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

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

CA distance fluctuations for 221128153433140407

--- 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 increase ref largest decrease
SER 122 0.35 MET 1 -0.04 GLY 161

PRO 123 0.37 GLU 2 -0.04 THR 23

PRO 123 0.35 LEU 3 -0.04 GLY 161

PRO 123 0.35 ARG 4 -0.03 GLY 161

PRO 123 0.33 HIS 5 -0.04 GLY 161

PRO 123 0.30 THR 6 -0.05 GLY 161

PRO 123 0.27 PRO 7 -0.06 GLY 161

PRO 123 0.25 ALA 8 -0.07 GLY 161

PRO 123 0.23 ARG 9 -0.09 GLY 161

PRO 123 0.25 ASP 10 -0.08 GLY 161

PRO 123 0.25 LEU 11 -0.07 GLY 161

PRO 123 0.23 ASP 12 -0.09 GLY 161

PRO 123 0.24 LYS 13 -0.08 GLY 161

PRO 123 0.28 PHE 14 -0.06 GLY 161

PRO 123 0.25 ILE 15 -0.07 GLY 161

PRO 123 0.23 GLU 16 -0.07 GLY 161

PRO 123 0.26 ASP 17 -0.06 GLU 16

PRO 123 0.29 HIS 18 -0.06 THR 23

PRO 123 0.27 LEU 19 -0.06 HIS 213

PRO 123 0.22 LEU 20 -0.06 GLY 161

PRO 123 0.19 PRO 21 -0.06 GLY 223

PRO 123 0.17 ASN 22 -0.08 THR 23

PRO 123 0.13 THR 23 -0.08 ASN 22

GLU 143 0.15 CYS 24 -0.09 GLY 223

GLU 143 0.16 PHE 25 -0.14 GLY 71

PRO 123 0.13 ARG 26 -0.10 GLY 71

PRO 123 0.09 THR 27 -0.12 GLY 71

PRO 123 0.09 GLN 28 -0.12 GLY 71

PRO 123 0.10 VAL 29 -0.09 GLY 71

PRO 123 0.07 LYS 30 -0.08 GLY 71

PRO 123 0.05 GLU 31 -0.07 GLY 71

PRO 123 0.05 ALA 32 -0.07 GLY 311

PRO 123 0.06 ILE 33 -0.06 ASN 307

PRO 123 0.04 ASP 34 -0.04 ASN 307

MET 1 0.04 ILE 35 -0.05 ASN 307

ARG 72 0.07 VAL 36 -0.05 ASN 307

LYS 220 0.05 CYS 37 -0.04 ASN 307

LYS 220 0.04 ARG 38 -0.05 PHE 39

LYS 220 0.07 PHE 39 -0.05 ARG 38

LYS 220 0.09 LEU 40 -0.03 ILE 98

ASN 224 0.07 LYS 41 -0.04 ASN 199

LYS 220 0.06 GLU 42 -0.05 ARG 43

LYS 220 0.08 ARG 43 -0.05 GLU 42

LYS 220 0.11 CYS 44 -0.05 GLU 126

GLY 223 0.12 PHE 45 -0.05 GLU 126

GLY 223 0.10 GLN 46 -0.05 GLU 126

LYS 220 0.12 GLY 47 -0.06 GLU 126

GLY 223 0.14 THR 48 -0.05 GLU 126

GLY 223 0.13 ALA 49 -0.04 ASN 199

ASN 224 0.14 ASP 50 -0.05 ASN 199

ASN 224 0.13 PRO 51 -0.05 ASN 199

ASN 224 0.14 VAL 52 -0.05 ASN 199

ASN 224 0.13 ARG 53 -0.06 ASN 199

ASN 224 0.12 VAL 54 -0.06 ASN 199

ASN 224 0.11 SER 55 -0.08 ASN 199

