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

* 7TIM dimero *

CA strain for 240110225701578599

--- normal mode 11 ---

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
ALA 2 ARG 3 0.0002

ARG 3 THR 4 -0.0001

THR 4 PHE 5 -0.0399

PHE 5 PHE 6 -0.0002

PHE 6 VAL 7 0.0000

VAL 7 GLY 8 -0.1179

GLY 8 GLY 9 -0.0003

GLY 9 ASN 10 0.0004

ASN 10 PHE 11 -0.1207

PHE 11 LYS 12 0.0001

LYS 12 LEU 13 -0.0001

LEU 13 ASN 14 0.0316

ASN 14 GLY 15 -0.0001

GLY 15 SER 16 -0.0003

SER 16 LYS 17 0.0953

LYS 17 GLN 18 0.0000

GLN 18 SER 19 0.0003

SER 19 ILE 20 0.1012

ILE 20 LYS 21 -0.0003

LYS 21 GLU 22 0.0003

GLU 22 ILE 23 0.0025

ILE 23 VAL 24 0.0001

VAL 24 GLU 25 -0.0002

GLU 25 ARG 26 -0.0631

ARG 26 LEU 27 -0.0001

LEU 27 ASN 28 -0.0001

ASN 28 THR 29 -0.0410

THR 29 ALA 30 -0.0001

ALA 30 SER 31 0.0003

SER 31 ILE 32 -0.0354

ILE 32 PRO 33 -0.0002

PRO 33 GLU 34 -0.0003

GLU 34 ASN 35 -0.0114

ASN 35 VAL 36 -0.0003

VAL 36 GLU 37 0.0002

GLU 37 VAL 38 -0.0626

VAL 38 VAL 39 0.0002

VAL 39 ILE 40 -0.0002

ILE 40 CYS 41 -0.0265

CYS 41 PRO 42 0.0003

PRO 42 PRO 43 -0.0003

PRO 43 ALA 44 -0.1970

ALA 44 THR 45 -0.0001

THR 45 TYR 46 -0.0001

TYR 46 LEU 47 0.0753

LEU 47 ASP 48 0.0002

ASP 48 TYR 49 -0.0001

TYR 49 SER 50 -0.1992

SER 50 VAL 51 0.0000

VAL 51 SER 52 0.0003

SER 52 LEU 53 -0.0868

LEU 53 VAL 54 0.0000

VAL 54 LYS 55 0.0000

LYS 55 LYS 56 0.0029

LYS 56 PRO 57 0.0001

PRO 57 GLN 58 0.0001

GLN 58 VAL 59 -0.0699

VAL 59 THR 60 0.0001

THR 60 VAL 61 -0.0002

VAL 61 GLY 62 0.0265

GLY 62 ALA 63 -0.0001

ALA 63 GLN 64 0.0003

GLN 64 ASN 65 -0.0258

ASN 65 ALA 66 0.0005

ALA 66 TYR 67 -0.0003

TYR 67 LEU 68 0.1137

LEU 68 LYS 69 0.0001

LYS 69 ALA 70 -0.0001

ALA 70 SER 71 -0.0721

SER 71 GLY 72 0.0005

GLY 72 ALA 73 -0.0005

ALA 73 PHE 74 -0.0935

PHE 74 THR 75 0.0002

THR 75 GLY 76 -0.0001

GLY 76 GLU 77 -0.0707

GLU 77 ASN 78 0.0004

ASN 78 SER 79 0.0000

SER 79 VAL 80 0.0390

VAL 80 ASP 81 0.0004

ASP 81 GLN 82 0.0002

GLN 82 ILE 83 -0.1412

ILE 83 LYS 84 0.0002

LYS 84 ASP 85 -0.0001

ASP 85 VAL 86 0.0090

VAL 86 GLY 87 0.0001

GLY 87 ALA 88 0.0003

ALA 88 LYS 89 -0.1722

LYS 89 TRP 90 0.0003

TRP 90 VAL 91 -0.0000

VAL 91 ILE 92 -0.0659

ILE 92 LEU 93 0.0000

LEU 93 GLY 94 0.0000

GLY 94 HIS 95 -0.0514

HIS 95 SER 96 -0.0001

SER 96 GLU 97 0.0004

GLU 97 ARG 98 -0.1394

ARG 98 ARG 99 0.0003

ARG 99 SER 100 0.0002

SER 100 TYR 101 -0.0669

TYR 101 PHE 102 0.0004

