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

* Chappie dimer compare ver 3 *

CA strain for 221218005903105706

--- 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
MET 1 LYS 2 -0.0005

LYS 2 ASN 3 0.0003

ASN 3 GLY 4 -0.0516

GLY 4 PHE 5 0.0000

PHE 5 TYR 6 -0.0004

TYR 6 ALA 7 0.0386

ALA 7 THR 8 -0.0001

THR 8 TYR 9 0.0002

TYR 9 ARG 10 -0.0162

ARG 10 SER 11 0.0003

SER 11 LYS 12 -0.0002

LYS 12 ASN 13 0.0330

ASN 13 LYS 14 0.0003

LYS 14 GLY 15 -0.0001

GLY 15 LYS 16 0.0708

LYS 16 ASP 17 -0.0003

ASP 17 LYS 18 0.0002

LYS 18 ARG 19 -0.0766

ARG 19 SER 20 0.0000

SER 20 ILE 21 -0.0000

ILE 21 ASN 22 0.0049

ASN 22 LEU 23 0.0001

LEU 23 SER 24 -0.0000

SER 24 VAL 25 0.0086

VAL 25 PHE 26 -0.0004

PHE 26 LEU 27 -0.0001

LEU 27 ASN 28 0.0423

ASN 28 SER 29 -0.0001

SER 29 LEU 30 0.0000

LEU 30 ASN 34 -0.1221

ASN 34 HIS 35 -0.0002

HIS 35 HIS 36 -0.0002

HIS 36 LEU 37 -0.0041

LEU 37 GLN 38 0.0002

GLN 38 VAL 39 0.0001

VAL 39 GLY 40 0.0123

GLY 40 SER 41 0.0001

SER 41 ASN 42 -0.0003

ASN 42 TYR 43 -0.0144

TYR 43 LEU 44 0.0003

LEU 44 TYR 45 0.0001

TYR 45 ILE 46 -0.0833

ILE 46 HIS 47 -0.0001

HIS 47 LYS 48 0.0001

LYS 48 ILE 49 0.0703

ILE 49 ASP 50 0.0003

ASP 50 GLY 51 0.0001

GLY 51 LYS 52 -0.0888

LYS 52 THR 53 0.0002

THR 53 PHE 54 -0.0002

PHE 54 LEU 55 -0.0927

LEU 55 PHE 56 0.0002

PHE 56 THR 57 -0.0002

THR 57 LYS 58 -0.0555

LYS 58 THR 59 -0.0001

THR 59 ASN 60 0.0001

ASN 60 ASP 61 0.0379

ASP 61 LYS 62 0.0001

LYS 62 SER 63 0.0002

SER 63 LEU 64 -0.0292

LEU 64 VAL 65 -0.0003

VAL 65 GLN 66 0.0001

GLN 66 LYS 67 0.0155

LYS 67 ILE 68 0.0002

ILE 68 ASN 69 0.0001

ASN 69 ARG 70 0.0091

ARG 70 SER 71 -0.0000

SER 71 LYS 72 -0.0002

LYS 72 ALA 73 -0.0294

ALA 73 SER 74 -0.0001

SER 74 VAL 75 -0.0001

VAL 75 GLU 76 -0.0058

GLU 76 ASP 77 -0.0003

ASP 77 ILE 78 0.0001

ILE 78 LYS 79 -0.0033

LYS 79 ASN 80 0.0006

ASN 80 SER 81 -0.0003

SER 81 LEU 82 0.1107

LEU 82 ALA 83 0.0003

ALA 83 ASP 84 0.0000

ASP 84 ASP 85 0.0327

ASP 85 GLU 86 0.0001

GLU 86 SER 87 -0.0002

SER 87 LEU 88 -0.0000

LEU 88 GLY 89 -0.0001

GLY 89 PHE 90 -0.0002

PHE 90 PRO 91 -0.0599

PRO 91 SER 92 -0.0003

SER 92 PHE 93 0.0001

PHE 93 LEU 94 -0.0623

LEU 94 PHE 95 0.0001

PHE 95 VAL 96 0.0001

