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SWISS-MODEL Homology Modelling Report

Model Building Report

This document lists the results for the homology modelling project "C7BZB9" submitted to SWISS-MODEL workspace on Oct. 17, 2017, 6:43 p.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 2017-10-11, PDB release 2017-10-06) 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 102 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	QMEAN
	PDB	ProMod3 Version 1.0.2.	MONOMER	None	0.45	-3.82

QMEAN	-3.82
Cβ	-2.57
All Atom	-0.74
Solvation	-0.55
Torsion	-3.29

Template	Seq Identity	Oligo-state	Found by	Method	Resolution	Seq Similarity	Range	Coverage	Description
4cvm.1.A	23.28	monomer	HHblits	X-ray	2.06Å	0.31	149 - 488	0.68	UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D- ALANINE LIGASE

Ligand	Added to Model	Description
ALA	✕ - Binding site not conserved.	ALANINE
ANP	✕ - Binding site not conserved.	PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
FGA	✕ - Binding site not conserved.	GAMMA-D-GLUTAMIC ACID
MG	✕ - Binding site not conserved.	MAGNESIUM ION
MG	✕ - Binding site not conserved.	MAGNESIUM ION
MUB	✕ - Binding site not conserved.	N-ACETYLMURAMIC ACID
UDP	✕ - Binding site not conserved.	URIDINE-5'-DIPHOSPHATE

Target    MQSLSWLNLAFRWLFITGLGYYIMTLLQWYHYSVFRILTKHHKMRWHGIYFLLPLGVFILSYAFKMPFVFDFFCGVIQMP
4cvm.1.A  --------------------------------------------------------------------------------

Target    MLIVWAKRNDKPLVFTPRVKRFFIFLLLFLILHEILNTELVPLNGISLALAYLCLFIFVLSASLIFEKVLSKQYLQTAKD
4cvm.1.A  --------------------------------------------------------------------DTRAALGRLGAL

Target    KIASLKNLKVIAITGSFGKTSTKNFLLQILQTTF----NAHASPKSVNTLLGIANDINQNLDDKSEIYIAEAGARNKGDI
4cvm.1.A  NRRKF-TGPLAAMTGSSGKTTVKEMLASILRTQAGDAESVLATRGNLNNDLGVPLTLL-QLAPQHRSAVIELGASRIGEI

Target    KEITRLIEPHLAVIAEVGEQHLEYFKTLENICETKAELLDSKH-LEKAFCYSVEKIKPYA-P-KD-SPLINVSSL-----
4cvm.1.A  AYTVELTRPHVAIITNAGTAHVGEFGGPEKIVEAKGEILEGLAADGTAVLNLDDKAFDTWKARASGRPLLTFSLDRPQAD

Target    --VKNIQSTLKG-TSFEMLLDSVWERFETKVLGEFSAYNIASAILIAKYLGLETERIKRLVLELNPIAHRLQLLEV-NQK
4cvm.1.A  FRAADLQRDARGCMGFRLQGVAGEAQVQLNLLGRHNVANALAAAAAAHALGVPLDGIVAGLQALQPVKGRAVAQLTASGL

Target    IIIDDSFNGNLKGMLEGIRLASLYEGRKVIVTPGLV---ESNVESNEALAQKIDGVFDVAIITGELNSKTIASQLKTPQK
4cvm.1.A  RVIDDSYNANPASMLAAIDILSGFSGRTVLVLGDMGELGSWAEQAHREVGAYAAGKVSALYAVGPLMAH-AVQAFGATG-

Target    ILLKDKAQLENILQATTIQGDLILFANDAPNYI
4cvm.1.A  RHFADQASLIGALATED-PTTTILIKGS-----

Model #02	File	Built with	Oligo-State	Ligands	GMQE	QMEAN
	PDB	ProMod3 Version 1.0.2.	MONOMER	None	0.38	-4.96

QMEAN	-4.96
Cβ	-2.92
All Atom	-2.63
Solvation	-1.33
Torsion	-4.13

Template	Seq Identity	Oligo-state	Found by	Method	Resolution	Seq Similarity	Range	Coverage	Description
1eeh.1.A	16.34	monomer	HHblits	X-ray	1.90Å	0.29	167 - 492	0.62	UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE

Ligand	Added to Model	Description
UMA	✕ - Binding site not conserved.	URIDINE-5'-DIPHOSPHATE-N-ACETYLMURAMOYL-L-ALANINE

Target    MQSLSWLNLAFRWLFITGLGYYIMTLLQWYHYSVFRILTKHHKMRWHGIYFLLPLGVFILSYAFKMPFVFDFFCGVIQMP
1eeh.1.A  --------------------------------------------------------------------------------

