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

* EXSA_dimer1 *

CA strain for 2401041206373816311

--- normal mode 23 ---

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 GLN 2 0.0002

GLN 2 GLY 3 -0.1098

GLY 3 ALA 4 0.0002

ALA 4 LYS 5 -0.0000

LYS 5 SER 6 0.1840

SER 6 LEU 7 -0.0001

LEU 7 GLY 8 -0.0001

GLY 8 ARG 9 -0.0139

ARG 9 LYS 10 -0.0001

LYS 10 GLN 11 -0.0001

GLN 11 ILE 12 0.0265

ILE 12 THR 13 0.0003

THR 13 SER 14 -0.0002

SER 14 CYS 15 -0.2418

CYS 15 HIS 16 0.0000

HIS 16 TRP 17 -0.0001

TRP 17 ASN 18 -0.0616

ASN 18 ILE 19 -0.0002

ILE 19 PRO 20 0.0000

PRO 20 THR 21 -0.0135

THR 21 PHE 22 0.0002

PHE 22 GLU 23 0.0002

GLU 23 TYR 24 0.0947

TYR 24 ARG 25 -0.0000

ARG 25 VAL 26 -0.0000

VAL 26 ASN 27 -0.0612

ASN 27 LYS 28 0.0001

LYS 28 GLU 29 -0.0002

GLU 29 GLU 30 0.0249

GLU 30 GLY 31 0.0000

GLY 31 VAL 32 0.0000

VAL 32 TYR 33 0.0166

TYR 33 VAL 34 -0.0000

VAL 34 LEU 35 -0.0001

LEU 35 LEU 36 -0.0144

LEU 36 GLU 37 0.0003

GLU 37 GLY 38 0.0000

GLY 38 GLU 39 0.0643

GLU 39 LEU 40 0.0001

LEU 40 THR 41 0.0001

THR 41 VAL 42 -0.0023

VAL 42 GLN 43 0.0002

GLN 43 ASP 44 0.0000

ASP 44 ILE 45 -0.0311

ILE 45 ASP 46 0.0005

ASP 46 SER 47 -0.0002

SER 47 THR 48 0.0520

THR 48 PHE 49 -0.0002

PHE 49 CYS 50 0.0000

CYS 50 LEU 51 0.0745

LEU 51 ALA 52 0.0002

ALA 52 PRO 53 0.0003

PRO 53 GLY 54 -0.0881

GLY 54 GLU 55 -0.0001

GLU 55 LEU 56 0.0002

LEU 56 LEU 57 -0.0116

LEU 57 PHE 58 -0.0001

PHE 58 VAL 59 0.0001

VAL 59 ARG 60 -0.0177

ARG 60 ARG 61 0.0001

ARG 61 GLY 62 0.0004

GLY 62 SER 63 0.1076

SER 63 TYR 64 0.0001

TYR 64 VAL 65 -0.0001

VAL 65 VAL 66 -0.0225

VAL 66 SER 67 0.0001

SER 67 THR 68 -0.0003

THR 68 LYS 69 0.0063

LYS 69 GLY 70 -0.0000

GLY 70 LYS 71 -0.0003

LYS 71 ASP 72 -0.0429

ASP 72 SER 73 -0.0001

SER 73 ARG 74 -0.0002

ARG 74 ILE 75 0.0706

ILE 75 LEU 76 0.0002

LEU 76 TRP 77 -0.0002

TRP 77 ILE 78 0.0104

ILE 78 PRO 79 0.0004

PRO 79 LEU 80 -0.0004

LEU 80 SER 81 -0.0459

SER 81 ALA 82 -0.0001

ALA 82 GLN 83 0.0003

GLN 83 PHE 84 -0.1826

PHE 84 LEU 85 -0.0003

LEU 85 GLN 86 0.0005

GLN 86 GLY 87 -0.0643

GLY 87 PHE 88 0.0003

PHE 88 VAL 89 0.0000

VAL 89 GLN 90 0.0382

GLN 90 ARG 91 0.0001

ARG 91 PHE 92 -0.0002

PHE 92 GLY 93 0.2011

GLY 93 ALA 94 -0.0003

ALA 94 LEU 95 -0.0001

