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

* NMA2BCoF *

CA strain for 2502181855492627392

--- normal mode 20 ---

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 LEU 2 0.0002

LEU 2 TRP 3 -0.0000

TRP 3 SER 4 -0.0000

SER 4 VAL 5 0.0100

VAL 5 LEU 6 0.0002

LEU 6 ARG 7 0.0000

ARG 7 HIS 8 0.0005

HIS 8 ILE 9 0.0352

ILE 9 LEU 10 0.0002

LEU 10 TRP 11 0.0000

TRP 11 VAL 12 -0.0002

VAL 12 ALA 13 0.0565

ALA 13 LEU 14 -0.0002

LEU 14 LEU 15 0.0001

LEU 15 LEU 16 0.0000

LEU 16 LEU 17 0.0350

LEU 17 VAL 18 -0.0002

VAL 18 LEU 19 0.0000

LEU 19 SER 20 0.0003

SER 20 LEU 21 -0.0062

LEU 21 LEU 22 0.0004

LEU 22 GLY 23 0.0003

GLY 23 PHE 24 0.0000

PHE 24 VAL 25 -0.0227

VAL 25 ILE 26 0.0001

ILE 26 LEU 27 0.0001

LEU 27 LEU 28 0.0001

LEU 28 ARG 29 -0.0337

ARG 29 ASP 30 -0.0000

ASP 30 PRO 31 0.0003

PRO 31 LEU 32 -0.0002

LEU 32 ASN 33 -0.0037

ASN 33 ALA 34 0.0002

ALA 34 ASN 35 0.0001

ASN 35 LEU 36 -0.0000

LEU 36 VAL 37 0.0065

VAL 37 THR 38 0.0001

THR 38 GLN 39 -0.0004

GLN 39 ASN 40 -0.0003

ASN 40 ILE 41 0.0124

ILE 41 TYR 42 -0.0002

TYR 42 ILE 43 -0.0004

ILE 43 GLY 44 0.0003

GLY 44 TYR 45 0.0407

TYR 45 PHE 46 -0.0001

PHE 46 HIS 47 -0.0002

HIS 47 TYR 48 -0.0001

TYR 48 LEU 49 -0.0070

LEU 49 GLY 50 -0.0001

GLY 50 THR 51 -0.0002

THR 51 LEU 52 -0.0001

LEU 52 LEU 53 -0.0075

LEU 53 GLN 54 0.0000

GLN 54 GLY 55 0.0002

GLY 55 ASP 56 -0.0001

ASP 56 PHE 57 -0.0323

PHE 57 GLY 58 -0.0001

GLY 58 ILE 59 -0.0002

ILE 59 THR 60 0.0002

THR 60 TYR 61 -0.0213

TYR 61 ASN 62 -0.0001

ASN 62 GLY 63 -0.0002

GLY 63 GLY 64 -0.0001

GLY 64 LYS 65 -0.0057

LYS 65 SER 66 0.0002

SER 66 LEU 67 -0.0000

LEU 67 MET 68 0.0005

MET 68 ASN 69 0.0813

ASN 69 LEU 70 -0.0002

LEU 70 ILE 71 0.0003

ILE 71 LEU 72 0.0000

LEU 72 THR 73 0.1592

THR 73 VAL 74 0.0002

VAL 74 LEU 75 -0.0002

LEU 75 PRO 76 0.0003

PRO 76 PRO 77 0.0445

PRO 77 THR 78 -0.0002

THR 78 LEU 79 0.0001

LEU 79 GLU 80 -0.0002

GLU 80 LEU 81 0.0094

LEU 81 CYS 82 -0.0004

CYS 82 PHE 83 -0.0000

PHE 83 ILE 84 -0.0000

ILE 84 THR 85 0.0397

THR 85 LEU 86 -0.0000

LEU 86 PHE 87 0.0000

PHE 87 LEU 88 -0.0003

LEU 88 ALA 89 -0.0165

ALA 89 PHE 90 0.0002

PHE 90 ILE 91 -0.0003

ILE 91 PHE 92 0.0001

PHE 92 GLY 93 -0.0219

GLY 93 LEU 94 0.0001

LEU 94 PRO 95 -0.0004

PRO 95 LEU 96 -0.0005

LEU 96 GLY 97 -0.0234

GLY 97 ILE 98 0.0001

ILE 98 ILE 99 0.0004

ILE 99 SER 100 0.0001

SER 100 ALA 101 -0.0246

ALA 101 VAL 102 0.0001

VAL 102 ASN 103 -0.0001

ASN 103 SER 104 0.0002

SER 104 GLU 105 0.0065

