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

* TRANSFERASE 05-DEC-14 4RWQ *

CA distance fluctuations for 2401161742511318419

--- 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
GLY 180 0.08 MET 1 -0.43 GLN 141

GLY 180 0.10 GLU 2 -0.37 THR 68

GLY 180 0.11 LEU 3 -0.32 GLN 141

GLY 180 0.14 ARG 4 -0.25 GLN 141

GLY 180 0.13 HIS 5 -0.29 GLN 141

GLY 180 0.12 THR 6 -0.34 GLN 141

GLY 180 0.13 PRO 7 -0.33 LEU 140

GLY 180 0.14 ALA 8 -0.31 LEU 140

GLN 253 0.16 ARG 9 -0.33 LEU 140

GLY 180 0.09 ASP 10 -0.39 LEU 140

GLY 180 0.10 LEU 11 -0.35 LEU 140

GLU 126 0.07 ASP 12 -0.38 LEU 140

LEU 3 0.09 LYS 13 -0.47 LEU 140

THR 217 0.09 PHE 14 -0.45 LEU 140

THR 217 0.09 ILE 15 -0.39 LEU 140

THR 217 0.08 GLU 16 -0.49 LEU 140

THR 217 0.10 ASP 17 -0.63 LEU 140

THR 217 0.11 HIS 18 -0.52 GLN 141

THR 217 0.09 LEU 19 -0.33 GLN 141

LEU 69 0.08 LEU 20 -0.36 ARG 198

ARG 70 0.18 PRO 21 -0.46 ARG 198

GLY 71 0.20 ASN 22 -0.42 PRO 160

GLY 71 0.16 THR 23 -0.52 PRO 160

GLU 126 0.14 CYS 24 -0.45 PRO 160

GLU 126 0.14 PHE 25 -0.39 PRO 160

SER 73 0.13 ARG 26 -0.45 PRO 160

ASN 224 0.13 THR 27 -0.47 THR 159

ASN 224 0.15 GLN 28 -0.36 THR 159

ASN 224 0.16 VAL 29 -0.33 THR 159

ASN 224 0.15 LYS 30 -0.41 THR 159

ASN 224 0.15 GLU 31 -0.33 THR 159

ASN 224 0.17 ALA 32 -0.22 THR 159

ASN 224 0.18 ILE 33 -0.23 LYS 56

ASN 224 0.16 ASP 34 -0.30 LYS 56

ASN 224 0.16 ILE 35 -0.16 ASP 17

ASN 224 0.17 VAL 36 -0.16 ASP 17

ASN 224 0.18 CYS 37 -0.18 ASP 34

ASN 224 0.16 ARG 38 -0.14 GLU 31

ASN 224 0.15 PHE 39 -0.14 ASP 17

ASN 224 0.16 LEU 40 -0.13 ASP 17

GLY 311 0.16 LYS 41 -0.14 ASP 34

GLY 311 0.15 GLU 42 -0.12 ASP 17

GLY 311 0.15 ARG 43 -0.13 ASP 17

GLY 311 0.16 CYS 44 -0.12 ASP 17

GLY 311 0.16 PHE 45 -0.11 ASP 17

GLN 157 0.19 GLN 46 -0.11 ASP 17

GLN 157 0.19 GLY 47 -0.10 ASP 17

GLN 157 0.17 THR 48 -0.10 ASP 17

GLN 157 0.17 ALA 49 -0.09 ASP 17

GLY 311 0.19 ASP 50 -0.11 LYS 30

GLY 156 0.22 PRO 51 -0.14 ASP 34

GLY 311 0.21 VAL 52 -0.15 LYS 30

GLY 156 0.21 ARG 53 -0.16 ASP 34

SER 55 0.21 VAL 54 -0.19 ASP 34

VAL 54 0.21 SER 55 -0.24 LYS 30

