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

* zxy *

CA strain for 2404230453311989143

--- 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
MET 1 ASP 2 -0.0002

ASP 2 PRO 3 0.0177

PRO 3 LEU 4 -0.0000

LEU 4 GLY 5 -0.0325

GLY 5 LEU 6 -0.0002

LEU 6 GLN 7 0.0082

GLN 7 ASP 8 0.0002

ASP 8 PHE 9 0.0040

PHE 9 ASP 10 0.0001

ASP 10 LEU 11 0.0066

LEU 11 LEU 12 -0.0002

LEU 12 ARG 13 0.0132

ARG 13 VAL 14 -0.0002

VAL 14 ILE 15 0.0259

ILE 15 GLY 16 -0.0000

GLY 16 ARG 17 -0.0036

ARG 17 GLY 18 0.0002

GLY 18 SER 19 -0.0468

SER 19 TYR 20 -0.0002

TYR 20 ALA 21 0.0031

ALA 21 LYS 22 0.0000

LYS 22 VAL 23 0.0080

VAL 23 LEU 24 -0.0003

LEU 24 LEU 25 -0.0082

LEU 25 VAL 26 0.0002

VAL 26 ARG 27 0.0094

ARG 27 LEU 28 -0.0002

LEU 28 LYS 29 -0.0072

LYS 29 LYS 30 0.0003

LYS 30 THR 31 -0.0046

THR 31 ASP 32 0.0001

ASP 32 ARG 33 -0.0079

ARG 33 ILE 34 0.0003

ILE 34 TYR 35 0.0004

TYR 35 ALA 36 -0.0000

ALA 36 MET 37 -0.0160

MET 37 LYS 38 0.0000

LYS 38 VAL 39 0.0306

VAL 39 VAL 40 -0.0003

VAL 40 LYS 41 0.0300

LYS 41 LYS 42 -0.0003

LYS 42 GLU 43 -0.0067

GLU 43 LEU 44 -0.0000

LEU 44 VAL 45 -0.0057

VAL 45 ASN 46 0.0002

ASN 46 ASP 47 -0.0044

ASP 47 ASP 48 0.0000

ASP 48 GLU 49 0.0270

GLU 49 ASP 50 0.0003

ASP 50 ILE 51 -0.0051

ILE 51 ASP 52 0.0002

ASP 52 TRP 53 -0.0046

TRP 53 VAL 54 0.0000

VAL 54 GLN 55 -0.0295

GLN 55 THR 56 -0.0006

THR 56 GLU 57 -0.0010

GLU 57 LYS 58 -0.0000

LYS 58 HSD 59 -0.0412

HSD 59 VAL 60 0.0000

VAL 60 PHE 61 -0.0026

PHE 61 GLU 62 0.0003

GLU 62 GLN 63 -0.1103

GLN 63 ALA 64 -0.0002

ALA 64 SER 65 0.0056

SER 65 ASN 66 0.0001

ASN 66 HSD 67 -0.1950

HSD 67 PRO 68 0.0001

PRO 68 PHE 69 -0.0274

PHE 69 LEU 70 -0.0001

LEU 70 VAL 71 -0.0634

VAL 71 GLY 72 0.0004

GLY 72 LEU 73 -0.0838

LEU 73 HSD 74 0.0002

HSD 74 SER 75 -0.0419

SER 75 CYS 76 0.0004

CYS 76 PHE 77 -0.0524

PHE 77 GLN 78 -0.0001

GLN 78 THR 79 -0.0557

THR 79 GLU 80 -0.0001

GLU 80 SER 81 0.0269

SER 81 ARG 82 -0.0003

ARG 82 LEU 83 -0.0164

LEU 83 PHE 84 -0.0003

PHE 84 PHE 85 -0.0253

PHE 85 VAL 86 -0.0002

VAL 86 ILE 87 -0.0445

ILE 87 GLU 88 0.0001

GLU 88 TYR 89 0.0166

TYR 89 VAL 90 0.0003

VAL 90 ASN 91 0.0070

ASN 91 GLY 92 0.0001

GLY 92 GLY 93 -0.0053

GLY 93 ASP 94 -0.0000

ASP 94 LEU 95 0.0649

LEU 95 MET 96 0.0002

MET 96 PHE 97 -0.0026

PHE 97 HSD 98 0.0002

HSD 98 MET 99 0.0183

MET 99 GLN 100 -0.0003

GLN 100 ARG 101 -0.0194

ARG 101 GLN 102 -0.0001

GLN 102 ARG 103 -0.0035

ARG 103 LYS 104 0.0001

LYS 104 LEU 105 -0.0090

LEU 105 PRO 106 0.0001

PRO 106 GLU 107 0.0260

GLU 107 GLU 108 -0.0000

GLU 108 HSD 109 0.0080

HSD 109 ALA 110 -0.0004

ALA 110 ARG 111 0.0059

ARG 111 PHE 112 -0.0001

PHE 112 TYR 113 0.0165

TYR 113 SER 114 -0.0002

SER 114 ALA 115 -0.0056

ALA 115 GLU 116 -0.0000

GLU 116 ILE 117 0.0180

ILE 117 SER 118 -0.0002

