Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* DNA polimerase pura *

CA strain for 2610141424171094841

--- 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
GLU 9 THR 10 0.0004

THR 10 LEU 11 -0.0017

LEU 11 ASN 12 -0.0001

ASN 12 GLY 13 -0.0051

GLY 13 GLY 14 0.0003

GLY 14 ILE 15 0.0027

ILE 15 THR 16 -0.0002

THR 16 ASP 17 -0.0100

ASP 17 MET 18 0.0002

MET 18 LEU 19 0.0026

LEU 19 VAL 20 0.0000

VAL 20 GLU 21 -0.0330

GLU 21 LEU 22 0.0004

LEU 22 ALA 23 -0.0094

ALA 23 ASN 24 0.0002

ASN 24 PHE 25 -0.0098

PHE 25 GLU 26 0.0000

GLU 26 LYS 27 0.0003

LYS 27 ASN 28 0.0002

ASN 28 VAL 29 -0.0288

VAL 29 SER 30 0.0000

SER 30 GLN 31 -0.0066

GLN 31 ALA 32 0.0000

ALA 32 ILE 33 0.0001

ILE 33 HIS 34 -0.0002

HIS 34 LYS 35 -0.0001

LYS 35 TYR 36 0.0001

TYR 36 ASN 37 0.0004

ASN 37 ALA 38 0.0003

ALA 38 TYR 39 -0.0016

TYR 39 ARG 40 -0.0000

ARG 40 LYS 41 -0.0105

LYS 41 ALA 42 0.0002

ALA 42 ALA 43 -0.0031

ALA 43 SER 44 0.0003

SER 44 VAL 45 -0.0048

VAL 45 ILE 46 -0.0001

ILE 46 ALA 47 0.0015

ALA 47 LYS 48 0.0001

LYS 48 TYR 49 0.0020

TYR 49 PRO 50 -0.0001

PRO 50 HIS 51 0.0016

HIS 51 LYS 52 0.0004

LYS 52 ILE 53 0.0011

ILE 53 LYS 54 -0.0003

LYS 54 SER 55 0.0016

SER 55 GLY 56 0.0000

GLY 56 ALA 57 -0.0022

ALA 57 GLU 58 -0.0001

GLU 58 ALA 59 -0.0015

ALA 59 LYS 60 -0.0001

LYS 60 LYS 61 0.0047

LYS 61 LEU 62 -0.0001

LEU 62 PRO 63 -0.0022

PRO 63 GLY 64 0.0001

GLY 64 VAL 65 0.0006

VAL 65 GLY 66 -0.0003

GLY 66 THR 67 -0.0016

THR 67 LYS 68 -0.0001

LYS 68 ILE 69 -0.0023

ILE 69 ALA 70 0.0002

ALA 70 GLU 71 0.0021

GLU 71 LYS 72 -0.0002

LYS 72 ILE 73 0.0051

ILE 73 ASP 74 -0.0000

ASP 74 GLU 75 0.0267

GLU 75 PHE 76 -0.0003

PHE 76 LEU 77 0.0042

LEU 77 ALA 78 -0.0001

ALA 78 THR 79 0.0013

THR 79 GLY 80 0.0001

GLY 80 LYS 81 -0.0066

LYS 81 LEU 82 -0.0004

LEU 82 ARG 83 -0.0102

ARG 83 LYS 84 0.0000

LYS 84 LEU 85 -0.0358

LEU 85 GLU 86 0.0001

GLU 86 LYS 87 -0.0657

LYS 87 ILE 88 0.0000

ILE 88 ARG 89 -0.0137

ARG 89 GLN 90 0.0000

GLN 90 ASP 91 0.0354

ASP 91 ASP 92 0.0000

ASP 92 THR 93 -0.0316

THR 93 SER 94 -0.0002

SER 94 SER 95 -0.0116

SER 95 SER 96 -0.0003

SER 96 ILE 97 -0.0010

ILE 97 ASN 98 0.0001

ASN 98 PHE 99 -0.0290

PHE 99 LEU 100 0.0000

LEU 100 THR 101 -0.0005

THR 101 ARG 102 -0.0004

ARG 102 VAL 103 0.0012

VAL 103 THR 104 0.0000

THR 104 GLY 105 0.0068

GLY 105 ILE 106 0.0000

ILE 106 GLY 107 0.0111

GLY 107 PRO 108 0.0000

PRO 108 SER 109 -0.0047

SER 109 ALA 110 -0.0000

ALA 110 ALA 111 -0.0047

ALA 111 ARG 112 -0.0000

ARG 112 LYS 113 0.0033

LYS 113 LEU 114 -0.0000

LEU 114 VAL 115 -0.0087

VAL 115 ASP 116 -0.0001

ASP 116 GLU 117 -0.0037

GLU 117 GLY 118 0.0004

GLY 118 ILE 119 0.0253

ILE 119 LYS 120 -0.0003

