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

* *

CA strain for 221128151102134046

--- normal mode 9 ---

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 -0.0004

MET 1 GLU 2 0.0004

GLU 2 GLU 2 -0.0003

GLU 2 LEU 3 -0.0183

LEU 3 LEU 3 -0.0003

LEU 3 ARG 4 0.0001

ARG 4 ARG 4 0.0002

ARG 4 HIS 5 -0.0056

HIS 5 HIS 5 0.0001

HIS 5 THR 6 0.0001

THR 6 THR 6 -0.0001

THR 6 PRO 7 -0.0017

PRO 7 PRO 7 -0.0002

PRO 7 ALA 8 -0.0002

ALA 8 ALA 8 0.0007

ALA 8 ARG 9 0.0172

ARG 9 ARG 9 0.0003

ARG 9 ASP 10 -0.0002

ASP 10 ASP 10 0.0001

ASP 10 LEU 11 -0.0148

LEU 11 LEU 11 -0.0002

LEU 11 ASP 12 0.0002

ASP 12 ASP 12 0.0003

ASP 12 LYS 13 0.0358

LYS 13 LYS 13 0.0001

LYS 13 PHE 14 -0.0003

PHE 14 PHE 14 0.0003

PHE 14 ILE 15 -0.0442

ILE 15 ILE 15 0.0002

ILE 15 GLU 16 -0.0001

GLU 16 GLU 16 0.0000

GLU 16 ASP 17 -0.0747

ASP 17 ASP 17 0.0000

ASP 17 HIS 18 0.0002

HIS 18 HIS 18 -0.0002

HIS 18 LEU 19 0.0142

LEU 19 LEU 19 0.0003

LEU 19 LEU 20 0.0003

LEU 20 LEU 20 -0.0003

LEU 20 PRO 21 0.1319

PRO 21 PRO 21 -0.0001

PRO 21 ASN 22 -0.0006

ASN 22 ASN 22 -0.0002

ASN 22 THR 23 0.0337

THR 23 THR 23 0.0001

THR 23 CYS 24 -0.0002

CYS 24 CYS 24 -0.0001

CYS 24 PHE 25 0.0759

PHE 25 PHE 25 -0.0004

PHE 25 ARG 26 -0.0004

ARG 26 ARG 26 -0.0003

ARG 26 THR 27 -0.0883

THR 27 THR 27 0.0002

THR 27 GLN 28 0.0003

GLN 28 GLN 28 -0.0004

GLN 28 VAL 29 -0.0282

VAL 29 VAL 29 0.0002

VAL 29 LYS 30 0.0000

LYS 30 LYS 30 0.0000

LYS 30 GLU 31 -0.1057

GLU 31 GLU 31 0.0008

GLU 31 ALA 32 -0.0002

ALA 32 ALA 32 -0.0001

ALA 32 ILE 33 -0.0372

ILE 33 ILE 33 -0.0003

ILE 33 ASP 34 -0.0002

ASP 34 ASP 34 -0.0001

ASP 34 ILE 35 -0.1960

ILE 35 ILE 35 0.0002

ILE 35 VAL 36 -0.0005

VAL 36 VAL 36 -0.0000

VAL 36 CYS 37 -0.0426

CYS 37 CYS 37 -0.0003

CYS 37 ARG 38 0.0005

ARG 38 ARG 38 0.0003

ARG 38 PHE 39 -0.1076

PHE 39 PHE 39 0.0000

PHE 39 LEU 40 -0.0005

LEU 40 LEU 40 -0.0006

LEU 40 LYS 41 -0.0238

LYS 41 LYS 41 -0.0001

LYS 41 GLU 42 -0.0005

GLU 42 GLU 42 0.0002

GLU 42 ARG 43 -0.1379

ARG 43 ARG 43 -0.0002

ARG 43 CYS 44 0.0006

CYS 44 CYS 44 0.0003

CYS 44 PHE 45 -0.0490

PHE 45 PHE 45 0.0004

PHE 45 GLN 46 -0.0000

GLN 46 GLN 46 0.0001

GLN 46 GLY 47 0.0147

GLY 47 GLY 47 -0.0002

GLY 47 THR 48 0.0004

THR 48 THR 48 -0.0002

THR 48 ALA 49 0.0280

ALA 49 ALA 49 0.0002

ALA 49 ASP 50 0.0005

ASP 50 ASP 50 -0.0002

ASP 50 PRO 51 0.0031

PRO 51 PRO 51 0.0001

PRO 51 VAL 52 -0.0005

VAL 52 VAL 52 -0.0003

