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

* *

CA strain for 221128151102134046

--- normal mode 8 ---

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 -0.0003

MET 1 GLU 2 0.0004

GLU 2 GLU 2 0.0003

GLU 2 LEU 3 0.0216

LEU 3 LEU 3 -0.0008

LEU 3 ARG 4 -0.0004

ARG 4 ARG 4 0.0003

ARG 4 HIS 5 0.0076

HIS 5 HIS 5 0.0005

HIS 5 THR 6 -0.0005

THR 6 THR 6 0.0007

THR 6 PRO 7 0.0257

PRO 7 PRO 7 0.0003

PRO 7 ALA 8 -0.0002

ALA 8 ALA 8 0.0002

ALA 8 ARG 9 -0.0342

ARG 9 ARG 9 -0.0003

ARG 9 ASP 10 0.0002

ASP 10 ASP 10 0.0001

ASP 10 LEU 11 0.0147

LEU 11 LEU 11 0.0005

LEU 11 ASP 12 0.0001

ASP 12 ASP 12 -0.0000

ASP 12 LYS 13 -0.0171

LYS 13 LYS 13 -0.0000

LYS 13 PHE 14 -0.0003

PHE 14 PHE 14 0.0000

PHE 14 ILE 15 -0.0295

ILE 15 ILE 15 0.0003

ILE 15 GLU 16 -0.0000

GLU 16 GLU 16 0.0003

GLU 16 ASP 17 -0.0881

ASP 17 ASP 17 0.0003

ASP 17 HIS 18 0.0003

HIS 18 HIS 18 0.0003

HIS 18 LEU 19 0.0008

LEU 19 LEU 19 -0.0001

LEU 19 LEU 20 -0.0002

LEU 20 LEU 20 -0.0001

LEU 20 PRO 21 -0.0086

PRO 21 PRO 21 0.0001

PRO 21 ASN 22 -0.0002

ASN 22 ASN 22 0.0004

ASN 22 THR 23 -0.1053

THR 23 THR 23 -0.0000

THR 23 CYS 24 0.0001

CYS 24 CYS 24 -0.0004

CYS 24 PHE 25 -0.0503

PHE 25 PHE 25 -0.0003

PHE 25 ARG 26 -0.0001

ARG 26 ARG 26 -0.0000

ARG 26 THR 27 0.0220

THR 27 THR 27 0.0000

THR 27 GLN 28 0.0000

GLN 28 GLN 28 -0.0002

GLN 28 VAL 29 -0.0607

VAL 29 VAL 29 -0.0002

VAL 29 LYS 30 -0.0002

LYS 30 LYS 30 -0.0002

LYS 30 GLU 31 0.0221

GLU 31 GLU 31 -0.0010

GLU 31 ALA 32 -0.0003

ALA 32 ALA 32 -0.0006

ALA 32 ILE 33 -0.0227

ILE 33 ILE 33 -0.0006

ILE 33 ASP 34 0.0000

ASP 34 ASP 34 0.0001

ASP 34 ILE 35 -0.0240

ILE 35 ILE 35 0.0005

ILE 35 VAL 36 -0.0002

VAL 36 VAL 36 -0.0003

VAL 36 CYS 37 0.0068

CYS 37 CYS 37 -0.0004

CYS 37 ARG 38 -0.0005

ARG 38 ARG 38 -0.0002

ARG 38 PHE 39 -0.0610

PHE 39 PHE 39 -0.0004

PHE 39 LEU 40 -0.0001

LEU 40 LEU 40 0.0005

LEU 40 LYS 41 -0.0325

LYS 41 LYS 41 -0.0005

LYS 41 GLU 42 0.0001

GLU 42 GLU 42 0.0000

GLU 42 ARG 43 -0.1046

ARG 43 ARG 43 0.0001

ARG 43 CYS 44 -0.0004

CYS 44 CYS 44 -0.0001

CYS 44 PHE 45 0.0675

PHE 45 PHE 45 -0.0001

PHE 45 GLN 46 -0.0001

GLN 46 GLN 46 0.0000

GLN 46 GLY 47 -0.0396

GLY 47 GLY 47 -0.0001

GLY 47 THR 48 -0.0002

THR 48 THR 48 0.0002

THR 48 ALA 49 0.0009

ALA 49 ALA 49 0.0002

ALA 49 ASP 50 -0.0002

ASP 50 ASP 50 0.0004

ASP 50 PRO 51 -0.0053

PRO 51 PRO 51 -0.0002

PRO 51 VAL 52 0.0001

