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

* 2QLE *

CA strain for 240228055824920786

--- normal mode 13 ---

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
GLY 1 GLU 2 -0.0000

GLU 2 GLU 3 0.0616

GLU 3 LEU 4 0.0002

LEU 4 PHE 5 -0.1138

PHE 5 THR 6 0.0001

THR 6 GLY 7 0.1173

GLY 7 VAL 8 -0.0003

VAL 8 VAL 9 -0.1027

VAL 9 PRO 10 -0.0001

PRO 10 ILE 11 0.0263

ILE 11 LEU 12 0.0001

LEU 12 VAL 13 0.0541

VAL 13 GLU 14 0.0001

GLU 14 LEU 15 0.0138

LEU 15 ASP 16 0.0001

ASP 16 GLY 17 -0.0222

GLY 17 ASP 18 -0.0000

ASP 18 VAL 19 -0.0384

VAL 19 ASN 20 -0.0001

ASN 20 GLY 21 -0.1112

GLY 21 HIS 22 -0.0004

HIS 22 LYS 23 -0.1680

LYS 23 PHE 24 -0.0003

PHE 24 SER 25 -0.2601

SER 25 SER 25 -0.0054

SER 25 VAL 26 -0.0002

VAL 26 SER 27 -0.0667

SER 27 SER 27 -0.0011

SER 27 GLY 28 0.0002

GLY 28 GLU 29 0.0205

GLU 29 GLY 30 -0.0000

GLY 30 GLU 31 -0.0137

GLU 31 GLY 32 0.0002

GLY 32 ASP 33 -0.0394

ASP 33 ALA 34 0.0003

ALA 34 THR 35 -0.0799

THR 35 TYR 36 0.0003

TYR 36 GLY 37 0.0566

GLY 37 LYS 38 0.0003

LYS 38 LEU 39 0.0334

LEU 39 THR 40 0.0003

THR 40 THR 40 0.0937

THR 40 LEU 41 0.0384

LEU 41 LYS 42 -0.0000

LYS 42 PHE 43 -0.1174

PHE 43 ILE 44 -0.0001

ILE 44 CYS 45 -0.1140

CYS 45 THR 46 0.0001

THR 46 THR 47 -0.1747

THR 47 GLY 48 0.0001

GLY 48 LYS 49 -0.1062

LYS 49 LEU 50 0.0001

LEU 50 PRO 51 -0.5566

PRO 51 VAL 52 0.0000

VAL 52 PRO 53 0.1354

PRO 53 TRP 54 0.0002

TRP 54 PRO 55 -0.0379

PRO 55 THR 56 0.0005

THR 56 LEU 57 0.0876

LEU 57 VAL 58 0.0002

VAL 58 THR 59 -0.1911

THR 59 THR 60 -0.0001

THR 60 PHE 61 0.0827

PHE 61 VAL 62 0.0001

VAL 62 GLN 63 -0.3338

GLN 63 CYS 64 -0.0002

CYS 64 PHE 65 0.0247

PHE 65 SER 66 0.0001

SER 66 ARG 67 0.0249

ARG 67 TYR 68 0.0000

TYR 68 PRO 69 0.1132

PRO 69 ASP 70 0.0002

ASP 70 HIS 71 0.0725

HIS 71 MET 72 -0.0002

MET 72 LYS 73 0.1464

LYS 73 ARG 74 -0.0002

ARG 74 HIS 75 -0.0518

HIS 75 ASP 76 -0.0003

ASP 76 PHE 77 -0.0991

PHE 77 PHE 78 0.0001

PHE 78 LYS 79 0.1454

LYS 79 SER 80 0.0001

SER 80 ALA 81 -0.0652

ALA 81 MET 82 0.0001

MET 82 PRO 83 -0.0701

PRO 83 GLU 84 0.0003

GLU 84 GLY 85 0.1395

GLY 85 TYR 86 0.0004

TYR 86 VAL 87 0.1598

VAL 87 GLN 88 -0.0002

GLN 88 GLU 89 0.3746

GLU 89 ARG 90 0.0000

ARG 90 THR 91 0.3997

THR 91 ILE 92 0.0002

ILE 92 PHE 93 0.0941

PHE 93 PHE 94 0.0004

PHE 94 LYS 95 0.0104

LYS 95 ASP 96 0.0000

ASP 96 ASP 97 -0.2482

ASP 97 GLY 98 0.0002

GLY 98 ASN 99 0.1009

ASN 99 TYR 100 0.0001

TYR 100 LYS 101 0.0831

LYS 101 THR 102 -0.0005

THR 102 ARG 103 0.3133

ARG 103 ALA 104 0.0002

ALA 104 GLU 105 0.2297

GLU 105 VAL 106 0.0004

VAL 106 LYS 107 0.1064

LYS 107 PHE 108 -0.0003

PHE 108 GLU 109 0.0593

GLU 109 GLY 110 0.0001

GLY 110 ASP 111 -0.1155

ASP 111 THR 112 0.0000

THR 112 LEU 113 0.0861

LEU 113 VAL 114 0.0000

VAL 114 ASN 115 0.1277

ASN 115 ARG 116 -0.0001

ARG 116 ILE 117 0.0769

ILE 117 GLU 118 0.0002

GLU 118 LEU 119 0.1191

LEU 119 LYS 120 0.0004

LYS 120 GLY 121 0.0303

