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

* BIOSYNTHETIC PROTEIN 11-MAY-21 7MSP *

CA strain for 2605100231101288398

--- 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
LEU 3 SER 4 0.0000

SER 4 ASP 5 0.0000

ASP 5 ILE 6 0.0002

ILE 6 TYR 7 -0.0005

TYR 7 LEU 8 0.0001

LEU 8 GLU 9 -0.0000

GLU 9 LEU 10 0.0002

LEU 10 LYS 11 -0.0019

LYS 11 LYS 12 -0.0000

LYS 12 GLY 13 -0.0000

GLY 13 TYR 14 -0.0001

TYR 14 ALA 15 0.0013

ALA 15 ASP 16 -0.0005

ASP 16 SER 17 0.0001

SER 17 LEU 18 -0.0003

LEU 18 LEU 19 -0.0021

LEU 19 TYR 20 -0.0001

TYR 20 SER 21 -0.0000

SER 21 ASP 22 -0.0005

ASP 22 LEU 23 -0.0047

LEU 23 SER 24 0.0001

SER 24 LEU 25 0.0000

LEU 25 LEU 26 0.0001

LEU 26 VAL 27 0.0009

VAL 27 ASN 28 -0.0003

ASN 28 ILE 29 -0.0004

ILE 29 MET 30 -0.0000

MET 30 GLU 31 0.0000

GLU 31 TYR 32 -0.0000

TYR 32 GLU 33 0.0003

GLU 33 LYS 34 0.0002

LYS 34 ASP 35 -0.0008

ASP 35 ILE 36 0.0001

ILE 36 ASP 37 -0.0005

ASP 37 VAL 38 -0.0000

VAL 38 MET 39 0.0005

MET 39 SER 40 0.0002

SER 40 ILE 41 -0.0002

ILE 41 GLN 42 0.0003

GLN 42 SER 43 -0.0054

SER 43 LEU 44 0.0000

LEU 44 VAL 45 -0.0001

VAL 45 ALA 46 0.0001

ALA 46 GLY 47 -0.0090

GLY 47 TYR 48 0.0001

TYR 48 GLU 49 0.0004

GLU 49 LYS 50 -0.0001

LYS 50 SER 51 -0.0097

SER 51 ASP 52 0.0003

ASP 52 THR 53 -0.0000

THR 53 PRO 54 0.0002

PRO 54 THR 55 -0.0271

THR 55 ILE 56 0.0001

ILE 56 THR 57 -0.0003

THR 57 CYS 58 -0.0003

CYS 58 GLY 59 -0.0063

GLY 59 ILE 60 -0.0001

ILE 60 ILE 61 0.0003

ILE 61 VAL 62 -0.0002

VAL 62 TYR 63 -0.0046

TYR 63 ASN 64 -0.0003

ASN 64 GLU 65 -0.0002

GLU 65 SER 66 0.0002

SER 66 LYS 67 -0.0093

LYS 67 ARG 68 -0.0001

ARG 68 ILE 69 0.0002

ILE 69 LYS 70 0.0002

LYS 70 LYS 71 0.0071

LYS 71 CYS 72 0.0000

CYS 72 LEU 73 -0.0002

LEU 73 ASN 74 0.0001

ASN 74 SER 75 -0.0001

SER 75 VAL 76 0.0002

VAL 76 LYS 77 0.0003

LYS 77 ASP 78 0.0000

ASP 78 ASP 79 -0.0091

ASP 79 PHE 80 -0.0000

PHE 80 ASN 81 0.0001

ASN 81 GLU 82 -0.0003

GLU 82 ILE 83 -0.0095

ILE 83 ILE 84 0.0002

ILE 84 VAL 85 -0.0001

VAL 85 LEU 86 0.0001

LEU 86 ASP 87 -0.0042

ASP 87 SER 88 0.0003

SER 88 TYR 89 -0.0002

TYR 89 SER 90 0.0000

SER 90 THR 91 -0.0007

THR 91 ASP 92 0.0000

ASP 92 ASP 93 0.0000

ASP 93 THR 94 -0.0001

THR 94 VAL 95 -0.0037

VAL 95 ASP 96 0.0000

ASP 96 ILE 97 0.0002

ILE 97 ILE 98 -0.0003

ILE 98 LYS 99 -0.0025

