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* Holo AMPK *

CA strain for 260711185133617066

--- 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
GLY 11 SER 12 0.0002

SER 12 VAL 13 -0.0000

VAL 13 LYS 14 0.0001

LYS 14 ILE 15 -0.0002

ILE 15 GLY 16 -0.0005

GLY 16 HIS 17 0.0003

HIS 17 TYR 18 0.0000

TYR 18 ILE 19 0.0003

ILE 19 LEU 20 0.0000

LEU 20 GLY 21 -0.0071

GLY 21 ASP 22 -0.0001

ASP 22 THR 23 0.0005

THR 23 LEU 24 -0.0002

LEU 24 GLY 25 -0.0002

GLY 25 VAL 26 -0.0309

VAL 26 GLY 27 -0.0002

GLY 27 THR 28 0.0004

THR 28 PHE 29 0.0001

PHE 29 GLY 30 0.0003

GLY 30 LYS 31 -0.0268

LYS 31 VAL 32 0.0003

VAL 32 LYS 33 0.0001

LYS 33 VAL 34 -0.0002

VAL 34 GLY 35 0.0001

GLY 35 LYS 36 -0.0270

LYS 36 HIS 37 -0.0001

HIS 37 GLU 38 0.0001

GLU 38 LEU 39 0.0002

LEU 39 THR 40 0.0002

THR 40 GLY 41 -0.0033

GLY 41 HIS 42 0.0001

HIS 42 LYS 43 0.0000

LYS 43 VAL 44 -0.0001

VAL 44 ALA 45 0.0004

ALA 45 VAL 46 0.0043

VAL 46 LYS 47 -0.0000

LYS 47 ILE 48 -0.0003

ILE 48 LEU 49 0.0000

LEU 49 ASN 50 0.0001

ASN 50 ARG 51 -0.0013

ARG 51 GLN 52 0.0002

GLN 52 LYS 53 -0.0004

LYS 53 ILE 54 0.0001

ILE 54 ARG 55 -0.0000

ARG 55 SER 56 0.0106

SER 56 LEU 57 0.0002

LEU 57 ASP 58 -0.0001

ASP 58 VAL 59 0.0003

VAL 59 VAL 60 0.0002

VAL 60 GLY 61 -0.0121

GLY 61 LYS 62 0.0003

LYS 62 ILE 63 0.0002

ILE 63 ARG 64 -0.0002

ARG 64 ARG 65 -0.0003

ARG 65 GLU 66 0.0020

GLU 66 ILE 67 0.0004

ILE 67 GLN 68 -0.0002

GLN 68 ASN 69 -0.0003

ASN 69 LEU 70 -0.0002

LEU 70 LYS 71 0.0561

LYS 71 LEU 72 0.0001

LEU 72 PHE 73 0.0000

PHE 73 ARG 74 -0.0000

ARG 74 HIS 75 -0.0000

HIS 75 PRO 76 -0.0236

PRO 76 HIS 77 0.0001

HIS 77 ILE 78 0.0002

ILE 78 ILE 79 -0.0003

ILE 79 LYS 80 0.0001

LYS 80 LEU 81 -0.1123

LEU 81 TYR 82 0.0004

TYR 82 GLN 83 0.0002

GLN 83 VAL 84 0.0000

VAL 84 ILE 85 0.0000

ILE 85 SER 86 -0.0749

SER 86 THR 87 -0.0000

THR 87 PRO 88 -0.0003

PRO 88 SER 89 0.0002

SER 89 ASP 90 -0.0003

ASP 90 ILE 91 0.0131

ILE 91 PHE 92 0.0002

PHE 92 MET 93 -0.0001

MET 93 VAL 94 -0.0003

VAL 94 MET 95 0.0001

MET 95 GLU 96 -0.0833

GLU 96 TYR 97 0.0002

TYR 97 VAL 98 0.0001

VAL 98 SER 99 0.0003

SER 99 GLY 100 0.0001

GLY 100 GLY 101 -0.0964

GLY 101 GLU 102 0.0001

GLU 102 LEU 103 0.0002

LEU 103 PHE 104 0.0000

PHE 104 ASP 105 0.0000

ASP 105 TYR 106 0.0060

TYR 106 ILE 107 0.0000

ILE 107 CYS 108 -0.0003

CYS 108 LYS 109 -0.0002

LYS 109 ASN 110 0.0000

ASN 110 GLY 111 -0.0152

GLY 111 ARG 112 -0.0001

ARG 112 LEU 113 0.0000

LEU 113 ASP 114 -0.0002

ASP 114 GLU 115 -0.0003

GLU 115 LYS 116 -0.0026

LYS 116 GLU 117 -0.0002

GLU 117 SER 118 -0.0002

