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

* TRANSFERASE 14-DEC-16 5U8E *

CA strain for 22100401573516779

--- 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 VAL 2 -0.0001

VAL 2 ASP 3 -0.0128

ASP 3 GLN 4 0.0001

GLN 4 ALA 5 0.0014

ALA 5 THR 6 -0.0001

THR 6 LEU 7 0.0018

LEU 7 ASP 8 -0.0001

ASP 8 LYS 9 0.0080

LYS 9 LEU 10 0.0001

LEU 10 GLU 11 -0.0136

GLU 11 ALA 12 0.0001

ALA 12 GLY 13 0.0169

GLY 13 PHE 14 -0.0000

PHE 14 LYS 15 -0.0024

LYS 15 LYS 16 0.0002

LYS 16 LEU 17 0.0146

LEU 17 GLN 18 -0.0001

GLN 18 ASP 19 -0.0062

ASP 19 ALA 20 -0.0003

ALA 20 THR 21 -0.0117

THR 21 ASP 22 0.0003

ASP 22 LYS 24 0.0358

LYS 24 SER 25 -0.0002

SER 25 LEU 26 0.0291

LEU 26 LEU 27 0.0003

LEU 27 LYS 28 0.0182

LYS 28 LYS 29 -0.0001

LYS 29 TYR 30 -0.0158

TYR 30 LEU 31 0.0003

LEU 31 ASN 32 0.0063

ASN 32 ARG 33 -0.0003

ARG 33 GLU 34 -0.0058

GLU 34 VAL 35 -0.0000

VAL 35 PHE 36 -0.0000

PHE 36 ASP 37 -0.0003

ASP 37 GLN 38 -0.0144

GLN 38 CYS 39 0.0000

CYS 39 LYS 40 -0.0068

LYS 40 SER 41 0.0001

SER 41 LEU 42 -0.0360

LEU 42 LYS 43 0.0001

LYS 43 THR 44 -0.0312

THR 44 ALA 45 0.0003

ALA 45 LEU 46 0.0110

LEU 46 GLY 47 0.0003

GLY 47 ALA 48 -0.0140

ALA 48 THR 49 -0.0001

THR 49 LEU 50 -0.0085

LEU 50 LEU 51 0.0001

LEU 51 ASP 52 0.0016

ASP 52 CYS 53 0.0005

CYS 53 ILE 54 -0.0315

ILE 54 GLN 55 0.0004

GLN 55 SER 56 0.0184

SER 56 GLY 57 0.0001

GLY 57 VAL 58 0.0215

VAL 58 GLU 59 0.0000

GLU 59 ASN 60 0.0112

ASN 60 LEU 61 0.0003

LEU 61 ASP 62 0.0086

ASP 62 SER 63 -0.0004

SER 63 GLY 64 0.0485

GLY 64 VAL 65 0.0002

VAL 65 GLY 66 0.0563

GLY 66 ILE 67 0.0004

ILE 67 TYR 68 -0.0405

TYR 68 ALA 69 -0.0002

ALA 69 PRO 70 0.0209

PRO 70 ASP 71 -0.0001

ASP 71 ALA 72 -0.0574

ALA 72 GLU 73 -0.0000

GLU 73 ALA 74 0.0013

ALA 74 TYR 75 0.0003

TYR 75 THR 76 0.0119

THR 76 LEU 77 -0.0002

LEU 77 PHE 78 0.0046

PHE 78 ALA 79 0.0000

ALA 79 PRO 80 -0.0231

PRO 80 ILE 81 0.0001

ILE 81 PHE 82 -0.0096

PHE 82 ASN 83 -0.0000

ASN 83 PRO 84 -0.0232

PRO 84 ILE 85 0.0002

ILE 85 ILE 86 0.0237

ILE 86 GLU 87 -0.0004

GLU 87 ASP 88 -0.0178

ASP 88 TYR 89 0.0001

TYR 89 HIS 90 0.0810

HIS 90 GLU 91 0.0002

GLU 91 GLY 92 0.0130

GLY 92 PHE 93 -0.0003

PHE 93 LYS 94 -0.0021

LYS 94 PRO 95 -0.0000

PRO 95 THR 96 -0.0271

THR 96 ASP 97 0.0002

ASP 97 LYS 98 0.0033

LYS 98 HIS 99 0.0002

HIS 99 PRO 100 0.0135

PRO 100 PRO 101 0.0002

PRO 101 THR 102 0.0205

THR 102 ASP 103 0.0003

ASP 103 PHE 104 -0.0172

PHE 104 GLY 105 -0.0004

GLY 105 ASP 106 -0.0378

ASP 106 ILE 107 -0.0001

ILE 107 ASN 108 -0.0077

ASN 108 THR 109 0.0001

THR 109 ILE 110 -0.0029

ILE 110 VAL 111 -0.0000

VAL 111 ASN 112 -0.0592

ASN 112 VAL 113 0.0003

VAL 113 ASP 114 -0.0166

ASP 114 PRO 115 0.0001

PRO 115 SER 116 -0.0157

SER 116 GLY 117 0.0002

GLY 117 LYS 118 -0.0067

LYS 118 TYR 119 0.0002

TYR 119 VAL 120 0.0208

VAL 120 VAL 121 -0.0002

VAL 121 SER 122 0.0495

