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***  METAL BINDING PROTEIN 30-OCT-99 1D9Y  ***

CA distance fluctuations for 23012322232774474

---  normal mode 8  ---

This matrix displays the maximum distance fluctuations between all pairs of CA atoms and between the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Distance increases are plotted in blue and decreases in red for the strongest 10% of the residue pair distance changes. Every pixel corresponds to a single residue. Grey lines are drawn every 10 residues, yellow lines every 100 residues (counting from the upper left corner).

The following table indicates for every residue the two corresponding residues with the strongest CA distance fluctuations.

[HELP on distance fluctuations]

GD ok
largest increasereflargest decrease
LYS 309 0.29 ASP 1 -0.11 ALA 281
LYS 309 0.31 ILE 2 -0.10 ALA 281
LYS 309 0.36 THR 3 -0.08 ALA 281
LYS 309 0.35 VAL 4 -0.08 PRO 266
LYS 309 0.40 TYR 5 -0.09 ARG 202
ALA 173 0.39 ASN 6 -0.11 ARG 202
THR 138 0.40 GLY 7 -0.13 GLU 203
LYS 174 0.37 GLN 8 -0.12 ARG 202
LYS 174 0.46 HIS 9 -0.16 ARG 202
LYS 174 0.49 LYS 10 -0.17 ARG 202
SER 176 0.42 GLU 11 -0.17 LYS 10
LYS 174 0.33 ALA 12 -0.10 VAL 261
LYS 174 0.37 ALA 13 -0.10 ALA 260
LYS 174 0.37 GLN 14 -0.13 ALA 260
VAL 177 0.31 ALA 15 -0.13 ALA 260
LYS 174 0.27 VAL 16 -0.15 PRO 279
ALA 173 0.31 ALA 17 -0.13 PRO 279
VAL 177 0.31 ASP 18 -0.13 PRO 279
VAL 177 0.26 ALA 19 -0.17 ALA 281
ALA 173 0.25 PHE 20 -0.17 ALA 281
ALA 173 0.28 THR 21 -0.15 ALA 281
VAL 177 0.25 ARG 22 -0.17 ALA 281
ALA 173 0.22 ALA 23 -0.19 ALA 281
ALA 173 0.23 THR 24 -0.18 ALA 281
ALA 173 0.26 GLY 25 -0.15 ALA 281
ALA 173 0.27 ILE 26 -0.14 ALA 281
ALA 173 0.31 LYS 27 -0.12 ALA 281
ALA 173 0.35 VAL 28 -0.10 ALA 281
ALA 173 0.38 LYS 29 -0.09 ALA 260
ALA 173 0.44 LEU 30 -0.09 ALA 260
ALA 173 0.46 ASN 31 -0.13 ARG 202
ALA 173 0.55 CYS 32 -0.15 GLU 203
ALA 173 0.53 ALA 33 -0.21 GLU 203
THR 138 0.57 LYS 34 -0.22 GLU 203
LYS 309 0.43 GLY 35 -0.15 GLU 203
LYS 309 0.51 ASP 36 -0.17 GLU 203
LYS 309 0.67 GLN 37 -0.18 GLU 203
LYS 309 0.53 LEU 38 -0.15 GLU 203
LYS 309 0.44 ALA 39 -0.13 GLU 203
LYS 309 0.56 GLY 40 -0.14 GLU 203
LYS 309 0.57 GLN 41 -0.14 GLU 203
LYS 309 0.45 ILE 42 -0.11 GLU 203
LYS 309 0.42 LYS 43 -0.11 GLU 203
LYS 309 0.50 GLU 44 -0.12 GLU 203
