Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* 6csc_aligned_close *

CA distance fluctuations for 2604241133101949041

--- normal mode 16 ---

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 312 0.06 ALA 1 -0.09 ILE 21

GLY 312 0.05 SER 2 -0.09 LYS 339

SER 424 0.05 SER 3 -0.09 LYS 339

SER 424 0.05 THR 4 -0.09 LYS 339

SER 424 0.06 ASN 5 -0.08 LYS 339

GLY 312 0.07 LEU 6 -0.09 GLY 29

SER 424 0.07 LYS 7 -0.08 GLY 29

SER 424 0.07 ASP 8 -0.08 LYS 166

GLY 312 0.07 VAL 9 -0.08 LYS 339

GLY 312 0.09 LEU 10 -0.09 GLY 29

GLY 312 0.09 ALA 11 -0.11 LYS 166

PRO 422 0.10 SER 12 -0.08 THR 165

PRO 422 0.11 LEU 13 -0.08 THR 165

PRO 422 0.13 ILE 14 -0.09 THR 165

PRO 422 0.15 PRO 15 -0.10 THR 165

PRO 422 0.16 LYS 16 -0.06 THR 165

PRO 422 0.18 GLU 17 -0.08 ILE 21

PRO 422 0.20 GLN 18 -0.07 GLY 29

PRO 422 0.20 ALA 19 -0.06 LYS 339

PRO 422 0.22 ARG 20 -0.07 GLN 100

PRO 422 0.26 ILE 21 -0.14 GLY 99

PRO 422 0.25 LYS 22 -0.09 GLU 54

PRO 422 0.22 THR 23 -0.08 GLY 68

PRO 422 0.23 PHE 24 -0.12 GLU 54

PRO 422 0.25 ARG 25 -0.20 GLU 54

PRO 422 0.18 GLN 26 -0.16 ILE 52

PRO 422 0.17 GLN 27 -0.15 GLY 50

PRO 422 0.20 HIS 28 -0.20 GLY 50

PRO 422 0.20 GLY 29 -0.37 ILE 52

PRO 422 0.14 ASN 30 -0.37 GLY 50

PRO 422 0.22 THR 31 -0.23 GLY 50

PRO 422 0.27 ALA 32 -0.23 GLY 50

PRO 422 0.42 VAL 33 -0.18 ASP 59

PRO 422 0.40 GLY 34 -0.18 ASP 61

PRO 422 0.41 GLN 35 -0.18 ASP 61

LYS 423 0.43 ILE 36 -0.15 ASP 61

LYS 423 0.30 THR 37 -0.15 ASP 61

GLY 312 0.30 VAL 38 -0.13 ASP 61

GLY 312 0.33 ASP 39 -0.14 PRO 60

GLY 312 0.33 MET 40 -0.15 PRO 60

GLY 312 0.33 SER 41 -0.16 ASN 30

GLY 312 0.39 TYR 42 -0.14 SER 426

GLY 312 0.41 GLY 43 -0.14 PRO 422

GLY 312 0.40 GLY 44 -0.28 PRO 422

GLY 312 0.34 MET 45 -0.21 ASN 30

GLY 312 0.33 ARG 46 -0.16 ASN 30

GLY 312 0.28 GLY 47 -0.22 PRO 60

GLY 312 0.27 MET 48 -0.20 ASN 30

GLY 312 0.23 LYS 49 -0.25 ASN 30

PRO 422 0.28 GLY 50 -0.37 ASN 30

GLY 312 0.20 LEU 51 -0.33 GLY 29

GLY 312 0.18 ILE 52 -0.37 GLY 29

GLY 312 0.16 TYR 53 -0.29 GLY 29

GLY 312 0.13 GLU 54 -0.27 GLY 29

GLY 312 0.11 THR 55 -0.22 GLY 29

GLY 312 0.12 SER 56 -0.22 GLY 29

GLY 312 0.14 VAL 57 -0.23 GLY 29

GLY 312 0.13 LEU 58 -0.20 GLY 29

GLY 312 0.12 ASP 59 -0.20 GLY 47