PHE 102 HIS 103 -0.0000

HIS 103 GLU 104 0.0363

GLU 104 ASP 105 -0.0004

ASP 105 ASP 106 -0.0002

ASP 106 LYS 107 -0.0727

LYS 107 PHE 108 0.0004

PHE 108 ILE 109 -0.0001

ILE 109 ALA 110 0.0678

ALA 110 ASP 111 -0.0002

ASP 111 LYS 112 0.0001

LYS 112 THR 113 0.0339

THR 113 LYS 114 -0.0002

LYS 114 PHE 115 -0.0001

PHE 115 ALA 116 -0.0208

ALA 116 LEU 117 -0.0000

LEU 117 GLY 118 -0.0004

GLY 118 GLN 119 0.0340

GLN 119 GLY 120 -0.0003

GLY 120 VAL 121 -0.0000

VAL 121 GLY 122 -0.0557

GLY 122 VAL 123 0.0004

VAL 123 ILE 124 -0.0001

ILE 124 LEU 125 -0.0346

LEU 125 CYS 126 -0.0002

CYS 126 ILE 127 0.0003

ILE 127 GLY 128 -0.1875

GLY 128 GLU 129 -0.0001

GLU 129 THR 130 0.0003

THR 130 LEU 131 -0.1042

LEU 131 GLU 132 0.0000

GLU 132 GLU 133 -0.0001

GLU 133 LYS 134 0.0264

LYS 134 LYS 135 -0.0001

LYS 135 ALA 136 -0.0001

ALA 136 GLY 137 0.1191

GLY 137 LYS 138 0.0001

LYS 138 THR 139 -0.0004

THR 139 LEU 140 0.0791

LEU 140 ASP 141 -0.0000

ASP 141 VAL 142 -0.0001

VAL 142 VAL 143 -0.0569

VAL 143 GLU 144 0.0002

GLU 144 ARG 145 0.0001

ARG 145 GLN 146 0.0194

GLN 146 LEU 147 0.0003

LEU 147 ASN 148 0.0001

ASN 148 ALA 149 0.0348

ALA 149 VAL 150 -0.0003

VAL 150 LEU 151 -0.0001

LEU 151 GLU 152 0.0364

GLU 152 GLU 153 0.0000

GLU 153 VAL 154 0.0000

VAL 154 LYS 155 0.0721

LYS 155 ASP 156 -0.0004

ASP 156 TRP 157 -0.0000

TRP 157 THR 158 -0.0078

THR 158 ASN 159 -0.0004

ASN 159 VAL 160 0.0000

VAL 160 VAL 161 0.0408

VAL 161 VAL 162 -0.0001

VAL 162 ALA 163 -0.0002

ALA 163 TYR 164 0.0213

TYR 164 GLU 165 0.0000

GLU 165 PRO 166 -0.0003

PRO 166 VAL 167 0.0237

VAL 167 TRP 168 -0.0001

TRP 168 ALA 169 -0.0000

ALA 169 ILE 170 -0.1779

ILE 170 GLY 171 -0.0001

GLY 171 THR 172 0.0001

THR 172 GLY 173 -0.0072

GLY 173 LEU 174 -0.0001

LEU 174 ALA 175 -0.0003

ALA 175 ALA 176 -0.0599

ALA 176 THR 177 0.0003

THR 177 PRO 178 -0.0001

PRO 178 GLU 179 -0.0011

GLU 179 ASP 180 -0.0001

ASP 180 ALA 181 -0.0000

ALA 181 GLN 182 -0.0460

GLN 182 ASP 183 0.0001

ASP 183 ILE 184 -0.0002

ILE 184 HIS 185 0.0509

HIS 185 ALA 186 0.0001

ALA 186 SER 187 0.0002

SER 187 ILE 188 -0.0306

ILE 188 ARG 189 0.0002

ARG 189 LYS 190 -0.0001

LYS 190 PHE 191 -0.0153

PHE 191 LEU 192 0.0001

LEU 192 ALA 193 0.0002

ALA 193 SER 194 -0.0271

SER 194 LYS 195 -0.0003

LYS 195 LEU 196 0.0001

LEU 196 GLY 197 0.0408

GLY 197 ASP 198 0.0001

ASP 198 LYS 199 0.0001

LYS 199 ALA 200 0.0374

