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

* *

CA strain for 230101190352136506

--- normal mode 17 ---

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 -0.0002

ASP 2 MET 3 0.0572

MET 3 ILE 4 -0.0002

ILE 4 ARG 5 -0.0010

ARG 5 LEU 6 -0.0001

LEU 6 ALA 7 0.0176

ALA 7 THR 8 0.0000

THR 8 ASN 9 0.0175

ASN 9 LYS 10 0.0000

LYS 10 PHE 11 0.0107

PHE 11 SER 12 -0.0002

SER 12 GLU 13 -0.0286

GLU 13 ASP 14 -0.0005

ASP 14 ASN 15 0.0252

ASN 15 LYS 16 0.0003

LYS 16 ILE 17 0.0951

ILE 17 GLY 18 -0.0001

GLY 18 GLU 19 0.0241

GLU 19 GLY 20 0.0000

GLY 20 GLY 21 -0.0101

GLY 21 PHE 22 -0.0002

PHE 22 GLY 23 0.0081

GLY 23 ASP 24 -0.0002

ASP 24 VAL 25 -0.0257

VAL 25 TYR 26 -0.0002

TYR 26 LYS 27 -0.0444

LYS 27 GLY 28 -0.0000

GLY 28 MET 29 -0.0620

MET 29 PHE 30 0.0001

PHE 30 PRO 31 -0.0013

PRO 31 ASN 32 -0.0001

ASN 32 GLY 33 -0.0443

GLY 33 TYR 34 -0.0000

TYR 34 GLU 35 -0.0311

GLU 35 ILE 36 0.0002

ILE 36 ALA 37 -0.0166

ALA 37 VAL 38 0.0001

VAL 38 LYS 39 -0.0048

LYS 39 ARG 40 0.0001

ARG 40 LEU 41 0.0252

LEU 41 ILE 42 -0.0001

ILE 42 ARG 43 -0.0926

ARG 43 ASN 44 -0.0003

ASN 44 SER 45 -0.1390

SER 45 SER 46 -0.0002

SER 46 GLN 47 -0.0484

GLN 47 GLY 48 0.0002

GLY 48 ALA 49 0.0396

ALA 49 VAL 50 0.0001

VAL 50 GLU 51 0.0368

GLU 51 PHE 52 0.0001

PHE 52 LYS 53 -0.0139

LYS 53 ASN 54 0.0004

ASN 54 GLU 55 0.0150

GLU 55 VAL 56 -0.0003

VAL 56 LEU 57 -0.0112

LEU 57 LEU 58 0.0003

LEU 58 ILE 59 0.0186

ILE 59 ALA 60 0.0003

ALA 60 LYS 61 0.0138

LYS 61 LEU 62 -0.0004

LEU 62 GLN 63 -0.0164

GLN 63 HIS 64 0.0000

HIS 64 ARG 65 -0.0645

ARG 65 ASN 66 0.0001

ASN 66 LEU 67 0.0010

LEU 67 VAL 68 0.0002

VAL 68 ARG 69 -0.0143

ARG 69 LEU 70 0.0001

LEU 70 LEU 71 0.0405

LEU 71 GLY 72 0.0003

GLY 72 PHE 73 0.0313

PHE 73 CYS 74 -0.0000

CYS 74 ILE 75 0.0252

ILE 75 GLN 76 -0.0004

GLN 76 ARG 77 0.0047

ARG 77 ASN 78 0.0004

ASN 78 GLU 79 -0.0592

GLU 79 LYS 80 0.0002

LYS 80 ILE 81 0.0336

ILE 81 LEU 82 0.0001

LEU 82 ILE 83 0.0121

ILE 83 TYR 84 -0.0000

TYR 84 GLU 85 -0.0440

GLU 85 TYR 86 0.0000

TYR 86 MET 87 0.0091

MET 87 HIS 88 -0.0001

HIS 88 ASN 89 -0.0497

ASN 89 LYS 90 0.0001

LYS 90 SER 91 -0.0137

SER 91 LEU 92 0.0000

LEU 92 ASP 93 -0.0350

ASP 93 TYR 94 0.0000

TYR 94 TYR 95 0.0236

TYR 95 LEU 96 0.0004

LEU 96 PHE 97 -0.0124

PHE 97 SER 98 -0.0001

SER 98 PRO 99 0.0146

PRO 99 GLU 100 -0.0001

GLU 100 ASN 101 -0.0146

ASN 101 HIS 102 -0.0004

HIS 102 ARG 103 0.0256

ARG 103 LYS 104 0.0004

LYS 104 LEU 105 -0.0090

LEU 105 THR 106 -0.0003

THR 106 TRP 107 0.0294

TRP 107 HIS 108 0.0002

HIS 108 ALA 109 0.0206

ALA 109 ARG 110 0.0002

ARG 110 TYR 111 0.0155

TYR 111 LYS 112 0.0001

LYS 112 ILE 113 0.0016

