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

* trishna *

CA strain for 22012410212955232

--- 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 5 ARG 6 -0.0003

ARG 6 THR 7 0.0001

THR 7 ILE 8 -0.0000

ILE 8 GLY 9 0.0264

GLY 9 ILE 10 0.0000

ILE 10 ILE 11 -0.0001

ILE 11 GLY 12 0.0002

GLY 12 ALA 13 0.0154

ALA 13 PRO 14 0.0001

PRO 14 PHE 15 0.0003

PHE 15 SER 16 -0.0002

SER 16 LYS 17 -0.0020

LYS 17 GLY 18 -0.0001

GLY 18 GLN 19 -0.0001

GLN 19 PRO 20 -0.0003

PRO 20 ARG 21 0.0048

ARG 21 GLY 22 -0.0004

GLY 22 GLY 23 -0.0000

GLY 23 VAL 24 0.0002

VAL 24 GLU 25 -0.0324

GLU 25 GLU 26 0.0002

GLU 26 GLY 27 -0.0001

GLY 27 PRO 28 -0.0001

PRO 28 THR 29 -0.0362

THR 29 VAL 30 -0.0003

VAL 30 LEU 31 -0.0002

LEU 31 ARG 32 -0.0002

ARG 32 LYS 33 -0.0105

LYS 33 ALA 34 0.0001

ALA 34 GLY 35 -0.0001

GLY 35 LEU 36 0.0000

LEU 36 LEU 37 -0.0043

LEU 37 GLU 38 0.0003

GLU 38 LYS 39 0.0003

LYS 39 LEU 40 -0.0002

LEU 40 LYS 41 -0.0005

LYS 41 GLU 42 0.0005

GLU 42 GLN 43 -0.0000

GLN 43 GLU 44 0.0003

GLU 44 CYS 45 0.0215

CYS 45 ASP 46 0.0002

ASP 46 VAL 47 -0.0001

VAL 47 LYS 48 -0.0005

LYS 48 ASP 49 0.0229

ASP 49 TYR 50 0.0001

TYR 50 GLY 51 -0.0003

GLY 51 ASP 52 0.0000

ASP 52 LEU 53 0.0050

LEU 53 PRO 54 -0.0002

PRO 54 PHE 55 -0.0000

PHE 55 ALA 56 0.0001

ALA 56 ASP 57 0.1626

ASP 57 ILE 58 -0.0005

ILE 58 PRO 59 -0.0000

PRO 59 ASN 60 0.0001

ASN 60 ASP 61 -0.0100

ASP 61 SER 62 0.0002

SER 62 PRO 63 0.0001

PRO 63 PHE 64 -0.0001

PHE 64 GLN 65 -0.0279

GLN 65 ILE 66 -0.0002

ILE 66 VAL 67 0.0002

VAL 67 LYS 68 0.0000

LYS 68 ASN 69 0.0014

ASN 69 PRO 70 -0.0001

PRO 70 ARG 71 0.0001

ARG 71 SER 72 0.0001

SER 72 VAL 73 0.0388

VAL 73 GLY 74 -0.0001

GLY 74 LYS 75 0.0000

LYS 75 ALA 76 0.0005

ALA 76 SER 77 0.0247

SER 77 GLU 78 -0.0001

GLU 78 GLN 79 0.0002

GLN 79 LEU 80 0.0002

LEU 80 ALA 81 0.0271

ALA 81 GLY 82 -0.0002

GLY 82 LYS 83 -0.0002

LYS 83 VAL 84 0.0001

VAL 84 ALA 85 0.0054

ALA 85 GLU 86 -0.0001

GLU 86 VAL 87 0.0001

VAL 87 LYS 88 -0.0003

LYS 88 LYS 89 0.0010

LYS 89 ASN 90 -0.0002

ASN 90 GLY 91 0.0002

GLY 91 ARG 92 0.0001

ARG 92 ILE 93 -0.0011

ILE 93 SER 94 0.0001

SER 94 LEU 95 -0.0000

