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

* EXSA_dimer1 *

CA strain for 2401041206373816311

--- normal mode 20 ---

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 -0.0001

GLN 2 GLY 3 -0.0102

GLY 3 ALA 4 0.0001

ALA 4 LYS 5 -0.0003

LYS 5 SER 6 -0.1915

SER 6 LEU 7 0.0002

LEU 7 GLY 8 0.0003

GLY 8 ARG 9 0.0516

ARG 9 LYS 10 -0.0001

LYS 10 GLN 11 -0.0000

GLN 11 ILE 12 0.1247

ILE 12 THR 13 -0.0002

THR 13 SER 14 0.0003

SER 14 CYS 15 -0.0473

CYS 15 HIS 16 -0.0001

HIS 16 TRP 17 0.0002

TRP 17 ASN 18 -0.0055

ASN 18 ILE 19 0.0001

ILE 19 PRO 20 0.0000

PRO 20 THR 21 -0.0039

THR 21 PHE 22 -0.0004

PHE 22 GLU 23 0.0001

GLU 23 TYR 24 0.0182

TYR 24 ARG 25 -0.0004

ARG 25 VAL 26 0.0003

VAL 26 ASN 27 -0.0106

ASN 27 LYS 28 0.0001

LYS 28 GLU 29 -0.0000

GLU 29 GLU 30 0.0161

GLU 30 GLY 31 -0.0003

GLY 31 VAL 32 0.0004

VAL 32 TYR 33 -0.0040

TYR 33 VAL 34 -0.0000

VAL 34 LEU 35 -0.0002

LEU 35 LEU 36 -0.0136

LEU 36 GLU 37 -0.0002

GLU 37 GLY 38 0.0002

GLY 38 GLU 39 -0.0011

GLU 39 LEU 40 0.0001

LEU 40 THR 41 0.0003

THR 41 VAL 42 -0.0063

VAL 42 GLN 43 0.0004

GLN 43 ASP 44 -0.0001

ASP 44 ILE 45 -0.0025

ILE 45 ASP 46 0.0000

ASP 46 SER 47 0.0002

SER 47 THR 48 0.0093

THR 48 PHE 49 0.0002

PHE 49 CYS 50 0.0001

CYS 50 LEU 51 0.0201

LEU 51 ALA 52 0.0000

ALA 52 PRO 53 0.0001

PRO 53 GLY 54 -0.0175

GLY 54 GLU 55 0.0004

GLU 55 LEU 56 -0.0003

LEU 56 LEU 57 0.0208

LEU 57 PHE 58 0.0001

PHE 58 VAL 59 -0.0001

VAL 59 ARG 60 0.0039

ARG 60 ARG 61 0.0004

ARG 61 GLY 62 -0.0001

GLY 62 SER 63 0.0114

SER 63 TYR 64 0.0003

TYR 64 VAL 65 0.0001

VAL 65 VAL 66 -0.0130

VAL 66 SER 67 0.0001

SER 67 THR 68 0.0001

THR 68 LYS 69 0.0022

LYS 69 GLY 70 -0.0002

GLY 70 LYS 71 -0.0001

LYS 71 ASP 72 -0.0134

ASP 72 SER 73 0.0002

SER 73 ARG 74 0.0001

ARG 74 ILE 75 0.0092

ILE 75 LEU 76 0.0000

LEU 76 TRP 77 -0.0000

TRP 77 ILE 78 0.0008

ILE 78 PRO 79 0.0001

PRO 79 LEU 80 -0.0000

LEU 80 SER 81 0.0162

SER 81 ALA 82 0.0002

ALA 82 GLN 83 -0.0001

GLN 83 PHE 84 0.1569

PHE 84 LEU 85 0.0001

LEU 85 GLN 86 -0.0003

GLN 86 GLY 87 0.0238

GLY 87 PHE 88 -0.0000

PHE 88 VAL 89 -0.0001

VAL 89 GLN 90 -0.0278

GLN 90 ARG 91 -0.0000

ARG 91 PHE 92 0.0000

PHE 92 GLY 93 0.0141

GLY 93 ALA 94 -0.0002

