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

* TRANSFERASE/RNA 05-DEC-14 4RWN *

CA strain for 22121617313095401

--- 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
MET 1 GLU 2 -0.0002

GLU 2 LEU 3 0.0008

LEU 3 ARG 4 -0.0001

ARG 4 HIS 5 0.0173

HIS 5 THR 6 -0.0001

THR 6 PRO 7 0.0098

PRO 7 ALA 8 0.0000

ALA 8 ARG 9 -0.0021

ARG 9 ASP 10 -0.0003

ASP 10 LEU 11 0.0065

LEU 11 ASP 12 0.0003

ASP 12 LYS 13 0.0017

LYS 13 PHE 14 -0.0001

PHE 14 ILE 15 0.0111

ILE 15 GLU 16 0.0000

GLU 16 ASP 17 -0.0616

ASP 17 HIS 18 -0.0001

HIS 18 LEU 19 0.0268

LEU 19 LEU 20 -0.0000

LEU 20 PRO 21 0.0059

PRO 21 ASN 22 0.0001

ASN 22 THR 23 -0.0823

THR 23 CYS 24 0.0001

CYS 24 PHE 25 -0.0054

PHE 25 ARG 26 -0.0002

ARG 26 THR 27 -0.0247

THR 27 GLN 28 -0.0002

GLN 28 VAL 29 -0.0263

VAL 29 LYS 30 -0.0002

LYS 30 GLU 31 0.0162

GLU 31 ALA 32 -0.0004

ALA 32 ILE 33 -0.0105

ILE 33 ASP 34 -0.0001

ASP 34 ILE 35 -0.0208

ILE 35 VAL 36 0.0000

VAL 36 CYS 37 0.0079

CYS 37 ARG 38 -0.0001

ARG 38 PHE 39 -0.0507

PHE 39 LEU 40 -0.0002

LEU 40 LYS 41 0.0002

LYS 41 GLU 42 -0.0000

GLU 42 ARG 43 -0.0477

ARG 43 CYS 44 0.0000

CYS 44 PHE 45 0.0256

PHE 45 GLN 46 0.0001

GLN 46 GLY 47 -0.0245

GLY 47 THR 48 0.0001

THR 48 ALA 49 0.0375

ALA 49 ASP 50 -0.0003

ASP 50 PRO 51 -0.0287

PRO 51 VAL 52 0.0000

VAL 52 ARG 53 -0.0303

ARG 53 VAL 54 0.0000

VAL 54 SER 55 -0.0018

SER 55 LYS 56 -0.0000

LYS 56 VAL 57 0.0228

VAL 57 VAL 58 -0.0002

VAL 58 LYS 59 0.0073

LYS 59 GLY 60 0.0005

GLY 60 GLY 61 0.0877

GLY 61 SER 62 -0.0002

SER 62 SER 63 -0.0421

SER 63 GLY 64 0.0002

GLY 64 LYS 65 -0.0219

LYS 65 GLY 66 -0.0000

GLY 66 THR 67 -0.0042

THR 67 THR 68 -0.0005

THR 68 LEU 69 -0.0044

LEU 69 ARG 70 -0.0001

ARG 70 GLY 71 0.1159

GLY 71 ARG 72 0.0000

ARG 72 SER 73 0.1087

SER 73 ASP 74 -0.0002

ASP 74 ALA 75 0.0861

ALA 75 ASP 76 0.0002

ASP 76 LEU 77 0.0834

LEU 77 VAL 78 -0.0004

VAL 78 VAL 79 0.0160

VAL 79 PHE 80 0.0001

PHE 80 LEU 81 -0.0095

LEU 81 THR 82 0.0001

THR 82 LYS 83 -0.0069

LYS 83 LEU 84 0.0002

LEU 84 THR 85 0.0148

THR 85 SER 86 -0.0000

SER 86 PHE 87 0.0231

PHE 87 GLU 88 0.0004

GLU 88 ASP 89 0.0137

ASP 89 GLN 90 -0.0002

GLN 90 LEU 91 0.0012