VAL 52 VAL 52 0.0003

VAL 52 ARG 53 -0.0053

ARG 53 ARG 53 0.0006

ARG 53 VAL 54 -0.0005

VAL 54 VAL 54 0.0005

VAL 54 SER 55 0.0020

SER 55 SER 55 -0.0001

SER 55 LYS 56 -0.0002

LYS 56 LYS 56 0.0006

LYS 56 VAL 57 0.0349

VAL 57 VAL 57 0.0004

VAL 57 VAL 58 -0.0007

VAL 58 VAL 58 0.0007

VAL 58 LYS 59 0.0229

LYS 59 LYS 59 0.0006

LYS 59 GLY 60 0.0000

GLY 60 GLY 60 -0.0000

GLY 60 GLY 61 0.0268

GLY 61 GLY 61 -0.0005

GLY 61 SER 62 -0.0002

SER 62 SER 62 0.0002

SER 62 SER 63 -0.0132

SER 63 SER 63 0.0004

SER 63 GLY 64 -0.0000

GLY 64 GLY 64 -0.0008

GLY 64 LYS 65 -0.0194

LYS 65 LYS 65 0.0001

LYS 65 GLY 66 0.0001

GLY 66 GLY 66 0.0001

GLY 66 THR 67 -0.0066

THR 67 THR 67 -0.0004

THR 67 THR 68 0.0000

THR 68 THR 68 -0.0008

THR 68 LEU 69 -0.0471

LEU 69 LEU 69 -0.0001

LEU 69 ARG 70 0.0004

ARG 70 ARG 70 0.0001

ARG 70 GLY 71 0.2893

GLY 71 GLY 71 -0.0004

GLY 71 ARG 72 0.0003

ARG 72 ARG 72 0.0000

ARG 72 SER 73 0.0544

SER 73 SER 73 0.0002

SER 73 ASP 74 -0.0003

ASP 74 ASP 74 0.0001

ASP 74 ALA 75 0.1296

ALA 75 ALA 75 0.0006

ALA 75 ASP 76 0.0002

ASP 76 ASP 76 -0.0007

ASP 76 LEU 77 0.0706

LEU 77 LEU 77 -0.0006

LEU 77 VAL 78 -0.0006

VAL 78 VAL 78 0.0005

VAL 78 VAL 79 -0.0134

VAL 79 VAL 79 0.0000

VAL 79 PHE 80 0.0004

PHE 80 PHE 80 -0.0004

PHE 80 LEU 81 -0.0144

LEU 81 LEU 81 0.0001

LEU 81 THR 82 0.0004

THR 82 THR 82 0.0000

THR 82 LYS 83 -0.0112

LYS 83 LYS 83 -0.0000

LYS 83 LEU 84 -0.0000

LEU 84 LEU 84 0.0003

LEU 84 THR 85 0.0100

THR 85 THR 85 -0.0002

THR 85 SER 86 -0.0004

SER 86 SER 86 0.0002

SER 86 PHE 87 0.0050

PHE 87 PHE 87 0.0004

PHE 87 GLU 88 -0.0001

GLU 88 GLU 88 -0.0003

GLU 88 ASP 89 0.0059

ASP 89 ASP 89 -0.0001

ASP 89 GLN 90 0.0004

GLN 90 GLN 90 0.0002

GLN 90 LEU 91 -0.0002

LEU 91 LEU 91 -0.0004

LEU 91 ARG 92 0.0003

ARG 92 ARG 92 -0.0005

ARG 92 ARG 93 -0.0200

ARG 93 ARG 93 0.0002

ARG 93 ARG 94 -0.0001

ARG 94 ARG 94 0.0004

ARG 94 GLY 95 0.0454

GLY 95 GLY 95 -0.0002

GLY 95 GLU 96 0.0002

GLU 96 GLU 96 0.0003

GLU 96 PHE 97 0.0265

PHE 97 PHE 97 0.0001

PHE 97 ILE 98 0.0000

ILE 98 ILE 98 -0.0004

ILE 98 GLN 99 0.0175

GLN 99 GLN 99 0.0001

GLN 99 GLU 100 -0.0001

GLU 100 GLU 100 -0.0003

GLU 100 ILE 101 0.0512

ILE 101 ILE 101 0.0002

ILE 101 ARG 102 -0.0002

ARG 102 ARG 102 0.0002

ARG 102 ARG 103 0.0320

ARG 103 ARG 103 0.0001

ARG 103 GLN 104 0.0003

GLN 104 GLN 104 0.0001

GLN 104 LEU 105 0.0460

LEU 105 LEU 105 -0.0001

