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

* Jon *

CA strain for 22011415395742824

--- 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
MET 1 MET 1 -0.0021

MET 1 ILE 2 0.0450

ILE 2 SER 3 -0.0654

SER 3 LEU 4 0.0050

LEU 4 LEU 4 0.0093

LEU 4 ILE 5 -0.0005

ILE 5 ILE 5 0.0034

ILE 5 ALA 6 -0.0559

ALA 6 ALA 7 0.0430

ALA 7 ALA 7 0.0081

ALA 7 LEU 8 -0.0023

LEU 8 LEU 8 0.0087

LEU 8 ALA 9 -0.0062

ALA 9 VAL 10 0.0364

VAL 10 VAL 10 -0.0035

VAL 10 VAL 10 -0.0033

VAL 10 VAL 10 -0.0040

VAL 10 ASP 11 -0.0319

ASP 11 ASP 11 0.0060

ASP 11 ASP 11 0.0035

ASP 11 ASP 11 0.0076

ASP 11 ARG 12 0.0124

ARG 12 ARG 12 -0.0100

ARG 12 ARG 12 0.0030

ARG 12 ARG 12 0.0036

ARG 12 VAL 13 0.0188

VAL 13 VAL 13 -0.0012

VAL 13 VAL 13 -0.0007

VAL 13 VAL 13 -0.0029

VAL 13 ILE 14 0.0055

ILE 14 ILE 14 -0.0000

ILE 14 ILE 14 -0.0286

ILE 14 ILE 14 -0.0285

ILE 14 GLY 15 -0.0173

GLY 15 MET 16 0.0177

MET 16 GLU 17 0.0151

GLU 17 ASN 18 -0.0845

ASN 18 ASN 18 0.0011

ASN 18 ALA 19 0.3194

ALA 19 ALA 19 0.0011

ALA 19 MET 20 0.1077

MET 20 MET 20 0.0048

MET 20 PRO 21 -0.0459

PRO 21 PRO 21 0.0010

PRO 21 TRP 22 0.0857

TRP 22 TRP 22 0.0011

TRP 22 ASN 23 0.0126

ASN 23 ASN 23 -0.0001

ASN 23 LEU 24 -0.0500

LEU 24 LEU 24 0.0153

LEU 24 PRO 25 -0.0338

PRO 25 PRO 25 0.0018

PRO 25 ALA 26 -0.0769

ALA 26 ALA 26 0.0046

ALA 26 ASP 27 0.0094

ASP 27 ASP 27 0.0162

ASP 27 LEU 28 0.0816

LEU 28 ALA 29 -0.1594

ALA 29 TRP 30 0.0766

TRP 30 PHE 31 0.2285

PHE 31 LYS 32 -0.0503

LYS 32 ARG 33 0.0287

ARG 33 ARG 33 0.0040

ARG 33 ARG 33 0.0080

ARG 33 ASN 34 0.0343

ASN 34 ASN 34 -0.0008

ASN 34 ASN 34 -0.0002

ASN 34 THR 35 0.0207

THR 35 THR 35 -0.0048

THR 35 THR 35 0.0030

THR 35 LEU 36 -0.0150

LEU 36 ASN 37 -0.0010

ASN 37 ASN 37 -0.0012

ASN 37 ASN 37 -0.0004

ASN 37 LYS 38 0.0011

LYS 38 LYS 38 -0.0057

LYS 38 LYS 38 -0.0024

LYS 38 PRO 39 0.0013

PRO 39 VAL 40 -0.0095

VAL 40 VAL 40 0.0041

VAL 40 VAL 40 0.0020

VAL 40 ILE 41 0.0081

ILE 41 ILE 41 -0.0027

ILE 41 ILE 41 0.0082

ILE 41 MET 42 0.0058

MET 42 GLY 43 0.0050

GLY 43 ARG 44 -0.0569

ARG 44 ARG 44 -0.0048

ARG 44 ARG 44 0.0051

ARG 44 HIS 45 0.0489

HIS 45 HIS 45 0.0140

HIS 45 HIS 45 -0.0008

HIS 45 THR 46 0.0102

THR 46 THR 46 -0.0227

THR 46 THR 46 -0.0027

THR 46 TRP 47 -0.0250

TRP 47 TRP 47 -0.0048

TRP 47 TRP 47 -0.0023

TRP 47 GLU 48 -0.0131

GLU 48 GLU 48 -0.0019

GLU 48 GLU 48 -0.0012

GLU 48 SER 49 0.0937

SER 49 SER 49 -0.0020

SER 49 SER 49 0.0009

SER 49 ILE 50 -0.0796

ILE 50 ILE 50 0.0021

ILE 50 ILE 50 -0.0186

ILE 50 GLY 51 0.0455

GLY 51 ARG 52 0.0061

ARG 52 ARG 52 -0.0185

ARG 52 ARG 52 0.1878

ARG 52 PRO 53 -0.0404

PRO 53 LEU 54 0.1266

LEU 54 LEU 54 -0.0031

