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

* 1xmm_test *

CA strain for 2402071547251848064

--- normal mode 9 ---

This graph displays the distance variation between successive pairs of CA atoms in the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Large distance variations can be an indicator for residue pairs that support the important strain in that particular normal mode movement. Note that residue pairs between chain breaks or at flexible ends of the protein may also exhibit large CA-CA distance variations. If more than one residues ae grouped together into a rigid block (NRBL>1), CA-CA distance variations between CA atoms in the same block will be very low.

This feature is still experimental and will be further developped in the future.

CA i CA i+1 vari
VAL 40 ARG 41 -0.0002

ARG 41 LEU 42 0.0001

LEU 42 PRO 43 -0.0589

PRO 43 PHE 44 -0.0003

PHE 44 SER 45 -0.0000

SER 45 GLY 46 0.0616

GLY 46 PHE 47 0.0003

PHE 47 ARG 48 -0.0001

ARG 48 LEU 49 0.0802

LEU 49 GLN 50 0.0000

GLN 50 LYS 51 -0.0002

LYS 51 VAL 52 0.0677

VAL 52 LEU 53 0.0001

LEU 53 ARG 54 0.0001

ARG 54 GLU 55 0.0530

GLU 55 SER 56 0.0002

SER 56 ALA 57 -0.0001

ALA 57 ARG 58 0.0283

ARG 58 ASP 59 0.0001

ASP 59 LYS 60 0.0001

LYS 60 ILE 61 0.0712

ILE 61 ILE 62 -0.0002

ILE 62 PHE 63 0.0003

PHE 63 LEU 64 0.0471

LEU 64 HIS 65 0.0001

HIS 65 GLY 66 0.0001

GLY 66 LYS 67 0.0722

LYS 67 VAL 68 -0.0001

VAL 68 ASN 69 0.0000

ASN 69 ASP 79 -0.0203

ASP 79 ALA 80 0.0003

ALA 80 VAL 81 -0.0002

VAL 81 VAL 82 -0.0184

VAL 82 ILE 83 -0.0000

ILE 83 LEU 84 0.0004

LEU 84 GLU 85 0.0031

GLU 85 LYS 86 -0.0001

LYS 86 THR 87 0.0001

THR 87 PRO 88 0.0253

PRO 88 PHE 89 0.0004

PHE 89 GLN 90 -0.0001

GLN 90 VAL 91 0.0405

VAL 91 GLU 92 -0.0000

GLU 92 GLN 93 0.0001

GLN 93 VAL 94 -0.0088

VAL 94 ALA 95 0.0001

ALA 95 GLN 96 -0.0000

GLN 96 LEU 97 0.0209

LEU 97 LEU 98 -0.0001

LEU 98 THR 99 0.0000

THR 99 GLY 100 -0.0051

GLY 100 SER 101 -0.0004

SER 101 PRO 102 -0.0002

PRO 102 GLU 103 -0.0631

GLU 103 LEU 104 -0.0003

LEU 104 GLN 105 0.0000

GLN 105 LEU 106 0.0462

LEU 106 GLN 107 0.0002

GLN 107 PHE 108 0.0002

PHE 108 SER 109 -0.0281

SER 109 ASN 110 0.0002

ASN 110 ASP 111 -0.0000

ASP 111 ILE 112 0.0113

ILE 112 TYR 113 -0.0004

TYR 113 SER 114 0.0004

SER 114 THR 115 -0.0205

THR 115 TYR 116 0.0001

TYR 116 HIS 117 -0.0002

HIS 117 LEU 118 0.0974

LEU 118 PHE 119 -0.0002

PHE 119 PRO 120 0.0002

PRO 120 PRO 121 0.1264

PRO 121 ARG 122 0.0004