GLY 312 0.13 PRO 60 -0.22 GLY 47

GLY 312 0.11 ASP 61 -0.18 GLN 35

GLY 312 0.09 GLU 62 -0.16 VAL 33

GLY 312 0.10 GLY 63 -0.17 GLY 29

GLY 312 0.10 ILE 64 -0.18 GLY 29

GLY 312 0.09 ARG 65 -0.19 GLY 29

GLY 312 0.08 PHE 66 -0.19 GLY 29

GLY 312 0.09 ARG 67 -0.19 GLY 29

GLY 312 0.09 GLY 68 -0.19 GLY 29

GLY 312 0.07 PHE 69 -0.16 GLY 29

GLY 312 0.06 SER 70 -0.16 GLY 29

LEU 230 0.04 ILE 71 -0.15 GLY 29

GLU 226 0.05 PRO 72 -0.13 GLY 29

ASP 59 0.04 GLU 73 -0.13 GLY 29

GLY 312 0.03 CYS 74 -0.14 GLY 29

GLU 226 0.03 GLN 75 -0.16 GLU 335

ASP 59 0.03 LYS 76 -0.17 LYS 339

ASP 59 0.03 LEU 77 -0.15 LYS 339

ASP 59 0.03 LEU 78 -0.15 LYS 339

ASN 212 0.02 PRO 79 -0.16 LYS 339

SER 210 0.03 LYS 80 -0.18 LYS 339

HIS 211 0.04 ALA 81 -0.17 LYS 339

ASN 212 0.04 GLY 82 -0.17 LYS 339

HIS 211 0.04 GLY 84 -0.23 LYS 339

PRO 222 0.04 GLU 85 -0.28 LYS 339

SER 210 0.03 GLU 86 -0.22 LYS 339

SER 210 0.03 PRO 87 -0.16 LYS 339

SER 210 0.03 LEU 88 -0.13 LYS 339

SER 70 0.03 PRO 89 -0.13 GLY 29

GLY 312 0.03 GLU 90 -0.12 GLY 29

GLY 312 0.03 GLY 91 -0.12 GLY 29

GLY 312 0.05 LEU 92 -0.14 GLY 29

GLY 312 0.06 PHE 93 -0.15 GLY 29

GLY 312 0.06 TRP 94 -0.13 GLY 29

GLY 312 0.06 LEU 95 -0.15 GLY 29

GLY 312 0.08 LEU 96 -0.17 GLY 29

GLY 312 0.09 VAL 97 -0.16 GLY 29

GLY 312 0.08 THR 98 -0.14 GLY 29

GLY 312 0.08 GLY 99 -0.16 GLY 29

GLY 312 0.07 GLN 100 -0.13 GLY 29

GLY 312 0.05 ILE 101 -0.12 GLY 29

GLY 312 0.04 PRO 102 -0.11 LYS 339

GLY 312 0.03 THR 103 -0.12 LYS 339

LYS 206 0.03 PRO 104 -0.13 LYS 339

SER 424 0.03 GLU 105 -0.12 LYS 339

SER 424 0.04 GLN 106 -0.11 LYS 339

SER 424 0.03 VAL 107 -0.11 LYS 339

SER 424 0.03 SER 108 -0.11 LYS 339

SER 424 0.04 TRP 109 -0.10 LYS 339

SER 424 0.03 VAL 110 -0.10 GLY 29

SER 424 0.02 SER 111 -0.10 GLY 29

SER 424 0.03 LYS 112 -0.09 GLY 29

SER 424 0.03 GLU 113 -0.09 GLY 29

ARG 313 0.03 TRP 114 -0.10 GLY 29

SER 426 0.02 ALA 115 -0.09 GLY 29

SER 426 0.03 LYS 116 -0.09 GLY 29

SER 426 0.04 ARG 117 -0.09 GLY 29

ILE 36 0.03 ALA 118 -0.09 GLY 29

ILE 36 0.03 ALA 119 -0.09 ASN 30

TYR 304 0.04 LEU 120 -0.10 PRO 422

TYR 304 0.05 PRO 121 -0.10 PRO 422

TYR 304 0.05 SER 122 -0.11 PRO 422

TYR 304 0.07 HIS 123 -0.13 PRO 422

