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

* 123454321 *

CA strain for 250414051307299329

--- 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
ALA 1 GLY 2 0.0001

GLY 2 VAL 3 0.0000

VAL 3 ALA 4 0.0001

ALA 4 LYS 5 -0.0039

LYS 5 PHE 6 -0.0001

PHE 6 ALA 7 0.0001

ALA 7 LYS 8 -0.0003

LYS 8 TYR 9 0.1262

TYR 9 PRO 10 0.0000

PRO 10 LEU 11 0.0001

LEU 11 THR 12 -0.0002

THR 12 PHE 13 -0.1341

PHE 13 GLY 14 0.0002

GLY 14 PRO 15 0.0000

PRO 15 SER 16 -0.0001

SER 16 PRO 17 -0.0272

PRO 17 ILE 18 0.0001

ILE 18 SER 19 0.0003

SER 19 ASN 20 0.0000

ASN 20 LEU 21 -0.0837

LEU 21 ASN 22 0.0002

ASN 22 ARG 23 -0.0000

ARG 23 LEU 24 0.0001

LEU 24 SER 25 -0.0269

SER 25 GLN 26 -0.0001

GLN 26 HIS 27 0.0002

HIS 27 LEU 28 0.0003

LEU 28 GLY 29 -0.0164

GLY 29 SER 30 0.0000

SER 30 LYS 31 -0.0002

LYS 31 VAL 32 0.0005

VAL 32 ASN 33 0.0599

ASN 33 VAL 34 0.0001

VAL 34 TYR 35 -0.0001

TYR 35 ALA 36 0.0001

ALA 36 LYS 37 0.0341

LYS 37 ARG 38 0.0001

ARG 38 GLU 39 -0.0002

GLU 39 ASP 40 0.0001

ASP 40 CYS 41 -0.0251

CYS 41 ASN 42 -0.0003

ASN 42 SER 43 0.0000

SER 43 GLY 44 0.0002

GLY 44 LEU 45 -0.0872

LEU 45 ALA 46 -0.0002

ALA 46 PHE 47 -0.0005

PHE 47 GLY 48 -0.0003

GLY 48 GLY 49 0.0416

GLY 49 ASN 50 0.0001

ASN 50 THR 51 -0.0003

THR 51 LEU 52 -0.0002

LEU 52 ARG 53 0.0637

ARG 53 LYS 54 -0.0003

LYS 54 LEU 55 -0.0004

LEU 55 GLU 56 0.0002

GLU 56 TYR 57 -0.0411

TYR 57 ILE 58 0.0001

ILE 58 VAL 59 0.0001

VAL 59 PRO 60 0.0002

PRO 60 ASP 61 -0.0514

ASP 61 ILE 62 0.0001

ILE 62 VAL 63 -0.0002

VAL 63 GLU 64 0.0002

GLU 64 GLY 65 -0.0298

GLY 65 ASP 66 -0.0004

ASP 66 TYR 67 0.0001

TYR 67 THR 68 -0.0004

THR 68 HIS 69 0.0300

HIS 69 LEU 70 -0.0001

LEU 70 VAL 71 0.0001

VAL 71 SER 72 -0.0003

SER 72 ILE 73 0.0203

ILE 73 GLY 74 0.0002

GLY 74 GLY 75 0.0001

GLY 75 ARG 76 -0.0002

ARG 76 GLN 77 0.0309

GLN 77 SER 78 0.0001

SER 78 ASN 79 0.0001

ASN 79 GLN 80 0.0001

GLN 80 THR 81 0.0112

THR 81 ARG 82 0.0000

ARG 82 MET 83 -0.0000

MET 83 VAL 84 0.0002

VAL 84 ALA 85 -0.0050

ALA 85 ALA 86 0.0001

ALA 86 LEU 87 -0.0000

LEU 87 ALA 88 0.0001

ALA 88 ALA 89 -0.0268

ALA 89 LYS 90 0.0001

LYS 90 LEU 91 0.0003

LEU 91 GLY 92 0.0002

GLY 92 LYS 93 -0.1758

LYS 93 LYS 94 -0.0006

LYS 94 CYS 95 -0.0001

CYS 95 VAL 96 0.0002

VAL 96 LEU 97 -0.0047

LEU 97 ILE 98 0.0004

ILE 98 GLN 99 -0.0002

GLN 99 GLU 100 -0.0001