LEU 95 VAL 96 0.0000

VAL 96 LEU 97 0.0138

LEU 97 GLY 98 -0.0001

GLY 98 GLY 99 -0.0001

GLY 99 ASP 100 0.0004

ASP 100 HIS 101 0.0064

HIS 101 SER 102 0.0004

SER 102 LEU 103 -0.0001

LEU 103 ALA 104 -0.0000

ALA 104 ILE 105 0.0057

ILE 105 GLY 106 0.0003

GLY 106 SER 107 0.0003

SER 107 ILE 108 -0.0001

ILE 108 SER 109 -0.0035

SER 109 GLY 110 0.0003

GLY 110 HIS 111 0.0002

HIS 111 ALA 112 -0.0001

ALA 112 ARG 113 -0.0090

ARG 113 VAL 114 0.0003

VAL 114 HIS 115 -0.0002

HIS 115 PRO 116 -0.0000

PRO 116 ASP 117 0.0140

ASP 117 LEU 118 -0.0002

LEU 118 GLY 119 0.0003

GLY 119 VAL 120 -0.0000

VAL 120 ILE 121 -0.0028

ILE 121 TRP 122 0.0000

TRP 122 VAL 123 0.0003

VAL 123 ASP 124 -0.0004

ASP 124 ALA 125 -0.0020

ALA 125 HIS 126 0.0002

HIS 126 THR 127 -0.0004

THR 127 ASP 128 -0.0001

ASP 128 ILE 129 0.0279

ILE 129 ASN 130 -0.0004

ASN 130 THR 131 0.0001

THR 131 PRO 132 0.0001

PRO 132 LEU 133 0.0143

LEU 133 THR 134 -0.0000

THR 134 THR 135 -0.0000

THR 135 THR 136 -0.0001

THR 136 SER 137 -0.0055

SER 137 GLY 138 -0.0002

GLY 138 ASN 139 0.0002

ASN 139 LEU 140 0.0004

LEU 140 HIS 141 -0.0044

HIS 141 GLY 142 -0.0000

GLY 142 GLN 143 0.0004

GLN 143 PRO 144 -0.0004

PRO 144 VAL 145 -0.0160

VAL 145 SER 146 0.0001

SER 146 PHE 147 0.0001

PHE 147 LEU 148 -0.0004

LEU 148 LEU 149 0.0137

LEU 149 LYS 150 0.0003

LYS 150 GLU 151 -0.0001

GLU 151 LEU 152 -0.0002

LEU 152 LYS 153 0.0281

LYS 153 GLY 154 -0.0001

GLY 154 LYS 155 -0.0000

LYS 155 ILE 156 0.0000

ILE 156 PRO 157 0.0121

PRO 157 ASP 158 -0.0001

ASP 158 VAL 159 0.0001

VAL 159 PRO 160 -0.0005

PRO 160 GLY 161 0.0125

GLY 161 PHE 162 -0.0000

PHE 162 SER 163 -0.0003

SER 163 TRP 164 -0.0002

TRP 164 VAL 165 0.0219

VAL 165 THR 166 0.0000

THR 166 PRO 167 0.0001

PRO 167 CYS 168 -0.0004

CYS 168 ILE 169 0.0338

ILE 169 SER 170 -0.0001

SER 170 ALA 171 -0.0001

ALA 171 LYS 172 -0.0002

LYS 172 ASP 173 -0.0079

ASP 173 ILE 174 -0.0001

ILE 174 VAL 175 0.0001

VAL 175 TYR 176 -0.0004

TYR 176 ILE 177 0.0011

ILE 177 GLY 178 -0.0003

GLY 178 LEU 179 0.0004

LEU 179 ARG 180 -0.0004

ARG 180 ASP 181 -0.0036

ASP 181 VAL 182 0.0001

VAL 182 ASP 183 -0.0003

ASP 183 PRO 184 0.0003

PRO 184 GLY 185 0.0090

