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

* 01-JUN-22 *

CA strain for 240221025813253280

--- normal mode 7 ---

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 0.0002

ALA 2 ASN 3 -0.0028

ASN 3 SER 4 0.0000

SER 4 ALA 5 -0.0061

ALA 5 SER 6 -0.0002

SER 6 PRO 7 -0.1559

PRO 7 GLU 8 0.0000

GLU 8 GLN 9 -0.0126

GLN 9 ASN 10 0.0002

ASN 10 GLN 11 0.0084

GLN 11 ASN 12 -0.0000

ASN 12 HIS 13 0.0046

HIS 13 CYS 14 -0.0003

CYS 14 SER 15 -0.0028

SER 15 ALA 16 0.0004

ALA 16 ILE 17 -0.0009

ILE 17 ASN 18 0.0001

ASN 18 ASN 19 0.0005

ASN 19 SER 20 0.0000

SER 20 ILE 21 -0.0007

ILE 21 PRO 22 0.0000

PRO 22 LEU 23 -0.0023

LEU 23 MET 24 0.0002

MET 24 GLN 25 -0.0032

GLN 25 GLY 26 0.0001

GLY 26 ASN 27 -0.0025

ASN 27 LEU 28 -0.0001

LEU 28 PRO 29 0.0020

PRO 29 THR 30 -0.0001

THR 30 LEU 31 -0.0022

LEU 31 THR 32 0.0001

THR 32 LEU 33 0.0002

LEU 33 SER 34 0.0000

SER 34 GLY 35 0.0001

GLY 35 LYS 36 -0.0002

LYS 36 ILE 37 -0.0002

ILE 37 ARG 38 -0.0000

ARG 38 VAL 39 -0.0002

VAL 39 THR 40 -0.0001

THR 40 VAL 41 -0.0000

VAL 41 THR 42 0.0006

THR 42 PHE 43 -0.0000

PHE 43 PHE 44 -0.0002

PHE 44 LEU 45 0.0002

LEU 45 PHE 46 -0.0000

PHE 46 LEU 47 -0.0001

LEU 47 LEU 48 -0.0001

LEU 48 SER 49 0.0006

SER 49 ALA 50 -0.0001

ALA 50 THR 51 0.0005

THR 51 PHE 52 0.0001

PHE 52 ASN 53 0.0002

ASN 53 ALA 54 0.0002

ALA 54 SER 55 0.0003

SER 55 PHE 56 0.0001

PHE 56 LEU 57 -0.0003

LEU 57 LEU 58 -0.0002

LEU 58 LYS 59 0.0004

LYS 59 LEU 60 0.0002

LEU 60 GLN 61 0.0003

GLN 61 LYS 62 -0.0003

LYS 62 TRP 63 0.0001

TRP 63 THR 64 -0.0001

THR 64 GLN 65 0.0004

GLN 65 LYS 66 0.0004

LYS 66 LYS 67 -0.0002

LYS 67 GLU 68 0.0002

GLU 68 LYS 69 0.0002

LYS 69 GLY 70 -0.0001

GLY 70 LYS 71 -0.0001

LYS 71 LYS 72 0.0000

LYS 72 LEU 73 -0.0003

LEU 73 SER 74 0.0001

SER 74 ARG 75 -0.0002

ARG 75 MET 76 0.0001

MET 76 LYS 77 -0.0004

LYS 77 LEU 78 -0.0000

LEU 78 LEU 79 0.0003

LEU 79 LEU 80 -0.0002

LEU 80 LYS 81 0.0000

LYS 81 HIS 82 0.0004

HIS 82 LEU 83 0.0002

LEU 83 THR 84 -0.0001

THR 84 LEU 85 0.0001

LEU 85 ALA 86 -0.0001

ALA 86 ASN 87 -0.0002

ASN 87 LEU 88 0.0001

LEU 88 LEU 89 -0.0000

LEU 89 GLU 90 -0.0002

GLU 90 THR 91 0.0003

THR 91 LEU 92 -0.0003

LEU 92 ILE 93 -0.0000

ILE 93 VAL 94 -0.0000

VAL 94 MET 95 0.0002

MET 95 PRO 96 0.0002

PRO 96 LEU 97 0.0005

LEU 97 ASP 98 -0.0002

ASP 98 GLY 99 0.0001

GLY 99 MET 100 -0.0001

MET 100 TRP 101 -0.0006

TRP 101 ASN 102 -0.0002

ASN 102 ILE 103 0.0008

ILE 103 THR 104 0.0001

THR 104 VAL 105 -0.0010

VAL 105 GLN 106 0.0001

GLN 106 TRP 107 -0.0006

TRP 107 TYR 108 0.0001

TYR 108 ALA 109 -0.0006

ALA 109 GLY 110 0.0001

GLY 110 GLU 111 0.0011

GLU 111 LEU 112 -0.0001

