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

* EXSA_dimer1 *

CA strain for 2401041206373816311

--- normal mode 29 ---

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 -0.0288

GLY 3 ALA 4 0.0001

ALA 4 LYS 5 0.0000

LYS 5 SER 6 -0.1339

SER 6 LEU 7 -0.0001

LEU 7 GLY 8 -0.0001

GLY 8 ARG 9 -0.0276

ARG 9 LYS 10 0.0003

LYS 10 GLN 11 -0.0002

GLN 11 ILE 12 -0.1002

ILE 12 THR 13 -0.0000

THR 13 SER 14 -0.0001

SER 14 CYS 15 -0.2146

CYS 15 HIS 16 -0.0004

HIS 16 TRP 17 0.0001

TRP 17 ASN 18 -0.1850

ASN 18 ILE 19 -0.0003

ILE 19 PRO 20 0.0002

PRO 20 THR 21 -0.0116

THR 21 PHE 22 0.0004

PHE 22 GLU 23 -0.0003

GLU 23 TYR 24 -0.2326

TYR 24 ARG 25 -0.0001

ARG 25 VAL 26 -0.0001

VAL 26 ASN 27 -0.1154

ASN 27 LYS 28 0.0003

LYS 28 GLU 29 0.0001

GLU 29 GLU 30 -0.0198

GLU 30 GLY 31 -0.0003

GLY 31 VAL 32 -0.0000

VAL 32 TYR 33 0.0550

TYR 33 VAL 34 -0.0004

VAL 34 LEU 35 0.0002

LEU 35 LEU 36 -0.0265

LEU 36 GLU 37 0.0004

GLU 37 GLY 38 -0.0004

GLY 38 GLU 39 -0.1537

GLU 39 LEU 40 -0.0001

LEU 40 THR 41 0.0002

THR 41 VAL 42 -0.0071

VAL 42 GLN 43 -0.0002

GLN 43 ASP 44 -0.0001

ASP 44 ILE 45 0.0189

ILE 45 ASP 46 -0.0001

ASP 46 SER 47 0.0001

SER 47 THR 48 -0.1282

THR 48 PHE 49 0.0001

PHE 49 CYS 50 0.0002

CYS 50 LEU 51 -0.1264

LEU 51 ALA 52 0.0003

ALA 52 PRO 53 0.0002

PRO 53 GLY 54 0.2309

GLY 54 GLU 55 0.0000

GLU 55 LEU 56 0.0000

LEU 56 LEU 57 -0.0057

LEU 57 PHE 58 -0.0001

PHE 58 VAL 59 -0.0001

VAL 59 ARG 60 0.0501

ARG 60 ARG 61 -0.0000

ARG 61 GLY 62 0.0005

GLY 62 SER 63 -0.1812

SER 63 TYR 64 -0.0003

TYR 64 VAL 65 0.0000

VAL 65 VAL 66 -0.0238

VAL 66 SER 67 0.0005

SER 67 THR 68 -0.0000

THR 68 LYS 69 -0.0642

LYS 69 GLY 70 0.0003

GLY 70 LYS 71 -0.0002

LYS 71 ASP 72 -0.1220

ASP 72 SER 73 -0.0005

SER 73 ARG 74 0.0000

ARG 74 ILE 75 0.0086

ILE 75 LEU 76 0.0001

LEU 76 TRP 77 -0.0000

TRP 77 ILE 78 -0.0494

ILE 78 PRO 79 -0.0002

PRO 79 LEU 80 -0.0000

LEU 80 SER 81 0.2173

SER 81 ALA 82 -0.0001

ALA 82 GLN 83 -0.0003

GLN 83 PHE 84 0.1080

PHE 84 LEU 85 -0.0001

LEU 85 GLN 86 -0.0002

GLN 86 GLY 87 -0.0146

GLY 87 PHE 88 0.0001

PHE 88 VAL 89 -0.0002

VAL 89 GLN 90 0.0261

GLN 90 ARG 91 0.0002

ARG 91 PHE 92 -0.0001

PHE 92 GLY 93 0.1129

GLY 93 ALA 94 -0.0003

