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

* mexA_monomer *

CA strain for 22011814491968286

--- normal mode 8 ---

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
CYS 1 GLY 2 0.0002

GLY 2 LYS 3 -0.0021

LYS 3 SER 4 -0.0010

SER 4 GLU 5 -0.0015

GLU 5 ALA 6 0.0000

ALA 6 PRO 7 -0.0333

PRO 7 PRO 8 -0.0000

PRO 8 PRO 9 0.0781

PRO 9 ALA 10 -0.0004

ALA 10 GLN 11 -0.0138

GLN 11 THR 12 0.0003

THR 12 PRO 13 -0.0049

PRO 13 GLU 14 -0.0000

GLU 14 VAL 15 0.0013

VAL 15 GLY 16 -0.0002

GLY 16 ILE 17 0.0002

ILE 17 VAL 18 -0.0003

VAL 18 THR 19 0.0009

THR 19 LEU 20 -0.0001

LEU 20 GLU 21 0.0063

GLU 21 ALA 22 -0.0002

ALA 22 GLN 23 0.0056

GLN 23 THR 24 0.0004

THR 24 VAL 25 -0.0020

VAL 25 THR 26 0.0001

THR 26 LEU 27 -0.0015

LEU 27 ASN 28 0.0001

ASN 28 THR 29 -0.0091

THR 29 GLU 30 0.0001

GLU 30 LEU 31 -0.0043

LEU 31 PRO 32 0.0002

PRO 32 GLY 33 -0.0067

GLY 33 ARG 34 0.0000

ARG 34 THR 35 -0.0012

THR 35 ASN 36 -0.0004

ASN 36 ALA 37 -0.0056

ALA 37 PHE 38 -0.0000

PHE 38 ARG 39 0.0084

ARG 39 ILE 40 0.0005

ILE 40 ALA 41 0.0065

ALA 41 GLU 42 -0.0003

GLU 42 VAL 43 0.0018

VAL 43 ARG 44 0.0002

ARG 44 PRO 45 0.0034

PRO 45 GLN 46 0.0001

GLN 46 VAL 47 0.0001

VAL 47 ASN 48 0.0002

ASN 48 GLY 49 -0.0006

GLY 49 ILE 50 0.0002

ILE 50 ILE 51 -0.0000

ILE 51 LEU 52 -0.0001

LEU 52 LYS 53 -0.0036

LYS 53 ARG 54 0.0002

ARG 54 LEU 55 0.0009

LEU 55 PHE 56 -0.0001

PHE 56 LYS 57 -0.0006

LYS 57 GLU 58 0.0001

GLU 58 GLY 59 -0.0070

GLY 59 SER 60 -0.0000

SER 60 ASP 61 0.0010

ASP 61 VAL 62 0.0000

VAL 62 LYS 63 -0.0020

LYS 63 ALA 64 0.0002

ALA 64 GLY 65 0.0034

GLY 65 GLN 66 -0.0002

GLN 66 GLN 67 0.0032

GLN 67 LEU 68 -0.0003

LEU 68 TYR 69 0.0014

TYR 69 GLN 70 0.0002

GLN 70 ILE 71 -0.0007

ILE 71 ASP 72 0.0000

ASP 72 PRO 73 -0.0052

PRO 73 ALA 74 -0.0001

ALA 74 THR 75 -0.0004

THR 75 TYR 76 -0.0001

TYR 76 GLU 77 0.0020

GLU 77 ALA 78 0.0001

ALA 78 ASP 79 0.0005

ASP 79 TYR 80 0.0003

TYR 80 GLN 81 0.0019

GLN 81 SER 82 -0.0006

SER 82 ALA 83 0.0001

ALA 83 GLN 84 0.0000

GLN 84 ALA 85 0.0018

ALA 85 ASN 86 -0.0002

ASN 86 LEU 87 0.0011

LEU 87 ALA 88 0.0002

ALA 88 SER 89 0.0009

SER 89 THR 90 -0.0002

THR 90 GLN 91 -0.0000

GLN 91 GLU 92 -0.0001

GLU 92 GLN 93 0.0002

GLN 93 ALA 94 -0.0002

ALA 94 GLN 95 -0.0004

GLN 95 ARG 96 -0.0000

ARG 96 TYR 97 0.0001

TYR 97 LYS 98 0.0003

LYS 98 LEU 99 -0.0002

LEU 99 LEU 100 0.0001

LEU 100 VAL 101 -0.0003

VAL 101 ALA 102 0.0001

ALA 102 ASP 103 0.0005

ASP 103 GLN 104 0.0000

GLN 104 ALA 105 -0.0003

ALA 105 VAL 106 -0.0000

VAL 106 SER 107 -0.0001

SER 107 LYS 108 -0.0001

LYS 108 GLN 109 -0.0004

GLN 109 GLN 110 -0.0004

GLN 110 TYR 111 0.0004

TYR 111 ALA 112 0.0002

ALA 112 ASP 113 -0.0003

ASP 113 ALA 114 0.0001

ALA 114 ASN 115 -0.0005

ASN 115 ALA 116 -0.0000

ALA 116 ALA 117 -0.0003

ALA 117 TYR 118 0.0002

