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

* 1xmm_test *

CA strain for 2402071547251848064

--- normal mode 8 ---

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 0.0003

ARG 41 LEU 42 0.0000

LEU 42 PRO 43 0.0100

PRO 43 PHE 44 -0.0000

PHE 44 SER 45 -0.0002

SER 45 GLY 46 -0.0092

GLY 46 PHE 47 -0.0001

PHE 47 ARG 48 0.0001

ARG 48 LEU 49 -0.0010

LEU 49 GLN 50 0.0004

GLN 50 LYS 51 -0.0001

LYS 51 VAL 52 -0.0171

VAL 52 LEU 53 -0.0001

LEU 53 ARG 54 0.0003

ARG 54 GLU 55 -0.0039

GLU 55 SER 56 0.0003

SER 56 ALA 57 0.0002

ALA 57 ARG 58 -0.0088

ARG 58 ASP 59 -0.0000

ASP 59 LYS 60 0.0001

LYS 60 ILE 61 -0.0489

ILE 61 ILE 62 -0.0002

ILE 62 PHE 63 -0.0001

PHE 63 LEU 64 -0.0515

LEU 64 HIS 65 -0.0000

HIS 65 GLY 66 -0.0001

GLY 66 LYS 67 -0.0106

LYS 67 VAL 68 0.0000

VAL 68 ASN 69 0.0001

ASN 69 ASP 79 0.0052

ASP 79 ALA 80 -0.0001

ALA 80 VAL 81 0.0003

VAL 81 VAL 82 -0.0368

VAL 82 ILE 83 -0.0001

ILE 83 LEU 84 -0.0000

LEU 84 GLU 85 -0.0969

GLU 85 LYS 86 -0.0000

LYS 86 THR 87 -0.0000

THR 87 PRO 88 -0.0921

PRO 88 PHE 89 -0.0001

PHE 89 GLN 90 -0.0001

GLN 90 VAL 91 -0.0327

VAL 91 GLU 92 0.0003

GLU 92 GLN 93 -0.0001

GLN 93 VAL 94 -0.0103

VAL 94 ALA 95 -0.0002

ALA 95 GLN 96 0.0001

GLN 96 LEU 97 0.0054

LEU 97 LEU 98 0.0002

LEU 98 THR 99 -0.0002

THR 99 GLY 100 0.0092

GLY 100 SER 101 -0.0002

SER 101 PRO 102 -0.0001

PRO 102 GLU 103 0.0376

GLU 103 LEU 104 0.0000

LEU 104 GLN 105 -0.0003

GLN 105 LEU 106 -0.0691

LEU 106 GLN 107 -0.0004

GLN 107 PHE 108 0.0001

PHE 108 SER 109 0.0067

SER 109 ASN 110 0.0001

ASN 110 ASP 111 0.0002

ASP 111 ILE 112 -0.0350

ILE 112 TYR 113 -0.0000

TYR 113 SER 114 -0.0000

SER 114 THR 115 -0.0127

THR 115 TYR 116 0.0003

TYR 116 HIS 117 0.0002

HIS 117 LEU 118 -0.0648

LEU 118 PHE 119 0.0001

PHE 119 PRO 120 -0.0002

PRO 120 PRO 121 -0.0532

PRO 121 ARG 122 0.0000

ARG 122 GLN 123 -0.0002

GLN 123 LEU 124 0.0383

LEU 124 ASN 125 -0.0001

ASN 125 ASP 126 0.0000

ASP 126 VAL 127 -0.0366

VAL 127 LYS 128 0.0005

LYS 128 THR 129 -0.0001

THR 129 THR 130 -0.0683

THR 130 VAL 131 -0.0002

VAL 131 VAL 132 0.0004

VAL 132 TYR 133 -0.0283

TYR 133 PRO 134 -0.0004

PRO 134 ALA 135 0.0002

ALA 135 THR 136 -0.0247

THR 136 GLU 137 -0.0000

GLU 137 LYS 138 0.0001

LYS 138 HIS 139 -0.0168

HIS 139 LEU 140 0.0003

LEU 140 GLN 141 0.0002

GLN 141 LYS 142 -0.0072

