@text 
 Nat Struct Biol 1995 Oct;2(10):906-10 
 Localized perturbations in CheY structure monitored by NMR identify a CheA binding interface.
 Swanson RV, Lowry DF, Matsumura P, McEvoy MM, Simon MI, Dahlquist FW
 Division of Biology, California Institute of Technology, Pasadena 91125, USA. 
 Phosphotransfer between the autophosphorylating histidine kinase CheA and the response regulator CheY represents a crucial step in the bacterial chemotaxis signal transduction pathway. The 15N-1H correlation spectrum of CheY complexed with an amino-terminal fragment of CheA exhibits specific localized differences in chemical shifts when compared to the spectrum of uncomplexed CheY. When mapped onto the three-dimensional structure of CheY, these changes define a region distinct from the active site. A single amino-acid substitution within this binding region on CheY, alanine to valine at position 103, significantly decreases the affinity of CheY for CheA. The binding face described by these changes partially overlaps a flagellar switch binding surface previously defined by mutagenesis. 


 J Bacteriol 1992 Oct;174(19):6247-55 
 A chemotactic signaling surface on CheY defined by suppressors of flagellar switch mutations.
 Roman SJ, Meyers M, Volz K, Matsumura P
 Department of Microbiology and Immunology, University of Illinois, Chicago 60680. 
 CheY is the response regulator protein that interacts with the flagellar switch apparatus to modulate flagellar rotation during chemotactic signaling. CheY can be phosphorylated and dephosphorylated in vitro, and evidence indicates that CheY-P is the activated form that induces clockwise flagellar rotation, resulting in a tumble in the cell's swimming pattern. The flagellar switch apparatus is a complex macromolecular structure composed of at least three gene products, FliG, FliM, and FliN. Genetic analysis of Escherichia coli has identified fliG and fliM as genes in which mutations occur that allele specifically suppress cheY mutations, indicating interactions among these gene products. We have generated a class of cheY mutations selected for dominant suppression of fliG mutations. Interestingly, these cheY mutations dominantly suppressed both fliG and fliM mutations; this is consistent with the idea that the CheY protein interacts with both switch gene products during signaling. Biochemical characterization of wild-type and suppressor CheY proteins did not reveal altered phosphorylation properties or evidence for phosphorylation-dependent CheY multimerization. These data indicate that suppressor CheY proteins are specifically altered in the ability to transduce chemotactic
signals to the switch at some point subsequent to phosphorylation. Physical mapping of suppressor amino acid substitutions on the crystal structure of CheY revealed a high degree of spatial clustering, suggesting that this region of CheY is a signaling surface that transduces chemotactic signals to the switch. 

 J Bacteriol 1992 Feb;174(3):793-806 
 Molecular analysis of the flagellar switch protein FliM of Salmonella typhimurium.
 Sockett H, Yamaguchi S, Kihara M, Irikura VM, Macnab RM
 Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06511. 
