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

* *

CA strain for 240112142738850346

--- normal mode 13 ---

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
MET 1 VAL 2 -0.0001

VAL 2 ARG 3 0.0077

ARG 3 GLU 4 0.0004

GLU 4 GLU 5 -0.0002

GLU 5 VAL 6 -0.0001

VAL 6 ALA 7 -0.0034

ALA 7 GLY 8 0.0003

GLY 8 SER 9 -0.0193

SER 9 THR 10 0.0002

THR 10 GLN 11 0.0110

GLN 11 THR 12 0.0000

THR 12 LEU 13 0.0314

LEU 13 GLN 14 -0.0006

GLN 14 TRP 15 0.0471

TRP 15 LYS 16 0.0001

LYS 16 CYS 17 0.0588

CYS 17 VAL 18 -0.0002

VAL 18 GLU 19 0.0315

GLU 19 SER 20 -0.0000

SER 20 ARG 21 0.0393

ARG 21 VAL 22 0.0000

VAL 22 ASP 23 0.0005

ASP 23 SER 24 -0.0002

SER 24 LYS 25 -0.0059

LYS 25 ARG 26 -0.0002

ARG 26 LEU 27 -0.0205

LEU 27 TYR 28 0.0001

TYR 28 TYR 29 0.0019

TYR 29 GLY 30 0.0001

GLY 30 ARG 31 0.0118

ARG 31 PHE 32 -0.0002

PHE 32 ILE 33 0.0296

ILE 33 LEU 34 0.0000

LEU 34 SER 35 0.0086

SER 35 PRO 36 0.0000

PRO 36 LEU 37 -0.0174

LEU 37 ARG 38 0.0000

ARG 38 LYS 39 0.0013

LYS 39 GLY 40 0.0000

GLY 40 GLN 41 -0.0038

GLN 41 ALA 42 -0.0003

ALA 42 ASP 43 -0.0045

ASP 43 THR 44 0.0000

THR 44 VAL 45 0.0015

VAL 45 GLY 46 0.0001

GLY 46 ILE 47 0.0035

ILE 47 ALA 48 -0.0003

ALA 48 LEU 49 -0.0032

LEU 49 ARG 50 0.0000

ARG 50 ARG 51 0.0163

ARG 51 ALA 52 -0.0002

ALA 52 LEU 53 -0.0043

LEU 53 LEU 54 -0.0001

LEU 54 GLY 55 0.0097

GLY 55 GLU 56 -0.0000

GLU 56 ILE 57 0.0027

ILE 57 GLU 58 -0.0004

GLU 58 GLY 59 0.0036

GLY 59 ALA 60 0.0001

ALA 60 CYS 61 0.0090

CYS 61 ILE 62 0.0001

ILE 62 THR 63 0.0038

THR 63 ARG 64 -0.0002

ARG 64 ALA 65 -0.0020

ALA 65 LYS 66 -0.0000

LYS 66 PHE 67 0.0019

PHE 67 GLY 68 0.0001

GLY 68 SER 69 0.0030

SER 69 VAL 70 -0.0001

VAL 70 PRO 71 0.0019

PRO 71 HIS 72 0.0004

HIS 72 GLU 73 0.0002

GLU 73 TYR 74 -0.0001

TYR 74 SER 75 -0.0004

SER 75 THR 76 0.0002

THR 76 ILE 77 -0.0007

ILE 77 ALA 78 0.0001

ALA 78 GLY 79 -0.0003

GLY 79 ILE 80 0.0002

ILE 80 GLU 81 0.0003

GLU 81 GLU 82 0.0002

GLU 82 SER 83 0.0028

SER 83 VAL 84 0.0000

VAL 84 GLN 85 -0.0006

GLN 85 GLU 86 -0.0001

GLU 86 ILE 87 0.0012

ILE 87 LEU 88 0.0003

LEU 88 LEU 89 0.0038

LEU 89 ASN 90 0.0001

ASN 90 LEU 91 0.0015

LEU 91 LYS 92 0.0002

LYS 92 GLU 93 0.0146

GLU 93 ILE 94 -0.0003

ILE 94 VAL 95 0.0022

VAL 95 LEU 96 0.0003

LEU 96 ARG 97 0.0091

ARG 97 SER 98 -0.0001

SER 98 ASN 99 -0.0090

ASN 99 LEU 100 -0.0000

LEU 100 TYR 101 -0.0011

TYR 101 GLY 102 0.0002

GLY 102 VAL 103 0.0156

VAL 103 ARG 104 -0.0004

ARG 104 ASP 105 0.0129

ASP 105 ALA 106 0.0001

ALA 106 SER 107 0.0122

SER 107 ILE 108 0.0001

ILE 108 CYS 109 0.0057

CYS 109 VAL 110 -0.0000

VAL 110 LYS 111 0.0068

LYS 111 GLY 112 0.0003

GLY 112 PRO 113 -0.0006

PRO 113 ARG 114 -0.0002

ARG 114 TYR 115 -0.0029

TYR 115 ILE 116 -0.0001

ILE 116 THR 117 0.0038

THR 117 ALA 118 -0.0002