ASN 224 0.10 LYS 56 -0.07 ASN 199

ASN 224 0.09 VAL 57 -0.05 ASN 199

ASN 224 0.08 VAL 58 -0.05 ASN 199

PRO 123 0.07 LYS 59 -0.03 ASN 307

GLY 61 0.09 GLY 60 -0.04 ASP 300

PRO 123 0.13 GLY 61 -0.07 VAL 308

PRO 123 0.16 SER 62 -0.06 VAL 308

PRO 123 0.13 SER 63 -0.06 VAL 308

PRO 123 0.09 GLY 64 -0.04 ASN 307

PRO 123 0.11 LYS 65 -0.04 PRO 160

PRO 123 0.14 GLY 66 -0.05 PRO 160

PRO 123 0.17 THR 67 -0.05 GLY 161

PRO 123 0.20 THR 68 -0.06 TYR 230

PRO 123 0.25 LEU 69 -0.07 PRO 228

PRO 123 0.24 ARG 70 -0.07 GLY 223

PRO 123 0.23 GLY 71 -0.14 PHE 25

PRO 123 0.28 ARG 72 -0.12 ASN 224

LEU 69 0.21 SER 73 -0.13 PRO 228

PRO 123 0.18 ASP 74 -0.11 PRO 228

PRO 123 0.11 ALA 75 -0.09 VAL 308

GLN 216 0.11 ASP 76 -0.09 ASN 307

GLN 216 0.11 LEU 77 -0.06 GLY 306

ASN 224 0.14 VAL 78 -0.04 GLY 306

ASN 224 0.14 VAL 79 -0.04 ASN 199

ASN 224 0.15 PHE 80 -0.06 ASN 199

ASN 224 0.16 LEU 81 -0.06 ASN 199

ASN 224 0.15 THR 82 -0.07 ASN 199

ASN 224 0.18 LYS 83 -0.05 ASN 199

ASN 224 0.20 LEU 84 -0.05 ASN 199

ASN 224 0.19 THR 85 -0.06 ASN 199

ASN 224 0.21 SER 86 -0.05 ASN 199

ASN 224 0.24 PHE 87 -0.06 VAL 120

ASN 224 0.26 GLU 88 -0.06 GLU 126

ASN 224 0.25 ASP 89 -0.05 GLU 126

ASN 224 0.26 GLN 90 -0.04 VAL 120

ASN 224 0.31 LEU 91 -0.06 VAL 120

ASN 224 0.31 ARG 92 -0.08 GLU 126

ASN 224 0.27 ARG 93 -0.07 GLU 126

ASN 224 0.28 ARG 94 -0.04 PHE 97

ASN 224 0.30 GLY 95 -0.08 GLU 126

ASN 224 0.25 GLU 96 -0.08 GLU 126

ASN 224 0.21 PHE 97 -0.06 GLU 126

GLY 223 0.23 ILE 98 -0.05 GLU 184

GLY 223 0.22 GLN 99 -0.10 GLU 126

GLY 223 0.18 GLU 100 -0.08 GLU 126

LYS 220 0.16 ILE 101 -0.06 GLU 126

LYS 220 0.18 ARG 102 -0.07 GLU 126

LYS 220 0.16 ARG 103 -0.08 ARG 124

LYS 220 0.13 GLN 104 -0.06 GLU 126

MET 1 0.12 LEU 105 -0.06 ASN 307

MET 1 0.13 GLU 106 -0.07 ARG 124

MET 1 0.11 ALA 107 -0.07 ARG 124

MET 1 0.09 CYS 108 -0.05 ASN 307

MET 1 0.11 GLN 109 -0.07 ASN 307

MET 1 0.11 ARG 110 -0.06 ARG 124

MET 1 0.08 GLU 111 -0.05 ASN 307

MET 1 0.08 GLN 112 -0.06 GLY 311

MET 1 0.07 LYS 113 -0.06 ASN 307

MET 1 0.09 PHE 114 -0.07 GLY 311

MET 1 0.12 LYS 115 -0.09 GLY 311

MET 1 0.15 VAL 116 -0.09 ASN 307

MET 1 0.19 THR 117 -0.11 GLY 311

