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

* *

CA strain for 230101190352136506

--- normal mode 18 ---

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
PHE 1 ASP 2 0.0001

ASP 2 MET 3 0.0049

MET 3 ILE 4 -0.0002

ILE 4 ARG 5 0.0058

ARG 5 LEU 6 0.0000

LEU 6 ALA 7 -0.0268

ALA 7 THR 8 0.0001

THR 8 ASN 9 -0.0015

ASN 9 LYS 10 0.0000

LYS 10 PHE 11 -0.0013

PHE 11 SER 12 0.0000

SER 12 GLU 13 0.0181

GLU 13 ASP 14 -0.0003

ASP 14 ASN 15 0.0155

ASN 15 LYS 16 0.0003

LYS 16 ILE 17 -0.0438

ILE 17 GLY 18 -0.0000

GLY 18 GLU 19 -0.2613

GLU 19 GLY 20 -0.0000

GLY 20 GLY 21 -0.0614

GLY 21 PHE 22 0.0003

PHE 22 GLY 23 -0.1412

GLY 23 ASP 24 0.0000

ASP 24 VAL 25 -0.0700

VAL 25 TYR 26 0.0001

TYR 26 LYS 27 -0.0645

LYS 27 GLY 28 -0.0001

GLY 28 MET 29 -0.0349

MET 29 PHE 30 0.0002

PHE 30 PRO 31 -0.0103

PRO 31 ASN 32 0.0001

ASN 32 GLY 33 -0.0844

GLY 33 TYR 34 -0.0001

TYR 34 GLU 35 -0.0796

GLU 35 ILE 36 0.0001

ILE 36 ALA 37 -0.0424

ALA 37 VAL 38 -0.0003

VAL 38 LYS 39 -0.0116

LYS 39 ARG 40 -0.0005

ARG 40 LEU 41 -0.0738

LEU 41 ILE 42 0.0001

ILE 42 ARG 43 -0.0003

ARG 43 ASN 44 0.0001

ASN 44 SER 45 -0.2036

SER 45 SER 46 -0.0001

SER 46 GLN 47 -0.0044

GLN 47 GLY 48 -0.0002

GLY 48 ALA 49 0.0882

ALA 49 VAL 50 -0.0004

VAL 50 GLU 51 0.0055

GLU 51 PHE 52 0.0001

PHE 52 LYS 53 -0.0019

LYS 53 ASN 54 -0.0001

ASN 54 GLU 55 0.0080

GLU 55 VAL 56 -0.0001

VAL 56 LEU 57 0.0251

LEU 57 LEU 58 -0.0000

LEU 58 ILE 59 0.0680

ILE 59 ALA 60 -0.0001

ALA 60 LYS 61 0.0475

LYS 61 LEU 62 -0.0001

LEU 62 GLN 63 0.0252

GLN 63 HIS 64 0.0001

HIS 64 ARG 65 0.0017

ARG 65 ASN 66 -0.0004

ASN 66 LEU 67 -0.0927

LEU 67 VAL 68 -0.0001

VAL 68 ARG 69 -0.0262

ARG 69 LEU 70 -0.0004

LEU 70 LEU 71 0.0776

LEU 71 GLY 72 0.0001

GLY 72 PHE 73 0.0212

PHE 73 CYS 74 0.0002

CYS 74 ILE 75 0.0077

ILE 75 GLN 76 -0.0000

GLN 76 ARG 77 0.0149

ARG 77 ASN 78 0.0000

ASN 78 GLU 79 -0.0696

GLU 79 LYS 80 0.0002

LYS 80 ILE 81 0.0360

ILE 81 LEU 82 0.0003

LEU 82 ILE 83 0.0240

ILE 83 TYR 84 -0.0002

TYR 84 GLU 85 -0.0369

GLU 85 TYR 86 -0.0003

TYR 86 MET 87 -0.0892

MET 87 HIS 88 -0.0002

HIS 88 ASN 89 -0.0689

ASN 89 LYS 90 -0.0000

LYS 90 SER 91 -0.0505

SER 91 LEU 92 0.0005

LEU 92 ASP 93 0.0263

ASP 93 TYR 94 -0.0000

TYR 94 TYR 95 0.0024

TYR 95 LEU 96 -0.0000

LEU 96 PHE 97 -0.0030

PHE 97 SER 98 0.0001

SER 98 PRO 99 0.0113

PRO 99 GLU 100 0.0001

GLU 100 ASN 101 0.0270

ASN 101 HIS 102 0.0001

HIS 102 ARG 103 -0.0229

ARG 103 LYS 104 0.0003

LYS 104 LEU 105 0.0537

LEU 105 THR 106 -0.0001

THR 106 TRP 107 0.0344

TRP 107 HIS 108 0.0002

HIS 108 ALA 109 -0.0802

ALA 109 ARG 110 -0.0002

ARG 110 TYR 111 0.0504

TYR 111 LYS 112 -0.0000

LYS 112 ILE 113 0.0053

ILE 113 ILE 114 -0.0003

