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

* *

CA strain for 230101190352136506

--- normal mode 21 ---

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 -0.0000

ASP 2 MET 3 0.0193

MET 3 ILE 4 0.0001

ILE 4 ARG 5 0.0007

ARG 5 LEU 6 -0.0002

LEU 6 ALA 7 0.0232

ALA 7 THR 8 -0.0001

THR 8 ASN 9 0.0166

ASN 9 LYS 10 -0.0000

LYS 10 PHE 11 -0.0065

PHE 11 SER 12 -0.0001

SER 12 GLU 13 -0.0149

GLU 13 ASP 14 0.0004

ASP 14 ASN 15 0.0077

ASN 15 LYS 16 -0.0005

LYS 16 ILE 17 0.0268

ILE 17 GLY 18 -0.0001

GLY 18 GLU 19 0.0393

GLU 19 GLY 20 0.0001

GLY 20 GLY 21 -0.0015

GLY 21 PHE 22 -0.0002

PHE 22 GLY 23 -0.0064

GLY 23 ASP 24 0.0003

ASP 24 VAL 25 0.0071

VAL 25 TYR 26 -0.0003

TYR 26 LYS 27 -0.0117

LYS 27 GLY 28 -0.0003

GLY 28 MET 29 -0.0334

MET 29 PHE 30 -0.0001

PHE 30 PRO 31 0.0043

PRO 31 ASN 32 0.0001

ASN 32 GLY 33 -0.0082

GLY 33 TYR 34 0.0000

TYR 34 GLU 35 -0.0008

GLU 35 ILE 36 0.0000

ILE 36 ALA 37 -0.0100

ALA 37 VAL 38 0.0004

VAL 38 LYS 39 -0.0171

LYS 39 ARG 40 0.0002

ARG 40 LEU 41 0.0080

LEU 41 ILE 42 -0.0002

ILE 42 ARG 43 -0.0064

ARG 43 ASN 44 -0.0000

ASN 44 SER 45 0.0265

SER 45 SER 46 0.0000

SER 46 GLN 47 -0.0371

GLN 47 GLY 48 0.0002

GLY 48 ALA 49 -0.0130

ALA 49 VAL 50 -0.0000

VAL 50 GLU 51 0.0281

GLU 51 PHE 52 -0.0001

PHE 52 LYS 53 -0.0047

LYS 53 ASN 54 -0.0001

ASN 54 GLU 55 0.0001

GLU 55 VAL 56 0.0001

VAL 56 LEU 57 0.0149

LEU 57 LEU 58 -0.0003

LEU 58 ILE 59 -0.0109

ILE 59 ALA 60 0.0004

ALA 60 LYS 61 0.0260

LYS 61 LEU 62 -0.0002

LEU 62 GLN 63 -0.0400

GLN 63 HIS 64 0.0000

HIS 64 ARG 65 -0.0877

ARG 65 ASN 66 0.0001

ASN 66 LEU 67 -0.0236

LEU 67 VAL 68 -0.0001

VAL 68 ARG 69 0.0028

ARG 69 LEU 70 -0.0004

LEU 70 LEU 71 0.0142

LEU 71 GLY 72 -0.0003

GLY 72 PHE 73 0.0033

PHE 73 CYS 74 0.0000

CYS 74 ILE 75 0.0101

ILE 75 GLN 76 -0.0003

GLN 76 ARG 77 0.0017

ARG 77 ASN 78 -0.0001

ASN 78 GLU 79 -0.0032

GLU 79 LYS 80 -0.0003

LYS 80 ILE 81 -0.0093

ILE 81 LEU 82 0.0001

LEU 82 ILE 83 -0.0263

ILE 83 TYR 84 0.0002

TYR 84 GLU 85 -0.0517

GLU 85 TYR 86 -0.0004

TYR 86 MET 87 -0.0024

MET 87 HIS 88 -0.0003

HIS 88 ASN 89 -0.0291

ASN 89 LYS 90 0.0000

LYS 90 SER 91 0.0309

SER 91 LEU 92 0.0002

LEU 92 ASP 93 0.0565

ASP 93 TYR 94 -0.0004

TYR 94 TYR 95 0.0126

TYR 95 LEU 96 0.0000

LEU 96 PHE 97 -0.0134

PHE 97 SER 98 0.0001

SER 98 PRO 99 0.0321

PRO 99 GLU 100 0.0000

GLU 100 ASN 101 -0.0606

ASN 101 HIS 102 -0.0000

HIS 102 ARG 103 0.0734

ARG 103 LYS 104 0.0003

LYS 104 LEU 105 -0.0128

LEU 105 THR 106 -0.0001

THR 106 TRP 107 -0.0002

TRP 107 HIS 108 -0.0004

HIS 108 ALA 109 -0.0421

ALA 109 ARG 110 0.0004

ARG 110 TYR 111 0.0283

TYR 111 LYS 112 0.0003

