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

* *

CA strain for 240112142738850346

--- normal mode 15 ---

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 VAL 2 0.0002

VAL 2 ARG 3 -0.0073

ARG 3 GLU 4 -0.0002

GLU 4 GLU 5 -0.0006

GLU 5 VAL 6 -0.0002

VAL 6 ALA 7 0.0117

ALA 7 GLY 8 -0.0003

GLY 8 SER 9 0.0363

SER 9 THR 10 0.0001

THR 10 GLN 11 -0.0289

GLN 11 THR 12 -0.0003

THR 12 LEU 13 0.0326

LEU 13 GLN 14 0.0000

GLN 14 TRP 15 -0.0110

TRP 15 LYS 16 -0.0004

LYS 16 CYS 17 -0.0071

CYS 17 VAL 18 0.0000

VAL 18 GLU 19 0.0122

GLU 19 SER 20 0.0000

SER 20 ARG 21 0.0028

ARG 21 VAL 22 0.0000

VAL 22 ASP 23 -0.0039

ASP 23 SER 24 -0.0000

SER 24 LYS 25 0.0056

LYS 25 ARG 26 -0.0002

ARG 26 LEU 27 0.0144

LEU 27 TYR 28 -0.0004

TYR 28 TYR 29 0.0151

TYR 29 GLY 30 0.0000

GLY 30 ARG 31 0.0152

ARG 31 PHE 32 -0.0000

PHE 32 ILE 33 -0.0030

ILE 33 LEU 34 0.0002

LEU 34 SER 35 -0.0094

SER 35 PRO 36 -0.0004

PRO 36 LEU 37 0.0104

LEU 37 ARG 38 0.0002

ARG 38 LYS 39 0.0002

LYS 39 GLY 40 0.0000

GLY 40 GLN 41 0.0044

GLN 41 ALA 42 -0.0000

ALA 42 ASP 43 0.0004

ASP 43 THR 44 0.0001

THR 44 VAL 45 0.0046

VAL 45 GLY 46 0.0001

GLY 46 ILE 47 0.0012

ILE 47 ALA 48 -0.0002

ALA 48 LEU 49 -0.0006

LEU 49 ARG 50 0.0002

ARG 50 ARG 51 0.0013

ARG 51 ALA 52 0.0003

ALA 52 LEU 53 0.0017

LEU 53 LEU 54 -0.0001

LEU 54 GLY 55 0.0012

GLY 55 GLU 56 0.0001

GLU 56 ILE 57 -0.0093

ILE 57 GLU 58 0.0003

GLU 58 GLY 59 -0.0034

GLY 59 ALA 60 -0.0002

ALA 60 CYS 61 0.0012

CYS 61 ILE 62 0.0004

ILE 62 THR 63 -0.0003

THR 63 ARG 64 0.0004

ARG 64 ALA 65 -0.0010

ALA 65 LYS 66 0.0000

LYS 66 PHE 67 -0.0006

PHE 67 GLY 68 0.0001

GLY 68 SER 69 0.0006

SER 69 VAL 70 -0.0000

VAL 70 PRO 71 -0.0001

PRO 71 HIS 72 -0.0001

HIS 72 GLU 73 0.0004

GLU 73 TYR 74 0.0002

TYR 74 SER 75 -0.0008

SER 75 THR 76 0.0002

THR 76 ILE 77 -0.0004

ILE 77 ALA 78 -0.0003

ALA 78 GLY 79 0.0003

GLY 79 ILE 80 0.0000

ILE 80 GLU 81 -0.0002

GLU 81 GLU 82 -0.0002

GLU 82 SER 83 -0.0011

SER 83 VAL 84 -0.0001

VAL 84 GLN 85 -0.0001

GLN 85 GLU 86 0.0001

GLU 86 ILE 87 -0.0009

ILE 87 LEU 88 -0.0001

LEU 88 LEU 89 -0.0017

LEU 89 ASN 90 -0.0001

ASN 90 LEU 91 -0.0008

LEU 91 LYS 92 -0.0000

LYS 92 GLU 93 -0.0023

GLU 93 ILE 94 -0.0003

ILE 94 VAL 95 0.0039

VAL 95 LEU 96 0.0001

LEU 96 ARG 97 -0.0002

ARG 97 SER 98 0.0002

SER 98 ASN 99 0.0006

ASN 99 LEU 100 0.0001

LEU 100 TYR 101 -0.0015

TYR 101 GLY 102 0.0001

GLY 102 VAL 103 -0.0067

VAL 103 ARG 104 -0.0000

ARG 104 ASP 105 -0.0052

ASP 105 ALA 106 0.0004

ALA 106 SER 107 -0.0070

SER 107 ILE 108 -0.0000

ILE 108 CYS 109 -0.0032

CYS 109 VAL 110 0.0001

VAL 110 LYS 111 -0.0027

LYS 111 GLY 112 0.0004

GLY 112 PRO 113 -0.0022

PRO 113 ARG 114 0.0002

ARG 114 TYR 115 0.0033

TYR 115 ILE 116 0.0001

ILE 116 THR 117 0.0034

THR 117 ALA 118 0.0003

