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

* taherm *

CA strain for 2504072114572541312

--- 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
GLY 2 GLU 3 0.0001

GLU 3 THR 4 -0.0736

THR 4 PHE 5 -0.0002

PHE 5 ARG 6 -0.1047

ARG 6 LEU 7 -0.0001

LEU 7 GLY 8 -0.0783

GLY 8 VAL 9 -0.0001

VAL 9 LEU 10 -0.1472

LEU 10 PRO 11 0.0002

PRO 11 PHE 12 -0.0944

PHE 12 GLY 13 0.0002

GLY 13 THR 14 -0.0422

THR 14 ALA 15 -0.0002

ALA 15 SER 16 0.0838

SER 16 SER 16 0.0269

SER 16 TRP 17 -0.0001

TRP 17 GLU 18 -0.1246

GLU 18 ALA 19 0.0000

ALA 19 ALA 20 0.1580

ALA 20 VAL 21 0.0001

VAL 21 ILE 22 -0.0823

ILE 22 LYS 23 0.0004

LYS 23 ALA 24 0.2998

ALA 24 ARG 25 -0.0002

ARG 25 GLY 26 -0.1307

GLY 26 PHE 27 -0.0001

PHE 27 ASP 28 -0.0491

ASP 28 THR 29 -0.0000

THR 29 ALA 30 0.0356

ALA 30 ASN 31 -0.0000

ASN 31 GLY 32 -0.1136

GLY 32 PHE 33 0.0002

PHE 33 THR 34 -0.0135

THR 34 LEU 35 0.0001

LEU 35 ASP 36 -0.0991

ASP 36 ILE 37 0.0003

ILE 37 VAL 38 0.0069

VAL 38 LYS 39 0.0003

LYS 39 LEU 40 -0.1510

LEU 40 ALA 41 -0.0001

ALA 41 GLY 42 -0.2347

GLY 42 ASN 43 -0.0003

ASN 43 ASP 44 0.0751

ASP 44 ALA 45 -0.0002

ALA 45 ALA 46 -0.0137

ALA 46 ARG 47 0.0001

ARG 47 ILE 48 0.0400

ILE 48 ALA 49 -0.0000

ALA 49 PHE 50 -0.0521

PHE 50 LEU 51 -0.0004

LEU 51 GLY 52 -0.0453

GLY 52 GLY 53 -0.0003

GLY 53 GLN 54 0.0246

GLN 54 VAL 55 0.0003

VAL 55 ASP 56 -0.0518

ASP 56 ALA 57 -0.0000

ALA 57 ILE 58 -0.0327

ILE 58 VAL 59 0.0000

VAL 59 GLY 60 0.0014

GLY 60 ASP 61 -0.0001

ASP 61 LEU 62 0.0114

LEU 62 ILE 63 -0.0005

ILE 63 PHE 64 0.0082

PHE 64 ALA 65 -0.0002

ALA 65 ALA 66 0.0504

ALA 66 ARG 67 0.0002

ARG 67 ARG 67 0.1028

ARG 67 LEU 68 0.1601

LEU 68 GLY 69 0.0000

GLY 69 ASN 70 0.1176

ASN 70 ASN 70 0.0393

ASN 70 GLU 71 -0.0002

GLU 71 GLY 72 0.1620

GLY 72 ARG 73 0.0002

ARG 73 GLY 74 0.0887

GLY 74 VAL 75 0.0003

VAL 75 ARG 76 -0.0116

ARG 76 ARG 76 -0.1163

ARG 76 PHE 77 -0.0002

PHE 77 SER 78 0.0187

SER 78 SER 78 0.0280

SER 78 PRO 79 -0.0006

PRO 79 TYR 80 0.1514

TYR 80 SER 81 -0.0002

SER 81 THR 82 -0.0734

THR 82 THR 83 0.0001

THR 83 GLU 84 -0.0588

GLU 84 GLY 85 -0.0001

GLY 85 ALA 86 0.0732

ALA 86 LEU 87 -0.0002

LEU 87 MET 88 0.0206

MET 88 VAL 89 0.0003

VAL 89 PRO 90 0.0757

PRO 90 ALA 91 -0.0003

ALA 91 GLY 92 -0.1662

GLY 92 SER 93 -0.0002

SER 93 PRO 94 0.0076

PRO 94 ILE 95 0.0004

ILE 95 THR 96 0.0586

THR 96 ASP 97 -0.0003

ASP 97 LEU 98 0.1670

LEU 98 LYS 99 0.0001

LYS 99 GLY 100 0.0144

GLY 100 LEU 101 0.0004

LEU 101 ALA 102 -0.1181

ALA 102 GLY 103 -0.0002

GLY 103 LYS 104 -0.0619

LYS 104 ARG 105 -0.0001

ARG 105 LEU 106 0.0276

LEU 106 GLY 107 0.0002

GLY 107 VAL 108 0.0752

