Pages 1–7 1qj4 Evolutionary trace report by report maker January 28, 2010

4.3.1 Alistat 7 4.3.2 CE 7 4.3.3 DSSP 7 4.3.4 HSSP 7 4.3.5 LaTex 7 4.3.6 Muscle 7 4.3.7 Pymol 7 4.4 Note about ET Viewer 7 4.5 Citing this work 7 4.6 About report maker 7 4.7 Attachments 7

1 INTRODUCTION From the original Protein Data Bank entry (PDB id 1qj4): Title: Hydroxynitrile-lyase from hevea brasiliensis at atomic resolu- tion Compound: Mol id: 1; molecule: hydroxynitrile lyase; chain: a; synonym: oxynitrile lyase; ec: 4.2.1.39; engineered: yes Organism, scientific name: Hevea Brasiliensis; 1qj4 contains a single unique chain 1qj4A (256 residues long). CONTENTS

1 Introduction 1 2 CHAIN 1QJ4A 2 Chain 1qj4A 1 2.1 P52704 overview 2.1 P52704 overview 1 2.2 Multiple sequence alignment for 1qj4A 1 From SwissProt, id P52704, 100% identical to 1qj4A: 2.3 Residue ranking in 1qj4A 1 Description: (S)-acetone-cyanohydrin lyase (EC 4.1.2.39) ((S)- 2.4 Top ranking residues in 1qj4A and their position on hydroxynitrile lyase) ((S)-hydroxynitrilase) (Oxynitrilase). the structure 2 Organism, scientific name: Hevea brasiliensis (Para rubber tree). 2.4.1 Clustering of residues at 25% coverage. 2 Taxonomy: Eukaryota; Viridiplantae; Streptophyta; Embryophyta; 2.4.2 Overlap with known functional surfaces at Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core 25% coverage. 2 eudicotyledons; rosids; eurosids I; Malpighiales; Euphorbiaceae; 2.4.3 Possible novel functional surfaces at 25% Crotonoideae; Micrandreae; Hevea. coverage. 4 Function: Involved in cyanogenesis, the release of HCN from inju- red tissues. Decomposes a varieties of (R) or (S) cyanohydrins into 3 Notes on using trace results 5 HCN and the corresponding aldehydes and ketones. The natural 3.1 Coverage 5 substrate of this enzyme is (S)-acetone cyanohydrin. 3.2 Known substitutions 6 Catalytic activity: 2-hydroxyisobutyronitrile = cyanide + acetone. 3.3 Surface 6 Subunit: Homodimer. 3.4 Number of contacts 6 Ptm: The N-terminus is blocked. 3.5 Annotation 6 Similarity: Belongs to the AB hydrolase superfamily. Hydroxynitrile 3.6 Mutation suggestions 6 lyase family. About: This Swiss-Prot entry is copyright. It is produced through a 4 Appendix 6 collaboration between the Swiss Institute of Bioinformatics and the 4.1 File formats 6 EMBL outstation - the European Bioinformatics Institute. There are 4.2 Color schemes used 6 no restrictions on its use as long as its content is in no way modified 4.3 Credits 7 and this statement is not removed.

1 Lichtarge lab 2006 2.4 Top ranking residues in 1qj4A and their position on the structure In the following we consider residues ranking among top 25% of resi- dues in the protein . Figure 3 shows residues in 1qj4A colored by their importance: bright red and yellow indicate more conserved/important residues (see Appendix for the coloring scheme). A Pymol script for producing this figure can be found in the attachment.

Fig. 1. Residues 2-129 in 1qj4A colored by their relative importance. (See Appendix, Fig.9, for the coloring scheme.)

Fig. 2. Residues 130-257 in 1qj4A colored by their relative importance. (See Appendix, Fig.9, for the coloring scheme.)

2.2 Multiple sequence alignment for 1qj4A For the chain 1qj4A, the alignment 1qj4A.msf (attached) with 33 sequences was used. The alignment was downloaded from the HSSP database, and fragments shorter than 75% of the query as well as duplicate sequences were removed. It can be found in the attachment to this report, under the name of 1qj4A.msf. Its statistics, from the Fig. 3. Residues in 1qj4A, colored by their relative importance. Clockwise: alistat program are the following: front, back, top and bottom views.

