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

* trishna *

CA strain for 22012410212955232

--- 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
SER 5 ARG 6 -0.0003

ARG 6 THR 7 -0.0001

THR 7 ILE 8 -0.0001

ILE 8 GLY 9 -0.0136

GLY 9 ILE 10 -0.0001

ILE 10 ILE 11 0.0004

ILE 11 GLY 12 -0.0002

GLY 12 ALA 13 -0.0161

ALA 13 PRO 14 0.0002

PRO 14 PHE 15 0.0001

PHE 15 SER 16 -0.0001

SER 16 LYS 17 -0.0200

LYS 17 GLY 18 -0.0001

GLY 18 GLN 19 0.0003

GLN 19 PRO 20 -0.0004

PRO 20 ARG 21 -0.0008

ARG 21 GLY 22 0.0004

GLY 22 GLY 23 0.0000

GLY 23 VAL 24 0.0000

VAL 24 GLU 25 0.0109

GLU 25 GLU 26 -0.0000

GLU 26 GLY 27 -0.0004

GLY 27 PRO 28 -0.0003

PRO 28 THR 29 -0.0216

THR 29 VAL 30 -0.0002

VAL 30 LEU 31 -0.0003

LEU 31 ARG 32 0.0001

ARG 32 LYS 33 -0.0060

LYS 33 ALA 34 -0.0000

ALA 34 GLY 35 0.0002

GLY 35 LEU 36 -0.0001

LEU 36 LEU 37 0.0077

LEU 37 GLU 38 0.0000

GLU 38 LYS 39 0.0001

LYS 39 LEU 40 -0.0001

LEU 40 LYS 41 -0.0000

LYS 41 GLU 42 -0.0001

GLU 42 GLN 43 -0.0002

GLN 43 GLU 44 -0.0003

GLU 44 CYS 45 -0.0243

CYS 45 ASP 46 -0.0001

ASP 46 VAL 47 0.0002

VAL 47 LYS 48 0.0000

LYS 48 ASP 49 -0.0203

ASP 49 TYR 50 0.0001

TYR 50 GLY 51 0.0003

GLY 51 ASP 52 -0.0003

ASP 52 LEU 53 -0.0430

LEU 53 PRO 54 -0.0001

PRO 54 PHE 55 -0.0003

PHE 55 ALA 56 0.0002

ALA 56 ASP 57 -0.1236

ASP 57 ILE 58 -0.0001

ILE 58 PRO 59 0.0004

PRO 59 ASN 60 0.0002

ASN 60 ASP 61 0.0364

ASP 61 SER 62 0.0002

SER 62 PRO 63 -0.0000

PRO 63 PHE 64 -0.0004

PHE 64 GLN 65 -0.0177

GLN 65 ILE 66 0.0000

ILE 66 VAL 67 0.0000

VAL 67 LYS 68 0.0002

LYS 68 ASN 69 -0.0201

ASN 69 PRO 70 0.0004

PRO 70 ARG 71 0.0001

ARG 71 SER 72 -0.0001

SER 72 VAL 73 -0.0115

VAL 73 GLY 74 0.0001

GLY 74 LYS 75 0.0000

LYS 75 ALA 76 -0.0001

ALA 76 SER 77 -0.0062

SER 77 GLU 78 -0.0002

GLU 78 GLN 79 0.0007

GLN 79 LEU 80 0.0000

LEU 80 ALA 81 0.0055

ALA 81 GLY 82 -0.0000

GLY 82 LYS 83 -0.0000

LYS 83 VAL 84 -0.0002

VAL 84 ALA 85 0.0038

ALA 85 GLU 86 -0.0004

GLU 86 VAL 87 0.0002

VAL 87 LYS 88 0.0002

LYS 88 LYS 89 0.0015

LYS 89 ASN 90 0.0002

ASN 90 GLY 91 -0.0002

GLY 91 ARG 92 -0.0002

ARG 92 ILE 93 0.0059

ILE 93 SER 94 -0.0002

SER 94 LEU 95 -0.0004