ALA 118 GLN 119 -0.0010

GLN 119 ASP 120 -0.0002

ASP 120 ILE 121 0.0053

ILE 121 ILE 122 0.0001

ILE 122 LEU 123 0.0194

LEU 123 PRO 124 0.0002

PRO 124 PRO 125 0.0031

PRO 125 SER 126 -0.0002

SER 126 VAL 127 -0.0075

VAL 127 GLU 128 0.0005

GLU 128 ILE 129 -0.0061

ILE 129 VAL 130 0.0002

VAL 130 ASP 131 0.0134

ASP 131 THR 132 -0.0001

THR 132 ALA 133 0.0063

ALA 133 GLN 134 0.0003

GLN 134 PRO 135 0.0016

PRO 135 ILE 136 0.0001

ILE 136 ALA 137 0.0020

ALA 137 ASN 138 0.0001

ASN 138 LEU 139 -0.0013

LEU 139 THR 140 -0.0002

THR 140 GLU 141 -0.0014

GLU 141 PRO 142 -0.0001

PRO 142 ILE 143 0.0006

ILE 143 ASP 144 0.0000

ASP 144 PHE 145 -0.0016

PHE 145 CYS 146 -0.0000

CYS 146 ILE 147 0.0014

ILE 147 ASP 148 -0.0001

ASP 148 LEU 149 0.0016

LEU 149 GLN 150 0.0002

GLN 150 ILE 151 0.0061

ILE 151 LYS 152 0.0000

LYS 152 ARG 153 0.0251

ARG 153 ASP 154 0.0001

ASP 154 ARG 155 -0.0089

ARG 155 GLY 156 0.0000

GLY 156 TYR 157 -0.0353

TYR 157 GLN 158 0.0003

GLN 158 THR 159 -0.0094

THR 159 GLU 160 -0.0002

GLU 160 LEU 161 -0.0070

LEU 161 ARG 162 0.0001

ARG 162 LYS 163 0.0005

LYS 163 ASN 164 -0.0002

ASN 164 TYR 165 0.0000

TYR 165 GLN 166 -0.0002

GLN 166 ASP 167 -0.0017

ASP 167 GLY 168 0.0001

GLY 168 SER 169 -0.0003

SER 169 TYR 170 0.0003

TYR 170 PRO 171 -0.0062

PRO 171 ILE 172 -0.0001

ILE 172 ASP 173 -0.0080

ASP 173 ALA 174 0.0001

ALA 174 VAL 175 -0.0108

VAL 175 SER 176 -0.0000

SER 176 MET 177 -0.0175

MET 177 PRO 178 -0.0001

PRO 178 VAL 179 -0.0015

VAL 179 ARG 180 -0.0001

ARG 180 ASN 181 -0.0580

ASN 181 VAL 182 0.0003

VAL 182 ASN 183 -0.0344

ASN 183 TYR 184 0.0002

TYR 184 SER 185 -0.0219

SER 185 ILE 186 0.0003

ILE 186 PHE 187 -0.0130

PHE 187 SER 188 -0.0000

SER 188 CYS 189 -0.0510

CYS 189 GLY 190 0.0003

GLY 190 ASN 191 0.0054

ASN 191 GLY 192 0.0000

GLY 192 ASN 193 0.0025

ASN 193 GLU 194 0.0003

GLU 194 LYS 195 -0.0050

LYS 195 HIS 196 0.0000

HIS 196 GLU 197 -0.0266

GLU 197 ILE 198 0.0000

ILE 198 LEU 199 -0.0085

LEU 199 PHE 200 0.0000

PHE 200 LEU 201 -0.0104

LEU 201 GLU 202 0.0000

GLU 202 ILE 203 -0.0162

ILE 203 TRP 204 -0.0000

TRP 204 THR 205 -0.0174

THR 205 ASN 206 -0.0002

ASN 206 GLY 207 -0.0021

GLY 207 SER 208 0.0002

SER 208 LEU 209 0.0253

LEU 209 THR 210 0.0002

THR 210 PRO 211 0.0179

PRO 211 LYS 212 -0.0003

LYS 212 GLU 213 0.0069

GLU 213 ALA 214 0.0002

ALA 214 LEU 215 0.0220

LEU 215 TYR 216 -0.0000

TYR 216 GLU 217 -0.0064

GLU 217 ALA 218 -0.0004

ALA 218 SER 219 -0.0119

SER 219 ARG 220 -0.0001

ARG 220 ASN 221 0.0164

ASN 221 LEU 222 0.0004

LEU 222 ILE 223 -0.0079

ILE 223 ASP 224 -0.0000

ASP 224 LEU 225 0.0015

LEU 225 PHE 226 -0.0003

PHE 226 LEU 227 -0.0367

LEU 227 PRO 228 -0.0000

PRO 228 PHE 229 0.0246

PHE 229 LEU 230 0.0001

LEU 230 HIS 231 -0.0155

HIS 231 ALA 232 0.0001

ALA 232 GLU 233 -0.0245

GLU 233 GLU 234 0.0003

