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

* *

CA strain for 221128151102134046

--- normal mode 10 ---

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 MET 1 0.0002

MET 1 GLU 2 -0.0001

GLU 2 GLU 2 -0.0003

GLU 2 LEU 3 -0.0062

LEU 3 LEU 3 0.0001

LEU 3 ARG 4 -0.0000

ARG 4 ARG 4 -0.0004

ARG 4 HIS 5 -0.0155

HIS 5 HIS 5 0.0006

HIS 5 THR 6 -0.0001

THR 6 THR 6 0.0005

THR 6 PRO 7 0.0565

PRO 7 PRO 7 0.0005

PRO 7 ALA 8 0.0003

ALA 8 ALA 8 -0.0002

ALA 8 ARG 9 -0.0792

ARG 9 ARG 9 0.0004

ARG 9 ASP 10 0.0000

ASP 10 ASP 10 0.0001

ASP 10 LEU 11 0.0062

LEU 11 LEU 11 0.0003

LEU 11 ASP 12 -0.0002

ASP 12 ASP 12 -0.0003

ASP 12 LYS 13 0.0794

LYS 13 LYS 13 0.0003

LYS 13 PHE 14 -0.0001

PHE 14 PHE 14 0.0003

PHE 14 ILE 15 0.0583

ILE 15 ILE 15 0.0002

ILE 15 GLU 16 0.0002

GLU 16 GLU 16 -0.0000

GLU 16 ASP 17 -0.0301

ASP 17 ASP 17 -0.0001

ASP 17 HIS 18 -0.0001

HIS 18 HIS 18 0.0000

HIS 18 LEU 19 -0.0098

LEU 19 LEU 19 0.0001

LEU 19 LEU 20 -0.0001

LEU 20 LEU 20 -0.0006

LEU 20 PRO 21 0.1495

PRO 21 PRO 21 0.0001

PRO 21 ASN 22 0.0004

ASN 22 ASN 22 0.0005

ASN 22 THR 23 0.0101

THR 23 THR 23 0.0003

THR 23 CYS 24 -0.0001

CYS 24 CYS 24 -0.0005

CYS 24 PHE 25 0.0187

PHE 25 PHE 25 0.0001

PHE 25 ARG 26 -0.0001

ARG 26 ARG 26 0.0002

ARG 26 THR 27 -0.0393

THR 27 THR 27 -0.0004

THR 27 GLN 28 -0.0001

GLN 28 GLN 28 -0.0005

GLN 28 VAL 29 -0.0066

VAL 29 VAL 29 0.0003

VAL 29 LYS 30 -0.0002

LYS 30 LYS 30 0.0000

LYS 30 GLU 31 -0.0306

GLU 31 GLU 31 -0.0003

GLU 31 ALA 32 -0.0003

ALA 32 ALA 32 0.0002

ALA 32 ILE 33 -0.0210

ILE 33 ILE 33 -0.0002

ILE 33 ASP 34 0.0003

ASP 34 ASP 34 0.0003

ASP 34 ILE 35 -0.1144

ILE 35 ILE 35 -0.0000

ILE 35 VAL 36 -0.0002

VAL 36 VAL 36 0.0006

VAL 36 CYS 37 -0.0088

CYS 37 CYS 37 0.0005

CYS 37 ARG 38 -0.0005

ARG 38 ARG 38 0.0003

ARG 38 PHE 39 -0.0072

PHE 39 PHE 39 -0.0006

PHE 39 LEU 40 0.0000

LEU 40 LEU 40 -0.0006

LEU 40 LYS 41 0.0154

LYS 41 LYS 41 0.0000

LYS 41 GLU 42 0.0001

GLU 42 GLU 42 0.0000

GLU 42 ARG 43 0.0385

ARG 43 ARG 43 0.0002

ARG 43 CYS 44 0.0001

CYS 44 CYS 44 0.0002

CYS 44 PHE 45 -0.0356

PHE 45 PHE 45 0.0002

PHE 45 GLN 46 0.0004

GLN 46 GLN 46 -0.0008

GLN 46 GLY 47 0.0890

GLY 47 GLY 47 -0.0002

GLY 47 THR 48 -0.0001

THR 48 THR 48 0.0004

THR 48 ALA 49 -0.0156

ALA 49 ALA 49 -0.0002

ALA 49 ASP 50 0.0000

ASP 50 ASP 50 -0.0000

ASP 50 PRO 51 0.0174

PRO 51 PRO 51 -0.0003

PRO 51 VAL 52 -0.0001

VAL 52 VAL 52 0.0003

