45%
4%
2.6
2W8G_C
63.9
1.50E−12
25%
45%
4%
2.6
2W8G_D
63.9
1.50E−12
25%
45%
4%
2.6
2W8G_E
63.9
1.50E−12
25%
45%
4%
2.6
1I9B_A
43.9
2.70E−05
24%
40%
3%
2.7
1I9B_B
43.9
2.70E−05
24%
40%
3%
2.7
1I9B_C
43.9
2.70E−05
24%
40%
3%
2.7
1I9B_D
43.9
2.70E−05
24%
40%
3%
2.7
1I9B_E
43.9
2.70E−05
24%
40%
3%
2.7
2WNL_A
63.5
2.60E−12
24%
44%
4%
2.7
2WNL_B
63.5
2.60E−12
24%
44%
4%
2.7
2WNL_C
63.5
2.60E−12
24%
44%
4%
2.7
2WNL_D
63.5
2.60E−12
24%
44%
4%
2.7
2WNL_E
63.5
2.60E−12
24%
44%
4%
2.7
2WNL_F
63.5
2.60E−12
24%
44%
4%
2.7
2WNL_G
63.5
2.60E−12
24%
44%
4%
2.7
2WNL_H
63.5
2.60E−12
24%
44%
4%
2.7
2WNL_I
63.5
2.60E−12
24%
44%
4%
2.7
2WNL_J
63.5
2.60E−12
24%
44%
4%
2.7
2ZJV_A
43.9
2.90E−05
24%
41%
3%
2.7
2ZJV_B
43.9
2.90E−05
24%
41%
3%
2.7
2ZJV_C
43.9
2.90E−05
24%
41%
3%
2.7
2ZJV_D
43.9
2.90E−05
24%
41%
3%
2.7
2ZJV_E
43.9
2.90E−05
24%
41%
3%
2.7
3U8M_A
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_B
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_C
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_D
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_E
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_F
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_G
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_H
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_I
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_J
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_K
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_L
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_M
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_N
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_O
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_P
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_Q
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_R
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_S
44.3
2.20E−05
24%
40%
3%
2.7
3U8M_T
44.3
2.20E−05
24%
40%
3%
2.7
2W8F_A
