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

* EXSA_dimer1 *

CA strain for 2401041206373816311

--- normal mode 24 ---

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 -0.0000

GLN 2 GLY 3 0.1316

GLY 3 ALA 4 0.0001

ALA 4 LYS 5 0.0002

LYS 5 SER 6 -0.3508

SER 6 LEU 7 -0.0001

LEU 7 GLY 8 -0.0001

GLY 8 ARG 9 -0.0048

ARG 9 LYS 10 0.0000

LYS 10 GLN 11 0.0000

GLN 11 ILE 12 0.1158

ILE 12 THR 13 -0.0001

THR 13 SER 14 0.0001

SER 14 CYS 15 -0.1805

CYS 15 HIS 16 0.0005

HIS 16 TRP 17 -0.0004

TRP 17 ASN 18 -0.0456

ASN 18 ILE 19 -0.0004

ILE 19 PRO 20 -0.0000

PRO 20 THR 21 -0.0075

THR 21 PHE 22 0.0002

PHE 22 GLU 23 -0.0000

GLU 23 TYR 24 0.0199

TYR 24 ARG 25 0.0000

ARG 25 VAL 26 -0.0001

VAL 26 ASN 27 -0.0601

ASN 27 LYS 28 0.0002

LYS 28 GLU 29 -0.0001

GLU 29 GLU 30 -0.0083

GLU 30 GLY 31 -0.0001

GLY 31 VAL 32 -0.0004

VAL 32 TYR 33 0.0137

TYR 33 VAL 34 0.0001

VAL 34 LEU 35 -0.0004

LEU 35 LEU 36 -0.0186

LEU 36 GLU 37 -0.0000

GLU 37 GLY 38 -0.0001

GLY 38 GLU 39 0.0100

GLU 39 LEU 40 -0.0003

LEU 40 THR 41 0.0004

THR 41 VAL 42 0.0040

VAL 42 GLN 43 0.0001

GLN 43 ASP 44 -0.0000

ASP 44 ILE 45 -0.0373

ILE 45 ASP 46 0.0000

ASP 46 SER 47 -0.0002

SER 47 THR 48 0.0110

THR 48 PHE 49 0.0001

PHE 49 CYS 50 0.0001

CYS 50 LEU 51 -0.0024

LEU 51 ALA 52 0.0000

ALA 52 PRO 53 0.0002

PRO 53 GLY 54 -0.0281

GLY 54 GLU 55 0.0003

GLU 55 LEU 56 -0.0001

LEU 56 LEU 57 -0.0536

LEU 57 PHE 58 -0.0000

PHE 58 VAL 59 0.0000

VAL 59 ARG 60 0.0038

ARG 60 ARG 61 -0.0000

ARG 61 GLY 62 0.0002

GLY 62 SER 63 -0.0219

SER 63 TYR 64 -0.0002

TYR 64 VAL 65 0.0001

VAL 65 VAL 66 -0.0105

VAL 66 SER 67 0.0005

SER 67 THR 68 -0.0004

THR 68 LYS 69 -0.0034

LYS 69 GLY 70 -0.0002

GLY 70 LYS 71 -0.0002

LYS 71 ASP 72 -0.0314

ASP 72 SER 73 0.0001

SER 73 ARG 74 -0.0002

ARG 74 ILE 75 0.0433

ILE 75 LEU 76 -0.0001

LEU 76 TRP 77 0.0003

TRP 77 ILE 78 -0.0072

ILE 78 PRO 79 -0.0003

PRO 79 LEU 80 -0.0004

LEU 80 SER 81 0.0156

SER 81 ALA 82 0.0000

ALA 82 GLN 83 -0.0001

GLN 83 PHE 84 -0.0482

PHE 84 LEU 85 -0.0001

LEU 85 GLN 86 0.0002

GLN 86 GLY 87 -0.0636

GLY 87 PHE 88 -0.0003

PHE 88 VAL 89 0.0002

VAL 89 GLN 90 0.0851

GLN 90 ARG 91 0.0002

ARG 91 PHE 92 0.0001

PHE 92 GLY 93 0.0953

GLY 93 ALA 94 0.0002

