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

* EXSA_dimer1 *

CA strain for 2401041206373816311

--- normal mode 15 ---

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 0.0067

GLY 3 ALA 4 -0.0004

ALA 4 LYS 5 0.0001

LYS 5 SER 6 -0.0888

SER 6 LEU 7 -0.0005

LEU 7 GLY 8 0.0002

GLY 8 ARG 9 0.1159

ARG 9 LYS 10 0.0001

LYS 10 GLN 11 0.0000

GLN 11 ILE 12 0.0173

ILE 12 THR 13 -0.0001

THR 13 SER 14 0.0001

SER 14 CYS 15 0.1143

CYS 15 HIS 16 -0.0002

HIS 16 TRP 17 -0.0000

TRP 17 ASN 18 0.0558

ASN 18 ILE 19 0.0000

ILE 19 PRO 20 -0.0004

PRO 20 THR 21 0.0025

THR 21 PHE 22 0.0001

PHE 22 GLU 23 0.0002

GLU 23 TYR 24 0.0256

TYR 24 ARG 25 -0.0001

ARG 25 VAL 26 0.0002

VAL 26 ASN 27 0.0104

ASN 27 LYS 28 -0.0001

LYS 28 GLU 29 0.0000

GLU 29 GLU 30 0.0174

GLU 30 GLY 31 0.0000

GLY 31 VAL 32 -0.0004

VAL 32 TYR 33 0.0032

TYR 33 VAL 34 0.0001

VAL 34 LEU 35 0.0000

LEU 35 LEU 36 0.0213

LEU 36 GLU 37 0.0000

GLU 37 GLY 38 -0.0004

GLY 38 GLU 39 0.0662

GLU 39 LEU 40 -0.0002

LEU 40 THR 41 0.0001

THR 41 VAL 42 -0.0235

VAL 42 GLN 43 0.0002

GLN 43 ASP 44 -0.0005

ASP 44 ILE 45 -0.0005

ILE 45 ASP 46 -0.0003

ASP 46 SER 47 0.0005

SER 47 THR 48 0.0281

THR 48 PHE 49 0.0000

PHE 49 CYS 50 -0.0002

CYS 50 LEU 51 0.0781

LEU 51 ALA 52 0.0000

ALA 52 PRO 53 -0.0003

PRO 53 GLY 54 -0.0156

GLY 54 GLU 55 -0.0000

GLU 55 LEU 56 0.0001

LEU 56 LEU 57 0.0575

LEU 57 PHE 58 0.0002

PHE 58 VAL 59 0.0000

VAL 59 ARG 60 0.0086

ARG 60 ARG 61 0.0003

ARG 61 GLY 62 -0.0002

GLY 62 SER 63 -0.0544

SER 63 TYR 64 -0.0001

TYR 64 VAL 65 -0.0002

VAL 65 VAL 66 0.0060

VAL 66 SER 67 0.0001

SER 67 THR 68 -0.0001

THR 68 LYS 69 0.0158

LYS 69 GLY 70 0.0003

GLY 70 LYS 71 0.0000

LYS 71 ASP 72 0.0666

ASP 72 SER 73 -0.0004

SER 73 ARG 74 0.0004

ARG 74 ILE 75 -0.0072

ILE 75 LEU 76 0.0003

LEU 76 TRP 77 0.0000

TRP 77 ILE 78 0.0513

ILE 78 PRO 79 0.0000

PRO 79 LEU 80 -0.0004

LEU 80 SER 81 0.1727

SER 81 ALA 82 -0.0000

ALA 82 GLN 83 0.0002

GLN 83 PHE 84 0.2241

PHE 84 LEU 85 -0.0002

LEU 85 GLN 86 0.0002

GLN 86 GLY 87 -0.0212

GLY 87 PHE 88 -0.0004

PHE 88 VAL 89 0.0004

VAL 89 GLN 90 -0.0406

GLN 90 ARG 91 0.0000

ARG 91 PHE 92 0.0002

PHE 92 GLY 93 -0.0499

GLY 93 ALA 94 0.0001

ALA 94 LEU 95 0.0004