 Defects in the chemotaxis proteins CheY and CheZ of Salmonella typhimurium can be suppressed by mutations in the flagellar switch, such that swarming of a
pseudorevertant on semisolid plates is significantly better than that of its parent. cheY suppressors contribute to a clockwise switch bias, and cheZ suppressors contribute to a counterclockwise bias. Among the three known switch genes, fliM contributes most examples of such suppressor mutations. We have investigated the changes in FliM that are responsible for suppression, as well as the changes in CheY or CheZ that are being compensated for. Ten independently isolated parental cheY mutations represented nine distinct mutations, one an amino acid duplication and the rest missense mutations. Several of the altered amino acids lie on one face of the three-dimensional structure of CheY (A. M. Stock, J. M. Mottonen, J. B. Stock, and C. E. Schutt, Nature (London) 337:745-749, 1989; K. Volz and P. Matsumura, J. Biol. Chem. 266:15511-15519, 1991); this face may constitute the binding site for the switch. All 10 cheZ mutations were distinct, with several of them resulting in premature termination. cheY and cheZ suppressors in FliM occurred in clusters, which in general did not overlap. A few cheZ suppressors and one cheY suppressor involved changes near the N terminus of FliM, but neither cheY nor cheZ suppressors involved changes near the C terminus. Among the strongest cheY suppressors were changes from Arg to a neutral amino acid or from Val to Glu, suggesting that electrostatic interactions may play an important role in switching. A given cheY or cheZ mutation could be suppressed by many different fliM mutations; conversely, a given fliM mutation was often encountered as a suppressor of more than one cheY or cheZ mutation. The data suggest that an important factor in suppression is a balancing of the shift in switch bias introduced by alteration of CheY or CheZ with an appropriate opposing shift introduced by alteration of FliM. For strains with a severe parental mutation, such as the cheZ null mutations, adjustment of switch bias is essentially the only factor in suppression, since the attractant L-aspartate caused at most a slight further enhancement of the swarming rate over that occurring in the absence of a chemotactic stimulus. We discuss a model for switching in which there are distinct interactions for the counterclockwise and clockwise states, with suppression occurring by impairment of one of the states and hence by relative enhancement of the other state. 

 Proc Natl Acad Sci U S A 1998 Jun 23;95(13):7333-8 
 Two binding modes reveal flexibility in kinase/response regulator interactions in the bacterial chemotaxis pathway.
