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    		 BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE                             

Alpha amylase or a-(1,4)-glucan-4-glucanohydrolase, is an enzyme that catalyzes the hydrolysis of a-D-(1,4)-glucosidic linkages in starch and other related carbohydrates. The enzyme from Bacillus Stearothermophilus is thermo-stable and is found to be active at 75C for about 50 min.  It undergoes irreversible thermo-inactivation at 90C. Due to these properties, this enzyme finds wide applications in the textile industry for removal of starch in a process called de-sizing. The cotton fibers are starched before they are weaved to give them enough tensile strength to withstand weaving. After, that they have to be de-starched or "de-sized" before further use. Treatment with a thermo-stable enzyme that specifically removes starch without damaging the material would be an ideal step in this process. The alpha amylase characterized here could be a potential candidate for such industrial applications. 

The three dimensional structure of shows that it consists of a single polypeptide chain folded into three distinct domains as observed commonly in most alpha-amylases. As compared to other amylases, this enzyme has some voids in the alpha helical region close to the active site that decrease their hydrophobic interactions and the inter-helical compactness. They also have fewer hydrogen bonds near the active site that could also contribute to the decreased thermo-stability. It has also been calculated that the solvent-ASA of the charged residues is almost half as compared to other amylases that could affect the thermo-stability of the enzyme. Even though it is not as stable as B. amyloliquefaciens alpha-amylase (90C, pH 6.5 and 270 min.) it is ideal for industrial applications because at its temperature optima it doesn't undergo thermo-inactivation.

This enzyme acts on polysaccharides and hence has multiple binding sites for the polymers. Apart from the active site where the cleavage takes place, they have extended substrate-binding sites to anchor the polysaccharide. The Ca-Na-Ca metal triad found in these enzymes act as stabilizing sites for the polysaccharides. Studies on the triad show that the Sodium atom is responsible for the stability and in some cases they can diffuse in and out of the molecule. It has also been shown in alpha amylases from similar organisms that there is a specific orientation of the metal triad and a potentially a cis-peptide bond could be involved in the binding pocket.

References:
Crystal Structure of Bacillus Stearothermophilus a-amylase: Possible factors determining the thermostability 
Duvjir Suvd et al, J. Biochem. Vol.129, pp. 461-468 (2001).      

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Domain A is the compact core structure with a (b/a)8- barrel.  Domain B consists of a sheet of four anti-parallel beta sheets with long loops between the beta sheets.  Domain C contains 8 beta strands folded into a Greek key motif forming the globular unit. 
View 1 shows the b/a barrel of Domain A very clearly with the active site of the molecule in the center.
View 2 shows all the three distinct domains with the beta sheet of domain C in the left corner followed by the beta-alpha barrel of Domain A and the globular Domain C subunit.
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@text 
 coordinates from file: C:\Documents and Settings\Administrator.TULANE-SOQ7Y2D1\Desktop\1HVX.pdb 
HEADER    HYDROLASE                               08-JAN-01   1HVX              
TITLE     BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE                             
KEYWDS   3 THERMOSTABILITY, CALCIUM, SODIUM                                     
@kinemage 2 
@caption 
This is a backbone view of the molecule showing the Ca-Na-Ca binding site on the interior of domain B spanning to the interface with Domain A. There is a third Ca binding site that is also found in the Greek key motif in co-operation with domain A. The calcium atoms are shown in pink and the sodium atom in green while the backbone atoms are colored purple. The Ca-Na-Ca triad is found in a negatively charged pocket where it seems to neutralize the environment and stabilize the molecule.

@onewidth 
@whitebackground
@zoom 1.00
@group {1HVX 1} 
@subgroup {mainchain} 
@vectorlist {Calphas} color= purple
{ ca  ala a 1 } P 28.156, 5.289, -20.716 { ca  ala a 1 } L 28.156, 5.289, -20.716
{ ca  ala a 2 } L 31.154, 5.550, -18.345
{ ca  pro a 3 } L 30.192, 3.558, -15.204
{ ca  phe a 4 } L 31.008, 4.250, -11.560
{ ca  asn a 5 } L 30.554, 1.717, -8.786
{ ca  gly a 6 } L 28.262, 2.533, -5.897
{ ca  thr a 7 } L 29.803, 2.783, -2.432
{ ca  met a 8 } L 27.965, 3.660, 0.786
{ ca  met a 9 } L 29.343, 4.950, 4.084
{ ca  gln a 10 } L 27.698, 4.778, 7.508
{ ca  tyr a 11 } L 28.559, 8.254, 8.738
{ ca  phe a 12 } L 28.508, 7.809, 12.531
{ ca  glu a 13 } L 29.589, 5.550, 15.370
{ ca  trp a 14 } L 28.162, 4.926, 18.833
{ ca  tyr a 15 } L 30.640, 6.807, 21.035
{ ca  leu a 16 } L 30.653, 10.162, 19.251
{ ca  pro a 17 } L 30.625, 13.035, 21.753
{ ca  asp a 18 } L 27.380, 14.963, 22.271
{ ca  asp a 19 } L 28.612, 18.257, 20.847
{ ca  gly a 20 } L 26.299, 18.961, 17.916
