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* Holo AMPK *

CA strain for 260711185133617066

--- normal mode 7 ---

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 0.0000

SER 12 VAL 13 -0.0001

VAL 13 LYS 14 -0.0003

LYS 14 ILE 15 0.0002

ILE 15 GLY 16 -0.0020

GLY 16 HIS 17 0.0002

HIS 17 TYR 18 0.0002

TYR 18 ILE 19 0.0003

ILE 19 LEU 20 -0.0000

LEU 20 GLY 21 -0.0003

GLY 21 ASP 22 0.0003

ASP 22 THR 23 -0.0002

THR 23 LEU 24 -0.0001

LEU 24 GLY 25 -0.0003

GLY 25 VAL 26 0.0117

VAL 26 GLY 27 -0.0002

GLY 27 THR 28 -0.0003

THR 28 PHE 29 -0.0004

PHE 29 GLY 30 -0.0001

GLY 30 LYS 31 0.0023

LYS 31 VAL 32 0.0000

VAL 32 LYS 33 -0.0001

LYS 33 VAL 34 0.0000

VAL 34 GLY 35 0.0000

GLY 35 LYS 36 -0.0013

LYS 36 HIS 37 0.0001

HIS 37 GLU 38 -0.0002

GLU 38 LEU 39 -0.0001

LEU 39 THR 40 0.0002

THR 40 GLY 41 -0.0062

GLY 41 HIS 42 -0.0004

HIS 42 LYS 43 0.0002

LYS 43 VAL 44 0.0001

VAL 44 ALA 45 0.0002

ALA 45 VAL 46 0.0065

VAL 46 LYS 47 -0.0003

LYS 47 ILE 48 -0.0003

ILE 48 LEU 49 -0.0002

LEU 49 ASN 50 0.0002

ASN 50 ARG 51 0.0018

ARG 51 GLN 52 -0.0003

GLN 52 LYS 53 0.0002

LYS 53 ILE 54 0.0001

ILE 54 ARG 55 -0.0004

ARG 55 SER 56 -0.0020

SER 56 LEU 57 -0.0001

LEU 57 ASP 58 -0.0003

ASP 58 VAL 59 -0.0001

VAL 59 VAL 60 -0.0000

VAL 60 GLY 61 0.0010

GLY 61 LYS 62 0.0000

LYS 62 ILE 63 0.0001

ILE 63 ARG 64 -0.0000

ARG 64 ARG 65 0.0002

ARG 65 GLU 66 -0.0011

GLU 66 ILE 67 -0.0002

ILE 67 GLN 68 -0.0003

GLN 68 ASN 69 0.0001

ASN 69 LEU 70 -0.0003

LEU 70 LYS 71 -0.0138

LYS 71 LEU 72 0.0000

LEU 72 PHE 73 -0.0003

PHE 73 ARG 74 0.0003

ARG 74 HIS 75 0.0000

HIS 75 PRO 76 0.0016

PRO 76 HIS 77 0.0000

HIS 77 ILE 78 -0.0002

ILE 78 ILE 79 -0.0002

ILE 79 LYS 80 -0.0000

LYS 80 LEU 81 0.0299

LEU 81 TYR 82 0.0003

TYR 82 GLN 83 -0.0002

GLN 83 VAL 84 -0.0002

VAL 84 ILE 85 0.0000

ILE 85 SER 86 0.0098

SER 86 THR 87 0.0001

THR 87 PRO 88 -0.0000

PRO 88 SER 89 -0.0000

SER 89 ASP 90 -0.0001

ASP 90 ILE 91 0.0004

ILE 91 PHE 92 0.0001

PHE 92 MET 93 -0.0000

MET 93 VAL 94 -0.0002

VAL 94 MET 95 0.0001

MET 95 GLU 96 0.0074

GLU 96 TYR 97 -0.0004

TYR 97 VAL 98 -0.0002

VAL 98 SER 99 -0.0001

SER 99 GLY 100 0.0000

GLY 100 GLY 101 0.0105

GLY 101 GLU 102 -0.0003

GLU 102 LEU 103 -0.0003

LEU 103 PHE 104 -0.0002

PHE 104 ASP 105 -0.0001

ASP 105 TYR 106 0.0016

TYR 106 ILE 107 0.0000

ILE 107 CYS 108 0.0001

CYS 108 LYS 109 0.0005

LYS 109 ASN 110 -0.0000

ASN 110 GLY 111 -0.0024

GLY 111 ARG 112 -0.0000

ARG 112 LEU 113 0.0005

LEU 113 ASP 114 0.0000

ASP 114 GLU 115 -0.0001

GLU 115 LYS 116 0.0009

LYS 116 GLU 117 0.0001