VAL 96 GLU 97 -0.1059

GLU 97 GLY 98 -0.0003

GLY 98 ASP 99 -0.0002

ASP 99 THR 100 0.0461

THR 100 ILE 101 -0.0000

ILE 101 GLY 102 0.0003

GLY 102 PHE 103 -0.0392

PHE 103 ALA 104 -0.0000

ALA 104 ARG 105 0.0004

ARG 105 THR 106 -0.0346

THR 106 VAL 107 0.0001

VAL 107 PHE 108 0.0000

PHE 108 GLY 109 -0.0326

GLY 109 PRO 110 -0.0001

PRO 110 THR 111 -0.0004

THR 111 THR 112 0.0457

THR 112 SER 113 0.0002

SER 113 ASP 114 0.0001

ASP 114 LEU 115 -0.0285

LEU 115 THR 116 0.0001

THR 116 ASP 117 -0.0000

ASP 117 PHE 118 0.0266

PHE 118 LEU 119 -0.0002

LEU 119 ILE 120 -0.0001

ILE 120 GLY 121 0.0458

GLY 121 LYS 122 0.0000

LYS 122 GLY 123 0.0005

GLY 123 MET 124 -0.0845

MET 124 SER 125 0.0002

SER 125 LEU 126 -0.0001

LEU 126 SER 127 0.0239

SER 127 SER 128 -0.0002

SER 128 GLY 129 -0.0001

GLY 129 GLU 130 -0.0251

GLU 130 ARG 131 0.0001

ARG 131 VAL 132 -0.0003

VAL 132 GLN 133 0.0266

GLN 133 ILE 134 0.0000

ILE 134 GLU 135 -0.0002

GLU 135 PRO 136 0.0046

PRO 136 LEU 137 -0.0003

LEU 137 MET 138 -0.0002

MET 138 ARG 139 0.0386

ARG 139 GLY 140 0.0001

GLY 140 THR 141 0.0000

THR 141 THR 142 0.0529

THR 142 LYS 143 -0.0002

LYS 143 ASP 144 -0.0000

ASP 144 ASP 145 -0.0297

ASP 145 VAL 146 -0.0003

VAL 146 MET 147 0.0000

MET 147 HIS 148 -0.0316

HIS 148 MET 149 -0.0001

MET 149 HIS 150 0.0002

HIS 150 PHE 151 -0.0131

PHE 151 ILE 152 0.0002

ILE 152 GLY 153 -0.0004

GLY 153 ARG 154 -0.0861

ARG 154 THR 155 0.0001

THR 155 THR 156 -0.0002

THR 156 VAL 157 0.0499

VAL 157 LYS 158 -0.0001

LYS 158 VAL 159 0.0003

VAL 159 GLU 160 -0.0004

GLU 160 ALA 161 -0.0003

ALA 161 LYS 162 -0.0002

LYS 162 LEU 163 -0.0031

LEU 163 PRO 164 0.0002

PRO 164 VAL 165 -0.0001

VAL 165 PHE 166 0.0435

PHE 166 GLY 167 -0.0002

GLY 167 ASP 168 -0.0004

ASP 168 ILE 169 0.0077

ILE 169 LEU 170 0.0005

LEU 170 LYS 171 0.0000

LYS 171 VAL 172 0.0122

VAL 172 LEU 173 -0.0003

LEU 173 GLY 174 -0.0001

GLY 174 ALA 175 0.0104

ALA 175 THR 176 0.0001

THR 176 ASP 177 0.0001

ASP 177 ILE 178 -0.0158

ILE 178 GLU 179 0.0001

GLU 179 GLY 180 0.0001

GLY 180 GLU 181 -0.0026

GLU 181 LEU 182 0.0002

LEU 182 PHE 183 0.0000

PHE 183 ASP 184 -0.1362

ASP 184 SER 185 -0.0003

SER 185 LEU 186 -0.0002

LEU 186 ASP 187 0.0302

ASP 187 ILE 188 -0.0001