SER 118 ARG 119 -0.0001

ARG 119 ARG 120 0.0000

ARG 120 LEU 121 -0.0007

LEU 121 PHE 122 -0.0001

PHE 122 GLN 123 0.0003

GLN 123 GLN 124 -0.0002

GLN 124 ILE 125 -0.0000

ILE 125 LEU 126 0.0081

LEU 126 SER 127 -0.0000

SER 127 GLY 128 0.0002

GLY 128 VAL 129 0.0002

VAL 129 ASP 130 0.0001

ASP 130 TYR 131 -0.0388

TYR 131 CYS 132 0.0001

CYS 132 HIS 133 -0.0000

HIS 133 ARG 134 -0.0001

ARG 134 HIS 135 -0.0000

HIS 135 MET 136 0.0374

MET 136 VAL 137 0.0003

VAL 137 VAL 138 -0.0004

VAL 138 HIS 139 0.0003

HIS 139 ARG 140 -0.0002

ARG 140 ASP 141 -0.0367

ASP 141 LEU 142 0.0001

LEU 142 LYS 143 -0.0002

LYS 143 PRO 144 0.0000

PRO 144 GLU 145 0.0001

GLU 145 ASN 146 0.0138

ASN 146 VAL 147 -0.0002

VAL 147 LEU 148 0.0002

LEU 148 LEU 149 -0.0004

LEU 149 ASP 150 0.0003

ASP 150 ALA 151 -0.0325

ALA 151 HIS 152 0.0000

HIS 152 MET 153 0.0003

MET 153 ASN 154 0.0002

ASN 154 ALA 155 -0.0003

ALA 155 LYS 156 0.0242

LYS 156 ILE 157 0.0001

ILE 157 ALA 158 -0.0001

ALA 158 ASP 159 -0.0002

ASP 159 PHE 160 0.0002

PHE 160 GLY 161 0.0008

GLY 161 LEU 162 0.0001

LEU 162 SER 163 -0.0000

SER 163 ASN 164 0.0002

ASN 164 MET 165 -0.0002

MET 165 MET 166 0.0519

MET 166 SER 167 0.0001

SER 167 ASP 168 0.0002

ASP 168 GLY 169 0.0002

GLY 169 GLU 170 -0.0002

GLU 170 PHE 171 0.0472

PHE 171 LEU 172 0.0001

LEU 172 ARG 173 -0.0001

ARG 173 SER 175 -0.0115

SER 175 CYS 176 0.0000

CYS 176 GLY 177 0.0002

GLY 177 SER 178 0.0001

SER 178 PRO 179 -0.0003

PRO 179 ASN 180 0.0273

ASN 180 TYR 181 0.0002

TYR 181 ALA 182 0.0001

ALA 182 ALA 183 -0.0001

ALA 183 PRO 184 0.0004

PRO 184 GLU 185 0.0038

GLU 185 VAL 186 -0.0000

VAL 186 ILE 187 0.0000

ILE 187 SER 188 0.0000

SER 188 GLY 189 0.0002

GLY 189 ARG 190 -0.0299

ARG 190 LEU 191 0.0001

LEU 191 TYR 192 0.0000

TYR 192 ALA 193 -0.0002

ALA 193 GLY 194 0.0005

GLY 194 PRO 195 -0.0138

PRO 195 GLU 196 -0.0001

GLU 196 VAL 197 -0.0000

VAL 197 ASP 198 0.0001

ASP 198 ILE 199 0.0004

ILE 199 TRP 200 -0.0062

TRP 200 SER 201 0.0001

SER 201 SER 202 -0.0000

SER 202 GLY 203 -0.0005

GLY 203 VAL 204 0.0000

VAL 204 ILE 205 -0.0212

ILE 205 LEU 206 -0.0000

LEU 206 TYR 207 -0.0002

TYR 207 ALA 208 0.0000

ALA 208 LEU 209 0.0000

LEU 209 LEU 210 0.0142

LEU 210 CYS 211 0.0002

CYS 211 GLY 212 -0.0002

GLY 212 THR 213 0.0000

THR 213 LEU 214 0.0001

LEU 214 PRO 215 -0.0106

PRO 215 PHE 216 0.0001

PHE 216 ASP 217 -0.0001

ASP 217 ASP 218 -0.0002

ASP 218 ASP 219 -0.0002

ASP 219 HIS 220 -0.0022

HIS 220 VAL 221 -0.0000

VAL 221 PRO 222 -0.0002

PRO 222 THR 223 0.0000

THR 223 LEU 224 -0.0001

LEU 224 PHE 225 -0.0070