ALA 94 LEU 95 0.0003

LEU 95 LEU 96 0.0075

LEU 96 SER 97 -0.0002

SER 97 GLU 98 0.0003

GLU 98 VAL 99 -0.0081

VAL 99 GLU 100 -0.0001

GLU 100 ARG 101 -0.0004

ARG 101 CYS 102 0.0655

CYS 102 ASP 103 0.0001

ASP 103 GLU 104 -0.0002

GLU 104 PRO 105 0.0252

PRO 105 VAL 106 -0.0002

VAL 106 PRO 107 0.0002

PRO 107 GLY 108 0.0516

GLY 108 ILE 109 0.0000

ILE 109 ILE 110 0.0001

ILE 110 ALA 111 0.0202

ALA 111 PHE 112 -0.0002

PHE 112 ALA 113 -0.0001

ALA 113 ALA 114 0.0413

ALA 114 THR 115 0.0000

THR 115 PRO 116 0.0001

PRO 116 LEU 117 -0.0212

LEU 117 LEU 118 -0.0000

LEU 118 ALA 119 0.0001

ALA 119 GLY 120 0.0347

GLY 120 CYS 121 0.0002

CYS 121 VAL 122 0.0004

VAL 122 LYS 123 0.0155

LYS 123 GLY 124 -0.0002

GLY 124 LEU 125 -0.0000

LEU 125 LYS 126 -0.0065

LYS 126 GLU 127 0.0000

GLU 127 LEU 128 0.0001

LEU 128 LEU 129 -0.0064

LEU 129 VAL 130 -0.0003

VAL 130 HIS 131 -0.0004

HIS 131 GLU 132 -0.0159

GLU 132 HIS 133 0.0000

HIS 133 PRO 134 -0.0003

PRO 134 PRO 135 -0.0197

PRO 135 MET 136 0.0001

MET 136 LEU 137 -0.0001

LEU 137 ALA 138 0.0394

ALA 138 CYS 139 -0.0004

CYS 139 LEU 140 -0.0000

LEU 140 LYS 141 -0.0128

LYS 141 ILE 142 0.0002

ILE 142 GLU 143 -0.0001

GLU 143 GLU 144 -0.0132

GLU 144 LEU 145 0.0001

LEU 145 LEU 146 0.0002

LEU 146 MET 147 -0.0097

MET 147 LEU 148 -0.0001

LEU 148 PHE 149 -0.0001

PHE 149 ALA 150 -0.0012

ALA 150 PHE 151 0.0001

PHE 151 SER 152 -0.0002

SER 152 PRO 153 0.0324

PRO 153 GLN 154 0.0000

GLN 154 GLY 155 0.0002

GLY 155 PRO 156 0.0174

PRO 156 LEU 157 -0.0000

LEU 157 LEU 158 0.0001

LEU 158 MET 159 -0.0033

MET 159 SER 160 0.0001

SER 160 VAL 161 0.0001

VAL 161 LEU 162 -0.0111

LEU 162 ARG 163 -0.0006

ARG 163 GLN 164 0.0002

GLN 164 LEU 165 -0.0464

LEU 165 SER 166 -0.0002

SER 166 ASN 167 -0.0003

ASN 167 ARG 168 0.0760

ARG 168 HIS 169 0.0002

HIS 169 VAL 170 0.0001

VAL 170 GLU 171 -0.0215

GLU 171 ARG 172 -0.0003

ARG 172 LEU 173 0.0000

LEU 173 GLN 174 0.0274

GLN 174 LEU 175 0.0004

LEU 175 PHE 176 -0.0004

PHE 176 MET 177 0.0574

MET 177 GLU 178 -0.0001

GLU 178 LYS 179 0.0001

LYS 179 HIS 180 -0.0346

HIS 180 TYR 181 0.0002

TYR 181 LEU 182 0.0001

LEU 182 ASN 183 -0.0030

ASN 183 GLU 184 -0.0001

GLU 184 TRP 185 -0.0000

TRP 185 LYS 186 -0.0700

LYS 186 LEU 187 0.0003

