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

* *

CA strain for 230101190352136506

--- normal mode 14 ---

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 -0.0001

ASP 2 MET 3 -0.1171

MET 3 ILE 4 0.0002

ILE 4 ARG 5 0.0305

ARG 5 LEU 6 0.0001

LEU 6 ALA 7 -0.0650

ALA 7 THR 8 -0.0001

THR 8 ASN 9 -0.0208

ASN 9 LYS 10 0.0002

LYS 10 PHE 11 0.0056

PHE 11 SER 12 -0.0001

SER 12 GLU 13 0.0198

GLU 13 ASP 14 0.0005

ASP 14 ASN 15 -0.0158

ASN 15 LYS 16 -0.0002

LYS 16 ILE 17 -0.0883

ILE 17 GLY 18 -0.0002

GLY 18 GLU 19 0.1712

GLU 19 GLY 20 0.0003

GLY 20 GLY 21 -0.0307

GLY 21 PHE 22 0.0000

PHE 22 GLY 23 0.0510

GLY 23 ASP 24 -0.0001

ASP 24 VAL 25 0.0540

VAL 25 TYR 26 0.0002

TYR 26 LYS 27 0.0625

LYS 27 GLY 28 -0.0000

GLY 28 MET 29 0.1060

MET 29 PHE 30 0.0001

PHE 30 PRO 31 0.0172

PRO 31 ASN 32 0.0001

ASN 32 GLY 33 -0.0820

GLY 33 TYR 34 0.0003

TYR 34 GLU 35 -0.0673

GLU 35 ILE 36 -0.0004

ILE 36 ALA 37 0.0730

ALA 37 VAL 38 -0.0004

VAL 38 LYS 39 0.0480

LYS 39 ARG 40 0.0002

ARG 40 LEU 41 0.0310

LEU 41 ILE 42 -0.0001

ILE 42 ARG 43 0.0274

ARG 43 ASN 44 0.0000

ASN 44 SER 45 0.1437

SER 45 SER 46 0.0000

SER 46 GLN 47 -0.0075

GLN 47 GLY 48 0.0003

GLY 48 ALA 49 -0.1243

ALA 49 VAL 50 0.0002

VAL 50 GLU 51 -0.0024

GLU 51 PHE 52 0.0000

PHE 52 LYS 53 0.0339

LYS 53 ASN 54 -0.0002

ASN 54 GLU 55 -0.0178

GLU 55 VAL 56 0.0001

VAL 56 LEU 57 0.1104

LEU 57 LEU 58 -0.0001

LEU 58 ILE 59 0.0400

ILE 59 ALA 60 -0.0004

ALA 60 LYS 61 0.0555

LYS 61 LEU 62 -0.0005

LEU 62 GLN 63 0.0102

GLN 63 HIS 64 0.0002

HIS 64 ARG 65 -0.0629

ARG 65 ASN 66 -0.0002

ASN 66 LEU 67 -0.0310

LEU 67 VAL 68 0.0002

VAL 68 ARG 69 -0.0330

ARG 69 LEU 70 0.0003

LEU 70 LEU 71 0.0793

LEU 71 GLY 72 0.0002

GLY 72 PHE 73 -0.1404

PHE 73 CYS 74 -0.0000

CYS 74 ILE 75 -0.1000

ILE 75 GLN 76 0.0001

GLN 76 ARG 77 0.0088

ARG 77 ASN 78 -0.0000

ASN 78 GLU 79 0.0028

GLU 79 LYS 80 -0.0001

LYS 80 ILE 81 -0.0444

ILE 81 LEU 82 0.0001

LEU 82 ILE 83 -0.0142

ILE 83 TYR 84 -0.0000

TYR 84 GLU 85 -0.0759

GLU 85 TYR 86 -0.0001

TYR 86 MET 87 -0.2692

MET 87 HIS 88 0.0003

HIS 88 ASN 89 -0.2092

ASN 89 LYS 90 -0.0000

LYS 90 SER 91 -0.0216

SER 91 LEU 92 -0.0001

LEU 92 ASP 93 -0.0013

ASP 93 TYR 94 -0.0003

TYR 94 TYR 95 0.0076

TYR 95 LEU 96 -0.0001

LEU 96 PHE 97 -0.0080

PHE 97 SER 98 -0.0001

SER 98 PRO 99 -0.0236

PRO 99 GLU 100 0.0002

GLU 100 ASN 101 -0.0012

ASN 101 HIS 102 0.0006

HIS 102 ARG 103 -0.0035

ARG 103 LYS 104 -0.0001

LYS 104 LEU 105 0.0605

LEU 105 THR 106 0.0003

THR 106 TRP 107 -0.0195

TRP 107 HIS 108 0.0002

HIS 108 ALA 109 -0.1169

ALA 109 ARG 110 0.0003

ARG 110 TYR 111 0.0202

TYR 111 LYS 112 -0.0000

