Homology Modelling Report

Model Building Report

This document lists the results for the homology modelling project "Untitled Project" submitted to SWISS-MODEL workspace on May 8, 2024, 11:09 a.m..The submitted primary amino acid sequence is given in Table T1.

If you use any results in your research, please cite the relevant publications:

Results

The SWISS-MODEL template library (SMTL version 2024-05-04, PDB release 2024-04-27) was searched with for evolutionary related structures matching the target sequence in Table T1. For details on the template search, see Materials and Methods. Overall 4535 templates were found (Table T2).

Models

The following models were built (see Materials and Methods "Model Building"):

Model #01

File Built with Oligo-State Ligands GMQE QMEANDisCo Global
PDB ProMod3 3.4.0 homo-dimer (matching prediction)
2 x FE2: FE (II) ION;
1 x XPE: 3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL;
0.81 0.80 ± 0.05
Template Seq Identity Oligo-state QSQE Found by Method Resolution Seq Similarity Range Coverage Description
3ovp.1.A 55.75 homo-dimer 0.78 HHblits X-ray 1.70Å 0.46 3 - 234 0.95 Ribulose-phosphate 3-epimerase

Included Ligands

Ligand Description
2 x FE2
FE (II) ION
1 x XPE
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL

Excluded ligands

Ligand Name.Number Reason for Exclusion Description
XPE.2 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.4 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.6 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.7 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.8 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL

Target    MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPGDASNTEKKPTAFFDCH
3ovp.1.A ASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLG-----------QDPFFDMH

Target MMVENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQ
3ovp.1.A MMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQ

Target KFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSRDLLD
3ovp.1.A KFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAAQKRSLD-


Target MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPGDASNTEKKPTAFFDCH
3ovp.1.B ASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLG-----------QDPFFDMH

Target MMVENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQ
3ovp.1.B MMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQ

Target KFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSRDLLD
3ovp.1.B KFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAAQKRSLD-




Model #02

File Built with Oligo-State Ligands GMQE QMEANDisCo Global
PDB ProMod3 3.4.0 homo-dimer (matching prediction)
2 x FE2: FE (II) ION;
0.81 0.80 ± 0.05
Template Seq Identity Oligo-state QSQE Found by Method Resolution Seq Similarity Range Coverage Description
3ovq.1.A 55.75 homo-dimer 0.78 HHblits X-ray 2.00Å 0.46 3 - 232 0.95 Ribulose-phosphate 3-epimerase

Included Ligands

Ligand Description
2 x FE2
FE (II) ION

Excluded ligands

Ligand Name.Number Reason for Exclusion Description
5RP.2 Binding site not conserved.
RIBULOSE-5-PHOSPHATE
5RP.8 Binding site not conserved.
RIBULOSE-5-PHOSPHATE
XPE.3 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.4 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.5 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.6 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.9 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.10 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.11 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL

Target    MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPGDASNTEKKPTAFFDCH
3ovq.1.A ASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLG-----------QDPFFDMH

Target MMVENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQ
3ovq.1.A MMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQ

Target KFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSRDLLD
3ovq.1.A KFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAAQKRSLD-


Target MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPGDASNTEKKPTAFFDCH
3ovq.1.B ASGCKIGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLG-----------QDPFFDMH

Target MMVENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQ
3ovq.1.B MMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQ

Target KFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSRDLLD
3ovq.1.B KFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAAQKRSLD-




Model #03

File Built with Oligo-State Ligands GMQE QMEANDisCo Global
PDB ProMod3 3.4.0 homo-dimer (matching prediction)
2 x FE2: FE (II) ION;
1 x XPE: 3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL;
0.80 0.79 ± 0.05
Template Seq Identity Oligo-state QSQE Found by Method Resolution Seq Similarity Range Coverage Description
3ovp.1.A 57.27 homo-dimer 0.77 BLAST X-ray 1.70Å 0.47 6 - 234 0.92 Ribulose-phosphate 3-epimerase

Included Ligands

Ligand Description
2 x FE2
FE (II) ION
1 x XPE
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL

Excluded ligands

Ligand Name.Number Reason for Exclusion Description
XPE.2 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.4 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.6 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.7 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL
XPE.8 Binding site not conserved.
3,6,9,12,15,18,21,24,27-NONAOXANONACOSANE-1,29-DIOL