VAL 52 ARG 53 0.0056

ARG 53 ARG 53 0.0000

ARG 53 VAL 54 0.0006

VAL 54 VAL 54 0.0000

VAL 54 SER 55 -0.0769

SER 55 SER 55 0.0003

SER 55 LYS 56 0.0001

LYS 56 LYS 56 0.0001

LYS 56 VAL 57 -0.0020

VAL 57 VAL 57 0.0002

VAL 57 VAL 58 0.0007

VAL 58 VAL 58 -0.0010

VAL 58 LYS 59 -0.0054

LYS 59 LYS 59 0.0001

LYS 59 GLY 60 0.0003

GLY 60 GLY 60 -0.0002

GLY 60 GLY 61 0.0724

GLY 61 GLY 61 -0.0001

GLY 61 SER 62 -0.0003

SER 62 SER 62 -0.0004

SER 62 SER 63 0.0645

SER 63 SER 63 -0.0001

SER 63 GLY 64 0.0000

GLY 64 GLY 64 -0.0001

GLY 64 LYS 65 0.0126

LYS 65 LYS 65 -0.0002

LYS 65 GLY 66 0.0000

GLY 66 GLY 66 -0.0002

GLY 66 THR 67 0.0146

THR 67 THR 67 -0.0001

THR 67 THR 68 -0.0002

THR 68 THR 68 -0.0005

THR 68 LEU 69 -0.0395

LEU 69 LEU 69 -0.0002

LEU 69 ARG 70 0.0001

ARG 70 ARG 70 0.0000

ARG 70 GLY 71 -0.0452

GLY 71 GLY 71 -0.0002

GLY 71 ARG 72 -0.0005

ARG 72 ARG 72 0.0002

ARG 72 SER 73 -0.0237

SER 73 SER 73 0.0002

SER 73 ASP 74 -0.0003

ASP 74 ASP 74 0.0000

ASP 74 ALA 75 0.0276

ALA 75 ALA 75 0.0002

ALA 75 ASP 76 -0.0002

ASP 76 ASP 76 -0.0002

ASP 76 LEU 77 -0.0236

LEU 77 LEU 77 -0.0000

LEU 77 VAL 78 -0.0003

VAL 78 VAL 78 -0.0001

VAL 78 VAL 79 0.0292

VAL 79 VAL 79 0.0001

VAL 79 PHE 80 0.0001

PHE 80 PHE 80 -0.0001

PHE 80 LEU 81 0.0178

LEU 81 LEU 81 -0.0001

LEU 81 THR 82 0.0002

THR 82 THR 82 -0.0002

THR 82 LYS 83 0.0505

LYS 83 LYS 83 -0.0002

LYS 83 LEU 84 -0.0004

LEU 84 LEU 84 -0.0006

LEU 84 THR 85 0.0079

THR 85 THR 85 0.0005

THR 85 SER 86 -0.0001

SER 86 SER 86 -0.0002

SER 86 PHE 87 -0.0102

PHE 87 PHE 87 0.0000

PHE 87 GLU 88 -0.0002

GLU 88 GLU 88 0.0001

GLU 88 ASP 89 0.0262

ASP 89 ASP 89 0.0004

ASP 89 GLN 90 -0.0000

GLN 90 GLN 90 0.0003

GLN 90 LEU 91 0.0195

LEU 91 LEU 91 0.0004

LEU 91 ARG 92 -0.0001

ARG 92 ARG 92 -0.0007

ARG 92 ARG 93 0.0439

ARG 93 ARG 93 -0.0006

ARG 93 ARG 94 0.0001

ARG 94 ARG 94 -0.0003

ARG 94 GLY 95 -0.0459

GLY 95 GLY 95 -0.0008

GLY 95 GLU 96 -0.0004

GLU 96 GLU 96 -0.0004

GLU 96 PHE 97 -0.0255

PHE 97 PHE 97 0.0009

PHE 97 ILE 98 0.0006

ILE 98 ILE 98 0.0004

ILE 98 GLN 99 -0.0011

GLN 99 GLN 99 0.0005

GLN 99 GLU 100 -0.0003

GLU 100 GLU 100 -0.0004

GLU 100 ILE 101 -0.0078

ILE 101 ILE 101 -0.0002

ILE 101 ARG 102 0.0003

ARG 102 ARG 102 -0.0003

ARG 102 ARG 103 -0.0431

ARG 103 ARG 103 -0.0004

ARG 103 GLN 104 0.0000

GLN 104 GLN 104 -0.0004

GLN 104 LEU 105 0.0128

LEU 105 LEU 105 0.0005

LEU 105 GLU 106 -0.0001

GLU 106 GLU 106 -0.0004

