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

* *

CA strain for 221128151102134046

--- 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
MET 1 MET 1 -0.0002

MET 1 GLU 2 0.0001

GLU 2 GLU 2 -0.0001

GLU 2 LEU 3 -0.0279

LEU 3 LEU 3 0.0003

LEU 3 ARG 4 0.0002

ARG 4 ARG 4 -0.0002

ARG 4 HIS 5 0.0267

HIS 5 HIS 5 -0.0001

HIS 5 THR 6 0.0001

THR 6 THR 6 -0.0006

THR 6 PRO 7 -0.0008

PRO 7 PRO 7 -0.0004

PRO 7 ALA 8 -0.0001

ALA 8 ALA 8 0.0002

ALA 8 ARG 9 0.0116

ARG 9 ARG 9 0.0003

ARG 9 ASP 10 -0.0003

ASP 10 ASP 10 -0.0004

ASP 10 LEU 11 0.0097

LEU 11 LEU 11 0.0002

LEU 11 ASP 12 0.0001

ASP 12 ASP 12 -0.0004

ASP 12 LYS 13 -0.0726

LYS 13 LYS 13 0.0002

LYS 13 PHE 14 0.0003

PHE 14 PHE 14 0.0005

PHE 14 ILE 15 -0.0454

ILE 15 ILE 15 -0.0004

ILE 15 GLU 16 0.0001

GLU 16 GLU 16 0.0003

GLU 16 ASP 17 0.0414

ASP 17 ASP 17 -0.0003

ASP 17 HIS 18 0.0001

HIS 18 HIS 18 -0.0006

HIS 18 LEU 19 0.0099

LEU 19 LEU 19 0.0001

LEU 19 LEU 20 -0.0008

LEU 20 LEU 20 0.0005

LEU 20 PRO 21 0.0032

PRO 21 PRO 21 -0.0003

PRO 21 ASN 22 0.0001

ASN 22 ASN 22 0.0003

ASN 22 THR 23 0.0456

THR 23 THR 23 0.0000

THR 23 CYS 24 0.0003

CYS 24 CYS 24 -0.0000

CYS 24 PHE 25 0.0193

PHE 25 PHE 25 -0.0003

PHE 25 ARG 26 0.0003

ARG 26 ARG 26 -0.0003

ARG 26 THR 27 0.1722

THR 27 THR 27 0.0003

THR 27 GLN 28 0.0001

GLN 28 GLN 28 0.0000

GLN 28 VAL 29 0.0056

VAL 29 VAL 29 0.0000

VAL 29 LYS 30 0.0003

LYS 30 LYS 30 -0.0002

LYS 30 GLU 31 -0.0271

GLU 31 GLU 31 -0.0003

GLU 31 ALA 32 0.0003

ALA 32 ALA 32 0.0000

ALA 32 ILE 33 -0.0129

ILE 33 ILE 33 0.0001

ILE 33 ASP 34 0.0004

ASP 34 ASP 34 -0.0002

ASP 34 ILE 35 0.0683

ILE 35 ILE 35 -0.0004

ILE 35 VAL 36 -0.0003

VAL 36 VAL 36 0.0001

VAL 36 CYS 37 -0.0306

CYS 37 CYS 37 -0.0002

CYS 37 ARG 38 -0.0000

ARG 38 ARG 38 0.0002

ARG 38 PHE 39 0.0567

PHE 39 PHE 39 0.0004

PHE 39 LEU 40 -0.0003

LEU 40 LEU 40 0.0003

LEU 40 LYS 41 -0.0135

LYS 41 LYS 41 -0.0006

LYS 41 GLU 42 -0.0003

GLU 42 GLU 42 0.0008

GLU 42 ARG 43 0.1218

ARG 43 ARG 43 0.0003

ARG 43 CYS 44 -0.0001

CYS 44 CYS 44 -0.0000

CYS 44 PHE 45 -0.0418

PHE 45 PHE 45 -0.0003

PHE 45 GLN 46 0.0000

GLN 46 GLN 46 -0.0000

GLN 46 GLY 47 0.0190

GLY 47 GLY 47 0.0002

GLY 47 THR 48 -0.0003

THR 48 THR 48 -0.0003

THR 48 ALA 49 -0.0239

ALA 49 ALA 49 0.0002

ALA 49 ASP 50 0.0000

ASP 50 ASP 50 0.0001

ASP 50 PRO 51 -0.0072

PRO 51 PRO 51 0.0000

PRO 51 VAL 52 -0.0001

VAL 52 VAL 52 0.0001

VAL 52 ARG 53 -0.0088