ARG 122 GLN 123 -0.0002

GLN 123 LEU 124 -0.0319

LEU 124 ASN 125 0.0001

ASN 125 ASP 126 -0.0004

ASP 126 VAL 127 0.0589

VAL 127 LYS 128 0.0002

LYS 128 THR 129 0.0000

THR 129 THR 130 0.0403

THR 130 VAL 131 0.0000

VAL 131 VAL 132 -0.0001

VAL 132 TYR 133 0.0137

TYR 133 PRO 134 0.0004

PRO 134 ALA 135 -0.0001

ALA 135 THR 136 0.0032

THR 136 GLU 137 0.0000

GLU 137 LYS 138 0.0003

LYS 138 HIS 139 0.0230

HIS 139 LEU 140 0.0002

LEU 140 GLN 141 -0.0004

GLN 141 LYS 142 0.0701

LYS 142 TYR 143 0.0001

TYR 143 LEU 144 -0.0000

LEU 144 ARG 145 0.1434

ARG 145 GLN 146 -0.0004

GLN 146 ASP 147 -0.0000

ASP 147 LEU 148 0.1609

LEU 148 ARG 149 0.0002

ARG 149 LEU 150 -0.0001

LEU 150 ILE 151 0.1293

ILE 151 ARG 152 0.0002

ARG 152 GLU 153 -0.0003

GLU 153 THR 154 0.0614

THR 154 GLY 155 -0.0004

GLY 155 ASP 156 0.0002

ASP 156 ASP 157 0.0072

ASP 157 TYR 158 -0.0003

TYR 158 ARG 159 0.0001

ARG 159 ASN 160 0.0031

ASN 160 ILE 161 0.0003

ILE 161 THR 162 -0.0001

THR 162 LEU 163 0.0210

LEU 163 PRO 164 0.0001

PRO 164 HIS 165 0.0002

HIS 165 LEU 166 -0.0204

LEU 166 GLU 167 0.0003

GLU 167 SER 168 0.0002

SER 168 GLN 169 -0.0099

GLN 169 SER 170 -0.0000

SER 170 LEU 171 -0.0001

LEU 171 SER 172 -0.0504

SER 172 ILE 173 -0.0001

ILE 173 GLN 174 0.0004

GLN 174 TRP 175 0.0066

TRP 175 VAL 176 0.0000

VAL 176 TYR 177 -0.0001

TYR 177 ASN 178 0.0033

ASN 178 ILE 179 -0.0001

ILE 179 LEU 180 -0.0002

LEU 180 ASP 181 0.0037

ASP 181 LYS 182 0.0000

LYS 182 LYS 183 0.0000

LYS 183 ALA 184 0.0312

ALA 184 GLU 185 0.0001

GLU 185 ALA 186 0.0002

ALA 186 ASP 187 -0.0046

ASP 187 ARG 188 0.0000

ARG 188 ILE 189 0.0001

ILE 189 VAL 190 -0.0034

VAL 190 PHE 191 0.0001

PHE 191 GLU 192 -0.0000

GLU 192 ASN 193 0.0185

ASN 193 PRO 194 -0.0001

PRO 194 ASP 195 0.0003

ASP 195 PRO 196 -0.0039

PRO 196 SER 197 0.0002

SER 197 ASP 198 0.0000

ASP 198 GLY 199 0.0153

GLY 199 PHE 200 0.0001

PHE 200 VAL 201 0.0001

VAL 201 LEU 202 0.0043

LEU 202 ILE 203 0.0002

ILE 203 PRO 204 -0.0004

PRO 204 ASP 205 -0.0034

ASP 205 LEU 206 -0.0001

LEU 206 LYS 207 0.0001

LYS 207 TRP 208 0.0143

TRP 208 ASN 209 0.0000

ASN 209 GLN 210 -0.0000

GLN 210 GLN 211 -0.0084

GLN 211 GLN 212 -0.0000

GLN 212 LEU 213 -0.0000

LEU 213 ASP 214 -0.0253

ASP 214 ASP 215 0.0003

ASP 215 LEU 216 -0.0002

LEU 216 TYR 217 -0.0095

TYR 217 LEU 218 -0.0002

LEU 218 ILE 219 0.0001

ILE 219 ALA 220 0.0100

ALA 220 ILE 221 0.0001

ILE 221 CYS 222 0.0003

CYS 222 HIS 223 0.0024

