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

* PERIPLASMIC BINDING PROTEIN 25-JUN-97 1ANF *

CA distance fluctuations for 2604251423122313351

--- normal mode 13 ---

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
ALA 84 0.03 LYS 1 -0.05 LYS 370

ALA 84 0.03 ILE 2 -0.05 TYR 341

ALA 84 0.03 GLU 3 -0.05 TYR 341

ALA 84 0.03 GLU 4 -0.04 THR 345

ALA 84 0.04 GLY 5 -0.04 THR 345

ALA 84 0.04 LYS 6 -0.04 THR 345

ALA 84 0.04 LEU 7 -0.05 TYR 341

ALA 84 0.03 VAL 8 -0.05 TYR 341

ALA 84 0.03 ILE 9 -0.05 TYR 341

ALA 84 0.02 TRP 10 -0.06 TYR 341

ALA 84 0.02 ILE 11 -0.06 THR 345

ASN 294 0.02 ASN 12 -0.07 GLU 153

LYS 15 0.03 GLY 13 -0.06 GLN 152

ASN 294 0.02 ASP 14 -0.05 GLU 153

GLY 13 0.03 LYS 15 -0.05 GLY 228

ASN 294 0.03 GLY 16 -0.05 TRP 230

ALA 292 0.03 TYR 17 -0.05 ALA 231

GLY 19 0.04 ASN 18 -0.06 SER 233

ASN 18 0.04 GLY 19 -0.07 LYS 297

ALA 84 0.03 LEU 20 -0.05 LYS 297

ALA 84 0.03 ALA 21 -0.06 ASP 236

ALA 84 0.03 GLU 22 -0.06 LYS 25

ALA 84 0.04 VAL 23 -0.07 VAL 293

ALA 84 0.04 GLY 24 -0.05 ASP 236

ALA 84 0.04 LYS 25 -0.06 GLU 22

ALA 84 0.04 LYS 26 -0.05 ALA 292

ALA 84 0.04 PHE 27 -0.05 ASN 124

ALA 84 0.04 GLU 28 -0.05 ASP 236

ALA 84 0.04 LYS 29 -0.06 ASP 236

ALA 84 0.04 ASP 30 -0.05 ASN 124

ALA 84 0.05 THR 31 -0.04 ASN 124

ALA 84 0.04 GLY 32 -0.05 THR 237

ALA 84 0.04 ILE 33 -0.05 THR 237

ALA 84 0.04 LYS 34 -0.05 THR 237

ALA 84 0.04 VAL 35 -0.05 THR 237

ALA 84 0.03 THR 36 -0.06 THR 237

ALA 84 0.03 VAL 37 -0.05 THR 345

ALA 84 0.03 GLU 38 -0.06 THR 345

ALA 84 0.02 HIS 39 -0.06 THR 345

ALA 84 0.02 PRO 40 -0.07 THR 345

ALA 292 0.02 ASP 41 -0.08 THR 345

LEU 43 0.02 LYS 42 -0.09 THR 345

LYS 42 0.02 LEU 43 -0.08 TYR 341

PHE 67 0.02 GLU 44 -0.09 TYR 341

TYR 70 0.02 GLU 45 -0.11 TYR 341

GLY 143 0.01 LYS 46 -0.08 TYR 341

ALA 84 0.01 PHE 47 -0.08 TYR 341

GLY 143 0.01 PRO 48 -0.08 TYR 341

GLY 143 0.01 GLN 49 -0.08 TYR 341

ALA 84 0.02 VAL 50 -0.07 TYR 341

ALA 84 0.02 ALA 51 -0.06 LYS 370

LYS 102 0.01 ALA 52 -0.07 LYS 370

ALA 84 0.02 THR 53 -0.06 LYS 370

ALA 84 0.02 GLY 54 -0.05 LYS 370

ALA 84 0.02 ASP 55 -0.05 TYR 341

ALA 84 0.02 GLY 56 -0.06 TYR 341

ALA 84 0.03 PRO 57 -0.06 TYR 341

ALA 84 0.03 ASP 58 -0.05 TYR 341

ALA 84 0.03 ILE 59 -0.05 TYR 341