LYS 142 TYR 143 0.0001

TYR 143 LEU 144 0.0002

LEU 144 ARG 145 0.1419

ARG 145 GLN 146 -0.0002

GLN 146 ASP 147 -0.0003

ASP 147 LEU 148 0.0537

LEU 148 ARG 149 0.0000

ARG 149 LEU 150 -0.0000

LEU 150 ILE 151 0.0147

ILE 151 ARG 152 -0.0003

ARG 152 GLU 153 -0.0002

GLU 153 THR 154 0.0008

THR 154 GLY 155 -0.0002

GLY 155 ASP 156 0.0001

ASP 156 ASP 157 0.0241

ASP 157 TYR 158 -0.0001

TYR 158 ARG 159 -0.0002

ARG 159 ASN 160 0.0323

ASN 160 ILE 161 0.0001

ILE 161 THR 162 -0.0003

THR 162 LEU 163 0.0092

LEU 163 PRO 164 0.0001

PRO 164 HIS 165 0.0001

HIS 165 LEU 166 -0.0339

LEU 166 GLU 167 -0.0001

GLU 167 SER 168 0.0002

SER 168 GLN 169 -0.0096

GLN 169 SER 170 -0.0002

SER 170 LEU 171 0.0001

LEU 171 SER 172 -0.0426

SER 172 ILE 173 0.0002

ILE 173 GLN 174 0.0001

GLN 174 TRP 175 0.0058

TRP 175 VAL 176 0.0002

VAL 176 TYR 177 -0.0001

TYR 177 ASN 178 -0.0062

ASN 178 ILE 179 0.0000

ILE 179 LEU 180 -0.0000

LEU 180 ASP 181 -0.0005

ASP 181 LYS 182 -0.0001

LYS 182 LYS 183 -0.0001

LYS 183 ALA 184 0.0302

ALA 184 GLU 185 0.0000

GLU 185 ALA 186 0.0001

ALA 186 ASP 187 0.0078

ASP 187 ARG 188 0.0001

ARG 188 ILE 189 -0.0002

ILE 189 VAL 190 0.0067

VAL 190 PHE 191 -0.0003

PHE 191 GLU 192 -0.0001

GLU 192 ASN 193 0.0006

ASN 193 PRO 194 -0.0000

PRO 194 ASP 195 -0.0003

ASP 195 PRO 196 0.0189

PRO 196 SER 197 0.0001

SER 197 ASP 198 0.0002

ASP 198 GLY 199 -0.0008

GLY 199 PHE 200 0.0002

PHE 200 VAL 201 -0.0000

VAL 201 LEU 202 0.0164

LEU 202 ILE 203 -0.0004

ILE 203 PRO 204 0.0001

PRO 204 ASP 205 -0.0088

ASP 205 LEU 206 -0.0001

LEU 206 LYS 207 -0.0000

LYS 207 TRP 208 0.0005

TRP 208 ASN 209 0.0000

ASN 209 GLN 210 0.0002

GLN 210 GLN 211 -0.0219

GLN 211 GLN 212 0.0003

GLN 212 LEU 213 -0.0001

LEU 213 ASP 214 0.0100

ASP 214 ASP 215 -0.0003

ASP 215 LEU 216 -0.0001

LEU 216 TYR 217 -0.0332

TYR 217 LEU 218 -0.0002

LEU 218 ILE 219 0.0002

ILE 219 ALA 220 0.0422

ALA 220 ILE 221 0.0003

ILE 221 CYS 222 -0.0004

CYS 222 HIS 223 0.0284

HIS 223 ARG 224 -0.0003

ARG 224 ARG 225 0.0004

ARG 225 GLY 226 0.0139

GLY 226 ILE 227 0.0001

ILE 227 ARG 228 -0.0000

ARG 228 SER 229 0.0126

SER 229 LEU 230 0.0002

LEU 230 ARG 231 -0.0002

ARG 231 ASP 232 0.0186

ASP 232 LEU 233 0.0003

LEU 233 THR 234 -0.0002

THR 234 PRO 235 0.0397

PRO 235 GLU 236 -0.0001

GLU 236 HIS 237 -0.0002

HIS 237 LEU 238 0.0126

LEU 238 PRO 239 -0.0002

