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

* Mak_Prdx1_Model *

CA strain for 23011808392224348

--- 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
SER 3 GLY 4 -0.0001

GLY 4 ASN 5 0.0140

ASN 5 ALA 6 0.0001

ALA 6 LYS 7 -0.1192

LYS 7 ILE 8 -0.0002

ILE 8 GLY 9 -0.0089

GLY 9 HIS 10 0.0001

HIS 10 PRO 11 -0.0400

PRO 11 ALA 12 0.0001

ALA 12 PRO 13 -0.0922

PRO 13 SER 14 -0.0004

SER 14 PHE 15 -0.2046

PHE 15 LYS 16 -0.0002

LYS 16 ALA 17 -0.0223

ALA 17 THR 18 0.0001

THR 18 ALA 19 -0.0094

ALA 19 VAL 20 0.0001

VAL 20 MET 21 0.0158

MET 21 PRO 22 -0.0002

PRO 22 ASP 23 0.0292

ASP 23 GLY 24 0.0000

GLY 24 GLN 25 -0.0386

GLN 25 PHE 26 0.0001

PHE 26 LYS 27 -0.0995

LYS 27 ASP 28 -0.0002

ASP 28 ILE 29 -0.0262

ILE 29 SER 30 -0.0001

SER 30 LEU 31 -0.1278

LEU 31 SER 32 0.0002

SER 32 ASP 33 0.0232

ASP 33 TYR 34 0.0002

TYR 34 LYS 35 -0.0739

LYS 35 GLY 36 -0.0001

GLY 36 LYS 37 -0.0171

LYS 37 TYR 38 0.0003

TYR 38 VAL 39 -0.0780

VAL 39 VAL 40 -0.0004

VAL 40 PHE 41 0.0316

PHE 41 PHE 42 -0.0001

PHE 42 PHE 43 0.0049

PHE 43 TYR 44 0.0002

TYR 44 PRO 45 0.0399

PRO 45 LEU 46 -0.0002

LEU 46 ASP 47 0.0596

ASP 47 PHE 48 -0.0001

PHE 48 THR 49 0.2161

THR 49 PHE 50 0.0001

PHE 50 VAL 51 0.2257

VAL 51 CYS 52 -0.0000

CYS 52 PRO 53 -0.1092

PRO 53 THR 54 0.0002

THR 54 GLU 55 -0.0380

GLU 55 ILE 56 -0.0005

ILE 56 ILE 57 0.0594

ILE 57 ALA 58 0.0002

ALA 58 PHE 59 -0.0357

PHE 59 SER 60 0.0000

SER 60 ASP 61 0.0871

ASP 61 ARG 62 0.0004

ARG 62 ALA 63 0.0170

ALA 63 GLU 64 -0.0001

GLU 64 GLU 65 0.0049

GLU 65 PHE 66 0.0002

PHE 66 LYS 67 0.0017

LYS 67 LYS 68 0.0001

LYS 68 LEU 69 0.0076

LEU 69 ASN 70 -0.0001

ASN 70 CYS 71 0.0008

CYS 71 GLN 72 -0.0000

GLN 72 VAL 73 -0.0284

VAL 73 ILE 74 -0.0003

ILE 74 GLY 75 0.0052

GLY 75 ALA 76 0.0001

ALA 76 SER 77 0.0351

SER 77 VAL 78 0.0001

VAL 78 ASP 79 -0.0598

ASP 79 SER 80 -0.0002

SER 80 HIS 81 0.0090

HIS 81 PHE 82 0.0002

PHE 82 SER 83 0.0722

SER 83 HIS 84 -0.0002

HIS 84 LEU 85 -0.0188

LEU 85 ALA 86 0.0001

ALA 86 TRP 87 0.0791

TRP 87 ILE 88 0.0001

ILE 88 ASN 89 -0.0176

ASN 89 THR 90 0.0003

THR 90 PRO 91 -0.0053

PRO 91 LYS 92 0.0004

LYS 92 LYS 93 0.0050

LYS 93 GLN 94 0.0002

GLN 94 GLY 95 0.1801

GLY 95 GLY 96 -0.0002

GLY 96 LEU 97 -0.1350

LEU 97 GLY 98 -0.0003

GLY 98 PRO 99 -0.1515

PRO 99 MET 100 0.0000

MET 100 ASN 101 -0.1253

ASN 101 ILE 102 -0.0001

ILE 102 PRO 103 0.0707

PRO 103 LEU 104 -0.0004

LEU 104 VAL 105 -0.0236

VAL 105 SER 106 -0.0002

SER 106 ASP 107 -0.0789

ASP 107 PRO 108 0.0000

PRO 108 LYS 109 -0.0253

LYS 109 ARG 110 -0.0001

ARG 110 THR 111 0.0250

THR 111 ILE 112 -0.0000

ILE 112 ALA 113 0.0083

ALA 113 GLN 114 0.0001

GLN 114 ASP 115 0.0118

ASP 115 TYR 116 -0.0001

TYR 116 GLY 117 0.0024

GLY 117 VAL 118 -0.0000

VAL 118 LEU 119 -0.0206

LEU 119 LYS 120 0.0003