 McEvoy MM, Hausrath AC, Randolph GB, Remington SJ, Dahlquist FW
 Institute of Molecular Biology, University of Oregon, Eugene, OR 97403, USA. 
 The crystal structure at 2.0-A resolution of the complex of the Escherichia coli chemotaxis response regulator CheY and the phosphoacceptor-binding domain (P2)of the kinase CheA is presented. The binding interface involves the fourth and fifth helices and fifth beta-strand of CheY and both helices of P2. Surprisingly, the two heterodimers in the asymmetric unit have two different binding modes involving the same interface, suggesting some flexibility in the binding regions. Significant conformational changes have occurred in CheY compared with previously determined unbound structures. The active site of CheY is exposed by the binding of the kinase domain, possibly to enhance phosphotransfer from CheA to CheY. The conformational changes upon complex formation as well as the observation that there are two different binding modes suggest that the plasticity of CheY is an essential feature of response regulator function. 

 coordinates from file: D:\PDB\CHEAY_~2.PDB 
@kinemage 1 
@caption 
 Crystal structure of CheY-CheA(158-226) (CheA P2 domain).  Colored side chains indicate important sites in CheY: phosphorylation (red), CheA-binding (yellow), FliG-suppressors (green), FliM-parental (blue)
@view1
@zoom 1.00 
@zslab 200 
@center 45.370 44.967 64.076 
@matrix 
 0.20935 -0.28198  0.93630  0.17679  0.95265  0.24737 -0.96173  0.11374  0.24929
@onewidth 
@group {CheA P2 domain}x
@vectorlist {ca-ca} color= white 
{ ca  ala a 2 } P 32.428, 50.671, 68.341 { ca  ala a 2 } L 32.428, 50.671, 68.341
{ ca  asp a 3 } L 30.737, 50.394, 71.614
{ ca  lys a 4 } L 32.036, 53.167, 73.797
{ ca  glu a 5 } L 30.944, 50.876, 76.588
{ ca  leu a 6 } L 32.665, 47.659, 75.330
{ ca  lys a 7 } L 34.085, 45.891, 78.353
{ ca  phe a 8 } L 37.642, 46.165, 78.246
{ ca  leu a 9 } L 39.496, 43.806, 80.407
{ ca  val a 10 } L 42.630, 45.802, 80.428
{ ca  val a 11 } L 44.801, 42.908, 81.514
{ ca  asp a 12 } L 47.935, 44.326, 82.696
{ ca  asp a 13 } L 49.672, 44.236, 85.847
{ ca  phe a 14 } L 50.568, 48.191, 85.645
{ ca  ser a 15 } L 48.189, 50.866, 87.118
{ ca  thr a 16 } L 49.156, 54.271, 85.533
{ ca  met a 17 } L 49.070, 52.751, 82.047
{ ca  arg a 18 } L 45.907, 51.193, 82.829
{ ca  arg a 19 } L 45.088, 54.940, 83.781
{ ca  ile a 20 } L 46.168, 56.743, 80.678
{ ca  val a 21 } L 44.797, 53.930, 78.539
{ ca  arg a 22 } L 41.846, 54.812, 80.520
{ ca  asn a 23 } L 42.191, 58.625, 79.966
{ ca  leu a 24 } L 42.820, 58.285, 76.255
{ ca  leu a 25 } L 39.954, 55.930, 75.955
{ ca  lys a 26 } L 38.391, 58.983, 77.660
{ ca  glu a 27 } L 39.451, 61.826, 75.414
{ ca  leu a 28 } L 38.241, 59.473, 72.653