GLY 185 GLU 186 -0.0002

GLU 186 HIS 187 -0.0003

HIS 187 TYR 188 0.0000

TYR 188 ILE 189 0.0075

ILE 189 LEU 190 -0.0003

LEU 190 LYS 191 -0.0002

LYS 191 THR 192 -0.0002

THR 192 LEU 193 0.0047

LEU 193 GLY 194 0.0002

GLY 194 ILE 195 -0.0001

ILE 195 LYS 196 -0.0004

LYS 196 TYR 197 0.0053

TYR 197 PHE 198 0.0001

PHE 198 SER 199 -0.0001

SER 199 MET 200 -0.0000

MET 200 THR 201 -0.0083

THR 201 GLU 202 0.0000

GLU 202 VAL 203 -0.0001

VAL 203 ASP 204 -0.0003

ASP 204 ARG 205 -0.0074

ARG 205 LEU 206 -0.0004

LEU 206 GLY 207 0.0001

GLY 207 ILE 208 0.0001

ILE 208 GLY 209 -0.0045

GLY 209 LYS 210 -0.0000

LYS 210 VAL 211 -0.0001

VAL 211 MET 212 -0.0004

MET 212 GLU 213 -0.0047

GLU 213 GLU 214 -0.0003

GLU 214 THR 215 -0.0000

THR 215 LEU 216 -0.0002

LEU 216 SER 217 -0.0119

SER 217 TYR 218 0.0002

TYR 218 LEU 219 -0.0001

LEU 219 LEU 220 -0.0001

LEU 220 GLY 221 0.0020

GLY 221 ARG 222 -0.0000

ARG 222 LYS 223 -0.0002

LYS 223 LYS 224 0.0004

LYS 224 ARG 225 0.0036

ARG 225 PRO 226 0.0002

PRO 226 ILE 227 0.0001

ILE 227 HIS 228 -0.0000

HIS 228 LEU 229 -0.0087

LEU 229 SER 230 -0.0006

SER 230 PHE 231 -0.0001

PHE 231 ASP 232 0.0003

ASP 232 VAL 233 -0.0031

VAL 233 ASP 234 0.0001

ASP 234 GLY 235 -0.0002

GLY 235 LEU 236 -0.0000

LEU 236 ASP 237 0.0054

ASP 237 PRO 238 -0.0000

PRO 238 SER 239 -0.0001

SER 239 PHE 240 0.0001

PHE 240 THR 241 -0.0160

THR 241 PRO 242 0.0002

PRO 242 ALA 243 -0.0003

ALA 243 THR 244 -0.0002

THR 244 GLY 245 0.0058

GLY 245 THR 246 -0.0001

THR 246 PRO 247 -0.0004

PRO 247 VAL 248 0.0002

VAL 248 VAL 249 -0.0158

VAL 249 GLY 250 0.0004

GLY 250 GLY 251 0.0001

GLY 251 LEU 252 -0.0000

LEU 252 THR 253 0.0093

THR 253 TYR 254 0.0002

TYR 254 ARG 255 -0.0000

ARG 255 GLU 256 -0.0001

GLU 256 GLY 257 0.0120

GLY 257 LEU 258 0.0001

LEU 258 TYR 259 -0.0001

TYR 259 ILE 260 -0.0002

ILE 260 THR 261 0.0036

THR 261 GLU 262 -0.0004

GLU 262 GLU 263 0.0001

GLU 263 ILE 264 -0.0001

ILE 264 TYR 265 0.0020

TYR 265 LYS 266 -0.0002

LYS 266 THR 267 -0.0002

THR 267 GLY 268 -0.0003

GLY 268 LEU 269 0.0012

LEU 269 LEU 270 -0.0001

LEU 270 SER 271 -0.0001

SER 271 GLY 272 -0.0004

GLY 272 LEU 273 0.0015