Target    MLIVWAKRNDKPLVFTPRVKRFFIFLLLFLILHEILNTELVPLNGISLALAYLCLFIFVLSASLIFEKVLSKQYLQTAKD
1eeh.1.A  --------------------------------------------------------------------------------

Target    KIASLKNLKVIAITGSFGKTSTKNFLLQILQTTFNAHASPKSVNTLLGIANDINQNLDDKSEIYIAEAGARNKGDIKEIT
1eeh.1.A  ------QAPIVAITGSNGKSTVTTLVGEMAKAAGVNVGVGGNI----GLPAL--MLLDDECELYVLELSSFQLE----TT

Target    RLIEPHLAVIAEVGEQHLEYFK-TLENICETKAELLDSKHLEKAFCYSVEKIKPYA-PKDSPLINVSSLVKNIQ---STL
1eeh.1.A  SSLQAVAATILNVTEDHMDRYPFGLQQYRAAKLRIYENA--KVCVVNADDALTMPIRGADERCVSFGVNMGDYHLNHQQG

Target    KGTSFEMLLDSVW--ERFETKVLGEFSAYNIASAILIAKYLGLETERIKRLVLELNPIAHRLQLLE-VNQKIIIDDSFNG
1eeh.1.A  ETW-LRV--KGEKVLNVKEMKLSGQHNYTNALAALALADAAGLPRASSLKALTTFTGLPHRFEVVLEHNGVRWINDSKAT

Target    NLKGMLEGIRLASLYEGRKVIVTPGLVESNVESNEALAQKIDGVFDVAIITGELNSKTIASQLKTPQKILLKDKAQLENI
1eeh.1.A  NVGSTEAALNGLH-VDGTLHLLLGGDGK-SA-DFSPLARYLNGDNVRLYCFGRDGAQ-LAALRPE-VAEQTETMEQAMRL

Target    LQATTIQGDLILFANDAPNYI
1eeh.1.A  LAPRVQPGDMVLLSPACASL-

Materials and Methods

Template Search

Template search with Blast and HHBlits has been performed against the SWISS-MODEL template library (SMTL, last update: 2017-10-11, last included PDB release: 2017-10-06).

The target sequence was searched with BLAST (Altschul et al., 1997) against the primary amino acid sequence contained in the SMTL. A total of 10 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 94 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.

MQSLSWLNLAFRWLFITGLGYYIMTLLQWYHYSVFRILTKHHKMRWHGIYFLLPLGVFILSYAFKMPFVFDFFCGVIQMPMLIVWAKRNDKPLVFTPRVK
RFFIFLLLFLILHEILNTELVPLNGISLALAYLCLFIFVLSASLIFEKVLSKQYLQTAKDKIASLKNLKVIAITGSFGKTSTKNFLLQILQTTFNAHASP
KSVNTLLGIANDINQNLDDKSEIYIAEAGARNKGDIKEITRLIEPHLAVIAEVGEQHLEYFKTLENICETKAELLDSKHLEKAFCYSVEKIKPYAPKDSP
LINVSSLVKNIQSTLKGTSFEMLLDSVWERFETKVLGEFSAYNIASAILIAKYLGLETERIKRLVLELNPIAHRLQLLEVNQKIIIDDSFNGNLKGMLEG
IRLASLYEGRKVIVTPGLVESNVESNEALAQKIDGVFDVAIITGELNSKTIASQLKTPQKILLKDKAQLENILQATTIQGDLILFANDAPNYI

Table T2:

