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

* testNMAJB *

CA strain for 2404031516062184733

--- 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
MET 1 GLY 2 0.0002

GLY 2 GLY 3 -0.0988

GLY 3 GLN 4 -0.0002

GLN 4 VAL 5 0.0648

VAL 5 SER 6 0.0001

SER 6 ALA 7 0.0453

ALA 7 SER 8 -0.0000

SER 8 ASN 9 0.0597

ASN 9 SER 10 -0.0003

SER 10 PHE 11 -0.0916

PHE 11 SER 12 -0.0002

SER 12 ARG 13 -0.0454

ARG 13 LEU 14 0.0002

LEU 14 HIS 15 0.0153

HIS 15 CYS 16 -0.0002

CYS 16 ARG 17 0.0396

ARG 17 ASN 18 0.0001

ASN 18 ALA 19 -0.1205

ALA 19 ASN 20 0.0000

ASN 20 GLU 21 -0.0304

GLU 21 ASP 22 -0.0000

ASP 22 TRP 23 0.0387

TRP 23 MET 24 0.0000

MET 24 SER 25 -0.0214

SER 25 ALA 26 0.0004

ALA 26 LEU 27 0.0203

LEU 27 CYS 28 -0.0000

CYS 28 PRO 29 -0.1527

PRO 29 ARG 30 0.0003

ARG 30 LEU 31 -0.0231

LEU 31 TRP 32 0.0004

TRP 32 ASP 33 -0.0398

ASP 33 VAL 34 -0.0002

VAL 34 PRO 35 0.0643

PRO 35 LEU 36 0.0000

LEU 36 HIS 37 0.0233

HIS 37 HIS 38 -0.0004

HIS 38 LEU 39 0.0304

LEU 39 SER 40 0.0002

SER 40 ILE 41 -0.0182

ILE 41 PRO 42 0.0003

PRO 42 GLY 43 -0.0625

GLY 43 SER 44 0.0003

SER 44 HIS 45 -0.0049

HIS 45 ASP 46 -0.0001

ASP 46 THR 47 0.0646

THR 47 MET 48 -0.0001

MET 48 THR 49 -0.0954

THR 49 TYR 50 -0.0004

TYR 50 CYS 51 0.0512

CYS 51 LEU 52 -0.0003

LEU 52 ASN 53 -0.0569

ASN 53 LYS 54 0.0001

LYS 54 LYS 55 -0.0226

LYS 55 SER 56 0.0002

SER 56 PRO 57 -0.0411

PRO 57 ILE 58 -0.0001

ILE 58 SER 59 -0.0658

SER 59 HIS 60 -0.0002

HIS 60 GLU 61 -0.0793

GLU 61 GLU 62 0.0001

GLU 62 SER 63 0.0907

SER 63 ARG 64 0.0000

ARG 64 LEU 65 0.0461

LEU 65 LEU 66 0.0000

LEU 66 GLN 67 -0.1019

GLN 67 LEU 68 -0.0000

LEU 68 LEU 69 -0.0472

LEU 69 ASN 70 0.0003

ASN 70 LYS 71 0.1063

LYS 71 ALA 72 -0.0003

ALA 72 LEU 73 0.0660

LEU 73 PRO 74 0.0002

PRO 74 CYS 75 -0.0024

CYS 75 ILE 76 0.0006

ILE 76 THR 77 -0.1154

THR 77 ARG 78 -0.0003

ARG 78 PRO 79 -0.0171

PRO 79 VAL 80 -0.0001

VAL 80 VAL 81 0.0248

VAL 81 LEU 82 -0.0001

LEU 82 LYS 83 -0.1213

LYS 83 TRP 84 -0.0001

TRP 84 SER 85 0.0479

SER 85 VAL 86 0.0002

VAL 86 THR 87 -0.2363

THR 87 GLN 88 0.0001

GLN 88 ALA 89 0.0386

ALA 89 LEU 90 -0.0000

LEU 90 ASP 91 0.0946

ASP 91 VAL 92 0.0000

VAL 92 THR 93 -0.1036

THR 93 GLU 94 0.0002

GLU 94 GLN 95 0.0468

GLN 95 LEU 96 -0.0001

LEU 96 ASP 97 0.0489

ASP 97 ALA 98 -0.0001

ALA 98 GLY 99 -0.0360

GLY 99 VAL 100 0.0003

VAL 100 ARG 101 -0.0677

ARG 101 TYR 102 -0.0003

TYR 102 LEU 103 -0.0615

LEU 103 ASP 104 -0.0002

ASP 104 LEU 105 0.0698

LEU 105 ARG 106 -0.0000

ARG 106 ILE 107 0.1839

ILE 107 ALA 108 -0.0004

ALA 108 HIS 109 0.0545

HIS 109 MET 110 -0.0001

MET 110 LEU 111 0.1883

LEU 111 GLU 112 0.0001

