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

* EXP_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *

CA strain for 24021912332929451

--- 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
PRO 1 LEU 2 0.0003

LEU 2 ILE 3 -0.0960

ILE 3 ASN 4 -0.0001

ASN 4 SER 5 -0.0616

SER 5 ARG 6 -0.0001

ARG 6 THR 7 0.0361

THR 7 GLY 8 -0.0000

GLY 8 SER 9 -0.0074

SER 9 ILE 10 -0.0004

ILE 10 TYR 11 -0.0667

TYR 11 ILE 12 -0.0002

ILE 12 VAL 13 -0.1715

VAL 13 LYS 14 -0.0001

LYS 14 PRO 15 -0.2209

PRO 15 LYS 16 -0.0002

LYS 16 MET 17 -0.0088

MET 17 HIS 18 -0.0002

HIS 18 GLY 19 0.0096

GLY 19 PRO 20 0.0001

PRO 20 ALA 21 -0.0212

ALA 21 GLU 22 0.0001

GLU 22 VAL 23 -0.0065

VAL 23 ALA 24 -0.0005

ALA 24 PHE 25 -0.0127

PHE 25 THR 26 -0.0003

THR 26 CYS 27 0.0031

CYS 27 GLU 28 0.0001

GLU 28 LEU 29 0.0207

LEU 29 PHE 30 -0.0001

PHE 30 SER 31 -0.0063

SER 31 ARG 32 0.0004

ARG 32 VAL 33 -0.0052

VAL 33 GLU 34 0.0000

GLU 34 ASP 35 0.0038

ASP 35 VAL 36 0.0001

VAL 36 LEU 37 -0.0026

LEU 37 GLY 38 0.0004

GLY 38 LEU 39 -0.0030

LEU 39 PRO 40 0.0001

PRO 40 GLN 41 0.0097

GLN 41 ASN 42 0.0002

ASN 42 THR 43 -0.0031

THR 43 MET 44 0.0001

MET 44 LYS 45 0.0201

LYS 45 ILE 46 0.0001

ILE 46 GLY 47 0.0008

GLY 47 ILE 48 -0.0003

ILE 48 MET 49 -0.0304

MET 49 ASP 50 0.0001

ASP 50 GLU 51 -0.0218

GLU 51 GLU 52 -0.0001

GLU 52 ARG 53 -0.0398

ARG 53 ARG 54 0.0001

ARG 54 THR 55 0.0291

THR 55 THR 56 0.0001

THR 56 VAL 57 -0.0207

VAL 57 ASN 58 0.0000

ASN 58 LEU 59 0.0156

LEU 59 LYS 60 -0.0003

LYS 60 ALA 61 -0.0540

ALA 61 CYS 62 -0.0000

CYS 62 ILE 63 -0.0105

ILE 63 LYS 64 -0.0002

LYS 64 ALA 65 -0.0573

ALA 65 ALA 66 -0.0002

ALA 66 ALA 67 -0.0449

ALA 67 ASP 68 -0.0000

ASP 68 ARG 69 -0.0310

ARG 69 VAL 70 0.0001

VAL 70 VAL 71 0.0330

VAL 71 PHE 72 0.0001

PHE 72 ILE 73 0.0921

ILE 73 ASN 74 -0.0004

ASN 74 THR 75 -0.0093

THR 75 GLY 76 0.0001

GLY 76 PHE 77 -0.0192

PHE 77 LEU 78 0.0004

LEU 78 ASP 79 0.0159

ASP 79 ARG 80 -0.0005

ARG 80 THR 81 -0.0039

THR 81 GLY 82 0.0003

GLY 82 ASP 83 0.0084

ASP 83 GLU 84 0.0005

GLU 84 ILE 85 0.0166

ILE 85 HIS 86 -0.0003

HIS 86 THR 87 0.0173

THR 87 SER 88 -0.0002

SER 88 MET 89 0.0273

MET 89 GLU 90 0.0002

GLU 90 ALA 91 0.0073

ALA 91 GLY 92 -0.0000

GLY 92 PRO 93 -0.0036

PRO 93 MET 94 -0.0001

MET 94 VAL 95 -0.0014

VAL 95 ARG 96 0.0001

ARG 96 LYS 97 -0.0304

LYS 97 GLY 98 0.0003

GLY 98 THR 99 0.0056

THR 99 MET 100 0.0003

MET 100 LYS 101 0.0027

LYS 101 SER 102 0.0002

SER 102 GLN 103 -0.0165

GLN 103 PRO 104 0.0003

PRO 104 TRP 105 -0.0057

TRP 105 ILE 106 -0.0002

ILE 106 LEU 107 0.0111

LEU 107 ALA 108 -0.0001

ALA 108 TYR 109 -0.0210

TYR 109 GLU 110 -0.0001

GLU 110 ASP 111 -0.0115

ASP 111 HIS 112 -0.0002

HIS 112 ASN 113 0.0291

ASN 113 VAL 114 -0.0001

VAL 114 ASP 115 -0.0171

ASP 115 ALA 116 0.0000

ALA 116 GLY 117 0.0179

GLY 117 LEU 118 0.0001

LEU 118 ALA 119 -0.0318

ALA 119 ALA 120 0.0001

