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

* 1OVA copy *

CA distance fluctuations for 2402070055341766116

--- normal mode 9 ---

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
ARG 58 0.07 GLY 1 -0.24 GLU 254

ARG 58 0.06 SER 2 -0.13 THR 257

ARG 58 0.08 ILE 3 -0.09 THR 257

GLY 292 0.04 GLY 4 -0.09 THR 257

GLU 17 0.04 ALA 5 -0.15 THR 257

GLY 292 0.05 ALA 6 -0.14 ASN 252

GLU 17 0.05 SER 7 -0.08 MET 35

GLU 17 0.04 MET 8 -0.11 PHE 59

ASP 13 0.06 GLU 9 -0.24 ASN 252

GLU 17 0.05 PHE 10 -0.16 ASN 252

GLU 17 0.04 CYS 11 -0.11 VAL 56

PHE 253 0.05 PHE 12 -0.20 VAL 56

GLU 9 0.06 ASP 13 -0.23 GLU 248

GLU 17 0.08 VAL 14 -0.17 PHE 15

PHE 253 0.08 PHE 15 -0.22 MET 291

PHE 253 0.07 LYS 16 -0.32 MET 291

VAL 14 0.08 GLU 17 -0.23 MET 291

GLN 157 0.06 LEU 18 -0.17 THR 195

ARG 153 0.08 LYS 19 -0.22 ALA 290

ASN 252 0.07 VAL 20 -0.26 ALA 290

ARG 153 0.08 HIS 21 -0.19 SER 286

ARG 153 0.09 HIS 22 -0.17 SER 286

SER 249 0.11 ALA 23 -0.21 ALA 290

GLU 245 0.13 ASN 24 -0.25 VAL 194

ARG 153 0.12 GLU 25 -0.15 HIS 22

ARG 153 0.12 ASN 26 -0.12 SER 286

ARG 153 0.09 ILE 27 -0.11 VAL 287

ARG 153 0.07 PHE 28 -0.07 MET 291

LYS 19 0.04 TYR 29 -0.04 MET 291

SER 36 0.04 CYS 30 -0.03 SER 96

GLU 331 0.04 PRO 31 -0.04 GLN 147

ALA 328 0.08 ILE 32 -0.07 LEU 97

LYS 175 0.11 ALA 33 -0.07 SER 7

ALA 328 0.07 ILE 34 -0.07 SER 249

SER 229 0.08 MET 35 -0.10 ASN 252

THR 88 0.13 SER 36 -0.07 ARG 100

PRO 90 0.14 ALA 37 -0.08 SER 249

LYS 89 0.12 LEU 38 -0.13 SER 249

LYS 89 0.17 ALA 39 -0.13 ASN 252

LYS 89 0.21 MET 40 -0.11 SER 249

LYS 89 0.17 VAL 41 -0.14 SER 249

LYS 89 0.17 TYR 42 -0.16 SER 249

LYS 89 0.21 LEU 43 -0.14 SER 249

LYS 89 0.20 GLY 44 -0.15 SER 249

LYS 89 0.17 ALA 45 -0.17 SER 249

LYS 89 0.15 LYS 46 -0.19 SER 249

LYS 89 0.13 ASP 47 -0.21 SER 249

LYS 89 0.11 SER 48 -0.24 SER 249

LYS 89 0.12 THR 49 -0.22 SER 249

LYS 89 0.13 ARG 50 -0.21 SER 249

LYS 89 0.11 THR 51 -0.24 SER 249

LYS 89 0.09 GLN 52 -0.27 SER 249

LYS 89 0.10 ILE 53 -0.23 SER 249

LYS 89 0.10 ASN 54 -0.23 SER 249

LYS 89 0.08 LYS 55 -0.28 ILE 250

GLY 292 0.07 VAL 56 -0.27 SER 249

GLY 292 0.07 VAL 57 -0.21 ASN 252

ILE 3 0.08 ARG 58 -0.23 ASN 252

LYS 89 0.09 PHE 59 -0.21 ASN 252

LYS 89 0.08 ASP 60 -0.23 ASN 252

SER 229 0.09 LYS 60 -0.23 GLU 254

SER 229 0.11 LEU 61 -0.17 GLU 254

