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

* Chappie dimer compare ver 3 *

CA strain for 221218005903105706

--- normal mode 8 ---

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 -0.0001

LYS 2 ASN 3 0.0001

ASN 3 GLY 4 0.0678

GLY 4 PHE 5 0.0001

PHE 5 TYR 6 0.0002

TYR 6 ALA 7 0.0087

ALA 7 THR 8 -0.0001

THR 8 TYR 9 0.0003

TYR 9 ARG 10 0.0132

ARG 10 SER 11 -0.0003

SER 11 LYS 12 0.0003

LYS 12 ASN 13 0.0144

ASN 13 LYS 14 -0.0002

LYS 14 GLY 15 -0.0001

GLY 15 LYS 16 0.0241

LYS 16 ASP 17 -0.0002

ASP 17 LYS 18 0.0004

LYS 18 ARG 19 -0.0513

ARG 19 SER 20 0.0002

SER 20 ILE 21 -0.0003

ILE 21 ASN 22 -0.0181

ASN 22 LEU 23 -0.0000

LEU 23 SER 24 -0.0002

SER 24 VAL 25 0.0552

VAL 25 PHE 26 -0.0003

PHE 26 LEU 27 0.0001

LEU 27 ASN 28 0.0028

ASN 28 SER 29 -0.0002

SER 29 LEU 30 -0.0001

LEU 30 ASN 34 -0.0218

ASN 34 HIS 35 0.0002

HIS 35 HIS 36 0.0000

HIS 36 LEU 37 0.0045

LEU 37 GLN 38 0.0001

GLN 38 VAL 39 -0.0004

VAL 39 GLY 40 0.0067

GLY 40 SER 41 0.0001

SER 41 ASN 42 -0.0001

ASN 42 TYR 43 0.0091

TYR 43 LEU 44 0.0002

LEU 44 TYR 45 -0.0004

TYR 45 ILE 46 0.0393

ILE 46 HIS 47 0.0005

HIS 47 LYS 48 -0.0003

LYS 48 ILE 49 0.0116

ILE 49 ASP 50 -0.0002

ASP 50 GLY 51 0.0004

GLY 51 LYS 52 -0.0342

LYS 52 THR 53 -0.0000

THR 53 PHE 54 0.0002

PHE 54 LEU 55 0.0006

LEU 55 PHE 56 0.0002

PHE 56 THR 57 -0.0004

THR 57 LYS 58 0.0115

LYS 58 THR 59 0.0002

THR 59 ASN 60 -0.0001

ASN 60 ASP 61 -0.0043

ASP 61 LYS 62 0.0002

LYS 62 SER 63 -0.0004

SER 63 LEU 64 0.0013

LEU 64 VAL 65 0.0000

VAL 65 GLN 66 0.0001

GLN 66 LYS 67 0.0038

LYS 67 ILE 68 -0.0000

ILE 68 ASN 69 0.0000

ASN 69 ARG 70 -0.0175

ARG 70 SER 71 -0.0001

SER 71 LYS 72 0.0002

LYS 72 ALA 73 0.0276

ALA 73 SER 74 -0.0002

SER 74 VAL 75 0.0001

VAL 75 GLU 76 -0.0087

GLU 76 ASP 77 0.0001

ASP 77 ILE 78 0.0002

ILE 78 LYS 79 0.0159

LYS 79 ASN 80 -0.0001

ASN 80 SER 81 -0.0001

SER 81 LEU 82 -0.0193

LEU 82 ALA 83 0.0000

ALA 83 ASP 84 0.0004

ASP 84 ASP 85 -0.0079

ASP 85 GLU 86 0.0003

GLU 86 SER 87 0.0000

SER 87 LEU 88 -0.0060

LEU 88 GLY 89 0.0001

GLY 89 PHE 90 0.0000

PHE 90 PRO 91 0.0075

PRO 91 SER 92 0.0003

SER 92 PHE 93 -0.0002

PHE 93 LEU 94 -0.0048

LEU 94 PHE 95 -0.0001

PHE 95 VAL 96 -0.0003

