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

* GG domain *

CA strain for 2503041457022018102

--- normal mode 9 ---

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 GLU 2 -0.0001

GLU 2 ALA 3 -0.0002

ALA 3 LEU 4 -0.0001

LEU 4 ILE 5 -0.0003

ILE 5 PRO 6 -0.0006

PRO 6 VAL 7 -0.0002

VAL 7 ILE 8 0.0002

ILE 8 ASN 9 0.0002

ASN 9 LYS 10 -0.0003

LYS 10 LEU 11 0.0001

LEU 11 GLN 12 0.0002

GLN 12 ASP 13 -0.0000

ASP 13 VAL 14 -0.0000

VAL 14 PHE 15 -0.0001

PHE 15 ASN 16 -0.0000

ASN 16 THR 17 -0.0002

THR 17 VAL 18 -0.0002

VAL 18 GLY 19 0.0000

GLY 19 ALA 20 -0.0003

ALA 20 ASP 21 -0.0002

ASP 21 ILE 22 0.0006

ILE 22 ILE 23 0.0001

ILE 23 GLN 24 0.0002

GLN 24 LEU 25 0.0002

LEU 25 PRO 26 -0.0001

PRO 26 GLN 27 -0.0002

GLN 27 ILE 28 0.0002

ILE 28 VAL 29 0.0002

VAL 29 VAL 30 0.0005

VAL 30 VAL 31 0.0003

VAL 31 GLY 32 -0.0004

GLY 32 THR 33 0.0001

THR 33 GLN 34 0.0002

GLN 34 SER 35 0.0003

SER 35 SER 36 -0.0000

SER 36 GLY 37 0.0000

GLY 37 LYS 38 0.0004

LYS 38 SER 39 -0.0001

SER 39 SER 40 0.0002

SER 40 VAL 41 0.0003

VAL 41 LEU 42 0.0002

LEU 42 GLU 43 0.0001

GLU 43 SER 44 -0.0000

SER 44 LEU 45 0.0002

LEU 45 VAL 46 -0.0000

VAL 46 GLY 47 -0.0002

GLY 47 ARG 48 -0.0002

ARG 48 ASP 49 -0.0001

ASP 49 LEU 50 -0.0001

LEU 50 LEU 51 -0.0003

LEU 51 PRO 52 0.0001

PRO 52 ARG 53 0.0002

ARG 53 GLY 54 0.0002

GLY 54 THR 55 -0.0001

THR 55 GLY 56 -0.0003

GLY 56 ILE 57 0.0000

ILE 57 VAL 58 0.0004

VAL 58 THR 59 0.0001

THR 59 ARG 60 0.0003

ARG 60 ARG 61 -0.0003

ARG 61 PRO 62 0.0000

PRO 62 LEU 63 -0.0002

LEU 63 ILE 64 0.0001

ILE 64 LEU 65 -0.0002

LEU 65 GLN 66 0.0002

GLN 66 LEU 67 0.0000

LEU 67 VAL 68 0.0001

VAL 68 HSD 69 -0.0000

HSD 69 VAL 70 0.0000

VAL 70 SER 71 0.0001

SER 71 GLN 72 -0.0000

GLN 72 GLU 73 0.0001

GLU 73 ASP 74 -0.0002

ASP 74 LYS 75 -0.0001

LYS 75 ARG 76 -0.0002

ARG 76 LYS 77 0.0003

LYS 77 THR 78 -0.0003

THR 78 THR 79 0.0004

THR 79 GLY 80 0.0003

GLY 80 GLU 81 -0.0002

GLU 81 GLU 82 -0.0002

GLU 82 ASN 83 0.0002

ASN 83 GLY 84 -0.0001

GLY 84 VAL 85 0.0000

VAL 85 GLU 86 -0.0004

GLU 86 ALA 87 0.0001

ALA 87 GLU 88 -0.0000

GLU 88 GLU 89 0.0001

GLU 89 TRP 90 -0.0001

TRP 90 GLY 91 0.0002

GLY 91 LYS 92 -0.0005

LYS 92 PHE 93 0.0003

PHE 93 LEU 94 -0.0001