ILE 188 VAL 189 -0.0001

VAL 189 ILE 190 -0.0289

ILE 190 LYS 191 -0.0000

LYS 191 PRO 192 0.0000

PRO 192 LYS 193 -0.0064

LYS 193 PHE 194 0.0001

PHE 194 LYS 195 -0.0003

LYS 195 ARG 196 -0.0048

ARG 196 ASP 197 0.0005

ASP 197 ILE 198 -0.0004

ILE 198 LYS 199 -0.0043

LYS 199 LYS 200 0.0004

LYS 200 VAL 201 -0.0001

VAL 201 ALA 202 0.0225

ALA 202 LYS 203 0.0003

LYS 203 ASP 204 0.0000

ASP 204 ILE 205 -0.0214

ILE 205 ILE 206 0.0002

ILE 206 PHE 207 -0.0001

PHE 207 ASN 208 0.0105

ASN 208 PRO 209 -0.0002

PRO 209 SER 210 0.0002

SER 210 PRO 211 0.0095

PRO 211 GLN 212 0.0000

GLN 212 PHE 213 0.0002

PHE 213 SER 214 -0.0742

SER 214 ASP 215 -0.0001

ASP 215 ILE 216 -0.0003

ILE 216 SER 217 -0.0004

SER 217 LEU 218 -0.0001

LEU 218 ARG 219 0.0000

ARG 219 ALA 220 -0.0605

ALA 220 LYS 221 -0.0001

LYS 221 ASP 222 -0.0002

ASP 222 GLU 223 0.0655

GLU 223 ALA 224 0.0001

ALA 224 GLY 225 0.0002

GLY 225 ASP 226 0.0367

ASP 226 LEU 228 -0.0353

LEU 228 THR 229 0.0001

THR 229 GLU 230 0.0000

GLU 230 HIS 231 -0.0109

HIS 231 TYR 232 -0.0004

TYR 232 LEU 233 0.0001

LEU 233 SER 234 -0.0086

SER 234 GLU 235 -0.0001

GLU 235 LYS 236 -0.0001

LYS 236 GLY 237 -0.0214

GLY 237 HIS 238 -0.0002

HIS 238 LEU 239 0.0002

LEU 239 SER 240 0.1763

SER 240 ALA 241 0.0004

ALA 241 PRO 242 -0.0004

PRO 242 LEU 243 0.1120

LEU 243 ASN 244 -0.0000

ASN 244 LYS 245 -0.0001

LYS 245 VAL 246 -0.0411

VAL 246 THR 247 0.0002

THR 247 ASN 248 -0.0001

ASN 248 ALA 249 -0.0420

ALA 249 GLU 250 0.0001

GLU 250 ILE 251 0.0002

ILE 251 ALA 252 -0.0049

ALA 252 GLU 253 -0.0001

GLU 253 GLU 254 0.0003

GLU 254 MET 255 -0.0137

MET 255 ALA 256 0.0003

ALA 256 TYR 257 0.0003

TYR 257 CYS 258 0.0640

CYS 258 TYR 259 0.0003

TYR 259 ALA 260 -0.0002

ALA 260 ARG 261 -0.0733

ARG 261 MET 262 -0.0003

MET 262 LYS 263 0.0001

LYS 263 SER 264 -0.2080

SER 264 ASP 265 0.0001

ASP 265 ILE 266 0.0001

ILE 266 LEU 267 0.0349

LEU 267 GLU 268 0.0004

GLU 268 CYS 269 0.0000

CYS 269 PHE 270 0.0444

PHE 270 LYS 271 -0.0001

LYS 271 ARG 272 0.0003

ARG 272 GLN 273 0.1404

GLN 273 VAL 274 0.0005

VAL 274 GLY 275 0.0001

GLY 275 LYS 276 0.0762

LYS 276 VAL 277 0.0001

VAL 277 LYS 278 0.0001

LYS 278 ASP 279 -0.3078

ASP 279 MET 1 -0.0834