ALA 200 ALA 201 0.0001

ALA 201 SER 202 -0.0002

SER 202 GLU 203 -0.0056

GLU 203 LEU 204 -0.0001

LEU 204 ARG 205 -0.0002

ARG 205 ILE 206 0.0247

ILE 206 LEU 207 0.0000

LEU 207 TYR 208 0.0001

TYR 208 GLY 209 -0.0372

GLY 209 GLY 210 0.0003

GLY 210 SER 211 -0.0001

SER 211 ALA 212 0.0827

ALA 212 ASN 213 0.0002

ASN 213 GLY 214 -0.0004

GLY 214 SER 215 -0.0215

SER 215 ASN 216 -0.0004

ASN 216 ALA 217 -0.0002

ALA 217 VAL 218 -0.0601

VAL 218 THR 219 -0.0000

THR 219 PHE 220 -0.0004

PHE 220 LYS 221 0.0233

LYS 221 ASP 222 0.0001

ASP 222 LYS 223 -0.0002

LYS 223 ALA 224 0.0286

ALA 224 ASP 225 -0.0002

ASP 225 VAL 226 0.0001

VAL 226 ASP 227 0.0219

ASP 227 GLY 228 -0.0002

GLY 228 PHE 229 0.0002

PHE 229 LEU 230 -0.1394

LEU 230 VAL 231 0.0003

VAL 231 GLY 232 -0.0002

GLY 232 GLY 233 0.0827

GLY 233 ALA 234 0.0001

ALA 234 SER 235 0.0003

SER 235 LEU 236 -0.0574

LEU 236 LYS 237 0.0001

LYS 237 PRO 238 -0.0002

PRO 238 GLU 239 -0.0715

GLU 239 PHE 240 -0.0003

PHE 240 VAL 241 -0.0002

VAL 241 ASP 242 -0.0401

ASP 242 ILE 243 0.0003

ILE 243 ILE 244 -0.0003

ILE 244 ASN 245 -0.0306

ASN 245 SER 246 0.0003

SER 246 ARG 247 -0.0000

ARG 247 ASN 248 0.0318

ASN 248 ALA 2 -0.0788

ALA 2 ARG 3 0.0001

ARG 3 THR 4 -0.0002

THR 4 PHE 5 -0.0112

PHE 5 PHE 6 0.0002

PHE 6 VAL 7 0.0002

VAL 7 GLY 8 -0.1655

GLY 8 GLY 9 -0.0003

GLY 9 ASN 10 0.0003

ASN 10 PHE 11 -0.1340

PHE 11 LYS 12 0.0002

LYS 12 LEU 13 -0.0003

LEU 13 ASN 14 0.0360

ASN 14 GLY 15 0.0001

GLY 15 SER 16 -0.0001

SER 16 LYS 17 0.1033

LYS 17 GLN 18 -0.0001

GLN 18 SER 19 0.0001

SER 19 ILE 20 0.1089

ILE 20 LYS 21 0.0001

LYS 21 GLU 22 0.0001

GLU 22 ILE 23 0.0351

ILE 23 VAL 24 -0.0001

VAL 24 GLU 25 0.0000

GLU 25 ARG 26 -0.0507

ARG 26 LEU 27 0.0003

LEU 27 ASN 28 -0.0003

ASN 28 THR 29 -0.0313

THR 29 ALA 30 -0.0002

ALA 30 SER 31 0.0002

SER 31 ILE 32 -0.0289

ILE 32 PRO 33 -0.0001

PRO 33 GLU 34 0.0004

GLU 34 ASN 35 -0.0295

ASN 35 VAL 36 -0.0002

VAL 36 GLU 37 -0.0001

GLU 37 VAL 38 -0.1069

VAL 38 VAL 39 0.0003

VAL 39 ILE 40 0.0001

ILE 40 CYS 41 -0.0529

CYS 41 PRO 42 0.0001

PRO 42 PRO 43 0.0002

PRO 43 ALA 44 -0.1939

ALA 44 THR 45 0.0001

THR 45 TYR 46 0.0002

TYR 46 LEU 47 0.0566

LEU 47 ASP 48 0.0000

ASP 48 TYR 49 -0.0002

TYR 49 SER 50 -0.2002

SER 50 VAL 51 -0.0001

VAL 51 SER 52 -0.0001

SER 52 LEU 53 -0.0627

LEU 53 VAL 54 0.0003

VAL 54 LYS 55 -0.0003

LYS 55 LYS 56 -0.0242

