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

* 123454321 *

CA strain for 250414051307299329

--- 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
ALA 1 GLY 2 -0.0001

GLY 2 VAL 3 -0.0002

VAL 3 ALA 4 0.0003

ALA 4 LYS 5 -0.0373

LYS 5 PHE 6 0.0001

PHE 6 ALA 7 0.0000

ALA 7 LYS 8 -0.0003

LYS 8 TYR 9 0.1192

TYR 9 PRO 10 0.0001

PRO 10 LEU 11 -0.0003

LEU 11 THR 12 0.0001

THR 12 PHE 13 0.0720

PHE 13 GLY 14 0.0003

GLY 14 PRO 15 0.0001

PRO 15 SER 16 0.0001

SER 16 PRO 17 -0.0240

PRO 17 ILE 18 0.0000

ILE 18 SER 19 0.0001

SER 19 ASN 20 -0.0002

ASN 20 LEU 21 0.0388

LEU 21 ASN 22 0.0001

ASN 22 ARG 23 -0.0000

ARG 23 LEU 24 -0.0003

LEU 24 SER 25 -0.1620

SER 25 GLN 26 -0.0003

GLN 26 HIS 27 0.0001

HIS 27 LEU 28 0.0002

LEU 28 GLY 29 0.0359

GLY 29 SER 30 -0.0001

SER 30 LYS 31 0.0001

LYS 31 VAL 32 0.0001

VAL 32 ASN 33 0.0275

ASN 33 VAL 34 0.0000

VAL 34 TYR 35 -0.0003

TYR 35 ALA 36 0.0002

ALA 36 LYS 37 0.0068

LYS 37 ARG 38 0.0001

ARG 38 GLU 39 0.0000

GLU 39 ASP 40 -0.0001

ASP 40 CYS 41 0.0551

CYS 41 ASN 42 -0.0001

ASN 42 SER 43 0.0002

SER 43 GLY 44 -0.0003

GLY 44 LEU 45 0.0138

LEU 45 ALA 46 -0.0003

ALA 46 PHE 47 0.0004

PHE 47 GLY 48 0.0004

GLY 48 GLY 49 0.0631

GLY 49 ASN 50 -0.0000

ASN 50 THR 51 0.0003

THR 51 LEU 52 0.0003

LEU 52 ARG 53 0.0282

ARG 53 LYS 54 0.0001

LYS 54 LEU 55 -0.0001

LEU 55 GLU 56 0.0002

GLU 56 TYR 57 0.0264

TYR 57 ILE 58 0.0002

ILE 58 VAL 59 -0.0002

VAL 59 PRO 60 0.0004

PRO 60 ASP 61 -0.0397

ASP 61 ILE 62 0.0002

ILE 62 VAL 63 0.0000

VAL 63 GLU 64 0.0002

GLU 64 GLY 65 -0.0196

GLY 65 ASP 66 0.0003

ASP 66 TYR 67 -0.0002

TYR 67 THR 68 0.0002

THR 68 HIS 69 -0.0439

HIS 69 LEU 70 0.0000

LEU 70 VAL 71 0.0001

VAL 71 SER 72 -0.0002

SER 72 ILE 73 -0.0089

ILE 73 GLY 74 -0.0000

GLY 74 GLY 75 0.0001

GLY 75 ARG 76 0.0001

ARG 76 GLN 77 -0.0387

GLN 77 SER 78 0.0002

SER 78 ASN 79 -0.0002

ASN 79 GLN 80 0.0001

GLN 80 THR 81 0.0625

THR 81 ARG 82 -0.0002

ARG 82 MET 83 -0.0002

MET 83 VAL 84 0.0001

VAL 84 ALA 85 0.1242

ALA 85 ALA 86 0.0001

ALA 86 LEU 87 0.0000

LEU 87 ALA 88 -0.0002

ALA 88 ALA 89 0.1603

ALA 89 LYS 90 0.0000

LYS 90 LEU 91 0.0003

LEU 91 GLY 92 -0.0000

GLY 92 LYS 93 0.2742

LYS 93 LYS 94 0.0001

LYS 94 CYS 95 -0.0002

CYS 95 VAL 96 -0.0000

VAL 96 LEU 97 -0.0259

LEU 97 ILE 98 -0.0000

ILE 98 GLN 99 0.0000

GLN 99 GLU 100 0.0002

GLU 100 ASP 101 -0.0381

