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

* *

CA strain for 240322152211123579

--- 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
GLU 26 MET 27 -0.0001

MET 27 THR 28 -0.0034

THR 28 ARG 29 -0.0001

ARG 29 ILE 30 -0.0370

ILE 30 GLY 31 0.0001

GLY 31 VAL 32 -0.0185

VAL 32 VAL 33 -0.0000

VAL 33 ARG 34 0.0411

ARG 34 ASN 35 -0.0001

ASN 35 PRO 36 -0.0330

PRO 36 LYS 37 0.0002

LYS 37 SER 38 0.0462

SER 38 HIS 39 0.0002

HIS 39 GLY 40 -0.0696

GLY 40 ASN 41 0.0002

ASN 41 ARG 42 -0.0085

ARG 42 ILE 43 0.0003

ILE 43 ARG 44 -0.0696

ARG 44 PRO 45 -0.0002

PRO 45 PRO 46 -0.0504

PRO 46 GLY 47 0.0004

GLY 47 PRO 48 0.0240

PRO 48 ALA 49 -0.0004

ALA 49 PRO 50 -0.0894

PRO 50 GLU 51 0.0001

GLU 51 ASP 52 0.0388

ASP 52 VAL 53 -0.0002

VAL 53 ARG 54 -0.0208

ARG 54 LEU 55 -0.0003

LEU 55 VAL 56 -0.0644

VAL 56 GLU 57 0.0003

GLU 57 PRO 58 -0.1080

PRO 58 ILE 59 -0.0003

ILE 59 GLY 60 -0.2157

GLY 60 ARG 61 0.0001

ARG 61 GLU 62 -0.0259

GLU 62 ALA 63 0.0000

ALA 63 LEU 64 0.0068

LEU 64 LYS 65 -0.0001

LYS 65 ALA 66 -0.0278

ALA 66 ALA 67 0.0001

ALA 67 LEU 68 0.0115

LEU 68 ASP 69 0.0001

ASP 69 ASP 70 -0.0202

ASP 70 PHE 71 -0.0002

PHE 71 ALA 72 0.0130

ALA 72 ARG 73 -0.0002

ARG 73 THR 74 0.0070

THR 74 GLY 75 0.0001

GLY 75 LEU 76 -0.0156

LEU 76 ASP 77 0.0001

ASP 77 LEU 78 -0.0402

LEU 78 LEU 79 -0.0003

LEU 79 VAL 80 -0.0022

VAL 80 ILE 81 0.0001

ILE 81 ASP 82 0.0476

ASP 82 GLY 83 -0.0002

GLY 83 GLY 84 -0.1142

GLY 84 ASP 85 0.0002

ASP 85 GLY 86 -0.0652

GLY 86 THR 87 -0.0002

THR 87 VAL 88 0.0372

VAL 88 ARG 89 -0.0001

ARG 89 ASP 90 0.0165

ASP 90 VAL 91 -0.0002

VAL 91 ILE 92 0.0013

ILE 92 SER 93 -0.0001

SER 93 LEU 94 -0.0508

LEU 94 LEU 95 0.0002

LEU 95 PRO 96 -0.0003

PRO 96 HIS 97 0.0000

HIS 97 THR 98 -0.0053

THR 98 PHE 99 0.0002

PHE 99 GLY 100 0.0241

GLY 100 GLU 101 -0.0004

GLU 101 ALA 102 0.0583

ALA 102 THR 103 -0.0002

THR 103 PRO 104 0.0682

PRO 104 LEU 105 -0.0002

LEU 105 LEU 106 -0.0072

LEU 106 ALA 107 -0.0003

ALA 107 VAL 108 -0.0295

VAL 108 LEU 109 -0.0005

LEU 109 PRO 110 -0.0176

PRO 110 SER 111 -0.0001

SER 111 GLY 112 -0.1112

GLY 112 LYS 113 -0.0004

LYS 113 THR 114 -0.0154

THR 114 ASN 115 0.0003

ASN 115 VAL 116 -0.0233

VAL 116 LEU 117 -0.0002

LEU 117 ALA 118 -0.0162

ALA 118 ILE 119 -0.0002

ILE 119 ASP 120 0.0360

ASP 120 LEU 121 -0.0002

LEU 121 GLY 122 0.0574

GLY 122 THR 123 -0.0000

THR 123 SER 124 0.0454

SER 124 GLU 125 0.0002

GLU 125 GLY 126 -0.0195

GLY 126 TRP 127 0.0003

TRP 127 ARG 128 0.0774

ARG 128 LEU 129 -0.0001

