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

* *

CA strain for 22092323273356655

--- 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
MET 1 HIS 2 0.0001

HIS 2 GLU 3 -0.0001

GLU 3 LEU 4 -0.0003

LEU 4 LEU 5 -0.0004

LEU 5 THR 6 -0.0003

THR 6 VAL 7 -0.0004

VAL 7 GLN 8 0.0002

GLN 8 GLN 9 0.0002

GLN 9 VAL 10 -0.0001

VAL 10 ASP 11 0.0010

ASP 11 PRO 12 0.0004

PRO 12 TRP 13 0.0014

TRP 13 LEU 14 -0.0001

LEU 14 GLN 15 0.0017

GLN 15 PHE 16 0.0004

PHE 16 ASN 17 0.0034

ASN 17 PRO 18 0.0003

PRO 18 HIS 19 0.0027

HIS 19 ILE 20 0.0001

ILE 20 VAL 21 -0.0018

VAL 21 SER 22 0.0004

SER 22 GLY 23 0.0009

GLY 23 TYR 24 0.0001

TYR 24 ARG 25 0.0011

ARG 25 PRO 26 0.0001

PRO 26 ARG 27 -0.0002

ARG 27 MET 28 -0.0002

MET 28 SER 29 0.0000

SER 29 VAL 30 -0.0001

VAL 30 ARG 31 -0.0001

ARG 31 ALA 32 0.0000

ALA 32 ALA 33 0.0001

ALA 33 LEU 34 0.0001

LEU 34 ARG 35 -0.0006

ARG 35 SER 36 0.0001

SER 36 PHE 37 0.0006

PHE 37 PHE 38 0.0002

PHE 38 GLU 39 -0.0003

GLU 39 TRP 40 -0.0002

TRP 40 HIS 41 0.0003

HIS 41 ASN 42 -0.0000

ASN 42 GLU 43 0.0010

GLU 43 SER 44 -0.0003

SER 44 PHE 45 -0.0003

PHE 45 ASN 46 0.0001

ASN 46 VAL 47 0.0001

VAL 47 TRP 48 0.0001

TRP 48 SER 49 0.0014

SER 49 HIS 50 0.0001

HIS 50 ALA 51 0.0012

ALA 51 LEU 52 0.0000

LEU 52 ALA 53 0.0013

ALA 53 ALA 54 -0.0002

ALA 54 CYS 55 -0.0003

CYS 55 PHE 56 0.0002

PHE 56 VAL 57 0.0002

VAL 57 LEU 58 0.0002

LEU 58 TYR 59 -0.0006

TYR 59 LEU 60 0.0003

LEU 60 ALA 61 -0.0011

ALA 61 LEU 62 0.0002

LEU 62 PHE 63 0.0005

PHE 63 PRO 64 0.0001

PRO 64 PRO 65 -0.0092

PRO 65 THR 66 -0.0002

THR 66 MET 67 -0.0067

MET 67 GLU 68 0.0002

GLU 68 ILE 69 -0.0183

ILE 69 SER 70 0.0005

SER 70 THR 71 -0.0548

THR 71 THR 72 0.0001

THR 72 SER 73 -0.0064

SER 73 THR 74 0.0001

THR 74 VAL 75 -0.0271

VAL 75 ASN 76 0.0001

ASN 76 GLY 77 -0.0105

GLY 77 ARG 78 -0.0001

ARG 78 GLY 79 0.0044

GLY 79 VAL 80 -0.0000

VAL 80 GLY 81 -0.0209

GLY 81 THR 82 0.0001

THR 82 SER 83 0.0193

SER 83 GLY 84 0.0003

GLY 84 MET 85 -0.0193

MET 85 ALA 86 0.0001

ALA 86 PRO 87 0.0162

PRO 87 THR 88 -0.0002

THR 88 ASP 89 -0.0071

ASP 89 VAL 90 -0.0002

VAL 90 SER 91 -0.0402

SER 91 LEU 92 -0.0001

LEU 92 THR 93 -0.0024

THR 93 PRO 94 -0.0000

PRO 94 HIS 95 -0.0021

HIS 95 ASP 96 -0.0004

ASP 96 ARG 97 0.0027

ARG 97 ARG 98 -0.0001

ARG 98 TRP 99 0.0045

TRP 99 LEU 100 -0.0003

LEU 100 GLY 101 0.0014

GLY 101 SER 102 -0.0004

SER 102 SER 103 0.0027

SER 103 SER 104 -0.0002

SER 104 GLU 105 0.0058

GLU 105 HIS 106 0.0001

HIS 106 LEU 107 0.0070

LEU 107 LEU 108 -0.0001

LEU 108 GLY 109 0.0003

GLY 109 ALA 110 0.0002

ALA 110 SER 111 0.0105

SER 111 SER 112 -0.0001

SER 112 THR 113 -0.0050

THR 113 THR 114 0.0001

THR 114 THR 115 0.0026

THR 115 PHE 116 -0.0001

PHE 116 ARG 117 -0.0013

ARG 117 CYS 118 -0.0003

