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

* *

CA strain for 240322152211123579

--- 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
GLU 26 MET 27 0.0000

MET 27 THR 28 -0.0278

THR 28 ARG 29 0.0003

ARG 29 ILE 30 -0.0033

ILE 30 GLY 31 -0.0003

GLY 31 VAL 32 0.0043

VAL 32 VAL 33 0.0003

VAL 33 ARG 34 -0.0295

ARG 34 ASN 35 0.0001

ASN 35 PRO 36 -0.0128

PRO 36 LYS 37 -0.0004

LYS 37 SER 38 0.0452

SER 38 HIS 39 -0.0001

HIS 39 GLY 40 -0.0478

GLY 40 ASN 41 -0.0001

ASN 41 ARG 42 0.0069

ARG 42 ILE 43 -0.0002

ILE 43 ARG 44 -0.0125

ARG 44 PRO 45 -0.0000

PRO 45 PRO 46 -0.0003

PRO 46 GLY 47 -0.0000

GLY 47 PRO 48 0.0045

PRO 48 ALA 49 -0.0001

ALA 49 PRO 50 -0.0081

PRO 50 GLU 51 -0.0001

GLU 51 ASP 52 -0.0052

ASP 52 VAL 53 -0.0001

VAL 53 ARG 54 0.0118

ARG 54 LEU 55 -0.0001

LEU 55 VAL 56 -0.0195

VAL 56 GLU 57 -0.0000

GLU 57 PRO 58 -0.0455

PRO 58 ILE 59 -0.0003

ILE 59 GLY 60 -0.0722

GLY 60 ARG 61 -0.0002

ARG 61 GLU 62 0.0300

GLU 62 ALA 63 0.0001

ALA 63 LEU 64 0.0251

LEU 64 LYS 65 -0.0001

LYS 65 ALA 66 0.0189

ALA 66 ALA 67 0.0002

ALA 67 LEU 68 -0.0122

LEU 68 ASP 69 0.0002

ASP 69 ASP 70 0.0026

ASP 70 PHE 71 0.0000

PHE 71 ALA 72 -0.0064

ALA 72 ARG 73 0.0000

ARG 73 THR 74 0.0097

THR 74 GLY 75 -0.0003

GLY 75 LEU 76 -0.0451

LEU 76 ASP 77 0.0001

ASP 77 LEU 78 -0.0186

LEU 78 LEU 79 0.0002

LEU 79 VAL 80 -0.0030

VAL 80 ILE 81 -0.0000

ILE 81 ASP 82 -0.0101

ASP 82 GLY 83 0.0001

GLY 83 GLY 84 0.0285

GLY 84 ASP 85 0.0001

ASP 85 GLY 86 0.0051

GLY 86 THR 87 -0.0004

THR 87 VAL 88 -0.0038

VAL 88 ARG 89 -0.0003

ARG 89 ASP 90 0.0679

ASP 90 VAL 91 0.0003

VAL 91 ILE 92 -0.0050

ILE 92 SER 93 -0.0002

SER 93 LEU 94 0.0463

LEU 94 LEU 95 0.0003

LEU 95 PRO 96 0.0173

PRO 96 HIS 97 0.0000

HIS 97 THR 98 0.0982

THR 98 PHE 99 -0.0003

PHE 99 GLY 100 -0.0549

GLY 100 GLU 101 -0.0001

GLU 101 ALA 102 0.0443

ALA 102 THR 103 0.0001

THR 103 PRO 104 0.0626

PRO 104 LEU 105 -0.0001

LEU 105 LEU 106 0.0233

LEU 106 ALA 107 0.0000

ALA 107 VAL 108 -0.0108

VAL 108 LEU 109 -0.0000

LEU 109 PRO 110 -0.0060

PRO 110 SER 111 0.0000

SER 111 GLY 112 -0.1045

GLY 112 LYS 113 0.0002

LYS 113 THR 114 0.2052

THR 114 ASN 115 0.0001

ASN 115 VAL 116 0.0760

VAL 116 LEU 117 0.0003

LEU 117 ALA 118 -0.0366

ALA 118 ILE 119 -0.0002

ILE 119 ASP 120 0.0569

ASP 120 LEU 121 -0.0003

LEU 121 GLY 122 0.0737

GLY 122 THR 123 0.0006

THR 123 SER 124 0.0351

SER 124 GLU 125 -0.0001

GLU 125 GLY 126 -0.0102

GLY 126 TRP 127 -0.0001

TRP 127 ARG 128 0.0155

ARG 128 LEU 129 -0.0001

