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

* IMMUNE SYSTEM 28-JAN-19 6NT5 *

CA strain for 2504011532321665694

--- 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
SER 4 SER 5 0.0001

SER 5 LEU 6 -0.0004

LEU 6 HIS 7 -0.0078

HIS 7 PRO 8 -0.0003

PRO 8 SER 9 -0.0000

SER 9 ILE 10 0.0273

ILE 10 PRO 11 0.0002

PRO 11 CYS 12 -0.0003

CYS 12 PRO 13 0.0269

PRO 13 ARG 14 0.0002

ARG 14 GLY 15 0.0000

GLY 15 HIS 16 -0.0210

HIS 16 GLY 17 -0.0002

GLY 17 ALA 18 -0.0001

ALA 18 GLN 19 0.0218

GLN 19 LYS 20 0.0003

LYS 20 ALA 21 -0.0001

ALA 21 ALA 22 -0.0065

ALA 22 LEU 23 -0.0001

LEU 23 VAL 24 0.0000

VAL 24 LEU 25 -0.0223

LEU 25 LEU 26 0.0002

LEU 26 SER 27 0.0002

SER 27 ALA 28 -0.0307

ALA 28 CYS 29 0.0002

CYS 29 LEU 30 0.0001

LEU 30 VAL 31 -0.0124

VAL 31 THR 32 0.0000

THR 32 LEU 33 0.0001

LEU 33 TRP 34 0.0320

TRP 34 GLY 35 0.0000

GLY 35 LEU 44 -0.0946

LEU 44 ARG 45 -0.0001

ARG 45 TYR 46 -0.0003

TYR 46 LEU 47 0.0103

LEU 47 VAL 48 0.0002

VAL 48 LEU 49 0.0003

LEU 49 HIS 50 0.0104

HIS 50 LEU 51 -0.0003

LEU 51 ALA 52 0.0006

ALA 52 SER 53 -0.0018

SER 53 LEU 54 0.0002

LEU 54 GLN 55 -0.0001

GLN 55 LEU 56 0.0229

LEU 56 GLY 57 0.0001

GLY 57 LEU 58 0.0000

LEU 58 LEU 59 -0.0034

LEU 59 LEU 60 0.0000

LEU 60 ASN 61 0.0001

ASN 61 GLY 62 0.0263

GLY 62 VAL 63 0.0003

VAL 63 CYS 64 0.0001

CYS 64 SER 65 0.0016

SER 65 LEU 66 -0.0005

LEU 66 ALA 67 0.0004

ALA 67 GLU 68 -0.0145

GLU 68 GLU 69 -0.0001

GLU 69 LEU 70 -0.0001

LEU 70 ARG 71 -0.0097

ARG 71 HIS 72 0.0002

HIS 72 ILE 73 -0.0002

ILE 73 HIS 74 0.0356

HIS 74 SER 75 0.0001

SER 75 ARG 76 -0.0003

ARG 76 TYR 77 -0.0287

TYR 77 ARG 78 0.0004

ARG 78 TYR 81 0.0125

TYR 81 TRP 82 0.0000

TRP 82 ARG 83 0.0000

ARG 83 THR 84 0.0005

THR 84 VAL 85 -0.0001

VAL 85 ARG 86 0.0000

ARG 86 ALA 87 -0.0066

ALA 87 CYS 88 -0.0002

CYS 88 LEU 89 -0.0002

LEU 89 GLY 90 0.0087

GLY 90 CYS 91 -0.0000

CYS 91 PRO 92 -0.0002

PRO 92 LEU 93 -0.0029

LEU 93 ARG 94 -0.0001

ARG 94 ARG 95 0.0003

ARG 95 GLY 96 -0.0035

GLY 96 ALA 97 0.0004

ALA 97 LEU 98 -0.0003

LEU 98 LEU 99 0.0119

LEU 99 LEU 100 0.0001

LEU 100 LEU 101 -0.0001

LEU 101 SER 102 -0.0084

SER 102 ILE 103 -0.0000

ILE 103 TYR 104 -0.0003

TYR 104 PHE 105 0.0039

PHE 105 TYR 106 -0.0003

TYR 106 PHE 117 0.0094

PHE 117 THR 118 -0.0000

THR 118 TRP 119 0.0001

TRP 119 MET 120 0.0092

MET 120 LEU 121 -0.0003

LEU 121 ALA 122 -0.0003

