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

* bacteriorhodopsin *

CA strain for 2404222055381936730

--- normal mode 11 ---

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
ILE 4 THR 5 0.0001

THR 5 GLY 6 0.0045

GLY 6 ARG 7 0.0001

ARG 7 PRO 8 -0.0118

PRO 8 GLU 9 -0.0003

GLU 9 TRP 10 0.0129

TRP 10 ILE 11 -0.0002

ILE 11 TRP 12 -0.0363

TRP 12 LEU 13 0.0001

LEU 13 ALA 14 0.0027

ALA 14 LEU 15 -0.0000

LEU 15 GLY 16 -0.0138

GLY 16 THR 17 0.0002

THR 17 ALA 18 -0.0367

ALA 18 LEU 19 -0.0003

LEU 19 MET 20 0.0515

MET 20 GLY 21 -0.0002

GLY 21 LEU 22 -0.1354

LEU 22 GLY 23 0.0004

GLY 23 THR 24 -0.0073

THR 24 LEU 25 0.0001

LEU 25 TYR 26 -0.0569

TYR 26 PHE 27 0.0001

PHE 27 LEU 28 0.0165

LEU 28 VAL 29 0.0002

VAL 29 LYS 30 0.0456

LYS 30 GLY 31 0.0000

GLY 31 MET 32 -0.0612

MET 32 GLY 33 -0.0001

GLY 33 VAL 34 -0.0193

VAL 34 SER 35 -0.0001

SER 35 ASP 36 -0.0171

ASP 36 PRO 37 0.0000

PRO 37 ASP 38 -0.0038

ASP 38 ALA 39 -0.0001

ALA 39 LYS 40 0.0322

LYS 40 LYS 41 -0.0000

LYS 41 PHE 42 0.0273

PHE 42 TYR 43 0.0001

TYR 43 ALA 44 -0.0016

ALA 44 ILE 45 0.0004

ILE 45 THR 46 0.0048

THR 46 THR 47 -0.0003

THR 47 LEU 48 -0.0501

LEU 48 VAL 49 0.0000

VAL 49 PRO 50 0.0493

PRO 50 ALA 51 -0.0001

ALA 51 ILE 52 -0.1234

ILE 52 ALA 53 0.0004

ALA 53 PHE 54 0.0080

PHE 54 THR 55 -0.0002

THR 55 MET 56 -0.0713

MET 56 TYR 57 -0.0003

TYR 57 LEU 58 -0.0219

LEU 58 SER 59 -0.0000

SER 59 MET 60 0.0082

MET 60 LEU 61 0.0004

LEU 61 LEU 62 -0.0425

LEU 62 GLY 63 -0.0001

GLY 63 TYR 64 0.0084

TYR 64 GLY 65 0.0001

GLY 65 LEU 66 0.0057

LEU 66 THR 67 -0.0003

THR 67 MET 68 0.0243

MET 68 VAL 69 0.0003

VAL 69 PRO 70 0.0359

PRO 70 PHE 71 -0.0003

PHE 71 GLY 72 0.0250

GLY 72 GLY 73 0.0002

GLY 73 GLU 74 -0.0350

GLU 74 GLN 75 -0.0003

GLN 75 ASN 76 -0.0922

ASN 76 PRO 77 0.0001

PRO 77 ILE 78 0.0381

ILE 78 TYR 79 -0.0003

TYR 79 TRP 80 0.0426

TRP 80 ALA 81 0.0001

ALA 81 ARG 82 0.0144

ARG 82 TYR 83 -0.0003

TYR 83 ALA 84 -0.0231

ALA 84 ASP 85 0.0002

ASP 85 TRP 86 0.0338

TRP 86 LEU 87 0.0002

LEU 87 PHE 88 -0.0448

PHE 88 THR 89 -0.0002

THR 89 THR 90 0.0010

THR 90 PRO 91 -0.0006

PRO 91 LEU 92 -0.0639

LEU 92 LEU 93 -0.0000

LEU 93 LEU 94 -0.0143

LEU 94 LEU 95 -0.0004

LEU 95 ASP 96 -0.0146

ASP 96 LEU 97 0.0001

LEU 97 ALA 98 -0.0790

ALA 98 LEU 99 -0.0001

LEU 99 LEU 100 0.0574

LEU 100 VAL 101 0.0002

VAL 101 ASP 102 -0.0601

ASP 102 ALA 103 -0.0002

ALA 103 ASP 104 -0.0430

ASP 104 GLN 105 -0.0004

GLN 105 GLY 106 -0.0111

GLY 106 THR 107 -0.0003

THR 107 ILE 108 -0.0180

ILE 108 LEU 109 -0.0002

LEU 109 ALA 110 -0.0606

ALA 110 LEU 111 -0.0002

LEU 111 VAL 112 0.0215

VAL 112 GLY 113 0.0000

GLY 113 ALA 114 -0.0657

ALA 114 ASP 115 0.0001

ASP 115 GLY 116 -0.0004

GLY 116 ILE 117 0.0001

ILE 117 MET 118 -0.0369

MET 118 ILE 119 0.0001

ILE 119 GLY 120 -0.0220

GLY 120 THR 121 -0.0000

THR 121 GLY 122 0.0316

GLY 122 LEU 123 -0.0001

