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

* Chappie dimer compare ver 3 *

CA strain for 221218005903105706

--- normal mode 7 ---

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 -0.0003

ASN 3 GLY 4 -0.0309

GLY 4 PHE 5 -0.0002

PHE 5 TYR 6 0.0001

TYR 6 ALA 7 0.0113

ALA 7 THR 8 0.0003

THR 8 TYR 9 -0.0004

TYR 9 ARG 10 -0.0053

ARG 10 SER 11 -0.0005

SER 11 LYS 12 0.0003

LYS 12 ASN 13 0.0236

ASN 13 LYS 14 -0.0001

LYS 14 GLY 15 -0.0002

GLY 15 LYS 16 0.0412

LYS 16 ASP 17 -0.0001

ASP 17 LYS 18 0.0000

LYS 18 ARG 19 -0.0062

ARG 19 SER 20 -0.0001

SER 20 ILE 21 0.0000

ILE 21 ASN 22 0.0062

ASN 22 LEU 23 0.0000

LEU 23 SER 24 0.0004

SER 24 VAL 25 0.0003

VAL 25 PHE 26 0.0001

PHE 26 LEU 27 -0.0003

LEU 27 ASN 28 0.0115

ASN 28 SER 29 0.0004

SER 29 LEU 30 0.0001

LEU 30 ASN 34 -0.0349

ASN 34 HIS 35 -0.0001

HIS 35 HIS 36 0.0002

HIS 36 LEU 37 -0.0024

LEU 37 GLN 38 -0.0002

GLN 38 VAL 39 -0.0001

VAL 39 GLY 40 0.0030

GLY 40 SER 41 -0.0001

SER 41 ASN 42 -0.0002

ASN 42 TYR 43 -0.0045

TYR 43 LEU 44 0.0000

LEU 44 TYR 45 -0.0000

TYR 45 ILE 46 -0.0254

ILE 46 HIS 47 -0.0001

HIS 47 LYS 48 -0.0002

LYS 48 ILE 49 0.0253

ILE 49 ASP 50 0.0002

ASP 50 GLY 51 -0.0002

GLY 51 LYS 52 -0.0291

LYS 52 THR 53 -0.0001

THR 53 PHE 54 -0.0001

PHE 54 LEU 55 -0.0314

LEU 55 PHE 56 0.0002

PHE 56 THR 57 -0.0002

THR 57 LYS 58 -0.0198

LYS 58 THR 59 0.0001

THR 59 ASN 60 -0.0005

ASN 60 ASP 61 0.0113

ASP 61 LYS 62 0.0000

LYS 62 SER 63 0.0000

SER 63 LEU 64 -0.0069

LEU 64 VAL 65 0.0005

VAL 65 GLN 66 -0.0001

GLN 66 LYS 67 0.0040

LYS 67 ILE 68 0.0001

ILE 68 ASN 69 0.0002

ASN 69 ARG 70 0.0004

ARG 70 SER 71 -0.0002

SER 71 LYS 72 -0.0000

LYS 72 ALA 73 -0.0036

ALA 73 SER 74 0.0002

SER 74 VAL 75 -0.0001

VAL 75 GLU 76 -0.0023

GLU 76 ASP 77 -0.0001

ASP 77 ILE 78 0.0002

ILE 78 LYS 79 -0.0001

LYS 79 ASN 80 -0.0000

ASN 80 SER 81 -0.0000

SER 81 LEU 82 0.0408

LEU 82 ALA 83 0.0001

ALA 83 ASP 84 -0.0001

ASP 84 ASP 85 0.0214

ASP 85 GLU 86 -0.0001

GLU 86 SER 87 0.0001

SER 87 LEU 88 0.0019

LEU 88 GLY 89 0.0002

GLY 89 PHE 90 0.0001

PHE 90 PRO 91 -0.0206

PRO 91 SER 92 -0.0002

SER 92 PHE 93 -0.0002

PHE 93 LEU 94 -0.0253

LEU 94 PHE 95 0.0001

PHE 95 VAL 96 -0.0000

VAL 96 GLU 97 -0.0403