ALA 122 LEU 123 -0.0283

LEU 123 LEU 124 -0.0002

LEU 124 GLY 125 0.0001

GLY 125 LEU 126 0.0066

LEU 126 SER 127 -0.0003

SER 127 GLN 128 0.0003

GLN 128 ALA 129 0.0058

ALA 129 LEU 130 -0.0001

LEU 130 ASN 131 0.0000

ASN 131 ILE 132 0.0322

ILE 132 LEU 133 -0.0002

LEU 133 LEU 134 0.0002

LEU 134 GLY 135 -0.0419

GLY 135 LEU 136 -0.0001

LEU 136 LYS 137 -0.0000

LYS 137 GLY 138 -0.0082

GLY 138 LEU 139 0.0002

LEU 139 ALA 140 -0.0000

ALA 140 PRO 141 -0.0131

PRO 141 ALA 142 0.0002

ALA 142 GLU 143 0.0000

GLU 143 ILE 144 0.0073

ILE 144 SER 145 -0.0002

SER 145 ALA 146 0.0001

ALA 146 VAL 147 0.0288

VAL 147 CYS 148 -0.0002

CYS 148 GLU 149 0.0001

GLU 149 LYS 150 0.0368

LYS 150 GLY 151 -0.0004

GLY 151 ASN 152 0.0001

ASN 152 PHE 153 0.0456

PHE 153 ASN 154 0.0001

ASN 154 VAL 155 -0.0000

VAL 155 ALA 156 0.0074

ALA 156 HIS 157 -0.0001

HIS 157 GLY 158 0.0002

GLY 158 LEU 159 -0.0221

LEU 159 ALA 160 -0.0002

ALA 160 TRP 161 -0.0001

TRP 161 SER 162 -0.0443

SER 162 TYR 163 0.0001

TYR 163 TYR 164 -0.0003

TYR 164 ILE 165 -0.0145

ILE 165 GLY 166 -0.0001

GLY 166 TYR 167 0.0001

TYR 167 LEU 168 0.0028

LEU 168 ARG 169 0.0000

ARG 169 LEU 170 0.0001

LEU 170 ILE 171 -0.1349

ILE 171 LEU 172 -0.0001

LEU 172 PRO 173 0.0002

PRO 173 GLU 174 -0.1132

GLU 174 LEU 175 0.0000

LEU 175 GLN 176 0.0001

GLN 176 ALA 177 -0.0175

ALA 177 ARG 178 0.0002

ARG 178 ILE 179 0.0001

ILE 179 ARG 180 -0.0020

ARG 180 THR 181 0.0003

THR 181 TYR 182 -0.0001

TYR 182 ASN 183 0.0135

ASN 183 GLN 184 -0.0002

GLN 184 HIS 185 -0.0002

HIS 185 TYR 186 -0.0090

TYR 186 ASN 187 -0.0003

ASN 187 ASN 188 -0.0002

ASN 188 LEU 189 -0.0110

LEU 189 ALA 193 -0.0125

ALA 193 VAL 194 -0.0001

VAL 194 SER 195 0.0002

SER 195 GLN 196 -0.0086

GLN 196 ARG 197 0.0002

ARG 197 LEU 198 -0.0001

LEU 198 TYR 199 0.0231

TYR 199 ILE 200 0.0003

ILE 200 LEU 201 -0.0003

LEU 201 LEU 202 0.0461

LEU 202 PRO 203 0.0003

PRO 203 LEU 204 -0.0001

LEU 204 ASP 205 0.0135

ASP 205 CYS 206 -0.0000

CYS 206 GLY 207 0.0002

GLY 207 VAL 208 0.1139

VAL 208 PRO 209 0.0001

PRO 209 ASP 210 -0.0001

ASP 210 ASN 211 0.0393

ASN 211 LEU 212 0.0000

LEU 212 SER 213 0.0004

SER 213 MET 214 0.0132

MET 214 ALA 215 -0.0002

ALA 215 ASP 216 -0.0003

ASP 216 PRO 217 0.0119

PRO 217 ASN 218 -0.0000

ASN 218 ILE 219 0.0002

ILE 219 ARG 220 0.0055

ARG 220 PHE 221 0.0002

PHE 221 LEU 222 -0.0001

LEU 222 ASP 223 -0.0377