Format: MSF Number of sequences: 33 Total number of residues: 8290 2.4.1 Clustering of residues at 25% coverage. Fig. 4 shows the Smallest: 237 top 25% of all residues, this time colored according to clusters they Largest: 256 belong to. The clusters in Fig.4 are composed of the residues listed Average length: 251.2 in Table 1. Alignment length: 256 Table 1. Average identity: 42% cluster size member Most related pair: 99% color residues Most unrelated pair: 26% red 63 7,8,9,10,11,14,15,16,17,19 Most distant seq: 35% 21,23,26,27,30,31,33,35,37 38,40,42,57,60,61,72,73,76 Furthermore, 3% of residues show as conserved in this alignment. 77,78,79,80,82,83,87,89,94 The alignment consists of 93% eukaryotic ( 93% plantae), and 3% 96,101,102,105,107,108,161 prokaryotic sequences. (Descriptions of some sequences were not 164,165,168,172,174,194,195 readily available.) The file containing the sequence descriptions can 196,199,207,215,234,235,238 be found in the attachment, under the name 1qj4A.descr. 240,242,245,249,252

Table 1. Clusters of top ranking residues in 1qj4A. 2.3 Residue ranking in 1qj4A The 1qj4A sequence is shown in Figs. 1–2, with each residue colored according to its estimated importance. The full listing of residues 2.4.2 Overlap with known functional surfaces at 25% coverage. in 1qj4A can be found in the file called 1qj4A.ranks sorted in the The name of the ligand is composed of the source PDB identifier attachment. and the heteroatom name used in that file.

2 Table 2. continued res type subst’s cvg noc/ dist (%) bb (A˚ ) K(3) V(3) 172 L L(81) 0.19 19/6 3.74 V(6) S(12) 21 K K(87) 0.20 6/3 4.04 R(12) 23 K A(21) 0.21 25/1 2.77 V(18) K(51) I(9) 164 E E(72) 0.25 33/19 3.13 G(6) K(9) Q(12)

Table 2. The top 25% of residues in 1qj4A at the interface with 1qj4A1. (Field names: res: residue number in the PDB entry; type: amino acid type; substs: substitutions seen in the alignment; with the percentage of each type Fig. 4. Residues in 1qj4A, colored according to the cluster they belong to: in the bracket; noc/bb: number of contacts with the ligand, with the number of red, followed by blue and yellow are the largest clusters (see Appendix for contacts realized through backbone atoms given in the bracket; dist: distance the coloring scheme). Clockwise: front, back, top and bottom views. The of closest apporach to the ligand. ) corresponding Pymol script is attached.

Table 3. Interface with 1qj4A1.Table 2 lists the top 25% of residues at res type disruptive the interface with 1qj4A1. The following table (Table 3) suggests mutations possible disruptive replacements for these residues (see Section 3.6). 17 W (KE)(TQD)(SNCRG)(M) 42 G (KER)(FQMWHD)(NYLPI)(SVA) Table 2. 168 L (YR)(H)(TKE)(SQCDG) res type subst’s cvg noc/ dist 174 R (D)(TY)(FEVLAWPI)(CG) ˚ (%) bb (A) 37 D (R)(FWH)(Y)(VCAG) 17 W W(100) 0.03 21/14 3.69 16 A (KER)(Y)(QHD)(N) 42 G G(100) 0.03 4/4 3.74 19 W (K)(E)(Q)(D) 168 L L(96) 0.06 33/2 3.55 165 E (FWH)(R)(YVCAG)(T) V(3) 35 A (KR)(YE)(H)(Q) 174 R T(3) 0.06 7/0 3.96 27 E (FYW)(H)(CG)(TVA) R(93) 172 L (R)(Y)(H)(K) K(3) 21 K (Y)(T)(FW)(SVCAG) 37 D D(93) 0.08 1/0 4.96 23 K (Y)(T)(FW)(H) E(3) 164 E (FW)(H)(Y)(VA) N(3) 16 A A(84) 0.09 11/8 3.32 Table 3. List of disruptive mutations for the top 25% of residues in 1qj4A, G(15) that are at the interface with 1qj4A1. 19 W W(93) 0.10 6/5 3.94 Y(6) 165 E D(90) 0.11 1/1 4.92 Figure 5 shows residues in 1qj4A colored by their importance, at the E(9) interface with 1qj4A1. 35 A S(3) 0.12 1/0 3.95 Glycerol binding site. Table 4 lists the top 25% of residues at the A(87) interface with 1qj4GOL300 (glycerol). The following table (Table V(9) 5) suggests possible disruptive replacements for these residues (see 27 E E(60) 0.18 4/0 4.14 Section 3.6). R(33) continued in next column

3 Table 5. continued res type disruptive mutations 14 H (E)(T)(Q)(D)

Table 5. List of disruptive mutations for the top 25% of residues in 1qj4A, that are at the interface with glycerol.

