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

* *

CA strain for 22123114225973881

--- normal mode 8 ---

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
PHE 1 ASP 2 0.0003

ASP 2 MET 3 -0.0048

MET 3 ILE 4 0.0002

ILE 4 ARG 5 0.0013

ARG 5 LEU 6 -0.0001

LEU 6 ALA 7 -0.0054

ALA 7 THR 8 -0.0001

THR 8 ASN 9 -0.0030

ASN 9 LYS 10 0.0001

LYS 10 PHE 11 0.0034

PHE 11 SER 12 -0.0003

SER 12 GLU 13 0.0025

GLU 13 ASP 14 -0.0002

ASP 14 ASN 15 -0.0021

ASN 15 LYS 16 -0.0004

LYS 16 ILE 17 -0.0131

ILE 17 GLY 18 0.0000

GLY 18 GLU 19 0.0150

GLU 19 GLY 20 0.0002

GLY 20 GLY 21 0.0616

GLY 21 PHE 22 -0.0000

PHE 22 GLY 23 0.0302

GLY 23 ASP 24 -0.0001

ASP 24 VAL 25 0.0065

VAL 25 TYR 26 -0.0004

TYR 26 LYS 27 0.0077

LYS 27 GLY 28 0.0001

GLY 28 MET 29 0.0113

MET 29 PHE 30 -0.0000

PHE 30 PRO 31 0.0014

PRO 31 ASN 32 -0.0001

ASN 32 GLY 33 0.0005

GLY 33 TYR 34 -0.0005

TYR 34 GLU 35 0.0018

GLU 35 ILE 36 -0.0001

ILE 36 ALA 37 0.0058

ALA 37 VAL 38 0.0002

VAL 38 LYS 39 0.0132

LYS 39 ARG 40 -0.0000

ARG 40 LEU 41 0.0105

LEU 41 ILE 42 -0.0001

ILE 42 ARG 43 0.0021

ARG 43 ASN 44 0.0003

ASN 44 SER 45 0.0211

SER 45 SER 46 -0.0003

SER 46 GLN 47 -0.0060

GLN 47 GLY 48 -0.0000

GLY 48 ALA 49 -0.0168

ALA 49 VAL 50 -0.0000

VAL 50 GLU 51 -0.0024

GLU 51 PHE 52 -0.0004

PHE 52 LYS 53 0.0016

LYS 53 ASN 54 -0.0001

ASN 54 GLU 55 0.0032

GLU 55 VAL 56 -0.0004

VAL 56 LEU 57 0.0006

LEU 57 LEU 58 -0.0000

LEU 58 ILE 59 0.0019

ILE 59 ALA 60 0.0002

ALA 60 LYS 61 -0.0069

LYS 61 LEU 62 -0.0004

LEU 62 GLN 63 0.0018

GLN 63 HIS 64 -0.0002

HIS 64 ARG 65 -0.0019

ARG 65 ASN 66 0.0002

ASN 66 LEU 67 0.0002

LEU 67 VAL 68 -0.0001

VAL 68 ARG 69 0.0012

ARG 69 LEU 70 -0.0003

LEU 70 LEU 71 0.0003

LEU 71 GLY 72 0.0004

GLY 72 PHE 73 -0.0089

PHE 73 CYS 74 0.0002

CYS 74 ILE 75 -0.0071

ILE 75 GLN 76 0.0000

GLN 76 ARG 77 0.0000

ARG 77 ASN 78 -0.0003

ASN 78 GLU 79 0.0010

GLU 79 LYS 80 -0.0002

LYS 80 ILE 81 -0.0084

ILE 81 LEU 82 0.0001

LEU 82 ILE 83 -0.0023

ILE 83 TYR 84 0.0000

TYR 84 GLU 85 -0.0002

GLU 85 TYR 86 0.0001

TYR 86 MET 87 -0.0129

MET 87 HIS 88 0.0002

HIS 88 ASN 89 -0.0063

ASN 89 LYS 90 -0.0002

LYS 90 SER 91 0.0119

SER 91 LEU 92 0.0001

LEU 92 ASP 93 -0.0041

ASP 93 TYR 94 0.0002

TYR 94 TYR 95 0.0003

TYR 95 LEU 96 -0.0003

LEU 96 PHE 97 0.0003

PHE 97 SER 98 0.0001

SER 98 PRO 99 0.0016

PRO 99 GLU 100 -0.0000

GLU 100 ASN 101 -0.0029

ASN 101 HIS 102 0.0002

HIS 102 ARG 103 0.0043

ARG 103 LYS 104 -0.0000

LYS 104 LEU 105 0.0004

LEU 105 THR 106 0.0005

THR 106 TRP 107 -0.0072

TRP 107 HIS 108 0.0000

HIS 108 ALA 109 -0.0068

ALA 109 ARG 110 -0.0002

ARG 110 TYR 111 -0.0013

TYR 111 LYS 112 -0.0000

LYS 112 ILE 113 0.0042

ILE 113 ILE 114 0.0004

