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

* *

CA strain for 240112142738850346

--- 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
MET 1 VAL 2 0.0000

VAL 2 ARG 3 -0.0205

ARG 3 GLU 4 0.0001

GLU 4 GLU 5 0.0023

GLU 5 VAL 6 -0.0001

VAL 6 ALA 7 -0.0218

ALA 7 GLY 8 -0.0001

GLY 8 SER 9 0.0300

SER 9 THR 10 -0.0003

THR 10 GLN 11 0.0184

GLN 11 THR 12 -0.0001

THR 12 LEU 13 -0.0160

LEU 13 GLN 14 -0.0001

GLN 14 TRP 15 -0.0014

TRP 15 LYS 16 0.0000

LYS 16 CYS 17 0.0128

CYS 17 VAL 18 -0.0003

VAL 18 GLU 19 0.0200

GLU 19 SER 20 -0.0003

SER 20 ARG 21 0.0137

ARG 21 VAL 22 0.0001

VAL 22 ASP 23 -0.0022

ASP 23 SER 24 0.0004

SER 24 LYS 25 -0.0017

LYS 25 ARG 26 -0.0002

ARG 26 LEU 27 0.0032

LEU 27 TYR 28 -0.0004

TYR 28 TYR 29 0.0086

TYR 29 GLY 30 0.0003

GLY 30 ARG 31 0.0117

ARG 31 PHE 32 0.0000

PHE 32 ILE 33 0.0081

ILE 33 LEU 34 0.0001

LEU 34 SER 35 0.0069

SER 35 PRO 36 0.0001

PRO 36 LEU 37 0.0082

LEU 37 ARG 38 -0.0001

ARG 38 LYS 39 -0.0104

LYS 39 GLY 40 0.0002

GLY 40 GLN 41 0.0070

GLN 41 ALA 42 0.0003

ALA 42 ASP 43 -0.0014

ASP 43 THR 44 0.0003

THR 44 VAL 45 0.0066

VAL 45 GLY 46 -0.0000

GLY 46 ILE 47 0.0022

ILE 47 ALA 48 -0.0001

ALA 48 LEU 49 0.0006

LEU 49 ARG 50 -0.0001

ARG 50 ARG 51 0.0108

ARG 51 ALA 52 0.0001

ALA 52 LEU 53 0.0017

LEU 53 LEU 54 0.0002

LEU 54 GLY 55 0.0130

GLY 55 GLU 56 0.0003

GLU 56 ILE 57 0.0038

ILE 57 GLU 58 0.0000

GLU 58 GLY 59 -0.0014

GLY 59 ALA 60 0.0003

ALA 60 CYS 61 -0.0009

CYS 61 ILE 62 -0.0004

ILE 62 THR 63 0.0013

THR 63 ARG 64 0.0002

ARG 64 ALA 65 -0.0014

ALA 65 LYS 66 0.0002

LYS 66 PHE 67 -0.0006

PHE 67 GLY 68 0.0004

GLY 68 SER 69 0.0008

SER 69 VAL 70 -0.0001

VAL 70 PRO 71 -0.0001

PRO 71 HIS 72 0.0003

HIS 72 GLU 73 0.0004

GLU 73 TYR 74 -0.0002

TYR 74 SER 75 -0.0003

SER 75 THR 76 -0.0001

THR 76 ILE 77 -0.0006

ILE 77 ALA 78 -0.0001

ALA 78 GLY 79 -0.0001

GLY 79 ILE 80 -0.0001

ILE 80 GLU 81 0.0000

GLU 81 GLU 82 0.0004

GLU 82 SER 83 0.0005

SER 83 VAL 84 -0.0002

VAL 84 GLN 85 0.0002

GLN 85 GLU 86 -0.0002

GLU 86 ILE 87 0.0000

ILE 87 LEU 88 0.0003

LEU 88 LEU 89 0.0014

LEU 89 ASN 90 -0.0000

ASN 90 LEU 91 -0.0005

LEU 91 LYS 92 -0.0001

LYS 92 GLU 93 0.0059

GLU 93 ILE 94 0.0007

ILE 94 VAL 95 -0.0003

VAL 95 LEU 96 0.0003

LEU 96 ARG 97 0.0006

ARG 97 SER 98 0.0000

SER 98 ASN 99 0.0001

ASN 99 LEU 100 -0.0001

LEU 100 TYR 101 0.0012

TYR 101 GLY 102 -0.0005

GLY 102 VAL 103 0.0008

VAL 103 ARG 104 -0.0001

ARG 104 ASP 105 0.0008

ASP 105 ALA 106 -0.0003

ALA 106 SER 107 0.0013

SER 107 ILE 108 -0.0003

ILE 108 CYS 109 0.0006

CYS 109 VAL 110 0.0000

VAL 110 LYS 111 0.0008

LYS 111 GLY 112 -0.0001

GLY 112 PRO 113 -0.0006

PRO 113 ARG 114 0.0000

ARG 114 TYR 115 0.0002

TYR 115 ILE 116 0.0000

ILE 116 THR 117 0.0016