LEU 105 GLU 106 0.0004

GLU 106 GLU 106 -0.0002

GLU 106 ALA 107 0.0029

ALA 107 ALA 107 0.0001

ALA 107 CYS 108 0.0005

CYS 108 CYS 108 0.0004

CYS 108 GLN 109 0.0069

GLN 109 GLN 109 0.0003

GLN 109 ARG 110 -0.0005

ARG 110 ARG 110 0.0004

ARG 110 GLU 111 0.0007

GLU 111 GLU 111 0.0004

GLU 111 GLN 112 0.0002

GLN 112 GLN 112 -0.0003

GLN 112 LYS 113 0.0023

LYS 113 LYS 113 0.0002

LYS 113 PHE 114 0.0002

PHE 114 PHE 114 -0.0003

PHE 114 LYS 115 0.0045

LYS 115 LYS 115 0.0007

LYS 115 VAL 116 0.0002

VAL 116 VAL 116 0.0002

VAL 116 THR 117 -0.0163

THR 117 THR 117 -0.0006

THR 117 PHE 118 0.0001

PHE 118 PHE 118 0.0003

PHE 118 GLU 119 -0.0165

GLU 119 GLU 119 0.0009

GLU 119 VAL 120 0.0004

VAL 120 VAL 120 0.0002

VAL 120 GLN 121 -0.2078

GLN 121 GLN 121 -0.0004

GLN 121 SER 122 0.0001

SER 122 SER 122 0.0004

SER 122 PRO 123 0.0350

PRO 123 PRO 123 -0.0005

PRO 123 ARG 124 0.0002

ARG 124 ARG 124 -0.0007

ARG 124 ARG 125 0.0552

ARG 125 ARG 125 -0.0001

ARG 125 GLU 126 0.0002

GLU 126 GLU 126 -0.0003

GLU 126 ASN 127 -0.0174

ASN 127 ASN 127 -0.0002

ASN 127 PRO 128 0.0001

PRO 128 PRO 128 -0.0000

PRO 128 ARG 129 -0.0069

ARG 129 ARG 129 0.0002

ARG 129 ALA 130 -0.0001

ALA 130 ALA 130 0.0002

ALA 130 LEU 131 -0.2011

LEU 131 LEU 131 0.0009

LEU 131 SER 132 -0.0002

SER 132 SER 132 0.0004

SER 132 PHE 133 -0.0343

PHE 133 PHE 133 -0.0001

PHE 133 VAL 134 -0.0003

VAL 134 VAL 134 -0.0000

VAL 134 LEU 135 -0.0138

LEU 135 LEU 135 -0.0002

LEU 135 SER 136 -0.0003

SER 136 SER 136 -0.0002

SER 136 SER 137 -0.0264

SER 137 SER 137 -0.0005

SER 137 PRO 138 -0.0003

PRO 138 PRO 138 -0.0001

PRO 138 GLN 139 0.0129

GLN 139 GLN 139 0.0002

GLN 139 LEU 140 0.0003

LEU 140 LEU 140 -0.0005

LEU 140 GLN 141 0.0465

GLN 141 GLN 141 -0.0001

GLN 141 GLN 142 -0.0000

GLN 142 GLN 142 0.0003

GLN 142 GLU 143 0.0216

GLU 143 GLU 143 -0.0002

GLU 143 VAL 144 0.0002

VAL 144 VAL 144 -0.0008

VAL 144 GLU 145 0.0197

GLU 145 GLU 145 -0.0003

GLU 145 PHE 146 0.0003

PHE 146 PHE 146 -0.0004

PHE 146 ASP 147 -0.0034

ASP 147 ASP 147 -0.0002

ASP 147 VAL 148 0.0002

VAL 148 VAL 148 0.0002

VAL 148 LEU 149 -0.0414

LEU 149 LEU 149 -0.0001

LEU 149 PRO 150 0.0001

PRO 150 PRO 150 -0.0001

PRO 150 ALA 151 -0.0073

ALA 151 ALA 151 0.0001

ALA 151 PHE 152 0.0004

PHE 152 PHE 152 -0.0001

PHE 152 ASP 153 0.0021

ASP 153 ASP 153 -0.0006

ASP 153 ALA 154 0.0000

ALA 154 ALA 154 -0.0005

ALA 154 LEU 155 -0.0775

