Should you encounter any unexpected behaviour,
please let us know.

* CHAPERONE 1SVT *

CA distance fluctuations for 2404010833281775939

--- normal mode 20 ---

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 increase ref largest decrease
GLY 110 0.16 ALA 2 -0.80 ARG 58

GLY 110 0.24 ALA 3 -0.61 ARG 58

ASP 5 0.38 LYS 4 -0.59 GLN 72

LYS 4 0.38 ASP 5 -0.43 GLN 72

GLY 110 0.30 VAL 6 -0.38 GLN 72

GLY 110 0.35 LYS 7 -0.25 GLN 72

GLY 110 0.40 PHE 8 -0.24 GLU 461

GLY 110 0.48 GLY 9 -0.21 GLU 461

ALA 108 0.41 ASN 10 -0.22 GLU 461

LYS 7 0.23 ASP 11 -0.27 GLU 461

LYS 7 0.21 ALA 12 -0.30 GLU 461

LYS 7 0.14 ARG 13 -0.32 GLU 461

LYS 7 0.15 VAL 14 -0.36 GLU 461

PRO 525 0.14 LYS 15 -0.38 GLU 461

THR 517 0.09 MET 16 -0.37 GLU 461

ILE 60 0.15 LEU 17 -0.42 GLU 461

ILE 60 0.19 ARG 18 -0.48 GLU 461

ALA 71 0.29 GLY 19 -0.43 GLU 461

ILE 60 0.16 VAL 20 -0.42 GLY 70

LEU 23 0.16 ASN 21 -0.49 LEU 456

ILE 60 0.18 VAL 22 -0.46 LEU 456

ASN 21 0.16 LEU 23 -0.48 ALA 2

GLN 97 0.14 ALA 24 -0.41 ALA 2

ALA 26 0.18 ASP 25 -0.48 LEU 456

ASP 25 0.18 ALA 26 -0.48 ALA 2

ALA 98 0.09 VAL 27 -0.51 ALA 2

ALA 446 0.07 LYS 28 -0.44 ALA 2

ALA 446 0.09 VAL 29 -0.45 ALA 2

ALA 446 0.07 THR 30 -0.47 ALA 2

PHE 44 0.08 LEU 31 -0.44 ALA 2

GLY 88 0.14 GLY 32 -0.41 ALA 2

SER 151 0.18 PRO 33 -0.40 ALA 2

CYS 458 0.11 LYS 34 -0.42 ALA 2

LYS 51 0.09 GLY 35 -0.43 ALA 2

ALA 446 0.06 ARG 36 -0.45 ALA 2

ALA 446 0.06 ASN 37 -0.49 ALA 2

ALA 443 0.05 VAL 38 -0.51 ALA 2

SER 55 0.07 VAL 39 -0.52 ALA 2

VAL 22 0.14 LEU 40 -0.59 ALA 2

ARG 58 0.23 ASP 41 -0.54 ALA 2

ASP 179 0.34 LYS 42 -0.62 ALA 2

ASP 179 0.37 SER 43 -0.54 ALA 2

ASP 179 0.57 PHE 44 -0.65 ALA 2

GLU 386 0.60 GLY 45 -0.60 ALA 2

GLU 386 0.26 ALA 46 -0.52 ALA 2

SER 55 0.17 PRO 47 -0.53 ALA 2

SER 55 0.19 THR 48 -0.56 ALA 2

GLY 45 0.09 ILE 49 -0.53 ALA 2

GLY 45 0.13 THR 50 -0.56 ALA 2

PHE 44 0.12 LYS 51 -0.53 ALA 2

PHE 44 0.20 ASP 52 -0.57 ALA 2

PHE 44 0.17 GLY 53 -0.57 ALA 2

PHE 44 0.25 VAL 54 -0.65 ALA 2

LYS 42 0.29 SER 55 -0.68 ALA 2

LYS 42 0.17 VAL 56 -0.63 ALA 2

LYS 42 0.19 ALA 57 -0.66 ALA 2

LYS 42 0.32 ARG 58 -0.80 ALA 2

ARG 58 0.22 GLU 59 -0.74 ALA 2

GLY 19 0.20 ILE 60 -0.62 ALA 2

GLY 19 0.16 GLU 61 -0.70 ASP 523

GLN 72 0.14 LEU 62 -0.45 GLY 459

ASN 68 0.16 GLU 63 -0.45 GLY 459

LYS 65 0.16 ASP 64 -0.42 GLY 459

