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

* taherm *

CA strain for 2504072114572541312

--- normal mode 8 ---

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
GLY 2 GLU 3 -0.0001

GLU 3 THR 4 -0.0013

THR 4 PHE 5 0.0002

PHE 5 ARG 6 -0.0255

ARG 6 LEU 7 -0.0002

LEU 7 GLY 8 0.0249

GLY 8 VAL 9 -0.0002

VAL 9 LEU 10 0.0783

LEU 10 PRO 11 0.0002

PRO 11 PHE 12 0.0999

PHE 12 GLY 13 0.0002

GLY 13 THR 14 -0.0533

THR 14 ALA 15 0.0000

ALA 15 SER 16 0.0319

SER 16 SER 16 0.1075

SER 16 TRP 17 -0.0003

TRP 17 GLU 18 -0.0150

GLU 18 ALA 19 0.0000

ALA 19 ALA 20 0.0614

ALA 20 VAL 21 -0.0002

VAL 21 ILE 22 -0.0130

ILE 22 LYS 23 -0.0002

LYS 23 ALA 24 -0.0254

ALA 24 ARG 25 0.0000

ARG 25 GLY 26 -0.0497

GLY 26 PHE 27 -0.0001

PHE 27 ASP 28 -0.0670

ASP 28 THR 29 0.0001

THR 29 ALA 30 -0.0046

ALA 30 ASN 31 -0.0002

ASN 31 GLY 32 -0.0162

GLY 32 PHE 33 0.0002

PHE 33 THR 34 0.0113

THR 34 LEU 35 -0.0000

LEU 35 ASP 36 -0.0957

ASP 36 ILE 37 0.0002

ILE 37 VAL 38 -0.1457

VAL 38 LYS 39 -0.0001

LYS 39 LEU 40 -0.1678

LEU 40 ALA 41 0.0001

ALA 41 GLY 42 -0.1354

GLY 42 ASN 43 0.0002

ASN 43 ASP 44 0.0710

ASP 44 ALA 45 0.0001

ALA 45 ALA 46 -0.0616

ALA 46 ARG 47 0.0001

ARG 47 ILE 48 -0.0894

ILE 48 ALA 49 0.0001

ALA 49 PHE 50 0.0078

PHE 50 LEU 51 -0.0001

LEU 51 GLY 52 -0.1074

GLY 52 GLY 53 0.0001

GLY 53 GLN 54 -0.0336

GLN 54 VAL 55 -0.0001

VAL 55 ASP 56 0.0694

ASP 56 ALA 57 -0.0001

ALA 57 ILE 58 0.0153

ILE 58 VAL 59 0.0002

VAL 59 GLY 60 -0.1671

GLY 60 ASP 61 -0.0001

ASP 61 LEU 62 -0.0083

LEU 62 ILE 63 -0.0001

ILE 63 PHE 64 -0.1488

PHE 64 ALA 65 0.0003

ALA 65 ALA 66 -0.0246

ALA 66 ARG 67 -0.0001

ARG 67 ARG 67 0.0596

ARG 67 LEU 68 -0.1215

LEU 68 GLY 69 -0.0000

GLY 69 ASN 70 -0.0091

ASN 70 ASN 70 0.0182

ASN 70 GLU 71 -0.0002

GLU 71 GLY 72 0.0871

GLY 72 ARG 73 -0.0003

ARG 73 GLY 74 -0.0173

GLY 74 VAL 75 0.0000

VAL 75 ARG 76 0.0058

ARG 76 ARG 76 0.0572

ARG 76 PHE 77 -0.0002

PHE 77 SER 78 -0.0112

SER 78 SER 78 -0.0051

SER 78 PRO 79 0.0004

PRO 79 TYR 80 0.0085

TYR 80 SER 81 -0.0002

SER 81 THR 82 0.1358

THR 82 THR 83 -0.0000

THR 83 GLU 84 0.0975

GLU 84 GLY 85 -0.0000

GLY 85 ALA 86 -0.0115

ALA 86 LEU 87 -0.0001

LEU 87 MET 88 -0.0525

MET 88 VAL 89 0.0001

VAL 89 PRO 90 -0.0236

PRO 90 ALA 91 -0.0001

ALA 91 GLY 92 0.0412

GLY 92 SER 93 -0.0002

SER 93 PRO 94 -0.0096

PRO 94 ILE 95 0.0001

ILE 95 THR 96 0.0142

THR 96 ASP 97 -0.0002

ASP 97 LEU 98 -0.0938

LEU 98 LYS 99 0.0001

LYS 99 GLY 100 -0.0705

GLY 100 LEU 101 0.0000

LEU 101 ALA 102 0.0546

ALA 102 GLY 103 -0.0001

GLY 103 LYS 104 -0.0158

LYS 104 ARG 105 0.0003

ARG 105 LEU 106 0.0422

LEU 106 GLY 107 -0.0002

GLY 107 VAL 108 0.0997

VAL 108 ALA 109 -0.0003