GLY 311 0.17 LYS 56 -0.31 LYS 30

ASN 224 0.17 VAL 57 -0.30 LYS 30

PRO 228 0.17 VAL 58 -0.34 LYS 30

CYS 37 0.17 LYS 59 -0.26 PRO 21

PRO 228 0.18 GLY 60 -0.23 PRO 21

LYS 205 0.13 GLY 61 -0.17 PRO 21

ILE 33 0.14 SER 62 -0.15 PRO 21

LYS 30 0.13 SER 63 -0.13 GLY 161

ARG 26 0.13 GLY 64 -0.16 PRO 160

GLY 223 0.17 LYS 65 -0.17 GLU 2

ASN 22 0.16 GLY 66 -0.24 GLU 2

ASN 22 0.18 THR 67 -0.27 GLU 2

ASN 22 0.19 THR 68 -0.37 GLU 2

PRO 21 0.14 LEU 69 -0.34 GLU 2

PRO 21 0.18 ARG 70 -0.32 GLY 71

ASN 22 0.20 GLY 71 -0.33 MET 1

GLY 223 0.18 ARG 72 -0.24 GLU 2

ASN 224 0.17 SER 73 -0.18 GLU 2

ASN 224 0.23 ASP 74 -0.13 GLU 2

ASN 224 0.21 ALA 75 -0.14 PRO 21

ASN 224 0.24 ASP 76 -0.14 PRO 21

ASN 224 0.22 LEU 77 -0.17 PRO 21

ASN 224 0.22 VAL 78 -0.17 PRO 21

ASN 224 0.20 VAL 79 -0.18 LYS 30

GLY 311 0.21 PHE 80 -0.22 LYS 30

GLY 311 0.22 LEU 81 -0.19 LYS 30

GLY 156 0.24 THR 82 -0.19 LYS 30

GLY 311 0.25 LYS 83 -0.17 LYS 30

GLY 311 0.27 LEU 84 -0.16 LYS 30

GLY 311 0.28 THR 85 -0.16 LYS 30

GLY 311 0.33 SER 86 -0.15 LYS 30

GLY 311 0.36 PHE 87 -0.15 THR 23

GLY 311 0.38 GLU 88 -0.11 LYS 30

GLY 311 0.31 ASP 89 -0.12 LYS 30

GLY 311 0.30 GLN 90 -0.12 LYS 30

GLY 311 0.32 LEU 91 -0.08 PRO 21

GLY 311 0.29 ARG 92 -0.08 LYS 30

GLY 311 0.25 ARG 93 -0.09 PRO 21

ASP 312 0.25 ARG 94 -0.08 PRO 21

LYS 225 0.21 GLY 95 -0.10 PRO 128

ASP 312 0.20 GLU 96 -0.09 PRO 128

ASP 312 0.20 PHE 97 -0.10 PRO 21

LYS 225 0.20 ILE 98 -0.10 ARG 129

ASP 312 0.16 GLN 99 -0.19 ARG 129

ASP 312 0.17 GLU 100 -0.12 ARG 129

ASN 224 0.17 ILE 101 -0.13 ASP 17

ASN 224 0.17 ARG 102 -0.13 ASP 17

ASP 312 0.14 ARG 103 -0.14 ASP 17

ASN 224 0.14 GLN 104 -0.14 ASP 17

ASN 224 0.16 LEU 105 -0.16 ASP 17

ASN 224 0.14 GLU 106 -0.17 MET 1

ASN 224 0.13 ALA 107 -0.16 ASP 17

ASN 224 0.14 CYS 108 -0.17 ASP 17

ASN 224 0.13 GLN 109 -0.20 ASP 17

ASN 224 0.11 ARG 110 -0.19 MET 1

ASN 224 0.12 GLU 111 -0.18 ASP 17

ASN 224 0.13 GLN 112 -0.19 ASP 17

ASN 224 0.12 LYS 113 -0.21 ASP 17

ASN 224 0.14 PHE 114 -0.24 ASP 17

ASN 224 0.13 LYS 115 -0.28 ASP 17

THR 117 0.15 VAL 116 -0.32 ASP 17