LEU 95 LEU 96 -0.0228

LEU 96 SER 97 0.0004

SER 97 GLU 98 0.0003

GLU 98 VAL 99 -0.0501

VAL 99 GLU 100 0.0004

GLU 100 ARG 101 -0.0002

ARG 101 CYS 102 0.0080

CYS 102 ASP 103 0.0002

ASP 103 GLU 104 0.0002

GLU 104 PRO 105 0.0657

PRO 105 VAL 106 0.0001

VAL 106 PRO 107 0.0003

PRO 107 GLY 108 0.1199

GLY 108 ILE 109 0.0006

ILE 109 ILE 110 -0.0004

ILE 110 ALA 111 -0.0009

ALA 111 PHE 112 0.0000

PHE 112 ALA 113 0.0001

ALA 113 ALA 114 -0.0104

ALA 114 THR 115 0.0002

THR 115 PRO 116 -0.0004

PRO 116 LEU 117 0.0249

LEU 117 LEU 118 -0.0000

LEU 118 ALA 119 -0.0002

ALA 119 GLY 120 0.1115

GLY 120 CYS 121 -0.0000

CYS 121 VAL 122 -0.0003

VAL 122 LYS 123 0.0523

LYS 123 GLY 124 -0.0001

GLY 124 LEU 125 0.0002

LEU 125 LYS 126 0.0178

LYS 126 GLU 127 0.0002

GLU 127 LEU 128 -0.0004

LEU 128 LEU 129 -0.0507

LEU 129 VAL 130 0.0001

VAL 130 HIS 131 -0.0002

HIS 131 GLU 132 0.0177

GLU 132 HIS 133 -0.0001

HIS 133 PRO 134 0.0003

PRO 134 PRO 135 -0.0337

PRO 135 MET 136 -0.0003

MET 136 LEU 137 0.0001

LEU 137 ALA 138 0.0023

ALA 138 CYS 139 -0.0000

CYS 139 LEU 140 0.0002

LEU 140 LYS 141 0.0167

LYS 141 ILE 142 -0.0001

ILE 142 GLU 143 0.0002

GLU 143 GLU 144 -0.0212

GLU 144 LEU 145 -0.0000

LEU 145 LEU 146 -0.0001

LEU 146 MET 147 -0.0355

MET 147 LEU 148 0.0002

LEU 148 PHE 149 0.0001

PHE 149 ALA 150 -0.0017

ALA 150 PHE 151 0.0001

PHE 151 SER 152 0.0003

SER 152 PRO 153 0.0527

PRO 153 GLN 154 0.0004

GLN 154 GLY 155 -0.0000

GLY 155 PRO 156 -0.0086

PRO 156 LEU 157 -0.0001

LEU 157 LEU 158 -0.0002

LEU 158 MET 159 -0.0161

MET 159 SER 160 0.0003

SER 160 VAL 161 -0.0002

VAL 161 LEU 162 -0.0112

LEU 162 ARG 163 0.0003

ARG 163 GLN 164 0.0000

GLN 164 LEU 165 0.0469

LEU 165 SER 166 0.0002

SER 166 ASN 167 0.0004

ASN 167 ARG 168 0.0056

ARG 168 HIS 169 -0.0001

HIS 169 VAL 170 0.0006

VAL 170 GLU 171 -0.0574

GLU 171 ARG 172 0.0001

ARG 172 LEU 173 -0.0001

LEU 173 GLN 174 0.0016

GLN 174 LEU 175 -0.0001

LEU 175 PHE 176 0.0002

PHE 176 MET 177 0.1199

MET 177 GLU 178 -0.0004

GLU 178 LYS 179 0.0002

LYS 179 HIS 180 0.1120

HIS 180 TYR 181 0.0003

TYR 181 LEU 182 0.0004

LEU 182 ASN 183 -0.0771

ASN 183 GLU 184 0.0000

GLU 184 TRP 185 -0.0002

TRP 185 LYS 186 -0.0737

LYS 186 LEU 187 0.0001

LEU 187 SER 188 -0.0002