TYR 304 0.07 VAL 124 -0.14 PRO 422

TYR 304 0.06 VAL 125 -0.13 PRO 422

TYR 304 0.06 THR 126 -0.13 PRO 422

TYR 304 0.08 MET 127 -0.15 PRO 422

TYR 304 0.07 LEU 128 -0.15 PRO 422

LYS 300 0.06 ASP 129 -0.14 PRO 422

ASP 291 0.08 ASN 130 -0.16 PRO 422

ASP 291 0.09 PHE 131 -0.17 PRO 422

ASP 291 0.11 PRO 132 -0.17 PRO 422

ASP 291 0.11 THR 133 -0.17 PRO 422

ASP 291 0.14 ASN 134 -0.18 PRO 422

GLN 287 0.12 LEU 135 -0.20 PRO 422

GLN 287 0.12 HIS 136 -0.19 PRO 422

TYR 304 0.09 PRO 137 -0.18 PRO 422

TYR 304 0.11 MET 138 -0.19 PRO 422

TYR 304 0.12 SER 139 -0.21 PRO 422

TYR 304 0.10 GLN 140 -0.19 PRO 422

TYR 304 0.08 LEU 141 -0.18 PRO 422

TYR 304 0.10 SER 142 -0.21 PRO 422

TYR 304 0.10 ALA 143 -0.20 PRO 422

TYR 304 0.08 ALA 144 -0.17 PRO 422

TYR 304 0.08 ILE 145 -0.17 PRO 422

ARG 313 0.10 THR 146 -0.19 PRO 422

TYR 304 0.09 ALA 147 -0.16 PRO 422

TYR 304 0.07 LEU 148 -0.14 PRO 422

ARG 313 0.09 ASN 149 -0.13 PRO 422

ARG 313 0.08 SER 150 -0.12 PRO 422

ARG 313 0.07 GLU 151 -0.10 ASN 30

ARG 313 0.08 SER 152 -0.11 ASN 30

SER 426 0.08 ASN 153 -0.10 ASN 30

GLY 312 0.10 PHE 154 -0.11 ASN 30

GLY 312 0.11 ALA 155 -0.11 ASN 30

SER 426 0.11 ARG 156 -0.09 ASN 30

SER 426 0.12 ALA 157 -0.09 ASN 30

SER 426 0.14 TYR 158 -0.10 ASN 30

SER 426 0.17 ALA 159 -0.08 ASN 30

SER 426 0.16 GLU 160 -0.07 ASP 8

SER 424 0.19 GLY 161 -0.08 ASP 8

SER 424 0.17 ILE 162 -0.08 ALA 11

SER 424 0.18 ASN 163 -0.09 ALA 11

SER 424 0.19 ARG 164 -0.07 PRO 15

SER 424 0.16 THR 165 -0.10 PRO 15

SER 424 0.13 LYS 166 -0.11 ALA 11

SER 424 0.13 TYR 167 -0.10 ASN 30

GLY 312 0.11 TRP 168 -0.11 GLY 29

SER 424 0.09 GLU 169 -0.09 GLY 29

SER 424 0.09 PHE 170 -0.10 ASN 30

GLY 312 0.10 VAL 171 -0.12 GLY 29

GLY 312 0.08 TYR 172 -0.12 GLY 29

GLY 312 0.07 GLU 173 -0.10 GLY 29

ARG 313 0.08 ASP 174 -0.11 GLY 29

GLY 312 0.07 ALA 175 -0.13 GLY 29

GLY 312 0.05 MET 176 -0.12 GLY 29

ARG 313 0.05 ASP 177 -0.11 GLY 29

ARG 313 0.06 LEU 178 -0.12 GLY 29

ARG 313 0.05 ILE 179 -0.12 GLY 29

ARG 313 0.04 ALA 180 -0.11 GLY 29

ARG 313 0.04 LYS 181 -0.11 GLY 29

TYR 304 0.04 LEU 182 -0.12 PRO 422

TRP 209 0.03 PRO 183 -0.11 GLY 29

TYR 304 0.03 CYS 184 -0.11 PRO 422

TYR 304 0.05 VAL 185 -0.13 PRO 422

TYR 304 0.04 ALA 186 -0.13 PRO 422