VAL 52 ARG 53 0.0413

ARG 53 ARG 53 0.0002

ARG 53 VAL 54 -0.0002

VAL 54 VAL 54 -0.0001

VAL 54 SER 55 -0.0368

SER 55 SER 55 -0.0003

SER 55 LYS 56 -0.0000

LYS 56 LYS 56 -0.0001

LYS 56 VAL 57 0.0077

VAL 57 VAL 57 0.0004

VAL 57 VAL 58 0.0005

VAL 58 VAL 58 -0.0002

VAL 58 LYS 59 0.0357

LYS 59 LYS 59 -0.0001

LYS 59 GLY 60 -0.0003

GLY 60 GLY 60 -0.0001

GLY 60 GLY 61 0.0043

GLY 61 GLY 61 -0.0001

GLY 61 SER 62 0.0001

SER 62 SER 62 -0.0002

SER 62 SER 63 -0.0222

SER 63 SER 63 0.0001

SER 63 GLY 64 -0.0000

GLY 64 GLY 64 0.0004

GLY 64 LYS 65 0.0394

LYS 65 LYS 65 -0.0004

LYS 65 GLY 66 -0.0003

GLY 66 GLY 66 0.0005

GLY 66 THR 67 -0.0228

THR 67 THR 67 -0.0004

THR 67 THR 68 -0.0000

THR 68 THR 68 -0.0003

THR 68 LEU 69 0.0064

LEU 69 LEU 69 -0.0002

LEU 69 ARG 70 0.0001

ARG 70 ARG 70 -0.0002

ARG 70 GLY 71 0.1144

GLY 71 GLY 71 0.0002

GLY 71 ARG 72 -0.0005

ARG 72 ARG 72 0.0003

ARG 72 SER 73 0.1153

SER 73 SER 73 -0.0001

SER 73 ASP 74 -0.0002

ASP 74 ASP 74 -0.0000

ASP 74 ALA 75 0.1134

ALA 75 ALA 75 0.0003

ALA 75 ASP 76 0.0006

ASP 76 ASP 76 -0.0001

ASP 76 LEU 77 0.0291

LEU 77 LEU 77 -0.0002

LEU 77 VAL 78 -0.0000

VAL 78 VAL 78 -0.0004

VAL 78 VAL 79 -0.0126

VAL 79 VAL 79 0.0002

VAL 79 PHE 80 -0.0003

PHE 80 PHE 80 0.0001

PHE 80 LEU 81 0.0179

LEU 81 LEU 81 -0.0001

LEU 81 THR 82 -0.0000

THR 82 THR 82 -0.0006

THR 82 LYS 83 0.0694

LYS 83 LYS 83 0.0001

LYS 83 LEU 84 0.0001

LEU 84 LEU 84 0.0003

LEU 84 THR 85 0.0095

THR 85 THR 85 0.0001

THR 85 SER 86 0.0004

SER 86 SER 86 -0.0005

SER 86 PHE 87 -0.0444

PHE 87 PHE 87 -0.0002

PHE 87 GLU 88 -0.0001

GLU 88 GLU 88 0.0001

GLU 88 ASP 89 -0.0361

ASP 89 ASP 89 -0.0003

ASP 89 GLN 90 -0.0001

GLN 90 GLN 90 -0.0001

GLN 90 LEU 91 0.0035

LEU 91 LEU 91 0.0000

LEU 91 ARG 92 -0.0002

ARG 92 ARG 92 0.0001

ARG 92 ARG 93 0.0385

ARG 93 ARG 93 0.0002

ARG 93 ARG 94 -0.0005

ARG 94 ARG 94 -0.0003

ARG 94 GLY 95 0.0981

GLY 95 GLY 95 -0.0004

GLY 95 GLU 96 -0.0001

GLU 96 GLU 96 0.0001

GLU 96 PHE 97 0.0165

PHE 97 PHE 97 -0.0004

PHE 97 ILE 98 -0.0001

ILE 98 ILE 98 0.0002

ILE 98 GLN 99 -0.0194

GLN 99 GLN 99 0.0005

GLN 99 GLU 100 -0.0005

GLU 100 GLU 100 -0.0002

GLU 100 ILE 101 -0.0126

ILE 101 ILE 101 0.0007

ILE 101 ARG 102 0.0003

ARG 102 ARG 102 0.0003

ARG 102 ARG 103 0.0942

ARG 103 ARG 103 0.0001

ARG 103 GLN 104 0.0004

GLN 104 GLN 104 0.0002

GLN 104 LEU 105 -0.0085

LEU 105 LEU 105 0.0001

LEU 105 GLU 106 0.0004