LEU 94 HSD 95 0.0003

HSD 95 THR 96 0.0001

THR 96 LYS 97 0.0000

LYS 97 ASN 98 0.0001

ASN 98 LYS 99 0.0001

LYS 99 LEU 100 0.0000

LEU 100 TYR 101 -0.0002

TYR 101 THR 102 0.0002

THR 102 ASP 103 -0.0001

ASP 103 PHE 104 0.0000

PHE 104 ASP 105 0.0003

ASP 105 GLU 106 0.0002

GLU 106 ILE 107 -0.0003

ILE 107 ARG 108 0.0000

ARG 108 GLN 109 0.0001

GLN 109 GLU 110 -0.0002

GLU 110 ILE 111 0.0001

ILE 111 GLU 112 0.0004

GLU 112 ASN 113 -0.0001

ASN 113 GLU 114 -0.0000

GLU 114 THR 115 0.0002

THR 115 GLU 116 -0.0004

GLU 116 ARG 117 -0.0000

ARG 117 ILE 118 -0.0004

ILE 118 SER 119 0.0001

SER 119 GLY 120 0.0003

GLY 120 ASN 121 -0.0002

ASN 121 ASN 122 0.0001

ASN 122 LYS 123 0.0002

LYS 123 GLY 124 0.0000

GLY 124 VAL 125 0.0001

VAL 125 SER 126 -0.0003

SER 126 PRO 127 -0.0001

PRO 127 GLU 128 -0.0003

GLU 128 PRO 129 -0.0000

PRO 129 ILE 130 0.0001

ILE 130 HSD 131 0.0003

HSD 131 LEU 132 -0.0001

LEU 132 LYS 133 0.0002

LYS 133 ILE 134 -0.0001

ILE 134 PHE 135 -0.0001

PHE 135 SER 136 0.0000

SER 136 PRO 137 0.0001

PRO 137 ASN 138 0.0002

ASN 138 VAL 139 0.0001

VAL 139 VAL 140 -0.0002

VAL 140 ASN 141 -0.0000

ASN 141 LEU 142 0.0002

LEU 142 THR 143 0.0002

THR 143 LEU 144 -0.0001

LEU 144 VAL 145 0.0000

VAL 145 ASP 146 0.0003

ASP 146 LEU 147 -0.0002

LEU 147 PRO 148 0.0000

PRO 148 GLY 149 -0.0001

GLY 149 MET 150 -0.0002

MET 150 THR 151 0.0002

THR 151 LYS 152 -0.0001

LYS 152 VAL 153 -0.0001

VAL 153 PRO 154 0.0002

PRO 154 VAL 155 -0.0002

VAL 155 GLY 156 0.0002

GLY 156 ASP 157 -0.0001

ASP 157 GLN 158 -0.0002

GLN 158 PRO 159 0.0002

PRO 159 LYS 160 0.0004

LYS 160 ASP 161 0.0002

ASP 161 ILE 162 -0.0000

ILE 162 GLU 163 -0.0002

GLU 163 LEU 164 0.0002

LEU 164 GLN 165 -0.0002

GLN 165 ILE 166 -0.0001

ILE 166 ARG 167 -0.0002

ARG 167 GLU 168 0.0001

GLU 168 LEU 169 0.0003

LEU 169 ILE 170 -0.0002

ILE 170 LEU 171 -0.0001

LEU 171 ARG 172 0.0003

ARG 172 PHE 173 0.0002

PHE 173 ILE 174 -0.0003

ILE 174 SER 175 -0.0002

SER 175 ASN 176 0.0001

ASN 176 PRO 177 0.0003

PRO 177 ASN 178 -0.0001

ASN 178 SER 179 0.0002

SER 179 ILE 180 0.0002

ILE 180 ILE 181 -0.0003

ILE 181 LEU 182 0.0001

LEU 182 ALA 183 0.0000

ALA 183 VAL 184 -0.0002

VAL 184 THR 185 -0.0002

THR 185 ALA 186 -0.0005