ILE 113 ILE 114 0.0001

ILE 114 ARG 115 -0.0062

ARG 115 GLY 116 -0.0000

GLY 116 ILE 117 0.0233

ILE 117 ALA 118 -0.0000

ALA 118 ARG 119 0.0304

ARG 119 GLY 120 -0.0002

GLY 120 ILE 121 0.0137

ILE 121 LEU 122 0.0000

LEU 122 TYR 123 0.0172

TYR 123 LEU 124 0.0001

LEU 124 HIS 125 0.0192

HIS 125 GLU 126 -0.0002

GLU 126 ASP 127 0.0163

ASP 127 SER 128 -0.0004

SER 128 HIS 129 -0.0123

HIS 129 LEU 130 0.0003

LEU 130 LYS 131 0.0078

LYS 131 ILE 132 0.0003

ILE 132 ILE 133 0.0501

ILE 133 HIS 134 0.0002

HIS 134 CYS 135 0.0529

CYS 135 ASP 136 0.0001

ASP 136 LEU 137 0.0081

LEU 137 LYS 138 -0.0003

LYS 138 PRO 139 0.0351

PRO 139 SER 140 0.0001

SER 140 ASN 141 0.0169

ASN 141 ILE 142 0.0000

ILE 142 LEU 143 0.0218

LEU 143 LEU 144 -0.0001

LEU 144 ASP 145 -0.0309

ASP 145 ASP 146 -0.0003

ASP 146 LYS 147 0.0599

LYS 147 MET 148 -0.0003

MET 148 ASN 149 -0.0821

ASN 149 ALA 150 0.0002

ALA 150 LYS 151 -0.0094

LYS 151 ILE 152 -0.0002

ILE 152 SER 153 -0.0072

SER 153 ASP 154 0.0000

ASP 154 PHE 155 0.0104

PHE 155 GLY 156 -0.0005

GLY 156 LEU 157 0.0641

LEU 157 ALA 158 0.0000

ALA 158 ARG 159 -0.0076

ARG 159 ILE 160 -0.0001

ILE 160 VAL 161 -0.0534

VAL 161 ALA 162 -0.0000

ALA 162 ILE 163 -0.0072

ILE 163 ASP 164 0.0003

ASP 164 GLN 165 0.0117

GLN 165 MET 166 -0.0003

MET 166 GLN 167 -0.0299

GLN 167 GLY 168 -0.0001

GLY 168 ASN 169 0.0132

ASN 169 THR 170 0.0001

THR 170 SER 171 0.1003

SER 171 ILE 172 0.0001

ILE 172 ILE 173 -0.0236

ILE 173 ALA 174 0.0002

ALA 174 GLY 175 0.0268

GLY 175 THR 176 0.0001

THR 176 TYR 177 0.2459

TYR 177 GLY 178 0.0004

GLY 178 TYR 179 0.0962

TYR 179 MET 180 0.0002

MET 180 SER 181 -0.0627

SER 181 PRO 182 0.0002

PRO 182 GLU 183 0.1089

GLU 183 TYR 184 -0.0002

TYR 184 ALA 185 0.0023

ALA 185 MET 186 0.0001

MET 186 LEU 187 0.0149

LEU 187 GLY 188 -0.0001

GLY 188 GLN 189 -0.0191

GLN 189 PHE 190 -0.0001

PHE 190 SER 191 -0.0682

SER 191 VAL 192 -0.0005

VAL 192 LYS 193 0.0899

LYS 193 SER 194 -0.0004

SER 194 ASP 195 -0.0316

ASP 195 VAL 196 -0.0001

VAL 196 PHE 197 -0.0081

PHE 197 SER 198 0.0005

SER 198 PHE 199 -0.0145

PHE 199 GLY 200 0.0003

GLY 200 VAL 201 0.0066

VAL 201 ILE 202 0.0004

ILE 202 MET 203 0.0293

MET 203 LEU 204 0.0000

LEU 204 GLU 205 -0.0039

GLU 205 ILE 206 0.0002

ILE 206 VAL 207 0.0134

VAL 207 SER 208 0.0005

SER 208 GLY 209 -0.0032

GLY 209 LYS 210 0.0000

LYS 210 ARG 211 0.0724

ARG 211 ASN 212 0.0005

ASN 212 VAL 213 0.0518

VAL 213 ASP 214 0.0003

ASP 214 TYR 215 -0.0201

TYR 215 ASN 216 0.0001

ASN 216 GLY 217 0.1350

GLY 217 VAL 218 -0.0000

VAL 218 ASN 219 0.0196

ASN 219 SER 220 -0.0001

SER 220 ILE 221 0.0892

ILE 221 ASP 222 -0.0000

