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SWISS-MODEL Homology Modelling Report

Model Building Report

This document lists the results for the homology modelling project "crp1wotemplate" submitted to SWISS-MODEL workspace on Feb. 11, 2017, 8:26 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:

Marco Biasini; Stefan Bienert; Andrew Waterhouse; Konstantin Arnold; Gabriel Studer; Tobias Schmidt; Florian Kiefer; Tiziano Gallo Cassarino; Martino Bertoni; Lorenza Bordoli; Torsten Schwede. (2014). SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Research (1 July 2014) 42 (W1): W252-W258; doi: 10.1093/nar/gku340.
Arnold, K., Bordoli, L., Kopp, J. and Schwede, T. (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics, 22, 195-201.
Benkert, P., Biasini, M. and Schwede, T. (2011) Toward the estimation of the absolute quality of individual protein structure models. Bioinformatics, 27, 343-350

Results

The SWISS-MODEL template library (SMTL version 2017-02-08, PDB release 2017-02-03) was searched with Blast (Altschul et al., 1997) and HHBlits (Remmert, et al., 2011) for evolutionary related structures matching the target sequence in Table T1. For details on the template search, see Materials and Methods. Overall 217 templates were found (Table T2).

Models

The following model was built (see Materials and Methods "Model Building"):

Model #01	File	Built with	Oligo-State	Ligands	GMQE	QMEAN
	PDB	ProMod3 Version 1.0.2.	MONOMER (matching prediction)	None	0.83	-0.54

QMEAN	-0.54
Cβ	-1.30
All Atom	-1.03
Solvation	-1.03
Torsion	0.01

Template	Seq Identity	Oligo-state	Found by	Method	Resolution	Seq Similarity	Range	Coverage	Description
4pbo.1.A	64.53	homo-trimer	BLAST	X-ray	1.70Å	0.50	3 - 206	0.99	C-reactive protein

The template contained no ligands.

Target    MVGLAGKVLLFPYETDFSYVKLTPKKPLGLSAFTLCMRVATELQGERQIILFAYRTPDFDELNLWREKDGRVSFYL--SG
4pbo.1.A  --NLSGKVLQFKTATDNSYVKLYPEKPLSLSAFTLCMRVATELPLDREVILFAYYTPDVDELNVWRERDGRVSLYIQSSK

Target    DGAFFNLPPLSTFRTHLCLSWSSRTGLAAFWVDGRRSAFQLYKPGHSIRPQGTALLGQDPDKLLGDFETVQSFAGELTDL
4pbo.1.A  DAAFFRLPPLSTLQTHLCVAWESATGLTAFWMDGRRSLHQVYRKGYSIRSGGTVVLGQDPDSYVGSFDVDQSFVGEIANL

Target    NMWDYVLTGNQIKALYFNHAQRVPKANVFEWSSIEYEIKGNVLVTQDD
4pbo.1.A  QMWDYVLSSAQIKAVYYNQDNRV-KGNVFDWDTIEYDVTGNVLVVPDN

Materials and Methods

Template Search

Template search with Blast and HHBlits has been performed against the SWISS-MODEL template library (SMTL, last update: 2017-02-08, last included PDB release: 2017-02-03).

The target sequence was searched with BLAST (Altschul et al., 1997) against the primary amino acid sequence contained in the SMTL. A total of 16 templates were found.

An initial HHblits profile has been built using the procedure outlined in (Remmert, et al., 2011), followed by 1 iteration of HHblits against NR20. The obtained profile has then be searched against all profiles of the SMTL. A total of 205 templates were found.

Template Selection

For each identified template, the template's quality has been predicted from features of the target-template alignment. The templates with the highest quality have then been selected for model building.

Model Building

Models are built based on the target-template alignment using ProMod3. 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. In case loop modelling with ProMod3 fails, an alternative model is built with PROMOD-II (Guex, et al., 1997).

Model Quality Estimation

The global and per-residue model quality has been assessed using the QMEAN scoring function (Benkert, et al., 2011) . For improved performance, weights of the individual QMEAN terms have been trained specifically for SWISS-MODEL.

Ligand Modelling

Ligands present in the template structure are transferred by homology to the model when the following criteria are met (Gallo -Casserino, to be published): (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

Homo-oligomeric structure of the target protein is predicted based on the analysis of pairwise interfaces of the identified template structures. For each relevant interface between polypeptide chains (interfaces with more than 10 residue-residue interactions), the QscoreOligomer (Mariani et al., 2011) is predicted from features such as similarity to target and frequency of observing this interface in the identified templates (Kiefer, Bertoni, Biasini, to be published). The prediction is performed with a random forest regressor using these features as input parameters to predict the probability of conservation for each interface. The QscoreOligomer of the whole complex is then calculated as the weight-averaged QscoreOligomer of the interfaces. The oligomeric state of the target is predicted to be the same as in the template when QscoreOligomer is predicted to be higher or equal to 0.5.