LEU 155 LEU 155 0.0008

LEU 155 GLY 156 0.0002

GLY 156 GLY 156 -0.0004

GLY 156 GLN 157 0.1213

GLN 157 GLN 157 0.0001

GLN 157 TRP 158 -0.0001

TRP 158 TRP 158 -0.0001

TRP 158 THR 159 0.0081

THR 159 THR 159 0.0006

THR 159 PRO 160 0.0004

PRO 160 PRO 160 0.0002

PRO 160 GLY 161 0.0357

GLY 161 GLY 161 0.0000

GLY 161 TYR 162 0.0003

TYR 162 TYR 162 -0.0002

TYR 162 LYS 163 0.0727

LYS 163 LYS 163 -0.0008

LYS 163 PRO 164 0.0005

PRO 164 PRO 164 0.0000

PRO 164 ASN 165 -0.1351

ASN 165 ASN 165 -0.0002

ASN 165 PRO 166 0.0001

PRO 166 PRO 166 0.0005

PRO 166 GLU 167 -0.0162

GLU 167 GLU 167 0.0001

GLU 167 ILE 168 0.0003

ILE 168 ILE 168 0.0002

ILE 168 TYR 169 -0.0067

TYR 169 TYR 169 0.0003

TYR 169 VAL 170 0.0000

VAL 170 VAL 170 0.0002

VAL 170 GLN 171 0.0199

GLN 171 GLN 171 0.0003

GLN 171 LEU 172 0.0001

LEU 172 LEU 172 -0.0003

LEU 172 ILE 173 -0.0375

ILE 173 ILE 173 0.0001

ILE 173 LYS 174 -0.0003

LYS 174 LYS 174 -0.0001

LYS 174 GLU 175 -0.0085

GLU 175 GLU 175 0.0004

GLU 175 CYS 176 -0.0003

CYS 176 CYS 176 -0.0004

CYS 176 LYS 177 -0.0078

LYS 177 LYS 177 0.0002

LYS 177 SER 178 0.0001

SER 178 SER 178 -0.0003

SER 178 ARG 179 -0.0315

ARG 179 ARG 179 -0.0001

ARG 179 GLY 180 -0.0004

GLY 180 GLY 180 0.0000

GLY 180 LYS 181 -0.0486

LYS 181 LYS 181 -0.0004

LYS 181 GLU 182 0.0003

GLU 182 GLU 182 -0.0000

GLU 182 GLY 183 -0.0434

GLY 183 GLY 183 0.0001

GLY 183 GLU 184 -0.0002

GLU 184 GLU 184 -0.0004

GLU 184 PHE 185 -0.0103

PHE 185 PHE 185 -0.0004

PHE 185 SER 186 -0.0002

SER 186 SER 186 -0.0003

SER 186 THR 187 -0.0721

THR 187 THR 187 0.0000

THR 187 CYS 188 0.0006

CYS 188 CYS 188 -0.0003

CYS 188 PHE 189 0.0118

PHE 189 PHE 189 0.0002

PHE 189 THR 190 0.0003

THR 190 THR 190 0.0004

THR 190 GLU 191 0.0451

GLU 191 GLU 191 -0.0003

GLU 191 LEU 192 0.0005

LEU 192 LEU 192 0.0005

LEU 192 GLN 193 -0.0078

GLN 193 GLN 193 0.0001

GLN 193 ARG 194 0.0003

ARG 194 ARG 194 0.1147

ARG 194 ARG 194 0.0002

ARG 194 ASP 195 0.0212

ASP 195 ASP 195 0.0003

ASP 195 PHE 196 -0.0006

PHE 196 PHE 196 -0.0000

PHE 196 LEU 197 -0.0617

LEU 197 LEU 197 -0.0003

LEU 197 ARG 198 -0.0002

ARG 198 ARG 198 -0.0002

ARG 198 ASN 199 -0.0240

ASN 199 ASN 199 -0.0002

ASN 199 ARG 200 -0.0006

ARG 200 ARG 200 0.0001

ARG 200 PRO 201 -0.0814

PRO 201 PRO 201 0.0003

PRO 201 THR 202 0.0008

THR 202 THR 202 -0.0003

THR 202 LYS 203 0.0453

LYS 203 LYS 203 -0.0001

LYS 203 LEU 204 0.0000