ASP 64 0.16 LYS 65 -0.48 GLU 61

THR 517 0.16 PHE 66 -0.37 GLY 459

THR 517 0.12 GLU 67 -0.43 GLU 461

GLU 63 0.16 ASN 68 -0.44 THR 522

THR 517 0.15 MET 69 -0.60 THR 522

THR 517 0.15 GLY 70 -0.42 VAL 20

GLY 19 0.29 ALA 71 -0.52 THR 522

SER 43 0.17 GLN 72 -0.74 THR 522

SER 43 0.16 MET 73 -0.60 THR 522

SER 43 0.16 VAL 74 -0.51 ALA 2

LYS 42 0.21 LYS 75 -0.63 ALA 2

PHE 44 0.24 GLU 76 -0.66 ALA 2

PHE 44 0.22 VAL 77 -0.56 ALA 2

PHE 44 0.24 ALA 78 -0.60 ALA 2

PHE 44 0.30 SER 79 -0.69 ALA 2

PHE 44 0.29 LYS 80 -0.63 ALA 2

PHE 44 0.27 ALA 81 -0.56 ALA 2

PHE 44 0.32 ASN 82 -0.61 ALA 2

PHE 44 0.36 ASP 83 -0.63 ALA 2

PHE 44 0.31 ALA 84 -0.55 ALA 2

PHE 44 0.27 ALA 85 -0.52 ALA 2

PHE 44 0.30 GLY 86 -0.55 ALA 2

PHE 44 0.24 ASP 87 -0.53 ALA 2

PHE 44 0.19 GLY 88 -0.50 ALA 2

PHE 44 0.21 THR 89 -0.55 ALA 2

PHE 44 0.15 THR 90 -0.51 ALA 2

PHE 44 0.14 THR 91 -0.45 ALA 2

PHE 44 0.17 ALA 92 -0.46 ALA 2

PHE 44 0.15 THR 93 -0.48 ALA 2

PHE 44 0.11 VAL 94 -0.41 ALA 2

PHE 44 0.13 LEU 95 -0.36 ALA 2

PHE 44 0.14 ALA 96 -0.38 ALA 2

ALA 24 0.14 GLN 97 -0.33 THR 522

PHE 44 0.10 ALA 98 -0.43 ALA 449

PHE 44 0.12 ILE 99 -0.33 ALA 446

ALA 24 0.11 ILE 100 -0.32 SER 463

ASN 10 0.18 THR 101 -0.44 SER 463

ASN 10 0.19 GLU 102 -0.43 SER 463

ASN 10 0.18 GLY 103 -0.33 SER 463

ASN 10 0.26 LEU 104 -0.35 SER 463

ASN 10 0.33 LYS 105 -0.41 SER 463

GLY 9 0.28 ALA 106 -0.34 SER 463

GLY 9 0.33 VAL 107 -0.30 SER 463

GLY 9 0.43 ALA 108 -0.32 SER 463

GLY 9 0.36 ALA 109 -0.33 SER 463

GLY 9 0.48 GLY 110 -0.30 SER 463

GLY 9 0.36 MET 111 -0.28 SER 463

GLU 518 0.34 ASN 112 -0.24 SER 463

GLU 518 0.25 PRO 113 -0.24 SER 463

GLU 518 0.16 MET 114 -0.20 SER 463

GLU 518 0.15 ASP 115 -0.19 SER 463

GLY 9 0.17 LEU 116 -0.23 SER 463

PHE 44 0.14 LYS 117 -0.19 SER 463

PHE 44 0.15 ARG 118 -0.15 SER 463

PHE 44 0.13 GLY 119 -0.14 SER 463

PHE 44 0.14 ILE 120 -0.19 ALA 2

PHE 44 0.16 ASP 121 -0.23 ALA 2

PHE 44 0.15 LYS 122 -0.19 ALA 2

PHE 44 0.14 ALA 123 -0.20 ALA 2

PHE 44 0.16 VAL 124 -0.26 ALA 2

PHE 44 0.17 THR 125 -0.25 ALA 2

PHE 44 0.15 ALA 126 -0.23 ALA 2

PHE 44 0.15 ALA 127 -0.27 ALA 2

PHE 44 0.17 VAL 128 -0.30 ALA 2

PHE 44 0.16 GLU 129 -0.27 ALA 2

GLY 474 0.15 GLU 130 -0.26 ALA 2

PHE 44 0.15 LEU 131 -0.31 ALA 2

PHE 44 0.16 LYS 132 -0.30 ALA 2

GLY 474 0.19 ALA 133 -0.27 ALA 2