GLU 105 GLN 106 -0.0005

GLN 106 VAL 107 0.0005

VAL 107 PHE 108 0.0004

PHE 108 ALA 109 0.0027

ALA 109 LYS 110 -0.0001

LYS 110 SER 111 -0.0002

SER 111 LEU 112 -0.0000

LEU 112 GLN 113 0.0035

GLN 113 ILE 114 -0.0006

ILE 114 LEU 115 -0.0000

LEU 115 SER 116 0.0001

SER 116 TYR 117 -0.0164

TYR 117 VAL 118 0.0000

VAL 118 GLY 119 0.0000

GLY 119 LEU 120 -0.0003

LEU 120 SER 121 -0.0388

SER 121 ILE 122 0.0001

ILE 122 PRO 123 -0.0002

PRO 123 ILE 124 -0.0003

ILE 124 PHE 125 -0.0464

PHE 125 TRP 126 -0.0001

TRP 126 LEU 127 -0.0002

LEU 127 ALA 128 0.0003

ALA 128 PRO 129 0.0008

PRO 129 ILE 130 0.0000

ILE 130 LEU 131 -0.0002

LEU 131 LEU 132 0.0003

LEU 132 TYR 133 0.0228

TYR 133 VAL 134 0.0003

VAL 134 ALA 135 -0.0002

ALA 135 ALA 136 -0.0002

ALA 136 LEU 137 0.0450

LEU 137 SER 138 -0.0000

SER 138 HIS 139 -0.0003

HIS 139 TRP 140 0.0003

TRP 140 GLU 141 0.0191

GLU 141 ILE 142 -0.0000

ILE 142 ALA 143 -0.0000

ALA 143 ALA 144 -0.0000

ALA 144 ILE 145 0.0833

ILE 145 GLY 146 -0.0001

GLY 146 GLN 147 -0.0001

GLN 147 TYR 148 0.0000

TYR 148 ASN 149 -0.0296

ASN 149 LEU 150 -0.0001

LEU 150 LEU 151 -0.0000

LEU 151 TYR 152 -0.0001

TYR 152 GLU 153 0.0385

GLU 153 ILE 154 0.0003

ILE 154 LYS 155 0.0001

LYS 155 SER 156 -0.0001

SER 156 ILE 157 -0.0156

ILE 157 THR 158 0.0002

THR 158 GLY 159 0.0000

GLY 159 PHE 160 0.0003

PHE 160 PRO 161 0.0202

PRO 161 VAL 162 0.0001

VAL 162 ILE 163 0.0001

ILE 163 ASP 164 -0.0002

ASP 164 MET 165 0.0049

MET 165 TRP 166 -0.0001

TRP 166 PHE 167 -0.0002

PHE 167 MET 168 0.0002

MET 168 GLU 169 0.0179

GLU 169 VAL 170 -0.0000

VAL 170 PRO 171 0.0002

PRO 171 TYR 172 0.0002

TYR 172 ARG 173 0.0191

ARG 173 THR 174 0.0001

THR 174 LYS 175 -0.0001

LYS 175 ILE 176 -0.0004

ILE 176 VAL 177 0.0303

VAL 177 GLN 178 0.0003

GLN 178 ASN 179 0.0003

ASN 179 ILE 180 -0.0001

ILE 180 LEU 181 0.0016

LEU 181 GLN 182 0.0000

GLN 182 HIS 183 0.0001

HIS 183 LEU 184 -0.0004

LEU 184 ALA 185 -0.0265

ALA 185 LEU 186 0.0000

LEU 186 PRO 187 -0.0001

PRO 187 THR 188 -0.0002

THR 188 LEU 189 0.0083

LEU 189 VAL 190 0.0000

VAL 190 LEU 191 -0.0001

LEU 191 CYS 192 0.0000

CYS 192 ILE 193 0.0286

ILE 193 LEU 194 -0.0001

LEU 194 PRO 195 -0.0001

PRO 195 THR 196 0.0001

THR 196 MET 197 0.0203

MET 197 GLU 198 -0.0000

GLU 198 ILE 199 -0.0000

ILE 199 ILE 200 0.0003

ILE 200 ARG 201 -0.0128

ARG 201 ILE 202 0.0003

ILE 202 ILE 203 -0.0004

ILE 203 HIS 204 -0.0003

HIS 204 GLN 205 -0.0257

GLN 205 ARG 206 0.0002

ARG 206 ALA 207 0.0003

ALA 207 GLU 208 0.0002

