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

* *

CA strain for 230101190352136506

--- normal mode 15 ---

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 -0.0000

ASP 2 MET 3 -0.0401

MET 3 ILE 4 0.0003

ILE 4 ARG 5 0.0249

ARG 5 LEU 6 0.0001

LEU 6 ALA 7 -0.0345

ALA 7 THR 8 0.0002

THR 8 ASN 9 -0.0162

ASN 9 LYS 10 0.0002

LYS 10 PHE 11 -0.0035

PHE 11 SER 12 0.0000

SER 12 GLU 13 0.0254

GLU 13 ASP 14 -0.0002

ASP 14 ASN 15 -0.0162

ASN 15 LYS 16 -0.0000

LYS 16 ILE 17 -0.1434

ILE 17 GLY 18 -0.0003

GLY 18 GLU 19 -0.0226

GLU 19 GLY 20 -0.0000

GLY 20 GLY 21 0.0541

GLY 21 PHE 22 -0.0003

PHE 22 GLY 23 -0.0468

GLY 23 ASP 24 -0.0001

ASP 24 VAL 25 0.0140

VAL 25 TYR 26 0.0000

TYR 26 LYS 27 0.0424

LYS 27 GLY 28 -0.0003

GLY 28 MET 29 0.0596

MET 29 PHE 30 -0.0004

PHE 30 PRO 31 0.0085

PRO 31 ASN 32 -0.0003

ASN 32 GLY 33 -0.0381

GLY 33 TYR 34 0.0002

TYR 34 GLU 35 -0.0279

GLU 35 ILE 36 -0.0001

ILE 36 ALA 37 0.0220

ALA 37 VAL 38 -0.0003

VAL 38 LYS 39 0.0388

LYS 39 ARG 40 -0.0001

ARG 40 LEU 41 0.0182

LEU 41 ILE 42 0.0000

ILE 42 ARG 43 -0.0352

ARG 43 ASN 44 0.0002

ASN 44 SER 45 -0.0672

SER 45 SER 46 0.0003

SER 46 GLN 47 -0.0058

GLN 47 GLY 48 -0.0001

GLY 48 ALA 49 0.0198

ALA 49 VAL 50 -0.0004

VAL 50 GLU 51 -0.0127

GLU 51 PHE 52 -0.0002

PHE 52 LYS 53 0.0357

LYS 53 ASN 54 -0.0001

ASN 54 GLU 55 -0.0164

GLU 55 VAL 56 -0.0000

VAL 56 LEU 57 0.0853

LEU 57 LEU 58 0.0001

LEU 58 ILE 59 0.0108

ILE 59 ALA 60 0.0002

ALA 60 LYS 61 0.0610

LYS 61 LEU 62 0.0001

LEU 62 GLN 63 0.0085

GLN 63 HIS 64 0.0000

HIS 64 ARG 65 -0.0008

ARG 65 ASN 66 -0.0002

ASN 66 LEU 67 -0.0278

LEU 67 VAL 68 -0.0001

VAL 68 ARG 69 0.0337

ARG 69 LEU 70 -0.0001

LEU 70 LEU 71 0.0312

LEU 71 GLY 72 0.0005

GLY 72 PHE 73 0.0094

PHE 73 CYS 74 0.0003

CYS 74 ILE 75 -0.0101

ILE 75 GLN 76 0.0002

GLN 76 ARG 77 0.0338

ARG 77 ASN 78 0.0000

ASN 78 GLU 79 -0.0266

GLU 79 LYS 80 -0.0001

LYS 80 ILE 81 -0.0116

ILE 81 LEU 82 -0.0002

LEU 82 ILE 83 -0.0021

ILE 83 TYR 84 0.0005

TYR 84 GLU 85 0.0094

GLU 85 TYR 86 -0.0000

TYR 86 MET 87 -0.1152

MET 87 HIS 88 -0.0003

HIS 88 ASN 89 -0.0476

ASN 89 LYS 90 -0.0002

LYS 90 SER 91 0.0131

SER 91 LEU 92 -0.0000

LEU 92 ASP 93 0.0631

ASP 93 TYR 94 -0.0001

TYR 94 TYR 95 -0.0045

TYR 95 LEU 96 -0.0002

LEU 96 PHE 97 0.0263

PHE 97 SER 98 -0.0001

SER 98 PRO 99 -0.0322

PRO 99 GLU 100 -0.0003

GLU 100 ASN 101 0.0101

ASN 101 HIS 102 0.0000

HIS 102 ARG 103 -0.0313

ARG 103 LYS 104 0.0000

LYS 104 LEU 105 0.0493

LEU 105 THR 106 0.0000

THR 106 TRP 107 0.0088

TRP 107 HIS 108 0.0000

HIS 108 ALA 109 -0.0812

ALA 109 ARG 110 -0.0001

ARG 110 TYR 111 0.0292

TYR 111 LYS 112 0.0001