GLY 474 0.17 LEU 134 -0.29 ALA 2

PHE 44 0.15 SER 135 -0.32 ALA 2

ILE 489 0.16 VAL 136 -0.32 ALA 2

ILE 489 0.22 PRO 137 -0.34 ALA 2

ILE 489 0.19 CYS 138 -0.36 ALA 2

PHE 44 0.19 SER 139 -0.35 ALA 2

PHE 44 0.19 ASP 140 -0.34 ALA 2

PHE 44 0.19 SER 141 -0.36 ALA 2

THR 482 0.17 LYS 142 -0.36 ALA 2

THR 482 0.19 ALA 143 -0.37 ALA 2

PHE 44 0.20 ILE 144 -0.39 ALA 2

PHE 44 0.18 ALA 145 -0.40 ALA 2

THR 482 0.21 GLN 146 -0.40 ALA 2

ALA 481 0.20 VAL 147 -0.42 ALA 2

PHE 44 0.20 GLY 148 -0.44 ALA 2

ALA 481 0.20 THR 149 -0.43 ALA 2

ALA 481 0.27 ILE 150 -0.44 ALA 2

ALA 481 0.20 SER 151 -0.48 ALA 2

PHE 44 0.18 ALA 152 -0.47 ALA 2

PRO 33 0.13 ASN 153 -0.45 ALA 2

ALA 481 0.18 SER 154 -0.42 ALA 2

PHE 44 0.15 ASP 155 -0.42 ALA 2

PHE 44 0.17 GLU 156 -0.40 ALA 2

PHE 44 0.21 THR 157 -0.39 ALA 2

PHE 44 0.23 VAL 158 -0.42 ALA 2

PHE 44 0.21 GLY 159 -0.41 ALA 2

PHE 44 0.21 LYS 160 -0.39 ALA 2

PHE 44 0.26 LEU 161 -0.39 ALA 2

PHE 44 0.27 ILE 162 -0.41 ALA 2

PHE 44 0.24 ALA 163 -0.39 ALA 2

PHE 44 0.25 GLU 164 -0.37 ALA 2

PHE 44 0.29 ALA 165 -0.39 ALA 2

PHE 44 0.27 MET 166 -0.39 ALA 2

PHE 44 0.25 ASP 167 -0.37 ALA 2

PHE 44 0.27 LYS 168 -0.36 ALA 2

PHE 44 0.29 VAL 169 -0.38 ALA 2

PHE 44 0.26 GLY 170 -0.37 ALA 2

PHE 44 0.26 LYS 171 -0.38 ALA 2

PHE 44 0.28 GLU 172 -0.39 ALA 2

PHE 44 0.30 GLY 173 -0.41 ALA 2

PHE 44 0.33 VAL 174 -0.43 ALA 2

PHE 44 0.35 ILE 175 -0.43 ALA 2

PHE 44 0.41 THR 176 -0.45 ALA 2

PHE 44 0.44 VAL 177 -0.45 ALA 2

PHE 44 0.53 GLU 178 -0.43 ALA 2

PHE 44 0.57 ASP 179 -0.41 ALA 2

PHE 44 0.49 GLY 180 -0.38 ALA 2

PHE 44 0.49 THR 181 -0.34 ALA 2

PHE 44 0.40 GLY 182 -0.34 ALA 2

PHE 44 0.35 LEU 183 -0.36 ALA 2

PHE 44 0.33 GLN 184 -0.36 ALA 2

PHE 44 0.34 ASP 185 -0.39 ALA 2

PHE 44 0.35 GLU 186 -0.37 ALA 2

PHE 44 0.34 LEU 187 -0.37 ALA 2

PHE 44 0.36 ASP 188 -0.36 ALA 2

PHE 44 0.32 VAL 189 -0.37 ALA 2

PHE 44 0.31 VAL 190 -0.37 ALA 2

PHE 44 0.27 GLU 191 -0.36 ALA 2

PHE 44 0.26 GLY 192 -0.37 ALA 2

PHE 44 0.27 MET 193 -0.38 ALA 2

PHE 44 0.28 GLN 194 -0.40 ALA 2

PHE 44 0.30 PHE 195 -0.43 ALA 2

PHE 44 0.32 ASP 196 -0.45 ALA 2

PHE 44 0.29 ARG 197 -0.43 ALA 2

PHE 44 0.26 GLY 198 -0.41 ALA 2

PHE 44 0.23 TYR 199 -0.38 ALA 2

PHE 44 0.23 LEU 200 -0.38 ALA 2

PHE 44 0.21 SER 201 -0.36 ALA 2

PHE 44 0.20 PRO 202 -0.36 ALA 2