LEU 95 LEU 96 0.0052

LEU 96 SER 97 0.0003

SER 97 GLU 98 -0.0003

GLU 98 VAL 99 -0.0139

VAL 99 GLU 100 0.0000

GLU 100 ARG 101 -0.0002

ARG 101 CYS 102 -0.1027

CYS 102 ASP 103 0.0001

ASP 103 GLU 104 0.0002

GLU 104 PRO 105 -0.0093

PRO 105 VAL 106 -0.0000

VAL 106 PRO 107 -0.0005

PRO 107 GLY 108 -0.0659

GLY 108 ILE 109 -0.0001

ILE 109 ILE 110 0.0002

ILE 110 ALA 111 0.0626

ALA 111 PHE 112 -0.0003

PHE 112 ALA 113 0.0001

ALA 113 ALA 114 0.0759

ALA 114 THR 115 0.0005

THR 115 PRO 116 -0.0004

PRO 116 LEU 117 -0.0217

LEU 117 LEU 118 -0.0000

LEU 118 ALA 119 0.0000

ALA 119 GLY 120 0.0748

GLY 120 CYS 121 0.0000

CYS 121 VAL 122 0.0002

VAL 122 LYS 123 0.0640

LYS 123 GLY 124 -0.0002

GLY 124 LEU 125 -0.0003

LEU 125 LYS 126 -0.0243

LYS 126 GLU 127 0.0001

GLU 127 LEU 128 -0.0001

LEU 128 LEU 129 0.0242

LEU 129 VAL 130 0.0002

VAL 130 HIS 131 0.0003

HIS 131 GLU 132 0.0535

GLU 132 HIS 133 -0.0004

HIS 133 PRO 134 0.0003

PRO 134 PRO 135 -0.0290

PRO 135 MET 136 0.0003

MET 136 LEU 137 -0.0003

LEU 137 ALA 138 -0.0071

ALA 138 CYS 139 0.0001

CYS 139 LEU 140 0.0003

LEU 140 LYS 141 -0.0135

LYS 141 ILE 142 -0.0004

ILE 142 GLU 143 -0.0002

GLU 143 GLU 144 0.0052

GLU 144 LEU 145 0.0001

LEU 145 LEU 146 -0.0004

LEU 146 MET 147 0.0277

MET 147 LEU 148 -0.0001

LEU 148 PHE 149 -0.0001

PHE 149 ALA 150 -0.0171

ALA 150 PHE 151 -0.0001

PHE 151 SER 152 0.0001

SER 152 PRO 153 0.0240

PRO 153 GLN 154 0.0002

GLN 154 GLY 155 0.0000

GLY 155 PRO 156 -0.0159

PRO 156 LEU 157 0.0002

LEU 157 LEU 158 0.0000

LEU 158 MET 159 -0.0364

MET 159 SER 160 -0.0004

SER 160 VAL 161 0.0001

VAL 161 LEU 162 -0.0425

LEU 162 ARG 163 -0.0000

ARG 163 GLN 164 0.0002

GLN 164 LEU 165 -0.0024

LEU 165 SER 166 0.0000

SER 166 ASN 167 -0.0004

ASN 167 ARG 168 -0.0394

ARG 168 HIS 169 -0.0003

HIS 169 VAL 170 0.0001

VAL 170 GLU 171 -0.0125

GLU 171 ARG 172 0.0002

ARG 172 LEU 173 -0.0002

LEU 173 GLN 174 0.0516

GLN 174 LEU 175 -0.0003

LEU 175 PHE 176 -0.0003

PHE 176 MET 177 0.0353

MET 177 GLU 178 -0.0001

GLU 178 LYS 179 0.0000

LYS 179 HIS 180 0.0208

HIS 180 TYR 181 -0.0001

TYR 181 LEU 182 0.0001

LEU 182 ASN 183 -0.0757

ASN 183 GLU 184 -0.0003

GLU 184 TRP 185 0.0001

TRP 185 LYS 186 -0.1996

LYS 186 LEU 187 -0.0000