63.9
1.50E−12
25%
45%
4%
2.7
2W8F_B
63.9
1.50E−12
25%
45%
4%
2.7
2W8F_C
63.9
1.50E−12
25%
45%
4%
2.7
2W8F_D
63.9
1.50E−12
25%
45%
4%
2.7
2W8F_E
63.9
1.50E−12
25%
45%
4%
2.7
2W8F_F
63.9
1.50E−12
25%
45%
4%
2.7
2W8F_G
63.9
1.50E−12
25%
45%
4%
2.7
2W8F_H
63.9
1.50E−12
25%
45%
4%
2.7
2W8F_I
63.9
1.50E−12
25%
45%
4%
2.7
2W8F_J
63.9
1.50E−12
25%
45%
4%
2.7
2XZ5_A
62.4
5.50E−12
25%
44%
4%
2.8
2XZ5_B
62.4
5.50E−12
25%
44%
4%
2.8
2XZ5_C
62.4
5.50E−12
25%
44%
4%
2.8
2XZ5_D
62.4
5.50E−12
25%
44%
4%
2.8
2XZ5_E
62.4
5.50E−12
25%
44%
4%
2.8
3SQ6_A
85.1
6.50E−20
28%
48%
4%
2.8
3SQ6_B
85.1
6.50E−20
28%
48%
4%
2.8
3SQ6_C
85.1
6.50E−20
28%
48%
4%
2.8
3SQ6_D
85.1
6.50E−20
28%
48%
4%
2.8
3SQ6_E
85.1
6.50E−20
28%
48%
4%
2.8
3SQ6_F
85.1
6.50E−20
28%
48%
4%
2.8
3SQ6_G
85.1
6.50E−20
28%
48%
4%
2.8
3SQ6_H
85.1
6.50E−20
28%
48%
4%
2.8
3SQ6_I
85.1
6.50E−20
28%
48%
4%
2.8
3SQ6_J
85.1
6.50E−20
28%
48%
4%
2.8
3TLU_A
40
0.00074
24%
42%
7%
2.85
3TLU_B
40
0.00074
24%
42%
7%
2.85
3TLU_C
40
0.00074
24%
42%
7%
2.85
3TLU_D
40
0.00074
24%
42%
7%
2.85
3TLU_E
40
0.00074
24%
42%
7%
2.85
2PH9_A
63.5
2.30E−12
24%
44%
4%
2.88
2PH9_B
63.5
2.30E−12
24%
44%
4%
2.88
2PH9_C
63.5
2.30E−12
24%
44%
4%
2.88
2PH9_D
63.5
2.30E−12
24%
44%
4%
2.88
2PH9_E
63.5
2.30E−12
24%
44%
4%
2.88
3EAM_A
42.7
9.30E−05
24%
43%
7%
2.9
3EAM_B
42.7
9.30E−05
24%
43%
7%
2.9
3EAM_C
42.7
9.30E−05
24%
43%
7%
2.9
3EAM_D
42.7
9.30E−05
24%
43%
7%
2.9
3EAM_E
42.7
9.30E−05
24%
43%
7%
2.9
3TLV_A
40
0.00068
24%
42%
7%
2.9
3TLV_B
40
0.00068
24%
42%
7%
2.9
3TLV_C
40
0.00068
24%
42%
7%
2.9
3TLV_D
40
0.00068
24%
42%
7%
2.9
3TLV_E
40
0.00068
24%
42%
7%
2.9
3UU5_A
40
0.0007
24%
42%
7%
2.9
3UU5_B
40
0.0007
24%
42%
7%
2.9
3UU5_C
40
0.0007
24%
42%
7%
2.9
3UU5_D
40
0.0007
24%
42%
7%
2.9
3UU5_E
40
0.0007
24%
42%
7%
2.9
3UUB_A
40
0.00074
24%
42%
7%
2.9
3UUB_B
40
0.00074
24%
42%
7%
2.9
3UUB_C
40
0.00074
24%
42%
7%
2.9
3UUB_D
40
0.00074
24%
42%
7%
2.9
3UUB_E
40
0.00074
24%
42%
7%
2.9
3UUB_F