LYS 99 CYS 100 0.0002

CYS 100 ASP 101 0.0003

ASP 101 PHE 102 0.0000

PHE 102 PRO 103 -0.0014

PRO 103 ASP 104 0.0003

ASP 104 VAL 105 0.0001

VAL 105 GLU 106 -0.0004

GLU 106 ILE 107 -0.0009

ILE 107 LYS 108 -0.0002

LYS 108 TYR 109 -0.0000

TYR 109 GLU 110 -0.0000

GLU 110 LYS 111 -0.0061

LYS 111 TRP 112 0.0001

TRP 112 LYS 113 0.0001

LYS 113 ASN 114 -0.0003

ASN 114 ASP 115 -0.0054

ASP 115 PHE 116 0.0003

PHE 116 SER 117 -0.0002

SER 117 TYR 118 -0.0001

TYR 118 ALA 119 0.0026

ALA 119 ARG 120 -0.0001

ARG 120 ASN 121 0.0000

ASN 121 LYS 122 0.0001

LYS 122 ILE 123 -0.0064

ILE 123 ILE 124 0.0002

ILE 124 GLU 125 0.0003

GLU 125 TYR 126 0.0001

TYR 126 ALA 127 -0.0159

ALA 127 THR 128 -0.0001

THR 128 SER 129 -0.0001

SER 129 GLU 130 0.0004

GLU 130 TRP 131 0.0023

TRP 131 ILE 132 0.0000

ILE 132 TYR 133 0.0003

TYR 133 PHE 134 -0.0001

PHE 134 ILE 135 -0.0111

ILE 135 ASP 136 -0.0000

ASP 136 ALA 137 -0.0002

ALA 137 ASP 138 0.0005

ASP 138 ASN 139 0.0023

ASN 139 LEU 140 0.0001

LEU 140 TYR 141 -0.0002

TYR 141 SER 142 0.0001

SER 142 LYS 143 -0.0065

LYS 143 GLU 144 0.0002

GLU 144 ASN 145 -0.0003

ASN 145 LYS 146 -0.0001

LYS 146 GLY 147 0.0218

GLY 147 LYS 148 -0.0002

LYS 148 ILE 149 -0.0001

ILE 149 ALA 150 -0.0000

ALA 150 LYS 151 -0.0115

LYS 151 VAL 152 -0.0005

VAL 152 ALA 153 -0.0001

ALA 153 ARG 154 0.0000

ARG 154 VAL 155 -0.0031

VAL 155 LEU 156 0.0003

LEU 156 GLU 157 0.0001

GLU 157 PHE 158 -0.0001

PHE 158 PHE 159 -0.0011

PHE 159 SER 160 0.0001

SER 160 ILE 161 0.0001

ILE 161 ASP 162 0.0001

ASP 162 CYS 163 -0.0016

CYS 163 VAL 164 -0.0002

VAL 164 VAL 165 0.0002

VAL 165 SER 166 0.0000

SER 166 PRO 167 0.0029

PRO 167 TYR 168 -0.0004

TYR 168 ILE 169 -0.0002

ILE 169 GLU 170 0.0003

GLU 170 GLU 171 0.0177

GLU 171 TYR 172 0.0000

TYR 172 THR 173 -0.0002

THR 173 GLY 174 -0.0002

GLY 174 HIS 175 -0.0099

HIS 175 LEU 176 -0.0004

LEU 176 TYR 177 0.0003

TYR 177 SER 178 -0.0004

SER 178 ASP 179 -0.0205

ASP 179 THR 180 0.0001

THR 180 ARG 181 -0.0001

ARG 181 ARG 182 -0.0004

ARG 182 MET 183 0.0021

MET 183 PHE 184 -0.0003

PHE 184 ARG 185 0.0001

ARG 185 LEU 186 -0.0000

LEU 186 ASN 187 0.0037

ASN 187 GLY 188 -0.0000

GLY 188 LYS 189 0.0001

LYS 189 VAL 190 0.0001

VAL 190 LYS 191 -0.0185

LYS 191 PHE 192 0.0001

PHE 192 HIS 193 0.0001

HIS 193 GLY 194 0.0005