GLU 208 TYR 209 -0.0343

TYR 209 ILE 210 -0.0000

ILE 210 LEU 211 0.0000

LEU 211 ASN 212 -0.0003

ASN 212 GLN 213 -0.0215

GLN 213 ASN 214 0.0000

ASN 214 PHE 215 -0.0002

PHE 215 SER 216 -0.0001

SER 216 LYS 217 -0.0176

LYS 217 VAL 218 -0.0001

VAL 218 ALA 219 0.0001

ALA 219 THR 220 0.0001

THR 220 THR 221 -0.0181

THR 221 ARG 222 0.0001

ARG 222 GLY 223 0.0003

GLY 223 TRP 224 -0.0001

TRP 224 SER 225 -0.0237

SER 225 LYS 226 -0.0004

LYS 226 TRP 227 -0.0002

TRP 227 LYS 228 -0.0003

LYS 228 ILE 229 0.0092

ILE 229 LEU 230 0.0001

LEU 230 HIS 231 0.0001

HIS 231 GLN 232 0.0006

GLN 232 TYR 233 0.0063

TYR 233 VAL 234 -0.0003

VAL 234 PHE 235 0.0000

PHE 235 ARG 236 0.0000

ARG 236 ASN 237 0.0170

ASN 237 THR 238 0.0000

THR 238 PHE 239 -0.0004

PHE 239 PRO 240 0.0002

PRO 240 LEU 241 0.0009

LEU 241 LEU 242 -0.0002

LEU 242 VAL 243 -0.0000

VAL 243 PRO 244 0.0001

PRO 244 GLN 245 -0.0195

GLN 245 VAL 246 0.0000

VAL 246 PRO 247 -0.0001

PRO 247 ARG 248 -0.0004

ARG 248 VAL 249 0.0230

VAL 249 PHE 250 -0.0002

PHE 250 THR 251 -0.0004

THR 251 LEU 252 -0.0001

LEU 252 VAL 253 0.0328

VAL 253 LEU 254 0.0002

LEU 254 THR 255 -0.0002

THR 255 GLN 256 0.0000

GLN 256 CYS 257 0.0134

CYS 257 MET 258 -0.0001

MET 258 LEU 259 -0.0002

LEU 259 VAL 260 -0.0003

VAL 260 GLU 261 -0.0075

GLU 261 THR 262 0.0000

THR 262 ALA 263 -0.0004

ALA 263 LEU 264 0.0001

LEU 264 GLY 265 0.0760

GLY 265 TRP 266 0.0004

TRP 266 PRO 267 0.0002

PRO 267 GLY 268 -0.0003

GLY 268 ILE 269 -0.0188

ILE 269 GLY 270 0.0000

GLY 270 ARG 271 0.0001

ARG 271 TRP 272 0.0001

TRP 272 LEU 273 -0.0788

LEU 273 ILE 274 -0.0001

ILE 274 ASN 275 0.0002

ASN 275 ALA 276 0.0002

ALA 276 VAL 277 -0.0250

VAL 277 ASN 278 0.0001

ASN 278 GLU 279 -0.0002

GLU 279 GLN 280 -0.0001

GLN 280 ASP 281 -0.0123

ASP 281 TYR 282 -0.0003

TYR 282 ASN 283 0.0001

ASN 283 SER 284 0.0001

SER 284 ILE 285 0.0143

ILE 285 ALA 286 -0.0003

ALA 286 ALA 287 0.0003

ALA 287 GLY 288 -0.0002

GLY 288 VAL 289 0.0361

VAL 289 ILE 290 0.0002

ILE 290 VAL 291 0.0001

VAL 291 ILE 292 -0.0003

ILE 292 GLY 293 0.0308

GLY 293 VAL 294 -0.0006

VAL 294 CYS 295 -0.0001

CYS 295 ILE 296 -0.0001

ILE 296 ILE 297 0.0042

ILE 297 LEU 298 0.0004

LEU 298 ILE 299 0.0002

ILE 299 ASP 300 0.0002

ASP 300 THR 301 -0.0017

THR 301 PHE 302 0.0002

PHE 302 THR 303 -0.0001

THR 303 LYS 304 0.0001

LYS 304 ILE 305 -0.0228

ILE 305 PHE 306 -0.0003

PHE 306 THR 307 0.0000

THR 307 PHE 308 0.0003

PHE 308 ILE 309 0.0306

ILE 309 LEU 310 -0.0001