HIS 223 ARG 224 -0.0001

ARG 224 ARG 225 -0.0002

ARG 225 GLY 226 0.0551

GLY 226 ILE 227 -0.0000

ILE 227 ARG 228 0.0001

ARG 228 SER 229 0.0086

SER 229 LEU 230 0.0001

LEU 230 ARG 231 0.0001

ARG 231 ASP 232 0.0504

ASP 232 LEU 233 0.0000

LEU 233 THR 234 -0.0003

THR 234 PRO 235 0.0223

PRO 235 GLU 236 0.0003

GLU 236 HIS 237 0.0000

HIS 237 LEU 238 -0.0164

LEU 238 PRO 239 0.0002

PRO 239 LEU 240 -0.0002

LEU 240 LEU 241 -0.0126

LEU 241 ARG 242 -0.0000

ARG 242 ASN 243 -0.0001

ASN 243 ILE 244 -0.0051

ILE 244 LEU 245 0.0002

LEU 245 HIS 246 -0.0000

HIS 246 GLN 247 0.0519

GLN 247 GLY 248 0.0004

GLY 248 GLN 249 -0.0002

GLN 249 GLU 250 0.0141

GLU 250 ALA 251 -0.0001

ALA 251 ILE 252 0.0000

ILE 252 LEU 253 -0.0100

LEU 253 GLN 254 -0.0001

GLN 254 ARG 255 -0.0002

ARG 255 TYR 256 -0.0009

TYR 256 ARG 257 -0.0001

ARG 257 MET 258 -0.0000

MET 258 LYS 259 0.1440

LYS 259 GLY 260 -0.0001

GLY 260 ASP 261 0.0001

ASP 261 HIS 262 0.0404

HIS 262 LEU 263 0.0002

LEU 263 ARG 264 0.0000

ARG 264 VAL 265 -0.0315

VAL 265 TYR 266 -0.0004

TYR 266 LEU 267 0.0001

LEU 267 HIS 268 0.0021

HIS 268 TYR 269 -0.0002

TYR 269 LEU 270 0.0000

LEU 270 PRO 271 -0.0187

PRO 271 SER 272 0.0000

SER 272 TYR 273 -0.0001

TYR 273 TYR 274 -0.0102

TYR 274 HIS 275 -0.0002

HIS 275 LEU 276 -0.0001

LEU 276 HIS 277 -0.0056

HIS 277 VAL 278 -0.0002

VAL 278 HIS 279 0.0001

HIS 279 PHE 280 0.0110

PHE 280 THR 281 0.0002

THR 281 ALA 282 -0.0002

ALA 282 LEU 283 0.0537

LEU 283 GLY 284 -0.0003

GLY 284 PHE 285 0.0000

PHE 285 GLU 286 -0.0941

GLU 286 ALA 287 0.0000

ALA 287 PRO 288 0.0003

PRO 288 GLY 289 0.0277

GLY 289 SER 290 -0.0003

SER 290 GLY 291 -0.0001

GLY 291 VAL 292 -0.0764

VAL 292 GLU 293 0.0000

GLU 293 ARG 294 -0.0000

ARG 294 ALA 295 0.0288

ALA 295 HIS 296 0.0000

HIS 296 LEU 297 0.0001

LEU 297 LEU 298 -0.0023

LEU 298 ALA 299 -0.0001

ALA 299 GLU 300 -0.0001

GLU 300 VAL 301 -0.0400

VAL 301 ILE 302 -0.0001

ILE 302 GLU 303 -0.0004

GLU 303 ASN 304 -0.0348

ASN 304 LEU 305 0.0002

LEU 305 GLU 306 0.0001

GLU 306 CYS 307 0.0245

CYS 307 ASP 308 0.0002

ASP 308 PRO 309 -0.0000

PRO 309 ARG 310 -0.0015

ARG 310 HIS 311 0.0001

HIS 311 TYR 312 -0.0002

TYR 312 GLN 313 -0.0130

GLN 313 GLN 314 0.0002

GLN 314 ARG 315 -0.0003

ARG 315 THR 316 0.0590

THR 316 LEU 317 -0.0000

LEU 317 THR 318 0.0001

THR 318 PHE 319 0.0471

PHE 319 ALA 320 0.0001

ALA 320 LEU 321 0.0000

LEU 321 ARG 322 0.1895

ARG 322 ALA 323 -0.0001

ALA 323 ASP 324 -0.0003