{ ca  thr a 21 } L 29.083, 18.896, 15.336
{ ca  leu a 22 } L 28.233, 15.926, 13.083
{ ca  trp a 23 } L 26.074, 17.787, 10.541
{ ca  thr a 24 } L 28.875, 20.374, 10.245
{ ca  lys a 25 } L 31.460, 17.618, 9.668
{ ca  val a 26 } L 29.348, 16.115, 6.872
{ ca  ala a 27 } L 29.302, 19.493, 5.152
{ ca  asn a 28 } L 33.063, 19.847, 5.650
{ ca  glu a 29 } L 34.055, 16.363, 4.439
{ ca  ala a 30 } L 31.611, 15.930, 1.527
{ ca  asn a 31 } L 34.041, 16.744, -1.294
{ ca  asn a 32 } L 36.895, 14.725, 0.194
{ ca  leu a 33 } L 34.694, 11.637, 0.487
{ ca  ser a 34 } L 33.131, 12.232, -2.916
{ ca  ser a 35 } L 36.520, 12.323, -4.666
{ ca  leu a 36 } L 37.298, 8.851, -3.262
{ ca  gly a 37 } L 34.213, 7.335, -4.882
{ ca  ile a 38 } L 31.744, 7.358, -1.980
{ ca  thr a 39 } L 28.351, 7.777, -3.639
{ ca  ala a 40 } L 25.988, 7.760, -0.651
{ ca  leu a 41 } L 25.960, 8.468, 3.075
{ ca  trp a 42 } L 23.805, 6.790, 5.699
{ ca  leu a 43 } L 23.171, 9.399, 8.400
{ ca  pro a 44 } L 22.036, 8.620, 11.988
{ ca  pro a 45 } L 18.458, 9.418, 13.177
{ ca  ala a 46 } L 18.061, 13.195, 12.754
{ ca  tyr a 47 } L 15.008, 13.663, 15.009
{ ca  lys a 48 } L 14.698, 14.291, 18.768
{ ca  gly a 49 } L 15.292, 11.308, 21.037
{ ca  thr a 50 } L 14.671, 10.864, 24.777
{ ca  ser a 51 } L 17.403, 13.432, 25.490
{ ca  arg a 52 } L 19.994, 15.517, 23.661
{ ca  ser a 53 } L 22.603, 12.751, 24.115
{ ca  asp a 54 } L 20.470, 9.986, 22.607
{ ca  val a 55 } L 22.232, 8.255, 19.706
{ ca  gly a 56 } L 18.820, 8.447, 18.016
{ ca  tyr a 57 } L 17.133, 5.071, 18.531
{ ca  gly a 58 } L 15.186, 6.228, 21.579
{ ca  val a 59 } L 12.957, 8.298, 19.312
{ ca  tyr a 60 } L 10.649, 10.860, 20.872
{ ca  asp a 61 } L 9.448, 13.187, 18.094
{ ca  leu a 62 } L 9.806, 12.409, 14.371
{ ca  tyr a 63 } L 8.948, 16.016, 13.455
{ ca  asp a 64 } L 11.624, 17.609, 15.624
{ ca  leu a 65 } L 14.839, 17.631, 13.587
{ ca  gly a 66 } L 16.656, 19.612, 16.289
{ ca  glu a 67 } L 14.311, 22.566, 15.864
{ ca  phe a 68 } L 12.125, 22.756, 18.974
{ ca  asn a 69 } L 12.992, 23.052, 22.646
{ ca  gln a 70 } L 11.986, 19.582, 23.838
{ ca  lys a 71 } L 13.733, 16.965, 25.980
{ ca  gly a 72 } L 16.173, 19.434, 27.508
{ ca  ala a 73 } L 17.437, 21.032, 24.303
{ ca  val a 74 } L 16.726, 22.370, 20.842
{ ca  arg a 75 } L 19.466, 20.505, 18.978
{ ca  thr a 76 } L 19.813, 16.732, 18.690
{ ca  lys a 77 } L 23.173, 15.101, 19.561
{ ca  tyr a 78 } L 24.138, 15.844, 15.949
{ ca  gly a 79 } L 23.113, 19.458, 15.486
{ ca  thr a 80 } L 20.214, 21.693, 14.491
{ ca  lys a 81 } L 17.617, 21.533, 11.696
{ ca  ala a 82 } L 19.367, 24.244, 9.648
{ ca  gln a 83 } L 22.692, 22.401, 10.004
{ ca  tyr a 84 } L 21.119, 19.109, 8.852
{ ca  leu a 85 } L 19.746, 20.773, 5.706
{ ca  gln a 86 } L 23.142, 22.345, 4.967
{ ca  ala a 87 } L 24.737, 18.898, 5.294
{ ca  ile a 88 } L 22.267, 17.531, 2.732
{ ca  gln a 89 } L 23.054, 20.494, 0.441
{ ca  ala a 90 } L 26.800, 19.864, 0.619
{ ca  ala a 91 } L 26.394, 16.119, -0.033
{ ca  his a 92 } L 24.218, 16.763, -3.086
{ ca  ala a 93 } L 26.580, 19.457, -4.387
{ ca  ala a 94 } L 29.385, 16.860, -4.172
{ ca  gly a 95 } L 27.283, 14.345, -6.103
{ ca  met a 96 } L 26.370, 12.074, -3.201
{ ca  gln a 97 } L 23.057, 10.647, -2.043
{ ca  val a 98 } L 21.822, 10.795, 1.537
{ ca  tyr a 99 } L 20.000, 7.948, 3.293
{ ca  ala a 100 } L 18.081, 8.717, 6.475
{ ca  asp a 101 } L 17.752, 6.372, 9.441
{ ca  val a 102 } L 14.089, 5.482, 10.134
{ ca  val a 103 } L 13.051, 4.240, 13.617
{ ca  phe a 104 } L 9.409, 3.001, 13.633
{ ca  asp a 105 } L 9.486, 0.133, 16.141
{ ca  his a 106 } L 8.906, 2.071, 19.344
{ ca  lys a 107 } L 8.580, 5.485, 20.937
{ ca  gly a 108 } L 10.145, 6.696, 24.174
{ ca  gly a 109 } L 10.387, 9.784, 26.355
{ ca  ala a 110 } L 6.610, 10.061, 26.847
{ ca  asp a 111 } L 5.417, 13.307, 28.399
{ ca  gly a 112 } L 3.053, 11.559, 30.787
{ ca  thr a 113 } L 1.427, 8.326, 31.906
{ ca  glu a 114 } L -2.009, 6.813, 31.345
{ ca  trp a 115 } L -3.889, 4.124, 33.243
{ ca  val a 116 } L -4.320, 1.115, 30.956
{ ca  asp a 117 } L -5.655, -2.428, 31.301
{ ca  ala a 118 } L -2.866, -4.869, 30.509
{ ca  val a 119 } L -1.763, -8.480, 30.892
{ ca  glu a 120 } L 1.713, -9.926, 31.508
{ ca  val a 121 } L 3.189, -12.195, 28.839
{ ca  asn a 122 } L 6.049, -14.701, 28.990
{ ca  pro a 123 } L 9.358, -12.947, 28.071
{ ca  ser a 124 } L 10.451, -16.174, 26.334
{ ca  asp a 125 } L 7.070, -16.651, 24.638
{ ca  arg a 126 } L 5.170, -13.395, 24.242
{ ca  asn a 127 } L 2.243, -15.426, 22.902
{ ca  gln a 128 } L 1.623, -16.896, 26.369
{ ca  glu a 129 } L -0.189, -14.679, 28.886
{ ca  ile a 130 } L 1.059, -15.315, 32.431
{ ca  ser a 131 } L -1.260, -13.217, 34.568
{ ca  gly a 132 } L -4.778, -11.897, 34.691
{ ca  thr a 133 } L -5.723, -8.449, 33.439
{ ca  tyr a 134 } L -4.866, -5.472, 35.640
{ ca  gln a 135 } L -4.430, -1.707, 35.507
{ ca  ile a 136 } L -0.946, -0.281, 35.093
{ ca  gln a 137 } L 0.357, 3.274, 34.766
{ ca  ala a 138 } L 2.111, 3.356, 31.386
{ ca  trp a 139 } L 4.286, 6.034, 29.737
{ ca  thr a 140 } L 2.198, 6.495, 26.593
{ ca  lys a 141 } L 1.117, 10.151, 26.494
{ ca  phe a 142 } L 2.935, 12.143, 23.791
{ ca  asp a 143 } L 1.908, 15.814, 23.432
{ ca  phe a 144 } L 5.104, 17.479, 22.117
{ ca  pro a 145 } L 4.959, 20.654, 24.284