GLU 106 ALA 107 -0.0218

ALA 107 ALA 107 0.0001

ALA 107 CYS 108 -0.0001

CYS 108 CYS 108 -0.0000

CYS 108 GLN 109 -0.0368

GLN 109 GLN 109 -0.0005

GLN 109 ARG 110 0.0002

ARG 110 ARG 110 -0.0000

ARG 110 GLU 111 0.0109

GLU 111 GLU 111 0.0007

GLU 111 GLN 112 0.0001

GLN 112 GLN 112 -0.0006

GLN 112 LYS 113 -0.0622

LYS 113 LYS 113 -0.0008

LYS 113 PHE 114 -0.0002

PHE 114 PHE 114 -0.0003

PHE 114 LYS 115 -0.0039

LYS 115 LYS 115 -0.0000

LYS 115 VAL 116 0.0004

VAL 116 VAL 116 0.0002

VAL 116 THR 117 -0.0239

THR 117 THR 117 -0.0001

THR 117 PHE 118 -0.0002

PHE 118 PHE 118 -0.0000

PHE 118 GLU 119 -0.0412

GLU 119 GLU 119 -0.0004

GLU 119 VAL 120 0.0003

VAL 120 VAL 120 -0.0003

VAL 120 GLN 121 0.1248

GLN 121 GLN 121 -0.0005

GLN 121 SER 122 0.0001

SER 122 SER 122 -0.0002

SER 122 PRO 123 -0.0004

PRO 123 PRO 123 0.0005

PRO 123 ARG 124 -0.0001

ARG 124 ARG 124 -0.0001

ARG 124 ARG 125 -0.0411

ARG 125 ARG 125 0.0002

ARG 125 GLU 126 0.0001

GLU 126 GLU 126 -0.0002

GLU 126 ASN 127 -0.0927

ASN 127 ASN 127 0.0001

ASN 127 PRO 128 0.0001

PRO 128 PRO 128 0.0001

PRO 128 ARG 129 0.0039

ARG 129 ARG 129 0.0001

ARG 129 ALA 130 -0.0003

ALA 130 ALA 130 0.0004

ALA 130 LEU 131 0.2135

LEU 131 LEU 131 -0.0004

LEU 131 SER 132 0.0001

SER 132 SER 132 0.0003

SER 132 PHE 133 0.0052

PHE 133 PHE 133 0.0000

PHE 133 VAL 134 0.0003

VAL 134 VAL 134 -0.0002

VAL 134 LEU 135 -0.0470

LEU 135 LEU 135 -0.0001

LEU 135 SER 136 0.0000

SER 136 SER 136 0.0001

SER 136 SER 137 -0.0104

SER 137 SER 137 0.0002

SER 137 PRO 138 0.0002

PRO 138 PRO 138 0.0001

PRO 138 GLN 139 -0.0553

GLN 139 GLN 139 0.0003

GLN 139 LEU 140 0.0006

LEU 140 LEU 140 0.0005

LEU 140 GLN 141 0.0985

GLN 141 GLN 141 -0.0000

GLN 141 GLN 142 0.0005

GLN 142 GLN 142 0.0002

GLN 142 GLU 143 -0.0787

GLU 143 GLU 143 0.0002

GLU 143 VAL 144 0.0003

VAL 144 VAL 144 0.0001

VAL 144 GLU 145 0.0147

GLU 145 GLU 145 -0.0007

GLU 145 PHE 146 -0.0003

PHE 146 PHE 146 0.0001

PHE 146 ASP 147 0.0074

ASP 147 ASP 147 0.0001

ASP 147 VAL 148 0.0003

VAL 148 VAL 148 -0.0000

VAL 148 LEU 149 0.0620

LEU 149 LEU 149 0.0001

LEU 149 PRO 150 -0.0004

PRO 150 PRO 150 -0.0003

PRO 150 ALA 151 0.0047

ALA 151 ALA 151 0.0001

ALA 151 PHE 152 -0.0001

PHE 152 PHE 152 0.0003

PHE 152 ASP 153 0.0461

ASP 153 ASP 153 -0.0004

ASP 153 ALA 154 0.0001

ALA 154 ALA 154 -0.0002

ALA 154 LEU 155 0.0895

LEU 155 LEU 155 -0.0002

LEU 155 GLY 156 0.0001

GLY 156 GLY 156 -0.0005

