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

* hCasq1_no_cal *

CA strain for 250214081644157677

--- 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
GLU 2 GLY 3 0.0001

GLY 3 LEU 4 -0.0071

LEU 4 ASP 5 0.0001

ASP 5 PHE 6 0.0083

PHE 6 PRO 7 0.0001

PRO 7 GLU 8 0.0355

GLU 8 TYR 9 0.0001

TYR 9 ASP 10 -0.0268

ASP 10 GLY 11 0.0000

GLY 11 VAL 12 -0.0053

VAL 12 ASP 13 0.0004

ASP 13 ARG 14 0.0014

ARG 14 VAL 15 0.0001

VAL 15 ILE 16 -0.0061

ILE 16 ASN 17 -0.0001

ASN 17 VAL 18 -0.0015

VAL 18 ASN 19 0.0000

ASN 19 ALA 20 -0.0007

ALA 20 LYS 21 0.0002

LYS 21 ASN 22 -0.0005

ASN 22 TYR 23 -0.0001

TYR 23 LYS 24 0.0003

LYS 24 ASN 25 -0.0003

ASN 25 VAL 26 -0.0004

VAL 26 PHE 27 0.0002

PHE 27 LYS 28 -0.0010

LYS 28 LYS 29 -0.0005

LYS 29 TYR 30 0.0016

TYR 30 GLU 31 0.0000

GLU 31 VAL 32 0.0015

VAL 32 LEU 33 -0.0003

LEU 33 ALA 34 0.0006

ALA 34 LEU 35 -0.0001

LEU 35 LEU 36 0.0014

LEU 36 TYR 37 -0.0003

TYR 37 HSE 38 0.0004

HSE 38 GLU 39 0.0001

GLU 39 PRO 40 0.0001

PRO 40 PRO 41 -0.0000

PRO 41 GLU 42 0.0000

GLU 42 ASP 43 0.0001

ASP 43 ASP 44 -0.0002

ASP 44 LYS 45 0.0003

LYS 45 ALA 46 -0.0003

ALA 46 SER 47 0.0002

SER 47 GLN 48 0.0004

GLN 48 ARG 49 -0.0000

ARG 49 GLN 50 -0.0002

GLN 50 PHE 51 -0.0002

PHE 51 GLU 52 0.0020

GLU 52 MET 53 0.0004

MET 53 GLU 54 0.0006

GLU 54 GLU 55 0.0002

GLU 55 LEU 56 0.0069

LEU 56 ILE 57 0.0001

ILE 57 LEU 58 0.0020

LEU 58 GLU 59 0.0004

GLU 59 LEU 60 0.0028

LEU 60 ALA 61 0.0001

ALA 61 ALA 62 0.0014

ALA 62 GLN 63 -0.0001

GLN 63 VAL 64 0.0093

VAL 64 LEU 65 -0.0002

LEU 65 GLU 66 0.0035

GLU 66 ASP 67 -0.0005

ASP 67 LYS 68 -0.0030

LYS 68 GLY 69 0.0001

GLY 69 VAL 70 0.0023

VAL 70 GLY 71 -0.0003

GLY 71 PHE 72 0.0027

PHE 72 GLY 73 -0.0001

GLY 73 LEU 74 -0.0004

LEU 74 VAL 75 0.0001

VAL 75 ASP 76 -0.0001

ASP 76 SER 77 -0.0002

SER 77 GLU 78 -0.0009

GLU 78 LYS 79 -0.0002

LYS 79 ASP 80 0.0005

ASP 80 ALA 81 0.0001

ALA 81 ALA 82 0.0010

ALA 82 VAL 83 -0.0001

VAL 83 ALA 84 -0.0006

ALA 84 LYS 85 -0.0000

LYS 85 LYS 86 0.0003

LYS 86 LEU 87 0.0002

LEU 87 GLY 88 -0.0019

GLY 88 LEU 89 0.0001

LEU 89 THR 90 -0.0003

THR 90 GLU 91 0.0002

GLU 91 VAL 92 0.0002

VAL 92 ASP 93 -0.0004

ASP 93 SER 94 -0.0014

SER 94 MET 95 0.0000

MET 95 TYR 96 0.0020

TYR 96 VAL 97 0.0001

VAL 97 PHE 98 -0.0006

PHE 98 LYS 99 0.0000

LYS 99 GLY 100 0.0024

GLY 100 ASP 101 -0.0001

ASP 101 GLU 102 -0.0025

GLU 102 VAL 103 0.0001

VAL 103 ILE 104 -0.0015

ILE 104 GLU 105 -0.0002

GLU 105 TYR 106 0.0007

TYR 106 ASP 107 -0.0004

ASP 107 GLY 108 0.0008

GLY 108 GLU 109 -0.0001

GLU 109 PHE 110 0.0011

PHE 110 SER 111 0.0001

SER 111 ALA 112 0.0097

ALA 112 ASP 113 0.0001

ASP 113 THR 114 0.0071

THR 114 ILE 115 0.0004

ILE 115 VAL 116 0.0018

VAL 116 GLU 117 0.0002

GLU 117 PHE 118 -0.0002

PHE 118 LEU 119 0.0003

LEU 119 LEU 120 -0.0015

LEU 120 ASP 121 -0.0004

ASP 121 VAL 122 0.0005