LEU 95 VAL 96 0.0000

VAL 96 LEU 97 0.0160

LEU 97 GLY 98 0.0002

GLY 98 GLY 99 -0.0004

GLY 99 ASP 100 -0.0002

ASP 100 HIS 101 -0.0010

HIS 101 SER 102 -0.0001

SER 102 LEU 103 -0.0001

LEU 103 ALA 104 0.0001

ALA 104 ILE 105 0.0006

ILE 105 GLY 106 -0.0001

GLY 106 SER 107 -0.0000

SER 107 ILE 108 -0.0000

ILE 108 SER 109 0.0011

SER 109 GLY 110 -0.0001

GLY 110 HIS 111 0.0001

HIS 111 ALA 112 -0.0001

ALA 112 ARG 113 0.0037

ARG 113 VAL 114 0.0000

VAL 114 HIS 115 0.0001

HIS 115 PRO 116 0.0001

PRO 116 ASP 117 -0.0021

ASP 117 LEU 118 -0.0000

LEU 118 GLY 119 0.0003

GLY 119 VAL 120 0.0000

VAL 120 ILE 121 -0.0077

ILE 121 TRP 122 -0.0002

TRP 122 VAL 123 0.0002

VAL 123 ASP 124 -0.0000

ASP 124 ALA 125 -0.0065

ALA 125 HIS 126 -0.0002

HIS 126 THR 127 0.0003

THR 127 ASP 128 -0.0002

ASP 128 ILE 129 0.0033

ILE 129 ASN 130 0.0000

ASN 130 THR 131 0.0001

THR 131 PRO 132 -0.0000

PRO 132 LEU 133 0.0026

LEU 133 THR 134 -0.0001

THR 134 THR 135 0.0003

THR 135 THR 136 -0.0000

THR 136 SER 137 -0.0158

SER 137 GLY 138 -0.0003

GLY 138 ASN 139 -0.0002

ASN 139 LEU 140 0.0006

LEU 140 HIS 141 0.0230

HIS 141 GLY 142 0.0002

GLY 142 GLN 143 -0.0001

GLN 143 PRO 144 0.0000

PRO 144 VAL 145 0.0004

VAL 145 SER 146 0.0002

SER 146 PHE 147 -0.0001

PHE 147 LEU 148 -0.0001

LEU 148 LEU 149 0.0002

LEU 149 LYS 150 0.0000

LYS 150 GLU 151 0.0001

GLU 151 LEU 152 0.0000

LEU 152 LYS 153 0.0107

LYS 153 GLY 154 -0.0001

GLY 154 LYS 155 -0.0003

LYS 155 ILE 156 0.0002

ILE 156 PRO 157 0.0173

PRO 157 ASP 158 -0.0000

ASP 158 VAL 159 -0.0000

VAL 159 PRO 160 0.0001

PRO 160 GLY 161 -0.0259

GLY 161 PHE 162 0.0004

PHE 162 SER 163 -0.0001

SER 163 TRP 164 -0.0001

TRP 164 VAL 165 0.0031

VAL 165 THR 166 -0.0002

THR 166 PRO 167 -0.0000

PRO 167 CYS 168 -0.0001

CYS 168 ILE 169 -0.0049

ILE 169 SER 170 -0.0003

SER 170 ALA 171 0.0001

ALA 171 LYS 172 0.0002

LYS 172 ASP 173 0.0044

ASP 173 ILE 174 -0.0004

ILE 174 VAL 175 0.0002

VAL 175 TYR 176 0.0003

TYR 176 ILE 177 -0.0023

ILE 177 GLY 178 -0.0004

GLY 178 LEU 179 -0.0001

LEU 179 ARG 180 0.0001

ARG 180 ASP 181 0.0355

ASP 181 VAL 182 -0.0004

VAL 182 ASP 183 0.0003

ASP 183 PRO 184 -0.0002

PRO 184 GLY 185 -0.0166

