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

* EUTLA *

CA strain for 22123022061855342

--- 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
ASP 7 PRO 8 0.0001

PRO 8 ILE 9 0.0002

ILE 9 ARG 10 0.0357

ARG 10 GLU 11 0.0001

GLU 11 TRP 12 0.0002

TRP 12 ILE 13 -0.0005

ILE 13 LEU 14 0.0002

LEU 14 THR 15 -0.0000

THR 15 GLU 16 -0.0058

GLU 16 GLY 17 0.0002

GLY 17 LYS 18 0.0003

LYS 18 ALA 19 -0.0029

ALA 19 THR 20 -0.0000

THR 20 GLN 21 -0.0002

GLN 21 ILE 22 0.0364

ILE 22 THR 23 -0.0001

THR 23 LYS 24 0.0001

LYS 24 ILE 25 0.0606

ILE 25 GLY 26 0.0001

GLY 26 SER 27 0.0003

SER 27 VAL 28 0.1604

VAL 28 GLY 29 -0.0001

GLY 29 GLY 30 0.0000

GLY 30 GLY 31 0.4366

GLY 31 CYS 32 -0.0000

CYS 32 ILE 33 -0.0000

ILE 33 ASN 34 0.2488

ASN 34 LEU 35 0.0004

LEU 35 ALA 36 0.0002

ALA 36 SER 37 0.1462

SER 37 HIS 38 -0.0001

HIS 38 TYR 39 -0.0001

TYR 39 GLN 40 0.0373

GLN 40 THR 41 0.0001

THR 41 ASP 42 -0.0000

ASP 42 ALA 43 0.0049

ALA 43 GLY 44 0.0001

GLY 44 SER 45 -0.0000

SER 45 PHE 46 0.0058

PHE 46 PHE 47 -0.0000

PHE 47 VAL 48 -0.0002

VAL 48 LYS 49 0.0620

LYS 49 THR 50 0.0004

THR 50 ASN 51 -0.0002

ASN 51 ARG 52 -0.0156

ARG 52 SER 53 -0.0003

SER 53 ILE 54 -0.0001

ILE 54 GLY 55 0.0330

GLY 55 PRO 56 -0.0001

PRO 56 ALA 57 -0.0001

ALA 57 MET 58 -0.0079

MET 58 PHE 59 -0.0000

PHE 59 GLU 60 -0.0001

GLU 60 GLY 61 -0.0359

GLY 61 GLU 62 0.0001

GLU 62 ALA 63 -0.0002

ALA 63 LEU 64 -0.0163

LEU 64 GLY 65 0.0003

GLY 65 LEU 66 0.0002

LEU 66 GLU 67 0.0299

GLU 67 ALA 68 -0.0001

ALA 68 MET 69 0.0002

MET 69 TYR 70 -0.0108

TYR 70 GLU 71 0.0005

GLU 71 THR 72 0.0001

THR 72 ARG 73 0.0040

ARG 73 THR 74 -0.0000

THR 74 ILE 75 0.0002

ILE 75 ARG 76 0.0016

ARG 76 VAL 77 -0.0004

VAL 77 PRO 78 -0.0000

PRO 78 ASN 79 -0.0532

ASN 79 PRO 80 0.0002

PRO 80 HIS 81 0.0000

HIS 81 LYS 82 -0.0142

LYS 82 ALA 83 -0.0003

ALA 83 GLY 84 -0.0000

GLY 84 GLU 85 -0.0110

GLU 85 LEU 86 -0.0000

LEU 86 PRO 87 -0.0001

PRO 87 THR 88 -0.0068

THR 88 GLY 89 -0.0003

GLY 89 GLY 90 0.0002

GLY 90 SER 91 -0.0019

SER 91 TYR 92 -0.0001

TYR 92 ILE 93 0.0002

ILE 93 ILE 94 -0.0160

ILE 94 MET 95 0.0002

MET 95 GLU 96 -0.0002

GLU 96 PHE 97 -0.0414

PHE 97 ILE 98 0.0001

ILE 98 ASP 99 0.0002

ASP 99 PHE 100 -0.1003

PHE 100 GLY 101 -0.0002

GLY 101 GLY 102 0.0001

GLY 102 SER 103 -0.1747

SER 103 ARG 104 -0.0002

