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

* *

CA strain for 240507033556759822

--- 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
SER 1 GLY 2 -0.0003

GLY 2 PHE 3 0.0005

PHE 3 LYS 4 -0.0002

LYS 4 LYS 5 -0.0000

LYS 5 LEU 6 0.0085

LEU 6 VAL 7 0.0000

VAL 7 SER 8 -0.0000

SER 8 PRO 9 -0.0000

PRO 9 SER 10 0.0001

SER 10 SER 11 0.0048

SER 11 ALA 12 0.0000

ALA 12 VAL 13 -0.0003

VAL 13 GLU 14 -0.0001

GLU 14 LYS 15 0.0002

LYS 15 CYS 16 0.0325

CYS 16 ILE 17 0.0002

ILE 17 VAL 18 -0.0001

VAL 18 SER 19 0.0001

SER 19 VAL 20 0.0000

VAL 20 SER 21 0.0089

SER 21 TYR 22 0.0003

TYR 22 ARG 23 -0.0001

ARG 23 GLY 24 0.0002

GLY 24 ASN 25 0.0001

ASN 25 ASN 26 0.0097

ASN 26 LEU 27 -0.0001

LEU 27 ASN 28 0.0004

ASN 28 GLY 29 0.0002

GLY 29 LEU 30 0.0001

LEU 30 TRP 31 -0.0048

TRP 31 LEU 32 0.0000

LEU 32 GLY 33 0.0000

GLY 33 ASP 34 0.0001

ASP 34 SER 35 0.0000

SER 35 ILE 36 -0.0006

ILE 36 TYR 37 -0.0002

TYR 37 CYS 38 -0.0002

CYS 38 PRO 39 0.0000

PRO 39 ARG 40 -0.0001

ARG 40 HIS 41 0.0046

HIS 41 VAL 42 0.0000

VAL 42 LEU 43 0.0001

LEU 43 GLY 44 -0.0003

GLY 44 LYS 45 0.0003

LYS 45 PHE 46 0.0067

PHE 46 SER 47 -0.0002

SER 47 GLY 48 -0.0003

GLY 48 ASP 49 0.0000

ASP 49 GLN 50 0.0005

GLN 50 TRP 51 0.0542

TRP 51 GLY 52 -0.0002

GLY 52 ASP 53 0.0001

ASP 53 VAL 54 -0.0000

VAL 54 LEU 55 0.0001

LEU 55 ASN 56 -0.0196

ASN 56 LEU 57 0.0001

LEU 57 ALA 58 0.0000

ALA 58 ASN 59 0.0001

ASN 59 ASN 60 -0.0000

ASN 60 HIS 61 0.0077

HIS 61 GLU 62 0.0001

GLU 62 PHE 63 0.0002

PHE 63 GLU 64 0.0002

GLU 64 VAL 65 0.0004

VAL 65 VAL 66 0.0143

VAL 66 THR 67 0.0000

THR 67 GLN 68 -0.0001

GLN 68 ASN 69 0.0002

ASN 69 GLY 70 0.0001

GLY 70 VAL 71 0.0002

VAL 71 THR 72 0.0000

THR 72 LEU 73 0.0002

LEU 73 ASN 74 -0.0001

ASN 74 VAL 75 0.0000

VAL 75 VAL 76 0.0014

VAL 76 SER 77 0.0004

SER 77 ARG 78 -0.0004

ARG 78 ARG 79 0.0004

ARG 79 LEU 80 -0.0003

LEU 80 LYS 81 -0.0184

LYS 81 GLY 82 0.0004

GLY 82 ALA 83 -0.0001

ALA 83 VAL 84 0.0001

VAL 84 LEU 85 0.0004

LEU 85 ILE 86 0.0030

ILE 86 LEU 87 0.0001

LEU 87 GLN 88 -0.0000

GLN 88 THR 89 -0.0000

THR 89 ALA 90 -0.0001

ALA 90 VAL 91 0.0070

VAL 91 ALA 92 -0.0003

ALA 92 ASN 93 -0.0001

ASN 93 ALA 94 0.0000

ALA 94 GLU 95 0.0002

GLU 95 THR 96 0.0020

THR 96 PRO 97 0.0003

PRO 97 LYS 98 -0.0001

LYS 98 TYR 99 0.0002

TYR 99 LYS 100 -0.0000

LYS 100 PHE 101 0.0056

PHE 101 VAL 102 0.0000

VAL 102 LYS 103 0.0005

LYS 103 ALA 104 -0.0002

ALA 104 ASN 105 -0.0001

ASN 105 CYS 106 -0.0221

CYS 106 GLY 107 -0.0002

GLY 107 ASP 108 0.0002

ASP 108 SER 109 -0.0001

SER 109 PHE 110 -0.0003

PHE 110 THR 111 0.0041

THR 111 ILE 112 0.0005

ILE 112 ALA 113 -0.0000

ALA 113 CYS 114 0.0001

CYS 114 SER 115 -0.0001

SER 115 TYR 116 -0.0072