ALA 94 LEU 95 -0.0000

LEU 95 LEU 96 0.0045

LEU 96 SER 97 0.0003

SER 97 GLU 98 -0.0001

GLU 98 VAL 99 -0.0081

VAL 99 GLU 100 0.0001

GLU 100 ARG 101 -0.0003

ARG 101 CYS 102 -0.0134

CYS 102 ASP 103 -0.0001

ASP 103 GLU 104 0.0004

GLU 104 PRO 105 -0.0184

PRO 105 VAL 106 0.0001

VAL 106 PRO 107 0.0002

PRO 107 GLY 108 0.0159

GLY 108 ILE 109 -0.0001

ILE 109 ILE 110 0.0003

ILE 110 ALA 111 -0.0406

ALA 111 PHE 112 0.0003

PHE 112 ALA 113 0.0003

ALA 113 ALA 114 -0.0107

ALA 114 THR 115 -0.0001

THR 115 PRO 116 -0.0003

PRO 116 LEU 117 0.0239

LEU 117 LEU 118 0.0001

LEU 118 ALA 119 -0.0001

ALA 119 GLY 120 -0.0262

GLY 120 CYS 121 0.0004

CYS 121 VAL 122 -0.0001

VAL 122 LYS 123 0.0022

LYS 123 GLY 124 -0.0000

GLY 124 LEU 125 0.0005

LEU 125 LYS 126 0.0318

LYS 126 GLU 127 0.0003

GLU 127 LEU 128 0.0004

LEU 128 LEU 129 -0.0132

LEU 129 VAL 130 -0.0000

VAL 130 HIS 131 -0.0004

HIS 131 GLU 132 0.0651

GLU 132 HIS 133 0.0000

HIS 133 PRO 134 -0.0000

PRO 134 PRO 135 -0.0340

PRO 135 MET 136 0.0001

MET 136 LEU 137 0.0001

LEU 137 ALA 138 0.0510

ALA 138 CYS 139 0.0003

CYS 139 LEU 140 -0.0000

LEU 140 LYS 141 0.0135

LYS 141 ILE 142 0.0004

ILE 142 GLU 143 -0.0005

GLU 143 GLU 144 0.0125

GLU 144 LEU 145 -0.0004

LEU 145 LEU 146 0.0004

LEU 146 MET 147 -0.0682

MET 147 LEU 148 -0.0001

LEU 148 PHE 149 -0.0001

PHE 149 ALA 150 0.0117

ALA 150 PHE 151 0.0003

PHE 151 SER 152 -0.0002

SER 152 PRO 153 -0.0219

PRO 153 GLN 154 0.0002

GLN 154 GLY 155 -0.0001

GLY 155 PRO 156 0.0001

PRO 156 LEU 157 -0.0005

LEU 157 LEU 158 0.0001

LEU 158 MET 159 0.0591

MET 159 SER 160 0.0002

SER 160 VAL 161 -0.0002

VAL 161 LEU 162 0.0580

LEU 162 ARG 163 -0.0001

ARG 163 GLN 164 0.0002

GLN 164 LEU 165 0.0164

LEU 165 SER 166 0.0000

SER 166 ASN 167 -0.0003

ASN 167 ARG 168 0.2690

ARG 168 HIS 169 -0.0002

HIS 169 VAL 170 0.0002

VAL 170 GLU 171 0.0529

GLU 171 ARG 172 -0.0000

ARG 172 LEU 173 -0.0003

LEU 173 GLN 174 0.0082

GLN 174 LEU 175 -0.0000

LEU 175 PHE 176 -0.0002

PHE 176 MET 177 -0.0996

MET 177 GLU 178 -0.0000

GLU 178 LYS 179 -0.0003

LYS 179 HIS 180 -0.0181

HIS 180 TYR 181 0.0001

TYR 181 LEU 182 -0.0001

LEU 182 ASN 183 0.0633

ASN 183 GLU 184 -0.0001

GLU 184 TRP 185 -0.0001

TRP 185 LYS 186 -0.1392