GLU 117 SER 118 0.0003

SER 118 ARG 119 0.0004

ARG 119 ARG 120 0.0001

ARG 120 LEU 121 -0.0007

LEU 121 PHE 122 0.0000

PHE 122 GLN 123 -0.0005

GLN 123 GLN 124 0.0000

GLN 124 ILE 125 -0.0003

ILE 125 LEU 126 0.0001

LEU 126 SER 127 0.0001

SER 127 GLY 128 0.0000

GLY 128 VAL 129 -0.0003

VAL 129 ASP 130 0.0000

ASP 130 TYR 131 0.0049

TYR 131 CYS 132 -0.0001

CYS 132 HIS 133 0.0004

HIS 133 ARG 134 -0.0003

ARG 134 HIS 135 -0.0002

HIS 135 MET 136 0.0015

MET 136 VAL 137 -0.0000

VAL 137 VAL 138 0.0003

VAL 138 HIS 139 0.0001

HIS 139 ARG 140 -0.0005

ARG 140 ASP 141 0.0069

ASP 141 LEU 142 -0.0000

LEU 142 LYS 143 -0.0001

LYS 143 PRO 144 -0.0002

PRO 144 GLU 145 0.0003

GLU 145 ASN 146 -0.0074

ASN 146 VAL 147 -0.0001

VAL 147 LEU 148 -0.0002

LEU 148 LEU 149 0.0001

LEU 149 ASP 150 0.0004

ASP 150 ALA 151 -0.0022

ALA 151 HIS 152 -0.0004

HIS 152 MET 153 0.0003

MET 153 ASN 154 0.0000

ASN 154 ALA 155 0.0001

ALA 155 LYS 156 0.0009

LYS 156 ILE 157 0.0004

ILE 157 ALA 158 -0.0001

ALA 158 ASP 159 0.0001

ASP 159 PHE 160 -0.0000

PHE 160 GLY 161 -0.0142

GLY 161 LEU 162 0.0000

LEU 162 SER 163 0.0002

SER 163 ASN 164 -0.0002

ASN 164 MET 165 0.0003

MET 165 MET 166 0.0488

MET 166 SER 167 0.0004

SER 167 ASP 168 -0.0002

ASP 168 GLY 169 -0.0001

GLY 169 GLU 170 0.0001

GLU 170 PHE 171 0.0290

PHE 171 LEU 172 -0.0000

LEU 172 ARG 173 -0.0000

ARG 173 SER 175 -0.0068

SER 175 CYS 176 -0.0002

CYS 176 GLY 177 0.0002

GLY 177 SER 178 -0.0004

SER 178 PRO 179 -0.0002

PRO 179 ASN 180 0.0054

ASN 180 TYR 181 0.0001

TYR 181 ALA 182 -0.0001

ALA 182 ALA 183 0.0002

ALA 183 PRO 184 0.0001

PRO 184 GLU 185 0.0053

GLU 185 VAL 186 0.0001

VAL 186 ILE 187 -0.0001

ILE 187 SER 188 0.0001

SER 188 GLY 189 -0.0000

GLY 189 ARG 190 -0.0149

ARG 190 LEU 191 -0.0002

LEU 191 TYR 192 0.0003

TYR 192 ALA 193 -0.0001

ALA 193 GLY 194 -0.0002

GLY 194 PRO 195 -0.0205

PRO 195 GLU 196 -0.0001

GLU 196 VAL 197 -0.0000

VAL 197 ASP 198 -0.0002

ASP 198 ILE 199 0.0003

ILE 199 TRP 200 0.0019

TRP 200 SER 201 -0.0004

SER 201 SER 202 0.0003

SER 202 GLY 203 0.0002

GLY 203 VAL 204 -0.0002

VAL 204 ILE 205 -0.0016

ILE 205 LEU 206 0.0000

LEU 206 TYR 207 0.0000

TYR 207 ALA 208 -0.0001

ALA 208 LEU 209 -0.0002

LEU 209 LEU 210 0.0002

LEU 210 CYS 211 -0.0004

CYS 211 GLY 212 0.0002

GLY 212 THR 213 0.0000

THR 213 LEU 214 -0.0004

LEU 214 PRO 215 -0.0041

PRO 215 PHE 216 0.0002

PHE 216 ASP 217 -0.0002

ASP 217 ASP 218 -0.0000

ASP 218 ASP 219 -0.0001

ASP 219 HIS 220 -0.0005

HIS 220 VAL 221 0.0003

VAL 221 PRO 222 0.0004

PRO 222 THR 223 -0.0000