ILE 114 ARG 115 0.0041

ARG 115 GLY 116 -0.0003

GLY 116 ILE 117 0.0015

ILE 117 ALA 118 0.0001

ALA 118 ARG 119 0.0012

ARG 119 GLY 120 -0.0000

GLY 120 ILE 121 -0.0054

ILE 121 LEU 122 -0.0001

LEU 122 TYR 123 0.0070

TYR 123 LEU 124 -0.0001

LEU 124 HIS 125 -0.0047

HIS 125 GLU 126 -0.0002

GLU 126 ASP 127 -0.0024

ASP 127 SER 128 -0.0001

SER 128 HIS 129 -0.0020

HIS 129 LEU 130 0.0002

LEU 130 LYS 131 -0.0047

LYS 131 ILE 132 -0.0001

ILE 132 ILE 133 -0.0088

ILE 133 HIS 134 -0.0004

HIS 134 CYS 135 0.0072

CYS 135 ASP 136 -0.0003

ASP 136 LEU 137 0.0149

LEU 137 LYS 138 -0.0002

LYS 138 PRO 139 0.0104

PRO 139 SER 140 0.0000

SER 140 ASN 141 -0.0091

ASN 141 ILE 142 -0.0001

ILE 142 LEU 143 0.0117

LEU 143 LEU 144 -0.0002

LEU 144 ASP 145 0.0113

ASP 145 ASP 146 0.0003

ASP 146 LYS 147 -0.0130

LYS 147 MET 148 -0.0003

MET 148 ASN 149 0.0008

ASN 149 ALA 150 0.0003

ALA 150 LYS 151 -0.0004

LYS 151 ILE 152 -0.0006

ILE 152 SER 153 0.0066

SER 153 ASP 154 0.0002

ASP 154 PHE 155 -0.0150

PHE 155 GLY 156 -0.0003

GLY 156 LEU 157 0.0295

LEU 157 ALA 158 0.0000

ALA 158 ARG 159 0.0050

ARG 159 ILE 160 -0.0001

ILE 160 VAL 161 0.0119

VAL 161 ALA 162 0.0000

ALA 162 ILE 163 0.0084

ILE 163 ASP 164 -0.0004

ASP 164 GLN 165 -0.0089

GLN 165 MET 166 0.0004

MET 166 GLN 167 -0.0401

GLN 167 GLY 168 0.0001

GLY 168 ASN 169 -0.0289

ASN 169 THR 170 -0.0004

THR 170 SER 171 0.0352

SER 171 ILE 172 0.0005

ILE 172 ILE 173 -0.0241

ILE 173 ALA 174 -0.0000

ALA 174 GLY 175 0.0519

GLY 175 THR 176 0.0002

THR 176 TYR 177 -0.0338

TYR 177 GLY 178 -0.0001

GLY 178 TYR 179 0.0503

TYR 179 MET 180 -0.0003

MET 180 SER 181 -0.0208

SER 181 PRO 182 -0.0002

PRO 182 GLU 183 0.0230

GLU 183 TYR 184 -0.0003

TYR 184 ALA 185 -0.0153

ALA 185 MET 186 -0.0003

MET 186 LEU 187 -0.0011

LEU 187 GLY 188 0.0001

GLY 188 GLN 189 -0.0203

GLN 189 PHE 190 -0.0002

PHE 190 SER 191 -0.0298

SER 191 VAL 192 -0.0003

VAL 192 LYS 193 0.0201

LYS 193 SER 194 0.0001

SER 194 ASP 195 -0.0189

ASP 195 VAL 196 0.0000

VAL 196 PHE 197 0.0011

PHE 197 SER 198 0.0002

SER 198 PHE 199 0.0001

PHE 199 GLY 200 -0.0002

GLY 200 VAL 201 0.0089

VAL 201 ILE 202 -0.0001

ILE 202 MET 203 0.0105

MET 203 LEU 204 0.0003

LEU 204 GLU 205 -0.0032

GLU 205 ILE 206 -0.0001

ILE 206 VAL 207 0.0001

VAL 207 SER 208 -0.0001

SER 208 GLY 209 -0.0045

GLY 209 LYS 210 0.0000

LYS 210 ARG 211 0.0205

ARG 211 ASN 212 0.0000

ASN 212 VAL 213 0.0202

VAL 213 ASP 214 0.0003

ASP 214 TYR 215 -0.0050

TYR 215 ASN 216 -0.0001

ASN 216 GLY 217 0.0074

GLY 217 VAL 218 -0.0000

VAL 218 ASN 219 0.0007

ASN 219 SER 220 0.0004

SER 220 ILE 221 0.0123

ILE 221 ASP 222 0.0002

ASP 222 ASP 223 -0.0113

ASP 223 LEU 224 -0.0003

LEU 224 VAL 225 -0.0025