GLU 106 GLU 106 0.0002

GLU 106 ALA 107 0.0492

ALA 107 ALA 107 -0.0000

ALA 107 CYS 108 0.0006

CYS 108 CYS 108 -0.0000

CYS 108 GLN 109 -0.0009

GLN 109 GLN 109 -0.0001

GLN 109 ARG 110 -0.0003

ARG 110 ARG 110 0.0003

ARG 110 GLU 111 0.0062

GLU 111 GLU 111 -0.0001

GLU 111 GLN 112 0.0003

GLN 112 GLN 112 0.0006

GLN 112 LYS 113 -0.0266

LYS 113 LYS 113 0.0009

LYS 113 PHE 114 -0.0004

PHE 114 PHE 114 0.0009

PHE 114 LYS 115 -0.0106

LYS 115 LYS 115 -0.0002

LYS 115 VAL 116 0.0004

VAL 116 VAL 116 -0.0005

VAL 116 THR 117 0.0303

THR 117 THR 117 -0.0002

THR 117 PHE 118 -0.0002

PHE 118 PHE 118 -0.0007

PHE 118 GLU 119 0.1580

GLU 119 GLU 119 -0.0003

GLU 119 VAL 120 -0.0001

VAL 120 VAL 120 -0.0001

VAL 120 GLN 121 0.6459

GLN 121 GLN 121 0.0001

GLN 121 SER 122 -0.0001

SER 122 SER 122 -0.0001

SER 122 PRO 123 -0.1196

PRO 123 PRO 123 -0.0002

PRO 123 ARG 124 -0.0000

ARG 124 ARG 124 0.0000

ARG 124 ARG 125 -0.1054

ARG 125 ARG 125 0.0001

ARG 125 GLU 126 0.0000

GLU 126 GLU 126 0.0002

GLU 126 ASN 127 0.0995

ASN 127 ASN 127 0.0003

ASN 127 PRO 128 -0.0003

PRO 128 PRO 128 -0.0001

PRO 128 ARG 129 0.3802

ARG 129 ARG 129 0.0006

ARG 129 ALA 130 -0.0005

ALA 130 ALA 130 0.0001

ALA 130 LEU 131 -0.0792

LEU 131 LEU 131 0.0001

LEU 131 SER 132 0.0001

SER 132 SER 132 0.0003

SER 132 PHE 133 0.0386

PHE 133 PHE 133 0.0002

PHE 133 VAL 134 -0.0001

VAL 134 VAL 134 -0.0004

VAL 134 LEU 135 -0.0661

LEU 135 LEU 135 -0.0000

LEU 135 SER 136 -0.0001

SER 136 SER 136 -0.0007

SER 136 SER 137 -0.0109

SER 137 SER 137 0.0003

SER 137 PRO 138 0.0002

PRO 138 PRO 138 0.0005

PRO 138 GLN 139 -0.0335

GLN 139 GLN 139 0.0004

GLN 139 LEU 140 0.0005

LEU 140 LEU 140 -0.0003

LEU 140 GLN 141 0.0460

GLN 141 GLN 141 0.0001

GLN 141 GLN 142 -0.0001

GLN 142 GLN 142 0.0001

GLN 142 GLU 143 -0.0650

GLU 143 GLU 143 -0.0001

GLU 143 VAL 144 -0.0005

VAL 144 VAL 144 0.0004

VAL 144 GLU 145 -0.0187

GLU 145 GLU 145 -0.0004

GLU 145 PHE 146 -0.0001

PHE 146 PHE 146 0.0002

PHE 146 ASP 147 0.0434

ASP 147 ASP 147 -0.0000

ASP 147 VAL 148 0.0004

VAL 148 VAL 148 -0.0001

VAL 148 LEU 149 -0.0047

LEU 149 LEU 149 -0.0002

LEU 149 PRO 150 0.0004

PRO 150 PRO 150 0.0001

PRO 150 ALA 151 0.0006

ALA 151 ALA 151 0.0000

ALA 151 PHE 152 0.0001

PHE 152 PHE 152 -0.0001

PHE 152 ASP 153 0.0352

ASP 153 ASP 153 0.0001

ASP 153 ALA 154 0.0002

ALA 154 ALA 154 -0.0005

ALA 154 LEU 155 0.0849

LEU 155 LEU 155 0.0005

LEU 155 GLY 156 0.0001

