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

* Chappie dimer compare ver 3 *

CA strain for 221218005903105706

--- normal mode 11 ---

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 LYS 2 0.0002

LYS 2 ASN 3 0.0003

ASN 3 GLY 4 0.0856

GLY 4 PHE 5 0.0003

PHE 5 TYR 6 -0.0002

TYR 6 ALA 7 0.0035

ALA 7 THR 8 0.0002

THR 8 TYR 9 -0.0001

TYR 9 ARG 10 0.0007

ARG 10 SER 11 -0.0001

SER 11 LYS 12 -0.0002

LYS 12 ASN 13 0.0106

ASN 13 LYS 14 0.0004

LYS 14 GLY 15 -0.0001

GLY 15 LYS 16 0.0226

LYS 16 ASP 17 -0.0003

ASP 17 LYS 18 0.0002

LYS 18 ARG 19 -0.0782

ARG 19 SER 20 -0.0002

SER 20 ILE 21 -0.0000

ILE 21 ASN 22 -0.0299

ASN 22 LEU 23 -0.0001

LEU 23 SER 24 -0.0003

SER 24 VAL 25 0.0903

VAL 25 PHE 26 -0.0004

PHE 26 LEU 27 0.0002

LEU 27 ASN 28 -0.0006

ASN 28 SER 29 -0.0001

SER 29 LEU 30 -0.0005

LEU 30 ASN 34 -0.0247

ASN 34 HIS 35 0.0001

HIS 35 HIS 36 0.0001

HIS 36 LEU 37 0.0242

LEU 37 GLN 38 -0.0000

GLN 38 VAL 39 0.0002

VAL 39 GLY 40 0.0432

GLY 40 SER 41 -0.0001

SER 41 ASN 42 -0.0000

ASN 42 TYR 43 0.0155

TYR 43 LEU 44 -0.0001

LEU 44 TYR 45 -0.0001

TYR 45 ILE 46 0.0565

ILE 46 HIS 47 0.0000

HIS 47 LYS 48 0.0002

LYS 48 ILE 49 0.0562

ILE 49 ASP 50 0.0000

ASP 50 GLY 51 0.0002

GLY 51 LYS 52 -0.1091

LYS 52 THR 53 0.0002

THR 53 PHE 54 -0.0003

PHE 54 LEU 55 -0.0245

LEU 55 PHE 56 -0.0000

PHE 56 THR 57 -0.0004

THR 57 LYS 58 -0.0133

LYS 58 THR 59 -0.0000

THR 59 ASN 60 0.0000

ASN 60 ASP 61 -0.0020

ASP 61 LYS 62 0.0002

LYS 62 SER 63 -0.0000

SER 63 LEU 64 -0.0203

LEU 64 VAL 65 0.0001

VAL 65 GLN 66 -0.0000

GLN 66 LYS 67 0.0056

LYS 67 ILE 68 0.0002

ILE 68 ASN 69 0.0000

ASN 69 ARG 70 -0.0076

ARG 70 SER 71 0.0002

SER 71 LYS 72 -0.0001

LYS 72 ALA 73 0.0324

ALA 73 SER 74 -0.0001

SER 74 VAL 75 -0.0000

VAL 75 GLU 76 -0.0165

GLU 76 ASP 77 -0.0005

ASP 77 ILE 78 0.0002

ILE 78 LYS 79 0.0218

LYS 79 ASN 80 -0.0003

ASN 80 SER 81 0.0003

SER 81 LEU 82 0.0264

LEU 82 ALA 83 0.0003

ALA 83 ASP 84 -0.0002

ASP 84 ASP 85 -0.0569

ASP 85 GLU 86 0.0000

GLU 86 SER 87 0.0002

SER 87 LEU 88 -0.0105

LEU 88 GLY 89 0.0003

GLY 89 PHE 90 -0.0001

PHE 90 PRO 91 -0.0489

PRO 91 SER 92 0.0002

SER 92 PHE 93 -0.0000

PHE 93 LEU 94 -0.0010

LEU 94 PHE 95 0.0004

PHE 95 VAL 96 -0.0002

VAL 96 GLU 97 -0.0294