References

Altschul, S.F., Madden, T.L., Schaffer, A.A., Zhang, J., Zhang, Z., Miller, W. and Lipman, D.J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res, 25, 3389-3402.
Remmert, M., Biegert, A., Hauser, A. and Soding, J. (2012) HHblits: lightning-fast iterative protein sequence searching by HMM-HMM alignment. Nat Methods, 9, 173-175.
Guex, N. and Peitsch, M.C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis, 18, 2714-2723.
Sali, A. and Blundell, T.L. (1993) Comparative protein modelling by satisfaction of spatial restraints. J Mol Biol, 234, 779-815.
Benkert, P., Biasini, M. and Schwede, T. (2011) Toward the estimation of the absolute quality of individual protein structure models. Bioinformatics, 27, 343-350.
Mariani, V., Kiefer, F., Schmidt, T., Haas, J. and Schwede, T. (2011) Assessment of template based protein structure predictions in CASP9. Proteins, 79 Suppl 10, 37-58.

Table T1:

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

MVGLAGKVLLFPYETDFSYVKLTPKKPLGLSAFTLCMRVATELQGERQIILFAYRTPDFDELNLWREKDGRVSFYLSGDGAFFNLPPLSTFRTHLCLSWS
SRTGLAAFWVDGRRSAFQLYKPGHSIRPQGTALLGQDPDKLLGDFETVQSFAGELTDLNMWDYVLTGNQIKALYFNHAQRVPKANVFEWSSIEYEIKGNV
LVTQDD

Table T2:

Template	Seq Identity	Oligo-state	Found by	Method	Resolution	Seq Similarity	Coverage	Description
4pbp.1.A	64.53	homo-trimer	BLAST	X-ray	1.65Å	0.50	0.99	C-reactive protein
4pbo.1.A	64.53	homo-trimer	BLAST	X-ray	1.70Å	0.50	0.99	C-reactive protein
4pbo.1.A	62.75	homo-trimer	HHblits	X-ray	1.70Å	0.49	0.99	C-reactive protein
4pbp.1.A	62.75	homo-trimer	HHblits	X-ray	1.65Å	0.49	0.99	C-reactive protein
1b09.1.A	33.33	homo-pentamer	HHblits	X-ray	2.50Å	0.39	0.98	PROTEIN (C-REACTIVE PROTEIN)
1gnh.1.D	33.33	homo-pentamer	HHblits	X-ray	3.00Å	0.39	0.98	C-REACTIVE PROTEIN
1lj7.1.A	33.33	homo-pentamer	HHblits	X-ray	3.15Å	0.39	0.98	C-reactive protein
3pvn.4.D	33.33	homo-pentamer	HHblits	X-ray	1.98Å	0.39	0.98	C-reactive protein
3pvn.2.A	33.33	homo-pentamer	HHblits	X-ray	1.98Å	0.39	0.98	C-reactive protein
3pvn.3.B	33.33	homo-pentamer	HHblits	X-ray	1.98Å	0.39	0.98	C-reactive protein
3pvn.3.C	33.33	homo-pentamer	HHblits	X-ray	1.98Å	0.39	0.98	C-reactive protein
1b09.1.A	34.87	homo-pentamer	BLAST	X-ray	2.50Å	0.39	0.95	PROTEIN (C-REACTIVE PROTEIN)
1gnh.1.D	34.87	homo-pentamer	BLAST	X-ray	3.00Å	0.39	0.95	C-REACTIVE PROTEIN
1lj7.1.A	34.87	homo-pentamer	BLAST	X-ray	3.15Å	0.39	0.95	C-reactive protein
3pvn.4.D	34.87	homo-pentamer	BLAST	X-ray	1.98Å	0.39	0.95	C-reactive protein
3pvn.2.A	34.87	homo-pentamer	BLAST	X-ray	1.98Å	0.39	0.95	C-reactive protein
3pvn.3.B	34.87	homo-pentamer	BLAST	X-ray	1.98Å	0.39	0.95	C-reactive protein
3pvn.3.C	34.87	homo-pentamer	BLAST	X-ray	1.98Å	0.39	0.95	C-reactive protein
2a3w.1.A	34.17	homo-10-mer	HHblits	X-ray	2.20Å	0.37	0.97	Serum amyloid P-component
3d5o.1.D	34.17	hetero-oligomer	HHblits	X-ray	2.80Å	0.37	0.97	Serum amyloid P-component
3d5o.1.E	34.17	hetero-oligomer	HHblits	X-ray	2.80Å	0.37	0.97	Serum amyloid P-component
3d5o.1.F	34.17	hetero-oligomer	HHblits	X-ray	2.80Å	0.37	0.97	Serum amyloid P-component
3d5o.1.B	34.17	hetero-oligomer	HHblits	X-ray	2.80Å	0.37	0.97	Serum amyloid P-component
3d5o.1.C	34.17	hetero-oligomer	HHblits	X-ray	2.80Å	0.37	0.97	Serum amyloid P-component
2a3w.1.A	36.27	homo-10-mer	BLAST	X-ray	2.20Å	0.38	0.94	Serum amyloid P-component
3d5o.1.D	36.27	hetero-oligomer	BLAST	X-ray	2.80Å	0.38	0.94	Serum amyloid P-component
3d5o.1.E	36.27	hetero-oligomer	BLAST	X-ray	2.80Å	0.38	0.94	Serum amyloid P-component
3d5o.1.F	36.27	hetero-oligomer	BLAST	X-ray	2.80Å	0.38	0.94	Serum amyloid P-component
3d5o.1.B	36.27	hetero-oligomer	BLAST	X-ray	2.80Å	0.38	0.94	Serum amyloid P-component
3d5o.1.C	36.27	hetero-oligomer	BLAST	X-ray	2.80Å	0.38	0.94	Serum amyloid P-component
3flt.1.A	23.38	homo-16-mer	HHblits	X-ray	2.70Å	0.33	0.98	SAP-like pentraxin
4qvs.1.A	18.34	homo-dimer	HHblits	X-ray	2.10Å	0.29	0.82	S-layer domain-containing protein
4dqa.1.A	13.94	monomer	HHblits	X-ray	1.50Å	0.27	0.80	uncharacterized protein