VAL 96 GLU 97 -0.0173

GLU 97 GLY 98 -0.0000

GLY 98 ASP 99 -0.0001

ASP 99 THR 100 0.0350

THR 100 ILE 101 0.0003

ILE 101 GLY 102 -0.0003

GLY 102 PHE 103 0.0277

PHE 103 ALA 104 -0.0002

ALA 104 ARG 105 0.0002

ARG 105 THR 106 0.0218

THR 106 VAL 107 0.0002

VAL 107 PHE 108 -0.0001

PHE 108 GLY 109 0.0125

GLY 109 PRO 110 0.0002

PRO 110 THR 111 0.0000

THR 111 THR 112 0.0308

THR 112 SER 113 0.0001

SER 113 ASP 114 0.0000

ASP 114 LEU 115 0.0133

LEU 115 THR 116 0.0001

THR 116 ASP 117 0.0001

ASP 117 PHE 118 -0.0039

PHE 118 LEU 119 -0.0002

LEU 119 ILE 120 -0.0000

ILE 120 GLY 121 -0.0027

GLY 121 LYS 122 -0.0001

LYS 122 GLY 123 0.0001

GLY 123 MET 124 -0.0535

MET 124 SER 125 0.0002

SER 125 LEU 126 -0.0001

LEU 126 SER 127 0.0221

SER 127 SER 128 -0.0001

SER 128 GLY 129 -0.0003

GLY 129 GLU 130 -0.0057

GLU 130 ARG 131 -0.0005

ARG 131 VAL 132 0.0001

VAL 132 GLN 133 -0.0837

GLN 133 ILE 134 -0.0001

ILE 134 GLU 135 0.0000

GLU 135 PRO 136 -0.1351

PRO 136 LEU 137 -0.0002

LEU 137 MET 138 0.0000

MET 138 ARG 139 0.0663

ARG 139 GLY 140 0.0002

GLY 140 THR 141 -0.0000

THR 141 THR 142 -0.0401

THR 142 LYS 143 0.0000

LYS 143 ASP 144 0.0003

ASP 144 ASP 145 0.0133

ASP 145 VAL 146 -0.0003

VAL 146 MET 147 0.0004

MET 147 HIS 148 -0.0027

HIS 148 MET 149 0.0001

MET 149 HIS 150 -0.0001

HIS 150 PHE 151 0.0358

PHE 151 ILE 152 0.0005

ILE 152 GLY 153 0.0001

GLY 153 ARG 154 0.1082

ARG 154 THR 155 -0.0001

THR 155 THR 156 0.0003

THR 156 VAL 157 -0.0434

VAL 157 LYS 158 -0.0004

LYS 158 VAL 159 0.0000

VAL 159 GLU 160 -0.0174

GLU 160 ALA 161 -0.0001

ALA 161 LYS 162 0.0001

LYS 162 LEU 163 -0.0290

LEU 163 PRO 164 -0.0001

PRO 164 VAL 165 -0.0001

VAL 165 PHE 166 -0.0901

PHE 166 GLY 167 0.0001

GLY 167 ASP 168 0.0001

ASP 168 ILE 169 0.0290

ILE 169 LEU 170 0.0001

LEU 170 LYS 171 0.0002

LYS 171 VAL 172 -0.0140

VAL 172 LEU 173 -0.0000

LEU 173 GLY 174 -0.0000

GLY 174 ALA 175 0.0048

ALA 175 THR 176 -0.0002

THR 176 ASP 177 0.0002

ASP 177 ILE 178 0.0205

ILE 178 GLU 179 -0.0003

GLU 179 GLY 180 0.0001

GLY 180 GLU 181 -0.0084

GLU 181 LEU 182 0.0002

LEU 182 PHE 183 0.0002

PHE 183 ASP 184 0.1458

ASP 184 SER 185 0.0000

SER 185 LEU 186 -0.0001

LEU 186 ASP 187 0.0213

ASP 187 ILE 188 -0.0000