ARG 53 ARG 53 -0.0004

ARG 53 VAL 54 -0.0003

VAL 54 VAL 54 0.0005

VAL 54 SER 55 0.0390

SER 55 SER 55 -0.0003

SER 55 LYS 56 -0.0002

LYS 56 LYS 56 0.0005

LYS 56 VAL 57 0.0138

VAL 57 VAL 57 0.0001

VAL 57 VAL 58 0.0003

VAL 58 VAL 58 -0.0006

VAL 58 LYS 59 0.0180

LYS 59 LYS 59 -0.0001

LYS 59 GLY 60 -0.0000

GLY 60 GLY 60 -0.0001

GLY 60 GLY 61 0.1432

GLY 61 GLY 61 -0.0002

GLY 61 SER 62 0.0004

SER 62 SER 62 -0.0000

SER 62 SER 63 0.0903

SER 63 SER 63 -0.0000

SER 63 GLY 64 -0.0001

GLY 64 GLY 64 -0.0001

GLY 64 LYS 65 0.0234

LYS 65 LYS 65 0.0003

LYS 65 GLY 66 0.0000

GLY 66 GLY 66 -0.0001

GLY 66 THR 67 0.0403

THR 67 THR 67 -0.0005

THR 67 THR 68 0.0005

THR 68 THR 68 -0.0005

THR 68 LEU 69 -0.0203

LEU 69 LEU 69 -0.0007

LEU 69 ARG 70 0.0002

ARG 70 ARG 70 0.0003

ARG 70 GLY 71 -0.0888

GLY 71 GLY 71 -0.0002

GLY 71 ARG 72 -0.0001

ARG 72 ARG 72 -0.0001

ARG 72 SER 73 0.0717

SER 73 SER 73 0.0008

SER 73 ASP 74 0.0001

ASP 74 ASP 74 0.0002

ASP 74 ALA 75 0.0914

ALA 75 ALA 75 0.0001

ALA 75 ASP 76 0.0003

ASP 76 ASP 76 -0.0003

ASP 76 LEU 77 0.0340

LEU 77 LEU 77 -0.0006

LEU 77 VAL 78 -0.0003

VAL 78 VAL 78 -0.0001

VAL 78 VAL 79 0.0160

VAL 79 VAL 79 -0.0005

VAL 79 PHE 80 0.0004

PHE 80 PHE 80 -0.0000

PHE 80 LEU 81 0.0022

LEU 81 LEU 81 0.0002

LEU 81 THR 82 0.0001

THR 82 THR 82 0.0001

THR 82 LYS 83 -0.0206

LYS 83 LYS 83 -0.0002

LYS 83 LEU 84 -0.0004

LEU 84 LEU 84 -0.0001

LEU 84 THR 85 -0.0227

THR 85 THR 85 -0.0005

THR 85 SER 86 -0.0005

SER 86 SER 86 0.0002

SER 86 PHE 87 0.0283

PHE 87 PHE 87 -0.0001

PHE 87 GLU 88 -0.0002

GLU 88 GLU 88 0.0005

GLU 88 ASP 89 -0.0369

ASP 89 ASP 89 -0.0001

ASP 89 GLN 90 0.0003

GLN 90 GLN 90 0.0004

GLN 90 LEU 91 -0.0122

LEU 91 LEU 91 0.0006

LEU 91 ARG 92 0.0003

ARG 92 ARG 92 -0.0002

ARG 92 ARG 93 0.0393

ARG 93 ARG 93 0.0002

ARG 93 ARG 94 -0.0002

ARG 94 ARG 94 0.0001

ARG 94 GLY 95 -0.0054

GLY 95 GLY 95 -0.0003

GLY 95 GLU 96 -0.0006

GLU 96 GLU 96 -0.0002

GLU 96 PHE 97 -0.0209

PHE 97 PHE 97 -0.0001

PHE 97 ILE 98 -0.0002

ILE 98 ILE 98 -0.0005

ILE 98 GLN 99 -0.0574

GLN 99 GLN 99 -0.0002

GLN 99 GLU 100 -0.0000

GLU 100 GLU 100 -0.0000

GLU 100 ILE 101 -0.0572

ILE 101 ILE 101 -0.0001

ILE 101 ARG 102 0.0003

ARG 102 ARG 102 0.0002

ARG 102 ARG 103 0.0628

ARG 103 ARG 103 -0.0004

ARG 103 GLN 104 0.0000

GLN 104 GLN 104 -0.0001

GLN 104 LEU 105 -0.0403

LEU 105 LEU 105 -0.0003

LEU 105 GLU 106 0.0004

GLU 106 GLU 106 -0.0002