TYR 116 GLY 117 0.0003

GLY 117 GLY 118 0.0003

GLY 118 THR 119 -0.0001

THR 119 VAL 120 0.0000

VAL 120 ILE 121 0.0019

ILE 121 GLY 122 0.0002

GLY 122 LEU 123 -0.0001

LEU 123 TYR 124 -0.0000

TYR 124 PRO 125 -0.0001

PRO 125 VAL 126 0.0111

VAL 126 THR 127 -0.0001

THR 127 MET 128 -0.0000

MET 128 ARG 129 -0.0000

ARG 129 SER 130 0.0001

SER 130 ASN 131 -0.0122

ASN 131 GLY 132 -0.0002

GLY 132 THR 133 0.0000

THR 133 ILE 134 -0.0002

ILE 134 ARG 135 0.0003

ARG 135 ALA 136 0.0013

ALA 136 SER 137 -0.0003

SER 137 PHE 138 0.0002

PHE 138 LEU 139 0.0000

LEU 139 ALA 140 -0.0005

ALA 140 GLY 141 -0.0068

GLY 141 ALA 142 0.0001

ALA 142 CYS 143 0.0002

CYS 143 GLY 144 -0.0001

GLY 144 SER 145 0.0000

SER 145 VAL 146 0.0009

VAL 146 GLY 147 0.0002

GLY 147 PHE 148 -0.0004

PHE 148 ASN 149 -0.0002

ASN 149 ILE 150 -0.0001

ILE 150 GLU 151 -0.0003

GLU 151 LYS 152 -0.0001

LYS 152 GLY 153 -0.0000

GLY 153 VAL 154 0.0000

VAL 154 VAL 155 -0.0002

VAL 155 ASN 156 0.0052

ASN 156 PHE 157 0.0000

PHE 157 PHE 158 0.0002

PHE 158 TYR 159 0.0000

TYR 159 MET 160 0.0001

MET 160 HIS 161 0.0138

HIS 161 HIS 162 -0.0002

HIS 162 LEU 163 0.0003

LEU 163 GLU 164 -0.0003

GLU 164 LEU 165 0.0001

LEU 165 PRO 166 0.0061

PRO 166 ASN 167 0.0001

ASN 167 ALA 168 -0.0001

ALA 168 LEU 169 0.0001

LEU 169 HIS 170 0.0001

HIS 170 THR 171 0.0044

THR 171 GLY 172 -0.0000

GLY 172 THR 173 -0.0001

THR 173 ASP 174 0.0000

ASP 174 LEU 175 0.0004

LEU 175 MET 176 0.0029

MET 176 GLY 177 0.0003

GLY 177 GLU 178 0.0003

GLU 178 PHE 179 0.0003

PHE 179 TYR 180 -0.0001

TYR 180 GLY 181 0.0148

GLY 181 GLY 182 -0.0003

GLY 182 TYR 183 0.0000

TYR 183 VAL 184 0.0000

VAL 184 ASP 185 -0.0002

ASP 185 GLU 186 0.0317

GLU 186 GLU 187 -0.0004

GLU 187 VAL 188 -0.0002

VAL 188 ALA 189 0.0001

ALA 189 GLN 190 -0.0001

GLN 190 ARG 191 -0.0415

ARG 191 VAL 192 0.0001

VAL 192 PRO 193 -0.0003

PRO 193 PRO 194 0.0000

PRO 194 ASP 195 0.0002

ASP 195 ASN 196 -0.0236

ASN 196 LEU 197 0.0000

LEU 197 VAL 198 0.0003

VAL 198 THR 199 0.0001

THR 199 ASN 200 0.0003

ASN 200 ASN 201 0.0011

ASN 201 ILE 202 -0.0005

ILE 202 VAL 203 0.0001

VAL 203 ALA 204 -0.0000

ALA 204 TRP 205 -0.0001

TRP 205 LEU 206 -0.0029

LEU 206 TYR 207 0.0004

TYR 207 ALA 208 0.0001

ALA 208 ALA 209 0.0000

ALA 209 ILE 210 0.0000

ILE 210 ILE 211 0.0000

ILE 211 SER 212 -0.0000

SER 212 VAL 213 -0.0001

VAL 213 SER 219 0.0004

SER 219 GLN 220 0.0004

GLN 220 PRO 221 -0.0004

PRO 221 LYS 222 0.0002

LYS 222 TRP 223 0.0002

TRP 223 LEU 224 0.0025

LEU 224 GLU 225 0.0005

GLU 225 SER 226 -0.0003

SER 226 THR 227 0.0004

THR 227 THR 228 0.0001

THR 228 VAL 229 0.0001

VAL 229 SER 230 0.0003

SER 230 ILE 231 -0.0000

ILE 231 GLU 232 -0.0000

GLU 232 ASP 233 -0.0003