GLU 97 GLY 98 0.0000

GLY 98 ASP 99 -0.0003

ASP 99 THR 100 0.0107

THR 100 ILE 101 0.0002

ILE 101 GLY 102 -0.0002

GLY 102 PHE 103 -0.0253

PHE 103 ALA 104 -0.0000

ALA 104 ARG 105 0.0000

ARG 105 THR 106 -0.0191

THR 106 VAL 107 0.0001

VAL 107 PHE 108 -0.0003

PHE 108 GLY 109 -0.0108

GLY 109 PRO 110 0.0001

PRO 110 THR 111 -0.0000

THR 111 THR 112 0.0124

THR 112 SER 113 -0.0000

SER 113 ASP 114 -0.0003

ASP 114 LEU 115 -0.0104

LEU 115 THR 116 -0.0004

THR 116 ASP 117 -0.0001

ASP 117 PHE 118 0.0079

PHE 118 LEU 119 0.0001

LEU 119 ILE 120 -0.0001

ILE 120 GLY 121 0.0110

GLY 121 LYS 122 -0.0004

LYS 122 GLY 123 0.0003

GLY 123 MET 124 -0.0282

MET 124 SER 125 -0.0003

SER 125 LEU 126 -0.0000

LEU 126 SER 127 0.0055

SER 127 SER 128 -0.0001

SER 128 GLY 129 0.0001

GLY 129 GLU 130 -0.0077

GLU 130 ARG 131 0.0002

ARG 131 VAL 132 -0.0003

VAL 132 GLN 133 0.0139

GLN 133 ILE 134 -0.0004

ILE 134 GLU 135 0.0005

GLU 135 PRO 136 -0.0054

PRO 136 LEU 137 0.0001

LEU 137 MET 138 -0.0000

MET 138 ARG 139 0.0197

ARG 139 GLY 140 0.0003

GLY 140 THR 141 -0.0002

THR 141 THR 142 0.0344

THR 142 LYS 143 0.0000

LYS 143 ASP 144 -0.0001

ASP 144 ASP 145 -0.0186

ASP 145 VAL 146 0.0003

VAL 146 MET 147 0.0001

MET 147 HIS 148 -0.0268

HIS 148 MET 149 -0.0002

MET 149 HIS 150 0.0003

HIS 150 PHE 151 0.0252

PHE 151 ILE 152 0.0000

ILE 152 GLY 153 0.0001

GLY 153 ARG 154 -0.0323

ARG 154 THR 155 -0.0004

THR 155 THR 156 0.0003

THR 156 VAL 157 0.0076

VAL 157 LYS 158 0.0003

LYS 158 VAL 159 -0.0000

VAL 159 GLU 160 -0.0069

GLU 160 ALA 161 -0.0003

ALA 161 LYS 162 -0.0000

LYS 162 LEU 163 -0.0320

LEU 163 PRO 164 0.0000

PRO 164 VAL 165 -0.0000

VAL 165 PHE 166 -0.0232

PHE 166 GLY 167 0.0001

GLY 167 ASP 168 0.0003

ASP 168 ILE 169 0.0160

ILE 169 LEU 170 0.0001

LEU 170 LYS 171 0.0003

LYS 171 VAL 172 0.0045

VAL 172 LEU 173 0.0003

LEU 173 GLY 174 0.0002

GLY 174 ALA 175 0.0120

ALA 175 THR 176 0.0002

THR 176 ASP 177 -0.0003

ASP 177 ILE 178 -0.0129

ILE 178 GLU 179 0.0003

GLU 179 GLY 180 0.0003

GLY 180 GLU 181 -0.0104

GLU 181 LEU 182 -0.0000

LEU 182 PHE 183 0.0002

PHE 183 ASP 184 -0.0892

ASP 184 SER 185 0.0004

SER 185 LEU 186 0.0001

LEU 186 ASP 187 0.0169

ASP 187 ILE 188 0.0001

