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

* 7tim E:) *

CA strain for 2405231911392957911

--- 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
ALA 2 ARG 3 0.0002

ARG 3 THR 4 -0.0001

THR 4 PHE 5 -0.0277

PHE 5 PHE 6 -0.0000

PHE 6 VAL 7 0.0001

VAL 7 GLY 8 -0.0080

GLY 8 GLY 9 0.0003

GLY 9 ASN 10 0.0000

ASN 10 PHE 11 -0.0018

PHE 11 LYS 12 -0.0002

LYS 12 LEU 13 -0.0001

LEU 13 ASN 14 0.0047

ASN 14 GLY 15 -0.0001

GLY 15 SER 16 -0.0002

SER 16 LYS 17 -0.0443

LYS 17 GLN 18 -0.0002

GLN 18 SER 19 -0.0002

SER 19 ILE 20 -0.0143

ILE 20 LYS 21 0.0001

LYS 21 GLU 22 -0.0003

GLU 22 ILE 23 -0.0095

ILE 23 VAL 24 -0.0003

VAL 24 GLU 25 0.0002

GLU 25 ARG 26 -0.0186

ARG 26 LEU 27 0.0004

LEU 27 ASN 28 -0.0003

ASN 28 THR 29 -0.0210

THR 29 ALA 30 -0.0000

ALA 30 SER 31 -0.0000

SER 31 ILE 32 -0.0005

ILE 32 PRO 33 -0.0002

PRO 33 GLU 34 0.0002

GLU 34 ASN 35 0.0052

ASN 35 VAL 36 -0.0001

VAL 36 GLU 37 -0.0003

GLU 37 VAL 38 0.0477

VAL 38 VAL 39 0.0003

VAL 39 ILE 40 -0.0002

ILE 40 CYS 41 0.0147

CYS 41 PRO 42 0.0001

PRO 42 PRO 43 0.0001

PRO 43 ALA 44 -0.0130

ALA 44 THR 45 0.0003

THR 45 TYR 46 -0.0002

TYR 46 LEU 47 0.0766

LEU 47 ASP 48 0.0002

ASP 48 TYR 49 0.0001

TYR 49 SER 50 0.0265

SER 50 VAL 51 -0.0004

VAL 51 SER 52 -0.0001

SER 52 LEU 53 -0.0598

LEU 53 VAL 54 -0.0002

VAL 54 LYS 55 0.0002

LYS 55 LYS 56 0.0831

LYS 56 PRO 57 0.0000

PRO 57 GLN 58 -0.0001

GLN 58 VAL 59 0.0005

VAL 59 THR 60 0.0001

THR 60 VAL 61 0.0001

VAL 61 GLY 62 -0.0613

GLY 62 ALA 63 -0.0002

ALA 63 GLN 64 -0.0001

GLN 64 ASN 65 -0.0162

ASN 65 ALA 66 0.0001

ALA 66 TYR 67 -0.0000

TYR 67 LEU 68 -0.0468

LEU 68 LYS 69 -0.0001

LYS 69 ALA 70 0.0004

ALA 70 SER 71 0.0125

SER 71 GLY 72 -0.0001

GLY 72 ALA 73 0.0000

ALA 73 PHE 74 0.0007

PHE 74 THR 75 -0.0001

THR 75 GLY 76 -0.0001

GLY 76 GLU 77 -0.1073

GLU 77 ASN 78 -0.0000

ASN 78 SER 79 0.0002

SER 79 VAL 80 -0.0686

VAL 80 ASP 81 -0.0003

ASP 81 GLN 82 0.0003

GLN 82 ILE 83 -0.0087

ILE 83 LYS 84 -0.0000

LYS 84 ASP 85 -0.0001

ASP 85 VAL 86 -0.0178

VAL 86 GLY 87 -0.0000

GLY 87 ALA 88 0.0002

ALA 88 LYS 89 0.1325

LYS 89 TRP 90 -0.0002

TRP 90 VAL 91 -0.0000

VAL 91 ILE 92 -0.0068

ILE 92 LEU 93 -0.0000

LEU 93 GLY 94 0.0000

GLY 94 HIS 95 -0.0095

HIS 95 SER 96 0.0002

SER 96 GLU 97 -0.0000

GLU 97 ARG 98 0.0130

ARG 98 ARG 99 -0.0001

ARG 99 SER 100 0.0003

SER 100 TYR 101 -0.1422

TYR 101 PHE 102 0.0002

PHE 102 HIS 103 -0.0001