GLU 234 GLU 235 0.0081

GLU 235 GLY 236 -0.0001

GLY 236 ALA 237 0.0035

ALA 237 SER 238 0.0000

SER 238 PHE 239 0.0016

PHE 239 GLU 240 -0.0003

GLU 240 GLU 241 -0.0006

GLU 241 ASN 242 -0.0001

ASN 242 LYS 243 0.0014

LYS 243 ASN 244 -0.0003

ASN 244 ARG 245 -0.0235

ARG 245 PHE 246 -0.0004

PHE 246 THR 247 0.0115

THR 247 PRO 248 0.0001

PRO 248 PRO 249 -0.0224

PRO 249 LEU 250 0.0002

LEU 250 PHE 251 0.0142

PHE 251 THR 252 -0.0001

THR 252 PHE 253 0.0049

PHE 253 GLN 254 0.0000

GLN 254 LYS 255 0.0178

LYS 255 ARG 256 -0.0001

ARG 256 LEU 257 0.0013

LEU 257 THR 258 -0.0003

THR 258 ASN 259 0.0233

ASN 259 LEU 260 -0.0003

LEU 260 LYS 261 -0.0072

LYS 261 LYS 262 0.0001

LYS 262 ASN 263 0.0115

ASN 263 LYS 264 -0.0004

LYS 264 LYS 265 0.0047

LYS 265 GLY 266 0.0002

GLY 266 ILE 267 -0.0314

ILE 267 PRO 268 0.0000

PRO 268 LEU 269 -0.0079

LEU 269 ASN 270 0.0001

ASN 270 CYS 271 0.0101

CYS 271 ILE 272 -0.0002

ILE 272 PHE 273 -0.0203

PHE 273 ILE 274 0.0000

ILE 274 ASP 275 -0.0094

ASP 275 GLN 276 0.0002

GLN 276 LEU 277 0.0261

LEU 277 GLU 278 -0.0004

GLU 278 LEU 279 0.0040

LEU 279 THR 280 0.0001

THR 280 SER 281 0.0016

SER 281 ARG 282 -0.0000

ARG 282 THR 283 -0.0002

THR 283 TYR 284 -0.0002

TYR 284 ASN 285 -0.0052

ASN 285 CYS 286 0.0001

CYS 286 LEU 287 0.0026

LEU 287 LYS 288 -0.0002

LYS 288 ARG 289 -0.0049

ARG 289 ALA 290 -0.0003

ALA 290 ASN 291 0.0011

ASN 291 ILE 292 0.0002

ILE 292 HIS 293 -0.0058

HIS 293 THR 294 0.0003

THR 294 LEU 295 0.0011

LEU 295 LEU 296 -0.0001

LEU 296 ASP 297 0.0212

ASP 297 LEU 298 0.0000

LEU 298 LEU 299 -0.0040

LEU 299 SER 300 -0.0002

SER 300 LYS 301 0.0055

LYS 301 THR 302 0.0003

THR 302 GLU 303 -0.0025

GLU 303 GLU 304 0.0001

GLU 304 ASP 305 -0.0012

ASP 305 LEU 306 0.0002

LEU 306 LEU 307 0.0008

LEU 307 ARG 308 0.0001

ARG 308 ILE 309 -0.0039

ILE 309 ASP 310 -0.0002

ASP 310 SER 311 0.0006

SER 311 PHE 312 -0.0001

PHE 312 ARG 313 -0.0007

ARG 313 MET 314 0.0000

MET 314 GLU 315 0.0020

GLU 315 ASP 316 0.0001

ASP 316 ARG 317 -0.0006

ARG 317 LYS 318 0.0003

LYS 318 HIS 319 0.0038

HIS 319 ILE 320 0.0004

ILE 320 TRP 321 0.0001

TRP 321 ASP 322 0.0000

ASP 322 THR 323 0.0018

THR 323 LEU 324 0.0002

LEU 324 GLU 325 0.0030

GLU 325 LYS 326 0.0002

LYS 326 HIS 327 -0.0106

HIS 327 LEU 328 -0.0002

LEU 328 PRO 329 0.0106

PRO 329 ILE 330 0.0000

ILE 330 ASP 331 0.0012

ASP 331 LEU 332 0.0002

LEU 332 LEU 333 -0.0016

LEU 333 LYS 334 0.0001

LYS 334 ASN 335 -0.0011

ASN 335 LYS 336 -0.0002

LYS 336 LEU 337 0.0006

LEU 337 SER 338 -0.0002

SER 338 PHE 339 0.0036

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 25th, 2023.

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

*** ***

CA strain for 240112142738850346

--- normal mode 13 ---

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

* *