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

* TRANSFERASE/RNA 05-DEC-14 4RWN *

CA distance fluctuations for 22091916134154503

--- normal mode 11 ---

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
ASP 248 0.05 MET 1 -0.17 GLN 347

ASP 248 0.04 GLU 2 -0.21 GLN 347

PRO 123 0.05 LEU 3 -0.23 GLN 347

PRO 123 0.06 ARG 4 -0.27 GLN 347

PRO 123 0.05 HIS 5 -0.23 GLN 347

PRO 123 0.05 THR 6 -0.20 GLN 347

PRO 123 0.05 PRO 7 -0.19 GLN 347

PRO 123 0.06 ALA 8 -0.17 GLN 347

SER 250 0.08 ARG 9 -0.10 GLN 347

ASP 248 0.07 ASP 10 -0.12 GLN 347

ASP 248 0.05 LEU 11 -0.14 GLN 347

ASP 248 0.08 ASP 12 -0.08 GLN 347

ASP 248 0.08 LYS 13 -0.08 GLN 347

ASP 248 0.06 PHE 14 -0.13 GLN 347

ASP 248 0.06 ILE 15 -0.11 GLN 347

ASP 248 0.07 GLU 16 -0.07 ASN 22

ASP 248 0.06 ASP 17 -0.09 GLN 347

LYS 220 0.06 HIS 18 -0.12 GLN 347

LYS 220 0.06 LEU 19 -0.11 GLN 347

LYS 220 0.06 LEU 20 -0.08 GLY 66

LYS 220 0.08 PRO 21 -0.11 GLY 66

LYS 220 0.09 ASN 22 -0.11 PRO 160

LYS 220 0.09 THR 23 -0.14 PRO 160

LYS 220 0.12 CYS 24 -0.12 PRO 160

GLY 71 0.14 PHE 25 -0.10 PRO 160

ASN 224 0.10 ARG 26 -0.13 SER 63

ASN 224 0.11 THR 27 -0.13 PRO 160

ASN 224 0.14 GLN 28 -0.10 PRO 160

ASN 224 0.15 VAL 29 -0.10 GLN 157

ASN 224 0.13 LYS 30 -0.12 GLN 157

ASN 224 0.13 GLU 31 -0.11 GLN 157

ASN 224 0.15 ALA 32 -0.08 GLN 157

ASN 224 0.14 ILE 33 -0.09 GLN 157

ASN 224 0.12 ASP 34 -0.11 LYS 56

ASN 224 0.13 ILE 35 -0.08 LYS 56

ASN 224 0.13 VAL 36 -0.06 LYS 56

ASN 224 0.12 CYS 37 -0.09 LYS 56

ASN 224 0.11 ARG 38 -0.06 LYS 56

ASN 224 0.11 PHE 39 -0.07 ARG 124

ASN 224 0.10 LEU 40 -0.08 ARG 124

LYS 348 0.11 LYS 41 -0.07 ARG 53

LYS 348 0.10 GLU 42 -0.07 ARG 124

ASN 224 0.09 ARG 43 -0.09 ARG 124

ASN 224 0.09 CYS 44 -0.11 ARG 124

ASN 224 0.07 PHE 45 -0.11 ARG 124

LYS 348 0.08 GLN 46 -0.11 ARG 124

LYS 225 0.06 GLY 47 -0.13 ARG 124

GLN 157 0.07 THR 48 -0.15 ARG 124

GLN 157 0.09 ALA 49 -0.16 ARG 124

GLN 157 0.10 ASP 50 -0.14 ARG 124

GLN 157 0.11 PRO 51 -0.10 ARG 124

GLN 157 0.09 VAL 52 -0.10 ARG 124

LYS 348 0.11 ARG 53 -0.08 ARG 124

LYS 348 0.12 VAL 54 -0.06 THR 82

LYS 348 0.15 SER 55 -0.07 ASP 34

LYS 348 0.16 LYS 56 -0.11 ASP 34

