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

* TRANSFERASE 05-DEC-14 4RWQ *

CA strain for 2503071135273397621

--- normal mode 9 ---

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 -0.0000

GLU 2 LEU 3 0.0173

LEU 3 ARG 4 0.0001

ARG 4 HIS 5 0.0091

HIS 5 THR 6 0.0001

THR 6 PRO 7 0.0520

PRO 7 ALA 8 0.0005

ALA 8 ARG 9 -0.0483

ARG 9 ASP 10 0.0002

ASP 10 LEU 11 0.0437

LEU 11 ASP 12 -0.0001

ASP 12 LYS 13 -0.0406

LYS 13 PHE 14 -0.0005

PHE 14 ILE 15 -0.0331

ILE 15 GLU 16 0.0003

GLU 16 ASP 17 -0.0220

ASP 17 HIS 18 -0.0003

HIS 18 LEU 19 -0.0657

LEU 19 LEU 20 -0.0001

LEU 20 PRO 21 0.2052

PRO 21 ASN 22 -0.0003

ASN 22 THR 23 -0.0065

THR 23 CYS 24 0.0000

CYS 24 PHE 25 0.0065

PHE 25 ARG 26 0.0001

ARG 26 THR 27 0.0252

THR 27 GLN 28 0.0000

GLN 28 VAL 29 -0.0293

VAL 29 LYS 30 0.0003

LYS 30 GLU 31 -0.0048

GLU 31 ALA 32 0.0001

ALA 32 ILE 33 -0.0920

ILE 33 ASP 34 0.0001

ASP 34 ILE 35 -0.0081

ILE 35 VAL 36 0.0002

VAL 36 CYS 37 -0.0904

CYS 37 ARG 38 -0.0000

ARG 38 PHE 39 -0.0454

PHE 39 LEU 40 0.0002

LEU 40 LYS 41 -0.0278

LYS 41 GLU 42 -0.0000

GLU 42 ARG 43 -0.0291

ARG 43 CYS 44 -0.0002

CYS 44 PHE 45 0.0178

PHE 45 GLN 46 0.0001

GLN 46 GLY 47 0.0173

GLY 47 THR 48 0.0003

THR 48 ALA 49 0.0061

ALA 49 ASP 50 -0.0002

ASP 50 PRO 51 0.0005

PRO 51 VAL 52 0.0002

VAL 52 ARG 53 -0.0244

ARG 53 VAL 54 0.0002

VAL 54 SER 55 -0.0308

SER 55 LYS 56 0.0003

LYS 56 VAL 57 -0.0299

VAL 57 VAL 58 0.0000

VAL 58 LYS 59 -0.0277

LYS 59 GLY 60 0.0003

GLY 60 GLY 61 -0.0478

GLY 61 SER 62 0.0001

SER 62 SER 63 -0.1367

SER 63 GLY 64 0.0000

GLY 64 LYS 65 -0.0208

LYS 65 GLY 66 0.0002

GLY 66 THR 67 0.0157

THR 67 THR 68 0.0001

THR 68 LEU 69 0.0049

LEU 69 ARG 70 0.0003

ARG 70 GLY 71 0.2184

GLY 71 ARG 72 0.0001

ARG 72 SER 73 -0.0530

SER 73 ASP 74 0.0002

ASP 74 ALA 75 -0.0614

ALA 75 ASP 76 0.0002

ASP 76 LEU 77 0.0320

LEU 77 VAL 78 -0.0003

VAL 78 VAL 79 0.0428

VAL 79 PHE 80 0.0004

PHE 80 LEU 81 0.0278

LEU 81 THR 82 0.0002

THR 82 LYS 83 0.0010

LYS 83 LEU 84 -0.0002

LEU 84 THR 85 -0.0701

THR 85 SER 86 -0.0001

SER 86 PHE 87 -0.0060

PHE 87 GLU 88 -0.0001

GLU 88 ASP 89 0.0005

ASP 89 GLN 90 -0.0004

GLN 90 LEU 91 -0.0327

LEU 91 ARG 92 0.0004

ARG 92 ARG 93 0.0315

ARG 93 ARG 94 0.0001

ARG 94 GLY 95 -0.0372

GLY 95 GLU 96 -0.0001

GLU 96 PHE 97 0.0128

PHE 97 ILE 98 0.0004

ILE 98 GLN 99 -0.0422

GLN 99 GLU 100 -0.0001

GLU 100 ILE 101 0.0115

ILE 101 ARG 102 -0.0000

ARG 102 ARG 103 -0.0983

ARG 103 GLN 104 -0.0003

GLN 104 LEU 105 0.0770

LEU 105 GLU 106 0.0000

GLU 106 ALA 107 -0.0515

ALA 107 CYS 108 -0.0001

CYS 108 GLN 109 -0.0051

GLN 109 ARG 110 -0.0001

ARG 110 GLU 111 -0.0188

GLU 111 GLN 112 0.0001

GLN 112 LYS 113 0.0351

LYS 113 PHE 114 -0.0000

PHE 114 LYS 115 0.0301

LYS 115 VAL 116 0.0001

VAL 116 THR 117 -0.0180

THR 117 PHE 118 -0.0002

PHE 118 GLU 119 -0.0656