{ ca  gly a 29 } L 35.084, 58.777, 74.456
{ ca  phe a 30 } L 35.648, 55.210, 75.908
{ ca  asn a 31 } L 35.074, 55.123, 79.615
{ ca  asn a 32 } L 34.265, 51.428, 80.507
{ ca  val a 33 } L 37.509, 49.883, 81.543
{ ca  glu a 34 } L 38.336, 47.078, 83.997
{ ca  glu a 35 } L 41.675, 46.027, 85.165
{ ca  ala a 36 } L 43.132, 42.531, 85.804
{ ca  glu a 37 } L 46.488, 41.635, 86.907
{ ca  asp a 38 } L 47.157, 38.059, 85.344
{ ca  gly a 39 } L 46.216, 34.894, 83.323
{ ca  val a 40 } L 45.002, 32.658, 86.243
{ ca  asp a 41 } L 43.334, 35.876, 87.644
{ ca  ala a 42 } L 42.120, 36.635, 84.203
{ ca  leu a 43 } L 41.277, 32.872, 83.591
{ ca  asn a 44 } L 39.697, 32.782, 86.919
{ ca  lys a 45 } L 38.059, 36.136, 86.025
{ ca  leu a 46 } L 37.269, 34.799, 82.591
{ ca  gln a 47 } L 36.086, 31.466, 84.069
{ ca  ala a 48 } L 33.502, 33.837, 85.268
{ ca  gly a 49 } L 32.721, 35.617, 82.011
{ ca  gly a 50 } L 31.403, 38.945, 80.717
{ ca  tyr a 51 } L 34.646, 39.859, 79.072
{ ca  gly a 52 } L 34.416, 41.063, 75.522
{ ca  phe a 53 } L 37.684, 42.486, 74.692
{ ca  val a 54 } L 40.739, 41.330, 76.139
{ ca  ile a 55 } L 43.230, 44.111, 75.860
{ ca  ser a 56 } L 45.695, 41.831, 77.162
{ ca  asp a 57 } L 49.060, 42.749, 77.726
{ ca  trp a 58 } L 51.270, 39.992, 76.470
{ ca  asn a 59 } L 52.878, 39.288, 79.797
{ ca  met a 60 } L 51.618, 38.230, 83.191
{ ca  pro a 61 } L 52.267, 35.753, 86.003
{ ca  asn a 62 } L 50.673, 32.177, 86.629
{ ca  met a 63 } L 49.601, 31.937, 83.064
{ ca  asp a 64 } L 50.497, 34.406, 80.340
{ ca  gly a 65 } L 48.755, 35.913, 77.348
{ ca  leu a 66 } L 49.134, 32.789, 75.045
{ ca  glu a 67 } L 48.625, 29.913, 77.523
{ ca  leu a 68 } L 45.768, 32.023, 78.449
{ ca  leu a 69 } L 45.002, 32.041, 74.776
{ ca  lys a 70 } L 45.599, 28.158, 74.187
{ ca  thr a 71 } L 43.919, 26.989, 77.173
{ ca  ile a 72 } L 41.328, 29.416, 76.152
{ ca  arg a 73 } L 41.415, 27.601, 72.855
{ ca  ala a 74 } L 41.571, 23.786, 73.933
{ ca  asp a 75 } L 38.800, 24.455, 76.323
{ ca  gly a 76 } L 35.372, 24.016, 74.991
{ ca  ala a 77 } L 33.888, 27.231, 76.385
{ ca  met a 78 } L 36.354, 30.052, 75.803
{ ca  ser a 79 } L 37.856, 28.893, 72.607
{ ca  ala a 80 } L 36.986, 32.089, 70.547
{ ca  leu a 81 } L 37.405, 35.361, 72.628
{ ca  pro a 82 } L 39.010, 38.442, 70.826
{ ca  val a 83 } L 42.179, 39.085, 72.342
{ ca  leu a 84 } L 43.870, 42.354, 71.343
{ ca  met a 85 } L 47.182, 41.582, 72.291
{ ca  val a 86 } L 48.700, 44.801, 73.439
{ ca  thr a 87 } L 52.179, 44.829, 72.592
{ ca  ala a 88 } L 54.862, 47.354, 73.332
{ ca  glu a 89 } L 56.119, 46.877, 69.765
{ ca  ala a 90 } L 54.922, 45.542, 66.384
{ ca  lys a 91 } L 56.715, 42.127, 66.118
{ ca  lys a 92 } L 56.080, 39.302, 63.583
{ ca  glu a 93 } L 56.288, 36.020, 65.650