LEU 187 SER 188 0.0004

SER 188 ASP 189 -0.0012

ASP 189 PHE 190 -0.0001

PHE 190 SER 191 -0.0001

SER 191 ARG 192 0.0265

ARG 192 GLU 193 0.0001

GLU 193 PHE 194 0.0002

PHE 194 GLY 195 0.0012

GLY 195 MET 196 -0.0001

MET 196 GLY 197 -0.0003

GLY 197 LEU 198 0.0113

LEU 198 THR 199 -0.0001

THR 199 THR 200 0.0003

THR 200 PHE 201 0.0373

PHE 201 LYS 202 0.0002

LYS 202 GLU 203 -0.0004

GLU 203 LEU 204 -0.0268

LEU 204 PHE 205 0.0003

PHE 205 GLY 206 -0.0004

GLY 206 SER 207 0.0334

SER 207 VAL 208 0.0002

VAL 208 TYR 209 -0.0000

TYR 209 GLY 210 0.0119

GLY 210 VAL 211 0.0000

VAL 211 SER 212 0.0001

SER 212 PRO 213 -0.0520

PRO 213 ARG 214 0.0001

ARG 214 ALA 215 0.0002

ALA 215 TRP 216 -0.0086

TRP 216 ILE 217 0.0001

ILE 217 SER 218 0.0004

SER 218 GLU 219 0.0040

GLU 219 ARG 220 0.0002

ARG 220 ARG 221 0.0000

ARG 221 ILE 222 0.0844

ILE 222 LEU 223 0.0003

LEU 223 TYR 224 -0.0001

TYR 224 ALA 225 0.0055

ALA 225 HIS 226 0.0002

HIS 226 GLN 227 0.0003

GLN 227 LEU 228 -0.0204

LEU 228 LEU 229 -0.0000

LEU 229 LEU 230 0.0003

LEU 230 ASN 231 -0.0714

ASN 231 SER 232 -0.0002

SER 232 ASP 233 0.0001

ASP 233 MET 234 0.0888

MET 234 SER 235 -0.0002

SER 235 ILE 236 -0.0002

ILE 236 VAL 237 -0.0374

VAL 237 ASP 238 -0.0000

ASP 238 ILE 239 -0.0002

ILE 239 ALA 240 0.0182

ALA 240 MET 241 -0.0001

MET 241 GLU 242 -0.0001

GLU 242 ALA 243 0.0227

ALA 243 GLY 244 0.0000

GLY 244 PHE 245 0.0002

PHE 245 SER 246 -0.0132

SER 246 SER 247 -0.0000

SER 247 GLN 248 0.0001

GLN 248 SER 249 0.0166

SER 249 TYR 250 0.0003

TYR 250 PHE 251 -0.0002

PHE 251 THR 252 0.0201

THR 252 GLN 253 -0.0002

GLN 253 SER 254 -0.0001

SER 254 TYR 255 0.0451

TYR 255 ARG 256 -0.0002

ARG 256 ARG 257 -0.0001

ARG 257 ARG 258 -0.0984

ARG 258 PHE 259 0.0005

PHE 259 GLY 260 -0.0001

GLY 260 CYS 261 -0.0678

CYS 261 THR 262 0.0000

THR 262 PRO 263 0.0002

PRO 263 SER 264 0.0298

SER 264 ARG 265 -0.0005

ARG 265 SER 266 0.0004

SER 266 ARG 267 -0.0327

ARG 267 GLN 268 -0.0001

GLN 268 GLY 269 -0.0000

GLY 269 LYS 270 -0.0051

LYS 270 ASP 271 0.0001

ASP 271 GLU 272 -0.0001

GLU 272 CYS 273 0.0924

CYS 273 ARG 274 -0.0001

ARG 274 ALA 275 -0.0001

ALA 275 LYS 276 -0.2871

LYS 276 ASN 277 0.0002

ASN 277 ASN 278 -0.0001

ASN 278 NMA 278 -0.0000

