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

* 01-JUN-22 *

CA strain for 240221025813253280

--- 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 ALA 2 0.0001

ALA 2 ASN 3 0.0120

ASN 3 SER 4 0.0001

SER 4 ALA 5 0.0644

ALA 5 SER 6 -0.0003

SER 6 PRO 7 -0.1586

PRO 7 GLU 8 0.0001

GLU 8 GLN 9 0.0937

GLN 9 ASN 10 -0.0002

ASN 10 GLN 11 -0.0506

GLN 11 ASN 12 -0.0001

ASN 12 HIS 13 0.0284

HIS 13 CYS 14 0.0001

CYS 14 SER 15 -0.0118

SER 15 ALA 16 0.0002

ALA 16 ILE 17 0.0926

ILE 17 ASN 18 -0.0000

ASN 18 ASN 19 0.0188

ASN 19 SER 20 -0.0003

SER 20 ILE 21 0.0124

ILE 21 PRO 22 0.0001

PRO 22 LEU 23 0.0055

LEU 23 MET 24 -0.0003

MET 24 GLN 25 0.0122

GLN 25 GLY 26 0.0000

GLY 26 ASN 27 0.0120

ASN 27 LEU 28 -0.0001

LEU 28 PRO 29 -0.0516

PRO 29 THR 30 -0.0001

THR 30 LEU 31 -0.0023

LEU 31 THR 32 -0.0001

THR 32 LEU 33 -0.0164

LEU 33 SER 34 0.0001

SER 34 GLY 35 0.0049

GLY 35 LYS 36 -0.0001

LYS 36 ILE 37 0.0023

ILE 37 ARG 38 0.0005

ARG 38 VAL 39 0.0040

VAL 39 THR 40 0.0002

THR 40 VAL 41 0.0060

VAL 41 THR 42 0.0003

THR 42 PHE 43 -0.0008

PHE 43 PHE 44 0.0003

PHE 44 LEU 45 0.0048

LEU 45 PHE 46 0.0002

PHE 46 LEU 47 -0.0002

LEU 47 LEU 48 0.0002

LEU 48 SER 49 -0.0023

SER 49 ALA 50 -0.0000

ALA 50 THR 51 -0.0001

THR 51 PHE 52 0.0001

PHE 52 ASN 53 -0.0035

ASN 53 ALA 54 0.0000

ALA 54 SER 55 0.0009

SER 55 PHE 56 0.0003

PHE 56 LEU 57 -0.0016

LEU 57 LEU 58 -0.0000

LEU 58 LYS 59 0.0012

LYS 59 LEU 60 -0.0004

LEU 60 GLN 61 -0.0005

GLN 61 LYS 62 -0.0003

LYS 62 TRP 63 0.0000

TRP 63 THR 64 -0.0005

THR 64 GLN 65 -0.0007

GLN 65 LYS 66 -0.0001

LYS 66 LYS 67 -0.0004

LYS 67 GLU 68 0.0003

GLU 68 LYS 69 0.0014

LYS 69 GLY 70 -0.0004

GLY 70 LYS 71 -0.0014

LYS 71 LYS 72 -0.0000

LYS 72 LEU 73 0.0003

LEU 73 SER 74 -0.0005

SER 74 ARG 75 -0.0032

ARG 75 MET 76 -0.0003

MET 76 LYS 77 0.0035

LYS 77 LEU 78 0.0002

LEU 78 LEU 79 -0.0053

LEU 79 LEU 80 -0.0002

LEU 80 LYS 81 0.0015

LYS 81 HIS 82 0.0004

HIS 82 LEU 83 -0.0028

LEU 83 THR 84 0.0004

THR 84 LEU 85 -0.0013

LEU 85 ALA 86 -0.0004

ALA 86 ASN 87 -0.0009

ASN 87 LEU 88 0.0004

LEU 88 LEU 89 0.0010

LEU 89 GLU 90 -0.0001

GLU 90 THR 91 -0.0053

THR 91 LEU 92 -0.0001

LEU 92 ILE 93 0.0030

ILE 93 VAL 94 -0.0001

VAL 94 MET 95 -0.0006

MET 95 PRO 96 0.0001

PRO 96 LEU 97 0.0050

LEU 97 ASP 98 0.0002

ASP 98 GLY 99 0.0011

GLY 99 MET 100 0.0000

MET 100 TRP 101 0.0025

TRP 101 ASN 102 0.0000

ASN 102 ILE 103 -0.0091

ILE 103 THR 104 -0.0002

THR 104 VAL 105 0.0068

VAL 105 GLN 106 0.0001

GLN 106 TRP 107 0.0053

TRP 107 TYR 108 0.0002

TYR 108 ALA 109 0.0081

ALA 109 GLY 110 0.0001

GLY 110 GLU 111 -0.0195

GLU 111 LEU 112 -0.0000

LEU 112 LEU 113 0.0045

LEU 113 CYS 114 0.0001

CYS 114 LYS 115 0.0051

