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

* 01-JUN-22 *

CA strain for 240221025813253280

--- normal mode 11 ---

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 0.0002

ALA 2 ASN 3 -0.0102

ASN 3 SER 4 0.0003

SER 4 ALA 5 -0.1069

ALA 5 SER 6 -0.0009

SER 6 PRO 7 0.0396

PRO 7 GLU 8 -0.0002

GLU 8 GLN 9 0.1085

GLN 9 ASN 10 -0.0002

ASN 10 GLN 11 0.0436

GLN 11 ASN 12 -0.0000

ASN 12 HIS 13 0.0422

HIS 13 CYS 14 -0.0000

CYS 14 SER 15 0.0772

SER 15 ALA 16 0.0000

ALA 16 ILE 17 -0.0330

ILE 17 ASN 18 -0.0000

ASN 18 ASN 19 -0.0235

ASN 19 SER 20 0.0000

SER 20 ILE 21 0.0181

ILE 21 PRO 22 -0.0000

PRO 22 LEU 23 0.0240

LEU 23 MET 24 0.0000

MET 24 GLN 25 0.0191

GLN 25 GLY 26 -0.0004

GLY 26 ASN 27 0.0219

ASN 27 LEU 28 0.0002

LEU 28 PRO 29 -0.0610

PRO 29 THR 30 -0.0000

THR 30 LEU 31 0.0126

LEU 31 THR 32 0.0000

THR 32 LEU 33 -0.0210

LEU 33 SER 34 0.0000

SER 34 GLY 35 0.0048

GLY 35 LYS 36 -0.0000

LYS 36 ILE 37 0.0047

ILE 37 ARG 38 -0.0001

ARG 38 VAL 39 0.0054

VAL 39 THR 40 -0.0001

THR 40 VAL 41 0.0056

VAL 41 THR 42 0.0001

THR 42 PHE 43 0.0014

PHE 43 PHE 44 -0.0001

PHE 44 LEU 45 0.0039

LEU 45 PHE 46 0.0001

PHE 46 LEU 47 0.0013

LEU 47 LEU 48 0.0004

LEU 48 SER 49 -0.0014

SER 49 ALA 50 -0.0001

ALA 50 THR 51 -0.0032

THR 51 PHE 52 -0.0002

PHE 52 ASN 53 -0.0027

ASN 53 ALA 54 0.0001

ALA 54 SER 55 -0.0025

SER 55 PHE 56 0.0003

PHE 56 LEU 57 -0.0014

LEU 57 LEU 58 -0.0003

LEU 58 LYS 59 -0.0012

LYS 59 LEU 60 -0.0001

LEU 60 GLN 61 0.0011

GLN 61 LYS 62 -0.0001

LYS 62 TRP 63 -0.0021

TRP 63 THR 64 0.0002

THR 64 GLN 65 0.0024

GLN 65 LYS 66 0.0001

LYS 66 LYS 67 -0.0001

LYS 67 GLU 68 -0.0002

GLU 68 LYS 69 0.0061

LYS 69 GLY 70 0.0003

GLY 70 LYS 71 -0.0046

LYS 71 LYS 72 0.0003

LYS 72 LEU 73 -0.0051

LEU 73 SER 74 0.0002

SER 74 ARG 75 -0.0096

ARG 75 MET 76 -0.0004

MET 76 LYS 77 0.0028

LYS 77 LEU 78 -0.0000

LEU 78 LEU 79 -0.0101

LEU 79 LEU 80 -0.0001

LEU 80 LYS 81 0.0042

LYS 81 HIS 82 0.0003

HIS 82 LEU 83 -0.0040

LEU 83 THR 84 -0.0002

THR 84 LEU 85 -0.0041

LEU 85 ALA 86 0.0004

ALA 86 ASN 87 -0.0006

ASN 87 LEU 88 -0.0001

LEU 88 LEU 89 -0.0069

LEU 89 GLU 90 0.0001

GLU 90 THR 91 -0.0039

THR 91 LEU 92 -0.0002

LEU 92 ILE 93 -0.0016

ILE 93 VAL 94 0.0002

VAL 94 MET 95 0.0015

MET 95 PRO 96 0.0002

PRO 96 LEU 97 0.0002

LEU 97 ASP 98 -0.0002

ASP 98 GLY 99 0.0016

GLY 99 MET 100 0.0005

MET 100 TRP 101 0.0050

TRP 101 ASN 102 0.0000

ASN 102 ILE 103 -0.0125

ILE 103 THR 104 -0.0001

THR 104 VAL 105 0.0141

VAL 105 GLN 106 -0.0001

GLN 106 TRP 107 0.0089

TRP 107 TYR 108 -0.0000

TYR 108 ALA 109 0.0100

ALA 109 GLY 110 0.0002

GLY 110 GLU 111 -0.0210

GLU 111 LEU 112 0.0000

LEU 112 LEU 113 -0.0024

LEU 113 CYS 114 0.0002

