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

* Mak_Prdx1_Model *

CA strain for 23011808392224348

--- normal mode 7 ---

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 0.0000

GLY 4 ASN 5 -0.0131

ASN 5 ALA 6 0.0002

ALA 6 LYS 7 0.4131

LYS 7 ILE 8 -0.0001

ILE 8 GLY 9 -0.0072

GLY 9 HIS 10 0.0003

HIS 10 PRO 11 0.0611

PRO 11 ALA 12 0.0002

ALA 12 PRO 13 0.0272

PRO 13 SER 14 0.0001

SER 14 PHE 15 0.1499

PHE 15 LYS 16 0.0001

LYS 16 ALA 17 0.0537

ALA 17 THR 18 -0.0005

THR 18 ALA 19 0.0005

ALA 19 VAL 20 -0.0002

VAL 20 MET 21 -0.0038

MET 21 PRO 22 -0.0000

PRO 22 ASP 23 -0.0082

ASP 23 GLY 24 -0.0001

GLY 24 GLN 25 0.0047

GLN 25 PHE 26 0.0000

PHE 26 LYS 27 0.0064

LYS 27 ASP 28 -0.0000

ASP 28 ILE 29 0.0078

ILE 29 SER 30 -0.0001

SER 30 LEU 31 0.0589

LEU 31 SER 32 0.0001

SER 32 ASP 33 -0.0192

ASP 33 TYR 34 -0.0001

TYR 34 LYS 35 0.0013

LYS 35 GLY 36 -0.0000

GLY 36 LYS 37 0.0223

LYS 37 TYR 38 -0.0001

TYR 38 VAL 39 -0.0007

VAL 39 VAL 40 -0.0000

VAL 40 PHE 41 -0.0111

PHE 41 PHE 42 0.0001

PHE 42 PHE 43 -0.0207

PHE 43 TYR 44 -0.0002

TYR 44 PRO 45 0.0397

PRO 45 LEU 46 -0.0004

LEU 46 ASP 47 0.1219

ASP 47 PHE 48 -0.0001

PHE 48 THR 49 -0.1140

THR 49 PHE 50 0.0004

PHE 50 VAL 51 -0.1007

VAL 51 CYS 52 -0.0002

CYS 52 PRO 53 0.0987

PRO 53 THR 54 0.0000

THR 54 GLU 55 -0.0463

GLU 55 ILE 56 0.0001

ILE 56 ILE 57 0.0195

ILE 57 ALA 58 0.0003

ALA 58 PHE 59 -0.0172

PHE 59 SER 60 0.0001

SER 60 ASP 61 -0.0312

ASP 61 ARG 62 -0.0001

ARG 62 ALA 63 -0.0043

ALA 63 GLU 64 0.0001

GLU 64 GLU 65 -0.0395

GLU 65 PHE 66 0.0002

PHE 66 LYS 67 0.0203

LYS 67 LYS 68 0.0004

LYS 68 LEU 69 -0.0571

LEU 69 ASN 70 0.0000

ASN 70 CYS 71 -0.0028

CYS 71 GLN 72 -0.0003

GLN 72 VAL 73 0.0169

VAL 73 ILE 74 0.0003

ILE 74 GLY 75 -0.0101

GLY 75 ALA 76 -0.0003

ALA 76 SER 77 -0.0053

SER 77 VAL 78 0.0001

VAL 78 ASP 79 0.0849

ASP 79 SER 80 0.0000

SER 80 HIS 81 0.0073

HIS 81 PHE 82 0.0001

PHE 82 SER 83 -0.0265

SER 83 HIS 84 -0.0000

HIS 84 LEU 85 0.0334

LEU 85 ALA 86 0.0002

ALA 86 TRP 87 -0.0423

TRP 87 ILE 88 0.0000

ILE 88 ASN 89 -0.0025

ASN 89 THR 90 0.0001

THR 90 PRO 91 0.0365

PRO 91 LYS 92 -0.0000

LYS 92 LYS 93 -0.0624

LYS 93 GLN 94 -0.0001

GLN 94 GLY 95 0.0030

GLY 95 GLY 96 -0.0002

GLY 96 LEU 97 -0.0202

LEU 97 GLY 98 0.0002

GLY 98 PRO 99 -0.0038

PRO 99 MET 100 0.0001

MET 100 ASN 101 -0.0430

ASN 101 ILE 102 0.0003

ILE 102 PRO 103 -0.0146

PRO 103 LEU 104 -0.0003

LEU 104 VAL 105 -0.0060

VAL 105 SER 106 -0.0000

SER 106 ASP 107 0.0147

ASP 107 PRO 108 -0.0001

PRO 108 LYS 109 0.0205

LYS 109 ARG 110 0.0003

ARG 110 THR 111 0.0098

THR 111 ILE 112 0.0004

ILE 112 ALA 113 -0.0691

ALA 113 GLN 114 0.0002

GLN 114 ASP 115 -0.0235

ASP 115 TYR 116 -0.0001

TYR 116 GLY 117 -0.1348

GLY 117 VAL 118 -0.0003