LYS 186 LEU 187 0.0002

LEU 187 SER 188 -0.0001

SER 188 ASP 189 -0.0032

ASP 189 PHE 190 -0.0004

PHE 190 SER 191 -0.0001

SER 191 ARG 192 -0.1241

ARG 192 GLU 193 -0.0001

GLU 193 PHE 194 -0.0001

PHE 194 GLY 195 -0.0233

GLY 195 MET 196 0.0002

MET 196 GLY 197 -0.0000

GLY 197 LEU 198 0.0751

LEU 198 THR 199 -0.0001

THR 199 THR 200 -0.0005

THR 200 PHE 201 -0.0736

PHE 201 LYS 202 -0.0003

LYS 202 GLU 203 0.0001

GLU 203 LEU 204 0.2432

LEU 204 PHE 205 -0.0003

PHE 205 GLY 206 -0.0004

GLY 206 SER 207 0.0183

SER 207 VAL 208 0.0001

VAL 208 TYR 209 0.0002

TYR 209 GLY 210 0.0183

GLY 210 VAL 211 0.0003

VAL 211 SER 212 -0.0001

SER 212 PRO 213 0.0782

PRO 213 ARG 214 0.0002

ARG 214 ALA 215 0.0000

ALA 215 TRP 216 0.0767

TRP 216 ILE 217 -0.0001

ILE 217 SER 218 -0.0003

SER 218 GLU 219 -0.0314

GLU 219 ARG 220 0.0001

ARG 220 ARG 221 -0.0001

ARG 221 ILE 222 -0.0150

ILE 222 LEU 223 0.0003

LEU 223 TYR 224 -0.0003

TYR 224 ALA 225 0.0126

ALA 225 HIS 226 0.0003

HIS 226 GLN 227 0.0003

GLN 227 LEU 228 0.0412

LEU 228 LEU 229 -0.0002

LEU 229 LEU 230 -0.0001

LEU 230 ASN 231 -0.0122

ASN 231 SER 232 0.0000

SER 232 ASP 233 -0.0001

ASP 233 MET 234 0.0561

MET 234 SER 235 -0.0001

SER 235 ILE 236 0.0000

ILE 236 VAL 237 -0.0581

VAL 237 ASP 238 -0.0003

ASP 238 ILE 239 0.0000

ILE 239 ALA 240 -0.0150

ALA 240 MET 241 0.0003

MET 241 GLU 242 0.0004

GLU 242 ALA 243 -0.0600

ALA 243 GLY 244 -0.0002

GLY 244 PHE 245 0.0004

PHE 245 SER 246 0.0752

SER 246 SER 247 -0.0001

SER 247 GLN 248 0.0001

GLN 248 SER 249 -0.0141

SER 249 TYR 250 -0.0001

TYR 250 PHE 251 0.0003

PHE 251 THR 252 -0.0727

THR 252 GLN 253 0.0003

GLN 253 SER 254 -0.0001

SER 254 TYR 255 0.0072

TYR 255 ARG 256 -0.0002

ARG 256 ARG 257 -0.0003

ARG 257 ARG 258 0.0156

ARG 258 PHE 259 -0.0001

PHE 259 GLY 260 0.0004

GLY 260 CYS 261 0.0347

CYS 261 THR 262 -0.0003

THR 262 PRO 263 0.0003

PRO 263 SER 264 -0.0359

SER 264 ARG 265 0.0001

ARG 265 SER 266 0.0000

SER 266 ARG 267 0.0278

ARG 267 GLN 268 -0.0003

GLN 268 GLY 269 0.0000

GLY 269 LYS 270 0.0893

LYS 270 ASP 271 -0.0002

ASP 271 GLU 272 -0.0002

GLU 272 CYS 273 0.0450

CYS 273 ARG 274 0.0002

ARG 274 ALA 275 0.0001

ALA 275 LYS 276 -0.2281

LYS 276 ASN 277 0.0002

ASN 277 ASN 278 -0.0001