ASP 101 TRP 102 -0.0001

TRP 102 VAL 103 -0.0001

VAL 103 PRO 104 0.0002

PRO 104 ILE 105 -0.0164

ILE 105 PRO 106 -0.0002

PRO 106 GLU 107 -0.0002

GLU 107 ALA 108 -0.0001

ALA 108 GLU 109 0.0103

GLU 109 LYS 110 -0.0000

LYS 110 ASP 111 0.0003

ASP 111 VAL 112 -0.0006

VAL 112 TYR 113 -0.0203

TYR 113 ASN 114 -0.0000

ASN 114 ARG 115 0.0001

ARG 115 VAL 116 0.0001

VAL 116 GLY 117 -0.0097

GLY 117 ASN 118 0.0002

ASN 118 ILE 119 0.0000

ILE 119 GLU 120 -0.0001

GLU 120 LEU 121 0.0082

LEU 121 SER 122 0.0001

SER 122 ARG 123 0.0001

ARG 123 ILE 124 0.0003

ILE 124 MET 125 0.0458

MET 125 GLY 126 0.0000

GLY 126 ALA 127 -0.0002

ALA 127 ASP 128 0.0001

ASP 128 VAL 129 0.0383

VAL 129 ARG 130 0.0002

ARG 130 VAL 131 -0.0002

VAL 131 ILE 132 0.0001

ILE 132 GLU 133 0.0505

GLU 133 ASP 134 -0.0003

ASP 134 GLY 135 0.0004

GLY 135 PHE 136 -0.0000

PHE 136 ASP 137 -0.0052

ASP 137 ILE 138 -0.0001

ILE 138 GLY 139 -0.0001

GLY 139 MET 140 0.0001

MET 140 ARG 141 -0.0113

ARG 141 LYS 142 0.0004

LYS 142 SER 143 -0.0001

SER 143 PHE 144 0.0000

PHE 144 ALA 145 -0.0259

ALA 145 ASN 146 -0.0001

ASN 146 ALA 147 -0.0000

ALA 147 LEU 148 0.0002

LEU 148 GLN 149 -0.0321

GLN 149 GLU 150 0.0000

GLU 150 LEU 151 0.0002

LEU 151 GLU 152 -0.0002

GLU 152 ASP 153 -0.0119

ASP 153 ALA 154 -0.0004

ALA 154 GLY 155 -0.0000

GLY 155 HIS 156 -0.0001

HIS 156 LYS 157 -0.0693

LYS 157 PRO 158 -0.0002

PRO 158 TYR 159 0.0003

TYR 159 PRO 160 0.0003

PRO 160 ILE 161 -0.0407

ILE 161 PRO 162 0.0001

PRO 162 ALA 163 -0.0002

ALA 163 GLY 164 -0.0005

GLY 164 CYS 165 -0.0119

CYS 165 SER 166 0.0004

SER 166 GLU 167 -0.0004

GLU 167 HIS 168 -0.0004

HIS 168 LYS 169 -0.0135

LYS 169 TYR 170 -0.0002

TYR 170 GLY 171 0.0001

GLY 171 GLY 172 0.0003

GLY 172 LEU 173 -0.0285

LEU 173 GLY 174 -0.0001

GLY 174 PHE 175 0.0002

PHE 175 VAL 176 0.0002

VAL 176 GLY 177 -0.0055

GLY 177 PHE 178 0.0002

PHE 178 ALA 179 -0.0000

ALA 179 ASP 180 0.0000

ASP 180 GLU 181 0.0030

GLU 181 VAL 182 -0.0001

VAL 182 ILE 183 0.0004

ILE 183 ASN 184 -0.0004

ASN 184 GLN 185 0.0105

GLN 185 GLU 186 -0.0001

GLU 186 VAL 187 0.0001

VAL 187 GLU 188 0.0000

GLU 188 LEU 189 0.0200

LEU 189 GLY 190 0.0000

GLY 190 ILE 191 -0.0002

ILE 191 LYS 192 0.0003

LYS 192 PHE 193 0.0358

PHE 193 ASP 194 -0.0002

ASP 194 LYS 195 -0.0001

LYS 195 ILE 196 0.0003

ILE 196 VAL 197 0.0458

VAL 197 VAL 198 0.0001