ASP 233 TYR 234 -0.0018

TYR 234 ASN 235 0.0001

ASN 235 ARG 236 0.0002

ARG 236 TRP 237 -0.0000

TRP 237 ALA 238 -0.0003

ALA 238 SER 239 -0.0032

SER 239 ASP 240 0.0002

ASP 240 ASN 241 -0.0001

ASN 241 GLY 242 0.0002

GLY 242 PHE 243 -0.0004

PHE 243 THR 244 -0.0043

THR 244 PRO 245 -0.0002

PRO 245 PHE 246 0.0004

PHE 246 SER 247 0.0000

SER 247 THR 248 0.0000

THR 248 SER 249 -0.0058

SER 249 THR 250 0.0003

THR 250 ALA 251 0.0003

ALA 251 ILE 252 0.0003

ILE 252 THR 253 -0.0003

THR 253 LYS 254 0.0002

LYS 254 LEU 255 -0.0001

LEU 255 SER 256 -0.0004

SER 256 ALA 257 0.0002

ALA 257 ILE 258 -0.0001

ILE 258 THR 259 0.0007

THR 259 GLY 260 -0.0000

GLY 260 VAL 261 -0.0000

VAL 261 ASP 262 -0.0002

ASP 262 VAL 263 -0.0000

VAL 263 CYS 264 -0.0002

CYS 264 LYS 265 0.0000

LYS 265 LEU 266 -0.0001

LEU 266 LEU 267 -0.0002

LEU 267 ARG 268 -0.0001

ARG 268 THR 269 0.0065

THR 269 ILE 270 0.0001

ILE 270 MET 271 -0.0001

MET 271 VAL 272 0.0003

VAL 272 LYS 273 0.0000

LYS 273 SER 274 -0.0041

SER 274 ALA 275 -0.0002

ALA 275 GLN 276 0.0001

GLN 276 TRP 277 -0.0000

TRP 277 GLY 278 -0.0000

GLY 278 SER 279 -0.0033

SER 279 ASP 280 0.0001

ASP 280 PRO 281 -0.0001

PRO 281 ILE 282 0.0001

ILE 282 LEU 283 0.0003

LEU 283 GLY 284 0.0064

GLY 284 GLN 285 -0.0001

GLN 285 TYR 286 0.0001

TYR 286 ASN 287 -0.0001

ASN 287 PHE 288 -0.0000

PHE 288 GLU 289 -0.0014

GLU 289 ASP 290 0.0002

ASP 290 GLU 291 -0.0001

GLU 291 LEU 292 -0.0000

LEU 292 THR 293 -0.0002

THR 293 PRO 294 -0.0024

PRO 294 GLU 295 0.0001

GLU 295 SER 296 0.0002

SER 296 VAL 297 0.0002

VAL 297 PHE 298 -0.0003

PHE 298 ASN 299 -0.0004

ASN 299 GLN 300 0.0002

GLN 300 VAL 301 -0.0001

VAL 301 SER 0 -0.0024

SER 0 SER 1 -0.0002

SER 1 GLY 2 -0.0002

GLY 2 PHE 3 0.0002

PHE 3 LYS 4 -0.0003

LYS 4 LYS 5 -0.0178

LYS 5 LEU 6 0.0005

LEU 6 VAL 7 -0.0004

VAL 7 SER 8 -0.0001

SER 8 PRO 9 -0.0000

PRO 9 SER 10 0.0069

SER 10 SER 11 -0.0003

SER 11 ALA 12 -0.0000

ALA 12 VAL 13 0.0000

VAL 13 GLU 14 0.0002

GLU 14 LYS 15 0.0037

LYS 15 CYS 16 -0.0003

CYS 16 ILE 17 0.0002

ILE 17 VAL 18 -0.0004

VAL 18 SER 19 0.0004

SER 19 VAL 20 0.0109

VAL 20 SER 21 0.0003

SER 21 TYR 22 -0.0000

TYR 22 ARG 23 -0.0001

ARG 23 GLY 24 0.0001

GLY 24 ASN 25 0.0003

ASN 25 ASN 26 0.0004

ASN 26 LEU 27 -0.0000

LEU 27 ASN 28 0.0001

ASN 28 GLY 29 0.0001

GLY 29 LEU 30 -0.0045

LEU 30 TRP 31 -0.0005

TRP 31 LEU 32 0.0002

LEU 32 GLY 33 0.0001

GLY 33 ASP 34 0.0003

ASP 34 SER 35 -0.0024

SER 35 ILE 36 -0.0001

ILE 36 TYR 37 0.0001

TYR 37 CYS 38 0.0002

CYS 38 PRO 39 -0.0002

PRO 39 ARG 40 0.0042

ARG 40 HIS 41 0.0002

HIS 41 VAL 42 -0.0005

VAL 42 LEU 43 0.0002

LEU 43 GLY 44 0.0000

GLY 44 LYS 45 -0.0059

LYS 45 PHE 46 -0.0004

PHE 46 SER 47 -0.0001