ALA 94 LEU 95 -0.0002

LEU 95 LEU 96 -0.0161

LEU 96 SER 97 0.0000

SER 97 GLU 98 -0.0003

GLU 98 VAL 99 0.0586

VAL 99 GLU 100 -0.0001

GLU 100 ARG 101 -0.0003

ARG 101 CYS 102 -0.0326

CYS 102 ASP 103 -0.0004

ASP 103 GLU 104 0.0001

GLU 104 PRO 105 -0.0338

PRO 105 VAL 106 0.0001

VAL 106 PRO 107 0.0001

PRO 107 GLY 108 0.0105

GLY 108 ILE 109 -0.0001

ILE 109 ILE 110 -0.0003

ILE 110 ALA 111 -0.0285

ALA 111 PHE 112 0.0001

PHE 112 ALA 113 0.0001

ALA 113 ALA 114 -0.0604

ALA 114 THR 115 -0.0004

THR 115 PRO 116 0.0002

PRO 116 LEU 117 0.0313

LEU 117 LEU 118 0.0001

LEU 118 ALA 119 -0.0003

ALA 119 GLY 120 -0.0154

GLY 120 CYS 121 -0.0003

CYS 121 VAL 122 -0.0002

VAL 122 LYS 123 -0.0099

LYS 123 GLY 124 -0.0001

GLY 124 LEU 125 0.0003

LEU 125 LYS 126 0.0399

LYS 126 GLU 127 0.0001

GLU 127 LEU 128 0.0001

LEU 128 LEU 129 -0.0423

LEU 129 VAL 130 0.0003

VAL 130 HIS 131 0.0001

HIS 131 GLU 132 0.0313

GLU 132 HIS 133 0.0000

HIS 133 PRO 134 0.0001

PRO 134 PRO 135 -0.0289

PRO 135 MET 136 0.0002

MET 136 LEU 137 -0.0002

LEU 137 ALA 138 -0.1127

ALA 138 CYS 139 0.0001

CYS 139 LEU 140 0.0002

LEU 140 LYS 141 -0.0464

LYS 141 ILE 142 -0.0001

ILE 142 GLU 143 -0.0003

GLU 143 GLU 144 0.0126

GLU 144 LEU 145 0.0001

LEU 145 LEU 146 0.0001

LEU 146 MET 147 0.0035

MET 147 LEU 148 0.0002

LEU 148 PHE 149 -0.0000

PHE 149 ALA 150 0.0584

ALA 150 PHE 151 0.0002

PHE 151 SER 152 -0.0000

SER 152 PRO 153 -0.0233

PRO 153 GLN 154 0.0001

GLN 154 GLY 155 -0.0001

GLY 155 PRO 156 -0.0069

PRO 156 LEU 157 -0.0001

LEU 157 LEU 158 0.0001

LEU 158 MET 159 0.0216

MET 159 SER 160 0.0002

SER 160 VAL 161 0.0003

VAL 161 LEU 162 -0.0007

LEU 162 ARG 163 -0.0001

ARG 163 GLN 164 -0.0001

GLN 164 LEU 165 -0.0044

LEU 165 SER 166 0.0001

SER 166 ASN 167 -0.0001

ASN 167 ARG 168 -0.1042

ARG 168 HIS 169 0.0001

HIS 169 VAL 170 -0.0006

VAL 170 GLU 171 -0.0437

GLU 171 ARG 172 -0.0000

ARG 172 LEU 173 0.0001

LEU 173 GLN 174 0.0050

GLN 174 LEU 175 0.0005

LEU 175 PHE 176 -0.0001

PHE 176 MET 177 0.0346

MET 177 GLU 178 -0.0002

GLU 178 LYS 179 0.0001

LYS 179 HIS 180 0.0713

HIS 180 TYR 181 0.0000

TYR 181 LEU 182 -0.0002

LEU 182 ASN 183 0.0010

ASN 183 GLU 184 0.0001

GLU 184 TRP 185 0.0002

TRP 185 LYS 186 0.0861