HIS 103 GLU 104 -0.0399

GLU 104 ASP 105 0.0001

ASP 105 ASP 106 0.0003

ASP 106 LYS 107 0.0110

LYS 107 PHE 108 0.0001

PHE 108 ILE 109 -0.0003

ILE 109 ALA 110 -0.0424

ALA 110 ASP 111 -0.0000

ASP 111 LYS 112 -0.0002

LYS 112 THR 113 -0.0363

THR 113 LYS 114 0.0000

LYS 114 PHE 115 -0.0001

PHE 115 ALA 116 0.0041

ALA 116 LEU 117 0.0001

LEU 117 GLY 118 0.0001

GLY 118 GLN 119 0.0494

GLN 119 GLY 120 0.0001

GLY 120 VAL 121 -0.0002

VAL 121 GLY 122 0.0350

GLY 122 VAL 123 0.0002

VAL 123 ILE 124 -0.0001

ILE 124 LEU 125 0.0460

LEU 125 CYS 126 0.0002

CYS 126 ILE 127 -0.0000

ILE 127 GLY 128 0.0380

GLY 128 GLU 129 0.0004

GLU 129 THR 130 -0.0000

THR 130 LEU 131 -0.0028

LEU 131 GLU 132 -0.0002

GLU 132 GLU 133 0.0000

GLU 133 LYS 134 0.0147

LYS 134 LYS 135 0.0001

LYS 135 ALA 136 0.0002

ALA 136 GLY 137 0.0366

GLY 137 LYS 138 -0.0001

LYS 138 THR 139 -0.0001

THR 139 LEU 140 0.0156

LEU 140 ASP 141 0.0003

ASP 141 VAL 142 0.0002

VAL 142 VAL 143 -0.0009

VAL 143 GLU 144 -0.0001

GLU 144 ARG 145 -0.0003

ARG 145 GLN 146 0.0050

GLN 146 LEU 147 0.0001

LEU 147 ASN 148 -0.0004

ASN 148 ALA 149 -0.0001

ALA 149 VAL 150 0.0003

VAL 150 LEU 151 -0.0000

LEU 151 GLU 152 -0.0196

GLU 152 GLU 153 -0.0001

GLU 153 VAL 154 -0.0001

VAL 154 LYS 155 -0.0056

LYS 155 ASP 156 0.0000

ASP 156 TRP 157 -0.0002

TRP 157 THR 158 0.0200

THR 158 ASN 159 -0.0001

ASN 159 VAL 160 0.0004

VAL 160 VAL 161 -0.0092

VAL 161 VAL 162 -0.0002

VAL 162 ALA 163 -0.0001

ALA 163 TYR 164 0.0472

TYR 164 GLU 165 0.0002

GLU 165 PRO 166 -0.0000

PRO 166 VAL 167 -0.0065

VAL 167 TRP 168 0.0001

TRP 168 ALA 169 0.0001

ALA 169 ILE 170 -0.0596

ILE 170 GLY 171 0.0003

GLY 171 THR 172 -0.0000

THR 172 GLY 173 0.0098

GLY 173 LEU 174 -0.0005

LEU 174 ALA 175 0.0002

ALA 175 ALA 176 -0.0199

ALA 176 THR 177 -0.0001

THR 177 PRO 178 -0.0003

PRO 178 GLU 179 -0.0001

GLU 179 ASP 180 -0.0000

ASP 180 ALA 181 0.0003

ALA 181 GLN 182 -0.0155

GLN 182 ASP 183 -0.0000

ASP 183 ILE 184 0.0004

ILE 184 HIS 185 0.0185

HIS 185 ALA 186 -0.0002

ALA 186 SER 187 0.0002

SER 187 ILE 188 -0.0100

ILE 188 ARG 189 0.0004

ARG 189 LYS 190 -0.0002

LYS 190 PHE 191 -0.0084

PHE 191 LEU 192 0.0001

LEU 192 ALA 193 -0.0003

ALA 193 SER 194 -0.0037

SER 194 LYS 195 -0.0002

LYS 195 LEU 196 0.0001

LEU 196 GLY 197 -0.0170

GLY 197 ASP 198 0.0002

ASP 198 LYS 199 0.0001

LYS 199 ALA 200 0.0084

ALA 200 ALA 201 0.0002

ALA 201 SER 202 -0.0001