SER 229 0.14 PRO 62 -0.13 GLU 254

SER 229 0.17 GLY 63 -0.12 GLU 254

LYS 89 0.15 PHE 64 -0.16 ASN 252

LYS 89 0.14 GLY 64 -0.18 GLU 254

LYS 89 0.16 ASP 65 -0.18 ILE 250

LYS 89 0.19 ILE 66 -0.14 GLU 254

LYS 89 0.21 GLU 67 -0.13 ILE 250

LYS 89 0.21 ALA 68 -0.13 ILE 250

LYS 89 0.24 GLN 69 -0.11 ILE 250

LYS 89 0.27 CYS 70 -0.10 ASN 252

LYS 89 0.31 GLY 71 -0.08 SER 249

LYS 89 0.31 THR 72 -0.07 ILE 250

LYS 89 0.28 SER 73 -0.08 GLU 254

LYS 89 0.31 VAL 74 -0.07 LEU 120

LYS 89 0.23 ASN 75 -0.08 GLU 254

LYS 89 0.24 VAL 76 -0.10 ASN 252

LYS 89 0.20 HIS 77 -0.11 ASN 252

SER 229 0.21 SER 78 -0.09 TYR 121

SER 229 0.17 SER 79 -0.08 ASN 252

SER 229 0.16 LEU 80 -0.08 ARG 122

SER 229 0.21 ARG 81 -0.10 ARG 122

SER 229 0.25 ASP 82 -0.10 GLN 147

SER 229 0.19 ILE 83 -0.08 GLN 147

SER 229 0.18 LEU 84 -0.11 GLN 147

LEU 120 0.29 ASN 85 -0.13 ASN 149

SER 229 0.26 GLN 86 -0.12 ASN 149

LEU 120 0.24 ILE 87 -0.10 ASN 149

LEU 120 0.31 THR 88 -0.16 ASN 149

GLU 119 0.41 LYS 89 -0.17 ASN 149

GLU 119 0.40 PRO 90 -0.12 THR 231

GLU 119 0.36 ASN 91 -0.12 THR 231

GLU 119 0.30 ASP 92 -0.08 ILE 151

GLU 119 0.27 VAL 92 -0.08 LYS 175

LEU 177 0.27 TYR 93 -0.08 THR 231

LYS 118 0.27 SER 94 -0.10 ILE 151

LYS 175 0.25 PHE 95 -0.10 ILE 151

LYS 175 0.23 SER 96 -0.13 THR 88

LYS 175 0.23 LEU 97 -0.09 LEU 84

LYS 175 0.19 ALA 98 -0.09 ARG 81

LYS 175 0.18 SER 99 -0.07 ARG 81

PRO 90 0.18 ARG 100 -0.07 SER 36

PRO 90 0.18 LEU 101 -0.07 SER 249

PRO 90 0.16 TYR 102 -0.06 SER 249

PRO 90 0.17 ALA 103 -0.08 SER 249

PRO 90 0.15 GLU 104 -0.08 SER 249

PRO 90 0.18 GLU 105 -0.07 SER 249

PRO 90 0.17 ARG 106 -0.09 SER 249

PRO 90 0.18 TYR 107 -0.10 SER 249

PRO 90 0.21 PRO 108 -0.10 SER 249

PRO 90 0.23 ILE 109 -0.10 SER 249

PRO 90 0.24 LEU 110 -0.11 SER 249

PRO 90 0.28 PRO 111 -0.09 SER 249

PRO 90 0.27 GLU 112 -0.10 SER 249

PRO 90 0.27 TYR 113 -0.11 SER 249

PRO 90 0.31 LEU 114 -0.08 SER 249

PRO 90 0.34 GLN 115 -0.09 PRO 127

PRO 90 0.31 CYS 116 -0.09 SER 249

PRO 90 0.31 VAL 117 -0.08 ASN 252

PRO 90 0.39 LYS 118 -0.09 GLU 126

LYS 89 0.41 GLU 119 -0.08 GLU 126

LYS 89 0.39 LEU 120 -0.07 VAL 74

LYS 89 0.34 TYR 121 -0.09 SER 78

PRO 90 0.35 ARG 122 -0.10 ARG 81

PRO 90 0.29 GLY 123 -0.08 ARG 81

PRO 90 0.28 GLY 124 -0.07 ALA 6

PRO 90 0.25 LEU 125 -0.08 LYS 118