ARG 104 GLY 105 0.0001

GLY 105 ASN 106 0.0828

ASN 106 GLN 107 -0.0003

GLN 107 ALA 108 0.0001

ALA 108 GLU 109 -0.0180

GLU 109 LEU 110 0.0001

LEU 110 GLY 111 0.0002

GLY 111 ARG 112 -0.0095

ARG 112 LYS 113 0.0001

LYS 113 LEU 114 -0.0004

LEU 114 ALA 115 0.0007

ALA 115 GLU 116 0.0004

GLU 116 MET 117 0.0005

MET 117 HIS 118 -0.0040

HIS 118 LYS 119 0.0006

LYS 119 ALA 120 0.0003

ALA 120 GLY 121 0.0151

GLY 121 LYS 122 0.0000

LYS 122 THR 123 0.0002

THR 123 SER 124 -0.0012

SER 124 LYS 125 0.0002

LYS 125 GLY 126 -0.0001

GLY 126 PHE 127 -0.0090

PHE 127 GLY 128 0.0001

GLY 128 PHE 129 0.0000

PHE 129 GLU 130 -0.0091

GLU 130 VAL 131 -0.0001

VAL 131 ASP 132 0.0004

ASP 132 ASN 133 0.0135

ASN 133 THR 134 -0.0004

THR 134 ILE 135 0.0004

ILE 135 GLY 136 0.0223

GLY 136 SER 137 0.0001

SER 137 THR 138 -0.0002

THR 138 PRO 139 0.0706

PRO 139 GLN 140 0.0002

GLN 140 ILE 141 0.0001

ILE 141 ASN 142 0.0568

ASN 142 THR 143 0.0001

THR 143 TRP 144 -0.0000

TRP 144 SER 145 -0.0234

SER 145 SER 146 0.0001

SER 146 ASP 147 0.0002

ASP 147 TRP 148 -0.0050

TRP 148 ILE 149 -0.0000

ILE 149 GLU 150 -0.0003

GLU 150 PHE 151 -0.0142

PHE 151 TYR 152 0.0000

TYR 152 GLY 153 -0.0002

GLY 153 GLU 154 -0.0021

GLU 154 LYS 155 0.0000

LYS 155 ARG 156 0.0000

ARG 156 LEU 157 -0.0053

LEU 157 GLY 158 0.0002

GLY 158 TYR 159 0.0000

TYR 159 GLN 160 0.0232

GLN 160 LEU 161 0.0001

LEU 161 LYS 162 -0.0000

LYS 162 LEU 163 -0.0032

LEU 163 ALA 164 0.0004

ALA 164 ARG 165 -0.0002

ARG 165 ASP 166 -0.0081

ASP 166 GLN 167 -0.0001

GLN 167 TYR 168 -0.0005

TYR 168 GLY 169 -0.0591

GLY 169 ASP 170 0.0001

ASP 170 SER 171 -0.0001

SER 171 ALA 172 -0.0189

ALA 172 ILE 173 -0.0001

ILE 173 TYR 174 0.0004

TYR 174 GLN 175 -0.0039

GLN 175 LYS 176 0.0002

LYS 176 GLY 177 -0.0002

GLY 177 HIS 178 -0.0017

HIS 178 HIS 178 0.1548

HIS 178 THR 179 -0.0003

THR 179 LEU 180 0.0003

LEU 180 ILE 181 -0.0312

ILE 181 GLN 182 0.0002

GLN 182 ASN 183 0.0003

ASN 183 MET 184 0.0064

MET 184 ALA 185 0.0000

ALA 185 PRO 186 -0.0005

PRO 186 LEU 187 0.0084

LEU 187 PHE 188 -0.0004

PHE 188 GLU 189 0.0001

GLU 189 ASN 190 -0.0249

ASN 190 VAL 191 0.0001

VAL 191 VAL 192 0.0001

VAL 192 ILE 193 -0.0117

ILE 193 GLU 194 0.0002

GLU 194 PRO 195 -0.0001

PRO 195 CYS 196 0.0008

CYS 196 LEU 197 -0.0004

LEU 197 LEU 198 0.0000

LEU 198 HIS 199 0.0037

HIS 199 GLY 200 -0.0000