ALA 84 0.02 ILE 60 -0.06 TYR 341

LYS 42 0.02 PHE 61 -0.05 TYR 341

LYS 42 0.02 TRP 62 -0.06 TYR 341

ALA 215 0.02 ALA 63 -0.05 TYR 341

GLY 68 0.02 HIS 64 -0.04 ALA 168

SER 211 0.02 ASP 65 -0.04 ALA 168

SER 211 0.02 ARG 66 -0.05 SER 337

ALA 318 0.02 PHE 67 -0.06 LYS 370

ALA 318 0.02 GLY 68 -0.06 LYS 370

SER 211 0.02 GLY 69 -0.08 LYS 370

GLU 45 0.02 TYR 70 -0.07 LYS 370

GLU 45 0.02 ALA 71 -0.06 LYS 370

ALA 318 0.02 GLN 72 -0.07 LYS 370

ALA 318 0.02 SER 73 -0.07 LYS 370

LYS 102 0.02 GLY 74 -0.06 LYS 370

LYS 102 0.02 LEU 75 -0.06 LYS 370

ILE 104 0.02 LEU 76 -0.06 LYS 370

ALA 268 0.03 ALA 77 -0.05 LYS 370

ALA 268 0.02 GLU 78 -0.05 LYS 370

ALA 268 0.02 ILE 79 -0.05 GLY 174

SER 270 0.02 THR 80 -0.05 GLY 174

LYS 273 0.03 PRO 81 -0.06 GLY 174

GLU 274 0.04 ASP 82 -0.07 GLY 174

PHE 85 0.05 LYS 83 -0.10 GLY 174

PHE 85 0.09 ALA 84 -0.08 GLY 174

ALA 84 0.09 PHE 85 -0.06 GLY 174

ASP 87 0.02 GLN 86 -0.07 GLY 174

GLN 86 0.02 ASP 87 -0.08 GLY 174

ASN 18 0.02 LYS 88 -0.06 GLY 174

THR 237 0.02 LEU 89 -0.06 GLY 174

PRO 91 0.04 TYR 90 -0.07 GLN 325

TYR 90 0.04 PRO 91 -0.09 GLY 174

LYS 313 0.03 PHE 92 -0.08 GLY 174

ALA 312 0.03 THR 93 -0.07 GLU 328

LYS 313 0.02 TRP 94 -0.08 GLY 174

LYS 313 0.03 ASP 95 -0.10 GLY 174

ALA 318 0.03 ALA 96 -0.07 GLY 174

ALA 312 0.02 VAL 97 -0.06 GLY 174

ALA 318 0.02 ARG 98 -0.07 GLY 174

ALA 318 0.02 TYR 99 -0.06 LYS 175

ALA 318 0.02 ASN 100 -0.05 LYS 370

ALA 318 0.02 GLY 101 -0.07 GLY 174

LEU 76 0.02 LYS 102 -0.06 GLY 174

ALA 268 0.02 LEU 103 -0.06 GLY 174

LEU 76 0.02 ILE 104 -0.05 LYS 370

PRO 91 0.01 ALA 105 -0.05 LYS 370

PRO 91 0.02 TYR 106 -0.05 GLY 174

ALA 264 0.02 PRO 107 -0.05 GLY 174

GLY 13 0.02 ILE 108 -0.05 ALA 109

ALA 312 0.02 ALA 109 -0.05 ILE 108

ALA 96 0.03 VAL 110 -0.05 ALA 324

ALA 318 0.02 GLU 111 -0.04 LEU 284

VAL 259 0.03 ALA 112 -0.05 LEU 247

GLY 327 0.02 LEU 113 -0.05 GLY 300

TYR 242 0.03 SER 114 -0.05 GLY 300

LEU 247 0.03 LEU 115 -0.05 GLY 19

TYR 242 0.03 ILE 116 -0.05 GLY 19

PRO 248 0.04 TYR 117 -0.05 GLY 19

THR 249 0.03 ASN 118 -0.04 LYS 29

PRO 125 0.04 LYS 119 -0.05 LYS 29

THR 249 0.03 ASP 120 -0.04 LYS 29

ILE 132 0.02 LEU 121 -0.04 LYS 29

TRP 129 0.04 LEU 122 -0.05 PRO 315

GLY 252 0.04 PRO 123 -0.07 PRO 315