PHE 44 0.18 TYR 203 -0.34 ALA 2

PHE 44 0.19 PHE 204 -0.34 ALA 2

PHE 44 0.19 ILE 205 -0.35 ALA 2

PHE 44 0.18 ASN 206 -0.33 ALA 2

PHE 44 0.17 LYS 207 -0.34 ALA 2

PHE 44 0.17 PRO 208 -0.34 ALA 2

PHE 44 0.17 GLU 209 -0.35 ALA 2

PHE 44 0.19 THR 210 -0.36 ALA 2

PHE 44 0.20 GLY 211 -0.37 ALA 2

PHE 44 0.21 ALA 212 -0.37 ALA 2

PHE 44 0.20 VAL 213 -0.35 ALA 2

PHE 44 0.20 GLU 214 -0.34 ALA 2

PHE 44 0.19 LEU 215 -0.33 ALA 2

PHE 44 0.18 GLU 216 -0.32 ALA 2

PHE 44 0.18 SER 217 -0.32 ALA 2

PHE 44 0.19 PRO 218 -0.32 ALA 2

PHE 44 0.19 PHE 219 -0.32 ALA 2

PHE 44 0.20 ILE 220 -0.34 ALA 2

PHE 44 0.20 LEU 221 -0.34 ALA 2

PHE 44 0.22 LEU 222 -0.35 ALA 2

PHE 44 0.21 ALA 223 -0.35 ALA 2

PHE 44 0.22 ASP 224 -0.37 ALA 2

PHE 44 0.22 LYS 225 -0.36 ALA 2

PHE 44 0.21 LYS 226 -0.36 ALA 2

PHE 44 0.20 ILE 227 -0.34 ALA 2

PHE 44 0.19 SER 228 -0.33 ALA 2

PHE 44 0.18 ASN 229 -0.31 ALA 2

PHE 44 0.17 ILE 230 -0.30 ALA 2

PHE 44 0.17 ARG 231 -0.29 ALA 2

PHE 44 0.17 GLU 232 -0.30 ALA 2

PHE 44 0.18 MET 233 -0.30 ALA 2

PHE 44 0.17 LEU 234 -0.29 ALA 2

PHE 44 0.16 PRO 235 -0.28 ALA 2

PHE 44 0.17 VAL 236 -0.29 ALA 2

PHE 44 0.17 LEU 237 -0.30 ALA 2

PHE 44 0.16 GLU 238 -0.28 ALA 2

PHE 44 0.16 ALA 239 -0.28 ALA 2

PHE 44 0.17 VAL 240 -0.29 ALA 2

PHE 44 0.16 ALA 241 -0.28 ALA 2

PHE 44 0.15 LYS 242 -0.27 ALA 2

PHE 44 0.16 ALA 243 -0.28 ALA 2

PHE 44 0.16 GLY 244 -0.29 ALA 2

PHE 44 0.17 LYS 245 -0.30 ALA 2

PHE 44 0.18 PRO 246 -0.31 ALA 2

PHE 44 0.19 LEU 247 -0.33 ALA 2

PHE 44 0.21 LEU 248 -0.34 ALA 2

PHE 44 0.21 ILE 249 -0.35 ALA 2

PHE 44 0.23 ILE 250 -0.37 ALA 2

PHE 44 0.23 ALA 251 -0.37 ALA 2

PHE 44 0.24 GLU 252 -0.39 ALA 2

PHE 44 0.23 ASP 253 -0.38 ALA 2

PHE 44 0.22 VAL 254 -0.36 ALA 2

PHE 44 0.21 GLU 255 -0.36 ALA 2

PHE 44 0.19 GLY 256 -0.34 ALA 2

PHE 44 0.18 GLU 257 -0.32 ALA 2

PHE 44 0.19 ALA 258 -0.32 ALA 2

PHE 44 0.19 LEU 259 -0.34 ALA 2

PHE 44 0.18 ALA 260 -0.32 ALA 2

PHE 44 0.17 THR 261 -0.31 ALA 2

PHE 44 0.18 LEU 262 -0.32 ALA 2

PHE 44 0.18 VAL 263 -0.32 ALA 2

PHE 44 0.16 VAL 264 -0.30 ALA 2

PHE 44 0.16 ASN 265 -0.30 ALA 2

PHE 44 0.17 THR 266 -0.31 ALA 2

PHE 44 0.16 MET 267 -0.31 ALA 2

PHE 44 0.15 ARG 268 -0.29 ALA 2

PHE 44 0.15 GLY 269 -0.29 ALA 2

PHE 44 0.15 ILE 270 -0.29 ALA 2

PHE 44 0.16 VAL 271 -0.30 ALA 2

PHE 44 0.17 LYS 272 -0.31 ALA 2