LYS 348 0.12 VAL 57 -0.09 LYS 30

LYS 348 0.13 VAL 58 -0.11 LYS 30

LYS 348 0.11 LYS 59 -0.11 ARG 26

PRO 228 0.10 GLY 60 -0.09 ARG 26

PRO 228 0.11 GLY 61 -0.07 ARG 26

ASN 224 0.09 SER 62 -0.05 ARG 70

ASN 224 0.10 SER 63 -0.13 ARG 26

LYS 348 0.12 GLY 64 -0.13 ARG 26

LYS 348 0.13 LYS 65 -0.10 THR 23

ILE 349 0.13 GLY 66 -0.12 THR 23

GLU 241 0.07 THR 67 -0.06 GLY 161

ASN 224 0.08 THR 68 -0.07 GLN 347

ASN 224 0.09 LEU 69 -0.11 GLN 347

LYS 220 0.10 ARG 70 -0.09 GLN 347

PHE 25 0.14 GLY 71 -0.10 GLN 347

LYS 219 0.15 ARG 72 -0.12 ILE 349

ASN 224 0.16 SER 73 -0.09 ILE 349

ASN 224 0.19 ASP 74 -0.09 ILE 349

ASN 224 0.16 ALA 75 -0.08 ARG 26

ASN 224 0.15 ASP 76 -0.07 ARG 26

ASN 224 0.13 LEU 77 -0.08 ARG 26

ASN 224 0.11 VAL 78 -0.07 ARG 26

ASN 224 0.09 VAL 79 -0.06 ILE 33

LYS 348 0.09 PHE 80 -0.06 ASP 34

LYS 348 0.09 LEU 81 -0.06 VAL 54

GLN 157 0.11 THR 82 -0.06 VAL 54

GLN 157 0.08 LYS 83 -0.06 ARG 124

ASP 312 0.06 LEU 84 -0.05 ARG 26

LYS 348 0.07 THR 85 -0.05 VAL 54

ASP 312 0.07 SER 86 -0.07 ILE 349

ASP 312 0.08 PHE 87 -0.15 ILE 349

ASP 312 0.08 GLU 88 -0.20 ILE 349

ASP 312 0.07 ASP 89 -0.14 ILE 349

ASP 312 0.08 GLN 90 -0.15 ILE 349

ASP 312 0.08 LEU 91 -0.24 ILE 349

HIS 314 0.07 ARG 92 -0.23 ILE 349

HIS 314 0.07 ARG 93 -0.17 ILE 349

ASP 312 0.08 ARG 94 -0.17 ILE 349

HIS 314 0.08 GLY 95 -0.21 ILE 349

HIS 314 0.07 GLU 96 -0.17 ARG 124

LYS 225 0.07 PHE 97 -0.14 ARG 124

LYS 225 0.09 ILE 98 -0.16 ARG 124

LYS 225 0.07 GLN 99 -0.23 ARG 124

LYS 225 0.07 GLU 100 -0.18 ARG 124

ASN 224 0.09 ILE 101 -0.14 ARG 124

ASN 224 0.10 ARG 102 -0.16 ARG 124

LYS 225 0.08 ARG 103 -0.18 ARG 124

ASN 224 0.09 GLN 104 -0.14 ARG 124

ASN 224 0.11 LEU 105 -0.11 ARG 124

ASN 224 0.10 GLU 106 -0.12 ARG 124

ASN 224 0.09 ALA 107 -0.12 ARG 124

ASN 224 0.10 CYS 108 -0.09 ARG 124

ASN 224 0.12 GLN 109 -0.08 ARG 124

ASN 224 0.10 ARG 110 -0.09 ARG 124

ASN 224 0.10 GLU 111 -0.08 ARG 124

ASN 224 0.11 GLN 112 -0.06 ARG 124

ASN 224 0.12 LYS 113 -0.06 ARG 124

ASN 224 0.14 PHE 114 -0.05 ARG 124

ASN 224 0.15 LYS 115 -0.07 ILE 349

ASN 224 0.16 VAL 116 -0.10 ILE 349

ASN 224 0.17 THR 117 -0.15 ILE 349

ASN 224 0.17 PHE 118 -0.18 ILE 349