LEU 129 GLU 130 -0.0189

GLU 130 ASP 131 -0.0000

ASP 131 ALA 132 0.0109

ALA 132 LEU 133 -0.0004

LEU 133 ARG 134 0.0185

ARG 134 ALA 135 -0.0006

ALA 135 ALA 136 -0.0065

ALA 136 ARG 137 0.0004

ARG 137 ARG 138 0.0469

ARG 138 GLU 139 -0.0001

GLU 139 ASN 140 0.0042

ASN 140 PRO 141 -0.0001

PRO 141 THR 142 -0.0505

THR 142 ILE 143 0.0005

ILE 143 LYS 144 -0.0370

LYS 144 SER 145 -0.0001

SER 145 ARG 146 0.0387

ARG 146 PRO 147 0.0001

PRO 147 PRO 148 0.0001

PRO 148 LEU 149 -0.0002

LEU 149 ARG 150 -0.0223

ARG 150 VAL 151 0.0001

VAL 151 SER 152 0.0051

SER 152 TRP 153 -0.0000

TRP 153 ALA 154 -0.0026

ALA 154 ASP 155 -0.0001

ASP 155 ASP 156 0.0030

ASP 156 LYS 157 -0.0002

LYS 157 PRO 158 0.0785

PRO 158 CYS 159 0.0004

CYS 159 LEU 160 0.0080

LEU 160 GLN 161 0.0002

GLN 161 GLY 162 -0.0100

GLY 162 PHE 163 -0.0004

PHE 163 PHE 164 -0.0833

PHE 164 PHE 165 -0.0003

PHE 165 GLY 166 -0.0941

GLY 166 ILE 167 -0.0002

ILE 167 GLY 168 0.0130

GLY 168 ALA 169 0.0000

ALA 169 PRO 170 -0.0788

PRO 170 VAL 171 -0.0002

VAL 171 LYS 172 0.0604

LYS 172 ALA 173 -0.0001

ALA 173 THR 174 -0.0698

THR 174 ASN 175 -0.0002

ASN 175 LEU 176 0.1220

LEU 176 ALA 177 -0.0002

ALA 177 GLN 178 -0.0601

GLN 178 ARG 179 0.0000

ARG 179 VAL 180 0.0006

VAL 180 HIS 181 0.0003

HIS 181 LYS 182 0.0881

LYS 182 VAL 183 -0.0004

VAL 183 GLY 184 -0.0578

GLY 184 PHE 185 0.0001

PHE 185 PHE 186 0.0736

PHE 186 HIS 187 -0.0000

HIS 187 ASN 188 -0.0202

ASN 188 PHE 189 0.0001

PHE 189 ALA 190 -0.0378

ALA 190 VAL 191 -0.0003

VAL 191 ALA 192 0.0152

ALA 192 LEU 193 -0.0001

LEU 193 THR 194 0.0865

THR 194 ILE 195 -0.0000

ILE 195 GLY 196 0.0196

GLY 196 THR 197 -0.0002

THR 197 ALA 198 0.0573

ALA 198 ALA 199 -0.0001

ALA 199 LEU 200 -0.0069

LEU 200 GLY 201 0.0002

GLY 201 ALA 202 0.0035

ALA 202 LEU 203 -0.0005

LEU 203 PHE 204 -0.0401

PHE 204 GLY 205 0.0003

GLY 205 GLY 206 0.0669

GLY 206 SER 207 -0.0001

SER 207 ARG 208 -0.0112

ARG 208 ASP 209 -0.0001

ASP 209 GLU 210 -0.0509

GLU 210 TRP 211 0.0000

TRP 211 ARG 212 -0.0010

ARG 212 GLU 213 -0.0000

GLU 213 GLY 214 0.0793

GLY 214 VAL 215 0.0001

VAL 215 PRO 216 0.0364

PRO 216 ALA 217 0.0002

ALA 217 ARG 218 0.0333

ARG 218 LEU 219 0.0001

LEU 219 VAL 220 0.0252

VAL 220 LEU 221 -0.0001

LEU 221 ASP 222 -0.0136

ASP 222 GLY 223 0.0003

GLY 223 GLU 224 -0.0018

GLU 224 ALA 225 -0.0002

ALA 225 GLN 226 0.0042

GLN 226 GLY 227 0.0000

GLY 227 GLU 228 0.0108

GLU 228 GLY 229 0.0000

GLY 229 HIS 230 0.0372

HIS 230 ARG 231 -0.0001

ARG 231 PHE 232 0.0209

PHE 232 ALA 233 -0.0000