PRO 239 LEU 240 -0.0002

LEU 240 LEU 241 -0.0072

LEU 241 ARG 242 -0.0001

ARG 242 ASN 243 0.0001

ASN 243 ILE 244 0.0177

ILE 244 LEU 245 0.0003

LEU 245 HIS 246 0.0002

HIS 246 GLN 247 -0.0335

GLN 247 GLY 248 0.0003

GLY 248 GLN 249 0.0003

GLN 249 GLU 250 -0.0138

GLU 250 ALA 251 -0.0001

ALA 251 ILE 252 -0.0002

ILE 252 LEU 253 -0.0085

LEU 253 GLN 254 -0.0002

GLN 254 ARG 255 0.0002

ARG 255 TYR 256 0.0067

TYR 256 ARG 257 -0.0003

ARG 257 MET 258 -0.0001

MET 258 LYS 259 -0.0104

LYS 259 GLY 260 0.0003

GLY 260 ASP 261 0.0001

ASP 261 HIS 262 -0.0245

HIS 262 LEU 263 0.0002

LEU 263 ARG 264 0.0000

ARG 264 VAL 265 0.0533

VAL 265 TYR 266 0.0002

TYR 266 LEU 267 0.0001

LEU 267 HIS 268 -0.0274

HIS 268 TYR 269 0.0001

TYR 269 LEU 270 -0.0003

LEU 270 PRO 271 0.0159

PRO 271 SER 272 -0.0001

SER 272 TYR 273 0.0001

TYR 273 TYR 274 -0.0002

TYR 274 HIS 275 -0.0000

HIS 275 LEU 276 -0.0004

LEU 276 HIS 277 0.0228

HIS 277 VAL 278 -0.0003

VAL 278 HIS 279 0.0004

HIS 279 PHE 280 -0.0058

PHE 280 THR 281 0.0001

THR 281 ALA 282 -0.0001

ALA 282 LEU 283 0.0813

LEU 283 GLY 284 -0.0000

GLY 284 PHE 285 0.0000

PHE 285 GLU 286 0.0033

GLU 286 ALA 287 0.0002

ALA 287 PRO 288 0.0002

PRO 288 GLY 289 0.1457

GLY 289 SER 290 0.0005

SER 290 GLY 291 0.0001

GLY 291 VAL 292 0.0177

VAL 292 GLU 293 0.0000

GLU 293 ARG 294 0.0000

ARG 294 ALA 295 -0.0444

ALA 295 HIS 296 -0.0000

HIS 296 LEU 297 0.0002

LEU 297 LEU 298 0.0327

LEU 298 ALA 299 -0.0001

ALA 299 GLU 300 0.0000

GLU 300 VAL 301 0.0012

VAL 301 ILE 302 -0.0003

ILE 302 GLU 303 0.0002

GLU 303 ASN 304 0.0361

ASN 304 LEU 305 -0.0001

LEU 305 GLU 306 0.0002

GLU 306 CYS 307 -0.0732

CYS 307 ASP 308 -0.0001

ASP 308 PRO 309 0.0001

PRO 309 ARG 310 0.0182

ARG 310 HIS 311 -0.0003

HIS 311 TYR 312 0.0001

TYR 312 GLN 313 0.0527

GLN 313 GLN 314 -0.0000

GLN 314 ARG 315 0.0004

ARG 315 THR 316 0.0309

THR 316 LEU 317 0.0000

LEU 317 THR 318 0.0004

THR 318 PHE 319 -0.0117

PHE 319 ALA 320 0.0002

ALA 320 LEU 321 -0.0001

LEU 321 ARG 322 0.0175

ARG 322 ALA 323 0.0001

ALA 323 ASP 324 -0.0002

ASP 324 ASP 325 0.0511

ASP 325 PRO 326 -0.0001

PRO 326 LEU 327 0.0000

LEU 327 LEU 328 -0.0072

LEU 328 LYS 329 0.0001

LYS 329 LEU 330 -0.0002

LEU 330 LEU 331 0.0027

LEU 331 GLN 332 0.0002

GLN 332 GLU 333 -0.0004

GLU 333 ALA 334 0.0062

ALA 334 GLN 335 -0.0002

