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

* *

CA strain for 2402132254012667902

--- 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 GLY 2 -0.0000

GLY 2 ASN 3 0.0034

ASN 3 SER 4 0.0002

SER 4 ALA 5 0.0012

ALA 5 SER 6 0.0000

SER 6 ARG 7 0.0018

ARG 7 SER 8 0.0001

SER 8 ASP 9 0.0036

ASP 9 PHE 10 0.0003

PHE 10 GLU 11 0.0007

GLU 11 TRP 12 0.0003

TRP 12 VAL 13 -0.0082

VAL 13 TYR 14 -0.0003

TYR 14 THR 15 -0.0006

THR 15 ASP 16 -0.0002

ASP 16 GLN 17 -0.0019

GLN 17 PRO 18 0.0000

PRO 18 HIS 19 0.0064

HIS 19 THR 20 0.0002

THR 20 GLN 21 -0.0014

GLN 21 ARG 22 0.0001

ARG 22 ARG 23 0.0003

ARG 23 LYS 24 -0.0001

LYS 24 GLU 25 -0.0012

GLU 25 ILE 26 -0.0002

ILE 26 LEU 27 0.0013

LEU 27 ALA 28 -0.0002

ALA 28 LYS 29 0.0008

LYS 29 TYR 30 -0.0002

TYR 30 PRO 31 0.0024

PRO 31 ALA 32 0.0001

ALA 32 ILE 33 -0.0009

ILE 33 LYS 34 -0.0001

LYS 34 ALA 35 -0.0003

ALA 35 LEU 36 -0.0002

LEU 36 MET 37 0.0025

MET 37 ARG 38 -0.0005

ARG 38 PRO 39 -0.0004

PRO 39 ASP 40 -0.0001

ASP 40 PRO 41 -0.0009

PRO 41 ARG 42 0.0000

ARG 42 LEU 43 0.0002

LEU 43 LYS 44 -0.0000

LYS 44 TRP 45 -0.0007

TRP 45 ALA 46 -0.0005

ALA 46 VAL 47 0.0012

VAL 47 LEU 48 0.0001

LEU 48 VAL 49 0.0014

VAL 49 LEU 50 0.0000

LEU 50 VAL 51 -0.0003

VAL 51 LEU 52 0.0003

LEU 52 VAL 53 0.0052

VAL 53 GLN 54 -0.0004

GLN 54 MET 55 -0.0020

MET 55 LEU 56 -0.0001

LEU 56 ALA 57 0.0019

ALA 57 CYS 58 0.0004

CYS 58 TRP 59 0.0007

TRP 59 LEU 60 0.0000

LEU 60 VAL 61 0.0007

VAL 61 ARG 62 0.0001

ARG 62 GLY 63 0.0028

GLY 63 LEU 64 0.0005

LEU 64 ALA 65 -0.0017

ALA 65 TRP 66 -0.0000

TRP 66 ARG 67 -0.0010

ARG 67 TRP 68 -0.0004

TRP 68 LEU 69 0.0027

LEU 69 LEU 70 -0.0003

LEU 70 PHE 71 -0.0013

PHE 71 TRP 72 -0.0003

TRP 72 ALA 73 0.0027

ALA 73 TYR 74 0.0003

TYR 74 ALA 75 0.0073

ALA 75 PHE 76 0.0001

PHE 76 GLY 77 0.0006

GLY 77 GLY 78 -0.0001

GLY 78 CYS 79 -0.0025

CYS 79 VAL 80 0.0002

VAL 80 ASN 81 -0.0019

ASN 81 HIS 82 0.0000

HIS 82 SER 83 0.0001

SER 83 LEU 84 0.0000

LEU 84 THR 85 0.0003

THR 85 LEU 86 -0.0002

LEU 86 ALA 87 0.0001

ALA 87 ILE 88 0.0002

ILE 88 HIS 89 0.0007

HIS 89 ASP 90 0.0001

ASP 90 ILE 91 0.0016

ILE 91 SER 92 -0.0004

SER 92 HIS 93 0.0040

HIS 93 ASN 94 -0.0000

ASN 94 ALA 95 -0.0038

ALA 95 ALA 96 -0.0003

ALA 96 PHE 97 0.0009

PHE 97 GLY 98 0.0002

GLY 98 THR 99 -0.0008

THR 99 GLY 100 -0.0004

GLY 100 ARG 101 0.0005

ARG 101 ALA 102 0.0000

ALA 102 ALA 103 0.0025

ALA 103 ARG 104 -0.0001

ARG 104 ASN 105 -0.0002

ASN 105 ARG 106 -0.0002

ARG 106 TRP 107 0.0015

TRP 107 LEU 108 -0.0001

LEU 108 ALA 109 -0.0001

ALA 109 VAL 110 0.0002

VAL 110 PHE 111 0.0023

PHE 111 ALA 112 0.0001

ALA 112 ASN 113 -0.0003