ASN 224 0.21 GLU 119 -0.23 ILE 349

ASN 224 0.20 VAL 120 -0.28 ILE 349

LYS 225 0.22 GLN 121 -0.30 ILE 349

LYS 225 0.31 ALA 122 -0.33 ILE 349

LYS 225 0.35 PRO 123 -0.34 ILE 349

ASP 312 0.27 ARG 124 -0.32 ILE 349

ASP 312 0.23 TRP 125 -0.35 ILE 349

GLY 180 0.23 GLY 126 -0.33 ILE 349

HIS 314 0.10 ASN 127 -0.32 ILE 349

ASP 312 0.11 PRO 128 -0.30 ILE 349

ASP 312 0.11 ARG 129 -0.25 ILE 349

LEU 131 0.13 ALA 130 -0.21 ILE 349

ASN 224 0.13 LEU 131 -0.17 ILE 349

ASN 224 0.18 SER 132 -0.18 ILE 349

ASN 224 0.19 PHE 133 -0.15 ILE 349

ASN 224 0.20 VAL 134 -0.12 ILE 349

ASN 224 0.18 LEU 135 -0.07 ILE 349

ASN 224 0.17 SER 136 -0.06 ASP 17

ASN 224 0.15 SER 137 -0.06 GLN 157

ASN 224 0.14 PRO 138 -0.07 GLN 157

ASN 224 0.14 GLN 139 -0.08 GLN 157

ASN 224 0.15 LEU 140 -0.08 GLN 157

GLY 223 0.16 GLN 141 -0.08 PRO 160

GLY 223 0.19 GLN 142 -0.06 ASP 17

ASN 224 0.20 GLU 143 -0.07 ASP 17

ASN 224 0.20 VAL 144 -0.06 ASP 17

ASN 224 0.22 GLU 145 -0.10 ILE 349

ASN 224 0.20 PHE 146 -0.09 ILE 349

ASN 224 0.18 ASP 147 -0.13 ILE 349

ASN 224 0.14 VAL 148 -0.09 ILE 349

ASN 224 0.11 LEU 149 -0.11 ILE 349

LYS 225 0.09 PRO 150 -0.08 ILE 349

ASP 312 0.08 ALA 151 -0.06 ILE 349

ASP 312 0.08 PHE 152 -0.06 ARG 26

LYS 348 0.12 ASP 153 -0.07 THR 27

LYS 348 0.12 ALA 154 -0.07 THR 27

LYS 348 0.18 LEU 155 -0.09 THR 27

ILE 349 0.20 GLY 156 -0.10 THR 27

ILE 349 0.28 GLN 157 -0.12 THR 27

ILE 349 0.33 TRP 158 -0.12 THR 27

ILE 349 0.45 THR 159 -0.13 THR 23

ILE 349 0.48 PRO 160 -0.14 THR 23

ILE 349 0.59 GLY 161 -0.14 ASN 199

ILE 349 0.53 TYR 162 -0.12 THR 23

ILE 349 0.43 LYS 163 -0.11 ASN 199

ILE 349 0.28 PRO 164 -0.10 THR 23

ILE 349 0.26 ASN 165 -0.09 THR 23

GLN 347 0.19 PRO 166 -0.08 THR 23

GLN 347 0.15 GLU 167 -0.08 THR 23

GLN 347 0.12 ILE 168 -0.08 THR 23

GLN 347 0.10 TYR 169 -0.07 THR 23

GLY 126 0.10 VAL 170 -0.08 ILE 349

GLY 126 0.09 GLN 171 -0.10 ILE 349

GLY 126 0.11 LEU 172 -0.17 ILE 349

GLY 126 0.13 ILE 173 -0.27 ILE 349

GLY 126 0.12 LYS 174 -0.26 ILE 349

GLY 126 0.13 GLU 175 -0.27 ILE 349

GLY 126 0.17 CYS 176 -0.37 ILE 349

GLY 126 0.17 LYS 177 -0.44 ILE 349

GLY 126 0.16 SER 178 -0.39 ILE 349

GLY 126 0.21 ARG 179 -0.42 ILE 349