LYS 120 ALA 121 0.0331

ALA 121 ASP 122 -0.0002

ASP 122 GLU 123 -0.0210

GLU 123 GLY 124 0.0003

GLY 124 ILE 125 0.0091

ILE 125 SER 126 -0.0001

SER 126 PHE 127 -0.0446

PHE 127 ARG 128 0.0000

ARG 128 GLY 129 0.0032

GLY 129 LEU 130 0.0003

LEU 130 PHE 131 -0.0211

PHE 131 ILE 132 -0.0003

ILE 132 ILE 133 0.0013

ILE 133 ASP 134 0.0001

ASP 134 ASP 135 -0.0113

ASP 135 LYS 136 0.0000

LYS 136 GLY 137 -0.0986

GLY 137 ILE 138 0.0000

ILE 138 LEU 139 0.0880

LEU 139 ARG 140 -0.0000

ARG 140 GLN 141 0.0091

GLN 141 ILE 142 -0.0001

ILE 142 THR 143 -0.0071

THR 143 ILE 144 -0.0003

ILE 144 ASN 145 0.0235

ASN 145 ASP 146 -0.0004

ASP 146 LEU 147 0.0759

LEU 147 PRO 148 0.0001

PRO 148 VAL 149 0.0109

VAL 149 GLY 150 -0.0002

GLY 150 ARG 151 -0.0299

ARG 151 SER 152 0.0001

SER 152 VAL 153 -0.0154

VAL 153 ASP 154 -0.0003

ASP 154 GLU 155 0.0442

GLU 155 ILE 156 -0.0002

ILE 156 LEU 157 -0.0087

LEU 157 ARG 158 0.0001

ARG 158 LEU 159 0.0108

LEU 159 VAL 160 -0.0002

VAL 160 GLN 161 0.0650

GLN 161 ALA 162 -0.0001

ALA 162 PHE 163 0.0431

PHE 163 GLN 164 -0.0001

GLN 164 PHE 165 -0.0013

PHE 165 THR 166 0.0001

THR 166 ASP 167 -0.1071

ASP 167 LYS 168 -0.0000

LYS 168 HIS 169 -0.0519

HIS 169 GLY 170 -0.0001

GLY 170 GLU 171 -0.2547

GLU 171 VAL 172 0.0001

VAL 172 CYS 173 0.0788

CYS 173 PRO 174 0.0000

PRO 174 ALA 175 -0.0693

ALA 175 SER 3 0.0467

SER 3 GLY 4 0.0000

GLY 4 ASN 5 -0.0132

ASN 5 ALA 6 0.0002

ALA 6 LYS 7 0.1326

LYS 7 ILE 8 -0.0000

ILE 8 GLY 9 0.0089

GLY 9 HIS 10 0.0003

HIS 10 PRO 11 0.0388

PRO 11 ALA 12 0.0001

ALA 12 PRO 13 0.0892

PRO 13 SER 14 0.0002

SER 14 PHE 15 0.2047

PHE 15 LYS 16 -0.0000

LYS 16 ALA 17 0.0154

ALA 17 THR 18 0.0005

THR 18 ALA 19 0.0067

ALA 19 VAL 20 -0.0003

VAL 20 MET 21 -0.0171

MET 21 PRO 22 -0.0005

PRO 22 ASP 23 -0.0287

ASP 23 GLY 24 -0.0002

GLY 24 GLN 25 0.0374

GLN 25 PHE 26 0.0003

PHE 26 LYS 27 0.0861

LYS 27 ASP 28 0.0001

ASP 28 ILE 29 0.0213

ILE 29 SER 30 -0.0001

SER 30 LEU 31 0.1295

LEU 31 SER 32 0.0002

SER 32 ASP 33 -0.0218

ASP 33 TYR 34 0.0002

TYR 34 LYS 35 0.0652

LYS 35 GLY 36 -0.0002

GLY 36 LYS 37 0.0182

LYS 37 TYR 38 -0.0001

TYR 38 VAL 39 0.0782

VAL 39 VAL 40 0.0002

VAL 40 PHE 41 -0.0337

PHE 41 PHE 42 0.0001

PHE 42 PHE 43 -0.0069

PHE 43 TYR 44 -0.0003

TYR 44 PRO 45 -0.0426

PRO 45 LEU 46 -0.0000

LEU 46 ASP 47 -0.0420

ASP 47 PHE 48 0.0000

PHE 48 THR 49 -0.2392

THR 49 PHE 50 -0.0002

PHE 50 VAL 51 -0.2222

VAL 51 CYS 52 -0.0001

CYS 52 PRO 53 0.1000

PRO 53 THR 54 -0.0003

THR 54 GLU 55 0.0806

GLU 55 ILE 56 -0.0000

ILE 56 ILE 57 -0.0607

ILE 57 ALA 58 0.0001

ALA 58 PHE 59 0.0392

PHE 59 SER 60 0.0001

SER 60 ASP 61 -0.0789

ASP 61 ARG 62 -0.0003

ARG 62 ALA 63 -0.0093

ALA 63 GLU 64 -0.0002

GLU 64 GLU 65 -0.0029

GLU 65 PHE 66 -0.0002

PHE 66 LYS 67 -0.0015

LYS 67 LYS 68 0.0001

LYS 68 LEU 69 -0.0061