GLU 106 ALA 107 0.0265

ALA 107 ALA 107 -0.0002

ALA 107 CYS 108 0.0001

CYS 108 CYS 108 0.0002

CYS 108 GLN 109 -0.0167

GLN 109 GLN 109 -0.0003

GLN 109 ARG 110 0.0002

ARG 110 ARG 110 -0.0002

ARG 110 GLU 111 -0.0118

GLU 111 GLU 111 0.0002

GLU 111 GLN 112 -0.0000

GLN 112 GLN 112 0.0002

GLN 112 LYS 113 0.0012

LYS 113 LYS 113 0.0004

LYS 113 PHE 114 0.0003

PHE 114 PHE 114 0.0001

PHE 114 LYS 115 -0.0430

LYS 115 LYS 115 0.0000

LYS 115 VAL 116 0.0001

VAL 116 VAL 116 -0.0000

VAL 116 THR 117 0.0123

THR 117 THR 117 0.0006

THR 117 PHE 118 -0.0003

PHE 118 PHE 118 -0.0004

PHE 118 GLU 119 0.1812

GLU 119 GLU 119 -0.0001

GLU 119 VAL 120 -0.0004

VAL 120 VAL 120 -0.0001

VAL 120 GLN 121 0.6044

GLN 121 GLN 121 -0.0001

GLN 121 SER 122 -0.0001

SER 122 SER 122 0.0001

SER 122 PRO 123 -0.1036

PRO 123 PRO 123 -0.0001

PRO 123 ARG 124 -0.0001

ARG 124 ARG 124 -0.0003

ARG 124 ARG 125 -0.0743

ARG 125 ARG 125 -0.0004

ARG 125 GLU 126 -0.0001

GLU 126 GLU 126 -0.0001

GLU 126 ASN 127 0.0899

ASN 127 ASN 127 0.0002

ASN 127 PRO 128 -0.0002

PRO 128 PRO 128 -0.0004

PRO 128 ARG 129 0.3628

ARG 129 ARG 129 0.0001

ARG 129 ALA 130 0.0003

ALA 130 ALA 130 0.0003

ALA 130 LEU 131 0.1193

LEU 131 LEU 131 0.0001

LEU 131 SER 132 0.0002

SER 132 SER 132 -0.0004

SER 132 PHE 133 0.0770

PHE 133 PHE 133 -0.0001

PHE 133 VAL 134 -0.0004

VAL 134 VAL 134 -0.0001

VAL 134 LEU 135 -0.0153

LEU 135 LEU 135 -0.0006

LEU 135 SER 136 0.0001

SER 136 SER 136 -0.0006

SER 136 SER 137 -0.0092

SER 137 SER 137 0.0001

SER 137 PRO 138 0.0003

PRO 138 PRO 138 -0.0005

PRO 138 GLN 139 -0.0086

GLN 139 GLN 139 0.0001

GLN 139 LEU 140 -0.0002

LEU 140 LEU 140 -0.0003

LEU 140 GLN 141 0.0240

GLN 141 GLN 141 -0.0003

GLN 141 GLN 142 0.0002

GLN 142 GLN 142 0.0000

GLN 142 GLU 143 -0.0333

GLU 143 GLU 143 -0.0001

GLU 143 VAL 144 0.0003

VAL 144 VAL 144 0.0005

VAL 144 GLU 145 -0.0212

GLU 145 GLU 145 0.0001

GLU 145 PHE 146 -0.0000

PHE 146 PHE 146 0.0001

PHE 146 ASP 147 0.0496

ASP 147 ASP 147 -0.0002

ASP 147 VAL 148 0.0007

VAL 148 VAL 148 -0.0008

VAL 148 LEU 149 0.0514

LEU 149 LEU 149 0.0001

LEU 149 PRO 150 -0.0003

PRO 150 PRO 150 -0.0004

PRO 150 ALA 151 -0.0059

ALA 151 ALA 151 -0.0001

ALA 151 PHE 152 0.0005

PHE 152 PHE 152 -0.0001

PHE 152 ASP 153 -0.0553

ASP 153 ASP 153 -0.0004

ASP 153 ALA 154 0.0001

ALA 154 ALA 154 -0.0001

ALA 154 LEU 155 -0.0998

LEU 155 LEU 155 0.0004

LEU 155 GLY 156 -0.0002

GLY 156 GLY 156 -0.0001

