@text 
EXERCISE 8. ASPARTATE TRANSCARBAMOYLASE - ALLOSTERISM IN


KINEMAGE 1: Quarternary Structure of ATCase and Its Allosteric Conformational Changes.
KINEMAGE 2: Conformational Changes Caused by the Binding of Substrate and Effectors.


	Aspartate transcarbamoylase (ATCase) is a multisubunit enzyme that catalyzes the reaction of carbamoyl phosphate with aspartate to yield N-carbamoyl phosphate and Pi (Section 12-4). This irreversible reaction constitutes the first committed step in the synthesis of pyrimidines (Section 26-3A). Since either a shortage or an excess of pyrimidines (cytosine and thymine) relative to purines (adenine and guanine) greatly increases the error rate in DNA synthesis, it is essential that the rate of pyrimidine synthesis be closely regulated to precisely satisfy the needs of the cell. In E. coli, this occurs through the control of the catalytic activity of ATCase: The enzyme is inhibited by CTP (Fig. 12-5), a product of the pyrimidine synthesis pathway (Fig. 12-6 and Section 26-3B), and is activated by ATP, whose high concentration indicates that purines are in excess. Both of these metabolites bind to a site on the enzyme different from its catalytic site, a so-called allosteric site, and hence ATCase is an allosteric enzyme. Indeed, ATCase closely follows the symmetry model of allosterism (Section 9-4B). 

	In the symmetry (or MWC) model of allosterism, a symmetric multisubunit enzyme has (at least) two conformational states: a less catalytically active state known as its T state and a more catalytically active state known as its R state. The conformational changes between the T and R states, nevertheless, preserve the symmetry of the enzyme (hence the name "symmetry model") so that, in this model, states in which the enzyme's various chemically equivalent subunits have different conformations are forbidden. Substrate(s) preferentially binds to the R state thereby stabilizing the protein in this conformation and increasing the protein's affinity for substrate. This cooperative process is known as a positive homotropic effect. Thus both aspartate and carbamoyl phosphate are positive homotropic effectors of ATCase. By the same token, activators preferentially bind to an allosteric site on the R-state enzyme, thereby also increasing its affinity for substrate (a positive heterotropic effect), whereas inhibitors preferentially bind to an allosteric site on the T-state enzyme, thereby decreasing its affinity for substrate (a negative heterotropic effect). Hence, ATP and CTP are positive and negative heterotropic effectors of ATCase.

	In this exercise we examine and compare the quaternary and tertiary structures of E. coli ATCase in its T and R states. We also inspect how the unreactive bisubstrate analog N-(phosphoacetyl)-L-aspartate (PALA; p. 339) binds to ATCase's active site and how the effectors ATP and CTP bind to the enzyme's allosteric site.


KINEMAGE 1: Quarternary Structure of ATCase and Its Allosteric Conformational Changes.


**************************** A Cautionary Note **************************
	ATCase is a very large protein. Thus, as you may have already noticed, MAGE takes considerably longer than usual to display this kinemage as well as to change the display. In particular, any attempt to rotate the entire protein must be done in small increments to get predictable results.
*********************************************************************

	E. coli ATCase is a 310-kD enzyme that consists of six copies each of two types of subunits: a 310-residue catalytic (c) subunit and a 158-residue regulatory (r) subunit (although its first 7 residues are not seen in the X-ray structures displayed here). Under mildly denaturing conditions, ATCase decomposes to yield trimers of catalytic subunits (c3) that are catalytically active but unresponsive to the presence of ATP and CTP, and dimers of regulatory subunits (r2) that bind ATP and CTP but are catalytically inactive.

	An ATCase molecule has D3 symmetry, that is, it has a 3-fold rotational axis which is perpendicular to three equivalent 2-fold rotational axes that are 60 degrees apart (Fig. 7-58b; the symmetry of a trigonal prism). KINEMAGE 1 opens in View1 showing the entire T state ATCase molecule as viewed along its 3-fold axis. The three subunits of the upper catalytic trimer (by custom, subunits c1, c2, and c3, starting on the left and going clockwise) are red and those of the lower catalytic trimer (c4, c5, and c6, which are respectively below c1, c2, and c3) are cyan. The members of the upper catalytic trimer can be better differentiated by clicking on the "Cat. Trimer" masterbutton which changes the colors of c2 and c3 to pink and pinktint. Each regulatory subunit is in direct contact with only one catalytic subunit and is assigned the same subscript (e.g., r1 contacts c1). The three upper regulatory subunits in View1 (r1, r2, and r3) are green and the lower three (r4, r5, and r6) are gold. The three regulatory dimers are each composed of a green and a gold subunit (r1 with r6, r2 with r4, and r3 with r5). 

	The asymmetric portion of a protein, which in ATCase consists of one catalytic subunit and its associated regulatory subunit (e.g., c1 and r1), is referred to as a protomer. By this terminology (Section 7-5A), which we use here, ATCase is a hexamer of protomers (although, since it consists of 12 subunits of two types, it may be alternatively described as being a heterododecamer). View2 shows ATCase along its 3-fold axis from the opposite direction as View1 (with the cyan and gold subunits on top), View3 shows ATCase in a perpendicular direction along a 2-fold axis with the r1-r6 regulatory dimer closest (seen from the lower left in View1), whereas View4 is along another 2-fold axis with the c3 and c6 subunits closest (seen from the bottom in View1). A close inspection of the ATCase structure reveals that although the protein has exact 3-fold symmetry, its 2-fold symmetry (that relating chemically identical subunits of different colors) is not quite perfect. This is because although the 3-fold axes of the protein molecule and the crystal that it forms coincide, this is not the case with the 2-fold axes. In solution, ATCase presumably has exact D3 symmetry. 

	To see how the T-state protein is constructed, again turn on View1, turn off the "Hexamer" master button, and turn on the "Protomer" masterbutton. This displays the c1-r1 protomer. Rotate this small portion of the entire protein around to convince yourself that its two subunits are in contact only over relatively small fractions of their surface areas. Now go back to View1, turn off "Protomer" and turn on "Dimer". The 2-fold axis relating the two protomers displayed (c1-r1 and c6-r6) runs from the lower left to the upper right of the display. View4 shows this dimer along its 2-fold axis as seen from the lower left of View1. Note that r1 contacts r6 via a beta pleated sheet. We shall examine this sheet in greater detail in KINEMAGE 2. Switch off the "Reg. Dimer" masterbutton to eliminate the r1-r 6 regulatory dimer from the display. It is now quite clear that c1 and c6 are not in contact with one another; their distances of closest approach are nearly 20 � as you should verify. 

	Go back to View1, turn off "Dimer" and turn on "Reg. Dimer" and "Tetramer". This adds the c2-r2-r4-c4 dimer to the display. Your perception of depth here might be enhanced by temporarily switching off "onewidth" under the "Display" pulldown menu. Now, turn off "Tetramer" and turn on "Hexamer" to add the c3-r3-r5-c5 dimer. Note that the three dimers are arranged in a manner reminiscent of the overlapping flaps of a closed cardboard carton with the first dimer over the second over the third over the first.

	To see how the subunits of a catalytic trimer contact each other, turn off the "Hexamer" and turn on the "Trimer" masterbuttons. Note that these contacts appear to be rather tenuous. We shall also examine these contacts in more detail in KINEMAGE 2.

	We have, so far, only seen T-state ATCase. Let us now examine R-state ATCase and compare it to the T-state enzyme. Turn on "Hexamer" to again display the entire T-state enzyme. Then click the "ANIMATE" hbutton to show the enzyme in its R state (toggling "ANIMATE" alternately displays ATCase's R and T states). Note that the T to R transition rotates the upper catalytic trimer counterclockwise relative to the lower catalytic trimer such that they more completely eclipse each other. This is a relative rotation of around 12 degrees. This conformational shift, in accord with the symmetry model of allosterism, maintains the enzyme's D3 symmetry.

	The allosteric changes in ATCase appear more dramatic in View4. Here it can be seen that the T to R transition causes the molecule to elongate along its 3-fold axis by around 11 �. This quaternary transition is accompanied by a major structural reorganization of the contacting residues in vertically aligned subunits (e.g., c3 and c6), the 240s loop (so-called because it encompasses residues 225-245). This reorganization can be more clearly seen by turning on the "240s Loop" masterbutton which colors the 240s loops of the upper catalytic trimer magenta and those of the lower catalytic trimer purple. We shall return to them presently. 

	View4 shows that, in the T to R transition, the regulatory dimers, the major links between the upper and lower catalytic trimers, rotate clockwise by 15 degrees without undergoing major tertiary structural reorganization (although we shall examine this change in greater detail in KINEMAGE 2). Thus, at the quaternary level, ATCase resembles a finely articulated mechanical device in which the simultaneous clockwise rotation of the three apparently rigid regulatory dimers levers apart the catalytic trimers.

	Now let us return to the 240s loops. Turn off the "Hexamer" and "Cat. Trimer" masterbuttons to display the six 240s loops by themselves. Note their changes in the allosteric transition in View1, View2, and View3. Turning on "Trimer" in these views as well as View2 highlights the structural relationships of the 240s loops to the catalytic trimers.

	Finally, let us examine the details of how the 240s loop undergoes the T to R transition. Go to View5, an expanded version of View4, switch off the "Cat. Trimer" and switch on the "c3, c6" and "240s SideCh." masterbuttons. The latter displays the side chains that undergo major structural rearrangements in the allosteric transitions, with those of the upper catalytic trimer yellow, those of the lower catalytic trimer orange, their nitrogen and oxygen atoms represented by blue and red balls, and the hydrogen bonds between them represented by dashed white lines. In the T state, the two contacting 240s loops between the c3 and c6 subunits (and, by symmetry, those of the c1-c4 and c2-c5 pairs) lie side by side and are joined by hydrogen bonds from each Tyr 165 to the Glu 239 of the adjoining subunit (Lys 164 on c3 also makes a hydrogen bonded salt bridge with Glu 239 on c6 but, in the corresponding c6-c3 interaction, the distance between these charged groups is too long for such an interaction; recall that the enzyme's 2-fold symmetry is only approximate in the X-ray structures displayed here). However, in the R state, Glu 239 makes intrasubunit hydrogen bonds with Tyr 165, which is bolstered by a hydrogen bonded salt bridge with Lys 164, also from the same subunit (upper right and lower left). The importance of these interactions in conformationally stabilizing ATCase is demonstrated by the mutation of Glu 239 to Gln. This converts ATCase to an enzyme that is devoid of both homotropic and heterotropic effects and which has a quaternary structure that is intermediate between the T and R states of the unmutated enzyme. The 240s loop in its T-state conformation is internally crosslinked by a hydrogen bond between Tyr 240 and Asp 271, which is ruptured in the R state. However, in the R state, the two apposed ends of the 240s loops (center) are joined by hydrophobic interactions involving the nonpolar portions of Pro 237, Ser 238, Tyr 240, and Ala 241, whereas the T state has no comparable intersubunit interactions.


KINEMAGE 2: Conformational Changes Caused by the Binding of Substrate and Effectors.

	This kinemage opens in View1 showing the T-state c1-r1 protomer as seen in View1 of KINEMAGE 1 when its "Protomer" masterbutton is on, that is, along ATCase's 3-fold axis. However, in this kinemage, the two domains of each subunit are differently colored: The catalytic subunit's carbamoyl phosphate and aspartate domains (which bind the enzyme's carbamoyl phosphate and aspartate substrates) are red and yellow, and the regulatory subunit's allosteric and zinc domains are green and seagreen. These four domains can be individually switched on and off using the "CP Domain", "Asp. Domain", "Allo. Domain", and "Zinc Domain" masterbuttons, respectively. Switching on the "Dimer" masterbutton turns on the c6 and r6 subunits, which are respectively cyan and gold as they are in KINEMAGE 1. In addition, the CTP bound to the T-state enzyme's allosteric site on the allosteric domain is shown in red. View2 is also along the 3-fold axis but viewed from the opposite side as View1. Clicking the "ANIMATE" button switches to the T state, in which the bisubstrate analog PALA (green) is bound at the enzyme's active site which, as you can see, spans the carbamoyl and aspartate domains of the catalytic subunits. Note that CTP is not bound to the R-state enzyme.