GLY 200 ASP 201 0.0001

ASP 201 LEU 202 -0.0134

LEU 202 TRP 203 0.0002

TRP 203 SER 204 -0.0001

SER 204 GLY 205 0.0014

GLY 205 ASN 206 0.0001

ASN 206 ILE 207 0.0000

ILE 207 ALA 208 0.0012

ALA 208 TYR 209 0.0000

TYR 209 ASP 210 0.0001

ASP 210 LYS 211 -0.0002

LYS 211 ASN 212 -0.0001

ASN 212 ASN 213 -0.0003

ASN 213 GLU 214 -0.0559

GLU 214 PRO 215 0.0003

PRO 215 VAL 216 0.0003

VAL 216 ILE 217 -0.0124

ILE 217 LEU 218 0.0000

LEU 218 ASP 219 0.0000

ASP 219 PRO 220 -0.0193

PRO 220 ALA 221 -0.0002

ALA 221 CYS 222 -0.0000

CYS 222 TYR 223 -0.0179

TYR 223 TYR 224 -0.0002

TYR 224 GLY 225 0.0002

GLY 225 HIS 226 -0.0050

HIS 226 ASN 227 -0.0002

ASN 227 GLU 228 -0.0000

GLU 228 ALA 229 -0.0084

ALA 229 ASP 230 0.0002

ASP 230 PHE 231 0.0001

PHE 231 GLY 232 -0.0224

GLY 232 MET 233 -0.0002

MET 233 SER 234 0.0004

SER 234 TRP 235 -0.1007

TRP 235 CYS 236 -0.0000

CYS 236 ALA 237 0.0001

ALA 237 GLY 238 -0.0053

GLY 238 PHE 239 -0.0001

PHE 239 GLY 240 -0.0001

GLY 240 GLU 241 -0.0583

GLU 241 SER 242 -0.0003

SER 242 PHE 243 -0.0002

PHE 243 TYR 244 0.0393

TYR 244 ASN 245 0.0003

ASN 245 ALA 246 -0.0004

ALA 246 TYR 247 0.0169

TYR 247 PHE 248 -0.0001

PHE 248 LYS 249 -0.0003

LYS 249 VAL 250 0.0019

VAL 250 MET 251 -0.0003

MET 251 PRO 252 0.0001

PRO 252 LYS 253 -0.0231

LYS 253 GLN 254 0.0003

GLN 254 ALA 255 -0.0001

ALA 255 GLY 256 -0.0160

GLY 256 TYR 257 0.0002

TYR 257 GLU 258 -0.0001

GLU 258 LYS 259 -0.0023

LYS 259 ARG 260 0.0002

ARG 260 ARG 261 -0.0000

ARG 261 ASP 262 -0.0401

ASP 262 LEU 263 0.0002

LEU 263 TYR 264 0.0003

TYR 264 LEU 265 -0.0089

LEU 265 LEU 266 0.0001

LEU 266 TYR 267 0.0000

TYR 267 HIS 268 0.0084

HIS 268 TYR 269 0.0003

TYR 269 LEU 270 0.0001

LEU 270 ASN 271 -0.0138

ASN 271 HIS 272 0.0001

HIS 272 TYR 273 0.0000

TYR 273 ASN 274 0.0126

ASN 274 LEU 275 -0.0002

LEU 275 PHE 276 0.0003

PHE 276 GLY 277 0.1137

GLY 277 SER 278 -0.0001

SER 278 GLY 279 0.0001

GLY 279 TYR 280 -0.0341

TYR 280 ARG 281 0.0004

ARG 281 SER 282 0.0001

SER 282 SER 283 -0.0771

SER 283 ALA 284 0.0002

ALA 284 MET 285 0.0000

MET 285 SER 286 0.0177

SER 286 ILE 287 -0.0004

ILE 287 ILE 288 0.0003

ILE 288 ASP 289 0.0387

ASP 289 ASP 290 -0.0002

ASP 290 TYR 291 -0.0002

TYR 291 LEU 292 0.0378

LEU 292 ARG 293 -0.0001

ARG 293 MET 294 -0.0001

MET 294 LEU 295 0.0086

LEU 295 ASP 7 0.0048