LYS 186 LEU 187 0.0001

LEU 187 SER 188 -0.0003

SER 188 ASP 189 0.0001

ASP 189 PHE 190 -0.0002

PHE 190 SER 191 0.0000

SER 191 ARG 192 0.0000

ARG 192 GLU 193 0.0003

GLU 193 PHE 194 0.0003

PHE 194 GLY 195 0.0015

GLY 195 MET 196 0.0001

MET 196 GLY 197 0.0002

GLY 197 LEU 198 -0.0290

LEU 198 THR 199 -0.0002

THR 199 THR 200 -0.0001

THR 200 PHE 201 -0.0032

PHE 201 LYS 202 -0.0001

LYS 202 GLU 203 -0.0003

GLU 203 LEU 204 -0.0412

LEU 204 PHE 205 -0.0005

PHE 205 GLY 206 -0.0003

GLY 206 SER 207 -0.0169

SER 207 VAL 208 0.0001

VAL 208 TYR 209 -0.0001

TYR 209 GLY 210 0.0124

GLY 210 VAL 211 0.0002

VAL 211 SER 212 0.0000

SER 212 PRO 213 -0.0078

PRO 213 ARG 214 0.0003

ARG 214 ALA 215 0.0002

ALA 215 TRP 216 0.0177

TRP 216 ILE 217 -0.0002

ILE 217 SER 218 0.0002

SER 218 GLU 219 -0.0045

GLU 219 ARG 220 -0.0002

ARG 220 ARG 221 0.0003

ARG 221 ILE 222 0.0354

ILE 222 LEU 223 0.0001

LEU 223 TYR 224 -0.0001

TYR 224 ALA 225 -0.0750

ALA 225 HIS 226 0.0003

HIS 226 GLN 227 0.0000

GLN 227 LEU 228 0.0127

LEU 228 LEU 229 -0.0003

LEU 229 LEU 230 -0.0005

LEU 230 ASN 231 0.0118

ASN 231 SER 232 -0.0002

SER 232 ASP 233 0.0000

ASP 233 MET 234 -0.0352

MET 234 SER 235 0.0002

SER 235 ILE 236 -0.0005

ILE 236 VAL 237 0.0079

VAL 237 ASP 238 -0.0001

ASP 238 ILE 239 -0.0004

ILE 239 ALA 240 -0.0102

ALA 240 MET 241 0.0001

MET 241 GLU 242 -0.0002

GLU 242 ALA 243 -0.0321

ALA 243 GLY 244 0.0001

GLY 244 PHE 245 -0.0001

PHE 245 SER 246 -0.0133

SER 246 SER 247 0.0002

SER 247 GLN 248 0.0001

GLN 248 SER 249 0.0005

SER 249 TYR 250 0.0001

TYR 250 PHE 251 0.0000

PHE 251 THR 252 0.0505

THR 252 GLN 253 0.0001

GLN 253 SER 254 -0.0005

SER 254 TYR 255 0.0025

TYR 255 ARG 256 -0.0003

ARG 256 ARG 257 0.0004

ARG 257 ARG 258 -0.0245

ARG 258 PHE 259 0.0003

PHE 259 GLY 260 0.0004

GLY 260 CYS 261 0.1006

CYS 261 THR 262 0.0002

THR 262 PRO 263 -0.0000

PRO 263 SER 264 -0.0048

SER 264 ARG 265 -0.0001

ARG 265 SER 266 -0.0002

SER 266 ARG 267 -0.0026

ARG 267 GLN 268 0.0005

GLN 268 GLY 269 0.0001

GLY 269 LYS 270 -0.0410

LYS 270 ASP 271 0.0002

ASP 271 GLU 272 0.0001

GLU 272 CYS 273 0.0093

CYS 273 ARG 274 0.0000

ARG 274 ALA 275 -0.0002

ALA 275 LYS 276 -0.3625

LYS 276 ASN 277 -0.0001

ASN 277 ASN 278 0.0002