VAL 198 CYS 199 0.0001

CYS 199 CYS 200 -0.0003

CYS 200 VAL 201 -0.0118

VAL 201 THR 202 -0.0000

THR 202 GLY 203 0.0000

GLY 203 SER 204 -0.0002

SER 204 THR 205 -0.0447

THR 205 THR 206 -0.0001

THR 206 ALA 207 -0.0001

ALA 207 GLY 208 -0.0002

GLY 208 ILE 209 -0.0117

ILE 209 LEU 210 0.0001

LEU 210 ALA 211 0.0001

ALA 211 GLY 212 -0.0003

GLY 212 MET 213 -0.0038

MET 213 ALA 214 0.0001

ALA 214 GLN 215 -0.0003

GLN 215 TYR 216 -0.0001

TYR 216 GLY 217 0.0078

GLY 217 ARG 218 -0.0000

ARG 218 GLN 219 0.0001

GLN 219 ASP 220 -0.0001

ASP 220 ASP 221 -0.0621

ASP 221 VAL 222 -0.0001

VAL 222 ILE 223 0.0001

ILE 223 ALA 224 0.0003

ALA 224 ILE 225 0.0001

ILE 225 ASP 226 0.0000

ASP 226 ALA 227 0.0003

ALA 227 SER 228 0.0001

SER 228 PHE 229 0.0069

PHE 229 THR 230 0.0001

THR 230 SER 231 -0.0000

SER 231 GLU 232 0.0003

GLU 232 LYS 233 0.0044

LYS 233 THR 234 -0.0001

THR 234 LYS 235 0.0002

LYS 235 GLU 236 0.0001

GLU 236 GLN 237 0.0152

GLN 237 THR 238 0.0003

THR 238 LEU 239 -0.0001

LEU 239 ARG 240 0.0000

ARG 240 ILE 241 0.0027

ILE 241 ALA 242 -0.0001

ALA 242 ASN 243 0.0002

ASN 243 ASN 244 0.0000

ASN 244 THR 245 -0.0005

THR 245 ALA 246 0.0002

ALA 246 LYS 247 -0.0000

LYS 247 LEU 248 -0.0002

LEU 248 ILE 249 -0.0105

ILE 249 GLY 250 -0.0002

GLY 250 VAL 251 -0.0001

VAL 251 GLU 252 -0.0002

GLU 252 HIS 253 -0.0101

HIS 253 GLU 254 -0.0001

GLU 254 PHE 255 0.0001

PHE 255 LYS 256 0.0001

LYS 256 ASP 257 -0.1116

ASP 257 PHE 258 0.0001

PHE 258 THR 259 0.0002

THR 259 LEU 260 0.0003

LEU 260 ASP 261 -0.1010

ASP 261 THR 262 -0.0002

THR 262 ARG 263 -0.0001

ARG 263 PHE 264 -0.0002

PHE 264 ALA 265 0.0820

ALA 265 TYR 266 0.0001

TYR 266 PRO 267 0.0003

PRO 267 CYS 268 -0.0000

CYS 268 TYR 269 0.0324

TYR 269 GLY 270 -0.0005

GLY 270 VAL 271 -0.0001

VAL 271 PRO 272 -0.0001

PRO 272 ASN 273 -0.0013

ASN 273 GLU 274 0.0002

GLU 274 GLY 275 0.0002

GLY 275 THR 276 -0.0002

THR 276 ILE 277 -0.0653

ILE 277 GLU 278 -0.0004

GLU 278 ALA 279 0.0002

ALA 279 ILE 280 0.0002

ILE 280 ARG 281 -0.1131

ARG 281 THR 282 0.0001

THR 282 CYS 283 -0.0002

CYS 283 ALA 284 -0.0000

ALA 284 GLU 285 -0.0322

GLU 285 GLN 286 0.0000

GLN 286 GLU 287 -0.0001

GLU 287 GLY 288 0.0001

GLY 288 VAL 289 -0.1528

VAL 289 LEU 290 -0.0001

LEU 290 THR 291 -0.0002

THR 291 ASP 292 0.0001

ASP 292 PRO 293 -0.0425

PRO 293 VAL 294 -0.0000

VAL 294 TYR 295 0.0003