CYS 114 LYS 115 0.0075

LYS 115 VAL 116 -0.0000

VAL 116 LEU 117 -0.0155

LEU 117 SER 118 0.0001

SER 118 TYR 119 0.0139

TYR 119 LEU 120 -0.0002

LEU 120 LYS 121 -0.0108

LYS 121 LEU 122 0.0002

LEU 122 PHE 123 0.0043

PHE 123 SER 124 -0.0003

SER 124 MET 125 0.0009

MET 125 TYR 126 -0.0002

TYR 126 ALA 127 -0.0104

ALA 127 PRO 128 -0.0001

PRO 128 ALA 129 -0.0035

ALA 129 PHE 130 -0.0004

PHE 130 MET 131 -0.0113

MET 131 MET 132 -0.0004

MET 132 VAL 133 -0.0024

VAL 133 VAL 134 -0.0003

VAL 134 ILE 135 0.0003

ILE 135 SER 136 -0.0000

SER 136 LEU 137 -0.0062

LEU 137 ASP 138 0.0000

ASP 138 ARG 139 0.0088

ARG 139 SER 140 0.0001

SER 140 LEU 141 -0.0241

LEU 141 ALA 142 0.0000

ALA 142 ILE 143 0.0367

ILE 143 THR 144 -0.0002

THR 144 ARG 145 0.0023

ARG 145 PRO 146 -0.0001

PRO 146 LEU 147 0.0098

LEU 147 ALA 148 0.0003

ALA 148 LEU 149 -0.0044

LEU 149 LYS 150 0.0002

LYS 150 SER 151 0.0100

SER 151 ASN 152 0.0000

ASN 152 SER 153 0.0009

SER 153 LYS 154 -0.0002

LYS 154 VAL 155 -0.0092

VAL 155 GLY 156 0.0004

GLY 156 GLN 157 -0.0037

GLN 157 SER 158 -0.0001

SER 158 MET 159 -0.0113

MET 159 VAL 160 -0.0001

VAL 160 GLY 161 -0.0054

GLY 161 LEU 162 -0.0002

LEU 162 ALA 163 -0.0033

ALA 163 TRP 164 0.0000

TRP 164 ILE 165 -0.0181

ILE 165 LEU 166 -0.0001

LEU 166 SER 167 0.0038

SER 167 SER 168 -0.0000

SER 168 VAL 169 -0.0034

VAL 169 PHE 170 0.0001

PHE 170 ALA 171 0.0022

ALA 171 GLY 172 0.0000

GLY 172 PRO 173 -0.0046

PRO 173 GLN 174 -0.0002

GLN 174 LEU 175 -0.0046

LEU 175 TYR 176 0.0000

TYR 176 ILE 177 -0.0043

ILE 177 PHE 178 -0.0003

PHE 178 ARG 179 0.0118

ARG 179 MET 180 0.0004

MET 180 ILE 181 0.0101

ILE 181 HIS 182 -0.0001

HIS 182 LEU 183 0.0158

LEU 183 ALA 184 0.0000

ALA 184 ASP 185 0.0006

ASP 185 SER 186 -0.0001

SER 186 SER 187 0.0120

SER 187 GLY 188 -0.0001

GLY 188 GLN 189 0.0044

GLN 189 THR 190 0.0003

THR 190 LYS 191 -0.0140

LYS 191 VAL 192 0.0002

VAL 192 PHE 193 -0.0093

PHE 193 SER 194 -0.0001

SER 194 GLN 195 0.0059

GLN 195 CYS 196 0.0003

CYS 196 VAL 197 0.0262

VAL 197 THR 198 0.0003

THR 198 HIS 199 0.0200

HIS 199 CYS 200 -0.0002

CYS 200 SER 201 -0.0261

SER 201 PHE 202 0.0002

PHE 202 SER 203 -0.0042

SER 203 GLN 204 -0.0000

GLN 204 TRP 205 0.0001

TRP 205 TRP 206 -0.0000

TRP 206 HIS 207 0.0064

HIS 207 GLN 208 -0.0000

GLN 208 ALA 209 -0.0243

ALA 209 PHE 210 -0.0002

PHE 210 TYR 211 0.0086

TYR 211 ASN 212 0.0005

ASN 212 PHE 213 -0.0110

PHE 213 PHE 214 0.0002

PHE 214 THR 215 0.0086

THR 215 PHE 216 0.0000

PHE 216 SER 217 0.0005

SER 217 CYS 218 -0.0001

CYS 218 LEU 219 -0.0018

LEU 219 PHE 220 -0.0001

PHE 220 ILE 221 0.0029

ILE 221 ILE 222 -0.0001

ILE 222 PRO 223 -0.0060

PRO 223 LEU 224 0.0004

LEU 224 PHE 225 0.0043