GLU 2 0.21 PHE 118 -0.12 ASN 307

LYS 220 0.28 GLU 119 -0.14 GLY 311

LYS 220 0.37 VAL 120 -0.17 GLY 311

LYS 220 0.45 GLN 121 -0.12 GLU 182

LYS 220 0.58 SER 122 -0.11 GLY 180

GLY 223 0.72 PRO 123 -0.12 GLY 180

GLY 223 0.58 ARG 124 -0.09 GLY 180

ASN 224 0.63 ARG 125 -0.14 GLY 180

ASN 224 0.55 GLU 126 -0.10 ARG 179

ASN 224 0.44 ASN 127 -0.08 ARG 179

ASN 224 0.42 PRO 128 -0.09 VAL 120

ASN 224 0.35 ARG 129 -0.09 VAL 120

ASN 224 0.28 ALA 130 -0.15 LEU 131

LYS 220 0.23 LEU 131 -0.15 ALA 130

ARG 72 0.23 SER 132 -0.12 ASN 307

ARG 72 0.21 PHE 133 -0.12 ASN 307

ARG 72 0.19 VAL 134 -0.12 GLY 311

HIS 18 0.13 LEU 135 -0.10 GLY 311

HIS 18 0.11 SER 136 -0.10 GLY 311

CYS 24 0.07 SER 137 -0.09 GLY 311

CYS 24 0.06 PRO 138 -0.09 ASN 224

CYS 24 0.04 GLN 139 -0.08 ASN 224

CYS 24 0.09 LEU 140 -0.10 ASN 224

CYS 24 0.13 GLN 141 -0.13 ASN 224

CYS 24 0.14 GLN 142 -0.15 ASN 224

PHE 25 0.16 GLU 143 -0.14 ASN 224

PHE 25 0.16 VAL 144 -0.11 GLY 310

ARG 72 0.21 GLU 145 -0.13 GLY 310

ARG 72 0.17 PHE 146 -0.12 ASN 307

ARG 72 0.19 ASP 147 -0.11 ASN 307

LYS 220 0.16 VAL 148 -0.08 GLY 306

ASN 224 0.21 LEU 149 -0.07 SER 186

ASN 224 0.21 PRO 150 -0.04 SER 186

ASN 224 0.21 ALA 151 -0.04 VAL 120

ASN 224 0.19 PHE 152 -0.05 ASN 199

ASN 224 0.16 ASP 153 -0.08 ASN 199

ASN 224 0.16 ALA 154 -0.08 ASN 199

ASN 224 0.13 LEU 155 -0.09 ASN 199

ASN 224 0.12 GLY 156 -0.10 ASN 199

ASN 165 0.15 GLN 157 -0.12 ASN 199

ASN 165 0.12 TRP 158 -0.14 ASN 199

LYS 163 0.09 THR 159 -0.15 ASN 199

ASN 224 0.05 PRO 160 -0.21 ASN 199

TYR 275 0.05 GLY 161 -0.19 ASN 199

THR 279 0.07 TYR 162 -0.15 THR 247

TRP 158 0.09 LYS 163 -0.15 ARG 245

TRP 158 0.10 PRO 164 -0.12 ARG 245

GLN 157 0.15 ASN 165 -0.12 ARG 245

GLN 157 0.11 PRO 166 -0.11 ARG 245

ASN 224 0.12 GLU 167 -0.10 ARG 245

ASN 224 0.14 ILE 168 -0.09 ARG 245

ASN 224 0.13 TYR 169 -0.08 ARG 245

GLY 311 0.14 VAL 170 -0.08 ARG 245

ASN 224 0.16 GLN 171 -0.07 VAL 120

ASN 224 0.18 LEU 172 -0.08 VAL 120

GLY 311 0.19 ILE 173 -0.10 VAL 120

GLY 311 0.19 LYS 174 -0.08 VAL 120

LYS 225 0.22 GLU 175 -0.08 VAL 120

ASP 312 0.25 CYS 176 -0.10 VAL 120

GLY 311 0.26 LYS 177 -0.11 VAL 120