LYS 309 0.46 GLU 45 -0.10 GLU 203
LYS 309 0.38 GLY 46 -0.08 GLU 203
LYS 309 0.35 SER 47 -0.06 GLU 203
LYS 309 0.40 ARG 48 -0.08 GLU 203
LYS 309 0.42 SER 49 -0.08 GLU 203
LYS 309 0.41 PRO 50 -0.07 ARG 202
LYS 309 0.39 ALA 51 -0.07 ARG 202
LYS 309 0.32 ASP 52 -0.09 ALA 281
LYS 309 0.29 VAL 53 -0.09 ALA 281
LYS 309 0.31 PHE 54 -0.06 ALA 281
LYS 309 0.27 TYR 55 -0.07 ALA 281
LYS 309 0.26 SER 56 -0.09 GLU 203
SER 139 0.18 GLU 57 -0.10 GLU 203
LYS 309 0.14 GLN 58 -0.08 GLU 203
LYS 309 0.11 ILE 59 -0.07 GLU 203
LYS 309 0.12 PRO 60 -0.09 GLU 203
LYS 309 0.24 ALA 61 -0.11 GLU 203
LYS 309 0.19 LEU 62 -0.07 GLU 203
LYS 309 0.11 ALA 63 -0.08 GLU 203
GLU 297 0.17 THR 64 -0.10 GLU 203
LYS 309 0.24 LEU 65 -0.09 GLU 203
LYS 309 0.15 SER 66 -0.08 THR 292
LYS 309 0.10 ALA 67 -0.07 GLU 203
LYS 309 0.18 ALA 68 -0.08 GLU 203
LYS 309 0.17 ASN 69 -0.06 SER 289
LYS 309 0.24 LEU 70 -0.06 GLU 203
LYS 309 0.21 LEU 71 -0.09 SER 289
LYS 309 0.19 GLU 72 -0.13 SER 289
LYS 309 0.14 PRO 73 -0.17 SER 289
LYS 309 0.13 LEU 74 -0.19 SER 289
LYS 309 0.11 PRO 75 -0.19 SER 289
LYS 309 0.08 ALA 76 -0.22 SER 289
LYS 309 0.09 SER 77 -0.22 ALA 281
LYS 309 0.11 THR 78 -0.21 ALA 281
LYS 309 0.09 ILE 79 -0.22 SER 289
PRO 269 0.07 ASN 80 -0.26 LYS 85
LYS 174 0.09 GLU 81 -0.29 ALA 281
GLU 203 0.07 THR 82 -0.30 ALA 281
SER 273 0.09 ARG 83 -0.28 LYS 85
PHE 275 0.09 GLY 84 -0.54 LYS 85
ASN 276 0.12 LYS 85 -0.54 GLY 84
ALA 63 0.11 GLY 86 -0.37 PRO 286
LYS 85 0.07 VAL 87 -0.32 PRO 286
ALA 63 0.10 PRO 88 -0.31 SER 289
ALA 63 0.07 VAL 89 -0.36 SER 289
ALA 67 0.07 ALA 90 -0.30 SER 289
GLU 81 0.07 ALA 91 -0.32 SER 289
GLU 81 0.06 LYS 92 -0.23 SER 289
LYS 309 0.08 LYS 93 -0.25 SER 289
LYS 309 0.13 ASP 94 -0.17 SER 289
LYS 309 0.14 TRP 95 -0.16 SER 289
LYS 309 0.12 VAL 96 -0.19 SER 289
LYS 309 0.10 ALA 97 -0.16 ALA 285
LYS 174 0.11 LEU 98 -0.18 ALA 281
LYS 174 0.09 SER 99 -0.13 ALA 281
LYS 85 0.10 GLY 100 -0.15 ARG 101
GLN 287 0.09 ARG 101 -0.15 GLY 100
GLN 287 0.11 SER 102 -0.15 ARG 103
CYS 32 0.10 ARG 103 -0.16 PRO 269
CYS 32 0.10 VAL 104 -0.16 PRO 269
CYS 32 0.13 VAL 105 -0.15 PRO 269
GLU 11 0.13 VAL 106 -0.13 ASN 276
CYS 32 0.13 TYR 107 -0.15 ASN 276
GLU 11 0.13 ASP 108 -0.13 ASN 276
CYS 32 0.08 THR 109 -0.18 ASN 276
CYS 32 0.10 ARG 110 -0.14 ASN 276
CYS 32 0.13 LYS 111 -0.14 ASN 276