SER 188 ASP 189 -0.0066

ASP 189 PHE 190 -0.0003

PHE 190 SER 191 0.0001

SER 191 ARG 192 -0.0161

ARG 192 GLU 193 -0.0001

GLU 193 PHE 194 0.0001

PHE 194 GLY 195 -0.0338

GLY 195 MET 196 0.0001

MET 196 GLY 197 -0.0000

GLY 197 LEU 198 0.0058

LEU 198 THR 199 -0.0002

THR 199 THR 200 -0.0000

THR 200 PHE 201 -0.0181

PHE 201 LYS 202 0.0001

LYS 202 GLU 203 -0.0004

GLU 203 LEU 204 -0.0484

LEU 204 PHE 205 0.0001

PHE 205 GLY 206 -0.0003

GLY 206 SER 207 -0.0416

SER 207 VAL 208 0.0002

VAL 208 TYR 209 -0.0001

TYR 209 GLY 210 -0.0605

GLY 210 VAL 211 -0.0001

VAL 211 SER 212 -0.0001

SER 212 PRO 213 0.0139

PRO 213 ARG 214 0.0002

ARG 214 ALA 215 0.0001

ALA 215 TRP 216 -0.0231

TRP 216 ILE 217 -0.0002

ILE 217 SER 218 -0.0003

SER 218 GLU 219 -0.0765

GLU 219 ARG 220 -0.0002

ARG 220 ARG 221 -0.0001

ARG 221 ILE 222 0.0379

ILE 222 LEU 223 0.0003

LEU 223 TYR 224 -0.0002

TYR 224 ALA 225 0.0536

ALA 225 HIS 226 -0.0002

HIS 226 GLN 227 0.0001

GLN 227 LEU 228 -0.0071

LEU 228 LEU 229 0.0001

LEU 229 LEU 230 -0.0001

LEU 230 ASN 231 0.0508

ASN 231 SER 232 0.0003

SER 232 ASP 233 -0.0001

ASP 233 MET 234 -0.0283

MET 234 SER 235 -0.0001

SER 235 ILE 236 0.0003

ILE 236 VAL 237 -0.0046

VAL 237 ASP 238 -0.0001

ASP 238 ILE 239 0.0001

ILE 239 ALA 240 -0.0661

ALA 240 MET 241 -0.0004

MET 241 GLU 242 0.0001

GLU 242 ALA 243 -0.0216

ALA 243 GLY 244 -0.0001

GLY 244 PHE 245 -0.0003

PHE 245 SER 246 -0.0171

SER 246 SER 247 0.0003

SER 247 GLN 248 0.0000

GLN 248 SER 249 0.0141

SER 249 TYR 250 -0.0001

TYR 250 PHE 251 0.0000

PHE 251 THR 252 0.0001

THR 252 GLN 253 -0.0001

GLN 253 SER 254 -0.0002

SER 254 TYR 255 -0.0180

TYR 255 ARG 256 -0.0000

ARG 256 ARG 257 -0.0000

ARG 257 ARG 258 -0.0016

ARG 258 PHE 259 0.0002

PHE 259 GLY 260 -0.0001

GLY 260 CYS 261 0.0021

CYS 261 THR 262 0.0000

THR 262 PRO 263 -0.0003

PRO 263 SER 264 0.0020

SER 264 ARG 265 -0.0003

ARG 265 SER 266 -0.0000

SER 266 ARG 267 0.0090

ARG 267 GLN 268 -0.0001

GLN 268 GLY 269 0.0002

GLY 269 LYS 270 0.0311

LYS 270 ASP 271 0.0003

ASP 271 GLU 272 -0.0003

GLU 272 CYS 273 0.0037

CYS 273 ARG 274 -0.0002

ARG 274 ALA 275 -0.0000

ALA 275 LYS 276 0.2490

LYS 276 ASN 277 -0.0001

ASN 277 ASN 278 -0.0000

ASN 278 NMA 278 0.0001

NMA 278 MET 1 -0.0053