GLY 185 GLU 186 -0.0001

GLU 186 HIS 187 0.0004

HIS 187 TYR 188 -0.0002

TYR 188 ILE 189 -0.0039

ILE 189 LEU 190 -0.0001

LEU 190 LYS 191 0.0001

LYS 191 THR 192 -0.0003

THR 192 LEU 193 0.0016

LEU 193 GLY 194 0.0001

GLY 194 ILE 195 -0.0001

ILE 195 LYS 196 -0.0000

LYS 196 TYR 197 -0.0060

TYR 197 PHE 198 0.0002

PHE 198 SER 199 0.0001

SER 199 MET 200 -0.0003

MET 200 THR 201 -0.0060

THR 201 GLU 202 0.0000

GLU 202 VAL 203 0.0001

VAL 203 ASP 204 0.0001

ASP 204 ARG 205 -0.0056

ARG 205 LEU 206 -0.0001

LEU 206 GLY 207 0.0001

GLY 207 ILE 208 -0.0000

ILE 208 GLY 209 -0.0083

GLY 209 LYS 210 0.0002

LYS 210 VAL 211 0.0002

VAL 211 MET 212 0.0001

MET 212 GLU 213 -0.0037

GLU 213 GLU 214 -0.0002

GLU 214 THR 215 0.0002

THR 215 LEU 216 0.0003

LEU 216 SER 217 0.0052

SER 217 TYR 218 -0.0001

TYR 218 LEU 219 -0.0002

LEU 219 LEU 220 0.0001

LEU 220 GLY 221 0.0027

GLY 221 ARG 222 0.0001

ARG 222 LYS 223 0.0002

LYS 223 LYS 224 0.0003

LYS 224 ARG 225 -0.0017

ARG 225 PRO 226 -0.0002

PRO 226 ILE 227 -0.0001

ILE 227 HIS 228 -0.0002

HIS 228 LEU 229 -0.0046

LEU 229 SER 230 0.0002

SER 230 PHE 231 0.0000

PHE 231 ASP 232 -0.0001

ASP 232 VAL 233 -0.0016

VAL 233 ASP 234 0.0000

ASP 234 GLY 235 0.0002

GLY 235 LEU 236 -0.0002

LEU 236 ASP 237 -0.0003

ASP 237 PRO 238 0.0001

PRO 238 SER 239 -0.0001

SER 239 PHE 240 -0.0001

PHE 240 THR 241 -0.0038

THR 241 PRO 242 -0.0002

PRO 242 ALA 243 0.0003

ALA 243 THR 244 -0.0001

THR 244 GLY 245 0.0207

GLY 245 THR 246 -0.0001

THR 246 PRO 247 0.0001

PRO 247 VAL 248 0.0001

VAL 248 VAL 249 0.0061

VAL 249 GLY 250 0.0002

GLY 250 GLY 251 0.0003

GLY 251 LEU 252 -0.0005

LEU 252 THR 253 0.0162

THR 253 TYR 254 -0.0003

TYR 254 ARG 255 -0.0002

ARG 255 GLU 256 -0.0000

GLU 256 GLY 257 0.0008

GLY 257 LEU 258 -0.0001

LEU 258 TYR 259 0.0003

TYR 259 ILE 260 -0.0000

ILE 260 THR 261 0.0018

THR 261 GLU 262 -0.0001

GLU 262 GLU 263 0.0003

GLU 263 ILE 264 0.0001

ILE 264 TYR 265 0.0078

TYR 265 LYS 266 -0.0003

LYS 266 THR 267 -0.0001

THR 267 GLY 268 -0.0001

GLY 268 LEU 269 0.0020

LEU 269 LEU 270 -0.0000

LEU 270 SER 271 0.0002

SER 271 GLY 272 -0.0001

GLY 272 LEU 273 0.0063

LEU 273 ASP 274 0.0001