ASN 278 NMA 278 0.0002

NMA 278 MET 1 -0.0322

MET 1 GLN 2 0.0001

GLN 2 GLY 3 -0.0172

GLY 3 ALA 4 0.0001

ALA 4 LYS 5 -0.0001

LYS 5 SER 6 0.0985

SER 6 LEU 7 -0.0001

LEU 7 GLY 8 0.0002

GLY 8 ARG 9 0.0044

ARG 9 LYS 10 -0.0002

LYS 10 GLN 11 -0.0002

GLN 11 ILE 12 0.0248

ILE 12 THR 13 0.0001

THR 13 SER 14 0.0000

SER 14 CYS 15 -0.0979

CYS 15 HIS 16 -0.0002

HIS 16 TRP 17 0.0002

TRP 17 ASN 18 -0.0217

ASN 18 ILE 19 -0.0001

ILE 19 PRO 20 0.0002

PRO 20 THR 21 -0.0043

THR 21 PHE 22 0.0000

PHE 22 GLU 23 0.0002

GLU 23 TYR 24 0.0532

TYR 24 ARG 25 -0.0001

ARG 25 VAL 26 0.0002

VAL 26 ASN 27 -0.0099

ASN 27 LYS 28 0.0000

LYS 28 GLU 29 -0.0004

GLU 29 GLU 30 -0.0056

GLU 30 GLY 31 0.0003

GLY 31 VAL 32 -0.0001

VAL 32 TYR 33 0.0107

TYR 33 VAL 34 0.0000

VAL 34 LEU 35 0.0001

LEU 35 LEU 36 0.0177

LEU 36 GLU 37 0.0006

GLU 37 GLY 38 -0.0005

GLY 38 GLU 39 0.0495

GLU 39 LEU 40 0.0002

LEU 40 THR 41 -0.0001

THR 41 VAL 42 0.0187

VAL 42 GLN 43 0.0002

GLN 43 ASP 44 0.0001

ASP 44 ILE 45 -0.0122

ILE 45 ASP 46 0.0004

ASP 46 SER 47 0.0002

SER 47 THR 48 0.0334

THR 48 PHE 49 0.0002

PHE 49 CYS 50 0.0001

CYS 50 LEU 51 0.0202

LEU 51 ALA 52 -0.0001

ALA 52 PRO 53 -0.0003

PRO 53 GLY 54 -0.0941

GLY 54 GLU 55 0.0001

GLU 55 LEU 56 -0.0001

LEU 56 LEU 57 -0.0042

LEU 57 PHE 58 0.0002

PHE 58 VAL 59 -0.0002

VAL 59 ARG 60 0.0193

ARG 60 ARG 61 0.0003

ARG 61 GLY 62 -0.0002

GLY 62 SER 63 0.0957

SER 63 TYR 64 -0.0002

TYR 64 VAL 65 -0.0001

VAL 65 VAL 66 -0.0073

VAL 66 SER 67 0.0003

SER 67 THR 68 0.0001

THR 68 LYS 69 0.0055

LYS 69 GLY 70 -0.0002

GLY 70 LYS 71 0.0001

LYS 71 ASP 72 -0.0186

ASP 72 SER 73 -0.0001

SER 73 ARG 74 -0.0003

ARG 74 ILE 75 0.0311

ILE 75 LEU 76 0.0004

LEU 76 TRP 77 -0.0001

TRP 77 ILE 78 0.0005

ILE 78 PRO 79 -0.0001

PRO 79 LEU 80 0.0002

LEU 80 SER 81 -0.0342

SER 81 ALA 82 -0.0001

ALA 82 GLN 83 -0.0001

GLN 83 PHE 84 0.0653

PHE 84 LEU 85 -0.0001

LEU 85 GLN 86 0.0003

GLN 86 GLY 87 -0.0062

GLY 87 PHE 88 -0.0004

PHE 88 VAL 89 0.0002

VAL 89 GLN 90 0.0220

GLN 90 ARG 91 0.0000

ARG 91 PHE 92 0.0002

PHE 92 GLY 93 -0.0464

GLY 93 ALA 94 -0.0002

ALA 94 LEU 95 -0.0002

LEU 95 LEU 96 0.0167

LEU 96 SER 97 0.0002

SER 97 GLU 98 -0.0003

GLU 98 VAL 99 -0.0109

VAL 99 GLU 100 0.0005