ILE 188 VAL 189 -0.0000

VAL 189 ILE 190 0.0555

ILE 190 LYS 191 0.0000

LYS 191 PRO 192 -0.0002

PRO 192 LYS 193 0.0187

LYS 193 PHE 194 -0.0003

PHE 194 LYS 195 0.0001

LYS 195 ARG 196 -0.0120

ARG 196 ASP 197 0.0003

ASP 197 ILE 198 0.0001

ILE 198 LYS 199 0.0418

LYS 199 LYS 200 -0.0003

LYS 200 VAL 201 -0.0001

VAL 201 ALA 202 -0.0077

ALA 202 LYS 203 0.0001

LYS 203 ASP 204 -0.0003

ASP 204 ILE 205 0.0177

ILE 205 ILE 206 0.0001

ILE 206 PHE 207 -0.0001

PHE 207 ASN 208 -0.0411

ASN 208 PRO 209 -0.0004

PRO 209 SER 210 -0.0001

SER 210 PRO 211 0.0063

PRO 211 GLN 212 0.0003

GLN 212 PHE 213 0.0001

PHE 213 SER 214 0.1175

SER 214 ASP 215 0.0001

ASP 215 ILE 216 0.0000

ILE 216 SER 217 0.0004

SER 217 LEU 218 0.0004

LEU 218 ARG 219 -0.0003

ARG 219 ALA 220 0.0632

ALA 220 LYS 221 -0.0002

LYS 221 ASP 222 0.0002

ASP 222 GLU 223 -0.0118

GLU 223 ALA 224 -0.0003

ALA 224 GLY 225 0.0002

GLY 225 ASP 226 0.0008

ASP 226 LEU 228 0.0406

LEU 228 THR 229 0.0001

THR 229 GLU 230 0.0003

GLU 230 HIS 231 0.0226

HIS 231 TYR 232 0.0001

TYR 232 LEU 233 0.0004

LEU 233 SER 234 0.0109

SER 234 GLU 235 0.0002

GLU 235 LYS 236 -0.0001

LYS 236 GLY 237 -0.0389

GLY 237 HIS 238 -0.0002

HIS 238 LEU 239 -0.0001

LEU 239 SER 240 0.0048

SER 240 ALA 241 0.0001

ALA 241 PRO 242 0.0003

PRO 242 LEU 243 -0.0351

LEU 243 ASN 244 -0.0001

ASN 244 LYS 245 -0.0001

LYS 245 VAL 246 -0.0151

VAL 246 THR 247 -0.0000

THR 247 ASN 248 0.0000

ASN 248 ALA 249 0.0014

ALA 249 GLU 250 -0.0002

GLU 250 ILE 251 0.0002

ILE 251 ALA 252 -0.0363

ALA 252 GLU 253 -0.0005

GLU 253 GLU 254 -0.0003

GLU 254 MET 255 -0.0134

MET 255 ALA 256 -0.0002

ALA 256 TYR 257 -0.0003

TYR 257 CYS 258 -0.0308

CYS 258 TYR 259 0.0002

TYR 259 ALA 260 0.0003

ALA 260 ARG 261 0.1047

ARG 261 MET 262 -0.0001

MET 262 LYS 263 0.0000

LYS 263 SER 264 0.0247

SER 264 ASP 265 -0.0003

ASP 265 ILE 266 0.0001

ILE 266 LEU 267 -0.0397

LEU 267 GLU 268 0.0001

GLU 268 CYS 269 -0.0002

CYS 269 PHE 270 0.0563

PHE 270 LYS 271 -0.0002

LYS 271 ARG 272 -0.0003

ARG 272 GLN 273 -0.0813

GLN 273 VAL 274 -0.0000

VAL 274 GLY 275 -0.0000

GLY 275 LYS 276 0.1929

LYS 276 VAL 277 -0.0001

VAL 277 LYS 278 -0.0000

LYS 278 ASP 279 -0.1820

ASP 279 MET 1 0.0716

MET 1 LYS 2 -0.0002