Target    MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPGDASNTEKKPTAFFDCH
3ovp.1.A -----IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQ-----------DPFFDMH

Target MMVENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQ
3ovp.1.A MMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQ

Target KFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSRDLLD
3ovp.1.A KFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAAQKRSL--


Target MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPGDASNTEKKPTAFFDCH
3ovp.1.B -----IGPSILNSDLANLGAECLRMLDSGADYLHLDVMDGHFVPNITFGHPVVESLRKQLGQ-----------DPFFDMH

Target MMVENPEKWVDDFAKCGADQFTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQ
3ovp.1.B MMVSKPEQWVKPMAVAGANQYTFHLEATENPGALIKDIRENGMKVGLAIKPGTSVEYLAPWANQIDMALVMTVEPGFGGQ

Target KFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAGANVIVAGTSVFTAADPHDVISFMKEEVSKELRSRDLLD
3ovp.1.B KFMEDMMPKVHWLRTQFPSLDIEVDGGVGPDTVHKCAEAGANMIVSGSAIMRSEDPRSVINLLRNVCSEAAQKRSL--




Materials and Methods

Template Search

Template search with has been performed against the SWISS-MODEL template library (SMTL, last update: 2024-05-04, last included PDB release: 2024-04-27).

Model Building

Models are built based on the target-template alignment using ProMod3 (Studer et al.). Coordinates which are conserved between the target and the template are copied from the template to the model. Insertions and deletions are remodelled using a fragment library. Side chains are then rebuilt. Finally, the geometry of the resulting model is regularized by using a force field.

Model Quality Estimation

The global and per-residue model quality has been assessed using the QMEAN scoring function (Studer et al.).

Ligand Modelling

Ligands present in the template structure are transferred by homology to the model when the following criteria are met: (a) The ligands are annotated as biologically relevant in the template library, (b) the ligand is in contact with the model, (c) the ligand is not clashing with the protein, (d) the residues in contact with the ligand are conserved between the target and the template. If any of these four criteria is not satisfied, a certain ligand will not be included in the model. The model summary includes information on why and which ligand has not been included.

Oligomeric State Conservation

The quaternary structure annotation of the template is used to model the target sequence in its oligomeric form. The method (Bertoni et al.) is based on a supervised machine learning algorithm, Support Vector Machines (SVM), which combines interface conservation, structural clustering, and other template features to provide a quaternary structure quality estimate (QSQE). The QSQE score is a number between 0 and 1, reflecting the expected accuracy of the interchain contacts for a model built based a given alignment and template. Higher numbers indicate higher reliability. This complements the GMQE score which estimates the accuracy of the tertiary structure of the resulting model.

References

Table T1:

Primary amino acid sequence for which templates were searched and models were built.

MVKPIIAPSILASDFANLGCECHKVINAGADWLHIDVMDGHFVPNITLGQPIVTSLRRSVPRPGDASNTEKKPTAFFDCHMMVENPEKWVDDFAKCGADQ
FTFHYEATQDPLHLVKLIKSKGIKAACAIKPGTSVDVLFELAPHLDMALVMTVEPGFGGQKFMEDMMPKVETLRAKFPHLNIQVDGGLGKETIPKAAKAG
ANVIVAGTSVFTAADPHDVISFMKEEVSKELRSRDLLD

Table T2:

Template Seq Identity Oligo-state QSQE Found by Method Resolution Seq Similarity Coverage Description
P46969.1.A 100.00 monomer - AFDB search AlphaFold v2 NA 0.62 1.00 Ribulose-phosphate 3-epimerase
3ovp.1.A 55.75 homo-dimer 0.78 HHblits X-ray 1.70Å 0.46 0.95 Ribulose-phosphate 3-epimerase
3ovq.1.B 55.75 homo-dimer 0.78 HHblits X-ray 2.00Å 0.46 0.95 Ribulose-phosphate 3-epimerase
3ovp.1.A 57.27 homo-dimer 0.77 BLAST X-ray 1.70Å 0.47 0.92 Ribulose-phosphate 3-epimerase
3ovq.1.B 57.27 homo-dimer 0.76 BLAST X-ray 2.00Å 0.47 0.92 Ribulose-phosphate 3-epimerase
3qc3.1.A 56.11 homo-dimer 0.75 HHblits X-ray 2.20Å 0.46 0.93 D-ribulose-5-phosphate-3-epimerase
3qc3.1.A 57.34 homo-dimer 0.74 BLAST X-ray 2.20Å 0.47 0.92 D-ribulose-5-phosphate-3-epimerase
1h1z.1.A 53.00 homo-dimer 0.71 HHblits X-ray 3.40Å 0.46 0.91 D-RIBULOSE-5-PHOSPHATE 3-EPIMERASE
4nu7.1.A 54.13 homo-dimer 0.68 HHblits X-ray 2.05Å 0.46 0.92 Ribulose-phosphate 3-epimerase
1h1z.1.A 55.50 homo-dimer 0.68 BLAST X-ray 3.40Å 0.47 0.88 D-RIBULOSE-5-PHOSPHATE 3-EPIMERASE
4nu7.1.A 55.35 homo-dimer 0.66 BLAST X-ray 2.05Å 0.46 0.90 Ribulose-phosphate 3-epimerase
1tqx.1.A 48.85 monomer - HHblits X-ray 2.00Å 0.43 0.91 D-ribulose-5-phosphate 3-epimerase, putative
2fli.1.A 41.86 homo-hexamer 0.44 HHblits X-ray 1.80Å 0.40 0.90 ribulose-phosphate 3-epimerase
7b1w.1.A 41.20 homo-hexamer 0.38 HHblits X-ray 1.94Å 0.40 0.91 Ribulose-phosphate 3-epimerase
5umf.1.A 41.94 homo-hexamer 0.38 HHblits X-ray 1.40Å 0.40 0.91 Ribulose-phosphate 3-epimerase
1rpx.1.A 40.00 homo-hexamer 0.38 HHblits X-ray 2.30Å 0.40 0.90 PROTEIN (RIBULOSE-PHOSPHATE 3-EPIMERASE)
1rpx.1.A 44.17 homo-hexamer 0.40 BLAST X-ray 2.30Å 0.42 0.87 PROTEIN (RIBULOSE-PHOSPHATE 3-EPIMERASE)
2fli.1.A 46.19 homo-hexamer 0.41 BLAST X-ray 1.80Å 0.42 0.83 ribulose-phosphate 3-epimerase
7u5y.1.A 40.74 homo-hexamer 0.37 HHblits X-ray 2.55Å 0.40 0.91 Ribulose-phosphate 3-epimerase
7b1w.1.A 45.63 homo-hexamer 0.40 BLAST X-ray 1.94Å 0.42 0.87 Ribulose-phosphate 3-epimerase
1tqj.1.A 41.74 homo-hexamer 0.35 HHblits X-ray 1.60Å 0.40 0.92 Ribulose-phosphate 3-epimerase
5umf.1.A 43.13 homo-hexamer 0.36 BLAST X-ray 1.40Å 0.41 0.89 Ribulose-phosphate 3-epimerase
1tqj.1.A 45.28 homo-hexamer 0.37 BLAST X-ray 1.60Å 0.42 0.89 Ribulose-phosphate 3-epimerase
7u5y.1.A 41.51 homo-hexamer 0.34 BLAST X-ray 2.55Å 0.40 0.89 Ribulose-phosphate 3-epimerase
7sbj.1.A 40.83 homo-trimer 0.30 HHblits X-ray 1.85Å 0.40 0.92 Ribulose-phosphate 3-epimerase
