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{{Theoretical_model}} <StructureSection load='Dnac_from_2ggz_a.pdb' size='400' side='right' scene='User:Eric_Martz/Sandbox_4/Dnac_model_from_2ggz_a/8' caption=''> ==Overview== ===Introduction=== The DnaC protein in ''[http://microbewiki.kenyon.edu/index.php/Escherichia_coli E. coli]'' is part of the DNA polymerase complex of proteins, which includes the [http://en.wikipedia.org/wiki/Replisome replisome] and [http://en.wikipedia.org/wiki/Primosome primosome], and which replicates genomic [[DNA]]. DnaC is believed to be involved in loading the DnaB helicase, which separates the strands of the DNA so that each can be copied by the DnaG polymerase. ===3D Structure: Homology Model=== No empirical (X-ray crystallographic) 3D structure for the ''[http://microbewiki.kenyon.edu/index.php/Escherichia_coli E. coli]'' DnaC protein ([http://www.uniprot.org/uniprot/P0AEF0 UniProt P0AEF0]) is available in November, 2012, although one or more [[#Crystal Structure of DnaC Is ''In The Pipeline'' |might become available]]. In view of this, [[Homology modeling|homology models]] were constructed using the automated Swiss-Model server<ref name="methods">A model was created in 2008 by Swiss-Model using its totally automated ''first approach'' mode with template [[2qgz]]. In 2012, Swiss-Model's automated mode chose a different template, [[3ecc]], and created a similar model. </ref><ref name="swissmodel">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. [http://bioinformatics.oxfordjournals.org/cgi/content/abstract/22/2/195 Free full text]. Server: [http://swissmodel.expasy.org swissmodel.expasy.org]</ref>. In 2008 (when this article was largely written and the molecular scenes were prepared), Swiss-Model deemed the only usable template<ref name="3ec2_notemplate">In December, 2008, Swiss-Model deemed the sequence alignment of ''E. coli'' DnaC with ''A. aeolicus'' DnaC to be too unreliable to permit using the [[3ec2]] structure of the latter as a template for homology modeling of <i>E. coli</i> DnaC.</ref> for the homology model to be the crystal structure of a "putative primosome component" from ''[http://microbewiki.kenyon.edu/index.php/Streptococcus_pyogenes Streptococcus pyogenes]'' ([[2qgz]]) determined by the Northeast Structural Genomics Consortium, "to be published". In 2012, after some changes to the Swiss-Model server, it chose a different template, producing a very similar homology model. This second template was a crystal structure of the DnaC helicase loader of ''[http://microbewiki.kenyon.edu/index.php/Aquifex_aeolicus Aquafex aeolicus]'' ([[3ecc]])<ref name="3ec2_notemplate" />. The agreement between the models built upon two templates, which templates have only 27% sequence identity with each other, gives confidence that fold and topology of the models are likely to be correct. Furthermore, the two homology models had identical registrations of sequence with structure (data not shown). Nevertheless, because the sequence identity between the templates and the target <i>E. coli</i> DnaC is only ~20%, there may be some error in the registration of the <i>E. coli</i> DnaC sequence with the model structure. Further, the positions of sidechains in homology models are generally unreliable. We thank the authors of [[2qgz]] for releasing their structure data at the [[Protein Data Bank]] prior to full publication. The molecular scenes below in this article utilize the 2008 model templated upon [[2qgz]]. As mentioned