LYS 2 ASN 3 0.0005

ASN 3 GLY 4 0.0618

GLY 4 PHE 5 0.0002

PHE 5 TYR 6 0.0000

TYR 6 ALA 7 0.0098

ALA 7 THR 8 0.0001

THR 8 TYR 9 0.0003

TYR 9 ARG 10 0.0136

ARG 10 SER 11 0.0000

SER 11 LYS 12 -0.0002

LYS 12 ASN 13 0.0115

ASN 13 LYS 14 0.0002

LYS 14 GLY 15 -0.0002

GLY 15 LYS 16 -0.0104

LYS 16 ASP 17 -0.0003

ASP 17 LYS 18 0.0004

LYS 18 ARG 19 -0.0410

ARG 19 SER 20 -0.0001

SER 20 ILE 21 0.0005

ILE 21 ASN 22 -0.0143

ASN 22 LEU 23 -0.0002

LEU 23 SER 24 0.0003

SER 24 VAL 25 0.0369

VAL 25 PHE 26 -0.0001

PHE 26 LEU 27 0.0003

LEU 27 ASN 28 0.0015

ASN 28 SER 29 0.0001

SER 29 LEU 30 -0.0001

LEU 30 LEU 31 -0.0099

LEU 31 ALA 32 -0.0002

ALA 32 ASP 33 -0.0001

ASP 33 ASN 34 -0.0083

ASN 34 HIS 35 0.0000

HIS 35 HIS 36 -0.0001

HIS 36 LEU 37 0.0067

LEU 37 GLN 38 0.0005

GLN 38 VAL 39 -0.0003

VAL 39 GLY 40 0.0133

GLY 40 SER 41 -0.0000

SER 41 ASN 42 -0.0002

ASN 42 TYR 43 0.0077

TYR 43 LEU 44 -0.0000

LEU 44 TYR 45 -0.0004

TYR 45 ILE 46 0.0363

ILE 46 HIS 47 0.0001

HIS 47 LYS 48 0.0002

LYS 48 ILE 49 0.0438

ILE 49 ASP 50 -0.0001

ASP 50 GLY 51 0.0003

GLY 51 LYS 52 -0.0139

LYS 52 THR 53 0.0001

THR 53 PHE 54 0.0001

PHE 54 LEU 55 -0.0060

LEU 55 PHE 56 -0.0001

PHE 56 THR 57 0.0003

THR 57 LYS 58 0.0082

LYS 58 THR 59 0.0003

THR 59 ASN 60 -0.0002

ASN 60 ASP 61 0.0032

ASP 61 LYS 62 -0.0000

LYS 62 SER 63 0.0000

SER 63 LEU 64 -0.0024

LEU 64 VAL 65 -0.0001

VAL 65 GLN 66 -0.0001

GLN 66 LYS 67 0.0028

LYS 67 ILE 68 0.0002

ILE 68 ASN 69 -0.0000

ASN 69 ARG 70 -0.0108

ARG 70 SER 71 0.0000

SER 71 LYS 72 -0.0000

LYS 72 ALA 73 0.0194

ALA 73 SER 74 -0.0001

SER 74 VAL 75 -0.0003

VAL 75 GLU 76 -0.0015

GLU 76 ASP 77 0.0003

ASP 77 ILE 78 0.0002

ILE 78 LYS 79 0.0373

LYS 79 ASN 80 -0.0000

ASN 80 SER 81 -0.0002

SER 81 LEU 82 -0.0003

LEU 82 ALA 83 0.0001

ALA 83 ASP 84 -0.0001

ASP 84 ASP 85 0.0006

ASP 85 GLU 86 -0.0002

GLU 86 SER 87 -0.0001

SER 87 LEU 88 -0.0018

LEU 88 GLY 89 -0.0001

GLY 89 PHE 90 0.0001

PHE 90 PRO 91 0.0020

PRO 91 SER 92 -0.0001

SER 92 PHE 93 0.0000

PHE 93 LEU 94 -0.0079

LEU 94 PHE 95 -0.0006

PHE 95 VAL 96 -0.0001

VAL 96 GLU 97 -0.0151

GLU 97 GLY 98 0.0001

GLY 98 ASP 99 -0.0001

ASP 99 THR 100 0.0749

THR 100 ILE 101 -0.0002

ILE 101 GLY 102 0.0002