{ ca  asn a 94 } L 54.177, 37.565, 68.295
{ ca  ile a 95 } L 51.969, 38.608, 65.569
{ ca  ile a 96 } L 52.088, 34.991, 64.109
{ ca  ala a 97 } L 52.085, 32.905, 67.216
{ ca  ala a 98 } L 49.217, 35.083, 68.116
{ ca  ala a 99 } L 47.869, 34.034, 64.793
{ ca  gln a 100 } L 48.532, 30.159, 65.029
{ ca  ala a 101 } L 47.249, 29.755, 68.547
{ ca  gly a 102 } L 44.268, 31.894, 67.473
{ ca  ala a 103 } L 44.708, 35.742, 68.544
{ ca  ser a 104 } L 42.537, 38.611, 67.134
{ ca  gly a 105 } L 44.796, 41.600, 66.635
{ ca  tyr a 106 } L 47.522, 43.771, 68.092
{ ca  val a 107 } L 48.338, 47.477, 69.085
{ ca  val a 108 } L 51.349, 49.482, 70.153
{ ca  lys a 109 } L 51.466, 51.841, 73.197
{ ca  pro a 110 } L 51.603, 54.694, 73.766
{ ca  phe a 111 } L 49.200, 55.937, 71.356
{ ca  thr a 112 } L 47.381, 59.231, 71.035
{ ca  ala a 113 } L 43.835, 59.334, 71.328
{ ca  ala a 114 } L 43.866, 59.536, 67.566
{ ca  thr a 115 } L 45.818, 56.264, 67.023
{ ca  leu a 116 } L 44.109, 53.994, 69.499
{ ca  glu a 117 } L 41.176, 55.285, 67.585
{ ca  glu a 118 } L 42.221, 53.654, 64.306
{ ca  lys a 119 } L 43.264, 50.084, 65.600
{ ca  leu a 120 } L 40.204, 49.445, 67.416
{ ca  asn a 121 } L 38.352, 50.190, 64.237
{ ca  lys a 122 } L 39.908, 47.379, 62.159
{ ca  ile a 123 } L 39.411, 44.468, 64.681
{ ca  phe a 124 } L 36.019, 45.620, 65.029
{ ca  glu a 125 } L 36.027, 45.442, 61.278
{ ca  lys a 126 } L 37.421, 41.843, 60.816
{ ca  leu a 127 } L 35.502, 40.145, 63.585
{ ca  gly a 128 } L 32.471, 41.858, 62.456
{ ca  met a 129 } L 32.209, 44.483, 65.120
@group {CheY}
@vectorlist {ca-ca} color= cyan
{ ca  pro c 159 } P 58.499, 33.695, 42.583 { ca  pro c 159 } L 58.499, 33.695, 42.583
{ ca  arg c 160 } L 55.280, 33.597, 44.466
{ ca  arg c 161 } L 53.275, 36.590, 43.946
{ ca  ile c 162 } L 50.783, 37.539, 46.504
{ ca  ile c 163 } L 47.811, 38.993, 45.217
{ ca  leu c 164 } L 45.693, 40.895, 47.659
{ ca  ser c 165 } L 42.612, 41.479, 45.998
{ ca  arg c 166 } L 39.824, 43.628, 47.018
{ ca  leu c 167 } L 41.135, 46.323, 49.498
{ ca  lys c 168 } L 39.468, 49.375, 51.133
{ ca  ala c 169 } L 39.858, 53.166, 51.339
{ ca  gly c 170 } L 42.895, 53.898, 53.363
{ ca  glu c 171 } L 43.423, 50.059, 53.454
{ ca  val c 172 } L 45.680, 50.353, 50.522
{ ca  asp c 173 } L 47.814, 52.676, 52.603
{ ca  leu c 174 } L 47.219, 50.685, 55.784
{ ca  leu c 175 } L 47.605, 47.122, 54.451
{ ca  glu c 176 } L 50.511, 48.561, 52.775
{ ca  glu c 177 } L 51.366, 49.615, 56.246
{ ca  glu c 178 } L 50.524, 46.113, 57.736
{ ca  leu c 179 } L 52.119, 43.783, 55.227
{ ca  gly c 180 } L 54.922, 46.233, 55.907
{ ca  his c 181 } L 55.133, 44.864, 59.461
{ ca  leu c 182 } L 55.429, 41.108, 58.405
{ ca  thr c 183 } L 57.359, 41.389, 55.213