MET 1 GLN 2 0.0000

GLN 2 GLY 3 -0.1394

GLY 3 ALA 4 0.0000

ALA 4 LYS 5 -0.0003

LYS 5 SER 6 0.2805

SER 6 LEU 7 -0.0001

LEU 7 GLY 8 -0.0002

GLY 8 ARG 9 0.0232

ARG 9 LYS 10 -0.0000

LYS 10 GLN 11 0.0001

GLN 11 ILE 12 0.0018

ILE 12 THR 13 0.0001

THR 13 SER 14 -0.0001

SER 14 CYS 15 -0.2985

CYS 15 HIS 16 0.0003

HIS 16 TRP 17 0.0001

TRP 17 ASN 18 -0.1206

ASN 18 ILE 19 -0.0002

ILE 19 PRO 20 -0.0003

PRO 20 THR 21 -0.0204

THR 21 PHE 22 0.0001

PHE 22 GLU 23 0.0001

GLU 23 TYR 24 0.0107

TYR 24 ARG 25 -0.0001

ARG 25 VAL 26 0.0001

VAL 26 ASN 27 -0.0911

ASN 27 LYS 28 0.0000

LYS 28 GLU 29 -0.0001

GLU 29 GLU 30 0.0171

GLU 30 GLY 31 0.0004

GLY 31 VAL 32 -0.0001

VAL 32 TYR 33 -0.0089

TYR 33 VAL 34 -0.0002

VAL 34 LEU 35 0.0001

LEU 35 LEU 36 -0.0230

LEU 36 GLU 37 -0.0003

GLU 37 GLY 38 0.0004

GLY 38 GLU 39 0.0096

GLU 39 LEU 40 -0.0002

LEU 40 THR 41 0.0001

THR 41 VAL 42 -0.0020

VAL 42 GLN 43 0.0000

GLN 43 ASP 44 0.0002

ASP 44 ILE 45 -0.0199

ILE 45 ASP 46 -0.0002

ASP 46 SER 47 0.0001

SER 47 THR 48 0.0164

THR 48 PHE 49 0.0001

PHE 49 CYS 50 -0.0000

CYS 50 LEU 51 0.0168

LEU 51 ALA 52 0.0002

ALA 52 PRO 53 -0.0002

PRO 53 GLY 54 -0.0590

GLY 54 GLU 55 0.0001

GLU 55 LEU 56 -0.0001

LEU 56 LEU 57 -0.0162

LEU 57 PHE 58 -0.0002

PHE 58 VAL 59 -0.0004

VAL 59 ARG 60 0.0014

ARG 60 ARG 61 0.0001

ARG 61 GLY 62 0.0001

GLY 62 SER 63 0.0133

SER 63 TYR 64 0.0003

TYR 64 VAL 65 -0.0002

VAL 65 VAL 66 -0.0178

VAL 66 SER 67 0.0001

SER 67 THR 68 -0.0001

THR 68 LYS 69 -0.0138

LYS 69 GLY 70 0.0002

GLY 70 LYS 71 0.0001

LYS 71 ASP 72 -0.0904

ASP 72 SER 73 0.0001

SER 73 ARG 74 -0.0004

ARG 74 ILE 75 0.0447

ILE 75 LEU 76 0.0001

LEU 76 TRP 77 0.0001

TRP 77 ILE 78 -0.0491

ILE 78 PRO 79 -0.0004

PRO 79 LEU 80 0.0002

LEU 80 SER 81 -0.0456

SER 81 ALA 82 0.0000

ALA 82 GLN 83 0.0003

GLN 83 PHE 84 -0.0322

PHE 84 LEU 85 0.0002

LEU 85 GLN 86 0.0004

GLN 86 GLY 87 -0.0467

GLY 87 PHE 88 0.0002

PHE 88 VAL 89 0.0002

VAL 89 GLN 90 0.0302

GLN 90 ARG 91 0.0000

ARG 91 PHE 92 0.0002

PHE 92 GLY 93 0.1037

GLY 93 ALA 94 0.0002

ALA 94 LEU 95 0.0001

LEU 95 LEU 96 -0.0272

LEU 96 SER 97 0.0001

SER 97 GLU 98 0.0001

GLU 98 VAL 99 -0.0766

VAL 99 GLU 100 0.0002

GLU 100 ARG 101 -0.0003

ARG 101 CYS 102 -0.0117