NMA 278 MET 1 -0.0312

MET 1 GLN 2 -0.0002

GLN 2 GLY 3 -0.0291

GLY 3 ALA 4 0.0002

ALA 4 LYS 5 -0.0001

LYS 5 SER 6 0.0433

SER 6 LEU 7 -0.0001

LEU 7 GLY 8 0.0001

GLY 8 ARG 9 0.0020

ARG 9 LYS 10 -0.0003

LYS 10 GLN 11 0.0001

GLN 11 ILE 12 0.0020

ILE 12 THR 13 -0.0001

THR 13 SER 14 -0.0000

SER 14 CYS 15 0.1228

CYS 15 HIS 16 -0.0000

HIS 16 TRP 17 -0.0001

TRP 17 ASN 18 0.0528

ASN 18 ILE 19 -0.0005

ILE 19 PRO 20 0.0003

PRO 20 THR 21 0.0037

THR 21 PHE 22 -0.0001

PHE 22 GLU 23 0.0002

GLU 23 TYR 24 0.0138

TYR 24 ARG 25 -0.0004

ARG 25 VAL 26 -0.0002

VAL 26 ASN 27 0.0302

ASN 27 LYS 28 0.0001

LYS 28 GLU 29 0.0003

GLU 29 GLU 30 -0.0016

GLU 30 GLY 31 -0.0000

GLY 31 VAL 32 -0.0000

VAL 32 TYR 33 -0.0184

TYR 33 VAL 34 0.0000

VAL 34 LEU 35 -0.0004

LEU 35 LEU 36 0.0176

LEU 36 GLU 37 0.0002

GLU 37 GLY 38 -0.0001

GLY 38 GLU 39 0.0359

GLU 39 LEU 40 0.0000

LEU 40 THR 41 -0.0001

THR 41 VAL 42 -0.0161

VAL 42 GLN 43 -0.0000

GLN 43 ASP 44 -0.0002

ASP 44 ILE 45 0.0030

ILE 45 ASP 46 -0.0004

ASP 46 SER 47 -0.0002

SER 47 THR 48 0.0088

THR 48 PHE 49 -0.0001

PHE 49 CYS 50 0.0003

CYS 50 LEU 51 0.0412

LEU 51 ALA 52 0.0001

ALA 52 PRO 53 0.0000

PRO 53 GLY 54 -0.0026

GLY 54 GLU 55 0.0000

GLU 55 LEU 56 -0.0000

LEU 56 LEU 57 0.0205

LEU 57 PHE 58 0.0000

PHE 58 VAL 59 0.0001

VAL 59 ARG 60 0.0068

ARG 60 ARG 61 -0.0000

ARG 61 GLY 62 -0.0004

GLY 62 SER 63 -0.0265

SER 63 TYR 64 0.0000

TYR 64 VAL 65 -0.0002

VAL 65 VAL 66 0.0099

VAL 66 SER 67 -0.0004

SER 67 THR 68 0.0003

THR 68 LYS 69 0.0109

LYS 69 GLY 70 0.0004

GLY 70 LYS 71 -0.0004

LYS 71 ASP 72 0.0512

ASP 72 SER 73 0.0000

SER 73 ARG 74 -0.0001

ARG 74 ILE 75 -0.0239

ILE 75 LEU 76 -0.0001

LEU 76 TRP 77 0.0000

TRP 77 ILE 78 0.0205

ILE 78 PRO 79 0.0000

PRO 79 LEU 80 -0.0000

LEU 80 SER 81 -0.0706

SER 81 ALA 82 0.0000

ALA 82 GLN 83 0.0000

GLN 83 PHE 84 -0.1213

PHE 84 LEU 85 -0.0001

LEU 85 GLN 86 -0.0001

GLN 86 GLY 87 0.0047

GLY 87 PHE 88 0.0002

PHE 88 VAL 89 -0.0002

VAL 89 GLN 90 -0.0009

GLN 90 ARG 91 -0.0002

ARG 91 PHE 92 0.0002

PHE 92 GLY 93 0.1054

GLY 93 ALA 94 0.0000

ALA 94 LEU 95 0.0003

LEU 95 LEU 96 0.0332

LEU 96 SER 97 -0.0003

SER 97 GLU 98 -0.0004

GLU 98 VAL 99 -0.0150

VAL 99 GLU 100 -0.0000