GLY 156 GLN 157 -0.0953

GLN 157 GLN 157 -0.0000

GLN 157 TRP 158 -0.0003

TRP 158 TRP 158 -0.0000

TRP 158 THR 159 0.0452

THR 159 THR 159 0.0001

THR 159 PRO 160 0.0000

PRO 160 PRO 160 -0.0002

PRO 160 GLY 161 -0.1024

GLY 161 GLY 161 -0.0002

GLY 161 TYR 162 0.0000

TYR 162 TYR 162 -0.0001

TYR 162 LYS 163 -0.0991

LYS 163 LYS 163 0.0002

LYS 163 PRO 164 -0.0004

PRO 164 PRO 164 -0.0005

PRO 164 ASN 165 0.0066

ASN 165 ASN 165 0.0001

ASN 165 PRO 166 0.0002

PRO 166 PRO 166 -0.0005

PRO 166 GLU 167 -0.0070

GLU 167 GLU 167 -0.0003

GLU 167 ILE 168 -0.0004

ILE 168 ILE 168 -0.0005

ILE 168 TYR 169 0.0253

TYR 169 TYR 169 0.0004

TYR 169 VAL 170 0.0001

VAL 170 VAL 170 -0.0004

VAL 170 GLN 171 0.0513

GLN 171 GLN 171 0.0002

GLN 171 LEU 172 -0.0002

LEU 172 LEU 172 0.0004

LEU 172 ILE 173 -0.0261

ILE 173 ILE 173 0.0003

ILE 173 LYS 174 -0.0001

LYS 174 LYS 174 0.0003

LYS 174 GLU 175 0.0086

GLU 175 GLU 175 -0.0002

GLU 175 CYS 176 -0.0000

CYS 176 CYS 176 0.0003

CYS 176 LYS 177 -0.0117

LYS 177 LYS 177 0.0003

LYS 177 SER 178 -0.0006

SER 178 SER 178 -0.0004

SER 178 ARG 179 0.0402

ARG 179 ARG 179 -0.0001

ARG 179 GLY 180 -0.0000

GLY 180 GLY 180 0.0002

GLY 180 LYS 181 -0.0099

LYS 181 LYS 181 -0.0000

LYS 181 GLU 182 -0.0005

GLU 182 GLU 182 -0.0002

GLU 182 GLY 183 -0.0170

GLY 183 GLY 183 0.0003

GLY 183 GLU 184 0.0006

GLU 184 GLU 184 -0.0001

GLU 184 PHE 185 -0.1459

PHE 185 PHE 185 0.0001

PHE 185 SER 186 0.0001

SER 186 SER 186 -0.0004

SER 186 THR 187 0.0337

THR 187 THR 187 0.0000

THR 187 CYS 188 0.0001

CYS 188 CYS 188 -0.0006

CYS 188 PHE 189 0.0640

PHE 189 PHE 189 -0.0000

PHE 189 THR 190 -0.0001

THR 190 THR 190 0.0003

THR 190 GLU 191 0.0699

GLU 191 GLU 191 0.0002

GLU 191 LEU 192 -0.0000

LEU 192 LEU 192 -0.0002

LEU 192 GLN 193 0.0118

GLN 193 GLN 193 0.0001

GLN 193 ARG 194 0.0004

ARG 194 ARG 194 0.1147

ARG 194 ARG 194 0.0002

ARG 194 ASP 195 0.0029

ASP 195 ASP 195 0.0000

ASP 195 PHE 196 -0.0001

PHE 196 PHE 196 0.0001

PHE 196 LEU 197 -0.1882

LEU 197 LEU 197 0.0006

LEU 197 ARG 198 -0.0002

ARG 198 ARG 198 -0.0005

ARG 198 ASN 199 0.1261

ASN 199 ASN 199 0.0001

ASN 199 ARG 200 0.0002

ARG 200 ARG 200 -0.0004

ARG 200 PRO 201 -0.0872

PRO 201 PRO 201 -0.0004

PRO 201 THR 202 -0.0005

THR 202 THR 202 0.0001

THR 202 LYS 203 0.0014

LYS 203 LYS 203 0.0005

LYS 203 LEU 204 -0.0006

LEU 204 LEU 204 -0.0004

LEU 204 LYS 205 0.0387

LYS 205 LYS 205 0.0001

LYS 205 SER 206 0.0002

SER 206 SER 206 0.0002