LYS 115 VAL 116 0.0001

VAL 116 LEU 117 -0.0079

LEU 117 SER 118 0.0002

SER 118 TYR 119 0.0048

TYR 119 LEU 120 -0.0005

LEU 120 LYS 121 -0.0057

LYS 121 LEU 122 -0.0001

LEU 122 PHE 123 -0.0003

PHE 123 SER 124 0.0001

SER 124 MET 125 0.0010

MET 125 TYR 126 0.0002

TYR 126 ALA 127 -0.0075

ALA 127 PRO 128 0.0002

PRO 128 ALA 129 -0.0029

ALA 129 PHE 130 -0.0003

PHE 130 MET 131 -0.0100

MET 131 MET 132 -0.0006

MET 132 VAL 133 -0.0001

VAL 133 VAL 134 0.0001

VAL 134 ILE 135 -0.0006

ILE 135 SER 136 0.0002

SER 136 LEU 137 -0.0016

LEU 137 ASP 138 0.0003

ASP 138 ARG 139 0.0035

ARG 139 SER 140 -0.0002

SER 140 LEU 141 -0.0101

LEU 141 ALA 142 -0.0002

ALA 142 ILE 143 0.0156

ILE 143 THR 144 -0.0003

THR 144 ARG 145 0.0017

ARG 145 PRO 146 0.0002

PRO 146 LEU 147 0.0040

LEU 147 ALA 148 0.0002

ALA 148 LEU 149 -0.0015

LEU 149 LYS 150 -0.0002

LYS 150 SER 151 0.0038

SER 151 ASN 152 0.0001

ASN 152 SER 153 0.0016

SER 153 LYS 154 -0.0002

LYS 154 VAL 155 -0.0027

VAL 155 GLY 156 -0.0000

GLY 156 GLN 157 -0.0013

GLN 157 SER 158 0.0002

SER 158 MET 159 -0.0038

MET 159 VAL 160 -0.0002

VAL 160 GLY 161 -0.0021

GLY 161 LEU 162 0.0004

LEU 162 ALA 163 0.0007

ALA 163 TRP 164 -0.0001

TRP 164 ILE 165 -0.0089

ILE 165 LEU 166 0.0002

LEU 166 SER 167 0.0026

SER 167 SER 168 0.0004

SER 168 VAL 169 0.0013

VAL 169 PHE 170 0.0000

PHE 170 ALA 171 0.0034

ALA 171 GLY 172 0.0001

GLY 172 PRO 173 -0.0037

PRO 173 GLN 174 0.0003

GLN 174 LEU 175 -0.0015

LEU 175 TYR 176 0.0003

TYR 176 ILE 177 -0.0008

ILE 177 PHE 178 0.0001

PHE 178 ARG 179 0.0227

ARG 179 MET 180 -0.0000

MET 180 ILE 181 0.0096

ILE 181 HIS 182 0.0000

HIS 182 LEU 183 0.0268

LEU 183 ALA 184 0.0001

ALA 184 ASP 185 -0.0114

ASP 185 SER 186 0.0000

SER 186 SER 187 0.0108

SER 187 GLY 188 0.0001

GLY 188 GLN 189 0.0059

GLN 189 THR 190 -0.0001

THR 190 LYS 191 -0.0100

LYS 191 VAL 192 -0.0000

VAL 192 PHE 193 -0.0121

PHE 193 SER 194 0.0001

SER 194 GLN 195 0.0045

GLN 195 CYS 196 -0.0003

CYS 196 VAL 197 0.0077

VAL 197 THR 198 -0.0001

THR 198 HIS 199 -0.0732

HIS 199 CYS 200 0.0001

CYS 200 SER 201 0.0062

SER 201 PHE 202 0.0001

PHE 202 SER 203 0.0020

SER 203 GLN 204 0.0003

GLN 204 TRP 205 0.0027

TRP 205 TRP 206 0.0003

TRP 206 HIS 207 0.0059

HIS 207 GLN 208 0.0001

GLN 208 ALA 209 -0.0211

ALA 209 PHE 210 -0.0001

PHE 210 TYR 211 0.0166

TYR 211 ASN 212 -0.0003

ASN 212 PHE 213 -0.0134

PHE 213 PHE 214 -0.0005

PHE 214 THR 215 0.0088

THR 215 PHE 216 0.0001

PHE 216 SER 217 0.0000

SER 217 CYS 218 -0.0001

CYS 218 LEU 219 -0.0030

LEU 219 PHE 220 -0.0002

PHE 220 ILE 221 0.0026

ILE 221 ILE 222 0.0001

ILE 222 PRO 223 -0.0035

PRO 223 LEU 224 0.0000

LEU 224 PHE 225 0.0058

PHE 225 ILE 226 0.0005

ILE 226 MET 227 0.0027