PHE 225 LYS 226 -0.0002

LYS 226 LYS 227 0.0002

LYS 227 ILE 228 -0.0000

ILE 228 CYS 229 0.0002

CYS 229 ASP 230 0.0200

ASP 230 GLY 231 -0.0001

GLY 231 ILE 232 -0.0004

ILE 232 PHE 233 0.0005

PHE 233 TYR 234 -0.0002

TYR 234 THR 235 0.0034

THR 235 PRO 236 0.0002

PRO 236 GLN 237 -0.0001

GLN 237 TYR 238 -0.0001

TYR 238 LEU 239 0.0002

LEU 239 ASN 240 -0.0049

ASN 240 PRO 241 0.0003

PRO 241 SER 242 0.0002

SER 242 VAL 243 -0.0000

VAL 243 ILE 244 -0.0003

ILE 244 SER 245 -0.0054

SER 245 LEU 246 0.0002

LEU 246 LEU 247 -0.0002

LEU 247 LYS 248 0.0000

LYS 248 HIS 249 -0.0001

HIS 249 MET 250 0.0024

MET 250 LEU 251 -0.0003

LEU 251 GLN 252 -0.0000

GLN 252 VAL 253 -0.0002

VAL 253 ASP 254 0.0000

ASP 254 PRO 255 -0.0347

PRO 255 MET 256 0.0003

MET 256 LYS 257 0.0003

LYS 257 ARG 258 -0.0007

ARG 258 ALA 259 -0.0002

ALA 259 THR 260 -0.0260

THR 260 ILE 261 -0.0001

ILE 261 LYS 262 0.0002

LYS 262 ASP 263 0.0000

ASP 263 ILE 264 0.0001

ILE 264 ARG 265 0.0171

ARG 265 GLU 266 -0.0001

GLU 266 HIS 267 0.0001

HIS 267 GLU 268 -0.0002

GLU 268 TRP 269 -0.0003

TRP 269 PHE 270 -0.0105

PHE 270 LYS 271 0.0002

LYS 271 GLN 272 -0.0002

GLN 272 ASP 273 -0.0002

ASP 273 LEU 274 0.0000

LEU 274 PRO 275 -0.0118

PRO 275 LYS 276 0.0002

LYS 276 TYR 277 0.0001

TYR 277 LEU 278 -0.0001

LEU 278 PHE 279 0.0003

PHE 279 PRO 280 0.0018

PRO 280 GLU 281 -0.0000

GLU 281 ASP 282 -0.0001

ASP 282 LYS 395 0.0670

LYS 395 ALA 396 -0.0000

ALA 396 LYS 397 0.0001

LYS 397 TRP 398 -0.0001

TRP 398 HIS 399 -0.0001

HIS 399 LEU 400 -0.0384

LEU 400 GLY 401 0.0003

GLY 401 ILE 402 -0.0000

ILE 402 ARG 403 -0.0001

ARG 403 SER 404 -0.0001

SER 404 GLN 405 -0.0052

GLN 405 SER 406 -0.0000

SER 406 ARG 407 -0.0002

ARG 407 PRO 408 -0.0000

PRO 408 ASN 409 0.0000

ASN 409 ASP 410 0.0000

ASP 410 ILE 411 -0.0005

ILE 411 MET 412 0.0000

MET 412 ALA 413 0.0003

ALA 413 GLU 414 0.0002

GLU 414 VAL 415 -0.0005

VAL 415 CYS 416 -0.0002

CYS 416 ARG 417 -0.0005

ARG 417 ALA 418 -0.0000

ALA 418 ILE 419 0.0000

ILE 419 LYS 420 -0.0023

LYS 420 GLN 421 -0.0001

GLN 421 LEU 422 0.0001

LEU 422 ASP 423 0.0003

ASP 423 TYR 424 -0.0004

TYR 424 GLU 425 0.0017

GLU 425 TRP 426 -0.0004

TRP 426 LYS 427 0.0003

LYS 427 VAL 428 -0.0001

VAL 428 VAL 429 -0.0002

VAL 429 ASN 430 0.0166

ASN 430 PRO 431 0.0004

PRO 431 TYR 432 0.0000

TYR 432 TYR 433 -0.0001

TYR 433 LEU 434 0.0005

LEU 434 ARG 435 0.0207

ARG 435 VAL 436 0.0002

VAL 436 ARG 437 0.0001

ARG 437 ARG 438 0.0001

ARG 438 LYS 439 -0.0002

LYS 439 ASN 440 0.0247

ASN 440 PRO 441 -0.0001

PRO 441 VAL 442 -0.0001