SER 206 LEU 207 0.0308

LEU 207 LEU 207 0.0004

LEU 207 ILE 208 -0.0001

ILE 208 ILE 208 -0.0000

ILE 208 ARG 209 0.0055

ARG 209 ARG 209 -0.0003

ARG 209 LEU 210 0.0004

LEU 210 LEU 210 0.0003

LEU 210 VAL 211 0.0876

VAL 211 VAL 211 -0.0002

VAL 211 LYS 212 -0.0003

LYS 212 LYS 212 0.0000

LYS 212 HIS 213 -0.0211

HIS 213 HIS 213 0.0002

HIS 213 TRP 214 -0.0004

TRP 214 TRP 214 0.0000

TRP 214 TYR 215 0.0120

TYR 215 TYR 215 0.0007

TYR 215 GLN 216 0.0001

GLN 216 GLN 216 0.0001

GLN 216 THR 217 -0.0176

THR 217 THR 217 0.0005

THR 217 CYS 218 0.0001

CYS 218 CYS 218 0.0000

CYS 218 LYS 219 -0.0670

LYS 219 LYS 219 0.0000

LYS 219 LYS 220 0.0006

LYS 220 LYS 220 -0.0004

LYS 220 THR 221 -0.0023

THR 221 THR 221 -0.0001

THR 221 HIS 222 0.0003

HIS 222 HIS 222 0.0004

HIS 222 GLY 223 -0.0559

GLY 223 GLY 223 -0.0001

GLY 223 ASN 224 0.0001

ASN 224 ASN 224 -0.0004

ASN 224 LYS 225 -0.0236

LYS 225 LYS 225 0.0000

LYS 225 LEU 226 -0.0002

LEU 226 LEU 226 0.0001

LEU 226 PRO 227 0.0532

PRO 227 PRO 227 0.0003

PRO 227 PRO 228 0.0004

PRO 228 PRO 228 0.0007

PRO 228 GLN 229 0.0213

GLN 229 GLN 229 0.0002

GLN 229 TYR 230 -0.0001

TYR 230 TYR 230 -0.0002

TYR 230 ALA 231 0.0708

ALA 231 ALA 231 0.0003

ALA 231 LEU 232 -0.0001

LEU 232 LEU 232 0.0003

LEU 232 GLU 233 0.0149

GLU 233 GLU 233 -0.0006

GLU 233 LEU 234 -0.0002

LEU 234 LEU 234 -0.0001

LEU 234 LEU 235 0.0277

LEU 235 LEU 235 -0.0002

LEU 235 THR 236 0.0003

THR 236 THR 236 -0.0007

THR 236 VAL 237 -0.0824

VAL 237 VAL 237 -0.0001

VAL 237 TYR 238 -0.0004

TYR 238 TYR 238 0.0004

TYR 238 ALA 239 0.0123

ALA 239 ALA 239 0.0007

ALA 239 TRP 240 -0.0001

TRP 240 TRP 240 -0.0006

TRP 240 GLU 241 -0.0336

GLU 241 GLU 241 0.0006

GLU 241 GLN 242 -0.0001

GLN 242 GLN 242 -0.0000

GLN 242 GLY 243 -0.0105

GLY 243 GLY 243 -0.0000

GLY 243 SER 244 0.0002

SER 244 SER 244 -0.0004

SER 244 ARG 245 -0.0393

ARG 245 ARG 245 -0.0001

ARG 245 LYS 246 -0.0004

LYS 246 LYS 246 0.0007

LYS 246 THR 247 -0.1613

THR 247 THR 247 0.0001

THR 247 ASP 248 -0.0001

ASP 248 ASP 248 0.0003

ASP 248 PHE 249 -0.1238

PHE 249 PHE 249 0.0004

PHE 249 SER 250 0.0001

SER 250 SER 250 -0.0002

SER 250 THR 251 0.0049

THR 251 THR 251 0.0004

THR 251 ALA 252 0.0000

ALA 252 ALA 252 -0.0000

ALA 252 GLN 253 0.0338

GLN 253 GLN 253 -0.0001

GLN 253 GLY 254 -0.0003

GLY 254 GLY 254 0.0002

GLY 254 PHE 255 -0.0418

PHE 255 PHE 255 0.0002

PHE 255 GLN 256 0.0001

GLN 256 GLN 256 -0.0001