GLY 194 LYS 195 -0.0334

LYS 195 VAL 196 0.0001

VAL 196 HIS 197 -0.0004

HIS 197 GLU 198 0.0001

GLU 198 GLU 199 -0.0186

GLU 199 PRO 200 0.0003

PRO 200 MET 201 0.0002

MET 201 ASN 202 -0.0001

ASN 202 TYR 203 -0.0010

TYR 203 ASN 204 -0.0001

ASN 204 HIS 205 -0.0003

HIS 205 SER 206 0.0002

SER 206 LEU 207 0.0112

LEU 207 PRO 208 0.0001

PRO 208 PHE 209 -0.0001

PHE 209 ASN 210 -0.0001

ASN 210 PHE 211 -0.0051

PHE 211 ILE 212 -0.0001

ILE 212 VAL 213 -0.0003

VAL 213 ASN 214 0.0004

ASN 214 LEU 215 0.0079

LEU 215 LYS 216 -0.0002

LYS 216 VAL 217 -0.0002

VAL 217 TYR 218 0.0001

TYR 218 HIS 219 0.0121

HIS 219 ASN 220 -0.0003

ASN 220 GLY 221 0.0000

GLY 221 TYR 222 -0.0005

TYR 222 ASN 223 -0.0054

ASN 223 PRO 224 -0.0002

PRO 224 SER 225 0.0001

SER 225 GLU 226 0.0003

GLU 226 ASN 227 -0.0054

ASN 227 ASN 228 0.0000

ASN 228 ILE 229 -0.0002

ILE 229 LYS 230 0.0001

LYS 230 SER 231 0.0044

SER 231 LYS 232 0.0004

LYS 232 THR 233 0.0001

THR 233 ARG 234 0.0003

ARG 234 ARG 235 -0.0333

ARG 235 ASN 236 0.0000

ASN 236 ILE 237 0.0001

ILE 237 ASN 238 -0.0001

ASN 238 LEU 239 -0.0148

LEU 239 THR 240 0.0001

THR 240 GLU 241 0.0004

GLU 241 GLU 242 -0.0002

GLU 242 MET 243 0.0074

MET 243 LEU 244 0.0000

LEU 244 ARG 245 0.0001

ARG 245 LEU 246 0.0002

LEU 246 GLU 247 0.0155

GLU 247 PRO 248 0.0001

PRO 248 GLU 249 -0.0002

GLU 249 ASN 250 0.0001

ASN 250 PRO 251 0.0060

PRO 251 LYS 252 -0.0003

LYS 252 TRP 253 0.0001

TRP 253 LEU 254 -0.0001

LEU 254 PHE 255 -0.0024

PHE 255 PHE 256 -0.0001

PHE 256 PHE 257 -0.0001

PHE 257 GLY 258 0.0004

GLY 258 ARG 259 -0.0076

ARG 259 GLU 260 0.0002

GLU 260 LEU 261 -0.0001

LEU 261 HIS 262 -0.0001

HIS 262 LEU 263 -0.0119

LEU 263 LEU 264 -0.0001

LEU 264 ASP 265 -0.0001

ASP 265 LYS 266 0.0001

LYS 266 ASP 267 -0.0117

ASP 267 GLU 268 -0.0001

GLU 268 GLU 269 0.0000

GLU 269 ALA 270 0.0001

ALA 270 ILE 271 0.0016

ILE 271 ASP 272 -0.0003

ASP 272 TYR 273 0.0001

TYR 273 LEU 274 0.0001

LEU 274 LYS 275 -0.0058

LYS 275 LYS 276 0.0004

LYS 276 SER 277 -0.0001

SER 277 ILE 278 0.0002

ILE 278 ASN 279 -0.0044

ASN 279 ASN 280 0.0002

ASN 280 TYR 281 -0.0002

TYR 281 LYS 282 0.0000

LYS 282 LYS 283 0.0021

LYS 283 PHE 284 -0.0004

PHE 284 ASN 285 -0.0003

ASN 285 ASP 286 -0.0001

ASP 286 GLN 287 0.0187

GLN 287 ARG 288 0.0002

ARG 288 HIS 289 0.0000