VAL 442 THR 443 -0.0002

THR 443 SER 444 0.0001

SER 444 THR 445 0.0086

THR 445 TYR 446 0.0002

TYR 446 SER 447 -0.0000

SER 447 LYS 448 -0.0001

LYS 448 MET 449 0.0000

MET 449 SER 450 0.0255

SER 450 LEU 451 0.0001

LEU 451 GLN 452 0.0003

GLN 452 LEU 453 -0.0004

LEU 453 TYR 454 0.0002

TYR 454 GLN 455 0.0123

GLN 455 VAL 456 -0.0002

VAL 456 ASP 457 0.0001

ASP 457 SER 458 -0.0005

SER 458 ARG 459 0.0000

ARG 459 THR 460 0.0021

THR 460 TYR 461 0.0001

TYR 461 LEU 462 0.0004

LEU 462 LEU 463 0.0000

LEU 463 ASP 464 0.0002

ASP 464 PHE 465 0.0056

PHE 465 ARG 466 0.0002

ARG 466 SER 467 -0.0002

SER 467 ILE 468 -0.0005

ILE 468 ASP 469 0.0004

ASP 469 ASP 470 0.0053

ASP 470 GLU 471 0.0001

GLU 471 LEU 526 0.0033

LEU 526 THR 527 0.0001

THR 527 PRO 528 0.0003

PRO 528 ARG 529 -0.0001

ARG 529 PRO 530 0.0003

PRO 530 GLY 531 -0.0001

GLY 531 SER 532 -0.0003

SER 532 HIS 533 0.0000

HIS 533 THR 534 0.0001

THR 534 ILE 535 -0.0001

ILE 535 GLU 536 0.0011

GLU 536 PHE 537 0.0002

PHE 537 PHE 538 0.0003

PHE 538 GLU 539 -0.0000

GLU 539 MET 540 0.0002

MET 540 CYS 541 -0.0004

CYS 541 ALA 542 -0.0001

ALA 542 ASN 543 0.0000

ASN 543 LEU 544 0.0004

LEU 544 ILE 545 0.0002

ILE 545 LYS 546 0.0052

LYS 546 ILE 547 -0.0001

ILE 547 LEU 548 -0.0000

LEU 548 ALA 549 -0.0001

ALA 549 PRO 74 -0.0163

PRO 74 ALA 75 0.0002

ALA 75 GLN 76 0.0000

GLN 76 ALA 77 0.0001

ALA 77 ARG 78 -0.0001

ARG 78 PRO 79 -0.0369

PRO 79 THR 80 0.0002

THR 80 VAL 81 0.0000

VAL 81 PHE 82 0.0002

PHE 82 ARG 83 0.0002

ARG 83 TRP 84 -0.0332

TRP 84 THR 85 0.0001

THR 85 GLY 86 -0.0003

GLY 86 GLY 87 0.0000

GLY 87 GLY 88 -0.0002

GLY 88 LYS 89 -0.0309

LYS 89 GLU 90 0.0002

GLU 90 VAL 91 0.0001

VAL 91 TYR 92 0.0001

TYR 92 LEU 93 0.0003

LEU 93 SER 94 0.0099

SER 94 GLY 95 0.0002

GLY 95 SER 96 0.0001

SER 96 PHE 97 -0.0000

PHE 97 ASN 98 -0.0005

ASN 98 ASN 99 0.0038

ASN 99 TRP 100 -0.0004

TRP 100 SER 101 0.0000

SER 101 LYS 102 -0.0001

LYS 102 LEU 103 -0.0000

LEU 103 PRO 104 0.0118

PRO 104 LEU 105 0.0000

LEU 105 THR 106 0.0001

THR 106 ARG 107 0.0001

ARG 107 ASP 108 -0.0000

ASP 108 HIS 109 0.0369

HIS 109 ASN 110 0.0001

ASN 110 ASN 111 -0.0000

ASN 111 PHE 112 0.0001

PHE 112 VAL 113 -0.0002

VAL 113 ALA 114 -0.0183

ALA 114 ILE 115 0.0001

ILE 115 LEU 116 -0.0001

LEU 116 ASP 117 -0.0001

ASP 117 LEU 118 -0.0001

LEU 118 PRO 119 0.0028

PRO 119 GLU 120 0.0003

GLU 120 GLY 121 -0.0001

GLY 121 GLU 122 0.0005

GLU 122 HIS 123 -0.0002

HIS 123 GLN 124 -0.0137

GLN 124 TYR 125 -0.0001

TYR 125 LYS 126 -0.0000

LYS 126 PHE 127 0.0004

PHE 127 PHE 128 -0.0000

PHE 128 VAL 129 -0.0006