LEU 187 SER 188 0.0001

SER 188 ASP 189 -0.0209

ASP 189 PHE 190 -0.0002

PHE 190 SER 191 -0.0001

SER 191 ARG 192 -0.0057

ARG 192 GLU 193 0.0001

GLU 193 PHE 194 -0.0000

PHE 194 GLY 195 -0.0099

GLY 195 MET 196 -0.0000

MET 196 GLY 197 -0.0001

GLY 197 LEU 198 0.0178

LEU 198 THR 199 -0.0002

THR 199 THR 200 -0.0001

THR 200 PHE 201 0.0066

PHE 201 LYS 202 0.0004

LYS 202 GLU 203 0.0001

GLU 203 LEU 204 0.0317

LEU 204 PHE 205 0.0005

PHE 205 GLY 206 -0.0004

GLY 206 SER 207 0.0359

SER 207 VAL 208 0.0000

VAL 208 TYR 209 -0.0001

TYR 209 GLY 210 0.0587

GLY 210 VAL 211 -0.0002

VAL 211 SER 212 0.0000

SER 212 PRO 213 -0.0424

PRO 213 ARG 214 -0.0001

ARG 214 ALA 215 0.0002

ALA 215 TRP 216 0.0654

TRP 216 ILE 217 0.0000

ILE 217 SER 218 0.0002

SER 218 GLU 219 0.0690

GLU 219 ARG 220 0.0002

ARG 220 ARG 221 -0.0002

ARG 221 ILE 222 0.0083

ILE 222 LEU 223 -0.0002

LEU 223 TYR 224 -0.0003

TYR 224 ALA 225 -0.0035

ALA 225 HIS 226 0.0002

HIS 226 GLN 227 -0.0002

GLN 227 LEU 228 0.0227

LEU 228 LEU 229 -0.0004

LEU 229 LEU 230 -0.0002

LEU 230 ASN 231 0.0508

ASN 231 SER 232 -0.0002

SER 232 ASP 233 0.0002

ASP 233 MET 234 -0.0877

MET 234 SER 235 -0.0004

SER 235 ILE 236 0.0003

ILE 236 VAL 237 -0.0140

VAL 237 ASP 238 0.0005

ASP 238 ILE 239 0.0001

ILE 239 ALA 240 -0.0422

ALA 240 MET 241 0.0002

MET 241 GLU 242 -0.0002

GLU 242 ALA 243 -0.0377

ALA 243 GLY 244 0.0000

GLY 244 PHE 245 -0.0001

PHE 245 SER 246 -0.0111

SER 246 SER 247 0.0003

SER 247 GLN 248 -0.0001

GLN 248 SER 249 0.0094

SER 249 TYR 250 -0.0002

TYR 250 PHE 251 -0.0002

PHE 251 THR 252 0.0174

THR 252 GLN 253 0.0000

GLN 253 SER 254 -0.0000

SER 254 TYR 255 0.0149

TYR 255 ARG 256 -0.0002

ARG 256 ARG 257 0.0001

ARG 257 ARG 258 -0.0125

ARG 258 PHE 259 -0.0003

PHE 259 GLY 260 0.0002

GLY 260 CYS 261 -0.0159

CYS 261 THR 262 0.0003

THR 262 PRO 263 0.0000

PRO 263 SER 264 -0.0066

SER 264 ARG 265 0.0002

ARG 265 SER 266 -0.0001

SER 266 ARG 267 0.0160

ARG 267 GLN 268 0.0001

GLN 268 GLY 269 0.0001

GLY 269 LYS 270 -0.0517

LYS 270 ASP 271 -0.0000

ASP 271 GLU 272 -0.0004

GLU 272 CYS 273 0.0203

CYS 273 ARG 274 -0.0002

ARG 274 ALA 275 0.0002

ALA 275 LYS 276 0.0014

LYS 276 ASN 277 0.0000

ASN 277 ASN 278 0.0001

ASN 278 NMA 278 0.0004