GLY 126 0.23 GLY 180 -0.52 ILE 349

GLY 126 0.22 LYS 181 -0.46 ILE 349

GLY 126 0.17 GLU 182 -0.48 ILE 349

TRP 125 0.16 GLY 183 -0.41 ILE 349

TRP 125 0.17 GLU 184 -0.35 ILE 349

TRP 125 0.12 PHE 185 -0.22 ILE 349

GLY 310 0.12 SER 186 -0.19 ILE 349

GLY 310 0.11 THR 187 -0.11 ILE 349

GLY 310 0.09 CYS 188 -0.07 ARG 26

LYS 348 0.10 PHE 189 -0.08 ARG 26

LYS 348 0.10 THR 190 -0.09 ARG 26

LYS 348 0.18 GLU 191 -0.10 ARG 26

LYS 348 0.21 LEU 192 -0.09 THR 23

LYS 348 0.12 GLN 193 -0.08 THR 23

LYS 348 0.16 ARG 194 -0.10 THR 23

LYS 348 0.16 ARG 194 -0.10 THR 23

ILE 349 0.27 ASP 195 -0.11 THR 23

LYS 348 0.25 PHE 196 -0.09 THR 23

LYS 348 0.20 LEU 197 -0.08 THR 23

ILE 349 0.27 ARG 198 -0.11 THR 23

ILE 349 0.39 ASN 199 -0.14 GLY 161

ILE 349 0.34 ARG 200 -0.09 ALA 274

ILE 349 0.36 PRO 201 -0.09 GLY 161

ILE 349 0.27 THR 202 -0.09 GLY 161

ILE 349 0.20 LYS 203 -0.07 GLY 161

ILE 349 0.16 LEU 204 -0.06 ALA 274

ILE 349 0.11 LYS 205 -0.06 GLY 161

GLU 241 0.07 SER 206 -0.07 GLN 347

PRO 123 0.07 LEU 207 -0.13 GLN 347

PRO 123 0.08 ILE 208 -0.15 GLN 347

PRO 123 0.07 ARG 209 -0.14 GLN 347

PRO 123 0.07 LEU 210 -0.20 GLN 347

PRO 123 0.09 VAL 211 -0.27 GLN 347

PRO 123 0.09 LYS 212 -0.24 ILE 349

PRO 123 0.06 HIS 213 -0.23 GLN 347

PRO 123 0.09 TRP 214 -0.31 ILE 349

PRO 123 0.12 TYR 215 -0.39 ILE 349

ARG 72 0.14 GLN 216 -0.34 ILE 349

GLN 142 0.11 THR 217 -0.36 ILE 349

PRO 123 0.14 CYS 218 -0.46 ILE 349

GLN 142 0.16 LYS 219 -0.46 ILE 349

GLN 142 0.17 LYS 220 -0.43 ILE 349

PRO 123 0.16 THR 221 -0.50 ILE 349

PRO 123 0.22 HIS 222 -0.57 ILE 349

ALA 122 0.24 GLY 223 -0.52 ILE 349

ALA 122 0.30 ASN 224 -0.55 ILE 349

PRO 123 0.35 LYS 225 -0.66 ILE 349

PRO 123 0.27 LEU 226 -0.65 ILE 349

PRO 123 0.24 PRO 227 -0.66 ILE 349

PRO 123 0.20 PRO 228 -0.52 ILE 349

PRO 123 0.14 GLN 229 -0.40 ILE 349

PRO 123 0.13 TYR 230 -0.33 ILE 349

PRO 123 0.15 ALA 231 -0.47 ILE 349

PRO 123 0.13 LEU 232 -0.40 ILE 349

PRO 123 0.10 GLU 233 -0.22 ILE 349

PRO 123 0.11 LEU 234 -0.23 ILE 349

PRO 123 0.11 LEU 235 -0.35 GLN 347

PRO 123 0.10 THR 236 -0.24 GLN 347

PRO 123 0.10 VAL 237 -0.08 GLN 347

PRO 123 0.08 TYR 238 -0.15 GLN 347

