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

* 1xmm_test *

CA strain for 2402071547251848064

--- normal mode 7 ---

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 -0.0000

ARG 41 LEU 42 -0.0000

LEU 42 PRO 43 0.0254

PRO 43 PHE 44 0.0004

PHE 44 SER 45 -0.0001

SER 45 GLY 46 -0.0085

GLY 46 PHE 47 -0.0002

PHE 47 ARG 48 0.0003

ARG 48 LEU 49 -0.0177

LEU 49 GLN 50 0.0001

GLN 50 LYS 51 -0.0001

LYS 51 VAL 52 -0.0055

VAL 52 LEU 53 0.0004

LEU 53 ARG 54 -0.0000

ARG 54 GLU 55 0.0007

GLU 55 SER 56 -0.0001

SER 56 ALA 57 -0.0002

ALA 57 ARG 58 0.0302

ARG 58 ASP 59 -0.0003

ASP 59 LYS 60 -0.0002

LYS 60 ILE 61 -0.0578

ILE 61 ILE 62 0.0001

ILE 62 PHE 63 -0.0002

PHE 63 LEU 64 -0.0551

LEU 64 HIS 65 -0.0000

HIS 65 GLY 66 -0.0004

GLY 66 LYS 67 -0.0277

LYS 67 VAL 68 -0.0000

VAL 68 ASN 69 0.0000

ASN 69 ASP 79 -0.0005

ASP 79 ALA 80 0.0000

ALA 80 VAL 81 0.0001

VAL 81 VAL 82 -0.0147

VAL 82 ILE 83 -0.0001

ILE 83 LEU 84 0.0001

LEU 84 GLU 85 -0.0902

GLU 85 LYS 86 -0.0003

LYS 86 THR 87 -0.0002

THR 87 PRO 88 -0.0880

PRO 88 PHE 89 -0.0001

PHE 89 GLN 90 0.0002

GLN 90 VAL 91 -0.0287

VAL 91 GLU 92 -0.0001

GLU 92 GLN 93 0.0001

GLN 93 VAL 94 0.0050

VAL 94 ALA 95 0.0001

ALA 95 GLN 96 -0.0003

GLN 96 LEU 97 0.0037

LEU 97 LEU 98 0.0001

LEU 98 THR 99 -0.0001

THR 99 GLY 100 -0.0054

GLY 100 SER 101 -0.0002

SER 101 PRO 102 0.0002

PRO 102 GLU 103 0.0163

GLU 103 LEU 104 -0.0003

LEU 104 GLN 105 0.0001

GLN 105 LEU 106 0.0768

LEU 106 GLN 107 0.0001

GLN 107 PHE 108 0.0001

PHE 108 SER 109 0.0483

SER 109 ASN 110 0.0001

ASN 110 ASP 111 0.0002

ASP 111 ILE 112 -0.0317

ILE 112 TYR 113 -0.0004

TYR 113 SER 114 0.0000

SER 114 THR 115 0.0488

THR 115 TYR 116 0.0002

TYR 116 HIS 117 0.0004

HIS 117 LEU 118 0.0053

LEU 118 PHE 119 -0.0002

PHE 119 PRO 120 -0.0001

PRO 120 PRO 121 0.0544

PRO 121 ARG 122 0.0001

ARG 122 GLN 123 -0.0002

GLN 123 LEU 124 -0.0084

LEU 124 ASN 125 -0.0002

ASN 125 ASP 126 -0.0000

ASP 126 VAL 127 0.0177

VAL 127 LYS 128 0.0003

LYS 128 THR 129 0.0002

THR 129 THR 130 -0.0105

THR 130 VAL 131 0.0001

VAL 131 VAL 132 -0.0000

VAL 132 TYR 133 -0.0228

TYR 133 PRO 134 -0.0003

PRO 134 ALA 135 -0.0004

ALA 135 THR 136 0.0011

THR 136 GLU 137 0.0003

GLU 137 LYS 138 -0.0002

LYS 138 HIS 139 -0.0006

HIS 139 LEU 140 -0.0003

LEU 140 GLN 141 0.0001

GLN 141 LYS 142 -0.0201