PHE 44 0.19 VAL 273 -0.33 ALA 2

PHE 44 0.20 ALA 274 -0.35 ALA 2

PHE 44 0.22 ALA 275 -0.36 ALA 2

PHE 44 0.24 VAL 276 -0.39 ALA 2

PHE 44 0.26 LYS 277 -0.41 ALA 2

PHE 44 0.26 ALA 278 -0.41 ALA 2

PHE 44 0.29 PRO 279 -0.44 ALA 2

PHE 44 0.31 GLY 280 -0.47 ALA 2

PHE 44 0.29 PHE 281 -0.47 ALA 2

PHE 44 0.27 GLY 282 -0.46 ALA 2

PHE 44 0.26 ASP 283 -0.44 ALA 2

PHE 44 0.28 ARG 284 -0.44 ALA 2

PHE 44 0.27 ARG 285 -0.43 ALA 2

PHE 44 0.25 LYS 286 -0.40 ALA 2

PHE 44 0.25 ALA 287 -0.40 ALA 2

PHE 44 0.27 MET 288 -0.41 ALA 2

PHE 44 0.25 LEU 289 -0.39 ALA 2

PHE 44 0.23 GLN 290 -0.37 ALA 2

PHE 44 0.24 ASP 291 -0.38 ALA 2

PHE 44 0.24 ILE 292 -0.37 ALA 2

PHE 44 0.22 ALA 293 -0.35 ALA 2

PHE 44 0.22 THR 294 -0.35 ALA 2

PHE 44 0.23 LEU 295 -0.35 ALA 2

PHE 44 0.21 THR 296 -0.34 ALA 2

PHE 44 0.20 GLY 297 -0.32 ALA 2

PHE 44 0.20 GLY 298 -0.33 ALA 2

PHE 44 0.20 THR 299 -0.33 ALA 2

PHE 44 0.21 VAL 300 -0.34 ALA 2

PHE 44 0.20 ILE 301 -0.33 ALA 2

PHE 44 0.20 SER 302 -0.34 ALA 2

PHE 44 0.19 GLU 303 -0.33 ALA 2

PHE 44 0.19 GLU 304 -0.34 ALA 2

PHE 44 0.18 ILE 305 -0.32 ALA 2

PHE 44 0.18 GLY 306 -0.30 ALA 2

PHE 44 0.18 MET 307 -0.31 ALA 2

PHE 44 0.18 GLU 308 -0.30 ALA 2

PHE 44 0.18 LEU 309 -0.31 ALA 2

PHE 44 0.17 GLU 310 -0.29 ALA 2

PHE 44 0.17 LYS 311 -0.28 ALA 2

PHE 44 0.18 ALA 312 -0.30 ALA 2

PHE 44 0.17 THR 313 -0.29 ALA 2

PHE 44 0.17 LEU 314 -0.29 ALA 2

PHE 44 0.17 GLU 315 -0.30 ALA 2

PHE 44 0.19 ASP 316 -0.31 ALA 2

PHE 44 0.19 LEU 317 -0.32 ALA 2

PHE 44 0.20 GLY 318 -0.33 ALA 2

PHE 44 0.20 GLN 319 -0.32 ALA 2

PHE 44 0.20 ALA 320 -0.33 ALA 2

PHE 44 0.19 LYS 321 -0.32 ALA 2

PHE 44 0.20 ARG 322 -0.34 ALA 2

PHE 44 0.22 VAL 323 -0.35 ALA 2

PHE 44 0.22 VAL 324 -0.37 ALA 2

PHE 44 0.24 ILE 325 -0.38 ALA 2

PHE 44 0.25 ASN 326 -0.39 ALA 2

PHE 44 0.25 LYS 327 -0.41 ALA 2

PHE 44 0.29 ASP 328 -0.43 ALA 2

PHE 44 0.28 THR 329 -0.42 ALA 2

PHE 44 0.26 THR 330 -0.40 ALA 2

PHE 44 0.25 THR 331 -0.39 ALA 2

PHE 44 0.24 ILE 332 -0.37 ALA 2

PHE 44 0.23 ILE 333 -0.35 ALA 2

PHE 44 0.21 ASP 334 -0.34 ALA 2

PHE 44 0.21 GLY 335 -0.33 ALA 2

PHE 44 0.20 VAL 336 -0.32 ALA 2

PHE 44 0.21 GLY 337 -0.32 ALA 2

PHE 44 0.21 GLU 338 -0.31 ALA 2

PHE 44 0.23 GLU 339 -0.30 ALA 2

PHE 44 0.21 ALA 340 -0.30 ALA 2

PHE 44 0.21 ALA 341 -0.32 ALA 2

PHE 44 0.23 ILE 342 -0.33 ALA 2