GLN 256 THR 257 0.0033

THR 257 THR 257 -0.0002

THR 257 VAL 258 -0.0006

VAL 258 VAL 258 -0.0002

VAL 258 LEU 259 -0.0339

LEU 259 LEU 259 0.0003

LEU 259 GLU 260 0.0007

GLU 260 GLU 260 -0.0000

GLU 260 LEU 261 0.0346

LEU 261 LEU 261 0.0004

LEU 261 VAL 262 -0.0000

VAL 262 VAL 262 0.0003

VAL 262 LEU 263 0.0206

LEU 263 LEU 263 0.0004

LEU 263 LYS 264 0.0002

LYS 264 LYS 264 -0.0006

LYS 264 HIS 265 -0.0620

HIS 265 HIS 265 0.0002

HIS 265 GLN 266 -0.0003

GLN 266 GLN 266 0.0004

GLN 266 LYS 267 -0.0702

LYS 267 LYS 267 0.0002

LYS 267 LEU 268 0.0003

LEU 268 LEU 268 0.0002

LEU 268 CYS 269 -0.0012

CYS 269 CYS 269 -0.0000

CYS 269 ILE 270 -0.0002

ILE 270 ILE 270 0.0001

ILE 270 PHE 271 0.0016

PHE 271 PHE 271 -0.0000

PHE 271 TRP 272 0.0002

TRP 272 TRP 272 0.0008

TRP 272 GLU 273 0.0577

GLU 273 GLU 273 -0.0004

GLU 273 ALA 274 0.0000

ALA 274 ALA 274 0.0002

ALA 274 TYR 275 0.0211

TYR 275 TYR 275 -0.0001

TYR 275 TYR 276 0.0008

TYR 276 TYR 276 -0.0004

TYR 276 ASP 277 -0.0363

ASP 277 ASP 277 -0.0003

ASP 277 PHE 278 0.0004

PHE 278 PHE 278 -0.0002

PHE 278 THR 279 0.0203

THR 279 THR 279 -0.0007

THR 279 ASN 280 -0.0003

ASN 280 ASN 280 -0.0003

ASN 280 PRO 281 -0.0150

PRO 281 PRO 281 -0.0006

PRO 281 VAL 282 0.0004

VAL 282 VAL 282 -0.0000

VAL 282 VAL 283 -0.0446

VAL 283 VAL 283 0.0001

VAL 283 GLY 284 -0.0003

GLY 284 GLY 284 -0.0005

GLY 284 ARG 285 -0.0344

ARG 285 ARG 285 0.0001

ARG 285 CYS 286 0.0001

CYS 286 CYS 286 -0.0005

CYS 286 MET 287 0.0162

MET 287 MET 287 0.0002

MET 287 LEU 288 -0.0003

LEU 288 LEU 288 -0.0001

LEU 288 GLN 289 -0.0458

GLN 289 GLN 289 -0.0002

GLN 289 GLN 290 0.0002

GLN 290 GLN 290 -0.0000

GLN 290 LEU 291 0.0290

LEU 291 LEU 291 -0.0007

LEU 291 LYS 292 0.0003

LYS 292 LYS 292 -0.0004

LYS 292 LYS 293 -0.0030

LYS 293 LYS 293 0.0008

LYS 293 PRO 294 0.0001

PRO 294 PRO 294 -0.0004

PRO 294 ARG 295 0.1823

ARG 295 ARG 295 0.0006

ARG 295 PRO 296 -0.0000

PRO 296 PRO 296 -0.0002

PRO 296 VAL 297 0.0400

VAL 297 VAL 297 -0.0002

VAL 297 ILE 298 -0.0000

ILE 298 ILE 298 0.0005

ILE 298 LEU 299 0.0935

LEU 299 LEU 299 0.0001

LEU 299 ASP 300 -0.0002

ASP 300 ASP 300 -0.0009

ASP 300 PRO 301 -0.0305

PRO 301 PRO 301 0.0002

PRO 301 ALA 302 -0.0008

ALA 302 ALA 302 0.0004

ALA 302 ASP 303 -0.0519

ASP 303 ASP 303 0.0006

ASP 303 PRO 304 0.0003

PRO 304 PRO 304 0.0007

PRO 304 THR 305 -0.0799

THR 305 THR 305 0.0002

THR 305 GLY 306 -0.0004

GLY 306 GLY 306 -0.0004