LYS 127 0.05 ASN 124 -0.08 PRO 315

LYS 119 0.04 PRO 125 -0.06 ALA 318

TRP 129 0.05 PRO 126 -0.06 ALA 318

ASN 124 0.05 LYS 127 -0.06 GLU 322

ASN 124 0.05 THR 128 -0.06 PRO 248

PRO 126 0.05 TRP 129 -0.04 GLU 322

ASN 124 0.05 GLU 130 -0.04 ALA 134

ASN 124 0.04 GLU 131 -0.05 GLU 322

LEU 122 0.03 ILE 132 -0.04 GLU 322

GLY 353 0.03 PRO 133 -0.04 GLU 322

GLY 353 0.03 ALA 134 -0.05 GLU 322

GLY 353 0.03 LEU 135 -0.05 VAL 246

GLY 353 0.03 ASP 136 -0.04 VAL 246

LYS 200 0.04 LYS 137 -0.04 VAL 246

GLY 353 0.03 GLU 138 -0.05 PRO 126

ILE 212 0.02 LEU 139 -0.04 PRO 125

ASN 205 0.03 LYS 140 -0.03 PRO 125

ASN 205 0.04 ALA 141 -0.04 PRO 125

ILE 212 0.04 LYS 142 -0.04 PRO 125

ILE 212 0.05 GLY 143 -0.02 LEU 121

ILE 212 0.03 LYS 144 -0.02 LYS 29

ILE 212 0.03 SER 145 -0.03 LYS 29

LEU 195 0.02 ALA 146 -0.03 LYS 29

ALA 364 0.02 LEU 147 -0.03 LYS 25

PHE 149 0.02 MET 148 -0.03 LYS 25

MET 148 0.02 PHE 149 -0.04 ASP 14

GLY 143 0.03 ASN 150 -0.05 ASN 12

GLY 143 0.03 LEU 151 -0.05 ASP 41

TYR 341 0.03 GLN 152 -0.07 ASP 41

SER 337 0.03 GLU 153 -0.07 ASN 12

ILE 178 0.02 PRO 154 -0.06 ASN 12

SER 337 0.02 TYR 155 -0.06 ASN 12

ILE 178 0.02 PHE 156 -0.05 ASN 12

MET 148 0.02 THR 157 -0.05 ASN 12

LEU 115 0.02 TRP 158 -0.05 TRP 62

LEU 115 0.03 PRO 159 -0.05 VAL 259

TYR 117 0.03 LEU 160 -0.04 THR 93

PRO 126 0.03 ILE 161 -0.04 THR 93

LEU 115 0.03 ALA 162 -0.05 PHE 92

LYS 119 0.03 ALA 163 -0.05 PHE 92

ASN 124 0.03 ASP 164 -0.05 PHE 92

ASN 124 0.03 GLY 165 -0.05 PHE 92

ASN 124 0.02 GLY 166 -0.05 PHE 92

LYS 326 0.03 TYR 167 -0.05 LYS 83

LYS 326 0.03 ALA 168 -0.05 LYS 83

GLN 325 0.03 PHE 169 -0.05 LYS 83

GLN 325 0.03 LYS 170 -0.06 LYS 83

GLN 325 0.03 TYR 171 -0.07 LYS 83

GLN 325 0.02 GLU 172 -0.07 LYS 83

ASP 180 0.03 ASN 173 -0.09 LYS 83

LYS 179 0.02 GLY 174 -0.10 LYS 83

ASP 209 0.01 LYS 175 -0.08 LYS 83

GLN 325 0.02 TYR 176 -0.07 LYS 83

ALA 342 0.02 ASP 177 -0.06 LYS 83

PHE 339 0.03 ILE 178 -0.06 LYS 83

ASN 173 0.02 LYS 179 -0.05 LYS 83

ASN 173 0.03 ASP 180 -0.05 LYS 83

LYS 326 0.02 VAL 181 -0.05 LYS 83

LYS 326 0.02 GLY 182 -0.05 LYS 83

PRO 126 0.02 VAL 183 -0.05 GLU 45

PRO 126 0.03 ASP 184 -0.05 GLU 45

ASN 124 0.03 ASN 185 -0.04 LYS 83

ASN 124 0.03 ALA 186 -0.04 LYS 83

ASN 124 0.03 GLY 187 -0.05 LYS 83

