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

* 01-JUN-22 *

CA strain for 240221025813253280

--- 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 ALA 2 -0.0006

ALA 2 ASN 3 0.0023

ASN 3 SER 4 -0.0005

SER 4 ALA 5 0.0287

ALA 5 SER 6 -0.0002

SER 6 PRO 7 -0.0397

PRO 7 GLU 8 -0.0001

GLU 8 GLN 9 -0.0149

GLN 9 ASN 10 -0.0004

ASN 10 GLN 11 0.0271

GLN 11 ASN 12 -0.0001

ASN 12 HIS 13 0.0122

HIS 13 CYS 14 0.0001

CYS 14 SER 15 0.0089

SER 15 ALA 16 0.0002

ALA 16 ILE 17 -0.0152

ILE 17 ASN 18 -0.0005

ASN 18 ASN 19 -0.0042

ASN 19 SER 20 0.0003

SER 20 ILE 21 -0.0001

ILE 21 PRO 22 -0.0001

PRO 22 LEU 23 0.0001

LEU 23 MET 24 -0.0002

MET 24 GLN 25 -0.0005

GLN 25 GLY 26 -0.0000

GLY 26 ASN 27 -0.0004

ASN 27 LEU 28 0.0005

LEU 28 PRO 29 0.0014

PRO 29 THR 30 0.0001

THR 30 LEU 31 0.0005

LEU 31 THR 32 -0.0005

THR 32 LEU 33 0.0002

LEU 33 SER 34 0.0002

SER 34 GLY 35 -0.0005

GLY 35 LYS 36 0.0001

LYS 36 ILE 37 0.0001

ILE 37 ARG 38 0.0002

ARG 38 VAL 39 0.0002

VAL 39 THR 40 -0.0003

THR 40 VAL 41 -0.0003

VAL 41 THR 42 -0.0001

THR 42 PHE 43 0.0007

PHE 43 PHE 44 0.0001

PHE 44 LEU 45 -0.0001

LEU 45 PHE 46 -0.0003

PHE 46 LEU 47 0.0002

LEU 47 LEU 48 0.0002

LEU 48 SER 49 -0.0002

SER 49 ALA 50 0.0001

ALA 50 THR 51 -0.0000

THR 51 PHE 52 -0.0001

PHE 52 ASN 53 0.0002

ASN 53 ALA 54 0.0001

ALA 54 SER 55 0.0000

SER 55 PHE 56 -0.0003

PHE 56 LEU 57 0.0001

LEU 57 LEU 58 0.0001

LEU 58 LYS 59 -0.0007

LYS 59 LEU 60 0.0001

LEU 60 GLN 61 0.0002

GLN 61 LYS 62 -0.0001

LYS 62 TRP 63 0.0001

TRP 63 THR 64 -0.0000

THR 64 GLN 65 0.0001

GLN 65 LYS 66 -0.0004

LYS 66 LYS 67 0.0002

LYS 67 GLU 68 -0.0002

GLU 68 LYS 69 0.0004

LYS 69 GLY 70 -0.0002

GLY 70 LYS 71 -0.0004

LYS 71 LYS 72 0.0001

LYS 72 LEU 73 -0.0004

LEU 73 SER 74 -0.0002

SER 74 ARG 75 0.0000

ARG 75 MET 76 0.0002

MET 76 LYS 77 -0.0001

LYS 77 LEU 78 -0.0002

LEU 78 LEU 79 -0.0001

LEU 79 LEU 80 -0.0001

LEU 80 LYS 81 0.0003

LYS 81 HIS 82 0.0002

HIS 82 LEU 83 -0.0001

LEU 83 THR 84 0.0001

THR 84 LEU 85 -0.0001

LEU 85 ALA 86 -0.0001

ALA 86 ASN 87 0.0000

ASN 87 LEU 88 -0.0000

LEU 88 LEU 89 -0.0010

LEU 89 GLU 90 0.0001

GLU 90 THR 91 0.0001

THR 91 LEU 92 0.0001

LEU 92 ILE 93 -0.0007

ILE 93 VAL 94 0.0000

VAL 94 MET 95 -0.0002

MET 95 PRO 96 -0.0001

PRO 96 LEU 97 -0.0005

LEU 97 ASP 98 -0.0001

ASP 98 GLY 99 0.0002

GLY 99 MET 100 0.0004

MET 100 TRP 101 -0.0005

TRP 101 ASN 102 0.0001

ASN 102 ILE 103 0.0001

ILE 103 THR 104 -0.0004

THR 104 VAL 105 -0.0001

VAL 105 GLN 106 -0.0003

GLN 106 TRP 107 0.0003

TRP 107 TYR 108 0.0002

TYR 108 ALA 109 -0.0007

ALA 109 GLY 110 0.0001

GLY 110 GLU 111 0.0011

GLU 111 LEU 112 -0.0001

LEU 112 LEU 113 -0.0005

LEU 113 CYS 114 0.0005