MET 1 LYS 2 -0.0002

LYS 2 ASN 3 -0.0001

ASN 3 GLY 4 -0.0377

GLY 4 PHE 5 0.0001

PHE 5 TYR 6 0.0003

TYR 6 ALA 7 0.0294

ALA 7 THR 8 0.0002

THR 8 TYR 9 -0.0002

TYR 9 ARG 10 -0.0085

ARG 10 SER 11 0.0003

SER 11 LYS 12 -0.0003

LYS 12 ASN 13 0.0060

ASN 13 LYS 14 0.0001

LYS 14 GLY 15 0.0001

GLY 15 LYS 16 -0.0236

LYS 16 ASP 17 0.0000

ASP 17 LYS 18 -0.0003

LYS 18 ARG 19 -0.0488

ARG 19 SER 20 -0.0000

SER 20 ILE 21 0.0001

ILE 21 ASN 22 0.0030

ASN 22 LEU 23 0.0000

LEU 23 SER 24 -0.0000

SER 24 VAL 25 0.0116

VAL 25 PHE 26 -0.0001

PHE 26 LEU 27 0.0000

LEU 27 ASN 28 0.0269

ASN 28 SER 29 0.0000

SER 29 LEU 30 0.0001

LEU 30 LEU 31 0.0367

LEU 31 ALA 32 -0.0002

ALA 32 ASP 33 -0.0002

ASP 33 ASN 34 0.0173

ASN 34 HIS 35 -0.0003

HIS 35 HIS 36 0.0002

HIS 36 LEU 37 0.0302

LEU 37 GLN 38 -0.0001

GLN 38 VAL 39 -0.0000

VAL 39 GLY 40 0.0323

GLY 40 SER 41 0.0002

SER 41 ASN 42 -0.0002

ASN 42 TYR 43 -0.0019

TYR 43 LEU 44 -0.0001

LEU 44 TYR 45 0.0001

TYR 45 ILE 46 -0.0416

ILE 46 HIS 47 0.0000

HIS 47 LYS 48 0.0002

LYS 48 ILE 49 0.0444

ILE 49 ASP 50 -0.0005

ASP 50 GLY 51 0.0003

GLY 51 LYS 52 -0.0635

LYS 52 THR 53 0.0001

THR 53 PHE 54 -0.0003

PHE 54 LEU 55 -0.0580

LEU 55 PHE 56 0.0001

PHE 56 THR 57 0.0001

THR 57 LYS 58 -0.0476

LYS 58 THR 59 0.0000

THR 59 ASN 60 0.0001

ASN 60 ASP 61 0.0305

ASP 61 LYS 62 -0.0005

LYS 62 SER 63 -0.0001

SER 63 LEU 64 -0.0369

LEU 64 VAL 65 -0.0000

VAL 65 GLN 66 0.0002

GLN 66 LYS 67 0.0055

LYS 67 ILE 68 0.0000

ILE 68 ASN 69 0.0004

ASN 69 ARG 70 0.0070

ARG 70 SER 71 -0.0001

SER 71 LYS 72 -0.0003

LYS 72 ALA 73 -0.0013

ALA 73 SER 74 0.0001

SER 74 VAL 75 0.0001

VAL 75 GLU 76 0.0136

GLU 76 ASP 77 -0.0003

ASP 77 ILE 78 0.0002

ILE 78 LYS 79 -0.0478

LYS 79 ASN 80 -0.0002

ASN 80 SER 81 0.0002

SER 81 LEU 82 0.0797

LEU 82 ALA 83 -0.0003

ALA 83 ASP 84 0.0002

ASP 84 ASP 85 -0.0034

ASP 85 GLU 86 -0.0001

GLU 86 SER 87 0.0003

SER 87 LEU 88 -0.0135

LEU 88 GLY 89 0.0001

GLY 89 PHE 90 -0.0003

PHE 90 PRO 91 -0.0725

PRO 91 SER 92 0.0003

SER 92 PHE 93 -0.0002

PHE 93 LEU 94 -0.0228

LEU 94 PHE 95 0.0001

PHE 95 VAL 96 0.0002

VAL 96 GLU 97 -0.0393

GLU 97 GLY 98 -0.0001

GLY 98 ASP 99 -0.0002

ASP 99 THR 100 0.1208

THR 100 ILE 101 -0.0001