PRO 123 0.09 ALA 239 -0.28 GLN 347

ILE 349 0.10 TRP 240 -0.06 LYS 264

LYS 348 0.25 GLU 241 -0.12 LYS 267

LYS 348 0.12 GLN 242 -0.17 LYS 267

LEU 346 0.12 GLY 243 -0.10 LYS 264

ILE 349 0.28 SER 244 -0.07 LYS 264

ILE 349 0.44 ARG 245 -0.09 LYS 267

ILE 349 0.44 LYS 246 -0.09 GLU 273

ILE 349 0.40 THR 247 -0.09 ALA 274

ILE 349 0.33 ASP 248 -0.07 ALA 274

ILE 349 0.23 PHE 249 -0.05 THR 23

ILE 349 0.11 SER 250 -0.06 GLN 347

PRO 123 0.07 THR 251 -0.12 GLN 347

PRO 123 0.07 ALA 252 -0.20 GLN 347

PRO 123 0.08 GLN 253 -0.21 GLN 347

PRO 123 0.09 GLY 254 -0.22 GLN 347

PRO 123 0.09 PHE 255 -0.30 GLN 347

PRO 123 0.10 GLN 256 -0.39 GLN 347

PRO 123 0.10 THR 257 -0.45 GLN 347

PRO 123 0.11 VAL 258 -0.48 GLN 347

PRO 123 0.12 LEU 259 -0.54 GLN 347

PRO 123 0.13 GLU 260 -0.70 GLN 347

PRO 123 0.13 LEU 261 -0.79 GLN 347

PRO 123 0.15 VAL 262 -0.69 GLN 347

PRO 123 0.15 LEU 263 -0.79 GLN 347

PRO 123 0.15 LYS 264 -0.99 GLN 347

PRO 123 0.17 HIS 265 -1.00 ILE 349

PRO 123 0.17 GLN 266 -1.28 ILE 349

PRO 123 0.14 LYS 267 -1.23 ILE 349

PRO 123 0.13 LEU 268 -1.04 LYS 348

ALA 342 0.11 CYS 269 -0.90 ILE 349

PRO 123 0.10 ILE 270 -0.55 LYS 348

MET 345 0.13 PHE 271 -0.29 ILE 349

LYS 348 0.15 TRP 272 -0.06 LYS 246

LYS 348 0.34 GLU 273 -0.09 THR 247

LYS 348 0.41 ALA 274 -0.10 ASN 199

LYS 348 0.30 TYR 275 -0.09 ASN 199

LYS 348 0.23 TYR 276 -0.08 ASN 199

GLN 347 0.26 ASP 277 -0.08 ASN 199

GLN 347 0.24 PHE 278 -0.07 THR 247

GLN 347 0.28 THR 279 -0.08 ASN 199

GLN 347 0.20 ASN 280 -0.08 ASN 199

GLN 347 0.15 PRO 281 -0.07 ILE 349

GLY 126 0.10 VAL 282 -0.16 ILE 349

GLN 347 0.10 VAL 283 -0.13 ILE 349

GLN 347 0.12 GLY 284 -0.18 ILE 349

PRO 123 0.10 ARG 285 -0.37 ILE 349

PRO 123 0.11 CYS 286 -0.42 ILE 349

PRO 123 0.11 MET 287 -0.41 ILE 349

PRO 123 0.11 LEU 288 -0.57 ILE 349

PRO 123 0.12 GLN 289 -0.72 ILE 349

PRO 123 0.13 GLN 290 -0.75 ILE 349

PRO 123 0.12 LEU 291 -0.85 ILE 349

PRO 123 0.12 LYS 292 -1.08 ILE 349

PRO 123 0.15 LYS 293 -1.15 ILE 349

PRO 123 0.16 PRO 294 -1.35 ILE 349

PRO 123 0.16 ARG 295 -1.31 ILE 349

PRO 123 0.16 PRO 296 -1.08 ILE 349

PRO 123 0.14 VAL 297 -0.91 ILE 349

PRO 123 0.13 ILE 298 -0.62 ILE 349