SER 47 GLY 48 -0.0000

GLY 48 ASP 49 0.0001

ASP 49 GLN 50 -0.0015

GLN 50 TRP 51 0.0001

TRP 51 GLY 52 0.0001

GLY 52 ASP 53 -0.0003

ASP 53 VAL 54 -0.0005

VAL 54 LEU 55 -0.0003

LEU 55 ASN 56 0.0000

ASN 56 LEU 57 -0.0001

LEU 57 ALA 58 -0.0003

ALA 58 ASN 59 0.0000

ASN 59 ASN 60 0.0017

ASN 60 HIS 61 0.0004

HIS 61 GLU 62 -0.0002

GLU 62 PHE 63 -0.0002

PHE 63 GLU 64 0.0001

GLU 64 VAL 65 0.0079

VAL 65 VAL 66 -0.0000

VAL 66 THR 67 -0.0001

THR 67 GLN 68 0.0001

GLN 68 ASN 69 0.0004

ASN 69 GLY 70 0.0032

GLY 70 VAL 71 -0.0000

VAL 71 THR 72 -0.0004

THR 72 LEU 73 0.0002

LEU 73 ASN 74 -0.0001

ASN 74 VAL 75 -0.0022

VAL 75 VAL 76 -0.0002

VAL 76 SER 77 0.0003

SER 77 ARG 78 -0.0005

ARG 78 ARG 79 0.0001

ARG 79 LEU 80 -0.0098

LEU 80 LYS 81 0.0001

LYS 81 GLY 82 -0.0001

GLY 82 ALA 83 -0.0002

ALA 83 VAL 84 0.0004

VAL 84 LEU 85 -0.0111

LEU 85 ILE 86 -0.0002

ILE 86 LEU 87 0.0001

LEU 87 GLN 88 0.0000

GLN 88 THR 89 -0.0000

THR 89 ALA 90 -0.0053

ALA 90 VAL 91 -0.0000

VAL 91 ALA 92 0.0002

ALA 92 ASN 93 -0.0004

ASN 93 ALA 94 0.0003

ALA 94 GLU 95 0.0084

GLU 95 THR 96 -0.0000

THR 96 PRO 97 -0.0003

PRO 97 LYS 98 -0.0001

LYS 98 TYR 99 0.0004

TYR 99 LYS 100 0.0040

LYS 100 PHE 101 -0.0002

PHE 101 VAL 102 0.0003

VAL 102 LYS 103 -0.0002

LYS 103 ALA 104 -0.0001

ALA 104 ASN 105 -0.0178

ASN 105 CYS 106 -0.0003

CYS 106 GLY 107 -0.0001

GLY 107 ASP 108 -0.0002

ASP 108 SER 109 -0.0000

SER 109 PHE 110 -0.0047

PHE 110 THR 111 -0.0002

THR 111 ILE 112 0.0003

ILE 112 ALA 113 0.0003

ALA 113 CYS 114 -0.0001

CYS 114 SER 115 -0.0057

SER 115 TYR 116 0.0002

TYR 116 GLY 117 -0.0000

GLY 117 GLY 118 0.0000

GLY 118 THR 119 0.0001

THR 119 VAL 120 0.0112

VAL 120 ILE 121 0.0002

ILE 121 GLY 122 -0.0001

GLY 122 LEU 123 -0.0000

LEU 123 TYR 124 0.0002

TYR 124 PRO 125 0.0084

PRO 125 VAL 126 -0.0005

VAL 126 THR 127 0.0001

THR 127 MET 128 -0.0002

MET 128 ARG 129 -0.0000

ARG 129 SER 130 0.0073

SER 130 ASN 131 -0.0002

ASN 131 GLY 132 -0.0001

GLY 132 THR 133 0.0002

THR 133 ILE 134 -0.0001

ILE 134 ARG 135 -0.0037

ARG 135 ALA 136 0.0001

ALA 136 SER 137 -0.0001

SER 137 PHE 138 -0.0001

PHE 138 LEU 139 -0.0002

LEU 139 ALA 140 0.0012

ALA 140 GLY 141 0.0000

GLY 141 ALA 142 0.0002

ALA 142 CYS 143 0.0001

CYS 143 GLY 144 0.0001

GLY 144 SER 145 0.0049

SER 145 VAL 146 0.0005

VAL 146 GLY 147 -0.0004

GLY 147 PHE 148 -0.0001

PHE 148 ASN 149 0.0004

ASN 149 ILE 150 -0.0001

ILE 150 GLU 151 -0.0001

GLU 151 LYS 152 0.0001

LYS 152 GLY 153 0.0001

GLY 153 VAL 154 -0.0003

VAL 154 VAL 155 0.0016

VAL 155 ASN 156 0.0001

ASN 156 PHE 157 -0.0002

PHE 157 PHE 158 -0.0001

PHE 158 TYR 159 0.0000

TYR 159 MET 160 -0.0066

MET 160 HIS 161 0.0001

HIS 161 HIS 162 -0.0000

HIS 162 LEU 163 -0.0002