TYR 295 GLU 296 -0.0002

GLU 296 GLY 297 0.0139

GLY 297 LYS 298 0.0003

LYS 298 SER 299 0.0003

SER 299 MET 300 0.0001

MET 300 GLN 301 0.0145

GLN 301 GLY 302 -0.0002

GLY 302 LEU 303 0.0001

LEU 303 ILE 304 -0.0003

ILE 304 ALA 305 -0.0486

ALA 305 LEU 306 0.0001

LEU 306 ILE 307 0.0001

ILE 307 LYS 308 0.0004

LYS 308 GLU 309 -0.0444

GLU 309 ASP 310 -0.0001

ASP 310 TYR 311 0.0001

TYR 311 PHE 312 0.0000

PHE 312 LYS 313 0.0491

LYS 313 PRO 314 0.0003

PRO 314 GLY 315 0.0001

GLY 315 ALA 316 0.0003

ALA 316 ASN 317 0.0307

ASN 317 VAL 318 -0.0000

VAL 318 LEU 319 -0.0001

LEU 319 TYR 320 -0.0002

TYR 320 VAL 321 0.0127

VAL 321 HIS 322 -0.0004

HIS 322 LEU 323 0.0005

LEU 323 GLY 324 0.0003

GLY 324 GLY 325 -0.0316

GLY 325 ALA 326 -0.0001

ALA 326 PRO 327 -0.0004

PRO 327 ALA 328 -0.0000

ALA 328 LEU 329 -0.0096

LEU 329 SER 330 0.0005

SER 330 ALA 331 0.0001

ALA 331 TYR 332 0.0000

TYR 332 SER 333 -0.0554

SER 333 SER 334 0.0001

SER 334 PHE 335 0.0002

PHE 335 PHE 336 -0.0004

PHE 336 PRO 337 -0.0884

PRO 337 THR 338 -0.0003

THR 338 LYS 339 -0.0001

LYS 339 THR 340 0.0001

THR 340 ALA 341 -0.0700

ALA 341 ALA 1 -0.0063

ALA 1 GLY 2 0.0000

GLY 2 VAL 3 0.0003

VAL 3 ALA 4 0.0004

ALA 4 LYS 5 0.0391

LYS 5 PHE 6 0.0002

PHE 6 ALA 7 -0.0001

ALA 7 LYS 8 -0.0001

LYS 8 TYR 9 -0.1336

TYR 9 PRO 10 0.0001

PRO 10 LEU 11 -0.0002

LEU 11 THR 12 0.0000

THR 12 PHE 13 -0.0692

PHE 13 GLY 14 0.0000

GLY 14 PRO 15 0.0003

PRO 15 SER 16 0.0001

SER 16 PRO 17 0.0175

PRO 17 ILE 18 -0.0002

ILE 18 SER 19 0.0000

SER 19 ASN 20 0.0001

ASN 20 LEU 21 -0.0320

LEU 21 ASN 22 -0.0000

ASN 22 ARG 23 -0.0001

ARG 23 LEU 24 0.0004

LEU 24 SER 25 0.1521

SER 25 GLN 26 0.0000

GLN 26 HIS 27 0.0001

HIS 27 LEU 28 -0.0002

LEU 28 GLY 29 -0.0232

GLY 29 SER 30 0.0000

SER 30 LYS 31 0.0000

LYS 31 VAL 32 0.0002

VAL 32 ASN 33 -0.0142

ASN 33 VAL 34 -0.0001

VAL 34 TYR 35 -0.0002

TYR 35 ALA 36 0.0002

ALA 36 LYS 37 -0.0013

LYS 37 ARG 38 -0.0003

ARG 38 GLU 39 -0.0000

GLU 39 ASP 40 0.0003

ASP 40 CYS 41 -0.0585

CYS 41 ASN 42 -0.0004

ASN 42 SER 43 -0.0003

SER 43 GLY 44 0.0001

GLY 44 LEU 45 -0.0028

LEU 45 ALA 46 -0.0002

ALA 46 PHE 47 0.0002

PHE 47 GLY 48 0.0001

GLY 48 GLY 49 -0.0812

GLY 49 ASN 50 0.0000

ASN 50 THR 51 -0.0001

THR 51 LEU 52 -0.0000

LEU 52 ARG 53 -0.0373

ARG 53 LYS 54 0.0003

LYS 54 LEU 55 -0.0001

LEU 55 GLU 56 0.0000