above, this model is very similar to the 2012 model templated upon [[3ec2]]. ====Intrinsically Unstructured N-Terminus==== The [[Intrinsically_Disordered_Protein#Prediction_Servers|FoldIndex]] server predicts that the amino terminus of DnaC residues 1-76 will be [[Intrinsically_Disordered_Protein|intrinsically unstructured]], that it, it will not participate in the stable fold of the remainder of the protein. ====Viewing and Download==== In addition to the interactive scenes below, the homology models can be downloaded from the Proteopedia server: * 2008 model residues 55-237 of ''E. coli'' DnaC: [[:Image:Dnac_from_2ggz_a.pdb|Dnac_from_2ggz_a.pdb]] / [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=http%3A//proteopedia.org/wiki/images/3/3e/Dnac_from_2ggz_a.pdb view and explore in FirstGlance in Jmol]. (Note that the PDB filename contains a typographical error: 2ggz should have been 2qgz.) * 2012 model residues 64-237 of ''E. coli'' DnaC: [[:Image:Dnac-64-237-from-3eccA.pdb.zip|Dnac-64-237-from-3eccA.pdb.zip]] / [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=http%3A//proteopedia.org/wiki/images/c/c0/Dnac-64-237-from-3eccA.pdb.zip view and explore in FirstGlance in Jmol]. ===Conclusions from Homology Model=== The following analysis utilizes the homology model templated on [[2qgz]]. The model templated on [[3ecc]] is very similar, with identical sequence-to-structure registration (not shown). When the two homology models are structurally aligned, 115 alpha carbon atoms can be aligned with RMS deviation of 1.4 &Aring; (not shown). The homology model (<scene name='User:Eric_Martz/Sandbox_4/Dnac_model_from_2ggz_a/8'>restore initial scene</scene>) represents 75% of the full length ''E. coli'' DnaC sequence, omitting 54 N-terminal residues, and 8 C-terminal residues. Note that the N-terminal 76 residues are predicted to be intrinsically unfolded (see [[#Intrinsically Unstructured N-Terminus|above]]). Several surface loops in the model (shown translucent white) have high uncertainty, since these are missing in the template ([[#Homology Model Construction|see below]]). Note that the homology model is somewhat unreliable about which residues are actually on the surface vs. largely buried, and hence the conclusions below are tentative. {{Template:ColorKey_Amino2CarboxyRainbow}} ====Evolutionary Conservation==== <scene name='User:Eric_Martz/Sandbox_4/Dnac_model_from_2ggz_a/9'>Two prominent patches</scene> of [[Conservation, Evolutionary|highly conserved residues]] are apparent. <blockquote> {{Template:ColorKey_ConSurf}} </blockquote> *'''Large conserved patch.''' The larger of the two conserved patches is adjacent to the positively charged patch, and includes Arg237 and His114, which are highly conserved (''ConSurf level 9''). The larger patch also includes highly conserved surface residues Asn113, Asp169, Glu170, Asn203. (There are also three highly conserved surface glycines in this patch, not listed because surface glycines are typically conserved for reasons of secondary structure rather than function.) These highly conserved residues (ConSurf level 9) are flanked by several conserved residues (''ConSurf level 8''), including Ile62, Asn73, and Thr110. Conserved (''level 8'') residues are uncommon elsewhere on the surface (except for the other conserved patch). :Results of a 2012 ConSurf analysis<ref name='2012consurf'>In the 2012 analysis, ConSurf found 47 unique sequences in ''Clean Uniprot''. The MSA had an average pairwise distance of 0.98.