VAL 129 ASP 130 -0.0003

ASP 130 GLY 131 0.0000

GLY 131 GLN 132 -0.0002

GLN 132 TRP 133 0.0000

TRP 133 THR 134 -0.0224

THR 134 HIS 135 -0.0001

HIS 135 ASP 136 0.0003

ASP 136 PRO 137 -0.0002

PRO 137 SER 138 -0.0000

SER 138 GLU 139 -0.0072

GLU 139 PRO 140 0.0002

PRO 140 ILE 141 -0.0002

ILE 141 VAL 142 0.0001

VAL 142 THR 143 -0.0001

THR 143 SER 144 0.0240

SER 144 GLN 145 0.0000

GLN 145 LEU 146 0.0002

LEU 146 GLY 147 0.0002

GLY 147 THR 148 0.0001

THR 148 VAL 149 0.0314

VAL 149 ASN 150 -0.0003

ASN 150 ASN 151 -0.0002

ASN 151 ILE 152 0.0004

ILE 152 ILE 153 -0.0003

ILE 153 GLN 154 -0.0587

GLN 154 VAL 155 -0.0000

VAL 155 LYS 156 -0.0004

LYS 156 LYS 157 0.0001

LYS 157 THR 158 0.0000

THR 158 ASP 159 0.0003

ASP 159 PHE 160 -0.0002

PHE 160 GLU 161 -0.0003

GLU 161 VAL 162 0.0003

VAL 162 PHE 163 -0.0001

PHE 163 ASP 164 -0.0457

ASP 164 ALA 165 0.0001

ALA 165 LEU 166 0.0004

LEU 166 MET 167 -0.0002

MET 167 VAL 168 0.0000

VAL 168 ASP 169 0.0165

ASP 169 SER 170 -0.0001

SER 170 GLN 171 0.0000

GLN 171 HIS 188 -0.0104

HIS 188 GLN 189 -0.0001

GLN 189 GLU 190 0.0005

GLU 190 PRO 191 0.0002

PRO 191 TYR 192 0.0000

TYR 192 VAL 193 0.0025

VAL 193 CYS 194 -0.0000

CYS 194 LYS 195 0.0002

LYS 195 ARG 201 0.0067

ARG 201 ALA 202 0.0002

ALA 202 PRO 203 0.0001

PRO 203 PRO 204 -0.0002

PRO 204 ILE 205 0.0001

ILE 205 LEU 206 -0.0079

LEU 206 PRO 207 0.0002

PRO 207 PRO 208 -0.0001

PRO 208 HIS 209 0.0001

HIS 209 LEU 210 0.0002

LEU 210 LEU 211 0.0249

LEU 211 GLN 212 -0.0001

GLN 212 VAL 213 0.0002

VAL 213 ILE 214 0.0001

ILE 214 LEU 215 -0.0005

LEU 215 ASN 216 0.0324

ASN 216 LYS 217 0.0001

LYS 217 ASP 218 -0.0001

ASP 218 THR 219 0.0003

THR 219 GLY 220 -0.0003

GLY 220 ILE 221 -0.0064

ILE 221 SER 222 0.0001

SER 222 CYS 223 -0.0002

CYS 223 ASP 224 -0.0002

ASP 224 PRO 225 0.0000

PRO 225 ALA 226 0.0149

ALA 226 LEU 227 0.0001

LEU 227 LEU 228 0.0001

LEU 228 PRO 229 -0.0001

PRO 229 GLU 230 -0.0001

GLU 230 PRO 231 -0.0267

PRO 231 ASN 232 0.0002

ASN 232 HIS 233 -0.0001

HIS 233 VAL 234 -0.0000

VAL 234 MET 235 -0.0003

MET 235 LEU 236 -0.0052

LEU 236 ASN 237 0.0003

ASN 237 HIS 238 0.0001

HIS 238 LEU 239 0.0002

LEU 239 TYR 240 -0.0004

TYR 240 ALA 241 0.0001

ALA 241 LEU 242 -0.0001

LEU 242 SER 243 -0.0004

SER 243 ILE 244 0.0001

ILE 244 LYS 245 -0.0002

LYS 245 ASP 246 -0.0156

ASP 246 GLY 247 0.0003

GLY 247 VAL 248 0.0003

VAL 248 MET 249 -0.0002

MET 249 VAL 250 -0.0003

VAL 250 LEU 251 0.0042

LEU 251 SER 252 0.0002

SER 252 ALA 253 -0.0003

ALA 253 THR 254 0.0002

THR 254 HIS 255 -0.0004

HIS 255 ARG 256 0.0020