ILE 114 ARG 115 0.0021

ARG 115 GLY 116 0.0002

GLY 116 ILE 117 -0.0533

ILE 117 ALA 118 0.0002

ALA 118 ARG 119 -0.0637

ARG 119 GLY 120 0.0000

GLY 120 ILE 121 0.0276

ILE 121 LEU 122 0.0002

LEU 122 TYR 123 -0.1387

TYR 123 LEU 124 0.0002

LEU 124 HIS 125 0.0198

HIS 125 GLU 126 -0.0001

GLU 126 ASP 127 -0.0195

ASP 127 SER 128 0.0004

SER 128 HIS 129 0.0506

HIS 129 LEU 130 -0.0000

LEU 130 LYS 131 0.0015

LYS 131 ILE 132 -0.0001

ILE 132 ILE 133 0.0382

ILE 133 HIS 134 -0.0005

HIS 134 CYS 135 0.0186

CYS 135 ASP 136 0.0002

ASP 136 LEU 137 -0.0161

LEU 137 LYS 138 -0.0001

LYS 138 PRO 139 -0.0281

PRO 139 SER 140 0.0000

SER 140 ASN 141 0.0355

ASN 141 ILE 142 -0.0001

ILE 142 LEU 143 -0.0398

LEU 143 LEU 144 -0.0001

LEU 144 ASP 145 0.0180

ASP 145 ASP 146 -0.0005

ASP 146 LYS 147 -0.1023

LYS 147 MET 148 -0.0004

MET 148 ASN 149 0.0835

ASN 149 ALA 150 -0.0000

ALA 150 LYS 151 -0.0821

LYS 151 ILE 152 -0.0004

ILE 152 SER 153 -0.1168

SER 153 ASP 154 -0.0003

ASP 154 PHE 155 0.0348

PHE 155 GLY 156 0.0002

GLY 156 LEU 157 0.0289

LEU 157 ALA 158 0.0003

ALA 158 ARG 159 -0.0320

ARG 159 ILE 160 -0.0001

ILE 160 VAL 161 -0.0412

VAL 161 ALA 162 -0.0004

ALA 162 ILE 163 -0.0236

ILE 163 ASP 164 0.0001

ASP 164 GLN 165 -0.0142

GLN 165 MET 166 0.0005

MET 166 GLN 167 -0.0062

GLN 167 GLY 168 -0.0000

GLY 168 ASN 169 0.0179

ASN 169 THR 170 -0.0002

THR 170 SER 171 -0.0542

SER 171 ILE 172 -0.0002

ILE 172 ILE 173 -0.0288

ILE 173 ALA 174 0.0002

ALA 174 GLY 175 -0.0596

GLY 175 THR 176 0.0002

THR 176 TYR 177 0.0911

TYR 177 GLY 178 0.0003

GLY 178 TYR 179 -0.0304

TYR 179 MET 180 0.0001

MET 180 SER 181 0.0191

SER 181 PRO 182 -0.0002

PRO 182 GLU 183 -0.0588

GLU 183 TYR 184 0.0001

TYR 184 ALA 185 0.0411

ALA 185 MET 186 -0.0000

MET 186 LEU 187 0.0015

LEU 187 GLY 188 0.0004

GLY 188 GLN 189 -0.0002

GLN 189 PHE 190 -0.0001

PHE 190 SER 191 0.0258

SER 191 VAL 192 -0.0001

VAL 192 LYS 193 -0.0594

LYS 193 SER 194 0.0000

SER 194 ASP 195 0.0128

ASP 195 VAL 196 -0.0001

VAL 196 PHE 197 0.0027

PHE 197 SER 198 0.0001

SER 198 PHE 199 -0.0060

PHE 199 GLY 200 -0.0001

GLY 200 VAL 201 -0.0049

VAL 201 ILE 202 0.0002

ILE 202 MET 203 -0.0244

MET 203 LEU 204 0.0001

LEU 204 GLU 205 0.0001

GLU 205 ILE 206 0.0001

ILE 206 VAL 207 -0.0149

VAL 207 SER 208 -0.0001

SER 208 GLY 209 0.0154

GLY 209 LYS 210 -0.0000

LYS 210 ARG 211 0.0027

ARG 211 ASN 212 -0.0001

ASN 212 VAL 213 -0.0414

VAL 213 ASP 214 -0.0001

ASP 214 TYR 215 -0.0563

TYR 215 ASN 216 0.0000

ASN 216 GLY 217 -0.2193

GLY 217 VAL 218 -0.0001

VAL 218 ASN 219 -0.0147

ASN 219 SER 220 -0.0003

SER 220 ILE 221 -0.1493

ILE 221 ASP 222 -0.0004

ASP 222 ASP 223 0.0307

ASP 223 LEU 224 0.0002