SER 122 THR 123 -0.0002

THR 123 HIS 124 0.0678

HIS 124 VAL 125 0.0003

VAL 125 ARG 126 0.0852

ARG 126 CYS 127 -0.0002

CYS 127 GLY 128 0.0869

GLY 128 ARG 129 0.0003

ARG 129 SER 130 0.0013

SER 130 LEU 131 -0.0002

LEU 131 LYS 132 0.0391

LYS 132 GLY 133 0.0003

GLY 133 TYR 134 -0.0400

TYR 134 PRO 135 0.0002

PRO 135 PHE 136 0.0175

PHE 136 ASN 137 -0.0001

ASN 137 PRO 138 0.0108

PRO 138 CYS 139 0.0002

CYS 139 LEU 140 -0.0145

LEU 140 THR 141 -0.0004

THR 141 GLU 142 0.0176

GLU 142 ALA 143 0.0000

ALA 143 ASN 144 0.0108

ASN 144 TYR 145 0.0002

TYR 145 LYS 146 -0.0067

LYS 146 GLU 147 0.0002

GLU 147 MET 148 0.0093

MET 148 GLU 149 -0.0003

GLU 149 ASP 150 0.0138

ASP 150 LYS 151 0.0005

LYS 151 VAL 152 0.0129

VAL 152 SER 153 0.0002

SER 153 ALA 154 0.0160

ALA 154 ILE 155 0.0001

ILE 155 PHE 156 0.0233

PHE 156 GLY 157 0.0001

GLY 157 THR 158 0.0153

THR 158 PHE 159 -0.0003

PHE 159 GLU 160 0.0017

GLU 160 GLY 161 0.0004

GLY 161 GLU 162 -0.0573

GLU 162 LEU 163 0.0002

LEU 163 LYS 164 -0.0172

LYS 164 GLY 165 0.0002

GLY 165 LYS 166 -0.0384

LYS 166 TYR 167 0.0002

TYR 167 TYR 168 -0.0136

TYR 168 PRO 169 -0.0002

PRO 169 LEU 170 -0.0183

LEU 170 THR 171 -0.0003

THR 171 GLY 172 0.0043

GLY 172 MET 173 -0.0001

MET 173 ASP 174 -0.0013

ASP 174 LYS 175 -0.0001

LYS 175 ALA 176 0.0036

ALA 176 THR 177 0.0000

THR 177 GLN 178 -0.0078

GLN 178 GLN 179 0.0001

GLN 179 GLN 180 0.0096

GLN 180 LEU 181 0.0001

LEU 181 ILE 182 -0.0002

ILE 182 ASP 183 0.0000

ASP 183 ASP 184 0.0123

ASP 184 HIS 185 0.0001

HIS 185 PHE 186 0.0016

PHE 186 LEU 187 -0.0001

LEU 187 PHE 188 0.0523

PHE 188 LYS 189 0.0001

LYS 189 GLU 190 0.0536

GLU 190 GLY 191 0.0000

GLY 191 ASP 192 0.0407

ASP 192 ARG 193 -0.0000

ARG 193 PHE 194 -0.0115

PHE 194 LEU 195 0.0001

LEU 195 GLN 196 0.0136

GLN 196 ALA 197 -0.0000

ALA 197 ALA 198 -0.0011

ALA 198 ASN 199 -0.0000

ASN 199 ALA 200 0.0412

ALA 200 CYS 201 -0.0003

CYS 201 ARG 202 -0.0156

ARG 202 TYR 203 0.0003

TYR 203 TRP 204 0.0310

TRP 204 PRO 205 0.0002

PRO 205 THR 206 -0.0041

THR 206 GLY 207 0.0005

GLY 207 ARG 208 0.0113

ARG 208 GLY 209 0.0002

GLY 209 ILE 210 0.0087

ILE 210 TYR 211 0.0002

TYR 211 HIS 212 0.0124

HIS 212 ASN 213 -0.0004

ASN 213 ASP 214 0.0022

ASP 214 ALA 215 -0.0003

ALA 215 LYS 216 0.0127

LYS 216 THR 217 0.0002

THR 217 PHE 218 -0.0020

PHE 218 LEU 219 0.0001

LEU 219 VAL 220 0.0085

VAL 220 TRP 221 0.0005

TRP 221 VAL 222 0.0213

VAL 222 ASN 223 0.0000

ASN 223 GLU 224 0.0192

GLU 224 GLU 225 -0.0000

GLU 225 ASP 226 0.0053

ASP 226 HIS 227 0.0003

HIS 227 LEU 228 0.0156

LEU 228 ARG 229 0.0002

ARG 229 ILE 230 0.0435

ILE 230 ILE 231 0.0004

ILE 231 SER 232 0.0464

SER 232 MET 233 -0.0002

MET 233 GLN 234 0.0778

GLN 234 LYS 235 0.0004

LYS 235 GLY 236 0.0361

GLY 236 GLY 237 -0.0002

GLY 237 ASP 238 -0.0686

ASP 238 LEU 239 -0.0003

LEU 239 LYS 240 -0.0009

LYS 240 THR 241 0.0003