GLU 112 GLY 113 -0.0121

GLY 113 SER 114 0.0005

SER 114 GLU 115 0.2125

GLU 115 LYS 116 -0.0001

LYS 116 ASN 117 -0.0268

ASN 117 LEU 118 -0.0000

LEU 118 HIS 119 0.1740

HIS 119 PHE 120 -0.0001

PHE 120 VAL 121 -0.1878

VAL 121 HIS 122 -0.0002

HIS 122 MET 123 0.0217

MET 123 VAL 124 -0.0003

VAL 124 TYR 125 -0.0206

TYR 125 THR 126 0.0002

THR 126 THR 127 -0.1235

THR 127 ALA 128 0.0000

ALA 128 LEU 129 0.0595

LEU 129 VAL 130 -0.0003

VAL 130 GLU 131 -0.0119

GLU 131 ASP 132 0.0002

ASP 132 THR 133 0.1008

THR 133 LEU 134 0.0001

LEU 134 THR 135 0.0160

THR 135 GLU 136 -0.0002

GLU 136 ILE 137 -0.0811

ILE 137 SER 138 -0.0004

SER 138 GLU 139 0.0515

GLU 139 TRP 140 -0.0003

TRP 140 LEU 141 -0.0604

LEU 141 GLU 142 0.0001

GLU 142 ARG 143 0.0346

ARG 143 HIS 144 0.0001

HIS 144 PRO 145 -0.0310

PRO 145 ARG 146 0.0002

ARG 146 GLU 147 -0.0030

GLU 147 VAL 148 -0.0002

VAL 148 VAL 149 -0.0444

VAL 149 ILE 150 -0.0000

ILE 150 LEU 151 -0.0221

LEU 151 ALA 152 0.0001

ALA 152 CYS 153 -0.0187

CYS 153 ARG 154 -0.0000

ARG 154 ASN 155 -0.0268

ASN 155 PHE 156 0.0000

PHE 156 GLU 157 0.0515

GLU 157 GLY 158 0.0000

GLY 158 LEU 159 -0.0958

LEU 159 SER 160 -0.0003

SER 160 GLU 161 0.0716

GLU 161 ASP 162 0.0001

ASP 162 LEU 163 0.0655

LEU 163 HIS 164 0.0000

HIS 164 GLU 165 0.0131

GLU 165 TYR 166 -0.0004

TYR 166 LEU 167 0.0200

LEU 167 VAL 168 -0.0002

VAL 168 ALA 169 0.0230

ALA 169 CYS 170 0.0004

CYS 170 ILE 171 -0.0479

ILE 171 LYS 172 -0.0002

LYS 172 ASN 173 0.0079

ASN 173 ILE 174 -0.0002

ILE 174 PHE 175 -0.0859

PHE 175 GLY 176 -0.0004

GLY 176 ASP 177 -0.0961

ASP 177 MET 178 -0.0001

MET 178 LEU 179 0.0141

LEU 179 CYS 180 0.0004

CYS 180 PRO 181 0.0046

PRO 181 ARG 182 -0.0001

ARG 182 GLY 183 -0.0723

GLY 183 GLU 184 0.0001

GLU 184 VAL 185 -0.0562

VAL 185 PRO 186 0.0000

PRO 186 THR 187 0.0192

THR 187 LEU 188 0.0000

LEU 188 ARG 189 -0.0261

ARG 189 GLN 190 -0.0000

GLN 190 LEU 191 -0.0460

LEU 191 TRP 192 0.0000

TRP 192 SER 193 -0.0555

SER 193 ARG 194 0.0002

ARG 194 GLY 195 -0.1191

GLY 195 GLN 196 -0.0000

GLN 196 GLN 197 -0.0383

GLN 197 VAL 198 0.0003

VAL 198 ILE 199 0.0148

ILE 199 VAL 200 0.0002

VAL 200 SER 201 0.0454

SER 201 TYR 202 0.0001

TYR 202 GLU 203 0.0088

GLU 203 ASP 204 0.0000

ASP 204 GLU 205 0.0576

GLU 205 SER 206 0.0002

SER 206 SER 207 -0.0133

SER 207 LEU 208 -0.0003

LEU 208 ARG 209 -0.0015

ARG 209 ARG 210 0.0002

ARG 210 HIS 211 -0.0226

HIS 211 HIS 212 0.0002

HIS 212 GLU 213 0.0059

GLU 213 LEU 214 -0.0002

LEU 214 TRP 215 -0.0582

TRP 215 PRO 216 -0.0001

PRO 216 GLY 217 0.0724

GLY 217 VAL 218 0.0002

VAL 218 PRO 219 0.0959

PRO 219 TYR 220 0.0003

TYR 220 TRP 221 0.2137

TRP 221 TRP 222 -0.0002