VAL 108 ALA 109 0.0004

ALA 109 GLY 110 0.0705

GLY 110 GLY 111 -0.0003

GLY 111 ALA 112 -0.0746

ALA 112 LEU 113 0.0003

LEU 113 ASP 114 -0.1001

ASP 114 LYS 115 -0.0004

LYS 115 ASN 116 0.0457

ASN 116 TRP 117 0.0002

TRP 117 ILE 118 -0.0447

ILE 118 LEU 119 -0.0000

LEU 119 LEU 119 -0.0117

LEU 119 LEU 120 0.0497

LEU 120 ARG 121 -0.0000

ARG 121 ALA 122 -0.0258

ALA 122 GLN 123 0.0004

GLN 123 ALA 124 -0.0587

ALA 124 ARG 125 0.0000

ARG 125 GLU 126 -0.0573

GLU 126 THR 127 -0.0001

THR 127 ALA 128 -0.0488

ALA 128 GLY 129 0.0001

GLY 129 LEU 130 -0.0644

LEU 130 GLU 131 0.0000

GLU 131 LEU 132 -0.0511

LEU 132 GLU 133 0.0002

GLU 133 ASN 134 0.1298

ASN 134 VAL 135 0.0001

VAL 135 ALA 136 -0.0650

ALA 136 GLN 137 -0.0001

GLN 137 ILE 138 0.1139

ILE 138 ALA 139 -0.0001

ALA 139 TYR 140 0.0884

TYR 140 GLY 141 -0.0003

GLY 141 ALA 142 0.0712

ALA 142 PRO 143 0.0001

PRO 143 PRO 144 -0.0284

PRO 144 LEU 145 0.0003

LEU 145 LEU 146 -0.0060

LEU 146 ALA 147 0.0002

ALA 147 GLN 148 -0.0021

GLN 148 LYS 149 -0.0003

LYS 149 LEU 150 0.0488

LEU 150 GLU 151 -0.0001

GLU 151 THR 152 0.0142

THR 152 GLY 153 -0.0000

GLY 153 GLU 154 -0.0091

GLU 154 LEU 155 0.0001

LEU 155 ASP 156 0.0977

ASP 156 ALA 157 0.0005

ALA 157 ALA 158 0.0124

ALA 158 LEU 159 0.0002

LEU 159 LEU 160 -0.1501

LEU 160 TRP 161 -0.0002

TRP 161 TRP 162 -0.0702

TRP 162 GLN 163 -0.0002

GLN 163 PHE 164 -0.0681

PHE 164 ALA 165 0.0001

ALA 165 ALA 166 -0.1958

ALA 166 ARG 167 0.0003

ARG 167 LEU 168 -0.3808

LEU 168 GLU 169 -0.0001

GLU 169 ALA 170 -0.0970

ALA 170 LYS 171 0.0001

LYS 171 GLY 172 -0.1908

GLY 172 PHE 173 0.0001

PHE 173 LYS 174 0.1032

LYS 174 ARG 175 -0.0003

ARG 175 LEU 176 -0.3929

LEU 176 ILE 177 0.0000

ILE 177 SER 178 -0.0505

SER 178 ALA 179 0.0003

ALA 179 ASP 180 -0.0192

ASP 180 ASP 181 -0.0000

ASP 181 VAL 182 -0.0443

VAL 182 MET 183 -0.0002

MET 183 ARG 184 -0.0090

ARG 184 ARG 184 0.0568

ARG 184 ALA 185 -0.0000

ALA 185 PHE 186 -0.0281

PHE 186 GLY 187 0.0001

GLY 187 ALA 188 -0.0498

ALA 188 LYS 189 0.0000

LYS 189 GLY 190 0.0272

GLY 190 ALA 191 0.0001

ALA 191 VAL 192 -0.0387

VAL 192 SER 193 0.0003

SER 193 SER 193 0.0058

SER 193 LEU 194 -0.0015

LEU 194 ILE 195 0.0000

ILE 195 ILE 195 0.0000

ILE 195 GLY 196 -0.0051

GLY 196 TYR 197 0.0003

TYR 197 LEU 198 -0.0010

LEU 198 TYR 199 0.0002

TYR 199 GLU 200 -0.0453

GLU 200 GLY 201 -0.0003

GLY 201 HIS 202 0.0860

HIS 202 THR 203 -0.0000

THR 203 VAL 204 0.0130

VAL 204 ALA 205 -0.0001

ALA 205 ASP 206 -0.0023

ASP 206 ARG 207 0.0001

ARG 207 GLY 208 0.0098

GLY 208 GLU 209 0.0003

GLU 209 VAL 210 0.0328

VAL 210 VAL 211 -0.0001

VAL 211 ARG 212 0.0568

ARG 212 GLY 213 0.0001