ASP 7 PRO 8 0.0001

PRO 8 ILE 9 0.0001

ILE 9 ARG 10 0.0354

ARG 10 GLU 11 0.0003

GLU 11 TRP 12 0.0000

TRP 12 ILE 13 0.0047

ILE 13 LEU 14 -0.0000

LEU 14 THR 15 0.0003

THR 15 GLU 16 -0.0126

GLU 16 GLY 17 0.0000

GLY 17 LYS 18 -0.0001

LYS 18 ALA 19 0.0009

ALA 19 THR 20 0.0004

THR 20 GLN 21 -0.0001

GLN 21 ILE 22 0.0359

ILE 22 THR 23 -0.0000

THR 23 LYS 24 -0.0003

LYS 24 ILE 25 0.0648

ILE 25 GLY 26 0.0001

GLY 26 SER 27 -0.0003

SER 27 VAL 28 0.1860

VAL 28 GLY 29 0.0005

GLY 29 GLY 30 -0.0003

GLY 30 GLY 31 0.4110

GLY 31 CYS 32 -0.0002

CYS 32 ILE 33 0.0002

ILE 33 ASN 34 0.2802

ASN 34 LEU 35 -0.0001

LEU 35 ALA 36 0.0002

ALA 36 SER 37 0.1393

SER 37 HIS 38 -0.0002

HIS 38 TYR 39 -0.0001

TYR 39 GLN 40 0.0349

GLN 40 THR 41 0.0001

THR 41 ASP 42 -0.0002

ASP 42 ALA 43 0.0071

ALA 43 GLY 44 -0.0000

GLY 44 SER 45 -0.0003

SER 45 PHE 46 0.0036

PHE 46 PHE 47 -0.0002

PHE 47 VAL 48 0.0002

VAL 48 LYS 49 0.0634

LYS 49 THR 50 -0.0000

THR 50 ASN 51 -0.0000

ASN 51 ARG 52 -0.0263

ARG 52 SER 53 0.0003

SER 53 ILE 54 0.0001

ILE 54 GLY 55 0.0216

GLY 55 PRO 56 -0.0002

PRO 56 ALA 57 -0.0003

ALA 57 MET 58 0.0021

MET 58 PHE 59 0.0001

PHE 59 GLU 60 -0.0001

GLU 60 GLY 61 -0.0337

GLY 61 GLU 62 -0.0001

GLU 62 ALA 63 0.0002

ALA 63 LEU 64 -0.0114

LEU 64 GLY 65 0.0002

GLY 65 LEU 66 -0.0000

LEU 66 GLU 67 0.0258

GLU 67 ALA 68 -0.0002

ALA 68 MET 69 0.0001

MET 69 TYR 70 -0.0116

TYR 70 GLU 71 -0.0003

GLU 71 THR 72 0.0004

THR 72 ARG 73 0.0026

ARG 73 THR 74 -0.0002

THR 74 ILE 75 -0.0002

ILE 75 ARG 76 0.0007

ARG 76 VAL 77 -0.0002

VAL 77 PRO 78 0.0001

PRO 78 ASN 79 -0.0396

ASN 79 PRO 80 -0.0001

PRO 80 HIS 81 0.0005

HIS 81 LYS 82 0.0023

LYS 82 ALA 83 0.0001

ALA 83 GLY 84 0.0000

GLY 84 GLU 85 0.0064

GLU 85 LEU 86 0.0004

LEU 86 PRO 87 0.0000

PRO 87 THR 88 0.0127

THR 88 GLY 89 -0.0002

GLY 89 GLY 90 0.0006

GLY 90 SER 91 0.0037

SER 91 TYR 92 -0.0001

TYR 92 ILE 93 0.0002

ILE 93 ILE 94 -0.0180

ILE 94 MET 95 -0.0000

MET 95 GLU 96 -0.0002

GLU 96 PHE 97 -0.0448

PHE 97 ILE 98 -0.0003

ILE 98 ASP 99 0.0002

ASP 99 PHE 100 -0.0890

PHE 100 GLY 101 -0.0002

GLY 101 GLY 102 0.0000

GLY 102 SER 103 -0.1922

SER 103 ARG 104 -0.0002

ARG 104 GLY 105 0.0000

GLY 105 ASN 106 0.1024

ASN 106 GLN 107 -0.0001

GLN 107 ALA 108 -0.0002

ALA 108 GLU 109 -0.0258

GLU 109 LEU 110 -0.0005

LEU 110 GLY 111 0.0003

