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

* BIOSYNTHETIC PROTEIN 11-MAY-21 7MSP *

CA strain for 2605100231101288398

--- normal mode 11 ---

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
LEU 3 SER 4 0.0001

SER 4 ASP 5 0.0001

ASP 5 ILE 6 -0.0002

ILE 6 TYR 7 0.0395

TYR 7 LEU 8 0.0003

LEU 8 GLU 9 0.0001

GLU 9 LEU 10 0.0003

LEU 10 LYS 11 0.0034

LYS 11 LYS 12 0.0001

LYS 12 GLY 13 0.0001

GLY 13 TYR 14 0.0001

TYR 14 ALA 15 0.0129

ALA 15 ASP 16 0.0002

ASP 16 SER 17 -0.0001

SER 17 LEU 18 0.0001

LEU 18 LEU 19 -0.0197

LEU 19 TYR 20 0.0001

TYR 20 SER 21 0.0001

SER 21 ASP 22 0.0002

ASP 22 LEU 23 -0.0373

LEU 23 SER 24 0.0001

SER 24 LEU 25 -0.0003

LEU 25 LEU 26 0.0000

LEU 26 VAL 27 -0.0164

VAL 27 ASN 28 -0.0001

ASN 28 ILE 29 0.0000

ILE 29 MET 30 0.0001

MET 30 GLU 31 -0.0154

GLU 31 TYR 32 0.0002

TYR 32 GLU 33 -0.0002

GLU 33 LYS 34 0.0000

LYS 34 ASP 35 -0.0776

ASP 35 ILE 36 0.0000

ILE 36 ASP 37 0.0002

ASP 37 VAL 38 -0.0001

VAL 38 MET 39 -0.0215

MET 39 SER 40 0.0002

SER 40 ILE 41 -0.0001

ILE 41 GLN 42 -0.0002

GLN 42 SER 43 0.0010

SER 43 LEU 44 0.0004

LEU 44 VAL 45 -0.0002

VAL 45 ALA 46 -0.0003

ALA 46 GLY 47 0.0063

GLY 47 TYR 48 -0.0002

TYR 48 GLU 49 -0.0000

GLU 49 LYS 50 0.0001

LYS 50 SER 51 0.0160

SER 51 ASP 52 -0.0001

ASP 52 THR 53 -0.0002

THR 53 PRO 54 0.0002

PRO 54 THR 55 0.0894

THR 55 ILE 56 -0.0005

ILE 56 THR 57 0.0001

THR 57 CYS 58 0.0005

CYS 58 GLY 59 0.0548

GLY 59 ILE 60 -0.0003

ILE 60 ILE 61 -0.0000

ILE 61 VAL 62 0.0003

VAL 62 TYR 63 0.0418

TYR 63 ASN 64 -0.0001

ASN 64 GLU 65 0.0001

GLU 65 SER 66 0.0001

SER 66 LYS 67 -0.0578

LYS 67 ARG 68 0.0002

ARG 68 ILE 69 0.0000

ILE 69 LYS 70 0.0002

LYS 70 LYS 71 -0.0799

LYS 71 CYS 72 -0.0001

CYS 72 LEU 73 -0.0001

LEU 73 ASN 74 0.0004

ASN 74 SER 75 0.0195

SER 75 VAL 76 0.0005

VAL 76 LYS 77 0.0000

LYS 77 ASP 78 -0.0002

ASP 78 ASP 79 0.0433

ASP 79 PHE 80 -0.0004

PHE 80 ASN 81 0.0002

ASN 81 GLU 82 0.0000

GLU 82 ILE 83 0.0278

ILE 83 ILE 84 -0.0004

ILE 84 VAL 85 0.0000

VAL 85 LEU 86 0.0001

LEU 86 ASP 87 0.0246

ASP 87 SER 88 0.0002

SER 88 TYR 89 -0.0001

TYR 89 SER 90 -0.0001

SER 90 THR 91 0.0072

THR 91 ASP 92 -0.0001

ASP 92 ASP 93 0.0000

ASP 93 THR 94 0.0002

THR 94 VAL 95 0.0053

VAL 95 ASP 96 -0.0002

ASP 96 ILE 97 -0.0001

ILE 97 ILE 98 -0.0001