GLU 100 ASP 101 0.0066

ASP 101 TRP 102 -0.0003

TRP 102 VAL 103 -0.0001

VAL 103 PRO 104 0.0000

PRO 104 ILE 105 0.0272

ILE 105 PRO 106 0.0000

PRO 106 GLU 107 0.0000

GLU 107 ALA 108 -0.0003

ALA 108 GLU 109 -0.0424

GLU 109 LYS 110 -0.0001

LYS 110 ASP 111 -0.0000

ASP 111 VAL 112 0.0005

VAL 112 TYR 113 0.0784

TYR 113 ASN 114 0.0002

ASN 114 ARG 115 -0.0003

ARG 115 VAL 116 0.0002

VAL 116 GLY 117 0.0089

GLY 117 ASN 118 0.0001

ASN 118 ILE 119 0.0001

ILE 119 GLU 120 -0.0003

GLU 120 LEU 121 -0.0275

LEU 121 SER 122 -0.0001

SER 122 ARG 123 -0.0003

ARG 123 ILE 124 0.0003

ILE 124 MET 125 0.0305

MET 125 GLY 126 -0.0001

GLY 126 ALA 127 -0.0001

ALA 127 ASP 128 -0.0001

ASP 128 VAL 129 -0.0828

VAL 129 ARG 130 -0.0001

ARG 130 VAL 131 0.0000

VAL 131 ILE 132 -0.0002

ILE 132 GLU 133 -0.0652

GLU 133 ASP 134 0.0002

ASP 134 GLY 135 -0.0003

GLY 135 PHE 136 0.0000

PHE 136 ASP 137 0.0126

ASP 137 ILE 138 0.0002

ILE 138 GLY 139 0.0003

GLY 139 MET 140 -0.0003

MET 140 ARG 141 0.0043

ARG 141 LYS 142 0.0001

LYS 142 SER 143 -0.0000

SER 143 PHE 144 -0.0000

PHE 144 ALA 145 0.0155

ALA 145 ASN 146 -0.0004

ASN 146 ALA 147 0.0000

ALA 147 LEU 148 -0.0000

LEU 148 GLN 149 -0.0177

GLN 149 GLU 150 -0.0001

GLU 150 LEU 151 -0.0001

LEU 151 GLU 152 0.0002

GLU 152 ASP 153 -0.0003

ASP 153 ALA 154 -0.0003

ALA 154 GLY 155 0.0002

GLY 155 HIS 156 0.0000

HIS 156 LYS 157 -0.0335

LYS 157 PRO 158 0.0000

PRO 158 TYR 159 0.0002

TYR 159 PRO 160 -0.0001

PRO 160 ILE 161 -0.0076

ILE 161 PRO 162 0.0000

PRO 162 ALA 163 -0.0004

ALA 163 GLY 164 0.0000

GLY 164 CYS 165 0.0263

CYS 165 SER 166 -0.0002

SER 166 GLU 167 -0.0001

GLU 167 HIS 168 -0.0000

HIS 168 LYS 169 0.0436

LYS 169 TYR 170 0.0002

TYR 170 GLY 171 -0.0003

GLY 171 GLY 172 -0.0002

GLY 172 LEU 173 0.0191

LEU 173 GLY 174 0.0002

GLY 174 PHE 175 -0.0001

PHE 175 VAL 176 0.0001

VAL 176 GLY 177 -0.0089

GLY 177 PHE 178 -0.0003

PHE 178 ALA 179 -0.0002

ALA 179 ASP 180 -0.0002

ASP 180 GLU 181 -0.0329

GLU 181 VAL 182 0.0001

VAL 182 ILE 183 -0.0001

ILE 183 ASN 184 -0.0002

ASN 184 GLN 185 -0.0371

GLN 185 GLU 186 0.0000

GLU 186 VAL 187 -0.0001

VAL 187 GLU 188 -0.0002

GLU 188 LEU 189 -0.0345

LEU 189 GLY 190 0.0003

GLY 190 ILE 191 0.0000

ILE 191 LYS 192 0.0003

LYS 192 PHE 193 0.0128

PHE 193 ASP 194 0.0004

ASP 194 LYS 195 -0.0001

LYS 195 ILE 196 -0.0001