ALA 120 GLY 121 -0.0270

GLY 121 PHE 122 -0.0000

PHE 122 SER 123 -0.0071

SER 123 GLY 124 -0.0001

GLY 124 ARG 125 0.0286

ARG 125 ALA 126 -0.0003

ALA 126 GLN 127 -0.0128

GLN 127 VAL 128 0.0003

VAL 128 GLY 129 -0.0541

GLY 129 LYS 130 0.0002

LYS 130 GLY 131 -0.0371

GLY 131 MET 132 0.0001

MET 132 TRP 133 -0.0168

TRP 133 THR 134 0.0001

THR 134 MET 135 -0.0053

MET 135 THR 136 0.0003

THR 136 GLU 137 0.0005

GLU 137 LEU 138 -0.0002

LEU 138 MET 139 -0.0090

MET 139 ALA 140 0.0003

ALA 140 ASP 141 -0.0039

ASP 141 MET 142 -0.0002

MET 142 VAL 143 0.0069

VAL 143 GLU 144 0.0000

GLU 144 THR 145 -0.0089

THR 145 LYS 146 0.0003

LYS 146 ILE 147 0.0066

ILE 147 ALA 148 0.0004

ALA 148 GLN 149 0.0017

GLN 149 PRO 150 -0.0003

PRO 150 ARG 151 -0.0008

ARG 151 ALA 152 0.0001

ALA 152 GLY 153 0.0015

GLY 153 ALA 154 0.0002

ALA 154 SER 155 0.0060

SER 155 THR 156 0.0000

THR 156 ALA 157 -0.0726

ALA 157 TRP 158 -0.0003

TRP 158 VAL 159 -0.0277

VAL 159 PRO 160 0.0002

PRO 160 SER 161 0.0003

SER 161 PRO 162 -0.0001

PRO 162 THR 163 0.0033

THR 163 ALA 164 0.0000

ALA 164 ALA 165 -0.0039

ALA 165 THR 166 -0.0000

THR 166 LEU 167 -0.0010

LEU 167 HIS 168 0.0003

HIS 168 ALA 169 0.0026

ALA 169 LEU 170 -0.0000

LEU 170 HIS 171 -0.0064

HIS 171 TYR 172 -0.0002

TYR 172 HIS 173 0.0144

HIS 173 GLN 174 -0.0003

GLN 174 VAL 175 -0.0046

VAL 175 ASP 176 -0.0003

ASP 176 VAL 177 0.0113

VAL 177 ALA 178 0.0001

ALA 178 ALA 179 0.0003

ALA 179 VAL 180 0.0001

VAL 180 GLN 181 0.0063

GLN 181 GLN 182 0.0002

GLN 182 GLY 183 0.0066

GLY 183 LEU 184 0.0002

LEU 184 ALA 185 -0.0069

ALA 185 GLY 186 0.0002

GLY 186 LYS 187 0.0206

LYS 187 ARG 188 0.0001

ARG 188 ARG 189 0.0137

ARG 189 ALA 190 -0.0000

ALA 190 THR 191 -0.0119

THR 191 ILE 192 0.0002

ILE 192 GLU 193 0.0180

GLU 193 GLN 194 0.0001

GLN 194 LEU 195 -0.0013

LEU 195 LEU 196 0.0001

LEU 196 THR 197 0.0274

THR 197 ILE 198 0.0001

ILE 198 PRO 199 0.0270

PRO 199 LEU 200 -0.0003

LEU 200 ALA 201 0.0223

ALA 201 LYS 202 0.0002

LYS 202 GLU 203 0.0117

GLU 203 LEU 204 0.0000

LEU 204 ALA 205 0.0047

ALA 205 TRP 206 0.0003

TRP 206 ALA 207 0.0051

ALA 207 PRO 208 -0.0001

PRO 208 ASP 209 -0.0004

ASP 209 GLU 210 -0.0002

GLU 210 ILE 211 -0.0058

ILE 211 ARG 212 0.0001

ARG 212 GLU 213 0.0008

GLU 213 GLU 214 -0.0001

GLU 214 VAL 215 0.0174

VAL 215 ASP 216 0.0001

ASP 216 ASN 217 -0.0017

ASN 217 ASN 218 -0.0002

ASN 218 CYS 219 0.0079

CYS 219 GLN 220 0.0002

GLN 220 SER 221 -0.0081

SER 221 ILE 222 -0.0001

ILE 222 LEU 223 -0.0056

LEU 223 GLY 224 0.0001

GLY 224 TYR 225 -0.0087

TYR 225 VAL 226 -0.0006

VAL 226 VAL 227 -0.0096

VAL 227 ARG 228 -0.0002

ARG 228 TRP 229 0.0036

TRP 229 VAL 230 -0.0001

VAL 230 ASP 231 -0.0057

ASP 231 GLN 232 -0.0001

GLN 232 GLY 233 -0.0005

GLY 233 VAL 234 0.0002

VAL 234 GLY 235 -0.0156

GLY 235 CYS 236 0.0003

CYS 236 SER 237 0.0071

SER 237 LYS 238 0.0003

LYS 238 VAL 239 -0.0028

VAL 239 PRO 240 -0.0002