LEU 204 LEU 204 -0.0001

LEU 204 LYS 205 0.0647

LYS 205 LYS 205 -0.0006

LYS 205 SER 206 0.0001

SER 206 SER 206 -0.0004

SER 206 LEU 207 0.0154

LEU 207 LEU 207 0.0001

LEU 207 ILE 208 -0.0001

ILE 208 ILE 208 -0.0000

ILE 208 ARG 209 -0.0261

ARG 209 ARG 209 -0.0002

ARG 209 LEU 210 0.0003

LEU 210 LEU 210 0.0004

LEU 210 VAL 211 0.0001

VAL 211 VAL 211 -0.0002

VAL 211 LYS 212 0.0002

LYS 212 LYS 212 0.0005

LYS 212 HIS 213 0.0816

HIS 213 HIS 213 0.0004

HIS 213 TRP 214 -0.0003

TRP 214 TRP 214 0.0002

TRP 214 TYR 215 0.0741

TYR 215 TYR 215 0.0003

TYR 215 GLN 216 -0.0001

GLN 216 GLN 216 0.0001

GLN 216 THR 217 0.0573

THR 217 THR 217 0.0002

THR 217 CYS 218 -0.0001

CYS 218 CYS 218 -0.0002

CYS 218 LYS 219 0.0190

LYS 219 LYS 219 0.0000

LYS 219 LYS 220 0.0004

LYS 220 LYS 220 0.0005

LYS 220 THR 221 -0.0014

THR 221 THR 221 0.0001

THR 221 HIS 222 -0.0004

HIS 222 HIS 222 -0.0003

HIS 222 GLY 223 0.0019

GLY 223 GLY 223 0.0000

GLY 223 ASN 224 -0.0005

ASN 224 ASN 224 0.0005

ASN 224 LYS 225 -0.0218

LYS 225 LYS 225 -0.0005

LYS 225 LEU 226 0.0006

LEU 226 LEU 226 -0.0001

LEU 226 PRO 227 0.0837

PRO 227 PRO 227 0.0001

PRO 227 PRO 228 0.0001

PRO 228 PRO 228 0.0004

PRO 228 GLN 229 -0.1062

GLN 229 GLN 229 -0.0002

GLN 229 TYR 230 -0.0003

TYR 230 TYR 230 0.0001

TYR 230 ALA 231 0.0153

ALA 231 ALA 231 -0.0003

ALA 231 LEU 232 0.0001

LEU 232 LEU 232 0.0005

LEU 232 GLU 233 0.0131

GLU 233 GLU 233 -0.0002

GLU 233 LEU 234 -0.0001

LEU 234 LEU 234 -0.0001

LEU 234 LEU 235 0.0082

LEU 235 LEU 235 0.0002

LEU 235 THR 236 -0.0006

THR 236 THR 236 0.0001

THR 236 VAL 237 -0.0410

VAL 237 VAL 237 -0.0007

VAL 237 TYR 238 0.0002

TYR 238 TYR 238 0.0002

TYR 238 ALA 239 -0.0669

ALA 239 ALA 239 0.0001

ALA 239 TRP 240 -0.0003

TRP 240 TRP 240 0.0003

TRP 240 GLU 241 -0.0475

GLU 241 GLU 241 -0.0000

GLU 241 GLN 242 0.0004

GLN 242 GLN 242 0.0001

GLN 242 GLY 243 -0.0184

GLY 243 GLY 243 -0.0002

GLY 243 SER 244 -0.0006

SER 244 SER 244 0.0003

SER 244 ARG 245 -0.0085

ARG 245 ARG 245 -0.0002

ARG 245 LYS 246 -0.0004

LYS 246 LYS 246 -0.0001

LYS 246 THR 247 -0.0003

THR 247 THR 247 -0.0002

THR 247 ASP 248 0.0005

ASP 248 ASP 248 -0.0000

ASP 248 PHE 249 -0.0143

PHE 249 PHE 249 -0.0008

PHE 249 SER 250 0.0000

SER 250 SER 250 0.0006

SER 250 THR 251 0.0154

THR 251 THR 251 0.0004

THR 251 ALA 252 0.0005

ALA 252 ALA 252 -0.0002

ALA 252 GLN 253 -0.0097

GLN 253 GLN 253 0.0002