ILE 101 GLY 102 0.0002

GLY 102 PHE 103 0.0332

PHE 103 ALA 104 -0.0001

ALA 104 ARG 105 -0.0002

ARG 105 THR 106 0.0091

THR 106 VAL 107 -0.0003

VAL 107 PHE 108 -0.0004

PHE 108 GLY 109 -0.0055

GLY 109 PRO 110 -0.0003

PRO 110 THR 111 -0.0000

THR 111 THR 112 0.0741

THR 112 SER 113 -0.0002

SER 113 ASP 114 -0.0003

ASP 114 LEU 115 -0.0143

LEU 115 THR 116 -0.0000

THR 116 ASP 117 -0.0001

ASP 117 PHE 118 0.0223

PHE 118 LEU 119 -0.0002

LEU 119 ILE 120 0.0001

ILE 120 GLY 121 0.0554

GLY 121 LYS 122 -0.0002

LYS 122 GLY 123 0.0005

GLY 123 MET 124 -0.0506

MET 124 SER 125 0.0000

SER 125 LEU 126 0.0000

LEU 126 SER 127 0.0053

SER 127 SER 128 0.0001

SER 128 GLY 129 0.0000

GLY 129 GLU 130 -0.0131

GLU 130 ARG 131 -0.0003

ARG 131 VAL 132 -0.0002

VAL 132 GLN 133 -0.0364

GLN 133 ILE 134 -0.0001

ILE 134 GLU 135 0.0001

GLU 135 PRO 136 -0.2338

PRO 136 LEU 137 -0.0000

LEU 137 MET 138 0.0002

MET 138 ARG 139 -0.0693

ARG 139 GLY 140 0.0004

GLY 140 THR 141 0.0002

THR 141 THR 142 -0.1059

THR 142 LYS 143 0.0001

LYS 143 ASP 144 0.0003

ASP 144 ASP 145 -0.0006

ASP 145 VAL 146 -0.0003

VAL 146 MET 147 -0.0001

MET 147 HIS 148 -0.0245

HIS 148 MET 149 -0.0002

MET 149 HIS 150 0.0003

HIS 150 PHE 151 0.0206

PHE 151 ILE 152 -0.0004

ILE 152 GLY 153 0.0000

GLY 153 ARG 154 -0.0135

ARG 154 THR 155 -0.0002

THR 155 THR 156 0.0001

THR 156 VAL 157 0.0010

VAL 157 LYS 158 -0.0002

LYS 158 VAL 159 -0.0003

VAL 159 GLU 160 -0.0110

GLU 160 ALA 161 -0.0002

ALA 161 LYS 162 -0.0004

LYS 162 LEU 163 0.0199

LEU 163 PRO 164 -0.0002

PRO 164 VAL 165 -0.0000

VAL 165 PHE 166 0.0221

PHE 166 GLY 167 -0.0004

GLY 167 ASP 168 0.0001

ASP 168 ILE 169 -0.0056

ILE 169 LEU 170 -0.0001

LEU 170 LYS 171 0.0000

LYS 171 VAL 172 -0.0168

VAL 172 LEU 173 -0.0000

LEU 173 GLY 174 -0.0002

GLY 174 ALA 175 -0.0132

ALA 175 THR 176 -0.0001

THR 176 ASP 177 0.0001

ASP 177 ILE 178 -0.0084

ILE 178 GLU 179 0.0002

GLU 179 GLY 180 -0.0004

GLY 180 GLU 181 0.0034

GLU 181 LEU 182 -0.0000

LEU 182 PHE 183 0.0001

PHE 183 ASP 184 -0.0621

ASP 184 SER 185 0.0003

SER 185 LEU 186 -0.0003

LEU 186 ASP 187 0.0308

ASP 187 ILE 188 -0.0002

ILE 188 VAL 189 -0.0004

VAL 189 ILE 190 0.0361

ILE 190 LYS 191 -0.0001

LYS 191 PRO 192 0.0002