ASP 324 ASP 325 0.1577

ASP 325 PRO 326 0.0000

PRO 326 LEU 327 -0.0003

LEU 327 LEU 328 0.0181

LEU 328 LYS 329 0.0002

LYS 329 LEU 330 0.0002

LEU 330 LEU 331 -0.0245

LEU 331 GLN 332 -0.0000

GLN 332 GLU 333 0.0003

GLU 333 ALA 334 0.0045

ALA 334 GLN 335 0.0001

GLN 335 GLN 336 0.0005

GLN 336 VAL 40 0.0676

VAL 40 ARG 41 -0.0000

ARG 41 LEU 42 -0.0002

LEU 42 PRO 43 -0.0331

PRO 43 PHE 44 -0.0002

PHE 44 SER 45 0.0003

SER 45 GLY 46 0.0141

GLY 46 PHE 47 -0.0000

PHE 47 ARG 48 0.0000

ARG 48 LEU 49 -0.0123

LEU 49 GLN 50 -0.0004

GLN 50 LYS 51 0.0001

LYS 51 VAL 52 0.0799

VAL 52 LEU 53 -0.0000

LEU 53 ARG 54 -0.0001

ARG 54 GLU 55 0.0055

GLU 55 SER 56 -0.0001

SER 56 ALA 57 -0.0002

ALA 57 ARG 58 0.0004

ARG 58 ASP 59 -0.0000

ASP 59 LYS 60 -0.0000

LYS 60 ILE 61 0.0365

ILE 61 ILE 62 0.0003

ILE 62 PHE 63 -0.0002

PHE 63 LEU 64 0.0492

LEU 64 HIS 65 0.0000

HIS 65 GLY 66 -0.0001

GLY 66 LYS 67 0.0359

LYS 67 VAL 68 -0.0003

VAL 68 GLU 78 -0.0282

GLU 78 ASP 79 0.0002

ASP 79 ALA 80 -0.0000

ALA 80 VAL 81 0.0118

VAL 81 VAL 82 -0.0004

VAL 82 ILE 83 0.0001

ILE 83 LEU 84 -0.0151

LEU 84 GLU 85 -0.0002

GLU 85 LYS 86 0.0003

LYS 86 THR 87 0.0553

THR 87 PRO 88 0.0001

PRO 88 PHE 89 0.0002

PHE 89 GLN 90 0.0170

GLN 90 VAL 91 0.0000

VAL 91 GLU 92 0.0001

GLU 92 GLN 93 -0.0424

GLN 93 VAL 94 0.0001

VAL 94 ALA 95 0.0001

ALA 95 GLN 96 -0.0013

GLN 96 LEU 97 0.0002

LEU 97 LEU 98 -0.0002

LEU 98 THR 99 -0.0101

THR 99 GLY 100 0.0001

GLY 100 SER 101 -0.0001

SER 101 PRO 102 -0.0634

PRO 102 GLU 103 -0.0002

GLU 103 LEU 104 0.0001

LEU 104 GLN 105 0.0472

GLN 105 LEU 106 -0.0004

LEU 106 GLN 107 0.0001

GLN 107 PHE 108 0.0483

PHE 108 SER 109 0.0004

SER 109 ASN 110 -0.0001

ASN 110 ILE 112 0.0356

ILE 112 TYR 113 0.0002

TYR 113 SER 114 0.0003

SER 114 THR 115 0.0497

THR 115 TYR 116 -0.0003

TYR 116 HIS 117 0.0002

HIS 117 LEU 118 0.0413

LEU 118 PHE 119 0.0000

PHE 119 PRO 120 -0.0004

PRO 120 PRO 121 0.0472

PRO 121 ARG 122 -0.0001

ARG 122 GLN 123 0.0002

GLN 123 LEU 124 0.0131

LEU 124 ASN 125 -0.0002

ASN 125 ASP 126 0.0003

ASP 126 VAL 127 -0.0618

VAL 127 LYS 128 0.0002

LYS 128 THR 129 0.0001

THR 129 THR 130 -0.0354

THR 130 VAL 131 0.0002

VAL 131 VAL 132 0.0000

VAL 132 TYR 133 0.0040

TYR 133 PRO 134 0.0002

PRO 134 ALA 135 0.0001

ALA 135 THR 136 -0.0170

THR 136 GLU 137 0.0002

GLU 137 LYS 138 0.0001

LYS 138 HIS 139 -0.0228

HIS 139 LEU 140 0.0001

LEU 140 GLN 141 0.0001

GLN 141 LYS 142 0.0051