GLU 56 TYR 57 -0.0262

TYR 57 ILE 58 0.0001

ILE 58 VAL 59 -0.0002

VAL 59 PRO 60 -0.0003

PRO 60 ASP 61 0.0383

ASP 61 ILE 62 0.0002

ILE 62 VAL 63 -0.0001

VAL 63 GLU 64 0.0001

GLU 64 GLY 65 0.0163

GLY 65 ASP 66 0.0001

ASP 66 TYR 67 0.0000

TYR 67 THR 68 -0.0000

THR 68 HIS 69 0.0511

HIS 69 LEU 70 -0.0004

LEU 70 VAL 71 0.0000

VAL 71 SER 72 0.0001

SER 72 ILE 73 0.0270

ILE 73 GLY 74 0.0001

GLY 74 GLY 75 -0.0001

GLY 75 ARG 76 0.0000

ARG 76 GLN 77 0.0488

GLN 77 SER 78 0.0000

SER 78 ASN 79 -0.0001

ASN 79 GLN 80 -0.0000

GLN 80 THR 81 -0.0452

THR 81 ARG 82 -0.0001

ARG 82 MET 83 -0.0001

MET 83 VAL 84 0.0001

VAL 84 ALA 85 -0.1112

ALA 85 ALA 86 0.0005

ALA 86 LEU 87 0.0001

LEU 87 ALA 88 0.0001

ALA 88 ALA 89 -0.1597

ALA 89 LYS 90 0.0001

LYS 90 LEU 91 0.0004

LEU 91 GLY 92 0.0001

GLY 92 LYS 93 -0.2689

LYS 93 LYS 94 -0.0000

LYS 94 CYS 95 0.0003

CYS 95 VAL 96 -0.0000

VAL 96 LEU 97 0.0219

LEU 97 ILE 98 -0.0003

ILE 98 GLN 99 -0.0002

GLN 99 GLU 100 0.0003

GLU 100 ASP 101 0.0316

ASP 101 TRP 102 -0.0004

TRP 102 VAL 103 0.0002

VAL 103 PRO 104 0.0002

PRO 104 ILE 105 -0.0068

ILE 105 PRO 106 0.0002

PRO 106 GLU 107 0.0001

GLU 107 ALA 108 0.0002

ALA 108 GLU 109 -0.0170

GLU 109 LYS 110 -0.0000

LYS 110 ASP 111 -0.0001

ASP 111 VAL 112 -0.0002

VAL 112 TYR 113 0.0186

TYR 113 ASN 114 0.0003

ASN 114 ARG 115 -0.0001

ARG 115 VAL 116 0.0003

VAL 116 GLY 117 -0.0012

GLY 117 ASN 118 0.0002

ASN 118 ILE 119 -0.0001

ILE 119 GLU 120 0.0005

GLU 120 LEU 121 -0.0175

LEU 121 SER 122 -0.0001

SER 122 ARG 123 -0.0002

ARG 123 ILE 124 -0.0002

ILE 124 MET 125 -0.0563

MET 125 GLY 126 -0.0000

GLY 126 ALA 127 -0.0002

ALA 127 ASP 128 0.0002

ASP 128 VAL 129 -0.0225

VAL 129 ARG 130 0.0002

ARG 130 VAL 131 0.0000

VAL 131 ILE 132 -0.0003

ILE 132 GLU 133 -0.0395

GLU 133 ASP 134 0.0001

ASP 134 GLY 135 0.0004

GLY 135 PHE 136 -0.0002

PHE 136 ASP 137 0.0128

ASP 137 ILE 138 0.0001

ILE 138 GLY 139 -0.0001

GLY 139 MET 140 -0.0001

MET 140 ARG 141 0.0274

ARG 141 LYS 142 -0.0001

LYS 142 SER 143 0.0001

SER 143 PHE 144 0.0001

PHE 144 ALA 145 0.0414

ALA 145 ASN 146 0.0000

ASN 146 ALA 147 0.0003

ALA 147 LEU 148 -0.0002

LEU 148 GLN 149 0.0241

GLN 149 GLU 150 0.0002

GLU 150 LEU 151 0.0001

LEU 151 GLU 152 -0.0003

GLU 152 ASP 153 0.0235

ASP 153 ALA 154 -0.0001

ALA 154 GLY 155 0.0000

GLY 155 HIS 156 0.0001

HIS 156 LYS 157 0.0363

