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

* hCasq2_no_cal *

CA strain for 250214075210134983

--- 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
GLY 1 LEU 2 -0.0001

LEU 2 ASN 3 -0.0287

ASN 3 PHE 4 -0.0001

PHE 4 PRO 5 0.0539

PRO 5 THR 6 0.0001

THR 6 TYR 7 -0.0219

TYR 7 ASP 8 -0.0004

ASP 8 GLY 9 -0.0551

GLY 9 LYS 10 -0.0001

LYS 10 ASP 11 0.0039

ASP 11 ARG 12 0.0000

ARG 12 VAL 13 0.0172

VAL 13 VAL 14 -0.0000

VAL 14 SER 15 -0.0147

SER 15 LEU 16 -0.0001

LEU 16 SER 17 -0.0043

SER 17 GLU 18 -0.0005

GLU 18 LYS 19 -0.0005

LYS 19 ASN 20 -0.0000

ASN 20 PHE 21 0.0037

PHE 21 LYS 22 0.0003

LYS 22 GLN 23 0.0014

GLN 23 VAL 24 -0.0000

VAL 24 LEU 25 0.0021

LEU 25 LYS 26 -0.0005

LYS 26 LYS 27 0.0101

LYS 27 TYR 28 -0.0001

TYR 28 ASP 29 -0.0087

ASP 29 LEU 30 -0.0001

LEU 30 LEU 31 0.0071

LEU 31 CYS 32 0.0004

CYS 32 LEU 33 -0.0076

LEU 33 TYR 34 -0.0000

TYR 34 TYR 35 0.0056

TYR 35 HSE 36 0.0001

HSE 36 GLU 37 0.0193

GLU 37 PRO 38 -0.0001

PRO 38 VAL 39 0.0161

VAL 39 SER 40 -0.0002

SER 40 SER 41 0.0064

SER 41 ASP 42 0.0000

ASP 42 LYS 43 0.0153

LYS 43 VAL 44 0.0001

VAL 44 THR 45 0.0104

THR 45 GLN 46 -0.0000

GLN 46 LYS 47 0.0050

LYS 47 GLN 48 -0.0001

GLN 48 PHE 49 -0.0083

PHE 49 GLN 50 -0.0002

GLN 50 LEU 51 -0.0011

LEU 51 LYS 52 -0.0001

LYS 52 GLU 53 -0.0023

GLU 53 ILE 54 0.0001

ILE 54 VAL 55 -0.0095

VAL 55 LEU 56 -0.0000

LEU 56 GLU 57 -0.0044

GLU 57 LEU 58 0.0002

LEU 58 VAL 59 -0.0306

VAL 59 ALA 60 0.0002

ALA 60 GLN 61 0.0295

GLN 61 VAL 62 0.0001

VAL 62 LEU 63 0.0610

LEU 63 GLU 64 0.0004

GLU 64 HSE 65 -0.0105

HSE 65 LYS 66 -0.0001

LYS 66 ALA 67 0.0280

ALA 67 ILE 68 0.0001

ILE 68 GLY 69 -0.0275

GLY 69 PHE 70 0.0000

PHE 70 VAL 71 -0.0080

VAL 71 MET 72 0.0002

MET 72 VAL 73 -0.0136

VAL 73 ASP 74 0.0001

ASP 74 ALA 75 -0.0020

ALA 75 LYS 76 0.0002

LYS 76 LYS 77 -0.0033

LYS 77 GLU 78 0.0001

GLU 78 ALA 79 -0.0027

ALA 79 LYS 80 0.0000

LYS 80 LEU 81 0.0060

LEU 81 ALA 82 -0.0002

ALA 82 LYS 83 -0.0087

LYS 83 LYS 84 0.0004

LYS 84 LEU 85 0.0113

LEU 85 GLY 86 0.0001

GLY 86 PHE 87 -0.0003

PHE 87 ASP 88 0.0000

ASP 88 GLU 89 -0.0088

GLU 89 GLU 90 -0.0004

GLU 90 GLY 91 -0.0283

GLY 91 SER 92 -0.0001

SER 92 LEU 93 -0.0003

LEU 93 TYR 94 -0.0002

TYR 94 ILE 95 0.0078

ILE 95 LEU 96 0.0002

LEU 96 LYS 97 0.0112

LYS 97 GLY 98 -0.0003

GLY 98 ASP 99 0.0035

ASP 99 ARG 100 -0.0000

ARG 100 THR 101 0.0492

THR 101 ILE 102 0.0001

ILE 102 GLU 103 -0.0076

GLU 103 PHE 104 -0.0002

PHE 104 ASP 105 -0.0494

ASP 105 GLY 106 -0.0002

GLY 106 GLU 107 0.0178

GLU 107 PHE 108 -0.0002

PHE 108 ALA 109 0.0351

ALA 109 ALA 110 0.0001

ALA 110 ASP 111 -0.0177

ASP 111 VAL 112 0.0003

VAL 112 LEU 113 0.0050

LEU 113 VAL 114 -0.0002

VAL 114 GLU 115 -0.0163

GLU 115 PHE 116 -0.0003

PHE 116 LEU 117 0.0151

LEU 117 LEU 118 -0.0004

LEU 118 ASP 119 -0.0422

ASP 119 LEU 120 0.0004

LEU 120 ILE 121 0.0009