ASN 113 LEU 114 -0.0001

LEU 114 PRO 115 0.0002

PRO 115 VAL 116 0.0001

VAL 116 GLY 117 -0.0003

GLY 117 VAL 118 -0.0001

VAL 118 PRO 119 0.0027

PRO 119 TYR 120 0.0004

TYR 120 ALA 121 -0.0012

ALA 121 ALA 122 0.0001

ALA 122 SER 123 0.0014

SER 123 PHE 124 -0.0001

PHE 124 LYS 125 0.0025

LYS 125 LYS 126 -0.0004

LYS 126 TYR 127 -0.0020

TYR 127 HIS 128 -0.0001

HIS 128 VAL 129 -0.0164

VAL 129 ASP 130 -0.0002

ASP 130 HIS 131 0.0187

HIS 131 HIS 132 0.0001

HIS 132 ARG 133 -0.0904

ARG 133 TYR 134 0.0000

TYR 134 LEU 135 -0.0164

LEU 135 GLY 136 0.0002

GLY 136 GLY 137 0.0112

GLY 137 ASP 138 0.0000

ASP 138 GLY 139 0.0169

GLY 139 LEU 140 0.0001

LEU 140 ASP 141 0.0969

ASP 141 VAL 142 0.0003

VAL 142 ASP 143 0.0274

ASP 143 VAL 144 -0.0002

VAL 144 PRO 145 0.0011

PRO 145 THR 146 -0.0001

THR 146 ARG 147 -0.0093

ARG 147 LEU 148 0.0003

LEU 148 GLU 149 0.0014

GLU 149 GLY 150 -0.0002

GLY 150 TRP 151 -0.0015

TRP 151 PHE 152 0.0001

PHE 152 PHE 153 -0.0007

PHE 153 CYS 154 0.0001

CYS 154 THR 155 0.0006

THR 155 PRO 156 0.0000

PRO 156 ALA 157 0.0002

ALA 157 ARG 158 -0.0000

ARG 158 LYS 159 -0.0002

LYS 159 LEU 160 -0.0002

LEU 160 LEU 161 -0.0003

LEU 161 TRP 162 0.0001

TRP 162 LEU 163 0.0007

LEU 163 VAL 164 0.0002

VAL 164 LEU 165 0.0020

LEU 165 GLN 166 0.0001

GLN 166 PRO 167 -0.0005

PRO 167 PHE 168 -0.0004

PHE 168 PHE 169 0.0084

PHE 169 TYR 170 0.0000

TYR 170 SER 171 -0.0036

SER 171 LEU 172 -0.0004

LEU 172 ARG 173 0.0021

ARG 173 PRO 174 0.0004

PRO 174 LEU 175 -0.0049

LEU 175 CYS 176 -0.0002

CYS 176 VAL 177 0.0242

VAL 177 HIS 178 -0.0000

HIS 178 PRO 179 -0.0041

PRO 179 LYS 180 -0.0003

LYS 180 ALA 181 0.0072

ALA 181 VAL 182 -0.0002

VAL 182 THR 183 -0.0062

THR 183 ARG 184 0.0004

ARG 184 MET 185 0.0032

MET 185 GLU 186 -0.0002

GLU 186 VAL 187 0.0032

VAL 187 LEU 188 0.0001

LEU 188 ASN 189 -0.0030

ASN 189 THR 190 0.0000

THR 190 LEU 191 -0.0010

LEU 191 VAL 192 -0.0000

VAL 192 GLN 193 -0.0035

GLN 193 LEU 194 -0.0004

LEU 194 ALA 195 -0.0017

ALA 195 ALA 196 0.0001

ALA 196 ASP 197 -0.0016

ASP 197 LEU 198 0.0001

LEU 198 ALA 199 0.0006

ALA 199 ILE 200 0.0002

ILE 200 PHE 201 -0.0010

PHE 201 ALA 202 -0.0003

ALA 202 LEU 203 -0.0005

LEU 203 TRP 204 0.0004

TRP 204 GLY 205 -0.0033

GLY 205 LEU 206 -0.0000

LEU 206 LYS 207 0.0002

LYS 207 PRO 208 0.0002

PRO 208 VAL 209 0.0023

VAL 209 VAL 210 0.0000

VAL 210 TYR 211 -0.0037

TYR 211 LEU 212 -0.0002

LEU 212 LEU 213 0.0014

LEU 213 ALA 214 -0.0001

ALA 214 SER 215 -0.0006

SER 215 SER 216 -0.0003

SER 216 PHE 217 -0.0092

PHE 217 LEU 218 -0.0001

LEU 218 GLY 219 0.0000

GLY 219 LEU 220 0.0000

LEU 220 GLY 221 -0.0056

GLY 221 LEU 222 -0.0003