GLU 119 VAL 120 -0.0001

VAL 120 GLN 121 -0.1511

GLN 121 SER 122 0.0005

SER 122 PRO 123 -0.0465

PRO 123 ARG 124 0.0001

ARG 124 ARG 125 -0.0355

ARG 125 GLU 126 -0.0001

GLU 126 ASN 127 -0.0299

ASN 127 PRO 128 -0.0001

PRO 128 ARG 129 -0.1498

ARG 129 ALA 130 0.0001

ALA 130 LEU 131 0.1124

LEU 131 SER 132 0.0003

SER 132 PHE 133 0.0677

PHE 133 VAL 134 -0.0001

VAL 134 LEU 135 0.0660

LEU 135 SER 136 -0.0002

SER 136 SER 137 0.0084

SER 137 PRO 138 -0.0001

PRO 138 GLN 139 0.0034

GLN 139 LEU 140 0.0004

LEU 140 GLN 141 -0.0212

GLN 141 GLN 142 -0.0004

GLN 142 GLU 143 0.0439

GLU 143 VAL 144 -0.0000

VAL 144 GLU 145 0.1422

GLU 145 PHE 146 -0.0001

PHE 146 ASP 147 0.0437

ASP 147 VAL 148 0.0000

VAL 148 LEU 149 0.0481

LEU 149 PRO 150 -0.0004

PRO 150 ALA 151 0.0721

ALA 151 PHE 152 -0.0002

PHE 152 ASP 153 0.0443

ASP 153 ALA 154 -0.0001

ALA 154 LEU 155 0.0580

LEU 155 GLY 156 0.0003

GLY 156 GLN 157 0.0306

GLN 157 TRP 158 -0.0002

TRP 158 THR 159 0.0084

THR 159 PRO 160 0.0001

PRO 160 GLY 161 -0.0176

GLY 161 TYR 162 0.0001

TYR 162 LYS 163 0.0842

LYS 163 PRO 164 -0.0002

PRO 164 ASN 165 -0.0341

ASN 165 PRO 166 -0.0000

PRO 166 GLU 167 0.0108

GLU 167 ILE 168 -0.0001

ILE 168 TYR 169 -0.0402

TYR 169 VAL 170 -0.0000

VAL 170 GLN 171 0.0322

GLN 171 LEU 172 0.0001

LEU 172 ILE 173 -0.0139

ILE 173 LYS 174 0.0002

LYS 174 GLU 175 0.0485

GLU 175 CYS 176 0.0004

CYS 176 LYS 177 -0.0001

LYS 177 SER 178 -0.0005

SER 178 ARG 179 0.0175

ARG 179 GLY 180 -0.0003

GLY 180 LYS 181 0.0329

LYS 181 GLU 182 0.0004

GLU 182 GLY 183 0.0257

GLY 183 GLU 184 0.0001

GLU 184 PHE 185 0.0101

PHE 185 SER 186 0.0003

SER 186 THR 187 0.0092

THR 187 CYS 188 0.0002

CYS 188 PHE 189 0.0271

PHE 189 THR 190 0.0001

THR 190 GLU 191 0.0005

GLU 191 LEU 192 0.0001

LEU 192 GLN 193 -0.0150

GLN 193 ARG 194 0.0004

ARG 194 ASP 195 -0.0552

ASP 195 PHE 196 -0.0003

PHE 196 LEU 197 -0.1176

LEU 197 ARG 198 0.0000

ARG 198 ASN 199 0.1296

ASN 199 ARG 200 -0.0003

ARG 200 PRO 201 -0.0111

PRO 201 THR 202 -0.0002

THR 202 LYS 203 -0.0229

LYS 203 LEU 204 -0.0000

LEU 204 LYS 205 0.0581

LYS 205 SER 206 -0.0001

SER 206 LEU 207 -0.0282

LEU 207 ILE 208 -0.0000

ILE 208 ARG 209 -0.0460

ARG 209 LEU 210 -0.0000

LEU 210 VAL 211 -0.0505

VAL 211 LYS 212 0.0001

LYS 212 HIS 213 -0.0519

HIS 213 TRP 214 0.0005

TRP 214 TYR 215 -0.0051

TYR 215 GLN 216 -0.0005

GLN 216 THR 217 0.0164

THR 217 CYS 218 -0.0000

CYS 218 LYS 219 0.0063

LYS 219 LYS 220 0.0000

LYS 220 THR 221 -0.0078

THR 221 HIS 222 -0.0002

HIS 222 GLY 223 -0.0282

GLY 223 ASN 224 -0.0004

ASN 224 LYS 225 0.0082

LYS 225 LEU 226 0.0001

LEU 226 PRO 227 0.0380

PRO 227 PRO 228 0.0002

PRO 228 GLN 229 0.0029

GLN 229 TYR 230 -0.0001

TYR 230 ALA 231 -0.0251

ALA 231 LEU 232 -0.0005

LEU 232 GLU 233 -0.0222

GLU 233 LEU 234 -0.0001

LEU 234 LEU 235 -0.0203

LEU 235 THR 236 0.0002