ILE 196 VAL 197 -0.0282

VAL 197 VAL 198 -0.0002

VAL 198 CYS 199 0.0002

CYS 199 CYS 200 -0.0002

CYS 200 VAL 201 -0.0279

VAL 201 THR 202 -0.0001

THR 202 GLY 203 -0.0003

GLY 203 SER 204 0.0003

SER 204 THR 205 -0.0058

THR 205 THR 206 -0.0001

THR 206 ALA 207 0.0002

ALA 207 GLY 208 -0.0002

GLY 208 ILE 209 0.0025

ILE 209 LEU 210 0.0002

LEU 210 ALA 211 -0.0004

ALA 211 GLY 212 0.0002

GLY 212 MET 213 0.0042

MET 213 ALA 214 -0.0000

ALA 214 GLN 215 -0.0004

GLN 215 TYR 216 -0.0000

TYR 216 GLY 217 0.0161

GLY 217 ARG 218 -0.0001

ARG 218 GLN 219 0.0004

GLN 219 ASP 220 -0.0001

ASP 220 ASP 221 -0.0299

ASP 221 VAL 222 0.0001

VAL 222 ILE 223 0.0004

ILE 223 ALA 224 0.0000

ALA 224 ILE 225 -0.0212

ILE 225 ASP 226 -0.0001

ASP 226 ALA 227 -0.0000

ALA 227 SER 228 -0.0004

SER 228 PHE 229 -0.0062

PHE 229 THR 230 -0.0001

THR 230 SER 231 -0.0001

SER 231 GLU 232 0.0002

GLU 232 LYS 233 -0.0043

LYS 233 THR 234 0.0001

THR 234 LYS 235 -0.0002

LYS 235 GLU 236 0.0003

GLU 236 GLN 237 -0.0005

GLN 237 THR 238 0.0001

THR 238 LEU 239 0.0003

LEU 239 ARG 240 -0.0003

ARG 240 ILE 241 0.0013

ILE 241 ALA 242 -0.0002

ALA 242 ASN 243 0.0002

ASN 243 ASN 244 0.0000

ASN 244 THR 245 -0.0059

THR 245 ALA 246 -0.0000

ALA 246 LYS 247 -0.0004

LYS 247 LEU 248 0.0000

LEU 248 ILE 249 -0.0003

ILE 249 GLY 250 -0.0003

GLY 250 VAL 251 0.0004

VAL 251 GLU 252 -0.0001

GLU 252 HIS 253 0.0052

HIS 253 GLU 254 0.0000

GLU 254 PHE 255 -0.0002

PHE 255 LYS 256 0.0002

LYS 256 ASP 257 0.0125

ASP 257 PHE 258 -0.0004

PHE 258 THR 259 0.0001

THR 259 LEU 260 -0.0003

LEU 260 ASP 261 0.0230

ASP 261 THR 262 0.0003

THR 262 ARG 263 0.0001

ARG 263 PHE 264 0.0003

PHE 264 ALA 265 -0.0438

ALA 265 TYR 266 -0.0004

TYR 266 PRO 267 0.0002

PRO 267 CYS 268 -0.0000

CYS 268 TYR 269 -0.0170

TYR 269 GLY 270 -0.0003

GLY 270 VAL 271 -0.0001

VAL 271 PRO 272 -0.0003

PRO 272 ASN 273 -0.0000

ASN 273 GLU 274 -0.0000

GLU 274 GLY 275 0.0002

GLY 275 THR 276 0.0001

THR 276 ILE 277 0.0027

ILE 277 GLU 278 0.0001

GLU 278 ALA 279 0.0001

ALA 279 ILE 280 0.0002

ILE 280 ARG 281 -0.0025

ARG 281 THR 282 0.0001

THR 282 CYS 283 0.0000

CYS 283 ALA 284 -0.0003

ALA 284 GLU 285 -0.0354

GLU 285 GLN 286 -0.0002

GLN 286 GLU 287 0.0002

GLU 287 GLY 288 0.0003

GLY 288 VAL 289 -0.1197

VAL 289 LEU 290 -0.0001

LEU 290 THR 291 0.0000

THR 291 ASP 292 -0.0000

ASP 292 PRO 293 0.0315

