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

* zxy *

CA strain for 2404230453311989143

--- 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
MET 1 ASP 2 -0.0002

ASP 2 PRO 3 -0.0127

PRO 3 LEU 4 -0.0004

LEU 4 GLY 5 0.0271

GLY 5 LEU 6 0.0001

LEU 6 GLN 7 -0.0071

GLN 7 ASP 8 0.0004

ASP 8 PHE 9 0.0094

PHE 9 ASP 10 -0.0001

ASP 10 LEU 11 -0.0207

LEU 11 LEU 12 -0.0005

LEU 12 ARG 13 -0.0580

ARG 13 VAL 14 -0.0002

VAL 14 ILE 15 0.0131

ILE 15 GLY 16 -0.0001

GLY 16 ARG 17 -0.0194

ARG 17 GLY 18 0.0001

GLY 18 SER 19 0.0323

SER 19 TYR 20 0.0001

TYR 20 ALA 21 -0.0077

ALA 21 LYS 22 -0.0002

LYS 22 VAL 23 -0.0007

VAL 23 LEU 24 0.0004

LEU 24 LEU 25 0.0175

LEU 25 VAL 26 0.0003

VAL 26 ARG 27 -0.0183

ARG 27 LEU 28 0.0000

LEU 28 LYS 29 0.0102

LYS 29 LYS 30 -0.0001

LYS 30 THR 31 0.0053

THR 31 ASP 32 0.0000

ASP 32 ARG 33 0.0326

ARG 33 ILE 34 0.0004

ILE 34 TYR 35 -0.0344

TYR 35 ALA 36 -0.0001

ALA 36 MET 37 0.0591

MET 37 LYS 38 0.0000

LYS 38 VAL 39 -0.0118

VAL 39 VAL 40 -0.0001

VAL 40 LYS 41 -0.0378

LYS 41 LYS 42 0.0001

LYS 42 GLU 43 0.0121

GLU 43 LEU 44 -0.0003

LEU 44 VAL 45 -0.0181

VAL 45 ASN 46 0.0001

ASN 46 ASP 47 0.0021

ASP 47 ASP 48 0.0003

ASP 48 GLU 49 -0.0725

GLU 49 ASP 50 -0.0001

ASP 50 ILE 51 0.0148

ILE 51 ASP 52 0.0002

ASP 52 TRP 53 0.0271

TRP 53 VAL 54 -0.0003

VAL 54 GLN 55 -0.0457

GLN 55 THR 56 0.0000

THR 56 GLU 57 -0.0560

GLU 57 LYS 58 0.0005

LYS 58 HSD 59 -0.0600

HSD 59 VAL 60 -0.0002

VAL 60 PHE 61 -0.0337

PHE 61 GLU 62 -0.0000

GLU 62 GLN 63 -0.0297

GLN 63 ALA 64 -0.0002

ALA 64 SER 65 0.0154

SER 65 ASN 66 -0.0000

ASN 66 HSD 67 0.0972

HSD 67 PRO 68 0.0001

PRO 68 PHE 69 0.0121

PHE 69 LEU 70 0.0003

LEU 70 VAL 71 0.0210

VAL 71 GLY 72 -0.0002

GLY 72 LEU 73 0.0947

LEU 73 HSD 74 0.0000

HSD 74 SER 75 0.0346

SER 75 CYS 76 -0.0002

CYS 76 PHE 77 0.0222

PHE 77 GLN 78 0.0001

GLN 78 THR 79 0.0522

THR 79 GLU 80 -0.0004

GLU 80 SER 81 -0.0348

SER 81 ARG 82 -0.0001

ARG 82 LEU 83 -0.0160

LEU 83 PHE 84 0.0003

PHE 84 PHE 85 0.0078

PHE 85 VAL 86 0.0002

VAL 86 ILE 87 0.0890

ILE 87 GLU 88 0.0002

GLU 88 TYR 89 -0.0727

TYR 89 VAL 90 -0.0001

VAL 90 ASN 91 -0.0509

ASN 91 GLY 92 0.0001

GLY 92 GLY 93 0.0539

GLY 93 ASP 94 -0.0002

ASP 94 LEU 95 0.0782

LEU 95 MET 96 0.0003

MET 96 PHE 97 0.0128

PHE 97 HSD 98 0.0001

HSD 98 MET 99 0.0579

MET 99 GLN 100 -0.0000

GLN 100 ARG 101 -0.0257

ARG 101 GLN 102 0.0001

GLN 102 ARG 103 0.0338

ARG 103 LYS 104 0.0000

LYS 104 LEU 105 -0.0119

LEU 105 PRO 106 -0.0002

PRO 106 GLU 107 0.0289

GLU 107 GLU 108 -0.0001

GLU 108 HSD 109 0.0223

HSD 109 ALA 110 -0.0000

ALA 110 ARG 111 -0.0056

ARG 111 PHE 112 0.0001

PHE 112 TYR 113 0.0025

TYR 113 SER 114 -0.0001

SER 114 ALA 115 0.0058

ALA 115 GLU 116 0.0000

GLU 116 ILE 117 -0.0004

ILE 117 SER 118 -0.0001

SER 118 LEU 119 0.0105