GLU 100 ARG 101 -0.0002

ARG 101 CYS 102 0.0500

CYS 102 ASP 103 -0.0002

ASP 103 GLU 104 -0.0001

GLU 104 PRO 105 -0.0417

PRO 105 VAL 106 0.0004

VAL 106 PRO 107 -0.0002

PRO 107 GLY 108 -0.0088

GLY 108 ILE 109 -0.0005

ILE 109 ILE 110 0.0002

ILE 110 ALA 111 0.0677

ALA 111 PHE 112 0.0002

PHE 112 ALA 113 0.0001

ALA 113 ALA 114 0.0566

ALA 114 THR 115 -0.0001

THR 115 PRO 116 0.0001

PRO 116 LEU 117 0.0080

LEU 117 LEU 118 0.0002

LEU 118 ALA 119 -0.0003

ALA 119 GLY 120 0.1669

GLY 120 CYS 121 -0.0003

CYS 121 VAL 122 -0.0001

VAL 122 LYS 123 0.0852

LYS 123 GLY 124 0.0002

GLY 124 LEU 125 -0.0000

LEU 125 LYS 126 0.0016

LYS 126 GLU 127 -0.0004

GLU 127 LEU 128 -0.0003

LEU 128 LEU 129 -0.0308

LEU 129 VAL 130 0.0002

VAL 130 HIS 131 -0.0000

HIS 131 GLU 132 -0.0028

GLU 132 HIS 133 0.0002

HIS 133 PRO 134 0.0001

PRO 134 PRO 135 -0.0299

PRO 135 MET 136 -0.0003

MET 136 LEU 137 0.0000

LEU 137 ALA 138 -0.0007

ALA 138 CYS 139 0.0003

CYS 139 LEU 140 -0.0001

LEU 140 LYS 141 0.0418

LYS 141 ILE 142 -0.0001

ILE 142 GLU 143 -0.0002

GLU 143 GLU 144 -0.0394

GLU 144 LEU 145 0.0001

LEU 145 LEU 146 -0.0003

LEU 146 MET 147 -0.0188

MET 147 LEU 148 0.0004

LEU 148 PHE 149 0.0001

PHE 149 ALA 150 0.0841

ALA 150 PHE 151 -0.0002

PHE 151 SER 152 0.0004

SER 152 PRO 153 0.0558

PRO 153 GLN 154 0.0001

GLN 154 GLY 155 0.0002

GLY 155 PRO 156 0.0884

PRO 156 LEU 157 0.0003

LEU 157 LEU 158 0.0002

LEU 158 MET 159 0.0108

MET 159 SER 160 -0.0002

SER 160 VAL 161 0.0004

VAL 161 LEU 162 -0.0034

LEU 162 ARG 163 0.0000

ARG 163 GLN 164 0.0001

GLN 164 LEU 165 -0.1049

LEU 165 SER 166 -0.0000

SER 166 ASN 167 -0.0002

ASN 167 ARG 168 0.0088

ARG 168 HIS 169 0.0003

HIS 169 VAL 170 0.0001

VAL 170 GLU 171 -0.0693

GLU 171 ARG 172 0.0001

ARG 172 LEU 173 -0.0001

LEU 173 GLN 174 0.0104

GLN 174 LEU 175 -0.0001

LEU 175 PHE 176 0.0003

PHE 176 MET 177 0.0410

MET 177 GLU 178 0.0002

GLU 178 LYS 179 -0.0001

LYS 179 HIS 180 0.0652

HIS 180 TYR 181 -0.0002

TYR 181 LEU 182 0.0001

LEU 182 ASN 183 -0.0515

ASN 183 GLU 184 -0.0001

GLU 184 TRP 185 -0.0001

TRP 185 LYS 186 0.0684

LYS 186 LEU 187 0.0004

LEU 187 SER 188 0.0002

SER 188 ASP 189 -0.0004

ASP 189 PHE 190 0.0002

PHE 190 SER 191 -0.0001

SER 191 ARG 192 0.0359