LEU 91 ARG 92 0.0002

ARG 92 ARG 93 -0.0077

ARG 93 ARG 94 0.0001

ARG 94 GLY 95 -0.0179

GLY 95 GLU 96 0.0000

GLU 96 PHE 97 -0.0050

PHE 97 ILE 98 0.0001

ILE 98 GLN 99 -0.0035

GLN 99 GLU 100 0.0002

GLU 100 ILE 101 0.0190

ILE 101 ARG 102 0.0001

ARG 102 ARG 103 0.0215

ARG 103 GLN 104 0.0004

GLN 104 LEU 105 0.0356

LEU 105 GLU 106 0.0002

GLU 106 ALA 107 0.0039

ALA 107 CYS 108 0.0002

CYS 108 GLN 109 0.0091

GLN 109 ARG 110 -0.0003

ARG 110 GLU 111 -0.0005

GLU 111 GLN 112 0.0003

GLN 112 LYS 113 0.0060

LYS 113 PHE 114 0.0001

PHE 114 LYS 115 -0.0198

LYS 115 VAL 116 -0.0000

VAL 116 THR 117 -0.0148

THR 117 PHE 118 -0.0001

PHE 118 GLU 119 -0.0087

GLU 119 VAL 120 0.0001

VAL 120 GLN 121 -0.0284

GLN 121 SER 122 0.0002

SER 122 PRO 123 0.0458

PRO 123 ARG 124 0.0002

ARG 124 ARG 125 0.0277

ARG 125 GLU 126 0.0001

GLU 126 ASN 127 -0.0483

ASN 127 PRO 128 -0.0001

PRO 128 ARG 129 0.0013

ARG 129 ALA 130 0.0002

ALA 130 LEU 131 -0.1540

LEU 131 SER 132 0.0002

SER 132 PHE 133 -0.0469

PHE 133 VAL 134 -0.0004

VAL 134 LEU 135 -0.0111

LEU 135 SER 136 0.0001

SER 136 SER 137 -0.0397

SER 137 PRO 138 -0.0001

PRO 138 GLN 139 0.0061

GLN 139 LEU 140 0.0001

LEU 140 GLN 141 0.0032

GLN 141 GLN 142 0.0002

GLN 142 GLU 143 0.0421

GLU 143 VAL 144 0.0003

VAL 144 GLU 145 -0.0228

GLU 145 PHE 146 0.0001

PHE 146 ASP 147 -0.0123

ASP 147 VAL 148 0.0001

VAL 148 LEU 149 0.0037

LEU 149 PRO 150 0.0001

PRO 150 ALA 151 -0.0161

ALA 151 PHE 152 0.0004

PHE 152 ASP 153 -0.0191

ASP 153 ALA 154 0.0004

ALA 154 LEU 155 -0.0446

LEU 155 GLY 156 0.0002

GLY 156 GLN 157 0.0840

GLN 157 TRP 158 0.0003

TRP 158 THR 159 -0.0526

THR 159 PRO 160 0.0004

PRO 160 GLY 161 0.0169

GLY 161 TYR 162 0.0001

TYR 162 LYS 163 0.0545

LYS 163 PRO 164 0.0000

PRO 164 ASN 165 0.0205

ASN 165 PRO 166 -0.0002

PRO 166 GLU 167 -0.0303

GLU 167 ILE 168 0.0002

ILE 168 TYR 169 0.0237

TYR 169 VAL 170 -0.0000

VAL 170 GLN 171 -0.0244

GLN 171 LEU 172 0.0001

LEU 172 ILE 173 -0.0127

ILE 173 LYS 174 -0.0003

LYS 174 GLU 175 -0.0320

GLU 175 CYS 176 0.0003

CYS 176 LYS 177 0.0114

LYS 177 SER 178 0.0003

SER 178 ARG 179 -0.0251

ARG 179 GLY 180 -0.0002

GLY 180 LYS 181 -0.0124