GLU 100 ARG 101 0.0003

ARG 101 CYS 102 0.0418

CYS 102 ASP 103 0.0004

ASP 103 GLU 104 0.0001

GLU 104 PRO 105 -0.1095

PRO 105 VAL 106 0.0002

VAL 106 PRO 107 0.0005

PRO 107 GLY 108 -0.1540

GLY 108 ILE 109 -0.0001

ILE 109 ILE 110 -0.0000

ILE 110 ALA 111 0.0411

ALA 111 PHE 112 0.0002

PHE 112 ALA 113 -0.0002

ALA 113 ALA 114 0.0427

ALA 114 THR 115 0.0003

THR 115 PRO 116 0.0001

PRO 116 LEU 117 -0.0051

LEU 117 LEU 118 0.0001

LEU 118 ALA 119 0.0003

ALA 119 GLY 120 0.0466

GLY 120 CYS 121 -0.0005

CYS 121 VAL 122 -0.0003

VAL 122 LYS 123 0.0406

LYS 123 GLY 124 -0.0000

GLY 124 LEU 125 -0.0001

LEU 125 LYS 126 -0.0163

LYS 126 GLU 127 0.0001

GLU 127 LEU 128 0.0000

LEU 128 LEU 129 0.0246

LEU 129 VAL 130 0.0004

VAL 130 HIS 131 -0.0000

HIS 131 GLU 132 0.0083

GLU 132 HIS 133 0.0000

HIS 133 PRO 134 -0.0003

PRO 134 PRO 135 0.0036

PRO 135 MET 136 0.0002

MET 136 LEU 137 0.0001

LEU 137 ALA 138 0.0458

ALA 138 CYS 139 0.0001

CYS 139 LEU 140 0.0000

LEU 140 LYS 141 0.0377

LYS 141 ILE 142 0.0001

ILE 142 GLU 143 0.0002

GLU 143 GLU 144 -0.0186

GLU 144 LEU 145 -0.0003

LEU 145 LEU 146 -0.0001

LEU 146 MET 147 -0.0153

MET 147 LEU 148 0.0002

LEU 148 PHE 149 0.0002

PHE 149 ALA 150 0.0265

ALA 150 PHE 151 -0.0004

PHE 151 SER 152 0.0002

SER 152 PRO 153 0.0238

PRO 153 GLN 154 0.0001

GLN 154 GLY 155 0.0002

GLY 155 PRO 156 0.0398

PRO 156 LEU 157 0.0000

LEU 157 LEU 158 0.0000

LEU 158 MET 159 0.0051

MET 159 SER 160 0.0004

SER 160 VAL 161 0.0004

VAL 161 LEU 162 -0.0144

LEU 162 ARG 163 -0.0001

ARG 163 GLN 164 0.0002

GLN 164 LEU 165 -0.1038

LEU 165 SER 166 -0.0003

SER 166 ASN 167 -0.0000

ASN 167 ARG 168 0.0115

ARG 168 HIS 169 0.0005

HIS 169 VAL 170 -0.0003

VAL 170 GLU 171 0.0085

GLU 171 ARG 172 -0.0003

ARG 172 LEU 173 0.0001

LEU 173 GLN 174 -0.0165

GLN 174 LEU 175 -0.0005

LEU 175 PHE 176 0.0002

PHE 176 MET 177 -0.0209

MET 177 GLU 178 -0.0003

GLU 178 LYS 179 -0.0000

LYS 179 HIS 180 -0.0121

HIS 180 TYR 181 0.0001

TYR 181 LEU 182 -0.0003

LEU 182 ASN 183 0.0340

ASN 183 GLU 184 0.0001

GLU 184 TRP 185 -0.0001

TRP 185 LYS 186 0.0302

LYS 186 LEU 187 -0.0002

LEU 187 SER 188 0.0005

SER 188 ASP 189 0.0111

ASP 189 PHE 190 -0.0001

PHE 190 SER 191 0.0001

SER 191 ARG 192 0.0205

ARG 192 GLU 193 -0.0000