TYR 118 LEU 119 -0.0005

LEU 119 GLN 120 0.0000

GLN 120 SER 121 -0.0004

SER 121 LYS 122 -0.0002

LYS 122 ALA 123 0.0003

ALA 123 ALA 124 0.0001

ALA 124 VAL 125 -0.0005

VAL 125 GLU 126 -0.0001

GLU 126 GLN 127 -0.0010

GLN 127 ALA 128 0.0001

ALA 128 ARG 129 -0.0002

ARG 129 ILE 130 -0.0003

ILE 130 ASN 131 -0.0008

ASN 131 LEU 132 -0.0001

LEU 132 ARG 133 0.0025

ARG 133 TYR 134 -0.0001

TYR 134 THR 135 -0.0002

THR 135 LYS 136 0.0001

LYS 136 VAL 137 0.0025

VAL 137 LEU 138 0.0004

LEU 138 SER 139 0.0072

SER 139 PRO 140 -0.0002

PRO 140 ILE 141 0.0112

ILE 141 SER 142 -0.0001

SER 142 GLY 143 -0.0005

GLY 143 ARG 144 -0.0001

ARG 144 ILE 145 -0.0037

ILE 145 GLY 146 0.0000

GLY 146 ARG 147 -0.0064

ARG 147 SER 148 -0.0001

SER 148 ALA 149 0.0004

ALA 149 VAL 150 -0.0002

VAL 150 THR 151 0.0014

THR 151 GLU 152 0.0002

GLU 152 GLY 153 0.0002

GLY 153 ALA 154 0.0000

ALA 154 LEU 155 0.0004

LEU 155 VAL 156 0.0001

VAL 156 THR 157 0.0007

THR 157 ASN 158 -0.0000

ASN 158 GLY 159 0.0010

GLY 159 GLN 160 0.0003

GLN 160 ALA 161 -0.0003

ALA 161 ASN 162 -0.0001

ASN 162 ALA 163 -0.0003

ALA 163 MET 164 -0.0001

MET 164 ALA 165 -0.0037

ALA 165 THR 166 0.0000

THR 166 VAL 167 0.0001

VAL 167 GLN 168 0.0001

GLN 168 GLN 169 0.0018

GLN 169 LEU 170 -0.0003

LEU 170 ASP 171 -0.0019

ASP 171 PRO 172 -0.0001

PRO 172 ILE 173 -0.0019

ILE 173 TYR 174 0.0001

TYR 174 VAL 175 0.0014

VAL 175 ASP 176 -0.0000

ASP 176 VAL 177 -0.0014

VAL 177 THR 178 0.0001

THR 178 GLN 179 0.0006

GLN 179 PRO 180 0.0002

PRO 180 SER 181 0.0030

SER 181 THR 182 -0.0000

THR 182 ALA 183 0.0004

ALA 183 LEU 184 0.0001

LEU 184 LEU 185 0.0028

LEU 185 ARG 186 0.0002

ARG 186 LEU 187 -0.0007

LEU 187 ARG 188 0.0003

ARG 188 ARG 189 0.0017

ARG 189 GLU 190 0.0004

GLU 190 LEU 191 -0.0024

LEU 191 ALA 192 0.0002

ALA 192 SER 193 -0.0014

SER 193 GLY 194 0.0000

GLY 194 GLN 195 0.0010

GLN 195 LEU 196 0.0001

LEU 196 GLU 197 0.0018

GLU 197 ARG 198 0.0002

ARG 198 ALA 199 0.0075

ALA 199 GLY 200 0.0001

GLY 200 ASP 201 0.0026

ASP 201 ASN 202 0.0003

ASN 202 ALA 203 0.0023

ALA 203 ALA 204 -0.0002

ALA 204 LYS 205 0.0038

LYS 205 VAL 206 0.0000

VAL 206 SER 207 -0.0021

SER 207 LEU 208 -0.0001

LEU 208 LYS 209 0.0014

LYS 209 LEU 210 -0.0003

LEU 210 GLU 211 0.0012

GLU 211 ASP 212 -0.0001

ASP 212 GLY 213 -0.0007

GLY 213 SER 214 0.0000

SER 214 GLN 215 0.0002

GLN 215 TYR 216 -0.0002

TYR 216 PRO 217 0.0016

PRO 217 LEU 218 0.0002

LEU 218 GLU 219 -0.0017

GLU 219 GLY 220 -0.0000

GLY 220 ARG 221 -0.0054

ARG 221 LEU 222 -0.0002

LEU 222 GLU 223 -0.0005

GLU 223 PHE 224 0.0000

PHE 224 SER 225 -0.0003

SER 225 GLU 226 -0.0001

GLU 226 VAL 227 0.0021

VAL 227 SER 228 0.0000

SER 228 VAL 229 -0.0013

VAL 229 ASP 230 0.0002

ASP 230 GLU 231 -0.0005

GLU 231 GLY 232 -0.0002

GLY 232 THR 233 0.0000

THR 233 GLY 234 0.0002

GLY 234 SER 235 0.0000