ILE 98 LYS 99 0.0032

LYS 99 CYS 100 0.0000

CYS 100 ASP 101 0.0000

ASP 101 PHE 102 -0.0000

PHE 102 PRO 103 -0.0141

PRO 103 ASP 104 -0.0000

ASP 104 VAL 105 0.0001

VAL 105 GLU 106 -0.0001

GLU 106 ILE 107 0.0403

ILE 107 LYS 108 -0.0001

LYS 108 TYR 109 0.0001

TYR 109 GLU 110 -0.0000

GLU 110 LYS 111 0.0790

LYS 111 TRP 112 -0.0002

TRP 112 LYS 113 0.0000

LYS 113 ASN 114 0.0002

ASN 114 ASP 115 -0.0165

ASP 115 PHE 116 0.0003

PHE 116 SER 117 -0.0002

SER 117 TYR 118 -0.0000

TYR 118 ALA 119 0.0076

ALA 119 ARG 120 -0.0000

ARG 120 ASN 121 -0.0000

ASN 121 LYS 122 0.0003

LYS 122 ILE 123 0.0182

ILE 123 ILE 124 0.0001

ILE 124 GLU 125 0.0001

GLU 125 TYR 126 0.0002

TYR 126 ALA 127 0.0728

ALA 127 THR 128 -0.0001

THR 128 SER 129 -0.0005

SER 129 GLU 130 0.0001

GLU 130 TRP 131 -0.0118

TRP 131 ILE 132 -0.0000

ILE 132 TYR 133 -0.0000

TYR 133 PHE 134 0.0001

PHE 134 ILE 135 -0.0316

ILE 135 ASP 136 0.0001

ASP 136 ALA 137 -0.0003

ALA 137 ASP 138 -0.0000

ASP 138 ASN 139 0.0197

ASN 139 LEU 140 0.0000

LEU 140 TYR 141 0.0001

TYR 141 SER 142 -0.0001

SER 142 LYS 143 -0.0162

LYS 143 GLU 144 0.0000

GLU 144 ASN 145 -0.0002

ASN 145 LYS 146 -0.0002

LYS 146 GLY 147 0.0746

GLY 147 LYS 148 0.0002

LYS 148 ILE 149 -0.0000

ILE 149 ALA 150 0.0004

ALA 150 LYS 151 0.0984

LYS 151 VAL 152 0.0003

VAL 152 ALA 153 0.0003

ALA 153 ARG 154 -0.0001

ARG 154 VAL 155 0.0140

VAL 155 LEU 156 0.0003

LEU 156 GLU 157 -0.0004

GLU 157 PHE 158 0.0002

PHE 158 PHE 159 0.0064

PHE 159 SER 160 -0.0000

SER 160 ILE 161 -0.0001

ILE 161 ASP 162 -0.0002

ASP 162 CYS 163 -0.0294

CYS 163 VAL 164 0.0002

VAL 164 VAL 165 0.0001

VAL 165 SER 166 -0.0003

SER 166 PRO 167 0.0185

PRO 167 TYR 168 0.0004

TYR 168 ILE 169 -0.0003

ILE 169 GLU 170 0.0001

GLU 170 GLU 171 -0.0067

GLU 171 TYR 172 0.0002

TYR 172 THR 173 0.0001

THR 173 GLY 174 0.0002

GLY 174 HIS 175 0.0160

HIS 175 LEU 176 -0.0001

LEU 176 TYR 177 0.0002

TYR 177 SER 178 0.0001

SER 178 ASP 179 0.0137

ASP 179 THR 180 0.0002

THR 180 ARG 181 0.0001

ARG 181 ARG 182 0.0003

ARG 182 MET 183 0.0044

MET 183 PHE 184 -0.0003

PHE 184 ARG 185 0.0003

ARG 185 LEU 186 -0.0000

LEU 186 ASN 187 -0.0381

ASN 187 GLY 188 0.0000

GLY 188 LYS 189 -0.0002

LYS 189 VAL 190 0.0000

VAL 190 LYS 191 -0.0171

LYS 191 PHE 192 -0.0002

PHE 192 HIS 193 0.0001

HIS 193 GLY 194 0.0004