LYS 56 PRO 57 -0.0001

PRO 57 GLN 58 -0.0000

GLN 58 VAL 59 -0.0675

VAL 59 THR 60 0.0001

THR 60 VAL 61 -0.0002

VAL 61 GLY 62 0.0264

GLY 62 ALA 63 -0.0002

ALA 63 GLN 64 0.0003

GLN 64 ASN 65 -0.0576

ASN 65 ALA 66 0.0001

ALA 66 TYR 67 -0.0004

TYR 67 LEU 68 0.1170

LEU 68 LYS 69 -0.0000

LYS 69 ALA 70 -0.0003

ALA 70 SER 71 -0.0764

SER 71 GLY 72 0.0003

GLY 72 ALA 73 -0.0001

ALA 73 PHE 74 -0.0978

PHE 74 THR 75 0.0000

THR 75 GLY 76 -0.0001

GLY 76 GLU 77 -0.0856

GLU 77 ASN 78 -0.0000

ASN 78 SER 79 -0.0000

SER 79 VAL 80 -0.0096

VAL 80 ASP 81 -0.0003

ASP 81 GLN 82 0.0001

GLN 82 ILE 83 -0.1302

ILE 83 LYS 84 -0.0002

LYS 84 ASP 85 -0.0000

ASP 85 VAL 86 0.0037

VAL 86 GLY 87 -0.0003

GLY 87 ALA 88 0.0002

ALA 88 LYS 89 -0.1748

LYS 89 TRP 90 -0.0001

TRP 90 VAL 91 -0.0001

VAL 91 ILE 92 -0.0356

ILE 92 LEU 93 0.0000

LEU 93 GLY 94 0.0001

GLY 94 HIS 95 -0.0512

HIS 95 SER 96 0.0002

SER 96 GLU 97 0.0005

GLU 97 ARG 98 -0.1232

ARG 98 ARG 99 -0.0001

ARG 99 SER 100 0.0001

SER 100 TYR 101 -0.0172

TYR 101 PHE 102 -0.0003

PHE 102 HIS 103 -0.0000

HIS 103 GLU 104 0.0786

GLU 104 ASP 105 -0.0001

ASP 105 ASP 106 0.0001

ASP 106 LYS 107 -0.0480

LYS 107 PHE 108 -0.0003

PHE 108 ILE 109 0.0002

ILE 109 ALA 110 0.0534

ALA 110 ASP 111 -0.0002

ASP 111 LYS 112 -0.0002

LYS 112 THR 113 0.0287

THR 113 LYS 114 0.0001

LYS 114 PHE 115 -0.0000

PHE 115 ALA 116 -0.0178

ALA 116 LEU 117 -0.0001

LEU 117 GLY 118 0.0004

GLY 118 GLN 119 0.0202

GLN 119 GLY 120 -0.0002

GLY 120 VAL 121 0.0003

VAL 121 GLY 122 -0.0410

GLY 122 VAL 123 -0.0000

VAL 123 ILE 124 0.0002

ILE 124 LEU 125 -0.0343

LEU 125 CYS 126 0.0001

CYS 126 ILE 127 0.0001

ILE 127 GLY 128 -0.1555

GLY 128 GLU 129 -0.0002

GLU 129 THR 130 0.0002

THR 130 LEU 131 -0.0867

LEU 131 GLU 132 -0.0002

GLU 132 GLU 133 -0.0001

GLU 133 LYS 134 0.0189

LYS 134 LYS 135 -0.0000

LYS 135 ALA 136 -0.0002

ALA 136 GLY 137 0.0658

GLY 137 LYS 138 0.0004

LYS 138 THR 139 -0.0003

THR 139 LEU 140 0.0371

LEU 140 ASP 141 0.0003

ASP 141 VAL 142 0.0002

VAL 142 VAL 143 -0.0562

VAL 143 GLU 144 0.0002

GLU 144 ARG 145 0.0000

ARG 145 GLN 146 0.0222

GLN 146 LEU 147 -0.0004

LEU 147 ASN 148 0.0000

ASN 148 ALA 149 0.0549

ALA 149 VAL 150 -0.0000

VAL 150 LEU 151 -0.0003

LEU 151 GLU 152 0.0417

GLU 152 GLU 153 0.0004

GLU 153 VAL 154 0.0001

VAL 154 LYS 155 0.0734

LYS 155 ASP 156 -0.0000

ASP 156 TRP 157 0.0003

TRP 157 THR 158 -0.0202