ALA 109 GLY 110 -0.0001

GLY 110 GLY 111 0.0002

GLY 111 ALA 112 -0.0895

ALA 112 LEU 113 -0.0001

LEU 113 ASP 114 -0.0266

ASP 114 LYS 115 -0.0001

LYS 115 ASN 116 0.0336

ASN 116 TRP 117 0.0001

TRP 117 ILE 118 0.0891

ILE 118 LEU 119 0.0002

LEU 119 LEU 119 0.0116

LEU 119 LEU 120 -0.0088

LEU 120 ARG 121 0.0000

ARG 121 ALA 122 -0.0280

ALA 122 GLN 123 0.0001

GLN 123 ALA 124 0.0427

ALA 124 ARG 125 -0.0003

ARG 125 GLU 126 0.0718

GLU 126 THR 127 -0.0003

THR 127 ALA 128 0.0008

ALA 128 GLY 129 -0.0003

GLY 129 LEU 130 -0.0203

LEU 130 GLU 131 0.0002

GLU 131 LEU 132 -0.0063

LEU 132 GLU 133 0.0002

GLU 133 ASN 134 -0.0373

ASN 134 VAL 135 0.0000

VAL 135 ALA 136 -0.0417

ALA 136 GLN 137 0.0001

GLN 137 ILE 138 -0.0149

ILE 138 ALA 139 0.0004

ALA 139 TYR 140 -0.0001

TYR 140 GLY 141 0.0000

GLY 141 ALA 142 -0.3853

ALA 142 PRO 143 0.0002

PRO 143 PRO 144 0.0469

PRO 144 LEU 145 -0.0002

LEU 145 LEU 146 -0.0450

LEU 146 ALA 147 0.0001

ALA 147 GLN 148 -0.0997

GLN 148 LYS 149 0.0001

LYS 149 LEU 150 -0.0015

LEU 150 GLU 151 0.0001

GLU 151 THR 152 -0.1312

THR 152 GLY 153 -0.0001

GLY 153 GLU 154 0.0042

GLU 154 LEU 155 -0.0001

LEU 155 ASP 156 -0.0433

ASP 156 ALA 157 -0.0001

ALA 157 ALA 158 0.0224

ALA 158 LEU 159 -0.0003

LEU 159 LEU 160 -0.0561

LEU 160 TRP 161 0.0000

TRP 161 TRP 162 0.0747

TRP 162 GLN 163 -0.0003

GLN 163 PHE 164 -0.1556

PHE 164 ALA 165 0.0001

ALA 165 ALA 166 0.0930

ALA 166 ARG 167 -0.0002

ARG 167 LEU 168 -0.1000

LEU 168 GLU 169 0.0001

GLU 169 ALA 170 -0.0155

ALA 170 LYS 171 0.0000

LYS 171 GLY 172 -0.0478

GLY 172 PHE 173 -0.0000

PHE 173 LYS 174 -0.1102

LYS 174 ARG 175 -0.0002

ARG 175 LEU 176 0.1969

LEU 176 ILE 177 -0.0002

ILE 177 SER 178 0.0115

SER 178 ALA 179 -0.0002

ALA 179 ASP 180 0.0249

ASP 180 ASP 181 -0.0000

ASP 181 VAL 182 0.0530

VAL 182 MET 183 -0.0003

MET 183 ARG 184 0.0362

ARG 184 ARG 184 -0.0705

ARG 184 ALA 185 0.0001

ALA 185 PHE 186 0.0018

PHE 186 GLY 187 0.0002

GLY 187 ALA 188 0.1156

ALA 188 LYS 189 -0.0000

LYS 189 GLY 190 0.0843

GLY 190 ALA 191 0.0002

ALA 191 VAL 192 0.0407

VAL 192 SER 193 -0.0001

SER 193 SER 193 0.0115

SER 193 LEU 194 0.0267

LEU 194 ILE 195 0.0003

ILE 195 ILE 195 0.0000

ILE 195 GLY 196 0.0586

GLY 196 TYR 197 -0.0000

TYR 197 LEU 198 -0.0373

LEU 198 TYR 199 0.0004

TYR 199 GLU 200 0.0167

GLU 200 GLY 201 -0.0006

GLY 201 HIS 202 -0.1303

HIS 202 THR 203 0.0002

THR 203 VAL 204 0.0175

VAL 204 ALA 205 0.0000

ALA 205 ASP 206 -0.0054

ASP 206 ARG 207 0.0003

ARG 207 GLY 208 0.0574

GLY 208 GLU 209 -0.0003

GLU 209 VAL 210 0.0510

VAL 210 VAL 211 0.0002

VAL 211 ARG 212 0.0080

ARG 212 GLY 213 -0.0000

GLY 213 PHE 214 0.0573

PHE 214 ALA 215 -0.0001

ALA 215 ARG 216 0.0994