NMA 278 MET 1 0.0334

MET 1 GLN 2 -0.0001

GLN 2 GLY 3 0.0038

GLY 3 ALA 4 -0.0000

ALA 4 LYS 5 0.0002

LYS 5 SER 6 -0.0853

SER 6 LEU 7 -0.0002

LEU 7 GLY 8 -0.0001

GLY 8 ARG 9 0.1262

ARG 9 LYS 10 0.0002

LYS 10 GLN 11 0.0001

GLN 11 ILE 12 0.0232

ILE 12 THR 13 0.0001

THR 13 SER 14 -0.0002

SER 14 CYS 15 0.0983

CYS 15 HIS 16 0.0003

HIS 16 TRP 17 -0.0004

TRP 17 ASN 18 0.0514

ASN 18 ILE 19 0.0002

ILE 19 PRO 20 -0.0001

PRO 20 THR 21 0.0022

THR 21 PHE 22 -0.0001

PHE 22 GLU 23 -0.0000

GLU 23 TYR 24 0.0260

TYR 24 ARG 25 0.0001

ARG 25 VAL 26 -0.0003

VAL 26 ASN 27 0.0026

ASN 27 LYS 28 -0.0000

LYS 28 GLU 29 -0.0001

GLU 29 GLU 30 0.0226

GLU 30 GLY 31 -0.0002

GLY 31 VAL 32 0.0004

VAL 32 TYR 33 0.0036

TYR 33 VAL 34 0.0001

VAL 34 LEU 35 -0.0001

LEU 35 LEU 36 0.0190

LEU 36 GLU 37 -0.0002

GLU 37 GLY 38 -0.0000

GLY 38 GLU 39 0.0672

GLU 39 LEU 40 0.0003

LEU 40 THR 41 -0.0001

THR 41 VAL 42 -0.0258

VAL 42 GLN 43 0.0000

GLN 43 ASP 44 -0.0002

ASP 44 ILE 45 -0.0011

ILE 45 ASP 46 -0.0004

ASP 46 SER 47 -0.0001

SER 47 THR 48 0.0334

THR 48 PHE 49 -0.0000

PHE 49 CYS 50 0.0003

CYS 50 LEU 51 0.0867

LEU 51 ALA 52 0.0003

ALA 52 PRO 53 0.0003

PRO 53 GLY 54 -0.0107

GLY 54 GLU 55 -0.0003

GLU 55 LEU 56 -0.0001

LEU 56 LEU 57 0.0641

LEU 57 PHE 58 0.0002

PHE 58 VAL 59 -0.0001

VAL 59 ARG 60 0.0081

ARG 60 ARG 61 0.0003

ARG 61 GLY 62 -0.0002

GLY 62 SER 63 -0.0532

SER 63 TYR 64 0.0001

TYR 64 VAL 65 -0.0000

VAL 65 VAL 66 0.0025

VAL 66 SER 67 -0.0002

SER 67 THR 68 -0.0002

THR 68 LYS 69 0.0150

LYS 69 GLY 70 0.0003

GLY 70 LYS 71 -0.0003

LYS 71 ASP 72 0.0637

ASP 72 SER 73 -0.0001

SER 73 ARG 74 -0.0002

ARG 74 ILE 75 -0.0050

ILE 75 LEU 76 -0.0002

LEU 76 TRP 77 -0.0002

TRP 77 ILE 78 0.0494

ILE 78 PRO 79 -0.0003

PRO 79 LEU 80 -0.0002

LEU 80 SER 81 0.1629

SER 81 ALA 82 0.0002

ALA 82 GLN 83 0.0003

GLN 83 PHE 84 0.2054

PHE 84 LEU 85 -0.0002

LEU 85 GLN 86 0.0001

GLN 86 GLY 87 -0.0276

GLY 87 PHE 88 -0.0004

PHE 88 VAL 89 0.0003

VAL 89 GLN 90 -0.0365

GLN 90 ARG 91 0.0002

ARG 91 PHE 92 0.0002

PHE 92 GLY 93 -0.0687

GLY 93 ALA 94 0.0002

ALA 94 LEU 95 -0.0000

LEU 95 LEU 96 0.0117

LEU 96 SER 97 0.0002

SER 97 GLU 98 -0.0004

GLU 98 VAL 99 -0.0030

VAL 99 GLU 100 0.0002

GLU 100 ARG 101 -0.0004