SER 118 LEU 119 -0.0187

LEU 119 ALA 120 -0.0001

ALA 120 LEU 121 -0.0018

LEU 121 ASN 122 0.0001

ASN 122 TYR 123 -0.1004

TYR 123 LEU 124 0.0001

LEU 124 HSD 125 -0.0148

HSD 125 GLU 126 -0.0000

GLU 126 ARG 127 -0.0424

ARG 127 GLY 128 0.0002

GLY 128 ILE 129 0.0046

ILE 129 ILE 130 -0.0001

ILE 130 TYR 131 -0.0043

TYR 131 ARG 132 -0.0001

ARG 132 ASP 133 -0.0394

ASP 133 LEU 134 -0.0002

LEU 134 LYS 135 -0.0235

LYS 135 LEU 136 -0.0002

LEU 136 ASP 137 0.0280

ASP 137 ASN 138 -0.0002

ASN 138 VAL 139 0.0001

VAL 139 LEU 140 -0.0004

LEU 140 LEU 141 -0.0033

LEU 141 ASP 142 -0.0004

ASP 142 SER 143 0.0003

SER 143 GLU 144 -0.0001

GLU 144 GLY 145 -0.0055

GLY 145 HSD 146 0.0002

HSD 146 ILE 147 0.0035

ILE 147 LYS 148 0.0002

LYS 148 LEU 149 0.0110

LEU 149 THR 150 0.0000

THR 150 ASP 151 0.0166

ASP 151 TYR 152 0.0001

TYR 152 GLY 153 0.0708

GLY 153 MET 154 -0.0002

MET 154 CYS 155 -0.0003

CYS 155 LYS 156 -0.0000

LYS 156 GLU 157 0.0179

GLU 157 GLY 158 0.0001

GLY 158 LEU 159 -0.0601

LEU 159 ARG 160 -0.0002

ARG 160 PRO 161 -0.0084

PRO 161 GLY 162 -0.0001

GLY 162 ASP 163 0.0091

ASP 163 THR 164 0.0001

THR 164 THR 165 0.0071

THR 165 SER 166 0.0001

SER 166 GLU 167 -0.0012

GLU 167 PHE 168 0.0001

PHE 168 CYS 169 0.0138

CYS 169 GLY 170 0.0005

GLY 170 THR 171 -0.0132

THR 171 PRO 172 -0.0003

PRO 172 ASN 173 -0.0158

ASN 173 TYR 174 0.0002

TYR 174 ILE 175 -0.0255

ILE 175 ALA 176 0.0000

ALA 176 PRO 177 0.0048

PRO 177 GLU 178 -0.0004

GLU 178 ILE 179 0.0203

ILE 179 LEU 180 0.0001

LEU 180 ARG 181 0.0058

ARG 181 GLY 182 0.0004

GLY 182 GLU 183 -0.0140

GLU 183 ASP 184 -0.0002

ASP 184 TYR 185 0.0074

TYR 185 GLY 186 0.0002

GLY 186 PHE 187 -0.0029

PHE 187 SER 188 -0.0003

SER 188 VAL 189 0.0082

VAL 189 ASP 190 -0.0004

ASP 190 TRP 191 0.0427

TRP 191 TRP 192 -0.0000

TRP 192 ALA 193 0.0251

ALA 193 LEU 194 -0.0003

LEU 194 GLY 195 0.0015

GLY 195 VAL 196 -0.0002

VAL 196 LEU 197 0.0013

LEU 197 MET 198 0.0004

MET 198 PHE 199 -0.0080

PHE 199 GLU 200 -0.0000

GLU 200 MET 201 -0.0131

MET 201 MET 202 -0.0004

MET 202 ALA 203 -0.0158

ALA 203 GLY 204 0.0003

GLY 204 ARG 205 -0.0235

ARG 205 SER 206 0.0003

SER 206 PRO 207 0.0166

PRO 207 PHE 208 -0.0002

PHE 208 ASP 209 -0.0248

ASP 209 ILE 210 -0.0000

ILE 210 VAL 211 -0.0140

VAL 211 GLY 212 -0.0002

GLY 212 SER 213 0.0010

SER 213 SER 214 -0.0000

SER 214 ASP 215 -0.0148

ASP 215 ASN 216 0.0002

ASN 216 PRO 217 -0.0054

PRO 217 ASP 218 -0.0005

ASP 218 GLN 219 0.0104

GLN 219 ASN 220 0.0001

ASN 220 THR 221 -0.0050

THR 221 GLU 222 0.0001

GLU 222 ASP 223 0.0005

ASP 223 TYR 224 0.0002

TYR 224 LEU 225 0.0225

LEU 225 PHE 226 -0.0002

PHE 226 GLN 227 0.0255

GLN 227 VAL 228 0.0001

VAL 228 ILE 229 -0.0296

ILE 229 LEU 230 -0.0000

LEU 230 GLU 231 -0.0034

GLU 231 LYS 232 -0.0005

LYS 232 GLN 233 -0.0068