PRO 293 VAL 294 -0.0003

VAL 294 TYR 295 0.0003

TYR 295 GLU 296 -0.0000

GLU 296 GLY 297 0.0033

GLY 297 LYS 298 0.0001

LYS 298 SER 299 -0.0000

SER 299 MET 300 -0.0003

MET 300 GLN 301 0.0159

GLN 301 GLY 302 -0.0001

GLY 302 LEU 303 -0.0002

LEU 303 ILE 304 -0.0002

ILE 304 ALA 305 0.0015

ALA 305 LEU 306 0.0000

LEU 306 ILE 307 -0.0001

ILE 307 LYS 308 0.0002

LYS 308 GLU 309 0.0194

GLU 309 ASP 310 -0.0001

ASP 310 TYR 311 0.0002

TYR 311 PHE 312 -0.0003

PHE 312 LYS 313 -0.0341

LYS 313 PRO 314 -0.0003

PRO 314 GLY 315 -0.0001

GLY 315 ALA 316 -0.0003

ALA 316 ASN 317 0.0534

ASN 317 VAL 318 0.0001

VAL 318 LEU 319 0.0002

LEU 319 TYR 320 -0.0001

TYR 320 VAL 321 0.0254

VAL 321 HIS 322 -0.0004

HIS 322 LEU 323 0.0000

LEU 323 GLY 324 0.0003

GLY 324 GLY 325 0.0475

GLY 325 ALA 326 0.0002

ALA 326 PRO 327 -0.0002

PRO 327 ALA 328 -0.0002

ALA 328 LEU 329 0.0223

LEU 329 SER 330 -0.0002

SER 330 ALA 331 -0.0001

ALA 331 TYR 332 -0.0002

TYR 332 SER 333 0.0750

SER 333 SER 334 0.0001

SER 334 PHE 335 -0.0004

PHE 335 PHE 336 0.0000

PHE 336 PRO 337 0.1075

PRO 337 THR 338 -0.0002

THR 338 LYS 339 -0.0002

LYS 339 THR 340 0.0002

THR 340 ALA 341 0.1914

ALA 341 ALA 1 0.0253

ALA 1 GLY 2 -0.0002

GLY 2 VAL 3 0.0003

VAL 3 ALA 4 0.0000

ALA 4 LYS 5 0.0091

LYS 5 PHE 6 -0.0001

PHE 6 ALA 7 0.0001

ALA 7 LYS 8 0.0001

LYS 8 TYR 9 0.1158

TYR 9 PRO 10 0.0001

PRO 10 LEU 11 0.0000

LEU 11 THR 12 0.0001

THR 12 PHE 13 -0.1113

PHE 13 GLY 14 -0.0003

GLY 14 PRO 15 -0.0000

PRO 15 SER 16 -0.0001

SER 16 PRO 17 -0.0166

PRO 17 ILE 18 0.0004

ILE 18 SER 19 -0.0004

SER 19 ASN 20 0.0001

ASN 20 LEU 21 -0.0754

LEU 21 ASN 22 -0.0002

ASN 22 ARG 23 -0.0001

ARG 23 LEU 24 -0.0003

LEU 24 SER 25 -0.0196

SER 25 GLN 26 0.0001

GLN 26 HIS 27 0.0001

HIS 27 LEU 28 0.0004

LEU 28 GLY 29 -0.0165

GLY 29 SER 30 0.0001

SER 30 LYS 31 -0.0001

LYS 31 VAL 32 0.0001

VAL 32 ASN 33 0.0527

ASN 33 VAL 34 -0.0002

VAL 34 TYR 35 0.0002

TYR 35 ALA 36 -0.0002

ALA 36 LYS 37 0.0431

LYS 37 ARG 38 -0.0001

ARG 38 GLU 39 0.0002

GLU 39 ASP 40 -0.0000

ASP 40 CYS 41 -0.0231

CYS 41 ASN 42 0.0000

ASN 42 SER 43 0.0001

SER 43 GLY 44 -0.0002

GLY 44 LEU 45 -0.1084

LEU 45 ALA 46 0.0002

ALA 46 PHE 47 -0.0000

PHE 47 GLY 48 -0.0002

GLY 48 GLY 49 0.0500

GLY 49 ASN 50 0.0001

ASN 50 THR 51 0.0002

THR 51 LEU 52 -0.0002

LEU 52 ARG 53 0.0600