LEU 222 HIS 223 0.0048

HIS 223 PRO 224 -0.0002

PRO 224 ILE 225 0.0008

ILE 225 SER 226 0.0003

SER 226 GLY 227 -0.0006

GLY 227 HIS 228 0.0002

HIS 228 PHE 229 0.0029

PHE 229 VAL 230 -0.0001

VAL 230 ALA 231 0.0024

ALA 231 GLU 232 -0.0004

GLU 232 HIS 233 -0.0001

HIS 233 TYR 234 -0.0004

TYR 234 MET 235 0.0010

MET 235 PHE 236 -0.0003

PHE 236 LEU 237 -0.0030

LEU 237 LYS 238 -0.0002

LYS 238 GLY 239 -0.0058

GLY 239 HIS 240 -0.0005

HIS 240 GLU 241 -0.0030

GLU 241 THR 242 -0.0003

THR 242 TYR 243 -0.0090

TYR 243 SER 244 -0.0001

SER 244 TYR 245 -0.0030

TYR 245 TYR 246 0.0002

TYR 246 GLY 247 -0.0026

GLY 247 PRO 248 0.0001

PRO 248 LEU 249 -0.0001

LEU 249 ASN 250 -0.0001

ASN 250 TRP 251 -0.0011

TRP 251 ILE 252 -0.0003

ILE 252 THR 253 0.0011

THR 253 PHE 254 -0.0002

PHE 254 ASN 255 -0.0046

ASN 255 VAL 256 0.0001

VAL 256 GLY 257 0.0014

GLY 257 TYR 258 0.0002

TYR 258 HIS 259 -0.0020

HIS 259 VAL 260 0.0001

VAL 260 GLU 261 0.0020

GLU 261 HIS 262 -0.0003

HIS 262 HIS 263 -0.0027

HIS 263 ASP 264 0.0001

ASP 264 PHE 265 0.0003

PHE 265 PRO 266 0.0002

PRO 266 SER 267 -0.0042

SER 267 ILE 268 -0.0000

ILE 268 PRO 269 -0.0008

PRO 269 GLY 270 -0.0001

GLY 270 TYR 271 -0.0017

TYR 271 ASN 272 -0.0001

ASN 272 LEU 273 0.0003

LEU 273 PRO 274 -0.0002

PRO 274 LEU 275 0.0005

LEU 275 VAL 276 -0.0000

VAL 276 ARG 277 0.0019

ARG 277 LYS 278 0.0004

LYS 278 ILE 279 0.0008

ILE 279 ALA 280 -0.0001

ALA 280 PRO 281 0.0022

PRO 281 GLU 282 0.0003

GLU 282 TYR 283 -0.0034

TYR 283 TYR 284 0.0000

TYR 284 ASP 285 -0.0042

ASP 285 HIS 286 0.0002

HIS 286 LEU 287 0.0013

LEU 287 PRO 288 -0.0002

PRO 288 GLN 289 0.0004

GLN 289 HIS 290 -0.0000

HIS 290 HIS 291 -0.0009

HIS 291 SER 292 -0.0002

SER 292 TRP 293 -0.0013

TRP 293 VAL 294 -0.0001

VAL 294 LYS 295 -0.0024

LYS 295 VAL 296 0.0000

VAL 296 LEU 297 -0.0005

LEU 297 TRP 298 0.0002

TRP 298 ASP 299 -0.0028

ASP 299 PHE 300 -0.0001

PHE 300 VAL 301 0.0002

VAL 301 PHE 302 -0.0001

PHE 302 GLU 303 -0.0004

GLU 303 ASP 304 -0.0001

ASP 304 SER 305 0.0002

SER 305 LEU 306 0.0000

LEU 306 GLY 307 0.0013

GLY 307 PRO 308 0.0001

PRO 308 TYR 309 -0.0007

TYR 309 ALA 310 -0.0002

ALA 310 ARG 311 -0.0023

ARG 311 VAL 312 -0.0003

VAL 312 LYS 313 0.0011

LYS 313 ARG 314 -0.0000

ARG 314 VAL 315 0.0070

VAL 315 TYR 316 -0.0003

TYR 316 ARG 317 -0.1844

ARG 317 LEU 318 0.0001

LEU 318 ALA 319 0.0129

ALA 319 LYS 320 -0.0001

LYS 320 ASP 321 0.0081

ASP 321 GLY 322 -0.0004

GLY 322 LEU 323 0.0495

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.

*** ***

CA strain for 2402132254012667902

--- normal mode 7 ---

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

* *