CYS 32 0.11 LEU 112 -0.17 ASN 276
CYS 32 0.08 SER 113 -0.21 ASN 276
LYS 119 0.08 GLU 114 -0.23 ASN 276
GLN 37 0.08 LYS 115 -0.24 VAL 272
GLN 37 0.11 ASP 116 -0.19 PRO 269
CYS 32 0.12 LEU 117 -0.20 PRO 269
GLN 37 0.14 GLU 118 -0.22 PRO 269
GLN 37 0.13 LYS 119 -0.24 PRO 269
GLN 37 0.16 SER 120 -0.23 PRO 269
GLN 37 0.18 VAL 121 -0.20 PRO 269
GLN 37 0.20 LEU 122 -0.19 PRO 269
GLN 37 0.20 ASN 123 -0.19 PRO 269
GLN 37 0.21 TYR 124 -0.16 PRO 269
GLN 37 0.26 ALA 125 -0.14 PRO 269
GLN 37 0.23 THR 126 -0.14 PRO 269
GLN 37 0.23 PRO 127 -0.13 PRO 269
CYS 32 0.20 LYS 128 -0.14 PRO 269
CYS 32 0.22 TRP 129 -0.13 PRO 269
CYS 32 0.25 LYS 130 -0.10 PRO 269
CYS 32 0.28 ASN 131 -0.08 PRO 269
CYS 32 0.24 ARG 132 -0.10 PRO 269
CYS 32 0.25 ILE 133 -0.10 PRO 269
CYS 32 0.30 GLY 134 -0.07 PRO 269
CYS 32 0.31 TYR 135 -0.08 THR 300
CYS 32 0.39 VAL 136 -0.10 THR 300
LYS 34 0.40 PRO 137 -0.16 THR 300
LYS 34 0.57 THR 138 -0.15 GLU 297
LYS 34 0.37 SER 139 -0.11 GLU 203
GLY 35 0.33 GLY 140 -0.11 GLU 203
GLY 35 0.19 ALA 141 -0.09 GLU 203
LYS 34 0.27 PHE 142 -0.09 ALA 91
ASP 36 0.32 LEU 143 -0.11 PRO 137
GLY 35 0.19 GLU 144 -0.13 ALA 91
GLN 37 0.20 GLN 145 -0.15 VAL 87
GLN 37 0.26 ILE 146 -0.15 ALA 91
GLY 40 0.22 VAL 147 -0.19 ALA 91
GLY 40 0.16 ALA 148 -0.22 VAL 87
GLY 40 0.19 ILE 149 -0.21 VAL 87
GLY 40 0.21 VAL 150 -0.22 ALA 91
GLY 40 0.17 LYS 151 -0.25 ALA 91
GLY 40 0.15 LEU 152 -0.24 VAL 87
GLY 40 0.17 LYS 153 -0.22 GLY 84
GLY 40 0.20 GLY 154 -0.22 ALA 91
GLY 40 0.24 GLU 155 -0.20 ALA 91
GLY 40 0.24 ALA 156 -0.18 ALA 91
GLN 37 0.23 ALA 157 -0.17 ALA 91
GLN 37 0.26 ALA 158 -0.16 ALA 91
GLN 37 0.31 LEU 159 -0.13 ALA 91
GLN 37 0.28 LYS 160 -0.13 PRO 269
GLN 37 0.27 TRP 161 -0.14 PRO 269
GLN 37 0.34 LEU 162 -0.10 ALA 91
GLN 37 0.34 LYS 163 -0.10 PRO 269
GLN 37 0.29 GLY 164 -0.12 PRO 269
GLN 37 0.31 LEU 165 -0.10 PRO 269
GLN 37 0.37 LYS 166 -0.07 PRO 269
GLN 37 0.32 GLU 167 -0.08 PRO 269
CYS 32 0.28 TYR 168 -0.09 PRO 269
CYS 32 0.30 GLY 169 -0.09 PRO 269
CYS 32 0.35 LYS 170 -0.09 MET 308
CYS 32 0.40 PRO 171 -0.14 MET 308
CYS 32 0.45 TYR 172 -0.11 THR 300
CYS 32 0.55 ALA 173 -0.11 LYS 204
LYS 10 0.49 LYS 174 -0.11 LYS 204
LYS 10 0.33 ASN 175 -0.10 GLU 203
GLU 11 0.42 SER 176 -0.14 LYS 204
LYS 10 0.44 VAL 177 -0.11 ASN 208
LYS 10 0.33 ALA 178 -0.09 GLU 297
GLU 11 0.29 LEU 179 -0.08 GLU 297