CYS 102 ASP 103 0.0001

ASP 103 GLU 104 -0.0001

GLU 104 PRO 105 0.0349

PRO 105 VAL 106 0.0006

VAL 106 PRO 107 -0.0002

PRO 107 GLY 108 0.0796

GLY 108 ILE 109 0.0001

ILE 109 ILE 110 0.0002

ILE 110 ALA 111 -0.0085

ALA 111 PHE 112 0.0001

PHE 112 ALA 113 0.0001

ALA 113 ALA 114 -0.0306

ALA 114 THR 115 -0.0003

THR 115 PRO 116 -0.0001

PRO 116 LEU 117 0.0216

LEU 117 LEU 118 -0.0000

LEU 118 ALA 119 -0.0001

ALA 119 GLY 120 0.0804

GLY 120 CYS 121 -0.0001

CYS 121 VAL 122 -0.0002

VAL 122 LYS 123 0.0386

LYS 123 GLY 124 -0.0001

GLY 124 LEU 125 -0.0000

LEU 125 LYS 126 0.0288

LYS 126 GLU 127 0.0002

GLU 127 LEU 128 0.0003

LEU 128 LEU 129 -0.0650

LEU 129 VAL 130 0.0001

VAL 130 HIS 131 -0.0001

HIS 131 GLU 132 -0.0245

GLU 132 HIS 133 0.0000

HIS 133 PRO 134 -0.0001

PRO 134 PRO 135 -0.0310

PRO 135 MET 136 0.0001

MET 136 LEU 137 -0.0000

LEU 137 ALA 138 -0.0047

ALA 138 CYS 139 -0.0004

CYS 139 LEU 140 -0.0002

LEU 140 LYS 141 -0.0068

LYS 141 ILE 142 -0.0000

ILE 142 GLU 143 0.0002

GLU 143 GLU 144 -0.0194

GLU 144 LEU 145 0.0001

LEU 145 LEU 146 -0.0001

LEU 146 MET 147 -0.0388

MET 147 LEU 148 -0.0000

LEU 148 PHE 149 -0.0003

PHE 149 ALA 150 -0.0224

ALA 150 PHE 151 -0.0002

PHE 151 SER 152 0.0001

SER 152 PRO 153 0.0405

PRO 153 GLN 154 0.0001

GLN 154 GLY 155 0.0002

GLY 155 PRO 156 0.0031

PRO 156 LEU 157 -0.0001

LEU 157 LEU 158 -0.0001

LEU 158 MET 159 -0.0183

MET 159 SER 160 0.0001

SER 160 VAL 161 0.0003

VAL 161 LEU 162 0.0062

LEU 162 ARG 163 -0.0002

ARG 163 GLN 164 0.0004

GLN 164 LEU 165 0.0494

LEU 165 SER 166 -0.0001

SER 166 ASN 167 0.0000

ASN 167 ARG 168 -0.0057

ARG 168 HIS 169 0.0002

HIS 169 VAL 170 0.0001

VAL 170 GLU 171 -0.0620

GLU 171 ARG 172 -0.0003

ARG 172 LEU 173 0.0001

LEU 173 GLN 174 0.0172

GLN 174 LEU 175 0.0002

LEU 175 PHE 176 -0.0000

PHE 176 MET 177 0.1511

MET 177 GLU 178 0.0004

GLU 178 LYS 179 -0.0001

LYS 179 HIS 180 0.1267

HIS 180 TYR 181 0.0001

TYR 181 LEU 182 0.0003

LEU 182 ASN 183 -0.0773

ASN 183 GLU 184 -0.0002

GLU 184 TRP 185 -0.0001

TRP 185 LYS 186 -0.0576

LYS 186 LEU 187 0.0001

LEU 187 SER 188 0.0004

SER 188 ASP 189 -0.0090

ASP 189 PHE 190 0.0003

PHE 190 SER 191 0.0002

SER 191 ARG 192 -0.0187

ARG 192 GLU 193 0.0001

GLU 193 PHE 194 -0.0002

PHE 194 GLY 195 -0.0368