PHE 44 0.23 GLN 343 -0.33 ALA 2

PHE 44 0.22 GLY 344 -0.33 ALA 2

PHE 44 0.23 ARG 345 -0.35 ALA 2

PHE 44 0.25 VAL 346 -0.35 ALA 2

PHE 44 0.24 ALA 347 -0.34 ALA 2

PHE 44 0.23 GLN 348 -0.35 ALA 2

PHE 44 0.26 ILE 349 -0.38 ALA 2

PHE 44 0.26 ARG 350 -0.37 ALA 2

PHE 44 0.24 GLN 351 -0.36 ALA 2

PHE 44 0.26 GLN 352 -0.40 ALA 2

PHE 44 0.28 ILE 353 -0.41 ALA 2

PHE 44 0.25 GLU 354 -0.38 ALA 2

PHE 44 0.25 GLU 355 -0.39 ALA 2

PHE 44 0.28 ALA 356 -0.44 ALA 2

PHE 44 0.27 THR 357 -0.45 ALA 2

PHE 44 0.30 SER 358 -0.51 ALA 2

PHE 44 0.34 ASP 359 -0.53 ALA 2

PHE 44 0.37 TYR 360 -0.55 ALA 2

PHE 44 0.32 ASP 361 -0.50 ALA 2

PHE 44 0.32 ARG 362 -0.47 ALA 2

PHE 44 0.36 GLU 363 -0.49 ALA 2

PHE 44 0.34 LYS 364 -0.48 ALA 2

PHE 44 0.31 LEU 365 -0.44 ALA 2

PHE 44 0.31 GLN 366 -0.43 ALA 2

PHE 44 0.33 GLU 367 -0.44 ALA 2

PHE 44 0.30 ARG 368 -0.42 ALA 2

PHE 44 0.28 VAL 369 -0.40 ALA 2

PHE 44 0.30 ALA 370 -0.40 ALA 2

PHE 44 0.29 LYS 371 -0.40 ALA 2

PHE 44 0.27 LEU 372 -0.37 ALA 2

PHE 44 0.26 ALA 373 -0.36 ALA 2

PHE 44 0.27 GLY 374 -0.37 ALA 2

PHE 44 0.30 GLY 375 -0.38 ALA 2

PHE 44 0.33 VAL 376 -0.40 ALA 2

PHE 44 0.35 ALA 377 -0.40 ALA 2

PHE 44 0.40 VAL 378 -0.40 ALA 2

PHE 44 0.39 ILE 379 -0.41 ALA 2

PHE 44 0.43 LYS 380 -0.40 ALA 2

PHE 44 0.41 VAL 381 -0.42 ALA 2

PHE 44 0.39 GLY 382 -0.39 ALA 2

GLY 45 0.38 ALA 383 -0.40 ALA 2

GLY 45 0.38 ALA 384 -0.37 ALA 2

GLY 45 0.48 THR 385 -0.38 ALA 2

GLY 45 0.60 GLU 386 -0.41 ALA 2

GLY 45 0.41 VAL 387 -0.46 ALA 2

GLY 45 0.35 GLU 388 -0.45 ALA 2

GLY 45 0.44 MET 389 -0.45 ALA 2

PHE 44 0.43 LYS 390 -0.50 ALA 2

PHE 44 0.27 GLU 391 -0.51 ALA 2

PHE 44 0.30 LYS 392 -0.48 ALA 2

PHE 44 0.40 LYS 393 -0.49 ALA 2

PHE 44 0.34 ALA 394 -0.53 ALA 2

PHE 44 0.26 ARG 395 -0.51 ALA 2

PHE 44 0.31 VAL 396 -0.48 ALA 2

PHE 44 0.36 GLU 397 -0.51 ALA 2

PHE 44 0.28 ASP 398 -0.53 ALA 2

PHE 44 0.25 ALA 399 -0.48 ALA 2

PHE 44 0.30 LEU 400 -0.47 ALA 2

PHE 44 0.29 HIS 401 -0.50 ALA 2

PHE 44 0.24 ALA 402 -0.47 ALA 2

PHE 44 0.23 THR 403 -0.44 ALA 2

PHE 44 0.27 ARG 404 -0.44 ALA 2

PHE 44 0.24 ALA 405 -0.44 ALA 2

PHE 44 0.21 ALA 406 -0.41 ALA 2

PHE 44 0.22 VAL 407 -0.39 ALA 2

PHE 44 0.24 GLU 408 -0.39 ALA 2

PHE 44 0.21 GLU 409 -0.38 ALA 2

PHE 44 0.18 GLY 410 -0.36 ALA 2

PHE 44 0.16 VAL 411 -0.37 ALA 2

PHE 44 0.14 VAL 412 -0.35 ALA 2