LYS 142 TYR 143 -0.0001

TYR 143 LEU 144 0.0002

LEU 144 ARG 145 0.0136

ARG 145 GLN 146 0.0004

GLN 146 ASP 147 -0.0003

ASP 147 LEU 148 -0.0279

LEU 148 ARG 149 -0.0002

ARG 149 LEU 150 0.0002

LEU 150 ILE 151 0.0589

ILE 151 ARG 152 0.0004

ARG 152 GLU 153 0.0000

GLU 153 THR 154 0.0231

THR 154 GLY 155 0.0003

GLY 155 ASP 156 0.0000

ASP 156 ASP 157 -0.0156

ASP 157 TYR 158 -0.0001

TYR 158 ARG 159 -0.0000

ARG 159 ASN 160 -0.0018

ASN 160 ILE 161 0.0001

ILE 161 THR 162 -0.0000

THR 162 LEU 163 0.0265

LEU 163 PRO 164 0.0002

PRO 164 HIS 165 0.0002

HIS 165 LEU 166 0.0245

LEU 166 GLU 167 0.0001

GLU 167 SER 168 -0.0001

SER 168 GLN 169 -0.0273

GLN 169 SER 170 0.0001

SER 170 LEU 171 0.0003

LEU 171 SER 172 0.0010

SER 172 ILE 173 0.0000

ILE 173 GLN 174 -0.0003

GLN 174 TRP 175 0.0158

TRP 175 VAL 176 0.0001

VAL 176 TYR 177 -0.0000

TYR 177 ASN 178 0.0015

ASN 178 ILE 179 -0.0003

ILE 179 LEU 180 -0.0004

LEU 180 ASP 181 0.0030

ASP 181 LYS 182 -0.0002

LYS 182 LYS 183 0.0001

LYS 183 ALA 184 -0.0041

ALA 184 GLU 185 -0.0002

GLU 185 ALA 186 -0.0003

ALA 186 ASP 187 -0.0023

ASP 187 ARG 188 -0.0001

ARG 188 ILE 189 0.0003

ILE 189 VAL 190 0.0115

VAL 190 PHE 191 0.0001

PHE 191 GLU 192 -0.0003

GLU 192 ASN 193 0.0189

ASN 193 PRO 194 0.0001

PRO 194 ASP 195 0.0001

ASP 195 PRO 196 -0.0016

PRO 196 SER 197 -0.0003

SER 197 ASP 198 0.0002

ASP 198 GLY 199 0.0182

GLY 199 PHE 200 -0.0001

PHE 200 VAL 201 -0.0004

VAL 201 LEU 202 0.0055

LEU 202 ILE 203 -0.0001

ILE 203 PRO 204 -0.0002

PRO 204 ASP 205 -0.0065

ASP 205 LEU 206 -0.0001

LEU 206 LYS 207 0.0004

LYS 207 TRP 208 -0.0181

TRP 208 ASN 209 -0.0000

ASN 209 GLN 210 -0.0002

GLN 210 GLN 211 0.0059

GLN 211 GLN 212 0.0001

GLN 212 LEU 213 0.0002

LEU 213 ASP 214 -0.0299

ASP 214 ASP 215 -0.0003

ASP 215 LEU 216 0.0003

LEU 216 TYR 217 0.0054

TYR 217 LEU 218 0.0004

LEU 218 ILE 219 -0.0002

ILE 219 ALA 220 0.0170

ALA 220 ILE 221 -0.0003

ILE 221 CYS 222 0.0003

CYS 222 HIS 223 0.0079

HIS 223 ARG 224 -0.0001

ARG 224 ARG 225 -0.0002

ARG 225 GLY 226 0.0536

GLY 226 ILE 227 0.0001

ILE 227 ARG 228 -0.0002

ARG 228 SER 229 -0.0021

SER 229 LEU 230 0.0002

LEU 230 ARG 231 0.0001

ARG 231 ASP 232 0.0252

ASP 232 LEU 233 0.0000

LEU 233 THR 234 -0.0001

THR 234 PRO 235 0.0046

PRO 235 GLU 236 -0.0000

GLU 236 HIS 237 0.0000

HIS 237 LEU 238 -0.0141

LEU 238 PRO 239 0.0001

PRO 239 LEU 240 -0.0001

LEU 240 LEU 241 -0.0105

LEU 241 ARG 242 0.0000

ARG 242 ASN 243 -0.0001