ILE 188 VAL 189 -0.0005

VAL 189 ILE 190 -0.0479

ILE 190 LYS 191 0.0001

LYS 191 PRO 192 0.0002

PRO 192 LYS 193 -0.0385

LYS 193 PHE 194 -0.0003

PHE 194 LYS 195 0.0000

LYS 195 ARG 196 -0.0236

ARG 196 ASP 197 0.0001

ASP 197 ILE 198 0.0002

ILE 198 LYS 199 0.0508

LYS 199 LYS 200 -0.0003

LYS 200 VAL 201 0.0000

VAL 201 ALA 202 0.0209

ALA 202 LYS 203 0.0001

LYS 203 ASP 204 0.0000

ASP 204 ILE 205 -0.0172

ILE 205 ILE 206 -0.0002

ILE 206 PHE 207 -0.0000

PHE 207 ASN 208 -0.0201

ASN 208 PRO 209 -0.0002

PRO 209 SER 210 0.0003

SER 210 PRO 211 0.0058

PRO 211 GLN 212 -0.0003

GLN 212 PHE 213 -0.0000

PHE 213 SER 214 0.0130

SER 214 ASP 215 -0.0000

ASP 215 ILE 216 -0.0004

ILE 216 SER 217 -0.0272

SER 217 LEU 218 -0.0002

LEU 218 ARG 219 0.0000

ARG 219 ALA 220 -0.0392

ALA 220 LYS 221 -0.0003

LYS 221 ASP 222 0.0000

ASP 222 GLU 223 0.0006

GLU 223 ALA 224 0.0002

ALA 224 GLY 225 -0.0001

GLY 225 ASP 226 0.0032

ASP 226 LEU 228 -0.0181

LEU 228 THR 229 0.0002

THR 229 GLU 230 0.0004

GLU 230 HIS 231 -0.0281

HIS 231 TYR 232 0.0001

TYR 232 LEU 233 -0.0001

LEU 233 SER 234 -0.0147

SER 234 GLU 235 0.0002

GLU 235 LYS 236 0.0003

LYS 236 GLY 237 -0.0010

GLY 237 HIS 238 -0.0001

HIS 238 LEU 239 0.0002

LEU 239 SER 240 0.1027

SER 240 ALA 241 -0.0003

ALA 241 PRO 242 0.0000

PRO 242 LEU 243 0.0538

LEU 243 ASN 244 0.0004

ASN 244 LYS 245 -0.0003

LYS 245 VAL 246 -0.0217

VAL 246 THR 247 -0.0003

THR 247 ASN 248 -0.0001

ASN 248 ALA 249 -0.0232

ALA 249 GLU 250 -0.0001

GLU 250 ILE 251 -0.0002

ILE 251 ALA 252 -0.0185

ALA 252 GLU 253 -0.0000

GLU 253 GLU 254 0.0002

GLU 254 MET 255 -0.0026

MET 255 ALA 256 0.0004

ALA 256 TYR 257 0.0001

TYR 257 CYS 258 0.0250

CYS 258 TYR 259 -0.0001

TYR 259 ALA 260 0.0003

ALA 260 ARG 261 -0.0142

ARG 261 MET 262 0.0002

MET 262 LYS 263 -0.0001

LYS 263 SER 264 -0.0962

SER 264 ASP 265 0.0001

ASP 265 ILE 266 -0.0005

ILE 266 LEU 267 0.0030

LEU 267 GLU 268 -0.0003

GLU 268 CYS 269 0.0001

CYS 269 PHE 270 -0.0192

PHE 270 LYS 271 0.0001

LYS 271 ARG 272 0.0003

ARG 272 GLN 273 0.0700

GLN 273 VAL 274 -0.0001

VAL 274 GLY 275 0.0003

GLY 275 LYS 276 -0.0757

LYS 276 VAL 277 0.0001

VAL 277 LYS 278 0.0001

LYS 278 ASP 279 -0.0556

ASP 279 MET 1 -0.1382

MET 1 LYS 2 -0.0005