{ ca  thr c 184 } L 58.443, 43.845, 52.483
{ ca  leu c 185 } L 56.477, 44.778, 49.441
{ ca  thr c 186 } L 57.814, 45.748, 46.117
{ ca  asp c 187 } L 56.148, 46.680, 42.852
{ ca  val c 188 } L 53.575, 48.212, 44.935
{ ca  val c 189 } L 50.805, 48.717, 42.712
{ ca  lys c 190 } L 48.522, 50.977, 44.705
{ ca  gly c 191 } L 45.525, 50.695, 42.554
{ ca  ala c 192 } L 42.544, 52.495, 43.562
{ ca  asp c 193 } L 41.753, 49.285, 45.469
{ ca  ser c 194 } L 44.436, 46.839, 45.049
{ ca  leu c 195 } L 47.645, 45.837, 46.255
{ ca  ser c 196 } L 49.819, 43.527, 44.552
{ ca  ala c 197 } L 53.223, 43.083, 45.385
{ ca  ile c 198 } L 55.660, 40.486, 44.992
{ ca  leu c 199 } L 56.279, 38.165, 47.982
{ ca  pro c 200 } L 59.573, 37.005, 49.335
{ ca  gly c 201 } L 58.762, 33.413, 50.672
{ ca  asp c 202 } L 60.004, 34.317, 54.167
{ ca  ile c 203 } L 57.012, 33.012, 55.824
{ ca  ala c 204 } L 55.294, 29.702, 55.460
{ ca  glu c 205 } L 52.523, 30.136, 53.167
{ ca  asp c 206 } L 50.506, 28.618, 55.980
{ ca  asp c 207 } L 51.630, 31.505, 58.285
{ ca  ile c 208 } L 51.300, 34.607, 56.040
{ ca  thr c 209 } L 47.996, 33.293, 55.549
{ ca  ala c 210 } L 47.579, 33.214, 59.248
{ ca  val c 211 } L 48.427, 36.981, 59.921
{ ca  leu c 212 } L 46.970, 38.843, 57.029
{ ca  cys c 213 } L 44.159, 36.848, 58.256
{ ca  phe c 214 } L 44.071, 39.482, 61.093
{ ca  val c 215 } L 42.799, 42.060, 58.598
{ ca  ile c 216 } L 41.859, 39.976, 55.522
{ ca  glu c 217 } L 40.868, 36.265, 54.576
{ ca  ala c 218 } L 42.457, 32.961, 53.189
{ ca  asp c 219 } L 40.953, 33.161, 49.799
{ ca  gln c 220 } L 41.862, 36.908, 49.275
{ ca  ile c 221 } L 45.165, 35.394, 49.186
{ ca  thr c 222 } L 46.520, 33.748, 46.246
{ ca  phe c 223 } L 49.909, 32.445, 45.740
{ ca  glu c 224 } L 50.746, 32.373, 42.060
{ ca  thr c 225 } L 53.948, 32.419, 40.027
@vectorlist {CheA-binding} color= yellow 
{ ca  met a 85 } P 47.182, 41.582, 72.291 { cb  met a 85 } L 48.110, 40.392, 71.848
{ cg  met a 85 } L 47.415, 38.993, 71.749
{ sd  met a 85 } L 47.160, 38.048, 73.335
{ ce  met a 85 } L 48.637, 38.430, 74.279
{ ca  val a 86 } P 48.700, 44.801, 73.439 { cb  val a 86 } L 48.334, 45.755, 74.594
{ cg1 val a 86 } L 49.379, 46.863, 74.712
{ cb  val a 86 } P 48.334, 45.755, 74.594 { cg2 val a 86 } L 47.040, 46.408, 74.290
{ ca  thr a 87 } P 52.179, 44.829, 72.592 { cb  thr a 87 } L 52.403, 43.999, 71.331
{ og1 thr a 87 } L 53.545, 43.173, 71.457
{ cb  thr a 87 } P 52.403, 43.999, 71.331 { cg2 thr a 87 } L 52.410, 44.902, 70.087
{ ca  asn a 94 } P 54.177, 37.565, 68.295 { cb  asn a 94 } L 54.443, 38.904, 68.997
{ cg  asn a 94 } L 55.355, 38.682, 70.179
{ od1 asn a 94 } L 55.995, 37.617, 70.285
{ cg  asn a 94 } P 55.355, 38.682, 70.179 { nd2 asn a 94 } L 55.408, 39.667, 71.075