LEU 310 ASP 311 0.0001

ASP 311 PRO 312 0.0001

PRO 312 PHE 313 -0.0280

PHE 313 LYS 314 0.0002

LYS 314 LYS 315 0.0001

LYS 315 LYS 316 0.0001

LYS 316 GLY 317 -0.0824

GLY 317 TRP 318 -0.0001

TRP 318 TYR 319 -0.0001

TYR 319 ALA 320 0.0002

ALA 320 LYS 321 -0.0447

LYS 321 MET 1 -0.1058

MET 1 GLN 2 0.0001

GLN 2 ASN 3 0.0001

ASN 3 LYS 4 -0.0001

LYS 4 GLU 5 0.0377

GLU 5 PRO 6 0.0002

PRO 6 ASP 7 -0.0004

ASP 7 GLU 8 -0.0000

GLU 8 PHE 9 0.1118

PHE 9 ARG 10 0.0001

ARG 10 GLU 11 -0.0001

GLU 11 SER 12 0.0003

SER 12 THR 13 0.0297

THR 13 SER 14 -0.0001

SER 14 ILE 15 0.0001

ILE 15 PHE 16 -0.0001

PHE 16 GLN 17 0.0320

GLN 17 ILE 18 -0.0003

ILE 18 TRP 19 -0.0004

TRP 19 LEU 20 -0.0002

LEU 20 ARG 21 -0.0094

ARG 21 PHE 22 0.0000

PHE 22 ARG 23 -0.0002

ARG 23 GLN 24 0.0002

GLN 24 ASN 25 -0.0449

ASN 25 THR 26 -0.0004

THR 26 ILE 27 0.0000

ILE 27 ALA 28 0.0004

ALA 28 LEU 29 0.0043

LEU 29 PHE 30 -0.0000

PHE 30 SER 31 -0.0000

SER 31 PHE 32 0.0002

PHE 32 TYR 33 -0.0131

TYR 33 LEU 34 -0.0003

LEU 34 LEU 35 0.0002

LEU 35 ILE 36 -0.0002

ILE 36 ALA 37 -0.0700

ALA 37 LEU 38 0.0000

LEU 38 ILE 39 -0.0001

ILE 39 PHE 40 0.0000

PHE 40 THR 41 -0.0119

THR 41 ALA 42 0.0002

ALA 42 LEU 43 0.0004

LEU 43 PHE 44 -0.0002

PHE 44 ALA 45 0.0033

ALA 45 SER 46 -0.0001

SER 46 TYR 47 0.0003

TYR 47 LEU 48 -0.0000

LEU 48 ALA 49 -0.0745

ALA 49 PRO 50 0.0002

PRO 50 TYR 51 0.0000

TYR 51 ALA 52 0.0001

ALA 52 ASP 53 -0.0139

ASP 53 ASN 54 -0.0003

ASN 54 ARG 55 0.0003

ARG 55 GLN 56 -0.0001

GLN 56 PHE 57 0.0259

PHE 57 ILE 58 0.0000

ILE 58 GLY 59 0.0002

GLY 59 GLN 60 0.0002

GLN 60 GLU 61 -0.0123

GLU 61 LEU 62 0.0002

LEU 62 MET 63 -0.0004

MET 63 PRO 64 -0.0003

PRO 64 PRO 65 0.0126

PRO 65 SER 66 0.0004

SER 66 TRP 67 0.0000

TRP 67 VAL 68 0.0000

VAL 68 ASP 69 -0.0377

ASP 69 ARG 70 -0.0000

ARG 70 GLY 71 0.0001

GLY 71 LYS 72 -0.0003

LYS 72 ILE 73 -0.0234

ILE 73 ALA 74 0.0003

ALA 74 PHE 75 -0.0002

PHE 75 PHE 76 0.0000

PHE 76 PHE 77 0.0142

PHE 77 GLY 78 -0.0002

GLY 78 THR 79 0.0004

THR 79 ASP 80 -0.0000

ASP 80 ASP 81 -0.0030

ASP 81 LEU 82 0.0005

LEU 82 GLY 83 -0.0001

GLY 83 ARG 84 -0.0003

ARG 84 ASP 85 -0.0114

ASP 85 ILE 86 0.0001

ILE 86 LEU 87 0.0002

LEU 87 SER 88 -0.0002

SER 88 ARG 89 -0.0088

ARG 89 LEU 90 -0.0003

LEU 90 ILE 91 -0.0003

ILE 91 MET 92 0.0002

MET 92 GLY 93 -0.0188

GLY 93 THR 94 -0.0001

THR 94 ARG 95 -0.0001

ARG 95 TYR 96 0.0001

TYR 96 THR 97 -0.0233

THR 97 LEU 98 -0.0002

LEU 98 GLY 99 -0.0001

GLY 99 SER 100 0.0000