PHE 225 ILE 226 -0.0001

ILE 226 MET 227 0.0035

MET 227 LEU 228 -0.0004

LEU 228 ILE 229 0.0013

ILE 229 CYS 230 -0.0001

CYS 230 ASN 231 -0.0033

ASN 231 ALA 232 -0.0001

ALA 232 LYS 233 0.0019

LYS 233 ILE 234 0.0002

ILE 234 ILE 235 0.0093

ILE 235 PHE 236 0.0002

PHE 236 THR 237 0.0037

THR 237 LEU 238 -0.0001

LEU 238 THR 239 0.0395

THR 239 ARG 240 -0.0001

ARG 240 VAL 241 -0.0151

VAL 241 LEU 242 0.0002

LEU 242 HIS 243 0.0100

HIS 243 GLN 244 0.0004

GLN 244 ASP 245 0.0255

ASP 245 PRO 246 0.0001

PRO 246 HIS 247 -0.0081

HIS 247 GLU 248 0.0002

GLU 248 LEU 249 0.0010

LEU 249 GLN 250 -0.0000

GLN 250 LEU 251 -0.0016

LEU 251 ASN 252 0.0004

ASN 252 GLN 253 -0.0076

GLN 253 SER 254 -0.0002

SER 254 LYS 255 0.0081

LYS 255 ASN 256 0.0003

ASN 256 ASN 257 0.0038

ASN 257 ILE 258 -0.0000

ILE 258 PRO 259 -0.0237

PRO 259 ARG 260 0.0002

ARG 260 ALA 261 -0.0176

ALA 261 ARG 262 -0.0000

ARG 262 LEU 263 0.0166

LEU 263 LYS 264 0.0004

LYS 264 THR 265 -0.0215

THR 265 LEU 266 0.0001

LEU 266 LYS 267 0.0075

LYS 267 MET 268 -0.0000

MET 268 THR 269 -0.0019

THR 269 VAL 270 -0.0001

VAL 270 ALA 271 -0.0045

ALA 271 PHE 272 -0.0004

PHE 272 ALA 273 0.0091

ALA 273 THR 274 -0.0000

THR 274 SER 275 -0.0107

SER 275 PHE 276 -0.0001

PHE 276 THR 277 0.0094

THR 277 VAL 278 0.0001

VAL 278 CYS 279 -0.0056

CYS 279 TRP 280 -0.0000

TRP 280 THR 281 0.0119

THR 281 PRO 282 0.0002

PRO 282 TYR 283 -0.0069

TYR 283 TYR 284 0.0001

TYR 284 VAL 285 0.0062

VAL 285 LEU 286 0.0001

LEU 286 GLY 287 0.0120

GLY 287 ILE 288 0.0002

ILE 288 TRP 289 -0.0008

TRP 289 TYR 290 0.0002

TYR 290 TRP 291 0.0312

TRP 291 PHE 292 -0.0000

PHE 292 ASP 293 -0.0267

ASP 293 PRO 294 0.0002

PRO 294 GLU 295 -0.0402

GLU 295 MET 296 -0.0001

MET 296 LEU 297 -0.0054

LEU 297 ASN 298 0.0001

ASN 298 ARG 299 0.0060

ARG 299 LEU 300 -0.0001

LEU 300 SER 301 -0.0344

SER 301 ASP 302 -0.0000

ASP 302 PRO 303 0.0122

PRO 303 VAL 304 -0.0003

VAL 304 ASN 305 -0.0105

ASN 305 HIS 306 0.0001

HIS 306 PHE 307 -0.0259

PHE 307 PHE 308 0.0003

PHE 308 PHE 309 -0.0118

PHE 309 LEU 310 -0.0000

LEU 310 PHE 311 -0.0278

PHE 311 ALA 312 -0.0000

ALA 312 PHE 313 0.0027

PHE 313 LEU 314 -0.0003

LEU 314 ASN 315 -0.0042

ASN 315 PRO 316 -0.0002

PRO 316 CYS 317 0.0016

CYS 317 PHE 318 0.0001

PHE 318 ASP 319 -0.0026

ASP 319 PRO 320 -0.0002

PRO 320 LEU 321 0.0002

LEU 321 ILE 322 -0.0002

ILE 322 TYR 323 0.0003

TYR 323 GLY 324 -0.0001

GLY 324 TYR 325 -0.0112

TYR 325 PHE 326 -0.0001

PHE 326 SER 327 0.0110

SER 327 LEU 328 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.

*** 01-JUN-22 ***

CA strain for 240221025813253280

--- normal mode 11 ---

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

* 01-JUN-22 *