{ ca  ile a 96 } P 52.088, 34.991, 64.109 { cb  ile a 96 } L 53.237, 34.387, 63.331
{ cg1 ile a 96 } L 53.359, 35.014, 61.964
{ cd1 ile a 96 } L 54.715, 34.751, 61.332
{ cb  ile a 96 } P 53.237, 34.387, 63.331 { cg2 ile a 96 } L 53.010, 32.882, 63.190
{ ca  ala a 103 } P 44.708, 35.742, 68.544 { cb  ala a 103 } L 45.924, 36.541, 68.924
{ ca  val a 107 } P 48.338, 47.477, 69.085 { cb  val a 107 } L 47.194, 48.320, 69.656
{ cg1 val a 107 } L 47.104, 48.030, 71.153
{ cb  val a 107 } P 47.194, 48.320, 69.656 { cg2 val a 107 } L 47.472, 49.833, 69.419
{ ca  lys a 122 } P 39.908, 47.379, 62.159 { cb  lys a 122 } L 41.271, 47.351, 61.504
{ cg  lys a 122 } L 41.366, 48.303, 60.321
{ cd  lys a 122 } L 41.306, 47.575, 58.983
{ ce  lys a 122 } L 40.315, 48.166, 57.985
{ nz  lys a 122 } L 40.795, 49.406, 57.373
{ ca  ile a 123 } P 39.411, 44.468, 64.681 { cb  ile a 123 } L 39.827, 44.295, 66.143
{ cg1 ile a 123 } L 41.330, 44.209, 66.262
{ cd1 ile a 123 } L 41.735, 44.500, 67.691
{ cb  ile a 123 } P 39.827, 44.295, 66.143 { cg2 ile a 123 } L 39.188, 43.049, 66.761
{ ca  lys a 126 } P 37.421, 41.843, 60.816 { cb  lys a 126 } L 38.889, 41.464, 60.877
{ cg  lys a 126 } L 39.071, 39.957, 61.013
{ cd  lys a 126 } L 39.875, 39.342, 59.880
{ ce  lys a 126 } L 39.896, 37.830, 59.973
{ nz  lys a 126 } L 40.613, 37.201, 58.853
@vectorlist { FliG supp.} color= green off
{ ca  val a 11 } P 44.801, 42.908, 81.514 { cb  val a 11 } L 44.713, 41.400, 81.098
{ cg1 val a 11 } L 45.279, 40.475, 82.179
{ cb  val a 11 } P 44.713, 41.400, 81.098 { cg2 val a 11 } L 43.290, 40.990, 80.816
{ ca  glu a 27 } P 39.451, 61.826, 75.414 { cb  glu a 27 } L 40.808, 62.511, 75.159
{ cg  glu a 27 } L 40.685, 63.747, 74.230
{ cd  glu a 27 } L 40.731, 65.091, 74.942
{ oe1 glu a 27 } L 40.716, 65.000, 76.252
{ cd  glu a 27 } P 40.731, 65.091, 74.942 { oe2 glu a 27 } L 40.745, 66.149, 74.356
{ ca  ala a 90 } P 54.922, 45.542, 66.384 { cb  ala a 90 } L 54.577, 46.509, 65.257
{ ca  val a 108 } P 51.349, 49.482, 70.153 { cb  val a 108 } L 52.342, 49.720, 69.058
{ cg1 val a 108 } L 53.693, 50.048, 69.678
{ cb  val a 108 } P 52.342, 49.720, 69.058 { cg2 val a 108 } L 52.379, 48.468, 68.189
{ ca  phe a 111 } P 49.200, 55.937, 71.356 { cb  phe a 111 } L 48.309, 54.814, 70.770
{ cg  phe a 111 } L 47.879, 53.859, 71.880
{ cd1 phe a 111 } L 46.728, 54.097, 72.629
{ ce1 phe a 111 } L 46.354, 53.237, 73.665
{ cz  phe a 111 } L 47.145, 52.135, 73.988
{ cg  phe a 111 } P 47.879, 53.859, 71.880 { cd2 phe a 111 } L 48.669, 52.766, 72.230
{ ce2 phe a 111 } L 48.313, 51.900, 73.267
{ cz  phe a 111 } L 47.145, 52.135, 73.988
{ ca  thr a 112 } P 47.381, 59.231, 71.035 { cb  thr a 112 } L 47.295, 60.292, 69.901
{ og1 thr a 112 } L 47.111, 59.698, 68.634