HIS 289 PHE 290 -0.0003

PHE 290 ILE 291 0.0212

ILE 291 ASP 292 0.0002

ASP 292 ALA 293 0.0002

ALA 293 LEU 294 0.0001

LEU 294 VAL 295 0.0007

VAL 295 LEU 296 -0.0003

LEU 296 LEU 297 -0.0000

LEU 297 CYS 298 -0.0001

CYS 298 THR 299 -0.0085

THR 299 LEU 300 0.0003

LEU 300 LEU 301 -0.0000

LEU 301 LEU 302 -0.0001

LEU 302 GLN 303 -0.0054

GLN 303 ARG 304 -0.0000

ARG 304 ASN 305 -0.0002

ASN 305 ASN 306 0.0000

ASN 306 TYR 307 -0.0095

TYR 307 VAL 308 0.0002

VAL 308 ASP 309 -0.0002

ASP 309 LEU 310 0.0003

LEU 310 THR 311 0.0012

THR 311 LEU 312 -0.0002

LEU 312 TYR 313 -0.0003

TYR 313 LEU 314 0.0001

LEU 314 ASP 315 -0.0060

ASP 315 ILE 316 0.0001

ILE 316 LEU 317 0.0003

LEU 317 GLU 318 -0.0000

GLU 318 THR 319 0.0086

THR 319 GLU 320 0.0002

GLU 320 TYR 321 0.0002

TYR 321 PRO 322 0.0001

PRO 322 ARG 323 -0.0248

ARG 323 CYS 324 0.0000

CYS 324 VAL 325 0.0001

VAL 325 ASP 326 -0.0004

ASP 326 VAL 327 0.0063

VAL 327 ASP 328 0.0002

ASP 328 TYR 329 -0.0002

TYR 329 PHE 330 0.0001

PHE 330 ARG 331 -0.0064

ARG 331 SER 332 0.0001

SER 332 ALA 333 0.0001

ALA 333 ILE 334 0.0005

ILE 334 LEU 335 -0.0329

LEU 335 LYS 2 -0.0047

LYS 2 LEU 3 -0.0000

LEU 3 SER 4 0.0002

SER 4 ASP 5 0.0003

ASP 5 ILE 6 0.0003

ILE 6 TYR 7 -0.0004

TYR 7 LEU 8 0.0003

LEU 8 GLU 9 -0.0002

GLU 9 LEU 10 -0.0017

LEU 10 LYS 11 0.0002

LYS 11 LYS 12 0.0002

LYS 12 GLY 13 0.0004

GLY 13 TYR 14 -0.0045

TYR 14 ALA 15 -0.0001

ALA 15 ASP 16 -0.0001

ASP 16 SER 17 -0.0000

SER 17 LEU 18 -0.0014

LEU 18 LEU 19 0.0001

LEU 19 TYR 20 0.0000

TYR 20 SER 21 -0.0002

SER 21 ASP 22 0.0002

ASP 22 LEU 23 0.0000

LEU 23 SER 24 -0.0000

SER 24 LEU 25 0.0001

LEU 25 LEU 26 -0.0033

LEU 26 VAL 27 0.0000

VAL 27 ASN 28 -0.0001

ASN 28 ILE 29 0.0005

ILE 29 MET 30 -0.0005

MET 30 GLU 31 0.0003

GLU 31 TYR 32 -0.0002

TYR 32 GLU 33 0.0001

GLU 33 LYS 34 0.0046

LYS 34 ASP 35 0.0002

ASP 35 ILE 36 -0.0001

ILE 36 ASP 37 -0.0000

ASP 37 VAL 38 0.0012

VAL 38 MET 39 0.0001

MET 39 SER 40 -0.0002

SER 40 ILE 41 -0.0002

ILE 41 GLN 42 0.0012

GLN 42 SER 43 -0.0004

SER 43 LEU 44 0.0001

LEU 44 VAL 45 -0.0004

VAL 45 ALA 46 -0.0029

ALA 46 GLY 47 -0.0001

GLY 47 TYR 48 0.0000

TYR 48 GLU 49 0.0001

GLU 49 LYS 50 -0.0003

LYS 50 SER 51 -0.0001

SER 51 ASP 52 0.0000

ASP 52 THR 53 0.0003

THR 53 PRO 54 -0.0200

PRO 54 THR 55 -0.0003