ASP 222 ASP 223 0.0044

ASP 223 LEU 224 -0.0001

LEU 224 VAL 225 0.0179

VAL 225 SER 226 0.0001

SER 226 HIS 227 -0.0116

HIS 227 ALA 228 0.0004

ALA 228 TRP 229 -0.0049

TRP 229 LYS 230 0.0002

LYS 230 LYS 231 -0.0231

LYS 231 TRP 232 0.0001

TRP 232 THR 233 0.0099

THR 233 GLU 234 0.0001

GLU 234 ASN 235 -0.0082

ASN 235 LYS 236 0.0004

LYS 236 GLN 237 0.0060

GLN 237 MET 238 0.0001

MET 238 GLU 239 0.0095

GLU 239 LEU 240 0.0001

LEU 240 LEU 241 -0.0370

LEU 241 ASP 242 0.0000

ASP 242 PRO 243 0.0044

PRO 243 ALA 244 -0.0002

ALA 244 LEU 245 -0.0007

LEU 245 THR 246 0.0002

THR 246 TYR 247 0.0136

TYR 247 SER 248 -0.0001

SER 248 PHE 249 -0.0300

PHE 249 SER 250 -0.0003

SER 250 GLU 251 -0.0041

GLU 251 THR 252 -0.0000

THR 252 GLU 253 0.0156

GLU 253 VAL 254 -0.0002

VAL 254 SER 255 -0.0069

SER 255 ARG 256 0.0001

ARG 256 CYS 257 0.0228

CYS 257 ILE 258 -0.0000

ILE 258 GLN 259 0.0094

GLN 259 LEU 260 -0.0001

LEU 260 GLY 261 0.0001

GLY 261 LEU 262 0.0002

LEU 262 LEU 263 0.0167

LEU 263 CYS 264 -0.0000

CYS 264 VAL 265 -0.0122

VAL 265 GLN 266 0.0001

GLN 266 GLU 267 -0.0765

GLU 267 ASN 268 -0.0003

ASN 268 PRO 269 0.0688

PRO 269 ASP 270 -0.0001

ASP 270 GLN 271 -0.0186

GLN 271 ARG 272 -0.0000

ARG 272 PRO 273 -0.0706

PRO 273 THR 274 0.0001

THR 274 MET 275 0.0430

MET 275 ALA 276 -0.0002

ALA 276 THR 277 0.0128

THR 277 ILE 278 0.0001

ILE 278 ALA 279 -0.0037

ALA 279 LEU 280 0.0001

LEU 280 TYR 281 0.0119

TYR 281 PHE 282 -0.0001

PHE 282 ASN 283 0.0130

ASN 283 ILE 284 0.0001

ILE 284 ASP 285 -0.0175

ASP 285 SER 286 0.0002

SER 286 ILE 287 -0.0238

ILE 287 ASP 288 -0.0001

ASP 288 LEU 289 -0.0562

LEU 289 PRO 290 0.0000

PRO 290 LEU 291 -0.0015

LEU 291 PRO 292 0.0001

PRO 292 GLN 293 -0.0824

GLN 293 GLN 294 0.0003

GLN 294 PRO 295 -0.0249

PRO 295 PRO 296 0.0003

PRO 296 PHE 297 0.0157

PHE 297 TYR 298 -0.0002

TYR 298 MET 299 -0.0406

MET 299 ARG 300 -0.0002

ARG 300 GLY 301 0.1947

GLY 301 LYS 302 -0.0001

LYS 302 ILE 303 -0.0393

ILE 303 GLU 304 0.0002

GLU 304 SER 305 0.0701

SER 305 LYS 306 -0.0003

LYS 306 VAL 307 0.0456

VAL 307 ALA 308 0.0003

ALA 308 SER 309 -0.0739

SER 309 LYS 310 0.0001

LYS 310 LYS 311 -0.0518

LYS 311 THR 312 0.0001

THR 312 MET 313 0.2549

MET 313 SER 314 -0.0002

SER 314 GLY 315 -0.0964

GLY 315 ARG 316 -0.0000

ARG 316 PRO 317 0.0053

PRO 317 ARG 318 0.0002

ARG 318 SER 319 0.1149

SER 319 TYR 320 -0.0000

TYR 320 SER 321 0.1615

SER 321 VAL 322 -0.0000

VAL 322 THR 323 -0.0240

THR 323 ARG 324 0.0000

ARG 324 PHE 325 0.2212

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 230101190352136506

--- normal mode 17 ---

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

* *