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

* bacteriorhodopsin *

CA strain for 2404222055381936730

--- 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
ILE 4 THR 5 0.0002

THR 5 GLY 6 0.0007

GLY 6 ARG 7 -0.0002

ARG 7 PRO 8 -0.0040

PRO 8 GLU 9 -0.0004

GLU 9 TRP 10 -0.0058

TRP 10 ILE 11 0.0001

ILE 11 TRP 12 -0.0059

TRP 12 LEU 13 -0.0002

LEU 13 ALA 14 0.0019

ALA 14 LEU 15 -0.0001

LEU 15 GLY 16 -0.0040

GLY 16 THR 17 -0.0001

THR 17 ALA 18 -0.0009

ALA 18 LEU 19 0.0002

LEU 19 MET 20 0.0110

MET 20 GLY 21 0.0000

GLY 21 LEU 22 -0.0148

LEU 22 GLY 23 0.0003

GLY 23 THR 24 0.0041

THR 24 LEU 25 -0.0000

LEU 25 TYR 26 -0.0446

TYR 26 PHE 27 -0.0000

PHE 27 LEU 28 0.0146

LEU 28 VAL 29 -0.0004

VAL 29 LYS 30 -0.0229

LYS 30 GLY 31 -0.0001

GLY 31 MET 32 0.0197

MET 32 GLY 33 -0.0002

GLY 33 VAL 34 -0.0067

VAL 34 SER 35 0.0001

SER 35 ASP 36 -0.0082

ASP 36 PRO 37 0.0001

PRO 37 ASP 38 0.0580

ASP 38 ALA 39 0.0003

ALA 39 LYS 40 0.0008

LYS 40 LYS 41 -0.0002

LYS 41 PHE 42 0.0173

PHE 42 TYR 43 -0.0001

TYR 43 ALA 44 -0.0148

ALA 44 ILE 45 0.0000

ILE 45 THR 46 0.0150

THR 46 THR 47 0.0002

THR 47 LEU 48 -0.0318

LEU 48 VAL 49 -0.0003

VAL 49 PRO 50 0.0115

PRO 50 ALA 51 0.0001

ALA 51 ILE 52 -0.0208

ILE 52 ALA 53 -0.0002

ALA 53 PHE 54 0.0212

PHE 54 THR 55 0.0002

THR 55 MET 56 -0.0184

MET 56 TYR 57 -0.0003

TYR 57 LEU 58 0.0180

LEU 58 SER 59 -0.0002

SER 59 MET 60 -0.0081

MET 60 LEU 61 0.0000

LEU 61 LEU 62 0.0086

LEU 62 GLY 63 -0.0003

GLY 63 TYR 64 0.0188

TYR 64 GLY 65 0.0002

GLY 65 LEU 66 -0.0396

LEU 66 THR 67 -0.0002

THR 67 MET 68 -0.0544

MET 68 VAL 69 0.0002

VAL 69 PRO 70 -0.0330

PRO 70 PHE 71 0.0002

PHE 71 GLY 72 -0.0170

GLY 72 GLY 73 -0.0001

GLY 73 GLU 74 0.0056

GLU 74 GLN 75 0.0002

GLN 75 ASN 76 0.0388

ASN 76 PRO 77 0.0000

PRO 77 ILE 78 -0.0049

ILE 78 TYR 79 -0.0002

TYR 79 TRP 80 0.0057

TRP 80 ALA 81 -0.0001

ALA 81 ARG 82 0.0131

ARG 82 TYR 83 0.0002

TYR 83 ALA 84 -0.0290

ALA 84 ASP 85 -0.0001

ASP 85 TRP 86 0.0210

TRP 86 LEU 87 -0.0002

LEU 87 PHE 88 -0.0530

PHE 88 THR 89 -0.0000

THR 89 THR 90 0.0191

THR 90 PRO 91 -0.0002

PRO 91 LEU 92 -0.0262

LEU 92 LEU 93 -0.0004

LEU 93 LEU 94 0.0187

LEU 94 LEU 95 0.0003

LEU 95 ASP 96 -0.0082

ASP 96 LEU 97 0.0001

LEU 97 ALA 98 0.0082

ALA 98 LEU 99 0.0002

LEU 99 LEU 100 -0.0152

LEU 100 VAL 101 -0.0000

VAL 101 ASP 102 -0.0086

ASP 102 ALA 103 0.0000

ALA 103 ASP 104 -0.0061

ASP 104 GLN 105 -0.0001

GLN 105 GLY 106 -0.0092

GLY 106 THR 107 0.0000

THR 107 ILE 108 0.0130

ILE 108 LEU 109 0.0006

LEU 109 ALA 110 -0.0251

ALA 110 LEU 111 0.0001

LEU 111 VAL 112 0.0161

VAL 112 GLY 113 0.0002

GLY 113 ALA 114 -0.0195

ALA 114 ASP 115 -0.0003

ASP 115 GLY 116 0.0134

GLY 116 ILE 117 -0.0001

ILE 117 MET 118 0.0082

MET 118 ILE 119 0.0000

ILE 119 GLY 120 -0.0051

GLY 120 THR 121 -0.0002

THR 121 GLY 122 -0.0100

GLY 122 LEU 123 -0.0002