1g9c.1.A	11.18	monomer	HHblits	X-ray	2.35Å	0.27	0.78	BOTULINUM NEUROTOXIN TYPE B
2np0.1.A	11.18	hetero-oligomer	HHblits	X-ray	2.62Å	0.27	0.78	Botulinum neurotoxin type B
4zkt.1.A	13.75	hetero-oligomer	HHblits	X-ray	3.05Å	0.26	0.78	Bontoxilysin A
3ffz.1.A	13.75	monomer	HHblits	X-ray	2.65Å	0.26	0.78	Botulinum neurotoxin type E
3ffz.2.A	13.75	monomer	HHblits	X-ray	2.65Å	0.26	0.78	Botulinum neurotoxin type E
5hon.1.A	15.92	monomer	HHblits	X-ray	2.00Å	0.28	0.76	Extracellular arabinanase
1diw.1.A	9.94	monomer	HHblits	X-ray	2.00Å	0.25	0.78	TETANUS TOXIN HC
1yxw.1.A	9.32	monomer	HHblits	X-ray	2.20Å	0.25	0.78	Tetanus toxin (Tentoxylysin)
1dll.1.A	9.32	monomer	HHblits	X-ray	1.80Å	0.25	0.78	TETANUS TOXIN
3hn1.1.A	9.32	monomer	HHblits	X-ray	2.10Å	0.25	0.78	Tetanus toxin
1a8d.1.A	9.32	monomer	HHblits	X-ray	1.57Å	0.25	0.78	TETANUS NEUROTOXIN
1af9.1.A	9.32	monomer	HHblits	X-ray	2.70Å	0.25	0.78	TETANUS NEUROTOXIN
1dfq.1.A	10.00	monomer	HHblits	X-ray	2.60Å	0.25	0.78	TETANUS TOXIN HC
1d0h.1.A	10.00	monomer	HHblits	X-ray	2.10Å	0.25	0.78	PROTEIN (TETANUS TOXIN HC)
5mc9.1.A	12.58	hetero-oligomer	HHblits	X-ray	2.13Å	0.25	0.77	Laminin subunit alpha-1
5ho2.1.A	14.74	monomer	HHblits	X-ray	2.37Å	0.27	0.76	Extracellular arabinanase
5ho0.1.A	14.74	monomer	HHblits	X-ray	2.35Å	0.27	0.76	Extracellular arabinanase
5hp6.1.A	14.74	monomer	HHblits	X-ray	2.09Å	0.27	0.76	Extracellular arabinanase
3asi.1.A	12.26	monomer	HHblits	X-ray	2.30Å	0.26	0.75	Neurexin-1-alpha
2sli.1.A	12.34	monomer	HHblits	X-ray	1.80Å	0.27	0.75	INTRAMOLECULAR TRANS-SIALIDASE
3vuo.1.A	12.99	monomer	HHblits	X-ray	3.90Å	0.26	0.75	NTNHA
2h0b.1.A	12.90	monomer	HHblits	X-ray	2.10Å	0.26	0.75	Neurexin-1-alpha
1pz8.1.A	14.19	monomer	HHblits	X-ray	2.35Å	0.26	0.75	Agrin
1pz9.2.A	14.19	monomer	HHblits	X-ray	2.80Å	0.26	0.75	Agrin
1pz9.1.A	14.19	monomer	HHblits	X-ray	2.80Å	0.26	0.75	Agrin
4xe9.1.A	11.84	monomer	HHblits	X-ray	1.84Å	0.27	0.74	Sialidase B
4xmi.1.A	11.84	monomer	HHblits	X-ray	1.97Å	0.27	0.74	Sialidase B
4c1w.1.A	15.03	monomer	HHblits	X-ray	1.84Å	0.27	0.74	NEURAMINIDASE
1q56.1.A	12.18	monomer	HHblits	NMR	NA	0.25	0.76	Agrin
3poy.1.A	14.38	monomer	HHblits	X-ray	3.02Å	0.26	0.74	Neurexin-1-alpha
3v0a.1.B	11.69	hetero-oligomer	HHblits	X-ray	2.70Å	0.26	0.75	NTNH
1kdm.1.A	14.84	homo-dimer	HHblits	X-ray	2.35Å	0.25	0.75	sex hormone-binding globulin
1kdk.1.A	14.84	homo-dimer	HHblits	X-ray	1.70Å	0.25	0.75	Sex Hormone-Binding Globulin
4xyx.1.A	12.00	monomer	HHblits	X-ray	2.10Å	0.27	0.73	Sialidase B
4xog.1.A	12.00	monomer	HHblits	X-ray	2.09Å	0.27	0.73	Sialidase B
4zkt.1.B	12.42	hetero-oligomer	HHblits	X-ray	3.05Å	0.26	0.74	Botulinum neurotoxin type E, nontoxic-nonhemagglutinin component, NTNH
1pz7.1.A	14.38	monomer	HHblits	X-ray	1.42Å	0.26	0.74	Agrin
1pz7.2.A	14.38	monomer	HHblits	X-ray	1.42Å	0.26	0.74	Agrin
4yw1.1.A	12.08	monomer	HHblits	X-ray	2.25Å	0.27	0.72	Neuraminidase C