GLY 194 LYS 195 -0.1203

LYS 195 VAL 196 0.0000

VAL 196 HIS 197 0.0001

HIS 197 GLU 198 0.0001

GLU 198 GLU 199 -0.1337

GLU 199 PRO 200 -0.0000

PRO 200 MET 201 0.0005

MET 201 ASN 202 -0.0004

ASN 202 TYR 203 -0.0006

TYR 203 ASN 204 0.0002

ASN 204 HIS 205 0.0004

HIS 205 SER 206 0.0001

SER 206 LEU 207 0.0188

LEU 207 PRO 208 0.0001

PRO 208 PHE 209 -0.0004

PHE 209 ASN 210 -0.0001

ASN 210 PHE 211 -0.0337

PHE 211 ILE 212 0.0004

ILE 212 VAL 213 0.0001

VAL 213 ASN 214 -0.0005

ASN 214 LEU 215 0.1106

LEU 215 LYS 216 -0.0001

LYS 216 VAL 217 0.0000

VAL 217 TYR 218 -0.0001

TYR 218 HIS 219 0.0343

HIS 219 ASN 220 -0.0002

ASN 220 GLY 221 -0.0003

GLY 221 TYR 222 -0.0003

TYR 222 ASN 223 -0.0251

ASN 223 PRO 224 -0.0001

PRO 224 SER 225 0.0000

SER 225 GLU 226 -0.0001

GLU 226 ASN 227 0.0138

ASN 227 ASN 228 -0.0005

ASN 228 ILE 229 -0.0001

ILE 229 LYS 230 0.0003

LYS 230 SER 231 -0.0128

SER 231 LYS 232 -0.0002

LYS 232 THR 233 -0.0002

THR 233 ARG 234 -0.0000

ARG 234 ARG 235 -0.0128

ARG 235 ASN 236 -0.0004

ASN 236 ILE 237 0.0000

ILE 237 ASN 238 -0.0001

ASN 238 LEU 239 -0.0095

LEU 239 THR 240 -0.0002

THR 240 GLU 241 -0.0001

GLU 241 GLU 242 0.0003

GLU 242 MET 243 -0.0025

MET 243 LEU 244 0.0004

LEU 244 ARG 245 0.0000

ARG 245 LEU 246 -0.0003

LEU 246 GLU 247 0.0256

GLU 247 PRO 248 -0.0003

PRO 248 GLU 249 0.0002

GLU 249 ASN 250 -0.0001

ASN 250 PRO 251 -0.0113

PRO 251 LYS 252 0.0004

LYS 252 TRP 253 -0.0001

TRP 253 LEU 254 0.0002

LEU 254 PHE 255 -0.0141

PHE 255 PHE 256 0.0000

PHE 256 PHE 257 0.0002

PHE 257 GLY 258 -0.0000

GLY 258 ARG 259 0.0000

ARG 259 GLU 260 0.0002

GLU 260 LEU 261 0.0001

LEU 261 HIS 262 0.0002

HIS 262 LEU 263 0.0141

LEU 263 LEU 264 0.0003

LEU 264 ASP 265 -0.0000

ASP 265 LYS 266 0.0001

LYS 266 ASP 267 0.0011

ASP 267 GLU 268 0.0001

GLU 268 GLU 269 0.0000

GLU 269 ALA 270 0.0003

ALA 270 ILE 271 0.0053

ILE 271 ASP 272 -0.0004

ASP 272 TYR 273 0.0002

TYR 273 LEU 274 -0.0002

LEU 274 LYS 275 0.0076

LYS 275 LYS 276 0.0000

LYS 276 SER 277 0.0000

SER 277 ILE 278 0.0003

ILE 278 ASN 279 0.0124

ASN 279 ASN 280 0.0000

ASN 280 TYR 281 -0.0002

TYR 281 LYS 282 -0.0001

LYS 282 LYS 283 0.0040

LYS 283 PHE 284 0.0002

PHE 284 ASN 285 0.0000

ASN 285 ASP 286 0.0002

ASP 286 GLN 287 0.0108

GLN 287 ARG 288 -0.0002

ARG 288 HIS 289 -0.0003