{ ca  gly a 146 } L 7.895, 22.272, 22.492
{ ca  arg a 147 } L 6.462, 21.789, 19.003
{ ca  gly a 148 } L 2.728, 22.135, 19.531
{ ca  asn a 149 } L 0.833, 21.589, 16.278
{ ca  thr a 150 } L 3.581, 22.673, 13.872
{ ca  tyr a 151 } L 3.775, 20.182, 10.957
{ ca  ser a 152 } L 1.394, 17.712, 12.623
{ ca  ser a 153 } L -1.320, 17.915, 15.272
{ ca  phe a 154 } L -1.240, 14.147, 15.936
{ ca  lys a 155 } L -0.989, 13.216, 19.640
{ ca  trp a 156 } L 0.026, 9.695, 20.645
{ ca  arg a 157 } L -1.891, 7.783, 23.341
{ ca  trp a 158 } L -1.962, 4.244, 24.777
{ ca  tyr a 159 } L -4.141, 2.723, 22.029
{ ca  his a 160 } L -1.537, 3.511, 19.352
{ ca  phe a 161 } L 0.775, 1.019, 21.078
{ ca  asp a 162 } L 0.678, -2.742, 21.724
{ ca  gly a 163 } L 2.499, -2.773, 25.047
{ ca  val a 164 } L 5.279, -1.466, 27.295
{ ca  asp a 165 } L 7.772, -2.996, 29.746
{ ca  trp a 166 } L 7.285, -0.883, 32.869
{ ca  asp a 167 } L 4.448, -0.192, 35.281
{ ca  glu a 168 } L 5.048, 3.211, 36.826
{ ca  ser a 169 } L 2.543, 2.497, 39.627
{ ca  arg a 170 } L 4.181, -0.611, 41.089
{ ca  lys a 171 } L 7.613, 0.160, 39.587
{ ca  leu a 172 } L 7.734, -3.271, 37.892
{ ca  ser a 173 } L 9.513, -4.619, 34.798
{ ca  arg a 174 } L 7.239, -7.024, 32.898
{ ca  ile a 175 } L 6.325, -7.355, 29.236
{ ca  tyr a 176 } L 2.821, -5.869, 29.331
{ ca  lys a 177 } L 0.391, -6.396, 26.442
{ ca  phe a 178 } L -2.500, -3.906, 26.283
{ ca  arg a 179 } L -6.152, -5.005, 26.287
{ ca  gly a 180 } L -8.717, -3.571, 23.882
{ ca  ile a 181 } L -10.716, -4.203, 20.747
{ ca  gly a 182 } L -8.247, -5.545, 18.192
{ ca  lys a 183 } L -5.266, -5.455, 20.570
{ ca  ala a 184 } L -2.580, -8.090, 20.000
{ ca  trp a 185 } L 1.087, -8.404, 19.028
{ ca  asp a 186 } L 1.596, -7.702, 15.317
{ ca  trp a 187 } L 2.207, -10.451, 12.776
{ ca  glu a 188 } L 4.208, -11.365, 10.873
{ ca  val a 189 } L 7.361, -10.651, 12.902
{ ca  asp a 190 } L 10.438, -12.621, 13.959
{ ca  thr a 191 } L 9.528, -15.817, 15.848
{ ca  glu a 192 } L 12.292, -15.690, 18.452
{ ca  asn a 193 } L 10.587, -15.513, 21.864
{ ca  gly a 194 } L 7.395, -16.787, 20.237
{ ca  asn a 195 } L 6.609, -13.358, 18.821
{ ca  tyr a 196 } L 9.374, -10.735, 18.796
{ ca  asp a 197 } L 7.138, -7.732, 18.165
{ ca  tyr a 198 } L 7.967, -6.128, 21.519
{ ca  leu a 199 } L 11.496, -4.804, 21.957
{ ca  met a 200 } L 11.653, -1.669, 24.158
{ ca  tyr a 201 } L 9.834, 1.493, 25.334
{ ca  ala a 202 } L 6.283, 1.839, 23.932
{ ca  asp a 203 } L 5.756, -0.663, 21.110
{ ca  leu a 204 } L 4.011, 0.726, 17.998
{ ca  asp a 205 } L 0.805, -0.998, 16.887
{ ca  met a 206 } L 1.262, -1.357, 13.118
{ ca  asp a 207 } L -2.278, -2.703, 12.851
{ ca  his a 208 } L -3.776, 0.583, 14.041
{ ca  pro a 209 } L -5.090, 2.531, 10.972
{ ca  glu a 210 } L -4.243, 5.952, 12.440
{ ca  val a 211 } L -0.656, 4.952, 13.189
{ ca  val a 212 } L -0.158, 3.736, 9.615
{ ca  thr a 213 } L -1.651, 6.953, 8.200
{ ca  glu a 214 } L 0.456, 9.149, 10.484
{ ca  leu a 215 } L 3.716, 7.390, 9.568
{ ca  lys a 216 } L 2.804, 7.659, 5.868
{ ca  ser a 217 } L 2.185, 11.408, 6.313
{ ca  trp a 218 } L 5.508, 11.830, 8.124
{ ca  gly a 219 } L 7.337, 9.946, 5.363
{ ca  lys a 220 } L 6.044, 12.274, 2.657
{ ca  trp a 221 } L 6.663, 15.356, 4.804
{ ca  tyr a 222 } L 10.225, 14.257, 5.595
{ ca  val a 223 } L 11.213, 13.655, 1.969
{ ca  asn a 224 } L 9.539, 16.873, 0.758
{ ca  thr a 225 } L 11.310, 18.895, 3.442
{ ca  thr a 226 } L 14.831, 17.390, 3.360
{ ca  asn a 227 } L 15.001, 15.983, -0.170
{ ca  ile a 228 } L 16.796, 12.867, 1.114
{ ca  asp a 229 } L 17.440, 10.036, -1.354
{ ca  gly a 230 } L 16.743, 6.838, 0.570
{ ca  phe a 231 } L 16.201, 5.122, 3.905
{ ca  arg a 232 } L 17.972, 2.842, 6.371
{ ca  leu a 233 } L 15.281, 0.932, 8.287
{ ca  asp a 234 } L 15.895, 0.158, 11.943
{ ca  ala a 235 } L 14.934, -3.117, 13.661
{ ca  val a 236 } L 12.777, -4.498, 10.849
{ ca  lys a 237 } L 12.467, -7.972, 12.403
{ ca  his a 238 } L 10.369, -6.450, 15.225
{ ca  ile a 239 } L 8.026, -4.685, 12.789
{ ca  lys a 240 } L 5.055, -6.269, 10.978
{ ca  phe a 241 } L 6.596, -7.515, 7.707
{ ca  ser a 242 } L 3.767, -6.322, 5.417
{ ca  phe a 243 } L 3.923, -2.744, 6.738
{ ca  phe a 244 } L 7.064, -1.694, 4.847
{ ca  pro a 245 } L 6.190, -2.607, 1.247
{ ca  asp a 246 } L 2.993, -0.591, 1.834
{ ca  trp a 247 } L 4.708, 2.414, 3.443
{ ca  leu a 248 } L 7.524, 2.433, 0.865
{ ca  ser a 249 } L 5.254, 2.276, -2.190
{ ca  tyr a 250 } L 3.229, 5.178, -0.792
{ ca  val a 251 } L 6.209, 7.449, -0.090
{ ca  arg a 252 } L 7.855, 6.564, -3.425
{ ca  ser a 253 } L 4.720, 7.262, -5.492
{ ca  gln a 254 } L 3.787, 10.453, -3.613
{ ca  thr a 255 } L 7.286, 11.942, -3.903
{ ca  gly a 256 } L 8.284, 10.528, -7.281
{ ca  lys a 257 } L 11.721, 9.521, -5.990
{ ca  pro a 258 } L 13.062, 5.944, -6.324
{ ca  leu a 259 } L 14.169, 6.001, -2.658
{ ca  phe a 260 } L 16.693, 3.174, -2.252
{ ca  thr a 261 } L 16.033, 1.325, 1.006
{ ca  val a 262 } L 18.088, -1.056, 3.131
{ ca  gly a 263 } L 16.636, -2.705, 6.202
{ ca  glu a 264 } L 18.341, -4.099, 9.289
{ ca  tyr a 265 } L 17.106, -7.638, 9.961
{ ca  trp a 266 } L 19.645, -8.818, 12.517
{ ca  ser a 267 } L 20.096, -12.558, 12.148
{ ca  tyr a 268 } L 22.904, -14.937, 11.242
{ ca  asp a 269 } L 20.305, -17.345, 9.836
{ ca  ile a 270 } L 20.190, -16.906, 6.054