ARG 101 CYS 102 -0.0888

CYS 102 ASP 103 0.0000

ASP 103 GLU 104 0.0003

GLU 104 PRO 105 -0.0008

PRO 105 VAL 106 -0.0002

VAL 106 PRO 107 0.0003

PRO 107 GLY 108 -0.0559

GLY 108 ILE 109 -0.0004

ILE 109 ILE 110 0.0002

ILE 110 ALA 111 0.0664

ALA 111 PHE 112 0.0000

PHE 112 ALA 113 -0.0002

ALA 113 ALA 114 0.0901

ALA 114 THR 115 -0.0000

THR 115 PRO 116 0.0002

PRO 116 LEU 117 -0.0240

LEU 117 LEU 118 -0.0000

LEU 118 ALA 119 0.0003

ALA 119 GLY 120 0.0788

GLY 120 CYS 121 -0.0002

CYS 121 VAL 122 -0.0001

VAL 122 LYS 123 0.0617

LYS 123 GLY 124 0.0003

GLY 124 LEU 125 -0.0003

LEU 125 LYS 126 -0.0282

LYS 126 GLU 127 0.0000

GLU 127 LEU 128 0.0002

LEU 128 LEU 129 0.0245

LEU 129 VAL 130 0.0002

VAL 130 HIS 131 -0.0001

HIS 131 GLU 132 0.0625

GLU 132 HIS 133 0.0002

HIS 133 PRO 134 -0.0001

PRO 134 PRO 135 -0.0385

PRO 135 MET 136 -0.0000

MET 136 LEU 137 0.0000

LEU 137 ALA 138 -0.0187

ALA 138 CYS 139 -0.0000

CYS 139 LEU 140 0.0002

LEU 140 LYS 141 -0.0017

LYS 141 ILE 142 -0.0004

ILE 142 GLU 143 -0.0004

GLU 143 GLU 144 0.0053

GLU 144 LEU 145 -0.0001

LEU 145 LEU 146 -0.0000

LEU 146 MET 147 0.0249

MET 147 LEU 148 0.0002

LEU 148 PHE 149 -0.0003

PHE 149 ALA 150 -0.0270

ALA 150 PHE 151 -0.0001

PHE 151 SER 152 -0.0003

SER 152 PRO 153 0.0318

PRO 153 GLN 154 -0.0004

GLN 154 GLY 155 -0.0002

GLY 155 PRO 156 -0.0178

PRO 156 LEU 157 -0.0000

LEU 157 LEU 158 0.0001

LEU 158 MET 159 -0.0368

MET 159 SER 160 0.0003

SER 160 VAL 161 -0.0001

VAL 161 LEU 162 -0.0408

LEU 162 ARG 163 0.0005

ARG 163 GLN 164 0.0001

GLN 164 LEU 165 0.0039

LEU 165 SER 166 0.0002

SER 166 ASN 167 0.0001

ASN 167 ARG 168 -0.0409

ARG 168 HIS 169 0.0001

HIS 169 VAL 170 0.0002

VAL 170 GLU 171 -0.0122

GLU 171 ARG 172 0.0003

ARG 172 LEU 173 0.0003

LEU 173 GLN 174 0.0572

GLN 174 LEU 175 0.0001

LEU 175 PHE 176 -0.0002

PHE 176 MET 177 0.0462

MET 177 GLU 178 -0.0002

GLU 178 LYS 179 0.0000

LYS 179 HIS 180 0.0335

HIS 180 TYR 181 -0.0002

TYR 181 LEU 182 0.0002

LEU 182 ASN 183 -0.0704

ASN 183 GLU 184 0.0001

GLU 184 TRP 185 -0.0004

TRP 185 LYS 186 -0.1777

LYS 186 LEU 187 0.0002

LEU 187 SER 188 0.0004

SER 188 ASP 189 -0.0183

ASP 189 PHE 190 0.0001

PHE 190 SER 191 0.0001

SER 191 ARG 192 -0.0046

ARG 192 GLU 193 0.0000