GLN 335 GLN 336 0.0004

GLN 336 VAL 40 -0.0544

VAL 40 ARG 41 -0.0003

ARG 41 LEU 42 0.0003

LEU 42 PRO 43 0.0087

PRO 43 PHE 44 -0.0002

PHE 44 SER 45 -0.0001

SER 45 GLY 46 0.0041

GLY 46 PHE 47 0.0001

PHE 47 ARG 48 -0.0000

ARG 48 LEU 49 0.0314

LEU 49 GLN 50 -0.0003

GLN 50 LYS 51 0.0000

LYS 51 VAL 52 0.0108

VAL 52 LEU 53 -0.0004

LEU 53 ARG 54 0.0001

ARG 54 GLU 55 -0.0605

GLU 55 SER 56 0.0001

SER 56 ALA 57 -0.0002

ALA 57 ARG 58 0.0582

ARG 58 ASP 59 0.0000

ASP 59 LYS 60 0.0004

LYS 60 ILE 61 -0.0741

ILE 61 ILE 62 0.0000

ILE 62 PHE 63 -0.0000

PHE 63 LEU 64 -0.0092

LEU 64 HIS 65 0.0002

HIS 65 GLY 66 0.0001

GLY 66 LYS 67 0.0148

LYS 67 VAL 68 -0.0000

VAL 68 GLU 78 0.0043

GLU 78 ASP 79 0.0003

ASP 79 ALA 80 -0.0001

ALA 80 VAL 81 0.0023

VAL 81 VAL 82 -0.0003

VAL 82 ILE 83 -0.0002

ILE 83 LEU 84 -0.0482

LEU 84 GLU 85 -0.0000

GLU 85 LYS 86 -0.0004

LYS 86 THR 87 -0.0045

THR 87 PRO 88 0.0004

PRO 88 PHE 89 0.0001

PHE 89 GLN 90 -0.0142

GLN 90 VAL 91 0.0001

VAL 91 GLU 92 -0.0001

GLU 92 GLN 93 -0.0033

GLN 93 VAL 94 0.0001

VAL 94 ALA 95 0.0000

ALA 95 GLN 96 -0.0089

GLN 96 LEU 97 0.0000

LEU 97 LEU 98 -0.0001

LEU 98 THR 99 -0.0056

THR 99 GLY 100 -0.0003

GLY 100 SER 101 0.0003

SER 101 PRO 102 -0.0079

PRO 102 GLU 103 -0.0002

GLU 103 LEU 104 0.0002

LEU 104 GLN 105 0.0045

GLN 105 LEU 106 0.0002

LEU 106 GLN 107 -0.0000

GLN 107 PHE 108 -0.0219

PHE 108 SER 109 -0.0001

SER 109 ASN 110 0.0003

ASN 110 ILE 112 0.0014

ILE 112 TYR 113 -0.0000

TYR 113 SER 114 -0.0001

SER 114 THR 115 -0.0511

THR 115 TYR 116 0.0001

TYR 116 HIS 117 -0.0001

HIS 117 LEU 118 -0.0010

LEU 118 PHE 119 0.0005

PHE 119 PRO 120 -0.0002

PRO 120 PRO 121 0.0017

PRO 121 ARG 122 0.0003

ARG 122 GLN 123 -0.0001

GLN 123 LEU 124 -0.0021

LEU 124 ASN 125 -0.0002

ASN 125 ASP 126 0.0000

ASP 126 VAL 127 -0.0004

VAL 127 LYS 128 -0.0002

LYS 128 THR 129 -0.0002

THR 129 THR 130 -0.0165

THR 130 VAL 131 -0.0004

VAL 131 VAL 132 -0.0000

VAL 132 TYR 133 -0.0005

TYR 133 PRO 134 0.0002

PRO 134 ALA 135 -0.0000

ALA 135 THR 136 0.0015

THR 136 GLU 137 0.0000

GLU 137 LYS 138 -0.0001

LYS 138 HIS 139 -0.0266

HIS 139 LEU 140 -0.0003

LEU 140 GLN 141 0.0001

GLN 141 LYS 142 -0.0069

LYS 142 TYR 143 -0.0000

TYR 143 LEU 144 -0.0002

LEU 144 ARG 145 0.0981

ARG 145 GLN 146 -0.0004

GLN 146 ASP 147 0.0002

ASP 147 LEU 148 0.0241