GLU 97 GLY 98 0.0003

GLY 98 ASP 99 -0.0001

ASP 99 THR 100 0.1199

THR 100 ILE 101 0.0004

ILE 101 GLY 102 0.0003

GLY 102 PHE 103 0.0444

PHE 103 ALA 104 -0.0002

ALA 104 ARG 105 0.0001

ARG 105 THR 106 0.0502

THR 106 VAL 107 -0.0000

VAL 107 PHE 108 0.0001

PHE 108 GLY 109 0.0382

GLY 109 PRO 110 -0.0001

PRO 110 THR 111 0.0000

THR 111 THR 112 0.1212

THR 112 SER 113 0.0000

SER 113 ASP 114 -0.0002

ASP 114 LEU 115 0.0272

LEU 115 THR 116 -0.0001

THR 116 ASP 117 -0.0003

ASP 117 PHE 118 -0.0141

PHE 118 LEU 119 -0.0001

LEU 119 ILE 120 -0.0003

ILE 120 GLY 121 0.0351

GLY 121 LYS 122 -0.0002

LYS 122 GLY 123 0.0001

GLY 123 MET 124 -0.0014

MET 124 SER 125 0.0001

SER 125 LEU 126 -0.0003

LEU 126 SER 127 0.0576

SER 127 SER 128 -0.0003

SER 128 GLY 129 0.0001

GLY 129 GLU 130 -0.0249

GLU 130 ARG 131 -0.0003

ARG 131 VAL 132 0.0002

VAL 132 GLN 133 -0.1977

GLN 133 ILE 134 0.0000

ILE 134 GLU 135 -0.0002

GLU 135 PRO 136 -0.4456

PRO 136 LEU 137 -0.0001

LEU 137 MET 138 0.0005

MET 138 ARG 139 0.0662

ARG 139 GLY 140 0.0003

GLY 140 THR 141 0.0001

THR 141 THR 142 -0.3381

THR 142 LYS 143 0.0005

LYS 143 ASP 144 0.0000

ASP 144 ASP 145 0.0744

ASP 145 VAL 146 0.0001

VAL 146 MET 147 -0.0000

MET 147 HIS 148 0.0224

HIS 148 MET 149 -0.0001

MET 149 HIS 150 -0.0002

HIS 150 PHE 151 0.0666

PHE 151 ILE 152 -0.0004

ILE 152 GLY 153 -0.0000

GLY 153 ARG 154 0.0312

ARG 154 THR 155 -0.0001

THR 155 THR 156 -0.0001

THR 156 VAL 157 -0.0639

VAL 157 LYS 158 0.0004

LYS 158 VAL 159 -0.0001

VAL 159 GLU 160 -0.0269

GLU 160 ALA 161 0.0002

ALA 161 LYS 162 0.0003

LYS 162 LEU 163 0.0323

LEU 163 PRO 164 -0.0004

PRO 164 VAL 165 -0.0000

VAL 165 PHE 166 -0.0367

PHE 166 GLY 167 -0.0001

GLY 167 ASP 168 -0.0001

ASP 168 ILE 169 -0.0139

ILE 169 LEU 170 -0.0001

LEU 170 LYS 171 -0.0000

LYS 171 VAL 172 -0.0434

VAL 172 LEU 173 0.0001

LEU 173 GLY 174 -0.0002

GLY 174 ALA 175 -0.0441

ALA 175 THR 176 -0.0005

THR 176 ASP 177 -0.0001

ASP 177 ILE 178 0.0048

ILE 178 GLU 179 -0.0001

GLU 179 GLY 180 0.0000

GLY 180 GLU 181 -0.0348

GLU 181 LEU 182 -0.0001

LEU 182 PHE 183 -0.0000

PHE 183 ASP 184 0.0853

ASP 184 SER 185 0.0001

SER 185 LEU 186 0.0003

LEU 186 ASP 187 0.0302

ASP 187 ILE 188 -0.0000

ILE 188 VAL 189 -0.0004

