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

* Psychrophile *

CA strain for 22042311551780060

--- 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
GLN 7 PHE 8 -0.0002

PHE 8 ASP 9 -0.0402

ASP 9 PRO 10 -0.0001

PRO 10 ILE 11 0.0244

ILE 11 LEU 12 0.0002

LEU 12 VAL 13 -0.0175

VAL 13 ALA 14 -0.0002

ALA 14 ASP 15 -0.0022

ASP 15 ILE 16 -0.0001

ILE 16 GLY 17 -0.0059

GLY 17 GLY 18 0.0003

GLY 18 THR 19 -0.0386

THR 19 ASN 20 0.0003

ASN 20 ALA 21 0.0075

ALA 21 ARG 22 0.0002

ARG 22 PHE 23 -0.0033

PHE 23 ALA 24 -0.0002

ALA 24 LEU 25 0.0256

LEU 25 ILE 26 0.0003

ILE 26 THR 27 0.0329

THR 27 ALA 28 0.0003

ALA 28 PHE 29 0.0141

PHE 29 ASP 30 0.0001

ASP 30 ALA 31 0.0291

ALA 31 ALA 32 0.0001

ALA 32 LYS 33 0.0501

LYS 33 ASN 34 0.0000

ASN 34 GLU 35 -0.0278

GLU 35 PHE 36 -0.0001

PHE 36 VAL 37 -0.1314

VAL 37 ILE 38 0.0001

ILE 38 GLU 39 -0.1245

GLU 39 TYR 40 0.0004

TYR 40 ASN 41 -0.0153

ASN 41 HIS 42 0.0001

HIS 42 THR 43 0.0510

THR 43 PHE 44 0.0001

PHE 44 PRO 45 0.0237

PRO 45 SER 46 -0.0004

SER 46 ALA 47 -0.0173

ALA 47 ASP 48 0.0004

ASP 48 PHE 49 0.0093

PHE 49 GLY 50 -0.0005

GLY 50 SER 51 0.0035

SER 51 LEU 52 0.0001

LEU 52 GLN 53 0.0052

GLN 53 ASN 54 0.0000

ASN 54 ALA 55 -0.0219

ALA 55 THR 56 0.0002

THR 56 ARG 57 0.0057

ARG 57 HIS 58 0.0000

HIS 58 TYR 59 -0.0185

TYR 59 LEU 60 0.0002

LEU 60 SER 61 0.0089

SER 61 THR 62 -0.0001

THR 62 VAL 63 0.0121

VAL 63 PRO 64 -0.0000

PRO 64 HIS 65 -0.0029

HIS 65 ILE 66 -0.0004

ILE 66 LYS 67 -0.0347

LYS 67 PRO 68 0.0001

PRO 68 VAL 69 0.0142

VAL 69 ARG 70 -0.0002

ARG 70 ALA 71 -0.0043

ALA 71 CYS 72 0.0000

CYS 72 LEU 73 -0.0286

LEU 73 ALA 74 -0.0003

ALA 74 VAL 75 -0.0109

VAL 75 ALA 76 -0.0001

ALA 76 GLY 77 0.0115

GLY 77 PRO 78 0.0002

PRO 78 ILE 79 -0.0404

ILE 79 LYS 80 0.0001

LYS 80 ALA 81 0.0065

ALA 81 GLY 82 0.0003

GLY 82 GLN 83 -0.0158

GLN 83 VAL 84 -0.0001

VAL 84 HIS 85 -0.0098

HIS 85 LEU 86 0.0000

LEU 86 THR 87 0.0145

THR 87 ASN 88 0.0001

ASN 88 LEU 89 0.0059

LEU 89 GLY 90 -0.0001

GLY 90 TRP 91 -0.0073

TRP 91 HIS 92 0.0001

HIS 92 PHE 93 -0.0383

PHE 93 SER 94 -0.0003

SER 94 VAL 95 0.0198

VAL 95 SER 96 0.0005

SER 96 GLU 97 0.0178

GLU 97 PHE 98 0.0003

PHE 98 LYS 99 -0.0242

LYS 99 GLN 100 -0.0002

GLN 100 ALA 101 0.0113

ALA 101 PHE 102 0.0004

PHE 102 SER 103 0.0343

SER 103 PHE 104 0.0000

PHE 104 LEU 105 0.0377

LEU 105 GLN 106 -0.0004

GLN 106 LEU 107 -0.0399

LEU 107 GLU 108 -0.0000

GLU 108 VAL 109 -0.0668

VAL 109 ILE 110 0.0001

ILE 110 ASN 111 0.0129

ASN 111 ASP 112 -0.0002

ASP 112 PHE 113 0.0341

PHE 113 ALA 114 0.0002

ALA 114 ALA 115 0.0037

ALA 115 PHE 116 0.0004

PHE 116 ALA 117 0.0501

ALA 117 TYR 118 0.0001