THR 223 LEU 224 -0.0000

LEU 224 PHE 225 -0.0003

PHE 225 LYS 226 0.0001

LYS 226 LYS 227 -0.0002

LYS 227 ILE 228 -0.0003

ILE 228 CYS 229 0.0002

CYS 229 ASP 230 0.0050

ASP 230 GLY 231 0.0002

GLY 231 ILE 232 0.0004

ILE 232 PHE 233 0.0000

PHE 233 TYR 234 -0.0000

TYR 234 THR 235 0.0036

THR 235 PRO 236 -0.0002

PRO 236 GLN 237 0.0003

GLN 237 TYR 238 -0.0002

TYR 238 LEU 239 0.0001

LEU 239 ASN 240 -0.0007

ASN 240 PRO 241 0.0002

PRO 241 SER 242 0.0005

SER 242 VAL 243 -0.0001

VAL 243 ILE 244 -0.0001

ILE 244 SER 245 0.0017

SER 245 LEU 246 -0.0002

LEU 246 LEU 247 -0.0004

LEU 247 LYS 248 0.0002

LYS 248 HIS 249 0.0001

HIS 249 MET 250 -0.0053

MET 250 LEU 251 -0.0001

LEU 251 GLN 252 0.0002

GLN 252 VAL 253 0.0001

VAL 253 ASP 254 -0.0002

ASP 254 PRO 255 -0.0159

PRO 255 MET 256 -0.0001

MET 256 LYS 257 0.0000

LYS 257 ARG 258 0.0001

ARG 258 ALA 259 -0.0002

ALA 259 THR 260 0.0034

THR 260 ILE 261 -0.0004

ILE 261 LYS 262 0.0003

LYS 262 ASP 263 0.0001

ASP 263 ILE 264 -0.0002

ILE 264 ARG 265 0.0077

ARG 265 GLU 266 -0.0001

GLU 266 HIS 267 -0.0001

HIS 267 GLU 268 0.0001

GLU 268 TRP 269 -0.0000

TRP 269 PHE 270 0.0015

PHE 270 LYS 271 0.0002

LYS 271 GLN 272 -0.0001

GLN 272 ASP 273 0.0002

ASP 273 LEU 274 0.0000

LEU 274 PRO 275 0.0087

PRO 275 LYS 276 0.0001

LYS 276 TYR 277 -0.0004

TYR 277 LEU 278 -0.0001

LEU 278 PHE 279 0.0000

PHE 279 PRO 280 -0.0027

PRO 280 GLU 281 0.0001

GLU 281 ASP 282 -0.0001

ASP 282 LYS 395 0.0594

LYS 395 ALA 396 -0.0003

ALA 396 LYS 397 0.0003

LYS 397 TRP 398 -0.0001

TRP 398 HIS 399 0.0002

HIS 399 LEU 400 -0.0131

LEU 400 GLY 401 0.0002

GLY 401 ILE 402 -0.0001

ILE 402 ARG 403 -0.0002

ARG 403 SER 404 0.0002

SER 404 GLN 405 -0.0031

GLN 405 SER 406 0.0001

SER 406 ARG 407 -0.0000

ARG 407 PRO 408 0.0004

PRO 408 ASN 409 0.0001

ASN 409 ASP 410 -0.0017

ASP 410 ILE 411 -0.0001

ILE 411 MET 412 0.0001

MET 412 ALA 413 -0.0003

ALA 413 GLU 414 -0.0000

GLU 414 VAL 415 0.0008

VAL 415 CYS 416 -0.0003

CYS 416 ARG 417 -0.0002

ARG 417 ALA 418 0.0002

ALA 418 ILE 419 -0.0000

ILE 419 LYS 420 -0.0010

LYS 420 GLN 421 -0.0001

GLN 421 LEU 422 0.0004

LEU 422 ASP 423 -0.0001

ASP 423 TYR 424 0.0002

TYR 424 GLU 425 0.0006

GLU 425 TRP 426 0.0001

TRP 426 LYS 427 0.0001

LYS 427 VAL 428 0.0002

VAL 428 VAL 429 -0.0002

VAL 429 ASN 430 0.0076

ASN 430 PRO 431 -0.0001

PRO 431 TYR 432 -0.0001

TYR 432 TYR 433 -0.0002

TYR 433 LEU 434 -0.0001

LEU 434 ARG 435 0.0103

ARG 435 VAL 436 -0.0003

VAL 436 ARG 437 -0.0001

ARG 437 ARG 438 -0.0001

ARG 438 LYS 439 -0.0000

LYS 439 ASN 440 0.0046

