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

* bacteriorhodopsin *

CA strain for 2404222055381936730

--- 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
ILE 4 THR 5 -0.0001

THR 5 GLY 6 0.0006

GLY 6 ARG 7 0.0002

ARG 7 PRO 8 -0.0010

PRO 8 GLU 9 0.0000

GLU 9 TRP 10 -0.0032

TRP 10 ILE 11 -0.0000

ILE 11 TRP 12 -0.0000

TRP 12 LEU 13 0.0001

LEU 13 ALA 14 -0.0021

ALA 14 LEU 15 0.0002

LEU 15 GLY 16 0.0014

GLY 16 THR 17 -0.0002

THR 17 ALA 18 -0.0037

ALA 18 LEU 19 0.0004

LEU 19 MET 20 0.0047

MET 20 GLY 21 0.0002

GLY 21 LEU 22 -0.0075

LEU 22 GLY 23 0.0000

GLY 23 THR 24 0.0043

THR 24 LEU 25 0.0002

LEU 25 TYR 26 -0.0158

TYR 26 PHE 27 0.0005

PHE 27 LEU 28 0.0150

LEU 28 VAL 29 -0.0001

VAL 29 LYS 30 -0.0089

LYS 30 GLY 31 -0.0000

GLY 31 MET 32 0.0271

MET 32 GLY 33 0.0004

GLY 33 VAL 34 -0.0114

VAL 34 SER 35 -0.0002

SER 35 ASP 36 -0.0188

ASP 36 PRO 37 -0.0001

PRO 37 ASP 38 0.0038

ASP 38 ALA 39 -0.0003

ALA 39 LYS 40 -0.0050

LYS 40 LYS 41 0.0002

LYS 41 PHE 42 0.0020

PHE 42 TYR 43 -0.0001

TYR 43 ALA 44 -0.0155

ALA 44 ILE 45 -0.0001

ILE 45 THR 46 0.0116

THR 46 THR 47 0.0000

THR 47 LEU 48 -0.0147

LEU 48 VAL 49 -0.0001

VAL 49 PRO 50 0.0042

PRO 50 ALA 51 -0.0003

ALA 51 ILE 52 -0.0099

ILE 52 ALA 53 0.0002

ALA 53 PHE 54 0.0130

PHE 54 THR 55 -0.0004

THR 55 MET 56 -0.0096

MET 56 TYR 57 0.0002

TYR 57 LEU 58 0.0139

LEU 58 SER 59 0.0005

SER 59 MET 60 -0.0053

MET 60 LEU 61 -0.0002

LEU 61 LEU 62 0.0080

LEU 62 GLY 63 -0.0003

GLY 63 TYR 64 0.0145

TYR 64 GLY 65 0.0002

GLY 65 LEU 66 -0.0260

LEU 66 THR 67 -0.0003

THR 67 MET 68 -0.0364

MET 68 VAL 69 -0.0003

VAL 69 PRO 70 -0.0209

PRO 70 PHE 71 -0.0000

PHE 71 GLY 72 -0.0104

GLY 72 GLY 73 0.0002

GLY 73 GLU 74 0.0021

GLU 74 GLN 75 0.0000

GLN 75 ASN 76 0.0244

ASN 76 PRO 77 -0.0001

PRO 77 ILE 78 -0.0033

ILE 78 TYR 79 -0.0005

TYR 79 TRP 80 0.0045

TRP 80 ALA 81 -0.0002

ALA 81 ARG 82 0.0077

ARG 82 TYR 83 -0.0000

TYR 83 ALA 84 -0.0125

ALA 84 ASP 85 -0.0006

ASP 85 TRP 86 0.0095

TRP 86 LEU 87 0.0004

LEU 87 PHE 88 -0.0186

PHE 88 THR 89 -0.0004

THR 89 THR 90 0.0070

THR 90 PRO 91 -0.0001

PRO 91 LEU 92 -0.0015

LEU 92 LEU 93 -0.0001

LEU 93 LEU 94 0.0038

LEU 94 LEU 95 -0.0000

LEU 95 ASP 96 0.0048

ASP 96 LEU 97 0.0000

LEU 97 ALA 98 0.0072

ALA 98 LEU 99 0.0002

LEU 99 LEU 100 -0.0111

LEU 100 VAL 101 0.0001

VAL 101 ASP 102 0.0085

ASP 102 ALA 103 0.0001

ALA 103 ASP 104 0.0035

ASP 104 GLN 105 -0.0003

GLN 105 GLY 106 -0.0052

GLY 106 THR 107 0.0001

THR 107 ILE 108 0.0074

ILE 108 LEU 109 -0.0000

LEU 109 ALA 110 -0.0059

ALA 110 LEU 111 -0.0001

LEU 111 VAL 112 0.0032

VAL 112 GLY 113 0.0001

GLY 113 ALA 114 -0.0076

ALA 114 ASP 115 0.0002

ASP 115 GLY 116 0.0051

GLY 116 ILE 117 0.0002

ILE 117 MET 118 0.0008

MET 118 ILE 119 -0.0001

ILE 119 GLY 120 -0.0014

GLY 120 THR 121 0.0001

THR 121 GLY 122 -0.0066

GLY 122 LEU 123 -0.0004