LEU 148 ARG 149 -0.0003

ARG 149 LEU 150 0.0002

LEU 150 ILE 151 0.0385

ILE 151 ARG 152 -0.0000

ARG 152 GLU 153 0.0004

GLU 153 THR 154 0.0050

THR 154 GLY 155 -0.0003

GLY 155 ASP 156 -0.0000

ASP 156 ASP 157 0.0080

ASP 157 TYR 158 -0.0001

TYR 158 ARG 159 0.0003

ARG 159 ASN 160 0.0158

ASN 160 ILE 161 -0.0001

ILE 161 THR 162 0.0001

THR 162 LEU 163 0.0167

LEU 163 PRO 164 0.0001

PRO 164 HIS 165 0.0001

HIS 165 LEU 166 0.0129

LEU 166 GLU 167 -0.0000

GLU 167 SER 168 0.0002

SER 168 GLN 169 -0.0242

GLN 169 SER 170 0.0005

SER 170 LEU 171 0.0000

LEU 171 SER 172 0.0322

SER 172 ILE 173 -0.0002

ILE 173 GLN 174 0.0001

GLN 174 TRP 175 0.0249

TRP 175 VAL 176 -0.0002

VAL 176 TYR 177 -0.0000

TYR 177 ASN 178 0.0018

ASN 178 ILE 179 -0.0001

ILE 179 LEU 180 -0.0001

LEU 180 ASP 181 0.0053

ASP 181 LYS 182 -0.0002

LYS 182 LYS 183 0.0002

LYS 183 ALA 184 -0.0099

ALA 184 GLU 185 -0.0004

GLU 185 ALA 186 0.0001

ALA 186 ASP 187 0.0079

ASP 187 ARG 188 0.0001

ARG 188 ILE 189 -0.0001

ILE 189 VAL 190 -0.0031

VAL 190 PHE 191 0.0003

PHE 191 GLU 192 0.0002

GLU 192 ASN 193 -0.0139

ASN 193 PRO 194 -0.0005

PRO 194 ASP 195 -0.0002

ASP 195 PRO 196 0.0235

PRO 196 SER 197 0.0000

SER 197 ASP 198 -0.0001

ASP 198 GLY 199 -0.0145

GLY 199 PHE 200 -0.0000

PHE 200 VAL 201 -0.0001

VAL 201 LEU 202 0.0066

LEU 202 ILE 203 0.0001

ILE 203 PRO 204 -0.0002

PRO 204 ASP 205 0.0053

ASP 205 LEU 206 0.0002

LEU 206 LYS 207 -0.0001

LYS 207 TRP 208 -0.0005

TRP 208 ASN 209 0.0001

ASN 209 GLN 210 -0.0001

GLN 210 GLN 211 0.0184

GLN 211 GLN 212 0.0005

GLN 212 LEU 213 -0.0002

LEU 213 ASP 214 0.0130

ASP 214 ASP 215 0.0002

ASP 215 LEU 216 0.0001

LEU 216 TYR 217 0.0073

TYR 217 LEU 218 -0.0000

LEU 218 ILE 219 -0.0003

ILE 219 ALA 220 0.0173

ALA 220 ILE 221 0.0005

ILE 221 CYS 222 -0.0001

CYS 222 HIS 223 0.0213

HIS 223 ARG 224 0.0003

ARG 224 ARG 225 0.0000

ARG 225 GLY 226 0.0582

GLY 226 ILE 227 0.0003

ILE 227 ARG 228 -0.0002

ARG 228 SER 229 0.0021

SER 229 LEU 230 -0.0002

LEU 230 ARG 231 -0.0004

ARG 231 ASP 232 0.0186

ASP 232 LEU 233 0.0003

LEU 233 THR 234 0.0000

THR 234 PRO 235 0.0335

PRO 235 GLU 236 0.0002

GLU 236 HIS 237 0.0002

HIS 237 LEU 238 0.0125

LEU 238 PRO 239 -0.0000

PRO 239 LEU 240 0.0000

LEU 240 LEU 241 -0.0103

LEU 241 ARG 242 0.0001

ARG 242 ASN 243 0.0002

ASN 243 ILE 244 0.0121

ILE 244 LEU 245 0.0004