LYS 300 0.03 ALA 187 -0.12 PRO 422

LYS 300 0.04 LYS 188 -0.13 PRO 422

LYS 300 0.06 ILE 189 -0.14 PRO 422

MET 387 0.06 TYR 190 -0.13 PRO 422

GLY 386 0.04 ARG 191 -0.12 PRO 422

LYS 300 0.05 ASN 192 -0.14 PRO 422

MET 387 0.07 LEU 193 -0.14 PRO 422

GLY 386 0.08 TYR 194 -0.13 PRO 422

GLY 386 0.06 ARG 195 -0.12 PRO 422

GLY 386 0.05 ALA 196 -0.12 PRO 422

LYS 300 0.04 GLY 197 -0.12 PRO 422

GLY 386 0.03 SER 198 -0.11 PRO 422

GLY 82 0.02 SER 199 -0.10 PRO 422

GLY 82 0.02 ILE 200 -0.10 PRO 422

GLY 82 0.03 GLY 201 -0.09 PRO 422

GLY 82 0.02 ALA 202 -0.08 GLY 29

GLY 82 0.02 ILE 203 -0.09 GLY 29

GLY 82 0.03 ASP 204 -0.08 GLY 29

PRO 104 0.02 SER 205 -0.08 GLY 29

PRO 104 0.03 LYS 206 -0.09 HIS 340

GLY 82 0.03 LEU 207 -0.10 HIS 340

PRO 79 0.02 ASP 208 -0.10 HIS 340

PRO 183 0.03 TRP 209 -0.11 GLY 29

GLY 84 0.04 SER 210 -0.11 GLY 29

GLY 84 0.04 HIS 211 -0.10 GLY 29

ALA 81 0.04 ASN 212 -0.10 GLY 29

GLY 84 0.03 PHE 213 -0.10 GLY 29

GLY 84 0.03 THR 214 -0.10 GLY 29

GLY 84 0.04 ASN 215 -0.09 GLY 29

GLY 84 0.03 MET 216 -0.10 PRO 422

GLY 84 0.02 LEU 217 -0.10 PRO 422

GLY 84 0.03 GLY 218 -0.10 SER 311

TYR 194 0.04 TYR 219 -0.10 SER 311

TYR 194 0.03 THR 220 -0.10 SER 311

TYR 194 0.04 ASP 221 -0.11 SER 311

CYS 332 0.04 PRO 222 -0.09 GLY 29

LEU 227 0.06 GLN 223 -0.12 LEU 341

CYS 332 0.05 PHE 224 -0.10 GLY 29

PRO 72 0.04 THR 225 -0.10 GLY 29

PRO 72 0.05 GLU 226 -0.16 HIS 340

GLN 223 0.06 LEU 227 -0.11 GLY 29

THR 225 0.03 MET 228 -0.11 GLY 29

PRO 72 0.04 ARG 229 -0.12 GLY 29

PRO 72 0.04 LEU 230 -0.12 GLY 29

ILE 71 0.03 TYR 231 -0.12 GLY 29

ILE 71 0.02 LEU 232 -0.13 GLY 29

ILE 71 0.03 THR 233 -0.14 GLY 29

GLY 312 0.03 ILE 234 -0.14 GLY 29

VAL 314 0.05 HIS 235 -0.15 GLY 29

GLY 312 0.06 SER 236 -0.16 GLY 29

GLY 312 0.10 ASP 237 -0.18 GLY 29

GLY 312 0.12 HIS 238 -0.19 GLY 29

GLY 312 0.15 GLU 239 -0.22 GLY 29

GLY 312 0.17 GLY 240 -0.23 GLY 29

GLY 312 0.21 GLY 241 -0.22 GLY 29

GLY 312 0.20 ASN 242 -0.18 GLY 29

GLY 312 0.21 VAL 243 -0.25 PRO 422

ARG 313 0.16 SER 244 -0.22 PRO 422

GLY 312 0.16 ALA 245 -0.19 GLY 29

GLY 312 0.20 HIS 246 -0.23 PRO 422

GLY 312 0.19 THR 247 -0.30 PRO 422

GLY 312 0.15 SER 248 -0.21 PRO 422

GLY 312 0.17 HIS 249 -0.21 GLY 29