SER 100 ALA 101 0.0107

ALA 101 LEU 102 -0.0001

LEU 102 LEU 103 -0.0003

LEU 103 VAL 104 0.0003

VAL 104 VAL 105 0.0662

VAL 105 PHE 106 0.0000

PHE 106 SER 107 0.0001

SER 107 VAL 108 0.0002

VAL 108 ALA 109 0.0749

ALA 109 ILE 110 -0.0003

ILE 110 ILE 111 0.0002

ILE 111 GLY 112 0.0003

GLY 112 GLY 113 0.0523

GLY 113 ALA 114 -0.0007

ALA 114 LEU 115 -0.0003

LEU 115 GLY 116 0.0003

GLY 116 ILE 117 0.0416

ILE 117 ILE 118 -0.0001

ILE 118 ALA 119 -0.0001

ALA 119 GLY 120 0.0003

GLY 120 LEU 121 0.0165

LEU 121 LEU 122 0.0002

LEU 122 LYS 123 0.0001

LYS 123 GLY 124 -0.0000

GLY 124 ILE 125 0.0368

ILE 125 LYS 126 0.0002

LYS 126 ALA 127 -0.0002

ALA 127 ARG 128 0.0002

ARG 128 PHE 129 0.0147

PHE 129 VAL 130 -0.0002

VAL 130 GLY 131 -0.0001

GLY 131 HIS 132 -0.0002

HIS 132 ILE 133 -0.0355

ILE 133 PHE 134 0.0000

PHE 134 ASP 135 0.0001

ASP 135 ALA 136 0.0000

ALA 136 PHE 137 -0.0188

PHE 137 LEU 138 0.0002

LEU 138 SER 139 0.0001

SER 139 LEU 140 0.0002

LEU 140 PRO 141 -0.0056

PRO 141 ILE 142 -0.0004

ILE 142 LEU 143 0.0000

LEU 143 LEU 144 0.0003

LEU 144 ILE 145 0.0109

ILE 145 ALA 146 -0.0002

ALA 146 VAL 147 -0.0001

VAL 147 VAL 148 0.0002

VAL 148 ILE 149 -0.0253

ILE 149 SER 150 0.0003

SER 150 THR 151 -0.0003

THR 151 LEU 152 0.0001

LEU 152 MET 153 -0.0154

MET 153 GLU 154 -0.0000

GLU 154 PRO 155 0.0002

PRO 155 SER 156 0.0001

SER 156 LEU 157 0.0058

LEU 157 TRP 158 0.0002

TRP 158 ASN 159 -0.0001

ASN 159 ALA 160 0.0004

ALA 160 MET 161 0.0635

MET 161 PHE 162 0.0002

PHE 162 ALA 163 -0.0004

ALA 163 THR 164 0.0002

THR 164 LEU 165 0.0528

LEU 165 LEU 166 0.0001

LEU 166 ALA 167 0.0001

ALA 167 ILE 168 0.0000

ILE 168 LEU 169 0.0357

LEU 169 PRO 170 0.0000

PRO 170 TYR 171 0.0003

TYR 171 PHE 172 0.0002

PHE 172 ILE 173 -0.0000

ILE 173 HIS 174 0.0001

HIS 174 THR 175 -0.0001

THR 175 ILE 176 0.0003

ILE 176 TYR 177 -0.0337

TYR 177 ARG 178 -0.0000

ARG 178 ALA 179 -0.0003

ALA 179 ILE 180 0.0004

ILE 180 GLN 181 -0.0163

GLN 181 LYS 182 0.0001

LYS 182 GLU 183 0.0000

GLU 183 LEU 184 0.0001

LEU 184 GLU 185 -0.0023

GLU 185 LYS 186 0.0000

LYS 186 ASP 187 -0.0001

ASP 187 TYR 188 -0.0001

TYR 188 VAL 189 0.0233

VAL 189 VAL 190 -0.0002

VAL 190 MET 191 0.0003

MET 191 LEU 192 -0.0001

LEU 192 LYS 193 0.0048

LYS 193 LEU 194 0.0002

LEU 194 GLU 195 -0.0000

GLU 195 GLY 196 0.0001

GLY 196 ILE 197 -0.0217

ILE 197 SER 198 -0.0002

SER 198 ASN 199 0.0000

ASN 199 GLN 200 -0.0001

GLN 200 ALA 201 0.0169

ALA 201 LEU 202 0.0004

LEU 202 LEU 203 0.0003