4yz1.1.A	12.08	monomer	HHblits	X-ray	1.97Å	0.27	0.72	Putative neuraminidase
3pve.1.A	15.23	monomer	HHblits	X-ray	1.40Å	0.26	0.73	Agrin, Agrin protein
5mc9.1.A	16.11	hetero-oligomer	HHblits	X-ray	2.13Å	0.27	0.72	Laminin subunit alpha-1
3v64.1.B	13.82	hetero-oligomer	HHblits	X-ray	2.85Å	0.25	0.74	Low-density lipoprotein receptor-related protein 4
3v64.1.C	13.82	hetero-oligomer	HHblits	X-ray	2.85Å	0.25	0.74	Low-density lipoprotein receptor-related protein 4
3v65.1.A	13.82	hetero-oligomer	HHblits	X-ray	3.30Å	0.25	0.74	Agrin
3v65.1.D	13.82	hetero-oligomer	HHblits	X-ray	3.30Å	0.25	0.74	Agrin
2jkb.1.A	12.16	monomer	HHblits	X-ray	1.54Å	0.27	0.72	SIALIDASE B
2wjs.1.A	14.67	monomer	HHblits	X-ray	2.80Å	0.26	0.73	LAMININ SUBUNIT ALPHA-2
2jd4.1.A	11.92	monomer	HHblits	X-ray	1.90Å	0.25	0.73	LAMININ SUBUNIT ALPHA-1
2jd4.2.A	11.92	monomer	HHblits	X-ray	1.90Å	0.25	0.73	LAMININ SUBUNIT ALPHA-1
2vw2.1.A	12.16	monomer	HHblits	X-ray	1.70Å	0.27	0.72	SIALIDASE B
2r16.1.A	15.44	monomer	HHblits	X-ray	1.04Å	0.26	0.72	Neurexin-1-alpha
5ik4.1.A	14.67	monomer	HHblits	X-ray	1.27Å	0.26	0.73	Laminin subunit alpha-2
1lhv.1.A	15.23	homo-dimer	HHblits	X-ray	2.00Å	0.25	0.73	SEX HORMONE-BINDING GLOBULIN
2wjs.1.A	14.19	monomer	HHblits	X-ray	2.80Å	0.26	0.72	LAMININ SUBUNIT ALPHA-2
5ik7.1.A	15.54	monomer	HHblits	X-ray	2.00Å	0.26	0.72	Laminin subunit alpha-2
5ik7.2.A	15.54	monomer	HHblits	X-ray	2.00Å	0.26	0.72	Laminin subunit alpha-2
1dyk.1.A	15.54	monomer	HHblits	X-ray	2.00Å	0.26	0.72	LAMININ ALPHA 2 CHAIN
1okq.1.A	14.09	monomer	HHblits	X-ray	2.80Å	0.25	0.72	LAMININ ALPHA 2 CHAIN
1d2s.1.A	16.11	homo-dimer	HHblits	X-ray	1.55Å	0.25	0.72	SEX HORMONE-BINDING GLOBULIN
3r05.1.A	12.93	monomer	HHblits	X-ray	2.95Å	0.26	0.71	Neurexin-1-alpha
1qu0.1.A	12.84	homo-dimer	HHblits	X-ray	2.35Å	0.25	0.72	LAMININ ALPHA2 CHAIN
3b3q.1.C	17.48	hetero-oligomer	HHblits	X-ray	2.40Å	0.27	0.69	NRXN1 protein
3poy.1.A	13.89	monomer	HHblits	X-ray	3.02Å	0.27	0.70	Neurexin-1-alpha
3qcw.1.A	13.89	monomer	HHblits	X-ray	2.65Å	0.27	0.70	Neurexin-1-alpha
3r05.1.A	13.99	monomer	HHblits	X-ray	2.95Å	0.27	0.69	Neurexin-1-alpha
3asi.1.A	19.15	monomer	HHblits	X-ray	2.30Å	0.28	0.68	Neurexin-1-alpha
2xb6.1.B	17.61	hetero-oligomer	HHblits	X-ray	2.60Å	0.27	0.69	NEUREXIN-1-BETA
2wqz.1.B	17.61	hetero-oligomer	HHblits	X-ray	3.90Å	0.27	0.69	NEUREXIN-1-BETA
3vkf.1.C	16.08	hetero-oligomer	HHblits	X-ray	3.30Å	0.27	0.69	Neurexin-1-beta
3vkf.1.D	16.08	hetero-oligomer	HHblits	X-ray	3.30Å	0.27	0.69	Neurexin-1-beta
1f5f.1.A	15.86	homo-dimer	HHblits	X-ray	1.70Å	0.26	0.70	SEX HORMONE-BINDING GLOBULIN
3sh4.1.A	15.60	monomer	HHblits	X-ray	1.50Å	0.27	0.68	LG3 peptide
3sh5.1.A	15.60	monomer	HHblits	X-ray	2.80Å	0.27	0.68	LG3 peptide
5fre.1.A	13.48	monomer	HHblits	X-ray	1.90Å	0.27	0.68	EXO-ALPHA-SIALIDASE