LYS 112 ILE 113 0.0181

ILE 113 ILE 114 0.0001

ILE 114 ARG 115 0.0060

ARG 115 GLY 116 -0.0002

GLY 116 ILE 117 -0.0188

ILE 117 ALA 118 0.0002

ALA 118 ARG 119 -0.0270

ARG 119 GLY 120 0.0003

GLY 120 ILE 121 0.0089

ILE 121 LEU 122 -0.0002

LEU 122 TYR 123 -0.0115

TYR 123 LEU 124 0.0001

LEU 124 HIS 125 0.0074

HIS 125 GLU 126 0.0001

GLU 126 ASP 127 -0.0031

ASP 127 SER 128 0.0002

SER 128 HIS 129 0.0079

HIS 129 LEU 130 0.0003

LEU 130 LYS 131 0.0107

LYS 131 ILE 132 0.0001

ILE 132 ILE 133 0.0122

ILE 133 HIS 134 -0.0002

HIS 134 CYS 135 0.0103

CYS 135 ASP 136 0.0003

ASP 136 LEU 137 -0.0148

LEU 137 LYS 138 -0.0002

LYS 138 PRO 139 -0.0260

PRO 139 SER 140 0.0001

SER 140 ASN 141 -0.0153

ASN 141 ILE 142 -0.0002

ILE 142 LEU 143 -0.0038

LEU 143 LEU 144 0.0000

LEU 144 ASP 145 0.0687

ASP 145 ASP 146 0.0002

ASP 146 LYS 147 -0.1107

LYS 147 MET 148 0.0003

MET 148 ASN 149 0.0680

ASN 149 ALA 150 0.0001

ALA 150 LYS 151 -0.0383

LYS 151 ILE 152 -0.0002

ILE 152 SER 153 -0.0568

SER 153 ASP 154 0.0000

ASP 154 PHE 155 -0.0234

PHE 155 GLY 156 0.0004

GLY 156 LEU 157 0.0327

LEU 157 ALA 158 -0.0001

ALA 158 ARG 159 -0.0290

ARG 159 ILE 160 -0.0002

ILE 160 VAL 161 0.0400

VAL 161 ALA 162 0.0004

ALA 162 ILE 163 -0.0047

ILE 163 ASP 164 0.0000

ASP 164 GLN 165 0.0030

GLN 165 MET 166 0.0001

MET 166 GLN 167 0.0193

GLN 167 GLY 168 -0.0002

GLY 168 ASN 169 0.0249

ASN 169 THR 170 -0.0001

THR 170 SER 171 0.0577

SER 171 ILE 172 -0.0001

ILE 172 ILE 173 0.0088

ILE 173 ALA 174 -0.0002

ALA 174 GLY 175 0.0075

GLY 175 THR 176 -0.0006

THR 176 TYR 177 0.0533

TYR 177 GLY 178 -0.0004

GLY 178 TYR 179 -0.0159

TYR 179 MET 180 -0.0002

MET 180 SER 181 -0.0031

SER 181 PRO 182 0.0002

PRO 182 GLU 183 0.0020

GLU 183 TYR 184 -0.0001

TYR 184 ALA 185 0.0482

ALA 185 MET 186 0.0001

MET 186 LEU 187 0.0363

LEU 187 GLY 188 0.0002

GLY 188 GLN 189 0.0098

GLN 189 PHE 190 0.0001

PHE 190 SER 191 0.0231

SER 191 VAL 192 0.0004

VAL 192 LYS 193 -0.0064

LYS 193 SER 194 0.0001

SER 194 ASP 195 0.0069

ASP 195 VAL 196 -0.0001

VAL 196 PHE 197 0.0246

PHE 197 SER 198 0.0004

SER 198 PHE 199 0.0080

PHE 199 GLY 200 0.0005

GLY 200 VAL 201 0.0131

VAL 201 ILE 202 -0.0001

ILE 202 MET 203 -0.0173

MET 203 LEU 204 -0.0003

LEU 204 GLU 205 0.0187

GLU 205 ILE 206 0.0002

ILE 206 VAL 207 -0.0131

VAL 207 SER 208 0.0003

SER 208 GLY 209 0.0464

GLY 209 LYS 210 -0.0001

LYS 210 ARG 211 -0.0520

ARG 211 ASN 212 0.0004

ASN 212 VAL 213 -0.0147

VAL 213 ASP 214 -0.0001

ASP 214 TYR 215 0.4442

TYR 215 ASN 216 0.0001

ASN 216 GLY 217 0.1030

GLY 217 VAL 218 0.0000

VAL 218 ASN 219 0.0049

ASN 219 SER 220 0.0001

SER 220 ILE 221 0.2411