GLY 156 GLN 157 0.0121

GLN 157 GLN 157 0.0003

GLN 157 TRP 158 0.0001

TRP 158 TRP 158 0.0009

TRP 158 THR 159 -0.0567

THR 159 THR 159 0.0004

THR 159 PRO 160 0.0000

PRO 160 PRO 160 -0.0002

PRO 160 GLY 161 -0.0044

GLY 161 GLY 161 -0.0005

GLY 161 TYR 162 -0.0003

TYR 162 TYR 162 -0.0002

TYR 162 LYS 163 -0.0614

LYS 163 LYS 163 0.0003

LYS 163 PRO 164 0.0001

PRO 164 PRO 164 -0.0000

PRO 164 ASN 165 0.0824

ASN 165 ASN 165 0.0005

ASN 165 PRO 166 0.0003

PRO 166 PRO 166 -0.0005

PRO 166 GLU 167 -0.0032

GLU 167 GLU 167 0.0001

GLU 167 ILE 168 -0.0005

ILE 168 ILE 168 -0.0000

ILE 168 TYR 169 -0.0356

TYR 169 TYR 169 -0.0008

TYR 169 VAL 170 -0.0001

VAL 170 VAL 170 -0.0000

VAL 170 GLN 171 -0.0611

GLN 171 GLN 171 0.0002

GLN 171 LEU 172 -0.0004

LEU 172 LEU 172 -0.0003

LEU 172 ILE 173 0.0420

ILE 173 ILE 173 0.0002

ILE 173 LYS 174 0.0002

LYS 174 LYS 174 0.0003

LYS 174 GLU 175 0.0085

GLU 175 GLU 175 0.0002

GLU 175 CYS 176 -0.0001

CYS 176 CYS 176 -0.0002

CYS 176 LYS 177 0.0211

LYS 177 LYS 177 0.0002

LYS 177 SER 178 0.0001

SER 178 SER 178 -0.0000

SER 178 ARG 179 0.0266

ARG 179 ARG 179 0.0004

ARG 179 GLY 180 0.0003

GLY 180 GLY 180 0.0003

GLY 180 LYS 181 0.0310

LYS 181 LYS 181 0.0002

LYS 181 GLU 182 -0.0004

GLU 182 GLU 182 -0.0004

GLU 182 GLY 183 0.0083

GLY 183 GLY 183 -0.0001

GLY 183 GLU 184 -0.0001

GLU 184 GLU 184 0.0005

GLU 184 PHE 185 -0.0090

PHE 185 PHE 185 0.0006

PHE 185 SER 186 0.0005

SER 186 SER 186 -0.0002

SER 186 THR 187 0.1055

THR 187 THR 187 0.0003

THR 187 CYS 188 0.0001

CYS 188 CYS 188 0.0003

CYS 188 PHE 189 -0.0376

PHE 189 PHE 189 0.0001

PHE 189 THR 190 -0.0004

THR 190 THR 190 0.0002

THR 190 GLU 191 0.0076

GLU 191 GLU 191 -0.0001

GLU 191 LEU 192 0.0001

LEU 192 LEU 192 -0.0007

LEU 192 GLN 193 -0.0244

GLN 193 GLN 193 0.0000

GLN 193 ARG 194 0.0001

ARG 194 ARG 194 0.0000

ARG 194 ARG 194 0.0003

ARG 194 ASP 195 0.0258

ASP 195 ASP 195 0.0003

ASP 195 PHE 196 -0.0002

PHE 196 PHE 196 -0.0000

PHE 196 LEU 197 0.0335

LEU 197 LEU 197 0.0004

LEU 197 ARG 198 -0.0003

ARG 198 ARG 198 -0.0001

ARG 198 ASN 199 0.0197

ASN 199 ASN 199 -0.0000

ASN 199 ARG 200 -0.0002

ARG 200 ARG 200 -0.0004

ARG 200 PRO 201 0.0076

PRO 201 PRO 201 -0.0000

PRO 201 THR 202 -0.0000

THR 202 THR 202 0.0003

THR 202 LYS 203 0.1392

LYS 203 LYS 203 0.0001

LYS 203 LEU 204 -0.0002

LEU 204 LEU 204 -0.0001

LEU 204 LYS 205 0.0972

LYS 205 LYS 205 0.0000

LYS 205 SER 206 -0.0001