LEU 123 VAL 124 -0.0083

VAL 124 GLY 125 0.0001

GLY 125 ALA 126 0.0063

ALA 126 LEU 127 -0.0002

LEU 127 THR 128 -0.0143

THR 128 LYS 129 -0.0002

LYS 129 VAL 130 -0.0008

VAL 130 TYR 131 0.0001

TYR 131 SER 132 -0.0007

SER 132 TYR 133 -0.0000

TYR 133 ARG 134 0.0004

ARG 134 PHE 135 -0.0001

PHE 135 VAL 136 -0.0127

VAL 136 TRP 137 0.0003

TRP 137 TRP 138 -0.0004

TRP 138 ALA 139 0.0002

ALA 139 ILE 140 -0.0230

ILE 140 SER 141 -0.0002

SER 141 THR 142 0.0053

THR 142 ALA 143 0.0003

ALA 143 ALA 144 -0.0053

ALA 144 MET 145 0.0001

MET 145 LEU 146 -0.0105

LEU 146 TYR 147 0.0002

TYR 147 ILE 148 0.0023

ILE 148 LEU 149 -0.0003

LEU 149 TYR 150 -0.0125

TYR 150 VAL 151 0.0004

VAL 151 LEU 152 -0.0084

LEU 152 PHE 153 0.0000

PHE 153 PHE 154 -0.0106

PHE 154 GLY 155 -0.0001

GLY 155 PHE 156 -0.0013

PHE 156 THR 157 0.0002

THR 157 SER 158 -0.0094

SER 158 LYS 159 0.0003

LYS 159 ALA 160 -0.0068

ALA 160 GLU 161 -0.0000

GLU 161 SER 162 0.0047

SER 162 MET 163 0.0003

MET 163 ARG 164 0.0658

ARG 164 PRO 165 -0.0004

PRO 165 GLU 166 0.0081

GLU 166 VAL 167 -0.0002

VAL 167 ALA 168 0.0016

ALA 168 SER 169 -0.0004

SER 169 THR 170 -0.0066

THR 170 PHE 171 -0.0001

PHE 171 LYS 172 -0.0143

LYS 172 VAL 173 -0.0001

VAL 173 LEU 174 -0.0039

LEU 174 ARG 175 0.0000

ARG 175 ASN 176 -0.0033

ASN 176 VAL 177 0.0001

VAL 177 THR 178 -0.0009

THR 178 VAL 179 -0.0003

VAL 179 VAL 180 -0.0116

VAL 180 LEU 181 0.0001

LEU 181 TRP 182 -0.0105

TRP 182 SER 183 0.0002

SER 183 ALA 184 0.0097

ALA 184 TYR 185 0.0003

TYR 185 PRO 186 -0.0020

PRO 186 VAL 187 0.0002

VAL 187 VAL 188 -0.0108

VAL 188 TRP 189 -0.0001

TRP 189 LEU 190 -0.0080

LEU 190 ILE 191 -0.0000

ILE 191 GLY 192 0.0006

GLY 192 SER 193 -0.0002

SER 193 GLU 194 -0.0082

GLU 194 GLY 195 -0.0005

GLY 195 ALA 196 -0.0146

ALA 196 GLY 197 0.0002

GLY 197 ILE 198 0.0007

ILE 198 VAL 199 -0.0003

VAL 199 PRO 200 -0.0108

PRO 200 LEU 201 -0.0003

LEU 201 ASN 202 0.0023

ASN 202 ILE 203 -0.0002

ILE 203 GLU 204 -0.0018

GLU 204 THR 205 0.0003

THR 205 LEU 206 0.0038

LEU 206 LEU 207 0.0003

LEU 207 PHE 208 -0.0053

PHE 208 MET 209 -0.0001

MET 209 VAL 210 -0.0021

VAL 210 LEU 211 -0.0000

LEU 211 ASP 212 0.0043

ASP 212 VAL 213 0.0000

VAL 213 SER 214 -0.0096

SER 214 ALA 215 -0.0002

ALA 215 LYS 216 0.0036

LYS 216 VAL 217 0.0000

VAL 217 GLY 218 -0.0152

GLY 218 PHE 219 -0.0002

PHE 219 GLY 220 0.0063

GLY 220 LEU 221 -0.0001

LEU 221 ILE 222 -0.0089

ILE 222 LEU 223 -0.0001

LEU 223 LEU 224 0.0015

LEU 224 ARG 225 -0.0005

ARG 225 SER 226 -0.0251

SER 226 ARG 227 -0.0001

ARG 227 ALA 228 0.0096

ALA 228 ILE 229 0.0001

ILE 229 PHE 230 -0.0314

PHE 230 GLY 231 -0.0002

GLY 231 GLU 232 0.1416

GLU 232 ALA 233 -0.0001

ALA 233 GLU 234 0.0169

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 9 ---

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

* bacteriorhodopsin *