LYS 181 GLU 182 -0.0003

GLU 182 GLY 183 -0.0008

GLY 183 GLU 184 0.0002

GLU 184 PHE 185 0.0179

PHE 185 SER 186 0.0000

SER 186 THR 187 -0.0595

THR 187 CYS 188 0.0001

CYS 188 PHE 189 -0.0199

PHE 189 THR 190 0.0001

THR 190 GLU 191 0.0084

GLU 191 LEU 192 0.0001

LEU 192 GLN 193 0.0219

GLN 193 ARG 194 -0.0001

ARG 194 ARG 194 0.1147

ARG 194 ASP 195 0.0112

ASP 195 PHE 196 -0.0001

PHE 196 LEU 197 -0.0693

LEU 197 ARG 198 -0.0003

ARG 198 ASN 199 -0.0074

ASN 199 ARG 200 -0.0003

ARG 200 PRO 201 -0.1320

PRO 201 THR 202 0.0006

THR 202 LYS 203 -0.0030

LYS 203 LEU 204 0.0001

LEU 204 LYS 205 0.0262

LYS 205 SER 206 -0.0001

SER 206 LEU 207 -0.0026

LEU 207 ILE 208 -0.0002

ILE 208 ARG 209 -0.0024

ARG 209 LEU 210 0.0001

LEU 210 VAL 211 -0.0010

VAL 211 LYS 212 0.0001

LYS 212 HIS 213 0.0537

HIS 213 TRP 214 -0.0003

TRP 214 TYR 215 0.0324

TYR 215 GLN 216 0.0001

GLN 216 THR 217 0.0361

THR 217 CYS 218 -0.0002

CYS 218 LYS 219 0.0221

LYS 219 LYS 220 0.0000

LYS 220 THR 221 -0.0068

THR 221 HIS 222 0.0000

HIS 222 GLY 223 0.0240

GLY 223 ASN 224 -0.0002

ASN 224 LYS 225 -0.0197

LYS 225 LEU 226 0.0002

LEU 226 PRO 227 0.0717

PRO 227 PRO 228 -0.0002

PRO 228 GLN 229 -0.0625

GLN 229 TYR 230 -0.0002

TYR 230 ALA 231 -0.0156

ALA 231 LEU 232 -0.0001

LEU 232 GLU 233 -0.0042

GLU 233 LEU 234 0.0002

LEU 234 LEU 235 0.0139

LEU 235 THR 236 0.0002

THR 236 VAL 237 -0.0070

VAL 237 TYR 238 -0.0003

TYR 238 ALA 239 -0.0335

ALA 239 TRP 240 -0.0001

TRP 240 GLU 241 -0.0161

GLU 241 GLN 242 0.0002

GLN 242 GLY 243 -0.0277

GLY 243 SER 244 -0.0006

SER 244 ARG 245 -0.0064

ARG 245 LYS 246 0.0000

LYS 246 THR 247 0.0130

THR 247 ASP 248 0.0003

ASP 248 PHE 249 -0.0132

PHE 249 SER 250 -0.0003

SER 250 THR 251 0.0166

THR 251 ALA 252 0.0000

ALA 252 GLN 253 -0.0021

GLN 253 GLY 254 0.0002

GLY 254 PHE 255 -0.0109

PHE 255 GLN 256 -0.0002

GLN 256 THR 257 -0.0175

THR 257 VAL 258 -0.0001

VAL 258 LEU 259 -0.0065

LEU 259 GLU 260 -0.0000

GLU 260 LEU 261 0.0035

LEU 261 VAL 262 -0.0005

VAL 262 LEU 263 -0.0044

LEU 263 LYS 264 -0.0000

LYS 264 HIS 265 0.0175

HIS 265 GLN 266 -0.0004

GLN 266 LYS 267 -0.0368

LYS 267 LEU 268 -0.0003

LEU 268 CYS 269 -0.0551