VAL 225 SER 226 -0.0002

SER 226 HIS 227 -0.0015

HIS 227 ALA 228 -0.0001

ALA 228 TRP 229 -0.0035

TRP 229 LYS 230 0.0001

LYS 230 LYS 231 -0.0029

LYS 231 TRP 232 -0.0001

TRP 232 THR 233 0.0011

THR 233 GLU 234 -0.0002

GLU 234 ASN 235 -0.0007

ASN 235 LYS 236 0.0003

LYS 236 GLN 237 0.0003

GLN 237 MET 238 0.0001

MET 238 GLU 239 0.0078

GLU 239 LEU 240 -0.0001

LEU 240 LEU 241 -0.0027

LEU 241 ASP 242 -0.0000

ASP 242 PRO 243 0.0004

PRO 243 ALA 244 -0.0002

ALA 244 LEU 245 -0.0043

LEU 245 THR 246 -0.0000

THR 246 TYR 247 0.0040

TYR 247 SER 248 -0.0001

SER 248 PHE 249 -0.0052

PHE 249 SER 250 0.0002

SER 250 GLU 251 -0.0011

GLU 251 THR 252 -0.0002

THR 252 GLU 253 0.0007

GLU 253 VAL 254 -0.0002

VAL 254 SER 255 -0.0027

SER 255 ARG 256 0.0000

ARG 256 CYS 257 0.0034

CYS 257 ILE 258 0.0001

ILE 258 GLN 259 -0.0006

GLN 259 LEU 260 0.0001

LEU 260 GLY 261 0.0052

GLY 261 LEU 262 -0.0002

LEU 262 LEU 263 0.0043

LEU 263 CYS 264 -0.0003

CYS 264 VAL 265 -0.0012

VAL 265 GLN 266 0.0000

GLN 266 GLU 267 -0.0185

GLU 267 ASN 268 -0.0001

ASN 268 PRO 269 0.0129

PRO 269 ASP 270 -0.0001

ASP 270 GLN 271 -0.0089

GLN 271 ARG 272 -0.0000

ARG 272 PRO 273 -0.0204

PRO 273 THR 274 -0.0002

THR 274 MET 275 -0.0028

MET 275 ALA 276 -0.0001

ALA 276 THR 277 0.0103

THR 277 ILE 278 -0.0002

ILE 278 ALA 279 -0.0037

ALA 279 LEU 280 0.0003

LEU 280 TYR 281 0.0052

TYR 281 PHE 282 -0.0002

PHE 282 ASN 283 0.0032

ASN 283 ILE 284 -0.0002

ILE 284 ASP 285 0.0005

ASP 285 SER 286 0.0001

SER 286 ILE 287 -0.0022

ILE 287 ASP 288 -0.0002

ASP 288 LEU 289 -0.0051

LEU 289 PRO 290 0.0001

PRO 290 LEU 291 0.0048

LEU 291 PRO 292 -0.0000

PRO 292 GLN 293 -0.0071

GLN 293 GLN 294 0.0000

GLN 294 PRO 295 -0.0030

PRO 295 PRO 296 0.0002

PRO 296 PHE 297 0.0148

PHE 297 TYR 298 0.0000

TYR 298 MET 299 0.0237

MET 299 ARG 300 -0.0001

ARG 300 GLY 301 -0.0052

GLY 301 LYS 302 -0.0000

LYS 302 ILE 303 0.0307

ILE 303 GLU 304 -0.0001

GLU 304 SER 305 0.0864

SER 305 LYS 306 -0.0001

LYS 306 VAL 307 -0.0193

VAL 307 ALA 308 -0.0003

ALA 308 SER 309 0.0516

SER 309 LYS 310 0.0000

LYS 310 LYS 311 -0.2695

LYS 311 THR 312 -0.0001

THR 312 MET 313 0.0389

MET 313 SER 314 -0.0004

SER 314 GLY 315 0.0554

GLY 315 ARG 316 0.0000

ARG 316 PRO 317 -0.0758

PRO 317 ARG 318 -0.0000

ARG 318 SER 319 -0.1323

SER 319 TYR 320 -0.0001

TYR 320 SER 321 -0.1138

SER 321 VAL 322 0.0001

VAL 322 THR 323 0.0112

THR 323 ARG 324 -0.0000

ARG 324 PHE 325 0.0535

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: October 18th, 2018.

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

*** ***

CA strain for 22123114225973881

--- normal mode 8 ---

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

* *