VAL 118 LEU 119 0.0275

LEU 119 LYS 120 -0.0003

LYS 120 ALA 121 -0.0286

ALA 121 ASP 122 -0.0000

ASP 122 GLU 123 0.0708

GLU 123 GLY 124 -0.0001

GLY 124 ILE 125 -0.0186

ILE 125 SER 126 0.0003

SER 126 PHE 127 -0.0445

PHE 127 ARG 128 0.0000

ARG 128 GLY 129 -0.0326

GLY 129 LEU 130 -0.0001

LEU 130 PHE 131 -0.0047

PHE 131 ILE 132 0.0001

ILE 132 ILE 133 0.0118

ILE 133 ASP 134 0.0002

ASP 134 ASP 135 -0.0034

ASP 135 LYS 136 -0.0002

LYS 136 GLY 137 0.0098

GLY 137 ILE 138 0.0002

ILE 138 LEU 139 -0.0260

LEU 139 ARG 140 0.0001

ARG 140 GLN 141 -0.0391

GLN 141 ILE 142 -0.0003

ILE 142 THR 143 -0.0673

THR 143 ILE 144 0.0004

ILE 144 ASN 145 -0.0485

ASN 145 ASP 146 -0.0001

ASP 146 LEU 147 -0.1013

LEU 147 PRO 148 -0.0003

PRO 148 VAL 149 -0.1102

VAL 149 GLY 150 0.0001

GLY 150 ARG 151 0.1003

ARG 151 SER 152 -0.0001

SER 152 VAL 153 0.1190

VAL 153 ASP 154 -0.0002

ASP 154 GLU 155 -0.1189

GLU 155 ILE 156 -0.0003

ILE 156 LEU 157 0.0526

LEU 157 ARG 158 0.0004

ARG 158 LEU 159 -0.0023

LEU 159 VAL 160 0.0001

VAL 160 GLN 161 -0.0423

GLN 161 ALA 162 -0.0001

ALA 162 PHE 163 -0.0100

PHE 163 GLN 164 0.0002

GLN 164 PHE 165 -0.1686

PHE 165 THR 166 0.0000

THR 166 ASP 167 0.0397

ASP 167 LYS 168 0.0000

LYS 168 HIS 169 0.0206

HIS 169 GLY 170 -0.0002

GLY 170 GLU 171 0.0407

GLU 171 VAL 172 -0.0002

VAL 172 CYS 173 0.0473

CYS 173 PRO 174 -0.0000

PRO 174 ALA 175 -0.0416

ALA 175 SER 3 -0.0174

SER 3 GLY 4 0.0002

GLY 4 ASN 5 -0.0219

ASN 5 ALA 6 0.0001

ALA 6 LYS 7 0.3940

LYS 7 ILE 8 -0.0003

ILE 8 GLY 9 -0.0002

GLY 9 HIS 10 -0.0002

HIS 10 PRO 11 0.0591

PRO 11 ALA 12 0.0002

ALA 12 PRO 13 0.0311

PRO 13 SER 14 -0.0001

SER 14 PHE 15 0.1525

PHE 15 LYS 16 -0.0002

LYS 16 ALA 17 0.0534

ALA 17 THR 18 0.0001

THR 18 ALA 19 0.0002

ALA 19 VAL 20 0.0000

VAL 20 MET 21 -0.0036

MET 21 PRO 22 0.0001

PRO 22 ASP 23 -0.0095

ASP 23 GLY 24 -0.0000

GLY 24 GLN 25 0.0050

GLN 25 PHE 26 -0.0004

PHE 26 LYS 27 0.0083

LYS 27 ASP 28 -0.0000

ASP 28 ILE 29 0.0088

ILE 29 SER 30 -0.0001

SER 30 LEU 31 0.0621

LEU 31 SER 32 -0.0001

SER 32 ASP 33 -0.0205

ASP 33 TYR 34 -0.0001

TYR 34 LYS 35 0.0013

LYS 35 GLY 36 -0.0001

GLY 36 LYS 37 0.0225

LYS 37 TYR 38 0.0001

TYR 38 VAL 39 -0.0008

VAL 39 VAL 40 0.0001

VAL 40 PHE 41 -0.0103

PHE 41 PHE 42 -0.0002

PHE 42 PHE 43 -0.0210

PHE 43 TYR 44 0.0003

TYR 44 PRO 45 0.0385

PRO 45 LEU 46 -0.0001

LEU 46 ASP 47 0.1180

ASP 47 PHE 48 -0.0000

PHE 48 THR 49 -0.1131

THR 49 PHE 50 -0.0001

PHE 50 VAL 51 -0.1059

VAL 51 CYS 52 0.0001

CYS 52 PRO 53 0.0901

PRO 53 THR 54 0.0001

THR 54 GLU 55 -0.0490

GLU 55 ILE 56 0.0002

ILE 56 ILE 57 0.0200

ILE 57 ALA 58 0.0002

ALA 58 PHE 59 -0.0204

PHE 59 SER 60 -0.0003

SER 60 ASP 61 -0.0269

ASP 61 ARG 62 -0.0001

ARG 62 ALA 63 -0.0004

ALA 63 GLU 64 0.0000