THR 55 ILE 56 0.0003

ILE 56 THR 57 -0.0000

THR 57 CYS 58 -0.0119

CYS 58 GLY 59 0.0000

GLY 59 ILE 60 -0.0004

ILE 60 ILE 61 0.0004

ILE 61 VAL 62 -0.0050

VAL 62 TYR 63 -0.0005

TYR 63 ASN 64 0.0002

ASN 64 GLU 65 -0.0004

GLU 65 SER 66 0.0046

SER 66 LYS 67 0.0004

LYS 67 ARG 68 0.0003

ARG 68 ILE 69 -0.0002

ILE 69 LYS 70 0.0015

LYS 70 LYS 71 0.0002

LYS 71 CYS 72 0.0001

CYS 72 LEU 73 -0.0002

LEU 73 ASN 74 0.0247

ASN 74 SER 75 0.0003

SER 75 VAL 76 0.0001

VAL 76 LYS 77 0.0000

LYS 77 ASP 78 -0.0092

ASP 78 ASP 79 -0.0000

ASP 79 PHE 80 0.0001

PHE 80 ASN 81 0.0000

ASN 81 GLU 82 -0.0058

GLU 82 ILE 83 0.0003

ILE 83 ILE 84 0.0000

ILE 84 VAL 85 0.0004

VAL 85 LEU 86 0.0003

LEU 86 ASP 87 -0.0000

ASP 87 SER 88 0.0002

SER 88 TYR 89 -0.0001

TYR 89 SER 90 0.0035

SER 90 THR 91 0.0001

THR 91 ASP 92 -0.0001

ASP 92 ASP 93 0.0003

ASP 93 THR 94 0.0004

THR 94 VAL 95 -0.0001

VAL 95 ASP 96 0.0002

ASP 96 ILE 97 0.0001

ILE 97 ILE 98 -0.0033

ILE 98 LYS 99 0.0004

LYS 99 CYS 100 0.0001

CYS 100 ASP 101 -0.0002

ASP 101 PHE 102 -0.0016

PHE 102 PRO 103 -0.0001

PRO 103 ASP 104 0.0002

ASP 104 VAL 105 -0.0002

VAL 105 GLU 106 -0.0022

GLU 106 ILE 107 0.0006

ILE 107 LYS 108 -0.0003

LYS 108 TYR 109 -0.0002

TYR 109 GLU 110 -0.0035

GLU 110 LYS 111 -0.0003

LYS 111 TRP 112 -0.0000

TRP 112 LYS 113 0.0001

LYS 113 ASN 114 -0.0163

ASN 114 ASP 115 0.0003

ASP 115 PHE 116 -0.0000

PHE 116 SER 117 0.0000

SER 117 TYR 118 0.0079

TYR 118 ALA 119 -0.0002

ALA 119 ARG 120 0.0001

ARG 120 ASN 121 0.0001

ASN 121 LYS 122 0.0112

LYS 122 ILE 123 -0.0001

ILE 123 ILE 124 0.0002

ILE 124 GLU 125 0.0001

GLU 125 TYR 126 0.0017

TYR 126 ALA 127 -0.0002

ALA 127 THR 128 0.0005

THR 128 SER 129 -0.0000

SER 129 GLU 130 -0.0123

GLU 130 TRP 131 -0.0002

TRP 131 ILE 132 -0.0000

ILE 132 TYR 133 0.0002

TYR 133 PHE 134 -0.0097

PHE 134 ILE 135 -0.0001

ILE 135 ASP 136 0.0001

ASP 136 ALA 137 -0.0003

ALA 137 ASP 138 -0.0060

ASP 138 ASN 139 -0.0002

ASN 139 LEU 140 0.0001

LEU 140 TYR 141 0.0002

TYR 141 SER 142 0.0159

SER 142 LYS 143 0.0002

LYS 143 GLU 144 -0.0003

GLU 144 ASN 145 0.0002

ASN 145 LYS 146 0.0064

LYS 146 GLY 147 0.0002

GLY 147 LYS 148 0.0003

LYS 148 ILE 149 0.0001

ILE 149 ALA 150 0.0108

ALA 150 LYS 151 -0.0002

LYS 151 VAL 152 0.0001

VAL 152 ALA 153 0.0003

ALA 153 ARG 154 -0.0010