ASN 440 PRO 441 0.0002

PRO 441 VAL 442 -0.0002

VAL 442 THR 443 0.0002

THR 443 SER 444 0.0003

SER 444 THR 445 0.0013

THR 445 TYR 446 -0.0003

TYR 446 SER 447 0.0004

SER 447 LYS 448 -0.0001

LYS 448 MET 449 0.0004

MET 449 SER 450 0.0089

SER 450 LEU 451 -0.0002

LEU 451 GLN 452 -0.0003

GLN 452 LEU 453 -0.0000

LEU 453 TYR 454 -0.0001

TYR 454 GLN 455 0.0039

GLN 455 VAL 456 0.0001

VAL 456 ASP 457 0.0001

ASP 457 SER 458 0.0002

SER 458 ARG 459 0.0002

ARG 459 THR 460 -0.0015

THR 460 TYR 461 0.0000

TYR 461 LEU 462 -0.0001

LEU 462 LEU 463 0.0001

LEU 463 ASP 464 -0.0000

ASP 464 PHE 465 0.0041

PHE 465 ARG 466 0.0002

ARG 466 SER 467 -0.0003

SER 467 ILE 468 -0.0001

ILE 468 ASP 469 0.0005

ASP 469 ASP 470 -0.0040

ASP 470 GLU 471 0.0002

GLU 471 LEU 526 0.0001

LEU 526 THR 527 0.0000

THR 527 PRO 528 0.0002

PRO 528 ARG 529 -0.0002

ARG 529 PRO 530 0.0001

PRO 530 GLY 531 -0.0010

GLY 531 SER 532 0.0003

SER 532 HIS 533 -0.0003

HIS 533 THR 534 -0.0003

THR 534 ILE 535 0.0000

ILE 535 GLU 536 0.0013

GLU 536 PHE 537 0.0001

PHE 537 PHE 538 0.0000

PHE 538 GLU 539 -0.0000

GLU 539 MET 540 -0.0002

MET 540 CYS 541 -0.0002

CYS 541 ALA 542 0.0001

ALA 542 ASN 543 -0.0003

ASN 543 LEU 544 0.0003

LEU 544 ILE 545 0.0001

ILE 545 LYS 546 0.0021

LYS 546 ILE 547 0.0003

ILE 547 LEU 548 -0.0002

LEU 548 ALA 549 -0.0001

ALA 549 PRO 74 -0.0018

PRO 74 ALA 75 0.0002

ALA 75 GLN 76 0.0002

GLN 76 ALA 77 0.0000

ALA 77 ARG 78 0.0003

ARG 78 PRO 79 0.0022

PRO 79 THR 80 -0.0001

THR 80 VAL 81 -0.0001

VAL 81 PHE 82 -0.0001

PHE 82 ARG 83 0.0002

ARG 83 TRP 84 0.0030

TRP 84 THR 85 0.0003

THR 85 GLY 86 -0.0003

GLY 86 GLY 87 0.0002

GLY 87 GLY 88 -0.0003

GLY 88 LYS 89 0.0012

LYS 89 GLU 90 0.0001

GLU 90 VAL 91 0.0000

VAL 91 TYR 92 -0.0002

TYR 92 LEU 93 -0.0001

LEU 93 SER 94 -0.0010

SER 94 GLY 95 0.0002

GLY 95 SER 96 -0.0000

SER 96 PHE 97 -0.0002

PHE 97 ASN 98 0.0000

ASN 98 ASN 99 0.0002

ASN 99 TRP 100 -0.0003

TRP 100 SER 101 0.0001

SER 101 LYS 102 0.0001

LYS 102 LEU 103 -0.0001

LEU 103 PRO 104 -0.0035

PRO 104 LEU 105 0.0002

LEU 105 THR 106 -0.0001

THR 106 ARG 107 0.0004

ARG 107 ASP 108 -0.0000

ASP 108 HIS 109 -0.0008

HIS 109 ASN 110 -0.0000

ASN 110 ASN 111 -0.0002

ASN 111 PHE 112 0.0002

PHE 112 VAL 113 -0.0001

VAL 113 ALA 114 0.0017

ALA 114 ILE 115 -0.0001

ILE 115 LEU 116 -0.0002

LEU 116 ASP 117 0.0000

ASP 117 LEU 118 0.0002

LEU 118 PRO 119 -0.0023

PRO 119 GLU 120 0.0002

GLU 120 GLY 121 -0.0002

GLY 121 GLU 122 -0.0000

GLU 122 HIS 123 0.0002

HIS 123 GLN 124 0.0018

GLN 124 TYR 125 0.0003

TYR 125 LYS 126 -0.0003