SER 206 SER 206 0.0003

SER 206 LEU 207 -0.0190

LEU 207 LEU 207 0.0002

LEU 207 ILE 208 -0.0000

ILE 208 ILE 208 -0.0002

ILE 208 ARG 209 0.0308

ARG 209 ARG 209 0.0003

ARG 209 LEU 210 0.0002

LEU 210 LEU 210 -0.0001

LEU 210 VAL 211 0.0094

VAL 211 VAL 211 0.0003

VAL 211 LYS 212 -0.0001

LYS 212 LYS 212 0.0001

LYS 212 HIS 213 -0.0437

HIS 213 HIS 213 -0.0002

HIS 213 TRP 214 -0.0002

TRP 214 TRP 214 -0.0001

TRP 214 TYR 215 -0.0100

TYR 215 TYR 215 -0.0004

TYR 215 GLN 216 0.0001

GLN 216 GLN 216 0.0000

GLN 216 THR 217 -0.0313

THR 217 THR 217 -0.0002

THR 217 CYS 218 0.0001

CYS 218 CYS 218 0.0004

CYS 218 LYS 219 -0.0350

LYS 219 LYS 219 -0.0001

LYS 219 LYS 220 0.0005

LYS 220 LYS 220 -0.0003

LYS 220 THR 221 -0.0184

THR 221 THR 221 0.0000

THR 221 HIS 222 0.0001

HIS 222 HIS 222 0.0001

HIS 222 GLY 223 -0.0188

GLY 223 GLY 223 0.0001

GLY 223 ASN 224 0.0005

ASN 224 ASN 224 -0.0003

ASN 224 LYS 225 0.0063

LYS 225 LYS 225 -0.0000

LYS 225 LEU 226 0.0007

LEU 226 LEU 226 -0.0003

LEU 226 PRO 227 -0.0546

PRO 227 PRO 227 0.0000

PRO 227 PRO 228 0.0003

PRO 228 PRO 228 0.0001

PRO 228 GLN 229 0.0990

GLN 229 GLN 229 0.0002

GLN 229 TYR 230 -0.0006

TYR 230 TYR 230 -0.0004

TYR 230 ALA 231 0.0212

ALA 231 ALA 231 0.0002

ALA 231 LEU 232 -0.0000

LEU 232 LEU 232 0.0002

LEU 232 GLU 233 0.0221

GLU 233 GLU 233 -0.0001

GLU 233 LEU 234 -0.0000

LEU 234 LEU 234 -0.0002

LEU 234 LEU 235 0.0129

LEU 235 LEU 235 -0.0002

LEU 235 THR 236 -0.0003

THR 236 THR 236 -0.0005

THR 236 VAL 237 0.0161

VAL 237 VAL 237 0.0004

VAL 237 TYR 238 0.0002

TYR 238 TYR 238 -0.0001

TYR 238 ALA 239 0.0019

ALA 239 ALA 239 0.0001

ALA 239 TRP 240 0.0001

TRP 240 TRP 240 -0.0001

TRP 240 GLU 241 -0.0845

GLU 241 GLU 241 0.0003

GLU 241 GLN 242 0.0003

GLN 242 GLN 242 0.0000

GLN 242 GLY 243 -0.0238

GLY 243 GLY 243 0.0005

GLY 243 SER 244 -0.0004

SER 244 SER 244 0.0002

SER 244 ARG 245 0.0390

ARG 245 ARG 245 -0.0008

ARG 245 LYS 246 0.0005

LYS 246 LYS 246 -0.0005

LYS 246 THR 247 -0.1111

THR 247 THR 247 0.0003

THR 247 ASP 248 -0.0004

ASP 248 ASP 248 0.0006

ASP 248 PHE 249 0.1639

PHE 249 PHE 249 -0.0003

PHE 249 SER 250 0.0003

SER 250 SER 250 -0.0005

SER 250 THR 251 -0.0241

THR 251 THR 251 0.0008

THR 251 ALA 252 -0.0004

ALA 252 ALA 252 0.0000

ALA 252 GLN 253 0.0179

GLN 253 GLN 253 0.0003

GLN 253 GLY 254 -0.0001

GLY 254 GLY 254 -0.0001

GLY 254 PHE 255 0.0343

PHE 255 PHE 255 -0.0003

PHE 255 GLN 256 0.0005

GLN 256 GLN 256 0.0004