LYS 112 ILE 113 0.0327

ILE 113 ILE 114 0.0000

ILE 114 ARG 115 0.0098

ARG 115 GLY 116 0.0001

GLY 116 ILE 117 -0.0189

ILE 117 ALA 118 0.0003

ALA 118 ARG 119 -0.0270

ARG 119 GLY 120 -0.0002

GLY 120 ILE 121 -0.0133

ILE 121 LEU 122 -0.0003

LEU 122 TYR 123 0.0219

TYR 123 LEU 124 0.0000

LEU 124 HIS 125 0.0157

HIS 125 GLU 126 -0.0002

GLU 126 ASP 127 -0.0070

ASP 127 SER 128 0.0002

SER 128 HIS 129 0.0100

HIS 129 LEU 130 0.0001

LEU 130 LYS 131 -0.0039

LYS 131 ILE 132 0.0002

ILE 132 ILE 133 -0.0180

ILE 133 HIS 134 0.0000

HIS 134 CYS 135 -0.0280

CYS 135 ASP 136 -0.0002

ASP 136 LEU 137 0.0380

LEU 137 LYS 138 -0.0001

LYS 138 PRO 139 0.0196

PRO 139 SER 140 0.0000

SER 140 ASN 141 -0.0398

ASN 141 ILE 142 -0.0003

ILE 142 LEU 143 0.0029

LEU 143 LEU 144 0.0002

LEU 144 ASP 145 0.0726

ASP 145 ASP 146 0.0001

ASP 146 LYS 147 -0.1686

LYS 147 MET 148 -0.0003

MET 148 ASN 149 0.0602

ASN 149 ALA 150 0.0000

ALA 150 LYS 151 -0.0429

LYS 151 ILE 152 -0.0002

ILE 152 SER 153 0.0406

SER 153 ASP 154 -0.0001

ASP 154 PHE 155 -0.0436

PHE 155 GLY 156 0.0001

GLY 156 LEU 157 0.1251

LEU 157 ALA 158 0.0002

ALA 158 ARG 159 -0.0341

ARG 159 ILE 160 0.0000

ILE 160 VAL 161 0.0939

VAL 161 ALA 162 0.0004

ALA 162 ILE 163 0.0126

ILE 163 ASP 164 0.0001

ASP 164 GLN 165 -0.0261

GLN 165 MET 166 0.0005

MET 166 GLN 167 -0.1007

GLN 167 GLY 168 0.0000

GLY 168 ASN 169 -0.1181

ASN 169 THR 170 0.0000

THR 170 SER 171 -0.0876

SER 171 ILE 172 0.0001

ILE 172 ILE 173 0.0104

ILE 173 ALA 174 0.0001

ALA 174 GLY 175 -0.0058

GLY 175 THR 176 -0.0003

THR 176 TYR 177 0.0910

TYR 177 GLY 178 -0.0001

GLY 178 TYR 179 0.0076

TYR 179 MET 180 0.0005

MET 180 SER 181 0.0145

SER 181 PRO 182 -0.0001

PRO 182 GLU 183 0.0393

GLU 183 TYR 184 0.0000

TYR 184 ALA 185 -0.0417

ALA 185 MET 186 0.0002

MET 186 LEU 187 -0.0148

LEU 187 GLY 188 -0.0003

GLY 188 GLN 189 -0.0436

GLN 189 PHE 190 -0.0005

PHE 190 SER 191 -0.0680

SER 191 VAL 192 -0.0001

VAL 192 LYS 193 0.0777

LYS 193 SER 194 0.0006

SER 194 ASP 195 -0.0283

ASP 195 VAL 196 -0.0001

VAL 196 PHE 197 -0.0188

PHE 197 SER 198 -0.0001

SER 198 PHE 199 -0.0041

PHE 199 GLY 200 -0.0000

GLY 200 VAL 201 -0.0168

VAL 201 ILE 202 -0.0000

ILE 202 MET 203 -0.0013

MET 203 LEU 204 -0.0000

LEU 204 GLU 205 -0.0245

GLU 205 ILE 206 0.0001

ILE 206 VAL 207 -0.0361

VAL 207 SER 208 0.0001

SER 208 GLY 209 -0.0339

GLY 209 LYS 210 -0.0002

LYS 210 ARG 211 0.0327

ARG 211 ASN 212 -0.0002

ASN 212 VAL 213 0.0110

VAL 213 ASP 214 0.0003

ASP 214 TYR 215 -0.0863

TYR 215 ASN 216 0.0000

ASN 216 GLY 217 -0.1272

GLY 217 VAL 218 0.0001

VAL 218 ASN 219 -0.0013

ASN 219 SER 220 0.0002

SER 220 ILE 221 -0.0938

