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

* TRANSFERASE 05-DEC-14 4RWQ *

CA strain for 2401161742511318419

--- normal mode 7 ---

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 0.0136

LEU 3 ARG 4 -0.0004

ARG 4 HIS 5 0.0071

HIS 5 THR 6 -0.0002

THR 6 PRO 7 0.0273

PRO 7 ALA 8 -0.0001

ALA 8 ARG 9 0.0155

ARG 9 ASP 10 0.0000

ASP 10 LEU 11 -0.0084

LEU 11 ASP 12 -0.0001

ASP 12 LYS 13 0.0365

LYS 13 PHE 14 -0.0004

PHE 14 ILE 15 -0.0275

ILE 15 GLU 16 0.0002

GLU 16 ASP 17 0.0172

ASP 17 HIS 18 0.0005

HIS 18 LEU 19 -0.0140

LEU 19 LEU 20 0.0001

LEU 20 PRO 21 -0.1186

PRO 21 ASN 22 0.0001

ASN 22 THR 23 -0.0096

THR 23 CYS 24 0.0001

CYS 24 PHE 25 0.0291

PHE 25 ARG 26 0.0002

ARG 26 THR 27 -0.0672

THR 27 GLN 28 0.0003

GLN 28 VAL 29 0.0424

VAL 29 LYS 30 -0.0001

LYS 30 GLU 31 0.0108

GLU 31 ALA 32 0.0003

ALA 32 ILE 33 0.0134

ILE 33 ASP 34 0.0003

ASP 34 ILE 35 -0.0087

ILE 35 VAL 36 -0.0000

VAL 36 CYS 37 0.0145

CYS 37 ARG 38 -0.0003

ARG 38 PHE 39 -0.0123

PHE 39 LEU 40 0.0003

LEU 40 LYS 41 0.0070

LYS 41 GLU 42 0.0001

GLU 42 ARG 43 -0.0064

ARG 43 CYS 44 0.0000

CYS 44 PHE 45 0.0121

PHE 45 GLN 46 -0.0004

GLN 46 GLY 47 -0.0077

GLY 47 THR 48 -0.0004

THR 48 ALA 49 0.0105

ALA 49 ASP 50 -0.0001

ASP 50 PRO 51 -0.0174

PRO 51 VAL 52 -0.0001

VAL 52 ARG 53 0.0302

ARG 53 VAL 54 0.0001

VAL 54 SER 55 -0.1255

SER 55 LYS 56 0.0002

LYS 56 VAL 57 0.0336

VAL 57 VAL 58 0.0002

VAL 58 LYS 59 0.0315

LYS 59 GLY 60 -0.0000

GLY 60 GLY 61 0.0037

GLY 61 SER 62 0.0002

SER 62 SER 63 0.0092

SER 63 GLY 64 0.0003

GLY 64 LYS 65 -0.0496

LYS 65 GLY 66 -0.0001

GLY 66 THR 67 -0.0068

THR 67 THR 68 -0.0001

THR 68 LEU 69 0.0266

LEU 69 ARG 70 0.0003

ARG 70 GLY 71 0.1127

GLY 71 ARG 72 -0.0000

ARG 72 SER 73 -0.0302

SER 73 ASP 74 -0.0004

ASP 74 ALA 75 0.0010

ALA 75 ASP 76 0.0001

ASP 76 LEU 77 0.0402

LEU 77 VAL 78 -0.0002

VAL 78 VAL 79 0.0189

VAL 79 PHE 80 -0.0001

PHE 80 LEU 81 -0.0233

LEU 81 THR 82 0.0003

THR 82 LYS 83 -0.0008

LYS 83 LEU 84 0.0000

LEU 84 THR 85 0.0426

THR 85 SER 86 0.0002

SER 86 PHE 87 -0.0056

PHE 87 GLU 88 -0.0002

GLU 88 ASP 89 0.0609

ASP 89 GLN 90 -0.0002

GLN 90 LEU 91 -0.0066

LEU 91 ARG 92 0.0001

ARG 92 ARG 93 0.0823

ARG 93 ARG 94 0.0001

ARG 94 GLY 95 0.0010

GLY 95 GLU 96 0.0002

GLU 96 PHE 97 -0.0158

PHE 97 ILE 98 -0.0000

ILE 98 GLN 99 0.0004

GLN 99 GLU 100 -0.0001

GLU 100 ILE 101 0.0056

ILE 101 ARG 102 0.0002

ARG 102 ARG 103 0.0074

ARG 103 GLN 104 0.0004

GLN 104 LEU 105 0.0377

LEU 105 GLU 106 -0.0001

GLU 106 ALA 107 0.0051

ALA 107 CYS 108 0.0002

CYS 108 GLN 109 0.0170

GLN 109 ARG 110 -0.0000

ARG 110 GLU 111 0.0175

GLU 111 GLN 112 -0.0001

GLN 112 LYS 113 -0.0111

LYS 113 PHE 114 0.0004

PHE 114 LYS 115 -0.0545

LYS 115 VAL 116 0.0003

VAL 116 THR 117 -0.0990

THR 117 PHE 118 -0.0001

PHE 118 GLU 119 -0.0787

GLU 119 VAL 120 -0.0001

VAL 120 GLN 121 -0.0382

GLN 121 SER 122 -0.0001