THR 117 ALA 118 -0.0003

ALA 118 GLN 119 -0.0002

GLN 119 ASP 120 -0.0004

ASP 120 ILE 121 0.0008

ILE 121 ILE 122 0.0001

ILE 122 LEU 123 0.0021

LEU 123 PRO 124 0.0000

PRO 124 PRO 125 -0.0005

PRO 125 SER 126 0.0002

SER 126 VAL 127 -0.0010

VAL 127 GLU 128 0.0003

GLU 128 ILE 129 -0.0004

ILE 129 VAL 130 -0.0004

VAL 130 ASP 131 0.0025

ASP 131 THR 132 -0.0002

THR 132 ALA 133 0.0005

ALA 133 GLN 134 -0.0000

GLN 134 PRO 135 0.0027

PRO 135 ILE 136 -0.0000

ILE 136 ALA 137 0.0009

ALA 137 ASN 138 -0.0000

ASN 138 LEU 139 0.0005

LEU 139 THR 140 0.0000

THR 140 GLU 141 -0.0004

GLU 141 PRO 142 0.0003

PRO 142 ILE 143 -0.0000

ILE 143 ASP 144 -0.0001

ASP 144 PHE 145 -0.0005

PHE 145 CYS 146 0.0001

CYS 146 ILE 147 -0.0011

ILE 147 ASP 148 0.0003

ASP 148 LEU 149 -0.0003

LEU 149 GLN 150 0.0002

GLN 150 ILE 151 -0.0003

ILE 151 LYS 152 0.0000

LYS 152 ARG 153 -0.0005

ARG 153 ASP 154 0.0000

ASP 154 ARG 155 0.0002

ARG 155 GLY 156 0.0002

GLY 156 TYR 157 -0.0072

TYR 157 GLN 158 0.0002

GLN 158 THR 159 -0.0032

THR 159 GLU 160 0.0003

GLU 160 LEU 161 -0.0027

LEU 161 ARG 162 0.0000

ARG 162 LYS 163 0.0006

LYS 163 ASN 164 0.0000

ASN 164 TYR 165 0.0007

TYR 165 GLN 166 0.0002

GLN 166 ASP 167 -0.0005

ASP 167 GLY 168 0.0003

GLY 168 SER 169 -0.0005

SER 169 TYR 170 0.0002

TYR 170 PRO 171 -0.0015

PRO 171 ILE 172 -0.0001

ILE 172 ASP 173 -0.0006

ASP 173 ALA 174 0.0004

ALA 174 VAL 175 0.0000

VAL 175 SER 176 -0.0000

SER 176 MET 177 0.0010

MET 177 PRO 178 -0.0005

PRO 178 VAL 179 0.0032

VAL 179 ARG 180 -0.0001

ARG 180 ASN 181 -0.0049

ASN 181 VAL 182 -0.0001

VAL 182 ASN 183 0.0019

ASN 183 TYR 184 -0.0000

TYR 184 SER 185 0.0124

SER 185 ILE 186 0.0001

ILE 186 PHE 187 0.0077

PHE 187 SER 188 0.0000

SER 188 CYS 189 0.0002

CYS 189 GLY 190 -0.0001

GLY 190 ASN 191 0.0112

ASN 191 GLY 192 0.0004

GLY 192 ASN 193 -0.0022

ASN 193 GLU 194 0.0001

GLU 194 LYS 195 -0.0031

LYS 195 HIS 196 0.0001

HIS 196 GLU 197 0.0026

GLU 197 ILE 198 0.0005

ILE 198 LEU 199 -0.0017

LEU 199 PHE 200 0.0001

PHE 200 LEU 201 0.0096

LEU 201 GLU 202 -0.0002

GLU 202 ILE 203 0.0062

ILE 203 TRP 204 -0.0002

TRP 204 THR 205 0.0026

THR 205 ASN 206 -0.0000

ASN 206 GLY 207 -0.0006

GLY 207 SER 208 -0.0000

SER 208 LEU 209 0.0010

LEU 209 THR 210 -0.0002

THR 210 PRO 211 0.0015

PRO 211 LYS 212 -0.0001

LYS 212 GLU 213 -0.0003

GLU 213 ALA 214 0.0001

ALA 214 LEU 215 -0.0023

LEU 215 TYR 216 -0.0004

TYR 216 GLU 217 -0.0075

GLU 217 ALA 218 0.0003

ALA 218 SER 219 -0.0052

SER 219 ARG 220 0.0002

ARG 220 ASN 221 -0.0096

ASN 221 LEU 222 -0.0000

LEU 222 ILE 223 0.0067

ILE 223 ASP 224 0.0001

ASP 224 LEU 225 -0.0086

LEU 225 PHE 226 -0.0003

PHE 226 LEU 227 0.0029

LEU 227 PRO 228 -0.0001

PRO 228 PHE 229 0.0110

PHE 229 LEU 230 -0.0000

LEU 230 HIS 231 -0.0432