GLY 102 PHE 103 0.0123

PHE 103 ALA 104 -0.0003

ALA 104 ARG 105 -0.0001

ARG 105 THR 106 0.0237

THR 106 VAL 107 -0.0000

VAL 107 PHE 108 -0.0002

PHE 108 GLY 109 0.0119

GLY 109 PRO 110 0.0004

PRO 110 THR 111 -0.0004

THR 111 THR 112 0.0438

THR 112 SER 113 -0.0002

SER 113 ASP 114 -0.0000

ASP 114 LEU 115 0.0122

LEU 115 THR 116 -0.0000

THR 116 ASP 117 0.0000

ASP 117 PHE 118 0.0001

PHE 118 LEU 119 -0.0003

LEU 119 ILE 120 0.0002

ILE 120 GLY 121 0.0056

GLY 121 LYS 122 0.0002

LYS 122 GLY 123 0.0000

GLY 123 MET 124 -0.0450

MET 124 SER 125 -0.0001

SER 125 LEU 126 0.0002

LEU 126 SER 127 0.0122

SER 127 SER 128 0.0001

SER 128 GLY 129 -0.0002

GLY 129 GLU 130 -0.0045

GLU 130 ARG 131 -0.0001

ARG 131 VAL 132 -0.0001

VAL 132 GLN 133 -0.0816

GLN 133 ILE 134 0.0000

ILE 134 GLU 135 0.0000

GLU 135 PRO 136 -0.2233

PRO 136 LEU 137 0.0000

LEU 137 MET 138 0.0003

MET 138 ARG 139 0.0673

ARG 139 GLY 140 0.0002

GLY 140 THR 141 -0.0002

THR 141 THR 142 -0.0249

THR 142 LYS 143 0.0004

LYS 143 ASP 144 0.0001

ASP 144 ASP 145 -0.0102

ASP 145 VAL 146 0.0002

VAL 146 MET 147 -0.0002

MET 147 HIS 148 -0.0138

HIS 148 MET 149 0.0004

MET 149 HIS 150 0.0001

HIS 150 PHE 151 0.0373

PHE 151 ILE 152 0.0002

ILE 152 GLY 153 0.0004

GLY 153 ARG 154 0.1096

ARG 154 THR 155 0.0001

THR 155 THR 156 -0.0001

THR 156 VAL 157 -0.0179

VAL 157 LYS 158 -0.0003

LYS 158 VAL 159 -0.0002

VAL 159 GLU 160 -0.0081

GLU 160 ALA 161 0.0002

ALA 161 LYS 162 0.0005

LYS 162 LEU 163 -0.0533

LEU 163 PRO 164 -0.0001

PRO 164 VAL 165 -0.0001

VAL 165 PHE 166 -0.0895

PHE 166 GLY 167 -0.0001

GLY 167 ASP 168 -0.0003

ASP 168 ILE 169 0.0337

ILE 169 LEU 170 0.0000

LEU 170 LYS 171 -0.0001

LYS 171 VAL 172 -0.0026

VAL 172 LEU 173 -0.0001

LEU 173 GLY 174 -0.0001

GLY 174 ALA 175 0.0093

ALA 175 THR 176 -0.0003

THR 176 ASP 177 -0.0001

ASP 177 ILE 178 0.0213

ILE 178 GLU 179 0.0001

GLU 179 GLY 180 -0.0004

GLY 180 GLU 181 -0.0127

GLU 181 LEU 182 0.0002

LEU 182 PHE 183 -0.0000

PHE 183 ASP 184 0.0896

ASP 184 SER 185 0.0001

SER 185 LEU 186 0.0000

LEU 186 ASP 187 0.0502

ASP 187 ILE 188 -0.0005

ILE 188 VAL 189 0.0000

VAL 189 ILE 190 0.0310

ILE 190 LYS 191 -0.0001

LYS 191 PRO 192 -0.0001

PRO 192 LYS 193 -0.0155

LYS 193 PHE 194 -0.0003