ARG 256 TYR 257 -0.0002

TYR 257 LYS 258 -0.0001

LYS 258 LYS 259 0.0002

LYS 259 LYS 260 0.0001

LYS 260 TYR 261 0.0015

TYR 261 VAL 262 0.0000

VAL 262 THR 263 0.0004

THR 263 THR 264 0.0000

THR 264 LEU 265 -0.0003

LEU 265 LEU 266 0.0118

LEU 266 TYR 267 -0.0004

TYR 267 LYS 268 0.0003

LYS 268 PRO 269 -0.0001

PRO 269 ILE 270 -0.0003

ILE 270 ASN 25 -0.0003

ASN 25 SER 26 0.0001

SER 26 VAL 27 0.0002

VAL 27 TYR 28 0.0000

TYR 28 THR 29 -0.0002

THR 29 SER 30 0.0071

SER 30 PHE 31 0.0001

PHE 31 MET 32 0.0002

MET 32 LYS 33 -0.0000

LYS 33 SER 34 -0.0001

SER 34 HIS 35 0.0068

HIS 35 ARG 36 -0.0002

ARG 36 CYS 37 0.0003

CYS 37 TYR 38 -0.0002

TYR 38 ASP 39 0.0002

ASP 39 LEU 40 -0.0030

LEU 40 ILE 41 0.0001

ILE 41 PRO 42 0.0000

PRO 42 THR 43 0.0001

THR 43 SER 44 -0.0003

SER 44 SER 45 0.0081

SER 45 LYS 46 0.0002

LYS 46 LEU 47 -0.0002

LEU 47 VAL 48 -0.0001

VAL 48 VAL 49 0.0003

VAL 49 PHE 50 0.0078

PHE 50 ASP 51 0.0004

ASP 51 THR 52 -0.0001

THR 52 SER 53 0.0003

SER 53 LEU 54 -0.0005

LEU 54 GLN 55 -0.0033

GLN 55 VAL 56 0.0001

VAL 56 LYS 57 0.0003

LYS 57 LYS 58 0.0000

LYS 58 ALA 59 0.0001

ALA 59 PHE 60 -0.0092

PHE 60 PHE 61 -0.0004

PHE 61 ALA 62 0.0002

ALA 62 LEU 63 -0.0001

LEU 63 VAL 64 0.0002

VAL 64 THR 65 -0.0454

THR 65 ASN 66 0.0000

ASN 66 GLY 67 -0.0001

GLY 67 VAL 68 -0.0001

VAL 68 ARG 69 0.0002

ARG 69 ALA 70 0.0197

ALA 70 ALA 71 -0.0002

ALA 71 PRO 72 0.0003

PRO 72 LEU 73 0.0003

LEU 73 TRP 74 -0.0005

TRP 74 ASP 75 0.0015

ASP 75 SER 76 -0.0002

SER 76 LYS 77 -0.0000

LYS 77 LYS 78 -0.0003

LYS 78 GLN 79 -0.0001

GLN 79 SER 80 0.0320

SER 80 PHE 81 0.0003

PHE 81 VAL 82 0.0002

VAL 82 GLY 83 -0.0001

GLY 83 MET 84 -0.0002

MET 84 LEU 85 0.0135

LEU 85 THR 86 0.0002

THR 86 ILE 87 -0.0000

ILE 87 THR 88 -0.0001

THR 88 ASP 89 -0.0000

ASP 89 PHE 90 0.0079

PHE 90 ILE 91 -0.0003

ILE 91 ASN 92 -0.0000

ASN 92 ILE 93 0.0000

ILE 93 LEU 94 0.0002

LEU 94 HIS 95 -0.0089

HIS 95 ARG 96 -0.0001

ARG 96 TYR 97 -0.0001

TYR 97 TYR 98 0.0003

TYR 98 LYS 99 0.0001

LYS 99 SER 100 0.0036

SER 100 ALA 101 -0.0002

ALA 101 LEU 102 0.0002

LEU 102 VAL 103 -0.0001

VAL 103 GLN 104 0.0002

GLN 104 ILE 105 0.0025

ILE 105 TYR 106 0.0001

TYR 106 GLU 107 -0.0000

GLU 107 LEU 108 -0.0000

LEU 108 GLU 109 0.0001

GLU 109 GLU 110 -0.0067

GLU 110 HIS 111 -0.0001

HIS 111 LYS 112 -0.0003

LYS 112 ILE 113 -0.0000

ILE 113 GLU 114 0.0001

GLU 114 THR 115 0.0128

THR 115 TRP 116 -0.0004

TRP 116 ARG 117 -0.0001

ARG 117 GLU 118 -0.0002

GLU 118 VAL 119 -0.0000

VAL 119 TYR 120 -0.0005

TYR 120 LEU 121 -0.0001

LEU 121 GLN 122 0.0000