GLU 193 PHE 194 0.0001

PHE 194 GLY 195 -0.0097

GLY 195 MET 196 0.0002

MET 196 GLY 197 -0.0000

GLY 197 LEU 198 0.0144

LEU 198 THR 199 -0.0000

THR 199 THR 200 -0.0001

THR 200 PHE 201 0.0037

PHE 201 LYS 202 0.0002

LYS 202 GLU 203 0.0001

GLU 203 LEU 204 0.0335

LEU 204 PHE 205 0.0000

PHE 205 GLY 206 0.0003

GLY 206 SER 207 0.0382

SER 207 VAL 208 0.0000

VAL 208 TYR 209 0.0004

TYR 209 GLY 210 0.0560

GLY 210 VAL 211 -0.0000

VAL 211 SER 212 -0.0001

SER 212 PRO 213 -0.0403

PRO 213 ARG 214 0.0001

ARG 214 ALA 215 0.0001

ALA 215 TRP 216 0.0565

TRP 216 ILE 217 -0.0000

ILE 217 SER 218 0.0000

SER 218 GLU 219 0.0566

GLU 219 ARG 220 -0.0002

ARG 220 ARG 221 -0.0001

ARG 221 ILE 222 0.0068

ILE 222 LEU 223 0.0002

LEU 223 TYR 224 0.0002

TYR 224 ALA 225 -0.0084

ALA 225 HIS 226 0.0002

HIS 226 GLN 227 -0.0005

GLN 227 LEU 228 0.0172

LEU 228 LEU 229 0.0001

LEU 229 LEU 230 -0.0002

LEU 230 ASN 231 0.0447

ASN 231 SER 232 -0.0001

SER 232 ASP 233 0.0001

ASP 233 MET 234 -0.0682

MET 234 SER 235 0.0002

SER 235 ILE 236 -0.0003

ILE 236 VAL 237 -0.0115

VAL 237 ASP 238 -0.0002

ASP 238 ILE 239 0.0002

ILE 239 ALA 240 -0.0349

ALA 240 MET 241 -0.0002

MET 241 GLU 242 0.0003

GLU 242 ALA 243 -0.0450

ALA 243 GLY 244 -0.0004

GLY 244 PHE 245 -0.0003

PHE 245 SER 246 -0.0109

SER 246 SER 247 -0.0002

SER 247 GLN 248 0.0001

GLN 248 SER 249 -0.0013

SER 249 TYR 250 0.0002

TYR 250 PHE 251 0.0001

PHE 251 THR 252 0.0190

THR 252 GLN 253 -0.0001

GLN 253 SER 254 -0.0000

SER 254 TYR 255 0.0150

TYR 255 ARG 256 0.0001

ARG 256 ARG 257 0.0001

ARG 257 ARG 258 -0.0033

ARG 258 PHE 259 0.0001

PHE 259 GLY 260 -0.0002

GLY 260 CYS 261 -0.0254

CYS 261 THR 262 -0.0001

THR 262 PRO 263 -0.0000

PRO 263 SER 264 -0.0013

SER 264 ARG 265 0.0002

ARG 265 SER 266 -0.0000

SER 266 ARG 267 0.0045

ARG 267 GLN 268 0.0001

GLN 268 GLY 269 -0.0001

GLY 269 LYS 270 -0.0427

LYS 270 ASP 271 -0.0001

ASP 271 GLU 272 -0.0000

GLU 272 CYS 273 0.0159

CYS 273 ARG 274 -0.0003

ARG 274 ALA 275 -0.0000

ALA 275 LYS 276 0.0069

LYS 276 ASN 277 0.0003

ASN 277 ASN 278 0.0001

ASN 278 NMA 278 -0.0001

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 15 ---

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

* EXSA_dimer1 *