PRO 240 ASP 241 -0.0023

ASP 241 ILE 242 0.0003

ILE 242 HIS 243 0.0028

HIS 243 ASP 244 -0.0000

ASP 244 VAL 245 -0.0032

VAL 245 ALA 246 -0.0002

ALA 246 LEU 247 -0.0032

LEU 247 MET 248 -0.0000

MET 248 GLU 249 0.0004

GLU 249 ASP 250 0.0002

ASP 250 ARG 251 0.0235

ARG 251 ALA 252 0.0003

ALA 252 THR 253 -0.0230

THR 253 LEU 254 -0.0003

LEU 254 ARG 255 0.0050

ARG 255 ILE 256 0.0001

ILE 256 SER 257 -0.0109

SER 257 SER 258 0.0003

SER 258 GLN 259 0.0131

GLN 259 LEU 260 0.0000

LEU 260 LEU 261 0.0096

LEU 261 ALA 262 0.0002

ALA 262 ASN 263 0.0202

ASN 263 TRP 264 -0.0004

TRP 264 LEU 265 0.0159

LEU 265 ARG 266 0.0004

ARG 266 HIS 267 0.0027

HIS 267 GLY 268 -0.0002

GLY 268 VAL 269 -0.0077

VAL 269 ILE 270 0.0001

ILE 270 THR 271 0.0101

THR 271 SER 272 0.0006

SER 272 ALA 273 -0.0035

ALA 273 ASP 274 -0.0005

ASP 274 VAL 275 -0.0113

VAL 275 ARG 276 0.0001

ARG 276 ALA 277 -0.0078

ALA 277 SER 278 0.0002

SER 278 LEU 279 0.0067

LEU 279 GLU 280 0.0003

GLU 280 ARG 281 0.0054

ARG 281 MET 282 -0.0001

MET 282 ALA 283 0.0102

ALA 283 PRO 284 0.0001

PRO 284 LEU 285 -0.0103

LEU 285 VAL 286 -0.0002

VAL 286 ASP 287 -0.0020

ASP 287 ARG 288 0.0000

ARG 288 GLN 289 -0.0022

GLN 289 ASN 290 0.0001

ASN 290 ALA 291 -0.0058

ALA 291 GLY 292 -0.0001

GLY 292 ASP 293 0.0002

ASP 293 VAL 294 0.0000

VAL 294 ALA 295 -0.0041

ALA 295 TYR 296 0.0003

TYR 296 ARG 297 0.0013

ARG 297 PRO 298 0.0001

PRO 298 MET 299 0.0033

MET 299 ALA 300 -0.0003

ALA 300 PRO 301 -0.0014

PRO 301 ASN 302 0.0001

ASN 302 PHE 303 0.0018

PHE 303 ASP 304 -0.0000

ASP 304 ASP 305 0.0130

ASP 305 SER 306 -0.0001

SER 306 ILE 307 -0.0078

ILE 307 ALA 308 -0.0001

ALA 308 PHE 309 0.0071

PHE 309 LEU 310 0.0000

LEU 310 ALA 311 -0.0124

ALA 311 ALA 312 -0.0002

ALA 312 GLN 313 0.0014

GLN 313 GLU 314 -0.0005

GLU 314 LEU 315 -0.0053

LEU 315 ILE 316 -0.0002

ILE 316 LEU 317 -0.0011

LEU 317 SER 318 0.0003

SER 318 GLY 319 -0.0060

GLY 319 ALA 320 0.0001

ALA 320 GLN 321 0.0078

GLN 321 GLN 322 -0.0001

GLN 322 PRO 323 -0.0304

PRO 323 ASN 324 -0.0000

ASN 324 GLY 325 0.0230

GLY 325 TYR 326 0.0005

TYR 326 THR 327 -0.0227

THR 327 GLU 328 0.0004

GLU 328 PRO 329 -0.0061

PRO 329 ILE 330 -0.0003

ILE 330 LEU 331 0.0126

LEU 331 HIS 332 -0.0001

HIS 332 ARG 333 -0.0004

ARG 333 ARG 334 0.0000

ARG 334 ARG 335 0.0101

ARG 335 ARG 336 0.0001

ARG 336 GLU 337 -0.0015

GLU 337 PHE 338 -0.0000

PHE 338 LYS 339 0.0093

LYS 339 ALA 340 -0.0000

ALA 340 ARG 341 0.0062

ARG 341 ALA 342 -0.0004

ALA 342 ALA 343 0.0071

ALA 343 GLU 344 -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).
Last modification: April 25th, 2023.

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

*** EXP_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 ***

CA strain for 24021912332929451

--- normal mode 7 ---

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

* EXP_6DNP_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *