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

* Chappie dimer compare ver 3 *

CA strain for 221218005903105706

--- 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
MET 1 LYS 2 -0.0000

LYS 2 ASN 3 -0.0003

ASN 3 GLY 4 -0.0901

GLY 4 PHE 5 0.0005

PHE 5 TYR 6 -0.0001

TYR 6 ALA 7 -0.0445

ALA 7 THR 8 -0.0002

THR 8 TYR 9 -0.0001

TYR 9 ARG 10 0.0379

ARG 10 SER 11 0.0001

SER 11 LYS 12 -0.0001

LYS 12 ASN 13 -0.0183

ASN 13 LYS 14 0.0003

LYS 14 GLY 15 0.0002

GLY 15 LYS 16 -0.1136

LYS 16 ASP 17 0.0002

ASP 17 LYS 18 -0.0002

LYS 18 ARG 19 0.0175

ARG 19 SER 20 -0.0003

SER 20 ILE 21 0.0001

ILE 21 ASN 22 0.0243

ASN 22 LEU 23 -0.0001

LEU 23 SER 24 -0.0002

SER 24 VAL 25 -0.0149

VAL 25 PHE 26 0.0001

PHE 26 LEU 27 -0.0001

LEU 27 ASN 28 0.0040

ASN 28 SER 29 -0.0004

SER 29 LEU 30 -0.0003

LEU 30 ASN 34 -0.0296

ASN 34 HIS 35 0.0005

HIS 35 HIS 36 0.0002

HIS 36 LEU 37 -0.0209

LEU 37 GLN 38 -0.0002

GLN 38 VAL 39 -0.0001

VAL 39 GLY 40 -0.0291

GLY 40 SER 41 0.0001

SER 41 ASN 42 0.0001

ASN 42 TYR 43 0.0001

TYR 43 LEU 44 -0.0000

LEU 44 TYR 45 0.0000

TYR 45 ILE 46 -0.0045

ILE 46 HIS 47 0.0001

HIS 47 LYS 48 0.0001

LYS 48 ILE 49 0.0050

ILE 49 ASP 50 0.0001

ASP 50 GLY 51 -0.0002

GLY 51 LYS 52 0.0078

LYS 52 THR 53 -0.0003

THR 53 PHE 54 0.0002

PHE 54 LEU 55 -0.0004

LEU 55 PHE 56 -0.0001

PHE 56 THR 57 -0.0002

THR 57 LYS 58 0.0162

LYS 58 THR 59 -0.0001

THR 59 ASN 60 -0.0003

ASN 60 ASP 61 0.0013

ASP 61 LYS 62 -0.0000

LYS 62 SER 63 -0.0004

SER 63 LEU 64 0.0096

LEU 64 VAL 65 -0.0001

VAL 65 GLN 66 0.0002

GLN 66 LYS 67 0.0036

LYS 67 ILE 68 0.0002

ILE 68 ASN 69 0.0001

ASN 69 ARG 70 -0.0310

ARG 70 SER 71 0.0002

SER 71 LYS 72 0.0002

LYS 72 ALA 73 0.0176

ALA 73 SER 74 -0.0001

SER 74 VAL 75 -0.0000

VAL 75 GLU 76 -0.0023

GLU 76 ASP 77 0.0002

ASP 77 ILE 78 -0.0002

ILE 78 LYS 79 0.0076

LYS 79 ASN 80 -0.0000

ASN 80 SER 81 -0.0003

SER 81 LEU 82 0.0030

LEU 82 ALA 83 -0.0001

ALA 83 ASP 84 -0.0001

ASP 84 ASP 85 0.0605

ASP 85 GLU 86 -0.0001

GLU 86 SER 87 -0.0004

SER 87 LEU 88 0.0006

LEU 88 GLY 89 -0.0003

GLY 89 PHE 90 0.0002

PHE 90 PRO 91 0.0259

PRO 91 SER 92 -0.0002

SER 92 PHE 93 0.0002

PHE 93 LEU 94 -0.0424

LEU 94 PHE 95 -0.0000

PHE 95 VAL 96 -0.0001

VAL 96 GLU 97 -0.0400

GLU 97 GLY 98 0.0003

GLY 98 ASP 99 -0.0001

ASP 99 THR 100 -0.0332

THR 100 ILE 101 0.0005

ILE 101 GLY 102 0.0000

GLY 102 PHE 103 -0.0277

PHE 103 ALA 104 0.0001

ALA 104 ARG 105 0.0000

ARG 105 THR 106 -0.0570

THR 106 VAL 107 0.0001

VAL 107 PHE 108 -0.0001

PHE 108 GLY 109 -0.0282

GLY 109 PRO 110 -0.0001

PRO 110 THR 111 0.0002

THR 111 THR 112 -0.0891

THR 112 SER 113 -0.0001

SER 113 ASP 114 -0.0000

ASP 114 LEU 115 -0.0131

LEU 115 THR 116 -0.0002

THR 116 ASP 117 0.0001

ASP 117 PHE 118 0.0101

PHE 118 LEU 119 0.0003

LEU 119 ILE 120 -0.0002

ILE 120 GLY 121 -0.0498

GLY 121 LYS 122 -0.0000

LYS 122 GLY 123 0.0000

GLY 123 MET 124 -0.1061

MET 124 SER 125 -0.0001

SER 125 LEU 126 -0.0001

LEU 126 SER 127 -0.0194

SER 127 SER 128 0.0000

SER 128 GLY 129 -0.0002

GLY 129 GLU 130 0.0151

GLU 130 ARG 131 -0.0006

ARG 131 VAL 132 0.0003

VAL 132 GLN 133 0.1047

GLN 133 ILE 134 0.0002

ILE 134 GLU 135 -0.0002

GLU 135 PRO 136 0.1533

PRO 136 LEU 137 -0.0005

LEU 137 MET 138 0.0001

MET 138 ARG 139 -0.0647

ARG 139 GLY 140 -0.0001

GLY 140 THR 141 -0.0003

THR 141 THR 142 0.1088

THR 142 LYS 143 -0.0004

LYS 143 ASP 144 -0.0003

ASP 144 ASP 145 -0.0219

ASP 145 VAL 146 -0.0003

VAL 146 MET 147 -0.0000

MET 147 HIS 148 0.0012

HIS 148 MET 149 -0.0003

MET 149 HIS 150 -0.0002

HIS 150 PHE 151 -0.0187

PHE 151 ILE 152 -0.0004

ILE 152 GLY 153 -0.0000

GLY 153 ARG 154 -0.0340

ARG 154 THR 155 -0.0003

THR 155 THR 156 -0.0003

THR 156 VAL 157 -0.0272

VAL 157 LYS 158 0.0000

LYS 158 VAL 159 0.0000

VAL 159 GLU 160 -0.0172

GLU 160 ALA 161 0.0001

ALA 161 LYS 162 0.0002

LYS 162 LEU 163 -0.0280

LEU 163 PRO 164 0.0001

PRO 164 VAL 165 0.0001

VAL 165 PHE 166 -0.0107

PHE 166 GLY 167 -0.0001

GLY 167 ASP 168 -0.0000

ASP 168 ILE 169 -0.0130

ILE 169 LEU 170 0.0001

LEU 170 LYS 171 -0.0000

LYS 171 VAL 172 -0.0515

VAL 172 LEU 173 0.0000

LEU 173 GLY 174 -0.0000

GLY 174 ALA 175 -0.0222

ALA 175 THR 176 0.0000

THR 176 ASP 177 -0.0000

ASP 177 ILE 178 0.0154

ILE 178 GLU 179 0.0001

GLU 179 GLY 180 -0.0001

GLY 180 GLU 181 -0.0046

GLU 181 LEU 182 0.0004

LEU 182 PHE 183 -0.0000

PHE 183 ASP 184 0.0630

ASP 184 SER 185 -0.0003

SER 185 LEU 186 -0.0000

LEU 186 ASP 187 -0.0108

ASP 187 ILE 188 -0.0001

ILE 188 VAL 189 0.0001

VAL 189 ILE 190 0.0014

ILE 190 LYS 191 0.0004

LYS 191 PRO 192 -0.0004

PRO 192 LYS 193 0.0199

LYS 193 PHE 194 -0.0002

PHE 194 LYS 195 -0.0001

LYS 195 ARG 196 0.0061

ARG 196 ASP 197 -0.0001

ASP 197 ILE 198 0.0000

ILE 198 LYS 199 0.0010

LYS 199 LYS 200 0.0002

LYS 200 VAL 201 -0.0001

VAL 201 ALA 202 0.0190

ALA 202 LYS 203 -0.0001

LYS 203 ASP 204 0.0004

ASP 204 ILE 205 -0.0070

ILE 205 ILE 206 -0.0002

ILE 206 PHE 207 0.0003

PHE 207 ASN 208 0.0110

ASN 208 PRO 209 0.0001

PRO 209 SER 210 0.0002

SER 210 PRO 211 -0.0128

PRO 211 GLN 212 -0.0001

GLN 212 PHE 213 0.0001

PHE 213 SER 214 -0.0112

SER 214 ASP 215 -0.0000

ASP 215 ILE 216 0.0000

ILE 216 SER 217 -0.0058

SER 217 LEU 218 0.0001

LEU 218 ARG 219 -0.0002

ARG 219 ALA 220 -0.0310

ALA 220 LYS 221 0.0002

LYS 221 ASP 222 -0.0001

ASP 222 GLU 223 0.0121

GLU 223 ALA 224 -0.0001

ALA 224 GLY 225 -0.0003

GLY 225 ASP 226 0.0099

ASP 226 LEU 228 -0.0050

LEU 228 THR 229 0.0003

THR 229 GLU 230 0.0004

GLU 230 HIS 231 -0.0414

HIS 231 TYR 232 -0.0002

TYR 232 LEU 233 0.0002

LEU 233 SER 234 -0.0580

SER 234 GLU 235 0.0004

GLU 235 LYS 236 -0.0002

LYS 236 GLY 237 0.2429

GLY 237 HIS 238 0.0003

HIS 238 LEU 239 -0.0000

LEU 239 SER 240 -0.0436

SER 240 ALA 241 0.0002

ALA 241 PRO 242 -0.0001

PRO 242 LEU 243 0.0561

LEU 243 ASN 244 -0.0002

ASN 244 LYS 245 0.0002

LYS 245 VAL 246 0.0251

VAL 246 THR 247 -0.0000

THR 247 ASN 248 0.0002

ASN 248 ALA 249 -0.0121

ALA 249 GLU 250 -0.0003

GLU 250 ILE 251 -0.0001

ILE 251 ALA 252 -0.0105

ALA 252 GLU 253 0.0002

GLU 253 GLU 254 -0.0002

GLU 254 MET 255 -0.0096

MET 255 ALA 256 0.0000

ALA 256 TYR 257 0.0005

TYR 257 CYS 258 -0.0099

CYS 258 TYR 259 0.0001

TYR 259 ALA 260 -0.0003

ALA 260 ARG 261 -0.0159

ARG 261 MET 262 -0.0004

MET 262 LYS 263 0.0002

LYS 263 SER 264 -0.0323

SER 264 ASP 265 -0.0002

ASP 265 ILE 266 -0.0001

ILE 266 LEU 267 -0.0376

LEU 267 GLU 268 -0.0002

GLU 268 CYS 269 0.0002

CYS 269 PHE 270 -0.0323

PHE 270 LYS 271 0.0001

LYS 271 ARG 272 -0.0001

ARG 272 GLN 273 -0.0419

GLN 273 VAL 274 -0.0004

VAL 274 GLY 275 0.0003

GLY 275 LYS 276 -0.2286

LYS 276 VAL 277 -0.0004

VAL 277 LYS 278 -0.0001

LYS 278 ASP 279 0.0010

ASP 279 MET 1 -0.1901

MET 1 LYS 2 -0.0004

LYS 2 ASN 3 0.0002

ASN 3 GLY 4 -0.0647

GLY 4 PHE 5 -0.0001

PHE 5 TYR 6 0.0002

TYR 6 ALA 7 -0.0100

ALA 7 THR 8 -0.0002

THR 8 TYR 9 -0.0000

TYR 9 ARG 10 0.0269

ARG 10 SER 11 0.0001

SER 11 LYS 12 0.0004

LYS 12 ASN 13 0.0110

ASN 13 LYS 14 0.0002

LYS 14 GLY 15 0.0002

GLY 15 LYS 16 0.0011

LYS 16 ASP 17 0.0002

ASP 17 LYS 18 0.0001

LYS 18 ARG 19 -0.0311

ARG 19 SER 20 0.0002

SER 20 ILE 21 0.0001

ILE 21 ASN 22 0.0184

ASN 22 LEU 23 -0.0000

LEU 23 SER 24 -0.0002

SER 24 VAL 25 -0.0017

VAL 25 PHE 26 0.0000

PHE 26 LEU 27 -0.0002

LEU 27 ASN 28 0.0142

ASN 28 SER 29 0.0002

SER 29 LEU 30 0.0003

LEU 30 LEU 31 0.0029

LEU 31 ALA 32 -0.0000

ALA 32 ASP 33 -0.0000

ASP 33 ASN 34 0.0298

ASN 34 HIS 35 -0.0002

HIS 35 HIS 36 0.0000

HIS 36 LEU 37 -0.0147

LEU 37 GLN 38 0.0001

GLN 38 VAL 39 -0.0003

VAL 39 GLY 40 -0.0241

GLY 40 SER 41 -0.0002

SER 41 ASN 42 -0.0001

ASN 42 TYR 43 -0.0020

TYR 43 LEU 44 -0.0000

LEU 44 TYR 45 0.0001

TYR 45 ILE 46 -0.0208

ILE 46 HIS 47 0.0001

HIS 47 LYS 48 -0.0002

LYS 48 ILE 49 0.0223

ILE 49 ASP 50 -0.0000

ASP 50 GLY 51 0.0001

GLY 51 LYS 52 -0.0180

LYS 52 THR 53 0.0002

THR 53 PHE 54 -0.0004

PHE 54 LEU 55 -0.0209

LEU 55 PHE 56 -0.0001

PHE 56 THR 57 -0.0002

THR 57 LYS 58 -0.0027

LYS 58 THR 59 -0.0002

THR 59 ASN 60 0.0002

ASN 60 ASP 61 0.0083

ASP 61 LYS 62 -0.0003

LYS 62 SER 63 -0.0000

SER 63 LEU 64 -0.0016

LEU 64 VAL 65 -0.0002

VAL 65 GLN 66 -0.0004

GLN 66 LYS 67 0.0025

LYS 67 ILE 68 -0.0004

ILE 68 ASN 69 -0.0000

ASN 69 ARG 70 -0.0272

ARG 70 SER 71 0.0004

SER 71 LYS 72 -0.0003

LYS 72 ALA 73 0.0094

ALA 73 SER 74 -0.0004

SER 74 VAL 75 -0.0004

VAL 75 GLU 76 0.0070

GLU 76 ASP 77 0.0003

ASP 77 ILE 78 -0.0005

ILE 78 LYS 79 0.0135

LYS 79 ASN 80 0.0001

ASN 80 SER 81 -0.0001

SER 81 LEU 82 0.0151

LEU 82 ALA 83 0.0001

ALA 83 ASP 84 0.0000

ASP 84 ASP 85 0.0751

ASP 85 GLU 86 0.0002

GLU 86 SER 87 -0.0000

SER 87 LEU 88 0.0056

LEU 88 GLY 89 0.0004

GLY 89 PHE 90 -0.0003

PHE 90 PRO 91 0.0097

PRO 91 SER 92 0.0002

SER 92 PHE 93 0.0001

PHE 93 LEU 94 -0.0498

LEU 94 PHE 95 -0.0002

PHE 95 VAL 96 0.0001

VAL 96 GLU 97 -0.0662

GLU 97 GLY 98 0.0002

GLY 98 ASP 99 -0.0001

ASP 99 THR 100 -0.0057

THR 100 ILE 101 0.0000

ILE 101 GLY 102 -0.0003

GLY 102 PHE 103 -0.0336

PHE 103 ALA 104 0.0001

ALA 104 ARG 105 0.0002

ARG 105 THR 106 -0.0676

THR 106 VAL 107 -0.0002

VAL 107 PHE 108 0.0000

PHE 108 GLY 109 -0.0310

GLY 109 PRO 110 0.0002

PRO 110 THR 111 -0.0001

THR 111 THR 112 -0.0635

THR 112 SER 113 0.0002

SER 113 ASP 114 -0.0002

ASP 114 LEU 115 -0.0097

LEU 115 THR 116 0.0000

THR 116 ASP 117 -0.0002

ASP 117 PHE 118 0.0022

PHE 118 LEU 119 0.0001

LEU 119 ILE 120 0.0000

ILE 120 GLY 121 -0.0324

GLY 121 LYS 122 -0.0002

LYS 122 GLY 123 -0.0001

GLY 123 MET 124 -0.1196

MET 124 SER 125 -0.0000

SER 125 LEU 126 -0.0000

LEU 126 SER 127 0.0198

SER 127 SER 128 -0.0002

SER 128 GLY 129 -0.0001

GLY 129 GLU 130 -0.0066

GLU 130 ARG 131 -0.0001

ARG 131 VAL 132 0.0000

VAL 132 GLN 133 0.0486

GLN 133 ILE 134 -0.0000

ILE 134 GLU 135 -0.0001

GLU 135 PRO 136 0.1731

PRO 136 LEU 137 0.0003

LEU 137 MET 138 -0.0002

MET 138 ARG 139 -0.0252

ARG 139 GLY 140 0.0001

GLY 140 THR 141 0.0003

THR 141 THR 142 0.0551

THR 142 LYS 143 -0.0000

LYS 143 ASP 144 0.0001

ASP 144 ASP 145 -0.0074

ASP 145 VAL 146 -0.0001

VAL 146 MET 147 -0.0004

MET 147 HIS 148 -0.0177

HIS 148 MET 149 -0.0003

MET 149 HIS 150 0.0003

HIS 150 PHE 151 -0.0074

PHE 151 ILE 152 -0.0000

ILE 152 GLY 153 -0.0003

GLY 153 ARG 154 -0.0159

ARG 154 THR 155 -0.0004

THR 155 THR 156 0.0001

THR 156 VAL 157 -0.0079

VAL 157 LYS 158 0.0002

LYS 158 VAL 159 -0.0004

VAL 159 GLU 160 -0.0128

GLU 160 ALA 161 0.0000

ALA 161 LYS 162 -0.0001

LYS 162 LEU 163 -0.0304

LEU 163 PRO 164 0.0001

PRO 164 VAL 165 0.0001

VAL 165 PHE 166 -0.0073

PHE 166 GLY 167 -0.0002

GLY 167 ASP 168 0.0003

ASP 168 ILE 169 0.0007

ILE 169 LEU 170 -0.0003

LEU 170 LYS 171 -0.0003

LYS 171 VAL 172 -0.0356

VAL 172 LEU 173 0.0001

LEU 173 GLY 174 -0.0001

GLY 174 ALA 175 -0.0132

ALA 175 THR 176 0.0003

THR 176 ASP 177 -0.0001

ASP 177 ILE 178 0.0088

ILE 178 GLU 179 0.0002

GLU 179 GLY 180 0.0002

GLY 180 GLU 181 -0.0018

GLU 181 LEU 182 -0.0001

LEU 182 PHE 183 0.0002

PHE 183 ASP 184 0.0207

ASP 184 SER 185 0.0001

SER 185 LEU 186 0.0003

LEU 186 ASP 187 -0.0138

ASP 187 ILE 188 0.0001

ILE 188 VAL 189 -0.0002

VAL 189 ILE 190 -0.0133

ILE 190 LYS 191 0.0002

LYS 191 PRO 192 -0.0003

PRO 192 LYS 193 0.0085

LYS 193 PHE 194 -0.0002

PHE 194 LYS 195 -0.0002

LYS 195 ARG 196 -0.0087

ARG 196 ASP 197 -0.0000

ASP 197 ILE 198 -0.0001

ILE 198 LYS 199 0.0343

LYS 199 LYS 200 0.0000

LYS 200 VAL 201 -0.0003

VAL 201 ALA 202 0.0277

ALA 202 LYS 203 0.0001

LYS 203 ASP 204 -0.0001

ASP 204 ILE 205 -0.0232

ILE 205 ILE 206 0.0000

ILE 206 PHE 207 -0.0003

PHE 207 ASN 208 0.0369

ASN 208 PRO 209 0.0001

PRO 209 SER 210 0.0005

SER 210 PRO 211 -0.0241

PRO 211 GLN 212 0.0001

GLN 212 PHE 213 0.0000

PHE 213 SER 214 -0.0529

SER 214 ASP 215 -0.0003

ASP 215 ILE 216 -0.0000

ILE 216 SER 217 -0.0235

SER 217 LEU 218 0.0004

LEU 218 ARG 219 -0.0004

ARG 219 ALA 220 -0.0208

ALA 220 LYS 221 -0.0001

LYS 221 ASP 222 0.0000

ASP 222 GLU 223 0.0084

GLU 223 ALA 224 -0.0001

ALA 224 GLY 225 -0.0002

GLY 225 ASP 226 0.0121

ASP 226 ILE 227 0.0003

ILE 227 LEU 228 -0.0003

LEU 228 THR 229 0.0195

THR 229 GLU 230 0.0002

GLU 230 HIS 231 -0.0001

HIS 231 TYR 232 -0.0149

TYR 232 LEU 233 -0.0005

LEU 233 SER 234 0.0001

SER 234 GLU 235 -0.0787

GLU 235 LYS 236 -0.0002

LYS 236 GLY 237 0.0005

GLY 237 HIS 238 0.2184

HIS 238 LEU 239 -0.0001

LEU 239 SER 240 0.0006

SER 240 ALA 241 0.0603

ALA 241 PRO 242 0.0001

PRO 242 LEU 243 0.0005

LEU 243 ASN 244 -0.0211

ASN 244 LYS 245 0.0001

LYS 245 VAL 246 0.0004

VAL 246 THR 247 -0.0064

THR 247 ASN 248 0.0001

ASN 248 ALA 249 0.0001

ALA 249 GLU 250 0.0016

GLU 250 ILE 251 0.0001

ILE 251 ALA 252 0.0002

ALA 252 GLU 253 0.0111

GLU 253 GLU 254 0.0002

GLU 254 MET 255 -0.0001

MET 255 ALA 256 -0.0129

ALA 256 TYR 257 -0.0002

TYR 257 CYS 258 0.0002

CYS 258 TYR 259 -0.0008

TYR 259 ALA 260 0.0003

ALA 260 ARG 261 -0.0003

ARG 261 MET 262 0.0268

MET 262 LYS 263 -0.0003

LYS 263 SER 264 0.0000

SER 264 ASP 265 0.0005

ASP 265 ILE 266 0.0002

ILE 266 LEU 267 -0.0003

LEU 267 GLU 268 0.0051

GLU 268 CYS 269 0.0000

CYS 269 PHE 270 0.0002

PHE 270 LYS 271 -0.3053

LYS 271 ARG 272 0.0002

ARG 272 GLN 273 0.0001

GLN 273 VAL 274 0.0048

VAL 274 GLY 275 0.0001

GLY 275 LYS 276 0.0005

LYS 276 VAL 277 -0.4011

VAL 277 LYS 278 0.0004

LYS 278 ASP 279 0.0003

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 9 ---

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

* Chappie dimer compare ver 3 *