GLN 253 GLY 254 -0.0001

GLY 254 GLY 254 -0.0005

GLY 254 PHE 255 -0.0229

PHE 255 PHE 255 -0.0006

PHE 255 GLN 256 -0.0007

GLN 256 GLN 256 0.0001

GLN 256 THR 257 -0.0230

THR 257 THR 257 -0.0002

THR 257 VAL 258 0.0003

VAL 258 VAL 258 0.0000

VAL 258 LEU 259 0.0028

LEU 259 LEU 259 -0.0001

LEU 259 GLU 260 -0.0001

GLU 260 GLU 260 0.0002

GLU 260 LEU 261 0.0036

LEU 261 LEU 261 -0.0001

LEU 261 VAL 262 -0.0004

VAL 262 VAL 262 0.0003

VAL 262 LEU 263 0.0157

LEU 263 LEU 263 0.0008

LEU 263 LYS 264 0.0001

LYS 264 LYS 264 -0.0007

LYS 264 HIS 265 -0.0228

HIS 265 HIS 265 0.0001

HIS 265 GLN 266 -0.0004

GLN 266 GLN 266 -0.0001

GLN 266 LYS 267 -0.0117

LYS 267 LYS 267 0.0001

LYS 267 LEU 268 -0.0003

LEU 268 LEU 268 0.0004

LEU 268 CYS 269 -0.0264

CYS 269 CYS 269 0.0002

CYS 269 ILE 270 -0.0002

ILE 270 ILE 270 0.0003

ILE 270 PHE 271 0.0024

PHE 271 PHE 271 -0.0004

PHE 271 TRP 272 -0.0003

TRP 272 TRP 272 0.0006

TRP 272 GLU 273 0.0880

GLU 273 GLU 273 -0.0004

GLU 273 ALA 274 -0.0003

ALA 274 ALA 274 -0.0004

ALA 274 TYR 275 0.0240

TYR 275 TYR 275 -0.0004

TYR 275 TYR 276 0.0002

TYR 276 TYR 276 -0.0000

TYR 276 ASP 277 0.0427

ASP 277 ASP 277 0.0002

ASP 277 PHE 278 0.0002

PHE 278 PHE 278 0.0003

PHE 278 THR 279 -0.0412

THR 279 THR 279 -0.0004

THR 279 ASN 280 -0.0001

ASN 280 ASN 280 -0.0001

ASN 280 PRO 281 0.0111

PRO 281 PRO 281 -0.0008

PRO 281 VAL 282 -0.0005

VAL 282 VAL 282 0.0001

VAL 282 VAL 283 -0.0089

VAL 283 VAL 283 0.0005

VAL 283 GLY 284 0.0002

GLY 284 GLY 284 0.0003

GLY 284 ARG 285 -0.0367

ARG 285 ARG 285 -0.0001

ARG 285 CYS 286 -0.0001

CYS 286 CYS 286 -0.0007

CYS 286 MET 287 0.0117

MET 287 MET 287 0.0003

MET 287 LEU 288 0.0002

LEU 288 LEU 288 0.0007

LEU 288 GLN 289 -0.0142

GLN 289 GLN 289 0.0005

GLN 289 GLN 290 0.0001

GLN 290 GLN 290 0.0002

GLN 290 LEU 291 0.0184

LEU 291 LEU 291 0.0003

LEU 291 LYS 292 -0.0002

LYS 292 LYS 292 0.0007

LYS 292 LYS 293 -0.0170

LYS 293 LYS 293 0.0004

LYS 293 PRO 294 0.0000

PRO 294 PRO 294 -0.0001

PRO 294 ARG 295 0.1497

ARG 295 ARG 295 0.0000

ARG 295 PRO 296 0.0003

PRO 296 PRO 296 -0.0006

PRO 296 VAL 297 0.0196

VAL 297 VAL 297 -0.0006

VAL 297 ILE 298 0.0002

ILE 298 ILE 298 -0.0002

ILE 298 LEU 299 0.0735

LEU 299 LEU 299 0.0001

LEU 299 ASP 300 0.0002

ASP 300 ASP 300 0.0001

ASP 300 PRO 301 0.0383

PRO 301 PRO 301 0.0004

PRO 301 ALA 302 -0.0004

ALA 302 ALA 302 0.0004

ALA 302 ASP 303 -0.0131

ASP 303 ASP 303 0.0003