5fra.1.A	13.48	monomer	HHblits	X-ray	2.00Å	0.27	0.68	SIALIDASE
2jd4.1.A	15.60	monomer	HHblits	X-ray	1.90Å	0.27	0.68	LAMININ SUBUNIT ALPHA-1
2jd4.2.A	15.60	monomer	HHblits	X-ray	1.90Å	0.27	0.68	LAMININ SUBUNIT ALPHA-1
3mw3.1.A	14.89	monomer	HHblits	X-ray	2.33Å	0.26	0.68	Neurexin-2-beta
1c4r.1.A	19.57	monomer	HHblits	X-ray	2.60Å	0.28	0.67	NEUREXIN-I BETA
3r4u.1.A	11.19	monomer	HHblits	X-ray	2.20Å	0.25	0.69	Botulinum neurotoxin type C1
3bop.1.A	16.43	monomer	HHblits	X-ray	3.00Å	0.27	0.68	beta-Neurexin 2D4
3bop.2.A	16.43	monomer	HHblits	X-ray	3.00Å	0.27	0.68	beta-Neurexin 2D4
3bop.3.A	16.43	monomer	HHblits	X-ray	3.00Å	0.27	0.68	beta-Neurexin 2D4
5ik7.1.A	13.38	monomer	HHblits	X-ray	2.00Å	0.26	0.69	Laminin subunit alpha-2
5ik7.2.A	13.38	monomer	HHblits	X-ray	2.00Å	0.26	0.69	Laminin subunit alpha-2
3n7l.1.A	9.79	monomer	HHblits	X-ray	2.00Å	0.25	0.69	Neurotoxin
4isq.1.A	9.79	hetero-oligomer	HHblits	X-ray	2.65Å	0.25	0.69	Neurotoxin
4isq.2.A	9.79	hetero-oligomer	HHblits	X-ray	2.65Å	0.25	0.69	Neurotoxin
4isq.3.A	9.79	hetero-oligomer	HHblits	X-ray	2.65Å	0.25	0.69	Neurotoxin
4isr.3.A	9.79	hetero-oligomer	HHblits	X-ray	2.59Å	0.25	0.69	Neurotoxin
3bod.1.A	16.55	monomer	HHblits	X-ray	1.70Å	0.27	0.67	Neurexin-1-alpha
3n7k.1.A	10.56	monomer	HHblits	X-ray	2.50Å	0.25	0.69	Botulinum neurotoxin type C1
2nz9.1.A	14.49	hetero-oligomer	HHblits	X-ray	3.79Å	0.27	0.67	Botulinum neurotoxin type A
3bta.1.A	14.49	monomer	HHblits	X-ray	3.20Å	0.27	0.67	PROTEIN (BOTULINUM NEUROTOXIN TYPE A)
3v0a.1.A	14.49	hetero-oligomer	HHblits	X-ray	2.70Å	0.27	0.67	BoNT/A
3v0c.1.A	14.49	monomer	HHblits	X-ray	4.30Å	0.27	0.67	BoNT/A
3n7m.1.A	9.15	monomer	HHblits	X-ray	2.60Å	0.25	0.69	Neurotoxin
4fvv.1.A	9.15	monomer	HHblits	X-ray	2.70Å	0.25	0.69	Neurotoxin
1okq.1.A	13.48	monomer	HHblits	X-ray	2.80Å	0.25	0.68	LAMININ ALPHA 2 CHAIN
3azw.1.A	9.15	monomer	HHblits	X-ray	2.99Å	0.25	0.69	D/C mosaic neurotoxin
3azw.2.A	9.15	monomer	HHblits	X-ray	2.99Å	0.25	0.69	D/C mosaic neurotoxin
3azv.1.A	9.15	monomer	HHblits	X-ray	3.10Å	0.25	0.69	D/C mosaic neurotoxin
3azv.2.A	9.15	monomer	HHblits	X-ray	3.10Å	0.25	0.69	D/C mosaic neurotoxin
5ik4.1.A	12.77	monomer	HHblits	X-ray	1.27Å	0.25	0.68	Laminin subunit alpha-2
3mw4.1.A	14.49	monomer	HHblits	X-ray	2.00Å	0.27	0.67	Neurexin-2-beta
4ra0.1.A	13.29	hetero-oligomer	HHblits	X-ray	3.07Å	0.24	0.69	Growth arrest-specific protein 6
2v73.1.A	13.57	monomer	HHblits	X-ray	2.20Å	0.25	0.68	PUTATIVE EXO-ALPHA-SIALIDASE
1dyk.1.A	12.77	monomer	HHblits	X-ray	2.00Å	0.25	0.68	LAMININ ALPHA 2 CHAIN
1mz6.1.A	15.94	monomer	HHblits	X-ray	2.90Å	0.27	0.67	sialidase
3obr.1.A	10.22	monomer	HHblits	X-ray	1.72Å	0.27	0.67	Botulinum neurotoxin type D
3pme.1.A	9.49	monomer	HHblits	X-ray	1.56Å	0.27	0.67	Type C neurotoxin
4f83.1.A	9.49	monomer	HHblits	X-ray	1.70Å	0.27	0.67	Type C neurotoxin