LYS 126 PHE 127 0.0001

PHE 127 PHE 128 -0.0001

PHE 128 VAL 129 0.0004

VAL 129 ASP 130 -0.0003

ASP 130 GLY 131 -0.0000

GLY 131 GLN 132 -0.0003

GLN 132 TRP 133 0.0004

TRP 133 THR 134 0.0012

THR 134 HIS 135 0.0003

HIS 135 ASP 136 -0.0002

ASP 136 PRO 137 0.0002

PRO 137 SER 138 -0.0002

SER 138 GLU 139 0.0012

GLU 139 PRO 140 0.0000

PRO 140 ILE 141 0.0000

ILE 141 VAL 142 -0.0003

VAL 142 THR 143 -0.0001

THR 143 SER 144 -0.0015

SER 144 GLN 145 0.0003

GLN 145 LEU 146 0.0001

LEU 146 GLY 147 0.0003

GLY 147 THR 148 0.0004

THR 148 VAL 149 -0.0026

VAL 149 ASN 150 0.0002

ASN 150 ASN 151 0.0003

ASN 151 ILE 152 0.0002

ILE 152 ILE 153 -0.0001

ILE 153 GLN 154 0.0063

GLN 154 VAL 155 -0.0002

VAL 155 LYS 156 -0.0000

LYS 156 LYS 157 -0.0001

LYS 157 THR 158 0.0002

THR 158 ASP 159 -0.0002

ASP 159 PHE 160 0.0004

PHE 160 GLU 161 -0.0001

GLU 161 VAL 162 -0.0001

VAL 162 PHE 163 -0.0004

PHE 163 ASP 164 0.0059

ASP 164 ALA 165 -0.0001

ALA 165 LEU 166 0.0000

LEU 166 MET 167 -0.0001

MET 167 VAL 168 -0.0000

VAL 168 ASP 169 -0.0018

ASP 169 SER 170 -0.0003

SER 170 GLN 171 0.0002

GLN 171 HIS 188 -0.1166

HIS 188 GLN 189 -0.0002

GLN 189 GLU 190 0.0002

GLU 190 PRO 191 -0.0000

PRO 191 TYR 192 -0.0000

TYR 192 VAL 193 0.0010

VAL 193 CYS 194 0.0001

CYS 194 LYS 195 -0.0004

LYS 195 ARG 201 0.0035

ARG 201 ALA 202 -0.0004

ALA 202 PRO 203 0.0001

PRO 203 PRO 204 0.0001

PRO 204 ILE 205 0.0000

ILE 205 LEU 206 -0.0035

LEU 206 PRO 207 0.0003

PRO 207 PRO 208 0.0002

PRO 208 HIS 209 -0.0003

HIS 209 LEU 210 0.0003

LEU 210 LEU 211 0.0099

LEU 211 GLN 212 -0.0001

GLN 212 VAL 213 -0.0003

VAL 213 ILE 214 0.0004

ILE 214 LEU 215 -0.0001

LEU 215 ASN 216 0.0091

ASN 216 LYS 217 -0.0002

LYS 217 ASP 218 -0.0001

ASP 218 THR 219 0.0001

THR 219 GLY 220 -0.0003

GLY 220 ILE 221 0.0085

ILE 221 SER 222 -0.0000

SER 222 CYS 223 0.0002

CYS 223 ASP 224 0.0001

ASP 224 PRO 225 -0.0004

PRO 225 ALA 226 0.0014

ALA 226 LEU 227 0.0002

LEU 227 LEU 228 0.0000

LEU 228 PRO 229 -0.0000

PRO 229 GLU 230 0.0001

GLU 230 PRO 231 0.0052

PRO 231 ASN 232 -0.0001

ASN 232 HIS 233 -0.0003

HIS 233 VAL 234 0.0000

VAL 234 MET 235 0.0000

MET 235 LEU 236 -0.0033

LEU 236 ASN 237 -0.0002

ASN 237 HIS 238 0.0003

HIS 238 LEU 239 -0.0001

LEU 239 TYR 240 -0.0000

TYR 240 ALA 241 0.0022

ALA 241 LEU 242 0.0002

LEU 242 SER 243 -0.0001

SER 243 ILE 244 0.0005

ILE 244 LYS 245 0.0002

LYS 245 ASP 246 -0.0040

ASP 246 GLY 247 0.0002

GLY 247 VAL 248 0.0002

VAL 248 MET 249 -0.0003

MET 249 VAL 250 -0.0003

VAL 250 LEU 251 0.0033

LEU 251 SER 252 -0.0001