CYS 118 THR 119 0.0024

THR 119 CYS 120 -0.0001

CYS 120 LEU 121 -0.0018

LEU 121 VAL 122 -0.0001

VAL 122 PHE 123 0.0009

PHE 123 PHE 124 0.0001

PHE 124 PHE 125 -0.0009

PHE 125 ILE 126 -0.0001

ILE 126 PHE 127 -0.0012

PHE 127 ILE 128 -0.0003

ILE 128 CYS 129 0.0006

CYS 129 SER 130 0.0001

SER 130 VAL 131 -0.0003

VAL 131 VAL 132 -0.0002

VAL 132 TYR 133 0.0016

TYR 133 HIS 134 -0.0002

HIS 134 LEU 135 -0.0006

LEU 135 PHE 136 -0.0001

PHE 136 MET 137 0.0010

MET 137 PRO 138 -0.0003

PRO 138 CYS 139 -0.0007

CYS 139 THR 140 0.0004

THR 140 THR 141 0.0006

THR 141 SER 142 0.0001

SER 142 GLU 143 -0.0005

GLU 143 SER 144 0.0002

SER 144 LEU 145 -0.0006

LEU 145 TYR 146 0.0001

TYR 146 ARG 147 0.0006

ARG 147 ARG 148 0.0001

ARG 148 LEU 149 -0.0008

LEU 149 LEU 150 0.0004

LEU 150 SER 151 0.0013

SER 151 CYS 152 -0.0002

CYS 152 ASP 153 -0.0002

ASP 153 VAL 154 0.0000

VAL 154 PHE 155 0.0011

PHE 155 GLY 156 0.0002

GLY 156 VAL 157 -0.0002

VAL 157 VAL 158 -0.0002

VAL 158 ILE 159 0.0002

ILE 159 CYS 160 -0.0003

CYS 160 ILE 161 0.0009

ILE 161 THR 162 0.0000

THR 162 GLY 163 0.0009

GLY 163 THR 164 -0.0001

THR 164 SER 165 -0.0008

SER 165 TRP 166 0.0000

TRP 166 SER 167 -0.0008

SER 167 LEU 168 0.0000

LEU 168 VAL 169 -0.0017

VAL 169 TYR 170 -0.0002

TYR 170 ARG 171 0.0031

ARG 171 GLY 172 0.0001

GLY 172 ASN 173 0.0007

ASN 173 ALA 174 0.0001

ALA 174 CYS 175 -0.0007

CYS 175 SER 176 0.0004

SER 176 GLN 177 -0.0012

GLN 177 ASN 178 0.0003

ASN 178 TRP 179 0.0012

TRP 179 SER 180 0.0002

SER 180 CYS 181 -0.0010

CYS 181 HIS 182 0.0001

HIS 182 VAL 183 0.0020

VAL 183 GLY 184 -0.0002

GLY 184 MET 185 -0.0001

MET 185 GLY 186 -0.0001

GLY 186 ALA 187 0.0017

ALA 187 LEU 188 -0.0000

LEU 188 LEU 189 -0.0011

LEU 189 LEU 190 -0.0002

LEU 190 SER 191 0.0004

SER 191 ALA 192 -0.0001

ALA 192 LEU 193 -0.0019

LEU 193 PHE 194 0.0001

PHE 194 VAL 195 0.0011

VAL 195 LEU 196 -0.0002

LEU 196 TYR 197 -0.0009

TYR 197 GLY 198 -0.0003

GLY 198 ALA 199 -0.0000

ALA 199 VAL 200 -0.0002

VAL 200 PHE 201 -0.0008

PHE 201 ASN 202 -0.0001

ASN 202 ALA 203 0.0026

ALA 203 SER 204 0.0001

SER 204 CYS 205 -0.0010

CYS 205 GLY 206 -0.0002

GLY 206 SER 207 0.0012

SER 207 PHE 208 -0.0000

PHE 208 GLY 209 0.0025

GLY 209 ARG 210 -0.0002

ARG 210 PHE 211 -0.0003

PHE 211 LYS 212 0.0001

LYS 212 ALA 213 0.0038

ALA 213 ILE 214 -0.0001

ILE 214 GLY 215 -0.0010

GLY 215 PHE 216 0.0000

PHE 216 HIS 217 0.0010

HIS 217 SER 218 0.0003

SER 218 VAL 219 0.0008

VAL 219 LEU 220 0.0004

LEU 220 ARG 221 -0.0010

ARG 221 PHE 222 0.0002

PHE 222 LEU 223 0.0019

LEU 223 ILE 224 0.0001

ILE 224 LEU 225 -0.0013

LEU 225 LEU 226 -0.0001

LEU 226 TRP 227 0.0011

TRP 227 VAL 228 0.0002

VAL 228 GLU 229 0.0002

GLU 229 LEU 230 0.0003

LEU 230 PRO 231 -0.0000

PRO 231 LYS 232 0.0001

LYS 232 VAL 233 0.0008