Fig. 5. Residues in 1qj4A, at the interface with 1qj4A1, colored by their rela- tive importance. 1qj4A1 is shown in backbone representation (See Appendix for the coloring scheme for the protein chain 1qj4A.)

Table 4. res type subst’s cvg noc/ dist antn (%) bb (A˚ ) 235 H H(100) 0.03 16/0 3.05 site 80 S S(90) 0.12 34/4 2.52 site A(3) Fig. 6. Residues in 1qj4A, at the interface with glycerol, colored by their D(6) relative importance. The ligand (glycerol) is colored green. Atoms further 11 T G(81) 0.13 25/2 2.28 than 30A˚ away from the geometric center of the ligand, as well as on the line T(15) of sight to the ligand were removed. (See Appendix for the coloring scheme N(3) for the protein chain 1qj4A.) 14 H S(3) 0.22 3/0 4.15 H(78) I(3) Figure 6 shows residues in 1qj4A colored by their importance, at the F(9) interface with 1qj4GOL300. L(6) 2.4.3 Possible novel functional surfaces at 25% coverage. One group of residues is conserved on the 1qj4A surface, away from (or Table 4. The top 25% of residues in 1qj4A at the interface with glyce- susbtantially larger than) other functional sites and interfaces reco- rol.(Field names: res: residue number in the PDB entry; type: amino acid gnizable in PDB entry 1qj4. It is shown in Fig. 7. The right panel type; substs: substitutions seen in the alignment; with the percentage of each shows (in blue) the rest of the larger cluster this surface belongs to. type in the bracket; noc/bb: number of contacts with the ligand, with the num- The residues belonging to this surface ”patch” are listed in Table ber of contacts realized through backbone atoms given in the bracket; dist: 6, while Table 7 suggests possible disruptive replacements for these distance of closest apporach to the ligand. ) residues (see Section 3.6). Table 6. Table 5. res type substitutions(%) cvg antn res type disruptive 17 W W(100) 0.03 mutations 30 G G(100) 0.03 235 H (E)(TQMD)(SNKVCLAPIG)(YR) 42 G G(100) 0.03 80 S (R)(K)(H)(Q) 235 H H(100) 0.03 site 11 T (R)(K)(FWH)(M) 60 P S(3)P(96) 0.04 continued in next column continued in next column

