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

* Mak_Prdx1_Model *

CA strain for 23011808392224348

--- 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
SER 3 GLY 4 -0.0003

GLY 4 ASN 5 0.0259

ASN 5 ALA 6 0.0002

ALA 6 LYS 7 -0.2085

LYS 7 ILE 8 0.0003

ILE 8 GLY 9 0.0310

GLY 9 HIS 10 0.0003

HIS 10 PRO 11 -0.1765

PRO 11 ALA 12 0.0002

ALA 12 PRO 13 0.0310

PRO 13 SER 14 0.0000

SER 14 PHE 15 -0.1731

PHE 15 LYS 16 -0.0000

LYS 16 ALA 17 -0.0384

ALA 17 THR 18 -0.0003

THR 18 ALA 19 -0.0001

ALA 19 VAL 20 -0.0002

VAL 20 MET 21 -0.0101

MET 21 PRO 22 0.0000

PRO 22 ASP 23 0.0099

ASP 23 GLY 24 -0.0002

GLY 24 GLN 25 -0.0157

GLN 25 PHE 26 -0.0001

PHE 26 LYS 27 -0.1176

LYS 27 ASP 28 0.0004

ASP 28 ILE 29 -0.0783

ILE 29 SER 30 -0.0001

SER 30 LEU 31 -0.1227

LEU 31 SER 32 -0.0000

SER 32 ASP 33 0.0320

ASP 33 TYR 34 0.0002

TYR 34 LYS 35 -0.0860

LYS 35 GLY 36 -0.0000

GLY 36 LYS 37 0.0237

LYS 37 TYR 38 -0.0002

TYR 38 VAL 39 -0.0176

VAL 39 VAL 40 -0.0001

VAL 40 PHE 41 0.0149

PHE 41 PHE 42 0.0000

PHE 42 PHE 43 -0.0065

PHE 43 TYR 44 0.0004

TYR 44 PRO 45 -0.0316

PRO 45 LEU 46 -0.0000

LEU 46 ASP 47 0.0877

ASP 47 PHE 48 -0.0002

PHE 48 THR 49 -0.0206

THR 49 PHE 50 -0.0001

PHE 50 VAL 51 0.0523

VAL 51 CYS 52 -0.0001

CYS 52 PRO 53 0.1953

PRO 53 THR 54 0.0000

THR 54 GLU 55 0.0485

GLU 55 ILE 56 -0.0002

ILE 56 ILE 57 0.0121

ILE 57 ALA 58 -0.0002

ALA 58 PHE 59 0.0054

PHE 59 SER 60 -0.0005

SER 60 ASP 61 0.0198

ASP 61 ARG 62 -0.0004

ARG 62 ALA 63 0.0069

ALA 63 GLU 64 -0.0000

GLU 64 GLU 65 -0.0479

GLU 65 PHE 66 0.0003

PHE 66 LYS 67 0.0330

LYS 67 LYS 68 -0.0001

LYS 68 LEU 69 -0.0906

LEU 69 ASN 70 0.0001

ASN 70 CYS 71 -0.0172

CYS 71 GLN 72 -0.0004

GLN 72 VAL 73 0.0275

VAL 73 ILE 74 0.0000

ILE 74 GLY 75 -0.0030

GLY 75 ALA 76 0.0001

ALA 76 SER 77 -0.0446

SER 77 VAL 78 0.0001

VAL 78 ASP 79 0.0637

ASP 79 SER 80 -0.0000

SER 80 HIS 81 0.0354

HIS 81 PHE 82 -0.0000

PHE 82 SER 83 0.0171

SER 83 HIS 84 0.0003

HIS 84 LEU 85 0.0181

LEU 85 ALA 86 -0.0001

ALA 86 TRP 87 0.0337

TRP 87 ILE 88 0.0004

ILE 88 ASN 89 -0.0229

ASN 89 THR 90 -0.0001

THR 90 PRO 91 -0.0004

PRO 91 LYS 92 -0.0003

LYS 92 LYS 93 -0.0167

LYS 93 GLN 94 0.0002

GLN 94 GLY 95 0.0933

GLY 95 GLY 96 0.0001

GLY 96 LEU 97 -0.0091

LEU 97 GLY 98 -0.0001

GLY 98 PRO 99 -0.0302

PRO 99 MET 100 0.0001

MET 100 ASN 101 -0.1387

ASN 101 ILE 102 -0.0000

ILE 102 PRO 103 0.0414

PRO 103 LEU 104 0.0002

LEU 104 VAL 105 0.0082

VAL 105 SER 106 -0.0001

SER 106 ASP 107 0.0150

ASP 107 PRO 108 -0.0000

PRO 108 LYS 109 -0.0026

LYS 109 ARG 110 0.0000

ARG 110 THR 111 -0.0031

THR 111 ILE 112 -0.0000

ILE 112 ALA 113 0.0323

ALA 113 GLN 114 -0.0001

GLN 114 ASP 115 0.0364

ASP 115 TYR 116 -0.0004

TYR 116 GLY 117 0.0289

GLY 117 VAL 118 0.0000