LYS 2 ASN 3 0.0000

ASN 3 GLY 4 0.0254

GLY 4 PHE 5 0.0001

PHE 5 TYR 6 -0.0004

TYR 6 ALA 7 -0.0120

ALA 7 THR 8 0.0002

THR 8 TYR 9 0.0000

TYR 9 ARG 10 0.0085

ARG 10 SER 11 0.0001

SER 11 LYS 12 -0.0003

LYS 12 ASN 13 -0.0001

ASN 13 LYS 14 -0.0004

LYS 14 GLY 15 0.0002

GLY 15 LYS 16 0.0070

LYS 16 ASP 17 0.0003

ASP 17 LYS 18 -0.0003

LYS 18 ARG 19 0.0058

ARG 19 SER 20 -0.0002

SER 20 ILE 21 -0.0003

ILE 21 ASN 22 -0.0110

ASN 22 LEU 23 -0.0004

LEU 23 SER 24 0.0004

SER 24 VAL 25 0.0069

VAL 25 PHE 26 0.0001

PHE 26 LEU 27 0.0002

LEU 27 ASN 28 -0.0102

ASN 28 SER 29 -0.0002

SER 29 LEU 30 0.0001

LEU 30 LEU 31 -0.0160

LEU 31 ALA 32 0.0000

ALA 32 ASP 33 -0.0001

ASP 33 ASN 34 -0.0112

ASN 34 HIS 35 -0.0001

HIS 35 HIS 36 0.0000

HIS 36 LEU 37 -0.0086

LEU 37 GLN 38 0.0001

GLN 38 VAL 39 -0.0003

VAL 39 GLY 40 -0.0075

GLY 40 SER 41 -0.0003

SER 41 ASN 42 0.0001

ASN 42 TYR 43 0.0046

TYR 43 LEU 44 0.0000

LEU 44 TYR 45 -0.0000

TYR 45 ILE 46 0.0291

ILE 46 HIS 47 -0.0002

HIS 47 LYS 48 -0.0000

LYS 48 ILE 49 -0.0066

ILE 49 ASP 50 -0.0001

ASP 50 GLY 51 0.0003

GLY 51 LYS 52 0.0219

LYS 52 THR 53 0.0000

THR 53 PHE 54 0.0005

PHE 54 LEU 55 0.0262

LEU 55 PHE 56 -0.0003

PHE 56 THR 57 0.0001

THR 57 LYS 58 0.0246

LYS 58 THR 59 0.0003

THR 59 ASN 60 -0.0001

ASN 60 ASP 61 -0.0112

ASP 61 LYS 62 0.0002

LYS 62 SER 63 0.0002

SER 63 LEU 64 0.0132

LEU 64 VAL 65 -0.0001

VAL 65 GLN 66 -0.0000

GLN 66 LYS 67 -0.0016

LYS 67 ILE 68 -0.0001

ILE 68 ASN 69 0.0002

ASN 69 ARG 70 -0.0039

ARG 70 SER 71 0.0001

SER 71 LYS 72 -0.0002

LYS 72 ALA 73 0.0044

ALA 73 SER 74 0.0002

SER 74 VAL 75 0.0001

VAL 75 GLU 76 -0.0061

GLU 76 ASP 77 -0.0001

ASP 77 ILE 78 0.0002

ILE 78 LYS 79 0.0239

LYS 79 ASN 80 -0.0001

ASN 80 SER 81 0.0001

SER 81 LEU 82 -0.0356

LEU 82 ALA 83 -0.0000

ALA 83 ASP 84 0.0001

ASP 84 ASP 85 -0.0088

ASP 85 GLU 86 0.0001

GLU 86 SER 87 0.0001

SER 87 LEU 88 0.0039

LEU 88 GLY 89 0.0001

GLY 89 PHE 90 0.0002

PHE 90 PRO 91 0.0299

PRO 91 SER 92 -0.0004

SER 92 PHE 93 0.0003

PHE 93 LEU 94 0.0106

LEU 94 PHE 95 0.0003

PHE 95 VAL 96 -0.0001

VAL 96 GLU 97 0.0147

GLU 97 GLY 98 -0.0002

GLY 98 ASP 99 -0.0002

ASP 99 THR 100 -0.0240

THR 100 ILE 101 -0.0002

ILE 101 GLY 102 0.0002