ASP 274 ILE 275 0.0002

ILE 275 MET 276 -0.0000

MET 276 GLU 277 0.0041

GLU 277 VAL 278 -0.0001

VAL 278 ASN 279 -0.0000

ASN 279 PRO 280 0.0002

PRO 280 SER 281 -0.0006

SER 281 LEU 282 0.0003

LEU 282 GLY 283 0.0002

GLY 283 LYS 284 -0.0002

LYS 284 THR 285 0.0441

THR 285 PRO 286 -0.0000

PRO 286 GLU 287 -0.0003

GLU 287 GLU 288 0.0000

GLU 288 VAL 289 0.0108

VAL 289 THR 290 0.0001

THR 290 ARG 291 0.0002

ARG 291 THR 292 0.0000

THR 292 VAL 293 0.0049

VAL 293 ASN 294 0.0000

ASN 294 THR 295 -0.0000

THR 295 ALA 296 -0.0003

ALA 296 VAL 297 0.0003

VAL 297 ALA 298 0.0001

ALA 298 ILE 299 0.0002

ILE 299 THR 300 -0.0000

THR 300 LEU 301 -0.0032

LEU 301 ALA 302 -0.0003

ALA 302 CYS 303 -0.0003

CYS 303 PHE 304 -0.0000

PHE 304 GLY 305 -0.0090

GLY 305 LEU 306 0.0001

LEU 306 ALA 307 -0.0003

ALA 307 ARG 308 0.0001

ARG 308 GLU 309 -0.0057

GLU 309 GLY 310 0.0000

GLY 310 ASN 311 0.0003

ASN 311 HIS 312 0.0001

HIS 312 LYS 313 0.0704

LYS 313 PRO 314 0.0003

PRO 314 ILE 315 -0.0001

ILE 315 ASP 316 0.0004

ASP 316 TYR 317 0.0108

TYR 317 LEU 318 -0.0000

LEU 318 SER 5 0.0139

SER 5 ARG 6 -0.0001

ARG 6 THR 7 -0.0000

THR 7 ILE 8 -0.0004

ILE 8 GLY 9 -0.0111

GLY 9 ILE 10 0.0003

ILE 10 ILE 11 0.0001

ILE 11 GLY 12 -0.0004

GLY 12 ALA 13 0.0016

ALA 13 PRO 14 0.0004

PRO 14 PHE 15 -0.0002

PHE 15 SER 16 -0.0001

SER 16 LYS 17 0.0015

LYS 17 GLY 18 0.0000

GLY 18 GLN 19 -0.0000

GLN 19 PRO 20 -0.0004

PRO 20 ARG 21 -0.0041

ARG 21 GLY 22 -0.0002

GLY 22 GLY 23 -0.0005

GLY 23 VAL 24 0.0000

VAL 24 GLU 25 -0.0013

GLU 25 GLU 26 -0.0002

GLU 26 GLY 27 -0.0001

GLY 27 PRO 28 0.0003

PRO 28 THR 29 0.0016

THR 29 VAL 30 -0.0000

VAL 30 LEU 31 0.0003

LEU 31 ARG 32 0.0006

ARG 32 LYS 33 0.0015

LYS 33 ALA 34 -0.0003

ALA 34 GLY 35 -0.0001

GLY 35 LEU 36 0.0000

LEU 36 LEU 37 -0.0023

LEU 37 GLU 38 0.0004

GLU 38 LYS 39 0.0001

LYS 39 LEU 40 0.0001

LEU 40 LYS 41 0.0017

LYS 41 GLU 42 0.0000

GLU 42 GLN 43 -0.0003

GLN 43 GLU 44 0.0002

GLU 44 CYS 45 -0.0120

CYS 45 ASP 46 -0.0003

ASP 46 VAL 47 0.0002

VAL 47 LYS 48 -0.0001

LYS 48 ASP 49 -0.0015

ASP 49 TYR 50 -0.0000

TYR 50 GLY 51 -0.0002

GLY 51 ASP 52 -0.0002

ASP 52 LEU 53 0.0125

LEU 53 PRO 54 0.0000