TYR 118 ALA 119 -0.0510

ALA 119 ALA 120 -0.0003

ALA 120 PRO 121 0.0115

PRO 121 TYR 122 0.0000

TYR 122 LEU 123 0.0460

LEU 123 ASP 124 0.0003

ASP 124 SER 125 0.0200

SER 125 ASN 126 0.0004

ASN 126 GLN 127 0.0232

GLN 127 ASN 128 -0.0002

ASN 128 VAL 129 0.0412

VAL 129 VAL 130 -0.0000

VAL 130 ILE 131 0.0389

ILE 131 LYS 132 -0.0001

LYS 132 ALA 133 -0.1495

ALA 133 GLY 134 -0.0001

GLY 134 GLN 135 -0.1637

GLN 135 ALA 136 0.0001

ALA 136 ASP 137 -0.1730

ASP 137 GLU 138 0.0001

GLU 138 ASN 139 -0.2908

ASN 139 SER 140 -0.0001

SER 140 ASN 141 0.0500

ASN 141 ILE 142 0.0001

ILE 142 ALA 143 0.0474

ALA 143 VAL 144 -0.0005

VAL 144 MET 145 0.1176

MET 145 GLY 146 0.0001

GLY 146 PRO 147 0.1424

PRO 147 GLY 148 0.0004

GLY 148 THR 149 -0.0413

THR 149 GLY 150 -0.0000

GLY 150 PHE 151 0.1244

PHE 151 GLY 152 -0.0002

GLY 152 ALA 153 0.2836

ALA 153 ALA 154 -0.0001

ALA 154 CYS 155 0.1998

CYS 155 LEU 156 0.0000

LEU 156 VAL 157 0.0873

VAL 157 ARG 158 -0.0001

ARG 158 THR 159 -0.1089

THR 159 ALA 160 -0.0001

ALA 160 GLN 161 -0.1373

GLN 161 SER 162 0.0001

SER 162 SER 163 -0.0939

SER 163 ALA 164 0.0002

ALA 164 VAL 165 0.0617

VAL 165 LEU 166 0.0002

LEU 166 SER 167 0.1730

SER 167 SER 168 0.0002

SER 168 GLU 169 0.1164

GLU 169 GLY 170 0.0003

GLY 170 GLY 171 0.0893

GLY 171 HIS 172 0.0002

HIS 172 ILE 173 -0.0151

ILE 173 SER 174 0.0002

SER 174 LEU 175 -0.0097

LEU 175 ALA 176 0.0003

ALA 176 ALA 177 -0.0606

ALA 177 VAL 178 -0.0001

VAL 178 THR 179 -0.0396

THR 179 ASP 180 -0.0003

ASP 180 LEU 181 0.0003

LEU 181 ASP 182 0.0002

ASP 182 ALA 183 0.0147

ALA 183 LYS 184 -0.0001

LYS 184 LEU 185 0.0208

LEU 185 LEU 186 0.0001

LEU 186 ILE 187 -0.0041

ILE 187 GLU 188 -0.0001

GLU 188 LEU 189 0.0129

LEU 189 ARG 190 0.0003

ARG 190 LYS 191 -0.0043

LYS 191 GLU 192 0.0002

GLU 192 HIS 193 0.0163

HIS 193 PRO 194 0.0004

PRO 194 HIS 195 0.0146

HIS 195 VAL 196 0.0002

VAL 196 SER 197 0.0066

SER 197 LEU 198 -0.0003

LEU 198 GLU 199 0.0032

GLU 199 THR 200 0.0001

THR 200 VAL 201 -0.0110

VAL 201 PHE 202 0.0001

PHE 202 SER 203 0.0141

SER 203 GLY 204 -0.0001

GLY 204 PRO 205 -0.0585

PRO 205 GLY 206 -0.0001

GLY 206 ILE 207 0.0245

ILE 207 ALA 208 0.0002

ALA 208 HIS 209 -0.0016

HIS 209 LEU 210 0.0001

LEU 210 TYR 211 0.0260

TYR 211 LYS 212 0.0002

LYS 212 ALA 213 -0.0274

ALA 213 MET 214 -0.0000

MET 214 ALA 215 -0.0242

ALA 215 ALA 216 -0.0000

ALA 216 VAL 217 -0.0432

VAL 217 ASN 218 -0.0001

ASN 218 GLY 219 -0.0263

GLY 219 ILE 220 0.0002

ILE 220 THR 221 -0.0173

THR 221 ALA 222 -0.0001

ALA 222 LYS 223 -0.0303

LYS 223 HIS 224 0.0004

HIS 224 LEU 225 0.0128

LEU 225 ASP 226 -0.0002

ASP 226 ALA 227 0.0433