ILE 221 ASP 222 -0.0001

ASP 222 ASP 223 -0.0515

ASP 223 LEU 224 -0.0002

LEU 224 VAL 225 -0.0122

VAL 225 SER 226 0.0001

SER 226 HIS 227 0.0327

HIS 227 ALA 228 -0.0001

ALA 228 TRP 229 -0.0462

TRP 229 LYS 230 0.0004

LYS 230 LYS 231 -0.0152

LYS 231 TRP 232 -0.0004

TRP 232 THR 233 -0.0133

THR 233 GLU 234 0.0000

GLU 234 ASN 235 -0.0041

ASN 235 LYS 236 0.0001

LYS 236 GLN 237 -0.0163

GLN 237 MET 238 0.0003

MET 238 GLU 239 -0.0674

GLU 239 LEU 240 -0.0001

LEU 240 LEU 241 -0.0470

LEU 241 ASP 242 0.0001

ASP 242 PRO 243 0.0013

PRO 243 ALA 244 0.0001

ALA 244 LEU 245 0.0257

LEU 245 THR 246 -0.0002

THR 246 TYR 247 -0.0089

TYR 247 SER 248 0.0001

SER 248 PHE 249 0.0569

PHE 249 SER 250 0.0001

SER 250 GLU 251 -0.0150

GLU 251 THR 252 -0.0002

THR 252 GLU 253 -0.0337

GLU 253 VAL 254 -0.0003

VAL 254 SER 255 -0.0167

SER 255 ARG 256 0.0002

ARG 256 CYS 257 -0.0196

CYS 257 ILE 258 -0.0002

ILE 258 GLN 259 -0.0098

GLN 259 LEU 260 -0.0004

LEU 260 GLY 261 -0.0103

GLY 261 LEU 262 -0.0004

LEU 262 LEU 263 -0.0383

LEU 263 CYS 264 -0.0001

CYS 264 VAL 265 0.0064

VAL 265 GLN 266 -0.0002

GLN 266 GLU 267 0.0207

GLU 267 ASN 268 -0.0002

ASN 268 PRO 269 -0.0036

PRO 269 ASP 270 -0.0003

ASP 270 GLN 271 0.0068

GLN 271 ARG 272 0.0003

ARG 272 PRO 273 0.0219

PRO 273 THR 274 0.0005

THR 274 MET 275 -0.0277

MET 275 ALA 276 -0.0001

ALA 276 THR 277 -0.0126

THR 277 ILE 278 -0.0002

ILE 278 ALA 279 -0.0022

ALA 279 LEU 280 0.0003

LEU 280 TYR 281 -0.0191

TYR 281 PHE 282 -0.0002

PHE 282 ASN 283 -0.0178

ASN 283 ILE 284 0.0003

ILE 284 ASP 285 0.0178

ASP 285 SER 286 0.0002

SER 286 ILE 287 0.0162

ILE 287 ASP 288 0.0000

ASP 288 LEU 289 0.0165

LEU 289 PRO 290 -0.0003

PRO 290 LEU 291 -0.0312

LEU 291 PRO 292 -0.0001

PRO 292 GLN 293 0.0401

GLN 293 GLN 294 -0.0001

GLN 294 PRO 295 0.0018

PRO 295 PRO 296 0.0003

PRO 296 PHE 297 0.0636

PHE 297 TYR 298 -0.0004

TYR 298 MET 299 0.0873

MET 299 ARG 300 -0.0000

ARG 300 GLY 301 -0.0464

GLY 301 LYS 302 0.0003

LYS 302 ILE 303 -0.0005

ILE 303 GLU 304 -0.0003

GLU 304 SER 305 -0.0392

SER 305 LYS 306 0.0002

LYS 306 VAL 307 -0.0058

VAL 307 ALA 308 0.0004

ALA 308 SER 309 0.0587

SER 309 LYS 310 -0.0000

LYS 310 LYS 311 -0.0019

LYS 311 THR 312 0.0003

THR 312 MET 313 -0.0731

MET 313 SER 314 0.0001

SER 314 GLY 315 -0.0654

GLY 315 ARG 316 0.0003

ARG 316 PRO 317 -0.1516

PRO 317 ARG 318 -0.0001

ARG 318 SER 319 0.0254

SER 319 TYR 320 0.0002

TYR 320 SER 321 0.0616

SER 321 VAL 322 -0.0000

VAL 322 THR 323 -0.0402

THR 323 ARG 324 0.0001

ARG 324 PHE 325 0.1096

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 15 ---

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

* *