GLY 477 0.15 ALA 413 -0.34 ALA 2

ALA 480 0.17 GLY 414 -0.38 ALA 2

ALA 480 0.19 GLY 415 -0.38 ALA 2

ALA 480 0.12 GLY 416 -0.37 ALA 2

VAL 465 0.10 VAL 417 -0.32 ALA 2

PHE 44 0.12 ALA 418 -0.31 ALA 2

PHE 44 0.12 LEU 419 -0.31 ALA 2

PHE 44 0.09 ILE 420 -0.28 ALA 2

GLU 130 0.11 ARG 421 -0.26 ALA 2

PHE 44 0.12 VAL 422 -0.25 ALA 2

PHE 44 0.11 ALA 423 -0.22 ALA 2

PHE 44 0.10 SER 424 -0.19 ALA 2

PHE 44 0.11 LYS 425 -0.19 ALA 2

PHE 44 0.12 LEU 426 -0.17 ALA 2

PHE 44 0.11 ALA 427 -0.14 ALA 2

GLY 9 0.12 ASP 428 -0.11 ALA 2

GLY 9 0.12 LEU 429 -0.12 ALA 2

GLY 9 0.14 ARG 430 -0.08 ALA 2

GLY 9 0.14 GLY 431 -0.09 SER 463

GLY 9 0.14 GLN 432 -0.10 SER 463

GLY 9 0.18 ASN 433 -0.14 SER 463

GLY 9 0.22 GLU 434 -0.18 ASN 467

GLY 9 0.24 ASP 435 -0.21 SER 463

GLY 9 0.17 GLN 436 -0.17 SER 463

GLY 9 0.18 ASN 437 -0.16 ASN 467

GLY 9 0.21 VAL 438 -0.23 ASN 467

GLY 9 0.17 GLY 439 -0.20 SER 463

ASN 10 0.13 ILE 440 -0.14 ASN 467

ASN 10 0.15 LYS 441 -0.21 ASN 467

ASN 10 0.15 VAL 442 -0.25 SER 463

PHE 44 0.13 ALA 443 -0.21 ALA 2

PHE 44 0.11 LEU 444 -0.20 ALA 2

ALA 446 0.18 ARG 445 -0.26 LYS 470

ARG 445 0.18 ALA 446 -0.33 ILE 99

PHE 44 0.11 MET 447 -0.29 ALA 2

PHE 44 0.07 GLU 448 -0.29 ALA 2

GLN 453 0.07 ALA 449 -0.43 ALA 98

PHE 44 0.08 PRO 450 -0.38 ALA 2

GLY 88 0.08 LEU 451 -0.34 ALA 2

SER 424 0.06 ARG 452 -0.39 ASN 21

ALA 449 0.07 GLN 453 -0.43 ASN 21

GLY 88 0.10 ILE 454 -0.38 ALA 2

ASP 87 0.09 VAL 455 -0.38 ASN 21

SER 424 0.06 LEU 456 -0.49 ASN 21

ALA 394 0.06 ASN 457 -0.47 ASP 25

SER 154 0.12 CYS 458 -0.41 ASP 25

SER 154 0.11 GLY 459 -0.46 VAL 22

SER 154 0.09 GLU 460 -0.43 ASN 21

GLY 415 0.08 GLU 461 -0.48 ARG 18

SER 424 0.06 PRO 462 -0.46 ASN 21

SER 424 0.07 SER 463 -0.44 THR 101

ALA 413 0.06 VAL 464 -0.39 ARG 18

GLY 415 0.10 VAL 465 -0.34 ARG 18

SER 424 0.08 ALA 466 -0.32 THR 101

LYS 425 0.06 ASN 467 -0.33 GLU 102

ALA 133 0.08 THR 468 -0.28 ARG 18

ALA 133 0.09 VAL 469 -0.29 ALA 2

GLU 130 0.08 LYS 470 -0.26 ARG 445

ALA 133 0.08 GLY 471 -0.24 ALA 2

ALA 133 0.11 GLY 472 -0.25 ALA 2

ALA 133 0.15 ASP 473 -0.24 ALA 2

ALA 133 0.19 GLY 474 -0.26 ALA 2

ALA 133 0.14 ASN 475 -0.29 ALA 2

ALA 133 0.12 TYR 476 -0.30 ALA 2

ALA 413 0.15 GLY 477 -0.32 ALA 2

ALA 413 0.14 TYR 478 -0.33 ALA 2

GLY 414 0.17 ASN 479 -0.35 ALA 2

GLY 415 0.19 ALA 480 -0.37 ALA 2