LYS 120 THR 121 -0.0132

THR 121 LEU 122 -0.0000

LEU 122 GLU 123 0.0149

GLU 123 ASP 124 -0.0003

ASP 124 LEU 125 0.0086

LEU 125 ARG 126 0.0004

ARG 126 LYS 127 0.0172

LYS 127 ASN 128 0.0001

ASN 128 GLU 129 -0.0373

GLU 129 ASP 130 0.0000

ASP 130 LYS 131 -0.0144

LYS 131 LEU 132 -0.0004

LEU 132 ASN 133 -0.0230

ASN 133 HIS 134 -0.0002

HIS 134 HIS 135 0.0208

HIS 135 GLN 136 0.0003

GLN 136 ARG 137 -0.0060

ARG 137 ILE 138 0.0002

ILE 138 GLY 139 0.0083

GLY 139 LEU 140 0.0001

LEU 140 LYS 141 -0.0844

LYS 141 TYR 142 0.0000

TYR 142 PHE 143 -0.0211

PHE 143 GLU 144 -0.0002

GLU 144 ASP 145 -0.0321

ASP 145 PHE 146 0.0001

PHE 146 GLU 147 -0.0172

GLU 147 LYS 148 0.0003

LYS 148 ARG 149 0.0511

ARG 149 ILE 150 0.0000

ILE 150 PRO 151 0.0113

PRO 151 ARG 152 0.0002

ARG 152 GLU 153 -0.0120

GLU 153 GLU 154 0.0000

GLU 154 MET 155 -0.0005

MET 155 LEU 156 -0.0002

LEU 156 GLN 157 -0.0233

GLN 157 MET 158 0.0001

MET 158 GLN 159 -0.0148

GLN 159 ASP 160 0.0001

ASP 160 ILE 161 -0.0060

ILE 161 VAL 162 0.0000

VAL 162 LEU 163 -0.0118

LEU 163 ASN 164 0.0004

ASN 164 GLU 165 0.0017

GLU 165 VAL 166 -0.0004

VAL 166 LYS 167 -0.0014

LYS 167 LYS 168 -0.0002

LYS 168 LEU 169 0.0093

LEU 169 ASP 170 0.0005

ASP 170 PRO 171 0.0007

PRO 171 GLU 172 0.0002

GLU 172 TYR 173 0.0130

TYR 173 ILE 174 0.0003

ILE 174 ALA 175 0.0103

ALA 175 THR 176 0.0001

THR 176 VAL 177 0.0107

VAL 177 CYS 178 -0.0001

CYS 178 GLY 179 0.0066

GLY 179 SER 180 -0.0002

SER 180 PHE 181 0.0030

PHE 181 ARG 182 -0.0002

ARG 182 ARG 183 -0.0032

ARG 183 GLY 184 -0.0003

GLY 184 ALA 185 0.0162

ALA 185 GLU 186 -0.0000

GLU 186 SER 187 -0.0042

SER 187 SER 188 0.0001

SER 188 GLY 189 0.0021

GLY 189 ASP 190 0.0003

ASP 190 MET 191 0.0035

MET 191 ASP 192 0.0004

ASP 192 VAL 193 0.0079

VAL 193 LEU 194 0.0002

LEU 194 LEU 195 0.0151

LEU 195 THR 196 0.0002

THR 196 HIS 197 0.0120

HIS 197 PRO 198 -0.0003

PRO 198 ASN 199 -0.0009

ASN 199 PHE 200 0.0001

PHE 200 THR 201 -0.0043

THR 201 SER 202 0.0002

SER 202 GLU 203 -0.0007

GLU 203 SER 204 0.0005

SER 204 SER 205 0.0007

SER 205 LYS 206 -0.0002

LYS 206 GLN 207 -0.0006

GLN 207 PRO 208 -0.0001

PRO 208 LYS 209 0.0053

LYS 209 LEU 210 -0.0000

LEU 210 LEU 211 0.0046

LEU 211 HIS 212 -0.0004

HIS 212 ARG 213 0.0141

ARG 213 VAL 214 0.0002

VAL 214 VAL 215 -0.0048

VAL 215 GLU 216 0.0000

GLU 216 GLN 217 0.0118

GLN 217 LEU 218 -0.0002

LEU 218 GLN 219 -0.0057

GLN 219 LYS 220 -0.0001

LYS 220 VAL 221 0.0087

VAL 221 ARG 222 -0.0000

ARG 222 PHE 223 0.0202

PHE 223 ILE 224 -0.0003

ILE 224 THR 225 -0.0703

THR 225 ASP 226 -0.0001

ASP 226 THR 227 0.0110

THR 227 LEU 228 0.0001

LEU 228 SER 229 0.0161

SER 229 LYS 230 0.0003