GLY 102 PHE 103 -0.0089

PHE 103 ALA 104 -0.0001

ALA 104 ARG 105 0.0000

ARG 105 THR 106 0.0078

THR 106 VAL 107 0.0002

VAL 107 PHE 108 0.0001

PHE 108 GLY 109 0.0081

GLY 109 PRO 110 0.0001

PRO 110 THR 111 0.0001

THR 111 THR 112 -0.0221

THR 112 SER 113 -0.0001

SER 113 ASP 114 0.0000

ASP 114 LEU 115 0.0130

LEU 115 THR 116 -0.0003

THR 116 ASP 117 0.0002

ASP 117 PHE 118 -0.0102

PHE 118 LEU 119 -0.0002

LEU 119 ILE 120 0.0003

ILE 120 GLY 121 -0.0174

GLY 121 LYS 122 0.0001

LYS 122 GLY 123 0.0002

GLY 123 MET 124 0.0169

MET 124 SER 125 -0.0000

SER 125 LEU 126 -0.0004

LEU 126 SER 127 0.0041

SER 127 SER 128 0.0000

SER 128 GLY 129 -0.0002

GLY 129 GLU 130 0.0037

GLU 130 ARG 131 0.0003

ARG 131 VAL 132 -0.0001

VAL 132 GLN 133 -0.0195

GLN 133 ILE 134 0.0004

ILE 134 GLU 135 0.0003

GLU 135 PRO 136 0.0593

PRO 136 LEU 137 -0.0001

LEU 137 MET 138 0.0002

MET 138 ARG 139 0.0224

ARG 139 GLY 140 0.0001

GLY 140 THR 141 0.0000

THR 141 THR 142 0.0106

THR 142 LYS 143 0.0001

LYS 143 ASP 144 -0.0002

ASP 144 ASP 145 0.0091

ASP 145 VAL 146 0.0000

VAL 146 MET 147 0.0001

MET 147 HIS 148 0.0539

HIS 148 MET 149 0.0001

MET 149 HIS 150 -0.0002

HIS 150 PHE 151 -0.0330

PHE 151 ILE 152 -0.0000

ILE 152 GLY 153 0.0003

GLY 153 ARG 154 0.0226

ARG 154 THR 155 -0.0003

THR 155 THR 156 0.0001

THR 156 VAL 157 -0.0202

VAL 157 LYS 158 0.0002

LYS 158 VAL 159 0.0001

VAL 159 GLU 160 -0.0100

GLU 160 ALA 161 -0.0000

ALA 161 LYS 162 -0.0001

LYS 162 LEU 163 0.0157

LEU 163 PRO 164 0.0001

PRO 164 VAL 165 0.0001

VAL 165 PHE 166 0.0065

PHE 166 GLY 167 0.0002

GLY 167 ASP 168 0.0002

ASP 168 ILE 169 -0.0111

ILE 169 LEU 170 0.0002

LEU 170 LYS 171 -0.0001

LYS 171 VAL 172 -0.0056

VAL 172 LEU 173 0.0000

LEU 173 GLY 174 0.0003

GLY 174 ALA 175 -0.0066

ALA 175 THR 176 0.0003

THR 176 ASP 177 0.0001

ASP 177 ILE 178 0.0203

ILE 178 GLU 179 -0.0001

GLU 179 GLY 180 0.0000

GLY 180 GLU 181 0.0174

GLU 181 LEU 182 -0.0001

LEU 182 PHE 183 -0.0000

PHE 183 ASP 184 0.0990

ASP 184 SER 185 0.0005

SER 185 LEU 186 -0.0002

LEU 186 ASP 187 -0.0161

ASP 187 ILE 188 -0.0000

ILE 188 VAL 189 0.0000

VAL 189 ILE 190 0.0509

ILE 190 LYS 191 0.0001

LYS 191 PRO 192 -0.0002

PRO 192 LYS 193 0.0525

LYS 193 PHE 194 -0.0001