3rmy.2.A	10.22	monomer	HHblits	X-ray	2.30Å	0.27	0.67	Botulinum neurotoxin type D
3rmy.1.A	10.22	monomer	HHblits	X-ray	2.30Å	0.27	0.67	Botulinum neurotoxin type D
3rmy.4.A	10.22	monomer	HHblits	X-ray	2.30Å	0.27	0.67	Botulinum neurotoxin type D
3ogg.1.A	10.22	monomer	HHblits	X-ray	1.65Å	0.27	0.67	Botulinum neurotoxin type D
3n7j.1.A	10.22	monomer	HHblits	X-ray	2.00Å	0.27	0.67	Botulinum neurotoxin type D
3rmx.1.A	10.22	monomer	HHblits	X-ray	2.75Å	0.27	0.67	Botulinum neurotoxin type D
3rmx.2.A	10.22	monomer	HHblits	X-ray	2.75Å	0.27	0.67	Botulinum neurotoxin type D
3rmx.3.A	10.22	monomer	HHblits	X-ray	2.75Å	0.27	0.67	Botulinum neurotoxin type D
3rmx.4.A	10.22	monomer	HHblits	X-ray	2.75Å	0.27	0.67	Botulinum neurotoxin type D
1wcs.1.A	16.79	monomer	HHblits	X-ray	2.80Å	0.27	0.67	SIALIDASE
2c5d.1.A	14.08	hetero-oligomer	HHblits	X-ray	3.30Å	0.24	0.69	GROWTH-ARREST-SPECIFIC PROTEIN 6 PRECURSOR
1h30.1.A	14.08	monomer	HHblits	X-ray	2.20Å	0.24	0.69	GROWTH-ARREST-SPECIFIC PROTEIN
2ags.1.A	16.06	monomer	HHblits	X-ray	1.70Å	0.27	0.67	sialidase
1n1s.1.A	16.06	monomer	HHblits	X-ray	1.64Å	0.26	0.67	Sialidase
5jlv.1.A	11.59	hetero-oligomer	HHblits	X-ray	2.00Å	0.26	0.67	Botulinum neurotoxin type A
5jlv.2.A	11.59	hetero-oligomer	HHblits	X-ray	2.00Å	0.26	0.67	Botulinum neurotoxin type A
5jmc.1.A	11.59	hetero-oligomer	HHblits	X-ray	2.64Å	0.26	0.67	Botulinum neurotoxin type A
4jra.1.A	11.59	hetero-oligomer	HHblits	X-ray	2.30Å	0.26	0.67	Botulinum neurotoxin type A
4jra.2.A	11.59	hetero-oligomer	HHblits	X-ray	2.30Å	0.26	0.67	Botulinum neurotoxin type A
5tpc.1.A	11.59	monomer	HHblits	X-ray	2.00Å	0.26	0.67	Botulinum neurotoxin type A
4iqp.1.A	11.59	monomer	HHblits	X-ray	2.30Å	0.26	0.67	Botulinum neurotoxin type A
3fuo.1.A	11.59	monomer	HHblits	X-ray	1.80Å	0.26	0.67	Botulinum neurotoxin type A
1s0i.1.A	13.87	monomer	HHblits	X-ray	1.60Å	0.26	0.67	trans-sialidase
3pjq.1.A	13.87	monomer	HHblits	X-ray	2.10Å	0.26	0.67	Trans-sialidase
1ms4.1.A	13.87	monomer	HHblits	X-ray	2.21Å	0.26	0.67	trans-sialidase
1ms0.2.A	13.87	monomer	HHblits	X-ray	2.50Å	0.26	0.67	trans-sialidase
1ms5.1.A	13.87	monomer	HHblits	X-ray	2.00Å	0.26	0.67	trans-sialidase
3rsj.1.A	11.68	monomer	HHblits	X-ray	2.00Å	0.26	0.67	BoNT/F
3fuq.1.A	11.68	monomer	HHblits	X-ray	2.10Å	0.26	0.67	BoNT/F (Neurotoxin type F)
3qcw.1.A	19.40	monomer	HHblits	X-ray	2.65Å	0.28	0.65	Neurexin-1-alpha
4kbb.1.A	11.03	hetero-oligomer	HHblits	X-ray	2.30Å	0.26	0.66	Botulinum neurotoxin type B
4kbb.2.A	11.03	hetero-oligomer	HHblits	X-ray	2.30Å	0.26	0.66	Botulinum neurotoxin type B
2c5d.1.A	14.07	hetero-oligomer	HHblits	X-ray	3.30Å	0.26	0.66	GROWTH-ARREST-SPECIFIC PROTEIN 6 PRECURSOR
1h30.1.A	14.07	monomer	HHblits	X-ray	2.20Å	0.26	0.66	GROWTH-ARREST-SPECIFIC PROTEIN
4ra0.1.A	14.18	hetero-oligomer	HHblits	X-ray	3.07Å	0.26	0.65	Growth arrest-specific protein 6