ILE 121 GLU 122 0.0002

GLU 122 ASP 123 -0.0525

ASP 123 PRO 124 -0.0001

PRO 124 VAL 125 -0.0200

VAL 125 GLU 126 -0.0000

GLU 126 ILE 127 -0.0197

ILE 127 ILE 128 -0.0001

ILE 128 SER 129 -0.0035

SER 129 SER 130 -0.0002

SER 130 LYS 131 -0.0047

LYS 131 LEU 132 -0.0002

LEU 132 GLU 133 -0.0019

GLU 133 VAL 134 0.0001

VAL 134 GLN 135 0.0023

GLN 135 ALA 136 0.0004

ALA 136 PHE 137 -0.0087

PHE 137 GLU 138 0.0003

GLU 138 ARG 139 0.0019

ARG 139 ILE 140 -0.0001

ILE 140 GLU 141 0.0591

GLU 141 ASP 142 -0.0000

ASP 142 TYR 143 0.0210

TYR 143 ILE 144 -0.0000

ILE 144 LYS 145 -0.0070

LYS 145 LEU 146 -0.0003

LEU 146 ILE 147 0.0002

ILE 147 GLY 148 -0.0002

GLY 148 PHE 149 -0.0003

PHE 149 PHE 150 0.0003

PHE 150 LYS 151 -0.0010

LYS 151 SER 152 -0.0003

SER 152 GLU 153 -0.0030

GLU 153 ASP 154 -0.0002

ASP 154 SER 155 -0.0014

SER 155 GLU 156 0.0003

GLU 156 TYR 157 -0.0030

TYR 157 TYR 158 0.0003

TYR 158 LYS 159 0.0070

LYS 159 ALA 160 -0.0001

ALA 160 PHE 161 -0.0018

PHE 161 GLU 162 -0.0003

GLU 162 GLU 163 0.0043

GLU 163 ALA 164 0.0001

ALA 164 ALA 165 -0.0050

ALA 165 GLU 166 0.0001

GLU 166 HSE 167 -0.0042

HSE 167 PHE 168 0.0005

PHE 168 GLN 169 0.0060

GLN 169 PRO 170 0.0002

PRO 170 TYR 171 -0.0194

TYR 171 ILE 172 0.0001

ILE 172 LYS 173 -0.0098

LYS 173 PHE 174 0.0001

PHE 174 PHE 175 -0.0067

PHE 175 ALA 176 -0.0001

ALA 176 THR 177 -0.0011

THR 177 PHE 178 0.0001

PHE 178 ASP 179 -0.0037

ASP 179 LYS 180 0.0000

LYS 180 GLY 181 0.0021

GLY 181 VAL 182 0.0001

VAL 182 ALA 183 0.0022

ALA 183 LYS 184 0.0000

LYS 184 LYS 185 -0.0001

LYS 185 LEU 186 -0.0002

LEU 186 SER 187 -0.0000

SER 187 LEU 188 0.0004

LEU 188 LYS 189 0.0002

LYS 189 MET 190 0.0006

MET 190 ASN 191 0.0020

ASN 191 GLU 192 -0.0001

GLU 192 VAL 193 -0.0010

VAL 193 ASP 194 -0.0001

ASP 194 PHE 195 -0.0107

PHE 195 TYR 196 0.0000

TYR 196 GLU 197 -0.0095

GLU 197 PRO 198 0.0002

PRO 198 PHE 199 0.0107

PHE 199 MET 200 -0.0002

MET 200 ASP 201 -0.0196

ASP 201 GLU 202 0.0001

GLU 202 PRO 203 0.0286

PRO 203 ILE 204 0.0001

ILE 204 ALA 205 -0.0055

ALA 205 ILE 206 0.0001

ILE 206 PRO 207 0.0039

PRO 207 ASN 208 0.0003

ASN 208 LYS 209 -0.0054

LYS 209 PRO 210 -0.0003

PRO 210 TYR 211 0.0147

TYR 211 THR 212 -0.0001

THR 212 GLU 213 0.0222

GLU 213 GLU 214 0.0000

GLU 214 GLU 215 0.0196

GLU 215 LEU 216 -0.0003

LEU 216 VAL 217 0.0090

VAL 217 GLU 218 -0.0000

GLU 218 PHE 219 0.0138

PHE 219 VAL 220 0.0002

VAL 220 LYS 221 0.0051

LYS 221 GLU 222 -0.0002

GLU 222 HSE 223 0.0039

HSE 223 GLN 224 -0.0003

GLN 224 ARG 225 -0.1073

ARG 225 PRO 226 -0.0003

PRO 226 THR 227 -0.0389

THR 227 LEU 228 -0.0000

LEU 228 ARG 229 0.0040

ARG 229 ARG 230 -0.0001

ARG 230 LEU 231 -0.0104

LEU 231 ARG 232 0.0002

ARG 232 PRO 233 -0.0366

PRO 233 GLU 234 0.0002

GLU 234 GLU 235 0.0069

GLU 235 MET 236 0.0000

MET 236 PHE 237 -0.0276

PHE 237 GLU 238 0.0001

GLU 238 THR 239 0.0158

