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

* TRANSFERASE 05-DEC-14 4RWQ *

CA strain for 2401161742511318419

--- normal mode 11 ---

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 -0.0003

GLU 2 LEU 3 -0.0472

LEU 3 ARG 4 -0.0003

ARG 4 HIS 5 -0.0105

HIS 5 THR 6 -0.0002

THR 6 PRO 7 -0.1144

PRO 7 ALA 8 -0.0000

ALA 8 ARG 9 0.1184

ARG 9 ASP 10 -0.0002

ASP 10 LEU 11 -0.0635

LEU 11 ASP 12 0.0002

ASP 12 LYS 13 0.0142

LYS 13 PHE 14 0.0001

PHE 14 ILE 15 -0.0778

ILE 15 GLU 16 0.0001

GLU 16 ASP 17 0.0122

ASP 17 HIS 18 0.0002

HIS 18 LEU 19 0.0421

LEU 19 LEU 20 0.0003

LEU 20 PRO 21 -0.2999

PRO 21 ASN 22 0.0001

ASN 22 THR 23 0.0438

THR 23 CYS 24 0.0003

CYS 24 PHE 25 0.1287

PHE 25 ARG 26 0.0001

ARG 26 THR 27 0.0604

THR 27 GLN 28 -0.0000

GLN 28 VAL 29 -0.0040

VAL 29 LYS 30 -0.0001

LYS 30 GLU 31 0.0511

GLU 31 ALA 32 -0.0000

ALA 32 ILE 33 -0.0826

ILE 33 ASP 34 0.0001

ASP 34 ILE 35 0.0555

ILE 35 VAL 36 0.0002

VAL 36 CYS 37 -0.0466

CYS 37 ARG 38 0.0002

ARG 38 PHE 39 0.0154

PHE 39 LEU 40 -0.0001

LEU 40 LYS 41 0.0051

LYS 41 GLU 42 -0.0001

GLU 42 ARG 43 0.0235

ARG 43 CYS 44 0.0001

CYS 44 PHE 45 -0.0334

PHE 45 GLN 46 -0.0003

GLN 46 GLY 47 -0.0040

GLY 47 THR 48 0.0003

THR 48 ALA 49 -0.0343

ALA 49 ASP 50 -0.0002

ASP 50 PRO 51 0.0171

PRO 51 VAL 52 0.0005

VAL 52 ARG 53 -0.1114

ARG 53 VAL 54 -0.0003

VAL 54 SER 55 0.2059

SER 55 LYS 56 -0.0000

LYS 56 VAL 57 -0.0869

VAL 57 VAL 58 0.0002

VAL 58 LYS 59 -0.0193

LYS 59 GLY 60 0.0000

GLY 60 GLY 61 0.0632

GLY 61 SER 62 0.0001

SER 62 SER 63 -0.0536

SER 63 GLY 64 -0.0002

GLY 64 LYS 65 -0.0793

LYS 65 GLY 66 -0.0001

GLY 66 THR 67 -0.0205

THR 67 THR 68 -0.0004

THR 68 LEU 69 -0.0980

LEU 69 ARG 70 -0.0004

ARG 70 GLY 71 -0.3176

GLY 71 ARG 72 0.0003

ARG 72 SER 73 -0.0402

SER 73 ASP 74 -0.0001

ASP 74 ALA 75 -0.0513

ALA 75 ASP 76 0.0000

ASP 76 LEU 77 0.0576

LEU 77 VAL 78 0.0002

VAL 78 VAL 79 0.0094

VAL 79 PHE 80 0.0000

PHE 80 LEU 81 0.0167

LEU 81 THR 82 0.0001

THR 82 LYS 83 -0.0563

LYS 83 LEU 84 -0.0005

LEU 84 THR 85 -0.0051

THR 85 SER 86 -0.0002

SER 86 PHE 87 0.0419

PHE 87 GLU 88 -0.0001

GLU 88 ASP 89 0.0291

ASP 89 GLN 90 0.0001

GLN 90 LEU 91 -0.0085

LEU 91 ARG 92 -0.0003

ARG 92 ARG 93 -0.0262

ARG 93 ARG 94 -0.0004

ARG 94 GLY 95 -0.0082

GLY 95 GLU 96 0.0001

GLU 96 PHE 97 0.0227

PHE 97 ILE 98 0.0000

ILE 98 GLN 99 -0.0450

GLN 99 GLU 100 0.0000

GLU 100 ILE 101 -0.0016

ILE 101 ARG 102 -0.0002

ARG 102 ARG 103 -0.0689

ARG 103 GLN 104 -0.0003

GLN 104 LEU 105 -0.0126

LEU 105 GLU 106 -0.0002

GLU 106 ALA 107 -0.0342

ALA 107 CYS 108 0.0001

CYS 108 GLN 109 -0.0152

GLN 109 ARG 110 0.0001

ARG 110 GLU 111 -0.0180

GLU 111 GLN 112 -0.0002

GLN 112 LYS 113 -0.0161

LYS 113 PHE 114 -0.0002

PHE 114 LYS 115 -0.0603

LYS 115 VAL 116 0.0000

VAL 116 THR 117 0.1463

THR 117 PHE 118 0.0000

PHE 118 GLU 119 0.1244

GLU 119 VAL 120 0.0001

VAL 120 GLN 121 0.0104