40
0.00074
24%
42%
7%
2.9
3UUB_G
40
0.00074
24%
42%
7%
2.9
3UUB_H
40
0.00074
24%
42%
7%
2.9
3UUB_I
40
0.00074
24%
42%
7%
2.9
3UUB_J
40
0.00074
24%
42%
7%
2.9
3SH1_A
65.5
4.80E−13
25%
43%
1%
2.9
3SH1_B
65.5
4.80E−13
25%
43%
1%
2.9
3SH1_C
65.5
4.80E−13
25%
43%
1%
2.9
3SH1_D
65.5
4.80E−13
25%
43%
1%
2.9
3SH1_E
65.5
4.80E−13
25%
43%
1%
2.9
3SH1_F
65.5
4.80E−13
25%
43%
1%
2.9
3SH1_G
65.5
4.80E−13
25%
43%
1%
2.9
3SH1_H
65.5
4.80E−13
25%
43%
1%
2.9
3SH1_I
65.5
4.80E−13
25%
43%
1%
2.9
3SH1_J
65.5
4.80E−13
25%
43%
1%
2.9
3RQW_A
27.3
9
18%
42%
10%
2.91
3RQW_B
27.3
9
18%
42%
10%
2.91
3RQW_C
27.3
9
18%
42%
10%
2.91
3RQW_D
27.3
9
18%
42%
10%
2.91
3RQW_E
27.3
9
18%
42%
10%
2.91
3RQW_F
27.3
9
18%
42%
10%
2.91
3RQW_G
27.3
9
18%
42%
10%
2.91
3RQW_H
27.3
9
18%
42%
10%
2.91
3RQW_I
27.3
9
18%
42%
10%
2.91
3RQW_J
27.3
9
18%
42%
10%
2.91
3UU6_A
40
0.00068
24%
42%
7%
2.98
3UU6_B
40
0.00068
24%
42%
7%
2.98
3UU6_C
40
0.00068
24%
42%
7%
2.98
3UU6_D
40
0.00068
24%
42%
7%
2.98
3UU6_E
40
0.00068
24%
42%
7%
2.98
4F8H_A
42.7
8.70E−05
24%
43%
7%
2.99
4F8H_B
42.7
8.70E−05
24%
43%
7%
2.99
4F8H_C
42.7
8.70E−05
24%
43%
7%
2.99
4F8H_D
42.7
8.70E−05
24%
43%
7%
2.99
4F8H_E
42.7
8.70E−05
24%
43%
7%
2.99
2BR7_A
63.9
1.50E−12
25%
45%
4%
3
2BR7_B
63.9
1.50E−12
25%
45%
4%
3
2BR7_C
63.9
1.50E−12
25%
45%
4%
3
2BR7_D
63.9
1.50E−12
25%
45%
4%
3
2BR7_E
63.9
1.50E−12
25%
45%
4%
3
3T4M_A
69.7
2.00E−14
26%
44%
1%
3
3T4M_B
69.7
2.00E−14
26%
44%
1%
3
3T4M_C
69.7
2.00E−14
26%
44%
1%
3
3T4M_D
69.7
2.00E−14
26%
44%
1%
3
3T4M_E
69.7
2.00E−14
26%
44%
1%
3
3T4M_F
69.7
2.00E−14
26%
44%
1%
3
3T4M_G
69.7
2.00E−14
26%
44%
1%
3
3T4M_H
69.7
2.00E−14
26%
44%
1%
3
3T4M_I
69.7
2.00E−14
26%
44%
1%
3
3T4M_J
69.7
2.00E−14
26%
44%
1%
3
1LDJ_A
28.1
7.2
29%
50%
15%
3
3UU4_A
40
0.00074
24%
42%
7%
3.05
3UU4_B
40
0.00074
24%
42%
7%
3.05
3UU4_C
40
0.00074
24%
42%
7%
3.05
3UU4_D
40
0.00074
24%
42%
7%
3.05
3UU4_E
40
0.00074
24%
42%
7%
3.05
3RQU_A
27.3
9
18%
42%
10%
3.09