LEU 123 VAL 124 -0.0666

VAL 124 GLY 125 -0.0001

GLY 125 ALA 126 -0.0083

ALA 126 LEU 127 0.0002

LEU 127 THR 128 -0.0608

THR 128 LYS 129 -0.0000

LYS 129 VAL 130 -0.0316

VAL 130 TYR 131 -0.0001

TYR 131 SER 132 -0.0005

SER 132 TYR 133 0.0000

TYR 133 ARG 134 -0.0084

ARG 134 PHE 135 0.0002

PHE 135 VAL 136 0.0135

VAL 136 TRP 137 -0.0002

TRP 137 TRP 138 0.0049

TRP 138 ALA 139 0.0001

ALA 139 ILE 140 -0.0060

ILE 140 SER 141 0.0000

SER 141 THR 142 0.0021

THR 142 ALA 143 0.0001

ALA 143 ALA 144 -0.0722

ALA 144 MET 145 0.0001

MET 145 LEU 146 0.0243

LEU 146 TYR 147 0.0002

TYR 147 ILE 148 -0.0056

ILE 148 LEU 149 0.0003

LEU 149 TYR 150 -0.0547

TYR 150 VAL 151 -0.0001

VAL 151 LEU 152 0.0103

LEU 152 PHE 153 0.0001

PHE 153 PHE 154 -0.0577

PHE 154 GLY 155 -0.0001

GLY 155 PHE 156 -0.0131

PHE 156 THR 157 0.0001

THR 157 SER 158 -0.0461

SER 158 LYS 159 -0.0000

LYS 159 ALA 160 0.0118

ALA 160 GLU 161 0.0002

GLU 161 SER 162 -0.0267

SER 162 MET 163 0.0003

MET 163 ARG 164 0.0904

ARG 164 PRO 165 -0.0001

PRO 165 GLU 166 -0.0054

GLU 166 VAL 167 0.0000

VAL 167 ALA 168 0.0118

ALA 168 SER 169 -0.0002

SER 169 THR 170 -0.0192

THR 170 PHE 171 -0.0002

PHE 171 LYS 172 0.0479

LYS 172 VAL 173 0.0001

VAL 173 LEU 174 0.0157

LEU 174 ARG 175 0.0003

ARG 175 ASN 176 -0.0106

ASN 176 VAL 177 0.0003

VAL 177 THR 178 0.0462

THR 178 VAL 179 0.0000

VAL 179 VAL 180 -0.0338

VAL 180 LEU 181 0.0001

LEU 181 TRP 182 0.0715

TRP 182 SER 183 -0.0001

SER 183 ALA 184 -0.1552

ALA 184 TYR 185 0.0002

TYR 185 PRO 186 0.0136

PRO 186 VAL 187 -0.0002

VAL 187 VAL 188 0.0134

VAL 188 TRP 189 -0.0000

TRP 189 LEU 190 0.0334

LEU 190 ILE 191 0.0002

ILE 191 GLY 192 -0.0315

GLY 192 SER 193 0.0003

SER 193 GLU 194 0.0614

GLU 194 GLY 195 -0.0004

GLY 195 ALA 196 0.0336

ALA 196 GLY 197 0.0002

GLY 197 ILE 198 0.0116

ILE 198 VAL 199 0.0001

VAL 199 PRO 200 -0.0117

PRO 200 LEU 201 0.0002

LEU 201 ASN 202 0.0192

ASN 202 ILE 203 0.0002

ILE 203 GLU 204 -0.0001

GLU 204 THR 205 0.0001

THR 205 LEU 206 -0.0066

LEU 206 LEU 207 -0.0003

LEU 207 PHE 208 0.0410

PHE 208 MET 209 -0.0004

MET 209 VAL 210 -0.0458

VAL 210 LEU 211 0.0001

LEU 211 ASP 212 0.0161

ASP 212 VAL 213 0.0000

VAL 213 SER 214 -0.0885

SER 214 ALA 215 -0.0003

ALA 215 LYS 216 0.0341

LYS 216 VAL 217 -0.0001

VAL 217 GLY 218 -0.0298

GLY 218 PHE 219 0.0001

PHE 219 GLY 220 0.0355

GLY 220 LEU 221 -0.0002

LEU 221 ILE 222 0.0114

ILE 222 LEU 223 0.0003

LEU 223 LEU 224 0.0613

LEU 224 ARG 225 0.0003

ARG 225 SER 226 -0.0663

SER 226 ARG 227 0.0001

ARG 227 ALA 228 0.0347

ALA 228 ILE 229 0.0000

ILE 229 PHE 230 -0.0423

PHE 230 GLY 231 0.0003

GLY 231 GLU 232 0.1059

GLU 232 ALA 233 -0.0002

ALA 233 GLU 234 -0.0947

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.

*** bacteriorhodopsin ***

CA strain for 2404222055381936730

--- normal mode 11 ---

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

* bacteriorhodopsin *