PRO 90 0.22 GLU 126 -0.09 LYS 118

PRO 90 0.20 PRO 127 -0.09 GLN 115

PRO 90 0.16 ILE 128 -0.07 GLN 115

ASP 184 0.14 ASN 129 -0.06 GLN 115

PRO 90 0.11 PHE 130 -0.05 SER 249

PRO 90 0.11 GLN 131 -0.06 SER 249

ASP 184 0.11 THR 132 -0.05 GLN 115

ASP 184 0.12 ALA 132 -0.06 GLN 115

ASP 184 0.10 ALA 133 -0.05 LYS 118

ASP 184 0.10 ASP 134 -0.05 LYS 118

ASP 184 0.14 GLN 135 -0.07 LYS 118

ASP 184 0.13 ALA 136 -0.07 LYS 118

ASP 184 0.12 ARG 137 -0.06 LYS 118

VAL 202 0.15 GLU 138 -0.06 GLU 119

ASP 184 0.17 LEU 139 -0.08 GLU 119

ASP 184 0.16 ILE 140 -0.06 ARG 81

VAL 202 0.15 ASN 141 -0.06 ARG 81

ASP 184 0.20 SER 142 -0.07 ASN 85

ASP 184 0.20 TRP 143 -0.08 ARG 81

ASP 184 0.19 VAL 144 -0.08 ASN 85

GLN 203 0.22 GLU 145 -0.09 ASN 85

ASP 184 0.25 SER 146 -0.12 ASN 85

ASP 184 0.25 GLN 147 -0.12 ASN 85

ASP 184 0.25 THR 148 -0.13 THR 88

ASP 184 0.30 ASN 149 -0.17 LYS 89

GLN 203 0.28 GLY 150 -0.13 LYS 89

VAL 202 0.26 ILE 151 -0.12 LYS 89

VAL 202 0.19 ILE 152 -0.08 THR 88

VAL 202 0.19 ARG 153 -0.08 LYS 89

LYS 200 0.14 ASN 154 -0.06 ASN 85

VAL 202 0.11 VAL 155 -0.05 ASN 85

VAL 202 0.07 LEU 156 -0.03 ARG 81

ASN 283 0.09 GLN 157 -0.05 ASN 154

ALA 290 0.08 PRO 158 -0.03 GLY 150

THR 294 0.06 SER 159 -0.03 LYS 118

PHE 297 0.07 SER 160 -0.04 GLN 197

SER 298 0.06 VAL 161 -0.04 TYR 282

PRO 90 0.06 ASP 162 -0.05 ALA 23

PRO 90 0.08 SER 162 -0.06 VAL 20

PRO 90 0.09 GLN 163 -0.10 VAL 20

PRO 90 0.09 THR 164 -0.09 VAL 20

PRO 90 0.12 ALA 165 -0.10 SER 249

PRO 90 0.13 MET 166 -0.09 SER 249

PRO 90 0.11 VAL 167 -0.07 SER 249

PRO 90 0.11 LEU 168 -0.07 SER 249

ASP 184 0.11 VAL 169 -0.05 ARG 81

LYS 175 0.11 ASN 170 -0.05 ARG 81

ASP 184 0.12 ALA 171 -0.06 ASN 85

ALA 323 0.16 ILE 172 -0.06 GLN 86

ALA 323 0.17 VAL 173 -0.07 LYS 89

LYS 175 0.19 PHE 174 -0.08 SER 94

PHE 95 0.25 LYS 175 -0.08 VAL 92

GLU 119 0.22 GLY 176 -0.08 VAL 92

TYR 93 0.27 LEU 177 -0.06 LYS 277

GLU 119 0.21 TRP 178 -0.04 ARG 330

GLU 119 0.21 GLU 179 -0.04 CYS 371

GLU 119 0.20 LYS 180 -0.05 CYS 371

GLU 119 0.21 ALA 181 -0.05 ASN 24

ASN 149 0.22 PHE 182 -0.06 ASN 24

ASN 149 0.26 LYS 183 -0.07 ASN 24

ASN 149 0.30 ASP 184 -0.07 ASN 24

ASN 149 0.28 GLU 185 -0.11 ALA 335

ASN 149 0.25 ASP 186 -0.12 ALA 335

ASN 149 0.28 THR 187 -0.09 ALA 335

ASN 149 0.27 GLN 188 -0.11 ALA 335