LEU 273 ASP 274 -0.0000

ASP 274 ILE 275 0.0005

ILE 275 MET 276 -0.0005

MET 276 GLU 277 -0.0074

GLU 277 VAL 278 0.0002

VAL 278 ASN 279 0.0001

ASN 279 PRO 280 0.0001

PRO 280 SER 281 0.0911

SER 281 LEU 282 -0.0001

LEU 282 GLY 283 -0.0000

GLY 283 LYS 284 -0.0004

LYS 284 THR 285 0.0303

THR 285 PRO 286 -0.0002

PRO 286 GLU 287 0.0000

GLU 287 GLU 288 -0.0001

GLU 288 VAL 289 0.0017

VAL 289 THR 290 0.0000

THR 290 ARG 291 0.0002

ARG 291 THR 292 -0.0002

THR 292 VAL 293 -0.0089

VAL 293 ASN 294 0.0002

ASN 294 THR 295 -0.0000

THR 295 ALA 296 0.0000

ALA 296 VAL 297 -0.0038

VAL 297 ALA 298 0.0002

ALA 298 ILE 299 -0.0000

ILE 299 THR 300 -0.0002

THR 300 LEU 301 0.0007

LEU 301 ALA 302 0.0002

ALA 302 CYS 303 -0.0001

CYS 303 PHE 304 0.0000

PHE 304 GLY 305 0.0164

GLY 305 LEU 306 0.0001

LEU 306 ALA 307 0.0003

ALA 307 ARG 308 -0.0001

ARG 308 GLU 309 -0.0669

GLU 309 GLY 310 -0.0001

GLY 310 ASN 311 -0.0005

ASN 311 HIS 312 0.0002

HIS 312 LYS 313 0.0209

LYS 313 PRO 314 0.0002

PRO 314 ILE 315 -0.0001

ILE 315 ASP 316 0.0002

ASP 316 TYR 317 -0.0051

TYR 317 LEU 318 0.0001

LEU 318 SER 5 -0.0550

SER 5 ARG 6 -0.0000

ARG 6 THR 7 0.0001

THR 7 ILE 8 -0.0001

ILE 8 GLY 9 0.0088

GLY 9 ILE 10 0.0001

ILE 10 ILE 11 -0.0002

ILE 11 GLY 12 0.0001

GLY 12 ALA 13 0.0018

ALA 13 PRO 14 0.0000

PRO 14 PHE 15 0.0001

PHE 15 SER 16 0.0001

SER 16 LYS 17 -0.0030

LYS 17 GLY 18 -0.0001

GLY 18 GLN 19 0.0001

GLN 19 PRO 20 0.0000

PRO 20 ARG 21 -0.0081

ARG 21 GLY 22 -0.0001

GLY 22 GLY 23 -0.0000

GLY 23 VAL 24 -0.0001

VAL 24 GLU 25 0.0021

GLU 25 GLU 26 -0.0001

GLU 26 GLY 27 -0.0002

GLY 27 PRO 28 0.0003

PRO 28 THR 29 -0.0006

THR 29 VAL 30 0.0003

VAL 30 LEU 31 -0.0002

LEU 31 ARG 32 0.0002

ARG 32 LYS 33 0.0006

LYS 33 ALA 34 0.0001

ALA 34 GLY 35 0.0002

GLY 35 LEU 36 -0.0002

LEU 36 LEU 37 0.0028

LEU 37 GLU 38 -0.0001

GLU 38 LYS 39 0.0001

LYS 39 LEU 40 -0.0000

LEU 40 LYS 41 0.0009

LYS 41 GLU 42 -0.0005

GLU 42 GLN 43 -0.0002

GLN 43 GLU 44 -0.0001

GLU 44 CYS 45 0.0237

CYS 45 ASP 46 0.0003

ASP 46 VAL 47 0.0001

VAL 47 LYS 48 0.0000

LYS 48 ASP 49 0.0080

ASP 49 TYR 50 0.0001

TYR 50 GLY 51 0.0002

GLY 51 ASP 52 -0.0000

ASP 52 LEU 53 0.0034

