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

* hCasq1_no_cal *

CA strain for 250214081644157677

--- normal mode 10 ---

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 -0.0000

GLY 3 LEU 4 0.0151

LEU 4 ASP 5 -0.0001

ASP 5 PHE 6 -0.0248

PHE 6 PRO 7 -0.0001

PRO 7 GLU 8 -0.1215

GLU 8 TYR 9 -0.0004

TYR 9 ASP 10 0.0118

ASP 10 GLY 11 -0.0002

GLY 11 VAL 12 -0.0089

VAL 12 ASP 13 -0.0001

ASP 13 ARG 14 -0.0042

ARG 14 VAL 15 0.0000

VAL 15 ILE 16 0.0059

ILE 16 ASN 17 0.0002

ASN 17 VAL 18 -0.0034

VAL 18 ASN 19 -0.0001

ASN 19 ALA 20 0.0030

ALA 20 LYS 21 -0.0003

LYS 21 ASN 22 0.0068

ASN 22 TYR 23 -0.0001

TYR 23 LYS 24 -0.0003

LYS 24 ASN 25 -0.0003

ASN 25 VAL 26 -0.0012

VAL 26 PHE 27 -0.0003

PHE 27 LYS 28 -0.0058

LYS 28 LYS 29 0.0004

LYS 29 TYR 30 0.0137

TYR 30 GLU 31 0.0000

GLU 31 VAL 32 -0.0034

VAL 32 LEU 33 0.0000

LEU 33 ALA 34 0.0001

ALA 34 LEU 35 0.0004

LEU 35 LEU 36 0.0043

LEU 36 TYR 37 -0.0000

TYR 37 HSE 38 -0.0178

HSE 38 GLU 39 0.0000

GLU 39 PRO 40 -0.0214

PRO 40 PRO 41 -0.0002

PRO 41 GLU 42 0.0035

GLU 42 ASP 43 -0.0000

ASP 43 ASP 44 -0.0042

ASP 44 LYS 45 0.0002

LYS 45 ALA 46 -0.0118

ALA 46 SER 47 0.0002

SER 47 GLN 48 -0.0016

GLN 48 ARG 49 -0.0003

ARG 49 GLN 50 -0.0007

GLN 50 PHE 51 0.0001

PHE 51 GLU 52 -0.0005

GLU 52 MET 53 -0.0003

MET 53 GLU 54 0.0006

GLU 54 GLU 55 -0.0003

GLU 55 LEU 56 -0.0044

LEU 56 ILE 57 -0.0001

ILE 57 LEU 58 0.0056

LEU 58 GLU 59 0.0005

GLU 59 LEU 60 -0.0035

LEU 60 ALA 61 -0.0002

ALA 61 ALA 62 -0.0038

ALA 62 GLN 63 0.0002

GLN 63 VAL 64 0.0035

VAL 64 LEU 65 -0.0004

LEU 65 GLU 66 -0.0019

GLU 66 ASP 67 -0.0001

ASP 67 LYS 68 0.0175

LYS 68 GLY 69 -0.0002

GLY 69 VAL 70 -0.0061

VAL 70 GLY 71 -0.0000

GLY 71 PHE 72 0.0155

PHE 72 GLY 73 -0.0000

GLY 73 LEU 74 0.0181

LEU 74 VAL 75 -0.0000

VAL 75 ASP 76 0.0061

ASP 76 SER 77 -0.0000

SER 77 GLU 78 -0.0034

GLU 78 LYS 79 -0.0000

LYS 79 ASP 80 -0.0006

ASP 80 ALA 81 -0.0001

ALA 81 ALA 82 0.0003

ALA 82 VAL 83 0.0003

VAL 83 ALA 84 -0.0078

ALA 84 LYS 85 -0.0004

LYS 85 LYS 86 -0.0030

LYS 86 LEU 87 -0.0002

LEU 87 GLY 88 -0.0046

GLY 88 LEU 89 -0.0005

LEU 89 THR 90 -0.0025

THR 90 GLU 91 0.0003

GLU 91 VAL 92 -0.0248

VAL 92 ASP 93 -0.0001

ASP 93 SER 94 -0.0328

SER 94 MET 95 -0.0002

MET 95 TYR 96 0.0100

TYR 96 VAL 97 0.0002

VAL 97 PHE 98 0.0000

PHE 98 LYS 99 -0.0004

LYS 99 GLY 100 0.0270

GLY 100 ASP 101 0.0001

ASP 101 GLU 102 -0.0123

GLU 102 VAL 103 0.0000

VAL 103 ILE 104 0.0224

ILE 104 GLU 105 -0.0003

GLU 105 TYR 106 0.0482

TYR 106 ASP 107 0.0002

ASP 107 GLY 108 0.0462

GLY 108 GLU 109 -0.0000

GLU 109 PHE 110 -0.0270

PHE 110 SER 111 -0.0002

SER 111 ALA 112 -0.0451

ALA 112 ASP 113 0.0002

ASP 113 THR 114 0.0254

THR 114 ILE 115 0.0001

ILE 115 VAL 116 -0.0235

VAL 116 GLU 117 0.0000

GLU 117 PHE 118 0.0070

PHE 118 LEU 119 -0.0001

LEU 119 LEU 120 -0.0120

LEU 120 ASP 121 0.0003

ASP 121 VAL 122 -0.0132