ASN 149 0.27 ALA 189 -0.11 ASN 24

ASN 149 0.24 MET 190 -0.12 ASN 24

GLY 150 0.22 PRO 191 -0.14 ASN 24

GLY 150 0.21 PHE 192 -0.16 ASN 24

GLY 150 0.18 ARG 193 -0.17 ASN 24

GLY 150 0.17 VAL 194 -0.25 ASN 24

GLY 150 0.15 THR 195 -0.21 ALA 290

GLY 150 0.15 GLU 196 -0.21 ALA 290

GLY 150 0.15 GLN 197 -0.21 ALA 290

GLY 150 0.18 GLU 198 -0.21 ASN 24

GLY 150 0.20 SER 199 -0.19 ASN 24

GLY 150 0.24 LYS 200 -0.18 ASN 24

GLY 150 0.26 PRO 201 -0.14 ASN 24

ASN 149 0.28 VAL 202 -0.13 ASN 24

ASN 149 0.30 GLN 203 -0.11 ASN 24

ASN 149 0.25 MET 204 -0.11 ASN 24

ASN 149 0.25 MET 205 -0.09 ASN 24

ASN 149 0.21 TYR 206 -0.09 ASN 24

ASN 149 0.19 GLN 207 -0.07 ASN 24

ASN 149 0.16 ILE 208 -0.07 MET 291

GLU 119 0.16 GLY 209 -0.08 VAL 333

VAL 74 0.15 LEU 210 -0.07 VAL 333

VAL 74 0.12 PHE 211 -0.07 VAL 332

VAL 74 0.09 ARG 212 -0.06 MET 291

ASN 149 0.07 VAL 213 -0.10 LYS 55

ASN 149 0.06 ALA 214 -0.13 LYS 55

ASN 149 0.07 SER 215 -0.14 LYS 55

GLY 150 0.07 MET 216 -0.17 LYS 55

GLY 150 0.07 ALA 217 -0.17 LYS 55

ILE 151 0.06 SER 218 -0.20 LYS 55

ILE 151 0.07 GLU 219 -0.21 LYS 55

GLY 150 0.08 LYS 220 -0.18 LYS 55

GLY 150 0.09 MET 221 -0.18 LYS 55

ASN 149 0.09 LYS 222 -0.15 LYS 55

ASN 149 0.08 ILE 223 -0.13 LYS 55

ASN 149 0.09 LEU 224 -0.10 MET 291

GLU 119 0.09 GLU 225 -0.07 MET 291

GLU 119 0.13 LEU 226 -0.05 MET 291

VAL 74 0.16 PRO 227 -0.04 MET 234

GLU 119 0.19 PHE 228 -0.05 ALA 229

VAL 74 0.23 ALA 229 -0.05 PHE 228

VAL 74 0.27 SER 229 -0.05 GLY 176

VAL 74 0.22 GLY 230 -0.07 ASN 91

ASP 82 0.22 THR 231 -0.12 PRO 90

ASP 82 0.17 MET 232 -0.09 ASN 91

ASP 82 0.13 SER 233 -0.05 ASN 91

GLU 119 0.11 MET 234 -0.05 MET 291

GLU 119 0.07 LEU 235 -0.08 MET 291

ASN 149 0.10 VAL 236 -0.12 MET 291

ASN 149 0.09 LEU 237 -0.15 MET 291

ASN 149 0.11 LEU 238 -0.16 MET 291

GLY 150 0.10 PRO 239 -0.18 MET 291

GLY 150 0.11 ASP 240 -0.17 MET 291

GLY 150 0.12 GLU 240 -0.19 MET 291

GLY 150 0.14 VAL 241 -0.19 ALA 290

GLY 150 0.12 SER 242 -0.22 ALA 290

GLY 150 0.10 GLY 243 -0.21 MET 291

ILE 151 0.10 LEU 244 -0.23 MET 291

ASN 24 0.13 GLU 245 -0.27 MET 291

ASN 24 0.09 GLN 246 -0.25 MET 291

ASN 24 0.08 LEU 247 -0.22 MET 291

ASN 24 0.10 GLU 248 -0.26 MET 291

ASN 24 0.12 SER 249 -0.29 MET 291

ASN 24 0.09 ILE 250 -0.28 LYS 55

ASN 24 0.08 ILE 251 -0.24 LYS 55