VAL 189 ILE 190 0.0136

ILE 190 LYS 191 0.0000

LYS 191 PRO 192 0.0002

PRO 192 LYS 193 -0.0320

LYS 193 PHE 194 0.0001

PHE 194 LYS 195 0.0000

LYS 195 ARG 196 0.0026

ARG 196 ASP 197 -0.0003

ASP 197 ILE 198 0.0001

ILE 198 LYS 199 0.0574

LYS 199 LYS 200 0.0003

LYS 200 VAL 201 0.0003

VAL 201 ALA 202 -0.0054

ALA 202 LYS 203 -0.0002

LYS 203 ASP 204 -0.0003

ASP 204 ILE 205 0.0435

ILE 205 ILE 206 0.0000

ILE 206 PHE 207 -0.0002

PHE 207 ASN 208 -0.0636

ASN 208 PRO 209 0.0003

PRO 209 SER 210 0.0003

SER 210 PRO 211 0.0169

PRO 211 GLN 212 -0.0002

GLN 212 PHE 213 -0.0001

PHE 213 SER 214 0.1779

SER 214 ASP 215 0.0002

ASP 215 ILE 216 -0.0001

ILE 216 SER 217 -0.0732

SER 217 LEU 218 -0.0001

LEU 218 ARG 219 -0.0001

ARG 219 ALA 220 -0.0164

ALA 220 LYS 221 -0.0000

LYS 221 ASP 222 0.0001

ASP 222 GLU 223 -0.0457

GLU 223 ALA 224 0.0001

ALA 224 GLY 225 -0.0000

GLY 225 ASP 226 -0.0488

ASP 226 LEU 228 -0.0466

LEU 228 THR 229 -0.0003

THR 229 GLU 230 -0.0000

GLU 230 HIS 231 -0.0161

HIS 231 TYR 232 -0.0001

TYR 232 LEU 233 0.0001

LEU 233 SER 234 0.0764

SER 234 GLU 235 -0.0003

GLU 235 LYS 236 0.0002

LYS 236 GLY 237 -0.3619

GLY 237 HIS 238 -0.0004

HIS 238 LEU 239 0.0001

LEU 239 SER 240 0.2747

SER 240 ALA 241 0.0002

ALA 241 PRO 242 -0.0001

PRO 242 LEU 243 -0.0430

LEU 243 ASN 244 0.0002

ASN 244 LYS 245 -0.0006

LYS 245 VAL 246 -0.0949

VAL 246 THR 247 0.0003

THR 247 ASN 248 -0.0002

ASN 248 ALA 249 -0.0190

ALA 249 GLU 250 -0.0003

GLU 250 ILE 251 0.0002

ILE 251 ALA 252 -0.0858

ALA 252 GLU 253 0.0002

GLU 253 GLU 254 -0.0001

GLU 254 MET 255 -0.0373

MET 255 ALA 256 0.0001

ALA 256 TYR 257 -0.0001

TYR 257 CYS 258 -0.0148

CYS 258 TYR 259 0.0001

TYR 259 ALA 260 -0.0002

ALA 260 ARG 261 0.2103

ARG 261 MET 262 -0.0003

MET 262 LYS 263 -0.0003

LYS 263 SER 264 -0.0726

SER 264 ASP 265 -0.0002

ASP 265 ILE 266 -0.0002

ILE 266 LEU 267 -0.0444

LEU 267 GLU 268 0.0000

GLU 268 CYS 269 0.0001

CYS 269 PHE 270 0.0299

PHE 270 LYS 271 0.0003

LYS 271 ARG 272 0.0003

ARG 272 GLN 273 -0.0088

GLN 273 VAL 274 0.0003

VAL 274 GLY 275 0.0002

GLY 275 LYS 276 -0.0162

LYS 276 VAL 277 0.0001

VAL 277 LYS 278 0.0000

LYS 278 ASP 279 -0.1388

ASP 279 MET 1 0.1267

MET 1 LYS 2 -0.0003

LYS 2 ASN 3 -0.0000

ASN 3 GLY 4 -0.0126