ASP 223 LYS 224 -0.0002

LYS 224 LEU 225 -0.0000

LEU 225 PRO 226 0.0054

PRO 226 GLN 227 -0.0001

GLN 227 TYR 240 0.0190

TYR 240 SER 241 -0.0003

SER 241 ASN 242 -0.0000

ASN 242 SER 243 -0.0869

SER 243 ILE 244 -0.0001

ILE 244 TYR 245 -0.0001

TYR 245 GLU 246 -0.0310

GLU 246 LEU 247 0.0002

LEU 247 LEU 248 -0.0001

LEU 248 GLY 251 0.0098

GLY 251 GLN 252 0.0002

GLN 252 ARG 253 -0.0001

ARG 253 ALA 254 0.0002

ALA 254 GLY 255 0.0001

GLY 255 THR 256 -0.0000

THR 256 CYS 257 0.0049

CYS 257 VAL 258 -0.0002

VAL 258 LEU 259 0.0000

LEU 259 GLU 260 0.0158

GLU 260 TYR 261 0.0000

TYR 261 ALA 262 -0.0002

ALA 262 THR 263 0.0170

THR 263 PRO 264 -0.0002

PRO 264 LEU 265 -0.0004

LEU 265 GLN 266 -0.0322

GLN 266 THR 267 -0.0001

THR 267 LEU 268 -0.0003

LEU 268 PHE 269 -0.0110

PHE 269 ALA 270 -0.0002

ALA 270 MET 271 0.0003

MET 271 SER 272 -0.0246

SER 272 GLN 273 0.0000

GLN 273 TYR 274 0.0000

TYR 274 SER 275 0.0265

SER 275 GLN 276 -0.0002

GLN 276 ALA 277 -0.0001

ALA 277 GLY 278 -0.0369

GLY 278 PHE 279 -0.0003

PHE 279 SER 280 -0.0003

SER 280 ARG 281 -0.0069

ARG 281 GLU 282 0.0001

GLU 282 ASP 283 -0.0001

ASP 283 ARG 284 0.0302

ARG 284 LEU 285 -0.0000

LEU 285 GLU 286 0.0004

GLU 286 GLN 287 0.0173

GLN 287 ALA 288 0.0001

ALA 288 LYS 289 0.0001

LYS 289 LEU 290 0.0414

LEU 290 PHE 291 -0.0002

PHE 291 CYS 292 0.0004

CYS 292 ARG 293 0.0119

ARG 293 THR 294 0.0001

THR 294 LEU 295 0.0005

LEU 295 GLU 296 0.0066

GLU 296 ASP 297 0.0004

ASP 297 ILE 298 0.0003

ILE 298 LEU 299 -0.0676

LEU 299 ALA 300 0.0000

ALA 300 ASP 301 -0.0003

ASP 301 ALA 302 -0.0651

ALA 302 PRO 303 -0.0000

PRO 303 GLU 304 -0.0001

GLU 304 SER 305 0.0004

SER 305 GLN 306 -0.0004

GLN 306 ASN 307 -0.0001

ASN 307 ASN 308 0.0226

ASN 308 CYS 309 -0.0000

CYS 309 ARG 310 0.0001

ARG 310 LEU 311 -0.0677

LEU 311 ILE 312 0.0003

ILE 312 ALA 313 -0.0002

ALA 313 TYR 314 -0.0194

TYR 314 GLN 315 -0.0001

GLN 315 GLU 316 0.0004

GLU 316 PRO 317 -0.0326

PRO 317 SER 322 0.0184

SER 322 PHE 323 -0.0002

PHE 323 SER 324 0.0003

SER 324 LEU 325 -0.0467

LEU 325 SER 326 -0.0004

SER 326 GLN 327 -0.0001

GLN 327 GLU 328 0.0320

GLU 328 VAL 329 -0.0000

VAL 329 LEU 330 0.0002

LEU 330 ARG 331 0.0044

ARG 331 HIS 332 0.0004

HIS 332 LEU 333 -0.0004

LEU 333 ARG 334 -0.0171

ARG 334 GLN 335 0.0002

GLN 335 GLU 336 0.0000

GLU 336 SER 4 -0.0594

SER 4 SER 5 -0.0002

SER 5 LEU 6 0.0002