{ ca  asn a 271 } L 16.782, -18.610, 6.000
{ ca  lys a 272 } L 15.085, -15.884, 8.055
{ ca  leu a 273 } L 16.596, -13.308, 5.706
{ ca  his a 274 } L 15.294, -15.219, 2.664
{ ca  asn a 275 } L 11.823, -15.355, 4.230
{ ca  tyr a 276 } L 11.844, -11.605, 4.862
{ ca  ile a 277 } L 12.906, -10.746, 1.310
{ ca  met a 278 } L 10.208, -13.086, -0.009
{ ca  lys a 279 } L 7.593, -11.566, 2.310
{ ca  thr a 280 } L 8.504, -8.016, 1.237
{ ca  asn a 281 } L 8.707, -8.738, -2.506
{ ca  gly a 282 } L 12.311, -7.557, -2.846
{ ca  thr a 283 } L 11.203, -3.991, -2.145
{ ca  met a 284 } L 14.352, -3.326, -0.085
{ ca  ser a 285 } L 17.905, -4.573, 0.368
{ ca  leu a 286 } L 19.154, -6.011, 3.682
{ ca  phe a 287 } L 22.451, -5.755, 5.560
{ ca  asp a 288 } L 24.468, -8.978, 5.220
{ ca  ala a 289 } L 24.731, -9.899, 8.929
{ ca  pro a 290 } L 25.836, -13.506, 8.177
{ ca  leu a 291 } L 28.897, -12.197, 6.292
{ ca  his a 292 } L 29.804, -10.029, 9.282
{ ca  asn a 293 } L 29.834, -13.147, 11.454
{ ca  lys a 294 } L 32.090, -14.894, 8.911
{ ca  phe a 295 } L 34.595, -11.995, 8.949
{ ca  tyr a 296 } L 34.498, -11.974, 12.730
{ ca  thr a 297 } L 34.970, -15.754, 13.018
{ ca  ala a 298 } L 37.916, -15.741, 10.606
{ ca  ser a 299 } L 39.640, -12.870, 12.443
{ ca  lys a 300 } L 39.663, -14.843, 15.696
{ ca  ser a 301 } L 40.685, -18.193, 14.201
{ ca  gly a 302 } L 44.395, -17.406, 13.930
{ ca  gly a 303 } L 44.573, -18.768, 10.397
{ ca  thr a 304 } L 42.698, -22.049, 10.909
{ ca  phe a 305 } L 39.497, -20.723, 9.307
{ ca  asp a 306 } L 38.832, -22.356, 5.920
{ ca  met a 307 } L 38.701, -19.376, 3.534
{ ca  arg a 308 } L 36.941, -21.538, 0.921
{ ca  thr a 309 } L 33.799, -21.244, 3.084
{ ca  leu a 310 } L 33.795, -17.432, 3.428
{ ca  met a 311 } L 30.725, -16.813, 1.220
{ ca  thr a 312 } L 28.723, -19.931, 2.036
{ ca  asn a 313 } L 25.249, -19.054, 3.329
{ ca  thr a 314 } L 25.550, -15.268, 3.105
{ ca  leu a 315 } L 23.270, -12.759, 1.347
{ ca  met a 316 } L 26.208, -11.623, -0.774
{ ca  lys a 317 } L 26.180, -15.144, -2.234
{ ca  asp a 318 } L 22.419, -15.871, -2.299
{ ca  gln a 319 } L 20.982, -12.449, -3.237
{ ca  pro a 320 } L 23.895, -10.316, -4.503
{ ca  thr a 321 } L 21.587, -7.574, -5.777
{ ca  leu a 322 } L 19.735, -7.127, -2.470
{ ca  ala a 323 } L 22.739, -7.339, -0.142
{ ca  val a 324 } L 24.436, -4.416, 1.594
{ ca  thr a 325 } L 27.782, -5.751, 2.776
{ ca  phe a 326 } L 29.790, -4.442, 5.742
{ ca  val a 327 } L 32.642, -5.360, 8.077
{ ca  asp a 328 } L 31.491, -3.691, 11.335
{ ca  asn a 329 } L 28.892, -1.131, 12.489
{ ca  his a 330 } L 27.712, 0.835, 15.568
{ ca  asp a 331 } L 26.140, -2.297, 17.114
{ ca  thr a 332 } L 29.170, -4.582, 16.685
{ ca  glu a 333 } L 31.510, -2.058, 18.349
{ ca  pro a 334 } L 33.266, -3.104, 21.590
{ ca  gly a 335 } L 30.958, -2.801, 24.589
{ ca  gln a 336 } L 27.836, -2.569, 22.425
{ ca  ala a 337 } L 24.719, -4.717, 22.042
{ ca  leu a 338 } L 25.904, -7.000, 19.244
{ ca  gln a 339 } L 29.629, -6.583, 19.942
{ ca  ser a 340 } L 31.593, -8.854, 17.614
{ ca  trp a 341 } L 34.427, -6.564, 16.517
{ ca  val a 342 } L 36.553, -7.848, 13.628
{ ca  asp a 343 } L 40.233, -7.862, 14.660
{ ca  pro a 344 } L 42.414, -5.147, 12.998
{ ca  trp a 345 } L 44.729, -7.609, 11.229
{ ca  phe a 346 } L 41.803, -9.077, 9.278
{ ca  lys a 347 } L 39.876, -5.836, 8.724
{ ca  pro a 348 } L 41.727, -4.773, 5.503
{ ca  leu a 349 } L 41.202, -8.245, 3.992
{ ca  ala a 350 } L 37.449, -8.020, 4.677
{ ca  tyr a 351 } L 37.288, -4.584, 3.045
{ ca  ala a 352 } L 39.165, -5.843, -0.017
{ ca  phe a 353 } L 36.602, -8.649, -0.252
{ ca  ile a 354 } L 33.506, -6.420, -0.200
{ ca  leu a 355 } L 34.975, -3.471, -2.147
{ ca  thr a 356 } L 36.485, -5.269, -5.145
{ ca  arg a 357 } L 33.993, -8.104, -5.766
{ ca  gln a 358 } L 30.922, -7.596, -7.984
{ ca  glu a 359 } L 28.377, -8.962, -5.497
{ ca  gly a 360 } L 26.639, -6.602, -3.100
{ ca  tyr a 361 } L 26.554, -2.902, -2.258
{ ca  pro a 362 } L 29.425, -2.226, 0.219
{ ca  cys a 363 } L 29.168, 0.050, 3.257
{ ca  val a 364 } L 32.240, 1.585, 4.906
{ ca  phe a 365 } L 32.033, 2.184, 8.664
{ ca  tyr a 366 } L 32.820, 5.647, 10.087
{ ca  gly a 367 } L 34.480, 4.029, 13.107
{ ca  asp a 368 } L 36.909, 2.122, 10.885
{ ca  tyr a 369 } L 37.653, 5.135, 8.713
{ ca  tyr a 370 } L 38.151, 7.744, 11.432
{ ca  gly a 371 } L 38.952, 5.470, 14.372
{ ca  ile a 372 } L 37.232, 5.079, 17.744
{ ca  pro a 373 } L 39.067, 7.086, 20.465
{ ca  gln a 374 } L 36.844, 5.486, 23.118
{ ca  tyr a 375 } L 38.774, 2.216, 22.860
{ ca  asn a 376 } L 42.038, 3.592, 21.439
{ ca  ile a 377 } L 41.101, 2.139, 18.042
{ ca  pro a 378 } L 43.152, 3.936, 15.332
{ ca  ser a 379 } L 42.074, 5.299, 11.956
{ ca  leu a 380 } L 42.363, 2.792, 9.085
{ ca  lys a 381 } L 42.010, 5.468, 6.403
{ ca  ser a 382 } L 45.521, 4.638, 5.121
{ ca  lys a 383 } L 44.450, 1.019, 4.526
{ ca  ile a 384 } L 40.947, 1.783, 3.237
{ ca  asp a 385 } L 41.727, 4.618, 0.782
{ ca  pro a 386 } L 43.729, 2.420, -1.631
{ ca  leu a 387 } L 40.807, -0.033, -1.623
{ ca  leu a 388 } L 38.340, 2.788, -2.369
{ ca  ile a 389 } L 40.445, 3.804, -5.370
{ ca  ala a 390 } L 40.460, 0.144, -6.504
{ ca  arg a 391 } L 36.644, 0.073, -6.503
{ ca  arg a 392 } L 36.385, 3.534, -8.079
{ ca  asp a 393 } L 38.722, 2.988, -11.061