7sbj.1.A 41.98 homo-trimer 0.28 BLAST X-ray 1.85Å 0.41 0.89 Ribulose-phosphate 3-epimerase
3inp.1.A 38.43 homo-12-mer 0.08 HHblits X-ray 2.05Å 0.39 0.91 D-ribulose-phosphate 3-epimerase
1tqx.1.A 51.16 monomer - BLAST X-ray 2.00Å 0.44 0.90 D-ribulose-5-phosphate 3-epimerase, putative
3inp.1.A 39.15 homo-12-mer 0.05 BLAST X-ray 2.05Å 0.40 0.89 D-ribulose-phosphate 3-epimerase
3ct7.1.A 36.84 homo-hexamer 0.33 BLAST X-ray 2.50Å 0.39 0.80 D-allulose-6-phosphate 3-epimerase
1so6.1.A 14.69 homo-dimer 0.23 HHblits X-ray 1.90Å 0.27 0.89 3-keto-L-gulonate 6-phosphate decarboxylase
1xby.1.A 15.24 homo-dimer 0.21 HHblits X-ray 1.58Å 0.27 0.88 3-keto-L-gulonate 6-phosphate decarboxylase
1so3.1.A 14.22 homo-dimer 0.18 HHblits X-ray 1.90Å 0.27 0.89 3-keto-L-gulonate 6-phosphate decarboxylase
1so4.1.A 14.22 homo-dimer 0.18 HHblits X-ray 1.70Å 0.27 0.89 3-keto-L-gulonate 6-phosphate decarboxylase
1so5.1.A 15.24 homo-dimer 0.16 HHblits X-ray 1.80Å 0.27 0.88 3-keto-L-gulonate 6-phosphate decarboxylase
3qmr.1.A 18.66 homo-dimer 0.22 HHblits X-ray 1.32Å 0.28 0.88 Orotidine 5'-phosphate decarboxylase
3qms.1.A 18.96 homo-dimer 0.21 HHblits X-ray 1.32Å 0.28 0.89 Orotidine 5'-phosphate decarboxylase
3m1z.1.A 19.05 homo-dimer 0.20 HHblits X-ray 1.42Å 0.28 0.88 Orotidine 5'-phosphate decarboxylase
3qez.1.A 18.48 homo-dimer 0.19 HHblits X-ray 1.54Å 0.28 0.89 Orotidine 5'-phosphate decarboxylase
3m5y.1.A 19.05 homo-dimer 0.20 HHblits X-ray 1.45Å 0.28 0.88 Orotidine 5'-phosphate decarboxylase
3lhw.1.A 18.27 homo-dimer 0.20 HHblits X-ray 1.35Å 0.28 0.87 Orotidine 5'-phosphate decarboxylase
3qf0.1.A 20.57 homo-dimer 0.20 HHblits X-ray 1.34Å 0.29 0.88 Orotidine 5'-phosphate decarboxylase
3pbu.1.A 19.62 homo-dimer 0.20 HHblits X-ray 1.30Å 0.29 0.88 Orotidine 5'-monophosphate decarboxylase
3m41.1.A 18.27 homo-dimer 0.18 HHblits X-ray 1.40Å 0.28 0.87 Orotidine 5'-phosphate decarboxylase
3p60.1.A 19.62 homo-dimer 0.18 HHblits X-ray 1.40Å 0.29 0.88 Orotidine 5'-monophosphate decarboxylase
3sec.1.A 19.52 homo-dimer 0.18 HHblits X-ray 1.70Å 0.28 0.88 Orotidine 5'-phosphate decarboxylase
1km0.1.A 19.05 homo-dimer 0.17 HHblits X-ray 1.70Å 0.28 0.88 OROTIDINE 5'-PHOSPHATE DECARBOXYLASE
1km0.1.B 19.05 homo-dimer 0.16 HHblits X-ray 1.70Å 0.28 0.88 OROTIDINE 5'-PHOSPHATE DECARBOXYLASE
1klz.1.A 19.05 homo-dimer 0.04 HHblits X-ray 1.50Å 0.29 0.88 OROTIDINE 5'-PHOSPHATE DECARBOXYLASE
1kly.1.A 19.05 homo-dimer 0.02 HHblits X-ray 1.50Å 0.28 0.88 OROTIDINE 5'-PHOSPHATE DECARBOXYLASE