LYS 157 PRO 158 0.0002

PRO 158 TYR 159 0.0001

TYR 159 PRO 160 -0.0004

PRO 160 ILE 161 0.0305

ILE 161 PRO 162 -0.0001

PRO 162 ALA 163 0.0004

ALA 163 GLY 164 -0.0001

GLY 164 CYS 165 0.0164

CYS 165 SER 166 0.0001

SER 166 GLU 167 -0.0000

GLU 167 HIS 168 0.0001

HIS 168 LYS 169 0.0233

LYS 169 TYR 170 0.0000

TYR 170 GLY 171 0.0001

GLY 171 GLY 172 0.0001

GLY 172 LEU 173 0.0337

LEU 173 GLY 174 -0.0003

GLY 174 PHE 175 -0.0000

PHE 175 VAL 176 0.0000

VAL 176 GLY 177 0.0020

GLY 177 PHE 178 -0.0001

PHE 178 ALA 179 0.0001

ALA 179 ASP 180 0.0002

ASP 180 GLU 181 -0.0092

GLU 181 VAL 182 0.0000

VAL 182 ILE 183 0.0002

ILE 183 ASN 184 -0.0001

ASN 184 GLN 185 -0.0090

GLN 185 GLU 186 0.0003

GLU 186 VAL 187 0.0001

VAL 187 GLU 188 -0.0002

GLU 188 LEU 189 -0.0164

LEU 189 GLY 190 -0.0000

GLY 190 ILE 191 0.0000

ILE 191 LYS 192 -0.0004

LYS 192 PHE 193 -0.0344

PHE 193 ASP 194 -0.0001

ASP 194 LYS 195 -0.0000

LYS 195 ILE 196 -0.0001

ILE 196 VAL 197 -0.0480

VAL 197 VAL 198 0.0001

VAL 198 CYS 199 0.0003

CYS 199 CYS 200 0.0000

CYS 200 VAL 201 0.0090

VAL 201 THR 202 -0.0002

THR 202 GLY 203 0.0001

GLY 203 SER 204 0.0003

SER 204 THR 205 0.0357

THR 205 THR 206 0.0003

THR 206 ALA 207 -0.0000

ALA 207 GLY 208 -0.0001

GLY 208 ILE 209 0.0100

ILE 209 LEU 210 -0.0002

LEU 210 ALA 211 -0.0002

ALA 211 GLY 212 0.0001

GLY 212 MET 213 0.0043

MET 213 ALA 214 0.0001

ALA 214 GLN 215 -0.0002

GLN 215 TYR 216 0.0004

TYR 216 GLY 217 -0.0052

GLY 217 ARG 218 0.0000

ARG 218 GLN 219 0.0002

GLN 219 ASP 220 -0.0002

ASP 220 ASP 221 0.0545

ASP 221 VAL 222 -0.0000

VAL 222 ILE 223 0.0001

ILE 223 ALA 224 -0.0001

ALA 224 ILE 225 -0.0142

ILE 225 ASP 226 -0.0002

ASP 226 ALA 227 0.0000

ALA 227 SER 228 0.0001

SER 228 PHE 229 -0.0103

PHE 229 THR 230 -0.0001

THR 230 SER 231 0.0000

SER 231 GLU 232 -0.0003

GLU 232 LYS 233 0.0077

LYS 233 THR 234 -0.0001

THR 234 LYS 235 0.0002

LYS 235 GLU 236 -0.0001

GLU 236 GLN 237 -0.0168

GLN 237 THR 238 0.0002

THR 238 LEU 239 -0.0001

LEU 239 ARG 240 0.0002

ARG 240 ILE 241 -0.0040

ILE 241 ALA 242 0.0001

ALA 242 ASN 243 -0.0000

ASN 243 ASN 244 0.0000

ASN 244 THR 245 -0.0090

THR 245 ALA 246 -0.0002

ALA 246 LYS 247 0.0001

LYS 247 LEU 248 -0.0001

LEU 248 ILE 249 0.0071

ILE 249 GLY 250 -0.0001

GLY 250 VAL 251 -0.0002

VAL 251 GLU 252 -0.0005

GLU 252 HIS 253 -0.0005

HIS 253 GLU 254 -0.0000