LEU 53 PRO 54 -0.0002

PRO 54 PHE 55 0.0002

PHE 55 ALA 56 0.0002

ALA 56 ASP 57 -0.0074

ASP 57 ILE 58 0.0005

ILE 58 PRO 59 -0.0003

PRO 59 ASN 60 0.0003

ASN 60 ASP 61 0.0015

ASP 61 SER 62 -0.0001

SER 62 PRO 63 0.0000

PRO 63 PHE 64 -0.0000

PHE 64 GLN 65 0.0054

GLN 65 ILE 66 0.0001

ILE 66 VAL 67 -0.0004

VAL 67 LYS 68 0.0000

LYS 68 ASN 69 0.0048

ASN 69 PRO 70 -0.0001

PRO 70 ARG 71 0.0002

ARG 71 SER 72 -0.0003

SER 72 VAL 73 -0.0018

VAL 73 GLY 74 0.0001

GLY 74 LYS 75 0.0002

LYS 75 ALA 76 -0.0001

ALA 76 SER 77 -0.0048

SER 77 GLU 78 0.0003

GLU 78 GLN 79 -0.0002

GLN 79 LEU 80 0.0002

LEU 80 ALA 81 -0.0105

ALA 81 GLY 82 -0.0002

GLY 82 LYS 83 0.0001

LYS 83 VAL 84 0.0002

VAL 84 ALA 85 -0.0032

ALA 85 GLU 86 0.0002

GLU 86 VAL 87 0.0001

VAL 87 LYS 88 0.0002

LYS 88 LYS 89 -0.0012

LYS 89 ASN 90 -0.0002

ASN 90 GLY 91 -0.0002

GLY 91 ARG 92 0.0001

ARG 92 ILE 93 -0.0054

ILE 93 SER 94 -0.0005

SER 94 LEU 95 -0.0002

LEU 95 VAL 96 -0.0000

VAL 96 LEU 97 -0.0108

LEU 97 GLY 98 -0.0003

GLY 98 GLY 99 0.0000

GLY 99 ASP 100 0.0003

ASP 100 HIS 101 -0.0002

HIS 101 SER 102 -0.0001

SER 102 LEU 103 -0.0003

LEU 103 ALA 104 0.0001

ALA 104 ILE 105 -0.0025

ILE 105 GLY 106 0.0001

GLY 106 SER 107 0.0002

SER 107 ILE 108 -0.0002

ILE 108 SER 109 0.0032

SER 109 GLY 110 -0.0001

GLY 110 HIS 111 0.0001

HIS 111 ALA 112 -0.0001

ALA 112 ARG 113 0.0069

ARG 113 VAL 114 -0.0001

VAL 114 HIS 115 0.0002

HIS 115 PRO 116 -0.0001

PRO 116 ASP 117 -0.0251

ASP 117 LEU 118 -0.0001

LEU 118 GLY 119 0.0003

GLY 119 VAL 120 0.0002

VAL 120 ILE 121 0.0042

ILE 121 TRP 122 0.0003

TRP 122 VAL 123 0.0000

VAL 123 ASP 124 -0.0000

ASP 124 ALA 125 -0.0038

ALA 125 HIS 126 -0.0000

HIS 126 THR 127 0.0002

THR 127 ASP 128 0.0001

ASP 128 ILE 129 -0.0079

ILE 129 ASN 130 -0.0002

ASN 130 THR 131 -0.0000

THR 131 PRO 132 0.0000

PRO 132 LEU 133 0.0052

LEU 133 THR 134 0.0002

THR 134 THR 135 0.0003

THR 135 THR 136 -0.0000

THR 136 SER 137 -0.0049

SER 137 GLY 138 0.0001

GLY 138 ASN 139 -0.0004

ASN 139 LEU 140 0.0000

LEU 140 HIS 141 -0.0007

HIS 141 GLY 142 -0.0001

GLY 142 GLN 143 -0.0000

GLN 143 PRO 144 0.0002

PRO 144 VAL 145 -0.0126