ALA 227 ALA 228 0.0000

ALA 228 GLN 229 0.0283

GLN 229 ILE 230 -0.0002

ILE 230 SER 231 0.0099

SER 231 ASN 232 -0.0001

ASN 232 LEU 233 -0.0180

LEU 233 ALA 234 0.0001

ALA 234 ASN 235 -0.0015

ASN 235 THR 236 -0.0000

THR 236 GLY 237 -0.0112

GLY 237 GLU 238 0.0005

GLU 238 CYS 239 -0.0222

CYS 239 GLU 240 0.0002

GLU 240 VAL 241 -0.0178

VAL 241 CYS 242 -0.0002

CYS 242 ASP 243 -0.0026

ASP 243 ALA 244 -0.0002

ALA 244 THR 245 0.0251

THR 245 LEU 246 0.0002

LEU 246 ASN 247 -0.0644

ASN 247 GLN 248 0.0001

GLN 248 PHE 249 0.0506

PHE 249 CYS 250 -0.0002

CYS 250 ASP 251 0.0142

ASP 251 TRP 252 0.0005

TRP 252 LEU 253 -0.0015

LEU 253 GLY 254 -0.0002

GLY 254 SER 255 0.0033

SER 255 ALA 256 0.0004

ALA 256 ALA 257 -0.0177

ALA 257 GLY 258 -0.0000

GLY 258 ASP 259 0.0139

ASP 259 LEU 260 -0.0002

LEU 260 ALA 261 0.0708

ALA 261 LEU 262 0.0002

LEU 262 ALA 263 -0.0850

ALA 263 TYR 264 0.0003

TYR 264 GLY 265 0.0584

GLY 265 ALA 266 0.0001

ALA 266 LEU 267 0.0004

LEU 267 GLY 268 0.0000

GLY 268 GLY 269 -0.1241

GLY 269 LEU 270 0.0001

LEU 270 PHE 271 -0.0200

PHE 271 ILE 272 -0.0002

ILE 272 GLY 273 0.0055

GLY 273 GLY 274 0.0002

GLY 274 GLY 275 0.0640

GLY 275 ILE 276 0.0002

ILE 276 LEU 277 -0.0693

LEU 277 PRO 278 -0.0002

PRO 278 ARG 279 0.1068

ARG 279 MET 280 -0.0003

MET 280 GLN 281 -0.0192

GLN 281 SER 282 0.0000

SER 282 ARG 283 0.0665

ARG 283 LEU 284 0.0002

LEU 284 LEU 285 -0.0159

LEU 285 GLU 286 0.0001

GLU 286 SER 287 0.0300

SER 287 ARG 288 -0.0001

ARG 288 PHE 289 0.0233

PHE 289 VAL 290 -0.0003

VAL 290 GLU 291 0.0308

GLU 291 ARG 292 0.0001

ARG 292 PHE 293 -0.0383

PHE 293 SER 294 -0.0002

SER 294 GLN 295 0.0057

GLN 295 LYS 296 0.0001

LYS 296 GLY 297 0.0232

GLY 297 ILE 298 -0.0001

ILE 298 MET 299 0.0192

MET 299 SER 300 0.0002

SER 300 GLN 301 -0.0091

GLN 301 TYR 302 -0.0001

TYR 302 ASN 303 -0.0049

ASN 303 GLY 304 -0.0004

GLY 304 GLN 305 -0.0188

GLN 305 VAL 306 0.0002

VAL 306 PRO 307 -0.0229

PRO 307 VAL 308 0.0001

VAL 308 THR 309 -0.0657

THR 309 LEU 310 0.0003

LEU 310 VAL 311 -0.0124

VAL 311 THR 312 -0.0003

THR 312 GLN 313 -0.0221

GLN 313 ASP 314 -0.0004

ASP 314 ASN 315 -0.0111

ASN 315 ILE 316 0.0000

ILE 316 PRO 317 0.0614

PRO 317 LEU 318 -0.0002

LEU 318 ILE 319 -0.0825

ILE 319 GLY 320 0.0001

GLY 320 ALA 321 0.0397

ALA 321 ALA 322 0.0004

ALA 322 ALA 323 -0.0157

ALA 323 CYS 324 -0.0000

CYS 324 LEU 325 0.1162

LEU 325 HIS 326 -0.0000

HIS 326 ASN 327 -0.0705

ASN 327 SER 328 0.0002

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.

*** Psychrophile ***

CA strain for 22042311551780060

--- normal mode 11 ---

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

* Psychrophile *