{ cb  thr a 112 } P 47.295, 60.292, 69.901 { cg2 thr a 112 } L 48.427, 61.294, 69.893
{ ca  glu a 117 } P 41.176, 55.285, 67.585 { cb  glu a 117 } L 40.967, 56.775, 67.272
{ cg  glu a 117 } L 39.515, 57.060, 66.861
{ cd  glu a 117 } L 39.185, 58.511, 66.555
{ oe1 glu a 117 } L 40.237, 59.298, 66.503
{ cd  glu a 117 } P 39.185, 58.511, 66.555 { oe2 glu a 117 } L 38.044, 58.902, 66.356
@vectorlist { FliM paren.} color= blue off
{ ca  leu a 9 } P 39.496, 43.806, 80.407 { cb  leu a 9 } L 39.468, 42.241, 80.560
{ cg  leu a 9 } L 40.315, 41.719, 81.755
{ cd1 leu a 9 } L 39.736, 42.205, 83.061
{ cg  leu a 9 } P 40.315, 41.719, 81.755 { cd2 leu a 9 } L 40.397, 40.183, 81.810
{ ca  lys a 45 } P 38.059, 36.136, 86.025 { cb  lys a 45 } L 38.821, 37.411, 85.764
{ cg  lys a 45 } L 38.870, 38.308, 86.967
{ cd  lys a 45 } L 39.280, 39.730, 86.623
{ ce  lys a 45 } L 39.837, 40.488, 87.830
{ nz  lys a 45 } L 39.133, 41.744, 88.125
{ ca  leu a 66 } P 49.134, 32.789, 75.045 { cb  leu a 66 } L 50.278, 32.385, 74.136
{ cg  leu a 66 } L 50.656, 33.414, 73.093
{ cd1 leu a 66 } L 51.789, 32.830, 72.279
{ cg  leu a 66 } P 50.656, 33.414, 73.093 { cd2 leu a 66 } L 49.483, 33.708, 72.166
{ ca  ala a 99 } P 47.869, 34.034, 64.793 { cb  ala a 99 } L 48.416, 34.496, 63.430
{ ca  ser a 104 } P 42.537, 38.611, 67.134 { cb  ser a 104 } L 41.310, 39.057, 67.888
{ og  ser a 104 } L 41.010, 38.065, 68.851
{ ca  pro a 110 } P 51.603, 54.694, 73.766 { cb  pro a 110 } L 52.122, 55.886, 74.547
{ cg  pro a 110 } L 53.406, 56.234, 73.858
{ cd  pro a 110 } L 53.889, 54.922, 73.247
{ n   pro a 110 } P 52.760, 53.954, 73.360 { cd  pro a 110 } L 53.889, 54.922, 73.247
{ ca  ala a 113 } P 43.835, 59.334, 71.328 { cb  ala a 113 } L 43.122, 60.604, 71.746
{ ca  thr a 115 } P 45.818, 56.264, 67.023 { cb  thr a 115 } L 47.215, 56.002, 67.414
{ og1 thr a 115 } L 48.044, 56.814, 66.632
{ cb  thr a 115 } P 47.215, 56.002, 67.414 { cg2 thr a 115 } L 47.464, 54.516, 67.186
@vectorlist {PO4 chelate} color= red 
{ ca  asp a 12 } P 47.935, 44.326, 82.696 { cb  asp a 12 } L 48.028, 45.765, 82.128
{ cg  asp a 12 } L 49.447, 46.143, 81.920
{ od1 asp a 12 } L 50.357, 45.471, 82.353
{ cg  asp a 12 } P 49.447, 46.143, 81.920 { od2 asp a 12 } L 49.604, 47.179, 81.110
{ ca  asp a 13 } P 49.672, 44.236, 85.847 { cb  asp a 13 } L 50.679, 43.154, 86.248
{ cg  asp a 13 } L 51.678, 42.900, 85.151
{ od1 asp a 13 } L 51.509, 43.232, 83.989
{ cg  asp a 13 } P 51.678, 42.900, 85.151 { od2 asp a 13 } L 52.763, 42.341, 85.591
{ ca  asp a 57 } P 49.060, 42.749, 77.726 { cb  asp a 57 } L 49.518, 43.367, 79.036
{ cg  asp a 57 } L 50.774, 44.089, 78.771
{ od1 asp a 57 } L 50.834, 44.954, 77.912
{ cg  asp a 57 } P 50.774, 44.089, 78.771 { od2 asp a 57 } L 51.808, 43.524, 79.350