LYS 142 TYR 143 -0.0000

TYR 143 LEU 144 0.0002

LEU 144 ARG 145 0.0179

ARG 145 GLN 146 -0.0000

GLN 146 ASP 147 0.0001

ASP 147 LEU 148 -0.0233

LEU 148 ARG 149 0.0003

ARG 149 LEU 150 -0.0000

LEU 150 ILE 151 0.0064

ILE 151 ARG 152 0.0000

ARG 152 GLU 153 0.0002

GLU 153 THR 154 0.0046

THR 154 GLY 155 -0.0003

GLY 155 ASP 156 -0.0001

ASP 156 ASP 157 0.0070

ASP 157 TYR 158 0.0002

TYR 158 ARG 159 -0.0003

ARG 159 ASN 160 0.0147

ASN 160 ILE 161 -0.0002

ILE 161 THR 162 0.0002

THR 162 LEU 163 -0.0004

LEU 163 PRO 164 0.0004

PRO 164 HIS 165 -0.0001

HIS 165 LEU 166 -0.0018

LEU 166 GLU 167 0.0000

GLU 167 SER 168 -0.0002

SER 168 GLN 169 -0.0050

GLN 169 SER 170 0.0004

SER 170 LEU 171 -0.0002

LEU 171 SER 172 -0.0517

SER 172 ILE 173 -0.0000

ILE 173 GLN 174 -0.0004

GLN 174 TRP 175 -0.0035

TRP 175 VAL 176 -0.0000

VAL 176 TYR 177 -0.0002

TYR 177 ASN 178 0.0002

ASN 178 ILE 179 0.0001

ILE 179 LEU 180 0.0001

LEU 180 ASP 181 0.0031

ASP 181 LYS 182 0.0005

LYS 182 LYS 183 -0.0001

LYS 183 ALA 184 0.0035

ALA 184 GLU 185 -0.0004

GLU 185 ALA 186 0.0003

ALA 186 ASP 187 -0.0084

ASP 187 ARG 188 0.0002

ARG 188 ILE 189 -0.0002

ILE 189 VAL 190 0.0138

VAL 190 PHE 191 0.0003

PHE 191 GLU 192 0.0001

GLU 192 ASN 193 0.0051

ASN 193 PRO 194 0.0000

PRO 194 ASP 195 0.0003

ASP 195 PRO 196 -0.0106

PRO 196 SER 197 0.0002

SER 197 ASP 198 -0.0003

ASP 198 GLY 199 0.0021

GLY 199 PHE 200 0.0001

PHE 200 VAL 201 -0.0001

VAL 201 LEU 202 -0.0020

LEU 202 ILE 203 0.0001

ILE 203 PRO 204 -0.0002

PRO 204 ASP 205 0.0006

ASP 205 LEU 206 -0.0000

LEU 206 LYS 207 0.0002

LYS 207 TRP 208 0.0059

TRP 208 ASN 209 -0.0001

ASN 209 GLN 210 -0.0002

GLN 210 GLN 211 0.0036

GLN 211 GLN 212 0.0002

GLN 212 LEU 213 -0.0005

LEU 213 ASP 214 -0.0181

ASP 214 ASP 215 0.0003

ASP 215 LEU 216 0.0001

LEU 216 TYR 217 0.0155

TYR 217 LEU 218 0.0001

LEU 218 ILE 219 -0.0004

ILE 219 ALA 220 -0.0091

ALA 220 ILE 221 -0.0001

ILE 221 CYS 222 -0.0001

CYS 222 HIS 223 -0.0085

HIS 223 ARG 224 -0.0004

ARG 224 ARG 225 0.0001

ARG 225 GLY 226 -0.0111

GLY 226 ILE 227 0.0000

ILE 227 ARG 228 0.0002

ARG 228 SER 229 -0.0052

SER 229 LEU 230 -0.0001

LEU 230 ARG 231 0.0002

ARG 231 ASP 232 -0.0103

ASP 232 LEU 233 -0.0003

LEU 233 THR 234 -0.0002

THR 234 PRO 235 -0.0161

PRO 235 GLU 236 0.0001

GLU 236 HIS 237 -0.0000

HIS 237 LEU 238 -0.0072

LEU 238 PRO 239 -0.0002