{ ca  tyr a 394 } L 39.438, -0.732, -11.428
{ ca  ala a 395 } L 36.800, -3.140, -10.068
{ ca  tyr a 396 } L 34.696, -3.489, -13.239
{ ca  gly a 397 } L 33.719, -6.286, -15.608
{ ca  thr a 398 } L 33.576, -10.080, -15.610
{ ca  gln a 399 } L 34.720, -11.745, -12.400
{ ca  his a 400 } L 36.729, -14.960, -11.996
{ ca  asp a 401 } L 36.766, -16.641, -8.596
{ ca  tyr a 402 } L 39.545, -18.571, -6.898
{ ca  leu a 403 } L 38.165, -19.722, -3.529
{ ca  asp a 404 } L 40.305, -22.840, -3.784
{ ca  his a 405 } L 42.611, -22.903, -0.758
{ ca  ser a 406 } L 42.076, -22.775, 3.020
{ ca  asp a 407 } L 44.345, -19.701, 3.307
{ ca  ile a 408 } L 44.916, -17.911, -0.001
{ ca  ile a 409 } L 41.814, -17.044, -2.026
{ ca  gly a 410 } L 41.470, -14.595, -4.882
{ ca  trp a 411 } L 39.372, -13.216, -7.718
{ ca  thr a 412 } L 39.846, -11.041, -10.805
{ ca  arg a 413 } L 37.817, -8.427, -12.679
{ ca  glu a 414 } L 38.453, -8.167, -16.441
{ ca  gly a 415 } L 37.539, -4.490, -16.657
{ ca  val a 416 } L 35.122, -2.938, -19.174
{ ca  thr a 417 } L 35.668, -1.256, -22.540
{ ca  glu a 418 } L 33.825, 1.900, -21.474
{ ca  lys a 419 } L 36.292, 2.292, -18.582
{ ca  pro a 420 } L 39.821, 2.250, -20.087
{ ca  gly a 421 } L 42.517, 1.117, -17.660
{ ca  ser a 422 } L 40.119, -1.002, -15.592
{ ca  gly a 423 } L 40.884, -4.572, -14.555
{ ca  leu a 424 } L 42.127, -6.042, -11.290
{ ca  ala a 425 } L 43.430, -9.137, -9.518
{ ca  ala a 426 } L 43.084, -9.425, -5.736
{ ca  leu a 427 } L 44.456, -11.915, -3.218
{ ca  ile a 428 } L 43.913, -12.190, 0.538
{ ca  thr a 429 } L 45.200, -14.765, 3.026
{ ca  asp a 430 } L 44.435, -15.497, 6.668
{ ca  gly a 431 } L 47.733, -17.372, 6.984
{ ca  pro a 432 } L 51.161, -17.511, 5.280
{ ca  gly a 433 } L 51.580, -15.789, 1.918
{ ca  gly a 434 } L 52.253, -17.286, -1.482
{ ca  ser a 435 } L 51.178, -16.982, -5.095
{ ca  lys a 436 } L 48.298, -18.011, -7.335
{ ca  trp a 437 } L 47.891, -18.058, -11.094
{ ca  met a 438 } L 44.755, -16.153, -12.073
{ ca  tyr a 439 } L 43.090, -15.204, -15.355
{ ca  val a 440 } L 42.644, -11.444, -15.867
{ ca  gly a 441 } L 41.794, -11.553, -19.546
{ ca  lys a 442 } L 43.567, -12.068, -22.854
{ ca  gln a 443 } L 43.104, -8.331, -23.490
{ ca  his a 444 } L 45.689, -7.556, -20.790
{ ca  ala a 445 } L 48.367, -9.797, -22.320
{ ca  gly a 446 } L 51.817, -8.270, -21.884
{ ca  lys a 447 } L 50.724, -5.590, -19.422
{ ca  val a 448 } L 52.485, -5.149, -16.086
{ ca  phe a 449 } L 50.415, -5.014, -12.885
{ ca  tyr a 450 } L 51.462, -3.500, -9.550
{ ca  asp a 451 } L 50.130, -3.702, -5.993
{ ca  leu a 452 } L 47.842, -0.700, -5.479
{ ca  thr a 453 } L 47.837, -1.325, -1.712
{ ca  gly a 454 } L 51.601, -0.736, -1.547
{ ca  asn a 455 } L 52.057, -3.938, 0.485
{ ca  arg a 456 } L 54.329, -5.468, -2.175
{ ca  ser a 457 } L 56.975, -3.737, -4.285
{ ca  asp a 458 } L 57.290, -6.368, -7.016
{ ca  thr a 459 } L 55.280, -6.446, -10.265
{ ca  val a 460 } L 53.470, -9.123, -12.287
{ ca  thr a 461 } L 53.473, -9.363, -16.095
{ ca  ile a 462 } L 50.467, -10.927, -17.845
{ ca  asn a 463 } L 51.378, -13.762, -20.220
{ ca  ser a 464 } L 50.063, -14.153, -23.764
{ ca  asp a 465 } L 47.138, -16.252, -22.498
{ ca  gly a 466 } L 45.878, -13.584, -20.098
{ ca  trp a 467 } L 47.146, -15.314, -16.952
{ ca  gly a 468 } L 49.433, -13.904, -14.277
{ ca  glu a 469 } L 51.073, -15.366, -11.172
{ ca  phe a 470 } L 49.940, -12.921, -8.525
{ ca  lys a 471 } L 51.435, -12.774, -5.031
{ ca  val a 472 } L 50.491, -11.833, -1.458
{ ca  asn a 473 } L 52.322, -11.519, 1.888
{ ca  gly a 474 } L 51.287, -13.514, 4.946
{ ca  gly a 475 } L 48.129, -12.352, 6.728
{ ca  ser a 476 } L 47.780, -9.595, 4.162
{ ca  val a 477 } L 46.115, -8.371, 0.962
{ ca  ser a 478 } L 47.424, -7.306, -2.427
{ ca  val a 479 } L 45.336, -5.670, -5.149
{ ca  trp a 480 } L 47.050, -5.821, -8.530
{ ca  val a 481 } L 46.058, -3.284, -11.183
{ ca  pro a 482 } L 47.505, -2.449, -14.641
{ ca  arg a 483 } L 50.116, 0.293, -14.920
@group {1HVX 2} 
@subgroup {het groups} 
@spherelist {het M} color= pink  radius= 0.5 
{Ca    ca   501 } -1.027, -4.975, 17.230
{Ca    ca   502 } 7.593, -3.938, 17.333
{Ca    ca   503 } 42.926, -20.529, 6.892
@vectorlist {het} color= pink  
{Ca    ca   501 } P -1.027, -4.975, 17.230 {Ca    ca   501 } L -1.027, -4.975, 17.230
{Ca    ca   502 } P 7.593, -3.938, 17.333 {Ca    ca   502 } L 7.593, -3.938, 17.333
{Ca    ca   503 } P 42.926, -20.529, 6.892 {Ca    ca   503 } L 42.926, -20.529, 6.892
@spherelist {het M} color= green radius= 0.5
{Na    na   504 } 3.472, -3.737, 17.594
@vectorlist {het} color= green
{Na    na   504 } P 3.472, -3.737, 17.594 {Na    na   504 } L 3.472, -3.737, 17.594
@text 
 coordinates from file: C:\Documents and Settings\Administrator.TULANE-SOQ7Y2D1\Desktop\1HVX.pdb 
HEADER    HYDROLASE                               08-JAN-01   1HVX              
TITLE     BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE                             
KEYWDS   3 THERMOSTABILITY, CALCIUM, SODIUM                                     
@kinemage 3 
@caption 
Active site of the molecule:
The active site is located at the C-terminal side of the molecule in domain A. The labeled residues Asp 234, Glu 264 and Asp 331 are assigned to be the catalytic residues in the molecule.