ALA 118 GLN 119 -0.0021

GLN 119 ASP 120 -0.0001

ASP 120 ILE 121 -0.0028

ILE 121 ILE 122 0.0004

ILE 122 LEU 123 -0.0068

LEU 123 PRO 124 -0.0002

PRO 124 PRO 125 -0.0010

PRO 125 SER 126 -0.0004

SER 126 VAL 127 0.0021

VAL 127 GLU 128 -0.0004

GLU 128 ILE 129 0.0009

ILE 129 VAL 130 -0.0001

VAL 130 ASP 131 -0.0021

ASP 131 THR 132 0.0001

THR 132 ALA 133 -0.0048

ALA 133 GLN 134 -0.0001

GLN 134 PRO 135 0.0050

PRO 135 ILE 136 -0.0003

ILE 136 ALA 137 0.0016

ALA 137 ASN 138 -0.0003

ASN 138 LEU 139 0.0018

LEU 139 THR 140 -0.0001

THR 140 GLU 141 0.0007

GLU 141 PRO 142 0.0003

PRO 142 ILE 143 -0.0009

ILE 143 ASP 144 0.0001

ASP 144 PHE 145 -0.0007

PHE 145 CYS 146 0.0000

CYS 146 ILE 147 -0.0030

ILE 147 ASP 148 0.0004

ASP 148 LEU 149 -0.0019

LEU 149 GLN 150 0.0000

GLN 150 ILE 151 0.0007

ILE 151 LYS 152 -0.0000

LYS 152 ARG 153 -0.0048

ARG 153 ASP 154 -0.0001

ASP 154 ARG 155 -0.0054

ARG 155 GLY 156 0.0002

GLY 156 TYR 157 0.0073

TYR 157 GLN 158 -0.0003

GLN 158 THR 159 0.0033

THR 159 GLU 160 0.0000

GLU 160 LEU 161 0.0034

LEU 161 ARG 162 -0.0005

ARG 162 LYS 163 -0.0007

LYS 163 ASN 164 -0.0001

ASN 164 TYR 165 -0.0002

TYR 165 GLN 166 -0.0004

GLN 166 ASP 167 0.0015

ASP 167 GLY 168 0.0003

GLY 168 SER 169 -0.0005

SER 169 TYR 170 0.0002

TYR 170 PRO 171 0.0010

PRO 171 ILE 172 0.0000

ILE 172 ASP 173 0.0014

ASP 173 ALA 174 -0.0004

ALA 174 VAL 175 0.0028

VAL 175 SER 176 0.0003

SER 176 MET 177 0.0036

MET 177 PRO 178 0.0002

PRO 178 VAL 179 0.0028

VAL 179 ARG 180 -0.0002

ARG 180 ASN 181 0.0177

ASN 181 VAL 182 -0.0003

VAL 182 ASN 183 0.0142

ASN 183 TYR 184 0.0003

TYR 184 SER 185 0.0155

SER 185 ILE 186 -0.0002

ILE 186 PHE 187 0.0101

PHE 187 SER 188 -0.0002

SER 188 CYS 189 0.0474

CYS 189 GLY 190 0.0001

GLY 190 ASN 191 0.0010

ASN 191 GLY 192 -0.0001

GLY 192 ASN 193 0.0061

ASN 193 GLU 194 0.0001

GLU 194 LYS 195 0.0120

LYS 195 HIS 196 0.0003

HIS 196 GLU 197 0.0185

GLU 197 ILE 198 0.0001

ILE 198 LEU 199 -0.0036

LEU 199 PHE 200 -0.0001

PHE 200 LEU 201 0.0143

LEU 201 GLU 202 0.0001

GLU 202 ILE 203 0.0163

ILE 203 TRP 204 0.0002

TRP 204 THR 205 0.0127

THR 205 ASN 206 0.0000

ASN 206 GLY 207 0.0001

GLY 207 SER 208 -0.0002

SER 208 LEU 209 -0.0010

LEU 209 THR 210 -0.0000

THR 210 PRO 211 0.0052

PRO 211 LYS 212 -0.0001

LYS 212 GLU 213 0.0051

GLU 213 ALA 214 -0.0000

ALA 214 LEU 215 -0.0013

LEU 215 TYR 216 0.0002

TYR 216 GLU 217 0.0018

GLU 217 ALA 218 0.0001

ALA 218 SER 219 -0.0084

SER 219 ARG 220 -0.0001

ARG 220 ASN 221 0.0218

ASN 221 LEU 222 -0.0001

LEU 222 ILE 223 -0.0111

ILE 223 ASP 224 -0.0000

ASP 224 LEU 225 0.0038

LEU 225 PHE 226 -0.0001

PHE 226 LEU 227 -0.0083

LEU 227 PRO 228 -0.0002

PRO 228 PHE 229 -0.0109

PHE 229 LEU 230 0.0003

LEU 230 HIS 231 -0.0182

HIS 231 ALA 232 0.0000

