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

* TRANSFERASE/RNA 05-DEC-14 4RWN *

CA strain for 221128153433140407

--- 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 -0.0005

GLU 2 LEU 3 -0.0228

LEU 3 ARG 4 0.0000

ARG 4 HIS 5 0.0070

HIS 5 THR 6 -0.0001

THR 6 PRO 7 0.0406

PRO 7 ALA 8 -0.0003

ALA 8 ARG 9 -0.0156

ARG 9 ASP 10 -0.0001

ASP 10 LEU 11 0.0153

LEU 11 ASP 12 0.0002

ASP 12 LYS 13 0.0421

LYS 13 PHE 14 -0.0002

PHE 14 ILE 15 0.0154

ILE 15 GLU 16 -0.0002

GLU 16 ASP 17 0.0216

ASP 17 HIS 18 -0.0001

HIS 18 LEU 19 -0.0234

LEU 19 LEU 20 -0.0002

LEU 20 PRO 21 0.0444

PRO 21 ASN 22 0.0002

ASN 22 THR 23 0.0294

THR 23 CYS 24 0.0002

CYS 24 PHE 25 -0.0256

PHE 25 ARG 26 -0.0000

ARG 26 THR 27 0.0512

THR 27 GLN 28 -0.0001

GLN 28 VAL 29 -0.0128

VAL 29 LYS 30 0.0004

LYS 30 GLU 31 -0.0540

GLU 31 ALA 32 0.0004

ALA 32 ILE 33 0.0026

ILE 33 ASP 34 -0.0002

ASP 34 ILE 35 -0.0782

ILE 35 VAL 36 0.0001

VAL 36 CYS 37 -0.0171

CYS 37 ARG 38 0.0000

ARG 38 PHE 39 -0.0596

PHE 39 LEU 40 0.0001

LEU 40 LYS 41 -0.0252

LYS 41 GLU 42 0.0001

GLU 42 ARG 43 -0.1310

ARG 43 CYS 44 0.0003

CYS 44 PHE 45 0.0116

PHE 45 GLN 46 0.0002

GLN 46 GLY 47 -0.0263

GLY 47 THR 48 -0.0001

THR 48 ALA 49 0.0212

ALA 49 ASP 50 0.0002

ASP 50 PRO 51 -0.0179

PRO 51 VAL 52 -0.0004

VAL 52 ARG 53 0.0007

ARG 53 VAL 54 0.0001

VAL 54 SER 55 -0.0417

SER 55 LYS 56 -0.0000

LYS 56 VAL 57 0.0147

VAL 57 VAL 58 -0.0000

VAL 58 LYS 59 0.0236

LYS 59 GLY 60 0.0002

GLY 60 GLY 61 0.0270

GLY 61 SER 62 0.0002

SER 62 SER 63 0.0790

SER 63 GLY 64 0.0001

GLY 64 LYS 65 0.0062

LYS 65 GLY 66 0.0001

GLY 66 THR 67 0.0585

THR 67 THR 68 0.0001

THR 68 LEU 69 -0.0173

LEU 69 ARG 70 0.0003

ARG 70 GLY 71 -0.0108

GLY 71 ARG 72 -0.0000

ARG 72 SER 73 -0.0088

SER 73 ASP 74 -0.0003

ASP 74 ALA 75 0.0635

ALA 75 ASP 76 0.0002

ASP 76 LEU 77 0.0068

LEU 77 VAL 78 0.0003

VAL 78 VAL 79 0.0313

VAL 79 PHE 80 0.0001

PHE 80 LEU 81 -0.0019

LEU 81 THR 82 0.0001

THR 82 LYS 83 0.0318

LYS 83 LEU 84 0.0001

LEU 84 THR 85 -0.0251

THR 85 SER 86 -0.0003

SER 86 PHE 87 0.0004

PHE 87 GLU 88 0.0000

GLU 88 ASP 89 0.0094

ASP 89 GLN 90 0.0002

GLN 90 LEU 91 0.0122

LEU 91 ARG 92 0.0002

ARG 92 ARG 93 0.0198

ARG 93 ARG 94 0.0001

ARG 94 GLY 95 0.0066

GLY 95 GLU 96 0.0001

GLU 96 PHE 97 -0.0023

PHE 97 ILE 98 0.0003

ILE 98 GLN 99 0.0252

GLN 99 GLU 100 0.0003

GLU 100 ILE 101 0.0006

ILE 101 ARG 102 0.0000

ARG 102 ARG 103 -0.0183

ARG 103 GLN 104 -0.0001

GLN 104 LEU 105 0.0190

LEU 105 GLU 106 0.0003

GLU 106 ALA 107 -0.0049

ALA 107 CYS 108 -0.0001

CYS 108 GLN 109 -0.0117

GLN 109 ARG 110 -0.0000

ARG 110 GLU 111 0.0135

GLU 111 GLN 112 0.0000

GLN 112 LYS 113 -0.0179

LYS 113 PHE 114 -0.0000

PHE 114 LYS 115 -0.0019

LYS 115 VAL 116 -0.0002

VAL 116 THR 117 -0.0299

THR 117 PHE 118 0.0003

PHE 118 GLU 119 -0.0399

GLU 119 VAL 120 0.0001

VAL 120 GLN 121 -0.0337

GLN 121 SER 122 -0.0004