4 Table 7. continued res type disruptive mutations 42 G (KER)(FQMWHD)(NYLPI)(SVA) 235 H (E)(TQMD)(SNKVCLAPIG)(YR) 60 P (R)(Y)(H)(K) 207 D (R)(FWH)(Y)(VCAG) 168 L (YR)(H)(TKE)(SQCDG) 174 R (D)(TY)(FEVLAWPI)(CG) 242 T (R)(K)(H)(FQW) 249 L (R)(TY)(KE)(SCHG) 37 D (R)(FWH)(Y)(VCAG) Fig. 7. A possible active surface on the chain 1qj4A. The larger cluster it 16 A (KER)(Y)(QHD)(N) belongs to is shown in blue. 165 E (FWH)(R)(YVCAG)(T) 35 A (KR)(YE)(H)(Q) Table 6. continued 80 S (R)(K)(H)(Q) res type substitutions(%) cvg antn 11 T (R)(K)(FWH)(M) 207 D D(96)N(3) 0.05 site 57 Y (K)(Q)(EM)(N) 168 L L(96)V(3) 0.06 101 V (YR)(KE)(H)(QD) 174 R T(3)R(93)K(3) 0.06 31 H (E)(Q)(TKD)(M) 242 T P(87)T(12) 0.07 27 E (FYW)(H)(CG)(TVA) 249 L L(96)F(3) 0.07 172 L (R)(Y)(H)(K) 37 D D(93)E(3)N(3) 0.08 21 K (Y)(T)(FW)(SVCAG) 16 A A(84)G(15) 0.09 240 T (KR)(FQMWH)(E)(NLPI) 165 E D(90)E(9) 0.11 23 K (Y)(T)(FW)(H) 35 A S(3)A(87)V(9) 0.12 161 C (KR)(E)(FQMWH)(D) 80 S S(90)A(3)D(6) 0.12 site 14 H (E)(T)(Q)(D) 11 T G(81)T(15)N(3) 0.13 33 V (R)(KYE)(H)(QD) 57 Y Y(93)F(3)H(3) 0.14 164 E (FW)(H)(Y)(VA) 101 V V(90)I(9) 0.14 245 I (YR)(H)(T)(KE) 31 H H(87)Y(3)L(3) 0.16 F(6) Table 7. Disruptive mutations for the surface patch in 1qj4A. 27 E E(60)R(33)K(3) 0.18 V(3) Another group of surface residues is shown in Fig.8. The right panel 172 L L(81)V(6)S(12) 0.19 shows (in blue) the rest of the larger cluster this surface belongs to. 21 K K(87)R(12) 0.20 240 T S(72)T(15)C(12) 0.20 23 K A(21)V(18)K(51) 0.21 I(9) 161 C C(33)S(66) 0.21 14 H S(3)H(78)I(3) 0.22 F(9)L(6) 33 V V(84)A(9)P(3) 0.23 C(3) 164 E E(72)G(6)K(9) 0.25 Q(12) 245 I V(15)L(78)I(6) 0.25

Table 6. Residues forming surface ”patch” in 1qj4A. Fig. 8. Another possible active surface on the chain 1qj4A. The larger cluster it belongs to is shown in blue.

Table 7. res type disruptive The residues belonging to this surface ”patch” are listed in Table mutations 8, while Table 9 suggests possible disruptive replacements for these 17 W (KE)(TQD)(SNCRG)(M) residues (see Section 3.6). 30 G (KER)(FQMWHD)(NYLPI)(SVA) continued in next column