LEU 129 GLU 130 -0.0743

GLU 130 ASP 131 -0.0000

ASP 131 ALA 132 0.0219

ALA 132 LEU 133 -0.0000

LEU 133 ARG 134 0.0037

ARG 134 ALA 135 0.0002

ALA 135 ALA 136 0.0198

ALA 136 ARG 137 0.0003

ARG 137 ARG 138 -0.0086

ARG 138 GLU 139 -0.0001

GLU 139 ASN 140 0.0523

ASN 140 PRO 141 -0.0001

PRO 141 THR 142 0.1037

THR 142 ILE 143 0.0001

ILE 143 LYS 144 0.2351

LYS 144 SER 145 -0.0002

SER 145 ARG 146 0.1633

ARG 146 PRO 147 -0.0001

PRO 147 PRO 148 0.0357

PRO 148 LEU 149 -0.0004

LEU 149 ARG 150 -0.0271

ARG 150 VAL 151 -0.0001

VAL 151 SER 152 0.0373

SER 152 TRP 153 -0.0003

TRP 153 ALA 154 0.0232

ALA 154 ASP 155 -0.0002

ASP 155 ASP 156 -0.0473

ASP 156 LYS 157 0.0002

LYS 157 PRO 158 -0.0186

PRO 158 CYS 159 0.0000

CYS 159 LEU 160 0.0902

LEU 160 GLN 161 -0.0000

GLN 161 GLY 162 -0.0088

GLY 162 PHE 163 0.0001

PHE 163 PHE 164 0.0123

PHE 164 PHE 165 -0.0003

PHE 165 GLY 166 0.0205

GLY 166 ILE 167 -0.0003

ILE 167 GLY 168 -0.0005

GLY 168 ALA 169 0.0000

ALA 169 PRO 170 0.0275

PRO 170 VAL 171 -0.0002

VAL 171 LYS 172 0.0383

LYS 172 ALA 173 0.0001

ALA 173 THR 174 0.0074

THR 174 ASN 175 -0.0001

ASN 175 LEU 176 0.0644

LEU 176 ALA 177 0.0001

ALA 177 GLN 178 0.0354

GLN 178 ARG 179 -0.0005

ARG 179 VAL 180 -0.0109

VAL 180 HIS 181 0.0000

HIS 181 LYS 182 -0.0349

LYS 182 VAL 183 0.0000

VAL 183 GLY 184 -0.0230

GLY 184 PHE 185 0.0001

PHE 185 PHE 186 -0.1070

PHE 186 HIS 187 -0.0001

HIS 187 ASN 188 0.0225

ASN 188 PHE 189 0.0001

PHE 189 ALA 190 0.0081

ALA 190 VAL 191 -0.0002

VAL 191 ALA 192 0.0080

ALA 192 LEU 193 -0.0002

LEU 193 THR 194 -0.1286

THR 194 ILE 195 0.0001

ILE 195 GLY 196 -0.0101

GLY 196 THR 197 -0.0003

THR 197 ALA 198 0.0091

ALA 198 ALA 199 0.0000

ALA 199 LEU 200 -0.1066

LEU 200 GLY 201 0.0001

GLY 201 ALA 202 -0.0202

ALA 202 LEU 203 -0.0002

LEU 203 PHE 204 0.0335

PHE 204 GLY 205 0.0002

GLY 205 GLY 206 -0.0872

GLY 206 SER 207 -0.0000

SER 207 ARG 208 0.0285

ARG 208 ASP 209 -0.0005

ASP 209 GLU 210 0.0498

GLU 210 TRP 211 -0.0003

TRP 211 ARG 212 -0.0784

ARG 212 GLU 213 -0.0002

GLU 213 GLY 214 -0.0019

GLY 214 VAL 215 0.0000

VAL 215 PRO 216 -0.0170

PRO 216 ALA 217 -0.0001

ALA 217 ARG 218 -0.0028

ARG 218 LEU 219 0.0000

LEU 219 VAL 220 -0.0020

VAL 220 LEU 221 0.0002

LEU 221 ASP 222 -0.0210

ASP 222 GLY 223 -0.0002

GLY 223 GLU 224 -0.0070

GLU 224 ALA 225 -0.0001

ALA 225 GLN 226 0.0040

GLN 226 GLY 227 0.0002

GLY 227 GLU 228 0.0103

GLU 228 GLY 229 0.0002

GLY 229 HIS 230 -0.0401

HIS 230 ARG 231 -0.0002

ARG 231 PHE 232 -0.0133

PHE 232 ALA 233 -0.0001