ASP 312 0.24 SER 178 -0.10 ARG 125

LYS 225 0.29 ARG 179 -0.12 ARG 125

ASP 312 0.34 GLY 180 -0.14 ARG 125

LYS 225 0.31 LYS 181 -0.13 VAL 120

GLY 310 0.31 GLU 182 -0.14 VAL 120

GLY 310 0.31 GLY 183 -0.14 VAL 120

ASN 224 0.32 GLU 184 -0.12 VAL 120

ASN 224 0.26 PHE 185 -0.09 VAL 120

PRO 228 0.23 SER 186 -0.09 VAL 120

ASN 224 0.21 THR 187 -0.06 VAL 120

ASN 224 0.18 CYS 188 -0.05 VAL 120

ASN 224 0.14 PHE 189 -0.06 VAL 120

ASN 224 0.12 THR 190 -0.07 ASP 147

ASN 224 0.09 GLU 191 -0.08 ASN 199

ASN 224 0.08 LEU 192 -0.08 PRO 201

ASN 224 0.07 GLN 193 -0.07 ASP 76

ARG 194 0.11 ARG 194 -0.05 ASP 76

ARG 194 0.11 ARG 194 -0.05 ASP 76

PRO 123 0.05 ASP 195 -0.09 PRO 201

PRO 123 0.06 PHE 196 -0.08 PRO 201

PRO 123 0.10 LEU 197 -0.08 GLY 161

PRO 123 0.09 ARG 198 -0.11 PRO 160

PRO 123 0.09 ASN 199 -0.21 PRO 160

PRO 123 0.11 ARG 200 -0.17 GLY 161

PRO 123 0.11 PRO 201 -0.18 GLY 161

PRO 123 0.13 THR 202 -0.14 GLY 161

PRO 123 0.16 LYS 203 -0.13 GLY 161

PRO 123 0.15 LEU 204 -0.12 GLY 161

PRO 123 0.17 LYS 205 -0.10 GLY 161

PRO 123 0.20 SER 206 -0.08 GLY 161

PRO 123 0.21 LEU 207 -0.08 GLY 161

PRO 123 0.21 ILE 208 -0.06 GLY 161

PRO 123 0.25 ARG 209 -0.05 GLY 161

PRO 123 0.27 LEU 210 -0.05 GLY 161

PRO 123 0.28 VAL 211 -0.04 GLY 161

PRO 123 0.31 LYS 212 -0.05 GLN 142

PRO 123 0.36 HIS 213 -0.06 LEU 19

PRO 123 0.36 TRP 214 -0.05 CYS 24

PRO 123 0.38 TYR 215 -0.07 GLN 142

PRO 123 0.46 GLN 216 -0.09 GLN 142

PRO 123 0.47 THR 217 -0.08 GLN 141

PRO 123 0.47 CYS 218 -0.08 GLN 142

PRO 123 0.57 LYS 219 -0.12 GLN 142

PRO 123 0.61 LYS 220 -0.11 GLN 141

PRO 123 0.57 THR 221 -0.10 GLN 141

PRO 123 0.57 HIS 222 -0.11 GLN 142

PRO 123 0.72 GLY 223 -0.15 GLN 142

PRO 123 0.65 ASN 224 -0.15 GLN 142

ARG 125 0.50 LYS 225 -0.14 GLN 142

ARG 125 0.41 LEU 226 -0.12 GLN 142

GLU 126 0.31 PRO 227 -0.12 GLN 142

GLU 184 0.31 PRO 228 -0.13 SER 73

ARG 125 0.29 GLN 229 -0.12 SER 73

GLU 184 0.20 TYR 230 -0.12 SER 73

GLY 183 0.19 ALA 231 -0.10 SER 73

PRO 123 0.21 LEU 232 -0.07 GLN 142

PRO 123 0.18 GLU 233 -0.06 ARG 72

PRO 123 0.12 LEU 234 -0.06 GLN 142

PRO 123 0.14 LEU 235 -0.05 GLN 142

PRO 123 0.16 THR 236 -0.06 ALA 274