ASN 278 NMA 278 -0.0001

NMA 278 MET 1 0.0202

MET 1 GLN 2 -0.0000

GLN 2 GLY 3 0.1338

GLY 3 ALA 4 0.0000

ALA 4 LYS 5 0.0001

LYS 5 SER 6 -0.3837

SER 6 LEU 7 -0.0003

LEU 7 GLY 8 -0.0000

GLY 8 ARG 9 -0.0432

ARG 9 LYS 10 -0.0003

LYS 10 GLN 11 -0.0002

GLN 11 ILE 12 0.1276

ILE 12 THR 13 0.0002

THR 13 SER 14 0.0001

SER 14 CYS 15 -0.1790

CYS 15 HIS 16 -0.0000

HIS 16 TRP 17 0.0001

TRP 17 ASN 18 -0.0520

ASN 18 ILE 19 0.0003

ILE 19 PRO 20 0.0001

PRO 20 THR 21 -0.0078

THR 21 PHE 22 0.0001

PHE 22 GLU 23 -0.0003

GLU 23 TYR 24 0.0074

TYR 24 ARG 25 -0.0000

ARG 25 VAL 26 -0.0002

VAL 26 ASN 27 -0.0867

ASN 27 LYS 28 0.0004

LYS 28 GLU 29 0.0002

GLU 29 GLU 30 -0.0050

GLU 30 GLY 31 0.0000

GLY 31 VAL 32 -0.0000

VAL 32 TYR 33 0.0057

TYR 33 VAL 34 0.0002

VAL 34 LEU 35 0.0001

LEU 35 LEU 36 -0.0214

LEU 36 GLU 37 0.0003

GLU 37 GLY 38 -0.0000

GLY 38 GLU 39 0.0243

GLU 39 LEU 40 0.0001

LEU 40 THR 41 0.0004

THR 41 VAL 42 -0.0053

VAL 42 GLN 43 -0.0000

GLN 43 ASP 44 -0.0001

ASP 44 ILE 45 -0.0362

ILE 45 ASP 46 -0.0002

ASP 46 SER 47 0.0003

SER 47 THR 48 0.0216

THR 48 PHE 49 0.0000

PHE 49 CYS 50 0.0003

CYS 50 LEU 51 0.0264

LEU 51 ALA 52 0.0001

ALA 52 PRO 53 0.0002

PRO 53 GLY 54 -0.0018

GLY 54 GLU 55 -0.0002

GLU 55 LEU 56 -0.0001

LEU 56 LEU 57 -0.0430

LEU 57 PHE 58 -0.0000

PHE 58 VAL 59 0.0001

VAL 59 ARG 60 -0.0086

ARG 60 ARG 61 -0.0002

ARG 61 GLY 62 -0.0002

GLY 62 SER 63 -0.0561

SER 63 TYR 64 0.0003

TYR 64 VAL 65 0.0005

VAL 65 VAL 66 -0.0136

VAL 66 SER 67 -0.0003

SER 67 THR 68 0.0002

THR 68 LYS 69 -0.0050

LYS 69 GLY 70 -0.0000

GLY 70 LYS 71 0.0003

LYS 71 ASP 72 -0.0223

ASP 72 SER 73 0.0003

SER 73 ARG 74 -0.0006

ARG 74 ILE 75 0.0388

ILE 75 LEU 76 0.0003

LEU 76 TRP 77 0.0002

TRP 77 ILE 78 -0.0133

ILE 78 PRO 79 0.0006

PRO 79 LEU 80 -0.0002

LEU 80 SER 81 0.0380

SER 81 ALA 82 0.0003

ALA 82 GLN 83 0.0000

GLN 83 PHE 84 -0.0106

PHE 84 LEU 85 -0.0000

LEU 85 GLN 86 -0.0002

GLN 86 GLY 87 -0.0872

GLY 87 PHE 88 -0.0005

PHE 88 VAL 89 0.0002

VAL 89 GLN 90 0.0931

GLN 90 ARG 91 0.0002

ARG 91 PHE 92 0.0004

PHE 92 GLY 93 0.0709

GLY 93 ALA 94 0.0002

ALA 94 LEU 95 -0.0002

LEU 95 LEU 96 -0.0356

LEU 96 SER 97 0.0003

SER 97 GLU 98 -0.0004

GLU 98 VAL 99 0.0517

VAL 99 GLU 100 0.0002