VAL 118 LEU 119 0.0096

LEU 119 LYS 120 0.0000

LYS 120 ALA 121 -0.0479

ALA 121 ASP 122 -0.0004

ASP 122 GLU 123 0.0710

GLU 123 GLY 124 0.0000

GLY 124 ILE 125 -0.0159

ILE 125 SER 126 0.0001

SER 126 PHE 127 0.0249

PHE 127 ARG 128 -0.0001

ARG 128 GLY 129 -0.0469

GLY 129 LEU 130 0.0003

LEU 130 PHE 131 0.0194

PHE 131 ILE 132 0.0003

ILE 132 ILE 133 0.0334

ILE 133 ASP 134 0.0000

ASP 134 ASP 135 -0.0124

ASP 135 LYS 136 0.0001

LYS 136 GLY 137 0.0519

GLY 137 ILE 138 0.0001

ILE 138 LEU 139 -0.0399

LEU 139 ARG 140 0.0001

ARG 140 GLN 141 0.0260

GLN 141 ILE 142 -0.0003

ILE 142 THR 143 0.0155

THR 143 ILE 144 -0.0005

ILE 144 ASN 145 -0.0532

ASN 145 ASP 146 -0.0003

ASP 146 LEU 147 -0.1305

LEU 147 PRO 148 0.0002

PRO 148 VAL 149 -0.0587

VAL 149 GLY 150 -0.0000

GLY 150 ARG 151 0.0096

ARG 151 SER 152 -0.0002

SER 152 VAL 153 0.0722

VAL 153 ASP 154 0.0002

ASP 154 GLU 155 0.0070

GLU 155 ILE 156 0.0000

ILE 156 LEU 157 0.0235

LEU 157 ARG 158 0.0001

ARG 158 LEU 159 0.0107

LEU 159 VAL 160 0.0002

VAL 160 GLN 161 -0.0251

GLN 161 ALA 162 -0.0000

ALA 162 PHE 163 -0.0284

PHE 163 GLN 164 0.0001

GLN 164 PHE 165 -0.1866

PHE 165 THR 166 0.0003

THR 166 ASP 167 -0.0868

ASP 167 LYS 168 -0.0002

LYS 168 HIS 169 -0.1026

HIS 169 GLY 170 -0.0000

GLY 170 GLU 171 -0.1116

GLU 171 VAL 172 -0.0003

VAL 172 CYS 173 0.0153

CYS 173 PRO 174 -0.0000

PRO 174 ALA 175 0.0015

ALA 175 SER 3 0.0283

SER 3 GLY 4 -0.0001

GLY 4 ASN 5 -0.0277

ASN 5 ALA 6 -0.0000

ALA 6 LYS 7 0.1950

LYS 7 ILE 8 0.0001

ILE 8 GLY 9 -0.0286

GLY 9 HIS 10 0.0001

HIS 10 PRO 11 0.1700

PRO 11 ALA 12 0.0003

ALA 12 PRO 13 -0.0219

PRO 13 SER 14 0.0000

SER 14 PHE 15 0.1712

PHE 15 LYS 16 -0.0001

LYS 16 ALA 17 0.0404

ALA 17 THR 18 -0.0003

THR 18 ALA 19 0.0010

ALA 19 VAL 20 0.0000

VAL 20 MET 21 0.0090

MET 21 PRO 22 -0.0003

PRO 22 ASP 23 -0.0062

ASP 23 GLY 24 0.0000

GLY 24 GLN 25 0.0179

GLN 25 PHE 26 -0.0003

PHE 26 LYS 27 0.1176

LYS 27 ASP 28 -0.0000

ASP 28 ILE 29 0.0793

ILE 29 SER 30 0.0001

SER 30 LEU 31 0.1304

LEU 31 SER 32 0.0000

SER 32 ASP 33 -0.0319

ASP 33 TYR 34 -0.0001

TYR 34 LYS 35 0.0908

LYS 35 GLY 36 0.0001

GLY 36 LYS 37 -0.0277

LYS 37 TYR 38 -0.0002

TYR 38 VAL 39 0.0187

VAL 39 VAL 40 0.0001

VAL 40 PHE 41 -0.0174

PHE 41 PHE 42 0.0003

PHE 42 PHE 43 0.0084

PHE 43 TYR 44 0.0002

TYR 44 PRO 45 0.0335

PRO 45 LEU 46 -0.0000

LEU 46 ASP 47 -0.0880

ASP 47 PHE 48 0.0003

PHE 48 THR 49 0.0251

THR 49 PHE 50 -0.0001

PHE 50 VAL 51 -0.0516

VAL 51 CYS 52 -0.0001

CYS 52 PRO 53 -0.1934

PRO 53 THR 54 -0.0003

THR 54 GLU 55 -0.0492

GLU 55 ILE 56 0.0003

ILE 56 ILE 57 -0.0081

ILE 57 ALA 58 0.0001

ALA 58 PHE 59 -0.0087

PHE 59 SER 60 -0.0002

SER 60 ASP 61 -0.0221

ASP 61 ARG 62 0.0002

ARG 62 ALA 63 -0.0066

ALA 63 GLU 64 -0.0000