PRO 239 LEU 240 -0.0000

LEU 240 LEU 241 0.0028

LEU 241 ARG 242 -0.0002

ARG 242 ASN 243 0.0004

ASN 243 ILE 244 -0.0132

ILE 244 LEU 245 0.0001

LEU 245 HIS 246 -0.0002

HIS 246 GLN 247 0.0152

GLN 247 GLY 248 -0.0000

GLY 248 GLN 249 0.0003

GLN 249 GLU 250 0.0025

GLU 250 ALA 251 0.0002

ALA 251 ILE 252 -0.0001

ILE 252 LEU 253 -0.0013

LEU 253 GLN 254 -0.0002

GLN 254 ARG 255 -0.0003

ARG 255 TYR 256 -0.0036

TYR 256 ARG 257 -0.0002

ARG 257 MET 258 -0.0000

MET 258 LYS 259 0.0490

LYS 259 GLY 260 0.0002

GLY 260 ASP 261 -0.0005

ASP 261 HIS 262 -0.0039

HIS 262 LEU 263 -0.0001

LEU 263 ARG 264 -0.0002

ARG 264 VAL 265 0.0018

VAL 265 TYR 266 -0.0000

TYR 266 LEU 267 -0.0002

LEU 267 HIS 268 -0.0006

HIS 268 TYR 269 -0.0004

TYR 269 LEU 270 -0.0004

LEU 270 PRO 271 -0.0601

PRO 271 SER 272 -0.0001

SER 272 TYR 273 -0.0002

TYR 273 TYR 274 -0.0074

TYR 274 HIS 275 0.0003

HIS 275 LEU 276 -0.0002

LEU 276 HIS 277 0.0067

HIS 277 VAL 278 -0.0002

VAL 278 HIS 279 0.0005

HIS 279 PHE 280 0.0195

PHE 280 THR 281 0.0000

THR 281 ALA 282 -0.0004

ALA 282 LEU 283 0.0199

LEU 283 GLY 284 0.0000

GLY 284 PHE 285 -0.0002

PHE 285 GLU 286 -0.0639

GLU 286 ALA 287 0.0002

ALA 287 PRO 288 -0.0001

PRO 288 GLY 289 -0.0446

GLY 289 SER 290 0.0002

SER 290 GLY 291 0.0001

GLY 291 VAL 292 -0.0228

VAL 292 GLU 293 -0.0001

GLU 293 ARG 294 0.0000

ARG 294 ALA 295 -0.0111

ALA 295 HIS 296 -0.0001

HIS 296 LEU 297 -0.0003

LEU 297 LEU 298 -0.0257

LEU 298 ALA 299 0.0002

ALA 299 GLU 300 0.0001

GLU 300 VAL 301 0.0134

VAL 301 ILE 302 -0.0001

ILE 302 GLU 303 -0.0000

GLU 303 ASN 304 -0.0116

ASN 304 LEU 305 0.0000

LEU 305 GLU 306 0.0001

GLU 306 CYS 307 0.0363

CYS 307 ASP 308 -0.0002

ASP 308 PRO 309 -0.0000

PRO 309 ARG 310 0.0016

ARG 310 HIS 311 0.0001

HIS 311 TYR 312 -0.0003

TYR 312 GLN 313 -0.0009

GLN 313 GLN 314 0.0001

GLN 314 ARG 315 -0.0001

ARG 315 THR 316 0.0034

THR 316 LEU 317 -0.0001

LEU 317 THR 318 0.0001

THR 318 PHE 319 -0.0298

PHE 319 ALA 320 -0.0001

ALA 320 LEU 321 -0.0000

LEU 321 ARG 322 -0.1098

ARG 322 ALA 323 0.0005

ALA 323 ASP 324 0.0004

ASP 324 ASP 325 -0.0643

ASP 325 PRO 326 0.0003

PRO 326 LEU 327 0.0004

LEU 327 LEU 328 -0.0247

LEU 328 LYS 329 0.0003

LYS 329 LEU 330 0.0001

LEU 330 LEU 331 -0.0016

LEU 331 GLN 332 0.0002

GLN 332 GLU 333 0.0002

GLU 333 ALA 334 0.0123

ALA 334 GLN 335 -0.0000