GLU 100 ARG 101 0.0002

ARG 101 CYS 102 -0.0294

CYS 102 ASP 103 0.0004

ASP 103 GLU 104 0.0001

GLU 104 PRO 105 -0.0118

PRO 105 VAL 106 -0.0001

VAL 106 PRO 107 -0.0000

PRO 107 GLY 108 0.0516

GLY 108 ILE 109 -0.0001

ILE 109 ILE 110 -0.0003

ILE 110 ALA 111 -0.0280

ALA 111 PHE 112 0.0003

PHE 112 ALA 113 0.0002

ALA 113 ALA 114 -0.0366

ALA 114 THR 115 0.0000

THR 115 PRO 116 -0.0003

PRO 116 LEU 117 0.0369

LEU 117 LEU 118 0.0000

LEU 118 ALA 119 -0.0001

ALA 119 GLY 120 -0.0105

GLY 120 CYS 121 -0.0004

CYS 121 VAL 122 0.0001

VAL 122 LYS 123 -0.0081

LYS 123 GLY 124 0.0002

GLY 124 LEU 125 0.0000

LEU 125 LYS 126 0.0297

LYS 126 GLU 127 0.0001

GLU 127 LEU 128 0.0000

LEU 128 LEU 129 -0.0357

LEU 129 VAL 130 -0.0003

VAL 130 HIS 131 -0.0000

HIS 131 GLU 132 0.0498

GLU 132 HIS 133 -0.0001

HIS 133 PRO 134 -0.0000

PRO 134 PRO 135 -0.0426

PRO 135 MET 136 0.0002

MET 136 LEU 137 -0.0001

LEU 137 ALA 138 -0.1176

ALA 138 CYS 139 0.0004

CYS 139 LEU 140 -0.0002

LEU 140 LYS 141 -0.0123

LYS 141 ILE 142 -0.0002

ILE 142 GLU 143 0.0000

GLU 143 GLU 144 0.0199

GLU 144 LEU 145 0.0003

LEU 145 LEU 146 -0.0001

LEU 146 MET 147 -0.0057

MET 147 LEU 148 -0.0002

LEU 148 PHE 149 -0.0004

PHE 149 ALA 150 0.0428

ALA 150 PHE 151 0.0001

PHE 151 SER 152 0.0000

SER 152 PRO 153 -0.0200

PRO 153 GLN 154 0.0002

GLN 154 GLY 155 0.0001

GLY 155 PRO 156 -0.0189

PRO 156 LEU 157 0.0005

LEU 157 LEU 158 0.0001

LEU 158 MET 159 0.0186

MET 159 SER 160 -0.0003

SER 160 VAL 161 -0.0002

VAL 161 LEU 162 0.0010

LEU 162 ARG 163 0.0002

ARG 163 GLN 164 -0.0004

GLN 164 LEU 165 0.0300

LEU 165 SER 166 -0.0006

SER 166 ASN 167 -0.0002

ASN 167 ARG 168 -0.1619

ARG 168 HIS 169 0.0002

HIS 169 VAL 170 -0.0002

VAL 170 GLU 171 -0.0450

GLU 171 ARG 172 -0.0003

ARG 172 LEU 173 0.0000

LEU 173 GLN 174 0.0027

GLN 174 LEU 175 0.0000

LEU 175 PHE 176 0.0001

PHE 176 MET 177 0.0538

MET 177 GLU 178 0.0000

GLU 178 LYS 179 0.0001

LYS 179 HIS 180 0.0820

HIS 180 TYR 181 -0.0002

TYR 181 LEU 182 0.0003

LEU 182 ASN 183 -0.0211

ASN 183 GLU 184 -0.0003

GLU 184 TRP 185 -0.0001

TRP 185 LYS 186 0.0523

LYS 186 LEU 187 -0.0000

LEU 187 SER 188 -0.0003

SER 188 ASP 189 -0.0025

ASP 189 PHE 190 0.0001

PHE 190 SER 191 0.0000

