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

* 1oxm *

CA strain for 2502181843402299115

--- 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
ARG 17 THR 18 -0.0000

THR 18 THR 19 -0.0013

THR 19 ARG 20 0.0001

ARG 20 ASP 21 -0.0008

ASP 21 ASP 22 -0.0000

ASP 22 LEU 23 0.0005

LEU 23 ILE 24 -0.0003

ILE 24 ASN 25 0.0007

ASN 25 GLY 26 -0.0000

GLY 26 ASN 27 -0.0023

ASN 27 SER 28 0.0000

SER 28 ALA 29 0.0004

ALA 29 SER 30 -0.0000

SER 30 CYS 31 0.0013

CYS 31 ALA 32 -0.0003

ALA 32 ASP 33 -0.0001

ASP 33 VAL 34 0.0000

VAL 34 ILE 35 -0.0013

ILE 35 PHE 36 -0.0002

PHE 36 ILE 37 0.0004

ILE 37 TYR 38 0.0001

TYR 38 ALA 39 -0.0018

ALA 39 ARG 40 0.0003

ARG 40 GLY 41 -0.0002

GLY 41 SER 42 0.0003

SER 42 THR 43 -0.0170

THR 43 GLU 44 0.0000

GLU 44 THR 45 -0.0134

THR 45 GLY 46 -0.0004

GLY 46 ASN 47 0.0008

ASN 47 LEU 48 0.0000

LEU 48 GLY 49 -0.0031

GLY 49 THR 50 -0.0002

THR 50 LEU 51 0.0011

LEU 51 GLY 52 0.0002

GLY 52 PRO 53 0.0010

PRO 53 SER 54 -0.0003

SER 54 ILE 55 0.0004

ILE 55 ALA 56 0.0001

ALA 56 SER 57 0.0012

SER 57 ASN 58 0.0003

ASN 58 LEU 59 -0.0016

LEU 59 GLU 60 -0.0000

GLU 60 SER 61 0.0013

SER 61 ALA 62 0.0001

ALA 62 PHE 63 0.0001

PHE 63 GLY 64 0.0001

GLY 64 LYS 65 0.0013

LYS 65 ASP 66 -0.0000

ASP 66 GLY 67 0.0002

GLY 67 VAL 68 -0.0002

VAL 68 TRP 69 -0.0003

TRP 69 ILE 70 0.0002

ILE 70 GLN 71 0.0005

GLN 71 GLY 72 0.0002

GLY 72 VAL 73 0.0023

VAL 73 GLY 74 -0.0001

GLY 74 GLY 75 0.0023

GLY 75 ALA 76 0.0001

ALA 76 TYR 77 -0.0009

TYR 77 ARG 78 0.0000

ARG 78 ALA 79 -0.0020

ALA 79 THR 80 0.0002

THR 80 LEU 81 0.0075

LEU 81 GLY 82 0.0002

GLY 82 ASP 83 0.0341

ASP 83 ASN 84 -0.0001

ASN 84 ALA 85 -0.0020

ALA 85 LEU 86 -0.0000

LEU 86 PRO 87 0.0046

PRO 87 ARG 88 -0.0001

ARG 88 GLY 89 0.0046

GLY 89 THR 90 -0.0003

THR 90 SER 91 0.0012

SER 91 SER 92 -0.0000

SER 92 ALA 93 -0.0014

ALA 93 ALA 94 -0.0002

ALA 94 ILE 95 -0.0030

ILE 95 ARG 96 0.0002

ARG 96 GLU 97 -0.0002

GLU 97 MET 98 -0.0001

MET 98 LEU 99 -0.0039

LEU 99 GLY 100 0.0003

GLY 100 LEU 101 0.0005

LEU 101 PHE 102 -0.0001

PHE 102 GLN 103 -0.0012

GLN 103 GLN 104 0.0001

GLN 104 ALA 105 0.0004

ALA 105 ASN 106 0.0001

ASN 106 THR 107 0.0005

THR 107 LYS 108 0.0001

LYS 108 CYS 109 -0.0008

CYS 109 PRO 110 0.0001

PRO 110 ASP 111 -0.0007

ASP 111 ALA 112 0.0000

ALA 112 THR 113 -0.0000

THR 113 LEU 114 -0.0001

LEU 114 ILE 115 -0.0021

ILE 115 ALA 116 0.0004

ALA 116 GLY 117 -0.0026

GLY 117 GLY 118 -0.0001

GLY 118 TYR 119 -0.0051

TYR 119 SER 120 0.0003

SER 120 GLN 121 0.0006

GLN 121 GLY 122 -0.0000

GLY 122 ALA 123 0.0018

ALA 123 ALA 124 -0.0003

ALA 124 LEU 125 0.0002

LEU 125 ALA 126 -0.0001

ALA 126 ALA 127 -0.0004

ALA 127 ALA 128 -0.0001

ALA 128 SER 129 0.0016

SER 129 ILE 130 -0.0003

ILE 130 GLU 131 0.0001

GLU 131 ASP 132 -0.0001

ASP 132 LEU 133 0.0034

LEU 133 ASP 134 0.0001

ASP 134 SER 135 -0.0000

SER 135 ALA 136 -0.0001

ALA 136 ILE 137 -0.0015

ILE 137 ARG 138 0.0001

ARG 138 ASP 139 0.0014

ASP 139 LYS 140 0.0001

LYS 140 ILE 141 -0.0011

ILE 141 ALA 142 -0.0002

ALA 142 GLY 143 -0.0004

GLY 143 THR 144 -0.0002

THR 144 VAL 145 -0.0035

VAL 145 LEU 146 0.0001

LEU 146 PHE 147 -0.0051

PHE 147 GLY 148 0.0004

GLY 148 TYR 149 -0.0088

TYR 149 THR 150 0.0004

THR 150 LYS 151 -0.0019

LYS 151 ASN 152 -0.0000

ASN 152 LEU 153 -0.0014

LEU 153 GLN 154 -0.0000

GLN 154 ASN 155 0.0118

ASN 155 ARG 156 -0.0001

ARG 156 GLY 157 0.0003

GLY 157 ARG 158 -0.0002

ARG 158 ILE 159 -0.0011

ILE 159 PRO 160 0.0001

PRO 160 ASN 161 0.0036

ASN 161 TYR 162 -0.0002

TYR 162 PRO 163 -0.0018

PRO 163 ALA 164 0.0002

ALA 164 ASP 165 0.0025

ASP 165 ARG 166 -0.0001

ARG 166 THR 167 -0.0006

THR 167 LYS 168 0.0004

LYS 168 VAL 169 -0.0019

VAL 169 PHE 170 -0.0003

PHE 170 CYS 171 -0.0006

CYS 171 ASN 172 0.0003

ASN 172 THR 173 0.0009

THR 173 GLY 174 0.0001

GLY 174 ASP 175 -0.0001

ASP 175 LEU 176 -0.0002

LEU 176 VAL 177 0.0044

VAL 177 CYS 178 -0.0002

CYS 178 THR 179 0.0003

THR 179 GLY 180 -0.0004

GLY 180 SER 181 0.0249

SER 181 LEU 182 0.0001

LEU 182 ILE 183 0.0337

ILE 183 VAL 184 0.0001

VAL 184 ALA 185 0.0208

ALA 185 ALA 186 -0.0003

ALA 186 PRO 187 -0.0602

PRO 187 HIS 188 0.0004

HIS 188 LEU 189 0.0102

LEU 189 ALA 190 0.0004

ALA 190 TYR 191 -0.0196

TYR 191 GLY 192 -0.0003

GLY 192 PRO 193 0.0001

PRO 193 ASP 194 -0.0003

ASP 194 ALA 195 0.0012

ALA 195 ARG 196 0.0001

ARG 196 GLY 197 0.0022

GLY 197 PRO 198 -0.0000

PRO 198 ALA 199 0.0022