LEU 6 HIS 7 -0.0078

HIS 7 PRO 8 0.0003

PRO 8 SER 9 0.0000

SER 9 ILE 10 0.0275

ILE 10 PRO 11 -0.0000

PRO 11 CYS 12 -0.0003

CYS 12 PRO 13 0.0276

PRO 13 ARG 14 0.0001

ARG 14 GLY 15 0.0002

GLY 15 HIS 16 -0.0191

HIS 16 GLY 17 -0.0003

GLY 17 ALA 18 -0.0003

ALA 18 GLN 19 0.0249

GLN 19 LYS 20 -0.0002

LYS 20 ALA 21 -0.0003

ALA 21 ALA 22 -0.0057

ALA 22 LEU 23 -0.0001

LEU 23 VAL 24 -0.0000

VAL 24 LEU 25 -0.0219

LEU 25 LEU 26 -0.0003

LEU 26 SER 27 0.0001

SER 27 ALA 28 -0.0295

ALA 28 CYS 29 -0.0000

CYS 29 LEU 30 -0.0002

LEU 30 VAL 31 -0.0126

VAL 31 THR 32 -0.0002

THR 32 LEU 33 -0.0000

LEU 33 TRP 34 0.0324

TRP 34 GLY 35 -0.0001

GLY 35 LEU 44 -0.0926

LEU 44 ARG 45 -0.0001

ARG 45 TYR 46 -0.0003

TYR 46 LEU 47 0.0097

LEU 47 VAL 48 0.0002

VAL 48 LEU 49 0.0000

LEU 49 HIS 50 0.0111

HIS 50 LEU 51 0.0003

LEU 51 ALA 52 0.0003

ALA 52 SER 53 -0.0015

SER 53 LEU 54 0.0005

LEU 54 GLN 55 -0.0002

GLN 55 LEU 56 0.0230

LEU 56 GLY 57 -0.0000

GLY 57 LEU 58 -0.0005

LEU 58 LEU 59 -0.0041

LEU 59 LEU 60 0.0000

LEU 60 ASN 61 -0.0000

ASN 61 GLY 62 0.0245

GLY 62 VAL 63 0.0002

VAL 63 CYS 64 0.0001

CYS 64 SER 65 0.0029

SER 65 LEU 66 -0.0002

LEU 66 ALA 67 0.0004

ALA 67 GLU 68 -0.0156

GLU 68 GLU 69 0.0003

GLU 69 LEU 70 0.0002

LEU 70 ARG 71 -0.0099

ARG 71 HIS 72 0.0001

HIS 72 ILE 73 -0.0003

ILE 73 HIS 74 0.0319

HIS 74 SER 75 -0.0002

SER 75 ARG 76 -0.0003

ARG 76 TYR 77 -0.0303

TYR 77 ARG 78 -0.0000

ARG 78 TYR 81 0.0113

TYR 81 TRP 82 -0.0001

TRP 82 ARG 83 0.0002

ARG 83 THR 84 0.0011

THR 84 VAL 85 0.0003

VAL 85 ARG 86 0.0000

ARG 86 ALA 87 -0.0056

ALA 87 CYS 88 -0.0001

CYS 88 LEU 89 -0.0001

LEU 89 GLY 90 0.0097

GLY 90 CYS 91 -0.0000

CYS 91 PRO 92 -0.0002

PRO 92 LEU 93 -0.0042

LEU 93 ARG 94 -0.0001

ARG 94 ARG 95 0.0002

ARG 95 GLY 96 -0.0044

GLY 96 ALA 97 -0.0001

ALA 97 LEU 98 0.0003

LEU 98 LEU 99 0.0148

LEU 99 LEU 100 0.0001

LEU 100 LEU 101 -0.0004

LEU 101 SER 102 -0.0092

SER 102 ILE 103 -0.0003

ILE 103 TYR 104 -0.0002

TYR 104 PHE 105 0.0034

PHE 105 TYR 106 0.0001

TYR 106 PHE 117 0.0094

PHE 117 THR 118 0.0000

THR 118 TRP 119 0.0000

TRP 119 MET 120 0.0083

MET 120 LEU 121 0.0000

LEU 121 ALA 122 0.0000

ALA 122 LEU 123 -0.0278

LEU 123 LEU 124 0.0003

LEU 124 GLY 125 0.0000

GLY 125 LEU 126 0.0067

LEU 126 SER 127 0.0003

SER 127 GLN 128 -0.0002

GLN 128 ALA 129 0.0043

ALA 129 LEU 130 -0.0001

LEU 130 ASN 131 -0.0001

