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

* zxy *

CA strain for 2404230438531985751

--- normal mode 10 ---

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 -0.0003

ASP 2 PRO 3 0.0131

PRO 3 LEU 4 0.0001

LEU 4 GLY 5 -0.0774

GLY 5 LEU 6 -0.0000

LEU 6 GLN 7 0.0317

GLN 7 ASP 8 0.0002

ASP 8 PHE 9 -0.0160

PHE 9 ASP 10 0.0002

ASP 10 LEU 11 -0.0612

LEU 11 LEU 12 -0.0003

LEU 12 ARG 13 -0.1236

ARG 13 VAL 14 -0.0002

VAL 14 ILE 15 0.0745

ILE 15 GLY 16 0.0000

GLY 16 ARG 17 -0.1561

ARG 17 GLY 18 0.0002

GLY 18 SER 19 -0.2705

SER 19 TYR 20 0.0000

TYR 20 ALA 21 -0.0427

ALA 21 LYS 22 0.0001

LYS 22 VAL 23 -0.0520

VAL 23 LEU 24 0.0002

LEU 24 LEU 25 -0.0128

LEU 25 VAL 26 -0.0001

VAL 26 ARG 27 -0.0501

ARG 27 LEU 28 0.0000

LEU 28 LYS 29 -0.0493

LYS 29 LYS 30 0.0001

LYS 30 THR 31 0.0028

THR 31 ASP 32 0.0002

ASP 32 ARG 33 0.0317

ARG 33 ILE 34 0.0001

ILE 34 TYR 35 -0.0699

TYR 35 ALA 36 -0.0000

ALA 36 MET 37 0.0658

MET 37 LYS 38 -0.0004

LYS 38 VAL 39 0.0511

VAL 39 VAL 40 -0.0002

VAL 40 LYS 41 -0.0177

LYS 41 LYS 42 0.0004

LYS 42 GLU 43 0.0090

GLU 43 LEU 44 0.0004

LEU 44 VAL 45 -0.0334

VAL 45 ASN 46 -0.0002

ASN 46 ASP 47 0.0216

ASP 47 ASP 48 -0.0000

ASP 48 GLU 49 -0.0268

GLU 49 ASP 50 -0.0000

ASP 50 ILE 51 -0.0161

ILE 51 ASP 52 -0.0000

ASP 52 TRP 53 -0.0477

TRP 53 VAL 54 -0.0001

VAL 54 GLN 55 -0.0241

GLN 55 THR 56 -0.0005

THR 56 GLU 57 -0.0340

GLU 57 LYS 58 -0.0002

LYS 58 HIS 59 -0.1407

HIS 59 VAL 60 -0.0003

VAL 60 PHE 61 -0.0766

PHE 61 GLU 62 0.0002

GLU 62 GLN 63 -0.2220

GLN 63 ALA 64 0.0002

ALA 64 SER 65 -0.0457

SER 65 ASN 66 -0.0000

ASN 66 HIS 67 -0.0493

HIS 67 PRO 68 0.0003

PRO 68 PHE 69 -0.0176

PHE 69 LEU 70 -0.0004

LEU 70 VAL 71 -0.0053

VAL 71 GLY 72 -0.0002

GLY 72 LEU 73 0.0563

LEU 73 HIS 74 0.0002

HIS 74 SER 75 0.0179

SER 75 CYS 76 0.0002

CYS 76 PHE 77 -0.0282

PHE 77 GLN 78 0.0001

GLN 78 THR 79 -0.0111

THR 79 GLU 80 0.0001

GLU 80 SER 81 -0.0213

SER 81 ARG 82 -0.0001

ARG 82 LEU 83 -0.0484

LEU 83 PHE 84 -0.0000

PHE 84 PHE 85 0.0054

PHE 85 VAL 86 -0.0001

VAL 86 ILE 87 0.0986

ILE 87 GLU 88 -0.0002

GLU 88 TYR 89 -0.0647

TYR 89 VAL 90 0.0002

VAL 90 ASN 91 -0.0206

ASN 91 GLY 92 -0.0003

GLY 92 GLY 93 0.0125

GLY 93 ASP 94 -0.0000

ASP 94 LEU 95 0.2196

LEU 95 MET 96 -0.0001

MET 96 PHE 97 0.0359

PHE 97 HIS 98 0.0001

HIS 98 MET 99 0.0604

MET 99 GLN 100 -0.0001

GLN 100 ARG 101 -0.0663

ARG 101 GLN 102 -0.0000

GLN 102 ARG 103 -0.0062

ARG 103 LYS 104 -0.0001

LYS 104 LEU 105 -0.0607

LEU 105 PRO 106 0.0002

PRO 106 GLU 107 0.0679

GLU 107 GLU 108 -0.0004

GLU 108 HIS 109 0.0735

HIS 109 ALA 110 -0.0005

ALA 110 ARG 111 -0.0214

ARG 111 PHE 112 -0.0002

PHE 112 TYR 113 0.0063

TYR 113 SER 114 -0.0003

SER 114 ALA 115 0.0003

ALA 115 GLU 116 -0.0006

GLU 116 ILE 117 -0.0202

ILE 117 SER 118 0.0002

