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

* TRANSFERASE 05-DEC-14 4RWQ *

CA strain for 2503071135273397621

--- 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 0.0001

GLU 2 LEU 3 -0.0137

LEU 3 ARG 4 -0.0001

ARG 4 HIS 5 -0.0144

HIS 5 THR 6 0.0002

THR 6 PRO 7 -0.0066

PRO 7 ALA 8 0.0002

ALA 8 ARG 9 0.0028

ARG 9 ASP 10 -0.0004

ASP 10 LEU 11 -0.0064

LEU 11 ASP 12 -0.0001

ASP 12 LYS 13 -0.0092

LYS 13 PHE 14 -0.0002

PHE 14 ILE 15 0.0372

ILE 15 GLU 16 -0.0003

GLU 16 ASP 17 -0.0099

ASP 17 HIS 18 -0.0001

HIS 18 LEU 19 0.0297

LEU 19 LEU 20 -0.0001

LEU 20 PRO 21 -0.1140

PRO 21 ASN 22 -0.0001

ASN 22 THR 23 0.0254

THR 23 CYS 24 0.0002

CYS 24 PHE 25 0.0163

PHE 25 ARG 26 -0.0000

ARG 26 THR 27 0.0176

THR 27 GLN 28 -0.0001

GLN 28 VAL 29 -0.0157

VAL 29 LYS 30 0.0002

LYS 30 GLU 31 -0.0438

GLU 31 ALA 32 -0.0002

ALA 32 ILE 33 -0.0383

ILE 33 ASP 34 -0.0002

ASP 34 ILE 35 -0.0342

ILE 35 VAL 36 0.0002

VAL 36 CYS 37 -0.0647

CYS 37 ARG 38 0.0002

ARG 38 PHE 39 -0.0300

PHE 39 LEU 40 0.0000

LEU 40 LYS 41 -0.0306

LYS 41 GLU 42 -0.0001

GLU 42 ARG 43 -0.0392

ARG 43 CYS 44 -0.0002

CYS 44 PHE 45 0.0160

PHE 45 GLN 46 0.0000

GLN 46 GLY 47 0.0214

GLY 47 THR 48 0.0002

THR 48 ALA 49 -0.0108

ALA 49 ASP 50 0.0001

ASP 50 PRO 51 -0.0073

PRO 51 VAL 52 0.0004

VAL 52 ARG 53 0.0341

ARG 53 VAL 54 0.0003

VAL 54 SER 55 -0.1010

SER 55 LYS 56 -0.0002

LYS 56 VAL 57 -0.0033

VAL 57 VAL 58 0.0001

VAL 58 LYS 59 0.0320

LYS 59 GLY 60 -0.0001

GLY 60 GLY 61 -0.0527

GLY 61 SER 62 0.0001

SER 62 SER 63 -0.0734

SER 63 GLY 64 0.0002

GLY 64 LYS 65 -0.1139

LYS 65 GLY 66 -0.0001

GLY 66 THR 67 0.0392

THR 67 THR 68 -0.0001

THR 68 LEU 69 -0.0137

LEU 69 ARG 70 0.0004

ARG 70 GLY 71 -0.1281

GLY 71 ARG 72 0.0001

ARG 72 SER 73 -0.0283

SER 73 ASP 74 -0.0000

ASP 74 ALA 75 -0.1113

ALA 75 ASP 76 0.0000

ASP 76 LEU 77 -0.0569

LEU 77 VAL 78 0.0002

VAL 78 VAL 79 -0.0040

VAL 79 PHE 80 0.0001

PHE 80 LEU 81 0.0135

LEU 81 THR 82 -0.0003

THR 82 LYS 83 0.0204

LYS 83 LEU 84 -0.0003

LEU 84 THR 85 -0.0345

THR 85 SER 86 -0.0002

SER 86 PHE 87 -0.0084

PHE 87 GLU 88 -0.0000

GLU 88 ASP 89 0.0691

ASP 89 GLN 90 -0.0001

GLN 90 LEU 91 -0.0254

LEU 91 ARG 92 -0.0001

ARG 92 ARG 93 0.1169

ARG 93 ARG 94 -0.0000

ARG 94 GLY 95 -0.0030

GLY 95 GLU 96 0.0002

GLU 96 PHE 97 -0.0393

PHE 97 ILE 98 -0.0000

ILE 98 GLN 99 -0.0118

GLN 99 GLU 100 0.0002

GLU 100 ILE 101 -0.0345

ILE 101 ARG 102 -0.0000

ARG 102 ARG 103 -0.0483

ARG 103 GLN 104 -0.0000

GLN 104 LEU 105 -0.0234

LEU 105 GLU 106 -0.0001

GLU 106 ALA 107 -0.0237

ALA 107 CYS 108 -0.0002

CYS 108 GLN 109 -0.0109

GLN 109 ARG 110 0.0001

ARG 110 GLU 111 -0.0168

GLU 111 GLN 112 -0.0001

GLN 112 LYS 113 0.0435

LYS 113 PHE 114 -0.0001

PHE 114 LYS 115 0.0741

LYS 115 VAL 116 -0.0001

VAL 116 THR 117 -0.0819

THR 117 PHE 118 0.0000

PHE 118 GLU 119 -0.0524

GLU 119 VAL 120 0.0001

VAL 120 GLN 121 -0.0649