ARG 53 LYS 54 -0.0001

LYS 54 LEU 55 0.0000

LEU 55 GLU 56 -0.0000

GLU 56 TYR 57 -0.0369

TYR 57 ILE 58 -0.0000

ILE 58 VAL 59 -0.0002

VAL 59 PRO 60 -0.0000

PRO 60 ASP 61 -0.0608

ASP 61 ILE 62 0.0003

ILE 62 VAL 63 0.0003

VAL 63 GLU 64 0.0000

GLU 64 GLY 65 -0.0266

GLY 65 ASP 66 -0.0002

ASP 66 TYR 67 -0.0002

TYR 67 THR 68 0.0001

THR 68 HIS 69 0.0343

HIS 69 LEU 70 -0.0001

LEU 70 VAL 71 -0.0001

VAL 71 SER 72 0.0000

SER 72 ILE 73 0.0327

ILE 73 GLY 74 -0.0001

GLY 74 GLY 75 -0.0001

GLY 75 ARG 76 0.0001

ARG 76 GLN 77 0.0386

GLN 77 SER 78 -0.0003

SER 78 ASN 79 0.0001

ASN 79 GLN 80 -0.0003

GLN 80 THR 81 0.0127

THR 81 ARG 82 -0.0000

ARG 82 MET 83 -0.0003

MET 83 VAL 84 -0.0000

VAL 84 ALA 85 -0.0010

ALA 85 ALA 86 -0.0004

ALA 86 LEU 87 0.0001

LEU 87 ALA 88 0.0001

ALA 88 ALA 89 -0.0350

ALA 89 LYS 90 -0.0003

LYS 90 LEU 91 -0.0000

LEU 91 GLY 92 0.0001

GLY 92 LYS 93 -0.1841

LYS 93 LYS 94 0.0000

LYS 94 CYS 95 0.0001

CYS 95 VAL 96 -0.0000

VAL 96 LEU 97 -0.0097

LEU 97 ILE 98 -0.0006

ILE 98 GLN 99 0.0002

GLN 99 GLU 100 -0.0003

GLU 100 ASP 101 0.0031

ASP 101 TRP 102 0.0001

TRP 102 VAL 103 -0.0003

VAL 103 PRO 104 0.0001

PRO 104 ILE 105 0.0065

ILE 105 PRO 106 -0.0001

PRO 106 GLU 107 0.0001

GLU 107 ALA 108 -0.0003

ALA 108 GLU 109 -0.0628

GLU 109 LYS 110 -0.0000

LYS 110 ASP 111 -0.0004

ASP 111 VAL 112 0.0000

VAL 112 TYR 113 0.0876

TYR 113 ASN 114 0.0001

ASN 114 ARG 115 -0.0001

ARG 115 VAL 116 -0.0001

VAL 116 GLY 117 0.0004

GLY 117 ASN 118 0.0004

ASN 118 ILE 119 -0.0003

ILE 119 GLU 120 -0.0004

GLU 120 LEU 121 -0.0359

LEU 121 SER 122 -0.0004

SER 122 ARG 123 -0.0000

ARG 123 ILE 124 -0.0003

ILE 124 MET 125 0.0316

MET 125 GLY 126 -0.0001

GLY 126 ALA 127 0.0004

ALA 127 ASP 128 -0.0004

ASP 128 VAL 129 -0.0619

VAL 129 ARG 130 0.0000

ARG 130 VAL 131 0.0001

VAL 131 ILE 132 -0.0004

ILE 132 GLU 133 -0.0627

GLU 133 ASP 134 -0.0002

ASP 134 GLY 135 0.0002

GLY 135 PHE 136 -0.0002

PHE 136 ASP 137 0.0158

ASP 137 ILE 138 0.0003

ILE 138 GLY 139 -0.0001

GLY 139 MET 140 0.0002

MET 140 ARG 141 0.0005

ARG 141 LYS 142 0.0001

LYS 142 SER 143 0.0002

SER 143 PHE 144 0.0003

PHE 144 ALA 145 0.0304

ALA 145 ASN 146 -0.0000

ASN 146 ALA 147 -0.0000

ALA 147 LEU 148 0.0002

LEU 148 GLN 149 -0.0094

GLN 149 GLU 150 -0.0002

GLU 150 LEU 151 -0.0000

LEU 151 GLU 152 -0.0002

GLU 152 ASP 153 -0.0113