GLN 335 GLN 336 0.0002

GLN 336 VAL 40 -0.0163

VAL 40 ARG 41 -0.0003

ARG 41 LEU 42 -0.0001

LEU 42 PRO 43 0.0382

PRO 43 PHE 44 -0.0000

PHE 44 SER 45 -0.0001

SER 45 GLY 46 -0.0039

GLY 46 PHE 47 0.0002

PHE 47 ARG 48 -0.0001

ARG 48 LEU 49 0.0004

LEU 49 GLN 50 -0.0003

GLN 50 LYS 51 0.0002

LYS 51 VAL 52 0.0110

VAL 52 LEU 53 0.0002

LEU 53 ARG 54 -0.0003

ARG 54 GLU 55 -0.0524

GLU 55 SER 56 0.0001

SER 56 ALA 57 0.0001

ALA 57 ARG 58 -0.0102

ARG 58 ASP 59 0.0003

ASP 59 LYS 60 0.0002

LYS 60 ILE 61 -0.0883

ILE 61 ILE 62 0.0001

ILE 62 PHE 63 0.0003

PHE 63 LEU 64 -0.0182

LEU 64 HIS 65 -0.0000

HIS 65 GLY 66 -0.0001

GLY 66 LYS 67 -0.0063

LYS 67 VAL 68 0.0005

VAL 68 GLU 78 0.0105

GLU 78 ASP 79 -0.0000

ASP 79 ALA 80 -0.0000

ALA 80 VAL 81 -0.0126

VAL 81 VAL 82 -0.0000

VAL 82 ILE 83 0.0002

ILE 83 LEU 84 -0.0230

LEU 84 GLU 85 0.0002

GLU 85 LYS 86 0.0000

LYS 86 THR 87 0.0519

THR 87 PRO 88 0.0001

PRO 88 PHE 89 -0.0003

PHE 89 GLN 90 -0.0191

GLN 90 VAL 91 -0.0001

VAL 91 GLU 92 -0.0001

GLU 92 GLN 93 -0.0320

GLN 93 VAL 94 -0.0004

VAL 94 ALA 95 -0.0003

ALA 95 GLN 96 -0.0259

GLN 96 LEU 97 0.0003

LEU 97 LEU 98 -0.0003

LEU 98 THR 99 -0.0146

THR 99 GLY 100 -0.0001

GLY 100 SER 101 0.0001

SER 101 PRO 102 -0.0280

PRO 102 GLU 103 -0.0001

GLU 103 LEU 104 -0.0002

LEU 104 GLN 105 0.0172

GLN 105 LEU 106 -0.0003

LEU 106 GLN 107 0.0001

GLN 107 PHE 108 0.0136

PHE 108 SER 109 0.0000

SER 109 ASN 110 -0.0001

ASN 110 ILE 112 0.0100

ILE 112 TYR 113 0.0002

TYR 113 SER 114 -0.0000

SER 114 THR 115 -0.0070

THR 115 TYR 116 0.0000

TYR 116 HIS 117 0.0003

HIS 117 LEU 118 0.0508

LEU 118 PHE 119 -0.0003

PHE 119 PRO 120 -0.0001

PRO 120 PRO 121 0.0798

PRO 121 ARG 122 -0.0002

ARG 122 GLN 123 0.0000

GLN 123 LEU 124 -0.0382

LEU 124 ASN 125 -0.0002

ASN 125 ASP 126 0.0000

ASP 126 VAL 127 0.0358

VAL 127 LYS 128 -0.0003

LYS 128 THR 129 0.0000

THR 129 THR 130 0.0252

THR 130 VAL 131 0.0004

VAL 131 VAL 132 0.0001

VAL 132 TYR 133 -0.0057

TYR 133 PRO 134 0.0002

PRO 134 ALA 135 -0.0002

ALA 135 THR 136 0.0422

THR 136 GLU 137 0.0002

GLU 137 LYS 138 -0.0000

LYS 138 HIS 139 -0.0133

HIS 139 LEU 140 0.0002

LEU 140 GLN 141 -0.0001

GLN 141 LYS 142 -0.0043

LYS 142 TYR 143 -0.0002

TYR 143 LEU 144 0.0001

LEU 144 ARG 145 0.0293

ARG 145 GLN 146 0.0001

GLN 146 ASP 147 -0.0001

ASP 147 LEU 148 0.0089