GLY 312 0.20 LEU 250 -0.26 PRO 422

GLY 312 0.18 VAL 251 -0.24 PRO 422

GLY 312 0.15 GLY 252 -0.18 ASN 30

GLY 312 0.17 SER 253 -0.20 ASN 30

GLY 312 0.17 ALA 254 -0.17 ASN 30

GLY 312 0.15 LEU 255 -0.16 ASN 30

GLY 312 0.14 SER 256 -0.15 ASN 30

GLY 312 0.12 ASP 257 -0.14 ASN 30

ARG 313 0.11 PRO 258 -0.14 ASN 30

ARG 313 0.10 TYR 259 -0.14 PRO 422

ARG 313 0.12 LEU 260 -0.19 PRO 422

ARG 313 0.13 SER 261 -0.19 PRO 422

ARG 313 0.11 PHE 262 -0.18 PRO 422

ARG 313 0.11 ALA 263 -0.21 PRO 422

ARG 313 0.15 ALA 264 -0.27 PRO 422

ARG 313 0.15 ALA 265 -0.24 PRO 422

ARG 313 0.12 MET 266 -0.22 PRO 422

ARG 313 0.15 ASN 267 -0.27 PRO 422

ARG 313 0.18 GLY 268 -0.28 PRO 422

ARG 313 0.14 LEU 269 -0.22 PRO 422

TYR 304 0.13 ALA 270 -0.22 PRO 422

ARG 313 0.18 GLY 271 -0.23 PRO 422

ARG 313 0.20 PRO 272 -0.19 PRO 422

ARG 313 0.25 LEU 273 -0.17 PRO 422

ARG 313 0.17 HIS 274 -0.18 PRO 422

TYR 304 0.11 GLY 275 -0.17 PRO 422

TYR 304 0.13 LEU 276 -0.17 PRO 422

TYR 304 0.12 ALA 277 -0.14 PRO 422

LEU 301 0.08 ASN 278 -0.13 PRO 422

LEU 301 0.09 GLN 279 -0.13 PRO 422

TYR 304 0.13 GLU 280 -0.13 GLY 312

LEU 301 0.12 VAL 281 -0.13 SER 311

LEU 301 0.09 LEU 282 -0.18 SER 311

LEU 301 0.12 LEU 283 -0.22 SER 311

LEU 301 0.15 TRP 284 -0.27 SER 311

ASP 295 0.11 LEU 285 -0.26 SER 311

ASN 134 0.12 SER 286 -0.29 SER 311

ASN 134 0.14 GLN 287 -0.37 SER 311

LYS 300 0.14 LEU 288 -0.34 SER 311

ASN 134 0.12 GLN 289 -0.28 SER 311

ASN 134 0.13 LYS 290 -0.33 SER 311

ASN 134 0.14 ASP 291 -0.32 SER 311

LEU 285 0.11 ASP 295 -0.13 SER 311

ASN 134 0.10 ALA 296 -0.14 SER 311

PRO 272 0.09 SER 297 -0.13 GLU 85

PRO 316 0.11 ASP 298 -0.13 GLU 85

PRO 272 0.12 GLU 299 -0.11 GLU 85

PRO 272 0.14 LYS 300 -0.09 GLU 85

TRP 284 0.15 LEU 301 -0.11 TYR 304

PRO 316 0.14 ARG 302 -0.08 GLU 85

PRO 272 0.15 ASP 303 -0.07 GLU 85

PRO 272 0.19 TYR 304 -0.13 LEU 349

GLY 44 0.17 ILE 305 -0.10 LEU 349

GLY 44 0.18 TRP 306 -0.10 ASP 291

GLY 44 0.22 ASN 307 -0.24 ASP 291

GLY 44 0.24 THR 308 -0.31 LEU 288

GLY 44 0.26 LEU 309 -0.19 LEU 288

GLY 43 0.30 ASN 310 -0.23 GLN 287

GLY 43 0.33 SER 311 -0.37 GLN 287

GLY 43 0.41 GLY 312 -0.29 GLN 287

GLY 44 0.33 ARG 313 -0.24 GLN 287

GLY 44 0.27 VAL 314 -0.18 TRP 284