The table above shows the top 50 filtered templates. A further 2,322 templates were found which were considered to be less suitable for modelling than the filtered list.
1a3w.1.A, 1a3x.1.A, 1a49.1.B, 1a49.2.B, 1a49.2.C, 1a4m.1.A, 1a53.1.A, 1a5a.1.A, 1al7.2.B, 1al8.1.A, 1aqf.1.A, 1aqf.1.D, 1aqf.2.C, 1aw1.1.A, 1aw2.1.B, 1b00.1.A, 1b00.2.A, 1b3o.2.C, 1bwk.1.A, 1bwl.1.A, 1cl1.1.C, 1dbt.1.A, 1dcf.1.A, 1dqw.1.A, 1dqx.1.A, 1dv7.1.A, 1dvj.1.A, 1dxe.1.A, 1e0t.1.A, 1e0u.1.A, 1e0u.1.C, 1e5e.1.A, 1ea0.1.A, 1eep.1.A, 1ep2.1.C, 1ep3.1.C, 1eua.1.B, 1eua.1.C, 1euc.1.A, 1f3w.1.A, 1f3x.1.A, 1f74.1.D, 1f76.1.A, 1f7b.1.A, 1fcb.1.A, 1fdy.1.D, 1fez.1.A, 1fez.1.B, 1fkw.1.A, 1fkx.1.A, 1fq0.1.B, 1fwr.1.A, 1g4e.1.A, 1g4p.1.A, 1g4s.2.A, 1g4t.2.A, 1g67.1.A, 1g69.1.A, 1geq.1.A, 1gox.1.A, 1gpw.1.A, 1gpw.3.A, 1gth.2.B, 1gwj.1.A, 1gyl.1.A, 1gyl.1.B, 1h1z.1.A, 1h5y.1.A, 1h7w.1.A, 1h7w.2.A, 1hg3.1.A, 1hl2.1.A, 1ho1.1.C, 1ho1.1.E, 1huv.1.A, 1i4n.1.A, 1icp.1.A, 1ixc.1.C, 1ixc.1.D, 1ixn.2.A, 1iz1.1.A, 1iz1.1.B, 1iz1.1.C, 1iz1.1.D, 1j2w.1.A, 1j2w.1.C, 1j5t.1.A, 1jcm.1.A, 1jcn.1.A, 1jjk.5.A, 1jqv.1.A, 1jqx.1.A, 1jr1.1.A, 1jr1.2.A, 1jrb.1.A, 1jrc.1.A, 1jub.1.A, 1jud.1.B, 1juk.1.A, 1jul.1.A, 1k02.1.A, 1k68.1.A, 1k77.1.A, 1ka9.1.B, 1kbi.1.A, 1kbi.1.B, 1kbj.1.A, 1kfc.1.A, 1kfk.1.A, 1kly.1.A, 1klz.1.A, 1km0.1.A, 1km0.1.B, 1km1.1.A, 1km2.1.A, 1km3.1.A, 1km4.1.A, 1km5.1.A, 1km6.1.A, 1l2u.1.A, 1l6w.1.A, 1ldc.1.A, 1ldc.1.B, 1llw.1.A, 1lol.1.A, 1lol.1.B, 1loq.1.A, 1los.1.A, 1los.2.A, 1lrt.1.A, 1ltd.1.A, 1m5t.1.A, 1m5w.1.A, 1m5w.1.B, 1m5w.1.D, 1m5w.1.E, 1m5w.1.F, 1m5w.1.G, 1m6j.1.A, 1me9.1.A, 1meh.1.A, 1mxs.1.A, 1mzh.1.A, 1mzh.1.B, 1n7k.1.A, 1nal.1.A, 1nf7.1.B, 1nvm.1.A, 1nvm.1.C, 1nxz.1.A, 1nxz.1.B, 1o4u.1.A, 1o5k.1.A, 1ofe.1.A, 1ojx.1.A, 1olt.1.A, 1ox6.2.A, 1oyb.1.B, 1p0n.1.A, 1p4c.1.A, 1p90.1.A, 1pii.1.A, 1pkl.1.C, 1pkl.2.C, 