ALA 186 ALA 187 0.0004

ALA 187 ASN 188 -0.0000

ASN 188 THR 189 0.0002

THR 189 ASP 190 -0.0002

ASP 190 MET 191 0.0001

MET 191 ALA 192 -0.0002

ALA 192 THR 193 -0.0003

THR 193 SER 194 0.0003

SER 194 GLU 195 0.0003

GLU 195 ALA 196 -0.0000

ALA 196 LEU 197 0.0001

LEU 197 LYS 198 0.0001

LYS 198 ILE 199 0.0001

ILE 199 SER 200 0.0003

SER 200 ARG 201 -0.0003

ARG 201 GLU 202 -0.0002

GLU 202 VAL 203 -0.0002

VAL 203 ASP 204 -0.0002

ASP 204 PRO 205 -0.0001

PRO 205 ASP 206 -0.0000

ASP 206 GLY 207 -0.0003

GLY 207 ARG 208 -0.0003

ARG 208 ARG 209 0.0002

ARG 209 THR 210 0.0000

THR 210 LEU 211 0.0000

LEU 211 ALA 212 0.0002

ALA 212 VAL 213 -0.0001

VAL 213 ILE 214 0.0004

ILE 214 THR 215 -0.0001

THR 215 LYS 216 -0.0000

LYS 216 LEU 217 0.0000

LEU 217 ASP 218 -0.0000

ASP 218 LEU 219 0.0001

LEU 219 MET 220 -0.0001

MET 220 ASP 221 0.0002

ASP 221 ALA 222 0.0001

ALA 222 GLY 223 0.0001

GLY 223 THR 224 0.0001

THR 224 ASP 225 -0.0002

ASP 225 ALA 226 0.0003

ALA 226 MET 227 -0.0001

MET 227 ASP 228 -0.0000

ASP 228 VAL 229 0.0004

VAL 229 LEU 230 -0.0003

LEU 230 MET 231 0.0002

MET 231 GLY 232 0.0003

GLY 232 ARG 233 -0.0002

ARG 233 VAL 234 -0.0002

VAL 234 ILE 235 0.0001

ILE 235 PRO 236 0.0001

PRO 236 VAL 237 0.0002

VAL 237 LYS 238 -0.0003

LYS 238 LEU 239 0.0002

LEU 239 GLY 240 -0.0002

GLY 240 ILE 241 0.0000

ILE 241 ILE 242 0.0003

ILE 242 GLY 243 -0.0004

GLY 243 VAL 244 0.0001

VAL 244 VAL 245 0.0003

VAL 245 ASN 246 -0.0003

ASN 246 ARG 247 0.0001

ARG 247 SER 248 -0.0001

SER 248 GLN 249 0.0001

GLN 249 LEU 250 0.0002

LEU 250 ASP 251 -0.0001

ASP 251 ILE 252 0.0000

ILE 252 ASN 253 0.0002

ASN 253 ASN 254 0.0003

ASN 254 LYS 255 -0.0002

LYS 255 LYS 256 -0.0001

LYS 256 SER 257 -0.0000

SER 257 VAL 258 0.0001

VAL 258 THR 259 -0.0002

THR 259 ASP 260 0.0002

ASP 260 SER 261 0.0002

SER 261 ILE 262 0.0000

ILE 262 ARG 263 -0.0003

ARG 263 ASP 264 0.0003

ASP 264 GLU 265 0.0001

GLU 265 TYR 266 -0.0000

TYR 266 ALA 267 -0.0003

ALA 267 PHE 268 0.0001

PHE 268 LEU 269 -0.0001

LEU 269 GLN 270 0.0002

GLN 270 LYS 271 -0.0001

LYS 271 LYS 272 -0.0000

LYS 272 TYR 273 -0.0000

TYR 273 PRO 274 0.0001

PRO 274 SER 275 0.0000

SER 275 LEU 276 -0.0002

LEU 276 ALA 277 -0.0000