LYS 19 0.07 ASN 252 -0.27 LYS 55

PHE 15 0.08 PHE 253 -0.21 ASP 60

VAL 20 0.06 GLU 254 -0.24 GLY 1

ASN 24 0.06 LYS 255 -0.22 LYS 55

GLY 369 0.06 LEU 256 -0.17 GLY 1

ASN 24 0.05 THR 257 -0.21 GLY 1

ASN 24 0.05 GLU 258 -0.20 GLY 1

PHE 355 0.04 TRP 259 -0.17 GLY 1

PHE 355 0.03 THR 260 -0.14 GLY 1

ASN 24 0.03 SER 261 -0.16 GLY 1

MET 216 0.03 SER 262 -0.12 GLY 1

SER 218 0.04 ASN 263 -0.14 GLY 1

MET 216 0.05 VAL 264 -0.14 GLY 1

ASN 149 0.04 MET 265 -0.11 GLY 1

VAL 74 0.06 GLU 265 -0.08 GLY 1

VAL 74 0.10 GLU 266 -0.06 VAL 332

VAL 74 0.10 ARG 267 -0.07 MET 291

GLU 119 0.12 LYS 268 -0.07 MET 291

ASN 149 0.13 ILE 269 -0.09 MET 291

ASN 149 0.16 LYS 270 -0.09 MET 291

ASN 149 0.17 VAL 271 -0.09 MET 291

ASN 149 0.19 TYR 272 -0.10 MET 291

ASN 149 0.20 LEU 273 -0.10 MET 291

ASN 149 0.23 PRO 274 -0.10 ASN 24

ASN 149 0.28 ARG 275 -0.08 HIS 22

ASN 149 0.25 MET 276 -0.07 HIS 22

ASN 149 0.24 LYS 277 -0.06 LEU 177

ILE 151 0.18 MET 278 -0.06 GLU 324

SER 373 0.14 GLU 279 -0.07 VAL 92

ARG 153 0.10 GLU 280 -0.05 TYR 93

HIS 21 0.07 LYS 281 -0.04 TYR 93

GLU 17 0.06 TYR 282 -0.11 ASN 283

GLN 157 0.09 ASN 283 -0.11 TYR 282

GLN 157 0.06 LEU 284 -0.10 THR 195

GLN 157 0.07 THR 285 -0.13 GLU 245

GLN 157 0.09 SER 286 -0.19 HIS 21

GLN 157 0.06 VAL 287 -0.17 GLU 245

GLY 292 0.08 LEU 288 -0.18 LYS 16

GLY 292 0.10 MET 289 -0.21 GLU 245

GLN 157 0.08 ALA 290 -0.26 VAL 20

GLY 1 0.05 MET 291 -0.32 LYS 16

MET 289 0.10 GLY 292 -0.28 SER 249

LYS 89 0.07 ILE 293 -0.24 SER 249

LYS 89 0.08 THR 294 -0.23 SER 249

PRO 90 0.09 ASP 295 -0.22 SER 249

PRO 90 0.11 VAL 296 -0.18 SER 249

PRO 90 0.09 PHE 297 -0.16 SER 249

PRO 90 0.10 SER 298 -0.18 SER 249

PRO 90 0.11 SER 299 -0.18 SER 249

PRO 90 0.11 SER 300 -0.20 SER 249

PRO 90 0.13 ALA 301 -0.19 SER 249

PRO 90 0.14 ASN 302 -0.18 SER 249

PRO 90 0.17 LEU 303 -0.16 SER 249

PRO 90 0.18 SER 304 -0.15 SER 249

PRO 90 0.20 GLY 305 -0.15 SER 249

PRO 90 0.21 ILE 306 -0.13 SER 249

PRO 90 0.20 SER 307 -0.12 SER 249

PRO 90 0.19 SER 308 -0.14 SER 249

PRO 90 0.17 ALA 309 -0.13 SER 249

PRO 90 0.15 GLU 310 -0.15 SER 249

PRO 90 0.13 SER 311 -0.14 SER 249

PRO 90 0.15 LEU 312 -0.14 SER 249

PRO 90 0.13 LYS 313 -0.15 SER 249

PRO 90 0.12 ILE 314 -0.13 SER 249

PRO 90 0.09 SER 315 -0.11 VAL 20

PHE 297 0.08 GLN 316 -0.08 TYR 282