ILE 221 ASP 222 -0.0004

ASP 222 ASP 223 0.0160

ASP 223 LEU 224 0.0001

LEU 224 VAL 225 -0.0047

VAL 225 SER 226 0.0002

SER 226 HIS 227 0.0019

HIS 227 ALA 228 -0.0001

ALA 228 TRP 229 -0.0046

TRP 229 LYS 230 -0.0001

LYS 230 LYS 231 0.0059

LYS 231 TRP 232 -0.0001

TRP 232 THR 233 -0.0130

THR 233 GLU 234 0.0002

GLU 234 ASN 235 -0.0046

ASN 235 LYS 236 0.0004

LYS 236 GLN 237 -0.0096

GLN 237 MET 238 0.0000

MET 238 GLU 239 0.0309

GLU 239 LEU 240 -0.0000

LEU 240 LEU 241 -0.0104

LEU 241 ASP 242 -0.0000

ASP 242 PRO 243 0.0041

PRO 243 ALA 244 -0.0003

ALA 244 LEU 245 -0.0061

LEU 245 THR 246 0.0000

THR 246 TYR 247 0.0272

TYR 247 SER 248 0.0001

SER 248 PHE 249 0.0258

PHE 249 SER 250 0.0000

SER 250 GLU 251 -0.0155

GLU 251 THR 252 0.0003

THR 252 GLU 253 -0.0248

GLU 253 VAL 254 -0.0003

VAL 254 SER 255 -0.0301

SER 255 ARG 256 -0.0000

ARG 256 CYS 257 -0.0193

CYS 257 ILE 258 0.0001

ILE 258 GLN 259 -0.0142

GLN 259 LEU 260 -0.0002

LEU 260 GLY 261 0.0018

GLY 261 LEU 262 -0.0001

LEU 262 LEU 263 0.0228

LEU 263 CYS 264 0.0001

CYS 264 VAL 265 -0.0051

VAL 265 GLN 266 -0.0001

GLN 266 GLU 267 -0.0180

GLU 267 ASN 268 0.0001

ASN 268 PRO 269 0.0428

PRO 269 ASP 270 -0.0001

ASP 270 GLN 271 0.0136

GLN 271 ARG 272 0.0001

ARG 272 PRO 273 -0.0690

PRO 273 THR 274 -0.0003

THR 274 MET 275 -0.0472

MET 275 ALA 276 0.0002

ALA 276 THR 277 0.0495

THR 277 ILE 278 0.0004

ILE 278 ALA 279 -0.0239

ALA 279 LEU 280 -0.0001

LEU 280 TYR 281 0.0064

TYR 281 PHE 282 0.0001

PHE 282 ASN 283 -0.0027

ASN 283 ILE 284 0.0002

ILE 284 ASP 285 0.0235

ASP 285 SER 286 0.0003

SER 286 ILE 287 0.0051

ILE 287 ASP 288 -0.0004

ASP 288 LEU 289 -0.0058

LEU 289 PRO 290 -0.0002

PRO 290 LEU 291 -0.0029

LEU 291 PRO 292 0.0001

PRO 292 GLN 293 -0.0449

GLN 293 GLN 294 0.0003

GLN 294 PRO 295 -0.0036

PRO 295 PRO 296 0.0002

PRO 296 PHE 297 -0.0146

PHE 297 TYR 298 -0.0001

TYR 298 MET 299 -0.0099

MET 299 ARG 300 0.0001

ARG 300 GLY 301 0.0537

GLY 301 LYS 302 0.0003

LYS 302 ILE 303 -0.0655

ILE 303 GLU 304 0.0003

GLU 304 SER 305 0.0309

SER 305 LYS 306 0.0002

LYS 306 VAL 307 0.0189

VAL 307 ALA 308 -0.0001

ALA 308 SER 309 -0.1510

SER 309 LYS 310 -0.0003

LYS 310 LYS 311 0.1258

LYS 311 THR 312 -0.0001

THR 312 MET 313 0.1673

MET 313 SER 314 -0.0002

SER 314 GLY 315 -0.0078

GLY 315 ARG 316 0.0001

ARG 316 PRO 317 0.5144

PRO 317 ARG 318 0.0001

ARG 318 SER 319 -0.1182

SER 319 TYR 320 0.0002

TYR 320 SER 321 0.0180

SER 321 VAL 322 0.0003

VAL 322 THR 323 -0.1013

THR 323 ARG 324 0.0001

ARG 324 PHE 325 -0.1729

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 14 ---

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

* *