TRP 222 GLY 223 0.1193

GLY 223 ASN 224 -0.0003

ASN 224 ARG 225 0.0287

ARG 225 VAL 226 0.0003

VAL 226 LYS 227 -0.0210

LYS 227 THR 228 -0.0001

THR 228 GLU 229 0.0949

GLU 229 ALA 230 -0.0000

ALA 230 LEU 231 0.0523

LEU 231 ILE 232 0.0002

ILE 232 ARG 233 0.0003

ARG 233 TYR 234 -0.0001

TYR 234 LEU 235 -0.0255

LEU 235 GLU 236 -0.0002

GLU 236 THR 237 -0.0257

THR 237 MET 238 0.0004

MET 238 LYS 239 -0.0065

LYS 239 SER 240 -0.0004

SER 240 CYS 241 0.0726

CYS 241 GLY 242 0.0001

GLY 242 ARG 243 -0.0358

ARG 243 PRO 244 0.0003

PRO 244 GLY 245 0.0566

GLY 245 GLY 246 -0.0002

GLY 246 LEU 247 -0.0687

LEU 247 PHE 248 -0.0003

PHE 248 VAL 249 0.0467

VAL 249 ALA 250 -0.0002

ALA 250 GLY 251 0.0025

GLY 251 ILE 252 0.0001

ILE 252 ASN 253 -0.0894

ASN 253 LEU 254 0.0003

LEU 254 THR 255 -0.3163

THR 255 GLU 256 0.0003

GLU 256 ASN 257 -0.2430

ASN 257 LEU 258 -0.0003

LEU 258 GLN 259 -0.0927

GLN 259 TYR 260 -0.0001

TYR 260 VAL 261 0.0385

VAL 261 LEU 262 -0.0000

LEU 262 ALA 263 0.0823

ALA 263 HIS 264 0.0002

HIS 264 PRO 265 0.0131

PRO 265 SER 266 -0.0002

SER 266 GLU 267 -0.0061

GLU 267 SER 268 -0.0000

SER 268 LEU 269 -0.0791

LEU 269 GLU 270 -0.0002

GLU 270 LYS 271 -0.0089

LYS 271 MET 272 -0.0003

MET 272 THR 273 -0.0551

THR 273 LEU 274 -0.0002

LEU 274 PRO 275 0.0474

PRO 275 ASN 276 0.0000

ASN 276 LEU 277 -0.1153

LEU 277 PRO 278 -0.0002

PRO 278 ARG 279 -0.0117

ARG 279 LEU 280 -0.0000

LEU 280 SER 281 -0.1694

SER 281 ALA 282 0.0002

ALA 282 TRP 283 0.0856

TRP 283 VAL 284 0.0002

VAL 284 ARG 285 -0.0378

ARG 285 GLU 286 -0.0001

GLU 286 GLN 287 0.0243

GLN 287 CYS 288 0.0000

CYS 288 PRO 289 -0.1168

PRO 289 GLY 290 0.0002

GLY 290 PRO 291 0.0260

PRO 291 GLY 292 -0.0000

GLY 292 SER 293 0.0738

SER 293 ARG 294 0.0003

ARG 294 CYS 295 0.0542

CYS 295 THR 296 0.0001

THR 296 ASN 297 -0.0313

ASN 297 ILE 298 -0.0002

ILE 298 ILE 299 -0.0261

ILE 299 ALA 300 0.0002

ALA 300 GLY 301 -0.0935

GLY 301 ASP 302 0.0002

ASP 302 PHE 303 0.0487

PHE 303 ILE 304 -0.0001

ILE 304 GLY 305 0.0243

GLY 305 ALA 306 0.0001

ALA 306 ASP 307 0.0462

ASP 307 GLY 308 -0.0000

GLY 308 PHE 309 0.1065

PHE 309 VAL 310 -0.0003

VAL 310 SER 311 -0.0011

SER 311 ASP 312 0.0003

ASP 312 VAL 313 -0.0467

VAL 313 ILE 314 -0.0003

ILE 314 ALA 315 0.0717

ALA 315 LEU 316 0.0002

LEU 316 ASN 317 -0.1833

ASN 317 GLN 318 -0.0002

GLN 318 LYS 319 0.1177

LYS 319 LEU 320 0.0003

LEU 320 LEU 321 0.0005

LEU 321 TRP 322 -0.0001

TRP 322 CYS 323 0.0670

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.

*** testNMAJB ***

CA strain for 2404031516062184733

--- normal mode 14 ---

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

* testNMAJB *