LEU 148 ARG 149 0.0001

ARG 149 LEU 150 0.0001

LEU 150 ILE 151 0.0011

ILE 151 ARG 152 -0.0003

ARG 152 GLU 153 0.0000

GLU 153 THR 154 -0.0042

THR 154 GLY 155 -0.0003

GLY 155 ASP 156 0.0003

ASP 156 ASP 157 -0.0042

ASP 157 TYR 158 -0.0004

TYR 158 ARG 159 0.0000

ARG 159 ASN 160 -0.0059

ASN 160 ILE 161 0.0001

ILE 161 THR 162 -0.0002

THR 162 LEU 163 0.0056

LEU 163 PRO 164 0.0003

PRO 164 HIS 165 -0.0003

HIS 165 LEU 166 0.0050

LEU 166 GLU 167 0.0003

GLU 167 SER 168 0.0004

SER 168 GLN 169 0.0139

GLN 169 SER 170 -0.0001

SER 170 LEU 171 0.0001

LEU 171 SER 172 -0.0122

SER 172 ILE 173 -0.0004

ILE 173 GLN 174 -0.0001

GLN 174 TRP 175 -0.0044

TRP 175 VAL 176 -0.0001

VAL 176 TYR 177 -0.0001

TYR 177 ASN 178 0.0120

ASN 178 ILE 179 -0.0002

ILE 179 LEU 180 -0.0002

LEU 180 ASP 181 0.0024

ASP 181 LYS 182 -0.0000

LYS 182 LYS 183 -0.0001

LYS 183 ALA 184 0.0083

ALA 184 GLU 185 0.0001

GLU 185 ALA 186 -0.0003

ALA 186 ASP 187 -0.0001

ASP 187 ARG 188 0.0002

ARG 188 ILE 189 0.0005

ILE 189 VAL 190 -0.0281

VAL 190 PHE 191 -0.0001

PHE 191 GLU 192 0.0000

GLU 192 ASN 193 0.0167

ASN 193 PRO 194 -0.0001

PRO 194 ASP 195 -0.0005

ASP 195 PRO 196 0.0017

PRO 196 SER 197 -0.0005

SER 197 ASP 198 -0.0001

ASP 198 GLY 199 0.0177

GLY 199 PHE 200 0.0001

PHE 200 VAL 201 -0.0001

VAL 201 LEU 202 0.0132

LEU 202 ILE 203 0.0002

ILE 203 PRO 204 0.0001

PRO 204 ASP 205 -0.0041

ASP 205 LEU 206 0.0000

LEU 206 LYS 207 0.0004

LYS 207 TRP 208 0.0133

TRP 208 ASN 209 0.0001

ASN 209 GLN 210 -0.0000

GLN 210 GLN 211 0.1000

GLN 211 GLN 212 0.0004

GLN 212 LEU 213 -0.0001

LEU 213 ASP 214 0.0249

ASP 214 ASP 215 -0.0000

ASP 215 LEU 216 -0.0006

LEU 216 TYR 217 0.0394

TYR 217 LEU 218 -0.0001

LEU 218 ILE 219 0.0001

ILE 219 ALA 220 0.0038

ALA 220 ILE 221 -0.0004

ILE 221 CYS 222 0.0002

CYS 222 HIS 223 -0.0104

HIS 223 ARG 224 -0.0001

ARG 224 ARG 225 -0.0002

ARG 225 GLY 226 0.0464

GLY 226 ILE 227 -0.0002

ILE 227 ARG 228 0.0003

ARG 228 SER 229 -0.0052

SER 229 LEU 230 -0.0002

LEU 230 ARG 231 0.0001

ARG 231 ASP 232 0.0058

ASP 232 LEU 233 -0.0002

LEU 233 THR 234 -0.0003

THR 234 PRO 235 -0.0083

PRO 235 GLU 236 -0.0001

GLU 236 HIS 237 -0.0003

HIS 237 LEU 238 -0.0080

LEU 238 PRO 239 -0.0002

PRO 239 LEU 240 -0.0002

LEU 240 LEU 241 -0.0064

LEU 241 ARG 242 0.0002

ARG 242 ASN 243 -0.0004

ASN 243 ILE 244 -0.0010

ILE 244 LEU 245 -0.0003