ARG 154 VAL 155 -0.0000

VAL 155 LEU 156 -0.0002

LEU 156 GLU 157 -0.0000

GLU 157 PHE 158 -0.0212

PHE 158 PHE 159 -0.0001

PHE 159 SER 160 -0.0002

SER 160 ILE 161 -0.0001

ILE 161 ASP 162 -0.0056

ASP 162 CYS 163 -0.0001

CYS 163 VAL 164 -0.0002

VAL 164 VAL 165 -0.0001

VAL 165 SER 166 0.0036

SER 166 PRO 167 -0.0001

PRO 167 TYR 168 -0.0004

TYR 168 ILE 169 0.0001

ILE 169 GLU 170 0.0139

GLU 170 GLU 171 -0.0002

GLU 171 TYR 172 0.0001

TYR 172 THR 173 0.0001

THR 173 GLY 174 0.0265

GLY 174 HIS 175 -0.0002

HIS 175 LEU 176 -0.0000

LEU 176 TYR 177 0.0000

TYR 177 SER 178 0.0236

SER 178 ASP 179 -0.0000

ASP 179 THR 180 -0.0004

THR 180 ARG 181 0.0005

ARG 181 ARG 182 0.0108

ARG 182 MET 183 -0.0001

MET 183 PHE 184 0.0000

PHE 184 ARG 185 0.0004

ARG 185 LEU 186 -0.0062

LEU 186 ASN 187 0.0001

ASN 187 GLY 188 0.0003

GLY 188 LYS 189 -0.0003

LYS 189 VAL 190 -0.0152

VAL 190 LYS 191 0.0001

LYS 191 PHE 192 -0.0000

PHE 192 HIS 193 0.0001

HIS 193 GLY 194 -0.0460

GLY 194 LYS 195 -0.0000

LYS 195 VAL 196 -0.0001

VAL 196 HIS 197 -0.0001

HIS 197 GLU 198 -0.0164

GLU 198 GLU 199 0.0002

GLU 199 PRO 200 0.0001

PRO 200 MET 201 -0.0004

MET 201 ASN 202 -0.0037

ASN 202 TYR 203 0.0002

TYR 203 ASN 204 -0.0000

ASN 204 HIS 205 0.0002

HIS 205 SER 206 -0.0018

SER 206 LEU 207 0.0002

LEU 207 PRO 208 0.0004

PRO 208 PHE 209 0.0002

PHE 209 ASN 210 -0.0061

ASN 210 PHE 211 0.0000

PHE 211 ILE 212 -0.0003

ILE 212 VAL 213 -0.0001

VAL 213 ASN 214 -0.0057

ASN 214 LEU 215 -0.0000

LEU 215 LYS 216 -0.0001

LYS 216 VAL 217 0.0001

VAL 217 TYR 218 0.0116

TYR 218 HIS 219 0.0000

HIS 219 ASN 220 0.0002

ASN 220 GLY 221 -0.0000

GLY 221 TYR 222 0.0077

TYR 222 ASN 223 0.0001

ASN 223 PRO 224 0.0002

PRO 224 SER 225 -0.0001

SER 225 GLU 226 0.0123

GLU 226 ASN 227 -0.0001

ASN 227 ASN 228 0.0001

ASN 228 ILE 229 0.0001

ILE 229 LYS 230 0.0168

LYS 230 SER 231 -0.0002

SER 231 LYS 232 0.0000

LYS 232 THR 233 -0.0002

THR 233 ARG 234 0.0038

ARG 234 ARG 235 0.0002

ARG 235 ASN 236 -0.0002

ASN 236 ILE 237 -0.0000

ILE 237 ASN 238 -0.0219

ASN 238 LEU 239 -0.0002

LEU 239 THR 240 0.0001

THR 240 GLU 241 0.0002

GLU 241 GLU 242 -0.0071

GLU 242 MET 243 0.0002

MET 243 LEU 244 0.0001

LEU 244 ARG 245 0.0003

ARG 245 LEU 246 0.0044

LEU 246 GLU 247 -0.0004

GLU 247 PRO 248 -0.0000

PRO 248 GLU 249 0.0003