VAL 122 LEU 123 0.0001

LEU 123 GLU 124 0.1496

GLU 124 ASP 125 0.0000

ASP 125 PRO 126 -0.0003

PRO 126 VAL 127 -0.0001

VAL 127 GLU 128 0.0035

GLU 128 LEU 129 -0.0000

LEU 129 ILE 130 0.0271

ILE 130 GLU 131 -0.0002

GLU 131 GLY 132 0.0011

GLY 132 GLU 133 0.0002

GLU 133 ARG 134 -0.0083

ARG 134 GLU 135 0.0001

GLU 135 LEU 136 0.0072

LEU 136 GLN 137 0.0002

GLN 137 ALA 138 0.0056

ALA 138 PHE 139 -0.0001

PHE 139 GLU 140 0.0045

GLU 140 ASN 141 -0.0003

ASN 141 ILE 142 -0.0049

ILE 142 GLU 143 -0.0000

GLU 143 ASP 144 -0.0045

ASP 144 GLU 145 0.0001

GLU 145 ILE 146 -0.0106

ILE 146 LYS 147 -0.0002

LYS 147 LEU 148 -0.0092

LEU 148 ILE 149 -0.0001

ILE 149 GLY 150 -0.0055

GLY 150 TYR 151 -0.0002

TYR 151 PHE 152 -0.0045

PHE 152 LYS 153 0.0000

LYS 153 SER 154 0.0009

SER 154 LYS 155 0.0000

LYS 155 ASP 156 -0.0027

ASP 156 SER 157 -0.0000

SER 157 GLU 158 0.0004

GLU 158 HSE 159 -0.0001

HSE 159 TYR 160 0.0065

TYR 160 LYS 161 -0.0002

LYS 161 ALA 162 0.0143

ALA 162 PHE 163 -0.0003

PHE 163 GLU 164 -0.0070

GLU 164 ASP 165 0.0004

ASP 165 ALA 166 0.0095

ALA 166 ALA 167 -0.0003

ALA 167 GLU 168 -0.0366

GLU 168 GLU 169 0.0002

GLU 169 PHE 170 -0.0095

PHE 170 HSE 171 -0.0004

HSE 171 PRO 172 0.0250

PRO 172 TYR 173 -0.0003

TYR 173 ILE 174 -0.0063

ILE 174 PRO 175 0.0001

PRO 175 PHE 176 -0.0151

PHE 176 PHE 177 -0.0001

PHE 177 ALA 178 -0.0154

ALA 178 THR 179 0.0002

THR 179 PHE 180 -0.0013

PHE 180 ASP 181 0.0001

ASP 181 SER 182 0.0041

SER 182 LYS 183 0.0000

LYS 183 VAL 184 0.0040

VAL 184 ALA 185 0.0001

ALA 185 LYS 186 0.0009

LYS 186 LYS 187 -0.0000

LYS 187 LEU 188 -0.0026

LEU 188 THR 189 0.0002

THR 189 LEU 190 -0.0037

LEU 190 LYS 191 -0.0001

LYS 191 LEU 192 -0.0010

LEU 192 ASN 193 -0.0005

ASN 193 GLU 194 0.0042

GLU 194 ILE 195 -0.0003

ILE 195 ASP 196 0.0024

ASP 196 PHE 197 -0.0000

PHE 197 TYR 198 -0.0004

TYR 198 GLU 199 -0.0001

GLU 199 ALA 200 -0.0172

ALA 200 PHE 201 -0.0001

PHE 201 MET 202 -0.0072

MET 202 GLU 203 0.0001

GLU 203 GLU 204 -0.0176

GLU 204 PRO 205 0.0001

PRO 205 VAL 206 -0.0093

VAL 206 THR 207 -0.0003

THR 207 ILE 208 -0.0066

ILE 208 PRO 209 -0.0001

PRO 209 ASP 210 0.0056

ASP 210 LYS 211 -0.0003

LYS 211 PRO 212 0.0028

PRO 212 ASN 213 0.0000

ASN 213 SER 214 -0.0158

SER 214 GLU 215 0.0001

GLU 215 GLU 216 0.0026

GLU 216 GLU 217 -0.0001

GLU 217 ILE 218 0.0009

ILE 218 VAL 219 -0.0005

VAL 219 ASN 220 -0.0115

ASN 220 PHE 221 -0.0002

PHE 221 VAL 222 0.0012

VAL 222 GLU 223 0.0003

GLU 223 GLU 224 -0.0118

GLU 224 HSE 225 0.0001

HSE 225 ARG 226 -0.0051

ARG 226 ARG 227 0.0001

ARG 227 SER 228 -0.0199

SER 228 THR 229 0.0003

THR 229 LEU 230 0.0012

LEU 230 ARG 231 0.0001

ARG 231 LYS 232 0.0188

LYS 232 LEU 233 0.0001

LEU 233 LYS 234 0.0307

LYS 234 PRO 235 -0.0003

PRO 235 GLU 236 -0.0256

GLU 236 SER 237 -0.0003

SER 237 MET 238 -0.0051

MET 238 TYR 239 0.0002

TYR 239 GLU 240 0.0065

GLU 240 THR 241 0.0005