ARG 192 GLU 193 -0.0000

GLU 193 PHE 194 -0.0003

PHE 194 GLY 195 -0.0076

GLY 195 MET 196 0.0004

MET 196 GLY 197 -0.0000

GLY 197 LEU 198 -0.0225

LEU 198 THR 199 0.0001

THR 199 THR 200 -0.0002

THR 200 PHE 201 0.0432

PHE 201 LYS 202 0.0004

LYS 202 GLU 203 -0.0002

GLU 203 LEU 204 -0.1335

LEU 204 PHE 205 0.0001

PHE 205 GLY 206 -0.0000

GLY 206 SER 207 -0.0010

SER 207 VAL 208 -0.0001

VAL 208 TYR 209 -0.0001

TYR 209 GLY 210 -0.0045

GLY 210 VAL 211 -0.0001

VAL 211 SER 212 -0.0000

SER 212 PRO 213 -0.0479

PRO 213 ARG 214 0.0000

ARG 214 ALA 215 -0.0000

ALA 215 TRP 216 -0.0238

TRP 216 ILE 217 0.0003

ILE 217 SER 218 0.0001

SER 218 GLU 219 0.0218

GLU 219 ARG 220 0.0004

ARG 220 ARG 221 -0.0005

ARG 221 ILE 222 -0.0201

ILE 222 LEU 223 -0.0002

LEU 223 TYR 224 0.0004

TYR 224 ALA 225 -0.0704

ALA 225 HIS 226 -0.0001

HIS 226 GLN 227 -0.0001

GLN 227 LEU 228 0.0385

LEU 228 LEU 229 -0.0003

LEU 229 LEU 230 -0.0001

LEU 230 ASN 231 0.0484

ASN 231 SER 232 0.0004

SER 232 ASP 233 -0.0001

ASP 233 MET 234 0.0197

MET 234 SER 235 -0.0000

SER 235 ILE 236 0.0000

ILE 236 VAL 237 -0.0068

VAL 237 ASP 238 -0.0001

ASP 238 ILE 239 -0.0000

ILE 239 ALA 240 0.0062

ALA 240 MET 241 -0.0000

MET 241 GLU 242 -0.0000

GLU 242 ALA 243 0.0612

ALA 243 GLY 244 0.0000

GLY 244 PHE 245 -0.0003

PHE 245 SER 246 -0.0089

SER 246 SER 247 0.0001

SER 247 GLN 248 0.0000

GLN 248 SER 249 0.0382

SER 249 TYR 250 -0.0000

TYR 250 PHE 251 0.0001

PHE 251 THR 252 0.0223

THR 252 GLN 253 0.0000

GLN 253 SER 254 0.0003

SER 254 TYR 255 -0.0061

TYR 255 ARG 256 0.0000

ARG 256 ARG 257 -0.0001

ARG 257 ARG 258 -0.0159

ARG 258 PHE 259 0.0002

PHE 259 GLY 260 0.0001

GLY 260 CYS 261 0.0352

CYS 261 THR 262 0.0000

THR 262 PRO 263 0.0001

PRO 263 SER 264 0.0075

SER 264 ARG 265 0.0002

ARG 265 SER 266 0.0000

SER 266 ARG 267 0.0073

ARG 267 GLN 268 -0.0000

GLN 268 GLY 269 0.0000

GLY 269 LYS 270 -0.0128

LYS 270 ASP 271 0.0001

ASP 271 GLU 272 -0.0000

GLU 272 CYS 273 -0.0635

CYS 273 ARG 274 0.0003

ARG 274 ALA 275 -0.0000

ALA 275 LYS 276 0.0589

LYS 276 ASN 277 -0.0003

ASN 277 ASN 278 -0.0003

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 29 ---

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

* EXSA_dimer1 *