GLU 254 PHE 255 0.0002

PHE 255 LYS 256 -0.0000

LYS 256 ASP 257 0.1154

ASP 257 PHE 258 0.0001

PHE 258 THR 259 -0.0003

THR 259 LEU 260 -0.0003

LEU 260 ASP 261 0.0887

ASP 261 THR 262 0.0002

THR 262 ARG 263 0.0002

ARG 263 PHE 264 0.0000

PHE 264 ALA 265 -0.0946

ALA 265 TYR 266 0.0003

TYR 266 PRO 267 -0.0001

PRO 267 CYS 268 -0.0003

CYS 268 TYR 269 -0.0255

TYR 269 GLY 270 -0.0005

GLY 270 VAL 271 0.0001

VAL 271 PRO 272 -0.0000

PRO 272 ASN 273 0.0044

ASN 273 GLU 274 -0.0002

GLU 274 GLY 275 0.0001

GLY 275 THR 276 -0.0002

THR 276 ILE 277 0.0904

ILE 277 GLU 278 -0.0002

GLU 278 ALA 279 -0.0003

ALA 279 ILE 280 -0.0003

ILE 280 ARG 281 0.1303

ARG 281 THR 282 0.0002

THR 282 CYS 283 -0.0002

CYS 283 ALA 284 -0.0000

ALA 284 GLU 285 0.0412

GLU 285 GLN 286 -0.0000

GLN 286 GLU 287 -0.0001

GLU 287 GLY 288 0.0003

GLY 288 VAL 289 0.1569

VAL 289 LEU 290 0.0002

LEU 290 THR 291 -0.0004

THR 291 ASP 292 0.0004

ASP 292 PRO 293 0.0514

PRO 293 VAL 294 0.0000

VAL 294 TYR 295 0.0001

TYR 295 GLU 296 -0.0002

GLU 296 GLY 297 -0.0087

GLY 297 LYS 298 -0.0002

LYS 298 SER 299 -0.0004

SER 299 MET 300 0.0001

MET 300 GLN 301 -0.0171

GLN 301 GLY 302 -0.0000

GLY 302 LEU 303 0.0003

LEU 303 ILE 304 0.0001

ILE 304 ALA 305 0.0586

ALA 305 LEU 306 -0.0001

LEU 306 ILE 307 0.0000

ILE 307 LYS 308 -0.0001

LYS 308 GLU 309 0.0425

GLU 309 ASP 310 0.0003

ASP 310 TYR 311 0.0001

TYR 311 PHE 312 0.0001

PHE 312 LYS 313 -0.0510

LYS 313 PRO 314 0.0001

PRO 314 GLY 315 0.0001

GLY 315 ALA 316 0.0003

ALA 316 ASN 317 -0.0298

ASN 317 VAL 318 -0.0001

VAL 318 LEU 319 0.0001

LEU 319 TYR 320 -0.0000

TYR 320 VAL 321 -0.0188

VAL 321 HIS 322 0.0002

HIS 322 LEU 323 -0.0002

LEU 323 GLY 324 0.0001

GLY 324 GLY 325 0.0285

GLY 325 ALA 326 -0.0000

ALA 326 PRO 327 -0.0001

PRO 327 ALA 328 -0.0002

ALA 328 LEU 329 0.0146

LEU 329 SER 330 0.0003

SER 330 ALA 331 0.0004

ALA 331 TYR 332 0.0000

TYR 332 SER 333 0.0438

SER 333 SER 334 0.0002

SER 334 PHE 335 0.0002

PHE 335 PHE 336 0.0003

PHE 336 PRO 337 0.0892

PRO 337 THR 338 -0.0003

THR 338 LYS 339 0.0001

LYS 339 THR 340 -0.0002

THR 340 ALA 341 0.0498

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 8th, 2025.

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

*** 123454321 ***

CA strain for 250414051307299329

--- normal mode 9 ---

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

* 123454321 *