PHE 194 LYS 195 -0.0001

LYS 195 ARG 196 -0.0060

ARG 196 ASP 197 -0.0001

ASP 197 ILE 198 0.0000

ILE 198 LYS 199 0.0559

LYS 199 LYS 200 0.0001

LYS 200 VAL 201 0.0000

VAL 201 ALA 202 -0.0112

ALA 202 LYS 203 -0.0003

LYS 203 ASP 204 -0.0001

ASP 204 ILE 205 0.0158

ILE 205 ILE 206 0.0002

ILE 206 PHE 207 -0.0001

PHE 207 ASN 208 -0.0605

ASN 208 PRO 209 0.0001

PRO 209 SER 210 -0.0000

SER 210 PRO 211 -0.0019

PRO 211 GLN 212 -0.0002

GLN 212 PHE 213 -0.0001

PHE 213 SER 214 0.1458

SER 214 ASP 215 0.0005

ASP 215 ILE 216 -0.0000

ILE 216 SER 217 -0.0100

SER 217 LEU 218 0.0001

LEU 218 ARG 219 0.0002

ARG 219 ALA 220 0.0654

ALA 220 LYS 221 -0.0004

LYS 221 ASP 222 -0.0001

ASP 222 GLU 223 -0.0064

GLU 223 ALA 224 0.0003

ALA 224 GLY 225 0.0002

GLY 225 ASP 226 -0.0128

ASP 226 ILE 227 0.0004

ILE 227 LEU 228 -0.0001

LEU 228 THR 229 -0.0661

THR 229 GLU 230 0.0002

GLU 230 HIS 231 0.0002

HIS 231 TYR 232 -0.0102

TYR 232 LEU 233 0.0001

LEU 233 SER 234 0.0003

SER 234 GLU 235 -0.0234

GLU 235 LYS 236 0.0003

LYS 236 GLY 237 0.0001

GLY 237 HIS 238 0.0604

HIS 238 LEU 239 -0.0002

LEU 239 SER 240 0.0000

SER 240 ALA 241 0.0541

ALA 241 PRO 242 0.0002

PRO 242 LEU 243 -0.0002

LEU 243 ASN 244 0.0199

ASN 244 LYS 245 -0.0001

LYS 245 VAL 246 -0.0002

VAL 246 THR 247 0.0010

THR 247 ASN 248 -0.0003

ASN 248 ALA 249 -0.0003

ALA 249 GLU 250 0.0250

GLU 250 ILE 251 -0.0001

ILE 251 ALA 252 0.0002

ALA 252 GLU 253 0.0365

GLU 253 GLU 254 0.0001

GLU 254 MET 255 0.0001

MET 255 ALA 256 -0.0365

ALA 256 TYR 257 0.0001

TYR 257 CYS 258 0.0000

CYS 258 TYR 259 -0.0950

TYR 259 ALA 260 -0.0002

ALA 260 ARG 261 -0.0002

ARG 261 MET 262 -0.1006

MET 262 LYS 263 -0.0001

LYS 263 SER 264 0.0003

SER 264 ASP 265 0.0282

ASP 265 ILE 266 -0.0002

ILE 266 LEU 267 0.0001

LEU 267 GLU 268 -0.0456

GLU 268 CYS 269 -0.0001

CYS 269 PHE 270 0.0002

PHE 270 LYS 271 -0.0806

LYS 271 ARG 272 0.0003

ARG 272 GLN 273 -0.0001

GLN 273 VAL 274 -0.1537

VAL 274 GLY 275 -0.0003

GLY 275 LYS 276 -0.0002

LYS 276 VAL 277 -0.2211

VAL 277 LYS 278 -0.0001

LYS 278 ASP 279 -0.0001

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 8 ---

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

* Chappie dimer compare ver 3 *