HIS 289 PHE 290 -0.0001

PHE 290 ILE 291 0.0082

ILE 291 ASP 292 0.0003

ASP 292 ALA 293 0.0003

ALA 293 LEU 294 -0.0000

LEU 294 VAL 295 0.0009

VAL 295 LEU 296 -0.0001

LEU 296 LEU 297 0.0002

LEU 297 CYS 298 -0.0001

CYS 298 THR 299 -0.0017

THR 299 LEU 300 0.0002

LEU 300 LEU 301 0.0004

LEU 301 LEU 302 0.0001

LEU 302 GLN 303 -0.0164

GLN 303 ARG 304 -0.0000

ARG 304 ASN 305 0.0003

ASN 305 ASN 306 0.0002

ASN 306 TYR 307 -0.0146

TYR 307 VAL 308 -0.0001

VAL 308 ASP 309 0.0001

ASP 309 LEU 310 0.0001

LEU 310 THR 311 -0.0053

THR 311 LEU 312 0.0001

LEU 312 TYR 313 -0.0002

TYR 313 LEU 314 0.0003

LEU 314 ASP 315 -0.0005

ASP 315 ILE 316 -0.0000

ILE 316 LEU 317 -0.0001

LEU 317 GLU 318 0.0003

GLU 318 THR 319 0.0063

THR 319 GLU 320 -0.0005

GLU 320 TYR 321 0.0002

TYR 321 PRO 322 -0.0001

PRO 322 ARG 323 -0.0316

ARG 323 CYS 324 -0.0003

CYS 324 VAL 325 0.0002

VAL 325 ASP 326 -0.0003

ASP 326 VAL 327 -0.0014

VAL 327 ASP 328 0.0002

ASP 328 TYR 329 0.0003

TYR 329 PHE 330 -0.0007

PHE 330 ARG 331 -0.0043

ARG 331 SER 332 -0.0001

SER 332 ALA 333 0.0002

ALA 333 ILE 334 0.0001

ILE 334 LEU 335 -0.0059

LEU 335 LYS 2 -0.0458

LYS 2 LEU 3 -0.0002

LEU 3 SER 4 0.0002

SER 4 ASP 5 -0.0003

ASP 5 ILE 6 -0.0118

ILE 6 TYR 7 0.0001

TYR 7 LEU 8 -0.0000

LEU 8 GLU 9 -0.0001

GLU 9 LEU 10 -0.0011

LEU 10 LYS 11 0.0001

LYS 11 LYS 12 -0.0004

LYS 12 GLY 13 0.0002

GLY 13 TYR 14 -0.0230

TYR 14 ALA 15 0.0000

ALA 15 ASP 16 0.0001

ASP 16 SER 17 -0.0005

SER 17 LEU 18 -0.0400

LEU 18 LEU 19 0.0001

LEU 19 TYR 20 -0.0001

TYR 20 SER 21 0.0002

SER 21 ASP 22 -0.0391

ASP 22 LEU 23 0.0001

LEU 23 SER 24 -0.0001

SER 24 LEU 25 -0.0003

LEU 25 LEU 26 -0.0101

LEU 26 VAL 27 -0.0002

VAL 27 ASN 28 0.0001

ASN 28 ILE 29 -0.0001

ILE 29 MET 30 -0.0569

MET 30 GLU 31 -0.0001

GLU 31 TYR 32 0.0002

TYR 32 GLU 33 0.0001

GLU 33 LYS 34 -0.0376

LYS 34 ASP 35 -0.0001

ASP 35 ILE 36 -0.0001

ILE 36 ASP 37 0.0004

ASP 37 VAL 38 0.0171

VAL 38 MET 39 -0.0000

MET 39 SER 40 -0.0001

SER 40 ILE 41 0.0002

ILE 41 GLN 42 -0.0100

GLN 42 SER 43 -0.0001

SER 43 LEU 44 -0.0000

LEU 44 VAL 45 -0.0000

VAL 45 ALA 46 -0.0020

ALA 46 GLY 47 -0.0002

GLY 47 TYR 48 -0.0000

TYR 48 GLU 49 -0.0002

GLU 49 LYS 50 0.0168

LYS 50 SER 51 -0.0003

SER 51 ASP 52 -0.0000

ASP 52 THR 53 0.0002

THR 53 PRO 54 -0.0699

PRO 54 THR 55 0.0005