MET 227 LEU 228 -0.0000

LEU 228 ILE 229 0.0035

ILE 229 CYS 230 0.0001

CYS 230 ASN 231 -0.0006

ASN 231 ALA 232 -0.0000

ALA 232 LYS 233 0.0037

LYS 233 ILE 234 0.0002

ILE 234 ILE 235 0.0061

ILE 235 PHE 236 0.0001

PHE 236 THR 237 0.0052

THR 237 LEU 238 -0.0003

LEU 238 THR 239 0.0199

THR 239 ARG 240 0.0003

ARG 240 VAL 241 -0.0057

VAL 241 LEU 242 -0.0000

LEU 242 HIS 243 0.0072

HIS 243 GLN 244 0.0002

GLN 244 ASP 245 0.0080

ASP 245 PRO 246 -0.0002

PRO 246 HIS 247 -0.0034

HIS 247 GLU 248 -0.0002

GLU 248 LEU 249 0.0012

LEU 249 GLN 250 0.0000

GLN 250 LEU 251 -0.0013

LEU 251 ASN 252 -0.0002

ASN 252 GLN 253 -0.0033

GLN 253 SER 254 0.0002

SER 254 LYS 255 0.0029

LYS 255 ASN 256 0.0001

ASN 256 ASN 257 0.0021

ASN 257 ILE 258 0.0000

ILE 258 PRO 259 -0.0087

PRO 259 ARG 260 0.0001

ARG 260 ALA 261 -0.0035

ALA 261 ARG 262 -0.0003

ARG 262 LEU 263 0.0041

LEU 263 LYS 264 -0.0000

LYS 264 THR 265 -0.0107

THR 265 LEU 266 -0.0002

LEU 266 LYS 267 0.0050

LYS 267 MET 268 -0.0001

MET 268 THR 269 -0.0019

THR 269 VAL 270 -0.0003

VAL 270 ALA 271 0.0005

ALA 271 PHE 272 0.0001

PHE 272 ALA 273 0.0020

ALA 273 THR 274 0.0000

THR 274 SER 275 -0.0010

SER 275 PHE 276 0.0002

PHE 276 THR 277 0.0047

THR 277 VAL 278 -0.0000

VAL 278 CYS 279 -0.0002

CYS 279 TRP 280 0.0004

TRP 280 THR 281 0.0052

THR 281 PRO 282 -0.0002

PRO 282 TYR 283 -0.0016

TYR 283 TYR 284 -0.0003

TYR 284 VAL 285 -0.0018

VAL 285 LEU 286 -0.0004

LEU 286 GLY 287 0.0090

GLY 287 ILE 288 0.0001

ILE 288 TRP 289 -0.0060

TRP 289 TYR 290 -0.0001

TYR 290 TRP 291 0.0255

TRP 291 PHE 292 -0.0002

PHE 292 ASP 293 -0.0001

ASP 293 PRO 294 -0.0001

PRO 294 GLU 295 0.0059

GLU 295 MET 296 0.0001

MET 296 LEU 297 -0.0040

LEU 297 ASN 298 -0.0000

ASN 298 ARG 299 0.0025

ARG 299 LEU 300 -0.0002

LEU 300 SER 301 -0.0047

SER 301 ASP 302 0.0004

ASP 302 PRO 303 0.0017

PRO 303 VAL 304 0.0001

VAL 304 ASN 305 0.0002

ASN 305 HIS 306 0.0003

HIS 306 PHE 307 -0.0108

PHE 307 PHE 308 0.0001

PHE 308 PHE 309 -0.0054

PHE 309 LEU 310 -0.0000

LEU 310 PHE 311 -0.0120

PHE 311 ALA 312 0.0002

ALA 312 PHE 313 -0.0004

PHE 313 LEU 314 -0.0000

LEU 314 ASN 315 -0.0024

ASN 315 PRO 316 -0.0003

PRO 316 CYS 317 0.0008

CYS 317 PHE 318 0.0001

PHE 318 ASP 319 -0.0019

ASP 319 PRO 320 -0.0002

PRO 320 LEU 321 -0.0004

LEU 321 ILE 322 -0.0003

ILE 322 TYR 323 -0.0008

TYR 323 GLY 324 0.0000

GLY 324 TYR 325 -0.0020

TYR 325 PHE 326 0.0002

PHE 326 SER 327 0.0017

SER 327 LEU 328 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 25th, 2023.

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

*** 01-JUN-22 ***

CA strain for 240221025813253280

--- normal mode 10 ---

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

* 01-JUN-22 *