ASN 124 0.03 ALA 188 -0.04 LYS 83

ASN 124 0.03 LYS 189 -0.05 LYS 42

ASN 124 0.04 ALA 190 -0.04 LYS 83

PRO 126 0.04 GLY 191 -0.04 THR 93

PRO 126 0.03 LEU 192 -0.05 ASP 41

VAL 357 0.04 THR 193 -0.05 ASP 41

GLU 130 0.03 PHE 194 -0.04 ASN 12

PRO 126 0.03 LEU 195 -0.04 ASN 12

PRO 133 0.03 VAL 196 -0.04 ASP 41

GLY 353 0.04 ASP 197 -0.04 ASN 12

GLY 353 0.03 LEU 198 -0.03 ASN 12

LYS 137 0.04 ILE 199 -0.04 ASN 12

ASN 201 0.06 LYS 200 -0.03 ASP 41

LYS 200 0.06 ASN 201 -0.03 TYR 90

GLY 353 0.04 LYS 202 -0.03 LYS 29

LYS 137 0.04 HIS 203 -0.03 LYS 29

ILE 348 0.03 MET 204 -0.03 LYS 29

ALA 141 0.04 ASN 205 -0.03 HIS 39

ILE 348 0.04 ALA 206 -0.04 ASP 41

ALA 141 0.04 ASP 207 -0.05 SER 352

GLY 143 0.04 THR 208 -0.03 HIS 39

GLY 143 0.03 ASP 209 -0.04 SER 352

GLY 143 0.03 TYR 210 -0.04 HIS 39

GLY 143 0.04 SER 211 -0.04 SER 238

GLY 143 0.05 ILE 212 -0.03 ARG 354

GLY 143 0.03 ALA 213 -0.03 THR 36

ALA 215 0.03 GLU 214 -0.03 THR 36

GLY 143 0.03 ALA 215 -0.03 ARG 354

GLY 143 0.04 ALA 216 -0.03 ASN 205

GLY 143 0.02 PHE 217 -0.03 LYS 29

LYS 219 0.03 ASN 218 -0.03 LYS 29

ASN 218 0.03 LYS 219 -0.02 LYS 29

SER 238 0.02 GLY 220 -0.03 LYS 29

LYS 142 0.03 GLU 221 -0.02 LYS 29

SER 337 0.02 THR 222 -0.03 LYS 29

TRP 129 0.02 ALA 223 -0.04 LYS 29

LEU 160 0.02 MET 224 -0.04 GLY 19

TYR 167 0.02 THR 225 -0.04 GLY 19

TYR 167 0.02 ILE 226 -0.05 ASN 227

GLY 327 0.02 ASN 227 -0.05 ILE 226

VAL 259 0.02 GLY 228 -0.05 GLY 19

ASN 234 0.02 PRO 229 -0.05 GLY 19

ALA 215 0.02 TRP 230 -0.05 GLY 19

ALA 215 0.02 ALA 231 -0.05 ASN 18

ASN 234 0.03 TRP 232 -0.06 GLY 19

GLU 310 0.04 SER 233 -0.06 ASN 18

GLU 310 0.03 ASN 234 -0.06 ASN 18

LYS 219 0.02 ILE 235 -0.06 ASN 18

THR 237 0.04 ASP 236 -0.06 ASN 18

GLU 310 0.05 THR 237 -0.06 ASN 18

GLU 310 0.03 SER 238 -0.05 ASN 18

GLU 310 0.03 LYS 239 -0.05 LYS 25

THR 245 0.03 VAL 240 -0.05 LYS 29

THR 249 0.03 ASN 241 -0.05 LYS 29

THR 245 0.04 TYR 242 -0.05 LYS 25

THR 245 0.04 GLY 243 -0.06 LYS 295

THR 245 0.03 VAL 244 -0.05 ASN 124

GLY 243 0.04 THR 245 -0.05 ILE 317

PRO 254 0.03 VAL 246 -0.05 ALA 301

TYR 242 0.04 LEU 247 -0.05 ALA 301

LYS 119 0.04 PRO 248 -0.06 THR 128

ASN 124 0.04 THR 249 -0.05 TYR 90

ASN 124 0.04 PHE 250 -0.05 TYR 90

ASN 124 0.04 LYS 251 -0.05 PHE 92