THR 241 ILE 242 0.0425

ILE 242 PHE 243 0.0004

PHE 243 GLN 244 0.0077

GLN 244 ARG 245 0.0002

ARG 245 LEU 246 -0.0113

LEU 246 VAL 247 0.0002

VAL 247 ASN 248 0.0692

ASN 248 ALA 249 -0.0001

ALA 249 VAL 250 -0.0105

VAL 250 ASN 251 0.0003

ASN 251 THR 252 0.0135

THR 252 ILE 253 -0.0002

ILE 253 GLU 254 0.0264

GLU 254 SER 255 0.0000

SER 255 LYS 256 -0.0103

LYS 256 LEU 257 -0.0002

LEU 257 PRO 258 0.0547

PRO 258 PHE 259 0.0003

PHE 259 SER 260 -0.0117

SER 260 ARG 261 0.0001

ARG 261 ASP 262 0.0192

ASP 262 ASP 263 0.0001

ASP 263 ARG 264 0.0229

ARG 264 LEU 265 0.0004

LEU 265 GLY 266 -0.0006

GLY 266 PHE 267 -0.0005

PHE 267 LEU 268 -0.0819

LEU 268 THR 269 0.0001

THR 269 PHE 270 0.0055

PHE 270 CYS 271 -0.0003

CYS 271 PRO 272 -0.0483

PRO 272 THR 273 0.0000

THR 273 ASN 274 0.0115

ASN 274 LEU 275 0.0001

LEU 275 GLY 276 0.0063

GLY 276 THR 277 -0.0002

THR 277 THR 278 0.0019

THR 278 ILE 279 0.0001

ILE 279 ARG 280 0.1033

ARG 280 ALA 281 0.0004

ALA 281 SER 282 0.0720

SER 282 VAL 283 -0.0003

VAL 283 HIS 284 0.0062

HIS 284 ILE 285 0.0002

ILE 285 ALA 286 0.0381

ALA 286 LEU 287 0.0002

LEU 287 PRO 288 0.0032

PRO 288 LYS 289 -0.0001

LYS 289 LEU 290 0.0079

LEU 290 ALA 291 -0.0002

ALA 291 LYS 292 0.0337

LYS 292 ASP 293 0.0001

ASP 293 LYS 294 0.0234

LYS 294 LYS 295 0.0002

LYS 295 GLN 296 -0.0217

GLN 296 LEU 297 -0.0001

LEU 297 GLU 298 0.0035

GLU 298 ALA 299 0.0003

ALA 299 ILE 300 -0.0070

ILE 300 ALA 301 0.0001

ALA 301 ALA 302 -0.0196

ALA 302 LYS 303 -0.0000

LYS 303 PHE 304 -0.0101

PHE 304 ASN 305 -0.0000

ASN 305 LEU 306 -0.0456

LEU 306 GLN 307 0.0002

GLN 307 VAL 308 0.0371

VAL 308 ARG 309 0.0002

ARG 309 GLY 320 0.0409

GLY 320 GLY 321 0.0001

GLY 321 VAL 322 0.0294

VAL 322 TYR 323 -0.0001

TYR 323 ASP 324 0.1076

ASP 324 ILE 325 -0.0001

ILE 325 SER 326 0.0754

SER 326 ASN 327 0.0000

ASN 327 LYS 328 0.0632

LYS 328 ARG 329 0.0001

ARG 329 ARG 330 0.0910

ARG 330 MET 331 0.0003

MET 331 GLY 332 0.0135

GLY 332 LEU 333 -0.0001

LEU 333 THR 334 0.0259

THR 334 GLU 335 0.0004

GLU 335 TYR 336 -0.0317

TYR 336 GLN 337 0.0004

GLN 337 ALA 338 0.0586

ALA 338 VAL 339 -0.0001

VAL 339 LYS 340 0.0212

LYS 340 GLU 341 -0.0002

GLU 341 MET 342 -0.0363

MET 342 GLN 343 0.0001

GLN 343 ASP 344 0.0226

ASP 344 GLY 345 0.0003

GLY 345 ILE 346 -0.0155

ILE 346 LEU 347 0.0002

LEU 347 GLU 348 -0.0140

GLU 348 MET 349 0.0001

MET 349 ILE 350 0.0369

ILE 350 LYS 351 -0.0001

LYS 351 MET 352 -0.0114

MET 352 GLU 353 -0.0002

GLU 353 GLU 354 0.0291

GLU 354 ALA 355 -0.0002

ALA 355 ALA 356 0.0050

ALA 356 PRO 357 -0.0003

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: October 18th, 2018.

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

*** TRANSFERASE 14-DEC-16 5U8E ***

CA strain for 22100401573516779

--- normal mode 7 ---

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

* TRANSFERASE 14-DEC-16 5U8E *