	Turn off the "Dimer" masterbutton and turn on all the domains of the c1-r1 protomer. Then toggle between the T and R states. Note that the most conspicuous conformational change in both subunits on undergoing a T to R transition is a coming together of their two domains by what appear to be hinge motions about their connecting polypeptide segments (the c1 subunit's interdomain interface can be seen more clearly if c1 is rotated by a few degrees about the x axis). Thus the interface between the c1 and r1 subunit, that of their carbamoyl phosphate and zinc domains, are relatively rigid although both domains can be seen to undergo significant conformational changes between the T and R conformations.

	Now, let us examine, in greater detail than in KINEMAGE 1, how the r1 and r6 subunits associate. Switch on the "Dimer" masterbutton and go to View3, the view along the 2-fold axis relating these two subunits. Temporarily switching off "onewidth" under the "Display" pulldown menu shows that this regulatory dimer is in the foreground. Switch off the "CTP" button for clarity and then switch on the "r1 Sheet" and "r6 Sheet" masterbuttons to highlight the 5-stranded antiparallel beta sheet in each regulatory subunit (greentint for r1 and yellowtint for r6). You can see that these two sheets are joined in antiparallel fashion across the 2-fold axis to form a 10-stranded antiparallel beta pleated sheet. Switching off all masterbuttons but "r1 Sheet" and "r6 Sheet" and then toggling the "ANIMATE" button demonstrates that this sheet undergoes little change in the T to R transition. View4 is along this sheet in the T state (a slight reorientation of the R-state sheet shows a similar view). Note that this sheet has the normal right handed twist (Section 7-1C) and that the first strand of the sheet is twisted by over 90 degrees relative to its last strand (the amount of twist can be measured by invoking "measures" under the "Other" pulldown menu and determining the torsional angle between equivalent pairs of atoms on the two strands). 

	 Although ATP preferentially binds to R-state ATCase and is therefore an activator of this enzyme, the only known X-ray structure of an ATCase-ATP complex is that of the T-state enzyme. We shall therefore examine the structure of T-state ATCase in complex with ATP and compare it with that of the CTP complex. Put the enzyme in the T state, turn on the ATP button, turn off the CTP button, and select View5 (which is approximately parallel to the 3-fold axis in the same direction as View1). The ATP is blue and its N, O, and P atoms are represented by blue, red, and gold balls. Turn on the "r1 Sheet" masterbutton to demonstrate that the ATP is bound under it in the present view, near the periphery of the protein. Turning on the "Effector sc" masterbutton shows the ATCase side chains involved in effector binding in seagreen with hydrogen bonds as dashed bluetint lines. Note that there are numerous hydrogen bonds from the protein's side chains and its main chain to the adenine ring as well as to the ribose residue and a phosphate group.

	Now turn off the "ATP" button and turn on the "CTP" button. The CTP is shown in red, the protein side chains involved in effector binding and the mainchain segments that differ conformationally from those of the ATP complex are orange, and the hydrogen bonds they make are dashed pinkint lines. The CTP also interacts with the protein through hydrogen bonds to ATCase's side chains and main chain but, as you can see by clicking on and off the "ATP" button, the positions and orientations of many of these groups differ significantly in the two complexes (the clutter of groups here may be partially alleviated by turning off the "Allo. Domain" and "r1 Sheet" masterbuttons). Note also that the binding position of CTP's nucleoside (base + ribose) moiety is rigidly shifted with respect to that of ATP such that CTP's O2 and N4 atoms (hydrogen bonding acceptors and donors) nearly coincide with the positions of ATP's N3 and N6 atoms (also hydrogen bonding acceptors and donors). In addition, the two triphosphate groups bind to ATCase in different conformations. These differences are almost certainly responsible for the different effects that ATP and CTP binding have on the conformation of ATCase in solution.

	Putting ATCase in the R state shows the side chains and main chain segments involved in T-state ATP and CTP binding in pink and green. By clicking on the "T State" button and turning on and off the "CTP" and "ATP" buttons, you can see that portions of the uncomplexed allosteric domain of the R-state regulatory subunits differ substantially in conformation from those of the T-state protein in complex with CTP and with ATP. 

	The regulatory subunits each bind a single zinc ion (Zn2+). Going to View6 and turning on the "Zn+Ligands" masterbutton in the T state reveals that the Zn2+ (large bluetint ball) is tetrahedrally liganded by four Cys residues (yellow with S atoms represented by yellow balls; the Zn-S bonds are white). Invoke "measures" under the "Other" pulldown menu to see how far the individual S-Zn-S bond angles deviate from the ideal tetrahedral angle of 109.5 degrees. Clicking on the "T State" button shows that there is little conformational difference around the Zn2+ ion between the T and R states (although there is a significant rigid shift in the position of the Zn2+ complex between the two states due to the domain closure in the regulatory subunit discussed above). It is therefore likely that the Zn2+ ion in ATCase functions to stabilize the enzyme's structure rather than having a regulatory or a catalytic role.

	Finally, let us see how PALA binding affects ATCase's conformation. In the R state, go to View1 and switch on all four "Domain" masterbuttons, the "Dimer" masterbutton, and the "PALA" button, the latter showing PALA in green. Alternating between the T state with CTP and/or ATP showing, and the R state with PALA showing, you can demontrate that the distances between ATCase's active sites (near the protein's 3-fold axis) and its effector sites (near the protein's periphery) are minimally around 60 �. Clearly, the influence of effector binding on ATCase's catalytic site cannot be direct but must be transmitted over long distances via conformational changes in the protein.

	Now go to View7 and put the enzyme in the R state with PALA showing. Note that this bisubstrate analog (whose N, O, and P atoms are represented by blue, red, and gold balls) binds to both the carbamoyl phosphate (red) and the aspartate (yellow) domains of the catalytic subunit. Turning on the "c2" masterbutton shows that the carbamoyl phosphate domain of catalytic subunit c2 (shown in pink with its so-called c80s loop, residues 75-87, in hotpink) also participates in binding PALA. Turning on the "PALA sc" masterbutton displays the ATCase side chains that participate in PALA binding with those of the carbamoyl phosphate domain in purple, those of the aspartate domain in cyan, and those of the c2 subunit in orange. Note the large number of hydrogen bonds and salt bridges (white dashed lines) through which PALA is bound to the protein. Repeatedly toggling the "ANIMATE" button shows that, on binding PALA and thereby converting from the T to R conformations, the protein's active site essentially collapses in on the PALA. It can be seen that, in doing so, the c80s loop of subunit c2 undergoes a significant conformational reorganization. This process presumably properly positions the enzyme's active site groups to catalyze the ATCase reaction. However, these groups have not yet been unequivocally identified.

	This exercise demonstrates that, although the differences in quaternary structure between the T and R states of ATCase are relatively simple, the details of their underlying tertiary conformational differences are exceedingly complex. We have no more than a rudimentary understanding of how the protein mechanically transmits the information among its twelve substrate- and effector-binding sites that substrate and/or effector have bound to them. An increased understanding of this process will almost certainly require a greater comprehension of intramolecular interactions in proteins than we presently have.