LEU 163 GLU 164 0.0003

GLU 164 LEU 165 0.0001

LEU 165 PRO 166 0.0002

PRO 166 ASN 167 -0.0000

ASN 167 ALA 168 -0.0003

ALA 168 LEU 169 0.0003

LEU 169 HIS 170 0.0009

HIS 170 THR 171 -0.0000

THR 171 GLY 172 0.0002

GLY 172 THR 173 0.0001

THR 173 ASP 174 -0.0004

ASP 174 LEU 175 -0.0039

LEU 175 MET 176 0.0001

MET 176 GLY 177 -0.0000

GLY 177 GLU 178 -0.0001

GLU 178 PHE 179 0.0004

PHE 179 TYR 180 -0.0171

TYR 180 GLY 181 0.0001

GLY 181 GLY 182 -0.0002

GLY 182 TYR 183 0.0002

TYR 183 VAL 184 0.0000

VAL 184 ASP 185 -0.0139

ASP 185 GLU 186 -0.0006

GLU 186 GLU 187 0.0004

GLU 187 VAL 188 -0.0003

VAL 188 ALA 189 0.0001

ALA 189 GLN 190 -0.0155

GLN 190 ARG 191 -0.0000

ARG 191 VAL 192 -0.0001

VAL 192 PRO 193 -0.0000

PRO 193 PRO 194 -0.0001

PRO 194 ASP 195 -0.0068

ASP 195 ASN 196 -0.0000

ASN 196 LEU 197 -0.0002

LEU 197 VAL 198 0.0004

VAL 198 THR 199 -0.0001

THR 199 ASN 200 -0.0011

ASN 200 ASN 201 0.0003

ASN 201 ILE 202 0.0002

ILE 202 VAL 203 -0.0000

VAL 203 ALA 204 -0.0000

ALA 204 TRP 205 -0.0003

TRP 205 LEU 206 0.0002

LEU 206 TYR 207 0.0002

TYR 207 ALA 208 0.0001

ALA 208 ALA 209 0.0000

ALA 209 ILE 210 -0.0190

ILE 210 ILE 211 -0.0002

ILE 211 SER 212 0.0001

SER 212 VAL 213 -0.0000

VAL 213 LYS 214 -0.0004

LYS 214 GLU 215 -0.0214

GLU 215 SER 216 -0.0001

SER 216 SER 217 -0.0000

SER 217 PHE 218 0.0000

PHE 218 SER 219 0.0003

SER 219 GLN 220 -0.2300

GLN 220 PRO 221 -0.0000

PRO 221 LYS 222 0.0001

LYS 222 TRP 223 -0.0004

TRP 223 LEU 224 -0.0003

LEU 224 GLU 225 -0.0165

GLU 225 SER 226 0.0002

SER 226 THR 227 -0.0002

THR 227 THR 228 -0.0001

THR 228 VAL 229 0.0000

VAL 229 SER 230 0.0009

SER 230 ILE 231 -0.0002

ILE 231 GLU 232 0.0003

GLU 232 ASP 233 0.0004

ASP 233 TYR 234 -0.0001

TYR 234 ASN 235 -0.0048

ASN 235 ARG 236 0.0004

ARG 236 TRP 237 0.0004

TRP 237 ALA 238 -0.0002

ALA 238 SER 239 0.0001

SER 239 ASP 240 -0.0014

ASP 240 ASN 241 -0.0002

ASN 241 GLY 242 -0.0001

GLY 242 PHE 243 0.0001

PHE 243 THR 244 0.0001

THR 244 PRO 245 -0.0042

PRO 245 PHE 246 0.0003

PHE 246 SER 247 0.0003

SER 247 THR 248 -0.0003

THR 248 SER 249 0.0001

SER 249 THR 250 0.0101

THR 250 ALA 251 0.0000

ALA 251 ILE 252 -0.0001

ILE 252 THR 253 0.0000

THR 253 LYS 254 -0.0003

LYS 254 LEU 255 -0.0026

LEU 255 SER 256 -0.0001

SER 256 ALA 257 0.0001

ALA 257 ILE 258 0.0002

ILE 258 THR 259 -0.0004

THR 259 GLY 260 -0.0044

GLY 260 VAL 261 0.0005

VAL 261 ASP 262 -0.0003

ASP 262 VAL 263 0.0004

VAL 263 CYS 264 -0.0002

CYS 264 LYS 265 0.0019

LYS 265 LEU 266 -0.0001

LEU 266 LEU 267 -0.0001

LEU 267 ARG 268 0.0000

ARG 268 THR 269 0.0002

THR 269 ILE 270 -0.0133

ILE 270 MET 271 0.0003

MET 271 VAL 272 -0.0001

VAL 272 LYS 273 0.0001

LYS 273 SER 274 -0.0002

SER 274 ALA 275 -0.0034