5 Table 8. 3.3 Surface res type substitutions(%) cvg To detect candidates for novel functional interfaces, first we look for 195 G G(100) 0.03 residues that are solvent accessible (according to DSSP program) by 72 E E(87)D(9)G(3) 0.15 2 at least 10A˚ , which is roughly the area needed for one water mole- 96 K K(93)R(6) 0.15 cule to come in the contact with the residue. Furthermore, we require 199 K K(30)R(69) 0.17 that these residues form a “cluster” of residues which have neighbor 73 K P(3)R(27)K(66) 0.20 within 5A˚ from any of their heavy atoms. E(3) Note, however, that, if our picture of protein evolution is correct, 94 C P(87)C(3)V(6) 0.23 the neighboring residues which are not surface accessible might be A(3) equally important in maintaining the interaction specificity - they 196 S R(3)S(81)A(9) 0.25 should not be automatically dropped from consideration when choo- T(6) sing the set for mutagenesis. (Especially if they form a cluster with the surface residues.) Table 8. Residues forming surface ”patch” in 1qj4A. 3.4 Number of contacts Another column worth noting is denoted “noc/bb”; it tells the num- Table 9. ber of contacts heavy atoms of the residue in question make across res type disruptive the interface, as well as how many of them are realized through the mutations backbone atoms (if all or most contacts are through the backbone, 195 G (KER)(FQMWHD)(NYLPI)(SVA) mutation presumably won’t have strong impact). Two heavy atoms 72 E (FWH)(R)(Y)(VA) are considered to be “in contact” if their centers are closer than 5A˚ . 96 K (Y)(T)(FW)(SVCAG) 3.5 Annotation 199 K (Y)(T)(FW)(SVCAG) 73 K (Y)(T)(FW)(CG) If the residue annotation is available (either from the pdb file or 94 C (R)(KE)(H)(YQD) from other sources), another column, with the header “annotation” 196 S (K)(R)(FQMWH)(E) appears. Annotations carried over from PDB are the following: site (indicating existence of related site record in PDB ), S-S (disulfide bond forming residue), hb (hydrogen bond forming residue, jb (james Table 9. Disruptive mutations for the surface patch in 1qj4A. bond forming residue), and sb (for salt bridge forming residue). 3.6 Mutation suggestions Mutation suggestions are completely heuristic and based on comple- 3 NOTES ON USING TRACE RESULTS mentarity with the substitutions found in the alignment. Note that 3.1 Coverage they are meant to be disruptive to the interaction of the protein Trace results are commonly expressed in terms of coverage: the resi- with its ligand. The attempt is made to complement the following due is important if its “coverage” is small - that is if it belongs to properties: small [AV GSTC], medium [LPNQDEMIK], large some small top percentage of residues [100% is all of the residues [WFYHR], hydrophobic [LPVAMWFI], polar [GTCY ]; posi- in a chain], according to trace. The ET results are presented in the tively [KHR], or negatively [DE] charged, aromatic [WFYH], form of a table, usually limited to top 25% percent of residues (or long aliphatic chain [EKRQM], OH-group possession [SDETY ], to some nearby percentage), sorted by the strength of the presumed and NH2 group possession [NQRK]. The suggestions are listed evolutionary pressure. (I.e., the smaller the coverage, the stronger the according to how different they appear to be from the original amino pressure on the residue.) Starting from the top of that list, mutating a acid, and they are grouped in round brackets if they appear equally couple of residues should affect the protein somehow, with the exact disruptive. From left to right, each bracketed group of amino acid effects to be determined experimentally. types resembles more strongly the original (i.e. is, presumably, less disruptive) These suggestions are tentative - they might prove disrup- 3.2 Known substitutions tive to the fold rather than to the interaction. Many researcher will One of the table columns is “substitutions” - other amino acid types choose, however, the straightforward alanine mutations, especially in seen at the same position in the alignment. These amino acid types the beginning stages of their investigation. may be interchangeable at that position in the protein, so if one wants to affect the protein by a point mutation, they should be avoided. For 4 APPENDIX example if the substitutions are “RVK” and the original protein has 4.1 File formats an R at that position, it is advisable to try anything, but RVK. Conver- sely, when looking for substitutions which will not affect the protein, Files with extension “ranks sorted” are the actual trace results. The one may try replacing, R with K, or (perhaps more surprisingly), with fields in the table in this file: V. The percentage of times the substitution appears in the alignment • alignment# number of the position in the alignment is given in the immediately following bracket. No percentage is given • residue# residue number in the PDB file in the cases when it is smaller than 1%. This is meant to be a rough • guide - due to rounding errors these percentages often do not add up type amino acid type to 100%. • rank rank of the position according to older version of ET