3RQU_B
27.3
9
18%
42%
10%
3.09
3RQU_C
27.3
9
18%
42%
10%
3.09
3RQU_D
27.3
9
18%
42%
10%
3.09
3RQU_E
27.3
9
18%
42%
10%
3.09
3RQU_F
27.3
9
18%
42%
10%
3.09
3RQU_G
27.3
9
18%
42%
10%
3.09
3RQU_H
27.3
9
18%
42%
10%
3.09
3RQU_I
27.3
9
18%
42%
10%
3.09
3RQU_J
27.3
9
18%
42%
10%
3.09
3EHZ_A
42.7
8.70E−05
24%
43%
7%
3.1
3EHZ_B
42.7
8.70E−05
24%
43%
7%
3.1
3EHZ_C
42.7
8.70E−05
24%
43%
7%
3.1
3EHZ_D
42.7
8.70E−05
24%
43%
7%
3.1
3EHZ_E
42.7
8.70E−05
24%
43%
7%
3.1
3GUA_A
63.5
2.30E−12
24%
43%
1%
3.1
3GUA_B
63.5
2.30E−12
24%
43%
1%
3.1
3GUA_C
63.5
2.30E−12
24%
43%
1%
3.1
3GUA_D
63.5
2.30E−12
24%
43%
1%
3.1
3GUA_E
63.5
2.30E−12
24%
43%
1%
3.1
3GUA_F
63.5
2.30E−12
24%
43%
1%
3.1
3GUA_G
63.5
2.30E−12
24%
43%
1%
3.1
3GUA_H
63.5
2.30E−12
24%
43%
1%
3.1
3GUA_I
63.5
2.30E−12
24%
43%
1%
3.1
3GUA_J
63.5
2.30E−12
24%
43%
1%
3.1
3SQ9_A
85.1
6.50E−20
28%
48%
4%
3.1
3SQ9_B
85.1
6.50E−20
28%
48%
4%
3.1
3SQ9_C
85.1
6.50E−20
28%
48%
4%
3.1
3SQ9_D
85.1
6.50E−20
28%
48%
4%
3.1
3SQ9_E
85.1
6.50E−20
28%
48%
4%
3.1
3SQ9_F
85.1
6.50E−20
28%
48%
4%
3.1
3SQ9_G
85.1
6.50E−20
28%
48%
4%
3.1
3SQ9_H
85.1
6.50E−20
28%
48%
4%
3.1
3SQ9_I
85.1
6.50E−20
28%
48%
4%
3.1
3SQ9_J
85.1
6.50E−20
28%
48%
4%
3.1
1LDK_A
28.5
4.9
29%
50%
15%
3.1
1U6G_A
28.1
7.2
29%
50%
15%
3.1
2XZ6_A
62.8
4.70E−12
25%
44%
4%
3.137
2XZ6_B
62.8
4.70E−12
25%
44%
4%
3.137
2XZ6_C
62.8
4.70E−12
25%
44%
4%
3.137
2XZ6_D
62.8
4.70E−12
25%
44%
4%
3.137
2XZ6_E
62.8
4.70E−12
25%
44%
4%
3.137
2XZ6_F
62.8
4.70E−12
25%
44%
4%
3.137
2XZ6_G
62.8
4.70E−12
25%
44%
4%
3.137
2XZ6_H
62.8
4.70E−12
25%
44%
4%
3.137
2XZ6_I
62.8
4.70E−12
25%
44%
4%
3.137
2XZ6_J
62.8
4.70E−12
25%
44%
4%
3.137
3LSV_A
42.7
9.60E−05
24%
43%
7%
3.15
3LSV_B
42.7
9.60E−05
24%
43%
7%
3.15
3LSV_C
42.7
9.60E−05
24%
43%
7%
3.15
3LSV_D
42.7
9.60E−05
24%
43%
7%
3.15
3LSV_E
42.7
9.60E−05
24%
43%
7%
3.15
3UU3_A
40
0.0007
24%
42%
7%
3.15
3UU3_B
40
0.0007
24%
42%
7%
3.15
3UU3_C
40
0.0007
24%
42%
7%
3.15
3UU3_D
40
0.0007