PRO 90 0.07 ALA 317 -0.07 SER 249

GLY 292 0.06 VAL 318 -0.06 TYR 282

GLY 292 0.05 HIS 319 -0.03 GLN 147

VAL 202 0.07 ALA 320 -0.04 GLN 86

SER 99 0.08 ALA 321 -0.05 TYR 93

THR 148 0.14 HIS 322 -0.07 SER 94

THR 148 0.20 ALA 323 -0.07 VAL 92

ASN 149 0.24 GLU 324 -0.06 GLU 279

ASN 149 0.24 ILE 325 -0.05 ASN 26

ASN 149 0.28 ASN 326 -0.06 MET 276

ASN 149 0.28 GLU 327 -0.06 ASN 24

ASN 149 0.25 ALA 328 -0.06 MET 276

TYR 93 0.24 GLY 329 -0.06 MET 276

GLU 119 0.25 ARG 330 -0.05 LYS 277

GLU 119 0.24 GLU 331 -0.04 VAL 372

GLU 119 0.22 VAL 332 -0.07 PHE 211

GLU 119 0.21 VAL 333 -0.08 GLY 209

GLU 119 0.22 GLY 334 -0.07 ASP 186

GLU 119 0.19 ALA 335 -0.12 ASP 186

GLU 119 0.19 GLU 336 -0.07 ASP 186

GLU 119 0.18 ALA 337 -0.08 ASP 240

ASN 149 0.17 GLY 338 -0.10 GLU 240

GLU 119 0.16 VAL 339 -0.09 ASP 240

ASN 149 0.16 ASP 340 -0.09 ASP 240

ASN 149 0.17 ALA 341 -0.11 ASP 240

ASN 149 0.15 ALA 342 -0.11 ASP 240

ASN 149 0.14 SER 343 -0.10 ASP 240

ASN 149 0.14 VAL 344 -0.11 ASP 240

ASN 149 0.14 SER 345 -0.12 ASP 240

ASN 149 0.12 GLU 346 -0.12 ASP 240

ASN 149 0.14 GLU 346 -0.12 MET 291

ASN 149 0.14 PHE 347 -0.12 MET 291

ASN 149 0.16 ARG 348 -0.13 MET 291

ASN 149 0.16 ALA 349 -0.13 MET 291

ASN 149 0.18 ASP 350 -0.14 ALA 290

GLY 150 0.16 HIS 351 -0.16 ALA 290

GLY 150 0.14 PRO 352 -0.18 MET 291

ILE 151 0.12 PHE 353 -0.16 MET 291

ILE 151 0.10 LEU 354 -0.16 MET 291

ASN 149 0.08 PHE 355 -0.11 MET 291

GLU 119 0.05 CYS 356 -0.08 MET 291

GLU 119 0.09 ILE 357 -0.06 TYR 93

VAL 74 0.08 LYS 358 -0.08 PRO 90

ASP 82 0.12 HIS 359 -0.10 PRO 90

VAL 74 0.11 ILE 360 -0.10 PRO 90

VAL 74 0.11 ALA 361 -0.12 PRO 90

SER 79 0.07 THR 362 -0.09 PRO 90

GLU 336 0.04 ASN 363 -0.08 PRO 90

GLU 336 0.05 ALA 364 -0.07 PRO 90

VAL 74 0.03 VAL 365 -0.06 PRO 90

LEU 120 0.07 LEU 366 -0.06 PRO 90

LEU 120 0.06 PHE 367 -0.05 TYR 93

GLU 254 0.05 PHE 368 -0.08 MET 291

ILE 151 0.07 GLY 369 -0.12 MET 291

ILE 151 0.10 ARG 370 -0.14 MET 291

ILE 151 0.15 CYS 371 -0.13 MET 291

ILE 151 0.16 VAL 372 -0.15 ALA 290

ILE 151 0.21 SER 373 -0.13 HIS 22

ILE 151 0.23 PRO 374 -0.10 HIS 22

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.

*** 1OVA copy ***

CA distance fluctuations for 2402070055341766116

--- normal mode 9 ---

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

* 1OVA copy *