LEU 112 LEU 113 -0.0001

LEU 113 CYS 114 -0.0000

CYS 114 LYS 115 -0.0001

LYS 115 VAL 116 0.0003

VAL 116 LEU 117 0.0004

LEU 117 SER 118 0.0002

SER 118 TYR 119 0.0002

TYR 119 LEU 120 -0.0001

LEU 120 LYS 121 0.0003

LYS 121 LEU 122 -0.0002

LEU 122 PHE 123 0.0001

PHE 123 SER 124 -0.0003

SER 124 MET 125 -0.0005

MET 125 TYR 126 0.0000

TYR 126 ALA 127 0.0006

ALA 127 PRO 128 -0.0002

PRO 128 ALA 129 -0.0000

ALA 129 PHE 130 0.0001

PHE 130 MET 131 0.0007

MET 131 MET 132 -0.0003

MET 132 VAL 133 0.0002

VAL 133 VAL 134 -0.0002

VAL 134 ILE 135 -0.0002

ILE 135 SER 136 0.0003

SER 136 LEU 137 -0.0001

LEU 137 ASP 138 0.0003

ASP 138 ARG 139 0.0001

ARG 139 SER 140 -0.0002

SER 140 LEU 141 0.0001

LEU 141 ALA 142 -0.0001

ALA 142 ILE 143 -0.0003

ILE 143 THR 144 -0.0003

THR 144 ARG 145 -0.0001

ARG 145 PRO 146 0.0003

PRO 146 LEU 147 -0.0003

LEU 147 ALA 148 -0.0001

ALA 148 LEU 149 -0.0001

LEU 149 LYS 150 0.0001

LYS 150 SER 151 0.0002

SER 151 ASN 152 0.0001

ASN 152 SER 153 -0.0002

SER 153 LYS 154 0.0001

LYS 154 VAL 155 0.0001

VAL 155 GLY 156 0.0001

GLY 156 GLN 157 -0.0003

GLN 157 SER 158 0.0004

SER 158 MET 159 -0.0000

MET 159 VAL 160 -0.0003

VAL 160 GLY 161 0.0004

GLY 161 LEU 162 0.0000

LEU 162 ALA 163 0.0001

ALA 163 TRP 164 0.0001

TRP 164 ILE 165 0.0006

ILE 165 LEU 166 -0.0003

LEU 166 SER 167 -0.0002

SER 167 SER 168 0.0002

SER 168 VAL 169 -0.0004

VAL 169 PHE 170 -0.0005

PHE 170 ALA 171 -0.0001

ALA 171 GLY 172 0.0002

GLY 172 PRO 173 0.0007

PRO 173 GLN 174 -0.0001

GLN 174 LEU 175 -0.0004

LEU 175 TYR 176 0.0002

TYR 176 ILE 177 0.0005

ILE 177 PHE 178 -0.0002

PHE 178 ARG 179 -0.0003

ARG 179 MET 180 0.0002

MET 180 ILE 181 0.0006

ILE 181 HIS 182 0.0001

HIS 182 LEU 183 -0.0010

LEU 183 ALA 184 -0.0000

ALA 184 ASP 185 0.0009

ASP 185 SER 186 -0.0002

SER 186 SER 187 -0.0014

SER 187 GLY 188 -0.0004

GLY 188 GLN 189 -0.0006

GLN 189 THR 190 0.0003

THR 190 LYS 191 0.0013

LYS 191 VAL 192 0.0000

VAL 192 PHE 193 0.0008

PHE 193 SER 194 0.0003

SER 194 GLN 195 -0.0002

GLN 195 CYS 196 -0.0001

CYS 196 VAL 197 -0.0005

VAL 197 THR 198 0.0005

THR 198 HIS 199 0.0004

HIS 199 CYS 200 0.0000

CYS 200 SER 201 0.0009

SER 201 PHE 202 0.0001

PHE 202 SER 203 0.0003

SER 203 GLN 204 -0.0002

GLN 204 TRP 205 -0.0004

TRP 205 TRP 206 -0.0005

TRP 206 HIS 207 -0.0005

HIS 207 GLN 208 0.0002

GLN 208 ALA 209 0.0010

ALA 209 PHE 210 -0.0000

PHE 210 TYR 211 -0.0004

TYR 211 ASN 212 -0.0001

ASN 212 PHE 213 0.0001

PHE 213 PHE 214 0.0002

PHE 214 THR 215 -0.0000

THR 215 PHE 216 0.0001

PHE 216 SER 217 -0.0001

SER 217 CYS 218 -0.0003

CYS 218 LEU 219 -0.0001

LEU 219 PHE 220 0.0002

PHE 220 ILE 221 0.0000

ILE 221 ILE 222 0.0000