ASP 153 ALA 154 -0.0002

ALA 154 GLY 155 -0.0001

GLY 155 HIS 156 0.0003

HIS 156 LYS 157 -0.0123

LYS 157 PRO 158 -0.0001

PRO 158 TYR 159 0.0002

TYR 159 PRO 160 0.0000

PRO 160 ILE 161 -0.0027

ILE 161 PRO 162 -0.0002

PRO 162 ALA 163 -0.0001

ALA 163 GLY 164 0.0001

GLY 164 CYS 165 0.0299

CYS 165 SER 166 0.0000

SER 166 GLU 167 -0.0002

GLU 167 HIS 168 0.0002

HIS 168 LYS 169 0.0498

LYS 169 TYR 170 -0.0001

TYR 170 GLY 171 0.0003

GLY 171 GLY 172 -0.0000

GLY 172 LEU 173 0.0163

LEU 173 GLY 174 0.0002

GLY 174 PHE 175 -0.0001

PHE 175 VAL 176 -0.0001

VAL 176 GLY 177 -0.0128

GLY 177 PHE 178 0.0003

PHE 178 ALA 179 0.0002

ALA 179 ASP 180 -0.0001

ASP 180 GLU 181 -0.0269

GLU 181 VAL 182 -0.0000

VAL 182 ILE 183 0.0002

ILE 183 ASN 184 -0.0000

ASN 184 GLN 185 -0.0410

GLN 185 GLU 186 -0.0004

GLU 186 VAL 187 -0.0002

VAL 187 GLU 188 0.0001

GLU 188 LEU 189 -0.0320

LEU 189 GLY 190 0.0000

GLY 190 ILE 191 0.0002

ILE 191 LYS 192 -0.0003

LYS 192 PHE 193 0.0205

PHE 193 ASP 194 -0.0002

ASP 194 LYS 195 -0.0003

LYS 195 ILE 196 0.0001

ILE 196 VAL 197 -0.0243

VAL 197 VAL 198 -0.0000

VAL 198 CYS 199 -0.0001

CYS 199 CYS 200 -0.0001

CYS 200 VAL 201 -0.0308

VAL 201 THR 202 0.0003

THR 202 GLY 203 0.0000

GLY 203 SER 204 0.0001

SER 204 THR 205 -0.0078

THR 205 THR 206 -0.0000

THR 206 ALA 207 -0.0004

ALA 207 GLY 208 0.0001

GLY 208 ILE 209 0.0014

ILE 209 LEU 210 -0.0000

LEU 210 ALA 211 0.0001

ALA 211 GLY 212 0.0001

GLY 212 MET 213 0.0049

MET 213 ALA 214 0.0001

ALA 214 GLN 215 -0.0002

GLN 215 TYR 216 0.0000

TYR 216 GLY 217 0.0176

GLY 217 ARG 218 -0.0003

ARG 218 GLN 219 0.0001

GLN 219 ASP 220 0.0001

ASP 220 ASP 221 -0.0303

ASP 221 VAL 222 -0.0002

VAL 222 ILE 223 0.0004

ILE 223 ALA 224 -0.0004

ALA 224 ILE 225 -0.0211

ILE 225 ASP 226 0.0003

ASP 226 ALA 227 -0.0006

ALA 227 SER 228 0.0003

SER 228 PHE 229 -0.0061

PHE 229 THR 230 0.0000

THR 230 SER 231 -0.0001

SER 231 GLU 232 0.0001

GLU 232 LYS 233 0.0073

LYS 233 THR 234 0.0002

THR 234 LYS 235 0.0004

LYS 235 GLU 236 0.0002

GLU 236 GLN 237 -0.0019

GLN 237 THR 238 0.0002

THR 238 LEU 239 -0.0004

LEU 239 ARG 240 0.0003

ARG 240 ILE 241 0.0009

ILE 241 ALA 242 0.0000

ALA 242 ASN 243 0.0001

ASN 243 ASN 244 0.0000

ASN 244 THR 245 -0.0056

THR 245 ALA 246 0.0002

ALA 246 LYS 247 -0.0004

LYS 247 LEU 248 0.0000

LEU 248 ILE 249 -0.0044

ILE 249 GLY 250 0.0002