SER 122 PRO 123 -0.0082

PRO 123 ARG 124 0.0002

ARG 124 ARG 125 0.0285

ARG 125 GLU 126 -0.0002

GLU 126 ASN 127 -0.0392

ASN 127 PRO 128 -0.0002

PRO 128 ARG 129 0.0306

ARG 129 ALA 130 -0.0001

ALA 130 LEU 131 0.0246

LEU 131 SER 132 -0.0003

SER 132 PHE 133 -0.0567

PHE 133 VAL 134 0.0000

VAL 134 LEU 135 -0.0259

LEU 135 SER 136 -0.0002

SER 136 SER 137 -0.0092

SER 137 PRO 138 0.0003

PRO 138 GLN 139 -0.0127

GLN 139 LEU 140 0.0002

LEU 140 GLN 141 0.0111

GLN 141 GLN 142 0.0000

GLN 142 GLU 143 -0.0991

GLU 143 VAL 144 -0.0002

VAL 144 GLU 145 -0.0918

GLU 145 PHE 146 0.0000

PHE 146 ASP 147 -0.0668

ASP 147 VAL 148 -0.0003

VAL 148 LEU 149 -0.0236

LEU 149 PRO 150 0.0001

PRO 150 ALA 151 -0.0150

ALA 151 PHE 152 -0.0003

PHE 152 ASP 153 0.0120

ASP 153 ALA 154 -0.0002

ALA 154 LEU 155 0.0168

LEU 155 GLY 156 0.0001

GLY 156 GLN 157 0.0514

GLN 157 TRP 158 0.0003

TRP 158 THR 159 -0.0086

THR 159 PRO 160 -0.0002

PRO 160 GLY 161 -0.0024

GLY 161 TYR 162 0.0001

TYR 162 LYS 163 -0.0355

LYS 163 PRO 164 -0.0001

PRO 164 ASN 165 0.0268

ASN 165 PRO 166 -0.0003

PRO 166 GLU 167 -0.0012

GLU 167 ILE 168 0.0002

ILE 168 TYR 169 -0.0091

TYR 169 VAL 170 -0.0001

VAL 170 GLN 171 -0.0745

GLN 171 LEU 172 -0.0002

LEU 172 ILE 173 -0.0118

ILE 173 LYS 174 0.0001

LYS 174 GLU 175 -0.0162

GLU 175 CYS 176 -0.0001

CYS 176 LYS 177 -0.0065

LYS 177 SER 178 0.0000

SER 178 ARG 179 -0.0074

ARG 179 GLY 180 -0.0002

GLY 180 LYS 181 -0.0266

LYS 181 GLU 182 0.0002

GLU 182 GLY 183 -0.0091

GLY 183 GLU 184 -0.0003

GLU 184 PHE 185 -0.0216

PHE 185 SER 186 0.0001

SER 186 THR 187 0.0813

THR 187 CYS 188 -0.0000

CYS 188 PHE 189 0.0017

PHE 189 THR 190 0.0002

THR 190 GLU 191 0.0225

GLU 191 LEU 192 0.0001

LEU 192 GLN 193 0.0094

GLN 193 ARG 194 0.0000

ARG 194 ARG 194 -0.0381

ARG 194 ASP 195 0.0135

ASP 195 PHE 196 0.0004

PHE 196 LEU 197 0.0452

LEU 197 ARG 198 0.0001

ARG 198 ASN 199 -0.0441

ASN 199 ARG 200 -0.0000

ARG 200 PRO 201 0.0660

PRO 201 THR 202 0.0001

THR 202 LYS 203 -0.0659

LYS 203 LEU 204 0.0003

LEU 204 LYS 205 -0.0041

LYS 205 SER 206 -0.0000

SER 206 LEU 207 0.0019

LEU 207 ILE 208 -0.0000

ILE 208 ARG 209 -0.0097

ARG 209 LEU 210 -0.0000

LEU 210 VAL 211 -0.0311

VAL 211 LYS 212 -0.0002

LYS 212 HIS 213 -0.0395

HIS 213 TRP 214 0.0005

TRP 214 TYR 215 -0.0483

TYR 215 GLN 216 0.0000

GLN 216 THR 217 0.0101

THR 217 CYS 218 -0.0001

CYS 218 LYS 219 -0.0107

LYS 219 LYS 220 0.0004

LYS 220 THR 221 0.0050

THR 221 HIS 222 -0.0000

HIS 222 GLY 223 0.0147

GLY 223 ASN 224 0.0000

ASN 224 LYS 225 -0.0311

LYS 225 LEU 226 -0.0003

LEU 226 PRO 227 0.0032

PRO 227 PRO 228 -0.0002

PRO 228 GLN 229 -0.0321

GLN 229 TYR 230 0.0002

TYR 230 ALA 231 0.0264

ALA 231 LEU 232 0.0004

LEU 232 GLU 233 0.0513

GLU 233 LEU 234 0.0000

LEU 234 LEU 235 0.0200

LEU 235 THR 236 -0.0000

THR 236 VAL 237 -0.0257

VAL 237 TYR 238 -0.0001

TYR 238 ALA 239 -0.0186