GLY 156 GLY 156 0.0004

GLY 156 GLN 157 0.0481

GLN 157 GLN 157 0.0001

GLN 157 TRP 158 -0.0000

TRP 158 TRP 158 -0.0004

TRP 158 THR 159 -0.0085

THR 159 THR 159 -0.0007

THR 159 PRO 160 0.0002

PRO 160 PRO 160 -0.0006

PRO 160 GLY 161 0.1140

GLY 161 GLY 161 0.0004

GLY 161 TYR 162 -0.0002

TYR 162 TYR 162 -0.0002

TYR 162 LYS 163 0.0983

LYS 163 LYS 163 -0.0002

LYS 163 PRO 164 -0.0007

PRO 164 PRO 164 -0.0006

PRO 164 ASN 165 -0.0611

ASN 165 ASN 165 0.0001

ASN 165 PRO 166 -0.0001

PRO 166 PRO 166 0.0006

PRO 166 GLU 167 -0.0001

GLU 167 GLU 167 0.0003

GLU 167 ILE 168 -0.0005

ILE 168 ILE 168 0.0005

ILE 168 TYR 169 -0.0171

TYR 169 TYR 169 0.0003

TYR 169 VAL 170 0.0002

VAL 170 VAL 170 0.0003

VAL 170 GLN 171 -0.0254

GLN 171 GLN 171 0.0001

GLN 171 LEU 172 -0.0004

LEU 172 LEU 172 -0.0001

LEU 172 ILE 173 -0.0551

ILE 173 ILE 173 -0.0002

ILE 173 LYS 174 -0.0000

LYS 174 LYS 174 0.0000

LYS 174 GLU 175 -0.0352

GLU 175 GLU 175 0.0001

GLU 175 CYS 176 -0.0002

CYS 176 CYS 176 -0.0004

CYS 176 LYS 177 0.0044

LYS 177 LYS 177 -0.0001

LYS 177 SER 178 0.0003

SER 178 SER 178 -0.0001

SER 178 ARG 179 -0.0306

ARG 179 ARG 179 -0.0004

ARG 179 GLY 180 0.0001

GLY 180 GLY 180 0.0001

GLY 180 LYS 181 0.0609

LYS 181 LYS 181 -0.0004

LYS 181 GLU 182 -0.0000

GLU 182 GLU 182 -0.0003

GLU 182 GLY 183 0.1170

GLY 183 GLY 183 -0.0000

GLY 183 GLU 184 0.0004

GLU 184 GLU 184 -0.0002

GLU 184 PHE 185 -0.0379

PHE 185 PHE 185 0.0000

PHE 185 SER 186 -0.0005

SER 186 SER 186 0.0000

SER 186 THR 187 -0.1486

THR 187 THR 187 0.0001

THR 187 CYS 188 -0.0002

CYS 188 CYS 188 0.0001

CYS 188 PHE 189 -0.0177

PHE 189 PHE 189 -0.0001

PHE 189 THR 190 0.0003

THR 190 THR 190 -0.0002

THR 190 GLU 191 -0.0348

GLU 191 GLU 191 0.0000

GLU 191 LEU 192 -0.0002

LEU 192 LEU 192 0.0001

LEU 192 GLN 193 0.0192

GLN 193 GLN 193 -0.0002

GLN 193 ARG 194 -0.0002

ARG 194 ARG 194 -0.0757

ARG 194 ARG 194 -0.0001

ARG 194 ASP 195 0.0116

ASP 195 ASP 195 0.0000

ASP 195 PHE 196 0.0003

PHE 196 PHE 196 0.0003

PHE 196 LEU 197 0.1329

LEU 197 LEU 197 0.0006

LEU 197 ARG 198 0.0001

ARG 198 ARG 198 -0.0007

ARG 198 ASN 199 -0.1092

ASN 199 ASN 199 0.0004

ASN 199 ARG 200 0.0002

ARG 200 ARG 200 -0.0003

ARG 200 PRO 201 -0.0307

PRO 201 PRO 201 -0.0007

PRO 201 THR 202 0.0001

THR 202 THR 202 0.0004

THR 202 LYS 203 -0.0055

LYS 203 LYS 203 0.0001

LYS 203 LEU 204 -0.0004

LEU 204 LEU 204 0.0003

LEU 204 LYS 205 -0.0046