GLY 250 VAL 251 0.0000

VAL 251 GLU 252 -0.0003

GLU 252 HIS 253 0.0020

HIS 253 GLU 254 0.0001

GLU 254 PHE 255 -0.0000

PHE 255 LYS 256 0.0001

LYS 256 ASP 257 0.0139

ASP 257 PHE 258 0.0000

PHE 258 THR 259 0.0004

THR 259 LEU 260 0.0005

LEU 260 ASP 261 0.0167

ASP 261 THR 262 -0.0001

THR 262 ARG 263 -0.0001

ARG 263 PHE 264 0.0003

PHE 264 ALA 265 -0.0531

ALA 265 TYR 266 -0.0002

TYR 266 PRO 267 0.0002

PRO 267 CYS 268 0.0003

CYS 268 TYR 269 -0.0133

TYR 269 GLY 270 0.0004

GLY 270 VAL 271 -0.0006

VAL 271 PRO 272 0.0002

PRO 272 ASN 273 -0.0116

ASN 273 GLU 274 -0.0000

GLU 274 GLY 275 -0.0000

GLY 275 THR 276 -0.0001

THR 276 ILE 277 0.0034

ILE 277 GLU 278 -0.0002

GLU 278 ALA 279 -0.0001

ALA 279 ILE 280 0.0001

ILE 280 ARG 281 0.0077

ARG 281 THR 282 -0.0000

THR 282 CYS 283 -0.0001

CYS 283 ALA 284 0.0001

ALA 284 GLU 285 -0.0237

GLU 285 GLN 286 -0.0005

GLN 286 GLU 287 0.0001

GLU 287 GLY 288 -0.0001

GLY 288 VAL 289 -0.0971

VAL 289 LEU 290 -0.0001

LEU 290 THR 291 -0.0002

THR 291 ASP 292 0.0001

ASP 292 PRO 293 0.0363

PRO 293 VAL 294 -0.0005

VAL 294 TYR 295 0.0000

TYR 295 GLU 296 -0.0002

GLU 296 GLY 297 0.0033

GLY 297 LYS 298 -0.0001

LYS 298 SER 299 -0.0003

SER 299 MET 300 -0.0005

MET 300 GLN 301 0.0163

GLN 301 GLY 302 -0.0003

GLY 302 LEU 303 0.0000

LEU 303 ILE 304 -0.0002

ILE 304 ALA 305 0.0066

ALA 305 LEU 306 0.0000

LEU 306 ILE 307 -0.0001

ILE 307 LYS 308 0.0001

LYS 308 GLU 309 0.0200

GLU 309 ASP 310 0.0004

ASP 310 TYR 311 -0.0002

TYR 311 PHE 312 0.0004

PHE 312 LYS 313 -0.0390

LYS 313 PRO 314 -0.0003

PRO 314 GLY 315 -0.0001

GLY 315 ALA 316 0.0003

ALA 316 ASN 317 0.0572

ASN 317 VAL 318 0.0001

VAL 318 LEU 319 0.0002

LEU 319 TYR 320 -0.0003

TYR 320 VAL 321 0.0286

VAL 321 HIS 322 0.0001

HIS 322 LEU 323 0.0001

LEU 323 GLY 324 0.0002

GLY 324 GLY 325 0.0488

GLY 325 ALA 326 -0.0004

ALA 326 PRO 327 -0.0001

PRO 327 ALA 328 0.0001

ALA 328 LEU 329 0.0142

LEU 329 SER 330 -0.0000

SER 330 ALA 331 0.0004

ALA 331 TYR 332 0.0004

TYR 332 SER 333 0.0532

SER 333 SER 334 -0.0000

SER 334 PHE 335 -0.0002

PHE 335 PHE 336 -0.0001

PHE 336 PRO 337 0.0854

PRO 337 THR 338 -0.0002

THR 338 LYS 339 0.0004

LYS 339 THR 340 -0.0002

THR 340 ALA 341 0.0474

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 8 ---

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

* 123454321 *