THR 239 TRP 240 -0.0001

TRP 240 GLU 241 -0.0297

GLU 241 ASP 242 -0.0002

ASP 242 ASP 243 0.0132

ASP 243 LEU 244 -0.0001

LEU 244 ASN 245 -0.0037

ASN 245 GLY 246 -0.0000

GLY 246 ILE 247 0.0080

ILE 247 HSE 248 -0.0001

HSE 248 ILE 249 0.0041

ILE 249 VAL 250 0.0003

VAL 250 ALA 251 -0.0027

ALA 251 PHE 252 -0.0002

PHE 252 ALA 253 0.0009

ALA 253 GLU 254 -0.0003

GLU 254 LYS 255 0.0064

LYS 255 SER 256 0.0000

SER 256 ASP 257 0.0111

ASP 257 PRO 258 -0.0001

PRO 258 ASP 259 -0.0018

ASP 259 GLY 260 -0.0000

GLY 260 TYR 261 0.0030

TYR 261 GLU 262 0.0000

GLU 262 PHE 263 -0.0063

PHE 263 LEU 264 0.0001

LEU 264 GLU 265 -0.0081

GLU 265 ILE 266 0.0001

ILE 266 LEU 267 -0.0039

LEU 267 LYS 268 -0.0000

LYS 268 GLN 269 -0.0033

GLN 269 VAL 270 -0.0004

VAL 270 ALA 271 -0.0063

ALA 271 ARG 272 0.0001

ARG 272 ASP 273 -0.0023

ASP 273 ASN 274 0.0003

ASN 274 THR 275 -0.0182

THR 275 ASP 276 -0.0001

ASP 276 ASN 277 -0.0106

ASN 277 PRO 278 0.0001

PRO 278 ASP 279 0.0020

ASP 279 LEU 280 0.0000

LEU 280 SER 281 -0.0008

SER 281 ILE 282 -0.0002

ILE 282 LEU 283 0.0076

LEU 283 TRP 284 -0.0002

TRP 284 ILE 285 -0.0068

ILE 285 ASP 286 0.0004

ASP 286 PRO 287 0.0145

PRO 287 ASP 288 -0.0002

ASP 288 ASP 289 -0.0173

ASP 289 PHE 290 -0.0003

PHE 290 PRO 291 0.0225

PRO 291 LEU 292 -0.0001

LEU 292 LEU 293 -0.0053

LEU 293 VAL 294 0.0002

VAL 294 ALA 295 0.0045

ALA 295 TYR 296 -0.0003

TYR 296 TRP 297 -0.0031

TRP 297 GLU 298 0.0001

GLU 298 LYS 299 0.0058

LYS 299 THR 300 0.0002

THR 300 PHE 301 0.0009

PHE 301 LYS 302 0.0001

LYS 302 ILE 303 0.0090

ILE 303 ASP 304 -0.0001

ASP 304 LEU 305 0.0028

LEU 305 PHE 306 -0.0002

PHE 306 ARG 307 -0.0079

ARG 307 PRO 308 0.0002

PRO 308 GLN 309 -0.0001

GLN 309 ILE 310 -0.0000

ILE 310 GLY 311 0.0023

GLY 311 VAL 312 0.0006

VAL 312 VAL 313 0.0039

VAL 313 ASN 314 -0.0000

ASN 314 VAL 315 -0.0016

VAL 315 THR 316 0.0001

THR 316 ASP 317 -0.0042

ASP 317 ALA 318 0.0003

ALA 318 ASP 319 -0.0018

ASP 319 SER 320 -0.0000

SER 320 VAL 321 -0.0003

VAL 321 TRP 322 0.0002

TRP 322 MET 323 -0.0004

MET 323 GLU 324 0.0001

GLU 324 ILE 325 -0.0003

ILE 325 PRO 326 0.0003

PRO 326 ASP 327 0.0065

ASP 327 ASP 328 0.0004

ASP 328 ASP 329 0.0029

ASP 329 ASP 330 0.0004

ASP 330 LEU 331 0.0064

LEU 331 PRO 332 0.0001

PRO 332 THR 333 0.0030

THR 333 ALA 334 -0.0003

ALA 334 GLU 335 -0.0005

GLU 335 GLU 336 0.0002

GLU 336 LEU 337 -0.0004

LEU 337 GLU 338 -0.0002

GLU 338 ASP 339 -0.0033

ASP 339 TRP 340 -0.0002

TRP 340 ILE 341 -0.0056

ILE 341 GLU 342 0.0001

GLU 342 ASP 343 -0.0024

ASP 343 VAL 344 -0.0002

VAL 344 LEU 345 -0.0076

LEU 345 SER 346 0.0002

SER 346 GLY 347 -0.0137

GLY 347 LYS 348 -0.0001

LYS 348 ILE 349 0.0093

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.

*** hCasq2_no_cal ***

CA strain for 250214075210134983

--- normal mode 10 ---

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

* hCasq2_no_cal *