@onewidth 
@whitebackground
@zoom 1.58
@zslab 243
@ztrans 25
@group {1HVX 1} 
@subgroup {mainchain} 
@vectorlist {Calphas} color= purple
{ ca  ala a 1 } P 28.156, 5.289, -20.716 { ca  ala a 1 } L 28.156, 5.289, -20.716
{ ca  ala a 2 } L 31.154, 5.550, -18.345
{ ca  pro a 3 } L 30.192, 3.558, -15.204
{ ca  phe a 4 } L 31.008, 4.250, -11.560
{ ca  asn a 5 } L 30.554, 1.717, -8.786
{ ca  gly a 6 } L 28.262, 2.533, -5.897
{ ca  thr a 7 } L 29.803, 2.783, -2.432
{ ca  met a 8 } L 27.965, 3.660, 0.786
{ ca  met a 9 } L 29.343, 4.950, 4.084
{ ca  gln a 10 } L 27.698, 4.778, 7.508
{ ca  tyr a 11 } L 28.559, 8.254, 8.738
{ ca  phe a 12 } L 28.508, 7.809, 12.531
{ ca  glu a 13 } L 29.589, 5.550, 15.370
{ ca  trp a 14 } L 28.162, 4.926, 18.833
{ ca  tyr a 15 } L 30.640, 6.807, 21.035
{ ca  leu a 16 } L 30.653, 10.162, 19.251
{ ca  pro a 17 } L 30.625, 13.035, 21.753
{ ca  asp a 18 } L 27.380, 14.963, 22.271
{ ca  asp a 19 } L 28.612, 18.257, 20.847
{ ca  gly a 20 } L 26.299, 18.961, 17.916
{ ca  thr a 21 } L 29.083, 18.896, 15.336
{ ca  leu a 22 } L 28.233, 15.926, 13.083
{ ca  trp a 23 } L 26.074, 17.787, 10.541
{ ca  thr a 24 } L 28.875, 20.374, 10.245
{ ca  lys a 25 } L 31.460, 17.618, 9.668
{ ca  val a 26 } L 29.348, 16.115, 6.872
{ ca  ala a 27 } L 29.302, 19.493, 5.152
{ ca  asn a 28 } L 33.063, 19.847, 5.650
{ ca  glu a 29 } L 34.055, 16.363, 4.439
{ ca  ala a 30 } L 31.611, 15.930, 1.527
{ ca  asn a 31 } L 34.041, 16.744, -1.294
{ ca  asn a 32 } L 36.895, 14.725, 0.194
{ ca  leu a 33 } L 34.694, 11.637, 0.487
{ ca  ser a 34 } L 33.131, 12.232, -2.916
{ ca  ser a 35 } L 36.520, 12.323, -4.666
{ ca  leu a 36 } L 37.298, 8.851, -3.262
{ ca  gly a 37 } L 34.213, 7.335, -4.882
{ ca  ile a 38 } L 31.744, 7.358, -1.980
{ ca  thr a 39 } L 28.351, 7.777, -3.639
{ ca  ala a 40 } L 25.988, 7.760, -0.651
{ ca  leu a 41 } L 25.960, 8.468, 3.075
{ ca  trp a 42 } L 23.805, 6.790, 5.699
{ ca  leu a 43 } L 23.171, 9.399, 8.400
{ ca  pro a 44 } L 22.036, 8.620, 11.988
{ ca  pro a 45 } L 18.458, 9.418, 13.177
{ ca  ala a 46 } L 18.061, 13.195, 12.754
{ ca  tyr a 47 } L 15.008, 13.663, 15.009
{ ca  lys a 48 } L 14.698, 14.291, 18.768
{ ca  gly a 49 } L 15.292, 11.308, 21.037
{ ca  thr a 50 } L 14.671, 10.864, 24.777
{ ca  ser a 51 } L 17.403, 13.432, 25.490
{ ca  arg a 52 } L 19.994, 15.517, 23.661
{ ca  ser a 53 } L 22.603, 12.751, 24.115
{ ca  asp a 54 } L 20.470, 9.986, 22.607
{ ca  val a 55 } L 22.232, 8.255, 19.706
{ ca  gly a 56 } L 18.820, 8.447, 18.016
{ ca  tyr a 57 } L 17.133, 5.071, 18.531
{ ca  gly a 58 } L 15.186, 6.228, 21.579
{ ca  val a 59 } L 12.957, 8.298, 19.312
{ ca  tyr a 60 } L 10.649, 10.860, 20.872
{ ca  asp a 61 } L 9.448, 13.187, 18.094
{ ca  leu a 62 } L 9.806, 12.409, 14.371
{ ca  tyr a 63 } L 8.948, 16.016, 13.455
{ ca  asp a 64 } L 11.624, 17.609, 15.624
{ ca  leu a 65 } L 14.839, 17.631, 13.587
{ ca  gly a 66 } L 16.656, 19.612, 16.289
{ ca  glu a 67 } L 14.311, 22.566, 15.864
{ ca  phe a 68 } L 12.125, 22.756, 18.974
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{ ca  val a 481 } L 46.058, -3.284, -11.183
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{ ca  arg a 483 } L 50.116, 0.293, -14.920
@group {1HVX 2} 
@subgroup {het groups} 
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{Ca    ca   502 } 7.593, -3.938, 17.333
{Ca    ca   503 } 42.926, -20.529, 6.892
@vectorlist {het} color= pink  
{Ca    ca   501 } P -1.027, -4.975, 17.230 {Ca    ca   501 } L -1.027, -4.975, 17.230
{Ca    ca   502 } P 7.593, -3.938, 17.333 {Ca    ca   502 } L 7.593, -3.938, 17.333
{Ca    ca   503 } P 42.926, -20.529, 6.892 {Ca    ca   503 } L 42.926, -20.529, 6.892
@spherelist {het M} color= green radius= 0.5
{Na    na   504 } 3.472, -3.737, 17.594
@vectorlist {het} color= green  
{Na    na   504 } P 3.472, -3.737, 17.594 {Na    na   504 } L 3.472, -3.737, 17.594
@labellist {drawn} color=cyan
{ ca  asp a 234 } L 15.895, 0.158, 11.943
{ ca  glu a 264 } L 18.341, -4.099, 9.289
{ ca  asp a 331 } L 26.140, -2.297, 17.114

@text

 coordinates from file: C:\Documents and Settings\Administrator.TULANE-SOQ7Y2D1\Desktop\1HVX.pdb 
HEADER    HYDROLASE                               08-JAN-01   1HVX              
TITLE     BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE                             
KEYWDS   3 THERMOSTABILITY, CALCIUM, SODIUM                                     
@kinemage 4
@caption

Metal ion binding sites:
The two calcium atoms Ca I and Ca II form a triad with the Na atom. The Ca I is coordinated to Asp 105 while the Ca II is coordinated through a water molecule to the side chain of Asp 207. Ca I of the triad is known to activate the extended substrate binding and is common feature of amylases in bacteria. The sodium atom accounts for the stability in this triad. The coordination geometry of both calcium ions in the metal triad can be described as a distorted pentagonal bi-pyramid and idealized as an octahedron, as is found for most calcium ions in proteins. 