THR 236 VAL 237 -0.0331

VAL 237 TYR 238 -0.0002

TYR 238 ALA 239 -0.1175

ALA 239 TRP 240 0.0000

TRP 240 GLU 241 -0.0380

GLU 241 GLN 242 -0.0001

GLN 242 GLY 243 -0.0439

GLY 243 SER 244 0.0002

SER 244 ARG 245 0.0242

ARG 245 LYS 246 0.0002

LYS 246 THR 247 0.0146

THR 247 ASP 248 -0.0000

ASP 248 PHE 249 -0.0125

PHE 249 SER 250 -0.0002

SER 250 THR 251 0.0455

THR 251 ALA 252 -0.0001

ALA 252 GLN 253 -0.0023

GLN 253 GLY 254 0.0000

GLY 254 PHE 255 0.0058

PHE 255 GLN 256 0.0004

GLN 256 THR 257 -0.0258

THR 257 VAL 258 0.0003

VAL 258 LEU 259 0.0046

LEU 259 GLU 260 -0.0002

GLU 260 LEU 261 -0.0349

LEU 261 VAL 262 0.0001

VAL 262 LEU 263 0.0104

LEU 263 LYS 264 0.0000

LYS 264 HIS 265 -0.0180

HIS 265 GLN 266 0.0003

GLN 266 LYS 267 0.0208

LYS 267 LEU 268 -0.0000

LEU 268 CYS 269 -0.0200

CYS 269 ILE 270 0.0001

ILE 270 PHE 271 0.0328

PHE 271 TRP 272 0.0000

TRP 272 GLU 273 -0.0730

GLU 273 ALA 274 0.0002

ALA 274 TYR 275 0.0092

TYR 275 TYR 276 -0.0000

TYR 276 ASP 277 -0.0185

ASP 277 PHE 278 0.0002

PHE 278 THR 279 0.0306

THR 279 ASN 280 0.0001

ASN 280 PRO 281 -0.0065

PRO 281 VAL 282 -0.0004

VAL 282 VAL 283 -0.0285

VAL 283 GLY 284 -0.0001

GLY 284 ARG 285 -0.0097

ARG 285 CYS 286 -0.0001

CYS 286 MET 287 -0.0647

MET 287 LEU 288 0.0003

LEU 288 GLN 289 0.0107

GLN 289 GLN 290 -0.0001

GLN 290 LEU 291 -0.1113

LEU 291 LYS 292 0.0004

LYS 292 LYS 293 0.1223

LYS 293 PRO 294 0.0000

PRO 294 ARG 295 -0.0010

ARG 295 PRO 296 0.0003

PRO 296 VAL 297 0.0191

VAL 297 ILE 298 -0.0002

ILE 298 LEU 299 -0.0015

LEU 299 ASP 300 -0.0003

ASP 300 PRO 301 0.0161

PRO 301 ALA 302 -0.0002

ALA 302 ASP 303 -0.0171

ASP 303 PRO 304 0.0001

PRO 304 THR 305 -0.0078

THR 305 GLY 306 0.0001

GLY 306 ASN 307 -0.0505

ASN 307 VAL 308 -0.0002

VAL 308 GLY 309 -0.0239

GLY 309 GLY 310 0.0005

GLY 310 GLY 311 0.0067

GLY 311 ASP 312 0.0002

ASP 312 THR 313 -0.0322

THR 313 HIS 314 -0.0002

HIS 314 SER 315 -0.0287

SER 315 TRP 316 0.0001

TRP 316 GLN 317 -0.0030

GLN 317 ARG 318 -0.0003

ARG 318 LEU 319 -0.0019

LEU 319 ALA 320 -0.0001

ALA 320 GLN 321 -0.0212

GLN 321 GLU 322 -0.0001

GLU 322 ALA 323 -0.0032

ALA 323 ARG 324 0.0000

ARG 324 VAL 325 -0.0162

VAL 325 TRP 326 0.0002

TRP 326 LEU 327 0.0139

LEU 327 GLY 328 0.0000

GLY 328 TYR 329 0.0006

TYR 329 PRO 330 0.0001

PRO 330 CYS 331 -0.0167

CYS 331 CYS 332 -0.0001

CYS 332 LYS 333 -0.0002

LYS 333 ASN 334 -0.0001

ASN 334 LEU 335 -0.0302

LEU 335 ASP 336 0.0002

ASP 336 GLY 337 0.0744

GLY 337 SER 338 -0.0002

SER 338 LEU 339 -0.0267

LEU 339 VAL 340 0.0003

VAL 340 GLY 341 -0.0687

GLY 341 ALA 342 0.0001

ALA 342 TRP 343 -0.0164

TRP 343 THR 344 -0.0002

THR 344 MET 345 -0.0280

MET 345 LEU 346 -0.0001

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 9 ---

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

* TRANSFERASE 05-DEC-14 4RWQ *