PHE 194 LYS 195 0.0001

LYS 195 ARG 196 0.0226

ARG 196 ASP 197 -0.0000

ASP 197 ILE 198 -0.0000

ILE 198 LYS 199 -0.0588

LYS 199 LYS 200 -0.0005

LYS 200 VAL 201 -0.0001

VAL 201 ALA 202 -0.0178

ALA 202 LYS 203 -0.0003

LYS 203 ASP 204 0.0002

ASP 204 ILE 205 0.0260

ILE 205 ILE 206 -0.0001

ILE 206 PHE 207 0.0004

PHE 207 ASN 208 0.0050

ASN 208 PRO 209 -0.0003

PRO 209 SER 210 0.0003

SER 210 PRO 211 -0.0099

PRO 211 GLN 212 0.0001

GLN 212 PHE 213 0.0001

PHE 213 SER 214 -0.0022

SER 214 ASP 215 -0.0003

ASP 215 ILE 216 0.0003

ILE 216 SER 217 0.0227

SER 217 LEU 218 0.0002

LEU 218 ARG 219 -0.0001

ARG 219 ALA 220 0.0205

ALA 220 LYS 221 0.0002

LYS 221 ASP 222 0.0002

ASP 222 GLU 223 -0.0054

GLU 223 ALA 224 -0.0004

ALA 224 GLY 225 -0.0001

GLY 225 ASP 226 -0.0145

ASP 226 ILE 227 0.0001

ILE 227 LEU 228 0.0001

LEU 228 THR 229 0.0042

THR 229 GLU 230 0.0002

GLU 230 HIS 231 -0.0002

HIS 231 TYR 232 0.0092

TYR 232 LEU 233 -0.0001

LEU 233 SER 234 -0.0000

SER 234 GLU 235 -0.0456

GLU 235 LYS 236 0.0002

LYS 236 GLY 237 0.0000

GLY 237 HIS 238 -0.0274

HIS 238 LEU 239 0.0004

LEU 239 SER 240 -0.0005

SER 240 ALA 241 -0.0646

ALA 241 PRO 242 0.0002

PRO 242 LEU 243 -0.0001

LEU 243 ASN 244 -0.0250

ASN 244 LYS 245 0.0001

LYS 245 VAL 246 0.0000

VAL 246 THR 247 -0.0298

THR 247 ASN 248 -0.0001

ASN 248 ALA 249 -0.0002

ALA 249 GLU 250 -0.0010

GLU 250 ILE 251 0.0002

ILE 251 ALA 252 -0.0003

ALA 252 GLU 253 0.0217

GLU 253 GLU 254 -0.0001

GLU 254 MET 255 0.0004

MET 255 ALA 256 -0.0504

ALA 256 TYR 257 -0.0003

TYR 257 CYS 258 -0.0001

CYS 258 TYR 259 -0.0606

TYR 259 ALA 260 0.0002

ALA 260 ARG 261 -0.0002

ARG 261 MET 262 0.0036

MET 262 LYS 263 -0.0001

LYS 263 SER 264 -0.0000

SER 264 ASP 265 0.0648

ASP 265 ILE 266 0.0002

ILE 266 LEU 267 0.0002

LEU 267 GLU 268 0.0647

GLU 268 CYS 269 0.0001

CYS 269 PHE 270 -0.0004

PHE 270 LYS 271 0.0300

LYS 271 ARG 272 -0.0002

ARG 272 GLN 273 0.0001

GLN 273 VAL 274 0.0272

VAL 274 GLY 275 -0.0003

GLY 275 LYS 276 0.0001

LYS 276 VAL 277 0.0549

VAL 277 LYS 278 0.0001

LYS 278 ASP 279 0.0002

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 7 ---

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

* Chappie dimer compare ver 3 *