24%
42%
7%
3.15
3UU3_E
40
0.0007
24%
42%
7%
3.15
2XQ9_A
42.7
8.60E−05
24%
43%
7%
3.2
2XQ9_B
42.7
8.60E−05
24%
43%
7%
3.2
2XQ9_C
42.7
8.60E−05
24%
43%
7%
3.2
2XQ9_D
42.7
8.60E−05
24%
43%
7%
3.2
2XQ9_E
42.7
8.60E−05
24%
43%
7%
3.2
3P4W_A
42.7
8.60E−05
24%
43%
7%
3.2
3P4W_B
42.7
8.60E−05
24%
43%
7%
3.2
3P4W_C
42.7
8.60E−05
24%
43%
7%
3.2
3P4W_D
42.7
8.60E−05
24%
43%
7%
3.2
3P4W_E
42.7
8.60E−05
24%
43%
7%
3.2
3TLS_A
42.7
9.00E−05
24%
43%
7%
3.2
3TLS_B
42.7
9.00E−05
24%
43%
7%
3.2
3TLS_C
42.7
9.00E−05
24%
43%
7%
3.2
3TLS_D
42.7
9.00E−05
24%
43%
7%
3.2
3TLS_E
42.7
9.00E−05
24%
43%
7%
3.2
4AFT_A
63.9
1.50E−12
25%
45%
4%
3.2
4AFT_B
63.9
1.50E−12
25%
45%
4%
3.2
4AFT_C
63.9
1.50E−12
25%
45%
4%
3.2
4AFT_D
63.9
1.50E−12
25%
45%
4%
3.2
4AFT_E
63.9
1.50E−12
25%
45%
4%
3.2
2XNT_A
63.5
2.80E−12
24%
44%
4%
3.21
2XNT_B
63.5
2.80E−12
24%
44%
4%
3.21
2XNT_C
63.5
2.80E−12
24%
44%
4%
3.21
2XNT_D
63.5
2.80E−12
24%
44%
4%
3.21
2XNT_E
63.5
2.80E−12
24%
44%
4%
3.21
2XNT_F
63.5
2.80E−12
24%
44%
4%
3.21
2XNT_G
63.5
2.80E−12
24%
44%
4%
3.21
2XNT_H
63.5
2.80E−12
24%
44%
4%
3.21
2XNT_I
63.5
2.80E−12
24%
44%
4%
3.21
2XNT_J
63.5
2.80E−12
24%
44%
4%
3.21
3UU8_A
40
0.00074
24%
42%
7%
3.25
3UU8_B
40
0.00074
24%
42%
7%
3.25
3UU8_C
40
0.00074
24%
42%
7%
3.25
3UU8_D
40
0.00074
24%
42%
7%
3.25
3UU8_E
40
0.00074
24%
42%
7%
3.25
2Y58_A
63.9
1.50E−12
25%
45%
4%
3.25
2Y58_B
63.9
1.50E−12
25%
45%
4%
3.25
2Y58_C
63.9
1.50E−12
25%
45%
4%
3.25
2Y58_D
63.9
1.50E−12
25%
45%
4%
3.25
2Y58_E
63.9
1.50E−12
25%
45%
4%
3.25
3RHW_A
46.2
6.90E−06
22%
44%
4%
3.26
3RHW_B
46.2
6.90E−06
22%
44%
4%
3.26
3RHW_C
46.2
6.90E−06
22%
44%
4%
3.26
3RHW_D
46.2
6.90E−06
22%
44%
4%
3.26
3RHW_E
46.2
6.90E−06
22%
44%
4%
3.26
2VL0_A
27.3
9.7
18%
42%
10%
3.3
2VL0_B
27.3
9.7
18%
42%
10%
3.3
2VL0_C
27.3
9.7
18%
42%
10%
3.3
2VL0_D
27.3
9.7
18%
42%
10%
3.3
2VL0_E
27.3
9.7
18%
42%
10%
3.3
2VL0_F
27.3
9.7
18%
42%
10%
3.3
2VL0_G
27.3
9.7
18%
42%
10%
3.3
2VL0_H
27.3
9.7
18%
42%