VAL 122 LEU 123 0.0001

LEU 123 GLU 124 0.0026

GLU 124 ASP 125 -0.0006

ASP 125 PRO 126 0.0002

PRO 126 VAL 127 0.0001

VAL 127 GLU 128 0.0015

GLU 128 LEU 129 -0.0002

LEU 129 ILE 130 0.0011

ILE 130 GLU 131 0.0004

GLU 131 GLY 132 -0.0003

GLY 132 GLU 133 -0.0000

GLU 133 ARG 134 -0.0002

ARG 134 GLU 135 0.0004

GLU 135 LEU 136 0.0003

LEU 136 GLN 137 0.0003

GLN 137 ALA 138 0.0000

ALA 138 PHE 139 0.0004

PHE 139 GLU 140 0.0010

GLU 140 ASN 141 0.0003

ASN 141 ILE 142 -0.0014

ILE 142 GLU 143 0.0002

GLU 143 ASP 144 -0.0014

ASP 144 GLU 145 0.0003

GLU 145 ILE 146 0.0004

ILE 146 LYS 147 -0.0002

LYS 147 LEU 148 -0.0004

LEU 148 ILE 149 -0.0001

ILE 149 GLY 150 -0.0001

GLY 150 TYR 151 -0.0002

TYR 151 PHE 152 0.0002

PHE 152 LYS 153 -0.0000

LYS 153 SER 154 0.0000

SER 154 LYS 155 -0.0000

LYS 155 ASP 156 0.0000

ASP 156 SER 157 0.0002

SER 157 GLU 158 0.0002

GLU 158 HSE 159 -0.0001

HSE 159 TYR 160 -0.0008

TYR 160 LYS 161 0.0003

LYS 161 ALA 162 0.0005

ALA 162 PHE 163 -0.0000

PHE 163 GLU 164 -0.0011

GLU 164 ASP 165 0.0003

ASP 165 ALA 166 0.0002

ALA 166 ALA 167 -0.0001

ALA 167 GLU 168 0.0004

GLU 168 GLU 169 -0.0002

GLU 169 PHE 170 -0.0008

PHE 170 HSE 171 0.0002

HSE 171 PRO 172 0.0035

PRO 172 TYR 173 -0.0001

TYR 173 ILE 174 -0.0015

ILE 174 PRO 175 -0.0001

PRO 175 PHE 176 -0.0005

PHE 176 PHE 177 0.0002

PHE 177 ALA 178 -0.0008

ALA 178 THR 179 0.0001

THR 179 PHE 180 -0.0002

PHE 180 ASP 181 -0.0003

ASP 181 SER 182 0.0005

SER 182 LYS 183 -0.0002

LYS 183 VAL 184 -0.0000

VAL 184 ALA 185 -0.0002

ALA 185 LYS 186 -0.0002

LYS 186 LYS 187 0.0001

LYS 187 LEU 188 0.0006

LEU 188 THR 189 0.0000

THR 189 LEU 190 -0.0002

LEU 190 LYS 191 -0.0001

LYS 191 LEU 192 0.0000

LEU 192 ASN 193 -0.0001

ASN 193 GLU 194 -0.0004

GLU 194 ILE 195 -0.0004

ILE 195 ASP 196 -0.0000

ASP 196 PHE 197 -0.0004

PHE 197 TYR 198 -0.0009

TYR 198 GLU 199 0.0002

GLU 199 ALA 200 -0.0008

ALA 200 PHE 201 -0.0003

PHE 201 MET 202 -0.0022

MET 202 GLU 203 0.0003

GLU 203 GLU 204 -0.0024

GLU 204 PRO 205 0.0003

PRO 205 VAL 206 -0.0013

VAL 206 THR 207 -0.0001

THR 207 ILE 208 -0.0005

ILE 208 PRO 209 -0.0001

PRO 209 ASP 210 0.0002

ASP 210 LYS 211 -0.0001

LYS 211 PRO 212 -0.0002

PRO 212 ASN 213 0.0005

ASN 213 SER 214 -0.0008

SER 214 GLU 215 0.0002

GLU 215 GLU 216 -0.0002

GLU 216 GLU 217 0.0002

GLU 217 ILE 218 0.0000

ILE 218 VAL 219 0.0002

VAL 219 ASN 220 -0.0016

ASN 220 PHE 221 0.0001

PHE 221 VAL 222 0.0012

VAL 222 GLU 223 -0.0004

GLU 223 GLU 224 -0.0006

GLU 224 HSE 225 0.0000

HSE 225 ARG 226 0.0041

ARG 226 ARG 227 0.0000

ARG 227 SER 228 -0.0004

SER 228 THR 229 -0.0002

THR 229 LEU 230 0.0003

LEU 230 ARG 231 0.0001

ARG 231 LYS 232 0.0024

LYS 232 LEU 233 0.0002

LEU 233 LYS 234 0.0074

LYS 234 PRO 235 0.0002

PRO 235 GLU 236 0.0026

GLU 236 SER 237 -0.0002

SER 237 MET 238 0.0001

MET 238 TYR 239 -0.0003

TYR 239 GLU 240 0.0058