LEU 54 LEU 54 0.0964

LEU 54 PRO 55 -0.0347

PRO 55 PRO 55 -0.0040

PRO 55 PRO 55 -0.0077

PRO 55 GLY 56 -0.0254

GLY 56 ARG 57 0.0042

ARG 57 ARG 57 0.0303

ARG 57 LYS 58 0.0819

LYS 58 ASN 59 -0.0305

ASN 59 ASN 59 -0.0013

ASN 59 ILE 60 0.0312

ILE 60 ILE 61 0.0050

ILE 61 ILE 61 0.0000

ILE 61 LEU 62 -0.0226

LEU 62 SER 63 -0.0751

SER 63 SER 64 -0.0079

SER 64 SER 64 -0.0028

SER 64 GLN 65 -0.0321

GLN 65 GLN 65 -0.0008

GLN 65 PRO 66 0.0090

PRO 66 PRO 66 0.0006

PRO 66 GLY 67 0.0303

GLY 67 THR 68 -0.0264

THR 68 THR 68 0.0018

THR 68 THR 68 0.0066

THR 68 ASP 69 0.0151

ASP 69 ASP 69 0.0006

ASP 69 ASP 69 -0.0029

ASP 69 ASP 70 0.0030

ASP 70 ASP 70 -0.0014

ASP 70 ASP 70 0.0064

ASP 70 ARG 71 0.0213

ARG 71 ARG 71 0.0032

ARG 71 ARG 71 -0.0035

ARG 71 VAL 72 -0.0147

VAL 72 VAL 72 0.0001

VAL 72 VAL 72 -0.0005

VAL 72 THR 73 -0.0320

THR 73 THR 73 0.0002

THR 73 THR 73 0.0122

THR 73 TRP 74 0.0351

TRP 74 TRP 74 -0.0006

TRP 74 TRP 74 0.0032

TRP 74 VAL 75 -0.0468

VAL 75 VAL 75 0.0127

VAL 75 VAL 75 0.0093

VAL 75 LYS 76 0.0119

LYS 76 LYS 76 -0.0032

LYS 76 LYS 76 0.0039

LYS 76 SER 77 -0.0767

SER 77 SER 77 -0.0034

SER 77 SER 77 0.0013

SER 77 VAL 78 -0.0709

VAL 78 VAL 78 -0.0006

VAL 78 VAL 78 0.0032

VAL 78 ASP 79 0.0523

ASP 79 ASP 79 0.0025

ASP 79 ASP 79 0.0011

ASP 79 GLU 80 -0.0210

GLU 80 ALA 81 0.0280

ALA 81 ILE 82 -0.0242

ILE 82 ILE 82 0.0074

ILE 82 ILE 82 -0.0349

ILE 82 ALA 83 -0.0007

ALA 83 ALA 83 -0.0017

ALA 83 ALA 83 -0.0065

ALA 83 ALA 84 -0.0040

ALA 84 CYS 85 -0.0044

CYS 85 CYS 85 -0.0266

CYS 85 GLY 86 -0.0069

GLY 86 ASP 87 -0.0164

ASP 87 ASP 87 0.0019

ASP 87 VAL 88 -0.0352

VAL 88 VAL 88 -0.0025

VAL 88 PRO 89 -0.0046

PRO 89 PRO 89 -0.0017

PRO 89 GLU 90 -0.0151

GLU 90 ILE 91 -0.0136

ILE 91 ILE 91 -0.0068

ILE 91 ILE 91 0.0179

ILE 91 MET 92 -0.0160

MET 92 VAL 93 -0.0121

VAL 93 VAL 93 0.0709

VAL 93 VAL 93 -0.0104

VAL 93 ILE 94 0.0213

ILE 94 ILE 94 -0.0060

ILE 94 ILE 94 0.0013

ILE 94 GLY 95 -0.0451

GLY 95 GLY 96 -0.0133

GLY 96 GLY 97 -0.1017

GLY 97 ARG 98 0.0511

ARG 98 ARG 98 0.0000

ARG 98 ARG 98 0.0018

ARG 98 VAL 99 -0.0090

VAL 99 VAL 99 -0.0023

VAL 99 VAL 99 -0.0261

VAL 99 TYR 100 -0.0438

TYR 100 GLU 101 0.0388

GLU 101 GLN 102 0.0245

GLN 102 PHE 103 0.0130

PHE 103 PHE 103 0.0136

PHE 103 LEU 104 -0.0920

LEU 104 LEU 104 0.0014

LEU 104 PRO 105 0.0213

PRO 105 PRO 105 -0.0028

PRO 105 LYS 106 0.0079

LYS 106 LYS 106 0.0045

LYS 106 ALA 107 -0.1328

ALA 107 ALA 107 -0.0008

ALA 107 GLN 108 -0.0407

GLN 108 GLN 108 0.0059

GLN 108 LYS 109 -0.0081

LYS 109 LYS 109 -0.0051

LYS 109 LEU 110 -0.0045

LEU 110 LEU 110 -0.0020

LEU 110 TYR 111 0.0153

TYR 111 TYR 111 0.0116