VAL 116 0.15 THR 117 -0.30 ASP 17

ASN 224 0.16 PHE 118 -0.25 ASP 17

ASN 224 0.15 GLU 119 -0.23 MET 1

ASN 224 0.16 VAL 120 -0.20 MET 1

ASN 224 0.17 GLN 121 -0.19 MET 1

PRO 138 0.17 SER 122 -0.17 MET 1

ASN 224 0.20 PRO 123 -0.12 MET 1

ASN 224 0.23 ARG 124 -0.10 MET 1

ASN 224 0.27 ARG 125 -0.09 ARG 103

ASN 224 0.39 GLU 126 -0.10 GLN 99

ASN 224 0.44 ASN 127 -0.13 GLN 99

LYS 225 0.42 PRO 128 -0.17 GLN 99

LYS 225 0.29 ARG 129 -0.19 GLN 99

ASN 224 0.29 ALA 130 -0.11 GLN 99

ASN 224 0.24 LEU 131 -0.11 MET 1

ASN 224 0.23 SER 132 -0.14 MET 1

ASN 224 0.21 PHE 133 -0.18 ASP 17

ASN 224 0.20 VAL 134 -0.22 ASP 17

ASN 224 0.19 LEU 135 -0.27 ASP 17

GLU 126 0.20 SER 136 -0.35 ASP 17

GLU 126 0.20 SER 137 -0.42 ASP 17

GLU 126 0.25 PRO 138 -0.47 ASP 17

GLU 126 0.22 GLN 139 -0.52 ASP 17

GLU 126 0.21 LEU 140 -0.63 ASP 17

GLU 126 0.25 GLN 141 -0.56 ASP 17

GLU 126 0.21 GLN 142 -0.47 ASP 17

GLU 126 0.21 GLU 143 -0.33 HIS 18

ASN 224 0.21 VAL 144 -0.25 HIS 18

ASN 224 0.24 GLU 145 -0.18 HIS 18

ASN 224 0.24 PHE 146 -0.15 ASP 17

ASN 224 0.28 ASP 147 -0.11 ASP 17

ASN 224 0.25 VAL 148 -0.11 PRO 21

ASN 224 0.26 LEU 149 -0.12 PRO 21

ASN 224 0.23 PRO 150 -0.13 PRO 21

GLY 311 0.26 ALA 151 -0.15 LYS 30

GLY 311 0.28 PHE 152 -0.18 LYS 30

GLY 311 0.25 ASP 153 -0.22 LYS 30

GLY 311 0.25 ALA 154 -0.24 THR 23

GLY 311 0.20 LEU 155 -0.29 THR 23

THR 82 0.24 GLY 156 -0.30 THR 27

PRO 51 0.21 GLN 157 -0.38 THR 27

PRO 51 0.17 TRP 158 -0.40 THR 27

GLY 47 0.15 THR 159 -0.48 THR 23

GLY 47 0.12 PRO 160 -0.52 THR 23

PRO 51 0.13 GLY 161 -0.49 THR 23

PRO 51 0.15 TYR 162 -0.43 THR 23

PRO 51 0.16 LYS 163 -0.38 THR 23

LYS 83 0.19 PRO 164 -0.34 THR 23

LYS 83 0.22 ASN 165 -0.31 THR 23

GLY 311 0.19 PRO 166 -0.27 THR 23

GLY 311 0.22 GLU 167 -0.25 THR 23

GLY 311 0.25 ILE 168 -0.25 THR 23

GLY 311 0.27 TYR 169 -0.23 THR 23

GLY 311 0.28 VAL 170 -0.21 THR 23

GLY 311 0.31 GLN 171 -0.20 THR 23

GLY 311 0.36 LEU 172 -0.18 THR 23

GLY 311 0.39 ILE 173 -0.17 THR 23

GLY 311 0.38 LYS 174 -0.16 THR 23

GLY 311 0.43 GLU 175 -0.14 THR 23

GLY 311 0.54 CYS 176 -0.12 THR 23