PRO 54 PHE 55 -0.0001

PHE 55 ALA 56 0.0004

ALA 56 ASP 57 -0.0067

ASP 57 ILE 58 -0.0002

ILE 58 PRO 59 0.0002

PRO 59 ASN 60 -0.0002

ASN 60 ASP 61 0.0027

ASP 61 SER 62 -0.0000

SER 62 PRO 63 -0.0000

PRO 63 PHE 64 0.0000

PHE 64 GLN 65 0.0018

GLN 65 ILE 66 -0.0003

ILE 66 VAL 67 -0.0003

VAL 67 LYS 68 0.0001

LYS 68 ASN 69 -0.0046

ASN 69 PRO 70 -0.0001

PRO 70 ARG 71 -0.0002

ARG 71 SER 72 -0.0001

SER 72 VAL 73 -0.0023

VAL 73 GLY 74 -0.0003

GLY 74 LYS 75 0.0002

LYS 75 ALA 76 -0.0002

ALA 76 SER 77 -0.0042

SER 77 GLU 78 0.0000

GLU 78 GLN 79 -0.0000

GLN 79 LEU 80 0.0003

LEU 80 ALA 81 -0.0125

ALA 81 GLY 82 -0.0002

GLY 82 LYS 83 -0.0001

LYS 83 VAL 84 0.0004

VAL 84 ALA 85 -0.0035

ALA 85 GLU 86 -0.0001

GLU 86 VAL 87 0.0002

VAL 87 LYS 88 -0.0002

LYS 88 LYS 89 -0.0026

LYS 89 ASN 90 0.0001

ASN 90 GLY 91 0.0003

GLY 91 ARG 92 0.0000

ARG 92 ILE 93 -0.0053

ILE 93 SER 94 0.0002

SER 94 LEU 95 0.0004

LEU 95 VAL 96 0.0001

VAL 96 LEU 97 -0.0021

LEU 97 GLY 98 -0.0006

GLY 98 GLY 99 0.0003

GLY 99 ASP 100 0.0002

ASP 100 HIS 101 0.0018

HIS 101 SER 102 -0.0002

SER 102 LEU 103 -0.0002

LEU 103 ALA 104 0.0000

ALA 104 ILE 105 0.0050

ILE 105 GLY 106 0.0002

GLY 106 SER 107 -0.0003

SER 107 ILE 108 0.0001

ILE 108 SER 109 0.0055

SER 109 GLY 110 -0.0001

GLY 110 HIS 111 0.0003

HIS 111 ALA 112 0.0000

ALA 112 ARG 113 0.0110

ARG 113 VAL 114 0.0001

VAL 114 HIS 115 0.0001

HIS 115 PRO 116 -0.0003

PRO 116 ASP 117 -0.0260

ASP 117 LEU 118 -0.0001

LEU 118 GLY 119 0.0003

GLY 119 VAL 120 0.0001

VAL 120 ILE 121 0.0012

ILE 121 TRP 122 0.0003

TRP 122 VAL 123 -0.0001

VAL 123 ASP 124 -0.0003

ASP 124 ALA 125 -0.0103

ALA 125 HIS 126 -0.0003

HIS 126 THR 127 0.0000

THR 127 ASP 128 0.0005

ASP 128 ILE 129 0.0031

ILE 129 ASN 130 0.0003

ASN 130 THR 131 0.0001

THR 131 PRO 132 0.0002

PRO 132 LEU 133 0.0047

LEU 133 THR 134 -0.0002

THR 134 THR 135 -0.0003

THR 135 THR 136 0.0000

THR 136 SER 137 -0.0195

SER 137 GLY 138 -0.0000

GLY 138 ASN 139 0.0002

ASN 139 LEU 140 0.0002

LEU 140 HIS 141 0.0042

HIS 141 GLY 142 -0.0001

GLY 142 GLN 143 -0.0001

GLN 143 PRO 144 -0.0001

PRO 144 VAL 145 -0.0035

VAL 145 SER 146 -0.0001

SER 146 PHE 147 0.0000