ASN 243 ILE 244 0.0026

ILE 244 LEU 245 0.0002

LEU 245 HIS 246 0.0001

HIS 246 GLN 247 0.0307

GLN 247 GLY 248 0.0002

GLY 248 GLN 249 -0.0003

GLN 249 GLU 250 -0.0058

GLU 250 ALA 251 0.0001

ALA 251 ILE 252 0.0000

ILE 252 LEU 253 -0.0128

LEU 253 GLN 254 0.0002

GLN 254 ARG 255 0.0001

ARG 255 TYR 256 0.0023

TYR 256 ARG 257 0.0002

ARG 257 MET 258 0.0002

MET 258 LYS 259 0.1536

LYS 259 GLY 260 -0.0001

GLY 260 ASP 261 -0.0002

ASP 261 HIS 262 0.0250

HIS 262 LEU 263 0.0002

LEU 263 ARG 264 0.0000

ARG 264 VAL 265 0.0072

VAL 265 TYR 266 -0.0001

TYR 266 LEU 267 0.0001

LEU 267 HIS 268 0.0122

HIS 268 TYR 269 -0.0001

TYR 269 LEU 270 -0.0001

LEU 270 PRO 271 -0.0074

PRO 271 SER 272 0.0001

SER 272 TYR 273 0.0004

TYR 273 TYR 274 -0.0520

TYR 274 HIS 275 -0.0003

HIS 275 LEU 276 0.0001

LEU 276 HIS 277 0.0211

HIS 277 VAL 278 0.0003

VAL 278 HIS 279 -0.0003

HIS 279 PHE 280 0.0242

PHE 280 THR 281 0.0003

THR 281 ALA 282 -0.0002

ALA 282 LEU 283 0.0511

LEU 283 GLY 284 -0.0001

GLY 284 PHE 285 0.0000

PHE 285 GLU 286 -0.0019

GLU 286 ALA 287 -0.0002

ALA 287 PRO 288 -0.0000

PRO 288 GLY 289 -0.0181

GLY 289 SER 290 0.0004

SER 290 GLY 291 0.0003

GLY 291 VAL 292 -0.0175

VAL 292 GLU 293 -0.0000

GLU 293 ARG 294 -0.0003

ARG 294 ALA 295 -0.0035

ALA 295 HIS 296 0.0002

HIS 296 LEU 297 0.0001

LEU 297 LEU 298 -0.0231

LEU 298 ALA 299 0.0000

ALA 299 GLU 300 0.0001

GLU 300 VAL 301 -0.0241

VAL 301 ILE 302 0.0002

ILE 302 GLU 303 0.0002

GLU 303 ASN 304 -0.0193

ASN 304 LEU 305 -0.0001

LEU 305 GLU 306 -0.0002

GLU 306 CYS 307 0.0099

CYS 307 ASP 308 0.0001

ASP 308 PRO 309 -0.0003

PRO 309 ARG 310 -0.0086

ARG 310 HIS 311 0.0001

HIS 311 TYR 312 0.0001

TYR 312 GLN 313 -0.0134

GLN 313 GLN 314 -0.0001

GLN 314 ARG 315 0.0001

ARG 315 THR 316 -0.0030

THR 316 LEU 317 0.0001

LEU 317 THR 318 -0.0002

THR 318 PHE 319 -0.0323

PHE 319 ALA 320 0.0000

ALA 320 LEU 321 0.0002

LEU 321 ARG 322 -0.0904

ARG 322 ALA 323 -0.0002

ALA 323 ASP 324 0.0002

ASP 324 ASP 325 -0.0562

ASP 325 PRO 326 -0.0002

PRO 326 LEU 327 -0.0003

LEU 327 LEU 328 0.0461

LEU 328 LYS 329 -0.0003

LYS 329 LEU 330 0.0003

LEU 330 LEU 331 -0.0168

LEU 331 GLN 332 -0.0003

GLN 332 GLU 333 0.0001

GLU 333 ALA 334 0.0027

ALA 334 GLN 335 0.0000

GLN 335 GLN 336 0.0000

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.

*** 1xmm_test ***

CA strain for 2402071547251848064

--- normal mode 9 ---

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

* 1xmm_test *