ALA 232 GLU 233 -0.0012

GLU 233 GLU 234 -0.0001

GLU 234 GLU 235 -0.0101

GLU 235 GLY 236 -0.0001

GLY 236 ALA 237 0.0101

ALA 237 SER 238 -0.0002

SER 238 PHE 239 0.0018

PHE 239 GLU 240 -0.0001

GLU 240 GLU 241 0.0045

GLU 241 ASN 242 0.0000

ASN 242 LYS 243 -0.0018

LYS 243 ASN 244 0.0001

ASN 244 ARG 245 0.0253

ARG 245 PHE 246 -0.0000

PHE 246 THR 247 0.0031

THR 247 PRO 248 -0.0002

PRO 248 PRO 249 -0.0116

PRO 249 LEU 250 -0.0003

LEU 250 PHE 251 0.0177

PHE 251 THR 252 0.0001

THR 252 PHE 253 0.0316

PHE 253 GLN 254 -0.0002

GLN 254 LYS 255 0.0270

LYS 255 ARG 256 0.0003

ARG 256 LEU 257 -0.0011

LEU 257 THR 258 -0.0001

THR 258 ASN 259 0.0253

ASN 259 LEU 260 -0.0001

LEU 260 LYS 261 0.0106

LYS 261 LYS 262 0.0001

LYS 262 ASN 263 0.0111

ASN 263 LYS 264 -0.0002

LYS 264 LYS 265 -0.0099

LYS 265 GLY 266 -0.0003

GLY 266 ILE 267 -0.0278

ILE 267 PRO 268 -0.0002

PRO 268 LEU 269 -0.0363

LEU 269 ASN 270 -0.0003

ASN 270 CYS 271 -0.0062

CYS 271 ILE 272 -0.0000

ILE 272 PHE 273 0.0314

PHE 273 ILE 274 0.0000

ILE 274 ASP 275 0.0138

ASP 275 GLN 276 0.0002

GLN 276 LEU 277 0.0069

LEU 277 GLU 278 -0.0000

GLU 278 LEU 279 -0.0027

LEU 279 THR 280 0.0000

THR 280 SER 281 -0.0037

SER 281 ARG 282 -0.0004

ARG 282 THR 283 0.0001

THR 283 TYR 284 0.0002

TYR 284 ASN 285 0.0086

ASN 285 CYS 286 0.0001

CYS 286 LEU 287 -0.0059

LEU 287 LYS 288 -0.0004

LYS 288 ARG 289 0.0078

ARG 289 ALA 290 -0.0000

ALA 290 ASN 291 -0.0045

ASN 291 ILE 292 0.0000

ILE 292 HIS 293 0.0058

HIS 293 THR 294 -0.0002

THR 294 LEU 295 -0.0045

LEU 295 LEU 296 -0.0002

LEU 296 ASP 297 -0.0335

ASP 297 LEU 298 0.0002

LEU 298 LEU 299 0.0067

LEU 299 SER 300 -0.0002

SER 300 LYS 301 -0.0250

LYS 301 THR 302 -0.0002

THR 302 GLU 303 -0.0019

GLU 303 GLU 304 0.0004

GLU 304 ASP 305 0.0020

ASP 305 LEU 306 -0.0003

LEU 306 LEU 307 -0.0042

LEU 307 ARG 308 -0.0002

ARG 308 ILE 309 0.0069

ILE 309 ASP 310 -0.0001

ASP 310 SER 311 -0.0010

SER 311 PHE 312 0.0001

PHE 312 ARG 313 0.0003

ARG 313 MET 314 0.0003

MET 314 GLU 315 -0.0020

GLU 315 ASP 316 -0.0001

ASP 316 ARG 317 0.0011

ARG 317 LYS 318 0.0005

LYS 318 HIS 319 -0.0006

HIS 319 ILE 320 -0.0002

ILE 320 TRP 321 -0.0001

TRP 321 ASP 322 -0.0001

ASP 322 THR 323 0.0009

THR 323 LEU 324 -0.0000

LEU 324 GLU 325 -0.0043

GLU 325 LYS 326 -0.0001

LYS 326 HIS 327 0.0126

HIS 327 LEU 328 -0.0000

LEU 328 PRO 329 -0.0127

PRO 329 ILE 330 0.0000

ILE 330 ASP 331 -0.0055

ASP 331 LEU 332 -0.0001

LEU 332 LEU 333 -0.0019

LEU 333 LYS 334 0.0004

LYS 334 ASN 335 0.0050

ASN 335 LYS 336 -0.0003

LYS 336 LEU 337 -0.0025

LEU 337 SER 338 -0.0003

SER 338 PHE 339 -0.0011

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.

*** ***

CA strain for 240112142738850346

--- normal mode 15 ---

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

* *