ILE 222 PRO 223 -0.0002

PRO 223 LEU 224 -0.0000

LEU 224 PHE 225 0.0001

PHE 225 ILE 226 0.0001

ILE 226 MET 227 -0.0003

MET 227 LEU 228 -0.0004

LEU 228 ILE 229 -0.0003

ILE 229 CYS 230 -0.0004

CYS 230 ASN 231 0.0001

ASN 231 ALA 232 0.0003

ALA 232 LYS 233 -0.0001

LYS 233 ILE 234 0.0002

ILE 234 ILE 235 -0.0004

ILE 235 PHE 236 0.0000

PHE 236 THR 237 -0.0003

THR 237 LEU 238 0.0001

LEU 238 THR 239 0.0000

THR 239 ARG 240 -0.0000

ARG 240 VAL 241 0.0003

VAL 241 LEU 242 -0.0001

LEU 242 HIS 243 0.0002

HIS 243 GLN 244 0.0002

GLN 244 ASP 245 -0.0001

ASP 245 PRO 246 0.0002

PRO 246 HIS 247 -0.0003

HIS 247 GLU 248 -0.0002

GLU 248 LEU 249 -0.0002

LEU 249 GLN 250 0.0005

GLN 250 LEU 251 -0.0002

LEU 251 ASN 252 0.0001

ASN 252 GLN 253 0.0000

GLN 253 SER 254 0.0000

SER 254 LYS 255 -0.0001

LYS 255 ASN 256 0.0001

ASN 256 ASN 257 0.0001

ASN 257 ILE 258 0.0001

ILE 258 PRO 259 -0.0002

PRO 259 ARG 260 0.0005

ARG 260 ALA 261 0.0002

ALA 261 ARG 262 -0.0002

ARG 262 LEU 263 -0.0001

LEU 263 LYS 264 -0.0002

LYS 264 THR 265 0.0001

THR 265 LEU 266 0.0000

LEU 266 LYS 267 0.0003

LYS 267 MET 268 -0.0003

MET 268 THR 269 -0.0004

THR 269 VAL 270 -0.0003

VAL 270 ALA 271 -0.0003

ALA 271 PHE 272 0.0001

PHE 272 ALA 273 0.0003

ALA 273 THR 274 0.0002

THR 274 SER 275 0.0004

SER 275 PHE 276 0.0002

PHE 276 THR 277 -0.0001

THR 277 VAL 278 0.0004

VAL 278 CYS 279 0.0003

CYS 279 TRP 280 0.0003

TRP 280 THR 281 -0.0000

THR 281 PRO 282 -0.0005

PRO 282 TYR 283 -0.0001

TYR 283 TYR 284 -0.0004

TYR 284 VAL 285 0.0000

VAL 285 LEU 286 0.0001

LEU 286 GLY 287 -0.0010

GLY 287 ILE 288 -0.0002

ILE 288 TRP 289 0.0004

TRP 289 TYR 290 0.0003

TYR 290 TRP 291 -0.0012

TRP 291 PHE 292 -0.0003

PHE 292 ASP 293 0.0005

ASP 293 PRO 294 -0.0001

PRO 294 GLU 295 -0.0001

GLU 295 MET 296 -0.0003

MET 296 LEU 297 0.0004

LEU 297 ASN 298 -0.0000

ASN 298 ARG 299 -0.0003

ARG 299 LEU 300 -0.0000

LEU 300 SER 301 0.0007

SER 301 ASP 302 -0.0000

ASP 302 PRO 303 0.0000

PRO 303 VAL 304 -0.0000

VAL 304 ASN 305 0.0003

ASN 305 HIS 306 -0.0002

HIS 306 PHE 307 0.0005

PHE 307 PHE 308 -0.0000

PHE 308 PHE 309 0.0003

PHE 309 LEU 310 0.0003

LEU 310 PHE 311 0.0005

PHE 311 ALA 312 -0.0000

ALA 312 PHE 313 0.0003

PHE 313 LEU 314 0.0000

LEU 314 ASN 315 0.0001

ASN 315 PRO 316 0.0002

PRO 316 CYS 317 0.0000

CYS 317 PHE 318 0.0000

PHE 318 ASP 319 -0.0001

ASP 319 PRO 320 -0.0000

PRO 320 LEU 321 -0.0001

LEU 321 ILE 322 -0.0003

ILE 322 TYR 323 -0.0002

TYR 323 GLY 324 -0.0002

GLY 324 TYR 325 0.0003

TYR 325 PHE 326 0.0005

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 7 ---

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

* 01-JUN-22 *