GLY 195 MET 196 0.0002

MET 196 GLY 197 -0.0000

GLY 197 LEU 198 0.0071

LEU 198 THR 199 0.0002

THR 199 THR 200 0.0003

THR 200 PHE 201 -0.0090

PHE 201 LYS 202 -0.0001

LYS 202 GLU 203 0.0003

GLU 203 LEU 204 -0.0016

LEU 204 PHE 205 -0.0003

PHE 205 GLY 206 0.0002

GLY 206 SER 207 -0.0056

SER 207 VAL 208 0.0001

VAL 208 TYR 209 0.0001

TYR 209 GLY 210 -0.0237

GLY 210 VAL 211 0.0002

VAL 211 SER 212 -0.0003

SER 212 PRO 213 -0.0124

PRO 213 ARG 214 -0.0001

ARG 214 ALA 215 -0.0003

ALA 215 TRP 216 -0.0254

TRP 216 ILE 217 0.0002

ILE 217 SER 218 0.0003

SER 218 GLU 219 -0.0756

GLU 219 ARG 220 0.0000

ARG 220 ARG 221 0.0001

ARG 221 ILE 222 0.0302

ILE 222 LEU 223 -0.0003

LEU 223 TYR 224 0.0001

TYR 224 ALA 225 0.0250

ALA 225 HIS 226 -0.0000

HIS 226 GLN 227 -0.0001

GLN 227 LEU 228 -0.0165

LEU 228 LEU 229 0.0002

LEU 229 LEU 230 -0.0002

LEU 230 ASN 231 0.0663

ASN 231 SER 232 0.0003

SER 232 ASP 233 0.0002

ASP 233 MET 234 -0.0211

MET 234 SER 235 0.0003

SER 235 ILE 236 0.0000

ILE 236 VAL 237 -0.0100

VAL 237 ASP 238 -0.0002

ASP 238 ILE 239 -0.0001

ILE 239 ALA 240 -0.0574

ALA 240 MET 241 0.0003

MET 241 GLU 242 -0.0001

GLU 242 ALA 243 -0.0222

ALA 243 GLY 244 0.0000

GLY 244 PHE 245 0.0002

PHE 245 SER 246 -0.0039

SER 246 SER 247 0.0000

SER 247 GLN 248 -0.0003

GLN 248 SER 249 -0.0105

SER 249 TYR 250 0.0001

TYR 250 PHE 251 -0.0001

PHE 251 THR 252 0.0070

THR 252 GLN 253 -0.0004

GLN 253 SER 254 -0.0000

SER 254 TYR 255 0.0016

TYR 255 ARG 256 0.0001

ARG 256 ARG 257 0.0001

ARG 257 ARG 258 0.0428

ARG 258 PHE 259 -0.0002

PHE 259 GLY 260 0.0000

GLY 260 CYS 261 -0.0394

CYS 261 THR 262 0.0002

THR 262 PRO 263 -0.0001

PRO 263 SER 264 0.0148

SER 264 ARG 265 -0.0000

ARG 265 SER 266 -0.0001

SER 266 ARG 267 -0.0014

ARG 267 GLN 268 0.0003

GLN 268 GLY 269 -0.0000

GLY 269 LYS 270 0.0397

LYS 270 ASP 271 0.0002

ASP 271 GLU 272 -0.0001

GLU 272 CYS 273 0.0125

CYS 273 ARG 274 0.0002

ARG 274 ALA 275 0.0003

ALA 275 LYS 276 0.3237

LYS 276 ASN 277 -0.0002

ASN 277 ASN 278 0.0001

ASN 278 NMA 278 -0.0002

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.

*** EXSA_dimer1 ***

CA strain for 2401041206373816311

--- normal mode 23 ---

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

* EXSA_dimer1 *