LEU 119 ALA 120 -0.0002

ALA 120 LEU 121 0.0169

LEU 121 ASN 122 0.0002

ASN 122 TYR 123 -0.0558

TYR 123 LEU 124 0.0004

LEU 124 HSD 125 0.0031

HSD 125 GLU 126 0.0001

GLU 126 ARG 127 -0.0602

ARG 127 GLY 128 0.0000

GLY 128 ILE 129 0.0303

ILE 129 ILE 130 0.0000

ILE 130 TYR 131 0.0425

TYR 131 ARG 132 0.0003

ARG 132 ASP 133 -0.0042

ASP 133 LEU 134 0.0001

LEU 134 LYS 135 -0.0102

LYS 135 LEU 136 0.0000

LEU 136 ASP 137 0.0350

ASP 137 ASN 138 0.0001

ASN 138 VAL 139 -0.0347

VAL 139 LEU 140 -0.0000

LEU 140 LEU 141 -0.0387

LEU 141 ASP 142 0.0004

ASP 142 SER 143 -0.0332

SER 143 GLU 144 0.0002

GLU 144 GLY 145 0.0061

GLY 145 HSD 146 -0.0001

HSD 146 ILE 147 -0.0233

ILE 147 LYS 148 0.0002

LYS 148 LEU 149 -0.0326

LEU 149 THR 150 -0.0000

THR 150 ASP 151 -0.0844

ASP 151 TYR 152 -0.0003

TYR 152 GLY 153 -0.0675

GLY 153 MET 154 0.0002

MET 154 CYS 155 0.0312

CYS 155 LYS 156 -0.0002

LYS 156 GLU 157 0.0693

GLU 157 GLY 158 0.0001

GLY 158 LEU 159 -0.2077

LEU 159 ARG 160 0.0000

ARG 160 PRO 161 -0.0322

PRO 161 GLY 162 0.0002

GLY 162 ASP 163 -0.0113

ASP 163 THR 164 0.0001

THR 164 THR 165 0.0132

THR 165 SER 166 -0.0002

SER 166 GLU 167 0.0195

GLU 167 PHE 168 0.0003

PHE 168 CYS 169 -0.0616

CYS 169 GLY 170 -0.0002

GLY 170 THR 171 0.0601

THR 171 PRO 172 0.0003

PRO 172 ASN 173 -0.0433

ASN 173 TYR 174 0.0002

TYR 174 ILE 175 -0.0213

ILE 175 ALA 176 -0.0000

ALA 176 PRO 177 -0.0052

PRO 177 GLU 178 0.0002

GLU 178 ILE 179 0.0106

ILE 179 LEU 180 0.0003

LEU 180 ARG 181 0.0152

ARG 181 GLY 182 0.0003

GLY 182 GLU 183 0.0005

GLU 183 ASP 184 -0.0001

ASP 184 TYR 185 0.0453

TYR 185 GLY 186 0.0003

GLY 186 PHE 187 0.0643

PHE 187 SER 188 -0.0002

SER 188 VAL 189 -0.0011

VAL 189 ASP 190 0.0001

ASP 190 TRP 191 -0.0306

TRP 191 TRP 192 0.0003

TRP 192 ALA 193 0.0221

ALA 193 LEU 194 0.0000

LEU 194 GLY 195 -0.0137

GLY 195 VAL 196 0.0002

VAL 196 LEU 197 0.0397

LEU 197 MET 198 0.0003

MET 198 PHE 199 0.0162

PHE 199 GLU 200 0.0002

GLU 200 MET 201 0.0336

MET 201 MET 202 -0.0003

MET 202 ALA 203 0.0111

ALA 203 GLY 204 0.0002

GLY 204 ARG 205 0.0458

ARG 205 SER 206 -0.0001

SER 206 PRO 207 0.0663

PRO 207 PHE 208 0.0000

PHE 208 ASP 209 -0.0730

ASP 209 ILE 210 0.0002

ILE 210 VAL 211 -0.0505

VAL 211 GLY 212 -0.0001

GLY 212 SER 213 0.0341

SER 213 SER 214 0.0001

SER 214 ASP 215 -0.0512

ASP 215 ASN 216 0.0001

ASN 216 PRO 217 -0.0038

PRO 217 ASP 218 -0.0001

ASP 218 GLN 219 0.0265

GLN 219 ASN 220 -0.0002

ASN 220 THR 221 -0.0073

THR 221 GLU 222 -0.0000

GLU 222 ASP 223 -0.0331

ASP 223 TYR 224 -0.0002

TYR 224 LEU 225 0.0616

LEU 225 PHE 226 -0.0001

PHE 226 GLN 227 0.0126

GLN 227 VAL 228 0.0004

VAL 228 ILE 229 -0.1097

ILE 229 LEU 230 -0.0003

LEU 230 GLU 231 -0.0860

GLU 231 LYS 232 -0.0004

LYS 232 GLN 233 0.0055

GLN 233 ILE 234 -0.0001

ILE 234 ARG 235 0.0226