GLN 121 SER 122 -0.0004

SER 122 PRO 123 0.0286

PRO 123 ARG 124 -0.0000

ARG 124 ARG 125 0.0030

ARG 125 GLU 126 0.0003

GLU 126 ASN 127 -0.0560

ASN 127 PRO 128 0.0002

PRO 128 ARG 129 -0.1165

ARG 129 ALA 130 0.0002

ALA 130 LEU 131 0.0776

LEU 131 SER 132 -0.0002

SER 132 PHE 133 0.1107

PHE 133 VAL 134 0.0003

VAL 134 LEU 135 0.1322

LEU 135 SER 136 -0.0002

SER 136 SER 137 0.0981

SER 137 PRO 138 -0.0001

PRO 138 GLN 139 -0.0069

GLN 139 LEU 140 0.0000

LEU 140 GLN 141 0.0311

GLN 141 GLN 142 0.0001

GLN 142 GLU 143 0.0725

GLU 143 VAL 144 0.0000

VAL 144 GLU 145 0.0691

GLU 145 PHE 146 0.0003

PHE 146 ASP 147 0.0511

ASP 147 VAL 148 -0.0001

VAL 148 LEU 149 0.0360

LEU 149 PRO 150 -0.0001

PRO 150 ALA 151 0.0680

ALA 151 PHE 152 0.0004

PHE 152 ASP 153 -0.0124

ASP 153 ALA 154 -0.0003

ALA 154 LEU 155 0.0308

LEU 155 GLY 156 0.0002

GLY 156 GLN 157 0.0643

GLN 157 TRP 158 -0.0002

TRP 158 THR 159 -0.0069

THR 159 PRO 160 0.0003

PRO 160 GLY 161 -0.0346

GLY 161 TYR 162 -0.0001

TYR 162 LYS 163 0.0672

LYS 163 PRO 164 -0.0003

PRO 164 ASN 165 -0.0749

ASN 165 PRO 166 0.0000

PRO 166 GLU 167 -0.0160

GLU 167 ILE 168 -0.0001

ILE 168 TYR 169 0.0449

TYR 169 VAL 170 -0.0003

VAL 170 GLN 171 0.0498

GLN 171 LEU 172 0.0000

LEU 172 ILE 173 -0.0018

ILE 173 LYS 174 -0.0003

LYS 174 GLU 175 0.0583

GLU 175 CYS 176 -0.0000

CYS 176 LYS 177 0.0239

LYS 177 SER 178 -0.0002

SER 178 ARG 179 -0.0022

ARG 179 GLY 180 -0.0001

GLY 180 LYS 181 0.0735

LYS 181 GLU 182 -0.0002

GLU 182 GLY 183 0.0263

GLY 183 GLU 184 0.0002

GLU 184 PHE 185 0.0240

PHE 185 SER 186 0.0001

SER 186 THR 187 0.0487

THR 187 CYS 188 -0.0001

CYS 188 PHE 189 0.0829

PHE 189 THR 190 -0.0001

THR 190 GLU 191 -0.0805

GLU 191 LEU 192 0.0003

LEU 192 GLN 193 0.0336

GLN 193 ARG 194 -0.0002

ARG 194 ASP 195 -0.1048

ASP 195 PHE 196 -0.0004

PHE 196 LEU 197 -0.2206

LEU 197 ARG 198 0.0002

ARG 198 ASN 199 0.1340

ASN 199 ARG 200 0.0004

ARG 200 PRO 201 -0.0793

PRO 201 THR 202 0.0003

THR 202 LYS 203 -0.1010

LYS 203 LEU 204 0.0000

LEU 204 LYS 205 -0.0305

LYS 205 SER 206 0.0002

SER 206 LEU 207 -0.1243

LEU 207 ILE 208 -0.0001

ILE 208 ARG 209 -0.2011

ARG 209 LEU 210 0.0003

LEU 210 VAL 211 0.0200

VAL 211 LYS 212 -0.0003

LYS 212 HIS 213 -0.1035

HIS 213 TRP 214 0.0000

TRP 214 TYR 215 0.0254

TYR 215 GLN 216 0.0000

GLN 216 THR 217 -0.0535

THR 217 CYS 218 0.0000

CYS 218 LYS 219 -0.0208

LYS 219 LYS 220 -0.0001

LYS 220 THR 221 0.1187

THR 221 HIS 222 -0.0002

HIS 222 GLY 223 -0.0570

GLY 223 ASN 224 -0.0002

ASN 224 LYS 225 -0.0165

LYS 225 LEU 226 0.0002

LEU 226 PRO 227 0.0497

PRO 227 PRO 228 0.0002

PRO 228 GLN 229 0.0073

GLN 229 TYR 230 0.0001

TYR 230 ALA 231 0.0568

ALA 231 LEU 232 -0.0002

LEU 232 GLU 233 -0.0517

GLU 233 LEU 234 -0.0005

LEU 234 LEU 235 0.1274

LEU 235 THR 236 -0.0001

THR 236 VAL 237 -0.0310

VAL 237 TYR 238 0.0002

TYR 238 ALA 239 0.1871