GLN 256 THR 257 0.0334

THR 257 THR 257 0.0001

THR 257 VAL 258 0.0000

VAL 258 VAL 258 -0.0003

VAL 258 LEU 259 -0.0034

LEU 259 LEU 259 -0.0004

LEU 259 GLU 260 0.0000

GLU 260 GLU 260 0.0003

GLU 260 LEU 261 -0.0027

LEU 261 LEU 261 0.0003

LEU 261 VAL 262 0.0002

VAL 262 VAL 262 0.0007

VAL 262 LEU 263 -0.0010

LEU 263 LEU 263 0.0004

LEU 263 LYS 264 0.0006

LYS 264 LYS 264 -0.0006

LYS 264 HIS 265 0.0079

HIS 265 HIS 265 -0.0001

HIS 265 GLN 266 -0.0003

GLN 266 GLN 266 -0.0008

GLN 266 LYS 267 0.0140

LYS 267 LYS 267 -0.0000

LYS 267 LEU 268 -0.0001

LEU 268 LEU 268 0.0002

LEU 268 CYS 269 0.0086

CYS 269 CYS 269 0.0001

CYS 269 ILE 270 -0.0001

ILE 270 ILE 270 0.0006

ILE 270 PHE 271 0.0026

PHE 271 PHE 271 0.0006

PHE 271 TRP 272 -0.0001

TRP 272 TRP 272 -0.0006

TRP 272 GLU 273 -0.0153

GLU 273 GLU 273 -0.0002

GLU 273 ALA 274 0.0002

ALA 274 ALA 274 0.0005

ALA 274 TYR 275 -0.0034

TYR 275 TYR 275 0.0000

TYR 275 TYR 276 0.0000

TYR 276 TYR 276 0.0007

TYR 276 ASP 277 -0.0082

ASP 277 ASP 277 0.0002

ASP 277 PHE 278 0.0008

PHE 278 PHE 278 -0.0000

PHE 278 THR 279 0.0087

THR 279 THR 279 -0.0000

THR 279 ASN 280 0.0001

ASN 280 ASN 280 -0.0002

ASN 280 PRO 281 -0.0158

PRO 281 PRO 281 0.0005

PRO 281 VAL 282 -0.0004

VAL 282 VAL 282 0.0000

VAL 282 VAL 283 -0.0012

VAL 283 VAL 283 -0.0004

VAL 283 GLY 284 -0.0001

GLY 284 GLY 284 0.0001

GLY 284 ARG 285 0.0260

ARG 285 ARG 285 -0.0002

ARG 285 CYS 286 -0.0004

CYS 286 CYS 286 -0.0002

CYS 286 MET 287 -0.0225

MET 287 MET 287 0.0001

MET 287 LEU 288 0.0004

LEU 288 LEU 288 0.0002

LEU 288 GLN 289 0.0303

GLN 289 GLN 289 0.0006

GLN 289 GLN 290 0.0002

GLN 290 GLN 290 0.0000

GLN 290 LEU 291 0.0071

LEU 291 LEU 291 -0.0005

LEU 291 LYS 292 -0.0000

LYS 292 LYS 292 0.0004

LYS 292 LYS 293 0.0247

LYS 293 LYS 293 -0.0001

LYS 293 PRO 294 0.0002

PRO 294 PRO 294 -0.0002

PRO 294 ARG 295 -0.0829

ARG 295 ARG 295 -0.0002

ARG 295 PRO 296 0.0001

PRO 296 PRO 296 -0.0004

PRO 296 VAL 297 -0.0236

VAL 297 VAL 297 -0.0002

VAL 297 ILE 298 0.0001

ILE 298 ILE 298 -0.0004

ILE 298 LEU 299 -0.0520

LEU 299 LEU 299 0.0007

LEU 299 ASP 300 -0.0006

ASP 300 ASP 300 -0.0001

ASP 300 PRO 301 -0.0255

PRO 301 PRO 301 0.0001

PRO 301 ALA 302 -0.0005

ALA 302 ALA 302 -0.0003

ALA 302 ASP 303 0.0253

ASP 303 ASP 303 0.0005

ASP 303 PRO 304 0.0002

PRO 304 PRO 304 -0.0006

PRO 304 THR 305 0.0217

THR 305 THR 305 -0.0000

THR 305 GLY 306 0.0005

GLY 306 GLY 306 0.0003