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{ ca  asp a 19 }28.612 18.257 20.847
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{ ca  val a 324 }24.436 -4.416 1.594
{ ca  thr a 325 }27.782 -5.751 2.776
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{ ca  cys a 363 }29.168 0.050 3.257
{ ca  val a 364 }32.240 1.585 4.906
{ ca  phe a 365 }32.033 2.184 8.664
{ ca  tyr a 366 }32.820 5.647 10.087
{ ca  gly a 367 }34.480 4.029 13.107
{ ca  asp a 368 }36.909 2.122 10.885
{ ca  tyr a 369 }37.653 5.135 8.713
{ ca  tyr a 370 }38.151 7.744 11.432
{ ca  gly a 371 }38.952 5.470 14.372
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{ ca  tyr a 375 }38.774 2.216 22.860
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{ ca  pro a 378 }43.152 3.936 15.332
{ ca  ser a 379 }42.074 5.299 11.956
{ ca  leu a 380 }42.363 2.792 9.085
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{ ca  ser a 382 }45.521 4.638 5.121
{ ca  lys a 383 }44.450 1.019 4.526
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{ ca  asp a 407 }44.345 -19.701 3.307
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{ ca  ile a 409 }41.814 -17.044 -2.026
{ ca  gly a 410 }41.470 -14.595 -4.882
{ ca  trp a 411 }39.372 -13.216 -7.718
{ ca  thr a 412 }39.846 -11.041 -10.805
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{ ca  glu a 418 }33.825 1.900 -21.474
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{ ca  pro a 420 }39.821 2.250 -20.087
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{ ca  asp a 234 }15.895 0.158 11.943
{ ca  glu a 264 }18.341 -4.099 9.289
{ ca  asp a 331 }26.140 -2.297 17.114
@group {1HVX 2}
@subgroup {het groups}
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{Ca    ca   502 }7.593 -3.938 17.333
{Ca    ca   503 }42.926 -20.529 6.892
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{Ca    ca   503 }P 42.926 -20.529 6.892
{"}42.926 -20.529 6.892
@spherelist {het M} color= green radius= 0.500
{Na    na   504 }3.472 -3.737 17.594
@vectorlist {het} color= green
{Na    na   504 }P 3.472 -3.737 17.594
{"}3.472 -3.737 17.594
@labellist {drawn} color= cyan
{ ca  asp a 105 }9.486 0.133 16.141
{ ca  asp a 207 }-2.278 -2.703 12.851
@text

 coordinates from file: C:\Documents and Settings\Administrator.TULANE-SOQ7Y2D1\Desktop\1HVX.pdb 
HEADER    HYDROLASE                               08-JAN-01   1HVX              
TITLE     BACILLUS STEAROTHERMOPHILUS ALPHA-AMYLASE                             
KEYWDS   3 THERMOSTABILITY, CALCIUM, SODIUM                                     
@kinemage 5
@caption

Metal ion binding sites:
The third calcium atom Ca III forms a bridge between domain A and domain C by coordinating the 6th alpha helix of domain A with the loop between the 1st and 2nd beta sheets of domain C. The coordinating residues are Phe305 and Ser406. This atom could contribute to the thermo stability of the enzyme as it forms a bridge between two domains of the enzyme and forms the major point of interaction between the two domains.

@onewidth
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@zoom 1.55
@zslab 298
@ztran 0
@center 23.287 0.670 8.663
@matrix
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@group {1HVX 1}
@subgroup {mainchain}
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{"}28.156 5.289 -20.716
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{ ca  phe a 4 }31.008 4.250 -11.560
{ ca  asn a 5 }30.554 1.717 -8.786
{ ca  gly a 6 }28.262 2.533 -5.897
{ ca  thr a 7 }29.803 2.783 -2.432
{ ca  met a 8 }27.965 3.660 0.786
{ ca  met a 9 }29.343 4.950 4.084
{ ca  gln a 10 }27.698 4.778 7.508
{ ca  tyr a 11 }28.559 8.254 8.738
{ ca  phe a 12 }28.508 7.809 12.531
{ ca  glu a 13 }29.589 5.550 15.370
{ ca  trp a 14 }28.162 4.926 18.833
{ ca  tyr a 15 }30.640 6.807 21.035
{ ca  leu a 16 }30.653 10.162 19.251
{ ca  pro a 17 }30.625 13.035 21.753
{ ca  asp a 18 }27.380 14.963 22.271
{ ca  asp a 19 }28.612 18.257 20.847
{ ca  gly a 20 }26.299 18.961 17.916
{ ca  thr a 21 }29.083 18.896 15.336
{ ca  leu a 22 }28.233 15.926 13.083
{ ca  trp a 23 }26.074 17.787 10.541
{ ca  thr a 24 }28.875 20.374 10.245
{ ca  lys a 25 }31.460 17.618 9.668
{ ca  val a 26 }29.348 16.115 6.872
{ ca  ala a 27 }29.302 19.493 5.152
{ ca  asn a 28 }33.063 19.847 5.650
{ ca  glu a 29 }34.055 16.363 4.439
{ ca  ala a 30 }31.611 15.930 1.527
{ ca  asn a 31 }34.041 16.744 -1.294
{ ca  asn a 32 }36.895 14.725 0.194
{ ca  leu a 33 }34.694 11.637 0.487
{ ca  ser a 34 }33.131 12.232 -2.916
{ ca  ser a 35 }36.520 12.323 -4.666
{ ca  leu a 36 }37.298 8.851 -3.262
{ ca  gly a 37 }34.213 7.335 -4.882
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{ ca  thr a 39 }28.351 7.777 -3.639
{ ca  ala a 40 }25.988 7.760 -0.651
{ ca  leu a 41 }25.960 8.468 3.075
{ ca  trp a 42 }23.805 6.790 5.699
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{ ca  pro a 44 }22.036 8.620 11.988
{ ca  pro a 45 }18.458 9.418 13.177
{ ca  ala a 46 }18.061 13.195 12.754