VAL 145 SER 146 -0.0001

SER 146 PHE 147 -0.0002

PHE 147 LEU 148 0.0005

LEU 148 LEU 149 -0.0110

LEU 149 LYS 150 0.0002

LYS 150 GLU 151 0.0000

GLU 151 LEU 152 -0.0003

LEU 152 LYS 153 -0.0035

LYS 153 GLY 154 0.0000

GLY 154 LYS 155 0.0001

LYS 155 ILE 156 -0.0000

ILE 156 PRO 157 -0.0100

PRO 157 ASP 158 -0.0003

ASP 158 VAL 159 0.0000

VAL 159 PRO 160 0.0002

PRO 160 GLY 161 -0.0010

GLY 161 PHE 162 -0.0001

PHE 162 SER 163 -0.0002

SER 163 TRP 164 -0.0003

TRP 164 VAL 165 -0.0103

VAL 165 THR 166 -0.0000

THR 166 PRO 167 0.0001

PRO 167 CYS 168 0.0003

CYS 168 ILE 169 -0.0345

ILE 169 SER 170 -0.0001

SER 170 ALA 171 0.0002

ALA 171 LYS 172 0.0003

LYS 172 ASP 173 0.0085

ASP 173 ILE 174 -0.0003

ILE 174 VAL 175 -0.0001

VAL 175 TYR 176 -0.0000

TYR 176 ILE 177 -0.0070

ILE 177 GLY 178 0.0001

GLY 178 LEU 179 -0.0001

LEU 179 ARG 180 -0.0001

ARG 180 ASP 181 0.0078

ASP 181 VAL 182 0.0001

VAL 182 ASP 183 -0.0002

ASP 183 PRO 184 0.0001

PRO 184 GLY 185 -0.0309

GLY 185 GLU 186 0.0001

GLU 186 HIS 187 0.0001

HIS 187 TYR 188 -0.0003

TYR 188 ILE 189 0.0018

ILE 189 LEU 190 -0.0003

LEU 190 LYS 191 -0.0001

LYS 191 THR 192 0.0000

THR 192 LEU 193 0.0224

LEU 193 GLY 194 0.0001

GLY 194 ILE 195 0.0001

ILE 195 LYS 196 -0.0005

LYS 196 TYR 197 -0.0193

TYR 197 PHE 198 0.0000

PHE 198 SER 199 0.0001

SER 199 MET 200 -0.0000

MET 200 THR 201 0.0781

THR 201 GLU 202 -0.0000

GLU 202 VAL 203 -0.0004

VAL 203 ASP 204 0.0002

ASP 204 ARG 205 0.0974

ARG 205 LEU 206 0.0005

LEU 206 GLY 207 -0.0003

GLY 207 ILE 208 0.0004

ILE 208 GLY 209 0.0334

GLY 209 LYS 210 0.0003

LYS 210 VAL 211 -0.0002

VAL 211 MET 212 -0.0002

MET 212 GLU 213 0.0015

GLU 213 GLU 214 0.0003

GLU 214 THR 215 -0.0002

THR 215 LEU 216 0.0004

LEU 216 SER 217 -0.0394

SER 217 TYR 218 0.0002

TYR 218 LEU 219 -0.0001

LEU 219 LEU 220 0.0001

LEU 220 GLY 221 -0.1279

GLY 221 ARG 222 -0.0005

ARG 222 LYS 223 0.0002

LYS 223 LYS 224 -0.0001

LYS 224 ARG 225 0.0289

ARG 225 PRO 226 -0.0000

PRO 226 ILE 227 -0.0003

ILE 227 HIS 228 0.0002

HIS 228 LEU 229 -0.0084

LEU 229 SER 230 -0.0001

SER 230 PHE 231 -0.0001

PHE 231 ASP 232 -0.0002

ASP 232 VAL 233 -0.0073

VAL 233 ASP 234 0.0001