GLN 121 SER 122 -0.0002

SER 122 PRO 123 -0.0029

PRO 123 ARG 124 -0.0002

ARG 124 ARG 125 -0.0516

ARG 125 GLU 126 0.0001

GLU 126 ASN 127 0.1110

ASN 127 PRO 128 -0.0001

PRO 128 ARG 129 -0.0811

ARG 129 ALA 130 0.0002

ALA 130 LEU 131 -0.0310

LEU 131 SER 132 -0.0005

SER 132 PHE 133 -0.0334

PHE 133 VAL 134 0.0000

VAL 134 LEU 135 -0.0605

LEU 135 SER 136 -0.0001

SER 136 SER 137 -0.0486

SER 137 PRO 138 0.0001

PRO 138 GLN 139 -0.0341

GLN 139 LEU 140 -0.0000

LEU 140 GLN 141 0.0410

GLN 141 GLN 142 0.0000

GLN 142 GLU 143 -0.0992

GLU 143 VAL 144 0.0002

VAL 144 GLU 145 -0.0980

GLU 145 PHE 146 0.0001

PHE 146 ASP 147 -0.0602

ASP 147 VAL 148 -0.0001

VAL 148 LEU 149 0.0421

LEU 149 PRO 150 0.0001

PRO 150 ALA 151 0.0235

ALA 151 PHE 152 -0.0001

PHE 152 ASP 153 0.0270

ASP 153 ALA 154 -0.0000

ALA 154 LEU 155 0.0676

LEU 155 GLY 156 0.0001

GLY 156 GLN 157 0.0043

GLN 157 TRP 158 -0.0004

TRP 158 THR 159 0.0294

THR 159 PRO 160 0.0000

PRO 160 GLY 161 0.0118

GLY 161 TYR 162 0.0001

TYR 162 LYS 163 -0.0159

LYS 163 PRO 164 -0.0004

PRO 164 ASN 165 0.0196

ASN 165 PRO 166 -0.0000

PRO 166 GLU 167 0.0343

GLU 167 ILE 168 0.0001

ILE 168 TYR 169 -0.0373

TYR 169 VAL 170 0.0002

VAL 170 GLN 171 0.0263

GLN 171 LEU 172 0.0001

LEU 172 ILE 173 0.0151

ILE 173 LYS 174 0.0001

LYS 174 GLU 175 0.0745

GLU 175 CYS 176 -0.0001

CYS 176 LYS 177 -0.0164

LYS 177 SER 178 -0.0003

SER 178 ARG 179 0.0554

ARG 179 GLY 180 0.0003

GLY 180 LYS 181 -0.0040

LYS 181 GLU 182 0.0002

GLU 182 GLY 183 -0.0053

GLY 183 GLU 184 -0.0000

GLU 184 PHE 185 -0.0501

PHE 185 SER 186 -0.0000

SER 186 THR 187 0.1316

THR 187 CYS 188 -0.0000

CYS 188 PHE 189 0.0306

PHE 189 THR 190 0.0001

THR 190 GLU 191 0.0185

GLU 191 LEU 192 0.0005

LEU 192 GLN 193 -0.0095

GLN 193 ARG 194 0.0002

ARG 194 ASP 195 0.0028

ASP 195 PHE 196 0.0001

PHE 196 LEU 197 0.0850

LEU 197 ARG 198 -0.0002

ARG 198 ASN 199 -0.0915

ASN 199 ARG 200 0.0004

ARG 200 PRO 201 0.0643

PRO 201 THR 202 -0.0002

THR 202 LYS 203 0.0396

LYS 203 LEU 204 0.0001

LEU 204 LYS 205 -0.0579

LYS 205 SER 206 -0.0001

SER 206 LEU 207 -0.0150

LEU 207 ILE 208 -0.0002

ILE 208 ARG 209 -0.0262

ARG 209 LEU 210 -0.0001

LEU 210 VAL 211 -0.0103

VAL 211 LYS 212 -0.0001

LYS 212 HIS 213 0.0064

HIS 213 TRP 214 0.0000

TRP 214 TYR 215 -0.0055

TYR 215 GLN 216 0.0000

GLN 216 THR 217 0.0078

THR 217 CYS 218 0.0002

CYS 218 LYS 219 0.0171

LYS 219 LYS 220 0.0000

LYS 220 THR 221 0.0957

THR 221 HIS 222 0.0004

HIS 222 GLY 223 -0.0013

GLY 223 ASN 224 0.0001

ASN 224 LYS 225 0.0055

LYS 225 LEU 226 0.0000

LEU 226 PRO 227 -0.0717

PRO 227 PRO 228 0.0003

PRO 228 GLN 229 0.0483

GLN 229 TYR 230 0.0000

TYR 230 ALA 231 0.0275

ALA 231 LEU 232 -0.0001

LEU 232 GLU 233 0.0194

GLU 233 LEU 234 -0.0002

LEU 234 LEU 235 -0.0049

LEU 235 THR 236 -0.0004

THR 236 VAL 237 0.0380

VAL 237 TYR 238 0.0005

TYR 238 ALA 239 0.0635

ALA 239 TRP 240 0.0001