SER 118 LEU 119 0.0035

LEU 119 ALA 120 -0.0002

ALA 120 LEU 121 0.0128

LEU 121 ASN 122 0.0003

ASN 122 TYR 123 -0.1309

TYR 123 LEU 124 -0.0000

LEU 124 HIS 125 0.0067

HIS 125 GLU 126 -0.0000

GLU 126 ARG 127 -0.0935

ARG 127 GLY 128 -0.0004

GLY 128 ILE 129 0.0399

ILE 129 ILE 130 -0.0000

ILE 130 TYR 131 0.0806

TYR 131 ARG 132 0.0001

ARG 132 ASP 133 0.0120

ASP 133 LEU 134 0.0000

LEU 134 LYS 135 -0.0026

LYS 135 LEU 136 0.0001

LEU 136 ASP 137 0.0567

ASP 137 ASN 138 -0.0002

ASN 138 VAL 139 -0.0767

VAL 139 LEU 140 0.0001

LEU 140 LEU 141 -0.1263

LEU 141 ASP 142 -0.0001

ASP 142 SER 143 -0.0892

SER 143 GLU 144 -0.0000

GLU 144 GLY 145 -0.0142

GLY 145 HIS 146 0.0002

HIS 146 ILE 147 -0.0847

ILE 147 LYS 148 -0.0002

LYS 148 LEU 149 -0.0721

LEU 149 THR 150 0.0001

THR 150 ASP 151 -0.0850

ASP 151 TYR 152 -0.0000

TYR 152 GLY 153 -0.1059

GLY 153 MET 154 -0.0003

MET 154 CYS 155 0.0641

CYS 155 LYS 156 -0.0002

LYS 156 GLU 157 0.0028

GLU 157 GLY 158 0.0000

GLY 158 LEU 159 -0.2601

LEU 159 ARG 160 -0.0005

ARG 160 PRO 161 -0.0293

PRO 161 GLY 162 0.0001

GLY 162 ASP 163 -0.0464

ASP 163 THR 164 0.0000

THR 164 THR 165 0.0094

THR 165 SER 166 0.0001

SER 166 GLU 167 -0.0082

GLU 167 PHE 168 0.0003

PHE 168 CYS 169 -0.0308

CYS 169 GLY 170 -0.0002

GLY 170 THR 171 -0.0143

THR 171 PRO 172 0.0001

PRO 172 ASN 173 0.0017

ASN 173 TYR 174 -0.0000

TYR 174 ILE 175 0.0068

ILE 175 ALA 176 -0.0000

ALA 176 PRO 177 -0.0021

PRO 177 GLU 178 -0.0002

GLU 178 ILE 179 -0.0369

ILE 179 LEU 180 0.0004

LEU 180 ARG 181 0.0033

ARG 181 GLY 182 0.0001

GLY 182 GLU 183 0.0246

GLU 183 ASP 184 -0.0000

ASP 184 TYR 185 0.0402

TYR 185 GLY 186 0.0003

GLY 186 PHE 187 0.0640

PHE 187 SER 188 0.0001

SER 188 VAL 189 -0.0373

VAL 189 ASP 190 -0.0002

ASP 190 TRP 191 -0.0646

TRP 191 TRP 192 -0.0000

TRP 192 ALA 193 -0.0256

ALA 193 LEU 194 -0.0001

LEU 194 GLY 195 -0.0027

GLY 195 VAL 196 0.0004

VAL 196 LEU 197 0.0178

LEU 197 MET 198 0.0000

MET 198 PHE 199 -0.0138

PHE 199 GLU 200 0.0001

GLU 200 MET 201 -0.0938

MET 201 MET 202 -0.0002

MET 202 ALA 203 -0.0214

ALA 203 GLY 204 0.0002

GLY 204 ARG 205 -0.1278

ARG 205 SER 206 0.0002

SER 206 PRO 207 -0.0166

PRO 207 PHE 208 0.0001

PHE 208 ASP 209 0.0705

ASP 209 ILE 210 0.0000

ILE 210 VAL 211 0.0129

VAL 211 GLY 212 0.0002

GLY 212 SER 213 -0.0736

SER 213 SER 214 0.0001

SER 214 ASP 215 0.0434

ASP 215 ASN 216 0.0004

ASN 216 PRO 217 -0.0277

PRO 217 ASP 218 -0.0004

ASP 218 GLN 219 0.0132

GLN 219 ASN 220 -0.0002

ASN 220 THR 221 0.0495

THR 221 GLU 222 0.0000

GLU 222 ASP 223 -0.0115

ASP 223 TYR 224 0.0001

TYR 224 LEU 225 -0.1082

LEU 225 PHE 226 0.0000

PHE 226 GLN 227 -0.0739

GLN 227 VAL 228 -0.0001

VAL 228 ILE 229 0.0970

ILE 229 LEU 230 -0.0003

LEU 230 GLU 231 0.0114

GLU 231 LYS 232 0.0002

LYS 232 GLN 233 0.0717

GLN 233 ILE 234 0.0000