PHE 147 LEU 148 -0.0002

LEU 148 LEU 149 0.0172

LEU 149 LYS 150 -0.0002

LYS 150 GLU 151 0.0002

GLU 151 LEU 152 0.0003

LEU 152 LYS 153 -0.0182

LYS 153 GLY 154 -0.0002

GLY 154 LYS 155 -0.0002

LYS 155 ILE 156 -0.0001

ILE 156 PRO 157 -0.0150

PRO 157 ASP 158 -0.0002

ASP 158 VAL 159 -0.0001

VAL 159 PRO 160 0.0004

PRO 160 GLY 161 -0.0056

GLY 161 PHE 162 0.0001

PHE 162 SER 163 -0.0001

SER 163 TRP 164 0.0000

TRP 164 VAL 165 0.0089

VAL 165 THR 166 0.0005

THR 166 PRO 167 0.0003

PRO 167 CYS 168 -0.0003

CYS 168 ILE 169 -0.0258

ILE 169 SER 170 -0.0001

SER 170 ALA 171 0.0003

ALA 171 LYS 172 0.0005

LYS 172 ASP 173 0.0367

ASP 173 ILE 174 0.0001

ILE 174 VAL 175 -0.0001

VAL 175 TYR 176 0.0001

TYR 176 ILE 177 -0.0001

ILE 177 GLY 178 0.0003

GLY 178 LEU 179 0.0001

LEU 179 ARG 180 0.0001

ARG 180 ASP 181 0.0321

ASP 181 VAL 182 -0.0002

VAL 182 ASP 183 -0.0003

ASP 183 PRO 184 0.0002

PRO 184 GLY 185 -0.1133

GLY 185 GLU 186 0.0000

GLU 186 HIS 187 -0.0002

HIS 187 TYR 188 0.0003

TYR 188 ILE 189 0.0310

ILE 189 LEU 190 0.0000

LEU 190 LYS 191 -0.0001

LYS 191 THR 192 0.0004

THR 192 LEU 193 0.0671

LEU 193 GLY 194 0.0003

GLY 194 ILE 195 -0.0001

ILE 195 LYS 196 0.0002

LYS 196 TYR 197 0.0012

TYR 197 PHE 198 0.0002

PHE 198 SER 199 -0.0000

SER 199 MET 200 0.0001

MET 200 THR 201 0.0387

THR 201 GLU 202 0.0004

GLU 202 VAL 203 -0.0002

VAL 203 ASP 204 -0.0003

ASP 204 ARG 205 0.0347

ARG 205 LEU 206 -0.0001

LEU 206 GLY 207 0.0003

GLY 207 ILE 208 -0.0001

ILE 208 GLY 209 0.0205

GLY 209 LYS 210 0.0002

LYS 210 VAL 211 -0.0002

VAL 211 MET 212 0.0001

MET 212 GLU 213 0.0195

GLU 213 GLU 214 0.0001

GLU 214 THR 215 -0.0000

THR 215 LEU 216 -0.0002

LEU 216 SER 217 0.0553

SER 217 TYR 218 -0.0000

TYR 218 LEU 219 -0.0004

LEU 219 LEU 220 -0.0002

LEU 220 GLY 221 -0.0049

GLY 221 ARG 222 0.0000

ARG 222 LYS 223 -0.0002

LYS 223 LYS 224 -0.0002

LYS 224 ARG 225 -0.0139

ARG 225 PRO 226 -0.0000

PRO 226 ILE 227 -0.0001

ILE 227 HIS 228 0.0000

HIS 228 LEU 229 0.0043

LEU 229 SER 230 -0.0002

SER 230 PHE 231 0.0002

PHE 231 ASP 232 0.0001

ASP 232 VAL 233 0.0034

VAL 233 ASP 234 0.0000

ASP 234 GLY 235 -0.0002

GLY 235 LEU 236 -0.0001

LEU 236 ASP 237 0.0018