TRP 240 GLU 241 0.0223

GLU 241 GLN 242 -0.0001

GLN 242 GLY 243 0.0188

GLY 243 SER 244 -0.0001

SER 244 ARG 245 0.0001

ARG 245 LYS 246 -0.0001

LYS 246 THR 247 -0.0101

THR 247 ASP 248 -0.0001

ASP 248 PHE 249 0.0194

PHE 249 SER 250 0.0002

SER 250 THR 251 -0.0332

THR 251 ALA 252 -0.0001

ALA 252 GLN 253 -0.0149

GLN 253 GLY 254 0.0000

GLY 254 PHE 255 0.0158

PHE 255 GLN 256 -0.0000

GLN 256 THR 257 0.0179

THR 257 VAL 258 0.0005

VAL 258 LEU 259 0.0153

LEU 259 GLU 260 -0.0003

GLU 260 LEU 261 -0.0049

LEU 261 VAL 262 0.0001

VAL 262 LEU 263 0.0009

LEU 263 LYS 264 -0.0001

LYS 264 HIS 265 -0.0199

HIS 265 GLN 266 -0.0001

GLN 266 LYS 267 0.0217

LYS 267 LEU 268 -0.0001

LEU 268 CYS 269 0.0652

CYS 269 ILE 270 0.0001

ILE 270 PHE 271 0.0518

PHE 271 TRP 272 0.0002

TRP 272 GLU 273 0.1045

GLU 273 ALA 274 0.0001

ALA 274 TYR 275 0.0079

TYR 275 TYR 276 0.0000

TYR 276 ASP 277 -0.0312

ASP 277 PHE 278 -0.0002

PHE 278 THR 279 0.0063

THR 279 ASN 280 -0.0002

ASN 280 PRO 281 -0.0460

PRO 281 VAL 282 -0.0000

VAL 282 VAL 283 0.0225

VAL 283 GLY 284 0.0000

GLY 284 ARG 285 -0.0181

ARG 285 CYS 286 -0.0003

CYS 286 MET 287 0.0454

MET 287 LEU 288 0.0002

LEU 288 GLN 289 -0.0029

GLN 289 GLN 290 -0.0002

GLN 290 LEU 291 0.0525

LEU 291 LYS 292 0.0000

LYS 292 LYS 293 -0.0259

LYS 293 PRO 294 -0.0001

PRO 294 ARG 295 -0.0308

ARG 295 PRO 296 0.0000

PRO 296 VAL 297 -0.0426

VAL 297 ILE 298 -0.0003

ILE 298 LEU 299 -0.0162

LEU 299 ASP 300 0.0002

ASP 300 PRO 301 -0.0357

PRO 301 ALA 302 0.0001

ALA 302 ASP 303 0.0078

ASP 303 PRO 304 -0.0002

PRO 304 THR 305 0.0212

THR 305 GLY 306 0.0003

GLY 306 ASN 307 -0.1302

ASN 307 VAL 308 -0.0001

VAL 308 GLY 309 -0.1113

GLY 309 GLY 310 -0.0002

GLY 310 GLY 311 0.0252

GLY 311 ASP 312 0.0001

ASP 312 THR 313 0.0072

THR 313 HIS 314 -0.0004

HIS 314 SER 315 0.0219

SER 315 TRP 316 0.0004

TRP 316 GLN 317 -0.0224

GLN 317 ARG 318 -0.0003

ARG 318 LEU 319 0.0003

LEU 319 ALA 320 0.0001

ALA 320 GLN 321 0.0340

GLN 321 GLU 322 -0.0001

GLU 322 ALA 323 0.0186

ALA 323 ARG 324 0.0001

ARG 324 VAL 325 0.0035

VAL 325 TRP 326 -0.0002

TRP 326 LEU 327 0.0080

LEU 327 GLY 328 0.0000

GLY 328 TYR 329 -0.0036

TYR 329 PRO 330 -0.0003

PRO 330 CYS 331 0.0156

CYS 331 CYS 332 -0.0000

CYS 332 LYS 333 -0.0047

LYS 333 ASN 334 0.0001

ASN 334 LEU 335 0.0062

LEU 335 ASP 336 -0.0000

ASP 336 GLY 337 -0.0433

GLY 337 SER 338 0.0003

SER 338 LEU 339 0.0044

LEU 339 VAL 340 -0.0000

VAL 340 GLY 341 0.0107

GLY 341 ALA 342 -0.0001

ALA 342 TRP 343 0.0270

TRP 343 THR 344 -0.0004

THR 344 MET 345 0.0030

MET 345 LEU 346 0.0000

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 8th, 2025.

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

*** TRANSFERASE 05-DEC-14 4RWQ ***

CA strain for 2503071135273397621

--- normal mode 8 ---

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

* TRANSFERASE 05-DEC-14 4RWQ *