ASN 131 ILE 132 0.0326

ILE 132 LEU 133 0.0000

LEU 133 LEU 134 -0.0003

LEU 134 GLY 135 -0.0434

GLY 135 LEU 136 -0.0002

LEU 136 LYS 137 -0.0001

LYS 137 GLY 138 -0.0077

GLY 138 LEU 139 0.0001

LEU 139 ALA 140 -0.0001

ALA 140 PRO 141 -0.0123

PRO 141 ALA 142 0.0001

ALA 142 GLU 143 -0.0004

GLU 143 ILE 144 0.0073

ILE 144 SER 145 0.0005

SER 145 ALA 146 -0.0003

ALA 146 VAL 147 0.0292

VAL 147 CYS 148 -0.0002

CYS 148 GLU 149 -0.0003

GLU 149 LYS 150 0.0353

LYS 150 GLY 151 -0.0002

GLY 151 ASN 152 0.0000

ASN 152 PHE 153 0.0463

PHE 153 ASN 154 0.0002

ASN 154 VAL 155 -0.0001

VAL 155 ALA 156 0.0066

ALA 156 HIS 157 -0.0001

HIS 157 GLY 158 0.0001

GLY 158 LEU 159 -0.0220

LEU 159 ALA 160 0.0005

ALA 160 TRP 161 -0.0001

TRP 161 SER 162 -0.0447

SER 162 TYR 163 0.0003

TYR 163 TYR 164 -0.0000

TYR 164 ILE 165 -0.0132

ILE 165 GLY 166 -0.0001

GLY 166 TYR 167 -0.0002

TYR 167 LEU 168 0.0026

LEU 168 ARG 169 -0.0004

ARG 169 LEU 170 -0.0002

LEU 170 ILE 171 -0.1342

ILE 171 LEU 172 0.0003

LEU 172 PRO 173 -0.0002

PRO 173 GLU 174 -0.1136

GLU 174 LEU 175 0.0001

LEU 175 GLN 176 -0.0003

GLN 176 ALA 177 -0.0181

ALA 177 ARG 178 -0.0000

ARG 178 ILE 179 0.0000

ILE 179 ARG 180 -0.0023

ARG 180 THR 181 -0.0002

THR 181 TYR 182 -0.0000

TYR 182 ASN 183 0.0140

ASN 183 GLN 184 0.0002

GLN 184 HIS 185 0.0002

HIS 185 TYR 186 -0.0100

TYR 186 ASN 187 0.0002

ASN 187 ASN 188 0.0000

ASN 188 LEU 189 -0.0118

LEU 189 ALA 193 -0.0133

ALA 193 VAL 194 -0.0001

VAL 194 SER 195 0.0000

SER 195 GLN 196 -0.0087

GLN 196 ARG 197 0.0001

ARG 197 LEU 198 -0.0002

LEU 198 TYR 199 0.0226

TYR 199 ILE 200 0.0001

ILE 200 LEU 201 0.0000

LEU 201 LEU 202 0.0446

LEU 202 PRO 203 0.0004

PRO 203 LEU 204 0.0002

LEU 204 ASP 205 0.0133

ASP 205 CYS 206 -0.0000

CYS 206 GLY 207 0.0003

GLY 207 VAL 208 0.1150

VAL 208 PRO 209 0.0001

PRO 209 ASP 210 0.0001

ASP 210 ASN 211 0.0404

ASN 211 LEU 212 -0.0004

LEU 212 SER 213 0.0002

SER 213 MET 214 0.0130

MET 214 ALA 215 -0.0002

ALA 215 ASP 216 0.0002

ASP 216 PRO 217 0.0108

PRO 217 ASN 218 0.0000

ASN 218 ILE 219 0.0004

ILE 219 ARG 220 0.0049

ARG 220 PHE 221 0.0001

PHE 221 LEU 222 0.0003

LEU 222 ASP 223 -0.0381

ASP 223 LYS 224 0.0005

LYS 224 LEU 225 -0.0002

LEU 225 PRO 226 0.0051

PRO 226 GLN 227 -0.0001

GLN 227 TYR 240 0.0190

TYR 240 SER 241 0.0002

SER 241 ASN 242 -0.0002

ASN 242 SER 243 -0.0868

SER 243 ILE 244 -0.0001