CYS 114 LYS 115 0.0000

LYS 115 VAL 116 0.0002

VAL 116 LEU 117 -0.0000

LEU 117 SER 118 -0.0001

SER 118 TYR 119 0.0003

TYR 119 LEU 120 -0.0001

LEU 120 LYS 121 0.0004

LYS 121 LEU 122 -0.0000

LEU 122 PHE 123 -0.0002

PHE 123 SER 124 0.0002

SER 124 MET 125 0.0001

MET 125 TYR 126 0.0001

TYR 126 ALA 127 -0.0001

ALA 127 PRO 128 -0.0000

PRO 128 ALA 129 0.0003

ALA 129 PHE 130 0.0002

PHE 130 MET 131 -0.0004

MET 131 MET 132 -0.0004

MET 132 VAL 133 -0.0000

VAL 133 VAL 134 0.0004

VAL 134 ILE 135 -0.0001

ILE 135 SER 136 -0.0001

SER 136 LEU 137 0.0000

LEU 137 ASP 138 -0.0002

ASP 138 ARG 139 -0.0005

ARG 139 SER 140 0.0001

SER 140 LEU 141 0.0001

LEU 141 ALA 142 0.0003

ALA 142 ILE 143 -0.0004

ILE 143 THR 144 -0.0001

THR 144 ARG 145 0.0001

ARG 145 PRO 146 -0.0002

PRO 146 LEU 147 -0.0002

LEU 147 ALA 148 -0.0002

ALA 148 LEU 149 -0.0002

LEU 149 LYS 150 0.0000

LYS 150 SER 151 -0.0000

SER 151 ASN 152 -0.0001

ASN 152 SER 153 -0.0001

SER 153 LYS 154 0.0001

LYS 154 VAL 155 0.0003

VAL 155 GLY 156 0.0001

GLY 156 GLN 157 0.0001

GLN 157 SER 158 0.0000

SER 158 MET 159 -0.0003

MET 159 VAL 160 0.0001

VAL 160 GLY 161 0.0001

GLY 161 LEU 162 -0.0002

LEU 162 ALA 163 0.0001

ALA 163 TRP 164 -0.0002

TRP 164 ILE 165 -0.0002

ILE 165 LEU 166 -0.0002

LEU 166 SER 167 0.0003

SER 167 SER 168 -0.0002

SER 168 VAL 169 0.0002

VAL 169 PHE 170 0.0001

PHE 170 ALA 171 -0.0002

ALA 171 GLY 172 0.0001

GLY 172 PRO 173 -0.0001

PRO 173 GLN 174 0.0003

GLN 174 LEU 175 -0.0002

LEU 175 TYR 176 0.0001

TYR 176 ILE 177 -0.0003

ILE 177 PHE 178 0.0001

PHE 178 ARG 179 -0.0024

ARG 179 MET 180 -0.0001

MET 180 ILE 181 -0.0005

ILE 181 HIS 182 -0.0002

HIS 182 LEU 183 -0.0020

LEU 183 ALA 184 0.0004

ALA 184 ASP 185 0.0013

ASP 185 SER 186 -0.0002

SER 186 SER 187 -0.0007

SER 187 GLY 188 0.0000

GLY 188 GLN 189 0.0000

GLN 189 THR 190 0.0001

THR 190 LYS 191 0.0005

LYS 191 VAL 192 -0.0000

VAL 192 PHE 193 0.0009

PHE 193 SER 194 0.0002

SER 194 GLN 195 -0.0001

GLN 195 CYS 196 0.0003

CYS 196 VAL 197 0.0009

VAL 197 THR 198 -0.0003

THR 198 HIS 199 0.0066

HIS 199 CYS 200 0.0002

CYS 200 SER 201 -0.0025

SER 201 PHE 202 0.0003

PHE 202 SER 203 -0.0005

SER 203 GLN 204 -0.0003

GLN 204 TRP 205 -0.0004

TRP 205 TRP 206 -0.0002

TRP 206 HIS 207 -0.0003

HIS 207 GLN 208 -0.0002

GLN 208 ALA 209 0.0003

ALA 209 PHE 210 0.0001

PHE 210 TYR 211 -0.0014

TYR 211 ASN 212 -0.0002

ASN 212 PHE 213 0.0008

PHE 213 PHE 214 0.0001

PHE 214 THR 215 0.0000

THR 215 PHE 216 -0.0001

PHE 216 SER 217 0.0002

SER 217 CYS 218 0.0002

CYS 218 LEU 219 0.0000

LEU 219 PHE 220 0.0000

PHE 220 ILE 221 -0.0002

ILE 221 ILE 222 -0.0000

ILE 222 PRO 223 0.0000

PRO 223 LEU 224 -0.0001

LEU 224 PHE 225 -0.0005