{ ca  tyr a 47 }15.008 13.663 15.009
{ ca  lys a 48 }14.698 14.291 18.768
{ ca  gly a 49 }15.292 11.308 21.037
{ ca  thr a 50 }14.671 10.864 24.777
{ ca  ser a 51 }17.403 13.432 25.490
{ ca  arg a 52 }19.994 15.517 23.661
{ ca  ser a 53 }22.603 12.751 24.115
{ ca  asp a 54 }20.470 9.986 22.607
{ ca  val a 55 }22.232 8.255 19.706
{ ca  gly a 56 }18.820 8.447 18.016
{ ca  tyr a 57 }17.133 5.071 18.531
{ ca  gly a 58 }15.186 6.228 21.579
{ ca  val a 59 }12.957 8.298 19.312
{ ca  tyr a 60 }10.649 10.860 20.872
{ ca  asp a 61 }9.448 13.187 18.094
{ ca  leu a 62 }9.806 12.409 14.371
{ ca  tyr a 63 }8.948 16.016 13.455
{ ca  asp a 64 }11.624 17.609 15.624
{ ca  leu a 65 }14.839 17.631 13.587
{ ca  gly a 66 }16.656 19.612 16.289
{ ca  glu a 67 }14.311 22.566 15.864
{ ca  phe a 68 }12.125 22.756 18.974
{ ca  asn a 69 }12.992 23.052 22.646
{ ca  gln a 70 }11.986 19.582 23.838
{ ca  lys a 71 }13.733 16.965 25.980
{ ca  gly a 72 }16.173 19.434 27.508
{ ca  ala a 73 }17.437 21.032 24.303
{ ca  val a 74 }16.726 22.370 20.842
{ ca  arg a 75 }19.466 20.505 18.978
{ ca  thr a 76 }19.813 16.732 18.690
{ ca  lys a 77 }23.173 15.101 19.561
{ ca  tyr a 78 }24.138 15.844 15.949
{ ca  gly a 79 }23.113 19.458 15.486
{ ca  thr a 80 }20.214 21.693 14.491
{ ca  lys a 81 }17.617 21.533 11.696
{ ca  ala a 82 }19.367 24.244 9.648
{ ca  gln a 83 }22.692 22.401 10.004
{ ca  tyr a 84 }21.119 19.109 8.852
{ ca  leu a 85 }19.746 20.773 5.706
{ ca  gln a 86 }23.142 22.345 4.967
{ ca  ala a 87 }24.737 18.898 5.294
{ ca  ile a 88 }22.267 17.531 2.732
{ ca  gln a 89 }23.054 20.494 0.441
{ ca  ala a 90 }26.800 19.864 0.619
{ ca  ala a 91 }26.394 16.119 -0.033
{ ca  his a 92 }24.218 16.763 -3.086
{ ca  ala a 93 }26.580 19.457 -4.387
{ ca  ala a 94 }29.385 16.860 -4.172
{ ca  gly a 95 }27.283 14.345 -6.103
{ ca  met a 96 }26.370 12.074 -3.201
{ ca  gln a 97 }23.057 10.647 -2.043
{ ca  val a 98 }21.822 10.795 1.537
{ ca  tyr a 99 }20.000 7.948 3.293
{ ca  ala a 100 }18.081 8.717 6.475
{ ca  asp a 101 }17.752 6.372 9.441
{ ca  val a 102 }14.089 5.482 10.134
{ ca  val a 103 }13.051 4.240 13.617
{ ca  phe a 104 }9.409 3.001 13.633
{ ca  his a 106 }8.906 2.071 19.344
{ ca  lys a 107 }8.580 5.485 20.937
{ ca  gly a 108 }10.145 6.696 24.174
{ ca  gly a 109 }10.387 9.784 26.355
{ ca  ala a 110 }6.610 10.061 26.847
{ ca  asp a 111 }5.417 13.307 28.399
{ ca  gly a 112 }3.053 11.559 30.787
{ ca  thr a 113 }1.427 8.326 31.906
{ ca  glu a 114 }-2.009 6.813 31.345
{ ca  trp a 115 }-3.889 4.124 33.243
{ ca  val a 116 }-4.320 1.115 30.956
{ ca  asp a 117 }-5.655 -2.428 31.301
{ ca  ala a 118 }-2.866 -4.869 30.509
{ ca  val a 119 }-1.763 -8.480 30.892
{ ca  glu a 120 }1.713 -9.926 31.508
{ ca  val a 121 }3.189 -12.195 28.839
{ ca  asn a 122 }6.049 -14.701 28.990
{ ca  pro a 123 }9.358 -12.947 28.071
{ ca  ser a 124 }10.451 -16.174 26.334
{ ca  asp a 125 }7.070 -16.651 24.638
{ ca  arg a 126 }5.170 -13.395 24.242
{ ca  asn a 127 }2.243 -15.426 22.902
{ ca  gln a 128 }1.623 -16.896 26.369
{ ca  glu a 129 }-0.189 -14.679 28.886
{ ca  ile a 130 }1.059 -15.315 32.431
{ ca  ser a 131 }-1.260 -13.217 34.568
{ ca  gly a 132 }-4.778 -11.897 34.691
{ ca  thr a 133 }-5.723 -8.449 33.439
{ ca  tyr a 134 }-4.866 -5.472 35.640
{ ca  gln a 135 }-4.430 -1.707 35.507
{ ca  ile a 136 }-0.946 -0.281 35.093
{ ca  gln a 137 }0.357 3.274 34.766
{ ca  ala a 138 }2.111 3.356 31.386
{ ca  trp a 139 }4.286 6.034 29.737
{ ca  thr a 140 }2.198 6.495 26.593
{ ca  lys a 141 }1.117 10.151 26.494
{ ca  phe a 142 }2.935 12.143 23.791
{ ca  asp a 143 }1.908 15.814 23.432
{ ca  phe a 144 }5.104 17.479 22.117
{ ca  pro a 145 }4.959 20.654 24.284
{ ca  gly a 146 }7.895 22.272 22.492
{ ca  arg a 147 }6.462 21.789 19.003
{ ca  gly a 148 }2.728 22.135 19.531
{ ca  asn a 149 }0.833 21.589 16.278
{ ca  thr a 150 }3.581 22.673 13.872
{ ca  tyr a 151 }3.775 20.182 10.957
{ ca  ser a 152 }1.394 17.712 12.623
{ ca  ser a 153 }-1.320 17.915 15.272
{ ca  phe a 154 }-1.240 14.147 15.936
{ ca  lys a 155 }-0.989 13.216 19.640
{ ca  trp a 156 }0.026 9.695 20.645
{ ca  arg a 157 }-1.891 7.783 23.341
{ ca  trp a 158 }-1.962 4.244 24.777
{ ca  tyr a 159 }-4.141 2.723 22.029
{ ca  his a 160 }-1.537 3.511 19.352
{ ca  phe a 161 }0.775 1.019 21.078
{ ca  asp a 162 }0.678 -2.742 21.724
{ ca  gly a 163 }2.499 -2.773 25.047
{ ca  val a 164 }5.279 -1.466 27.295
{ ca  asp a 165 }7.772 -2.996 29.746
{ ca  trp a 166 }7.285 -0.883 32.869
{ ca  asp a 167 }4.448 -0.192 35.281
{ ca  glu a 168 }5.048 3.211 36.826
{ ca  ser a 169 }2.543 2.497 39.627
{ ca  arg a 170 }4.181 -0.611 41.089
{ ca  lys a 171 }7.613 0.160 39.587
{ ca  leu a 172 }7.734 -3.271 37.892
{ ca  ser a 173 }9.513 -4.619 34.798
{ ca  arg a 174 }7.239 -7.024 32.898
{ ca  ile a 175 }6.325 -7.355 29.236
{ ca  tyr a 176 }2.821 -5.869 29.331
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{ ca  phe a 178 }-2.500 -3.906 26.283
{ ca  arg a 179 }-6.152 -5.005 26.287
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