SER 202 GLU 203 0.0227

GLU 203 LEU 204 0.0001

LEU 204 ARG 205 -0.0001

ARG 205 ILE 206 0.0075

ILE 206 LEU 207 -0.0001

LEU 207 TYR 208 0.0000

TYR 208 GLY 209 -0.0233

GLY 209 GLY 210 0.0001

GLY 210 SER 211 0.0001

SER 211 ALA 212 -0.0029

ALA 212 ASN 213 -0.0000

ASN 213 GLY 214 -0.0003

GLY 214 SER 215 -0.0064

SER 215 ASN 216 -0.0002

ASN 216 ALA 217 0.0000

ALA 217 VAL 218 -0.0060

VAL 218 THR 219 0.0000

THR 219 PHE 220 -0.0002

PHE 220 LYS 221 0.0061

LYS 221 ASP 222 -0.0002

ASP 222 LYS 223 -0.0001

LYS 223 ALA 224 -0.0139

ALA 224 ASP 225 0.0003

ASP 225 VAL 226 -0.0002

VAL 226 ASP 227 0.0262

ASP 227 GLY 228 0.0005

GLY 228 PHE 229 -0.0002

PHE 229 LEU 230 -0.0259

LEU 230 VAL 231 -0.0002

VAL 231 GLY 232 0.0003

GLY 232 GLY 233 0.0104

GLY 233 ALA 234 0.0003

ALA 234 SER 235 -0.0003

SER 235 LEU 236 -0.0153

LEU 236 LYS 237 -0.0001

LYS 237 PRO 238 0.0001

PRO 238 GLU 239 -0.0224

GLU 239 PHE 240 0.0002

PHE 240 VAL 241 0.0004

VAL 241 ASP 242 -0.0036

ASP 242 ILE 243 0.0003

ILE 243 ILE 244 0.0001

ILE 244 ASN 245 -0.0076

ASN 245 SER 246 0.0001

SER 246 ARG 247 0.0003

ARG 247 ASN 248 0.0022

ASN 248 ALA 2 0.0217

ALA 2 ARG 3 -0.0000

ARG 3 THR 4 -0.0001

THR 4 PHE 5 -0.0222

PHE 5 PHE 6 -0.0002

PHE 6 VAL 7 0.0003

VAL 7 GLY 8 -0.0039

GLY 8 GLY 9 0.0002

GLY 9 ASN 10 0.0003

ASN 10 PHE 11 0.0059

PHE 11 LYS 12 -0.0001

LYS 12 LEU 13 0.0005

LEU 13 ASN 14 0.0015

ASN 14 GLY 15 0.0003

GLY 15 SER 16 -0.0003

SER 16 LYS 17 -0.0403

LYS 17 GLN 18 -0.0003

GLN 18 SER 19 0.0002

SER 19 ILE 20 -0.0293

ILE 20 LYS 21 0.0000

LYS 21 GLU 22 -0.0002

GLU 22 ILE 23 -0.0081

ILE 23 VAL 24 -0.0000

VAL 24 GLU 25 -0.0000

GLU 25 ARG 26 -0.0105

ARG 26 LEU 27 0.0001

LEU 27 ASN 28 -0.0000

ASN 28 THR 29 -0.0286

THR 29 ALA 30 -0.0002

ALA 30 SER 31 0.0001

SER 31 ILE 32 -0.0157

ILE 32 PRO 33 0.0001

PRO 33 GLU 34 -0.0002

GLU 34 ASN 35 -0.0029

ASN 35 VAL 36 -0.0002

VAL 36 GLU 37 0.0002

GLU 37 VAL 38 0.0521

VAL 38 VAL 39 0.0002

VAL 39 ILE 40 -0.0005

ILE 40 CYS 41 0.0121

CYS 41 PRO 42 -0.0000

PRO 42 PRO 43 -0.0000

PRO 43 ALA 44 -0.0125

ALA 44 THR 45 -0.0002

THR 45 TYR 46 -0.0001

TYR 46 LEU 47 0.0822

LEU 47 ASP 48 0.0002

ASP 48 TYR 49 -0.0001

TYR 49 SER 50 0.0234

SER 50 VAL 51 -0.0004

VAL 51 SER 52 0.0002

SER 52 LEU 53 -0.0595

LEU 53 VAL 54 -0.0001

VAL 54 LYS 55 -0.0001

LYS 55 LYS 56 0.0747

LYS 56 PRO 57 0.0003

PRO 57 GLN 58 -0.0002

GLN 58 VAL 59 -0.0075