10%
3.3
2VL0_I
27.3
9.7
18%
42%
10%
3.3
2VL0_J
27.3
9.7
18%
42%
10%
3.3
2YKS_A
27.3
9.8
18%
42%
10%
3.3
2YKS_B
27.3
9.8
18%
42%
10%
3.3
2YKS_C
27.3
9.8
18%
42%
10%
3.3
2YKS_D
27.3
9.8
18%
42%
10%
3.3
2YKS_E
27.3
9.8
18%
42%
10%
3.3
2YKS_F
27.3
9.8
18%
42%
10%
3.3
2YKS_G
27.3
9.8
18%
42%
10%
3.3
2YKS_H
27.3
9.8
18%
42%
10%
3.3
2YKS_I
27.3
9.8
18%
42%
10%
3.3
2YKS_J
27.3
9.8
18%
42%
10%
3.3
3P50_A
42.7
8.60E−05
24%
43%
7%
3.3
3P50_B
42.7
8.60E−05
24%
43%
7%
3.3
3P50_C
42.7
8.60E−05
24%
43%
7%
3.3
3P50_D
42.7
8.60E−05
24%
43%
7%
3.3
3P50_E
42.7
8.60E−05
24%
43%
7%
3.3
3TLT_A
42.7
0.0001
24%
43%
7%
3.3
3TLT_B
42.7
0.0001
24%
43%
7%
3.3
3TLT_C
42.7
0.0001
24%
43%
7%
3.3
3TLT_D
42.7
0.0001
24%
43%
7%
3.3
3TLT_E
42.7
0.0001
24%
43%
7%
3.3
2Y57_A
63.9
1.50E−12
25%
45%
4%
3.3
2Y57_B
63.9
1.50E−12
25%
45%
4%
3.3
2Y57_C
63.9
1.50E−12
25%
45%
4%
3.3
2Y57_D
63.9
1.50E−12
25%
45%
4%
3.3
2Y57_E
63.9
1.50E−12
25%
45%
4%
3.3
2YN6_A
27.3
9
18%
42%
10%
3.31
2YN6_B
27.3
9
18%
42%
10%
3.31
2YN6_C
27.3
9
18%
42%
10%
3.31
2YN6_D
27.3
9
18%
42%
10%
3.31
2YN6_E
27.3
9
18%
42%
10%
3.31
3RIF_A
46.2
6.90E−06
22%
44%
4%
3.35
3RIF_B
46.2
6.90E−06
22%
44%
4%
3.35
3RIF_C
46.2
6.90E−06
22%
44%
4%
3.35
3RIF_D
46.2
6.90E−06
22%
44%
4%
3.35
3RIF_E
46.2
6.90E−06
22%
44%
4%
3.35
3RI5_A
46.2
6.90E−06
22%
44%
4%
3.4
3RI5_B
46.2
6.90E−06
22%
44%
4%
3.4
3RI5_C
46.2
6.90E−06
22%
44%
4%
3.4
3RI5_D
46.2
6.90E−06
22%
44%
4%
3.4
3RI5_E
46.2
6.90E−06
22%
44%
4%
3.4
2BYQ_A
63.5
2.60E−12
24%
44%
4%
3.4
2BYQ_B
63.5
2.60E−12
24%
44%
4%
3.4
2BYQ_C
63.5
2.60E−12
24%
44%
4%
3.4
2BYQ_D
63.5
2.60E−12
24%
44%
4%
3.4
2BYQ_E
63.5
2.60E−12
24%
44%
4%
3.4
2XQ7_A
42.7
8.70E−05
24%
43%
7%
3.4
2XQ7_B
42.7
8.70E−05
24%
43%
7%
3.4
2XQ7_C
42.7
8.70E−05
24%
43%
7%
3.4
2XQ7_D
42.7
8.70E−05
24%
43%
7%
3.4
2XQ7_E
42.7
8.70E−05
24%
43%
7%
3.4
3UQ4_A
27.3
8.9
18%
42%
10%
3.5
3UQ4_B
27.3
8.9
18%
42%
10%
3.5
3UQ4_C
27.3
8.9
18%
42%
10%
3.5
3UQ4_D
27.3
8.9
18%
42%
10%