CYS 269 ILE 270 0.0004

ILE 270 PHE 271 -0.0468

PHE 271 TRP 272 -0.0001

TRP 272 GLU 273 -0.0680

GLU 273 ALA 274 -0.0000

ALA 274 TYR 275 -0.0259

TYR 275 TYR 276 0.0000

TYR 276 ASP 277 0.0343

ASP 277 PHE 278 -0.0002

PHE 278 THR 279 -0.0304

THR 279 ASN 280 0.0001

ASN 280 PRO 281 0.0338

PRO 281 VAL 282 -0.0006

VAL 282 VAL 283 -0.0074

VAL 283 GLY 284 0.0001

GLY 284 ARG 285 0.0074

ARG 285 CYS 286 -0.0001

CYS 286 MET 287 -0.0243

MET 287 LEU 288 0.0002

LEU 288 GLN 289 0.0016

GLN 289 GLN 290 0.0001

GLN 290 LEU 291 -0.0183

LEU 291 LYS 292 -0.0000

LYS 292 LYS 293 0.0015

LYS 293 PRO 294 -0.0001

PRO 294 ARG 295 0.0279

ARG 295 PRO 296 -0.0004

PRO 296 VAL 297 0.0379

VAL 297 ILE 298 -0.0003

ILE 298 LEU 299 0.0288

LEU 299 ASP 300 0.0001

ASP 300 PRO 301 0.0376

PRO 301 ALA 302 0.0001

ALA 302 ASP 303 -0.0212

ASP 303 PRO 304 -0.0001

PRO 304 THR 305 -0.0178

THR 305 GLY 306 0.0001

GLY 306 ASN 307 0.1512

ASN 307 VAL 308 0.0001

VAL 308 GLY 309 0.0676

GLY 309 GLY 310 -0.0001

GLY 310 GLY 311 -0.0570

GLY 311 ASP 312 -0.0002

ASP 312 THR 313 0.0075

THR 313 HIS 314 -0.0001

HIS 314 SER 315 -0.0115

SER 315 TRP 316 0.0003

TRP 316 GLN 317 0.0141

GLN 317 ARG 318 0.0001

ARG 318 LEU 319 -0.0145

LEU 319 ALA 320 -0.0002

ALA 320 GLN 321 -0.0085

GLN 321 GLU 322 -0.0002

GLU 322 ALA 323 -0.0082

ALA 323 ARG 324 0.0001

ARG 324 VAL 325 -0.0032

VAL 325 TRP 326 -0.0000

TRP 326 LEU 327 0.0066

LEU 327 GLY 328 -0.0002

GLY 328 TYR 329 0.0002

TYR 329 PRO 330 0.0001

PRO 330 CYS 331 -0.0066

CYS 331 CYS 332 0.0001

CYS 332 LYS 333 -0.0013

LYS 333 ASN 334 0.0001

ASN 334 LEU 335 -0.0265

LEU 335 ASP 336 0.0001

ASP 336 GLY 337 0.0408

GLY 337 SER 338 0.0000

SER 338 LEU 339 0.0040

LEU 339 VAL 340 0.0002

VAL 340 GLY 341 -0.0262

GLY 341 ALA 342 -0.0002

ALA 342 TRP 343 -0.0325

TRP 343 THR 344 0.0002

THR 344 MET 345 -0.0226

MET 345 LEU 346 0.0000

LEU 346 GLN 347 -0.0047

GLN 347 LYS 348 0.0002

LYS 348 ILE 349 -0.0027

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.

*** TRANSFERASE/RNA 05-DEC-14 4RWN ***

CA strain for 22121617313095401

--- normal mode 8 ---

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

* TRANSFERASE/RNA 05-DEC-14 4RWN *