ALA 239 TRP 240 0.0002

TRP 240 GLU 241 -0.0441

GLU 241 GLN 242 0.0001

GLN 242 GLY 243 0.0567

GLY 243 SER 244 -0.0003

SER 244 ARG 245 0.0045

ARG 245 LYS 246 -0.0000

LYS 246 THR 247 -0.0217

THR 247 ASP 248 0.0004

ASP 248 PHE 249 -0.0149

PHE 249 SER 250 -0.0002

SER 250 THR 251 0.0045

THR 251 ALA 252 -0.0001

ALA 252 GLN 253 0.0440

GLN 253 GLY 254 0.0002

GLY 254 PHE 255 -0.0234

PHE 255 GLN 256 -0.0000

GLN 256 THR 257 0.0927

THR 257 VAL 258 0.0002

VAL 258 LEU 259 -0.0820

LEU 259 GLU 260 -0.0004

GLU 260 LEU 261 0.1777

LEU 261 VAL 262 0.0003

VAL 262 LEU 263 -0.0495

LEU 263 LYS 264 -0.0003

LYS 264 HIS 265 0.0838

HIS 265 GLN 266 0.0002

GLN 266 LYS 267 -0.0570

LYS 267 LEU 268 0.0002

LEU 268 CYS 269 0.2241

CYS 269 ILE 270 0.0001

ILE 270 PHE 271 0.0463

PHE 271 TRP 272 -0.0003

TRP 272 GLU 273 -0.0207

GLU 273 ALA 274 -0.0001

ALA 274 TYR 275 0.0342

TYR 275 TYR 276 -0.0001

TYR 276 ASP 277 -0.0527

ASP 277 PHE 278 0.0002

PHE 278 THR 279 0.0096

THR 279 ASN 280 -0.0002

ASN 280 PRO 281 0.0259

PRO 281 VAL 282 0.0003

VAL 282 VAL 283 -0.0490

VAL 283 GLY 284 -0.0002

GLY 284 ARG 285 -0.0102

ARG 285 CYS 286 -0.0002

CYS 286 MET 287 0.0135

MET 287 LEU 288 0.0001

LEU 288 GLN 289 -0.0600

GLN 289 GLN 290 0.0001

GLN 290 LEU 291 0.0565

LEU 291 LYS 292 0.0004

LYS 292 LYS 293 -0.0391

LYS 293 PRO 294 -0.0001

PRO 294 ARG 295 0.0893

ARG 295 PRO 296 -0.0001

PRO 296 VAL 297 0.1438

VAL 297 ILE 298 0.0001

ILE 298 LEU 299 0.1246

LEU 299 ASP 300 -0.0001

ASP 300 PRO 301 0.0419

PRO 301 ALA 302 -0.0002

ALA 302 ASP 303 -0.0304

ASP 303 PRO 304 0.0000

PRO 304 THR 305 -0.0417

THR 305 GLY 306 0.0002

GLY 306 ASN 307 0.3122

ASN 307 VAL 308 -0.0000

VAL 308 GLY 309 0.2106

GLY 309 GLY 310 0.0002

GLY 310 GLY 311 -0.0424

GLY 311 ASP 312 -0.0002

ASP 312 THR 313 -0.0130

THR 313 HIS 314 0.0001

HIS 314 SER 315 0.0287

SER 315 TRP 316 0.0001

TRP 316 GLN 317 0.0474

GLN 317 ARG 318 0.0001

ARG 318 LEU 319 -0.0395

LEU 319 ALA 320 0.0001

ALA 320 GLN 321 -0.0057

GLN 321 GLU 322 0.0003

GLU 322 ALA 323 -0.0805

ALA 323 ARG 324 0.0000

ARG 324 VAL 325 0.1378

VAL 325 TRP 326 0.0003

TRP 326 LEU 327 -0.0584

LEU 327 GLY 328 -0.0001

GLY 328 TYR 329 0.0502

TYR 329 PRO 330 -0.0000

PRO 330 CYS 331 -0.0201

CYS 331 CYS 332 -0.0001

CYS 332 LYS 333 0.0092

LYS 333 ASN 334 -0.0001

ASN 334 LEU 335 0.0644

LEU 335 ASP 336 -0.0001

ASP 336 GLY 337 -0.1486

GLY 337 SER 338 -0.0001

SER 338 LEU 339 0.0926

LEU 339 VAL 340 -0.0002

VAL 340 GLY 341 0.2799

GLY 341 ALA 342 -0.0003

ALA 342 TRP 343 0.1170

TRP 343 THR 344 -0.0000

THR 344 MET 345 0.0877

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 25th, 2023.

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

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

CA strain for 2401161742511318419

--- normal mode 11 ---

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

* TRANSFERASE 05-DEC-14 4RWQ *