GLY 111 ARG 112 -0.0084

ARG 112 LYS 113 0.0000

LYS 113 LEU 114 -0.0001

LEU 114 ALA 115 -0.0019

ALA 115 GLU 116 0.0003

GLU 116 MET 117 -0.0003

MET 117 HIS 118 -0.0031

HIS 118 LYS 119 0.0003

LYS 119 ALA 120 0.0004

ALA 120 GLY 121 0.0090

GLY 121 LYS 122 -0.0000

LYS 122 THR 123 -0.0001

THR 123 SER 124 -0.0038

SER 124 LYS 125 0.0000

LYS 125 GLY 126 -0.0001

GLY 126 PHE 127 -0.0066

PHE 127 GLY 128 0.0002

GLY 128 PHE 129 -0.0004

PHE 129 GLU 130 -0.0082

GLU 130 VAL 131 -0.0002

VAL 131 ASP 132 -0.0003

ASP 132 ASN 133 0.0167

ASN 133 THR 134 0.0002

THR 134 ILE 135 0.0002

ILE 135 GLY 136 0.0203

GLY 136 SER 137 -0.0003

SER 137 THR 138 0.0002

THR 138 PRO 139 0.0693

PRO 139 GLN 140 0.0002

GLN 140 ILE 141 -0.0001

ILE 141 ASN 142 0.0537

ASN 142 THR 143 0.0002

THR 143 TRP 144 -0.0002

TRP 144 SER 145 -0.0198

SER 145 SER 146 0.0001

SER 146 ASP 147 -0.0001

ASP 147 TRP 148 -0.0042

TRP 148 ILE 149 0.0001

ILE 149 GLU 150 -0.0003

GLU 150 PHE 151 -0.0131

PHE 151 TYR 152 0.0001

TYR 152 GLY 153 -0.0001

GLY 153 GLU 154 -0.0031

GLU 154 LYS 155 0.0002

LYS 155 ARG 156 0.0001

ARG 156 LEU 157 -0.0064

LEU 157 GLY 158 -0.0001

GLY 158 TYR 159 0.0001

TYR 159 GLN 160 0.0236

GLN 160 LEU 161 0.0002

LEU 161 LYS 162 0.0002

LYS 162 LEU 163 0.0003

LEU 163 ALA 164 -0.0003

ALA 164 ARG 165 0.0003

ARG 165 ASP 166 -0.0086

ASP 166 GLN 167 -0.0002

GLN 167 TYR 168 0.0001

TYR 168 GLY 169 -0.0507

GLY 169 ASP 170 0.0002

ASP 170 SER 171 -0.0004

SER 171 ALA 172 -0.0151

ALA 172 ILE 173 0.0001

ILE 173 TYR 174 -0.0004

TYR 174 GLN 175 -0.0028

GLN 175 LYS 176 0.0003

LYS 176 GLY 177 -0.0005

GLY 177 HIS 178 -0.0011

HIS 178 THR 179 0.0000

THR 179 LEU 180 -0.0002

LEU 180 ILE 181 -0.0330

ILE 181 GLN 182 -0.0004

GLN 182 ASN 183 -0.0002

ASN 183 MET 184 0.0099

MET 184 ALA 185 -0.0002

ALA 185 PRO 186 0.0001

PRO 186 LEU 187 0.0076

LEU 187 PHE 188 0.0003

PHE 188 GLU 189 0.0001

GLU 189 ASN 190 -0.0248

ASN 190 VAL 191 0.0004

VAL 191 VAL 192 0.0001

VAL 192 ILE 193 -0.0095

ILE 193 GLU 194 -0.0001

GLU 194 PRO 195 0.0001

PRO 195 CYS 196 -0.0003

CYS 196 LEU 197 -0.0000

LEU 197 LEU 198 -0.0001

LEU 198 HIS 199 0.0007

HIS 199 GLY 200 0.0002

GLY 200 ASP 201 0.0002

ASP 201 LEU 202 -0.0141

LEU 202 TRP 203 -0.0001

TRP 203 SER 204 0.0004

SER 204 GLY 205 -0.0026

GLY 205 ASN 206 0.0000

ASN 206 ILE 207 0.0001