LEU 273 0.18 VAL 315 -0.12 LEU 285

ILE 305 0.16 PRO 316 -0.11 LYS 366

LEU 301 0.08 GLY 317 -0.10 PRO 422

GLY 44 0.08 TYR 318 -0.08 GLY 29

GLY 312 0.14 GLY 319 -0.09 GLY 29

GLY 312 0.17 HIS 320 -0.10 GLY 29

GLY 312 0.21 ALA 321 -0.11 LEU 273

GLY 312 0.17 VAL 322 -0.12 GLY 29

GLY 312 0.14 LEU 323 -0.13 GLY 29

GLY 312 0.13 ARG 324 -0.14 ASP 39

GLY 312 0.09 LYS 325 -0.12 GLN 35

GLY 312 0.06 THR 326 -0.12 GLY 29

GLY 312 0.06 ASP 327 -0.14 GLY 29

GLY 312 0.04 PRO 328 -0.14 GLY 29

GLN 223 0.04 ARG 329 -0.14 GLY 29

GLN 223 0.02 TYR 330 -0.12 GLY 29

GLN 223 0.03 THR 331 -0.15 TYR 354

GLN 223 0.06 CYS 332 -0.13 GLY 29

GLN 223 0.04 GLN 333 -0.12 GLY 29

HIS 377 0.04 ARG 334 -0.13 GLU 85

TYR 385 0.04 GLU 335 -0.16 GLU 85

TYR 385 0.06 PHE 336 -0.21 GLU 85

VAL 380 0.05 ALA 337 -0.19 GLU 85

ASN 134 0.04 LEU 338 -0.21 GLU 85

TYR 194 0.04 LYS 339 -0.28 GLU 85

TYR 384 0.06 HIS 340 -0.24 GLU 85

ASN 134 0.06 LEU 341 -0.18 GLU 85

ASN 134 0.06 PRO 342 -0.17 GLU 85

ASN 134 0.07 SER 343 -0.15 GLU 85

ASN 134 0.07 ASP 344 -0.15 SER 311

ASN 134 0.08 PRO 345 -0.18 SER 311

ASN 134 0.08 MET 346 -0.19 SER 311

ASN 134 0.07 PHE 347 -0.14 SER 311

ASN 134 0.07 LYS 348 -0.15 THR 308

ASN 134 0.08 LEU 349 -0.17 THR 308

VAL 281 0.07 VAL 350 -0.15 THR 308

ASN 134 0.05 ALA 351 -0.13 THR 331

ASP 295 0.10 GLN 352 -0.14 THR 331

PRO 316 0.13 LEU 353 -0.11 THR 308

PRO 316 0.09 TYR 354 -0.15 THR 331

ASP 295 0.09 LYS 355 -0.14 THR 331

PRO 316 0.11 ILE 356 -0.10 THR 331

PRO 316 0.12 VAL 357 -0.07 THR 331

ASN 310 0.06 PRO 358 -0.08 GLY 29

ASP 298 0.09 ASN 359 -0.07 GLY 29

ASP 298 0.10 VAL 360 -0.05 GLU 85

ASN 310 0.12 LEU 361 -0.08 VAL 315

ASN 310 0.10 LEU 362 -0.08 THR 427

ASN 310 0.10 GLU 363 -0.06 THR 427

ASN 310 0.15 GLN 364 -0.10 VAL 315

ASN 310 0.14 GLY 365 -0.09 THR 427

GLY 312 0.19 LYS 366 -0.11 PRO 316

GLY 312 0.22 ALA 367 -0.08 THR 427

GLY 312 0.19 LYS 368 -0.12 THR 427

GLY 312 0.15 ASN 369 -0.10 ASP 39

GLY 312 0.12 PRO 370 -0.08 GLY 29

GLY 312 0.07 TRP 371 -0.10 GLY 29

GLY 312 0.04 PRO 372 -0.10 GLY 29

GLY 312 0.05 ASN 373 -0.12 GLY 29

GLY 312 0.03 VAL 374 -0.13 GLY 29

LEU 301 0.04 ASP 375 -0.11 GLY 29

GLY 44 0.04 ALA 376 -0.10 GLY 29