1pkm.1.A, 1pkn.1.A, 1pky.1.A, 1pvn.1.A, 1q6r.1.B, 1qap.1.A, 1qap.1.B, 1qcw.1.A, 1qh9.1.A, 1qo2.1.A, 1qo2.2.A, 1qpo.3.A, 1qtw.1.A, 1qum.1.B, 1r30.1.A, 1r3s.1.A, 1rd5.1.A, 1rd5.2.A, 1rdf.1.A, 1rdf.1.B, 1rdf.2.A, 1rdf.2.B, 1rdf.3.A, 1rdf.3.B, 1rlk.1.A, 1rpx.1.A, 1rqb.1.A, 1rql.1.A, 1rql.1.B, 1rv8.1.A, 1rv8.1.B, 1rzw.1.A, 1s3h.1.A, 1s5t.1.A, 1s5v.1.A, 1s5w.1.A, 1so3.1.A, 1so4.1.A, 1so5.1.A, 1so6.1.A, 1swv.1.A, 1sze.1.A, 1szg.1.A, 1t5a.1.A, 1t70.1.A, 1t7l.2.A, 1tb3.1.A, 1te2.1.A, 1thf.1.A, 1tjr.1.A, 1to3.1.A, 1tqj.1.A, 1tqx.1.A, 1tre.1.A, 1ttp.1.A, 1tv5.1.A, 1twd.1.A, 1twd.1.B, 1tww.1.A, 1twy.1.A, 1twy.2.A, 1twy.3.A, 1twy.5.A, 1twy.6.A, 1tx0.2.B, 1tyg.1.B, 1u1h.1.A, 1u1u.1.A, 1u5j.1.A, 1uip.1.A, 1uth.1.B, 1uum.1.A, 1uuo.1.A, 1v5x.1.A, 1v5x.1.B, 1v7y.2.A, 1v7y.3.A, 1vc4.1.A, 1vc4.2.A, 1vcf.2.B, 1vcg.2.B, 1vh7.1.A, 1vhc.1.A, 1vhk.1.A, 1vhk.1.B, 1vhn.1.A, 1vhy.1.A, 1viz.1.A, 1vlw.1.A, 1vqt.1.A, 1vrd.1.A, 1vs1.1.A, 1vs1.1.D, 1vyp.1.A, 1vys.1.A, 1vzw.1.A, 1w0m.1.A, 1w25.1.B, 1w3i.1.A, 1w3t.1.D, 1w8s.1.A, 1wa3.1.A, 1wau.1.A, 1wdw.1.A, 1wn2.1.A, 1wq5.3.B, 1wv2.1.A, 1wx0.1.A, 1wxj.1.A, 1x1o.1.A, 1x1o.1.B, 1x1o.1.C, 1x7i.1.A, 1x7i.1.B, 1xbx.1.A, 1xby.1.A, 1xc4.1.A, 1xcf.1.A, 1xi3.1.A, 1xky.1.A, 1xm3.1.A, 1xp3.1.A, 1xpg.1.A, 1xr2.1.A, 1xty.1.A, 1y0e.1.A, 1yad.1.B, 1yio.1.A, 1ypf.1.A, 1ytd.1.A, 1yx1.1.A, 1yx1.1.B, 1yxy.1.A, 1yya.1.A, 1z44.1.D, 1z88.1.A, 1z88.1.D, 1zes.1.A, 1zfj.1.A, 1zjh.1.C, 1zlp.1.A, 1zn2.1.A, 1znn.1.A, 1zrm.1.A, 1zs9.1.A, 1zy9.1.A, 2a0n.1.A, 2a1y.1.C, 2a6l.1.A, 2a6n.1.A, 2a7r.1.A, 2a85.1.A, 2aba.1.A, 2abb.1.A, 2agk.1.A, 2aqw.1.A, 2b0m.1.A, 2b4g.1.A, 2b7p.1.D, 2ble.1.A, 2btm.1.A, 2bx7.1.A, 2bzn.1.A, 2bzn.2.D, 2c0a.1.A, 2c3z.1.A, 2cff.1.A, 2cff.2.A, 2cu0.1.A, 2cx8.1.A, 2cx8.1.B, 2cz5.1.A, 2cz5.1.B, 2czd.1.A, 2czd.1.B, 2cze.1.A, 2cze.1.B, 2czf.1.A, 2czf.1.B, 2d3k.1.A, 