GLU 64 GLU 65 -0.0357

GLU 65 PHE 66 0.0003

PHE 66 LYS 67 0.0209

LYS 67 LYS 68 0.0001

LYS 68 LEU 69 -0.0579

LEU 69 ASN 70 -0.0002

ASN 70 CYS 71 -0.0019

CYS 71 GLN 72 0.0002

GLN 72 VAL 73 0.0141

VAL 73 ILE 74 -0.0001

ILE 74 GLY 75 -0.0089

GLY 75 ALA 76 -0.0002

ALA 76 SER 77 -0.0058

SER 77 VAL 78 0.0000

VAL 78 ASP 79 0.0844

ASP 79 SER 80 -0.0001

SER 80 HIS 81 0.0068

HIS 81 PHE 82 -0.0000

PHE 82 SER 83 -0.0281

SER 83 HIS 84 -0.0001

HIS 84 LEU 85 0.0353

LEU 85 ALA 86 -0.0002

ALA 86 TRP 87 -0.0418

TRP 87 ILE 88 -0.0002

ILE 88 ASN 89 -0.0009

ASN 89 THR 90 0.0001

THR 90 PRO 91 0.0326

PRO 91 LYS 92 -0.0004

LYS 92 LYS 93 -0.0644

LYS 93 GLN 94 0.0001

GLN 94 GLY 95 0.0095

GLY 95 GLY 96 0.0001

GLY 96 LEU 97 -0.0235

LEU 97 GLY 98 -0.0001

GLY 98 PRO 99 -0.0045

PRO 99 MET 100 -0.0000

MET 100 ASN 101 -0.0416

ASN 101 ILE 102 -0.0002

ILE 102 PRO 103 -0.0133

PRO 103 LEU 104 0.0001

LEU 104 VAL 105 -0.0061

VAL 105 SER 106 0.0001

SER 106 ASP 107 0.0151

ASP 107 PRO 108 -0.0002

PRO 108 LYS 109 0.0221

LYS 109 ARG 110 -0.0001

ARG 110 THR 111 0.0113

THR 111 ILE 112 0.0002

ILE 112 ALA 113 -0.0687

ALA 113 GLN 114 0.0002

GLN 114 ASP 115 -0.0188

ASP 115 TYR 116 0.0000

TYR 116 GLY 117 -0.1311

GLY 117 VAL 118 0.0001

VAL 118 LEU 119 0.0257

LEU 119 LYS 120 0.0004

LYS 120 ALA 121 -0.0274

ALA 121 ASP 122 -0.0002

ASP 122 GLU 123 0.0723

GLU 123 GLY 124 -0.0002

GLY 124 ILE 125 -0.0207

ILE 125 SER 126 -0.0000

SER 126 PHE 127 -0.0428

PHE 127 ARG 128 0.0000

ARG 128 GLY 129 -0.0365

GLY 129 LEU 130 0.0000

LEU 130 PHE 131 -0.0048

PHE 131 ILE 132 0.0002

ILE 132 ILE 133 0.0113

ILE 133 ASP 134 -0.0001

ASP 134 ASP 135 -0.0023

ASP 135 LYS 136 0.0002

LYS 136 GLY 137 0.0124

GLY 137 ILE 138 -0.0002

ILE 138 LEU 139 -0.0249

LEU 139 ARG 140 -0.0002

ARG 140 GLN 141 -0.0382

GLN 141 ILE 142 0.0000

ILE 142 THR 143 -0.0645

THR 143 ILE 144 -0.0001

ILE 144 ASN 145 -0.0437

ASN 145 ASP 146 -0.0002

ASP 146 LEU 147 -0.0853

LEU 147 PRO 148 0.0003

PRO 148 VAL 149 -0.1035

VAL 149 GLY 150 -0.0000

GLY 150 ARG 151 0.0943

ARG 151 SER 152 0.0000

SER 152 VAL 153 0.1234

VAL 153 ASP 154 -0.0001

ASP 154 GLU 155 -0.1161

GLU 155 ILE 156 0.0002

ILE 156 LEU 157 0.0524

LEU 157 ARG 158 0.0002

ARG 158 LEU 159 -0.0073

LEU 159 VAL 160 0.0000

VAL 160 GLN 161 -0.0427

GLN 161 ALA 162 -0.0002

ALA 162 PHE 163 -0.0113

PHE 163 GLN 164 0.0002

GLN 164 PHE 165 -0.1635

PHE 165 THR 166 -0.0000

THR 166 ASP 167 0.0317

ASP 167 LYS 168 -0.0002

LYS 168 HIS 169 0.0217

HIS 169 GLY 170 -0.0001

GLY 170 GLU 171 0.0446

GLU 171 VAL 172 -0.0001

VAL 172 CYS 173 0.0420

CYS 173 PRO 174 -0.0003

PRO 174 ALA 175 -0.0417

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 7 ---

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

* Mak_Prdx1_Model *