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

* *

CA strain for 230101190352136506

--- normal mode 11 ---

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 0.0003

ASP 2 MET 3 0.0302

MET 3 ILE 4 0.0000

ILE 4 ARG 5 0.0160

ARG 5 LEU 6 0.0002

LEU 6 ALA 7 -0.0074

ALA 7 THR 8 0.0001

THR 8 ASN 9 -0.0095

ASN 9 LYS 10 -0.0003

LYS 10 PHE 11 0.0053

PHE 11 SER 12 0.0003

SER 12 GLU 13 0.0177

GLU 13 ASP 14 -0.0003

ASP 14 ASN 15 -0.0097

ASN 15 LYS 16 -0.0003

LYS 16 ILE 17 -0.1786

ILE 17 GLY 18 -0.0001

GLY 18 GLU 19 -0.1545

GLU 19 GLY 20 0.0002

GLY 20 GLY 21 0.0585

GLY 21 PHE 22 -0.0000

PHE 22 GLY 23 0.0243

GLY 23 ASP 24 0.0003

ASP 24 VAL 25 -0.0401

VAL 25 TYR 26 0.0000

TYR 26 LYS 27 0.0079

LYS 27 GLY 28 -0.0004

GLY 28 MET 29 0.0103

MET 29 PHE 30 0.0001

PHE 30 PRO 31 -0.0039

PRO 31 ASN 32 -0.0003

ASN 32 GLY 33 0.0262

GLY 33 TYR 34 -0.0001

TYR 34 GLU 35 0.0209

GLU 35 ILE 36 0.0000

ILE 36 ALA 37 -0.0258

ALA 37 VAL 38 0.0001

VAL 38 LYS 39 0.0159

LYS 39 ARG 40 0.0002

ARG 40 LEU 41 0.0078

LEU 41 ILE 42 0.0003

ILE 42 ARG 43 -0.0467

ARG 43 ASN 44 0.0003

ASN 44 SER 45 -0.1280

SER 45 SER 46 0.0000

SER 46 GLN 47 0.0138

GLN 47 GLY 48 -0.0000

GLY 48 ALA 49 0.0877

ALA 49 VAL 50 0.0001

VAL 50 GLU 51 -0.0552

GLU 51 PHE 52 0.0005

PHE 52 LYS 53 0.0158

LYS 53 ASN 54 -0.0002

ASN 54 GLU 55 0.0058

GLU 55 VAL 56 0.0003

VAL 56 LEU 57 0.0238

LEU 57 LEU 58 0.0004

LEU 58 ILE 59 -0.0249

ILE 59 ALA 60 0.0001

ALA 60 LYS 61 -0.0005

LYS 61 LEU 62 0.0004

LEU 62 GLN 63 0.0054

GLN 63 HIS 64 0.0002

HIS 64 ARG 65 0.0497

ARG 65 ASN 66 -0.0003

ASN 66 LEU 67 0.0239

LEU 67 VAL 68 -0.0003

VAL 68 ARG 69 0.0634

ARG 69 LEU 70 0.0000

LEU 70 LEU 71 -0.0297

LEU 71 GLY 72 0.0000

GLY 72 PHE 73 0.0947

PHE 73 CYS 74 -0.0002

CYS 74 ILE 75 0.0486

ILE 75 GLN 76 0.0004

GLN 76 ARG 77 0.0368

ARG 77 ASN 78 0.0000

ASN 78 GLU 79 -0.0309

GLU 79 LYS 80 -0.0000

LYS 80 ILE 81 0.0014

ILE 81 LEU 82 0.0004

LEU 82 ILE 83 -0.0159

ILE 83 TYR 84 -0.0001

TYR 84 GLU 85 0.0601

GLU 85 TYR 86 0.0001

TYR 86 MET 87 0.0030

MET 87 HIS 88 -0.0000

HIS 88 ASN 89 0.0672

ASN 89 LYS 90 0.0004

LYS 90 SER 91 0.1163

SER 91 LEU 92 0.0001

LEU 92 ASP 93 0.0170

ASP 93 TYR 94 0.0004

TYR 94 TYR 95 -0.0269

TYR 95 LEU 96 -0.0000

LEU 96 PHE 97 0.0168

PHE 97 SER 98 0.0001

SER 98 PRO 99 -0.0189

PRO 99 GLU 100 0.0001

GLU 100 ASN 101 -0.0011

ASN 101 HIS 102 -0.0001

HIS 102 ARG 103 -0.0137

ARG 103 LYS 104 0.0002

LYS 104 LEU 105 0.0187

LEU 105 THR 106 -0.0002

THR 106 TRP 107 -0.0348

TRP 107 HIS 108 -0.0002

HIS 108 ALA 109 -0.0371

ALA 109 ARG 110 0.0001

ARG 110 TYR 111 -0.0099

TYR 111 LYS 112 -0.0003