THR 55 ILE 56 -0.0003

ILE 56 THR 57 -0.0001

THR 57 CYS 58 -0.0291

CYS 58 GLY 59 -0.0002

GLY 59 ILE 60 -0.0000

ILE 60 ILE 61 0.0002

ILE 61 VAL 62 -0.0045

VAL 62 TYR 63 -0.0003

TYR 63 ASN 64 -0.0002

ASN 64 GLU 65 0.0003

GLU 65 SER 66 0.0074

SER 66 LYS 67 -0.0003

LYS 67 ARG 68 0.0001

ARG 68 ILE 69 -0.0001

ILE 69 LYS 70 0.0192

LYS 70 LYS 71 -0.0001

LYS 71 CYS 72 0.0000

CYS 72 LEU 73 0.0000

LEU 73 ASN 74 0.0359

ASN 74 SER 75 -0.0003

SER 75 VAL 76 0.0000

VAL 76 LYS 77 -0.0002

LYS 77 ASP 78 -0.0662

ASP 78 ASP 79 -0.0000

ASP 79 PHE 80 -0.0002

PHE 80 ASN 81 0.0001

ASN 81 GLU 82 -0.0825

GLU 82 ILE 83 -0.0002

ILE 83 ILE 84 0.0002

ILE 84 VAL 85 0.0000

VAL 85 LEU 86 -0.0273

LEU 86 ASP 87 -0.0000

ASP 87 SER 88 0.0002

SER 88 TYR 89 -0.0001

TYR 89 SER 90 0.0130

SER 90 THR 91 0.0001

THR 91 ASP 92 -0.0000

ASP 92 ASP 93 -0.0002

ASP 93 THR 94 0.0029

THR 94 VAL 95 -0.0002

VAL 95 ASP 96 0.0002

ASP 96 ILE 97 -0.0000

ILE 97 ILE 98 -0.0091

ILE 98 LYS 99 -0.0002

LYS 99 CYS 100 0.0002

CYS 100 ASP 101 0.0002

ASP 101 PHE 102 -0.0073

PHE 102 PRO 103 0.0003

PRO 103 ASP 104 0.0003

ASP 104 VAL 105 -0.0003

VAL 105 GLU 106 0.0221

GLU 106 ILE 107 0.0002

ILE 107 LYS 108 0.0000

LYS 108 TYR 109 -0.0003

TYR 109 GLU 110 -0.0530

GLU 110 LYS 111 -0.0001

LYS 111 TRP 112 -0.0001

TRP 112 LYS 113 -0.0000

LYS 113 ASN 114 -0.1266

ASN 114 ASP 115 -0.0001

ASP 115 PHE 116 -0.0001

PHE 116 SER 117 -0.0002

SER 117 TYR 118 -0.0010

TYR 118 ALA 119 -0.0002

ALA 119 ARG 120 0.0004

ARG 120 ASN 121 0.0003

ASN 121 LYS 122 0.0206

LYS 122 ILE 123 0.0004

ILE 123 ILE 124 -0.0001

ILE 124 GLU 125 0.0001

GLU 125 TYR 126 0.0056

TYR 126 ALA 127 -0.0003

ALA 127 THR 128 0.0000

THR 128 SER 129 -0.0001

SER 129 GLU 130 -0.0325

GLU 130 TRP 131 0.0001

TRP 131 ILE 132 -0.0002

ILE 132 TYR 133 0.0003

TYR 133 PHE 134 0.0037

PHE 134 ILE 135 -0.0002

ILE 135 ASP 136 0.0002

ASP 136 ALA 137 -0.0001

ALA 137 ASP 138 0.0530

ASP 138 ASN 139 -0.0001

ASN 139 LEU 140 0.0002

LEU 140 TYR 141 0.0003

TYR 141 SER 142 0.0175

SER 142 LYS 143 0.0002

LYS 143 GLU 144 -0.0004

GLU 144 ASN 145 0.0002

ASN 145 LYS 146 0.0326

LYS 146 GLY 147 0.0001

GLY 147 LYS 148 -0.0002

LYS 148 ILE 149 -0.0001

ILE 149 ALA 150 0.0092

ALA 150 LYS 151 0.0002

LYS 151 VAL 152 -0.0002

VAL 152 ALA 153 -0.0001

ALA 153 ARG 154 -0.0079