SER 252 ALA 253 0.0001

ALA 253 THR 254 0.0003

THR 254 HIS 255 -0.0002

HIS 255 ARG 256 0.0042

ARG 256 TYR 257 0.0005

TYR 257 LYS 258 -0.0002

LYS 258 LYS 259 0.0003

LYS 259 LYS 260 0.0001

LYS 260 TYR 261 -0.0053

TYR 261 VAL 262 0.0000

VAL 262 THR 263 0.0003

THR 263 THR 264 0.0000

THR 264 LEU 265 0.0003

LEU 265 LEU 266 0.0046

LEU 266 TYR 267 0.0002

TYR 267 LYS 268 -0.0001

LYS 268 PRO 269 -0.0003

PRO 269 ILE 270 0.0002

ILE 270 ASN 25 -0.0004

ASN 25 SER 26 -0.0004

SER 26 VAL 27 0.0003

VAL 27 TYR 28 -0.0000

TYR 28 THR 29 -0.0001

THR 29 SER 30 0.0012

SER 30 PHE 31 0.0001

PHE 31 MET 32 -0.0001

MET 32 LYS 33 0.0001

LYS 33 SER 34 -0.0004

SER 34 HIS 35 0.0008

HIS 35 ARG 36 -0.0002

ARG 36 CYS 37 -0.0002

CYS 37 TYR 38 -0.0002

TYR 38 ASP 39 0.0002

ASP 39 LEU 40 -0.0032

LEU 40 ILE 41 -0.0001

ILE 41 PRO 42 -0.0001

PRO 42 THR 43 -0.0003

THR 43 SER 44 0.0002

SER 44 SER 45 0.0064

SER 45 LYS 46 -0.0003

LYS 46 LEU 47 -0.0002

LEU 47 VAL 48 0.0004

VAL 48 VAL 49 0.0003

VAL 49 PHE 50 0.0023

PHE 50 ASP 51 0.0002

ASP 51 THR 52 0.0003

THR 52 SER 53 0.0003

SER 53 LEU 54 -0.0001

LEU 54 GLN 55 -0.0031

GLN 55 VAL 56 -0.0001

VAL 56 LYS 57 0.0002

LYS 57 LYS 58 -0.0002

LYS 58 ALA 59 0.0002

ALA 59 PHE 60 -0.0045

PHE 60 PHE 61 -0.0001

PHE 61 ALA 62 0.0001

ALA 62 LEU 63 0.0001

LEU 63 VAL 64 -0.0003

VAL 64 THR 65 0.0005

THR 65 ASN 66 0.0000

ASN 66 GLY 67 -0.0001

GLY 67 VAL 68 0.0001

VAL 68 ARG 69 0.0004

ARG 69 ALA 70 0.0047

ALA 70 ALA 71 0.0003

ALA 71 PRO 72 -0.0005

PRO 72 LEU 73 0.0001

LEU 73 TRP 74 0.0002

TRP 74 ASP 75 0.0007

ASP 75 SER 76 -0.0004

SER 76 LYS 77 -0.0004

LYS 77 LYS 78 -0.0002

LYS 78 GLN 79 -0.0002

GLN 79 SER 80 0.0067

SER 80 PHE 81 -0.0000

PHE 81 VAL 82 -0.0002

VAL 82 GLY 83 -0.0002

GLY 83 MET 84 0.0001

MET 84 LEU 85 0.0034

LEU 85 THR 86 0.0000

THR 86 ILE 87 0.0000

ILE 87 THR 88 -0.0001

THR 88 ASP 89 -0.0002

ASP 89 PHE 90 0.0017

PHE 90 ILE 91 0.0001

ILE 91 ASN 92 -0.0003

ASN 92 ILE 93 -0.0001

ILE 93 LEU 94 0.0002

LEU 94 HIS 95 -0.0009

HIS 95 ARG 96 -0.0001

ARG 96 TYR 97 -0.0004

TYR 97 TYR 98 0.0005

TYR 98 LYS 99 0.0001

LYS 99 SER 100 0.0008

SER 100 ALA 101 -0.0002

ALA 101 LEU 102 0.0002

LEU 102 VAL 103 0.0001

VAL 103 GLN 104 -0.0003

GLN 104 ILE 105 0.0003

ILE 105 TYR 106 -0.0003

TYR 106 GLU 107 -0.0001

GLU 107 LEU 108 0.0000

LEU 108 GLU 109 -0.0001

GLU 109 GLU 110 -0.0021

GLU 110 HIS 111 0.0003

HIS 111 LYS 112 -0.0001

LYS 112 ILE 113 0.0000

ILE 113 GLU 114 0.0001

GLU 114 THR 115 0.0014

THR 115 TRP 116 0.0001

TRP 116 ARG 117 -0.0004

ARG 117 GLU 118 0.0002