2djx.1.A, 2du2.1.A, 2dw7.1.A, 2dzp.1.A, 2dzs.1.A, 2dzt.1.A, 2dzu.1.A, 2dzv.1.A, 2dzw.1.A, 2dzx.1.A, 2e09.1.A, 2e28.1.A, 2e6d.1.B, 2e6y.1.A, 2e77.1.B, 2eaw.1.A, 2egv.1.A, 2egv.1.B, 2egw.1.A, 2egw.1.B, 2ehh.1.A, 2ekc.1.A, 2ekc.2.A, 2esn.1.A, 2esn.1.B, 2esn.1.C, 2esn.1.D, 2f6g.1.A, 2f6g.1.B, 2f6p.1.A, 2f6p.1.B, 2f6u.1.A, 2f6x.1.A, 2f78.1.A, 2f78.1.B, 2f7a.1.A, 2f7a.1.B, 2f7b.1.A, 2f7c.1.A, 2f7f.1.A, 2f84.1.A, 2f8d.1.A, 2f97.1.B, 2fds.1.A, 2ffc.1.A, 2fi1.1.A, 2fli.1.A, 2fp4.1.A, 2fpt.1.A, 2fq6.1.B, 2fyi.1.A, 2fyi.1.B, 2fyi.2.A, 2g0t.1.A, 2g0w.1.A, 2g50.1.A, 2gjl.1.A, 2gm2.1.A, 2go7.1.A, 2guu.1.A, 2h6r.1.A, 2h6r.1.B, 2h6r.1.C, 2h6r.2.B, 2h8x.1.A, 2h8z.1.B, 2h99.1.A, 2h99.1.B, 2h9a.1.A, 2h9b.1.B, 2hdo.1.A, 2hi0.1.A, 2hi0.2.A, 2hmc.1.A, 2hs8.1.A, 2hsa.1.A, 2hsz.1.A, 2htm.1.A, 2hxr.1.A, 2hxr.1.B, 2iof.1.A, 2iof.1.B, 2ioh.1.A, 2iss.1.A, 2isv.1.B, 2isw.1.A, 2isw.1.B, 2iyn.1.A, 2iyn.3.A, 2iyn.4.B, 2j6x.1.A, 2j6x.1.B, 2j9x.1.A, 2j9y.1.A, 2j9z.1.A, 2jba.1.A, 2jbm.1.A, 2jgq.1.A, 2jgy.1.A, 2jgy.1.B, 2jk1.1.A, 2l82.1.A, 2lle.1.A, 2msn.1.A, 2mu1.1.A, 2nli.1.A, 2no4.1.A, 2no5.1.B, 2nq5.1.A, 2nq9.1.B, 2nqh.1.A, 2nqj.1.C, 2nu6.1.A, 2nu7.1.A, 2nua.1.A, 2nv1.1.A, 2nv2.1.A, 2nx9.1.A, 2nyv.1.A, 2nzl.1.A, 2o7q.2.A, 2oda.1.A, 2ojp.1.A, 2opj.1.A, 2oz0.1.A, 2oz0.1.B, 2oz8.1.A, 2pcq.1.A, 2pkf.1.B, 2pkf.3.A, 2pkn.1.A, 2pp1.2.B, 2pr7.1.A, 2pur.1.A, 2q3o.1.A, 2q3o.2.A, 2q3r.1.A, 2q8l.1.B, 2qcd.1.A, 2qcf.1.A, 2qf7.1.A, 2qf7.1.B, 2qjg.1.A, 2qr3.1.A, 2qr6.1.A, 2qvh.1.B, 2r14.1.A, 2r91.1.A, 2rdu.1.D, 2rfg.1.A, 2rkx.1.A, 2trs.1.C, 2tsy.1.C, 2tys.1.C, 2v0n.1.A, 2v0n.1.B, 2v30.1.A, 2v5j.1.A, 2v81.1.A, 2vdc.1.A, 2vep.1.A, 2vgb.1.A, 2vgf.1.A, 2vgf.1.C, 2vgg.1.A, 2vgi.1.A, 2vp8.1.A, 2vp8.1.B, 2vui.1.B, 2w0u.1.A, 2w6r.1.A, 2w79.1.A, 2w79.2.A, 2wb4.1.A, 2wb4.1.B, 2wjz.1.A, 2wkj.1.A, 2wm8.1.A, 2wnn.1.A, 2wnq.1.D, 2wo5.1.A, 