ILE 244 TYR 245 0.0000

TYR 245 GLU 246 -0.0302

GLU 246 LEU 247 -0.0000

LEU 247 LEU 248 -0.0001

LEU 248 GLY 251 0.0094

GLY 251 GLN 252 0.0001

GLN 252 ARG 253 -0.0005

ARG 253 ALA 254 0.0009

ALA 254 GLY 255 -0.0001

GLY 255 THR 256 -0.0001

THR 256 CYS 257 0.0051

CYS 257 VAL 258 0.0002

VAL 258 LEU 259 0.0001

LEU 259 GLU 260 0.0172

GLU 260 TYR 261 -0.0001

TYR 261 ALA 262 -0.0000

ALA 262 THR 263 0.0162

THR 263 PRO 264 0.0002

PRO 264 LEU 265 -0.0002

LEU 265 GLN 266 -0.0334

GLN 266 THR 267 -0.0001

THR 267 LEU 268 0.0002

LEU 268 PHE 269 -0.0105

PHE 269 ALA 270 0.0001

ALA 270 MET 271 -0.0001

MET 271 SER 272 -0.0247

SER 272 GLN 273 0.0001

GLN 273 TYR 274 0.0000

TYR 274 SER 275 0.0264

SER 275 GLN 276 0.0002

GLN 276 ALA 277 0.0002

ALA 277 GLY 278 -0.0369

GLY 278 PHE 279 -0.0001

PHE 279 SER 280 0.0004

SER 280 ARG 281 -0.0068

ARG 281 GLU 282 0.0002

GLU 282 ASP 283 -0.0002

ASP 283 ARG 284 0.0300

ARG 284 LEU 285 0.0004

LEU 285 GLU 286 0.0005

GLU 286 GLN 287 0.0178

GLN 287 ALA 288 0.0003

ALA 288 LYS 289 -0.0002

LYS 289 LEU 290 0.0415

LEU 290 PHE 291 0.0004

PHE 291 CYS 292 -0.0001

CYS 292 ARG 293 0.0113

ARG 293 THR 294 0.0003

THR 294 LEU 295 -0.0001

LEU 295 GLU 296 0.0077

GLU 296 ASP 297 0.0003

ASP 297 ILE 298 -0.0001

ILE 298 LEU 299 -0.0696

LEU 299 ALA 300 0.0003

ALA 300 ASP 301 -0.0002

ASP 301 ALA 302 -0.0662

ALA 302 PRO 303 0.0001

PRO 303 GLU 304 -0.0002

GLU 304 SER 305 0.0013

SER 305 GLN 306 0.0000

GLN 306 ASN 307 0.0002

ASN 307 ASN 308 0.0228

ASN 308 CYS 309 -0.0003

CYS 309 ARG 310 -0.0000

ARG 310 LEU 311 -0.0681

LEU 311 ILE 312 0.0001

ILE 312 ALA 313 0.0004

ALA 313 TYR 314 -0.0162

TYR 314 GLN 315 0.0003

GLN 315 GLU 316 -0.0003

GLU 316 PRO 317 -0.0308

PRO 317 SER 322 0.0178

SER 322 PHE 323 -0.0002

PHE 323 SER 324 -0.0001

SER 324 LEU 325 -0.0451

LEU 325 SER 326 0.0002

SER 326 GLN 327 -0.0003

GLN 327 GLU 328 0.0320

GLU 328 VAL 329 0.0001

VAL 329 LEU 330 -0.0002

LEU 330 ARG 331 0.0053

ARG 331 HIS 332 0.0002

HIS 332 LEU 333 0.0003

LEU 333 ARG 334 -0.0168

ARG 334 GLN 335 -0.0000

GLN 335 GLU 336 -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 8th, 2025.

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

*** IMMUNE SYSTEM 28-JAN-19 6NT5 ***

CA strain for 2504011532321665694

--- normal mode 11 ---

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

* IMMUNE SYSTEM 28-JAN-19 6NT5 *