THR 158 ASN 159 -0.0000

ASN 159 VAL 160 -0.0002

VAL 160 VAL 161 0.0492

VAL 161 VAL 162 0.0003

VAL 162 ALA 163 -0.0004

ALA 163 TYR 164 0.0062

TYR 164 GLU 165 0.0002

GLU 165 PRO 166 -0.0000

PRO 166 VAL 167 0.0077

VAL 167 TRP 168 -0.0001

TRP 168 ALA 169 -0.0003

ALA 169 ILE 170 -0.1352

ILE 170 GLY 171 -0.0003

GLY 171 THR 172 0.0005

THR 172 GLY 173 -0.0334

GLY 173 LEU 174 0.0001

LEU 174 ALA 175 -0.0004

ALA 175 ALA 176 -0.0500

ALA 176 THR 177 0.0001

THR 177 PRO 178 -0.0005

PRO 178 GLU 179 -0.0033

GLU 179 ASP 180 0.0001

ASP 180 ALA 181 -0.0000

ALA 181 GLN 182 -0.0276

GLN 182 ASP 183 0.0001

ASP 183 ILE 184 -0.0003

ILE 184 HIS 185 0.0312

HIS 185 ALA 186 0.0001

ALA 186 SER 187 0.0003

SER 187 ILE 188 -0.0089

ILE 188 ARG 189 -0.0001

ARG 189 LYS 190 -0.0001

LYS 190 PHE 191 0.0062

PHE 191 LEU 192 -0.0002

LEU 192 ALA 193 0.0002

ALA 193 SER 194 -0.0168

SER 194 LYS 195 0.0004

LYS 195 LEU 196 0.0000

LEU 196 GLY 197 0.0500

GLY 197 ASP 198 0.0003

ASP 198 LYS 199 -0.0001

LYS 199 ALA 200 0.0209

ALA 200 ALA 201 -0.0003

ALA 201 SER 202 -0.0001

SER 202 GLU 203 -0.0225

GLU 203 LEU 204 0.0002

LEU 204 ARG 205 -0.0002

ARG 205 ILE 206 0.0160

ILE 206 LEU 207 0.0003

LEU 207 TYR 208 -0.0005

TYR 208 GLY 209 -0.0181

GLY 209 GLY 210 0.0000

GLY 210 SER 211 -0.0001

SER 211 ALA 212 0.0879

ALA 212 ASN 213 -0.0001

ASN 213 GLY 214 -0.0001

GLY 214 SER 215 -0.0028

SER 215 ASN 216 0.0001

ASN 216 ALA 217 0.0000

ALA 217 VAL 218 -0.0665

VAL 218 THR 219 -0.0001

THR 219 PHE 220 0.0001

PHE 220 LYS 221 0.0037

LYS 221 ASP 222 -0.0001

ASP 222 LYS 223 -0.0001

LYS 223 ALA 224 0.0525

ALA 224 ASP 225 -0.0001

ASP 225 VAL 226 0.0002

VAL 226 ASP 227 0.0009

ASP 227 GLY 228 0.0001

GLY 228 PHE 229 0.0000

PHE 229 LEU 230 -0.1407

LEU 230 VAL 231 0.0000

VAL 231 GLY 232 0.0004

GLY 232 GLY 233 0.0754

GLY 233 ALA 234 -0.0002

ALA 234 SER 235 -0.0002

SER 235 LEU 236 -0.0388

LEU 236 LYS 237 -0.0003

LYS 237 PRO 238 0.0002

PRO 238 GLU 239 -0.0722

GLU 239 PHE 240 -0.0000

PHE 240 VAL 241 0.0000

VAL 241 ASP 242 -0.0366

ASP 242 ILE 243 0.0004

ILE 243 ILE 244 0.0000

ILE 244 ASN 245 -0.0270

ASN 245 SER 246 -0.0003

SER 246 ARG 247 0.0001

ARG 247 ASN 248 0.0500

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.

*** 7TIM dimero ***

CA strain for 240110225701578599

--- normal mode 11 ---

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

* 7TIM dimero *