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

* TRANSFERASE 05-DEC-14 4RWQ *

CA strain for 2401161742511318419

--- normal mode 10 ---

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 0.0314

LEU 3 ARG 4 0.0000

ARG 4 HIS 5 0.0016

HIS 5 THR 6 0.0003

THR 6 PRO 7 0.1323

PRO 7 ALA 8 -0.0001

ALA 8 ARG 9 -0.0301

ARG 9 ASP 10 0.0000

ASP 10 LEU 11 0.0234

LEU 11 ASP 12 -0.0002

ASP 12 LYS 13 -0.0068

LYS 13 PHE 14 -0.0000

PHE 14 ILE 15 0.0062

ILE 15 GLU 16 -0.0000

GLU 16 ASP 17 -0.0277

ASP 17 HIS 18 -0.0002

HIS 18 LEU 19 -0.0508

LEU 19 LEU 20 0.0001

LEU 20 PRO 21 0.0463

PRO 21 ASN 22 -0.0004

ASN 22 THR 23 0.0256

THR 23 CYS 24 -0.0001

CYS 24 PHE 25 0.0172

PHE 25 ARG 26 0.0002

ARG 26 THR 27 0.0781

THR 27 GLN 28 -0.0003

GLN 28 VAL 29 -0.0939

VAL 29 LYS 30 -0.0003

LYS 30 GLU 31 -0.0385

GLU 31 ALA 32 0.0002

ALA 32 ILE 33 -0.1170

ILE 33 ASP 34 0.0003

ASP 34 ILE 35 -0.0077

ILE 35 VAL 36 -0.0002

VAL 36 CYS 37 -0.1198

CYS 37 ARG 38 0.0000

ARG 38 PHE 39 -0.0017

PHE 39 LEU 40 -0.0000

LEU 40 LYS 41 -0.0303

LYS 41 GLU 42 -0.0000

GLU 42 ARG 43 -0.0106

ARG 43 CYS 44 0.0000

CYS 44 PHE 45 0.0185

PHE 45 GLN 46 -0.0004

GLN 46 GLY 47 0.0182

GLY 47 THR 48 -0.0005

THR 48 ALA 49 0.0123

ALA 49 ASP 50 -0.0000

ASP 50 PRO 51 0.0041

PRO 51 VAL 52 -0.0000

VAL 52 ARG 53 -0.0235

ARG 53 VAL 54 -0.0000

VAL 54 SER 55 -0.0051

SER 55 LYS 56 -0.0000

LYS 56 VAL 57 -0.0009

VAL 57 VAL 58 -0.0002

VAL 58 LYS 59 0.1785

LYS 59 GLY 60 0.0004

GLY 60 GLY 61 0.2378

GLY 61 SER 62 -0.0002

SER 62 SER 63 0.1623

SER 63 GLY 64 0.0005

GLY 64 LYS 65 -0.0998

LYS 65 GLY 66 0.0003

GLY 66 THR 67 0.0636

THR 67 THR 68 0.0001

THR 68 LEU 69 0.0627

LEU 69 ARG 70 0.0001

ARG 70 GLY 71 0.1363

GLY 71 ARG 72 0.0000

ARG 72 SER 73 0.0177

SER 73 ASP 74 0.0001

ASP 74 ALA 75 0.1227

ALA 75 ASP 76 -0.0001

ASP 76 LEU 77 0.1951

LEU 77 VAL 78 -0.0005

VAL 78 VAL 79 0.0671

VAL 79 PHE 80 0.0003

PHE 80 LEU 81 0.0406

LEU 81 THR 82 0.0002

THR 82 LYS 83 0.0041

LYS 83 LEU 84 -0.0001

LEU 84 THR 85 -0.0392

THR 85 SER 86 0.0003

SER 86 PHE 87 0.0145

PHE 87 GLU 88 0.0005

GLU 88 ASP 89 0.0102

ASP 89 GLN 90 -0.0001

GLN 90 LEU 91 -0.0081

LEU 91 ARG 92 -0.0001

ARG 92 ARG 93 -0.0172

ARG 93 ARG 94 -0.0001

ARG 94 GLY 95 0.0113

GLY 95 GLU 96 0.0001

GLU 96 PHE 97 -0.0069

PHE 97 ILE 98 0.0001

ILE 98 GLN 99 -0.0078

GLN 99 GLU 100 -0.0001

GLU 100 ILE 101 -0.0290

ILE 101 ARG 102 0.0001

ARG 102 ARG 103 0.0165

ARG 103 GLN 104 -0.0003

GLN 104 LEU 105 -0.0033

LEU 105 GLU 106 0.0001

GLU 106 ALA 107 0.0243

ALA 107 CYS 108 -0.0003

CYS 108 GLN 109 -0.0326

GLN 109 ARG 110 -0.0001

ARG 110 GLU 111 -0.0208

GLU 111 GLN 112 -0.0000

GLN 112 LYS 113 -0.0047

LYS 113 PHE 114 0.0001

PHE 114 LYS 115 0.0496

LYS 115 VAL 116 0.0000

VAL 116 THR 117 0.0440

THR 117 PHE 118 0.0002

PHE 118 GLU 119 0.0756