VAL 59 THR 60 -0.0001

THR 60 VAL 61 0.0005

VAL 61 GLY 62 -0.0577

GLY 62 ALA 63 -0.0003

ALA 63 GLN 64 0.0002

GLN 64 ASN 65 -0.0220

ASN 65 ALA 66 0.0003

ALA 66 TYR 67 0.0002

TYR 67 LEU 68 -0.0531

LEU 68 LYS 69 -0.0002

LYS 69 ALA 70 -0.0003

ALA 70 SER 71 0.0210

SER 71 GLY 72 0.0002

GLY 72 ALA 73 0.0000

ALA 73 PHE 74 -0.0059

PHE 74 THR 75 -0.0001

THR 75 GLY 76 0.0002

GLY 76 GLU 77 -0.1097

GLU 77 ASN 78 -0.0000

ASN 78 SER 79 -0.0002

SER 79 VAL 80 -0.0742

VAL 80 ASP 81 -0.0000

ASP 81 GLN 82 -0.0002

GLN 82 ILE 83 -0.0021

ILE 83 LYS 84 0.0000

LYS 84 ASP 85 0.0002

ASP 85 VAL 86 -0.0227

VAL 86 GLY 87 -0.0001

GLY 87 ALA 88 -0.0003

ALA 88 LYS 89 0.1250

LYS 89 TRP 90 -0.0002

TRP 90 VAL 91 0.0000

VAL 91 ILE 92 -0.0067

ILE 92 LEU 93 0.0002

LEU 93 GLY 94 -0.0003

GLY 94 HIS 95 -0.0036

HIS 95 SER 96 0.0001

SER 96 GLU 97 0.0004

GLU 97 ARG 98 0.0100

ARG 98 ARG 99 0.0001

ARG 99 SER 100 -0.0003

SER 100 TYR 101 -0.1557

TYR 101 PHE 102 0.0002

PHE 102 HIS 103 -0.0003

HIS 103 GLU 104 -0.0779

GLU 104 ASP 105 -0.0002

ASP 105 ASP 106 -0.0000

ASP 106 LYS 107 -0.0022

LYS 107 PHE 108 -0.0001

PHE 108 ILE 109 0.0000

ILE 109 ALA 110 -0.0387

ALA 110 ASP 111 0.0001

ASP 111 LYS 112 0.0002

LYS 112 THR 113 -0.0338

THR 113 LYS 114 -0.0001

LYS 114 PHE 115 -0.0002

PHE 115 ALA 116 -0.0053

ALA 116 LEU 117 -0.0002

LEU 117 GLY 118 0.0000

GLY 118 GLN 119 0.0469

GLN 119 GLY 120 -0.0000

GLY 120 VAL 121 -0.0000

VAL 121 GLY 122 0.0277

GLY 122 VAL 123 0.0003

VAL 123 ILE 124 -0.0001

ILE 124 LEU 125 0.0445

LEU 125 CYS 126 0.0003

CYS 126 ILE 127 -0.0000

ILE 127 GLY 128 0.0358

GLY 128 GLU 129 0.0002

GLU 129 THR 130 0.0000

THR 130 LEU 131 0.0012

LEU 131 GLU 132 0.0001

GLU 132 GLU 133 -0.0001

GLU 133 LYS 134 0.0154

LYS 134 LYS 135 -0.0001

LYS 135 ALA 136 -0.0003

ALA 136 GLY 137 0.0402

GLY 137 LYS 138 -0.0001

LYS 138 THR 139 0.0000

THR 139 LEU 140 0.0131

LEU 140 ASP 141 0.0000

ASP 141 VAL 142 -0.0002

VAL 142 VAL 143 -0.0007

VAL 143 GLU 144 -0.0001

GLU 144 ARG 145 -0.0002

ARG 145 GLN 146 -0.0031

GLN 146 LEU 147 -0.0000

LEU 147 ASN 148 -0.0001

ASN 148 ALA 149 -0.0015

ALA 149 VAL 150 -0.0001

VAL 150 LEU 151 0.0002

LEU 151 GLU 152 -0.0107

GLU 152 GLU 153 0.0002

GLU 153 VAL 154 -0.0001

VAL 154 LYS 155 -0.0141

LYS 155 ASP 156 0.0002

ASP 156 TRP 157 -0.0000

TRP 157 THR 158 0.0218

THR 158 ASN 159 0.0003

ASN 159 VAL 160 -0.0002

VAL 160 VAL 161 -0.0091