LEU 123 VAL 124 -0.0163

VAL 124 GLY 125 0.0000

GLY 125 ALA 126 0.0132

ALA 126 LEU 127 0.0001

LEU 127 THR 128 -0.0231

THR 128 LYS 129 0.0002

LYS 129 VAL 130 -0.0016

VAL 130 TYR 131 0.0002

TYR 131 SER 132 -0.0032

SER 132 TYR 133 -0.0001

TYR 133 ARG 134 0.0047

ARG 134 PHE 135 -0.0003

PHE 135 VAL 136 -0.0199

VAL 136 TRP 137 0.0004

TRP 137 TRP 138 0.0076

TRP 138 ALA 139 0.0001

ALA 139 ILE 140 -0.0404

ILE 140 SER 141 -0.0000

SER 141 THR 142 0.0140

THR 142 ALA 143 0.0000

ALA 143 ALA 144 -0.0210

ALA 144 MET 145 -0.0002

MET 145 LEU 146 -0.0134

LEU 146 TYR 147 0.0002

TYR 147 ILE 148 0.0086

ILE 148 LEU 149 -0.0001

LEU 149 TYR 150 -0.0297

TYR 150 VAL 151 -0.0003

VAL 151 LEU 152 -0.0081

LEU 152 PHE 153 0.0002

PHE 153 PHE 154 -0.0220

PHE 154 GLY 155 0.0002

GLY 155 PHE 156 -0.0018

PHE 156 THR 157 -0.0001

THR 157 SER 158 -0.0180

SER 158 LYS 159 -0.0002

LYS 159 ALA 160 -0.0073

ALA 160 GLU 161 0.0002

GLU 161 SER 162 0.0055

SER 162 MET 163 -0.0000

MET 163 ARG 164 0.0790

ARG 164 PRO 165 0.0005

PRO 165 GLU 166 -0.0423

GLU 166 VAL 167 -0.0002

VAL 167 ALA 168 0.0052

ALA 168 SER 169 -0.0002

SER 169 THR 170 -0.0321

THR 170 PHE 171 0.0002

PHE 171 LYS 172 -0.0051

LYS 172 VAL 173 0.0002

VAL 173 LEU 174 -0.0097

LEU 174 ARG 175 0.0001

ARG 175 ASN 176 -0.0061

ASN 176 VAL 177 0.0000

VAL 177 THR 178 0.0105

THR 178 VAL 179 -0.0001

VAL 179 VAL 180 -0.0332

VAL 180 LEU 181 0.0002

LEU 181 TRP 182 -0.0055

TRP 182 SER 183 0.0000

SER 183 ALA 184 -0.0177

ALA 184 TYR 185 0.0001

TYR 185 PRO 186 0.0105

PRO 186 VAL 187 0.0003

VAL 187 VAL 188 -0.0268

VAL 188 TRP 189 0.0001

TRP 189 LEU 190 -0.0063

LEU 190 ILE 191 0.0002

ILE 191 GLY 192 -0.0058

GLY 192 SER 193 0.0001

SER 193 GLU 194 -0.0103

GLU 194 GLY 195 -0.0003

GLY 195 ALA 196 -0.0250

ALA 196 GLY 197 -0.0002

GLY 197 ILE 198 0.0044

ILE 198 VAL 199 -0.0001

VAL 199 PRO 200 -0.0283

PRO 200 LEU 201 -0.0001

LEU 201 ASN 202 0.0105

ASN 202 ILE 203 -0.0002

ILE 203 GLU 204 -0.0082

GLU 204 THR 205 -0.0002

THR 205 LEU 206 0.0090

LEU 206 LEU 207 -0.0001

LEU 207 PHE 208 -0.0081

PHE 208 MET 209 0.0001

MET 209 VAL 210 -0.0127

VAL 210 LEU 211 -0.0003

LEU 211 ASP 212 0.0072

ASP 212 VAL 213 0.0004

VAL 213 SER 214 -0.0376

SER 214 ALA 215 0.0001

ALA 215 LYS 216 0.0033

LYS 216 VAL 217 -0.0001

VAL 217 GLY 218 -0.0526

GLY 218 PHE 219 -0.0001

PHE 219 GLY 220 0.0244

GLY 220 LEU 221 -0.0002

LEU 221 ILE 222 -0.0456

ILE 222 LEU 223 -0.0001

LEU 223 LEU 224 0.0085

LEU 224 ARG 225 -0.0001

ARG 225 SER 226 -0.0740

SER 226 ARG 227 0.0004

ARG 227 ALA 228 -0.0062

ALA 228 ILE 229 0.0001

ILE 229 PHE 230 -0.1199

PHE 230 GLY 231 -0.0002

GLY 231 GLU 232 -0.1221

GLU 232 ALA 233 0.0001

ALA 233 GLU 234 -0.0295

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 8 ---

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

* bacteriorhodopsin *