ASP 234 GLY 235 -0.0001

GLY 235 LEU 236 -0.0001

LEU 236 ASP 237 -0.0036

ASP 237 PRO 238 -0.0000

PRO 238 SER 239 0.0002

SER 239 PHE 240 0.0001

PHE 240 THR 241 -0.0011

THR 241 PRO 242 0.0001

PRO 242 ALA 243 0.0004

ALA 243 THR 244 -0.0001

THR 244 GLY 245 -0.0062

GLY 245 THR 246 -0.0002

THR 246 PRO 247 0.0000

PRO 247 VAL 248 -0.0001

VAL 248 VAL 249 0.0017

VAL 249 GLY 250 -0.0002

GLY 250 GLY 251 -0.0003

GLY 251 LEU 252 -0.0001

LEU 252 THR 253 -0.0164

THR 253 TYR 254 -0.0000

TYR 254 ARG 255 -0.0002

ARG 255 GLU 256 -0.0001

GLU 256 GLY 257 0.0178

GLY 257 LEU 258 0.0002

LEU 258 TYR 259 0.0002

TYR 259 ILE 260 0.0001

ILE 260 THR 261 0.0252

THR 261 GLU 262 0.0001

GLU 262 GLU 263 0.0002

GLU 263 ILE 264 -0.0000

ILE 264 TYR 265 0.0112

TYR 265 LYS 266 -0.0001

LYS 266 THR 267 -0.0004

THR 267 GLY 268 0.0002

GLY 268 LEU 269 -0.0054

LEU 269 LEU 270 -0.0002

LEU 270 SER 271 0.0002

SER 271 GLY 272 0.0002

GLY 272 LEU 273 -0.0162

LEU 273 ASP 274 -0.0004

ASP 274 ILE 275 0.0002

ILE 275 MET 276 0.0000

MET 276 GLU 277 -0.0131

GLU 277 VAL 278 0.0003

VAL 278 ASN 279 0.0004

ASN 279 PRO 280 -0.0001

PRO 280 SER 281 -0.0057

SER 281 LEU 282 -0.0001

LEU 282 GLY 283 -0.0004

GLY 283 LYS 284 0.0002

LYS 284 THR 285 -0.0029

THR 285 PRO 286 0.0002

PRO 286 GLU 287 0.0002

GLU 287 GLU 288 0.0001

GLU 288 VAL 289 -0.0039

VAL 289 THR 290 -0.0001

THR 290 ARG 291 0.0001

ARG 291 THR 292 0.0000

THR 292 VAL 293 0.0009

VAL 293 ASN 294 -0.0001

ASN 294 THR 295 0.0001

THR 295 ALA 296 0.0001

ALA 296 VAL 297 -0.0016

VAL 297 ALA 298 0.0001

ALA 298 ILE 299 0.0001

ILE 299 THR 300 0.0002

THR 300 LEU 301 0.0013

LEU 301 ALA 302 0.0003

ALA 302 CYS 303 0.0001

CYS 303 PHE 304 0.0003

PHE 304 GLY 305 0.0116

GLY 305 LEU 306 0.0000

LEU 306 ALA 307 0.0002

ALA 307 ARG 308 0.0000

ARG 308 GLU 309 -0.0418

GLU 309 GLY 310 0.0003

GLY 310 ASN 311 0.0002

ASN 311 HIS 312 0.0003

HIS 312 LYS 313 0.0124

LYS 313 PRO 314 0.0003

PRO 314 ILE 315 -0.0002

ILE 315 ASP 316 0.0002

ASP 316 TYR 317 -0.0001

TYR 317 LEU 318 0.0002

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 10 ---

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

* trishna *