LYS 112 ILE 113 0.0123

ILE 113 ILE 114 0.0000

ILE 114 ARG 115 0.0614

ARG 115 GLY 116 0.0003

GLY 116 ILE 117 0.0095

ILE 117 ALA 118 0.0000

ALA 118 ARG 119 0.0433

ARG 119 GLY 120 -0.0002

GLY 120 ILE 121 0.0090

ILE 121 LEU 122 -0.0001

LEU 122 TYR 123 0.0303

TYR 123 LEU 124 -0.0000

LEU 124 HIS 125 0.0153

HIS 125 GLU 126 -0.0003

GLU 126 ASP 127 0.0060

ASP 127 SER 128 -0.0004

SER 128 HIS 129 -0.0101

HIS 129 LEU 130 0.0001

LEU 130 LYS 131 0.0096

LYS 131 ILE 132 0.0000

ILE 132 ILE 133 0.0148

ILE 133 HIS 134 0.0003

HIS 134 CYS 135 -0.0078

CYS 135 ASP 136 0.0000

ASP 136 LEU 137 -0.0376

LEU 137 LYS 138 -0.0001

LYS 138 PRO 139 0.0222

PRO 139 SER 140 -0.0001

SER 140 ASN 141 0.0457

ASN 141 ILE 142 0.0001

ILE 142 LEU 143 0.0229

LEU 143 LEU 144 0.0002

LEU 144 ASP 145 0.0284

ASP 145 ASP 146 -0.0000

ASP 146 LYS 147 0.0089

LYS 147 MET 148 -0.0000

MET 148 ASN 149 -0.1134

ASN 149 ALA 150 0.0000

ALA 150 LYS 151 -0.0721

LYS 151 ILE 152 0.0002

ILE 152 SER 153 -0.0451

SER 153 ASP 154 -0.0002

ASP 154 PHE 155 0.0124

PHE 155 GLY 156 -0.0001

GLY 156 LEU 157 -0.0215

LEU 157 ALA 158 0.0004

ALA 158 ARG 159 0.0111

ARG 159 ILE 160 -0.0000

ILE 160 VAL 161 -0.0022

VAL 161 ALA 162 -0.0000

ALA 162 ILE 163 0.0087

ILE 163 ASP 164 -0.0000

ASP 164 GLN 165 -0.0203

GLN 165 MET 166 0.0000

MET 166 GLN 167 -0.0582

GLN 167 GLY 168 -0.0003

GLY 168 ASN 169 -0.0776

ASN 169 THR 170 -0.0001

THR 170 SER 171 -0.0759

SER 171 ILE 172 -0.0001

ILE 172 ILE 173 -0.0048

ILE 173 ALA 174 0.0001

ALA 174 GLY 175 -0.0581

GLY 175 THR 176 0.0001

THR 176 TYR 177 0.0827

TYR 177 GLY 178 0.0001

GLY 178 TYR 179 0.0993

TYR 179 MET 180 0.0002

MET 180 SER 181 0.0366

SER 181 PRO 182 0.0001

PRO 182 GLU 183 0.0044

GLU 183 TYR 184 0.0001

TYR 184 ALA 185 -0.0689

ALA 185 MET 186 -0.0000

MET 186 LEU 187 -0.1772

LEU 187 GLY 188 0.0003

GLY 188 GLN 189 0.0008

GLN 189 PHE 190 -0.0001

PHE 190 SER 191 -0.0572

SER 191 VAL 192 -0.0004

VAL 192 LYS 193 0.0153

LYS 193 SER 194 -0.0001

SER 194 ASP 195 0.0027

ASP 195 VAL 196 -0.0002

VAL 196 PHE 197 -0.0341

PHE 197 SER 198 -0.0002

SER 198 PHE 199 0.0073

PHE 199 GLY 200 0.0002

GLY 200 VAL 201 0.0033

VAL 201 ILE 202 0.0002

ILE 202 MET 203 -0.0056

MET 203 LEU 204 0.0003

LEU 204 GLU 205 0.0025

GLU 205 ILE 206 -0.0001

ILE 206 VAL 207 -0.0573

VAL 207 SER 208 0.0003

SER 208 GLY 209 -0.1457

GLY 209 LYS 210 -0.0003

LYS 210 ARG 211 -0.0821

ARG 211 ASN 212 -0.0001

ASN 212 VAL 213 0.0244

VAL 213 ASP 214 0.0001

ASP 214 TYR 215 0.1680

TYR 215 ASN 216 0.0000

ASN 216 GLY 217 -0.6768

GLY 217 VAL 218 0.0000

VAL 218 ASN 219 -0.0178

ASN 219 SER 220 0.0001

SER 220 ILE 221 0.0967