GLU 249 ASN 250 -0.0075

ASN 250 PRO 251 -0.0004

PRO 251 LYS 252 0.0001

LYS 252 TRP 253 0.0000

TRP 253 LEU 254 -0.0122

LEU 254 PHE 255 0.0001

PHE 255 PHE 256 0.0000

PHE 256 PHE 257 0.0003

PHE 257 GLY 258 -0.0129

GLY 258 ARG 259 -0.0000

ARG 259 GLU 260 -0.0000

GLU 260 LEU 261 -0.0000

LEU 261 HIS 262 -0.0132

HIS 262 LEU 263 -0.0001

LEU 263 LEU 264 -0.0004

LEU 264 ASP 265 -0.0000

ASP 265 LYS 266 0.0196

LYS 266 ASP 267 -0.0002

ASP 267 GLU 268 -0.0001

GLU 268 GLU 269 0.0001

GLU 269 ALA 270 0.0005

ALA 270 ILE 271 -0.0004

ILE 271 ASP 272 -0.0001

ASP 272 TYR 273 -0.0002

TYR 273 LEU 274 0.0072

LEU 274 LYS 275 0.0002

LYS 275 LYS 276 -0.0001

LYS 276 SER 277 -0.0003

SER 277 ILE 278 -0.0014

ILE 278 ASN 279 -0.0002

ASN 279 ASN 280 0.0004

ASN 280 TYR 281 0.0002

TYR 281 LYS 282 0.0007

LYS 282 LYS 283 0.0005

LYS 283 PHE 284 0.0001

PHE 284 ASN 285 -0.0005

ASN 285 ASP 286 -0.0213

ASP 286 GLN 287 0.0002

GLN 287 ARG 288 -0.0003

ARG 288 HIS 289 0.0002

HIS 289 PHE 290 0.0371

PHE 290 ILE 291 0.0004

ILE 291 ASP 292 -0.0000

ASP 292 ALA 293 0.0003

ALA 293 LEU 294 0.0234

LEU 294 VAL 295 -0.0000

VAL 295 LEU 296 0.0000

LEU 296 LEU 297 0.0002

LEU 297 CYS 298 -0.0014

CYS 298 THR 299 0.0001

THR 299 LEU 300 0.0000

LEU 300 LEU 301 -0.0002

LEU 301 LEU 302 -0.0257

LEU 302 GLN 303 0.0000

GLN 303 ARG 304 0.0004

ARG 304 ASN 305 -0.0000

ASN 305 ASN 306 0.0213

ASN 306 TYR 307 -0.0001

TYR 307 VAL 308 -0.0001

VAL 308 ASP 309 0.0001

ASP 309 LEU 310 0.0027

LEU 310 THR 311 -0.0002

THR 311 LEU 312 -0.0000

LEU 312 TYR 313 -0.0000

TYR 313 LEU 314 -0.0005

LEU 314 ASP 315 0.0002

ASP 315 ILE 316 0.0003

ILE 316 LEU 317 0.0003

LEU 317 GLU 318 -0.0213

GLU 318 THR 319 -0.0001

THR 319 GLU 320 -0.0003

GLU 320 TYR 321 -0.0001

TYR 321 PRO 322 0.0061

PRO 322 ARG 323 0.0000

ARG 323 CYS 324 0.0001

CYS 324 VAL 325 0.0001

VAL 325 ASP 326 -0.0249

ASP 326 VAL 327 0.0003

VAL 327 ASP 328 0.0001

ASP 328 TYR 329 0.0001

TYR 329 PHE 330 -0.0002

PHE 330 ARG 331 0.0001

ARG 331 SER 332 0.0003

SER 332 ALA 333 0.0001

ALA 333 ILE 334 -0.0204

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.

*** BIOSYNTHETIC PROTEIN 11-MAY-21 7MSP ***

CA strain for 2605100231101288398

--- normal mode 7 ---

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

* BIOSYNTHETIC PROTEIN 11-MAY-21 7MSP *