VAL 233 GLN 234 -0.0000

GLN 234 SER 235 0.0007

SER 235 GLN 236 0.0003

GLN 236 GLY 237 0.0024

GLY 237 TYR 238 -0.0003

TYR 238 HIS 239 -0.0044

HIS 239 GLN 240 -0.0005

GLN 240 ALA 241 0.0019

ALA 241 VAL 242 -0.0001

VAL 242 HIS 243 -0.0005

HIS 243 CYS 244 0.0000

CYS 244 HIS 245 -0.0013

HIS 245 ALA 246 -0.0003

ALA 246 MET 247 0.0021

MET 247 SER 248 -0.0001

SER 248 PHE 249 -0.0003

PHE 249 VAL 250 -0.0002

VAL 250 PHE 251 0.0024

PHE 251 LEU 252 -0.0002

LEU 252 ALA 253 0.0004

ALA 253 LEU 254 0.0001

LEU 254 GLY 255 0.0012

GLY 255 ALA 256 0.0000

ALA 256 VAL 257 0.0018

VAL 257 ILE 258 -0.0000

ILE 258 ASN 259 -0.0014

ASN 259 ALA 260 0.0001

ALA 260 LEU 261 0.0052

LEU 261 ARG 262 -0.0002

ARG 262 PHE 263 0.0011

PHE 263 PRO 264 0.0005

PRO 264 GLU 265 -0.0004

GLU 265 LYS 266 -0.0001

LYS 266 HIS 267 0.0026

HIS 267 LEU 268 -0.0000

LEU 268 ARG 269 0.0005

ARG 269 ARG 270 -0.0002

ARG 270 ALA 271 0.0027

ALA 271 THR 272 -0.0003

THR 272 ARG 273 -0.0000

ARG 273 LEU 274 0.0002

LEU 274 LEU 275 0.0003

LEU 275 PRO 276 -0.0001

PRO 276 ALA 277 0.0008

ALA 277 SER 278 -0.0000

SER 278 SER 279 -0.0005

SER 279 SER 280 -0.0001

SER 280 SER 281 0.0003

SER 281 PRO 282 -0.0002

PRO 282 GLU 283 -0.0004

GLU 283 ALA 284 -0.0000

ALA 284 THR 285 0.0007

THR 285 VAL 286 -0.0004

VAL 286 ALA 287 0.0002

ALA 287 SER 288 -0.0002

SER 288 ARG 289 0.0005

ARG 289 CYS 290 0.0003

CYS 290 TRP 291 -0.0002

TRP 291 ARG 292 0.0001

ARG 292 TRP 293 0.0009

TRP 293 LEU 294 -0.0004

LEU 294 GLY 295 0.0007

GLY 295 ARG 296 -0.0001

ARG 296 PHE 297 0.0008

PHE 297 VAL 298 -0.0003

VAL 298 VAL 299 0.0002

VAL 299 SER 300 0.0000

SER 300 GLY 301 0.0015

GLY 301 GLU 302 0.0002

GLU 302 GLU 303 0.0000

GLU 303 ILE 304 0.0005

ILE 304 ASP 305 -0.0008

ASP 305 TYR 306 0.0000

TYR 306 THR 307 -0.0006

THR 307 TRP 308 -0.0001

TRP 308 ASN 309 0.0012

ASN 309 SER 310 0.0000

SER 310 HIS 311 0.0000

HIS 311 GLY 312 0.0001

GLY 312 PHE 313 0.0001

PHE 313 TRP 314 0.0000

TRP 314 HIS 315 -0.0006

HIS 315 TYR 316 0.0002

TYR 316 CYS 317 0.0004

CYS 317 ILE 318 0.0002

ILE 318 ILE 319 0.0010

ILE 319 LEU 320 0.0001

LEU 320 SER 321 0.0011

SER 321 THR 322 -0.0003

THR 322 THR 323 0.0004

THR 323 MET 324 0.0002

MET 324 MET 325 -0.0003

MET 325 LEU 326 -0.0001

LEU 326 LEU 327 0.0016

LEU 327 GLY 328 0.0001

GLY 328 CYS 329 0.0025

CYS 329 TYR 330 0.0003

TYR 330 TYR 331 0.0067

TYR 331 ASP 332 -0.0001

ASP 332 LEU 333 -0.0015

LEU 333 GLU 334 -0.0001

GLU 334 GLU 335 0.0022

GLU 335 PHE 336 0.0001

PHE 336 GLU 337 0.0049

GLU 337 LEU 338 0.0001

LEU 338 ALA 339 0.0022

ALA 339 LYS 340 -0.0001

LYS 340 CYS 341 0.0017

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 22092323273356655

--- normal mode 8 ---

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

* *