3.5
3UQ4_E
27.3
8.9
18%
42%
10%
3.5
3UQ4_F
27.3
8.9
18%
42%
10%
3.5
3UQ4_G
27.3
8.9
18%
42%
10%
3.5
3UQ4_H
27.3
8.9
18%
42%
10%
3.5
3UQ4_I
27.3
8.9
18%
42%
10%
3.5
3UQ4_J
27.3
8.9
18%
42%
10%
3.5
2XQ3_A
42.7
8.70E−05
24%
43%
7%
3.5
2XQ3_B
42.7
8.70E−05
24%
43%
7%
3.5
2XQ3_C
42.7
8.70E−05
24%
43%
7%
3.5
2XQ3_D
42.7
8.70E−05
24%
43%
7%
3.5
2XQ3_E
42.7
8.70E−05
24%
43%
7%
3.5
2XQ5_A
42.7
8.70E−05
24%
43%
7%
3.5
2XQ5_B
42.7
8.70E−05
24%
43%
7%
3.5
2XQ5_C
42.7
8.70E−05
24%
43%
7%
3.5
2XQ5_D
42.7
8.70E−05
24%
43%
7%
3.5
2XQ5_E
42.7
8.70E−05
24%
43%
7%
3.5
3EI0_A
42.7
9.00E−05
24%
43%
7%
3.5
3EI0_B
42.7
9.00E−05
24%
43%
7%
3.5
3EI0_C
42.7
9.00E−05
24%
43%
7%
3.5
3EI0_D
42.7
9.00E−05
24%
43%
7%
3.5
3EI0_E
42.7
9.00E−05
24%
43%
7%
3.5
2Y56_A
63.9
1.50E−12
25%
45%
4%
3.59
2Y56_B
63.9
1.50E−12
25%
45%
4%
3.59
2Y56_C
63.9
1.50E−12
25%
45%
4%
3.59
2Y56_D
63.9
1.50E−12
25%
45%
4%
3.59
2Y56_E
63.9
1.50E−12
25%
45%
4%
3.59
2XQ4_A
42.7
8.70E−05
24%
43%
7%
3.6
2XQ4_B
42.7
8.70E−05
24%
43%
7%
3.6
2XQ4_C
42.7
8.70E−05
24%
43%
7%
3.6
2XQ4_D
42.7
8.70E−05
24%
43%
7%
3.6
2XQ4_E
42.7
8.70E−05
24%
43%
7%
3.6
2XQ8_A
42.7
8.70E−05
24%
43%
7%
3.6
2XQ8_B
42.7
8.70E−05
24%
43%
7%
3.6
2XQ8_C
42.7
8.70E−05
24%
43%
7%
3.6
2XQ8_D
42.7
8.70E−05
24%
43%
7%
3.6
2XQ8_E
42.7
8.70E−05
24%
43%
7%
3.6
2Y54_A
63.9
1.50E−12
25%
45%
4%
3.65
2Y54_B
63.9
1.50E−12
25%
45%
4%
3.65
2Y54_C
63.9
1.50E−12
25%
45%
4%
3.65
2Y54_D
63.9
1.50E−12
25%
45%
4%
3.65
2Y54_E
63.9
1.50E−12
25%
45%
4%
3.65
2XQ6_A
42.7
8.70E−05
24%
43%
7%
3.7
2XQ6_B
42.7
8.70E−05
24%
43%
7%
3.7
2XQ6_C
42.7
8.70E−05
24%
43%
7%
3.7
2XQ6_D
42.7
8.70E−05
24%
43%
7%
3.7
2XQ6_E
42.7
8.70E−05
24%
43%
7%
3.7
2XQA_A
42.7
8.70E−05
24%
43%
7%
3.7
2XQA_B
42.7
8.70E−05
24%
43%
7%
3.7
2XQA_C
42.7
8.70E−05
24%
43%
7%
3.7
2XQA_D
42.7
8.70E−05
24%
43%
7%
3.7
2XQA_E
42.7
8.70E−05
24%
43%
7%
3.7
3UQ7_A
27.3
9.4
18%
42%
10%
3.8
3UQ7_B
27.3
9.4
18%
42%
10%
3.8
3UQ7_C
27.3
9.4
18%
42%
10%
3.8