ILE 221 ASP 222 0.0002

ASP 222 ASP 223 0.0937

ASP 223 LEU 224 0.0000

LEU 224 VAL 225 -0.0492

VAL 225 SER 226 0.0003

SER 226 HIS 227 0.1481

HIS 227 ALA 228 0.0002

ALA 228 TRP 229 0.0440

TRP 229 LYS 230 -0.0004

LYS 230 LYS 231 0.0965

LYS 231 TRP 232 0.0001

TRP 232 THR 233 -0.0192

THR 233 GLU 234 0.0002

GLU 234 ASN 235 -0.0111

ASN 235 LYS 236 -0.0000

LYS 236 GLN 237 -0.0451

GLN 237 MET 238 0.0002

MET 238 GLU 239 0.0843

GLU 239 LEU 240 -0.0002

LEU 240 LEU 241 0.2114

LEU 241 ASP 242 -0.0001

ASP 242 PRO 243 0.0118

PRO 243 ALA 244 -0.0001

ALA 244 LEU 245 -0.0541

LEU 245 THR 246 -0.0002

THR 246 TYR 247 0.1442

TYR 247 SER 248 0.0001

SER 248 PHE 249 -0.0423

PHE 249 SER 250 0.0001

SER 250 GLU 251 -0.0390

GLU 251 THR 252 -0.0000

THR 252 GLU 253 0.0210

GLU 253 VAL 254 0.0002

VAL 254 SER 255 -0.0280

SER 255 ARG 256 0.0000

ARG 256 CYS 257 0.0281

CYS 257 ILE 258 0.0002

ILE 258 GLN 259 0.0078

GLN 259 LEU 260 0.0003

LEU 260 GLY 261 0.0028

GLY 261 LEU 262 0.0002

LEU 262 LEU 263 -0.0260

LEU 263 CYS 264 0.0003

CYS 264 VAL 265 -0.0556

VAL 265 GLN 266 -0.0001

GLN 266 GLU 267 0.0656

GLU 267 ASN 268 0.0002

ASN 268 PRO 269 -0.0132

PRO 269 ASP 270 -0.0001

ASP 270 GLN 271 0.0480

GLN 271 ARG 272 -0.0002

ARG 272 PRO 273 -0.1026

PRO 273 THR 274 -0.0001

THR 274 MET 275 -0.0053

MET 275 ALA 276 -0.0003

ALA 276 THR 277 0.0334

THR 277 ILE 278 0.0003

ILE 278 ALA 279 -0.0010

ALA 279 LEU 280 -0.0001

LEU 280 TYR 281 -0.0104

TYR 281 PHE 282 0.0000

PHE 282 ASN 283 0.0345

ASN 283 ILE 284 0.0002

ILE 284 ASP 285 -0.0149

ASP 285 SER 286 0.0001

SER 286 ILE 287 -0.0222

ILE 287 ASP 288 -0.0001

ASP 288 LEU 289 -0.0355

LEU 289 PRO 290 0.0003

PRO 290 LEU 291 -0.0475

LEU 291 PRO 292 0.0001

PRO 292 GLN 293 -0.0777

GLN 293 GLN 294 -0.0002

GLN 294 PRO 295 0.0086

PRO 295 PRO 296 0.0001

PRO 296 PHE 297 -0.2495

PHE 297 TYR 298 0.0001

TYR 298 MET 299 -0.0489

MET 299 ARG 300 -0.0001

ARG 300 GLY 301 0.0482

GLY 301 LYS 302 -0.0000

LYS 302 ILE 303 -0.0768

ILE 303 GLU 304 0.0001

GLU 304 SER 305 -0.0092

SER 305 LYS 306 -0.0001

LYS 306 VAL 307 -0.0885

VAL 307 ALA 308 -0.0001

ALA 308 SER 309 0.0357

SER 309 LYS 310 -0.0003

LYS 310 LYS 311 0.1825

LYS 311 THR 312 -0.0004

THR 312 MET 313 -0.0793

MET 313 SER 314 0.0000

SER 314 GLY 315 -0.2086

GLY 315 ARG 316 0.0000

ARG 316 PRO 317 0.2287

PRO 317 ARG 318 -0.0000

ARG 318 SER 319 -0.2585

SER 319 TYR 320 -0.0000

TYR 320 SER 321 -0.0270

SER 321 VAL 322 -0.0001

VAL 322 THR 323 0.0202

THR 323 ARG 324 0.0001

ARG 324 PHE 325 -0.2250

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 21 ---

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

* *