5tpb.2.A	14.18	monomer	HHblits	X-ray	2.60Å	0.26	0.65	Botulinum neurotoxin type A
5tpb.1.A	14.18	monomer	HHblits	X-ray	2.60Å	0.26	0.65	Botulinum neurotoxin type A
2nm1.1.A	10.53	hetero-oligomer	HHblits	X-ray	2.15Å	0.26	0.65	Botulinum neurotoxin type B
1z0h.1.A	10.53	monomer	HHblits	X-ray	2.00Å	0.26	0.65	Botulinum neurotoxin type B
1z0h.2.A	10.53	monomer	HHblits	X-ray	2.00Å	0.26	0.65	Botulinum neurotoxin type B
3biw.1.C	16.15	hetero-oligomer	HHblits	X-ray	3.50Å	0.27	0.63	Neurexin-1-beta
2r1d.1.A	16.15	monomer	HHblits	X-ray	2.60Å	0.27	0.63	Neurexin-1-beta
2r1d.2.A	16.15	monomer	HHblits	X-ray	2.60Å	0.27	0.63	Neurexin-1-beta
3flt.1.A	34.26	homo-16-mer	BLAST	X-ray	2.70Å	0.38	0.52	SAP-like pentraxin
2uur.1.A	16.94	monomer	HHblits	X-ray	1.80Å	0.27	0.60	COLLAGEN ALPHA-1(IX) CHAIN
2es3.1.A	13.93	monomer	HHblits	X-ray	1.85Å	0.26	0.59	Thrombospondin-1
2es3.2.A	13.93	monomer	HHblits	X-ray	1.85Å	0.26	0.59	Thrombospondin-1
2erf.1.A	13.93	monomer	HHblits	X-ray	1.45Å	0.26	0.59	Thrombospondin-1
1z78.1.A	13.45	monomer	HHblits	X-ray	1.80Å	0.26	0.58	Thrombospondin 1
2ouj.1.A	13.45	homo-dimer	HHblits	X-ray	1.90Å	0.26	0.58	Thrombospondin-1
1za4.1.A	13.45	monomer	HHblits	X-ray	1.90Å	0.26	0.58	Thrombospondin 1
2ouh.1.A	13.45	monomer	HHblits	X-ray	2.40Å	0.26	0.58	Thrombospondin-1
2ouh.2.A	13.45	monomer	HHblits	X-ray	2.40Å	0.26	0.58	Thrombospondin-1
2r1b.1.A	13.46	monomer	HHblits	X-ray	1.72Å	0.26	0.50	Neurexin-1-beta
3mw2.1.A	12.87	monomer	HHblits	X-ray	2.69Å	0.25	0.49	Neurexin-1-alpha
3zyp.1.A	7.14	monomer	HHblits	X-ray	1.50Å	0.24	0.41	CIP1
3mpp.1.A	11.25	monomer	HHblits	X-ray	1.98Å	0.26	0.39	Botulinum neurotoxin type G
1fv2.1.A	11.39	monomer	HHblits	X-ray	2.50Å	0.26	0.38	TETANUS TOXIN HEAVY CHAIN
1fv3.2.A	11.39	monomer	HHblits	X-ray	2.30Å	0.26	0.38	TETANUS TOXIN HEAVY CHAIN
1fv3.1.A	11.39	monomer	HHblits	X-ray	2.30Å	0.26	0.38	TETANUS TOXIN HEAVY CHAIN
3uv0.1.A	11.27	homo-dimer	HHblits	X-ray	1.90Å	0.26	0.34	Mutator 2, isoform B
2lc1.1.A	21.05	monomer	HHblits	NMR	NA	0.29	0.18	Putative uncharacterized protein TB39.8
2zzj.1.A	21.88	monomer	HHblits	X-ray	1.80Å	0.32	0.16	Glucuronan lyase A
5dxd.1.A	16.67	monomer	HHblits	X-ray	1.70Å	0.30	0.15	Putative beta-glucanase
4m01.1.A	9.68	monomer	HHblits	X-ray	2.10Å	0.26	0.15	Serine-rich adhesin for platelets
4m00.1.A	9.68	monomer	HHblits	X-ray	2.05Å	0.26	0.15	Serine-rich adhesin for platelets
4cpl.1.A	6.90	homo-tetramer	HHblits	X-ray	2.00Å	0.23	0.14	NEURAMINIDASE
4cpo.1.A	6.90	homo-dimer	HHblits	X-ray	2.20Å	0.22	0.14	NEURAMINIDASE
3po8.1.A	16.67	monomer	HHblits	X-ray	1.50Å	0.24	0.12	Putative uncharacterized protein TB39.8
3poa.1.A	16.67	hetero-oligomer	HHblits	X-ray	2.01Å	0.24	0.12	Putative uncharacterized protein TB39.8
3oun.1.A	17.39	hetero-oligomer	HHblits	X-ray	2.71Å	0.24	0.11	Putative uncharacterized protein TB39.8