ARG 154 VAL 155 0.0002

VAL 155 LEU 156 -0.0003

LEU 156 GLU 157 -0.0003

GLU 157 PHE 158 0.0197

PHE 158 PHE 159 -0.0002

PHE 159 SER 160 0.0004

SER 160 ILE 161 -0.0001

ILE 161 ASP 162 0.1617

ASP 162 CYS 163 0.0003

CYS 163 VAL 164 -0.0004

VAL 164 VAL 165 -0.0003

VAL 165 SER 166 -0.0306

SER 166 PRO 167 -0.0001

PRO 167 TYR 168 0.0001

TYR 168 ILE 169 -0.0002

ILE 169 GLU 170 -0.0461

GLU 170 GLU 171 0.0004

GLU 171 TYR 172 -0.0007

TYR 172 THR 173 0.0001

THR 173 GLY 174 -0.0546

GLY 174 HIS 175 -0.0002

HIS 175 LEU 176 -0.0000

LEU 176 TYR 177 -0.0002

TYR 177 SER 178 0.0473

SER 178 ASP 179 -0.0001

ASP 179 THR 180 0.0002

THR 180 ARG 181 -0.0001

ARG 181 ARG 182 0.0826

ARG 182 MET 183 -0.0003

MET 183 PHE 184 0.0003

PHE 184 ARG 185 -0.0000

ARG 185 LEU 186 -0.0014

LEU 186 ASN 187 -0.0000

ASN 187 GLY 188 0.0003

GLY 188 LYS 189 -0.0001

LYS 189 VAL 190 0.0187

VAL 190 LYS 191 0.0001

LYS 191 PHE 192 0.0002

PHE 192 HIS 193 0.0001

HIS 193 GLY 194 0.1071

GLY 194 LYS 195 -0.0002

LYS 195 VAL 196 -0.0000

VAL 196 HIS 197 0.0001

HIS 197 GLU 198 0.0647

GLU 198 GLU 199 -0.0005

GLU 199 PRO 200 0.0001

PRO 200 MET 201 -0.0002

MET 201 ASN 202 -0.0007

ASN 202 TYR 203 0.0001

TYR 203 ASN 204 0.0000

ASN 204 HIS 205 0.0002

HIS 205 SER 206 0.0129

SER 206 LEU 207 -0.0002

LEU 207 PRO 208 0.0003

PRO 208 PHE 209 -0.0000

PHE 209 ASN 210 -0.0382

ASN 210 PHE 211 0.0001

PHE 211 ILE 212 0.0000

ILE 212 VAL 213 0.0000

VAL 213 ASN 214 -0.0586

ASN 214 LEU 215 -0.0000

LEU 215 LYS 216 -0.0003

LYS 216 VAL 217 -0.0001

VAL 217 TYR 218 -0.0372

TYR 218 HIS 219 0.0001

HIS 219 ASN 220 -0.0005

ASN 220 GLY 221 -0.0001

GLY 221 TYR 222 -0.0121

TYR 222 ASN 223 -0.0002

ASN 223 PRO 224 0.0001

PRO 224 SER 225 -0.0003

SER 225 GLU 226 -0.0079

GLU 226 ASN 227 -0.0004

ASN 227 ASN 228 -0.0002

ASN 228 ILE 229 0.0003

ILE 229 LYS 230 -0.0096

LYS 230 SER 231 -0.0001

SER 231 LYS 232 -0.0004

LYS 232 THR 233 0.0002

THR 233 ARG 234 -0.0126

ARG 234 ARG 235 -0.0001

ARG 235 ASN 236 0.0001

ASN 236 ILE 237 -0.0001

ILE 237 ASN 238 -0.0099

ASN 238 LEU 239 -0.0002

LEU 239 THR 240 0.0002

THR 240 GLU 241 0.0001

GLU 241 GLU 242 0.0168

GLU 242 MET 243 0.0002

MET 243 LEU 244 0.0001

LEU 244 ARG 245 -0.0003

ARG 245 LEU 246 0.0081

LEU 246 GLU 247 0.0002

GLU 247 PRO 248 0.0002

PRO 248 GLU 249 -0.0002