PHE 225 ILE 226 -0.0002

ILE 226 MET 227 -0.0004

MET 227 LEU 228 -0.0003

LEU 228 ILE 229 -0.0009

ILE 229 CYS 230 0.0001

CYS 230 ASN 231 0.0005

ASN 231 ALA 232 0.0000

ALA 232 LYS 233 -0.0003

LYS 233 ILE 234 0.0000

ILE 234 ILE 235 0.0000

ILE 235 PHE 236 -0.0002

PHE 236 THR 237 -0.0004

THR 237 LEU 238 -0.0002

LEU 238 THR 239 -0.0006

THR 239 ARG 240 -0.0002

ARG 240 VAL 241 -0.0003

VAL 241 LEU 242 -0.0001

LEU 242 HIS 243 -0.0005

HIS 243 GLN 244 0.0000

GLN 244 ASP 245 -0.0004

ASP 245 PRO 246 0.0002

PRO 246 HIS 247 -0.0001

HIS 247 GLU 248 0.0002

GLU 248 LEU 249 0.0002

LEU 249 GLN 250 -0.0003

GLN 250 LEU 251 -0.0002

LEU 251 ASN 252 0.0001

ASN 252 GLN 253 0.0003

GLN 253 SER 254 0.0001

SER 254 LYS 255 0.0001

LYS 255 ASN 256 0.0003

ASN 256 ASN 257 -0.0001

ASN 257 ILE 258 -0.0002

ILE 258 PRO 259 0.0003

PRO 259 ARG 260 -0.0001

ARG 260 ALA 261 -0.0002

ALA 261 ARG 262 0.0000

ARG 262 LEU 263 -0.0001

LEU 263 LYS 264 -0.0000

LYS 264 THR 265 0.0003

THR 265 LEU 266 0.0002

LEU 266 LYS 267 -0.0003

LYS 267 MET 268 0.0003

MET 268 THR 269 0.0002

THR 269 VAL 270 0.0001

VAL 270 ALA 271 -0.0005

ALA 271 PHE 272 0.0004

PHE 272 ALA 273 0.0001

ALA 273 THR 274 -0.0001

THR 274 SER 275 -0.0006

SER 275 PHE 276 0.0000

PHE 276 THR 277 -0.0004

THR 277 VAL 278 0.0002

VAL 278 CYS 279 -0.0007

CYS 279 TRP 280 0.0001

TRP 280 THR 281 0.0005

THR 281 PRO 282 0.0000

PRO 282 TYR 283 -0.0004

TYR 283 TYR 284 -0.0001

TYR 284 VAL 285 0.0009

VAL 285 LEU 286 0.0001

LEU 286 GLY 287 -0.0003

GLY 287 ILE 288 -0.0001

ILE 288 TRP 289 0.0011

TRP 289 TYR 290 -0.0003

TYR 290 TRP 291 -0.0002

TRP 291 PHE 292 -0.0000

PHE 292 ASP 293 -0.0025

ASP 293 PRO 294 -0.0001

PRO 294 GLU 295 -0.0060

GLU 295 MET 296 0.0001

MET 296 LEU 297 0.0001

LEU 297 ASN 298 0.0000

ASN 298 ARG 299 -0.0002

ARG 299 LEU 300 -0.0002

LEU 300 SER 301 -0.0031

SER 301 ASP 302 -0.0001

ASP 302 PRO 303 0.0014

PRO 303 VAL 304 -0.0002

VAL 304 ASN 305 -0.0012

ASN 305 HIS 306 -0.0001

HIS 306 PHE 307 -0.0011

PHE 307 PHE 308 -0.0003

PHE 308 PHE 309 0.0001

PHE 309 LEU 310 0.0001

LEU 310 PHE 311 -0.0005

PHE 311 ALA 312 -0.0003

ALA 312 PHE 313 0.0004

PHE 313 LEU 314 -0.0001

LEU 314 ASN 315 0.0000

ASN 315 PRO 316 0.0001

PRO 316 CYS 317 0.0001

CYS 317 PHE 318 0.0000

PHE 318 ASP 319 0.0001

ASP 319 PRO 320 0.0004

PRO 320 LEU 321 0.0001

LEU 321 ILE 322 -0.0000

ILE 322 TYR 323 -0.0002

TYR 323 GLY 324 0.0001

GLY 324 TYR 325 -0.0005

TYR 325 PHE 326 0.0002

PHE 326 SER 327 0.0002

SER 327 LEU 328 -0.0000

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.

*** 01-JUN-22 ***

CA strain for 240221025813253280

--- normal mode 8 ---

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

* 01-JUN-22 *