GLU 11 0.33 GLN 180 -0.11 ASN 208
GLU 11 0.30 ALA 181 -0.09 LYS 309
GLU 11 0.24 VAL 182 -0.07 LYS 309
GLU 11 0.22 GLU 183 -0.08 ASN 208
GLU 11 0.24 ASN 184 -0.09 ASN 208
GLU 11 0.21 GLY 185 -0.07 ASN 276
CYS 32 0.26 GLU 186 -0.08 LYS 309
CYS 32 0.25 ILE 187 -0.07 ASN 276
CYS 32 0.20 ASP 188 -0.11 ASN 276
CYS 32 0.19 ALA 189 -0.11 ASN 276
CYS 32 0.22 ALA 190 -0.09 PRO 269
CYS 32 0.20 LEU 191 -0.11 PRO 269
CYS 32 0.18 ILE 192 -0.07 PRO 269
GLU 11 0.11 ASN 193 -0.07 PRO 269
GLU 278 0.11 ASN 194 -0.08 VAL 272
GLU 278 0.12 TYR 195 -0.09 LYS 34
GLU 11 0.17 TYR 196 -0.12 PHE 200
GLU 11 0.10 TRP 197 -0.06 ASN 276
GLU 278 0.13 HIS 198 -0.10 LYS 34
VAL 261 0.27 ALA 199 -0.17 LYS 34
VAL 261 0.20 PHE 200 -0.14 LYS 34
GLU 278 0.13 ALA 201 -0.12 LYS 34
THR 274 0.20 ARG 202 -0.19 LYS 34
VAL 261 0.24 GLU 203 -0.22 LYS 34
ALA 260 0.16 LYS 204 -0.17 LYS 34
THR 274 0.14 GLY 205 -0.15 LYS 34
GLU 278 0.15 VAL 206 -0.10 LYS 34
LYS 282 0.13 GLN 207 -0.09 LYS 34
LYS 282 0.10 ASN 208 -0.11 VAL 177
ASP 18 0.09 VAL 209 -0.07 VAL 177
GLU 11 0.09 HIS 210 -0.11 ASN 276
GLU 11 0.11 THR 211 -0.13 ASN 276
PHE 215 0.09 ARG 212 -0.21 ASN 276
GLN 207 0.09 LEU 213 -0.21 ASN 276
VAL 216 0.10 ASN 214 -0.22 VAL 272
GLN 207 0.11 PHE 215 -0.25 PRO 269
ASN 214 0.10 VAL 216 -0.26 PRO 269
GLN 207 0.11 ARG 217 -0.31 PRO 269
GLN 207 0.11 HIS 218 -0.33 PRO 269
GLY 40 0.10 ARG 219 -0.32 PRO 269
GLY 40 0.12 ASP 220 -0.27 PRO 269
GLY 40 0.14 PRO 221 -0.24 PRO 269
GLN 37 0.14 GLY 222 -0.21 PRO 269
GLY 40 0.10 ALA 223 -0.26 PRO 269
GLY 40 0.10 LEU 224 -0.24 PRO 269
GLN 287 0.14 VAL 225 -0.19 PRO 269
GLN 287 0.10 THR 226 -0.12 PRO 269
LYS 309 0.08 TYR 227 -0.10 THR 226
LYS 309 0.13 SER 228 -0.06 ALA 285
LYS 309 0.15 GLY 229 -0.10 ALA 285
LYS 309 0.21 ALA 230 -0.10 ALA 281
LYS 309 0.22 ALA 231 -0.10 SER 289
LYS 309 0.24 VAL 232 -0.10 ALA 281
LYS 309 0.28 LEU 233 -0.07 ALA 281
LYS 309 0.25 LYS 234 -0.08 SER 289
LYS 309 0.30 SER 235 -0.06 ALA 281
LYS 309 0.30 SER 236 -0.08 ALA 281
LYS 309 0.29 GLN 237 -0.09 ALA 281
LYS 309 0.27 ASN 238 -0.11 ALA 281
LYS 309 0.24 LYS 239 -0.12 ALA 281
LYS 309 0.21 ASP 240 -0.14 ALA 281
LYS 309 0.23 GLU 241 -0.15 ALA 281
LYS 309 0.25 ALA 242 -0.13 ALA 281
LYS 309 0.20 LYS 243 -0.15 ALA 281
LYS 309 0.19 LYS 244 -0.18 ALA 281
ALA 173 0.22 PHE 245 -0.16 ALA 281
LYS 309 0.19 VAL 246 -0.17 ALA 281