GLY 311 0.52 LYS 177 -0.11 THR 23

GLY 311 0.49 SER 178 -0.10 THR 23

GLY 311 0.53 ARG 179 -0.08 THR 23

GLY 311 0.67 GLY 180 -0.06 THR 23

GLY 311 0.73 LYS 181 -0.06 CYS 286

GLY 311 0.71 GLU 182 -0.09 THR 23

GLY 311 0.52 GLY 183 -0.11 THR 23

GLY 311 0.48 GLU 184 -0.08 THR 23

GLY 311 0.39 PHE 185 -0.14 THR 23

GLY 311 0.30 SER 186 -0.16 PRO 21

PRO 228 0.27 THR 187 -0.17 PRO 21

GLY 311 0.26 CYS 188 -0.20 THR 23

GLY 311 0.20 PHE 189 -0.25 THR 23

PRO 228 0.16 THR 190 -0.27 PRO 21

LYS 56 0.16 GLU 191 -0.35 ARG 26

LEU 346 0.13 LEU 192 -0.35 THR 23

LYS 56 0.15 GLN 193 -0.31 PRO 21

VAL 58 0.15 ARG 194 -0.40 PRO 21

LYS 41 0.14 ASP 195 -0.44 THR 23

LYS 41 0.13 PHE 196 -0.37 THR 23

CYS 37 0.13 LEU 197 -0.37 PRO 21

ARG 38 0.15 ARG 198 -0.49 THR 23

ARG 198 0.13 ASN 199 -0.41 THR 23

ARG 38 0.12 ARG 200 -0.35 THR 23

GLY 61 0.11 PRO 201 -0.34 THR 23

GLY 61 0.10 THR 202 -0.38 THR 23

GLY 61 0.09 LYS 203 -0.30 THR 23

GLY 61 0.11 LEU 204 -0.27 THR 23

GLY 61 0.13 LYS 205 -0.31 THR 23

GLY 61 0.09 SER 206 -0.26 LEU 140

PRO 128 0.10 LEU 207 -0.23 LEU 140

GLY 61 0.12 ILE 208 -0.22 PRO 21

GLU 126 0.10 ARG 209 -0.20 GLY 161

GLU 126 0.10 LEU 210 -0.21 LEU 140

LYS 181 0.13 VAL 211 -0.15 LEU 140

ASN 127 0.12 LYS 212 -0.12 GLY 161

GLU 126 0.11 HIS 213 -0.13 GLY 161

LYS 181 0.15 TRP 214 -0.11 LEU 140

LYS 181 0.18 TYR 215 -0.07 GLY 161

GLU 126 0.15 GLN 216 -0.08 GLY 161

LYS 181 0.15 THR 217 -0.10 GLY 337

LYS 181 0.21 CYS 218 -0.07 GLY 337

GLU 126 0.24 LYS 219 -0.06 GLY 337

GLU 126 0.23 LYS 220 -0.09 GLY 337

GLU 126 0.27 THR 221 -0.10 GLY 337

GLU 126 0.32 HIS 222 -0.07 GLY 337

GLU 126 0.39 GLY 223 -0.06 GLY 337

ASN 127 0.44 ASN 224 -0.07 GLY 311

PRO 128 0.42 LYS 225 -0.06 LEU 263

LYS 181 0.35 LEU 226 -0.06 LYS 264

LYS 181 0.35 PRO 227 -0.06 LEU 268

GLU 184 0.33 PRO 228 -0.07 PRO 294

GLU 184 0.19 GLN 229 -0.09 PRO 21

THR 187 0.18 TYR 230 -0.16 PRO 21

GLU 184 0.22 ALA 231 -0.13 PRO 21

GLU 184 0.18 LEU 232 -0.13 PRO 21

PRO 128 0.12 GLU 233 -0.20 PRO 21

ALA 342 0.14 LEU 234 -0.20 PRO 21

GLY 183 0.17 LEU 235 -0.15 PRO 21

GLU 184 0.13 THR 236 -0.17 THR 23