Template	Seq Identity	Oligo-state	Found by	Method	Resolution	Seq Similarity	Coverage	Description
2am2.1.A	20.54	monomer	HHblits	X-ray	2.80Å	0.31	0.68	UDP-N-acetylmuramoylalanine-D-glutamyl-lysine-D-alanyl-D-alanine ligase, MurF protein
3zm5.1.A	20.60	monomer	HHblits	X-ray	2.94Å	0.31	0.68	UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE
4qf5.1.A	22.75	monomer	HHblits	X-ray	2.80Å	0.31	0.68	UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
4qdi.1.A	22.75	monomer	HHblits	X-ray	1.80Å	0.31	0.68	UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
4ziy.1.A	22.82	monomer	HHblits	X-ray	1.85Å	0.31	0.68	UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
4cvl.1.A	23.28	monomer	HHblits	X-ray	2.98Å	0.31	0.68	UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE
4cvm.1.A	23.28	monomer	HHblits	X-ray	2.06Å	0.31	0.68	UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D- ALANINE LIGASE
3zl8.1.A	22.59	monomer	HHblits	X-ray	1.65Å	0.31	0.67	UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE
1gg4.1.A	20.66	monomer	HHblits	X-ray	2.30Å	0.30	0.68	UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMYL-2,6-DIAMINOPIMELATE-D-ALANYL-D-ALANYL LIGASE
4c12.1.A	18.10	homo-dimer	HHblits	X-ray	1.80Å	0.29	0.68	UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--L-LYSINE LIGASE
4bub.1.A	16.37	monomer	HHblits	X-ray	2.90Å	0.29	0.68	UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--LD-LYSINE LIGASE
4bub.2.A	16.37	monomer	HHblits	X-ray	2.90Å	0.29	0.68	UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--LD-LYSINE LIGASE
1e8c.1.A	15.73	monomer	HHblits	X-ray	2.00Å	0.29	0.68	UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE
3zl8.1.A	32.57	monomer	BLAST	X-ray	1.65Å	0.36	0.62	UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE
2xja.1.A	14.29	monomer	HHblits	X-ray	3.00Å	0.28	0.68	UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE
2wtz.1.A	14.29	monomer	HHblits	X-ray	3.00Å	0.28	0.68	UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE
1o5z.1.A	19.17	monomer	HHblits	X-ray	2.10Å	0.30	0.63	folylpolyglutamate synthase/dihydrofolate synthase
3hn7.1.A	16.98	monomer	HHblits	X-ray	1.65Å	0.28	0.65	UDP-N-acetylmuramate-L-alanine ligase
1p3d.1.A	17.95	monomer	HHblits	X-ray	1.70Å	0.29	0.63	UDP-N-acetylmuramate--alanine ligase
1gqq.1.A	17.95	homo-dimer	HHblits	X-ray	3.10Å	0.29	0.63	UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE
1gqq.1.B	17.95	homo-dimer	HHblits	X-ray	3.10Å	0.29	0.63	UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE
1p31.1.A	17.95	monomer	HHblits	X-ray	1.85Å	0.29	0.63	UDP-N-acetylmuramate--alanine ligase
1gqy.1.B	17.95	homo-dimer	HHblits	X-ray	1.80Å	0.29	0.63	UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE
1gqy.1.A	17.95	homo-dimer	HHblits	X-ray	1.80Å	0.29	0.63	UDP-N-ACETYLMURAMATE-L-ALANINE LIGASE
2f00.1.A	17.89	homo-dimer	HHblits	X-ray	2.50Å	0.29	0.63	UDP-N-acetylmuramate--L-alanine ligase
4hv4.1.A	17.25	monomer	HHblits	X-ray	2.25Å	0.29	0.63	UDP-N-acetylmuramate--L-alanine ligase
4hv4.2.A	17.25	monomer	HHblits	X-ray	2.25Å	0.29	0.63	UDP-N-acetylmuramate--L-alanine ligase
2vor.1.A	16.61	monomer	HHblits	X-ray	2.30Å	0.29	0.63	FOLYLPOLYGLUTAMATE SYNTHASE PROTEIN FOLC
2gcb.1.A	16.08	monomer	HHblits	X-ray	2.30Å	0.28	0.63	Folylpolyglutamate synthase
3nrs.1.A	16.03	monomer	HHblits	X-ray	1.80Å	0.28	0.63	Dihydrofolate:folylpolyglutamate synthetase
3pyz.1.A	16.03	monomer	HHblits	X-ray	2.10Å	0.28	0.63	Bifunctional folylpolyglutamate synthase/dihydrofolate synthase