SER 122 PRO 123 -0.0505

PRO 123 ARG 124 -0.0001

ARG 124 ARG 125 -0.0171

ARG 125 GLU 126 -0.0002

GLU 126 ASN 127 -0.0327

ASN 127 PRO 128 -0.0001

PRO 128 ARG 129 -0.0498

ARG 129 ALA 130 -0.0003

ALA 130 LEU 131 0.0087

LEU 131 SER 132 -0.0000

SER 132 PHE 133 -0.0354

PHE 133 VAL 134 -0.0003

VAL 134 LEU 135 -0.0337

LEU 135 SER 136 -0.0002

SER 136 SER 137 -0.0257

SER 137 PRO 138 0.0001

PRO 138 GLN 139 -0.0005

GLN 139 LEU 140 -0.0003

LEU 140 GLN 141 0.0015

GLN 141 GLN 142 0.0001

GLN 142 GLU 143 -0.0082

GLU 143 VAL 144 0.0005

VAL 144 GLU 145 0.0091

GLU 145 PHE 146 0.0003

PHE 146 ASP 147 -0.0173

ASP 147 VAL 148 -0.0005

VAL 148 LEU 149 -0.0261

LEU 149 PRO 150 0.0002

PRO 150 ALA 151 -0.0228

ALA 151 PHE 152 -0.0003

PHE 152 ASP 153 -0.0374

ASP 153 ALA 154 0.0000

ALA 154 LEU 155 -0.0546

LEU 155 GLY 156 -0.0003

GLY 156 GLN 157 -0.0596

GLN 157 TRP 158 -0.0001

TRP 158 THR 159 -0.0328

THR 159 PRO 160 0.0001

PRO 160 GLY 161 0.0120

GLY 161 TYR 162 0.0001

TYR 162 LYS 163 -0.0263

LYS 163 PRO 164 -0.0001

PRO 164 ASN 165 0.0155

ASN 165 PRO 166 0.0004

PRO 166 GLU 167 -0.0194

GLU 167 ILE 168 0.0000

ILE 168 TYR 169 0.0053

TYR 169 VAL 170 0.0003

VAL 170 GLN 171 -0.0367

GLN 171 LEU 172 0.0001

LEU 172 ILE 173 -0.0017

ILE 173 LYS 174 0.0002

LYS 174 GLU 175 -0.0124

GLU 175 CYS 176 -0.0001

CYS 176 LYS 177 0.0029

LYS 177 SER 178 -0.0001

SER 178 ARG 179 0.0011

ARG 179 GLY 180 0.0004

GLY 180 LYS 181 -0.0045

LYS 181 GLU 182 -0.0001

GLU 182 GLY 183 -0.0462

GLY 183 GLU 184 -0.0003

GLU 184 PHE 185 -0.0437

PHE 185 SER 186 -0.0004

SER 186 THR 187 0.0444

THR 187 CYS 188 0.0002

CYS 188 PHE 189 -0.0245

PHE 189 THR 190 -0.0001

THR 190 GLU 191 0.0520

GLU 191 LEU 192 -0.0002

LEU 192 GLN 193 -0.0092

GLN 193 ARG 194 0.0001

ARG 194 ASP 195 0.0472

ASP 195 PHE 196 -0.0004

PHE 196 LEU 197 0.0022

LEU 197 ARG 198 0.0001

ARG 198 ASN 199 -0.0081

ASN 199 ARG 200 -0.0002

ARG 200 PRO 201 -0.0543

PRO 201 THR 202 0.0001

THR 202 LYS 203 -0.0312

LYS 203 LEU 204 0.0002

LEU 204 LYS 205 -0.0104

LYS 205 SER 206 0.0002

SER 206 LEU 207 -0.0101

LEU 207 ILE 208 -0.0002

ILE 208 ARG 209 -0.0134

ARG 209 LEU 210 0.0000

LEU 210 VAL 211 -0.0283

VAL 211 LYS 212 -0.0001

LYS 212 HIS 213 0.0038

HIS 213 TRP 214 0.0001

TRP 214 TYR 215 -0.0073

TYR 215 GLN 216 0.0001

GLN 216 THR 217 0.0907

THR 217 CYS 218 0.0001

CYS 218 LYS 219 0.0162

LYS 219 LYS 220 0.0001

LYS 220 THR 221 0.0600

THR 221 HIS 222 -0.0002

HIS 222 GLY 223 -0.0058

GLY 223 ASN 224 0.0005

ASN 224 LYS 225 -0.0239

LYS 225 LEU 226 0.0002

LEU 226 PRO 227 0.0258

PRO 227 PRO 228 -0.0002

PRO 228 GLN 229 -0.0343

GLN 229 TYR 230 -0.0000

TYR 230 ALA 231 0.0157

ALA 231 LEU 232 -0.0003

LEU 232 GLU 233 -0.0052

GLU 233 LEU 234 -0.0001

LEU 234 LEU 235 -0.0043

LEU 235 THR 236 -0.0001

THR 236 VAL 237 -0.0307

VAL 237 TYR 238 0.0000

TYR 238 ALA 239 -0.0121