ILE 207 ALA 208 0.0047

ALA 208 TYR 209 0.0001

TYR 209 ASP 210 -0.0000

ASP 210 LYS 211 0.0071

LYS 211 ASN 212 -0.0000

ASN 212 ASN 213 0.0004

ASN 213 GLU 214 -0.0411

GLU 214 PRO 215 -0.0002

PRO 215 VAL 216 -0.0001

VAL 216 ILE 217 -0.0138

ILE 217 LEU 218 0.0002

LEU 218 ASP 219 -0.0002

ASP 219 PRO 220 -0.0224

PRO 220 ALA 221 0.0004

ALA 221 CYS 222 0.0001

CYS 222 TYR 223 -0.0193

TYR 223 TYR 224 -0.0001

TYR 224 GLY 225 0.0002

GLY 225 HIS 226 -0.0031

HIS 226 ASN 227 0.0003

ASN 227 GLU 228 -0.0000

GLU 228 ALA 229 -0.0065

ALA 229 ASP 230 -0.0002

ASP 230 PHE 231 0.0000

PHE 231 GLY 232 -0.0195

GLY 232 MET 233 0.0001

MET 233 SER 234 0.0003

SER 234 TRP 235 -0.0977

TRP 235 CYS 236 0.0002

CYS 236 ALA 237 -0.0001

ALA 237 GLY 238 0.0036

GLY 238 PHE 239 -0.0001

PHE 239 GLY 240 -0.0001

GLY 240 GLU 241 -0.0525

GLU 241 SER 242 0.0003

SER 242 PHE 243 0.0002

PHE 243 TYR 244 0.0347

TYR 244 ASN 245 -0.0001

ASN 245 ALA 246 -0.0002

ALA 246 TYR 247 0.0110

TYR 247 PHE 248 -0.0002

PHE 248 LYS 249 -0.0002

LYS 249 VAL 250 0.0047

VAL 250 MET 251 0.0000

MET 251 PRO 252 0.0001

PRO 252 LYS 253 -0.0174

LYS 253 GLN 254 0.0002

GLN 254 ALA 255 0.0000

ALA 255 GLY 256 -0.0098

GLY 256 TYR 257 -0.0002

TYR 257 GLU 258 -0.0004

GLU 258 LYS 259 -0.0012

LYS 259 ARG 260 0.0003

ARG 260 ARG 261 0.0003

ARG 261 ASP 262 -0.0373

ASP 262 LEU 263 -0.0001

LEU 263 TYR 264 -0.0000

TYR 264 LEU 265 -0.0065

LEU 265 LEU 266 0.0001

LEU 266 TYR 267 -0.0002

TYR 267 HIS 268 0.0086

HIS 268 TYR 269 0.0004

TYR 269 LEU 270 0.0001

LEU 270 ASN 271 -0.0150

ASN 271 HIS 272 -0.0003

HIS 272 TYR 273 0.0000

TYR 273 ASN 274 0.0101

ASN 274 LEU 275 -0.0000

LEU 275 PHE 276 -0.0002

PHE 276 GLY 277 0.1060

GLY 277 SER 278 0.0001

SER 278 GLY 279 0.0002

GLY 279 TYR 280 -0.0329

TYR 280 ARG 281 0.0000

ARG 281 SER 282 0.0005

SER 282 SER 283 -0.0634

SER 283 ALA 284 0.0001

ALA 284 MET 285 0.0000

MET 285 SER 286 0.0113

SER 286 ILE 287 -0.0001

ILE 287 ILE 288 -0.0002

ILE 288 ASP 289 0.0324

ASP 289 ASP 290 -0.0002

ASP 290 TYR 291 0.0001

TYR 291 LEU 292 0.0360

LEU 292 ARG 293 0.0002

ARG 293 MET 294 0.0001

MET 294 LEU 295 0.0049

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.

*** EUTLA ***

CA strain for 22123022061855342

--- normal mode 9 ---

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

* EUTLA *