ILE 150 0.27 ALA 481 -0.37 ALA 2

ILE 150 0.21 THR 482 -0.35 ALA 2

ILE 150 0.15 GLU 483 -0.34 ALA 2

CYS 138 0.14 GLU 484 -0.32 ALA 2

PRO 137 0.12 TYR 485 -0.31 ALA 2

PRO 137 0.14 GLY 486 -0.31 ALA 2

PRO 137 0.16 ASN 487 -0.31 ALA 2

PRO 137 0.16 MET 488 -0.34 ALA 2

PRO 137 0.22 ILE 489 -0.34 ALA 2

PRO 137 0.19 ASP 490 -0.33 ALA 2

PRO 137 0.16 MET 491 -0.36 ALA 2

CYS 138 0.19 GLY 492 -0.38 ALA 2

LEU 494 0.19 ILE 493 -0.39 ALA 2

ALA 481 0.19 LEU 494 -0.39 ALA 2

ALA 481 0.18 ASP 495 -0.41 ALA 2

PHE 44 0.19 PRO 496 -0.41 ALA 2

PHE 44 0.18 THR 497 -0.39 ALA 2

PHE 44 0.22 LYS 498 -0.41 ALA 2

PHE 44 0.21 VAL 499 -0.45 ALA 2

PHE 44 0.18 THR 500 -0.41 ALA 2

PHE 44 0.19 ARG 501 -0.39 ALA 2

PHE 44 0.22 SER 502 -0.44 ALA 2

PHE 44 0.20 ALA 503 -0.45 ALA 2

PHE 44 0.18 LEU 504 -0.39 ALA 2

PHE 44 0.20 GLN 505 -0.39 ALA 2

PHE 44 0.22 TYR 506 -0.46 ALA 2

PHE 44 0.18 ALA 507 -0.42 ALA 2

PHE 44 0.17 ALA 508 -0.34 ALA 2

PHE 44 0.19 SER 509 -0.39 ALA 2

PHE 44 0.19 VAL 510 -0.42 ALA 2

PHE 44 0.15 ALA 511 -0.32 ALA 2

PHE 44 0.16 GLY 512 -0.25 ALA 2

PHE 44 0.16 LEU 513 -0.26 ALA 2

SER 43 0.14 MET 514 -0.25 SER 463

SER 43 0.12 ILE 515 -0.28 SER 463

PRO 113 0.13 THR 516 -0.24 SER 463

PHE 66 0.16 THR 517 -0.25 SER 463

GLY 110 0.35 GLU 518 -0.24 GLU 461

GLY 110 0.31 CYS 519 -0.25 GLU 461

GLY 110 0.22 MET 520 -0.35 MET 73

GLY 110 0.22 VAL 521 -0.54 GLN 72

GLY 110 0.15 THR 522 -0.74 GLN 72

GLY 110 0.16 ASP 523 -0.70 GLU 61

GLY 110 0.21 LEU 524 -0.52 GLU 61

GLY 110 0.17 PRO 525 -0.40 GLU 61

If you find results from this site helpful for your research, please cite one of our papers:

K. Suhre & Y.H. Sanejouand, ElNemo: a normal mode web-server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Research, 32, W610-W614, 2004.
K. Suhre & Y.H. Sanejouand, On the potential of normal mode analysis for solving difficult molecular replacement problems. Acta Cryst. D vol.60, p796-799, 2004 © International Union of Crystallography.

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: April 25th, 2023.

Should you encounter any unexpected behaviour, please let us know.

*** CHAPERONE 1SVT ***

CA distance fluctuations for 2404010833281775939

--- normal mode 20 ---

Should you encounter any unexpected behaviour,
please let us know.

* CHAPERONE 1SVT *