SER 235 VAL 236 0.0001

VAL 236 THR 237 0.0025

THR 237 ILE 238 -0.0002

ILE 238 ARG 239 0.0018

ARG 239 ALA 240 0.0002

ALA 240 VAL 241 -0.0002

VAL 241 PHE 242 -0.0001

PHE 242 PRO 243 -0.0016

PRO 243 ASN 244 0.0002

ASN 244 PRO 245 -0.0007

PRO 245 ASN 246 0.0001

ASN 246 ASN 247 -0.0008

ASN 247 GLU 248 -0.0002

GLU 248 LEU 249 0.0018

LEU 249 LEU 250 -0.0000

LEU 250 PRO 251 0.0002

PRO 251 GLY 252 0.0005

GLY 252 MET 253 -0.0046

MET 253 PHE 254 -0.0002

PHE 254 VAL 255 -0.0030

VAL 255 HIS 256 -0.0002

HIS 256 ALA 257 -0.0005

ALA 257 GLN 258 0.0002

GLN 258 LEU 259 0.0007

LEU 259 GLN 260 0.0002

GLN 260 GLU 261 0.0030

GLU 261 GLY 262 0.0002

GLY 262 VAL 263 0.0055

VAL 263 LYS 264 0.0002

LYS 264 GLN 265 -0.0023

GLN 265 LYS 266 0.0001

LYS 266 ALA 267 -0.0035

ALA 267 ILE 268 0.0001

ILE 268 LEU 269 0.0036

LEU 269 ALA 270 -0.0002

ALA 270 PRO 271 0.0022

PRO 271 GLN 272 0.0002

GLN 272 GLN 273 -0.0069

GLN 273 GLY 274 0.0001

GLY 274 VAL 275 0.0000

VAL 275 THR 276 -0.0000

THR 276 ARG 277 0.0006

ARG 277 ASP 278 -0.0002

ASP 278 LEU 279 0.0003

LEU 279 LYS 280 0.0001

LYS 280 GLY 281 -0.0004

GLY 281 GLN 282 -0.0002

GLN 282 ALA 283 -0.0009

ALA 283 THR 284 -0.0003

THR 284 ALA 285 0.0009

ALA 285 LEU 286 0.0000

LEU 286 VAL 287 0.0002

VAL 287 VAL 288 0.0004

VAL 288 ASN 289 -0.0015

ASN 289 ALA 290 -0.0000

ALA 290 GLN 291 0.0006

GLN 291 ASN 292 0.0003

ASN 292 LYS 293 -0.0027

LYS 293 VAL 294 -0.0001

VAL 294 GLU 295 0.0012

GLU 295 LEU 296 0.0000

LEU 296 ARG 297 0.0003

ARG 297 VAL 298 -0.0002

VAL 298 ILE 299 0.0001

ILE 299 LYS 300 -0.0004

LYS 300 ALA 301 -0.0007

ALA 301 ASP 302 -0.0002

ASP 302 ARG 303 -0.0006

ARG 303 VAL 304 0.0001

VAL 304 ILE 305 0.0024

ILE 305 GLY 306 0.0003

GLY 306 ASP 307 -0.0050

ASP 307 LYS 308 0.0002

LYS 308 TRP 309 0.0021

TRP 309 LEU 310 0.0003

LEU 310 VAL 311 -0.0018

VAL 311 THR 312 -0.0001

THR 312 GLU 313 0.0042

GLU 313 GLY 314 0.0005

GLY 314 LEU 315 -0.0002

LEU 315 ASN 316 0.0001

ASN 316 ALA 317 -0.0018

ALA 317 GLY 318 -0.0002

GLY 318 ASP 319 0.0033

ASP 319 LYS 320 -0.0001

LYS 320 ILE 321 0.0009

ILE 321 ILE 322 -0.0000

ILE 322 THR 323 -0.0005

THR 323 GLU 324 0.0003

GLU 324 GLY 325 -0.0068

GLY 325 LEU 326 0.0001

LEU 326 GLN 327 -0.0025

GLN 327 PHE 328 0.0004

PHE 328 VAL 329 0.0054

VAL 329 GLN 330 0.0001

GLN 330 PRO 331 0.0021

PRO 331 GLY 332 -0.0001

GLY 332 VAL 333 -0.0016

VAL 333 GLU 334 0.0001

GLU 334 VAL 335 0.0026

VAL 335 LYS 336 -0.0000

LYS 336 THR 337 0.0157

THR 337 VAL 338 0.0001

VAL 338 PRO 339 0.0056

PRO 339 ALA 340 0.0001

ALA 340 LYS 341 0.0004

LYS 341 ASN 342 -0.0004

ASN 342 VAL 343 0.0006

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.

*** mexA_monomer ***

CA strain for 22011814491968286

--- normal mode 8 ---

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

* mexA_monomer *