GLY 306 ASN 307 0.1332

ASN 307 ASN 307 0.0004

ASN 307 VAL 308 -0.0001

VAL 308 VAL 308 -0.0001

VAL 308 GLY 309 0.0318

GLY 309 GLY 309 -0.0001

GLY 309 GLY 310 -0.0005

GLY 310 GLY 310 0.0005

GLY 310 GLY 311 -0.1292

GLY 311 GLY 311 -0.0004

GLY 311 ASP 312 -0.0002

ASP 312 ASP 312 0.0003

ASP 312 THR 313 -0.0175

THR 313 THR 313 0.0001

THR 313 HIS 314 -0.0004

HIS 314 HIS 314 -0.0002

HIS 314 SER 315 0.0322

SER 315 SER 315 -0.0002

SER 315 TRP 316 0.0004

TRP 316 TRP 316 -0.0006

TRP 316 GLN 317 -0.0169

GLN 317 GLN 317 0.0002

GLN 317 ARG 318 -0.0001

ARG 318 ARG 318 0.0001

ARG 318 LEU 319 -0.0351

LEU 319 LEU 319 -0.0004

LEU 319 ALA 320 -0.0003

ALA 320 ALA 320 -0.0005

ALA 320 GLN 321 -0.0773

GLN 321 GLN 321 0.0007

GLN 321 GLU 322 -0.0005

GLU 322 GLU 322 0.0001

GLU 322 ALA 323 -0.0737

ALA 323 ALA 323 -0.0002

ALA 323 ARG 324 -0.0004

ARG 324 ARG 324 0.0006

ARG 324 VAL 325 0.0593

VAL 325 VAL 325 -0.0001

VAL 325 TRP 326 -0.0003

TRP 326 TRP 326 0.0003

TRP 326 LEU 327 0.0120

LEU 327 LEU 327 -0.0006

LEU 327 GLY 328 0.0003

GLY 328 GLY 328 0.0003

GLY 328 TYR 329 -0.0001

TYR 329 TYR 329 -0.0004

TYR 329 PRO 330 0.0001

PRO 330 PRO 330 0.0004

PRO 330 CYS 331 0.0116

CYS 331 CYS 331 -0.0003

CYS 331 CYS 332 0.0002

CYS 332 CYS 332 -0.0003

CYS 332 LYS 333 0.0056

LYS 333 LYS 333 -0.0005

LYS 333 ASN 334 0.0001

ASN 334 ASN 334 -0.0002

ASN 334 LEU 335 0.0636

LEU 335 LEU 335 0.0001

LEU 335 ASP 336 0.0006

ASP 336 ASP 336 0.0002

ASP 336 GLY 337 0.0476

GLY 337 GLY 337 -0.0002

GLY 337 SER 338 0.0002

SER 338 SER 338 0.0004

SER 338 LEU 339 0.0444

LEU 339 LEU 339 0.0003

LEU 339 VAL 340 -0.0002

VAL 340 VAL 340 0.0001

VAL 340 GLY 341 0.1003

GLY 341 GLY 341 -0.0000

GLY 341 ALA 342 0.0002

ALA 342 ALA 342 0.0002

ALA 342 TRP 343 -0.0156

TRP 343 TRP 343 0.0004

TRP 343 THR 344 0.0000

THR 344 THR 344 0.0003

THR 344 MET 345 0.0324

MET 345 MET 345 0.0003

MET 345 LEU 346 -0.0002

LEU 346 LEU 346 -0.0003

LEU 346 GLN 347 -0.0161

GLN 347 GLN 347 0.0001

GLN 347 LYS 348 -0.0002

LYS 348 LYS 348 -0.0000

LYS 348 ILE 349 0.0133

ILE 349 ILE 349 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: October 18th, 2018.

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

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CA strain for 221128151102134046

--- normal mode 11 ---

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

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