PRO 192 LYS 193 0.0056

LYS 193 PHE 194 0.0001

PHE 194 LYS 195 -0.0001

LYS 195 ARG 196 0.0079

ARG 196 ASP 197 0.0001

ASP 197 ILE 198 0.0001

ILE 198 LYS 199 0.0084

LYS 199 LYS 200 0.0002

LYS 200 VAL 201 0.0003

VAL 201 ALA 202 0.0162

ALA 202 LYS 203 0.0003

LYS 203 ASP 204 0.0002

ASP 204 ILE 205 0.0070

ILE 205 ILE 206 -0.0001

ILE 206 PHE 207 0.0004

PHE 207 ASN 208 -0.0083

ASN 208 PRO 209 0.0001

PRO 209 SER 210 -0.0001

SER 210 PRO 211 0.0197

PRO 211 GLN 212 0.0002

GLN 212 PHE 213 -0.0001

PHE 213 SER 214 0.0517

SER 214 ASP 215 0.0003

ASP 215 ILE 216 0.0001

ILE 216 SER 217 -0.0071

SER 217 LEU 218 -0.0001

LEU 218 ARG 219 0.0003

ARG 219 ALA 220 -0.0052

ALA 220 LYS 221 0.0000

LYS 221 ASP 222 0.0003

ASP 222 GLU 223 0.0156

GLU 223 ALA 224 0.0004

ALA 224 GLY 225 0.0000

GLY 225 ASP 226 0.0225

ASP 226 ILE 227 0.0001

ILE 227 LEU 228 -0.0002

LEU 228 THR 229 -0.0062

THR 229 GLU 230 -0.0000

GLU 230 HIS 231 0.0001

HIS 231 TYR 232 0.0034

TYR 232 LEU 233 0.0000

LEU 233 SER 234 0.0001

SER 234 GLU 235 0.0874

GLU 235 LYS 236 0.0000

LYS 236 GLY 237 0.0001

GLY 237 HIS 238 -0.0350

HIS 238 LEU 239 -0.0000

LEU 239 SER 240 0.0003

SER 240 ALA 241 0.0872

ALA 241 PRO 242 0.0002

PRO 242 LEU 243 0.0001

LEU 243 ASN 244 0.0450

ASN 244 LYS 245 -0.0001

LYS 245 VAL 246 0.0002

VAL 246 THR 247 0.0692

THR 247 ASN 248 -0.0001

ASN 248 ALA 249 -0.0000

ALA 249 GLU 250 0.0055

GLU 250 ILE 251 -0.0002

ILE 251 ALA 252 -0.0000

ALA 252 GLU 253 -0.0182

GLU 253 GLU 254 -0.0002

GLU 254 MET 255 0.0000

MET 255 ALA 256 0.0945

ALA 256 TYR 257 -0.0002

TYR 257 CYS 258 0.0000

CYS 258 TYR 259 0.0367

TYR 259 ALA 260 0.0002

ALA 260 ARG 261 0.0001

ARG 261 MET 262 -0.0823

MET 262 LYS 263 0.0001

LYS 263 SER 264 0.0001

SER 264 ASP 265 -0.0762

ASP 265 ILE 266 0.0002

ILE 266 LEU 267 0.0002

LEU 267 GLU 268 -0.2485

GLU 268 CYS 269 0.0000

CYS 269 PHE 270 0.0001

PHE 270 LYS 271 -0.1560

LYS 271 ARG 272 0.0002

ARG 272 GLN 273 0.0001

GLN 273 VAL 274 -0.1617

VAL 274 GLY 275 -0.0001

GLY 275 LYS 276 0.0001

LYS 276 VAL 277 -0.3003

VAL 277 LYS 278 0.0004

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 10 ---

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

* Chappie dimer compare ver 3 *