LYS 112 ILE 113 -0.0008

ILE 113 ILE 114 0.0002

ILE 114 ARG 115 0.0172

ARG 115 GLY 116 0.0000

GLY 116 ILE 117 0.0013

ILE 117 ALA 118 0.0002

ALA 118 ARG 119 0.0079

ARG 119 GLY 120 -0.0001

GLY 120 ILE 121 -0.0055

ILE 121 LEU 122 -0.0001

LEU 122 TYR 123 0.0794

TYR 123 LEU 124 -0.0000

LEU 124 HIS 125 -0.0030

HIS 125 GLU 126 -0.0001

GLU 126 ASP 127 -0.0012

ASP 127 SER 128 0.0000

SER 128 HIS 129 -0.0159

HIS 129 LEU 130 -0.0001

LEU 130 LYS 131 -0.0015

LYS 131 ILE 132 -0.0000

ILE 132 ILE 133 -0.0481

ILE 133 HIS 134 -0.0002

HIS 134 CYS 135 0.0028

CYS 135 ASP 136 0.0002

ASP 136 LEU 137 -0.0412

LEU 137 LYS 138 0.0003

LYS 138 PRO 139 -0.0203

PRO 139 SER 140 0.0000

SER 140 ASN 141 -0.0881

ASN 141 ILE 142 -0.0001

ILE 142 LEU 143 0.0660

LEU 143 LEU 144 0.0000

LEU 144 ASP 145 0.0671

ASP 145 ASP 146 -0.0000

ASP 146 LYS 147 -0.0566

LYS 147 MET 148 -0.0002

MET 148 ASN 149 0.0414

ASN 149 ALA 150 0.0002

ALA 150 LYS 151 -0.0004

LYS 151 ILE 152 0.0003

ILE 152 SER 153 -0.0618

SER 153 ASP 154 0.0002

ASP 154 PHE 155 -0.1144

PHE 155 GLY 156 -0.0000

GLY 156 LEU 157 0.0130

LEU 157 ALA 158 0.0001

ALA 158 ARG 159 -0.0062

ARG 159 ILE 160 0.0002

ILE 160 VAL 161 0.0674

VAL 161 ALA 162 -0.0000

ALA 162 ILE 163 0.0216

ILE 163 ASP 164 -0.0005

ASP 164 GLN 165 -0.0120

GLN 165 MET 166 -0.0003

MET 166 GLN 167 -0.0353

GLN 167 GLY 168 -0.0001

GLY 168 ASN 169 -0.0488

ASN 169 THR 170 0.0002

THR 170 SER 171 -0.0117

SER 171 ILE 172 -0.0001

ILE 172 ILE 173 0.0113

ILE 173 ALA 174 0.0001

ALA 174 GLY 175 -0.0049

GLY 175 THR 176 0.0000

THR 176 TYR 177 -0.0172

TYR 177 GLY 178 -0.0004

GLY 178 TYR 179 0.0332

TYR 179 MET 180 0.0000

MET 180 SER 181 0.0011

SER 181 PRO 182 -0.0003

PRO 182 GLU 183 0.0090

GLU 183 TYR 184 0.0003

TYR 184 ALA 185 -0.0283

ALA 185 MET 186 -0.0001

MET 186 LEU 187 -0.0446

LEU 187 GLY 188 0.0002

GLY 188 GLN 189 0.0004

GLN 189 PHE 190 -0.0000

PHE 190 SER 191 -0.0019

SER 191 VAL 192 -0.0001

VAL 192 LYS 193 0.0282

LYS 193 SER 194 -0.0001

SER 194 ASP 195 0.0057

ASP 195 VAL 196 0.0002

VAL 196 PHE 197 -0.0065

PHE 197 SER 198 0.0001

SER 198 PHE 199 0.0036

PHE 199 GLY 200 -0.0003

GLY 200 VAL 201 -0.0002

VAL 201 ILE 202 -0.0003

ILE 202 MET 203 -0.0530

MET 203 LEU 204 -0.0002

LEU 204 GLU 205 -0.0025

GLU 205 ILE 206 0.0003

ILE 206 VAL 207 -0.0266

VAL 207 SER 208 0.0002

SER 208 GLY 209 -0.0114

GLY 209 LYS 210 -0.0001

LYS 210 ARG 211 -0.0371

ARG 211 ASN 212 0.0001

ASN 212 VAL 213 0.0236

VAL 213 ASP 214 0.0001

ASP 214 TYR 215 -0.0546

TYR 215 ASN 216 0.0001

ASN 216 GLY 217 -0.1012

GLY 217 VAL 218 0.0001

VAL 218 ASN 219 -0.0008

ASN 219 SER 220 -0.0000

SER 220 ILE 221 -0.1082