HIS 231 ALA 232 -0.0001

ALA 232 GLU 233 -0.0348

GLU 233 GLU 234 0.0005

GLU 234 GLU 235 -0.0005

GLU 235 GLY 236 -0.0001

GLY 236 ALA 237 0.0151

ALA 237 SER 238 -0.0004

SER 238 PHE 239 0.0039

PHE 239 GLU 240 -0.0001

GLU 240 GLU 241 0.0011

GLU 241 ASN 242 -0.0002

ASN 242 LYS 243 -0.0039

LYS 243 ASN 244 0.0000

ASN 244 ARG 245 0.0072

ARG 245 PHE 246 -0.0003

PHE 246 THR 247 0.0022

THR 247 PRO 248 0.0002

PRO 248 PRO 249 -0.0080

PRO 249 LEU 250 -0.0001

LEU 250 PHE 251 -0.0122

PHE 251 THR 252 -0.0001

THR 252 PHE 253 -0.0065

PHE 253 GLN 254 0.0003

GLN 254 LYS 255 -0.0097

LYS 255 ARG 256 -0.0001

ARG 256 LEU 257 0.0039

LEU 257 THR 258 0.0001

THR 258 ASN 259 0.0046

ASN 259 LEU 260 0.0006

LEU 260 LYS 261 -0.0060

LYS 261 LYS 262 -0.0001

LYS 262 ASN 263 0.0048

ASN 263 LYS 264 0.0001

LYS 264 LYS 265 0.0038

LYS 265 GLY 266 -0.0001

GLY 266 ILE 267 -0.0026

ILE 267 PRO 268 0.0000

PRO 268 LEU 269 0.0069

LEU 269 ASN 270 -0.0002

ASN 270 CYS 271 0.0014

CYS 271 ILE 272 0.0001

ILE 272 PHE 273 0.0004

PHE 273 ILE 274 -0.0001

ILE 274 ASP 275 0.0012

ASP 275 GLN 276 0.0003

GLN 276 LEU 277 0.0133

LEU 277 GLU 278 -0.0002

GLU 278 LEU 279 0.0010

LEU 279 THR 280 -0.0001

THR 280 SER 281 -0.0002

SER 281 ARG 282 0.0004

ARG 282 THR 283 -0.0001

THR 283 TYR 284 -0.0001

TYR 284 ASN 285 0.0011

ASN 285 CYS 286 0.0001

CYS 286 LEU 287 -0.0010

LEU 287 LYS 288 0.0000

LYS 288 ARG 289 0.0005

ARG 289 ALA 290 0.0001

ALA 290 ASN 291 -0.0013

ASN 291 ILE 292 -0.0001

ILE 292 HIS 293 -0.0004

HIS 293 THR 294 -0.0002

THR 294 LEU 295 -0.0015

LEU 295 LEU 296 0.0003

LEU 296 ASP 297 -0.0012

ASP 297 LEU 298 -0.0000

LEU 298 LEU 299 0.0002

LEU 299 SER 300 0.0002

SER 300 LYS 301 -0.0048

LYS 301 THR 302 0.0001

THR 302 GLU 303 -0.0012

GLU 303 GLU 304 0.0000

GLU 304 ASP 305 0.0004

ASP 305 LEU 306 -0.0003

LEU 306 LEU 307 -0.0005

LEU 307 ARG 308 0.0003

ARG 308 ILE 309 0.0006

ILE 309 ASP 310 -0.0003

ASP 310 SER 311 0.0004

SER 311 PHE 312 -0.0002

PHE 312 ARG 313 -0.0004

ARG 313 MET 314 0.0001

MET 314 GLU 315 0.0000

GLU 315 ASP 316 0.0002

ASP 316 ARG 317 -0.0001

ARG 317 LYS 318 0.0001

LYS 318 HIS 319 0.0011

HIS 319 ILE 320 -0.0002

ILE 320 TRP 321 -0.0004

TRP 321 ASP 322 -0.0002

ASP 322 THR 323 0.0009

THR 323 LEU 324 -0.0004

LEU 324 GLU 325 0.0001

GLU 325 LYS 326 0.0003

LYS 326 HIS 327 -0.0004

HIS 327 LEU 328 0.0004

LEU 328 PRO 329 0.0005

PRO 329 ILE 330 -0.0004

ILE 330 ASP 331 -0.0003

ASP 331 LEU 332 0.0000

LEU 332 LEU 333 -0.0016

LEU 333 LYS 334 -0.0001

LYS 334 ASN 335 0.0007

ASN 335 LYS 336 -0.0000

LYS 336 LEU 337 -0.0005

LEU 337 SER 338 0.0002

SER 338 PHE 339 0.0002

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 10 ---

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

* *