GLU 119 VAL 120 0.0001

VAL 120 GLN 121 0.1097

GLN 121 SER 122 0.0002

SER 122 PRO 123 0.0713

PRO 123 ARG 124 0.0002

ARG 124 ARG 125 0.0007

ARG 125 GLU 126 0.0000

GLU 126 ASN 127 0.1569

ASN 127 PRO 128 0.0004

PRO 128 ARG 129 0.1171

ARG 129 ALA 130 -0.0002

ALA 130 LEU 131 -0.0732

LEU 131 SER 132 0.0001

SER 132 PHE 133 -0.0215

PHE 133 VAL 134 0.0002

VAL 134 LEU 135 -0.0347

LEU 135 SER 136 0.0003

SER 136 SER 137 -0.0131

SER 137 PRO 138 -0.0003

PRO 138 GLN 139 -0.0263

GLN 139 LEU 140 0.0000

LEU 140 GLN 141 0.0362

GLN 141 GLN 142 -0.0001

GLN 142 GLU 143 -0.0633

GLU 143 VAL 144 -0.0002

VAL 144 GLU 145 -0.0517

GLU 145 PHE 146 -0.0003

PHE 146 ASP 147 0.0618

ASP 147 VAL 148 0.0001

VAL 148 LEU 149 0.0725

LEU 149 PRO 150 0.0002

PRO 150 ALA 151 0.0369

ALA 151 PHE 152 -0.0002

PHE 152 ASP 153 0.0142

ASP 153 ALA 154 -0.0000

ALA 154 LEU 155 0.0603

LEU 155 GLY 156 0.0002

GLY 156 GLN 157 0.0276

GLN 157 TRP 158 -0.0001

TRP 158 THR 159 0.0075

THR 159 PRO 160 -0.0004

PRO 160 GLY 161 -0.0099

GLY 161 TYR 162 0.0000

TYR 162 LYS 163 0.0705

LYS 163 PRO 164 -0.0000

PRO 164 ASN 165 -0.0442

ASN 165 PRO 166 0.0000

PRO 166 GLU 167 0.0061

GLU 167 ILE 168 0.0001

ILE 168 TYR 169 -0.0254

TYR 169 VAL 170 0.0000

VAL 170 GLN 171 0.0403

GLN 171 LEU 172 0.0001

LEU 172 ILE 173 -0.0292

ILE 173 LYS 174 0.0002

LYS 174 GLU 175 0.0751

GLU 175 CYS 176 0.0000

CYS 176 LYS 177 0.0045

LYS 177 SER 178 0.0001

SER 178 ARG 179 0.0230

ARG 179 GLY 180 -0.0002

GLY 180 LYS 181 0.0550

LYS 181 GLU 182 0.0001

GLU 182 GLY 183 0.0213

GLY 183 GLU 184 0.0003

GLU 184 PHE 185 0.0371

PHE 185 SER 186 0.0000

SER 186 THR 187 -0.0624

THR 187 CYS 188 -0.0001

CYS 188 PHE 189 -0.0201

PHE 189 THR 190 -0.0002

THR 190 GLU 191 0.0035

GLU 191 LEU 192 -0.0001

LEU 192 GLN 193 0.0148

GLN 193 ARG 194 0.0000

ARG 194 ASP 195 -0.1490

ASP 195 PHE 196 -0.0001

PHE 196 LEU 197 0.0087

LEU 197 ARG 198 -0.0002

ARG 198 ASN 199 0.0119

ASN 199 ARG 200 0.0001

ARG 200 PRO 201 -0.0585

PRO 201 THR 202 0.0004

THR 202 LYS 203 -0.0090

LYS 203 LEU 204 0.0001

LEU 204 LYS 205 -0.0465

LYS 205 SER 206 0.0001

SER 206 LEU 207 -0.0351

LEU 207 ILE 208 -0.0001

ILE 208 ARG 209 -0.0871

ARG 209 LEU 210 0.0002

LEU 210 VAL 211 -0.0152

VAL 211 LYS 212 -0.0000

LYS 212 HIS 213 0.0354

HIS 213 TRP 214 -0.0002

TRP 214 TYR 215 0.0416

TYR 215 GLN 216 -0.0002

GLN 216 THR 217 0.1898

THR 217 CYS 218 -0.0001

CYS 218 LYS 219 0.0360

LYS 219 LYS 220 0.0001

LYS 220 THR 221 0.2091

THR 221 HIS 222 0.0001

HIS 222 GLY 223 -0.0792

GLY 223 ASN 224 0.0001

ASN 224 LYS 225 -0.0200

LYS 225 LEU 226 0.0003

LEU 226 PRO 227 0.0926

PRO 227 PRO 228 0.0002

PRO 228 GLN 229 -0.0143

GLN 229 TYR 230 0.0001

TYR 230 ALA 231 -0.0041

ALA 231 LEU 232 0.0000

LEU 232 GLU 233 -0.0097

GLU 233 LEU 234 0.0003

LEU 234 LEU 235 -0.0387

LEU 235 THR 236 0.0001