PRO 123 0.12 VAL 237 -0.09 ALA 274

PRO 123 0.10 TYR 238 -0.09 ALA 274

PRO 123 0.13 ALA 239 -0.09 ALA 274

PRO 123 0.12 TRP 240 -0.12 ALA 274

PRO 123 0.09 GLU 241 -0.14 ALA 274

PRO 123 0.09 GLN 242 -0.12 GLU 273

PRO 123 0.12 GLY 243 -0.11 THR 279

PRO 123 0.12 SER 244 -0.13 GLY 161

PRO 123 0.10 ARG 245 -0.16 GLY 161

PRO 123 0.11 LYS 246 -0.17 GLY 161

PRO 123 0.12 THR 247 -0.18 GLY 161

PRO 123 0.14 ASP 248 -0.15 GLY 161

PRO 123 0.15 PHE 249 -0.13 GLY 161

PRO 123 0.18 SER 250 -0.10 GLY 161

PRO 123 0.20 THR 251 -0.10 GLY 161

PRO 123 0.22 ALA 252 -0.08 GLY 161

PRO 123 0.19 GLN 253 -0.09 GLY 161

PRO 123 0.19 GLY 254 -0.09 GLY 161

PRO 123 0.23 PHE 255 -0.07 GLY 161

PRO 123 0.22 GLN 256 -0.06 GLY 161

PRO 123 0.18 THR 257 -0.06 ALA 274

PRO 123 0.20 VAL 258 -0.05 ALA 274

PRO 123 0.24 LEU 259 -0.05 GLN 347

PRO 123 0.19 GLU 260 -0.07 GLN 347

PRO 123 0.16 LEU 261 -0.06 LYS 348

PRO 123 0.20 VAL 262 -0.06 GLN 142

PRO 123 0.19 LEU 263 -0.05 ILE 349

GLU 126 0.15 LYS 264 -0.07 ILE 349

GLU 126 0.15 HIS 265 -0.07 GLN 142

GLY 180 0.13 GLN 266 -0.07 GLN 142

GLU 126 0.09 LYS 267 -0.07 ILE 349

GLU 126 0.09 LEU 268 -0.06 GLN 142

GLY 180 0.05 CYS 269 -0.08 VAL 120

GLU 126 0.05 ILE 270 -0.07 VAL 120

ASN 307 0.03 PHE 271 -0.08 VAL 120

GLY 311 0.03 TRP 272 -0.08 ASP 277

GLY 311 0.05 GLU 273 -0.13 GLU 241

THR 159 0.04 ALA 274 -0.15 ARG 245

TRP 158 0.07 TYR 275 -0.12 ARG 245

TRP 158 0.07 TYR 276 -0.11 ARG 245

TRP 158 0.07 ASP 277 -0.12 ARG 245

GLY 311 0.07 PHE 278 -0.15 ILE 349

GLN 157 0.09 THR 279 -0.14 ILE 349

GLN 157 0.09 ASN 280 -0.11 ILE 349

GLY 311 0.09 PRO 281 -0.12 ILE 349

GLY 311 0.12 VAL 282 -0.10 ILE 349

GLY 311 0.12 VAL 283 -0.10 ILE 349

GLY 311 0.09 GLY 284 -0.13 ILE 349

GLY 311 0.10 ARG 285 -0.11 ILE 349

GLY 311 0.14 CYS 286 -0.12 VAL 120

GLY 311 0.11 MET 287 -0.11 VAL 120

GLY 311 0.08 LEU 288 -0.11 VAL 120

GLY 311 0.12 GLN 289 -0.13 VAL 120

GLY 311 0.13 GLN 290 -0.13 VAL 120

GLY 311 0.06 LEU 291 -0.12 VAL 120

GLY 311 0.05 LYS 292 -0.13 VAL 120

LYS 177 0.09 LYS 293 -0.14 VAL 120

GLY 180 0.11 PRO 294 -0.14 VAL 120

GLY 180 0.13 ARG 295 -0.10 VAL 120