</ref> (not shown) agreed quite well with the above results from the 2008 analysis<ref>In 2008, ConSurf found only 10 sequences in SwissProt, with an average pairwise distance (APD), in the multiple sequence alignment, of 1.6. The run shown here used 100 sequences from Uniprot, with an APD of 1.4.</ref>. All the residues highly conserved in the 2008 analysis were highly conserved (''ConSurf level 9'') in the 2012 analysis, except Asn113, which dropped to ''ConSurf level 8''. The three ''ConSurf level 8'' residues in 2008 achieved ''ConSurf level 9'' (maxumum conservation) in the 2012 analysis. The 2012 [[#ConSurf Coloring Script|ConSurf coloring script is listed below]]. *'''Small conserved patch.''' This patch consists of highly conserved (''ConSurf level 9'') residues Arg216, Asp219, Arg220, flanked by conserved ('''ConSurf level 8''') residue Asp189. Results of the 2012 analysis<ref name='2012consurf' /> (not shown) were in near perfect agreement, except that Asp189 achieved ''level 9''. *The <scene name='User:Eric_Martz/Sandbox_6/3ecc/1'>same two conserved surface patches</scene><ref>[http://consurf.tau.ac.il/results/1230090558/output.html ConSurf result] using 50 sequences from Uniprot, with an average pairwise distance in the multiple sequence alignment of 1.6.</ref> are observed on the 2.7 &Aring; crystal structure of DnaC from ''Aquifex aeolicus'' ([[3ecc]]), where the '''larger conserved patch is the binding site for ATP/ADP'''. ====Charge Distribution==== <scene name='User:Eric_Martz/Sandbox_6/Dnac_model_from_2ggz_a/1'>Cationic patch</scene>: The 2008 model displays a patch, about 20 x 30 &Aring;, containing six positively charged amino acids and no negative charges. The patch is near the bottom of this scene. Such a patch would be suitable for interaction with e.g. anionic phosphates in ATP/ADP or DNA. The positive charges are Arg55, Arg59, Arg63, Arg126, Lys128, and Arg237. His66 and His114 are near one end of this patch. <center> {{Template:ColorKey_Charge_Cationic}} / {{Template:ColorKey_Charge_Anionic}} </center> *<scene name='User:Eric_Martz/Sandbox_6/Dnac_model_from_2ggz_a/3'>Backbone trace</scene>. *<scene name='User:Eric_Martz/Sandbox_6/Dnac_model_from_2ggz_a/2'>Charge overlaid on backbone trace</scene>. However, '''this cationic patch is not seen''' in the 2012 model, which contains an uncharged patch in the same location ringed by negative charges (not shown). Three of the charged-patch residues in the 2008 model are near the N-terminus (Args 55, 59, 63). But the 2012 model omits these residues, starting at Pro64. Furthermore the sidechains of Arg126, Lys 128 and Arg237 point away from this region in the 2012 model. ==Homology Model Construction== [http://www.bio.umass.edu/micro/faculty/sandler.html Steve Sandler] kindly provided the following sequence for DnaC from E. coli (Uniprot P0AEF0, DNAC_ECOLI): <tt><big> MKNVGDLMQR LQKMMPAHIK PAFKTGEELL AWQKEQGAIR SAALERENRA <br> MKMQ<b>RTFNRS GIRPLHQNCS FENYRVECEG QMNALSKARQ YVEEFDGNIA <br> SFIFSGKPGT GKNHLAAAIC NELLLRGKSV LIITVADIMS AMKDTFRNSG <br> TSEEQLLNDL SNVDLLVIDE IGVQTESKYE KVIINQIVDR RSSSKRPTGM <br> LTNSNMEEMT KLLGERVMDR MRLGNSLWVI FNWDSYR</b>SRV TGKEY </big></tt> This sequence (245 amino acids) was submitted to Swiss Model in 2008, which generated the homology model shown here (<scene name='User:Eric_Martz/Sandbox_4/Dnac_model_from_2ggz_a/8'>restore initial scene</scene>) using [[2qgz]] chain A as a template, which has 18.6% sequence identity. Apparently Swiss Model used predicted secondary structure to help in the sequence alignment, but details are not clear to me<ref>Not clear to [[User:Eric Martz]] in December, 2008.