LEU 245 HIS 246 -0.0001

HIS 246 GLN 247 -0.0413

GLN 247 GLY 248 -0.0002

GLY 248 GLN 249 0.0004

GLN 249 GLU 250 -0.0199

GLU 250 ALA 251 -0.0000

ALA 251 ILE 252 0.0001

ILE 252 LEU 253 -0.0024

LEU 253 GLN 254 -0.0002

GLN 254 ARG 255 -0.0000

ARG 255 TYR 256 0.0042

TYR 256 ARG 257 0.0000

ARG 257 MET 258 0.0001

MET 258 LYS 259 -0.0584

LYS 259 GLY 260 -0.0001

GLY 260 ASP 261 -0.0005

ASP 261 HIS 262 -0.0225

HIS 262 LEU 263 0.0000

LEU 263 ARG 264 0.0001

ARG 264 VAL 265 0.0416

VAL 265 TYR 266 0.0000

TYR 266 LEU 267 -0.0000

LEU 267 HIS 268 -0.0047

HIS 268 TYR 269 -0.0001

TYR 269 LEU 270 0.0003

LEU 270 PRO 271 0.0322

PRO 271 SER 272 0.0001

SER 272 TYR 273 -0.0002

TYR 273 TYR 274 -0.0329

TYR 274 HIS 275 -0.0005

HIS 275 LEU 276 0.0000

LEU 276 HIS 277 0.0162

HIS 277 VAL 278 0.0005

VAL 278 HIS 279 -0.0001

HIS 279 PHE 280 -0.0022

PHE 280 THR 281 -0.0002

THR 281 ALA 282 0.0004

ALA 282 LEU 283 0.0114

LEU 283 GLY 284 0.0001

GLY 284 PHE 285 -0.0004

PHE 285 GLU 286 -0.0065

GLU 286 ALA 287 0.0001

ALA 287 PRO 288 0.0001

PRO 288 GLY 289 -0.0219

GLY 289 SER 290 0.0004

SER 290 GLY 291 0.0001

GLY 291 VAL 292 0.0385

VAL 292 GLU 293 0.0002

GLU 293 ARG 294 0.0001

ARG 294 ALA 295 -0.0252

ALA 295 HIS 296 -0.0002

HIS 296 LEU 297 0.0002

LEU 297 LEU 298 0.0277

LEU 298 ALA 299 -0.0001

ALA 299 GLU 300 -0.0002

GLU 300 VAL 301 0.0049

VAL 301 ILE 302 -0.0001

ILE 302 GLU 303 -0.0000

GLU 303 ASN 304 0.0389

ASN 304 LEU 305 0.0003

LEU 305 GLU 306 -0.0000

GLU 306 CYS 307 -0.0850

CYS 307 ASP 308 -0.0003

ASP 308 PRO 309 0.0002

PRO 309 ARG 310 0.0049

ARG 310 HIS 311 0.0001

HIS 311 TYR 312 -0.0001

TYR 312 GLN 313 0.0392

GLN 313 GLN 314 0.0000

GLN 314 ARG 315 -0.0003

ARG 315 THR 316 0.0269

THR 316 LEU 317 0.0001

LEU 317 THR 318 -0.0001

THR 318 PHE 319 0.0139

PHE 319 ALA 320 -0.0000

ALA 320 LEU 321 0.0000

LEU 321 ARG 322 -0.0014

ARG 322 ALA 323 0.0003

ALA 323 ASP 324 0.0003

ASP 324 ASP 325 -0.0439

ASP 325 PRO 326 -0.0002

PRO 326 LEU 327 0.0001

LEU 327 LEU 328 0.0220

LEU 328 LYS 329 0.0001

LYS 329 LEU 330 0.0004

LEU 330 LEU 331 -0.0074

LEU 331 GLN 332 0.0003

GLN 332 GLU 333 0.0002

GLU 333 ALA 334 -0.0054

ALA 334 GLN 335 -0.0000

GLN 335 GLN 336 -0.0001

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 8 ---

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

* 1xmm_test *