3UQ7_D
27.3
9.4
18%
42%
10%
3.8
3UQ7_E
27.3
9.4
18%
42%
10%
3.8
3UQ7_F
27.3
9.4
18%
42%
10%
3.8
3UQ7_G
27.3
9.4
18%
42%
10%
3.8
3UQ7_H
27.3
9.4
18%
42%
10%
3.8
3UQ7_I
27.3
9.4
18%
42%
10%
3.8
3UQ7_J
27.3
9.4
18%
42%
10%
3.8
3RIA_A
46.2
6.90E−06
22%
44%
4%
3.8
3RIA_B
46.2
6.90E−06
22%
44%
4%
3.8
3RIA_C
46.2
6.90E−06
22%
44%
4%
3.8
3RIA_D
46.2
6.90E−06
22%
44%
4%
3.8
3RIA_E
46.2
6.90E−06
22%
44%
4%
3.8
2BG9_B
176.4
1.20E−52
40%
65%
3%
4
2BG9_C
191.4
2.00E−58
42%
65%
5%
4
2BG9_A
192.6
7.00E−59
45%
63%
2%
4
2BG9_D
192.6
7.00E−59
45%
63%
2%
4
2BG9_E
199.1
2.60E−61
46%
67%
3%
4
3UQ5_A
27.3
9.4
18%
42%
10%
4.2
3UQ5_B
27.3
9.4
18%
42%
10%
4.2
3UQ5_C
27.3
9.4
18%
42%
10%
4.2
3UQ5_D
27.3
9.4
18%
42%
10%
4.2
3UQ5_E
27.3
9.4
18%
42%
10%
4.2
3UQ5_F
27.3
9.4
18%
42%
10%
4.2
3UQ5_G
27.3
9.4
18%
42%
10%
4.2
3UQ5_H
27.3
9.4
18%
42%
10%
4.2
3UQ5_I
27.3
9.4
18%
42%
10%
4.2
3UQ5_J
27.3
9.4
18%
42%
10%
4.2
1YI5_A
44.3
2.20E−05
24%
40%
3%
4.2
1YI5_B
44.3
2.20E−05
24%
40%
3%
4.2
1YI5_C
44.3
2.20E−05
24%
40%
3%
4.2
1YI5_D
44.3
2.20E−05
24%
40%
3%
4.2
1YI5_E
44.3
2.20E−05
24%
40%
3%
4.2
4AOE_A
57.4
2.90E−10
28%
49%
8%
5.8
4AOE_B
57.4
2.90E−10
28%
49%
8%
5.8
4AOE_C
57.4
2.90E−10
28%
49%
8%
5.8
4AOE_D
57.4
2.90E−10
28%
49%
8%
5.8
4AOE_E
57.4
2.90E−10
28%
49%
8%
5.8
4AOD_A
55.1
2.20E−09
24%
44%
6%
6
4AOD_B
55.1
2.20E−09
24%
44%
6%
6
4AOD_C
55.1
2.20E−09
24%
44%
6%
6
4AOD_D
55.1
2.20E−09
24%
44%
6%
6
4AOD_E
55.1
2.20E−09
24%
44%
6%
6
4AQ5_B
173.7
1.10E−50
39%
62%
5%
6.2
4AQ5_C
188.3
7.60E−56
39%
62%
7%
6.2
4AQ9_B
173.7
1.10E−50
39%
62%
5%
6.2
4AQ9_C
188.3
7.60E−56
39%
62%
7%
6.2
4AQ5_E
198.4
7.00E−60
44%
65%
6%
6.2
4AQ9_E
198.4
7.00E−60
44%
65%
6%
6.2
4AQ5_A
192.6
5.50E−58
45%
63%
2%
6.2
4AQ5_D
192.6
5.50E−58
45%
63%
2%
6.2
4AQ9_A
192.6
5.50E−58
45%
63%
2%
6.2
4AQ9_D
192.6
5.50E−58
45%
63%
2%
6.2
Docking poses of the 11 compounds in the homology model of human α4β2 nACHR
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