ALA 275 GLN 276 0.0002

GLN 276 TRP 277 -0.0000

TRP 277 GLY 278 -0.0002

GLY 278 SER 279 -0.0001

SER 279 ASP 280 0.0019

ASP 280 PRO 281 0.0000

PRO 281 ILE 282 -0.0003

ILE 282 LEU 283 -0.0002

LEU 283 GLY 284 -0.0000

GLY 284 GLN 285 -0.0067

GLN 285 TYR 286 -0.0002

TYR 286 ASN 287 -0.0003

ASN 287 PHE 288 0.0001

PHE 288 GLU 289 -0.0003

GLU 289 ASP 290 -0.0131

ASP 290 GLU 291 0.0001

GLU 291 LEU 292 -0.0005

LEU 292 THR 293 0.0000

THR 293 PRO 294 0.0000

PRO 294 GLU 295 0.0097

GLU 295 SER 296 0.0000

SER 296 VAL 297 0.0000

VAL 297 PHE 298 0.0000

PHE 298 ASN 299 -0.0001

ASN 299 GLN 300 0.0080

GLN 300 VAL 301 0.0002

VAL 301 GLY 302 0.0003

GLY 302 GLY 303 -0.0000

GLY 303 VAL 304 0.0001

VAL 304 ARG 305 0.0273

ARG 305 LEU 306 0.0002

LEU 306 LEU 6 -0.1103

LEU 6 VAL 7 -0.0002

VAL 7 SER 8 -0.0000

SER 8 PRO 9 -0.0002

PRO 9 SER 10 0.0003

SER 10 SER 11 -0.0182

SER 11 ALA 12 -0.0004

ALA 12 VAL 13 0.0001

VAL 13 GLU 14 -0.0003

GLU 14 LYS 15 -0.0001

LYS 15 CYS 16 -0.0007

CYS 16 ILE 17 -0.0001

ILE 17 VAL 18 -0.0001

VAL 18 SER 19 -0.0000

SER 19 VAL 20 -0.0002

VAL 20 SER 21 -0.0003

SER 21 TYR 22 -0.0000

TYR 22 ARG 23 -0.0001

ARG 23 GLY 24 0.0000

GLY 24 ASN 25 0.0002

ASN 25 ASN 26 -0.0143

ASN 26 LEU 27 -0.0002

LEU 27 ASN 28 -0.0002

ASN 28 GLY 29 -0.0003

GLY 29 LEU 30 0.0000

LEU 30 TRP 31 -0.0095

TRP 31 LEU 32 -0.0005

LEU 32 GLY 33 0.0002

GLY 33 ASP 34 -0.0002

ASP 34 SER 35 -0.0003

SER 35 ILE 36 -0.0039

ILE 36 TYR 37 -0.0004

TYR 37 CYS 38 0.0002

CYS 38 PRO 39 0.0003

PRO 39 ARG 40 0.0002

ARG 40 HIS 41 0.0100

HIS 41 VAL 42 0.0001

VAL 42 LEU 43 -0.0001

LEU 43 GLY 44 -0.0004

GLY 44 LYS 45 0.0001

LYS 45 PHE 46 -0.0141

PHE 46 SER 47 -0.0000

SER 47 GLY 48 -0.0001

GLY 48 ASP 49 -0.0001

ASP 49 GLN 50 0.0000

GLN 50 TRP 51 0.0057

TRP 51 GLY 52 0.0000

GLY 52 ASP 53 0.0003

ASP 53 VAL 54 0.0001

VAL 54 LEU 55 0.0002

LEU 55 ASN 56 -0.0023

ASN 56 LEU 57 0.0002

LEU 57 ALA 58 -0.0003

ALA 58 ASN 59 0.0002

ASN 59 ASN 60 0.0002

ASN 60 HIS 61 0.0008

HIS 61 GLU 62 -0.0001

GLU 62 PHE 63 0.0001

PHE 63 GLU 64 0.0001

GLU 64 VAL 65 -0.0000

VAL 65 VAL 66 -0.0033

VAL 66 THR 67 0.0001

THR 67 GLN 68 0.0001

GLN 68 ASN 69 -0.0001

ASN 69 GLY 70 0.0000

GLY 70 VAL 71 -0.0019

VAL 71 THR 72 -0.0001

THR 72 LEU 73 -0.0001

LEU 73 ASN 74 -0.0002

ASN 74 VAL 75 0.0001

VAL 75 VAL 76 -0.0052

VAL 76 SER 77 0.0000

SER 77 ARG 78 0.0001

ARG 78 ARG 79 0.0001

ARG 79 LEU 80 0.0001

LEU 80 LYS 81 0.0075

LYS 81 GLY 82 0.0001

GLY 82 ALA 83 -0.0001

ALA 83 VAL 84 0.0003

VAL 84 LEU 85 0.0000

LEU 85 ILE 86 -0.0065

ILE 86 LEU 87 -0.0002

LEU 87 GLN 88 0.0000

GLN 88 THR 89 -0.0003

THR 89 ALA 90 -0.0002

ALA 90 VAL 91 -0.0004

VAL 91 ALA 92 -0.0003

ALA 92 ASN 93 0.0006