</ref>. The homology model represents residues 55-237 (183 residues representing 75% of DnaC), shown in '''boldface in the above sequence'''. Because of the low sequence identity, this model may well contain significant errors, especially in registration<ref>''Registration'' refers to the positioning of amino acids along the backbone of the homology model. Amino acids are "in register" when correctly positioned. The sequence of the target protein (DnaC) can be thought of as sliding along the template backbone, as a consequence of the process of sequence alignment (or threading). The correct registration will be known only when an empirical crystallographic structure becomes available for DnaC.</ref>. In 2008, Swiss Model apparently used the [[temperature value]] field in the PDB file to indicate regions that are highly unreliable, namely the regions that are <font color="red"><b>red</b></font> when the model is <scene name='User:Eric_Martz/Sandbox_4/Dnac_model_from_2ggz_a/4'>colored by temperature</scene>. (This was no longer true in 2012.) These regions are shown as '''translucent white''' in the initial scene (using the Jmol command <i>select temperature >50</i>). The uncertainty in three of these regions is explained by gaps in the template model (see below). Although the details of these regions are even more uncertain than other regions, it seems likely that these loops are on the surface, if the homology model turns out to be substantially correct. As indicated [[#3D Structure: Homology Model|above]], in 2008, Swiss-Model found only one usable template for homology modeling, despite the existence of an empirical 3D crystal structure for DnaC with a slightly higher sequence identity. {{Clear}} ===Gaps in the Template Model=== The template was 2QGZ (<scene name='User:Eric_Martz/Sandbox_4/2qgz/3'>initial scene</scene>). The portion of the template used was Glu107-Arg300. Only the amino-terminal 6 residues were not used as template (translucent). Note that there are <scene name='User:Eric_Martz/Sandbox_4/2qgz/5'>three loops</scene> in this segment of the template that lack coordinates due to [[disorder]] in the crystal (marked with spacefilled alpha-carbon atoms). The missing loops are 202-205 (NGSV), 226-231 (EQATSW), and 268-275 (TIKGSDET). These gaps, which occur between the residues marked /\ below, were apparently ignored in making the model, which has a continuous main chain. {{Clear}} ==Confirmation of Homology Model By Related Structures== When the [[PDB]] is searched with the DnaC sequence, the best match (December, 2008) is 23% sequence identity with 183 amino acids in the DnaC helicase loader of ''Aquifex aeolicus'', [[3ec2]] and [[3ecc]]. In order to find whether these structures have the same fold as the template ([[2qgz]] with 19% sequence identity to ''E. coli'' DnaC) used for the homology model, <font color="#3030ff">'''2qgz'''</font> <scene name='User:Eric_Martz/Sandbox_6/2qgz_3ec2_aligned_pdb/1'>was structurally aligned</scene> with <font color="#ff0000">'''3ec2'''</font><ref>The structural alignment of 2qgz with 3ec2 was performed with the ''Magic Fit'' function of DeepView version 3.6beta2. 2qgz 115-259 aligned with 3ec2 42-185 (3 gaps in 3ec2's alignment: 128-9, 134-5, 155-9). 