THR 236 VAL 237 -0.0480

VAL 237 TYR 238 0.0001

TYR 238 ALA 239 -0.1541

ALA 239 TRP 240 0.0001

TRP 240 GLU 241 -0.0186

GLU 241 GLN 242 -0.0004

GLN 242 GLY 243 -0.0416

GLY 243 SER 244 0.0002

SER 244 ARG 245 -0.0058

ARG 245 LYS 246 -0.0002

LYS 246 THR 247 0.0086

THR 247 ASP 248 0.0006

ASP 248 PHE 249 0.0021

PHE 249 SER 250 -0.0002

SER 250 THR 251 0.0254

THR 251 ALA 252 0.0000

ALA 252 GLN 253 -0.0047

GLN 253 GLY 254 0.0004

GLY 254 PHE 255 -0.0076

PHE 255 GLN 256 -0.0000

GLN 256 THR 257 -0.0436

THR 257 VAL 258 -0.0001

VAL 258 LEU 259 -0.0050

LEU 259 GLU 260 0.0002

GLU 260 LEU 261 -0.0600

LEU 261 VAL 262 0.0002

VAL 262 LEU 263 0.0253

LEU 263 LYS 264 0.0000

LYS 264 HIS 265 0.0038

HIS 265 GLN 266 -0.0000

GLN 266 LYS 267 0.0082

LYS 267 LEU 268 0.0003

LEU 268 CYS 269 -0.1709

CYS 269 ILE 270 -0.0001

ILE 270 PHE 271 -0.1185

PHE 271 TRP 272 -0.0001

TRP 272 GLU 273 -0.1287

GLU 273 ALA 274 -0.0002

ALA 274 TYR 275 -0.0328

TYR 275 TYR 276 0.0000

TYR 276 ASP 277 -0.0275

ASP 277 PHE 278 0.0003

PHE 278 THR 279 0.0006

THR 279 ASN 280 -0.0001

ASN 280 PRO 281 -0.0077

PRO 281 VAL 282 0.0001

VAL 282 VAL 283 -0.0318

VAL 283 GLY 284 0.0002

GLY 284 ARG 285 -0.0006

ARG 285 CYS 286 0.0002

CYS 286 MET 287 -0.0422

MET 287 LEU 288 -0.0002

LEU 288 GLN 289 0.0123

GLN 289 GLN 290 -0.0001

GLN 290 LEU 291 -0.0688

LEU 291 LYS 292 -0.0002

LYS 292 LYS 293 0.0513

LYS 293 PRO 294 -0.0002

PRO 294 ARG 295 0.0261

ARG 295 PRO 296 -0.0000

PRO 296 VAL 297 0.0301

VAL 297 ILE 298 -0.0003

ILE 298 LEU 299 -0.0034

LEU 299 ASP 300 0.0002

ASP 300 PRO 301 0.0411

PRO 301 ALA 302 -0.0000

ALA 302 ASP 303 -0.0297

ASP 303 PRO 304 -0.0002

PRO 304 THR 305 -0.0125

THR 305 GLY 306 -0.0002

GLY 306 ASN 307 0.1263

ASN 307 VAL 308 0.0001

VAL 308 GLY 309 0.1383

GLY 309 GLY 310 0.0004

GLY 310 GLY 311 -0.0137

GLY 311 ASP 312 0.0001

ASP 312 THR 313 -0.0215

THR 313 HIS 314 -0.0002

HIS 314 SER 315 -0.0088

SER 315 TRP 316 -0.0001

TRP 316 GLN 317 0.0151

GLN 317 ARG 318 -0.0004

ARG 318 LEU 319 -0.0160

LEU 319 ALA 320 0.0000

ALA 320 GLN 321 0.0126

GLN 321 GLU 322 -0.0001

GLU 322 ALA 323 0.0000

ALA 323 ARG 324 0.0005

ARG 324 VAL 325 -0.0423

VAL 325 TRP 326 0.0001

TRP 326 LEU 327 0.0751

LEU 327 GLY 328 0.0003

GLY 328 TYR 329 -0.0167

TYR 329 PRO 330 0.0000

PRO 330 CYS 331 -0.0054

CYS 331 CYS 332 0.0001

CYS 332 LYS 333 0.0326

LYS 333 ASN 334 -0.0001

ASN 334 LEU 335 -0.0151

LEU 335 ASP 336 0.0002

ASP 336 GLY 337 0.1639

GLY 337 SER 338 0.0002

SER 338 LEU 339 -0.0616

LEU 339 VAL 340 -0.0004

VAL 340 GLY 341 -0.1247

GLY 341 ALA 342 0.0001

ALA 342 TRP 343 -0.0653

TRP 343 THR 344 0.0003

THR 344 MET 345 -0.0392

MET 345 LEU 346 -0.0002

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 10 ---

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

* TRANSFERASE 05-DEC-14 4RWQ *