THR 241 TRP 242 0.0051

TRP 242 GLU 243 0.0002

GLU 243 ASP 244 -0.0346

ASP 244 ASP 245 0.0003

ASP 245 MET 246 -0.0475

MET 246 ASP 247 -0.0000

ASP 247 GLY 248 0.0235

GLY 248 ILE 249 -0.0002

ILE 249 HSE 250 -0.0019

HSE 250 ILE 251 0.0002

ILE 251 VAL 252 0.0096

VAL 252 ALA 253 -0.0003

ALA 253 PHE 254 0.0071

PHE 254 ALA 255 -0.0003

ALA 255 GLU 256 -0.0008

GLU 256 GLU 257 -0.0002

GLU 257 ALA 258 -0.0071

ALA 258 ASP 259 0.0001

ASP 259 PRO 260 0.0065

PRO 260 ASP 261 -0.0003

ASP 261 GLY 262 0.0035

GLY 262 PHE 263 0.0002

PHE 263 GLU 264 0.0075

GLU 264 PHE 265 -0.0003

PHE 265 LEU 266 -0.0109

LEU 266 GLU 267 -0.0002

GLU 267 THR 268 0.0050

THR 268 LEU 269 0.0003

LEU 269 LYS 270 -0.0044

LYS 270 ALA 271 0.0005

ALA 271 VAL 272 -0.0018

VAL 272 ALA 273 -0.0002

ALA 273 GLN 274 0.0012

GLN 274 ASP 275 0.0003

ASP 275 ASN 276 -0.0069

ASN 276 THR 277 -0.0000

THR 277 GLU 278 0.0032

GLU 278 ASN 279 0.0002

ASN 279 PRO 280 -0.0114

PRO 280 ASP 281 -0.0001

ASP 281 LEU 282 0.0008

LEU 282 SER 283 0.0002

SER 283 ILE 284 0.0010

ILE 284 ILE 285 0.0001

ILE 285 TRP 286 0.0073

TRP 286 ILE 287 -0.0000

ILE 287 ASP 288 0.0017

ASP 288 PRO 289 0.0003

PRO 289 ASP 290 -0.0039

ASP 290 ASP 291 -0.0000

ASP 291 PHE 292 -0.0067

PHE 292 PRO 293 -0.0001

PRO 293 LEU 294 -0.0005

LEU 294 LEU 295 -0.0001

LEU 295 VAL 296 0.0063

VAL 296 PRO 297 -0.0002

PRO 297 TYR 298 0.0021

TYR 298 TRP 299 0.0003

TRP 299 GLU 300 -0.0040

GLU 300 LYS 301 0.0002

LYS 301 THR 302 0.0148

THR 302 PHE 303 0.0002

PHE 303 ASP 304 0.0017

ASP 304 ILE 305 -0.0002

ILE 305 ASP 306 -0.0015

ASP 306 LEU 307 0.0001

LEU 307 SER 308 0.0025

SER 308 ALA 309 -0.0001

ALA 309 PRO 310 -0.0016

PRO 310 GLN 311 -0.0000

GLN 311 ILE 312 0.0033

ILE 312 GLY 313 -0.0002

GLY 313 VAL 314 -0.0033

VAL 314 VAL 315 0.0003

VAL 315 ASN 316 -0.0002

ASN 316 VAL 317 -0.0004

VAL 317 THR 318 -0.0088

THR 318 ASP 319 -0.0003

ASP 319 ALA 320 -0.0055

ALA 320 ASP 321 -0.0001

ASP 321 SER 322 0.0003

SER 322 VAL 323 -0.0001

VAL 323 TRP 324 -0.0032

TRP 324 MET 325 -0.0001

MET 325 GLU 326 -0.0018

GLU 326 MET 327 0.0003

MET 327 ASP 328 -0.0026

ASP 328 ASP 329 0.0002

ASP 329 GLU 330 0.0090

GLU 330 GLU 331 -0.0000

GLU 331 ASP 332 -0.0058

ASP 332 LEU 333 -0.0001

LEU 333 PRO 334 0.0016

PRO 334 SER 335 -0.0003

SER 335 ALA 336 -0.0036

ALA 336 GLU 337 0.0003

GLU 337 GLU 338 0.0011

GLU 338 LEU 339 -0.0001

LEU 339 GLU 340 0.0048

GLU 340 ASP 341 0.0001

ASP 341 TRP 342 0.0052

TRP 342 LEU 343 -0.0001

LEU 343 GLU 344 0.0016

GLU 344 ASP 345 0.0000

ASP 345 VAL 346 -0.0020

VAL 346 LEU 347 0.0001

LEU 347 GLU 348 -0.0101

GLU 348 GLY 349 -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 8th, 2025.

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

*** hCasq1_no_cal ***

CA strain for 250214081644157677

--- normal mode 10 ---

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

* hCasq1_no_cal *