LEU 224 VAL 225 -0.0286

VAL 225 SER 226 -0.0001

SER 226 HIS 227 -0.0018

HIS 227 ALA 228 0.0002

ALA 228 TRP 229 0.0057

TRP 229 LYS 230 -0.0002

LYS 230 LYS 231 0.0050

LYS 231 TRP 232 0.0001

TRP 232 THR 233 -0.0268

THR 233 GLU 234 0.0002

GLU 234 ASN 235 0.0151

ASN 235 LYS 236 0.0001

LYS 236 GLN 237 -0.0230

GLN 237 MET 238 0.0000

MET 238 GLU 239 -0.0151

GLU 239 LEU 240 0.0004

LEU 240 LEU 241 0.0043

LEU 241 ASP 242 -0.0003

ASP 242 PRO 243 0.0020

PRO 243 ALA 244 0.0003

ALA 244 LEU 245 0.0322

LEU 245 THR 246 0.0002

THR 246 TYR 247 0.0114

TYR 247 SER 248 -0.0001

SER 248 PHE 249 0.0429

PHE 249 SER 250 0.0003

SER 250 GLU 251 -0.0156

GLU 251 THR 252 -0.0001

THR 252 GLU 253 -0.0513

GLU 253 VAL 254 0.0004

VAL 254 SER 255 -0.0054

SER 255 ARG 256 -0.0004

ARG 256 CYS 257 -0.0078

CYS 257 ILE 258 -0.0000

ILE 258 GLN 259 0.0043

GLN 259 LEU 260 -0.0002

LEU 260 GLY 261 0.0050

GLY 261 LEU 262 -0.0000

LEU 262 LEU 263 -0.0123

LEU 263 CYS 264 0.0000

CYS 264 VAL 265 -0.0001

VAL 265 GLN 266 0.0001

GLN 266 GLU 267 0.0526

GLU 267 ASN 268 -0.0000

ASN 268 PRO 269 -0.0376

PRO 269 ASP 270 0.0001

ASP 270 GLN 271 0.0263

GLN 271 ARG 272 0.0005

ARG 272 PRO 273 0.0137

PRO 273 THR 274 0.0002

THR 274 MET 275 -0.0123

MET 275 ALA 276 -0.0001

ALA 276 THR 277 -0.0830

THR 277 ILE 278 0.0000

ILE 278 ALA 279 0.0034

ALA 279 LEU 280 -0.0001

LEU 280 TYR 281 -0.0225

TYR 281 PHE 282 -0.0001

PHE 282 ASN 283 -0.0159

ASN 283 ILE 284 0.0000

ILE 284 ASP 285 0.0186

ASP 285 SER 286 0.0001

SER 286 ILE 287 0.0085

ILE 287 ASP 288 -0.0003

ASP 288 LEU 289 0.0509

LEU 289 PRO 290 -0.0001

PRO 290 LEU 291 -0.0121

LEU 291 PRO 292 0.0000

PRO 292 GLN 293 0.0596

GLN 293 GLN 294 0.0001

GLN 294 PRO 295 0.0175

PRO 295 PRO 296 0.0001

PRO 296 PHE 297 -0.0482

PHE 297 TYR 298 0.0002

TYR 298 MET 299 0.0207

MET 299 ARG 300 -0.0003

ARG 300 GLY 301 -0.0911

GLY 301 LYS 302 0.0001

LYS 302 ILE 303 0.0535

ILE 303 GLU 304 0.0002

GLU 304 SER 305 -0.0498

SER 305 LYS 306 0.0002

LYS 306 VAL 307 0.0557

VAL 307 ALA 308 -0.0002

ALA 308 SER 309 -0.1739

SER 309 LYS 310 -0.0001

LYS 310 LYS 311 -0.1341

LYS 311 THR 312 -0.0001

THR 312 MET 313 0.0613

MET 313 SER 314 -0.0000

SER 314 GLY 315 0.3085

GLY 315 ARG 316 0.0003

ARG 316 PRO 317 0.1230

PRO 317 ARG 318 0.0001

ARG 318 SER 319 -0.1916

SER 319 TYR 320 -0.0000

TYR 320 SER 321 0.0617

SER 321 VAL 322 -0.0000

VAL 322 THR 323 0.0404

THR 323 ARG 324 -0.0001

ARG 324 PHE 325 0.0990

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: October 18th, 2018.

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

*** ***

CA strain for 230101190352136506

--- normal mode 18 ---

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

* *