GLU 118 VAL 119 0.0003

VAL 119 TYR 120 0.0004

TYR 120 LEU 121 0.0002

LEU 121 GLN 122 -0.0004

GLN 122 ASP 123 0.0001

ASP 123 SER 124 0.0001

SER 124 PHE 125 0.0013

PHE 125 LYS 126 0.0003

LYS 126 PRO 127 -0.0003

PRO 127 LEU 128 -0.0000

LEU 128 VAL 129 -0.0002

VAL 129 CYS 130 0.0002

CYS 130 ILE 131 0.0004

ILE 131 SER 132 -0.0001

SER 132 PRO 133 0.0000

PRO 133 ASN 134 0.0001

ASN 134 ALA 135 0.0070

ALA 135 SER 136 0.0005

SER 136 LEU 137 0.0001

LEU 137 PHE 138 0.0003

PHE 138 ASP 139 0.0003

ASP 139 ALA 140 -0.0007

ALA 140 VAL 141 0.0001

VAL 141 SER 142 0.0002

SER 142 SER 143 -0.0000

SER 143 LEU 144 0.0004

LEU 144 ILE 145 0.0007

ILE 145 ARG 146 -0.0000

ARG 146 ASN 147 -0.0001

ASN 147 LYS 148 -0.0001

LYS 148 ILE 149 -0.0002

ILE 149 HIS 150 -0.0009

HIS 150 ARG 151 -0.0006

ARG 151 LEU 152 0.0003

LEU 152 PRO 153 0.0002

PRO 153 VAL 154 -0.0003

VAL 154 ILE 155 0.0073

ILE 155 ASP 156 -0.0001

ASP 156 PRO 157 0.0001

PRO 157 GLU 158 -0.0002

GLU 158 SER 159 -0.0000

SER 159 GLY 160 -0.0016

GLY 160 ASN 161 0.0002

ASN 161 THR 162 0.0000

THR 162 LEU 163 -0.0001

LEU 163 TYR 164 -0.0002

TYR 164 ILE 165 0.0042

ILE 165 LEU 166 -0.0001

LEU 166 THR 167 0.0000

THR 167 HIS 168 -0.0000

HIS 168 LYS 169 0.0004

LYS 169 ARG 170 0.0031

ARG 170 ILE 171 0.0001

ILE 171 LEU 172 0.0001

LEU 172 LYS 173 0.0004

LYS 173 PHE 174 0.0002

PHE 174 LEU 175 -0.0020

LEU 175 LYS 176 -0.0001

LYS 176 LEU 177 0.0002

LEU 177 PHE 178 0.0001

PHE 178 ILE 179 -0.0003

ILE 179 THR 180 0.0008

THR 180 GLU 181 -0.0001

GLU 181 PHE 182 0.0001

PHE 182 PRO 183 -0.0002

PRO 183 LYS 184 0.0003

LYS 184 PRO 185 -0.0005

PRO 185 GLU 186 -0.0003

GLU 186 PHE 187 -0.0001

PHE 187 MET 188 -0.0005

MET 188 SER 189 -0.0001

SER 189 LYS 190 -0.0010

LYS 190 SER 191 0.0000

SER 191 LEU 192 -0.0001

LEU 192 GLU 193 -0.0005

GLU 193 GLU 194 -0.0002

GLU 194 LEU 195 0.0006

LEU 195 GLN 196 -0.0001

GLN 196 ILE 197 -0.0003

ILE 197 GLY 198 0.0001

GLY 198 THR 199 -0.0005

THR 199 TYR 200 0.0013

TYR 200 ALA 201 0.0003

ALA 201 ASN 202 0.0002

ASN 202 ILE 203 0.0000

ILE 203 ALA 204 0.0001

ALA 204 MET 205 -0.0004

MET 205 VAL 206 -0.0000

VAL 206 ARG 207 -0.0001

ARG 207 THR 208 -0.0001

THR 208 THR 209 -0.0001

THR 209 THR 210 0.0010

THR 210 PRO 211 -0.0002

PRO 211 VAL 212 -0.0000

VAL 212 TYR 213 0.0005

TYR 213 VAL 214 -0.0000

VAL 214 ALA 215 -0.0001

ALA 215 LEU 216 0.0001

LEU 216 GLY 217 -0.0002

GLY 217 ILE 218 0.0001

ILE 218 PHE 219 -0.0001

PHE 219 VAL 220 -0.0001

VAL 220 GLN 221 0.0002

GLN 221 HIS 222 -0.0003

HIS 222 ARG 223 0.0003