ALA 277 ASN 278 -0.0002

ASN 278 ARG 279 0.0002

ARG 279 ASN 280 0.0000

ASN 280 GLY 281 -0.0004

GLY 281 THR 282 0.0002

THR 282 LYS 283 -0.0002

LYS 283 TYR 284 0.0001

TYR 284 LEU 285 -0.0001

LEU 285 ALA 286 0.0002

ALA 286 ARG 287 -0.0004

ARG 287 THR 288 -0.0001

THR 288 LEU 289 0.0003

LEU 289 ASN 290 0.0001

ASN 290 ARG 291 -0.0002

ARG 291 LEU 292 -0.0000

LEU 292 LEU 293 0.0002

LEU 293 MET 294 0.0004

MET 294 HSD 295 -0.0003

HSD 295 HSD 296 -0.0001

HSD 296 ILE 297 0.0001

ILE 297 ARG 298 0.0002

ARG 298 ASP 299 -0.0000

ASP 299 CYS 300 -0.0001

CYS 300 LEU 301 0.0001

LEU 301 PRO 302 0.0000

PRO 302 GLU 303 -0.0003

GLU 303 LEU 304 0.0002

LEU 304 LYS 305 -0.0004

LYS 305 THR 306 0.0004

THR 306 ARG 307 0.0003

ARG 307 ILE 308 0.0003

ILE 308 ASN 309 0.0001

ASN 309 VAL 310 -0.0003

VAL 310 LEU 311 -0.0004

LEU 311 ALA 312 -0.0005

ALA 312 ALA 313 -0.0000

ALA 313 GLN 314 0.0002

GLN 314 TYR 315 -0.0000

TYR 315 GLN 316 0.0001

GLN 316 SER 317 0.0003

SER 317 LEU 318 -0.0004

LEU 318 LEU 319 0.0002

LEU 319 ASN 320 -0.0000

ASN 320 SER 321 0.0004

SER 321 TYR 322 -0.0002

TYR 322 GLY 323 -0.0000

GLY 323 GLU 324 0.0000

GLU 324 PRO 325 -0.0002

PRO 325 VAL 326 -0.0000

VAL 326 ASP 327 0.0001

ASP 327 GLY 703 0.0002

GLY 703 SER 704 -0.0000

SER 704 GLY 705 0.0002

GLY 705 SER 706 -0.0003

SER 706 GLY 707 -0.0003

GLY 707 SER 708 -0.0000

SER 708 GLY 709 -0.0004

GLY 709 SER 710 0.0003

SER 710 LYS 711 0.0000

LYS 711 GLU 712 0.0003

GLU 712 ALA 713 -0.0003

ALA 713 ALA 714 -0.0003

ALA 714 ASP 715 -0.0001

ASP 715 MET 716 0.0005

MET 716 LEU 717 0.0003

LEU 717 LYS 718 -0.0001

LYS 718 ALA 719 0.0001

ALA 719 LEU 720 0.0001

LEU 720 GLN 721 -0.0002

GLN 721 GLY 722 -0.0002

GLY 722 ALA 723 0.0000

ALA 723 SER 724 -0.0005

SER 724 GLN 725 0.0002

GLN 725 ILE 726 -0.0001

ILE 726 ILE 727 0.0001

ILE 727 ALA 728 0.0002

ALA 728 GLU 729 0.0000

GLU 729 ILE 730 -0.0002

ILE 730 ARG 731 0.0004

ARG 731 GLU 732 -0.0000

GLU 732 THR 733 -0.0001

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 8th, 2025.

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

*** GG domain ***

CA strain for 2503041457022018102

--- normal mode 9 ---

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

* GG domain *