ILE 234 ARG 235 -0.0300

ARG 235 ILE 236 0.0001

ILE 236 PRO 237 -0.0521

PRO 237 ARG 238 0.0004

ARG 238 SER 239 0.0520

SER 239 LEU 240 0.0003

LEU 240 SER 241 0.0059

SER 241 VAL 242 -0.0002

VAL 242 LYS 243 -0.0511

LYS 243 ALA 244 0.0001

ALA 244 ALA 245 0.0370

ALA 245 SER 246 0.0003

SER 246 VAL 247 -0.0173

VAL 247 LEU 248 0.0000

LEU 248 LYS 249 0.0458

LYS 249 SER 250 0.0002

SER 250 PHE 251 0.0013

PHE 251 LEU 252 -0.0002

LEU 252 ASN 253 0.0073

ASN 253 LYS 254 -0.0001

LYS 254 ASP 255 0.0615

ASP 255 PRO 256 0.0002

PRO 256 LYS 257 0.0056

LYS 257 GLU 258 -0.0001

GLU 258 ARG 259 0.0077

ARG 259 LEU 260 -0.0003

LEU 260 GLY 261 -0.0497

GLY 261 CYS 262 -0.0000

CYS 262 HIS 263 -0.0117

HIS 263 PRO 264 -0.0001

PRO 264 GLN 265 -0.0316

GLN 265 THR 266 -0.0000

THR 266 GLY 267 -0.0227

GLY 267 PHE 268 -0.0002

PHE 268 ALA 269 -0.0277

ALA 269 ASP 270 0.0001

ASP 270 ILE 271 0.0060

ILE 271 GLN 272 -0.0000

GLN 272 GLY 273 -0.0259

GLY 273 HIS 274 0.0000

HIS 274 PRO 275 -0.0162

PRO 275 PHE 276 -0.0002

PHE 276 PHE 277 -0.0420

PHE 277 ARG 278 -0.0002

ARG 278 ASN 279 0.0163

ASN 279 VAL 280 -0.0002

VAL 280 ASP 281 -0.0745

ASP 281 TRP 282 -0.0004

TRP 282 ASP 283 0.0132

ASP 283 MET 284 0.0001

MET 284 MET 285 -0.0404

MET 285 GLU 286 -0.0002

GLU 286 GLN 287 0.0217

GLN 287 LYS 288 -0.0004

LYS 288 GLN 289 0.0234

GLN 289 VAL 290 0.0001

VAL 290 VAL 291 0.0556

VAL 291 PRO 292 -0.0001

PRO 292 PRO 293 -0.0368

PRO 293 PHE 294 -0.0002

PHE 294 LYS 295 0.1210

LYS 295 PRO 296 0.0001

PRO 296 ASN 297 0.1040

ASN 297 ILE 298 -0.0001

ILE 298 SER 299 -0.0339

SER 299 GLY 300 0.0000

GLY 300 GLU 301 0.0883

GLU 301 PHE 302 0.0002

PHE 302 GLY 303 0.1427

GLY 303 LEU 304 -0.0003

LEU 304 ASP 305 0.0937

ASP 305 ASN 306 0.0001

ASN 306 PHE 307 0.0645

PHE 307 ASP 308 -0.0002

ASP 308 SER 309 0.0853

SER 309 GLN 310 0.0003

GLN 310 PHE 311 -0.0169

PHE 311 THR 312 0.0004

THR 312 ASN 313 0.0599

ASN 313 GLU 314 0.0000

GLU 314 PRO 315 -0.0422

PRO 315 VAL 316 0.0002

VAL 316 GLN 317 0.1798

GLN 317 LEU 318 -0.0000

LEU 318 GLU 319 0.0426

GLU 319 PRO 320 0.0000

PRO 320 ASP 321 0.1093

ASP 321 ASP 322 -0.0000

ASP 322 ASP 323 0.0328

ASP 323 ASP 324 -0.0000

ASP 324 ILE 325 -0.0608

ILE 325 VAL 326 -0.0002

VAL 326 ARG 327 0.0582

ARG 327 LYS 328 -0.0001

LYS 328 ILE 329 -0.0401

ILE 329 ASP 330 0.0001

ASP 330 GLN 331 0.0350

GLN 331 SER 332 -0.0001

SER 332 GLU 333 -0.0624

GLU 333 PHE 334 -0.0002

PHE 334 GLU 335 0.0138

GLU 335 GLY 336 -0.0002

GLY 336 PHE 337 -0.0372

PHE 337 GLU 338 -0.0002

GLU 338 TYR 339 0.0392

TYR 339 ILE 340 0.0002

ILE 340 ASN 341 0.0001

ASN 341 PRO 342 -0.0000

PRO 342 LEU 343 -0.0036

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 2404230438531985751

--- normal mode 10 ---

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

* zxy *