6 by HHMI/Washington University School of Medicine, 1992-2001, and freely distributed under the GNU General Public License. 4.3.2 CE To map ligand binding sites from different source structures, report maker uses the CE program: COVERAGE http://cl.sdsc.edu/. Shindyalov IN, Bourne PE (1998) ”Protein structure alignment by incremental combinatorial extension V (CE) of the optimal path . Protein Engineering 11(9) 739-747. 100% 50% 30% 5% 4.3.3 DSSP In this work a residue is considered solvent accessi- ble if the DSSP program finds it exposed to water by at least 10A˚ 2, which is roughly the area needed for one water molecule to come in the contact with the residue. DSSP is copyrighted by W. Kabsch, C. Sander and MPI-MF, 1983, 1985, 1988, 1994 1995, CMBI version V by [email protected] November 18,2002, RELATIVE IMPORTANCE http://www.cmbi.kun.nl/gv/dssp/descrip.html. 4.3.4 HSSP Whenever available, report maker uses HSSP ali- Fig. 9. Coloring scheme used to color residues by their relative importance. gnment as a starting point for the analysis (sequences shorter than 75% of the query are taken out, however); R. Schneider, A. de Daruvar, and C. Sander. ”The HSSP database of protein structure- • variability has two subfields: sequence alignments.” Nucleic Acids Res., 25:226–230, 1997. 1. number of different amino acids appearing in in this column of the alignment http://swift.cmbi.kun.nl/swift/hssp/ 2. their type 4.3.5 LaTex The text for this report was processed using LATEX; • rho ET score - the smaller this value, the lesser variability of Leslie Lamport, “LaTeX: A Document Preparation System Addison- this position across the branches of the tree (and, presumably, Wesley,” Reading, Mass. (1986). the greater the importance for the protein) 4.3.6 Muscle When making alignments “from scratch”, report • cvg coverage - percentage of the residues on the structure which maker uses Muscle alignment program: Edgar, Robert C. (2004), have this rho or smaller ”MUSCLE: multiple sequence alignment with high accuracy and • gaps percentage of gaps in this column high throughput.” Nucleic Acids Research 32(5), 1792-97. 4.2 Color schemes used http://www.drive5.com/muscle/ The following color scheme is used in figures with residues colored 4.3.7 Pymol The figures in this report were produced using by cluster size: black is a single-residue cluster; clusters composed of Pymol. The scripts can be found in the attachment. Pymol more than one residue colored according to this hierarchy (ordered is an open-source application copyrighted by DeLano Scien- by descending size): red, blue, yellow, green, purple, azure, tur- tific LLC (2005). For more information about Pymol see quoise, brown, coral, magenta, LightSalmon, SkyBlue, violet, gold, http://pymol.sourceforge.net/. (Note for Windows bisque, LightSlateBlue, orchid, RosyBrown, MediumAquamarine, users: the attached package needs to be unzipped for Pymol to read DarkOliveGreen, CornflowerBlue, grey55, burlywood, LimeGreen, the scripts and launch the viewer.) tan, DarkOrange, DeepPink, maroon, BlanchedAlmond. The colors used to distinguish the residues by the estimated 4.4 Note about ET Viewer evolutionary pressure they experience can be seen in Fig. 9. Dan Morgan from the Lichtarge lab has developed a visualization tool specifically for viewing trace results. If you are interested, please 4.3 Credits visit: 4.3.1 Alistat alistat reads a multiple sequence alignment from the http://mammoth.bcm.tmc.edu/traceview/ file and shows a number of simple statistics about it. These stati- stics include the format, the number of sequences, the total number The viewer is self-unpacking and self-installing. Input files to be used of residues, the average and range of the sequence lengths, and the with ETV (extension .etvx) can be found in the attachment to the alignment length (e.g. including gap characters). Also shown are main report. some percent identities. A percent pairwise alignment identity is defi- ned as (idents / MIN(len1, len2)) where idents is the number of 4.5 Citing this work exact identities and len1, len2 are the unaligned lengths of the two The method used to rank residues and make predictions in this report sequences. The ”average percent identity”, ”most related pair”, and can be found in Mihalek, I., I. Res,ˇ O. Lichtarge. (2004). ”A Family of ”most unrelated pair” of the alignment are the average, maximum, Evolution-Entropy Hybrid Methods for Ranking of Protein Residues and minimum of all (N)(N-1)/2 pairs, respectively. The ”most distant by Importance” J. Mol. Bio. 336: 1265-82. For the original version seq” is calculated by finding the maximum pairwise identity (best of ET see O. Lichtarge, H.Bourne and F. Cohen (1996). ”An Evolu- relative) for all N sequences, then finding the minimum of these N tionary Trace Method Defines Binding Surfaces Common to Protein numbers (hence, the most outlying sequence). alistat is copyrighted Families” J. Mol. Bio. 257: 342-358.

7 report maker itself is described in Mihalek I., I. Res and O. • 1qj4A.cluster report.summary - Cluster report summary for Lichtarge (2006). ”Evolutionary Trace Report Maker: a new type 1qj4A of service for comparative analysis of proteins.” Bioinformatics • 1qj4A.ranks - Ranks file in sequence order for 1qj4A 22:1656-7. • 1qj4A.clusters - Cluster descriptions for 1qj4A 4.6 About report maker • 1qj4A.msf - the multiple sequence alignment used for the chain report maker was written in 2006 by Ivana Mihalek. The 1D ran- 1qj4A king visualization program was written by Ivica Res.ˇ report maker • 1qj4A.descr - description of sequences used in 1qj4A msf is copyrighted by Lichtarge Lab, Baylor College of Medicine, • 1qj4A.ranks sorted - full listing of residues and their ranking for Houston. 1qj4A 4.7 Attachments • 1qj4A.1qj4A1.if.pml - Pymol script for Figure 5 The following files should accompany this report: • 1qj4A.cbcvg - used by other 1qj4A – related pymol scripts • 1qj4A.complex.pdb - coordinates of 1qj4A with all of its inter- • 1qj4A.1qj4GOL300.if.pml - Pymol script for Figure 6 acting partners • 1qj4A.etvx - ET viewer input file for 1qj4A

8