1fgs.1.A	16.45	monomer	HHblits	X-ray	2.40Å	0.28	0.63	FOLYLPOLYGLUTAMATE SYNTHETASE
1jbw.1.A	16.45	monomer	HHblits	X-ray	1.85Å	0.28	0.63	FOLYLPOLYGLUTAMATE SYNTHASE
1jbv.1.A	16.45	monomer	HHblits	X-ray	1.95Å	0.28	0.63	FOLYLPOLYGLUTAMATE SYNTHASE
3lk7.1.A	17.59	monomer	HHblits	X-ray	1.50Å	0.29	0.62	UDP-N-acetylmuramoylalanine--D-glutamate ligase
2gc6.1.A	16.13	monomer	HHblits	X-ray	1.90Å	0.28	0.63	Folylpolyglutamate synthase
1uag.1.A	16.34	monomer	HHblits	X-ray	1.95Å	0.29	0.62	UDP-N-ACETYLMURAMOYL-L-ALANINE/:D-GLUTAMATE LIGASE
1eeh.1.A	16.34	monomer	HHblits	X-ray	1.90Å	0.29	0.62	UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE
2uag.1.A	16.34	monomer	HHblits	X-ray	1.70Å	0.29	0.62	PROTEIN (UDP-N-ACETYLMURAMOYL-L-ALANINE:D-GLUTAMATE LIGASE)
1e0d.1.A	16.34	monomer	HHblits	X-ray	2.40Å	0.29	0.62	UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
5a5e.1.A	16.34	monomer	HHblits	X-ray	1.84Å	0.29	0.62	UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
2y67.1.A	16.34	monomer	HHblits	X-ray	1.85Å	0.29	0.62	UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
5a5f.1.A	16.34	monomer	HHblits	X-ray	1.90Å	0.29	0.62	UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
2xpc.1.A	16.34	monomer	HHblits	X-ray	1.49Å	0.29	0.62	UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
2gc5.1.A	17.05	monomer	HHblits	X-ray	1.85Å	0.29	0.62	Folylpolyglutamate synthase
4buc.1.A	13.27	monomer	HHblits	X-ray	2.17Å	0.27	0.63	UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
4buc.2.A	13.27	monomer	HHblits	X-ray	2.17Å	0.27	0.63	UDP-N-ACETYLMURAMOYLALANINE--D-GLUTAMATE LIGASE
2gca.1.A	17.05	monomer	HHblits	X-ray	2.40Å	0.28	0.62	Folylpolyglutamate synthase
1w7k.1.A	16.61	monomer	HHblits	X-ray	2.10Å	0.28	0.62	FOLC BIFUNCTIONAL PROTEIN
1w78.1.A	16.61	monomer	HHblits	X-ray	1.82Å	0.28	0.62	FOLC BIFUNCTIONAL PROTEIN
1j6u.1.A	14.24	monomer	HHblits	X-ray	2.30Å	0.29	0.61	UDP-N-acetylmuramate-alanine ligase MurC
2am2.1.A	28.52	monomer	BLAST	X-ray	2.80Å	0.35	0.55	UDP-N-acetylmuramoylalanine-D-glutamyl-lysine-D-alanyl-D-alanine ligase, MurF protein
3zm5.1.A	28.52	monomer	BLAST	X-ray	2.94Å	0.35	0.55	UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE
1gg4.1.A	25.68	monomer	BLAST	X-ray	2.30Å	0.34	0.52	UDP-N-ACETYLMURAMOYLALANYL-D-GLUTAMYL-2,6-DIAMINOPIMELATE-D-ALANYL-D-ALANYL LIGASE
4cvl.1.A	28.93	monomer	BLAST	X-ray	2.98Å	0.34	0.49	UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE
4cvm.1.A	28.93	monomer	BLAST	X-ray	2.06Å	0.34	0.49	UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D- ALANINE LIGASE
4ziy.1.A	28.63	monomer	BLAST	X-ray	1.85Å	0.34	0.49	UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
4qf5.1.A	28.63	monomer	BLAST	X-ray	2.80Å	0.34	0.49	UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
4qdi.1.A	28.63	monomer	BLAST	X-ray	1.80Å	0.34	0.49	UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
4c12.1.A	27.10	homo-dimer	BLAST	X-ray	1.80Å	0.34	0.43	UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--L-LYSINE LIGASE
3eag.1.A	15.61	homo-dimer	HHblits	X-ray	2.55Å	0.29	0.42	UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase
3eag.1.B	15.61	homo-dimer	HHblits	X-ray	2.55Å	0.29	0.42	UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase
5vvw.1.A	18.37	homo-tetramer	HHblits	X-ray	2.30Å	0.29	0.40	UDP-N-acetylmuramate--L-alanine ligase
3mvn.1.A	16.96	monomer	HHblits	X-ray	1.90Å	0.27	0.23	UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-medo-diaminopimelate ligase