ALA 342 0.12 VAL 237 -0.22 THR 23

ALA 342 0.19 TYR 238 -0.19 THR 23

TYR 238 0.19 ALA 239 -0.18 THR 23

ASP 336 0.13 TRP 240 -0.20 THR 23

ASP 336 0.13 GLU 241 -0.21 THR 23

ASP 336 0.18 GLN 242 -0.18 THR 23

ASP 336 0.20 GLY 243 -0.17 THR 23

ASP 336 0.17 SER 244 -0.19 THR 23

ASP 336 0.13 ARG 245 -0.21 THR 23

ASP 336 0.11 LYS 246 -0.21 THR 23

ARG 38 0.08 THR 247 -0.24 THR 23

PRO 128 0.08 ASP 248 -0.23 LEU 140

PRO 128 0.09 PHE 249 -0.23 LEU 140

ARG 9 0.10 SER 250 -0.25 LEU 140

LYS 181 0.11 THR 251 -0.26 LEU 140

ARG 9 0.15 ALA 252 -0.25 LEU 140

ARG 9 0.16 GLN 253 -0.21 LEU 140

GLY 180 0.14 GLY 254 -0.20 LEU 140

GLY 180 0.15 PHE 255 -0.19 LEU 140

GLY 180 0.19 GLN 256 -0.17 LEU 140

CYS 269 0.18 THR 257 -0.16 LEU 140

GLY 180 0.19 VAL 258 -0.14 LEU 140

GLY 180 0.22 LEU 259 -0.12 LEU 140

LEU 339 0.25 GLU 260 -0.13 GLN 321

GLY 180 0.24 LEU 261 -0.15 ALA 239

GLY 180 0.26 VAL 262 -0.12 ALA 239

GLY 180 0.27 LEU 263 -0.15 GLN 317

LEU 339 0.26 LYS 264 -0.15 GLN 242

GLY 180 0.28 HIS 265 -0.15 GLN 242

GLY 180 0.29 GLN 266 -0.14 GLN 242

SER 338 0.28 LYS 267 -0.16 GLN 242

LEU 339 0.25 LEU 268 -0.14 TYR 238

LEU 339 0.26 CYS 269 -0.14 THR 23

ALA 342 0.23 ILE 270 -0.18 THR 23

ALA 342 0.20 PHE 271 -0.20 THR 23

LEU 346 0.18 TRP 272 -0.25 THR 23

LEU 346 0.17 GLU 273 -0.28 THR 23

LEU 346 0.16 ALA 274 -0.33 THR 23

LEU 346 0.14 TYR 275 -0.32 THR 23

LYS 83 0.15 TYR 276 -0.27 THR 23

LEU 346 0.14 ASP 277 -0.26 THR 23

ASP 336 0.14 PHE 278 -0.23 THR 23

LYS 83 0.13 THR 279 -0.25 THR 23

GLY 311 0.16 ASN 280 -0.24 THR 23

GLY 311 0.16 PRO 281 -0.21 THR 23

GLY 311 0.21 VAL 282 -0.20 THR 23

GLY 311 0.21 VAL 283 -0.21 THR 23

SER 338 0.16 GLY 284 -0.21 THR 23

SER 338 0.18 ARG 285 -0.18 THR 23

GLY 311 0.23 CYS 286 -0.17 THR 23

LEU 339 0.18 MET 287 -0.19 THR 23

SER 338 0.21 LEU 288 -0.17 THR 23

SER 338 0.20 GLN 289 -0.15 THR 23

LEU 339 0.21 GLN 290 -0.14 THR 23

SER 338 0.23 LEU 291 -0.15 THR 23

SER 338 0.24 LYS 292 -0.13 THR 23

LYS 177 0.31 LYS 293 -0.12 THR 23

GLY 180 0.30 PRO 294 -0.14 GLY 310

GLY 180 0.30 ARG 295 -0.10 THR 23