GLY 306 ASN 307 -0.0220

ASN 307 ASN 307 -0.0003

ASN 307 VAL 308 0.0007

VAL 308 VAL 308 -0.0002

VAL 308 GLY 309 0.0159

GLY 309 GLY 309 0.0005

GLY 309 GLY 310 -0.0001

GLY 310 GLY 310 0.0001

GLY 310 GLY 311 0.0597

GLY 311 GLY 311 -0.0000

GLY 311 ASP 312 0.0002

ASP 312 ASP 312 0.0000

ASP 312 THR 313 0.0049

THR 313 THR 313 -0.0004

THR 313 HIS 314 -0.0000

HIS 314 HIS 314 0.0001

HIS 314 SER 315 -0.0050

SER 315 SER 315 0.0006

SER 315 TRP 316 -0.0000

TRP 316 TRP 316 0.0004

TRP 316 GLN 317 -0.0124

GLN 317 GLN 317 0.0001

GLN 317 ARG 318 0.0004

ARG 318 ARG 318 -0.0003

ARG 318 LEU 319 0.0027

LEU 319 LEU 319 0.0000

LEU 319 ALA 320 -0.0001

ALA 320 ALA 320 0.0003

ALA 320 GLN 321 -0.0015

GLN 321 GLN 321 -0.0003

GLN 321 GLU 322 -0.0003

GLU 322 GLU 322 -0.0001

GLU 322 ALA 323 -0.0049

ALA 323 ALA 323 -0.0005

ALA 323 ARG 324 -0.0001

ARG 324 ARG 324 0.0006

ARG 324 VAL 325 0.0325

VAL 325 VAL 325 -0.0003

VAL 325 TRP 326 0.0002

TRP 326 TRP 326 -0.0000

TRP 326 LEU 327 0.0162

LEU 327 LEU 327 0.0004

LEU 327 GLY 328 -0.0001

GLY 328 GLY 328 -0.0003

GLY 328 TYR 329 0.0112

TYR 329 TYR 329 0.0002

TYR 329 PRO 330 0.0002

PRO 330 PRO 330 -0.0001

PRO 330 CYS 331 0.0135

CYS 331 CYS 331 0.0001

CYS 331 CYS 332 -0.0001

CYS 332 CYS 332 -0.0001

CYS 332 LYS 333 0.0076

LYS 333 LYS 333 0.0002

LYS 333 ASN 334 -0.0001

ASN 334 ASN 334 0.0005

ASN 334 LEU 335 -0.0669

LEU 335 LEU 335 -0.0005

LEU 335 ASP 336 -0.0006

ASP 336 ASP 336 0.0004

ASP 336 GLY 337 -0.0477

GLY 337 GLY 337 0.0004

GLY 337 SER 338 0.0003

SER 338 SER 338 0.0005

SER 338 LEU 339 -0.0173

LEU 339 LEU 339 -0.0001

LEU 339 VAL 340 -0.0004

VAL 340 VAL 340 0.0000

VAL 340 GLY 341 -0.0240

GLY 341 GLY 341 0.0000

GLY 341 ALA 342 -0.0002

ALA 342 ALA 342 0.0000

ALA 342 TRP 343 0.0448

TRP 343 TRP 343 -0.0001

TRP 343 THR 344 -0.0003

THR 344 THR 344 -0.0004

THR 344 MET 345 -0.0621

MET 345 MET 345 -0.0000

MET 345 LEU 346 0.0002

LEU 346 LEU 346 0.0004

LEU 346 GLN 347 0.0383

GLN 347 GLN 347 -0.0000

GLN 347 LYS 348 -0.0003

LYS 348 LYS 348 0.0002

LYS 348 ILE 349 -0.0172

ILE 349 ILE 349 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: October 18th, 2018.

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

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CA strain for 221128151102134046

--- normal mode 9 ---

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

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