TYR 111 LEU 112 -0.0355

LEU 112 THR 113 -0.0405

THR 113 THR 113 0.0086

THR 113 THR 113 -0.0087

THR 113 THR 113 -0.0017

THR 113 HIS 114 0.0110

HIS 114 HIS 114 0.0008

HIS 114 HIS 114 0.0037

HIS 114 HIS 114 0.0322

HIS 114 ILE 115 -0.0190

ILE 115 ASP 116 0.0298

ASP 116 ASP 116 0.0092

ASP 116 ALA 117 0.0920

ALA 117 ALA 117 -0.0001

ALA 117 GLU 118 -0.0106

GLU 118 GLU 118 -0.0034

GLU 118 VAL 119 0.0020

VAL 119 VAL 119 -0.0003

VAL 119 GLU 120 -0.0265

GLU 120 GLU 120 -0.0142

GLU 120 GLY 121 0.0209

GLY 121 ASP 122 -0.0311

ASP 122 THR 123 0.0467

THR 123 THR 123 0.0095

THR 123 HIS 124 -0.0038

HIS 124 PHE 125 -0.0035

PHE 125 PRO 126 0.0283

PRO 126 PRO 126 0.0054

PRO 126 PRO 126 0.0021

PRO 126 PRO 126 -0.0079

PRO 126 ASP 127 -0.0108

ASP 127 ASP 127 -0.0044

ASP 127 ASP 127 -0.0055

ASP 127 ASP 127 -0.0079

ASP 127 TYR 128 0.0067

TYR 128 TYR 128 -0.0015

TYR 128 TYR 128 0.0101

TYR 128 TYR 128 0.0021

TYR 128 GLU 129 -0.0153

GLU 129 PRO 130 -0.0027

PRO 130 PRO 130 0.0080

PRO 130 PRO 130 0.0049

PRO 130 ASP 131 -0.0024

ASP 131 ASP 131 -0.0009

ASP 131 ASP 131 0.0010

ASP 131 ASP 132 0.0056

ASP 132 ASP 132 -0.0130

ASP 132 ASP 132 -0.0009

ASP 132 TRP 133 0.0023

TRP 133 GLU 134 -0.0268

GLU 134 SER 135 -0.0956

SER 135 VAL 136 0.0257

VAL 136 VAL 136 0.0070

VAL 136 VAL 136 -0.0024

VAL 136 PHE 137 -0.0350

PHE 137 PHE 137 0.0019

PHE 137 PHE 137 -0.0007

PHE 137 SER 138 -0.0363

SER 138 SER 138 0.0004

SER 138 SER 138 0.0014

SER 138 GLU 139 -0.1040

GLU 139 GLU 139 -0.0061

GLU 139 GLU 139 -0.0048

GLU 139 PHE 140 -0.0124

PHE 140 HIS 141 -0.1314

HIS 141 HIS 141 -0.0144

HIS 141 HIS 141 -0.0012

HIS 141 ASP 142 -0.0002

ASP 142 ASP 142 -0.0197

ASP 142 ASP 142 -0.0120

ASP 142 ALA 143 0.0215

ALA 143 ASP 144 -0.0585

ASP 144 ASP 144 0.0038

ASP 144 ASP 144 0.0051

ASP 144 ALA 145 -0.1068

ALA 145 ALA 145 -0.0003

ALA 145 ALA 145 0.0002

ALA 145 GLN 146 0.0727

GLN 146 GLN 146 -0.0081

GLN 146 GLN 146 -0.0026

GLN 146 ASN 147 -0.0161

ASN 147 ASN 147 0.0044

ASN 147 ASN 147 0.0057

ASN 147 SER 148 -0.0258

SER 148 SER 148 -0.0049

SER 148 SER 148 0.0011

SER 148 HIS 149 -0.0561

HIS 149 HIS 149 0.0035

HIS 149 SER 150 0.0737

SER 150 TYR 151 -0.0300

TYR 151 TYR 151 -0.0043

TYR 151 PHE 153 -0.0292

PHE 153 PHE 153 0.0015

PHE 153 GLU 154 -0.1007

GLU 154 ILE 155 -0.0238

ILE 155 LEU 156 -0.0112

LEU 156 LEU 156 0.0131

LEU 156 GLU 157 -0.0109

GLU 157 GLU 157 0.0005

GLU 157 ARG 158 -0.0899

ARG 158 ARG 159 -0.0406

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.

*** Jon ***

CA strain for 22011415395742824

--- normal mode 7 ---

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

* Jon *