	The atomic coordinates for T-state ATCase in complex with ATP were obtained from 4AT1; those for R-state ATCase in complex with PALA were obtained from 8ATC; and those for CTP and the T-state ATCase residues that differ significantly in conformation from those in 4AT1 were obtained from 1RAI.
@kinemage 1 
@caption 
The quaternary structures of T- and R-state aspartate transcarbamoylase (ATCase). The ATCase is displayed with its upper catalytic trimer red, its lower catalytic trimer cyan, and its three regulatory dimers with their upper and lower subunits green and gold. Toggling the "ANIMATE" button alternately shows the enzyme in its T and R conformations. The "Cat. Trimer" masterbutton colors subunits c2 and c3 of the upper catalytic trimer pink and pinktint. The "240s Loop" masterbutton colors the 240s loops of the upper and lower catalytic trimers magenta and purple. The "240s SideCh." masterbutton displays the 240s loop side chains that undergo a conformational change in the T to R transition in yellow for c3 and in orange for c6. The hydrogen bonds linking these groups are represented by dashed white lines.
@onewidth 
@viewid {3-Fold, Top}
@zoom 1.15 
@zslab 210 
@center 58.173 30.828 33.230 
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 0.95406 -0.29958 -0.00556 -0.29961 -0.95404 -0.00658 -0.00333  0.00794 -0.99996
@2viewid {3-Fold, Bottom}
@2zoom 1.15 
@2zslab 210 
@2center 58.173 30.828 33.230 
@2matrix 
-0.93825 -0.34596  0.00020  0.34595 -0.93824 -0.00386  0.00152 -0.00355  0.99999
@3viewid {2-Fold, r1-r6}
@3zoom 1.56 
@3zslab 400 
@3center 30.834 74.469 40.128 
@3matrix 
 0.75834  0.07588 -0.64743  0.64771  0.02416  0.76150  0.07343 -0.99682 -0.03083
@4viewid {2-Fold, c3-c6}
@4zoom 1.15 
@4zslab 200 
@4center 58.274 25.541 41.844 
@4matrix 
 0.95700 -0.00006  0.29010 -0.29010 -0.00011  0.95700 -0.00002 -1.00000 -0.00012
@5viewid {240s Loop}
@5zoom 4.00 
@5zslab 200 
@5center 72.666 57.307 39.057 
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 0.95700 -0.00006  0.29010 -0.29010 -0.00011  0.95700 -0.00002 -1.00000 -0.00012
@group {T State} animate
@subgroup {dummy1} nobutton off master= {Protomer}
@subgroup {dummy2} nobutton off master= {Dimer}
@subgroup {dummy3} nobutton off master= {Tetramer}
@subgroup {dummy4} nobutton master= {Hexamer}
@subgroup {dummy5} nobutton off master= {------------}
@subgroup {dummy6} nobutton off master= {Reg. Dimer}
@subgroup {dummy7} nobutton off master= {Cat. Trimer}
@subgroup {dummy8} nobutton off master= {c3, c6}
@subgroup {dummy9} nobutton off master= {240s Loop}
@subgroup {dummy10} nobutton off master= {240s SideCh.}
@subgroup {Protomer-T} nobutton off master= {Protomer}
@vectorlist {dummyA} nobutton off
@vectorlist {c1T} nobutton color= red
{ ca  ala c1 1 } P 37.533, 46.851, -8.871 { ca  ala c1 1 } L 37.533, 46.851, -8.871
{ ca  asn c1 2 } L 36.400, 43.764, -6.903
{ ca  pro c1 3 } L 33.953, 44.626, -4.057
{ ca  leu c1 4 } L 36.585, 44.041, -1.367
{ ca  tyr c1 5 } L 39.553, 45.668, -3.175
{ ca  gln c1 6 } L 41.426, 47.827, -0.580
{ ca  lys c1 7 } L 38.829, 47.168, 2.116
{ ca  his c1 8 } L 39.750, 46.538, 5.737
{ ca  ile c1 9 } L 38.619, 43.087, 7.024
{ ca  ile c1 10 } L 37.852, 43.732, 10.644
{ ca  ser c1 11 } L 34.693, 42.044, 11.799
{ ca  ile c1 12 } L 32.321, 39.409, 10.412
{ ca  asn c1 13 } L 29.199, 41.443, 10.918
{ ca  asp c1 14 } L 30.753, 44.062, 8.544
{ ca  leu c1 15 } L 30.603, 41.620, 5.598
{ ca  ser c1 16 } L 27.390, 40.914, 3.743
{ ca  arg c1 17 } L 26.241, 37.596, 2.445
{ ca  asp c1 18 } L 27.499, 38.520, -0.986
{ ca  asp c1 19 } L 30.951, 39.372, 0.505
{ ca  leu c1 20 } L 31.215, 36.035, 2.344
{ ca  asn c1 21 } L 30.394, 34.372, -0.944
{ ca  leu c1 22 } L 32.816, 36.280, -3.038
{ ca  val c1 23 } L 35.510, 35.315, -0.543
{ ca  leu c1 24 } L 34.375, 31.696, -0.432
{ ca  ala c1 25 } L 34.217, 31.425, -4.241
{ ca  thr c1 26 } L 37.754, 32.841, -4.768
{ ca  ala c1 27 } L 39.109, 30.460, -2.164
{ ca  ala c1 28 } L 37.818, 27.495, -4.137
{ ca  lys c1 29 } L 39.444, 28.842, -7.328
{ ca  leu c1 30 } L 42.897, 29.411, -5.677
{ ca  lys c1 31 } L 42.645, 25.923, -4.336
{ ca  ala c1 32 } L 42.221, 24.252, -7.778
{ ca  asn c1 33 } L 44.417, 26.372, -10.082
{ ca  pro c1 34 } L 46.753, 28.371, -7.866
{ ca  gln c1 35 } L 48.547, 31.572, -8.874
{ ca  pro c1 36 } L 51.685, 31.564, -6.716
{ ca  glu c1 37 } L 53.165, 34.713, -8.239
{ ca  leu c1 38 } L 50.024, 36.948, -7.767
{ ca  leu c1 39 } L 51.383, 39.153, -4.983
{ ca  lys c1 40 } L 54.895, 39.129, -6.362
{ ca  his c1 41 } L 56.562, 42.300, -4.951
{ ca  lys c1 42 } L 54.087, 43.115, -2.176
{ ca  val c1 43 } L 55.373, 43.058, 1.487
{ ca  ile c1 44 } L 52.815, 42.158, 4.071
{ ca  ala c1 45 } L 53.595, 42.690, 7.783
{ ca  ser c1 46 } L 52.652, 39.882, 10.243
{ ca  cys c1 47 } L 52.240, 41.731, 13.533
{ ca  phe c1 48 } L 51.276, 39.417, 16.321
{ ca  phe c1 49 } L 51.245, 41.524, 19.425
{ ca  glu c1 50 } L 49.590, 38.455, 21.001
{ ca  ala c1 51 } L 51.329, 35.283, 19.752
{ ca  ser c1 52 } L 49.528, 32.312, 18.124
{ ca  thr c1 53 } L 51.675, 29.946, 16.180
{ ca  arg c1 54 } L 49.038, 28.166, 14.105
{ ca  thr c1 55 } L 47.431, 31.430, 12.936
{ ca  arg c1 56 } L 50.729, 33.066, 12.392
{ ca  leu c1 57 } L 51.980, 30.072, 10.403
{ ca  ser c1 58 } L 48.692, 29.777, 8.433
{ ca  phe c1 59 } L 48.661, 33.454, 7.320
{ ca  gln c1 60 } L 52.364, 33.506, 6.503
{ ca  thr c1 61 } L 52.028, 30.317, 4.397
{ ca  ser c1 62 } L 49.141, 32.039, 2.560
{ ca  met c1 63 } L 51.320, 35.158, 1.976
{ ca  his c1 64 } L 54.050, 32.898, 0.639
{ ca  arg c1 65 } L 51.772, 30.776, -1.592
{ ca  leu c1 66 } L 50.970, 33.964, -3.556
{ ca  gly c1 67 } L 54.568, 35.038, -3.851
{ ca  ala c1 68 } L 54.565, 37.813, -1.244
{ ca  ser c1 69 } L 57.238, 38.848, 1.325
{ ca  val c1 70 } L 56.521, 39.045, 4.949
{ ca  val c1 71 } L 58.094, 41.344, 7.584
{ ca  gly c1 72 } L 56.576, 40.827, 11.170
{ ca  phe c1 73 } L 56.862, 39.757, 14.847
{ ca  ser c1 74 } L 55.112, 38.187, 17.920
{ ca  asp c1 75 } L 55.667, 38.489, 21.752
{ ca  ser c1 76 } L 53.119, 38.023, 24.563
{ ca  ala c1 77 } L 56.009, 39.842, 26.422
{ ca  asn c1 78 } L 57.923, 43.205, 26.002
{ ca  thr c1 79 } L 58.919, 43.454, 22.308
{ ca  ser c1 80 } L 61.109, 46.638, 22.694
{ ca  leu c1 81 } L 60.022, 49.951, 20.926
{ ca  gly c1 82 } L 56.577, 48.485, 20.778
{ ca  lys c1 83 } L 56.111, 48.657, 24.557
{ ca  lys c1 84 } L 58.509, 51.664, 25.136
{ ca  gly c1 85 } L 55.713, 54.180, 25.500
{ ca  glu c1 86 } L 54.263, 53.421, 22.116
{ ca  thr c1 87 } L 50.719, 53.675, 21.450
{ ca  leu c1 88 } L 49.425, 51.201, 18.853
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{ ca  val r1 121 } L 40.671, 58.134, 19.769
{ ca  ser r1 122 } L 37.463, 59.933, 20.565
{ ca  ser r1 123 } L 34.922, 57.518, 21.924
{ ca  ser r1 124 } L 31.925, 56.507, 19.834
{ ca  phe r1 125 } L 28.858, 54.544, 20.648
{ ca  ala r1 126 } L 25.927, 53.708, 18.399
{ ca  val r1 127 } L 22.793, 54.641, 20.260
{ ca  arg r1 128 } L 19.670, 52.553, 19.834
{ ca  lys r1 129 } L 16.092, 52.035, 21.182
{ ca  arg r1 130 } L 14.055, 55.013, 22.504
{ ca  ala r1 131 } L 13.581, 56.029, 26.179
{ ca  asn r1 132 } L 12.804, 52.550, 27.879
{ ca  asp r1 133 } L 16.414, 51.409, 27.584
{ ca  ile r1 134 } L 19.065, 52.872, 25.473
{ ca  ala r1 135 } L 21.756, 50.464, 24.357
{ ca  leu r1 136 } L 25.085, 52.086, 23.628
{ ca  lys r1 137 } L 27.454, 49.995, 21.506
{ ca  cys r1 138 } L 31.180, 50.821, 21.515
{ ca  lys r1 139 } L 32.682, 51.346, 18.137
{ ca  tyr r1 140 } L 36.007, 49.703, 18.885
{ ca  cys r1 141 } L 35.359, 46.619, 21.020
{ ca  glu r1 142 } L 31.840, 46.324, 19.456
{ ca  lys r1 143 } L 30.355, 45.608, 22.951
{ ca  glu r1 144 } L 26.732, 46.697, 23.715
{ ca  phe r1 145 } L 26.053, 48.275, 27.179
{ ca  ser r1 146 } L 23.056, 49.629, 28.935
{ ca  his r1 147 } L 23.293, 53.387, 29.019
{ ca  asn r1 148 } L 22.859, 52.894, 32.777
{ ca  val r1 149 } L 26.383, 51.500, 33.079
{ ca  val r1 150 } L 28.173, 53.724, 30.547
{ ca  leu r1 151 } L 26.685, 56.843, 32.018
{ ca  ala r1 152 } L 28.160, 55.998, 35.407