SER 191 ARG 192 0.0152

ARG 192 GLU 193 -0.0000

GLU 193 PHE 194 0.0000

PHE 194 GLY 195 0.0068

GLY 195 MET 196 0.0002

MET 196 GLY 197 -0.0000

GLY 197 LEU 198 -0.0392

LEU 198 THR 199 0.0002

THR 199 THR 200 0.0000

THR 200 PHE 201 0.0044

PHE 201 LYS 202 0.0003

LYS 202 GLU 203 -0.0004

GLU 203 LEU 204 -0.0466

LEU 204 PHE 205 0.0005

PHE 205 GLY 206 -0.0001

GLY 206 SER 207 -0.0063

SER 207 VAL 208 0.0001

VAL 208 TYR 209 0.0002

TYR 209 GLY 210 0.0299

GLY 210 VAL 211 -0.0003

VAL 211 SER 212 0.0003

SER 212 PRO 213 -0.0234

PRO 213 ARG 214 0.0000

ARG 214 ALA 215 0.0000

ALA 215 TRP 216 0.0310

TRP 216 ILE 217 0.0000

ILE 217 SER 218 0.0003

SER 218 GLU 219 -0.0007

GLU 219 ARG 220 0.0001

ARG 220 ARG 221 0.0002

ARG 221 ILE 222 0.0512

ILE 222 LEU 223 0.0004

LEU 223 TYR 224 -0.0001

TYR 224 ALA 225 -0.0925

ALA 225 HIS 226 0.0001

HIS 226 GLN 227 -0.0003

GLN 227 LEU 228 0.0292

LEU 228 LEU 229 -0.0000

LEU 229 LEU 230 -0.0003

LEU 230 ASN 231 -0.0005

ASN 231 SER 232 0.0003

SER 232 ASP 233 0.0002

ASP 233 MET 234 -0.0126

MET 234 SER 235 -0.0001

SER 235 ILE 236 0.0002

ILE 236 VAL 237 0.0136

VAL 237 ASP 238 0.0001

ASP 238 ILE 239 -0.0003

ILE 239 ALA 240 -0.0151

ALA 240 MET 241 -0.0003

MET 241 GLU 242 -0.0003

GLU 242 ALA 243 -0.0274

ALA 243 GLY 244 -0.0001

GLY 244 PHE 245 -0.0003

PHE 245 SER 246 -0.0241

SER 246 SER 247 0.0005

SER 247 GLN 248 0.0001

GLN 248 SER 249 0.0164

SER 249 TYR 250 0.0002

TYR 250 PHE 251 0.0002

PHE 251 THR 252 0.0745

THR 252 GLN 253 0.0002

GLN 253 SER 254 -0.0001

SER 254 TYR 255 0.0077

TYR 255 ARG 256 0.0003

ARG 256 ARG 257 -0.0004

ARG 257 ARG 258 -0.0516

ARG 258 PHE 259 0.0001

PHE 259 GLY 260 0.0000

GLY 260 CYS 261 0.1081

CYS 261 THR 262 -0.0000

THR 262 PRO 263 0.0003

PRO 263 SER 264 -0.0091

SER 264 ARG 265 0.0003

ARG 265 SER 266 0.0001

SER 266 ARG 267 -0.0104

ARG 267 GLN 268 -0.0002

GLN 268 GLY 269 0.0001

GLY 269 LYS 270 -0.0358

LYS 270 ASP 271 -0.0001

ASP 271 GLU 272 0.0003

GLU 272 CYS 273 0.0189

CYS 273 ARG 274 -0.0001

ARG 274 ALA 275 -0.0001

ALA 275 LYS 276 -0.3714

LYS 276 ASN 277 0.0001

ASN 277 ASN 278 0.0003

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 24 ---

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

* EXSA_dimer1 *