LEU 203 LYS 204 0.0001

LYS 204 SER 205 0.0226

SER 205 THR 206 -0.0003

THR 206 ILE 207 0.0000

ILE 207 LEU 208 0.0003

LEU 208 PRO 209 -0.0060

PRO 209 ASN 210 0.0001

ASN 210 ILE 211 -0.0001

ILE 211 THR 212 0.0002

THR 212 VAL 213 -0.0201

VAL 213 ILE 214 0.0001

ILE 214 TYR 215 0.0002

TYR 215 ILE 216 0.0003

ILE 216 GLN 217 0.0085

GLN 217 GLU 218 -0.0003

GLU 218 VAL 219 -0.0005

VAL 219 ALA 220 -0.0001

ALA 220 ARG 221 0.0065

ARG 221 ALA 222 0.0002

ALA 222 PHE 223 -0.0000

PHE 223 VAL 224 0.0002

VAL 224 ILE 225 -0.0173

ILE 225 ALA 226 -0.0000

ALA 226 VAL 227 0.0000

VAL 227 LEU 228 0.0001

LEU 228 ASP 229 -0.0409

ASP 229 ILE 230 -0.0000

ILE 230 SER 231 0.0000

SER 231 ALA 232 0.0003

ALA 232 LEU 233 -0.0321

LEU 233 SER 234 0.0002

SER 234 PHE 235 0.0002

PHE 235 ILE 236 -0.0004

ILE 236 SER 237 -0.0359

SER 237 LEU 238 -0.0003

LEU 238 GLY 239 0.0001

GLY 239 ALA 240 -0.0002

ALA 240 GLN 241 0.0369

GLN 241 ARG 242 -0.0000

ARG 242 PRO 243 0.0005

PRO 243 THR 244 -0.0002

THR 244 PRO 245 -0.0224

PRO 245 GLU 246 0.0002

GLU 246 TRP 247 -0.0000

TRP 247 GLY 248 0.0002

GLY 248 ALA 249 -0.0364

ALA 249 MET 250 -0.0003

MET 250 ILE 251 -0.0003

ILE 251 LYS 252 0.0003

LYS 252 ASP 253 0.0457

ASP 253 SER 254 0.0002

SER 254 LEU 255 -0.0001

LEU 255 GLU 256 0.0003

GLU 256 LEU 257 0.0431

LEU 257 LEU 258 0.0002

LEU 258 TYR 259 0.0002

TYR 259 LEU 260 -0.0002

LEU 260 ALA 261 -0.0319

ALA 261 PRO 262 -0.0002

PRO 262 TRP 263 -0.0001

TRP 263 THR 264 0.0002

THR 264 VAL 265 -0.0302

VAL 265 LEU 266 -0.0000

LEU 266 LEU 267 0.0002

LEU 267 PRO 268 -0.0000

PRO 268 GLY 269 -0.0242

GLY 269 PHE 270 0.0004

PHE 270 ALA 271 -0.0003

ALA 271 ILE 272 -0.0002

ILE 272 ILE 273 -0.0055

ILE 273 PHE 274 -0.0003

PHE 274 THR 275 0.0002

THR 275 ILE 276 -0.0004

ILE 276 LEU 277 -0.0151

LEU 277 LEU 278 0.0002

LEU 278 SER 279 0.0000

SER 279 ILE 280 -0.0000

ILE 280 ILE 281 -0.0091

ILE 281 PHE 282 0.0003

PHE 282 SER 283 -0.0002

SER 283 ASN 284 0.0001

ASN 284 GLY 285 -0.0014

GLY 285 LEU 286 0.0003

LEU 286 THR 287 -0.0000

THR 287 LYS 288 -0.0003

LYS 288 ALA 289 0.0061

ALA 289 ILE 290 -0.0001

ILE 290 ASN 291 0.0002

ASN 291 GLN 292 -0.0002

GLN 292 HIS 293 -0.0231

HIS 293 GLN 294 -0.0002

GLN 294 GLU 295 -0.0004

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 8th, 2025.

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

*** NMA2BCoF ***

CA strain for 2502181855492627392

--- normal mode 20 ---

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

* NMA2BCoF *