2wsy.1.C, 2wv8.1.A, 2x30.1.A, 2x7v.1.A, 2y0f.1.A, 2y0f.1.B, 2y0f.2.A, 2y0f.2.B, 2y7d.1.D, 2y7f.1.A, 2y7k.1.A, 2y7k.1.B, 2y7k.2.A, 2y7p.1.B, 2y7r.1.A, 2y7r.4.B, 2y7w.1.A, 2y84.1.A, 2y84.1.B, 2y85.1.A, 2y88.1.A, 2y89.1.A, 2yce.1.A, 2ycl.1.A, 2yda.1.A, 2ygy.1.B, 2yr1.1.A, 2yr1.1.B, 2yw4.1.A, 2yxb.1.A, 2yxg.1.A, 2yy6.1.A, 2yy6.2.A, 2yyt.1.A, 2yyu.1.A, 2yyu.1.B, 2yzr.1.A, 2z6j.1.A, 2za1.1.A, 2za1.1.B, 2za2.1.A, 2za2.1.B, 2za3.1.A, 2za3.1.B, 2zay.1.A, 2zay.2.A, 2zbt.1.A, 2zds.1.A, 2zfa.1.C, 2zg6.1.A, 2zrz.1.A, 2zv3.1.A, 2zv3.3.B, 2zv3.4.A, 2zv3.4.B, 2zwy.1.A, 2zz2.1.B, 2zz3.1.A, 2zz4.1.A, 2zz5.1.A, 3a5f.1.C, 3a9i.1.A, 3aal.1.A, 3aam.1.A, 3ab7.1.A, 3ab7.3.A, 3ab8.1.A, 3ajx.1.A, 3aty.1.A, 3b0p.1.A, 3b0p.2.A, 3b0u.1.A, 3b0v.1.B, 3b8i.1.A, 3bg3.1.A, 3bg3.1.B, 3bg3.1.C, 3bg3.1.D, 3bg5.1.A, 3bg5.1.B, 3bg5.1.C, 3bg5.1.D, 3bg9.1.A, 3bic.1.A, 3bjf.1.A, 3bjt.1.A, 3bk0.1.B, 3bo9.1.A, 3bpw.1.A, 3bre.1.A, 3bre.1.B, 3bvj.1.B, 3bw2.1.A, 3bw3.1.A, 3bw4.1.A, 3c2e.1.A, 3c2f.1.A, 3c2r.1.A, 3c2v.1.A, 3c3n.1.A, 3c4u.1.B, 3c61.1.A, 3c85.1.A, 3c85.1.B, 3c85.2.A, 3c85.2.B, 3c97.1.A, 3ceu.1.A, 3ceu.2.A, 3ch0.1.A, 3chv.1.A, 3cjp.1.A, 3cpr.1.A, 3ct7.1.A, 3cu2.1.A, 3cwo.1.A, 3d0c.1.A, 3daq.1.A, 3den.1.A, 3dh7.1.A, 3di0.1.A, 3dx5.1.A, 3dxi.1.A, 3e0v.1.A, 3e0w.1.A, 3e96.1.A, 3eb2.1.A, 3elp.1.A, 3eoe.1.B, 3erj.1.A, 3erj.1.B, 3ewx.1.A, 3ewz.1.A, 3exr.1.A, 3exs.1.A, 3exs.2.B, 3eyw.1.A, 3eyw.1.B, 3f4n.1.A, 3f4w.1.A, 3fem.1.A, 3ffs.1.A, 3ffs.1.B, 3ffs.1.D, 3flu.1.A, 3fok.1.A, 3fwz.1.A, 3fxr.1.C, 3fxr.1.D, 3fzj.1.C, 3fzj.3.D, 3g0s.1.A, 3g18.1.B, 3g1f.5.A, 3g1h.1.B, 3g1h.6.B, 3g1s.1.A, 3g1v.1.B, 3g1y.1.A, 3g22.1.A, 3g2g.1.A, 3gak.1.A, 3gb6.1.A, 3gdk.1.A, 3gdl.1.A, 3gdm.1.A, 3gdr.1.A, 3gg8.1.A, 3gg8.1.B, 3gg8.1.C, 3gk0.1.A, 3gkf.1.A, 3glb.1.A, 3glb.1.B, 3glb.2.A, 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