GLY 4 PHE 5 -0.0004

PHE 5 TYR 6 0.0002

TYR 6 ALA 7 0.0557

ALA 7 THR 8 0.0000

THR 8 TYR 9 0.0001

TYR 9 ARG 10 -0.0050

ARG 10 SER 11 0.0003

SER 11 LYS 12 -0.0001

LYS 12 ASN 13 -0.0235

ASN 13 LYS 14 0.0001

LYS 14 GLY 15 -0.0001

GLY 15 LYS 16 0.0136

LYS 16 ASP 17 0.0001

ASP 17 LYS 18 0.0002

LYS 18 ARG 19 -0.0062

ARG 19 SER 20 -0.0003

SER 20 ILE 21 -0.0001

ILE 21 ASN 22 0.0258

ASN 22 LEU 23 0.0002

LEU 23 SER 24 -0.0002

SER 24 VAL 25 -0.0454

VAL 25 PHE 26 -0.0001

PHE 26 LEU 27 -0.0004

LEU 27 ASN 28 0.0237

ASN 28 SER 29 -0.0000

SER 29 LEU 30 0.0004

LEU 30 LEU 31 0.0365

LEU 31 ALA 32 -0.0002

ALA 32 ASP 33 -0.0003

ASP 33 ASN 34 0.0406

ASN 34 HIS 35 -0.0002

HIS 35 HIS 36 0.0003

HIS 36 LEU 37 -0.0073

LEU 37 GLN 38 -0.0003

GLN 38 VAL 39 0.0001

VAL 39 GLY 40 -0.0254

GLY 40 SER 41 -0.0003

SER 41 ASN 42 -0.0004

ASN 42 TYR 43 -0.0160

TYR 43 LEU 44 -0.0000

LEU 44 TYR 45 -0.0003

TYR 45 ILE 46 -0.0923

ILE 46 HIS 47 -0.0002

HIS 47 LYS 48 0.0000

LYS 48 ILE 49 -0.0575

ILE 49 ASP 50 -0.0002

ASP 50 GLY 51 0.0004

GLY 51 LYS 52 -0.0099

LYS 52 THR 53 -0.0003

THR 53 PHE 54 -0.0002

PHE 54 LEU 55 -0.0258

LEU 55 PHE 56 0.0000

PHE 56 THR 57 -0.0003

THR 57 LYS 58 -0.0275

LYS 58 THR 59 -0.0000

THR 59 ASN 60 0.0001

ASN 60 ASP 61 0.0166

ASP 61 LYS 62 -0.0002

LYS 62 SER 63 -0.0002

SER 63 LEU 64 -0.0072

LEU 64 VAL 65 -0.0000

VAL 65 GLN 66 -0.0003

GLN 66 LYS 67 0.0007

LYS 67 ILE 68 -0.0002

ILE 68 ASN 69 -0.0003

ASN 69 ARG 70 0.0056

ARG 70 SER 71 -0.0003

SER 71 LYS 72 0.0001

LYS 72 ALA 73 -0.0320

ALA 73 SER 74 0.0002

SER 74 VAL 75 -0.0001

VAL 75 GLU 76 0.0132

GLU 76 ASP 77 -0.0000

ASP 77 ILE 78 -0.0003

ILE 78 LYS 79 -0.0686

LYS 79 ASN 80 -0.0002

ASN 80 SER 81 -0.0000

SER 81 LEU 82 0.0116

LEU 82 ALA 83 -0.0002

ALA 83 ASP 84 0.0000

ASP 84 ASP 85 0.0452

ASP 85 GLU 86 0.0001

GLU 86 SER 87 0.0002

SER 87 LEU 88 0.0006

LEU 88 GLY 89 0.0002

GLY 89 PHE 90 0.0001

PHE 90 PRO 91 -0.0008

PRO 91 SER 92 -0.0001

SER 92 PHE 93 0.0000

PHE 93 LEU 94 -0.0221

LEU 94 PHE 95 -0.0002

PHE 95 VAL 96 -0.0002

VAL 96 GLU 97 -0.0376

GLU 97 GLY 98 0.0000

GLY 98 ASP 99 0.0003

ASP 99 THR 100 -0.0414

THR 100 ILE 101 -0.0000

ILE 101 GLY 102 0.0003

GLY 102 PHE 103 -0.0271

PHE 103 ALA 104 0.0004