ASN 124 0.05 GLY 252 -0.05 TYR 90

ASN 124 0.04 GLN 253 -0.05 TYR 90

TYR 242 0.03 PRO 254 -0.05 TYR 90

LEU 115 0.03 SER 255 -0.05 TYR 90

LEU 115 0.03 LYS 256 -0.06 VAL 259

GLY 327 0.03 PRO 257 -0.05 VAL 259

TYR 242 0.02 PHE 258 -0.07 VAL 259

ALA 112 0.03 VAL 259 -0.07 PHE 258

ALA 318 0.02 GLY 260 -0.05 VAL 261

ALA 312 0.02 VAL 261 -0.06 PHE 258

ALA 312 0.02 LEU 262 -0.05 PHE 258

LYS 42 0.02 SER 263 -0.05 PHE 258

PRO 107 0.02 ALA 264 -0.05 TYR 341

ALA 84 0.02 GLY 265 -0.05 TYR 341

ALA 84 0.02 ILE 266 -0.05 LYS 370

ALA 84 0.02 ASN 267 -0.05 LYS 370

ALA 77 0.03 ALA 268 -0.05 LYS 370

ALA 84 0.02 ALA 269 -0.05 LYS 370

ALA 84 0.03 SER 270 -0.05 LYS 370

ALA 84 0.03 PRO 271 -0.04 LYS 370

ALA 84 0.04 ASN 272 -0.04 TYR 341

ALA 84 0.04 LYS 273 -0.05 LYS 370

ALA 84 0.05 GLU 274 -0.04 LYS 370

ALA 84 0.05 LEU 275 -0.04 TYR 341

ALA 84 0.04 ALA 276 -0.04 TYR 341

ALA 84 0.05 LYS 277 -0.04 LYS 370

ALA 84 0.06 GLU 278 -0.04 LYS 370

ALA 84 0.05 PHE 279 -0.04 TYR 341

ALA 84 0.05 LEU 280 -0.04 GLY 174

ALA 84 0.06 GLU 281 -0.05 GLY 174

ALA 84 0.07 ASN 282 -0.04 GLY 174

ALA 84 0.05 TYR 283 -0.04 ASN 124

ALA 84 0.04 LEU 284 -0.05 ALA 109

ALA 84 0.04 LEU 285 -0.04 GLY 174

ALA 84 0.04 THR 286 -0.04 GLN 325

ALA 84 0.03 ASP 287 -0.05 ASN 124

ALA 84 0.03 GLU 288 -0.05 ASN 124

ALA 84 0.04 GLY 289 -0.05 ASN 124

TYR 17 0.03 LEU 290 -0.05 ASN 124

ALA 84 0.02 GLU 291 -0.05 ASN 124

GLY 19 0.04 ALA 292 -0.05 LYS 26

GLY 16 0.02 VAL 293 -0.07 VAL 23

GLY 16 0.03 ASN 294 -0.05 ASN 124

ALA 84 0.02 LYS 295 -0.06 GLY 243

GLY 13 0.02 ASP 296 -0.06 GLY 19

GLU 310 0.02 LYS 297 -0.07 GLY 19

SER 233 0.03 PRO 298 -0.05 GLY 19

SER 233 0.02 LEU 299 -0.05 VAL 23

SER 233 0.03 GLY 300 -0.06 THR 320

ALA 312 0.03 ALA 301 -0.06 ALA 324

THR 237 0.02 VAL 302 -0.05 GLN 325

THR 237 0.02 ALA 303 -0.07 GLN 325

THR 237 0.02 LEU 304 -0.06 GLN 325

THR 237 0.03 LYS 305 -0.07 GLN 325

THR 237 0.03 SER 306 -0.06 GLN 325

THR 237 0.03 TYR 307 -0.05 GLN 325

THR 237 0.03 GLU 308 -0.06 GLN 325

THR 237 0.04 GLU 309 -0.06 GLN 325

THR 237 0.05 GLU 310 -0.05 ASN 124

THR 237 0.04 LEU 311 -0.06 ASN 124

THR 237 0.04 ALA 312 -0.06 ASN 124

THR 237 0.03 LYS 313 -0.07 ASN 124

THR 237 0.04 ASP 314 -0.07 ASN 124