ASP 237 PRO 238 -0.0002

PRO 238 SER 239 -0.0005

SER 239 PHE 240 0.0001

PHE 240 THR 241 0.0065

THR 241 PRO 242 0.0000

PRO 242 ALA 243 -0.0001

ALA 243 THR 244 0.0001

THR 244 GLY 245 0.0029

GLY 245 THR 246 -0.0001

THR 246 PRO 247 0.0000

PRO 247 VAL 248 0.0001

VAL 248 VAL 249 0.0053

VAL 249 GLY 250 -0.0003

GLY 250 GLY 251 -0.0003

GLY 251 LEU 252 0.0005

LEU 252 THR 253 -0.0135

THR 253 TYR 254 -0.0002

TYR 254 ARG 255 0.0002

ARG 255 GLU 256 0.0001

GLU 256 GLY 257 -0.0094

GLY 257 LEU 258 0.0000

LEU 258 TYR 259 -0.0004

TYR 259 ILE 260 -0.0003

ILE 260 THR 261 -0.0245

THR 261 GLU 262 -0.0000

GLU 262 GLU 263 -0.0003

GLU 263 ILE 264 0.0001

ILE 264 TYR 265 -0.0290

TYR 265 LYS 266 0.0002

LYS 266 THR 267 0.0005

THR 267 GLY 268 -0.0001

GLY 268 LEU 269 0.0008

LEU 269 LEU 270 0.0001

LEU 270 SER 271 -0.0000

SER 271 GLY 272 -0.0001

GLY 272 LEU 273 -0.0040

LEU 273 ASP 274 0.0001

ASP 274 ILE 275 -0.0003

ILE 275 MET 276 0.0001

MET 276 GLU 277 -0.0037

GLU 277 VAL 278 -0.0000

VAL 278 ASN 279 -0.0001

ASN 279 PRO 280 0.0001

PRO 280 SER 281 0.0020

SER 281 LEU 282 -0.0005

LEU 282 GLY 283 -0.0001

GLY 283 LYS 284 0.0002

LYS 284 THR 285 -0.0032

THR 285 PRO 286 -0.0001

PRO 286 GLU 287 0.0001

GLU 287 GLU 288 -0.0002

GLU 288 VAL 289 0.0012

VAL 289 THR 290 0.0001

THR 290 ARG 291 -0.0002

ARG 291 THR 292 -0.0002

THR 292 VAL 293 -0.0012

VAL 293 ASN 294 -0.0001

ASN 294 THR 295 0.0003

THR 295 ALA 296 -0.0000

ALA 296 VAL 297 0.0017

VAL 297 ALA 298 -0.0003

ALA 298 ILE 299 -0.0000

ILE 299 THR 300 0.0000

THR 300 LEU 301 0.0032

LEU 301 ALA 302 -0.0000

ALA 302 CYS 303 -0.0002

CYS 303 PHE 304 -0.0001

PHE 304 GLY 305 0.0011

GLY 305 LEU 306 0.0002

LEU 306 ALA 307 -0.0003

ALA 307 ARG 308 -0.0000

ARG 308 GLU 309 0.0676

GLU 309 GLY 310 -0.0001

GLY 310 ASN 311 -0.0002

ASN 311 HIS 312 0.0000

HIS 312 LYS 313 -0.0754

LYS 313 PRO 314 -0.0002

PRO 314 ILE 315 -0.0001

ILE 315 ASP 316 -0.0000

ASP 316 TYR 317 -0.0034

TYR 317 LEU 318 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.

*** trishna ***

CA strain for 22012410212955232

--- normal mode 9 ---

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

* trishna *