LYS 205 LYS 205 0.0001

LYS 205 SER 206 -0.0002

SER 206 SER 206 -0.0002

SER 206 LEU 207 0.0319

LEU 207 LEU 207 -0.0006

LEU 207 ILE 208 -0.0003

ILE 208 ILE 208 -0.0001

ILE 208 ARG 209 -0.0138

ARG 209 ARG 209 -0.0002

ARG 209 LEU 210 -0.0003

LEU 210 LEU 210 0.0004

LEU 210 VAL 211 -0.0832

VAL 211 VAL 211 -0.0001

VAL 211 LYS 212 0.0002

LYS 212 LYS 212 -0.0003

LYS 212 HIS 213 0.0398

HIS 213 HIS 213 -0.0004

HIS 213 TRP 214 -0.0004

TRP 214 TRP 214 0.0001

TRP 214 TYR 215 -0.0030

TYR 215 TYR 215 -0.0003

TYR 215 GLN 216 -0.0002

GLN 216 GLN 216 0.0003

GLN 216 THR 217 0.1131

THR 217 THR 217 0.0003

THR 217 CYS 218 0.0004

CYS 218 CYS 218 0.0001

CYS 218 LYS 219 0.0130

LYS 219 LYS 219 -0.0004

LYS 219 LYS 220 -0.0001

LYS 220 LYS 220 0.0003

LYS 220 THR 221 0.0289

THR 221 THR 221 0.0006

THR 221 HIS 222 -0.0003

HIS 222 HIS 222 0.0004

HIS 222 GLY 223 -0.0228

GLY 223 GLY 223 -0.0004

GLY 223 ASN 224 0.0003

ASN 224 ASN 224 0.0004

ASN 224 LYS 225 0.0085

LYS 225 LYS 225 0.0000

LYS 225 LEU 226 0.0000

LEU 226 LEU 226 0.0002

LEU 226 PRO 227 0.1063

PRO 227 PRO 227 -0.0002

PRO 227 PRO 228 -0.0000

PRO 228 PRO 228 -0.0003

PRO 228 GLN 229 -0.0970

GLN 229 GLN 229 0.0007

GLN 229 TYR 230 0.0002

TYR 230 TYR 230 0.0001

TYR 230 ALA 231 -0.0269

ALA 231 ALA 231 0.0002

ALA 231 LEU 232 0.0006

LEU 232 LEU 232 -0.0000

LEU 232 GLU 233 0.0340

GLU 233 GLU 233 0.0002

GLU 233 LEU 234 0.0006

LEU 234 LEU 234 -0.0002

LEU 234 LEU 235 -0.0537

LEU 235 LEU 235 0.0004

LEU 235 THR 236 0.0001

THR 236 THR 236 -0.0001

THR 236 VAL 237 -0.0092

VAL 237 VAL 237 0.0005

VAL 237 TYR 238 0.0002

TYR 238 TYR 238 0.0006

TYR 238 ALA 239 -0.1238

ALA 239 ALA 239 -0.0001

ALA 239 TRP 240 -0.0002

TRP 240 TRP 240 -0.0003

TRP 240 GLU 241 0.0077

GLU 241 GLU 241 0.0001

GLU 241 GLN 242 0.0003

GLN 242 GLN 242 -0.0003

GLN 242 GLY 243 -0.0117

GLY 243 GLY 243 -0.0009

GLY 243 SER 244 0.0004

SER 244 SER 244 -0.0004

SER 244 ARG 245 -0.0033

ARG 245 ARG 245 -0.0000

ARG 245 LYS 246 0.0004

LYS 246 LYS 246 0.0004

LYS 246 THR 247 0.1844

THR 247 THR 247 0.0001

THR 247 ASP 248 -0.0000

ASP 248 ASP 248 -0.0004

ASP 248 PHE 249 0.0134

PHE 249 PHE 249 0.0003

PHE 249 SER 250 -0.0004

SER 250 SER 250 -0.0001

SER 250 THR 251 0.0228

THR 251 THR 251 -0.0001

THR 251 ALA 252 -0.0001

ALA 252 ALA 252 0.0002

ALA 252 GLN 253 -0.0378

GLN 253 GLN 253 0.0005

GLN 253 GLY 254 -0.0003

GLY 254 GLY 254 0.0003

GLY 254 PHE 255 -0.0129