ALA 233 VAL 234 -0.0579

VAL 234 ILE 235 -0.0001

ILE 235 ALA 236 -0.0591

ALA 236 THR 237 0.0001

THR 237 ALA 238 -0.0675

ALA 238 LEU 239 0.0001

LEU 239 LYS 240 -0.0223

LYS 240 ARG 241 0.0004

ARG 241 LEU 242 0.0236

LEU 242 PRO 243 -0.0002

PRO 243 PHE 244 0.0224

PHE 244 GLY 245 0.0001

GLY 245 LEU 246 -0.0408

LEU 246 LYS 247 0.0000

LYS 247 PRO 248 0.0041

PRO 248 PHE 249 -0.0002

PHE 249 GLY 250 0.0181

GLY 250 ALA 251 0.0000

ALA 251 PRO 252 -0.0657

PRO 252 ARG 253 0.0002

ARG 253 GLU 254 -0.1978

GLU 254 GLY 255 0.0001

GLY 255 LEU 256 0.0662

LEU 256 LYS 257 0.0002

LYS 257 LEU 258 -0.0247

LEU 258 LEU 259 0.0001

LEU 259 ASP 260 -0.0316

ASP 260 VAL 261 -0.0000

VAL 261 ASP 262 -0.0250

ASP 262 ALA 263 0.0002

ALA 263 PRO 264 0.0427

PRO 264 PRO 265 -0.0002

PRO 265 ARG 266 0.0462

ARG 266 ARG 267 -0.0004

ARG 267 LEU 268 0.0180

LEU 268 HIS 269 -0.0003

HIS 269 LYS 270 0.0078

LYS 270 ALA 271 0.0002

ALA 271 LEU 272 0.0042

LEU 272 PRO 273 0.0004

PRO 273 LEU 274 -0.0305

LEU 274 MET 275 0.0002

MET 275 LEU 276 -0.0087

LEU 276 SER 277 0.0000

SER 277 GLY 278 -0.0164

GLY 278 LYS 279 0.0005

LYS 279 VAL 280 0.0477

VAL 280 VAL 281 0.0001

VAL 281 PRO 282 0.0068

PRO 282 ALA 283 -0.0002

ALA 283 LEU 284 -0.0122

LEU 284 GLU 285 -0.0001

GLU 285 GLY 286 0.0003

GLY 286 LEU 287 0.0002

LEU 287 GLY 288 0.0051

GLY 288 TYR 289 -0.0003

TYR 289 ARG 290 -0.0558

ARG 290 ARG 291 0.0002

ARG 291 ARG 292 -0.0692

ARG 292 ASP 293 -0.0002

ASP 293 PRO 294 0.0008

PRO 294 ARG 295 0.0001

ARG 295 SER 296 -0.0004

SER 296 VAL 297 -0.0001

VAL 297 LYS 298 0.0137

LYS 298 LEU 299 -0.0001

LEU 299 SER 300 0.0094

SER 300 GLY 301 0.0003

GLY 301 GLY 302 -0.0809

GLY 302 ALA 303 -0.0002

ALA 303 PRO 304 -0.0603

PRO 304 PHE 305 0.0002

PHE 305 VAL 306 -0.0744

VAL 306 LEU 307 0.0001

LEU 307 ASP 308 -0.0841

ASP 308 GLY 309 0.0001

GLY 309 GLU 310 -0.0757

GLU 310 VAL 311 -0.0002

VAL 311 TYR 312 -0.0218

TYR 312 GLU 313 0.0001

GLU 313 GLY 314 -0.0949

GLY 314 GLY 315 0.0000

GLY 315 ASP 316 -0.0634

ASP 316 LEU 317 -0.0003

LEU 317 THR 318 0.0330

THR 318 ILE 319 0.0002

ILE 319 GLN 320 0.0516

GLN 320 LEU 321 0.0000

LEU 321 GLY 322 -0.0805

GLY 322 PRO 323 -0.0003

PRO 323 ALA 324 0.1191

ALA 324 LEU 325 0.0000

LEU 325 ARG 326 0.1298

ARG 326 PHE 327 0.0000

PHE 327 LEU 328 0.0582

LEU 328 VAL 329 0.0003

VAL 329 GLY 330 0.0268

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 240322152211123579

--- normal mode 8 ---

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

* *