ARG 235 ILE 236 -0.0001

ILE 236 PRO 237 0.0044

PRO 237 ARG 238 -0.0001

ARG 238 SER 239 0.0311

SER 239 LEU 240 0.0004

LEU 240 SER 241 -0.0094

SER 241 VAL 242 -0.0002

VAL 242 LYS 243 -0.0130

LYS 243 ALA 244 0.0002

ALA 244 ALA 245 -0.0072

ALA 245 SER 246 0.0001

SER 246 VAL 247 -0.0042

VAL 247 LEU 248 -0.0003

LEU 248 LYS 249 0.0486

LYS 249 SER 250 -0.0002

SER 250 PHE 251 -0.0168

PHE 251 LEU 252 -0.0002

LEU 252 ASN 253 0.0378

ASN 253 LYS 254 -0.0000

LYS 254 ASP 255 -0.0493

ASP 255 PRO 256 -0.0001

PRO 256 LYS 257 -0.0131

LYS 257 GLU 258 0.0001

GLU 258 ARG 259 0.0287

ARG 259 LEU 260 0.0004

LEU 260 GLY 261 -0.0366

GLY 261 CYS 262 0.0001

CYS 262 HSD 263 -0.0015

HSD 263 PRO 264 -0.0001

PRO 264 GLN 265 -0.0147

GLN 265 THR 266 -0.0001

THR 266 GLY 267 -0.0248

GLY 267 PHE 268 -0.0001

PHE 268 ALA 269 -0.0210

ALA 269 ASP 270 0.0001

ASP 270 ILE 271 0.0239

ILE 271 GLN 272 0.0001

GLN 272 GLY 273 -0.0273

GLY 273 HSD 274 -0.0004

HSD 274 PRO 275 0.0009

PRO 275 PHE 276 0.0002

PHE 276 PHE 277 -0.0328

PHE 277 ARG 278 -0.0000

ARG 278 ASN 279 0.0101

ASN 279 VAL 280 0.0002

VAL 280 ASP 281 -0.0331

ASP 281 TRP 282 -0.0002

TRP 282 ASP 283 -0.0064

ASP 283 MET 284 0.0003

MET 284 MET 285 -0.0065

MET 285 GLU 286 -0.0000

GLU 286 GLN 287 0.0003

GLN 287 LYS 288 0.0004

LYS 288 GLN 289 0.0185

GLN 289 VAL 290 0.0000

VAL 290 VAL 291 0.0209

VAL 291 PRO 292 0.0001

PRO 292 PRO 293 -0.0147

PRO 293 PHE 294 -0.0001

PHE 294 LYS 295 0.1309

LYS 295 PRO 296 0.0002

PRO 296 ASN 297 0.0592

ASN 297 ILE 298 -0.0000

ILE 298 SER 299 0.0153

SER 299 GLY 300 0.0001

GLY 300 GLU 301 -0.0108

GLU 301 PHE 302 -0.0005

PHE 302 GLY 303 0.0539

GLY 303 LEU 304 -0.0004

LEU 304 ASP 305 0.0152

ASP 305 ASN 306 -0.0001

ASN 306 PHE 307 -0.0218

PHE 307 ASP 308 0.0000

ASP 308 SER 309 0.0102

SER 309 GLN 310 0.0002

GLN 310 PHE 311 0.0004

PHE 311 THR 312 0.0002

THR 312 ASN 313 0.0202

ASN 313 GLU 314 0.0002

GLU 314 PRO 315 -0.0222

PRO 315 VAL 316 -0.0003

VAL 316 GLN 317 0.0953

GLN 317 LEU 318 0.0001

LEU 318 GLU 319 0.0509

GLU 319 PRO 320 0.0001

PRO 320 ASP 321 0.0743

ASP 321 ASP 322 -0.0001

ASP 322 ASP 323 0.0200

ASP 323 ASP 324 0.0000

ASP 324 ILE 325 -0.0875

ILE 325 VAL 326 -0.0002

VAL 326 ARG 327 0.0466

ARG 327 LYS 328 0.0001

LYS 328 ILE 329 -0.0467

ILE 329 ASP 330 -0.0005

ASP 330 GLN 331 0.0134

GLN 331 SER 332 -0.0001

SER 332 GLU 333 -0.0236

GLU 333 PHE 334 -0.0002

PHE 334 GLU 335 0.0023

GLU 335 GLY 336 0.0001

GLY 336 PHE 337 -0.0040

PHE 337 GLU 338 0.0002

GLU 338 TYR 339 0.0704

TYR 339 ILE 340 0.0000

ILE 340 ASN 341 0.0619

ASN 341 PRO 342 -0.0001

PRO 342 LEU 343 0.0107

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.

*** zxy ***

CA strain for 2404230453311989143

--- normal mode 9 ---

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

* zxy *