{ ca  asn r1 153 } L 31.950, 55.368, 34.541
@subgroup {Dimer-T} nobutton off master= {Dimer}
@vectorlist {dim-c1T} instance={c1T} nobutton color= red
@vectorlist {dim-r1T} master= {Reg. Dimer} instance={r1T} nobutton color= green
@vectorlist {dim-c1T-240s} master= {240s Loop} instance= {c1T-240s} nobutton off color= magenta
@vectorlist {c6T} nobutton color= cyan
{ ca  ala c6 1 } P 55.895, 61.355, 79.663 { ca  ala c6 1 } L 55.895, 61.355, 79.663
{ ca  asn c6 2 } L 59.022, 61.632, 77.512
{ ca  pro c6 3 } L 58.648, 64.012, 74.462
{ ca  leu c6 4 } L 59.032, 61.295, 71.723
{ ca  tyr c6 5 } L 56.444, 58.977, 73.354
{ ca  gln c6 6 } L 53.950, 57.485, 70.842
{ ca  lys c6 7 } L 55.252, 59.739, 68.173
{ ca  his c6 8 } L 55.808, 58.571, 64.616
{ ca  ile c6 9 } L 59.388, 59.163, 63.322
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{ ca  ile c6 12 } L 64.537, 64.372, 60.080
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{ ca  tyr c6 185 } L 82.905, 70.719, 51.970
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{ ca  met c6 201 } L 68.967, 76.189, 53.284
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{ ca  ala c6 208 } L 79.741, 77.968, 55.510
{ ca  trp c6 209 } L 80.335, 75.409, 52.709
{ ca  ser c6 210 } L 82.824, 75.146, 49.895
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{ ca  glu c6 216 } L 93.302, 66.033, 48.888
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{ ca  met c6 219 } L 92.179, 66.363, 54.097
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{ ca  val c6 309 } L 64.562, 56.003, 83.584
{ ca  leu c6 310 } L 67.861, 54.665, 82.822
@vectorlist {c6T-240s} nobutton off color= purple master= {240s Loop}
{ ca  leu c6 225 } P 84.642, 62.392, 55.791
{ ca  tyr c6 226 } L 81.194, 61.043, 54.694
{ ca  met c6 227 } L 81.637, 58.948, 51.566
{ ca  thr c6 228 } L 78.596, 57.965, 49.542
{ ca  arg c6 229 } L 78.339, 55.510, 46.610
{ ca  val c6 230 } L 78.731, 56.707, 43.036
{ ca  gln c6 231 } L 75.885, 54.945, 41.403
{ ca  lys c6 232 } L 77.436, 53.887, 38.054
{ ca  glu c6 233 } L 73.950, 53.640, 36.456
{ ca  arg c6 234 } L 73.594, 57.431, 36.782
{ ca  leu c6 235 } L 76.547, 57.846, 34.378
{ ca  asp c6 236 } L 77.761, 56.280, 31.225
{ n    pro c6 237 } L 79.041, 54.110, 31.319 
{ ca  pro c6 237 } L 80.267, 53.342, 31.468
{ ca  ser c6 238 } L 82.623, 55.794, 29.777
{ ca  glu c6 239 } L 81.592, 58.786, 31.945
{ ca  tyr c6 240 } L 82.151, 56.994, 35.223
{ ca  ala c6 241 } L 85.602, 55.783, 34.203
{ ca  asn c6 242 } L 86.933, 58.985, 32.762
{ ca  val c6 243 } L 86.483, 61.148, 35.789
{ ca  lys c6 244 } L 90.211, 61.858, 34.715
{ ca  ala c6 245 } L 91.523, 60.197, 38.005
@balllist {c6T-240s scN} nobutton off color= blue radius= 0.2 master= {240s SideCh.}
{ nz  lys c6 164 } 71.137, 66.503, 38.263
{ ne  arg c6 229 } 77.385, 51.969, 44.101
{ nh1 arg c6 229 } 76.450, 51.868, 41.991
{ nh2 arg c6 229 } 75.074, 51.614, 43.819
{ n   pro c6 237 } 79.041, 54.110, 31.319
@balllist {c6T-240s scO} nobutton off color= red radius= 0.2 master= {240s SideCh.}
{ oh  tyr c6 165 } 69.451, 62.559, 38.210
{ oe1 glu c6 233 } 72.504, 52.216, 40.169
{ oe2 glu c6 233 } 74.540, 51.615, 39.711
{ og  ser c6 238 } 81.979, 55.040, 27.537
{ oe1 glu c6 239 } 78.732, 62.242, 33.820
{ oe2 glu c6 239 } 77.725, 60.663, 32.710
{ oh  tyr c6 240 } 81.573, 53.254, 40.523
{ od1 asp c6 271 } 83.519, 53.062, 43.096
{ od2 asp c6 271 } 82.200, 51.349, 42.866
@vectorlist {c6T-240s sc} nobutton off color= orange master= {240s SideCh.}
{ ca  lys c6 164 } P 72.769, 64.943, 43.851 { cb  lys c6 164 } L 72.896, 64.853, 42.361
{ cg  lys c6 164 } L 71.662, 65.185, 41.569
{ cd  lys c6 164 } L 72.124, 65.250, 40.133
{ ce  lys c6 164 } L 70.894, 65.508, 39.294
{ nz  lys c6 164 } L 71.137, 66.503, 38.263
{ ca  tyr c6 165 } P 71.031, 61.751, 44.477 { cb  tyr c6 165 } L 71.075, 60.729, 43.360
{ cg  tyr c6 165 } L 70.679, 61.326, 42.000
{ cd1 tyr c6 165 } L 69.426, 61.867, 41.811
{ ce1 tyr c6 165 } L 69.023, 62.265, 40.544
{ cz  tyr c6 165 } L 69.879, 62.139, 39.464
{ oh  tyr c6 165 } L 69.451, 62.559, 38.210
{ cg  tyr c6 165 } P 70.679, 61.326, 42.000 { cd2 tyr c6 165 } L 71.541, 61.237, 40.916
{ ce2 tyr c6 165 } L 71.146, 61.619, 39.644
{ cz  tyr c6 165 } L 69.879, 62.139, 39.464
{ ca  arg c6 229 } P 78.339, 55.510, 46.610 { cb  arg c6 229 } L 77.512, 54.217, 46.658
{ cg  arg c6 229 } L 78.251, 52.960, 46.165
{ cd  arg c6 229 } L 77.332, 51.911, 45.562
{ ne  arg c6 229 } L 77.385, 51.969, 44.101
{ cz  arg c6 229 } L 76.302, 51.815, 43.316
{ nh1 arg c6 229 } L 76.450, 51.868, 41.991
{ cz  arg c6 229 } P 76.302, 51.815, 43.316 { nh2 arg c6 229 } L 75.074, 51.614, 43.819
{ ca  glu c6 233 } P 73.950, 53.640, 36.456 { cb  glu c6 233 } L 72.762, 52.894, 37.068
{ cg  glu c6 233 } L 72.995, 51.613, 37.901
{ cd  glu c6 233 } L 73.373, 51.833, 39.371
{ oe1 glu c6 233 } L 72.504, 52.216, 40.169
{ cd  glu c6 233 } P 73.373, 51.833, 39.371 { oe2 glu c6 233 } L 74.540, 51.615, 39.711
{ ca  pro c6 237 } P 80.267, 53.342, 31.468 { cb  pro c6 237 } L 80.000, 52.155, 30.594
{ cg  pro c6 237 } L 78.561, 51.861, 30.922
{ cd  pro c6 237 } L 77.962, 53.249, 30.850
{ n    pro c6 237 } L 79.041, 54.110, 31.319 
{ ca  pro c6 237 } L 80.267, 53.342, 31.468 
{ ca  ser c6 238 } P 82.623, 55.794, 29.777 { cb  ser c6 238 } L 82.463, 56.154, 28.295
{ og  ser c6 238 } L 81.979, 55.040, 27.537
{ ca  glu c6 239 } P 81.592, 58.786, 31.945 { cb  glu c6 239 } L 80.161, 59.323, 32.058
{ cg  glu c6 239 } L 80.108, 60.753, 32.616
{ cd  glu c6 239 } L 78.747, 61.254, 33.078
{ oe1 glu c6 239 } L 78.732, 62.242, 33.820
{ cd  glu c6 239 } P 78.747, 61.254, 33.078 { oe2 glu c6 239 } L 77.725, 60.663, 32.710
{ ca  tyr c6 240 } P 82.151, 56.994, 35.223 { cb  tyr c6 240 } L 81.505, 55.641, 35.432
{ cg  tyr c6 240 } L 81.611, 55.093, 36.840
{ cd1 tyr c6 240 } L 82.600, 54.186, 37.171
{ ce1 tyr c6 240 } L 82.640, 53.610, 38.426
{ cz  tyr c6 240 } L 81.659, 53.934, 39.329
{ oh  tyr c6 240 } L 81.573, 53.254, 40.523
{ cg  tyr c6 240 } P 81.611, 55.093, 36.840 { cd2 tyr c6 240 } L 80.682, 55.472, 37.784
{ ce2 tyr c6 240 } L 80.710, 54.892, 39.035
{ cz  tyr c6 240 } L 81.659, 53.934, 39.329
{ ca  ala c6 241 } P 85.602, 55.783, 34.203 { cb  ala c6 241 } L 85.797, 54.917, 32.975
{ ca  asp c6 271 } P 84.831, 50.509, 44.567 { cb  asp c6 271 } L 84.565, 50.893, 43.124
{ cg  asp c6 271 } L 83.338, 51.836, 43.015
{ od1 asp c6 271 } L 83.519, 53.062, 43.096
{ cg  asp c6 271 } P 83.338, 51.836, 43.015 { od2 asp c6 271 } L 82.200, 51.349, 42.866
@vectorlist {c6T-240s Hb} nobutton off color= white master= {240s SideCh.}
{ nz  lys c3 164 } P U 76.450, 62.104, 31.761 
{ oe2 glu c6 239 } L U 77.309, 61.133, 32.400 
{ oh  tyr c3 165 } P U 75.332, 60.320, 32.263 
{ oe2 glu c6 239 } L U 77.044, 60.565, 32.583 
{ oh  tyr c6 165 } P U 68.918, 63.010, 38.162 
{ oe1 glu c3 239 } L U 67.837, 63.925, 38.064 
{ od2 asp c6 271 } P U 82.058, 51.781, 42.334 
{ oh  tyr c6 240 } L U 81.715, 52.822, 41.055 
{ od1 asp c6 271 } P U 83.097, 53.104, 42.539 
{ oh  tyr c6 240 } L U 81.995, 53.212, 41.080 
{ oe2 glu c6 233 } P U 74.988, 51.674, 40.246 
{ nh1 arg c6 229 } L U 76.002, 51.809, 41.456 
@vectorlist {r6T} nobutton color= gold master= {Reg. Dimer}
{ ca  gly r6 8 } P 25.078, 92.609, 33.388 { ca  gly r6 8 } L 25.078, 92.609, 33.388
{ ca  val r6 9 } L 24.517, 90.142, 36.296
{ ca  glu r6 10 } L 23.829, 92.172, 39.556
{ ca  ala r6 11 } L 21.170, 91.767, 42.392
{ ca  ile r6 12 } L 20.230, 89.219, 45.108
{ ca  lys r6 13 } L 19.066, 89.676, 48.647
{ ca  arg r6 14 } L 21.688, 87.816, 50.686
{ ca  gly r6 15 } L 24.870, 85.796, 49.997
{ ca  thr r6 16 } L 28.294, 86.100, 48.369
{ ca  val r6 17 } L 29.091, 87.678, 45.022
{ ca  ile r6 18 } L 32.536, 86.786, 43.747
{ ca  asp r6 19 } L 33.466, 89.527, 41.372
{ ca  his r6 20 } L 36.424, 90.286, 39.050
{ ca  ile r6 21 } L 37.419, 86.653, 38.366
{ ca  pro r6 22 } L 39.899, 87.170, 35.448
{ ca  ala r6 23 } L 38.030, 85.328, 32.527
{ ca  gln r6 24 } L 38.110, 81.547, 31.956
{ ca  ile r6 25 } L 39.043, 81.126, 35.717
{ ca  gly r6 26 } L 35.356, 81.538, 36.589
{ ca  phe r6 27 } L 34.686, 78.112, 35.167
{ ca  lys r6 28 } L 37.780, 76.518, 36.810
{ ca  leu r6 29 } L 36.611, 77.816, 40.201
{ ca  leu r6 30 } L 33.186, 76.152, 39.997
{ ca  ser r6 31 } L 34.739, 72.822, 39.271
{ ca  leu r6 32 } L 37.743, 72.999, 41.634
{ ca  phe r6 33 } L 35.752, 74.302, 44.556
{ ca  lys r6 34 } L 32.571, 72.473, 43.732
{ ca  leu r6 35 } L 30.328, 75.570, 44.136
{ ca  thr r6 36 } L 27.571, 73.923, 41.958
{ ca  glu r6 37 } L 26.744, 71.170, 44.471
{ ca  thr r6 38 } L 24.219, 73.349, 46.204
{ ca  asp r6 39 } L 20.561, 73.620, 45.326
{ ca  gln r6 40 } L 20.629, 77.348, 45.678
{ ca  arg r6 41 } L 20.292, 80.267, 43.209
{ ca  ile r6 42 } L 23.625, 80.566, 41.311
{ ca  thr r6 43 } L 24.106, 83.119, 38.657
{ ca  ile r6 44 } L 27.236, 82.799, 36.673
{ ca  gly r6 45 } L 28.223, 85.305, 34.060
{ ca  leu r6 46 } L 31.169, 84.287, 31.879
{ ca  asn r6 47 } L 33.061, 86.821, 29.753
{ ca  leu r6 48 } L 31.130, 89.698, 31.064
{ ca  pro r6 49 } L 32.850, 92.642, 29.345
{ ca  ser r6 50 } L 33.298, 95.417, 31.879
{ ca  gly r6 51 } L 35.678, 97.873, 30.167
{ ca  glu r6 52 } L 36.835, 98.092, 33.821
{ ca  met r6 53 } L 38.954, 94.929, 33.278
{ ca  gly r6 54 } L 38.386, 94.028, 29.603
{ ca  arg r6 55 } L 36.603, 90.675, 30.178
{ ca  lys r6 56 } L 35.718, 88.910, 33.477
{ ca  asp r6 57 } L 33.566, 86.283, 35.194
{ ca  leu r6 58 } L 31.224, 86.581, 38.186
{ ca  ile r6 59 } L 29.712, 83.900, 40.503
{ ca  lys r6 60 } L 26.755, 84.830, 42.614
{ ca  ile r6 61 } L 25.773, 82.139, 45.111
{ ca  glu r6 62 } L 22.633, 83.108, 47.103
{ ca  asn r6 63 } L 22.107, 82.759, 50.907
{ ca  thr r6 64 } L 25.613, 81.346, 51.122
{ ca  phe r6 65 } L 28.696, 82.993, 52.699
{ ca  leu r6 66 } L 32.190, 81.748, 52.029
{ ca  ser r6 67 } L 34.478, 82.206, 54.937
{ ca  glu r6 68 } L 38.062, 83.213, 55.552
{ ca  asp r6 69 } L 39.829, 80.012, 54.492
{ ca  gln r6 70 } L 37.488, 79.470, 51.541
{ ca  val r6 71 } L 38.208, 83.024, 50.345
{ ca  asp r6 72 } L 41.989, 82.496, 50.591
{ ca  gln r6 73 } L 42.163, 79.377, 48.328
{ ca  leu r6 74 } L 40.979, 81.485, 45.423
{ ca  ala r6 75 } L 44.244, 83.356, 45.689
{ ca  leu r6 76 } L 46.174, 80.943, 43.541
{ ca  tyr r6 77 } L 43.646, 81.144, 40.721
{ ca  ala r6 78 } L 41.727, 84.481, 40.844
{ ca  pro r6 79 } L 44.192, 86.405, 43.109
{ ca  gln r6 80 } L 42.359, 89.695, 42.732
{ ca  ala r6 81 } L 38.704, 88.512, 43.153
{ ca  thr r6 82 } L 36.676, 90.931, 45.196
{ ca  val r6 83 } L 34.529, 88.643, 47.351
{ ca  asn r6 84 } L 31.327, 90.429, 48.504
{ ca  arg r6 85 } L 29.009, 89.686, 51.498
{ ca  ile r6 86 } L 25.593, 90.929, 50.208
{ ca  asp r6 87 } L 23.280, 90.777, 53.266
{ ca  asn r6 88 } L 20.059, 92.703, 52.829
{ ca  tyr r6 89 } L 20.003, 93.671, 49.193
{ ca  glu r6 90 } L 23.518, 95.305, 49.306
{ ca  val r6 91 } L 27.238, 95.004, 50.221
{ ca  val r6 92 } L 27.816, 94.322, 53.902
{ ca  gly r6 93 } L 31.603, 93.909, 53.452
{ ca  lys r6 94 } L 34.209, 93.058, 50.853
{ ca  ser r6 95 } L 37.385, 90.894, 50.935
{ ca  arg r6 96 } L 40.181, 89.981, 48.507
{ ca  pro r6 97 } L 42.292, 86.710, 48.390
{ ca  ser r6 98 } L 45.082, 86.395, 50.932
{ ca  leu r6 99 } L 47.569, 83.536, 50.200
{ ca  pro r6 100 } L 46.671, 80.638, 52.685
{ ca  glu r6 101 } L 49.516, 78.715, 54.446
{ ca  arg r6 102 } L 48.389, 75.397, 52.931
{ ca  ile r6 103 } L 46.286, 74.471, 49.823
{ ca  asp r6 104 } L 44.430, 71.161, 50.125
{ ca  asn r6 105 } L 42.522, 68.837, 47.946
{ ca  val r6 106 } L 42.586, 70.872, 44.760
{ ca  leu r6 107 } L 46.242, 70.402, 43.615
{ ca  val r6 108 } L 47.921, 67.289, 42.246
{ ca  cys r6 109 } L 51.473, 66.195, 43.097
{ ca  pro r6 110 } L 54.012, 66.548, 40.122
{ ca  asn r6 111 } L 56.064, 63.874, 41.830
{ ca  ser r6 112 } L 54.953, 60.899, 39.835
{ ca  asn r6 113 } L 56.266, 58.478, 42.473
{ ca  cys r6 114 } L 54.713, 60.489, 45.240
{ ca  ile r6 115 } L 52.384, 58.086, 46.849
{ ca  ser r6 116 } L 49.584, 60.633, 46.913
{ ca  his r6 117 } L 48.717, 59.310, 43.434
{ ca  ala r6 118 } L 47.315, 55.804, 44.053
{ ca  glu r6 119 } L 45.973, 56.192, 47.562
{ ca  pro r6 120 } L 42.860, 57.402, 49.325
{ ca  val r6 121 } L 44.278, 60.712, 50.423
{ ca  ser r6 122 } L 43.655, 64.354, 49.672
{ ca  ser r6 123 } L 46.669, 66.347, 48.685
{ ca  ser r6 124 } L 48.125, 68.917, 50.992
{ ca  phe r6 125 } L 50.664, 71.462, 49.796
{ ca  ala r6 126 } L 52.326, 74.208, 51.909
{ ca  val r6 127 } L 52.692, 77.600, 50.303
{ ca  arg r6 128 } L 55.847, 79.645, 50.503
{ ca  lys r6 129 } L 56.287, 82.732, 48.324
{ ca  arg r6 130 } L 59.791, 82.121, 47.155
{ ca  ala r6 131 } L 60.753, 85.606, 46.196
{ ca  asn r6 132 } L 59.731, 85.562, 42.531
{ ca  asp r6 133 } L 56.857, 83.048, 42.835
{ ca  ile r6 134 } L 55.288, 80.579, 45.185
{ ca  ala r6 135 } L 56.819, 77.210, 45.970
{ ca  leu r6 136 } L 54.527, 74.374, 47.271
{ ca  lys r6 137 } L 55.991, 71.511, 49.374
{ ca  cys r6 138 } L 53.914, 68.286, 49.272
{ ca  lys r6 139 } L 52.748, 66.959, 52.611
{ ca  tyr r6 140 } L 53.800, 63.458, 51.724
{ ca  cys r6 141 } L 56.798, 63.305, 49.401
{ ca  glu r6 142 } L 58.018, 66.580, 50.809
{ ca  lys r6 143 } L 59.236, 67.576, 47.310
{ ca  glu r6 144 } L 59.059, 71.377, 46.799
{ ca  phe r6 145 } L 57.716, 72.659, 43.447
{ ca  ser r6 146 } L 57.272, 75.872, 41.468
{ ca  his r6 147 } L 53.576, 76.534, 41.555
{ ca  asn r6 148 } L 53.726, 76.889, 37.737
{ ca  val r6 149 } L 54.903, 73.223, 37.553
{ ca  val r6 150 } L 52.130, 72.337, 39.995
{ ca  leu r6 151 } L 49.240, 74.106, 38.150
{ ca  ala r6 152 } L 49.946, 72.266, 34.873
{ ca  asn r6 153 } L 49.597, 68.855, 36.759
@subgroup {Tetramer-T} nobutton off master= {Tetramer}
@vectorlist {tet-c1T} instance= {c1T} nobutton color= red
@vectorlist {tet-c1T-240s} master= {240s Loop} instance= {c1T-240s} nobutton off color= magenta
@vectorlist {tet-c6T} instance= {c6T} nobutton color= cyan
@vectorlist {tet-c6T-240s} master= {240s Loop} instance= {c6T-240s} nobutton off color= purple
@balllist {tc6T-240scN} master= {240s SideCh.} instance= {c6T-240s scN} nobutton off color= blue
@balllist {tc6T-240scO} master= {240s SideCh.} instance= {c6T-240s scO} nobutton off color= red radius= 0.2 radius= 0.2
@vectorlist {t c6T-240 sc} master= {240s SideCh.} instance= {c6T-240s sc} nobutton off color= orange
@vectorlist {tc6T-240s Hb} master= {240s SideCh.} instance= {c6T-240s Hb} nobutton off color= white 
@vectorlist {tet-r1T}instance= {r1T} nobutton color= green 
@vectorlist {tet-r6T} instance= {r6T} nobutton color= gold 
@vectorlist {c2T} nobutton color= red
{ ca  ala c2 1 } P 62.791, 9.078, -8.871 { ca  ala c2 1 } L 62.791, 9.078, -8.871
{ ca  asn c2 2 } L 66.030, 9.640, -6.903
{ ca  pro c2 3 } L 66.507, 7.090, -4.057
{ ca  leu c2 4 } L 65.698, 9.662, -1.367
{ ca  tyr c2 5 } L 62.805, 11.419, -3.175
{ ca  gln c2 6 } L 59.999, 11.961, -0.580
{ ca  lys c2 7 } L 61.868, 10.042, 2.116
{ ca  his c2 8 } L 61.953, 11.155, 5.737
{ ca  ile c2 9 } L 65.507, 11.901, 7.024
{ ca  ile c2 10 } L 65.332, 10.914, 10.644
{ ca  ser c2 11 } L 68.373, 9.022, 11.799
{ ca  ile c2 12 } L 71.841, 8.285, 10.412
{ ca  asn c2 13 } L 71.641, 4.565, 10.918
{ ca  asp c2 14 } L 68.596, 4.601, 8.544
{ ca  leu c2 15 } L 70.786, 5.692, 5.598
{ ca  ser c2 16 } L 73.003, 3.263, 3.743
{ ca  arg c2 17 } L 76.451, 3.927, 2.445
{ ca  asp c2 18 } L 75.022, 4.554, -0.986
{ ca  asp c2 19 } L 72.558, 7.118, 0.505
{ ca  leu c2 20 } L 75.316, 9.015, 2.344
{ ca  asn c2 21 } L 77.167, 9.135, -0.944
{ ca  leu c2 22 } L 74.304, 10.279, -3.038
{ ca  val c2 23 } L 73.792, 13.094, -0.543
{ ca  leu c2 24 } L 77.494, 13.921, -0.432
{ ca  ala c2 25 } L 77.807, 13.919, -4.241
{ ca  thr c2 26 } L 74.813, 16.274, -4.768
{ ca  ala c2 27 } L 76.197, 18.638, -2.164
{ ca  ala c2 28 } L 79.410, 19.003, -4.137
{ ca  lys c2 29 } L 77.431, 19.738, -7.328
{ ca  leu c2 30 } L 75.212, 22.443, -5.677
{ ca  lys c2 31 } L 78.358, 23.969, -4.336
{ ca  ala c2 32 } L 80.017, 24.437, -7.778
{ ca  asn c2 33 } L 77.083, 25.279, -10.082
{ ca  pro c2 34 } L 74.184, 26.303, -7.866
{ ca  gln c2 35 } L 70.515, 26.256, -8.874
{ ca  pro c2 36 } L 68.953, 28.977, -6.716
{ ca  glu c2 37 } L 65.486, 28.684, -8.239
{ ca  leu c2 38 } L 65.121, 24.847, -7.767
{ ca  leu c2 39 } L 62.532, 24.921, -4.983
{ ca  lys c2 40 } L 60.797, 27.975, -6.362
{ ca  his c2 41 } L 57.217, 27.833, -4.951
{ ca  lys c2 42 } L 57.749, 25.282, -2.176
{ ca  val c2 43 } L 57.155, 26.424, 1.487
{ ca  ile c2 44 } L 59.214, 24.659, 4.071
{ ca  ala c2 45 } L 58.363, 25.068, 7.783
{ ca  ser c2 46 } L 61.266, 25.656, 10.243
{ ca  cys c2 47 } L 59.871, 24.374, 13.533
{ ca  phe c2 48 } L 62.357, 24.697, 16.321
{ ca  phe c2 49 } L 60.548, 23.616, 19.425
{ ca  glu c2 50 } L 64.033, 23.717, 21.001
{ ca  ala c2 51 } L 65.910, 26.809, 19.752
{ ca  ser c2 52 } L 69.384, 26.735, 18.124
{ ca  thr c2 53 } L 70.359, 29.778, 16.180
{ ca  arg c2 54 } L 73.219, 28.384, 14.105
{ ca  thr c2 55 } L 71.196, 25.360, 12.936
{ ca  arg c2 56 } L 68.130, 27.398, 12.392
{ ca  leu c2 57 } L 70.098, 29.979, 10.403
{ ca  ser c2 58 } L 71.997, 27.279, 8.433
{ ca  phe c2 59 } L 68.828, 25.413, 7.320
{ ca  gln c2 60 } L 66.932, 28.594, 6.503
{ ca  thr c2 61 } L 69.861, 29.898, 4.397
{ ca  ser c2 62 } L 69.814, 26.537, 2.560
{ ca  met c2 63 } L 66.023, 26.864, 1.976
{ ca  his c2 64 } L 66.615, 30.358, 0.639
{ ca  arg c2 65 } L 69.592, 29.447, -1.592
{ ca  leu c2 66 } L 67.232, 27.158, -3.556
{ ca  gly c2 67 } L 64.503, 29.737, -3.851
{ ca  ala c2 68 } L 62.101, 28.347, -1.244
{ ca  ser c2 69 } L 59.869, 30.144, 1.325
{ ca  val c2 70 } L 60.057, 29.425, 4.949
{ ca  val c2 71 } L 57.279, 29.637, 7.584
{ ca  gly c2 72 } L 58.486, 28.581, 11.170
{ ca  phe c2 73 } L 59.269, 29.364, 14.847
{ ca  ser c2 74 } L 61.504, 28.633, 17.920
{ ca  asp c2 75 } L 60.965, 28.963, 21.752
{ ca  ser c2 76 } L 62.643, 26.990, 24.563
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{ ca  arg r2 130 } L 67.461, -15.335, 22.504
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{ ca  asn r2 132 } L 70.220, -15.187, 27.879
{ ca  asp r2 133 } L 69.403, -11.490, 27.584
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{ ca  lys r2 137 } L 65.107, -1.222, 21.506
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{ ca  tyr r2 140 } L 61.084, 6.331, 18.885
{ ca  cys r2 141 } L 64.078, 7.311, 21.020
{ ca  glu r2 142 } L 66.093, 4.411, 19.456
{ ca  lys r2 143 } L 67.456, 3.483, 22.951
{ ca  glu r2 144 } L 68.324, -0.199, 23.715
{ ca  phe r2 145 } L 67.297, -1.576, 27.179
{ ca  ser r2 146 } L 67.623, -4.848, 28.935
{ ca  his r2 147 } L 64.250, -6.522, 29.019
{ ca  asn r2 148 } L 64.894, -6.651, 32.777
{ ca  val r2 149 } L 64.340, -2.902, 33.079
{ ca  val r2 150 } L 61.519, -2.464, 30.547
{ ca  leu r2 151 } L 59.561, -5.312, 32.018
{ ca  ala r2 152 } L 59.556, -3.612, 35.407
{ ca  asn r2 153 } L 58.206, -0.015, 34.541
@vectorlist {r4T} nobutton color=  gold
{ ca  gly r4 8 } P 29.392, -24.587, 33.388 { ca  gly r4 8 } L 29.392, -24.587, 33.388
{ ca  val r4 9 } L 31.809, -23.839, 36.296
{ ca  glu r4 10 } L 30.395, -25.450, 39.556
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{ ca  arg r4 14 } L 35.237, -25.126, 50.686
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{ ca  val r4 17 } L 31.655, -18.646, 45.022
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{ ca  asn r4 47 } L 30.413, -14.780, 29.753
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{ ca  ser r4 50 } L 22.850, -18.872, 31.879
{ ca  gly r4 51 } L 19.533, -18.039, 30.167
{ ca  glu r4 52 } L 18.765, -17.147, 33.821
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{ ca  gly r4 54 } L 21.509, -13.772, 29.603
{ ca  arg r4 55 } L 25.304, -13.639, 30.178
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{ ca  ile r4 61 } L 38.111, -18.750, 45.111
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{ ca  phe r4 65 } L 35.910, -16.646, 52.699
{ ca  leu r4 66 } L 35.241, -12.997, 52.029
{ ca  ser r4 67 } L 33.701, -11.245, 54.937
{ ca  glu r4 68 } L 31.037, -8.645, 55.552
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{ ca  val r4 71 } L 31.127, -8.424, 50.345
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{ ca  ala r4 75 } L 27.822, -3.363, 45.689
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{ ca  gln r4 80 } L 23.275, -8.165, 42.732
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{ ca  thr r4 82 } L 25.046, -13.704, 45.196
{ ca  val r4 83 } L 28.101, -14.419, 47.351
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{ ca  arg r4 85 } L 29.957, -19.721, 51.498
{ ca  ile r4 86 } L 30.589, -23.301, 50.208
{ ca  asp r4 87 } L 31.877, -25.228, 53.266
{ ca  asn r4 88 } L 31.820, -28.980, 52.829
{ ca  tyr r4 89 } L 31.009, -29.513, 49.193
{ ca  glu r4 90 } L 27.837, -27.286, 49.306
{ ca  val r4 91 } L 26.238, -23.914, 50.221
{ ca  val r4 92 } L 26.539, -23.072, 53.902
{ ca  gly r4 93 } L 25.003, -19.586, 53.452
{ ca  lys r4 94 } L 24.437, -16.904, 50.853
{ ca  ser r4 95 } L 24.723, -13.072, 50.935
{ ca  arg r4 96 } L 24.116, -10.194, 48.507
{ ca  pro r4 97 } L 25.893, -6.730, 48.390
{ ca  ser r4 98 } L 24.771, -4.156, 50.932
{ ca  leu r4 99 } L 26.003, -0.573, 50.200
{ ca  pro r4 100 } L 28.962, 0.098, 52.685
{ ca  glu r4 101 } L 29.205, 3.523, 54.446
{ ca  arg r4 102 } L 32.642, 4.206, 52.931
{ ca  ile r4 103 } L 34.495, 2.848, 49.823
{ ca  asp r4 104 } L 38.290, 2.896, 50.125
{ ca  asn r4 105 } L 41.256, 2.406, 47.946
{ ca  val r4 106 } L 39.462, 1.443, 44.760
{ ca  leu r4 107 } L 38.041, 4.845, 43.615
{ ca  val r4 108 } L 39.897, 7.855, 42.246
{ ca  cys r4 109 } L 39.069, 11.478, 43.097
{ ca  pro r4 110 } L 37.493, 13.500, 40.122
{ ca  asn r4 111 } L 38.783, 16.614, 41.830
{ ca  ser r4 112 } L 41.915, 17.140, 39.835
{ ca  asn r4 113 } L 43.355, 19.487, 42.473
{ ca  cys r4 114 } L 42.390, 17.137, 45.240
{ ca  ile r4 115 } L 45.636, 16.322, 46.849
{ ca  ser r4 116 } L 44.830, 12.623, 46.913
{ ca  his r4 117 } L 46.409, 12.534, 43.434
{ ca  ala r4 118 } L 50.146, 13.073, 44.053
{ ca  glu r4 119 } L 50.481, 11.717, 47.562
{ ca  pro r4 120 } L 50.990, 8.416, 49.325
{ ca  val r4 121 } L 47.414, 7.989, 50.423
{ ca  ser r4 122 } L 44.572, 5.628, 49.672
{ ca  ser r4 123 } L 41.339, 7.242, 48.685
{ ca  ser r4 124 } L 38.385, 7.218, 50.992
{ ca  phe r4 125 } L 34.912, 8.144, 49.796
{ ca  ala r4 126 } L 31.703, 8.210, 51.909
{ ca  val r4 127 } L 28.582, 6.831, 50.303
{ ca  arg r4 128 } L 25.234, 8.541, 50.503
{ ca  lys r4 129 } L 22.341, 7.379, 48.324
{ ca  arg r4 130 } L 21.118, 10.719, 47.155
{ ca  ala r4 131 } L 17.619, 9.809, 46.196
{ ca  asn r4 132 } L 18.168, 8.946, 42.531
{ ca  asp r4 133 } L 21.782, 7.714, 42.835
{ ca  ile r4 134 } L 24.705, 7.590, 45.185
{ ca  ala r4 135 } L 26.857, 10.600, 45.970
{ ca  leu r4 136 } L 30.459, 10.033, 47.271
{ ca  lys r4 137 } L 32.206, 12.733, 49.374
{ ca  cys r4 138 } L 36.037, 12.547, 49.272
{ ca  lys r4 139 } L 37.770, 12.200, 52.611
{ ca  tyr r4 140 } L 40.275, 14.862, 51.724
{ ca  cys r4 141 } L 38.909, 17.535, 49.401
{ ca  glu r4 142 } L 35.463, 16.954, 50.809
{ ca  lys r4 143 } L 33.991, 17.510, 47.310
{ ca  glu r4 144 } L 30.788, 15.457, 46.799
{ ca  phe r4 145 } L 30.349, 13.653, 43.447
{ ca  ser r4 146 } L 27.789, 11.662, 41.468
{ ca  his r4 147 } L 29.064, 8.130, 41.555
{ ca  asn r4 148 } L 28.681, 8.082, 37.737
{ ca  val r4 149 } L 31.267, 10.934, 37.553
{ ca  val r4 150 } L 33.421, 8.976, 39.995
{ ca  leu r4 151 } L 33.334, 5.589, 38.150
{ ca  ala r4 152 } L 34.575, 7.120, 34.873
{ ca  asn r4 153 } L 37.703, 8.523, 36.759
@subgroup {Hexamer-T} nobutton master= {Hexamer}
@vectorlist {hex-c1T} instance= {c1T} nobutton color= red 
@vectorlist {hex-c1T-240s} master= {240s Loop} instance= {c1T-240s} nobutton off color= magenta
@vectorlist {hex-c2T} instance= {c2T} nobutton color= red 
@vectorlist {hex-c2T-240s} master= {240s Loop} instance= {c2T-240s} nobutton off color= magenta
@vectorlist {hex-c4T} instance= {c4T} nobutton color= cyan 
@vectorlist {hex-c4T-240s} master= {240s Loop} instance= {c4T-240s} nobutton off color= purple
@vectorlist {hex-c6T} instance= {c6T} nobutton color= cyan 
@vectorlist {hex-c6T-240s} master= {240s Loop} instance= {c6T-240s} nobutton off color= purple
@vectorlist {hc6T-240 sc} master= {240s SideCh.} instance= {c6T-240s sc} nobutton off color= orange
@vectorlist {hc6T-240s Hb} master= {240s SideCh.} instance= {c6T-240s Hb} nobutton off color= white 
@vectorlist {hex-r1T} instance= {r1T} nobutton color= green 
@vectorlist {hex-r2T} instance= {r2T} nobutton color= green 
@vectorlist {hex-r4T} instance= {r4T} nobutton color= gold 
@balllist {hc6T-240scN} master= {240s SideCh.} instance= {c6T-240s scN} nobutton off color= blue  radius= 0.2
@balllist {hc6T-240scO} master= {240s SideCh.} instance= {c6T-240s scO} nobutton off color= red  radius= 0.2
@vectorlist {hex-r6T} instance= {r6T} nobutton color= gold 
@vectorlist {c3T} nobutton color= red
{ ca  ala c3 1 } P 82.956, 49.839, -8.871 { ca  ala c3 1 } L 82.956, 49.839, -8.871
{ ca  asn c3 2 } L 80.850, 52.364, -6.903
{ ca  pro c3 3 } L 82.820, 54.052, -4.057
{ ca  leu c3 4 } L 80.997, 52.065, -1.367
{ ca  tyr c3 5 } L 80.922, 48.681, -3.175
{ ca  gln c3 6 } L 81.855, 45.980, -0.580
{ ca  lys c3 7 } L 82.583, 48.558, 2.116
{ ca  his c3 8 } L 81.577, 48.076, 5.737
{ ca  ile c3 9 } L 79.154, 50.780, 7.024
{ ca  ile c3 10 } L 80.096, 51.122, 10.644
{ ca  ser c3 11 } L 80.214, 54.702, 11.799
{ ca  ile c3 12 } L 79.118, 58.074, 10.412
{ ca  asn c3 13 } L 82.440, 59.760, 10.918
{ ca  asp c3 14 } L 83.931, 57.105, 8.544
{ ca  leu c3 15 } L 81.891, 58.456, 5.598
{ ca  ser c3 16 } L 82.887, 61.591, 3.743
{ ca  arg c3 17 } L 80.588, 64.245, 2.445
{ ca  asp c3 18 } L 80.759, 62.694, -0.986
{ ca  asp c3 19 } L 79.771, 59.278, 0.505
{ ca  leu c3 20 } L 76.749, 60.718, 2.344
{ ca  asn c3 21 } L 75.719, 62.261, -0.944
{ ca  leu c3 22 } L 76.160, 59.209, -3.038
{ ca  val c3 23 } L 73.978, 57.359, -0.543
{ ca  leu c3 24 } L 71.411, 60.151, -0.432
{ ca  ala c3 25 } L 71.256, 60.424, -4.241
{ ca  thr c3 26 } L 70.713, 56.653, -4.768
{ ca  ala c3 27 } L 67.974, 56.670, -2.164
{ ca  ala c3 28 } L 66.052, 59.270, -4.137
{ ca  lys c3 29 } L 66.405, 57.188, -7.328
{ ca  leu c3 30 } L 65.171, 53.914, -5.677
{ ca  lys c3 31 } L 62.277, 55.876, -4.336
{ ca  ala c3 32 } L 61.042, 57.079, -7.778
{ ca  asn c3 33 } L 61.780, 54.117, -10.082
{ ca  pro c3 34 } L 62.343, 51.094, -7.866
{ ca  gln c3 35 } L 64.218, 47.940, -8.874
{ ca  pro c3 36 } L 62.642, 45.227, -6.716
{ ca  glu c3 37 } L 64.629, 42.371, -8.239
{ ca  leu c3 38 } L 68.135, 43.973, -7.767
{ ca  leu c3 39 } L 69.365, 41.694, -4.983
{ ca  lys c3 40 } L 67.588, 38.664, -6.362
{ ca  his c3 41 } L 69.501, 35.635, -4.951
{ ca  lys c3 42 } L 71.444, 37.371, -2.176
{ ca  val c3 43 } L 70.752, 36.286, 1.487
{ ca  ile c3 44 } L 71.251, 38.951, 4.071
{ ca  ala c3 45 } L 71.322, 38.010, 7.783
{ ca  ser c3 46 } L 69.362, 40.230, 10.243
{ ca  cys c3 47 } L 71.169, 39.663, 13.533
{ ca  phe c3 48 } L 69.647, 41.654, 16.321
{ ca  phe c3 49 } L 71.487, 40.628, 19.425
{ ca  glu c3 50 } L 69.657, 43.596, 21.001
{ ca  ala c3 51 } L 66.041, 43.676, 19.752
{ ca  ser c3 52 } L 64.368, 46.721, 18.124
{ ca  thr c3 53 } L 61.246, 46.044, 16.180
{ ca  arg c3 54 } L 61.023, 49.218, 14.105
{ ca  thr c3 55 } L 64.653, 48.978, 12.936
{ ca  arg c3 56 } L 64.421, 45.304, 12.392
{ ca  leu c3 57 } L 61.202, 45.717, 10.403
{ ca  ser c3 58 } L 62.591, 48.712, 8.433
{ ca  phe c3 59 } L 65.791, 46.901, 7.320
{ ca  gln c3 60 } L 63.984, 43.668, 6.503
{ ca  thr c3 61 } L 61.391, 45.553, 4.397
{ ca  ser c3 62 } L 64.325, 47.192, 2.560
{ ca  met c3 63 } L 65.937, 43.746, 1.976
{ ca  his c3 64 } L 62.615, 42.512, 0.639
{ ca  arg c3 65 } L 61.916, 45.545, -1.592
{ ca  leu c3 66 } L 65.078, 44.646, -3.556
{ ca  gly c3 67 } L 64.209, 40.993, -3.851
{ ca  ala c3 68 } L 66.614, 39.608, -1.244
{ ca  ser c3 69 } L 66.173, 36.776, 1.325
{ ca  val c3 70 } L 66.702, 37.298, 4.949
{ ca  val c3 71 } L 67.907, 34.787, 7.584
{ ca  gly c3 72 } L 68.218, 36.360, 11.170
{ ca  phe c3 73 } L 67.149, 36.647, 14.847
{ ca  ser c3 74 } L 66.664, 38.948, 17.920
{ ca  asp c3 75 } L 66.648, 38.316, 21.752
{ ca  ser c3 76 } L 67.518, 40.755, 24.563
{ ca  ala c3 77 } L 67.649, 37.343, 26.422
{ ca  asn c3 78 } L 69.604, 34.004, 26.002
{ ca  thr c3 79 } L 69.322, 33.017, 22.308
{ ca  ser c3 80 } L 70.984, 29.529, 22.694
{ ca  leu c3 81 } L 74.397, 28.813, 20.926
{ ca  gly c3 82 } L 74.850, 32.530, 20.778
{ ca  lys c3 83 } L 75.231, 32.847, 24.557
{ ca  lys c3 84 } L 76.637, 29.267, 25.136
{ ca  gly c3 85 } L 80.213, 30.431, 25.500
{ ca  glu c3 86 } L 80.281, 32.066, 22.116
{ ca  thr c3 87 } L 82.273, 35.008, 21.450
{ ca  leu c3 88 } L 80.778, 37.365, 18.853
{ ca  ala c3 89 } L 83.977, 36.679, 16.986
{ ca  asp c3 90 } L 83.031, 33.022, 16.502
{ ca  thr c3 91 } L 79.366, 33.789, 15.715
{ ca  ile c3 92 } L 80.572, 36.046, 12.947
{ ca  ser c3 93 } L 83.228, 33.648, 11.737
{ ca  val c3 94 } L 80.449, 31.164, 11.257
{ ca  ile c3 95 } L 77.650, 33.355, 9.695
{ ca  ser c3 96 } L 80.014, 34.974, 7.130
{ ca  thr c3 97 } L 80.359, 31.467, 5.798
{ ca  tyr c3 98 } L 76.569, 31.450, 5.005
{ ca  val c3 99 } L 75.503, 34.961, 4.017
{ ca  asp c3 100 } L 76.206, 37.807, 1.728
{ ca  ala c3 101 } L 75.940, 40.781, 4.093
{ ca  ile c3 102 } L 75.379, 41.051, 7.891
{ ca  val c3 103 } L 73.195, 43.851, 9.423
{ ca  met c3 104 } L 73.625, 43.734, 13.244
{ ca  arg c3 105 } L 72.409, 45.540, 16.341
{ ca  his c3 106 } L 74.203, 44.826, 19.577
{ ca  pro c3 107 } L 74.309, 46.041, 23.253
{ ca  gln c3 108 } L 78.073, 46.672, 23.622
{ ca  glu c3 109 } L 79.890, 49.474, 21.933
{ ca  gly c3 110 } L 82.213, 48.343, 19.172
{ ca  ala c3 111 } L 80.360, 45.118, 18.389
{ ca  ala c3 112 } L 80.070, 45.754, 14.680
{ ca  arg c3 113 } L 83.641, 46.965, 14.330
{ ca  leu c3 114 } L 85.049, 43.710, 15.923
{ ca  ala c3 115 } L 82.709, 41.847, 13.500
{ ca  thr c3 116 } L 84.409, 43.511, 10.554
{ ca  glu c3 117 } L 87.608, 41.598, 11.408
{ ca  phe c3 118 } L 85.957, 38.203, 11.465
{ ca  ser c3 119 } L 83.453, 38.556, 8.496
{ ca  gly c3 120 } L 86.049, 37.825, 5.733
{ ca  asn c3 121 } L 84.866, 39.836, 2.813
{ ca  val c3 122 } L 81.209, 39.885, 3.859
{ ca  pro c3 123 } L 80.202, 43.488, 4.536
{ ca  val c3 124 } L 78.636, 44.168, 7.912
{ ca  leu c3 125 } L 76.360, 47.198, 8.540
{ ca  asn c3 126 } L 75.704, 48.697, 11.911
{ ca  ala c3 127 } L 72.124, 48.879, 13.124
{ ca  gly c3 128 } L 73.330, 50.295, 16.490
{ ca  asp c3 129 } L 76.333, 49.247, 18.585
{ ca  gly c3 130 } L 75.620, 50.282, 22.189
{ ca  ser c3 131 } L 75.984, 54.009, 22.840
{ ca  asn c3 132 } L 78.458, 54.581, 20.017
{ ca  gln c3 133 } L 77.145, 54.577, 16.465
{ ca  his c3 134 } L 74.031, 54.159, 14.523
{ ca  pro c3 135 } L 74.976, 55.310, 10.969
{ ca  thr c3 136 } L 71.688, 54.079, 9.329
{ ca  gln c3 137 } L 69.380, 56.329, 11.286
{ ca  thr c3 138 } L 71.424, 59.415, 10.442
{ ca  leu c3 139 } L 71.367, 58.556, 6.776
{ ca  leu c3 140 } L 67.581, 58.511, 6.802
{ ca  asp c3 141 } L 67.498, 61.699, 9.012
{ ca  leu c3 142 } L 69.726, 63.504, 6.395
{ ca  phe c3 143 } L 67.641, 62.164, 3.512
{ ca  thr c3 144 } L 64.584, 63.535, 5.187
{ ca  ile c3 145 } L 66.272, 66.913, 6.023
{ ca  gln c3 146 } L 67.483, 67.213, 2.434
{ ca  gln c3 147 } L 64.123, 66.201, 0.982
{ ca  thr c3 148 } L 62.118, 68.735, 3.057
{ ca  glu c3 149 } L 64.626, 71.619, 2.819
{ ca  gly c3 150 } L 66.472, 71.188, -0.528
{ ca  arg c3 151 } L 69.964, 71.024, 1.020
{ ca  leu c3 152 } L 72.246, 70.000, 3.861
{ ca  asp c3 153 } L 74.044, 73.393, 3.901
{ ca  asn c3 154 } L 73.052, 76.672, 5.610
{ ca  leu c3 155 } L 70.387, 75.241, 7.767
{ ca  his c3 156 } L 69.416, 76.351, 11.215
{ ca  val c3 157 } L 68.819, 73.037, 12.918
{ ca  ala c3 158 } L 67.604, 72.949, 16.623
{ ca  met c3 159 } L 68.290, 69.707, 18.619
{ ca  val c3 160 } L 66.144, 69.164, 21.718
{ ca  gly c3 161 } L 65.860, 66.946, 24.872
{ ca  asp c3 162 } L 68.520, 64.434, 26.022
{ ca  leu c3 163 } L 71.439, 65.850, 24.133
{ ca  lys c3 164 } L 73.874, 64.100, 26.513
{ ca  tyr c3 165 } L 72.930, 60.495, 25.850
{ ca  gly c3 166 } L 70.946, 60.221, 22.577