ASN 93 ALA 94 -0.0004

ALA 94 GLU 95 0.0002

GLU 95 THR 96 -0.0068

THR 96 PRO 97 -0.0001

PRO 97 LYS 98 -0.0000

LYS 98 TYR 99 -0.0002

TYR 99 LYS 100 0.0002

LYS 100 PHE 101 0.0293

PHE 101 VAL 102 -0.0001

VAL 102 LYS 103 0.0000

LYS 103 ALA 104 0.0001

ALA 104 ASN 105 -0.0003

ASN 105 CYS 106 -0.0086

CYS 106 GLY 107 -0.0001

GLY 107 ASP 108 0.0002

ASP 108 SER 109 0.0002

SER 109 PHE 110 0.0003

PHE 110 THR 111 0.0049

THR 111 ILE 112 0.0004

ILE 112 ALA 113 -0.0002

ALA 113 CYS 114 0.0002

CYS 114 SER 115 -0.0005

SER 115 TYR 116 -0.0066

TYR 116 GLY 117 0.0003

GLY 117 GLY 118 -0.0002

GLY 118 THR 119 0.0004

THR 119 VAL 120 -0.0001

VAL 120 ILE 121 0.0011

ILE 121 GLY 122 -0.0001

GLY 122 LEU 123 -0.0002

LEU 123 TYR 124 0.0004

TYR 124 PRO 125 0.0001

PRO 125 VAL 126 -0.0250

VAL 126 THR 127 0.0002

THR 127 MET 128 0.0003

MET 128 ARG 129 -0.0001

ARG 129 SER 130 -0.0002

SER 130 ASN 131 -0.0260

ASN 131 GLY 132 0.0001

GLY 132 THR 133 0.0002

THR 133 ILE 134 -0.0000

ILE 134 ARG 135 0.0001

ARG 135 ALA 136 -0.0317

ALA 136 SER 137 -0.0001

SER 137 PHE 138 -0.0000

PHE 138 LEU 139 -0.0000

LEU 139 ALA 140 -0.0002

ALA 140 GLY 141 -0.0185

GLY 141 ALA 142 -0.0004

ALA 142 CYS 143 0.0002

CYS 143 GLY 144 0.0002

GLY 144 SER 145 0.0003

SER 145 VAL 146 0.0076

VAL 146 GLY 147 0.0003

GLY 147 PHE 148 -0.0002

PHE 148 ASN 149 0.0001

ASN 149 ILE 150 0.0004

ILE 150 GLU 151 -0.0837

GLU 151 LYS 152 0.0001

LYS 152 GLY 153 0.0002

GLY 153 VAL 154 -0.0000

VAL 154 VAL 155 0.0001

VAL 155 ASN 156 -0.0038

ASN 156 PHE 157 0.0001

PHE 157 PHE 158 0.0001

PHE 158 TYR 159 -0.0002

TYR 159 MET 160 -0.0000

MET 160 HIS 161 0.0257

HIS 161 HIS 162 0.0002

HIS 162 LEU 163 -0.0002

LEU 163 GLU 164 0.0001

GLU 164 LEU 165 0.0003

LEU 165 PRO 166 -0.0193

PRO 166 ASN 167 -0.0000

ASN 167 ALA 168 -0.0001

ALA 168 LEU 169 0.0002

LEU 169 HIS 170 0.0003

HIS 170 THR 171 0.0010

THR 171 GLY 172 -0.0003

GLY 172 THR 173 0.0002

THR 173 ASP 174 -0.0001

ASP 174 LEU 175 0.0004

LEU 175 MET 176 0.0002

MET 176 GLY 177 -0.0003

GLY 177 GLU 178 -0.0002

GLU 178 PHE 179 -0.0002

PHE 179 TYR 180 -0.0003

TYR 180 GLY 181 -0.0004

GLY 181 GLY 182 0.0001

GLY 182 TYR 183 -0.0000

TYR 183 VAL 184 -0.0001

VAL 184 ASP 185 0.0001

ASP 185 GLU 186 -0.0071

GLU 186 GLU 187 -0.0001

GLU 187 VAL 188 0.0004

VAL 188 ALA 189 0.0000

ALA 189 GLN 190 -0.0001

GLN 190 ARG 191 0.0252

ARG 191 VAL 192 -0.0002

VAL 192 PRO 193 -0.0001

PRO 193 PRO 194 -0.0001

PRO 194 ASP 195 0.0002

ASP 195 ASN 196 0.1045

ASN 196 LEU 197 0.0000

LEU 197 VAL 198 -0.0001

VAL 198 THR 199 0.0000

THR 199 ASN 200 0.0002

ASN 200 ASN 201 -0.0021

ASN 201 ILE 202 -0.0000

ILE 202 VAL 203 0.0002

VAL 203 ALA 204 0.0005

ALA 204 TRP 205 -0.0000