GLU 64 GLU 65 0.0470

GLU 65 PHE 66 -0.0004

PHE 66 LYS 67 -0.0315

LYS 67 LYS 68 -0.0001

LYS 68 LEU 69 0.0909

LEU 69 ASN 70 0.0001

ASN 70 CYS 71 0.0162

CYS 71 GLN 72 -0.0002

GLN 72 VAL 73 -0.0241

VAL 73 ILE 74 0.0001

ILE 74 GLY 75 0.0001

GLY 75 ALA 76 -0.0000

ALA 76 SER 77 0.0474

SER 77 VAL 78 -0.0000

VAL 78 ASP 79 -0.0655

ASP 79 SER 80 0.0002

SER 80 HIS 81 -0.0395

HIS 81 PHE 82 -0.0000

PHE 82 SER 83 -0.0187

SER 83 HIS 84 0.0001

HIS 84 LEU 85 -0.0210

LEU 85 ALA 86 0.0002

ALA 86 TRP 87 -0.0349

TRP 87 ILE 88 -0.0001

ILE 88 ASN 89 0.0268

ASN 89 THR 90 0.0000

THR 90 PRO 91 0.0047

PRO 91 LYS 92 0.0001

LYS 92 LYS 93 0.0067

LYS 93 GLN 94 0.0002

GLN 94 GLY 95 -0.1042

GLY 95 GLY 96 -0.0003

GLY 96 LEU 97 0.0129

LEU 97 GLY 98 -0.0003

GLY 98 PRO 99 0.0379

PRO 99 MET 100 -0.0002

MET 100 ASN 101 0.1381

ASN 101 ILE 102 0.0001

ILE 102 PRO 103 -0.0414

PRO 103 LEU 104 -0.0002

LEU 104 VAL 105 -0.0116

VAL 105 SER 106 -0.0002

SER 106 ASP 107 -0.0171

ASP 107 PRO 108 0.0002

PRO 108 LYS 109 0.0023

LYS 109 ARG 110 -0.0001

ARG 110 THR 111 0.0041

THR 111 ILE 112 0.0001

ILE 112 ALA 113 -0.0345

ALA 113 GLN 114 0.0001

GLN 114 ASP 115 -0.0345

ASP 115 TYR 116 0.0000

TYR 116 GLY 117 -0.0281

GLY 117 VAL 118 0.0003

VAL 118 LEU 119 -0.0096

LEU 119 LYS 120 -0.0004

LYS 120 ALA 121 0.0450

ALA 121 ASP 122 0.0001

ASP 122 GLU 123 -0.0786

GLU 123 GLY 124 0.0002

GLY 124 ILE 125 0.0182

ILE 125 SER 126 -0.0001

SER 126 PHE 127 -0.0267

PHE 127 ARG 128 -0.0003

ARG 128 GLY 129 0.0516

GLY 129 LEU 130 0.0001

LEU 130 PHE 131 -0.0190

PHE 131 ILE 132 -0.0004

ILE 132 ILE 133 -0.0359

ILE 133 ASP 134 -0.0001

ASP 134 ASP 135 0.0133

ASP 135 LYS 136 0.0004

LYS 136 GLY 137 -0.0422

GLY 137 ILE 138 0.0001

ILE 138 LEU 139 0.0393

LEU 139 ARG 140 -0.0000

ARG 140 GLN 141 -0.0356

GLN 141 ILE 142 -0.0001

ILE 142 THR 143 -0.0155

THR 143 ILE 144 -0.0000

ILE 144 ASN 145 0.0504

ASN 145 ASP 146 -0.0003

ASP 146 LEU 147 0.1360

LEU 147 PRO 148 0.0002

PRO 148 VAL 149 0.0572

VAL 149 GLY 150 -0.0001

GLY 150 ARG 151 -0.0077

ARG 151 SER 152 0.0001

SER 152 VAL 153 -0.0701

VAL 153 ASP 154 -0.0002

ASP 154 GLU 155 -0.0046

GLU 155 ILE 156 -0.0000

ILE 156 LEU 157 -0.0214

LEU 157 ARG 158 0.0001

ARG 158 LEU 159 -0.0075

LEU 159 VAL 160 0.0004

VAL 160 GLN 161 0.0251

GLN 161 ALA 162 0.0000

ALA 162 PHE 163 0.0227

PHE 163 GLN 164 -0.0001

GLN 164 PHE 165 0.1852

PHE 165 THR 166 -0.0002

THR 166 ASP 167 0.0771

ASP 167 LYS 168 0.0001

LYS 168 HIS 169 0.1138

HIS 169 GLY 170 -0.0000

GLY 170 GLU 171 0.1052

GLU 171 VAL 172 -0.0001

VAL 172 CYS 173 -0.0236

CYS 173 PRO 174 -0.0001

PRO 174 ALA 175 0.0102

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 9 ---

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

* Mak_Prdx1_Model *