ARG 223 VAL 224 0.0001

VAL 224 SER 225 -0.0009

SER 225 ALA 226 -0.0001

ALA 226 LEU 227 0.0000

LEU 227 PRO 228 0.0001

PRO 228 VAL 229 -0.0002

VAL 229 VAL 230 0.0001

VAL 230 ASP 231 0.0002

ASP 231 GLU 232 0.0001

GLU 232 LYS 233 -0.0001

LYS 233 GLY 234 0.0000

GLY 234 ARG 235 0.0003

ARG 235 VAL 236 0.0002

VAL 236 VAL 237 -0.0000

VAL 237 ASP 238 0.0000

ASP 238 ILE 239 -0.0001

ILE 239 TYR 240 -0.0026

TYR 240 SER 241 -0.0003

SER 241 LYS 242 0.0005

LYS 242 PHE 243 0.0000

PHE 243 ASP 244 0.0002

ASP 244 VAL 245 -0.0009

VAL 245 ILE 246 0.0003

ILE 246 ASN 247 -0.0001

ASN 247 LEU 248 0.0001

LEU 248 ALA 249 0.0003

ALA 249 ALA 250 0.0001

ALA 250 GLU 251 -0.0002

GLU 251 LYS 252 -0.0003

LYS 252 THR 253 -0.0002

THR 253 TYR 254 -0.0001

TYR 254 ASN 255 0.0009

ASN 255 ASN 256 0.0002

ASN 256 LEU 257 -0.0002

LEU 257 ASP 258 0.0002

ASP 258 VAL 259 0.0002

VAL 259 SER 260 -0.0014

SER 260 VAL 261 -0.0000

VAL 261 THR 262 0.0005

THR 262 LYS 263 0.0000

LYS 263 ALA 264 -0.0001

ALA 264 LEU 265 0.0000

LEU 265 GLN 266 0.0003

GLN 266 HIS 267 0.0001

HIS 267 ARG 268 -0.0001

ARG 268 SER 269 0.0002

SER 269 HIS 270 0.0013

HIS 270 TYR 271 -0.0001

TYR 271 PHE 272 0.0002

PHE 272 GLU 273 -0.0001

GLU 273 GLY 274 0.0001

GLY 274 VAL 275 -0.0004

VAL 275 LEU 276 0.0000

LEU 276 LYS 277 0.0001

LYS 277 CYS 278 -0.0004

CYS 278 TYR 279 -0.0000

TYR 279 LEU 280 -0.0004

LEU 280 HIS 281 -0.0003

HIS 281 GLU 282 0.0003

GLU 282 THR 283 -0.0000

THR 283 LEU 284 0.0001

LEU 284 GLU 285 -0.0001

GLU 285 THR 286 0.0004

THR 286 ILE 287 0.0006

ILE 287 ILE 288 0.0001

ILE 288 ASN 289 0.0002

ASN 289 ARG 290 0.0002

ARG 290 LEU 291 0.0001

LEU 291 VAL 292 0.0000

VAL 292 GLU 293 -0.0001

GLU 293 ALA 294 0.0003

ALA 294 GLU 295 -0.0012

GLU 295 VAL 296 -0.0003

VAL 296 HIS 297 -0.0004

HIS 297 ARG 298 0.0002

ARG 298 LEU 299 -0.0004

LEU 299 VAL 300 0.0008

VAL 300 VAL 301 0.0000

VAL 301 VAL 302 0.0000

VAL 302 ASP 303 -0.0002

ASP 303 GLU 304 -0.0000

GLU 304 ASN 305 0.0003

ASN 305 ASP 306 -0.0002

ASP 306 VAL 307 0.0001

VAL 307 VAL 308 -0.0004

VAL 308 LYS 309 0.0003

LYS 309 GLY 310 0.0014

GLY 310 ILE 311 0.0003

ILE 311 VAL 312 0.0001

VAL 312 SER 313 0.0001

SER 313 LEU 314 -0.0001

LEU 314 SER 315 -0.0004

SER 315 ASP 316 0.0001

ASP 316 ILE 317 -0.0002

ILE 317 LEU 318 -0.0001

LEU 318 GLN 319 -0.0001

GLN 319 ALA 320 -0.0016

ALA 320 LEU 321 0.0002

LEU 321 VAL 322 -0.0000

VAL 322 LEU 323 0.0001

LEU 323 THR 324 -0.0000

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 7 ---

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 *