3ufx.1.B	8.74	hetero-oligomer	HHblits	X-ray	2.35Å	0.25	0.21	Succinyl-CoA synthetase beta subunit
5ekz.1.A	4.92	monomer	HHblits	X-ray	2.00Å	0.24	0.12	Translational activator of cytochrome c oxidase 1
2j0u.1.A	36.67	hetero-oligomer	HHblits	X-ray	3.00Å	0.34	0.06	ATP-DEPENDENT RNA HELICASE DDX48
5l3w.1.A	26.67	monomer	HHblits	X-ray	2.40Å	0.31	0.06	Signal recognition particle receptor FtsY
2v3c.1.B	31.03	hetero-oligomer	HHblits	X-ray	2.50Å	0.34	0.06	SIGNAL RECOGNITION 54 KDA PROTEIN
2v3c.2.B	31.03	hetero-oligomer	HHblits	X-ray	2.50Å	0.34	0.06	SIGNAL RECOGNITION 54 KDA PROTEIN
1j8m.1.A	31.03	monomer	HHblits	X-ray	2.00Å	0.33	0.06	SIGNAL RECOGNITION 54 KDA PROTEIN
3kl4.1.A	24.14	hetero-oligomer	HHblits	X-ray	3.50Å	0.32	0.06	Signal recognition 54 kDa protein
4c7o.1.B	27.59	hetero-oligomer	HHblits	X-ray	2.60Å	0.31	0.06	SIGNAL RECOGNITION PARTICLE RECEPTOR FTSY
2j45.1.A	20.00	monomer	HHblits	X-ray	1.14Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
2j45.2.A	20.00	monomer	HHblits	X-ray	1.14Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
2j46.1.A	20.00	monomer	HHblits	X-ray	1.14Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
2j46.2.A	20.00	monomer	HHblits	X-ray	1.14Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
1o87.1.A	20.00	monomer	HHblits	X-ray	2.10Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
1o87.2.A	20.00	monomer	HHblits	X-ray	2.10Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
2c04.1.A	20.00	monomer	HHblits	X-ray	1.15Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
2c04.2.A	20.00	monomer	HHblits	X-ray	1.15Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
2c03.1.A	20.00	monomer	HHblits	X-ray	1.24Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
2c03.2.A	20.00	monomer	HHblits	X-ray	1.24Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
2ng1.1.A	20.00	monomer	HHblits	X-ray	2.02Å	0.28	0.06	SIGNAL SEQUENCE RECOGNITION PROTEIN FFH
1ls1.1.A	20.00	monomer	HHblits	X-ray	1.10Å	0.28	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
2qy9.1.A	27.59	monomer	HHblits	X-ray	1.90Å	0.31	0.06	Cell division protein ftsY
1fts.1.A	27.59	monomer	HHblits	X-ray	2.20Å	0.31	0.06	FTSY
2j28.1.H	24.14	hetero-oligomer	HHblits	EM	8.00Å	0.31	0.06	SIGNAL RECOGNITION PARTICLE 54
2xxa.1.A	24.14	hetero-oligomer	HHblits	X-ray	3.94Å	0.31	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
2xxa.2.A	24.14	hetero-oligomer	HHblits	X-ray	3.94Å	0.31	0.06	SIGNAL RECOGNITION PARTICLE PROTEIN
5gad.1.7	24.14	hetero-oligomer	HHblits	EM	NA	0.30	0.06	Signal recognition particle protein Ffh
3ug7.1.A	16.67	homo-tetramer	HHblits	X-ray	2.90Å	0.27	0.06	arsenical pump-driving ATPase
3ug6.1.A	16.67	homo-tetramer	HHblits	X-ray	3.30Å	0.27	0.06	arsenical pump-driving ATPase
5l3q.1.A	33.33	hetero-oligomer	HHblits	X-ray	3.20Å	0.32	0.05	Signal recognition particle 54 kDa protein
3ndb.1.B	34.62	hetero-oligomer	HHblits	X-ray	3.00Å	0.35	0.05	Signal recognition 54 kDa protein
4ue5.1.D	34.62	hetero-oligomer	HHblits	EM	9.00Å	0.33	0.05	SIGNAL RECOGNITION PARTICLE 54 KDA PROTEIN
3a4l.1.A	32.00	homo-dimer	HHblits	X-ray	1.80Å	0.35	0.05	L-seryl-tRNA(Sec) kinase
3a4l.1.B	32.00	homo-dimer	HHblits	X-ray	1.80Å	0.35	0.05	L-seryl-tRNA(Sec) kinase
3am1.1.C	32.00	homo-dimer	HHblits	X-ray	2.40Å	0.35	0.05	L-seryl-tRNA(Sec) kinase
1j8y.1.A	28.00	monomer	HHblits	X-ray	2.00Å	0.32	0.05	SIGNAL RECOGNITION 54 KDA PROTEIN
1xd9.1.A	25.00	homo-dimer	HHblits	X-ray	2.80Å	0.31	0.05	Nitrogenase iron protein 1
4rfv.1.A	26.09	homo-dimer	HHblits	X-ray	1.69Å	0.31	0.05	Bifunctional enzyme CysN/CysC