GLU 249 ASN 250 0.0344

ASN 250 PRO 251 0.0003

PRO 251 LYS 252 -0.0001

LYS 252 TRP 253 0.0003

TRP 253 LEU 254 0.0155

LEU 254 PHE 255 -0.0001

PHE 255 PHE 256 0.0002

PHE 256 PHE 257 0.0001

PHE 257 GLY 258 0.0041

GLY 258 ARG 259 -0.0002

ARG 259 GLU 260 -0.0001

GLU 260 LEU 261 0.0001

LEU 261 HIS 262 -0.0072

HIS 262 LEU 263 0.0003

LEU 263 LEU 264 -0.0001

LEU 264 ASP 265 -0.0004

ASP 265 LYS 266 -0.0168

LYS 266 ASP 267 0.0002

ASP 267 GLU 268 -0.0003

GLU 268 GLU 269 -0.0002

GLU 269 ALA 270 0.0116

ALA 270 ILE 271 0.0000

ILE 271 ASP 272 0.0000

ASP 272 TYR 273 0.0002

TYR 273 LEU 274 -0.0010

LEU 274 LYS 275 0.0001

LYS 275 LYS 276 -0.0002

LYS 276 SER 277 -0.0001

SER 277 ILE 278 -0.0122

ILE 278 ASN 279 0.0002

ASN 279 ASN 280 0.0002

ASN 280 TYR 281 -0.0001

TYR 281 LYS 282 -0.0204

LYS 282 LYS 283 -0.0000

LYS 283 PHE 284 -0.0004

PHE 284 ASN 285 0.0001

ASN 285 ASP 286 0.0705

ASP 286 GLN 287 -0.0002

GLN 287 ARG 288 0.0003

ARG 288 HIS 289 0.0002

HIS 289 PHE 290 0.0050

PHE 290 ILE 291 -0.0003

ILE 291 ASP 292 0.0002

ASP 292 ALA 293 0.0003

ALA 293 LEU 294 -0.0285

LEU 294 VAL 295 -0.0001

VAL 295 LEU 296 -0.0004

LEU 296 LEU 297 0.0004

LEU 297 CYS 298 -0.0206

CYS 298 THR 299 0.0002

THR 299 LEU 300 0.0004

LEU 300 LEU 301 0.0001

LEU 301 LEU 302 -0.0333

LEU 302 GLN 303 -0.0004

GLN 303 ARG 304 0.0001

ARG 304 ASN 305 -0.0000

ASN 305 ASN 306 -0.0330

ASN 306 TYR 307 -0.0005

TYR 307 VAL 308 -0.0001

VAL 308 ASP 309 0.0000

ASP 309 LEU 310 0.0386

LEU 310 THR 311 -0.0005

THR 311 LEU 312 0.0001

LEU 312 TYR 313 -0.0000

TYR 313 LEU 314 0.0362

LEU 314 ASP 315 0.0000

ASP 315 ILE 316 0.0003

ILE 316 LEU 317 0.0003

LEU 317 GLU 318 0.0168

GLU 318 THR 319 0.0001

THR 319 GLU 320 -0.0001

GLU 320 TYR 321 -0.0001

TYR 321 PRO 322 -0.0031

PRO 322 ARG 323 -0.0003

ARG 323 CYS 324 -0.0001

CYS 324 VAL 325 0.0003

VAL 325 ASP 326 0.0202

ASP 326 VAL 327 -0.0001

VAL 327 ASP 328 0.0000

ASP 328 TYR 329 -0.0001

TYR 329 PHE 330 0.0419

PHE 330 ARG 331 -0.0005

ARG 331 SER 332 -0.0001

SER 332 ALA 333 -0.0000

ALA 333 ILE 334 0.0557

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.

*** BIOSYNTHETIC PROTEIN 11-MAY-21 7MSP ***

CA strain for 2605100231101288398

--- normal mode 11 ---

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

* BIOSYNTHETIC PROTEIN 11-MAY-21 7MSP *