GLY 213 PHE 214 0.0186

PHE 214 ALA 215 0.0001

ALA 215 ARG 216 0.2252

ARG 216 ALA 217 0.0003

ALA 217 SER 218 -0.0281

SER 218 ALA 219 0.0003

ALA 219 ALA 220 0.1202

ALA 220 ALA 221 -0.0002

ALA 221 LYS 222 0.0606

LYS 222 ASP 223 -0.0004

ASP 223 ALA 224 0.0266

ALA 224 LEU 225 0.0001

LEU 225 ALA 226 0.0744

ALA 226 ASN 227 -0.0002

ASN 227 GLU 228 -0.0050

GLU 228 PRO 229 -0.0001

PRO 229 ALA 230 0.0279

ALA 230 LEU 231 -0.0002

LEU 231 TRP 232 -0.1881

TRP 232 GLU 233 0.0000

GLU 233 THR 234 -0.0716

THR 234 VAL 235 -0.0003

VAL 235 ARG 236 -0.1457

ARG 236 PRO 237 0.0001

PRO 237 LEU 238 0.1862

LEU 238 MET 239 0.0002

MET 239 ALA 240 0.0857

ALA 240 ALA 241 -0.0001

ALA 241 GLU 242 0.1088

GLU 242 ASP 243 0.0003

ASP 243 ASP 244 -0.0146

ASP 244 ALA 245 -0.0001

ALA 245 THR 246 0.1470

THR 246 PHE 247 0.0003

PHE 247 ALA 248 0.0954

ALA 248 THR 249 0.0000

THR 249 LEU 250 -0.0068

LEU 250 LYS 251 0.0004

LYS 251 ARG 252 0.0413

ARG 252 ASP 253 0.0002

ASP 253 PHE 254 -0.1005

PHE 254 LEU 255 -0.0000

LEU 255 ALA 256 -0.0733

ALA 256 GLY 257 0.0001

GLY 257 ILE 258 -0.0369

ILE 258 PRO 259 -0.0004

PRO 259 ARG 260 0.0112

ARG 260 ARG 261 -0.0000

ARG 261 PRO 262 -0.0163

PRO 262 ILE 263 0.0001

ILE 263 ALA 264 0.0330

ALA 264 ALA 265 -0.0001

ALA 265 GLU 266 0.0378

GLU 266 ARG 267 -0.0001

ARG 267 ALA 268 0.0362

ALA 268 ASP 269 0.0002

ASP 269 GLY 270 -0.0229

GLY 270 GLU 271 0.0001

GLU 271 ARG 272 0.0155

ARG 272 ILE 273 -0.0000

ILE 273 TYR 274 -0.0514

TYR 274 TYR 274 -0.0115

TYR 274 ALA 275 0.0002

ALA 275 ALA 275 0.0098

ALA 275 ALA 276 0.0027

ALA 276 ALA 276 0.0000

ALA 276 LEU 277 0.0002

LEU 277 LEU 277 0.0011

LEU 277 ASP 278 -0.0143

ASP 278 ASP 278 0.0002

ASP 278 ARG 279 -0.0005

ARG 279 ARG 279 -0.0003

ARG 279 LEU 280 -0.0103

LEU 280 LEU 280 -0.0002

LEU 280 ALA 281 -0.0002

ALA 281 ALA 281 -0.0001

ALA 281 GLY 282 0.0075

GLY 282 GLY 282 -0.0001

GLY 282 ALA 283 -0.0002

ALA 283 ALA 283 -0.0001

ALA 283 GLN 284 0.0335

GLN 284 GLN 284 -0.0002

GLN 284 LEU 285 -0.0003

LEU 285 LEU 285 -0.0001

LEU 285 LEU 286 -0.1096

LEU 286 LEU 286 -0.0002

LEU 286 GLY 287 0.0003

GLY 287 GLY 287 0.0001

GLY 287 VAL 288 -0.0225

VAL 288 VAL 288 0.0001

VAL 288 GLY 289 0.0001

GLY 289 GLY 289 0.0000

GLY 289 LYS 290 0.0143

LYS 290 LYS 290 0.0044

LYS 290 SER 291 -0.0001

SER 291 SER 291 0.0026

SER 291 LEU 292 0.1505

LEU 292 PRO 293 -0.0003

PRO 293 PRO 294 0.1516

PRO 294 ASP 295 0.0000

ASP 295 LEU 296 -0.0934

LEU 296 TYR 297 0.0004

TYR 297 LEU 298 0.3210

LEU 298 ASP 299 -0.0000

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 9 ---

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

* taherm *