ARG 216 ALA 217 -0.0000

ALA 217 SER 218 0.0630

SER 218 ALA 219 -0.0004

ALA 219 ALA 220 0.0822

ALA 220 ALA 221 -0.0001

ALA 221 LYS 222 0.1573

LYS 222 ASP 223 -0.0003

ASP 223 ALA 224 0.1040

ALA 224 LEU 225 0.0003

LEU 225 ALA 226 0.0877

ALA 226 ASN 227 -0.0003

ASN 227 GLU 228 0.0660

GLU 228 PRO 229 -0.0002

PRO 229 ALA 230 0.0484

ALA 230 LEU 231 0.0001

LEU 231 TRP 232 -0.0198

TRP 232 GLU 233 -0.0002

GLU 233 THR 234 -0.0142

THR 234 VAL 235 0.0000

VAL 235 ARG 236 0.0393

ARG 236 PRO 237 -0.0000

PRO 237 LEU 238 0.0197

LEU 238 MET 239 -0.0001

MET 239 ALA 240 0.0615

ALA 240 ALA 241 0.0001

ALA 241 GLU 242 -0.0326

GLU 242 ASP 243 0.0001

ASP 243 ASP 244 -0.0311

ASP 244 ALA 245 0.0002

ALA 245 THR 246 0.0332

THR 246 PHE 247 -0.0000

PHE 247 ALA 248 0.0184

ALA 248 THR 249 -0.0002

THR 249 LEU 250 0.0179

LEU 250 LYS 251 -0.0003

LYS 251 ARG 252 0.0701

ARG 252 ASP 253 -0.0001

ASP 253 PHE 254 -0.0138

PHE 254 LEU 255 -0.0002

LEU 255 ALA 256 0.2134

ALA 256 GLY 257 0.0000

GLY 257 ILE 258 0.0526

ILE 258 PRO 259 0.0003

PRO 259 ARG 260 0.0048

ARG 260 ARG 261 0.0004

ARG 261 PRO 262 -0.1425

PRO 262 ILE 263 -0.0001

ILE 263 ALA 264 0.0626

ALA 264 ALA 265 -0.0003

ALA 265 GLU 266 -0.0496

GLU 266 ARG 267 0.0002

ARG 267 ALA 268 -0.0142

ALA 268 ASP 269 0.0000

ASP 269 GLY 270 -0.0134

GLY 270 GLU 271 -0.0006

GLU 271 ARG 272 -0.0279

ARG 272 ILE 273 -0.0006

ILE 273 TYR 274 -0.0439

TYR 274 TYR 274 0.0059

TYR 274 ALA 275 -0.0002

ALA 275 ALA 275 -0.0034

ALA 275 ALA 276 -0.0702

ALA 276 ALA 276 -0.0009

ALA 276 LEU 277 0.0001

LEU 277 LEU 277 0.0005

LEU 277 ASP 278 -0.0079

ASP 278 ASP 278 0.0000

ASP 278 ARG 279 -0.0001

ARG 279 ARG 279 -0.0001

ARG 279 LEU 280 0.0022

LEU 280 LEU 280 -0.0000

LEU 280 ALA 281 -0.0001

ALA 281 ALA 281 -0.0000

ALA 281 GLY 282 -0.0110

GLY 282 GLY 282 -0.0002

GLY 282 ALA 283 -0.0002

ALA 283 ALA 283 -0.0003

ALA 283 GLN 284 0.0227

GLN 284 GLN 284 -0.0000

GLN 284 LEU 285 -0.0001

LEU 285 LEU 285 0.0002

LEU 285 LEU 286 0.0279

LEU 286 LEU 286 0.0000

LEU 286 GLY 287 0.0001

GLY 287 GLY 287 0.0001

GLY 287 VAL 288 -0.0149

VAL 288 VAL 288 0.0000

VAL 288 GLY 289 0.0003

GLY 289 GLY 289 0.0006

GLY 289 LYS 290 -0.0466

LYS 290 LYS 290 -0.0035

LYS 290 SER 291 -0.0001

SER 291 SER 291 0.0041

SER 291 LEU 292 0.0719

LEU 292 PRO 293 0.0002

PRO 293 PRO 294 0.0653

PRO 294 ASP 295 -0.0001

ASP 295 LEU 296 -0.0203

LEU 296 TYR 297 0.0002

TYR 297 LEU 298 0.1411

LEU 298 ASP 299 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 8th, 2025.

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

*** taherm ***

CA strain for 2504072114572541312

--- normal mode 8 ---

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

* taherm *