135 alpha carbons were aligned with RMS 2.76 Å. The sequence identity between 2qgz and 3ec2 is 28% over the 185 amino acid length of the shorter, 3ec2. ''Magic Fit'' is a sequence-alignment-guided structural alignment (see [[Structural_alignment_tools#DeepView_.3D_Swiss-PDBViewer|Structural alignment tools]]).</ref>. The similarity of folds lends considerable confidence to the homology model of ''E. coli'' DnaC. This was further confirmed by the 2012 Swiss Model run, when 3ecc was selected as the best template (see discussion above). The second best sequence-identity hit in the PDB is 39% identity with 54 amino acids (positions 9-63 of chain A) of replication factor C ([[2chg]]), which align with 72-124 of DnaC. When the above homology model of DnaC (made with template 2QGZ) is <scene name='User:Eric_Martz/Sandbox_4/2chg9-63_aligned_with_dnac_mod/1'>structurally aligned</scene> with residues 9-63 of 2CHG<ref>Structural alignment done with DeepView 3.6b3 using Magic Fit of carbon alphas.</ref>, 43 alpha carbons (out of 54) aligned with RMS deviation 2.3 &Aring;. <font color="#ff0000">'''Residues 21-63 of 2CHG'''</font> aligned with <font color="#3030ff">'''residues 80-124 of the DnaC homology model'''</font>. (Non-aligned portions are pastel.) This result adds firther confidence to this region of the homology model, since the structural alignment of 2CHG:A21-63 occurred in the same range as the sequence alignment (which was 72-124 in DnaC). ''Download'' the above structural alignments: *[[:Image:2qgz_3ec2_aligned.pdb|2qgz_3ec2_aligned.pdb]] *[[:Image:2chg9-63_aligned_with_dnac_model.pdb|2chg9-63_aligned_with_dnac_model.pdb]] {{Clear}} ==Crystal Structure of DnaC Is "In The Pipeline"== A sequence-based search at the international [http://targetdb.pdb.org/ Structural Genomics TargetDB] reveals that the closest completed structure is [[2qgz]], the one chosen by SwissModel as a template. ([[3ec2]] and [[3ecc]] were not determined by a structural genomics project.) A number of crystal and NMR structures have sequence identities up to 37% but over shorter stretches, and with higher E values. Diffraction data have been obtained (but the solved structure not yet deposited) for a ''Listeria monocytogenes'' sequence of 307 residues, pI 5.2, with an E value of 1.6e-05, though only 21% sequence identity. Diffraction-quality crystals (but not yet diffraction data) have not been obtained for any sequence with such a low E value. ''E. coli'' DnaC (245 residues, pI 9.4) has been crystallized by RIKEN Structural Genomics Initiative (Japan), but the crystals may not be of diffraction quality. It has been cloned, expressed as a soluble protein, and purified (but not yet crystallized) by 3 Structural Genomics Groups (RIKEN Structural Genomics Initiative (Japan), Montreal-Kingston Bacterial Structural Genomics Initiative, Midwest Center for Structural Genomics), as have several proteins with >40% sequence identity. Thus, there is reason for optimism that either a crystal structure, or a more suitable template for homology modeling, might be forthcoming. ==DnaC helicase loader 3D structures== [[DnaC helicase loader]] ==Additional Resources== For additional information, see: [[DNA Replication, Repair, and Recombination]] For additional information, see: [[Nucleic Acids]] <br /> </StructureSection> {| class="wikitable" style="text-align:center" |+ Templates for 2008 Homology Modeling of E. coli DnaC (245 amino acids) ! Name !! PDB Code (Resolution) !! Released !! Length (amino acids)^a !! Template alignment length^a: range (%) !! Target alignment length^a: range (%) !! Aligned Sequence Identity !! Expectations !! Swiss Model Result |- | Putative Primosome Component ''Streptococcus Pyogenes'' || 2qgz (2.4 &Aring;) || Jul 24 2007 || 183 (308) || 174:107-292 (95%) [sm] || (183): 55-237 (75%) [sm] || 18.6% [sm]; 19.7% [tdb] || 3.4e-28 [sm]; 0.00027 [tdb]; >10 [pdbB]; 0.0028 [pdbF] || [[:Image:Dnac_from_2ggz_a.pdb|DnaC modeled from 2qgz chain A]] |- | DnaC helicase loader ''Aquifex aeolicus'' || 3ec2 (2.7 &Aring;) || Nov 25 2008 || 175 (180) || 174: 6-179 (95%) [pdbB] || (163): 68-230 (67%) [pdbB] || 23.5% [pdbB] || 0.00059 [pdbB] || "Alignment is not good enough for Modelling" |} Sources: [http://swissmodel.expasy.org Swiss-Model] [sm]; [http://targetdb.pdb.org targetdb.pdb.org] [tdb]; [http://pdb.org pdb.org] using a BLAST search [pdbB], or a FASTA search [pdbF]. <br> (a) Lengths not in parentheses are for crystallographic results, and are counts of amino acids with coordinates; they exclude disordered residues ("gaps" in the model). Lengths in parentheses are for the target sequence of DnaC, or sequences of the crystallized protein (from SEQRES in the PDB file). Below is the alignment produced by Swiss Model, used in making the 3D model. Vertical bars for identity were inserted by hand (I may have missed some). <pre> | | | | || TARGET 55 R TFNRSGIRPL HQNCSFENYR VECEGQMNAL SKARQYVEEF 2qgzA 100 qkqaais--e riqlvslpks yrhihlsdid vnnasrmeaf saildfveqy TARGET sssss h h hhhhhhh hhhhhhhhh 2qgzA hhh h sss h h hhhhhhh hhhhhhhhh | | || || | | | TARGET 96 DGN-IASFIF SGKPGTGKNH LAAAICNELL L-RGKSVLII TVADIMSAMK 2qgzA 148 psaeqkglyl ygdmgigksy llaamahels ekkgvsttll hfpsfaidvk TARGET ssss ss hhh hhhhhhhhhh h h ssss sshhhhhhh 2qgzA ssss ss hhh hhhhhhhhhh hh ssss sshhhhhhh || | | || | TARGET 144 DTFRNSGTSE EQLLNDLSNV DLLVIDEIGV QTESKYEKVI INQIVDRRSS 2qgzA 198 naiske---- --eidavknv pvlilddiga vrde-----v lqvilqyrml /\ / \ TARGET hhh ssssss hhhhhhhhhh 2qgzA hh h ssssss hhhhhhhhhh | | ||| | | | TARGET 194 SKRPTGMLTN SNMEEMTKLL ---GERVMDR MRLGNSLWVI FNWDSYR 2qgzA 247 eelptfftsn ysfadlerkw awqakrvmer vr-ylarefh leganrr- /\ TARGET h ssssss hhhhh hhhh hh ssssss s 2qgzA h ssssss hhhh hhhh hh hh ssss s </pre> Below is the sequence with ATOM records (coordinates) from 2QGZ, numbered 100-300, showing the gaps as "...". This sequence listing was used to locate the positions marked /\ above. <pre> 1 .......... .......... .......... .......... .......... 51 .......... .......... .......... .......... .........Q 101 KQAAISERIQ LVSLPKSYRH IHLSDIDVNN ASRMEAFSAI LDFVEQYPSA 151 EQKGLYLYGD MGIGKSYLLA AMAHELSEKK GVSTTLLHFP SFAIDVKNAI 201 S....KEEID AVKNVPVLIL DDIGA..... .VRDEVLQVI LQYRMLEELP 251 TFFTSNYSFA DLERKWA... .....WQAKR VMERVRYLAR EFHLEGANRR </pre> (Copied from Protein Explorer's sequence display.) Below is the alignment of full-length DnaC with 2QGZ according to TargetDB (see above). Note that the 2QGZ structure begins at residue 100, and so the homology model begins with residue 55 of DnaC, indicated with &gt; below. <pre> ID: DR58 Center: NESGC E-value: 0.00028 Identity: 19.737% 10 20 30 Query MKNVGDLMQRLQKMMPAHIKPAFKTGEELLAWQKEQGA Q+ Q P++I +++ + + + Subjct EVASFISQHHLSQEQINLSLSKFNQFLVERQKYQLKDPSYIAKGYQPILAMNEGYADVSY 40 50 60 70 80 90 40 50 > 60 70 80 90 Query IRSAALERENRAMKMQRTFNRSGIRPLHQNCSFENYRVECEGQMNALSKARQYVEEF-DG +++ L + ++ +++ ++ ++ +++ + + V+ ++M+A+S ++VE++ ++ Subjct LETKELVEAQKQAAISERIQLVSLPKSYRHIHLSDIDVNNASRMEAFSAILDFVEQYPSA 100 110 120 130 140 150 100 110 120 130 140 150 Query NIASFIFSGKPGTGKNHLAAAICNELLLR-GKSVLIITVADIMSAMKDTFRNSGTSEEQL + ++ + G G GK++L AA+ +EL + G S+ ++ ++ +K+++ N++++EE Subjct EQKGLYLYGDMGIGKSYLLAAMAHELSEKKGVSTTLLHFPSFAIDVKNAISNGSVKEE-- 160 170 180 190 200 160 170 180 190 200 210 Query LNDLSNVDLLVIDEIGV-QTESKYEKVIINQIVDRRSSSKRPTGMLTNSNMEEMTK---- ++ ++NV +L++D+IG+ Q+ S + +++ I++ R + PT + +N ++ ++ + Subjct IDAVKNVPVLILDDIGAEQATSWVRDEVLQVILQYRMLEELPTFFTSNYSFADLERKWAT 210 220 230 240 250 260 220 230 240 Query LLG-------ERVMDRMRLGNSLWVIFNWDSYRSRVTGKEY + G +RVM+R+R Subjct IKGSDETWQAKRVMERVRYLAREFHLEGANRR 270 280 290 300 </pre> ==ConSurf Coloring Script== For an explanation of the evolutionary conservation results, [[#Evolutionary Conservation|see above]]. The script below is from the 2012 analysis<ref name='2012consurf' />. It can be run in Jmol to color the amino acids of DnaC by evolutionary conservation. CON10 marks insufficient data. CON9 is the highest level of conservation, and CON1 is the lowest (most variable). <pre> select all color [200,200,200] select PHE57 color [255,255,150] spacefill define CON10 selected select ILE62, ASN73, GLY106, GLY109, THR110, GLY111, LYS112, HIS114, LEU115 select selected or ALA116, ALA118, GLU153, LEU165, LEU166, ASP169, GLU170 select selected or GLY172, ASP189, ARG191, ASN203, ARG216, ASP219, ARG220 select selected or TRP233, SER235, ARG237 color [160,37,96] spacefill define CON9 selected select ARG55, SER60, GLY61, LEU65, PHE71, TYR74, ALA84, VAL92, PHE95, ASN113 select selected or ILE119, LEU123, VAL130, THR134, THR145, VAL163, ILE168 select selected or GLN174, SER177, GLU180, ILE187, SER192, PRO197, THR198 select selected or THR202, GLY214, MET221, SER226, PHE231 color [240,125,171] spacefill define CON8 selected select HIS66, GLN81, PHE102, VAL135, SER140, LYS143, SER152, LEU156, ASP164 select selected or VAL167, ILE171, ILE184, ASN185, VAL188, GLY199, LEU213 color [250,201,222] spacefill define CON7 selected select THR56, ARG59, CYS69, SER70, ALA88, TYR91, ILE99, SER101, PHE104, SER105 select selected or ALA117, CYS120, ASN121, LEU124, GLY127, SER129, ILE133 select selected or ALA136, ASP137, ILE138, MET139, PHE146, ILE183, GLN186 select selected or ARG190, SER193, MET200, LEU201, SER204, LEU223, GLY224 select selected or ASN225, VAL229 color [252,237,244] spacefill define CON6 selected select ASN58, ARG63, ASN68, VAL76, GLY80, LEU85, ASN98, ALA100, ILE103, LEU131 select selected or MET142, LEU157, LEU160, SER161, VAL182, SER194, ASN205 select selected or MET209, VAL217, TYR236 color [255,255,255] spacefill define CON5 selected select ARG89, GLU94, PRO108, SER149, GLU154, LYS178, TYR179, LYS181, ARG196 select selected or GLU215, LEU227 color [234,255,255] spacefill define CON4 selected select PRO64, GLN67, GLU72, CYS78, MET82, ILE132, GLU176, GLU208, ASN232 color [215,255,255] spacefill define CON3 selected select GLN90, ARG126, ALA141, VAL173, LYS195 color [140,255,255] spacefill define CON2 selected select ARG75, GLU77, GLU79, ASN83, SER86, LYS87, GLU93, ASP96, GLY97, LYS107 select selected or GLU122, LEU125, LYS128, ASP144, ARG147, ASN148, GLY150 select selected or THR151, GLN155, ASN158, ASP159, ASN162, THR175, MET206 select selected or GLU207, THR210, LYS211, LEU212, MET218, ARG222, TRP228 select selected or ILE230, ASP234 color [16,200,209] spacefill define CON1 selected </pre> ==Notes & References == <references />

• Template:Clear
• Template:ColorKey Amino2CarboxyRainbow
• Template:ColorKey Charge Anionic
• Template:ColorKey Charge Cationic
• Template:ColorKey ConSurf
• Template:Theoretical model (protected)

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