ALA 104 ARG 105 -0.0000

ARG 105 THR 106 -0.0497

THR 106 VAL 107 -0.0002

VAL 107 PHE 108 -0.0002

PHE 108 GLY 109 -0.0473

GLY 109 PRO 110 -0.0004

PRO 110 THR 111 0.0001

THR 111 THR 112 -0.0499

THR 112 SER 113 0.0003

SER 113 ASP 114 -0.0004

ASP 114 LEU 115 -0.0348

LEU 115 THR 116 -0.0000

THR 116 ASP 117 -0.0001

ASP 117 PHE 118 0.0169

PHE 118 LEU 119 -0.0001

LEU 119 ILE 120 -0.0001

ILE 120 GLY 121 0.0020

GLY 121 LYS 122 0.0002

LYS 122 GLY 123 0.0001

GLY 123 MET 124 -0.0563

MET 124 SER 125 0.0002

SER 125 LEU 126 0.0002

LEU 126 SER 127 -0.0129

SER 127 SER 128 0.0003

SER 128 GLY 129 -0.0002

GLY 129 GLU 130 0.0013

GLU 130 ARG 131 -0.0000

ARG 131 VAL 132 -0.0002

VAL 132 GLN 133 0.1570

GLN 133 ILE 134 -0.0002

ILE 134 GLU 135 0.0000

GLU 135 PRO 136 0.3725

PRO 136 LEU 137 -0.0001

LEU 137 MET 138 -0.0001

MET 138 ARG 139 0.1150

ARG 139 GLY 140 -0.0002

GLY 140 THR 141 -0.0001

THR 141 THR 142 0.1753

THR 142 LYS 143 -0.0003

LYS 143 ASP 144 -0.0001

ASP 144 ASP 145 0.0048

ASP 145 VAL 146 0.0003

VAL 146 MET 147 0.0002

MET 147 HIS 148 -0.0274

HIS 148 MET 149 -0.0002

MET 149 HIS 150 -0.0002

HIS 150 PHE 151 -0.0642

PHE 151 ILE 152 -0.0001

ILE 152 GLY 153 -0.0003

GLY 153 ARG 154 -0.0146

ARG 154 THR 155 -0.0000

THR 155 THR 156 -0.0002

THR 156 VAL 157 0.0436

VAL 157 LYS 158 -0.0002

LYS 158 VAL 159 -0.0002

VAL 159 GLU 160 0.0068

GLU 160 ALA 161 0.0002

ALA 161 LYS 162 -0.0000

LYS 162 LEU 163 0.0223

LEU 163 PRO 164 -0.0000

PRO 164 VAL 165 -0.0000

VAL 165 PHE 166 0.0568

PHE 166 GLY 167 0.0001

GLY 167 ASP 168 -0.0000

ASP 168 ILE 169 0.0052

ILE 169 LEU 170 -0.0003

LEU 170 LYS 171 0.0002

LYS 171 VAL 172 0.0436

VAL 172 LEU 173 -0.0002

LEU 173 GLY 174 -0.0000

GLY 174 ALA 175 0.0524

ALA 175 THR 176 -0.0000

THR 176 ASP 177 0.0001

ASP 177 ILE 178 -0.0099

ILE 178 GLU 179 -0.0003

GLU 179 GLY 180 0.0002

GLY 180 GLU 181 0.0151

GLU 181 LEU 182 -0.0002

LEU 182 PHE 183 -0.0002

PHE 183 ASP 184 -0.0485

ASP 184 SER 185 0.0003

SER 185 LEU 186 -0.0001

LEU 186 ASP 187 -0.0148

ASP 187 ILE 188 0.0000

ILE 188 VAL 189 0.0002

VAL 189 ILE 190 0.0076

ILE 190 LYS 191 0.0002

LYS 191 PRO 192 -0.0000

PRO 192 LYS 193 0.0112

LYS 193 PHE 194 0.0000

PHE 194 LYS 195 -0.0002

LYS 195 ARG 196 -0.0302