ILE 221 ASP 222 0.0002

ASP 222 ASP 223 0.0205

ASP 223 LEU 224 -0.0002

LEU 224 VAL 225 0.0203

VAL 225 SER 226 0.0000

SER 226 HIS 227 -0.0105

HIS 227 ALA 228 0.0001

ALA 228 TRP 229 0.0134

TRP 229 LYS 230 0.0003

LYS 230 LYS 231 -0.0046

LYS 231 TRP 232 0.0003

TRP 232 THR 233 0.0020

THR 233 GLU 234 0.0001

GLU 234 ASN 235 -0.0050

ASN 235 LYS 236 0.0000

LYS 236 GLN 237 0.0067

GLN 237 MET 238 -0.0003

MET 238 GLU 239 0.0191

GLU 239 LEU 240 0.0003

LEU 240 LEU 241 0.0022

LEU 241 ASP 242 0.0001

ASP 242 PRO 243 -0.0049

PRO 243 ALA 244 -0.0003

ALA 244 LEU 245 -0.0065

LEU 245 THR 246 0.0001

THR 246 TYR 247 -0.0020

TYR 247 SER 248 -0.0001

SER 248 PHE 249 0.0111

PHE 249 SER 250 0.0003

SER 250 GLU 251 -0.0041

GLU 251 THR 252 -0.0001

THR 252 GLU 253 -0.0047

GLU 253 VAL 254 0.0002

VAL 254 SER 255 -0.0095

SER 255 ARG 256 -0.0003

ARG 256 CYS 257 -0.0214

CYS 257 ILE 258 0.0003

ILE 258 GLN 259 -0.0016

GLN 259 LEU 260 0.0003

LEU 260 GLY 261 -0.0110

GLY 261 LEU 262 -0.0003

LEU 262 LEU 263 0.0222

LEU 263 CYS 264 0.0003

CYS 264 VAL 265 0.0029

VAL 265 GLN 266 0.0000

GLN 266 GLU 267 -0.0076

GLU 267 ASN 268 -0.0001

ASN 268 PRO 269 0.0124

PRO 269 ASP 270 0.0002

ASP 270 GLN 271 0.0128

GLN 271 ARG 272 0.0002

ARG 272 PRO 273 -0.0171

PRO 273 THR 274 -0.0001

THR 274 MET 275 -0.0214

MET 275 ALA 276 0.0000

ALA 276 THR 277 0.0504

THR 277 ILE 278 0.0002

ILE 278 ALA 279 -0.0144

ALA 279 LEU 280 0.0002

LEU 280 TYR 281 0.0126

TYR 281 PHE 282 -0.0006

PHE 282 ASN 283 -0.0045

ASN 283 ILE 284 0.0002

ILE 284 ASP 285 0.0175

ASP 285 SER 286 -0.0002

SER 286 ILE 287 0.0025

ILE 287 ASP 288 0.0002

ASP 288 LEU 289 -0.0176

LEU 289 PRO 290 -0.0001

PRO 290 LEU 291 0.0035

LEU 291 PRO 292 0.0001

PRO 292 GLN 293 -0.0356

GLN 293 GLN 294 -0.0003

GLN 294 PRO 295 -0.0020

PRO 295 PRO 296 -0.0001

PRO 296 PHE 297 -0.0161

PHE 297 TYR 298 -0.0001

TYR 298 MET 299 -0.0547

MET 299 ARG 300 0.0001

ARG 300 GLY 301 0.0593

GLY 301 LYS 302 0.0000

LYS 302 ILE 303 0.0142

ILE 303 GLU 304 0.0002

GLU 304 SER 305 -0.0242

SER 305 LYS 306 -0.0003

LYS 306 VAL 307 0.0077

VAL 307 ALA 308 0.0002

ALA 308 SER 309 0.0427

SER 309 LYS 310 0.0004

LYS 310 LYS 311 0.0138

LYS 311 THR 312 -0.0000

THR 312 MET 313 -0.1349

MET 313 SER 314 -0.0003

SER 314 GLY 315 0.0672

GLY 315 ARG 316 -0.0000

ARG 316 PRO 317 -0.1546

PRO 317 ARG 318 -0.0003

ARG 318 SER 319 0.1277

SER 319 TYR 320 -0.0000

TYR 320 SER 321 0.0280

SER 321 VAL 322 -0.0002

VAL 322 THR 323 0.0049

THR 323 ARG 324 -0.0001

ARG 324 PHE 325 0.1513

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 11 ---

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

* *