PHE 255 PHE 255 0.0003

PHE 255 GLN 256 0.0002

GLN 256 GLN 256 -0.0002

GLN 256 THR 257 -0.0547

THR 257 THR 257 -0.0003

THR 257 VAL 258 -0.0002

VAL 258 VAL 258 0.0001

VAL 258 LEU 259 0.0252

LEU 259 LEU 259 -0.0002

LEU 259 GLU 260 0.0003

GLU 260 GLU 260 -0.0006

GLU 260 LEU 261 -0.0562

LEU 261 LEU 261 0.0004

LEU 261 VAL 262 -0.0001

VAL 262 VAL 262 0.0004

VAL 262 LEU 263 0.0275

LEU 263 LEU 263 0.0004

LEU 263 LYS 264 0.0002

LYS 264 LYS 264 -0.0003

LYS 264 HIS 265 0.0296

HIS 265 HIS 265 -0.0001

HIS 265 GLN 266 0.0001

GLN 266 GLN 266 0.0002

GLN 266 LYS 267 0.0594

LYS 267 LYS 267 0.0002

LYS 267 LEU 268 0.0000

LEU 268 LEU 268 -0.0002

LEU 268 CYS 269 -0.0442

CYS 269 CYS 269 0.0001

CYS 269 ILE 270 -0.0004

ILE 270 ILE 270 -0.0000

ILE 270 PHE 271 -0.0017

PHE 271 PHE 271 -0.0001

PHE 271 TRP 272 -0.0001

TRP 272 TRP 272 -0.0004

TRP 272 GLU 273 0.0427

GLU 273 GLU 273 -0.0004

GLU 273 ALA 274 -0.0003

ALA 274 ALA 274 0.0002

ALA 274 TYR 275 0.0066

TYR 275 TYR 275 0.0002

TYR 275 TYR 276 0.0003

TYR 276 TYR 276 -0.0005

TYR 276 ASP 277 0.0593

ASP 277 ASP 277 0.0000

ASP 277 PHE 278 -0.0003

PHE 278 PHE 278 -0.0000

PHE 278 THR 279 -0.0324

THR 279 THR 279 0.0001

THR 279 ASN 280 -0.0000

ASN 280 ASN 280 0.0006

ASN 280 PRO 281 0.0152

PRO 281 PRO 281 -0.0000

PRO 281 VAL 282 -0.0004

VAL 282 VAL 282 0.0001

VAL 282 VAL 283 0.0290

VAL 283 VAL 283 0.0005

VAL 283 GLY 284 -0.0002

GLY 284 GLY 284 0.0006

GLY 284 ARG 285 -0.0019

ARG 285 ARG 285 0.0002

ARG 285 CYS 286 -0.0005

CYS 286 CYS 286 -0.0002

CYS 286 MET 287 -0.0226

MET 287 MET 287 -0.0005

MET 287 LEU 288 0.0001

LEU 288 LEU 288 0.0000

LEU 288 GLN 289 0.0095

GLN 289 GLN 289 -0.0005

GLN 289 GLN 290 -0.0001

GLN 290 GLN 290 -0.0004

GLN 290 LEU 291 -0.0740

LEU 291 LEU 291 -0.0001

LEU 291 LYS 292 0.0003

LYS 292 LYS 292 -0.0001

LYS 292 LYS 293 -0.0144

LYS 293 LYS 293 0.0001

LYS 293 PRO 294 0.0001

PRO 294 PRO 294 0.0003

PRO 294 ARG 295 -0.0473

ARG 295 ARG 295 0.0001

ARG 295 PRO 296 0.0001

PRO 296 PRO 296 -0.0001

PRO 296 VAL 297 -0.0129

VAL 297 VAL 297 -0.0005

VAL 297 ILE 298 0.0004

ILE 298 ILE 298 -0.0002

ILE 298 LEU 299 0.0076

LEU 299 LEU 299 0.0003

LEU 299 ASP 300 -0.0005

ASP 300 ASP 300 -0.0001

ASP 300 PRO 301 0.0393

PRO 301 PRO 301 0.0005

PRO 301 ALA 302 -0.0001

ALA 302 ALA 302 -0.0005

ALA 302 ASP 303 0.0312

ASP 303 ASP 303 -0.0000

ASP 303 PRO 304 0.0003

PRO 304 PRO 304 0.0001

PRO 304 THR 305 -0.0495