VAL 161 VAL 162 -0.0000

VAL 162 ALA 163 -0.0002

ALA 163 TYR 164 0.0440

TYR 164 GLU 165 -0.0004

GLU 165 PRO 166 -0.0001

PRO 166 VAL 167 -0.0081

VAL 167 TRP 168 -0.0001

TRP 168 ALA 169 -0.0002

ALA 169 ILE 170 -0.0539

ILE 170 GLY 171 -0.0002

GLY 171 THR 172 -0.0000

THR 172 GLY 173 0.0084

GLY 173 LEU 174 -0.0002

LEU 174 ALA 175 0.0000

ALA 175 ALA 176 -0.0238

ALA 176 THR 177 -0.0001

THR 177 PRO 178 -0.0001

PRO 178 GLU 179 -0.0013

GLU 179 ASP 180 -0.0000

ASP 180 ALA 181 0.0001

ALA 181 GLN 182 -0.0161

GLN 182 ASP 183 -0.0003

ASP 183 ILE 184 -0.0001

ILE 184 HIS 185 0.0164

HIS 185 ALA 186 0.0001

ALA 186 SER 187 -0.0000

SER 187 ILE 188 -0.0112

ILE 188 ARG 189 0.0000

ARG 189 LYS 190 -0.0001

LYS 190 PHE 191 -0.0072

PHE 191 LEU 192 0.0002

LEU 192 ALA 193 -0.0000

ALA 193 SER 194 -0.0031

SER 194 LYS 195 0.0004

LYS 195 LEU 196 -0.0001

LEU 196 GLY 197 -0.0130

GLY 197 ASP 198 -0.0002

ASP 198 LYS 199 -0.0001

LYS 199 ALA 200 0.0079

ALA 200 ALA 201 0.0000

ALA 201 SER 202 -0.0003

SER 202 GLU 203 0.0235

GLU 203 LEU 204 0.0003

LEU 204 ARG 205 -0.0001

ARG 205 ILE 206 0.0060

ILE 206 LEU 207 0.0000

LEU 207 TYR 208 0.0002

TYR 208 GLY 209 -0.0246

GLY 209 GLY 210 -0.0001

GLY 210 SER 211 0.0003

SER 211 ALA 212 -0.0046

ALA 212 ASN 213 0.0000

ASN 213 GLY 214 -0.0001

GLY 214 SER 215 -0.0076

SER 215 ASN 216 0.0000

ASN 216 ALA 217 0.0002

ALA 217 VAL 218 -0.0054

VAL 218 THR 219 0.0003

THR 219 PHE 220 -0.0003

PHE 220 LYS 221 0.0012

LYS 221 ASP 222 -0.0003

ASP 222 LYS 223 0.0000

LYS 223 ALA 224 -0.0173

ALA 224 ASP 225 0.0000

ASP 225 VAL 226 0.0003

VAL 226 ASP 227 0.0281

ASP 227 GLY 228 -0.0003

GLY 228 PHE 229 -0.0001

PHE 229 LEU 230 -0.0216

LEU 230 VAL 231 -0.0003

VAL 231 GLY 232 0.0001

GLY 232 GLY 233 0.0105

GLY 233 ALA 234 -0.0005

ALA 234 SER 235 -0.0001

SER 235 LEU 236 -0.0118

LEU 236 LYS 237 -0.0003

LYS 237 PRO 238 -0.0001

PRO 238 GLU 239 -0.0188

GLU 239 PHE 240 0.0001

PHE 240 VAL 241 -0.0005

VAL 241 ASP 242 -0.0025

ASP 242 ILE 243 0.0002

ILE 243 ILE 244 -0.0002

ILE 244 ASN 245 -0.0101

ASN 245 SER 246 0.0001

SER 246 ARG 247 -0.0003

ARG 247 ASN 248 -0.0360

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: April 25th, 2023.

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

*** 7tim E:) ***

CA strain for 2405231911392957911

--- normal mode 8 ---

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

* 7tim E:) *