ARG 196 ASP 197 0.0001

ASP 197 ILE 198 -0.0001

ILE 198 LYS 199 -0.0229

LYS 199 LYS 200 0.0002

LYS 200 VAL 201 0.0001

VAL 201 ALA 202 0.0110

ALA 202 LYS 203 0.0000

LYS 203 ASP 204 -0.0001

ASP 204 ILE 205 -0.0442

ILE 205 ILE 206 0.0002

ILE 206 PHE 207 -0.0002

PHE 207 ASN 208 0.0925

ASN 208 PRO 209 -0.0000

PRO 209 SER 210 -0.0004

SER 210 PRO 211 0.0019

PRO 211 GLN 212 -0.0002

GLN 212 PHE 213 0.0002

PHE 213 SER 214 -0.2325

SER 214 ASP 215 -0.0001

ASP 215 ILE 216 0.0002

ILE 216 SER 217 0.0615

SER 217 LEU 218 0.0001

LEU 218 ARG 219 -0.0005

ARG 219 ALA 220 -0.0621

ALA 220 LYS 221 -0.0000

LYS 221 ASP 222 -0.0000

ASP 222 GLU 223 0.0427

GLU 223 ALA 224 -0.0001

ALA 224 GLY 225 -0.0002

GLY 225 ASP 226 0.0441

ASP 226 ILE 227 0.0002

ILE 227 LEU 228 -0.0004

LEU 228 THR 229 0.1235

THR 229 GLU 230 -0.0001

GLU 230 HIS 231 0.0002

HIS 231 TYR 232 0.0212

TYR 232 LEU 233 0.0002

LEU 233 SER 234 0.0003

SER 234 GLU 235 0.0358

GLU 235 LYS 236 0.0002

LYS 236 GLY 237 0.0001

GLY 237 HIS 238 0.0039

HIS 238 LEU 239 -0.0000

LEU 239 SER 240 0.0001

SER 240 ALA 241 -0.0907

ALA 241 PRO 242 -0.0002

PRO 242 LEU 243 -0.0005

LEU 243 ASN 244 -0.0573

ASN 244 LYS 245 -0.0002

LYS 245 VAL 246 0.0000

VAL 246 THR 247 -0.0074

THR 247 ASN 248 -0.0001

ASN 248 ALA 249 -0.0004

ALA 249 GLU 250 -0.0514

GLU 250 ILE 251 0.0001

ILE 251 ALA 252 -0.0000

ALA 252 GLU 253 -0.0535

GLU 253 GLU 254 0.0001

GLU 254 MET 255 0.0004

MET 255 ALA 256 0.0580

ALA 256 TYR 257 0.0003

TYR 257 CYS 258 0.0001

CYS 258 TYR 259 0.1294

TYR 259 ALA 260 -0.0002

ALA 260 ARG 261 0.0000

ARG 261 MET 262 0.1845

MET 262 LYS 263 -0.0004

LYS 263 SER 264 -0.0002

SER 264 ASP 265 -0.0098

ASP 265 ILE 266 -0.0002

ILE 266 LEU 267 -0.0003

LEU 267 GLU 268 -0.0104

GLU 268 CYS 269 -0.0002

CYS 269 PHE 270 -0.0001

PHE 270 LYS 271 -0.0838

LYS 271 ARG 272 -0.0000

ARG 272 GLN 273 0.0001

GLN 273 VAL 274 0.0388

VAL 274 GLY 275 0.0000

GLY 275 LYS 276 0.0001

LYS 276 VAL 277 -0.1951

VAL 277 LYS 278 0.0005

LYS 278 ASP 279 0.0000

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.

*** Chappie dimer compare ver 3 ***

CA strain for 221218005903105706

--- normal mode 11 ---

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

* Chappie dimer compare ver 3 *