GLU 240 THR 241 0.0001

THR 241 TRP 242 -0.0014

TRP 242 GLU 243 0.0001

GLU 243 ASP 244 0.0014

ASP 244 ASP 245 -0.0004

ASP 245 MET 246 0.0007

MET 246 ASP 247 0.0003

ASP 247 GLY 248 0.0003

GLY 248 ILE 249 -0.0001

ILE 249 HSE 250 0.0006

HSE 250 ILE 251 0.0000

ILE 251 VAL 252 0.0003

VAL 252 ALA 253 -0.0000

ALA 253 PHE 254 -0.0002

PHE 254 ALA 255 0.0001

ALA 255 GLU 256 -0.0004

GLU 256 GLU 257 -0.0003

GLU 257 ALA 258 0.0002

ALA 258 ASP 259 0.0003

ASP 259 PRO 260 0.0001

PRO 260 ASP 261 0.0001

ASP 261 GLY 262 0.0006

GLY 262 PHE 263 -0.0002

PHE 263 GLU 264 0.0002

GLU 264 PHE 265 -0.0005

PHE 265 LEU 266 0.0005

LEU 266 GLU 267 0.0001

GLU 267 THR 268 0.0009

THR 268 LEU 269 -0.0005

LEU 269 LYS 270 0.0002

LYS 270 ALA 271 -0.0004

ALA 271 VAL 272 0.0004

VAL 272 ALA 273 0.0001

ALA 273 GLN 274 0.0007

GLN 274 ASP 275 -0.0002

ASP 275 ASN 276 -0.0001

ASN 276 THR 277 0.0004

THR 277 GLU 278 0.0006

GLU 278 ASN 279 0.0003

ASN 279 PRO 280 -0.0011

PRO 280 ASP 281 -0.0005

ASP 281 LEU 282 -0.0003

LEU 282 SER 283 0.0002

SER 283 ILE 284 0.0002

ILE 284 ILE 285 -0.0004

ILE 285 TRP 286 -0.0003

TRP 286 ILE 287 -0.0001

ILE 287 ASP 288 -0.0006

ASP 288 PRO 289 -0.0001

PRO 289 ASP 290 -0.0002

ASP 290 ASP 291 0.0002

ASP 291 PHE 292 -0.0005

PHE 292 PRO 293 -0.0003

PRO 293 LEU 294 -0.0000

LEU 294 LEU 295 0.0002

LEU 295 VAL 296 0.0005

VAL 296 PRO 297 0.0001

PRO 297 TYR 298 -0.0002

TYR 298 TRP 299 0.0002

TRP 299 GLU 300 -0.0004

GLU 300 LYS 301 -0.0004

LYS 301 THR 302 -0.0006

THR 302 PHE 303 -0.0002

PHE 303 ASP 304 -0.0006

ASP 304 ILE 305 -0.0002

ILE 305 ASP 306 -0.0001

ASP 306 LEU 307 -0.0000

LEU 307 SER 308 -0.0002

SER 308 ALA 309 0.0002

ALA 309 PRO 310 -0.0002

PRO 310 GLN 311 -0.0000

GLN 311 ILE 312 -0.0003

ILE 312 GLY 313 -0.0000

GLY 313 VAL 314 -0.0002

VAL 314 VAL 315 -0.0002

VAL 315 ASN 316 -0.0001

ASN 316 VAL 317 0.0000

VAL 317 THR 318 0.0001

THR 318 ASP 319 -0.0000

ASP 319 ALA 320 0.0003

ALA 320 ASP 321 0.0002

ASP 321 SER 322 -0.0002

SER 322 VAL 323 0.0004

VAL 323 TRP 324 -0.0006

TRP 324 MET 325 0.0001

MET 325 GLU 326 -0.0009

GLU 326 MET 327 0.0001

MET 327 ASP 328 -0.0008

ASP 328 ASP 329 0.0003

ASP 329 GLU 330 0.0006

GLU 330 GLU 331 0.0000

GLU 331 ASP 332 0.0003

ASP 332 LEU 333 -0.0001

LEU 333 PRO 334 -0.0003

PRO 334 SER 335 -0.0001

SER 335 ALA 336 -0.0005

ALA 336 GLU 337 -0.0002

GLU 337 GLU 338 0.0002

GLU 338 LEU 339 0.0001

LEU 339 GLU 340 -0.0000

GLU 340 ASP 341 0.0002

ASP 341 TRP 342 0.0004

TRP 342 LEU 343 0.0004

LEU 343 GLU 344 0.0005

GLU 344 ASP 345 0.0003

ASP 345 VAL 346 0.0003

VAL 346 LEU 347 0.0003

LEU 347 GLU 348 -0.0007

GLU 348 GLY 349 -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.

*** hCasq1_no_cal ***

CA strain for 250214081644157677

--- normal mode 7 ---

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

* hCasq1_no_cal *