ASP 303 PRO 304 0.0003

PRO 304 PRO 304 -0.0003

PRO 304 THR 305 -0.0438

THR 305 THR 305 -0.0006

THR 305 GLY 306 0.0001

GLY 306 GLY 306 -0.0006

GLY 306 ASN 307 0.0867

ASN 307 ASN 307 -0.0001

ASN 307 VAL 308 0.0006

VAL 308 VAL 308 -0.0004

VAL 308 GLY 309 0.0086

GLY 309 GLY 309 -0.0006

GLY 309 GLY 310 0.0000

GLY 310 GLY 310 -0.0003

GLY 310 GLY 311 -0.1210

GLY 311 GLY 311 0.0001

GLY 311 ASP 312 -0.0003

ASP 312 ASP 312 -0.0001

ASP 312 THR 313 -0.0091

THR 313 THR 313 -0.0006

THR 313 HIS 314 0.0002

HIS 314 HIS 314 0.0001

HIS 314 SER 315 0.0116

SER 315 SER 315 0.0003

SER 315 TRP 316 0.0005

TRP 316 TRP 316 0.0000

TRP 316 GLN 317 0.0097

GLN 317 GLN 317 0.0005

GLN 317 ARG 318 -0.0002

ARG 318 ARG 318 0.0004

ARG 318 LEU 319 -0.0166

LEU 319 LEU 319 0.0000

LEU 319 ALA 320 0.0003

ALA 320 ALA 320 0.0007

ALA 320 GLN 321 -0.0271

GLN 321 GLN 321 -0.0003

GLN 321 GLU 322 -0.0004

GLU 322 GLU 322 0.0006

GLU 322 ALA 323 -0.0082

ALA 323 ALA 323 0.0002

ALA 323 ARG 324 0.0001

ARG 324 ARG 324 0.0001

ARG 324 VAL 325 -0.0226

VAL 325 VAL 325 -0.0004

VAL 325 TRP 326 -0.0002

TRP 326 TRP 326 0.0003

TRP 326 LEU 327 0.0080

LEU 327 LEU 327 0.0000

LEU 327 GLY 328 -0.0000

GLY 328 GLY 328 -0.0000

GLY 328 TYR 329 -0.0035

TYR 329 TYR 329 0.0004

TYR 329 PRO 330 -0.0002

PRO 330 PRO 330 0.0002

PRO 330 CYS 331 0.0109

CYS 331 CYS 331 -0.0004

CYS 331 CYS 332 0.0001

CYS 332 CYS 332 0.0000

CYS 332 LYS 333 -0.0104

LYS 333 LYS 333 -0.0002

LYS 333 ASN 334 -0.0001

ASN 334 ASN 334 0.0003

ASN 334 LEU 335 0.0806

LEU 335 LEU 335 -0.0004

LEU 335 ASP 336 -0.0003

ASP 336 ASP 336 -0.0001

ASP 336 GLY 337 0.0645

GLY 337 GLY 337 0.0004

GLY 337 SER 338 -0.0001

SER 338 SER 338 0.0006

SER 338 LEU 339 0.0117

LEU 339 LEU 339 -0.0003

LEU 339 VAL 340 0.0001

VAL 340 VAL 340 0.0004

VAL 340 GLY 341 -0.0031

GLY 341 GLY 341 -0.0002

GLY 341 ALA 342 -0.0004

ALA 342 ALA 342 0.0000

ALA 342 TRP 343 -0.0727

TRP 343 TRP 343 0.0002

TRP 343 THR 344 0.0003

THR 344 THR 344 0.0001

THR 344 MET 345 0.0139

MET 345 MET 345 -0.0004

MET 345 LEU 346 0.0001

LEU 346 LEU 346 0.0006

LEU 346 GLN 347 0.0049

GLN 347 GLN 347 0.0003

GLN 347 LYS 348 0.0003

LYS 348 LYS 348 0.0001

LYS 348 ILE 349 0.0928

ILE 349 ILE 349 -0.0003

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 8 ---

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

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