ALA 239 TRP 240 0.0001

TRP 240 GLU 241 0.0033

GLU 241 GLN 242 -0.0004

GLN 242 GLY 243 0.0086

GLY 243 SER 244 -0.0000

SER 244 ARG 245 -0.0243

ARG 245 LYS 246 0.0001

LYS 246 THR 247 -0.0029

THR 247 ASP 248 0.0002

ASP 248 PHE 249 -0.0115

PHE 249 SER 250 -0.0001

SER 250 THR 251 0.0177

THR 251 ALA 252 -0.0001

ALA 252 GLN 253 0.0141

GLN 253 GLY 254 -0.0002

GLY 254 PHE 255 -0.0082

PHE 255 GLN 256 0.0004

GLN 256 THR 257 -0.0047

THR 257 VAL 258 0.0002

VAL 258 LEU 259 -0.0299

LEU 259 GLU 260 0.0001

GLU 260 LEU 261 0.0065

LEU 261 VAL 262 -0.0002

VAL 262 LEU 263 -0.0012

LEU 263 LYS 264 -0.0002

LYS 264 HIS 265 0.0264

HIS 265 GLN 266 0.0004

GLN 266 LYS 267 -0.0240

LYS 267 LEU 268 0.0001

LEU 268 CYS 269 -0.0684

CYS 269 ILE 270 -0.0003

ILE 270 PHE 271 -0.1143

PHE 271 TRP 272 0.0002

TRP 272 GLU 273 -0.0638

GLU 273 ALA 274 -0.0000

ALA 274 TYR 275 -0.0370

TYR 275 TYR 276 0.0002

TYR 276 ASP 277 0.0180

ASP 277 PHE 278 0.0000

PHE 278 THR 279 -0.0366

THR 279 ASN 280 -0.0002

ASN 280 PRO 281 0.0053

PRO 281 VAL 282 0.0001

VAL 282 VAL 283 0.0024

VAL 283 GLY 284 -0.0002

GLY 284 ARG 285 0.0130

ARG 285 CYS 286 -0.0001

CYS 286 MET 287 0.0259

MET 287 LEU 288 0.0003

LEU 288 GLN 289 0.0060

GLN 289 GLN 290 0.0000

GLN 290 LEU 291 0.0835

LEU 291 LYS 292 0.0002

LYS 292 LYS 293 -0.0814

LYS 293 PRO 294 -0.0002

PRO 294 ARG 295 0.0281

ARG 295 PRO 296 -0.0002

PRO 296 VAL 297 0.0097

VAL 297 ILE 298 0.0002

ILE 298 LEU 299 -0.0010

LEU 299 ASP 300 -0.0004

ASP 300 PRO 301 0.0152

PRO 301 ALA 302 -0.0001

ALA 302 ASP 303 -0.0127

ASP 303 PRO 304 0.0002

PRO 304 THR 305 0.0081

THR 305 GLY 306 -0.0003

GLY 306 ASN 307 0.1663

ASN 307 VAL 308 0.0001

VAL 308 GLY 309 0.1099

GLY 309 GLY 310 -0.0001

GLY 310 GLY 311 -0.0258

GLY 311 ASP 312 -0.0001

ASP 312 THR 313 0.0143

THR 313 HIS 314 0.0000

HIS 314 SER 315 0.0098

SER 315 TRP 316 0.0003

TRP 316 GLN 317 0.0114

GLN 317 ARG 318 -0.0000

ARG 318 LEU 319 -0.0036

LEU 319 ALA 320 -0.0002

ALA 320 GLN 321 0.0045

GLN 321 GLU 322 0.0001

GLU 322 ALA 323 -0.0056

ALA 323 ARG 324 0.0002

ARG 324 VAL 325 -0.0075

VAL 325 TRP 326 -0.0001

TRP 326 LEU 327 0.0292

LEU 327 GLY 328 -0.0002

GLY 328 TYR 329 -0.0106

TYR 329 PRO 330 -0.0001

PRO 330 CYS 331 -0.0009

CYS 331 CYS 332 0.0000

CYS 332 LYS 333 0.0173

LYS 333 ASN 334 0.0003

ASN 334 LEU 335 0.0087

LEU 335 ASP 336 0.0002

ASP 336 GLY 337 0.0371

GLY 337 SER 338 0.0001

SER 338 LEU 339 -0.0064

LEU 339 VAL 340 -0.0001

VAL 340 GLY 341 0.0029

GLY 341 ALA 342 0.0001

ALA 342 TRP 343 -0.0270

TRP 343 THR 344 0.0001

THR 344 MET 345 0.0076

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 25th, 2023.

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

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

CA strain for 2401161742511318419

--- normal mode 7 ---

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

* TRANSFERASE 05-DEC-14 4RWQ *