GLY 121 ILE 122 0.0001

ILE 122 ASP 123 -0.0117

ASP 123 PHE 124 -0.0000

PHE 124 LYS 125 0.1369

LYS 125 GLU 126 0.0003

GLU 126 ASP 127 -0.0045

ASP 127 GLY 128 -0.0001

GLY 128 ASN 129 0.1522

ASN 129 ILE 130 0.0001

ILE 130 LEU 131 0.0970

LEU 131 GLY 132 0.0001

GLY 132 HIS 133 -0.1460

HIS 133 LYS 134 -0.0001

LYS 134 LEU 135 -0.0991

LEU 135 GLU 136 -0.0003

GLU 136 TYR 137 0.5799

TYR 137 ASN 138 0.0002

ASN 138 TYR 139 -0.2033

TYR 139 ASN 140 -0.0001

ASN 140 SER 141 -0.0544

SER 141 SER 141 0.0164

SER 141 HIS 142 0.0001

HIS 142 ASN 143 -0.4218

ASN 143 VAL 144 0.0002

VAL 144 TYR 145 -0.2202

TYR 145 ILE 146 0.0002

ILE 146 MET 147 0.0510

MET 147 ALA 148 0.0002

ALA 148 ASP 149 -0.0237

ASP 149 LYS 150 0.0001

LYS 150 GLN 151 0.0438

GLN 151 LYS 152 -0.0002

LYS 152 ASN 153 0.1221

ASN 153 GLY 154 0.0003

GLY 154 ILE 155 0.1315

ILE 155 LYS 156 0.0003

LYS 156 VAL 157 -0.0778

VAL 157 ASN 158 -0.0002

ASN 158 PHE 159 -0.2769

PHE 159 LYS 160 0.0000

LYS 160 ILE 161 -0.2779

ILE 161 ARG 162 -0.0001

ARG 162 HIS 163 -0.1730

HIS 163 ASN 164 -0.0002

ASN 164 ILE 165 0.1181

ILE 165 GLU 166 0.0001

GLU 166 ASP 167 0.1168

ASP 167 GLY 168 0.0001

GLY 168 SER 169 -0.2960

SER 169 VAL 170 -0.0000

VAL 170 GLN 171 -0.2355

GLN 171 LEU 172 0.0004

LEU 172 ALA 173 -0.3940

ALA 173 ASP 174 -0.0003

ASP 174 HIS 175 -0.0357

HIS 175 TYR 176 0.0003

TYR 176 GLN 177 0.2571

GLN 177 GLN 178 -0.0003

GLN 178 ASN 179 0.2465

ASN 179 THR 180 -0.0002

THR 180 THR 180 -0.0131

THR 180 PRO 181 0.1812

PRO 181 ILE 182 -0.0001

ILE 182 GLY 183 0.0540

GLY 183 ASP 184 -0.0001

ASP 184 GLY 185 -0.1956

GLY 185 PRO 186 -0.0000

PRO 186 VAL 187 -0.0227

VAL 187 LEU 188 0.0003

LEU 188 LEU 189 0.0175

LEU 189 PRO 190 0.0000

PRO 190 ASP 191 0.0118

ASP 191 ASN 192 0.0000

ASN 192 HIS 193 -0.0800

HIS 193 TYR 194 0.0003

TYR 194 LEU 195 -0.1765

LEU 195 SER 196 -0.0001

SER 196 SER 196 0.0181

SER 196 SER 196 -0.0117

SER 196 THR 197 -0.2432

THR 197 GLN 198 0.0004

GLN 198 VAL 199 -0.2519

VAL 199 ALA 200 0.0000

ALA 200 LEU 201 -0.0492

LEU 201 SER 202 -0.0003

SER 202 LYS 203 0.3509

LYS 203 ASP 204 0.0000

ASP 204 PRO 205 -0.1886

PRO 205 ASN 206 -0.0000

ASN 206 GLU 207 -0.2554

GLU 207 LYS 208 0.0001

LYS 208 ARG 209 -0.5096

ARG 209 ASP 210 -0.0001

ASP 210 HIS 211 -0.0001

HIS 211 MET 212 -0.0002

MET 212 VAL 213 0.0117

VAL 213 LEU 214 -0.0002

LEU 214 LEU 214 0.0131

LEU 214 LEU 215 0.0278

LEU 215 GLU 216 0.0003

GLU 216 PHE 217 0.0358

PHE 217 VAL 218 -0.0003

VAL 218 VAL 218 -0.0110

VAL 218 THR 219 -0.0711

THR 219 THR 219 -0.0174

THR 219 ALA 220 -0.0001

ALA 220 ALA 221 -0.1241

ALA 221 GLY 222 -0.0005

GLY 222 ILE 223 -0.0680

ILE 223 THR 224 -0.0002

THR 224 HIS 225 -0.0144

HIS 225 GLY 226 -0.0001

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.

*** 2QLE ***

CA strain for 240228055824920786

--- normal mode 13 ---

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

* 2QLE *