ALA 239 TRP 240 0.0002

TRP 240 GLU 241 0.0216

GLU 241 GLN 242 0.0000

GLN 242 GLY 243 -0.0014

GLY 243 SER 244 -0.0003

SER 244 ARG 245 -0.0406

ARG 245 LYS 246 0.0000

LYS 246 THR 247 -0.0117

THR 247 ASP 248 0.0002

ASP 248 PHE 249 -0.1408

PHE 249 SER 250 0.0003

SER 250 THR 251 0.0210

THR 251 ALA 252 -0.0003

ALA 252 GLN 253 0.0375

GLN 253 GLY 254 -0.0002

GLY 254 PHE 255 -0.0220

PHE 255 GLN 256 0.0003

GLN 256 THR 257 0.0038

THR 257 VAL 258 -0.0000

VAL 258 LEU 259 -0.0213

LEU 259 GLU 260 -0.0000

GLU 260 LEU 261 0.0007

LEU 261 VAL 262 -0.0000

VAL 262 LEU 263 0.0084

LEU 263 LYS 264 0.0003

LYS 264 HIS 265 0.0110

HIS 265 GLN 266 0.0002

GLN 266 LYS 267 -0.0289

LYS 267 LEU 268 0.0000

LEU 268 CYS 269 -0.0652

CYS 269 ILE 270 -0.0000

ILE 270 PHE 271 -0.1003

PHE 271 TRP 272 0.0001

TRP 272 GLU 273 -0.0485

GLU 273 ALA 274 0.0001

ALA 274 TYR 275 -0.0343

TYR 275 TYR 276 -0.0001

TYR 276 ASP 277 0.0088

ASP 277 PHE 278 -0.0000

PHE 278 THR 279 -0.0299

THR 279 ASN 280 0.0000

ASN 280 PRO 281 -0.0029

PRO 281 VAL 282 0.0002

VAL 282 VAL 283 0.0158

VAL 283 GLY 284 -0.0002

GLY 284 ARG 285 0.0174

ARG 285 CYS 286 0.0004

CYS 286 MET 287 0.0198

MET 287 LEU 288 0.0001

LEU 288 GLN 289 0.0163

GLN 289 GLN 290 -0.0000

GLN 290 LEU 291 0.0731

LEU 291 LYS 292 -0.0002

LYS 292 LYS 293 -0.0695

LYS 293 PRO 294 -0.0001

PRO 294 ARG 295 0.0151

ARG 295 PRO 296 0.0001

PRO 296 VAL 297 -0.0182

VAL 297 ILE 298 -0.0001

ILE 298 LEU 299 -0.0032

LEU 299 ASP 300 0.0002

ASP 300 PRO 301 -0.0103

PRO 301 ALA 302 0.0004

ALA 302 ASP 303 -0.0043

ASP 303 PRO 304 0.0001

PRO 304 THR 305 0.0155

THR 305 GLY 306 -0.0001

GLY 306 ASN 307 0.1122

ASN 307 VAL 308 -0.0002

VAL 308 GLY 309 0.0606

GLY 309 GLY 310 0.0000

GLY 310 GLY 311 -0.0411

GLY 311 ASP 312 -0.0000

ASP 312 THR 313 0.0158

THR 313 HIS 314 -0.0001

HIS 314 SER 315 0.0183

SER 315 TRP 316 0.0000

TRP 316 GLN 317 0.0088

GLN 317 ARG 318 0.0002

ARG 318 LEU 319 0.0044

LEU 319 ALA 320 -0.0002

ALA 320 GLN 321 0.0014

GLN 321 GLU 322 0.0001

GLU 322 ALA 323 -0.0141

ALA 323 ARG 324 -0.0004

ARG 324 VAL 325 0.0077

VAL 325 TRP 326 0.0001

TRP 326 LEU 327 0.0091

LEU 327 GLY 328 -0.0000

GLY 328 TYR 329 0.0002

TYR 329 PRO 330 0.0001

PRO 330 CYS 331 0.0069

CYS 331 CYS 332 -0.0001

CYS 332 LYS 333 -0.0016

LYS 333 ASN 334 0.0000

ASN 334 LEU 335 -0.0142

LEU 335 ASP 336 -0.0000

ASP 336 GLY 337 0.0327

GLY 337 SER 338 -0.0003

SER 338 LEU 339 -0.0057

LEU 339 VAL 340 0.0002

VAL 340 GLY 341 0.0091

GLY 341 ALA 342 -0.0000

ALA 342 TRP 343 -0.0219

TRP 343 THR 344 0.0002

THR 344 MET 345 0.0135

MET 345 LEU 346 0.0001

LEU 346 GLN 347 -0.0024

GLN 347 LYS 348 0.0001

LYS 348 ILE 349 0.0049

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/RNA 05-DEC-14 4RWN ***

CA strain for 221128153433140407

--- normal mode 7 ---

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

* TRANSFERASE/RNA 05-DEC-14 4RWN *