ALA 233 VAL 234 0.0517

VAL 234 ILE 235 -0.0003

ILE 235 ALA 236 0.0692

ALA 236 THR 237 -0.0001

THR 237 ALA 238 0.0874

ALA 238 LEU 239 -0.0001

LEU 239 LYS 240 -0.0636

LYS 240 ARG 241 0.0001

ARG 241 LEU 242 -0.0385

LEU 242 PRO 243 0.0001

PRO 243 PHE 244 0.0302

PHE 244 GLY 245 -0.0003

GLY 245 LEU 246 -0.0124

LEU 246 LYS 247 -0.0002

LYS 247 PRO 248 -0.0018

PRO 248 PHE 249 -0.0002

PHE 249 GLY 250 0.0028

GLY 250 ALA 251 -0.0003

ALA 251 PRO 252 0.1145

PRO 252 ARG 253 -0.0001

ARG 253 GLU 254 -0.0083

GLU 254 GLY 255 0.0001

GLY 255 LEU 256 0.0879

LEU 256 LYS 257 0.0000

LYS 257 LEU 258 0.1146

LEU 258 LEU 259 0.0000

LEU 259 ASP 260 0.0445

ASP 260 VAL 261 0.0001

VAL 261 ASP 262 0.0248

ASP 262 ALA 263 -0.0000

ALA 263 PRO 264 -0.0239

PRO 264 PRO 265 -0.0005

PRO 265 ARG 266 -0.0403

ARG 266 ARG 267 0.0000

ARG 267 LEU 268 0.0036

LEU 268 HIS 269 0.0001

HIS 269 LYS 270 0.0372

LYS 270 ALA 271 -0.0001

ALA 271 LEU 272 -0.0087

LEU 272 PRO 273 0.0001

PRO 273 LEU 274 0.0212

LEU 274 MET 275 0.0002

MET 275 LEU 276 0.0008

LEU 276 SER 277 0.0000

SER 277 GLY 278 0.0019

GLY 278 LYS 279 -0.0004

LYS 279 VAL 280 0.0197

VAL 280 VAL 281 -0.0000

VAL 281 PRO 282 0.0036

PRO 282 ALA 283 -0.0001

ALA 283 LEU 284 0.0088

LEU 284 GLU 285 0.0002

GLU 285 GLY 286 0.0142

GLY 286 LEU 287 -0.0002

LEU 287 GLY 288 -0.0034

GLY 288 TYR 289 0.0002

TYR 289 ARG 290 0.0461

ARG 290 ARG 291 0.0002

ARG 291 ARG 292 -0.0343

ARG 292 ASP 293 -0.0003

ASP 293 PRO 294 0.0070

PRO 294 ARG 295 0.0001

ARG 295 SER 296 0.0027

SER 296 VAL 297 -0.0001

VAL 297 LYS 298 0.0256

LYS 298 LEU 299 0.0001

LEU 299 SER 300 0.0415

SER 300 GLY 301 -0.0000

GLY 301 GLY 302 -0.0404

GLY 302 ALA 303 -0.0001

ALA 303 PRO 304 -0.0464

PRO 304 PHE 305 -0.0001

PHE 305 VAL 306 -0.0548

VAL 306 LEU 307 -0.0002

LEU 307 ASP 308 -0.1112

ASP 308 GLY 309 -0.0001

GLY 309 GLU 310 -0.0509

GLU 310 VAL 311 -0.0004

VAL 311 TYR 312 0.1986

TYR 312 GLU 313 0.0001

GLU 313 GLY 314 -0.0767

GLY 314 GLY 315 0.0000

GLY 315 ASP 316 0.0021

ASP 316 LEU 317 0.0000

LEU 317 THR 318 0.0860

THR 318 ILE 319 0.0002

ILE 319 GLN 320 0.1232

GLN 320 LEU 321 -0.0006

LEU 321 GLY 322 0.0264

GLY 322 PRO 323 -0.0002

PRO 323 ALA 324 0.1368

ALA 324 LEU 325 -0.0002

LEU 325 ARG 326 0.1755

ARG 326 PHE 327 0.0005

PHE 327 LEU 328 0.1432

LEU 328 VAL 329 -0.0001

VAL 329 GLY 330 0.0281

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.

*** ***

CA strain for 240322152211123579

--- normal mode 10 ---

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

* *