GLN 233 ILE 234 0.0004

ILE 234 ARG 235 0.0165

ARG 235 ILE 236 0.0001

ILE 236 PRO 237 0.0057

PRO 237 ARG 238 -0.0000

ARG 238 SER 239 0.0051

SER 239 LEU 240 0.0000

LEU 240 SER 241 -0.0018

SER 241 VAL 242 0.0004

VAL 242 LYS 243 -0.0087

LYS 243 ALA 244 0.0001

ALA 244 ALA 245 -0.0128

ALA 245 SER 246 -0.0001

SER 246 VAL 247 0.0014

VAL 247 LEU 248 -0.0003

LEU 248 LYS 249 0.0118

LYS 249 SER 250 0.0002

SER 250 PHE 251 -0.0003

PHE 251 LEU 252 0.0001

LEU 252 ASN 253 0.0054

ASN 253 LYS 254 -0.0001

LYS 254 ASP 255 -0.0151

ASP 255 PRO 256 -0.0000

PRO 256 LYS 257 0.0019

LYS 257 GLU 258 0.0001

GLU 258 ARG 259 0.0048

ARG 259 LEU 260 0.0000

LEU 260 GLY 261 -0.0103

GLY 261 CYS 262 -0.0004

CYS 262 HSD 263 0.0065

HSD 263 PRO 264 -0.0001

PRO 264 GLN 265 0.0035

GLN 265 THR 266 -0.0000

THR 266 GLY 267 -0.0082

GLY 267 PHE 268 -0.0004

PHE 268 ALA 269 -0.0049

ALA 269 ASP 270 -0.0001

ASP 270 ILE 271 0.0102

ILE 271 GLN 272 0.0003

GLN 272 GLY 273 -0.0139

GLY 273 HSD 274 0.0001

HSD 274 PRO 275 0.0058

PRO 275 PHE 276 0.0001

PHE 276 PHE 277 -0.0238

PHE 277 ARG 278 -0.0001

ARG 278 ASN 279 0.0058

ASN 279 VAL 280 0.0000

VAL 280 ASP 281 -0.0216

ASP 281 TRP 282 0.0001

TRP 282 ASP 283 -0.0085

ASP 283 MET 284 0.0001

MET 284 MET 285 -0.0007

MET 285 GLU 286 -0.0001

GLU 286 GLN 287 0.0109

GLN 287 LYS 288 -0.0001

LYS 288 GLN 289 -0.0158

GLN 289 VAL 290 -0.0000

VAL 290 VAL 291 0.0097

VAL 291 PRO 292 0.0000

PRO 292 PRO 293 -0.0157

PRO 293 PHE 294 -0.0004

PHE 294 LYS 295 -0.0267

LYS 295 PRO 296 0.0001

PRO 296 ASN 297 -0.0071

ASN 297 ILE 298 -0.0003

ILE 298 SER 299 -0.0048

SER 299 GLY 300 -0.0001

GLY 300 GLU 301 0.0421

GLU 301 PHE 302 0.0001

PHE 302 GLY 303 0.0056

GLY 303 LEU 304 0.0000

LEU 304 ASP 305 0.0299

ASP 305 ASN 306 -0.0000

ASN 306 PHE 307 0.0687

PHE 307 ASP 308 -0.0002

ASP 308 SER 309 0.0316

SER 309 GLN 310 -0.0002

GLN 310 PHE 311 -0.0140

PHE 311 THR 312 0.0001

THR 312 ASN 313 0.0069

ASN 313 GLU 314 0.0001

GLU 314 PRO 315 0.0126

PRO 315 VAL 316 0.0004

VAL 316 GLN 317 0.0009

GLN 317 LEU 318 0.0000

LEU 318 GLU 319 -0.0228

GLU 319 PRO 320 0.0001

PRO 320 ASP 321 0.0089

ASP 321 ASP 322 0.0002

ASP 322 ASP 323 0.0181

ASP 323 ASP 324 0.0000

ASP 324 ILE 325 0.0313

ILE 325 VAL 326 -0.0002

VAL 326 ARG 327 -0.0051

ARG 327 LYS 328 -0.0001

LYS 328 ILE 329 -0.0092

ILE 329 ASP 330 -0.0002

ASP 330 GLN 331 -0.0119

GLN 331 SER 332 0.0001

SER 332 GLU 333 0.0114

GLU 333 PHE 334 -0.0000

PHE 334 GLU 335 0.0218

GLU 335 GLY 336 0.0001

GLY 336 PHE 337 0.0066

PHE 337 GLU 338 0.0003

GLU 338 TYR 339 -0.0940

TYR 339 ILE 340 -0.0000

ILE 340 ASN 341 -0.0744

ASN 341 PRO 342 -0.0002

PRO 342 LEU 343 -0.0035

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 7 ---

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

* zxy *