{ ca  arg c3 167 } L 73.170, 58.414, 19.952
{ ca  thr c3 168 } L 71.245, 60.125, 17.216
{ ca  val c3 169 } L 71.858, 63.769, 18.185
{ ca  his c3 170 } L 75.597, 63.191, 18.376
{ ca  ser c3 171 } L 75.760, 61.509, 14.948
{ ca  leu c3 172 } L 73.471, 64.097, 13.334
{ ca  thr c3 173 } L 75.708, 66.891, 14.530
{ ca  gln c3 174 } L 78.924, 65.146, 13.187
{ ca  ala c3 175 } L 77.266, 64.508, 9.863
{ ca  leu c3 176 } L 75.790, 68.003, 9.314
{ ca  ala c3 177 } L 79.116, 69.433, 10.474
{ ca  lys c3 178 } L 80.579, 67.988, 7.204
{ ca  phe c3 179 } L 78.410, 70.448, 5.239
{ ca  asp c3 180 } L 78.650, 74.226, 5.246
{ ca  gly c3 181 } L 76.911, 77.161, 6.843
{ ca  asn c3 182 } L 74.886, 75.325, 9.432
{ ca  arg c3 183 } L 73.815, 76.847, 12.674
{ ca  phe c3 184 } L 72.826, 74.701, 15.701
{ ca  tyr c3 185 } L 70.708, 75.573, 18.657
{ ca  phe c3 186 } L 70.959, 73.048, 21.458
{ ca  ile c3 187 } L 67.956, 72.980, 23.871
{ ca  ala c3 188 } L 68.594, 70.621, 26.757
{ ca  pro c3 189 } L 68.146, 70.267, 30.500
{ ca  asp c3 190 } L 71.630, 70.901, 31.865
{ ca  ala c3 191 } L 71.756, 67.467, 33.566
{ ca  leu c3 192 } L 71.471, 66.234, 29.958
{ ca  ala c3 193 } L 73.333, 68.802, 27.909
{ ca  met c3 194 } L 75.427, 68.343, 24.860
{ ca  pro c3 195 } L 78.893, 66.742, 25.544
{ ca  glu c3 196 } L 81.901, 68.975, 25.445
{ ca  tyr c3 197 } L 83.581, 67.098, 22.590
{ ca  ile c3 198 } L 80.689, 67.616, 20.104
{ ca  leu c3 199 } L 80.973, 71.285, 20.847
{ ca  asp c3 200 } L 84.805, 71.202, 20.665
{ ca  met c3 201 } L 84.732, 69.757, 17.169
{ ca  leu c3 202 } L 82.128, 72.309, 16.137
{ ca  asp c3 203 } L 84.519, 75.111, 17.139
{ ca  glu c3 204 } L 87.509, 73.552, 15.320
{ ca  lys c3 205 } L 85.551, 73.893, 12.147
{ ca  gly c3 206 } L 84.326, 77.374, 13.030
{ ca  ile c3 207 } L 80.705, 76.112, 13.079
{ ca  ala c3 208 } L 78.085, 78.278, 14.666
{ ca  trp c3 209 } L 76.058, 76.984, 17.683
{ ca  ser c3 210 } L 74.229, 78.413, 20.688
{ ca  leu c3 211 } L 72.557, 76.985, 23.829
{ ca  his c3 212 } L 68.858, 77.677, 24.667
{ ca  ser c3 213 } L 66.764, 77.074, 27.672
{ ca  ser c3 214 } L 63.544, 76.529, 25.717
{ ca  ile c3 215 } L 62.308, 75.917, 22.232
{ ca  glu c3 216 } L 60.219, 79.214, 22.106
{ ca  glu c3 217 } L 63.518, 81.230, 22.014
{ ca  val c3 218 } L 64.351, 79.758, 18.617
{ ca  met c3 219 } L 60.965, 78.736, 17.268
{ ca  ala c3 220 } L 61.083, 81.355, 14.550
{ ca  glu c3 221 } L 64.666, 80.748, 13.397
{ ca  val c3 222 } L 64.382, 77.093, 12.824
{ ca  asp c3 223 } L 64.330, 74.947, 9.826
{ ca  ile c3 224 } L 64.666, 71.405, 11.344
{ ca  leu c3 225 } L 63.561, 70.859, 15.002
{ ca  tyr c3 226 } L 65.087, 67.470, 16.025
{ ca  met c3 227 } L 63.269, 66.356, 19.114
{ ca  thr c3 228 } L 64.863, 63.599, 21.149
{ ca  arg c3 229 } L 63.058, 61.699, 23.887
{ ca  val c3 230 } L 63.879, 62.905, 27.406
{ ca  gln c3 231 } L 64.372, 59.455, 29.002
{ ca  lys c3 232 } L 62.607, 59.627, 32.367
{ ca  glu c3 233 } L 64.621, 57.229, 34.573
{ ca  arg c3 234 } L 67.921, 59.005, 34.105
{ ca  leu c3 235 } L 66.334, 61.627, 36.311
{ ca  asp c3 236 } L 64.586, 61.519, 39.543
{ n    pro c3 237 } L 62.079, 61.157, 39.320 
{ ca  pro c3 237 } L 60.728, 61.511, 38.890
{ ca  ser c3 238 } L 60.429, 64.757, 40.826
{ ca  glu c3 239 } L 63.468, 66.124, 38.952
{ ca  tyr c3 240 } L 62.129, 65.156, 35.593
{ ca  ala c3 241 } L 58.713, 66.829, 36.124
{ ca  asn c3 242 } L 60.040, 69.983, 37.840
{ ca  val c3 243 } L 61.625, 71.479, 34.734
{ ca  lys c3 244 } L 59.943, 74.896, 34.009
{ ca  ala c3 245 } L 57.100, 74.575, 31.395
{ ca  gln c3 246 } L 59.116, 71.772, 29.784
{ ca  phe c3 247 } L 60.857, 70.982, 26.591
{ ca  val c3 248 } L 57.864, 69.213, 24.899
{ ca  leu c3 249 } L 56.269, 70.469, 21.660
{ ca  arg c3 250 } L 52.665, 71.353, 21.473
{ ca  ala c3 251 } L 50.814, 72.608, 18.377
{ ca  ser c3 252 } L 50.563, 76.180, 19.695
{ ca  asp c3 253 } L 54.340, 76.570, 19.943
{ ca  leu c3 254 } L 54.430, 76.021, 16.209
{ ca  his c3 255 } L 52.502, 79.223, 15.543
{ ca  asn c3 256 } L 55.718, 81.213, 14.948
{ ca  ala c3 257 } L 57.662, 78.400, 13.200
{ ca  lys c3 258 } L 58.673, 78.925, 9.538
{ ca  ala c3 259 } L 56.479, 77.421, 6.776
{ ca  asn c3 260 } L 59.222, 74.923, 5.810
{ ca  met c3 261 } L 60.132, 74.002, 9.389
{ ca  lys c3 262 } L 59.584, 70.294, 10.029
{ ca  val c3 263 } L 59.703, 68.456, 13.333
{ ca  leu c3 264 } L 61.719, 65.288, 13.404
{ ca  his c3 265 } L 62.092, 62.629, 16.048
{ ca  pro c3 266 } L 63.851, 59.165, 15.864
{ ca  leu c3 267 } L 60.832, 57.577, 17.629
{ ca  pro c3 268 } L 59.502, 56.397, 20.169
{ ca  arg c3 269 } L 57.809, 59.588, 21.090
{ ca  val c3 270 } L 55.543, 59.763, 24.129
{ ca  asp c3 271 } L 54.987, 63.069, 26.097
{ ca  glu c3 272 } L 57.716, 64.981, 24.152
{ ca  ile c3 273 } L 55.357, 65.664, 21.178
{ ca  ala c3 274 } L 51.683, 66.079, 21.877
{ ca  thr c3 275 } L 49.033, 64.672, 19.314
{ ca  asp c3 276 } L 47.957, 68.131, 18.075
{ ca  val c3 277 } L 51.363, 68.422, 16.599
{ ca  asp c3 278 } L 50.577, 65.389, 14.378
{ ca  lys c3 279 } L 47.886, 67.375, 12.648
{ ca  thr c3 280 } L 49.946, 70.458, 11.674
{ ca  pro c3 281 } L 51.891, 70.242, 8.375
{ ca  his c3 282 } L 55.227, 70.596, 10.211
{ ca  ala c3 283 } L 54.843, 67.101, 11.655
{ ca  trp c3 284 } L 57.277, 64.952, 9.794
{ ca  tyr c3 285 } L 58.368, 62.055, 12.086
{ ca  phe c3 286 } L 56.329, 59.340, 10.541
{ ca  gln c3 287 } L 57.349, 60.384, 6.953
{ ca  gln c3 288 } L 60.933, 60.401, 8.314
{ ca  ala c3 289 } L 60.432, 56.737, 9.461
{ ca  gly c3 290 } L 59.118, 55.925, 6.001
{ ca  asn c3 291 } L 62.337, 57.306, 4.447
{ ca  gly c3 292 } L 64.029, 54.583, 6.495
{ ca  ile c3 293 } L 63.134, 52.142, 3.721
{ ca  phe c3 294 } L 64.561, 54.237, 0.863
{ ca  ala c3 295 } L 67.718, 55.231, 2.702
{ ca  arg c3 296 } L 68.513, 51.653, 3.758
{ ca  gln c3 297 } L 67.733, 50.351, 0.245
{ ca  ala c3 298 } L 70.379, 52.703, -1.141
{ ca  leu c3 299 } L 72.995, 51.468, 1.303
{ ca  leu c3 300 } L 72.163, 47.801, 0.641
{ ca  ala c3 301 } L 72.060, 48.375, -3.090
{ ca  leu c3 302 } L 75.411, 50.143, -3.024
{ ca  val c3 303 } L 77.424, 47.816, -0.758
{ ca  leu c3 304 } L 76.158, 44.788, -2.637
{ ca  asn c3 305 } L 76.181, 46.085, -6.210
{ ca  arg c3 306 } L 79.064, 46.799, -8.562
{ ca  asp c3 307 } L 77.665, 49.762, -10.538
{ ca  leu c3 308 } L 74.165, 51.039, -9.927
{ ca  val c3 309 } L 72.346, 52.156, -13.055
{ ca  leu c3 310 } L 69.254, 53.992, -11.895
@vectorlist {c3T-240s} nobutton off color= magenta master= {240s Loop}
{ ca  leu c3 225 } P 63.561, 70.859, 15.002
{ ca  tyr c3 226 } L 65.087, 67.470, 16.025
{ ca  met c3 227 } L 63.269, 66.356, 19.114
{ ca  thr c3 228 } L 64.863, 63.599, 21.149
{ ca  arg c3 229 } L 63.058, 61.699, 23.887
{ ca  val c3 230 } L 63.879, 62.905, 27.406
{ ca  gln c3 231 } L 64.372, 59.455, 29.002
{ ca  lys c3 232 } L 62.607, 59.627, 32.367
{ ca  glu c3 233 } L 64.621, 57.229, 34.573
{ ca  arg c3 234 } L 67.921, 59.005, 34.105
{ ca  leu c3 235 } L 66.334, 61.627, 36.311
{ ca  asp c3 236 } L 64.586, 61.519, 39.543
{ n    pro c3 237 } L 62.079, 61.157, 39.320 
{ ca  pro c3 237 } L 60.728, 61.511, 38.890
{ ca  ser c3 238 } L 60.429, 64.757, 40.826
{ ca  glu c3 239 } L 63.468, 66.124, 38.952
{ ca  tyr c3 240 } L 62.129, 65.156, 35.593
{ ca  ala c3 241 } L 58.713, 66.829, 36.124
{ ca  asn c3 242 } L 60.040, 69.983, 37.840
{ ca  val c3 243 } L 61.625, 71.479, 34.734
{ ca  lys c3 244 } L 59.943, 74.896, 34.009
{ ca  ala c3 245 } L 57.100, 74.575, 31.395
@balllist {c3T-240s scN} nobutton off color= blue radius= 0.2 master= {240s SideCh.}
{ nz  lys c3 164 } 76.034, 62.574, 31.451
{ ne  arg c3 229 } 60.985, 58.496, 25.552
{ nh1 arg c3 229 } 60.206, 58.915, 27.697
{ nh2 arg c3 229 } 62.060, 57.564, 27.445
{ n    pro c3 237 } 62.079, 61.157, 39.320 
@balllist {c3T-240s scO} nobutton off color= red radius= 0.2 master= {240s SideCh.}
{ oh  tyr c3 165 } 74.651, 60.222, 32.136
{ oe1 glu c3 233 } 63.624, 55.528, 31.507
{ oe2 glu c3 233 } 65.166, 54.108, 31.027
{ og  ser c3 238 } 60.646, 63.591, 42.965
{ oe1 glu c3 239 } 67.304, 64.376,