GLU 193 PHE 194 0.0002

PHE 194 GLY 195 0.0191

GLY 195 MET 196 -0.0002

MET 196 GLY 197 0.0003

GLY 197 LEU 198 -0.0135

LEU 198 THR 199 0.0001

THR 199 THR 200 0.0002

THR 200 PHE 201 0.0030

PHE 201 LYS 202 -0.0000

LYS 202 GLU 203 0.0002

GLU 203 LEU 204 -0.0733

LEU 204 PHE 205 0.0003

PHE 205 GLY 206 0.0000

GLY 206 SER 207 -0.0365

SER 207 VAL 208 0.0001

VAL 208 TYR 209 -0.0001

TYR 209 GLY 210 -0.0305

GLY 210 VAL 211 -0.0003

VAL 211 SER 212 0.0003

SER 212 PRO 213 0.0232

PRO 213 ARG 214 -0.0002

ARG 214 ALA 215 -0.0002

ALA 215 TRP 216 -0.0055

TRP 216 ILE 217 -0.0001

ILE 217 SER 218 0.0001

SER 218 GLU 219 -0.0037

GLU 219 ARG 220 0.0003

ARG 220 ARG 221 -0.0003

ARG 221 ILE 222 -0.0057

ILE 222 LEU 223 0.0002

LEU 223 TYR 224 0.0001

TYR 224 ALA 225 0.0142

ALA 225 HIS 226 -0.0003

HIS 226 GLN 227 -0.0002

GLN 227 LEU 228 -0.0123

LEU 228 LEU 229 -0.0003

LEU 229 LEU 230 0.0000

LEU 230 ASN 231 -0.0032

ASN 231 SER 232 0.0002

SER 232 ASP 233 -0.0002

ASP 233 MET 234 0.0570

MET 234 SER 235 0.0001

SER 235 ILE 236 -0.0000

ILE 236 VAL 237 -0.0048

VAL 237 ASP 238 0.0000

ASP 238 ILE 239 -0.0002

ILE 239 ALA 240 0.0179

ALA 240 MET 241 -0.0003

MET 241 GLU 242 0.0003

GLU 242 ALA 243 -0.0210

ALA 243 GLY 244 -0.0001

GLY 244 PHE 245 0.0001

PHE 245 SER 246 0.0103

SER 246 SER 247 -0.0002

SER 247 GLN 248 0.0003

GLN 248 SER 249 -0.0071

SER 249 TYR 250 -0.0000

TYR 250 PHE 251 -0.0003

PHE 251 THR 252 -0.0160

THR 252 GLN 253 0.0001

GLN 253 SER 254 -0.0004

SER 254 TYR 255 0.0082

TYR 255 ARG 256 -0.0003

ARG 256 ARG 257 0.0000

ARG 257 ARG 258 -0.0022

ARG 258 PHE 259 0.0003

PHE 259 GLY 260 0.0001

GLY 260 CYS 261 -0.0300

CYS 261 THR 262 0.0000

THR 262 PRO 263 0.0001

PRO 263 SER 264 0.0057

SER 264 ARG 265 -0.0002

ARG 265 SER 266 0.0002

SER 266 ARG 267 -0.0039

ARG 267 GLN 268 -0.0003

GLN 268 GLY 269 -0.0001

GLY 269 LYS 270 0.0373

LYS 270 ASP 271 -0.0002

ASP 271 GLU 272 -0.0001

GLU 272 CYS 273 0.0146

CYS 273 ARG 274 0.0000

ARG 274 ALA 275 -0.0001

ALA 275 LYS 276 0.0451

LYS 276 ASN 277 -0.0000

ASN 277 ASN 278 -0.0002

ASN 278 NMA 278 -0.0000

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 20 ---

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

* EXSA_dimer1 *