GLN 122 ASP 123 -0.0002

ASP 123 SER 124 0.0001

SER 124 PHE 125 0.0098

PHE 125 LYS 126 0.0004

LYS 126 PRO 127 0.0000

PRO 127 LEU 128 -0.0001

LEU 128 VAL 129 0.0003

VAL 129 CYS 130 -0.0015

CYS 130 ILE 131 -0.0003

ILE 131 SER 132 -0.0002

SER 132 PRO 133 0.0003

PRO 133 ASN 134 0.0003

ASN 134 ALA 135 0.0377

ALA 135 SER 136 -0.0004

SER 136 LEU 137 -0.0000

LEU 137 PHE 138 0.0001

PHE 138 ASP 139 -0.0002

ASP 139 ALA 140 -0.0031

ALA 140 VAL 141 -0.0000

VAL 141 SER 142 -0.0002

SER 142 SER 143 0.0004

SER 143 LEU 144 0.0001

LEU 144 ILE 145 0.0010

ILE 145 ARG 146 0.0001

ARG 146 ASN 147 0.0000

ASN 147 LYS 148 -0.0002

LYS 148 ILE 149 0.0003

ILE 149 HIS 150 -0.0078

HIS 150 ARG 151 -0.0000

ARG 151 LEU 152 -0.0003

LEU 152 PRO 153 0.0001

PRO 153 VAL 154 -0.0002

VAL 154 ILE 155 0.0100

ILE 155 ASP 156 -0.0003

ASP 156 PRO 157 -0.0001

PRO 157 GLU 158 0.0003

GLU 158 SER 159 0.0003

SER 159 GLY 160 0.0015

GLY 160 ASN 161 0.0002

ASN 161 THR 162 0.0003

THR 162 LEU 163 0.0000

LEU 163 TYR 164 0.0002

TYR 164 ILE 165 -0.0069

ILE 165 LEU 166 -0.0000

LEU 166 THR 167 0.0003

THR 167 HIS 168 -0.0000

HIS 168 LYS 169 0.0004

LYS 169 ARG 170 -0.0053

ARG 170 ILE 171 -0.0002

ILE 171 LEU 172 -0.0000

LEU 172 LYS 173 -0.0004

LYS 173 PHE 174 0.0002

PHE 174 LEU 175 -0.0094

LEU 175 LYS 176 0.0000

LYS 176 LEU 177 0.0004

LEU 177 PHE 178 -0.0002

PHE 178 ILE 179 -0.0000

ILE 179 THR 180 -0.0028

THR 180 GLU 181 0.0001

GLU 181 PHE 182 0.0001

PHE 182 PRO 183 0.0001

PRO 183 LYS 184 0.0002

LYS 184 PRO 185 -0.0041

PRO 185 GLU 186 0.0002

GLU 186 PHE 187 -0.0000

PHE 187 MET 188 0.0001

MET 188 SER 189 0.0005

SER 189 LYS 190 -0.0063

LYS 190 SER 191 -0.0002

SER 191 LEU 192 0.0001

LEU 192 GLU 193 -0.0004

GLU 193 GLU 194 -0.0003

GLU 194 LEU 195 0.0033

LEU 195 GLN 196 0.0000

GLN 196 ILE 197 -0.0003

ILE 197 GLY 198 0.0001

GLY 198 THR 199 -0.0001

THR 199 TYR 200 0.0064

TYR 200 ALA 201 0.0003

ALA 201 ASN 202 -0.0004

ASN 202 ILE 203 -0.0001

ILE 203 ALA 204 -0.0000

ALA 204 MET 205 -0.0015

MET 205 VAL 206 -0.0002

VAL 206 ARG 207 -0.0001

ARG 207 THR 208 -0.0001

THR 208 THR 209 0.0003

THR 209 THR 210 0.0119

THR 210 PRO 211 -0.0002

PRO 211 VAL 212 0.0003

VAL 212 TYR 213 0.0002

TYR 213 VAL 214 -0.0001

VAL 214 ALA 215 -0.0062

ALA 215 LEU 216 0.0003

LEU 216 GLY 217 -0.0001

GLY 217 ILE 218 -0.0002

ILE 218 PHE 219 0.0001

PHE 219 VAL 220 0.0007

VAL 220 GLN 221 0.0002

GLN 221 HIS 222 0.0002

HIS 222 ARG 223 -0.0002

ARG 223 VAL 224 -0.0001

VAL 224 SER 225 -0.0106

SER 225 ALA 226 0.0001

ALA 226 LEU 227 0.0001