PRO 123 0.12 LEU 299 -0.46 ILE 349

PRO 123 0.11 ASP 300 -0.27 ILE 349

PRO 123 0.10 PRO 301 -0.07 THR 23

PRO 123 0.10 ALA 302 -0.07 THR 23

PRO 123 0.11 ASP 303 -0.18 ILE 349

PRO 123 0.11 PRO 304 -0.27 ILE 349

PRO 123 0.13 THR 305 -0.42 ILE 349

PRO 123 0.15 GLY 306 -0.46 ILE 349

PRO 123 0.15 ASN 307 -0.63 ILE 349

PRO 123 0.16 VAL 308 -0.56 ILE 349

PRO 123 0.18 GLY 309 -0.76 ILE 349

PRO 123 0.23 GLY 310 -0.76 ILE 349

PRO 123 0.23 GLY 311 -0.94 ILE 349

PRO 123 0.30 ASP 312 -0.93 ILE 349

PRO 123 0.26 THR 313 -1.05 ILE 349

PRO 123 0.30 HIS 314 -0.93 ILE 349

PRO 123 0.28 SER 315 -0.81 ILE 349

PRO 123 0.23 TRP 316 -0.87 ILE 349

PRO 123 0.23 GLN 317 -0.90 ILE 349

PRO 123 0.23 ARG 318 -0.76 ILE 349

PRO 123 0.20 LEU 319 -0.68 ILE 349

PRO 123 0.18 ALA 320 -0.74 ILE 349

PRO 123 0.18 GLN 321 -0.69 ILE 349

PRO 123 0.16 GLU 322 -0.58 ILE 349

PRO 123 0.14 ALA 323 -0.55 ILE 349

PRO 123 0.14 ARG 324 -0.58 ILE 349

PRO 123 0.13 VAL 325 -0.50 ILE 349

PRO 123 0.11 TRP 326 -0.41 GLN 347

PRO 123 0.11 LEU 327 -0.44 GLN 347

PRO 123 0.10 GLY 328 -0.38 GLN 347

PRO 123 0.09 TYR 329 -0.32 GLN 347

PRO 123 0.07 PRO 330 -0.26 GLN 347

PRO 123 0.07 CYS 331 -0.26 GLN 347

PRO 123 0.08 CYS 332 -0.28 GLN 347

PRO 123 0.08 LYS 333 -0.24 GLN 347

LYS 267 0.07 ASN 334 -0.17 GLN 347

LYS 267 0.07 LEU 335 -0.14 GLN 347

LYS 267 0.08 ASP 336 -0.16 GLN 347

LYS 267 0.09 GLY 337 -0.22 GLN 347

LYS 267 0.10 SER 338 -0.23 GLN 347

LYS 267 0.09 LEU 339 -0.28 GLN 347

PRO 123 0.08 VAL 340 -0.22 GLN 347

CYS 269 0.10 GLY 341 -0.29 GLN 347

CYS 269 0.11 ALA 342 -0.36 GLN 347

PHE 271 0.09 TRP 343 -0.25 GLN 347

PHE 271 0.11 THR 344 -0.25 GLN 347

PHE 271 0.13 MET 345 -0.36 GLN 347

ARG 245 0.18 LEU 346 -0.33 LYS 267

GLY 161 0.32 GLN 347 -1.03 LYS 267

GLY 161 0.46 LYS 348 -1.17 LYS 267

GLY 161 0.59 ILE 349 -1.35 PRO 294

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: October 18th, 2018.

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

*** TRANSFERASE/RNA 05-DEC-14 4RWN ***

CA distance fluctuations for 22091916134154503

--- normal mode 11 ---

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

* TRANSFERASE/RNA 05-DEC-14 4RWN *