THR 237 0.03 PRO 315 -0.08 ASN 124

THR 237 0.03 ARG 316 -0.06 ASN 124

THR 237 0.03 ILE 317 -0.06 ASN 124

ILE 329 0.03 ALA 318 -0.07 ASN 124

LYS 239 0.03 ALA 319 -0.06 ASN 124

ILE 329 0.03 THR 320 -0.06 ALA 301

ILE 329 0.04 MET 321 -0.06 ALA 301

ILE 329 0.03 GLU 322 -0.06 LYS 127

GLY 327 0.03 ASN 323 -0.06 ALA 301

ILE 329 0.03 ALA 324 -0.06 ALA 303

GLU 328 0.03 GLN 325 -0.07 TYR 90

TYR 167 0.03 LYS 326 -0.06 TYR 90

ASN 323 0.03 GLY 327 -0.06 TYR 90

GLN 325 0.03 GLU 328 -0.07 PHE 92

MET 321 0.04 ILE 329 -0.07 GLU 328

MET 321 0.03 MET 330 -0.05 THR 93

MET 321 0.02 PRO 331 -0.05 LYS 83

MET 321 0.02 ASN 332 -0.05 LYS 83

MET 321 0.02 ILE 333 -0.05 LYS 370

SER 211 0.02 PRO 334 -0.07 LYS 370

ASP 209 0.02 GLN 335 -0.07 LYS 370

TYR 210 0.02 MET 336 -0.05 LYS 370

ASP 209 0.03 SER 337 -0.07 PRO 48

GLN 152 0.02 ALA 338 -0.06 PRO 48

ILE 178 0.03 PHE 339 -0.06 GLU 44

GLN 152 0.02 TRP 340 -0.07 GLU 44

ALA 206 0.03 TYR 341 -0.11 GLU 45

ILE 178 0.03 ALA 342 -0.08 GLU 45

ILE 178 0.02 VAL 343 -0.07 GLU 45

ALA 206 0.03 ARG 344 -0.08 LYS 42

ALA 206 0.03 THR 345 -0.09 LYS 42

ALA 364 0.03 ALA 346 -0.08 LYS 42

ALA 364 0.03 VAL 347 -0.07 LYS 42

ALA 206 0.04 ILE 348 -0.08 LYS 42

LYS 202 0.03 ASN 349 -0.08 LYS 42

LYS 137 0.03 ALA 350 -0.06 LYS 42

LYS 137 0.03 ALA 351 -0.05 ASP 41

LYS 202 0.04 SER 352 -0.06 ASP 41

ASN 201 0.05 GLY 353 -0.06 ASP 41

ASN 201 0.04 ARG 354 -0.07 LYS 42

ASN 201 0.03 GLN 355 -0.07 LYS 42

THR 193 0.04 THR 356 -0.06 LYS 42

THR 193 0.04 VAL 357 -0.06 LYS 42

GLU 130 0.03 ASP 358 -0.06 LYS 42

THR 193 0.03 GLU 359 -0.06 LYS 42

THR 193 0.03 ALA 360 -0.07 LYS 42

PRO 126 0.03 LEU 361 -0.06 GLU 45

PRO 126 0.02 LYS 362 -0.06 GLU 45

THR 366 0.03 ASP 363 -0.07 GLU 45

ALA 346 0.03 ALA 364 -0.07 GLU 45

PRO 126 0.02 GLN 365 -0.06 GLU 45

LYS 370 0.03 THR 366 -0.06 GLN 49

THR 369 0.03 ARG 367 -0.07 GLN 49

ILE 178 0.03 ILE 368 -0.06 PRO 48

ARG 367 0.03 THR 369 -0.06 GLY 69

THR 366 0.03 LYS 370 -0.08 GLY 69

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.

*** PERIPLASMIC BINDING PROTEIN 25-JUN-97 1ANF ***

CA distance fluctuations for 2604251423122313351

--- normal mode 13 ---

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

* PERIPLASMIC BINDING PROTEIN 25-JUN-97 1ANF *