LEU 227 PRO 228 -0.0001

PRO 228 VAL 229 0.0001

VAL 229 VAL 230 -0.0033

VAL 230 ASP 231 -0.0001

ASP 231 GLU 232 0.0002

GLU 232 LYS 233 -0.0000

LYS 233 GLY 234 0.0001

GLY 234 ARG 235 -0.0008

ARG 235 VAL 236 -0.0003

VAL 236 VAL 237 0.0001

VAL 237 ASP 238 0.0000

ASP 238 ILE 239 0.0001

ILE 239 TYR 240 -0.0025

TYR 240 SER 241 0.0005

SER 241 LYS 242 -0.0004

LYS 242 PHE 243 0.0001

PHE 243 ASP 244 -0.0000

ASP 244 VAL 245 0.0024

VAL 245 ILE 246 -0.0002

ILE 246 ASN 247 -0.0002

ASN 247 LEU 248 0.0003

LEU 248 ALA 249 0.0001

ALA 249 ALA 250 0.0075

ALA 250 GLU 251 0.0001

GLU 251 LYS 252 0.0002

LYS 252 THR 253 -0.0001

THR 253 TYR 254 -0.0001

TYR 254 ASN 255 0.0013

ASN 255 ASN 256 0.0003

ASN 256 LEU 257 -0.0002

LEU 257 ASP 258 0.0003

ASP 258 VAL 259 -0.0000

VAL 259 SER 260 -0.0024

SER 260 VAL 261 -0.0000

VAL 261 THR 262 -0.0002

THR 262 LYS 263 0.0004

LYS 263 ALA 264 -0.0001

ALA 264 LEU 265 0.0070

LEU 265 GLN 266 -0.0001

GLN 266 HIS 267 0.0001

HIS 267 ARG 268 -0.0002

ARG 268 SER 269 0.0001

SER 269 HIS 270 0.0041

HIS 270 TYR 271 0.0002

TYR 271 PHE 272 0.0000

PHE 272 GLU 273 0.0002

GLU 273 GLY 274 0.0002

GLY 274 VAL 275 -0.0023

VAL 275 LEU 276 0.0001

LEU 276 LYS 277 -0.0003

LYS 277 CYS 278 0.0002

CYS 278 TYR 279 -0.0001

TYR 279 LEU 280 0.0052

LEU 280 HIS 281 -0.0002

HIS 281 GLU 282 0.0003

GLU 282 THR 283 0.0000

THR 283 LEU 284 -0.0001

LEU 284 GLU 285 -0.0019

GLU 285 THR 286 -0.0003

THR 286 ILE 287 -0.0003

ILE 287 ILE 288 0.0003

ILE 288 ASN 289 -0.0001

ASN 289 ARG 290 0.0046

ARG 290 LEU 291 0.0000

LEU 291 VAL 292 0.0001

VAL 292 GLU 293 0.0003

GLU 293 ALA 294 0.0002

ALA 294 GLU 295 -0.0019

GLU 295 VAL 296 -0.0005

VAL 296 HIS 297 0.0003

HIS 297 ARG 298 -0.0003

ARG 298 LEU 299 0.0005

LEU 299 VAL 300 -0.0119

VAL 300 VAL 301 0.0001

VAL 301 VAL 302 -0.0002

VAL 302 ASP 303 -0.0001

ASP 303 GLU 304 0.0003

GLU 304 ASN 305 0.0006

ASN 305 ASP 306 -0.0001

ASP 306 VAL 307 0.0000

VAL 307 VAL 308 0.0002

VAL 308 LYS 309 -0.0001

LYS 309 GLY 310 0.0077

GLY 310 ILE 311 -0.0002

ILE 311 VAL 312 0.0001

VAL 312 SER 313 0.0002

SER 313 LEU 314 0.0000

LEU 314 SER 315 -0.0010

SER 315 ASP 316 0.0001

ASP 316 ILE 317 -0.0000

ILE 317 LEU 318 -0.0001

LEU 318 GLN 319 -0.0001

GLN 319 ALA 320 -0.0099

ALA 320 LEU 321 0.0001

LEU 321 VAL 322 0.0000

VAL 322 LEU 323 0.0006

LEU 323 THR 324 -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).
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.

*** Holo AMPK ***

CA strain for 260711185133617066

--- 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.

* Holo AMPK *