GLY 180 0.29 PRO 296 -0.10 THR 23

GLU 182 0.22 VAL 297 -0.14 PRO 294

LEU 261 0.21 ILE 298 -0.15 THR 23

ALA 342 0.20 LEU 299 -0.17 THR 23

ALA 342 0.17 ASP 300 -0.20 PRO 21

LEU 346 0.15 PRO 301 -0.25 THR 23

GLY 311 0.15 ALA 302 -0.26 THR 23

GLY 311 0.23 ASP 303 -0.21 THR 23

GLY 311 0.23 PRO 304 -0.20 THR 23

GLY 311 0.36 THR 305 -0.16 THR 23

GLY 310 0.35 GLY 306 -0.14 THR 23

GLY 306 0.31 ASN 307 -0.13 PRO 21

GLY 183 0.28 VAL 308 -0.12 PRO 21

GLY 183 0.37 GLY 309 -0.09 PRO 21

GLU 182 0.51 GLY 310 -0.14 PRO 294

LYS 181 0.73 GLY 311 -0.14 PRO 294

LYS 181 0.60 ASP 312 -0.10 GLN 266

GLY 180 0.49 THR 313 -0.11 GLN 266

LYS 181 0.47 HIS 314 -0.10 LYS 264

LYS 181 0.44 SER 315 -0.07 LYS 264

LYS 181 0.37 TRP 316 -0.09 GLN 242

GLY 180 0.38 GLN 317 -0.15 LEU 263

LYS 181 0.35 ARG 318 -0.10 LEU 263

LYS 181 0.31 LEU 319 -0.08 GLY 243

GLY 180 0.31 ALA 320 -0.12 GLU 260

GLY 180 0.31 GLN 321 -0.13 GLU 260

GLY 180 0.26 GLU 322 -0.09 THR 344

GLY 180 0.25 ALA 323 -0.09 THR 257

GLY 180 0.26 ARG 324 -0.14 ALA 342

GLY 180 0.24 VAL 325 -0.09 LEU 140

GLY 180 0.21 TRP 326 -0.13 LEU 140

GLY 180 0.22 LEU 327 -0.15 LEU 140

GLY 180 0.21 GLY 328 -0.16 LEU 140

GLY 180 0.18 TYR 329 -0.19 GLN 141

GLY 180 0.16 PRO 330 -0.25 GLN 141

GLY 180 0.15 CYS 331 -0.26 LEU 140

GLY 180 0.18 CYS 332 -0.23 LEU 140

LYS 267 0.19 LYS 333 -0.26 LEU 140

LYS 267 0.19 ASN 334 -0.29 LEU 140

GLY 341 0.22 LEU 335 -0.34 LEU 140

GLY 341 0.28 ASP 336 -0.30 LEU 140

LYS 267 0.22 GLY 337 -0.28 LEU 140

LYS 267 0.28 SER 338 -0.24 LEU 140

LYS 267 0.28 LEU 339 -0.21 LEU 140

GLY 341 0.28 VAL 340 -0.23 LEU 140

VAL 340 0.28 GLY 341 -0.19 LEU 140

CYS 269 0.23 ALA 342 -0.17 LEU 140

ASP 336 0.23 TRP 343 -0.17 LEU 140

ASP 336 0.26 THR 344 -0.16 LEU 140

ASP 336 0.23 MET 345 -0.15 THR 23

ASP 336 0.22 LEU 346 -0.15 THR 23

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.

*** TRANSFERASE 05-DEC-14 4RWQ ***

CA distance fluctuations for 2401161742511318419

--- normal mode 11 ---

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

* TRANSFERASE 05-DEC-14 4RWQ *