ALA 173 0.16 ALA 247 -0.21 ALA 281
ALA 173 0.18 PHE 248 -0.22 ALA 281
LYS 174 0.18 LEU 249 -0.20 ALA 281
LYS 174 0.14 ALA 250 -0.25 ALA 281
LYS 174 0.14 GLY 251 -0.27 ALA 281
GLU 203 0.15 LYS 252 -0.31 ALA 281
GLU 203 0.17 GLU 253 -0.27 ALA 281
LYS 174 0.19 GLY 254 -0.22 ALA 281
LYS 174 0.16 GLN 255 -0.25 ALA 281
GLU 203 0.20 ARG 256 -0.26 PRO 279
VAL 177 0.21 ALA 257 -0.20 PRO 279
SER 176 0.21 LEU 258 -0.17 PRO 279
ALA 199 0.17 THR 259 -0.18 PRO 279
GLU 203 0.24 ALA 260 -0.16 PRO 279
ALA 199 0.27 VAL 261 -0.11 LYS 10
SER 176 0.21 ARG 262 -0.09 LYS 10
ALA 199 0.12 ALA 263 -0.09 ASN 214
LYS 85 0.09 GLU 264 -0.10 ASN 214
LYS 85 0.10 TYR 265 -0.17 ILE 280
LEU 267 0.11 PRO 266 -0.21 ALA 281
PRO 266 0.11 LEU 267 -0.34 ALA 281
GLU 203 0.10 ASN 268 -0.39 ALA 281
GLU 203 0.10 PRO 269 -0.54 ALA 281
GLU 203 0.13 HIS 270 -0.47 ALA 281
GLU 203 0.14 VAL 271 -0.43 ALA 281
GLU 203 0.14 VAL 272 -0.53 PRO 279
ARG 202 0.15 SER 273 -0.30 PRO 279
ARG 202 0.20 THR 274 -0.19 PRO 279
ARG 202 0.16 PHE 275 -0.16 GLU 114
ARG 202 0.14 ASN 276 -0.23 GLU 114
ARG 202 0.12 LEU 277 -0.21 VAL 272
VAL 206 0.15 GLU 278 -0.32 VAL 272
VAL 206 0.12 PRO 279 -0.53 VAL 272
GLN 287 0.13 ILE 280 -0.43 PRO 269
GLN 287 0.15 ALA 281 -0.54 PRO 269
GLN 207 0.13 LYS 282 -0.41 PRO 269
GLN 207 0.11 LEU 283 -0.36 PRO 269
GLN 207 0.11 GLU 284 -0.40 PRO 269
GLN 287 0.09 ALA 285 -0.36 PRO 269
GLY 40 0.09 PRO 286 -0.37 GLY 86
ALA 281 0.15 GLN 287 -0.31 GLY 86
GLY 40 0.10 VAL 288 -0.31 VAL 87
ALA 281 0.09 SER 289 -0.36 VAL 89
GLY 86 0.11 ALA 290 -0.29 VAL 89
GLY 40 0.12 THR 291 -0.23 ALA 91
GLY 40 0.10 THR 292 -0.25 ALA 91
GLY 40 0.13 VAL 293 -0.11 ALA 91
GLY 40 0.18 SER 294 -0.16 ALA 91
GLY 40 0.19 GLU 295 -0.20 ALA 91
GLY 40 0.27 LYS 296 -0.13 ALA 91
GLY 40 0.39 GLU 297 -0.15 THR 138
GLY 40 0.33 HIS 298 -0.15 ALA 91
GLY 40 0.35 ALA 299 -0.13 ALA 91
GLY 40 0.50 THR 300 -0.16 PRO 137
GLY 40 0.46 ARG 301 -0.09 PRO 171
GLY 40 0.39 LEU 302 -0.10 ALA 91
GLN 37 0.49 LEU 303 -0.11 PRO 171
GLN 37 0.52 GLU 304 -0.10 PRO 171
GLN 37 0.42 GLN 305 -0.08 ALA 91
GLN 37 0.42 ALA 306 -0.08 ALA 91
GLN 37 0.47 GLY 307 -0.09 PRO 171
GLN 37 0.54 MET 308 -0.14 PRO 171
GLN 37 0.67 LYS 309 -0.12 PRO 171

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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.