ARG 334 0.04 HIS 377 -0.11 GLY 29

ASN 134 0.03 SER 378 -0.11 GLY 29

ASN 134 0.05 GLY 379 -0.11 SER 311

ASN 134 0.05 VAL 380 -0.14 SER 311

PHE 336 0.05 LEU 381 -0.11 SER 311

PHE 336 0.06 LEU 382 -0.12 SER 311

ASN 134 0.07 GLN 383 -0.16 SER 311

TYR 194 0.06 TYR 384 -0.15 SER 311

PHE 336 0.06 TYR 385 -0.14 SER 311

TYR 194 0.08 GLY 386 -0.16 SER 311

TYR 194 0.08 MET 387 -0.14 SER 311

ASN 134 0.07 THR 388 -0.16 SER 311

ASN 134 0.09 GLU 389 -0.13 SER 311

LYS 300 0.07 MET 390 -0.13 PRO 422

LYS 300 0.09 ASN 391 -0.15 PRO 422

LYS 300 0.07 TYR 392 -0.14 PRO 422

LYS 300 0.06 TYR 393 -0.13 PRO 422

TYR 304 0.07 THR 394 -0.15 PRO 422

TYR 304 0.06 VAL 395 -0.15 PRO 422

TYR 304 0.04 LEU 396 -0.13 PRO 422

TYR 304 0.05 PHE 397 -0.13 PRO 422

TYR 304 0.06 GLY 398 -0.15 PRO 422

TYR 304 0.04 VAL 399 -0.13 GLY 29

VAL 314 0.04 SER 400 -0.14 GLY 29

ARG 313 0.07 ARG 401 -0.15 GLY 29

ARG 313 0.08 ALA 402 -0.15 GLY 29

GLY 312 0.07 LEU 403 -0.16 GLY 29

GLY 312 0.09 GLY 404 -0.18 GLY 29

GLY 312 0.11 VAL 405 -0.18 GLY 29

GLY 312 0.10 LEU 406 -0.17 GLY 29

GLY 312 0.09 ALA 407 -0.18 GLY 29

GLY 312 0.12 GLN 408 -0.21 GLY 29

GLY 312 0.13 LEU 409 -0.19 GLY 29

GLY 312 0.11 ILE 410 -0.16 GLY 29

GLY 312 0.12 TRP 411 -0.19 GLY 29

GLY 312 0.15 SER 412 -0.21 GLY 29

GLY 312 0.14 ARG 413 -0.16 GLY 29

GLY 312 0.12 ALA 414 -0.14 GLY 29

PRO 422 0.16 LEU 415 -0.17 GLY 29

PRO 422 0.19 GLY 416 -0.15 ASN 30

PRO 422 0.22 PHE 417 -0.23 GLY 29

PRO 422 0.19 PRO 418 -0.24 ASN 30

SER 424 0.21 LEU 419 -0.23 ASN 30

SER 424 0.21 GLU 420 -0.25 ASN 30

ILE 36 0.29 ARG 421 -0.11 ASN 30

VAL 33 0.42 PRO 422 -0.30 THR 247

ILE 36 0.43 LYS 423 -0.19 GLY 44

ARG 421 0.27 SER 424 -0.17 GLY 44

ILE 36 0.20 MET 425 -0.14 GLY 44

GLY 161 0.19 SER 426 -0.14 TYR 42

SER 311 0.21 THR 427 -0.12 LYS 368

SER 311 0.19 ALA 428 -0.11 LYS 368

SER 311 0.18 GLY 429 -0.10 TYR 42

GLY 312 0.20 LEU 430 -0.13 TYR 42

SER 311 0.19 GLU 431 -0.11 LYS 368

SER 311 0.17 LYS 432 -0.09 LYS 368

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** 6csc_aligned_close ***

CA distance fluctuations for 2604241133101949041

--- normal mode 16 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* 6csc_aligned_close *