TRP 205 LEU 206 -0.0213

LEU 206 TYR 207 -0.0001

TYR 207 ALA 208 -0.0001

ALA 208 ALA 209 0.0002

ALA 209 ILE 210 -0.0004

ILE 210 ILE 211 -0.0057

ILE 211 SER 212 -0.0003

SER 212 VAL 213 -0.0004

VAL 213 LYS 214 -0.0002

LYS 214 GLU 215 0.0003

GLU 215 SER 216 -0.0097

SER 216 SER 217 0.0000

SER 217 PHE 218 -0.0000

PHE 218 SER 219 -0.0003

SER 219 GLN 220 0.0002

GLN 220 PRO 221 -0.0398

PRO 221 LYS 222 0.0000

LYS 222 TRP 223 0.0003

TRP 223 LEU 224 -0.0000

LEU 224 GLU 225 -0.0000

GLU 225 SER 226 -0.0035

SER 226 THR 227 0.0000

THR 227 THR 228 -0.0002

THR 228 VAL 229 -0.0001

VAL 229 SER 230 0.0002

SER 230 ILE 231 0.0090

ILE 231 GLU 232 0.0005

GLU 232 ASP 233 -0.0000

ASP 233 TYR 234 -0.0004

TYR 234 ASN 235 0.0000

ASN 235 ARG 236 0.0014

ARG 236 TRP 237 0.0000

TRP 237 ALA 238 -0.0004

ALA 238 SER 239 -0.0000

SER 239 ASP 240 0.0001

ASP 240 ASN 241 0.0035

ASN 241 GLY 242 -0.0001

GLY 242 PHE 243 0.0002

PHE 243 THR 244 -0.0003

THR 244 PRO 245 0.0000

PRO 245 PHE 246 0.0135

PHE 246 SER 247 0.0000

SER 247 THR 248 0.0002

THR 248 SER 249 0.0000

SER 249 THR 250 0.0002

THR 250 ALA 251 -0.0063

ALA 251 ILE 252 0.0001

ILE 252 THR 253 0.0000

THR 253 LYS 254 -0.0000

LYS 254 LEU 255 0.0002

LEU 255 SER 256 0.0041

SER 256 ALA 257 -0.0004

ALA 257 ILE 258 -0.0002

ILE 258 THR 259 -0.0001

THR 259 GLY 260 -0.0001

GLY 260 VAL 261 -0.1199

VAL 261 ASP 262 0.0004

ASP 262 VAL 263 -0.0003

VAL 263 CYS 264 0.0002

CYS 264 LYS 265 0.0002

LYS 265 LEU 266 -0.0023

LEU 266 LEU 267 -0.0003

LEU 267 ARG 268 0.0001

ARG 268 THR 269 -0.0002

THR 269 ILE 270 -0.0000

ILE 270 MET 271 -0.0011

MET 271 VAL 272 0.0001

VAL 272 LYS 273 0.0001

LYS 273 SER 274 0.0001

SER 274 ALA 275 0.0001

ALA 275 GLN 276 0.0061

GLN 276 TRP 277 -0.0001

TRP 277 GLY 278 -0.0000

GLY 278 SER 279 -0.0000

SER 279 ASP 280 -0.0000

ASP 280 PRO 281 0.0065

PRO 281 ILE 282 -0.0003

ILE 282 LEU 283 0.0003

LEU 283 GLY 284 0.0000

GLY 284 GLN 285 -0.0001

GLN 285 TYR 286 -0.0074

TYR 286 ASN 287 0.0002

ASN 287 PHE 288 -0.0000

PHE 288 GLU 289 -0.0003

GLU 289 ASP 290 -0.0004

ASP 290 GLU 291 -0.0221

GLU 291 LEU 292 0.0001

LEU 292 THR 293 0.0000

THR 293 PRO 294 -0.0001

PRO 294 GLU 295 0.0001

GLU 295 SER 296 0.0054

SER 296 VAL 297 -0.0005

VAL 297 PHE 298 -0.0002

PHE 298 ASN 299 0.0004

ASN 299 GLN 300 0.0001

GLN 300 VAL 301 0.0114

VAL 301 GLY 302 -0.0001

GLY 302 GLY 303 -0.0001

GLY 303 VAL 304 -0.0001

VAL 304 ARG 305 0.0001

ARG 305 LEU 306 0.0490

LEU 306 GLN 307 -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: April 25th, 2023.

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

*** ***

CA strain for 240507033556759822

--- normal mode 10 ---

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

* *