THR 305 THR 305 -0.0003

THR 305 GLY 306 -0.0003

GLY 306 GLY 306 -0.0005

GLY 306 ASN 307 0.0193

ASN 307 ASN 307 -0.0007

ASN 307 VAL 308 -0.0001

VAL 308 VAL 308 -0.0001

VAL 308 GLY 309 -0.0033

GLY 309 GLY 309 -0.0002

GLY 309 GLY 310 0.0005

GLY 310 GLY 310 0.0003

GLY 310 GLY 311 -0.0348

GLY 311 GLY 311 -0.0001

GLY 311 ASP 312 -0.0002

ASP 312 ASP 312 -0.0005

ASP 312 THR 313 0.0093

THR 313 THR 313 0.0006

THR 313 HIS 314 0.0001

HIS 314 HIS 314 -0.0001

HIS 314 SER 315 -0.0064

SER 315 SER 315 0.0009

SER 315 TRP 316 -0.0004

TRP 316 TRP 316 0.0006

TRP 316 GLN 317 0.0230

GLN 317 GLN 317 0.0006

GLN 317 ARG 318 0.0004

ARG 318 ARG 318 0.0002

ARG 318 LEU 319 0.0322

LEU 319 LEU 319 -0.0007

LEU 319 ALA 320 0.0003

ALA 320 ALA 320 0.0003

ALA 320 GLN 321 0.0035

GLN 321 GLN 321 -0.0002

GLN 321 GLU 322 -0.0003

GLU 322 GLU 322 -0.0001

GLU 322 ALA 323 0.0013

ALA 323 ALA 323 -0.0000

ALA 323 ARG 324 -0.0003

ARG 324 ARG 324 0.0000

ARG 324 VAL 325 -0.0617

VAL 325 VAL 325 -0.0001

VAL 325 TRP 326 0.0000

TRP 326 TRP 326 -0.0003

TRP 326 LEU 327 0.0161

LEU 327 LEU 327 -0.0004

LEU 327 GLY 328 -0.0003

GLY 328 GLY 328 0.0001

GLY 328 TYR 329 0.0117

TYR 329 TYR 329 -0.0002

TYR 329 PRO 330 0.0001

PRO 330 PRO 330 0.0002

PRO 330 CYS 331 0.0233

CYS 331 CYS 331 -0.0002

CYS 331 CYS 332 0.0004

CYS 332 CYS 332 0.0001

CYS 332 LYS 333 -0.0445

LYS 333 LYS 333 0.0006

LYS 333 ASN 334 -0.0001

ASN 334 ASN 334 0.0002

ASN 334 LEU 335 0.0467

LEU 335 LEU 335 0.0003

LEU 335 ASP 336 -0.0005

ASP 336 ASP 336 0.0004

ASP 336 GLY 337 0.0832

GLY 337 GLY 337 0.0001

GLY 337 SER 338 -0.0001

SER 338 SER 338 0.0004

SER 338 LEU 339 -0.0405

LEU 339 LEU 339 0.0002

LEU 339 VAL 340 -0.0001

VAL 340 VAL 340 0.0005

VAL 340 GLY 341 -0.1085

GLY 341 GLY 341 -0.0004

GLY 341 ALA 342 -0.0003

ALA 342 ALA 342 -0.0001

ALA 342 TRP 343 -0.1358

TRP 343 TRP 343 0.0004

TRP 343 THR 344 -0.0000

THR 344 THR 344 -0.0001

THR 344 MET 345 0.0102

MET 345 MET 345 0.0002

MET 345 LEU 346 0.0002

LEU 346 LEU 346 -0.0004

LEU 346 GLN 347 0.0085

GLN 347 GLN 347 0.0006

GLN 347 LYS 348 0.0000

LYS 348 LYS 348 -0.0003

LYS 348 ILE 349 0.1332

ILE 349 ILE 349 0.0004

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: October 18th, 2018.

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

*** ***

CA strain for 221128151102134046

--- normal mode 10 ---

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

* *