GLY 180 0.14 PRO 296 -0.08 GLN 142

GLY 180 0.09 VAL 297 -0.10 VAL 120

GLY 180 0.08 ILE 298 -0.09 VAL 120

GLY 311 0.06 LEU 299 -0.11 VAL 120

PRO 228 0.07 ASP 300 -0.10 VAL 120

ASN 224 0.06 PRO 301 -0.07 VAL 120

PRO 228 0.09 ALA 302 -0.08 VAL 120

PRO 228 0.13 ASP 303 -0.10 VAL 120

GLY 311 0.13 PRO 304 -0.10 VAL 120

GLY 311 0.18 THR 305 -0.13 VAL 120

GLY 310 0.22 GLY 306 -0.14 VAL 120

GLY 306 0.15 ASN 307 -0.15 VAL 120

GLY 183 0.21 VAL 308 -0.13 VAL 120

GLY 183 0.20 GLY 309 -0.11 GLU 145

GLU 182 0.31 GLY 310 -0.15 VAL 120

GLY 180 0.32 GLY 311 -0.17 VAL 120

GLY 180 0.34 ASP 312 -0.13 VAL 120

GLY 180 0.27 THR 313 -0.10 GLN 142

GLU 126 0.30 HIS 314 -0.11 GLN 142

GLU 126 0.33 SER 315 -0.11 GLN 142

GLU 126 0.26 TRP 316 -0.09 GLN 142

GLU 126 0.27 GLN 317 -0.09 GLN 142

PRO 123 0.33 ARG 318 -0.09 GLN 142

PRO 123 0.32 LEU 319 -0.08 GLN 142

PRO 123 0.27 ALA 320 -0.07 GLN 142

PRO 123 0.31 GLN 321 -0.06 GLN 142

PRO 123 0.35 GLU 322 -0.06 GLN 141

PRO 123 0.29 ALA 323 -0.05 GLN 142

PRO 123 0.28 ARG 324 -0.05 GLN 347

PRO 123 0.32 VAL 325 -0.04 GLN 347

PRO 123 0.32 TRP 326 -0.04 GLN 347

PRO 123 0.27 LEU 327 -0.05 GLN 347

PRO 123 0.28 GLY 328 -0.05 GLN 347

PRO 123 0.30 TYR 329 -0.04 GLY 161

PRO 123 0.28 PRO 330 -0.05 GLY 161

PRO 123 0.28 CYS 331 -0.06 GLY 161

PRO 123 0.25 CYS 332 -0.06 GLY 161

PRO 123 0.24 LYS 333 -0.07 GLY 161

PRO 123 0.22 ASN 334 -0.08 GLY 161

PRO 123 0.23 LEU 335 -0.08 GLY 161

PRO 123 0.23 ASP 336 -0.07 GLY 161

PRO 123 0.24 GLY 337 -0.06 GLY 161

PRO 123 0.22 SER 338 -0.06 GLY 161

PRO 123 0.22 LEU 339 -0.06 GLY 161

PRO 123 0.20 VAL 340 -0.08 GLY 161

PRO 123 0.18 GLY 341 -0.07 THR 279

PRO 123 0.17 ALA 342 -0.08 THR 279

PRO 123 0.15 TRP 343 -0.09 THR 279

PRO 123 0.12 THR 344 -0.10 THR 279

PRO 123 0.10 MET 345 -0.10 THR 279

PRO 123 0.08 LEU 346 -0.13 THR 279

PRO 123 0.05 GLN 347 -0.11 THR 279

ASN 199 0.05 LYS 348 -0.13 THR 279

ASN 199 0.06 ILE 349 -0.15 PHE 278

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 221128153433140407

--- normal mode 8 ---

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

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