LYS 230 GLY 231 0.0208

GLY 231 GLU 232 -0.0001

GLU 232 THR 233 0.0040

THR 233 LYS 234 0.0001

LYS 234 PHE 235 0.0038

PHE 235 MET 236 0.0005

MET 236 GLY 237 0.0047

GLY 237 VAL 238 -0.0002

VAL 238 CYS 239 0.0121

CYS 239 GLN 240 0.0003

GLN 240 LEU 241 -0.0001

LEU 241 PRO 242 0.0004

PRO 242 SER 243 0.0033

SER 243 GLU 244 0.0003

GLU 244 ASN 245 0.0019

ASN 245 GLU 249 -0.0020

GLU 249 TYR 250 -0.0004

TYR 250 PRO 251 -0.0216

PRO 251 HIS 252 -0.0000

HIS 252 ARG 253 0.0102

ARG 253 ARG 254 -0.0000

ARG 254 ILE 255 0.0371

ILE 255 ASP 256 0.0001

ASP 256 ILE 257 0.0185

ILE 257 ARG 258 0.0001

ARG 258 LEU 259 0.0165

LEU 259 ILE 260 -0.0001

ILE 260 PRO 261 0.0129

PRO 261 LYS 262 0.0001

LYS 262 ASP 263 -0.0286

ASP 263 GLN 264 0.0002

GLN 264 TYR 265 -0.0024

TYR 265 TYR 266 0.0002

TYR 266 CYS 267 -0.0189

CYS 267 GLY 268 0.0000

GLY 268 VAL 269 0.0009

VAL 269 LEU 270 -0.0001

LEU 270 TYR 271 0.0035

TYR 271 PHE 272 -0.0001

PHE 272 THR 273 -0.0012

THR 273 GLY 274 -0.0001

GLY 274 SER 275 -0.0004

SER 275 ASP 276 0.0000

ASP 276 ILE 277 0.0004

ILE 277 PHE 278 0.0000

PHE 278 ASN 279 0.0011

ASN 279 LYS 280 0.0001

LYS 280 ASN 281 0.0033

ASN 281 MET 282 0.0000

MET 282 ARG 283 -0.0038

ARG 283 ALA 284 -0.0002

ALA 284 HIS 285 0.0028

HIS 285 ALA 286 0.0003

ALA 286 LEU 287 -0.0010

LEU 287 GLU 288 0.0002

GLU 288 LYS 289 -0.0001

LYS 289 GLY 290 0.0002

GLY 290 PHE 291 -0.0033

PHE 291 THR 292 -0.0003

THR 292 ILE 293 0.0118

ILE 293 ASN 294 -0.0000

ASN 294 GLU 295 0.0122

GLU 295 TYR 296 0.0001

TYR 296 THR 297 0.0092

THR 297 ILE 298 0.0001

ILE 298 ARG 299 -0.0016

ARG 299 PRO 300 -0.0002

PRO 300 LEU 301 -0.0118

LEU 301 GLY 302 0.0000

GLY 302 VAL 303 -0.0143

VAL 303 THR 304 -0.0003

THR 304 GLY 305 0.0081

GLY 305 VAL 306 0.0002

VAL 306 ALA 307 -0.0068

ALA 307 GLY 308 0.0004

GLY 308 GLU 309 0.0003

GLU 309 PRO 310 0.0002

PRO 310 LEU 311 -0.0008

LEU 311 PRO 312 0.0001

PRO 312 VAL 313 -0.0094

VAL 313 ASP 314 -0.0002

ASP 314 SER 315 0.0058

SER 315 GLU 316 -0.0001

GLU 316 GLN 317 -0.0011

GLN 317 ASP 318 0.0001

ASP 318 ILE 319 0.0022

ILE 319 PHE 320 -0.0004

PHE 320 ASP 321 0.0046

ASP 321 TYR 322 0.0002

TYR 322 ILE 323 -0.0010

ILE 323 GLN 324 -0.0001

GLN 324 TRP 325 -0.0007

TRP 325 ARG 326 -0.0002

ARG 326 TYR 327 -0.0016

TYR 327 ARG 328 0.0004

ARG 328 GLU 329 -0.0087

GLU 329 PRO 330 -0.0002

PRO 330 LYS 331 0.0017

LYS 331 ASP 332 -0.0003

ASP 332 ARG 333 0.0013

ARG 333 SER 334 0.0002

SER 334 GLU 335 0.0028

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** DNA polimerase pura ***

CA strain for 2610141424171094841

--- normal mode 10 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* DNA polimerase pura *