LEU 69 ASN 70 -0.0002

ASN 70 CYS 71 -0.0045

CYS 71 GLN 72 0.0001

GLN 72 VAL 73 0.0261

VAL 73 ILE 74 0.0001

ILE 74 GLY 75 -0.0087

GLY 75 ALA 76 -0.0000

ALA 76 SER 77 -0.0381

SER 77 VAL 78 0.0004

VAL 78 ASP 79 0.0685

ASP 79 SER 80 0.0005

SER 80 HIS 81 -0.0032

HIS 81 PHE 82 -0.0002

PHE 82 SER 83 -0.0796

SER 83 HIS 84 -0.0001

HIS 84 LEU 85 0.0244

LEU 85 ALA 86 -0.0001

ALA 86 TRP 87 -0.0805

TRP 87 ILE 88 0.0002

ILE 88 ASN 89 0.0223

ASN 89 THR 90 -0.0000

THR 90 PRO 91 0.0000

PRO 91 LYS 92 -0.0002

LYS 92 LYS 93 -0.0142

LYS 93 GLN 94 0.0002

GLN 94 GLY 95 -0.1629

GLY 95 GLY 96 -0.0001

GLY 96 LEU 97 0.1364

LEU 97 GLY 98 0.0002

GLY 98 PRO 99 0.1427

PRO 99 MET 100 -0.0001

MET 100 ASN 101 0.1245

ASN 101 ILE 102 -0.0004

ILE 102 PRO 103 -0.0636

PRO 103 LEU 104 0.0003

LEU 104 VAL 105 0.0237

VAL 105 SER 106 -0.0002

SER 106 ASP 107 0.0834

ASP 107 PRO 108 0.0001

PRO 108 LYS 109 0.0264

LYS 109 ARG 110 -0.0002

ARG 110 THR 111 -0.0239

THR 111 ILE 112 0.0001

ILE 112 ALA 113 -0.0132

ALA 113 GLN 114 -0.0002

GLN 114 ASP 115 -0.0112

ASP 115 TYR 116 0.0002

TYR 116 GLY 117 -0.0109

GLY 117 VAL 118 -0.0003

VAL 118 LEU 119 0.0252

LEU 119 LYS 120 0.0002

LYS 120 ALA 121 -0.0384

ALA 121 ASP 122 -0.0004

ASP 122 GLU 123 0.0261

GLU 123 GLY 124 0.0003

GLY 124 ILE 125 -0.0126

ILE 125 SER 126 -0.0000

SER 126 PHE 127 0.0476

PHE 127 ARG 128 0.0003

ARG 128 GLY 129 -0.0167

GLY 129 LEU 130 -0.0003

LEU 130 PHE 131 0.0178

PHE 131 ILE 132 0.0002

ILE 132 ILE 133 -0.0041

ILE 133 ASP 134 -0.0002

ASP 134 ASP 135 0.0179

ASP 135 LYS 136 0.0001

LYS 136 GLY 137 0.0911

GLY 137 ILE 138 -0.0002

ILE 138 LEU 139 -0.0888

LEU 139 ARG 140 -0.0001

ARG 140 GLN 141 -0.0154

GLN 141 ILE 142 -0.0003

ILE 142 THR 143 -0.0009

THR 143 ILE 144 -0.0001

ILE 144 ASN 145 -0.0397

ASN 145 ASP 146 -0.0002

ASP 146 LEU 147 -0.1187

LEU 147 PRO 148 -0.0004

PRO 148 VAL 149 -0.0109

VAL 149 GLY 150 0.0002

GLY 150 ARG 151 0.0123

ARG 151 SER 152 -0.0003

SER 152 VAL 153 0.0149

VAL 153 ASP 154 -0.0000

ASP 154 GLU 155 -0.0414

GLU 155 ILE 156 -0.0002

ILE 156 LEU 157 0.0021

LEU 157 ARG 158 0.0001

ARG 158 LEU 159 -0.0119

LEU 159 VAL 160 0.0002

VAL 160 GLN 161 -0.0641

GLN 161 ALA 162 0.0000

ALA 162 PHE 163 -0.0387

PHE 163 GLN 164 0.0001

GLN 164 PHE 165 0.0332

PHE 165 THR 166 -0.0001

THR 166 ASP 167 0.0633

ASP 167 LYS 168 0.0002

LYS 168 HIS 169 0.0449

HIS 169 GLY 170 0.0002

GLY 170 GLU 171 0.2893

GLU 171 VAL 172 0.0000

VAL 172 CYS 173 -0.1263

CYS 173 PRO 174 0.0001

PRO 174 ALA 175 0.0738

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: October 18th, 2018.

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

*** Mak_Prdx1_Model ***

CA strain for 23011808392224348

--- normal mode 11 ---

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

* Mak_Prdx1_Model *