LEU 245 HIS 246 -0.0002

HIS 246 GLN 247 0.0025

GLN 247 GLY 248 0.0002

GLY 248 GLN 249 0.0003

GLN 249 GLU 250 -0.0121

GLU 250 ALA 251 0.0000

ALA 251 ILE 252 -0.0001

ILE 252 LEU 253 -0.0076

LEU 253 GLN 254 -0.0001

GLN 254 ARG 255 0.0000

ARG 255 TYR 256 0.0091

TYR 256 ARG 257 -0.0000

ARG 257 MET 258 -0.0001

MET 258 LYS 259 -0.0340

LYS 259 GLY 260 -0.0003

GLY 260 ASP 261 -0.0000

ASP 261 HIS 262 0.0129

HIS 262 LEU 263 0.0001

LEU 263 ARG 264 0.0002

ARG 264 VAL 265 -0.0045

VAL 265 TYR 266 0.0001

TYR 266 LEU 267 -0.0003

LEU 267 HIS 268 0.0131

HIS 268 TYR 269 0.0001

TYR 269 LEU 270 0.0000

LEU 270 PRO 271 0.0206

PRO 271 SER 272 0.0002

SER 272 TYR 273 0.0000

TYR 273 TYR 274 -0.0075

TYR 274 HIS 275 -0.0000

HIS 275 LEU 276 0.0000

LEU 276 HIS 277 0.0030

HIS 277 VAL 278 0.0000

VAL 278 HIS 279 0.0002

HIS 279 PHE 280 0.0001

PHE 280 THR 281 0.0001

THR 281 ALA 282 -0.0003

ALA 282 LEU 283 -0.0327

LEU 283 GLY 284 -0.0001

GLY 284 PHE 285 -0.0001

PHE 285 GLU 286 -0.0621

GLU 286 ALA 287 -0.0000

ALA 287 PRO 288 -0.0003

PRO 288 GLY 289 -0.0680

GLY 289 SER 290 -0.0002

SER 290 GLY 291 0.0001

GLY 291 VAL 292 -0.0500

VAL 292 GLU 293 0.0002

GLU 293 ARG 294 0.0000

ARG 294 ALA 295 0.0070

ALA 295 HIS 296 0.0002

HIS 296 LEU 297 0.0001

LEU 297 LEU 298 -0.0291

LEU 298 ALA 299 0.0001

ALA 299 GLU 300 -0.0000

GLU 300 VAL 301 -0.0134

VAL 301 ILE 302 0.0000

ILE 302 GLU 303 0.0002

GLU 303 ASN 304 -0.0076

ASN 304 LEU 305 0.0004

LEU 305 GLU 306 -0.0000

GLU 306 CYS 307 0.0222

CYS 307 ASP 308 0.0004

ASP 308 PRO 309 0.0002

PRO 309 ARG 310 -0.0035

ARG 310 HIS 311 0.0000

HIS 311 TYR 312 0.0004

TYR 312 GLN 313 -0.0254

GLN 313 GLN 314 0.0001

GLN 314 ARG 315 -0.0004

ARG 315 THR 316 -0.0091

THR 316 LEU 317 0.0001

LEU 317 THR 318 -0.0002

THR 318 PHE 319 0.0069

PHE 319 ALA 320 -0.0001

ALA 320 LEU 321 0.0004

LEU 321 ARG 322 0.0027

ARG 322 ALA 323 0.0002

ALA 323 ASP 324 -0.0001

ASP 324 ASP 325 -0.0377

ASP 325 PRO 326 0.0004

PRO 326 LEU 327 -0.0000

LEU 327 LEU 328 0.0182

LEU 328 LYS 329 0.0001

LYS 329 LEU 330 -0.0002

LEU 330 LEU 331 0.0020

LEU 331 GLN 332 -0.0000

GLN 332 GLU 333 -0.0000

GLU 333 ALA 334 0.0003

ALA 334 GLN 335 0.0001

GLN 335 GLN 336 0.0004

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 7 ---

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

* 1xmm_test *