ALA 199 PRO 200 -0.0001

PRO 200 GLU 201 0.0010

GLU 201 PHE 202 0.0003

PHE 202 LEU 203 0.0002

LEU 203 ILE 204 0.0003

ILE 204 GLU 205 0.0028

GLU 205 LYS 206 0.0001

LYS 206 VAL 207 0.0018

VAL 207 ARG 208 0.0001

ARG 208 ALA 209 0.0006

ALA 209 VAL 210 -0.0000

VAL 210 ARG 211 0.0024

ARG 211 GLY 212 0.0000

GLY 212 ARG 17 -0.1272

ARG 17 THR 18 -0.0001

THR 18 THR 19 -0.0006

THR 19 ARG 20 0.0001

ARG 20 ASP 21 -0.0014

ASP 21 ASP 22 -0.0002

ASP 22 LEU 23 0.0009

LEU 23 ILE 24 0.0003

ILE 24 ASN 25 0.0007

ASN 25 GLY 26 0.0001

GLY 26 ASN 27 -0.0023

ASN 27 SER 28 0.0002

SER 28 ALA 29 0.0014

ALA 29 SER 30 -0.0002

SER 30 CYS 31 0.0017

CYS 31 ALA 32 0.0002

ALA 32 ASP 33 -0.0000

ASP 33 VAL 34 -0.0001

VAL 34 ILE 35 -0.0009

ILE 35 PHE 36 0.0001

PHE 36 ILE 37 -0.0004

ILE 37 TYR 38 0.0003

TYR 38 ALA 39 -0.0015

ALA 39 ARG 40 0.0000

ARG 40 GLY 41 -0.0030

GLY 41 SER 42 -0.0001

SER 42 THR 43 -0.0122

THR 43 GLU 44 0.0001

GLU 44 THR 45 -0.0103

THR 45 GLY 46 -0.0003

GLY 46 ASN 47 0.0010

ASN 47 LEU 48 -0.0003

LEU 48 GLY 49 -0.0028

GLY 49 THR 50 -0.0001

THR 50 LEU 51 0.0024

LEU 51 GLY 52 -0.0002

GLY 52 PRO 53 -0.0003

PRO 53 SER 54 -0.0003

SER 54 ILE 55 0.0004

ILE 55 ALA 56 -0.0000

ALA 56 SER 57 0.0010

SER 57 ASN 58 -0.0003

ASN 58 LEU 59 -0.0026

LEU 59 GLU 60 0.0001

GLU 60 SER 61 0.0009

SER 61 ALA 62 -0.0001

ALA 62 PHE 63 -0.0000

PHE 63 GLY 64 0.0002

GLY 64 LYS 65 0.0016

LYS 65 ASP 66 0.0003

ASP 66 GLY 67 0.0002

GLY 67 VAL 68 0.0001

VAL 68 TRP 69 -0.0006

TRP 69 ILE 70 0.0001

ILE 70 GLN 71 0.0008

GLN 71 GLY 72 0.0003

GLY 72 VAL 73 0.0019

VAL 73 GLY 74 -0.0002

GLY 74 GLY 75 0.0019

GLY 75 ALA 76 0.0003

ALA 76 TYR 77 -0.0009

TYR 77 ARG 78 0.0001

ARG 78 ALA 79 -0.0029

ALA 79 THR 80 0.0001

THR 80 LEU 81 -0.0121

LEU 81 GLY 82 0.0002

GLY 82 ASP 83 0.0154

ASP 83 ASN 84 -0.0003

ASN 84 ALA 85 -0.0024

ALA 85 LEU 86 0.0003

LEU 86 PRO 87 0.0051

PRO 87 ARG 88 0.0004

ARG 88 GLY 89 0.0010

GLY 89 THR 90 0.0000

THR 90 SER 91 0.0013

SER 91 SER 92 0.0000

SER 92 ALA 93 0.0004

ALA 93 ALA 94 0.0001

ALA 94 ILE 95 -0.0025

ILE 95 ARG 96 -0.0003

ARG 96 GLU 97 0.0010

GLU 97 MET 98 -0.0000

MET 98 LEU 99 -0.0028

LEU 99 GLY 100 -0.0002

GLY 100 LEU 101 0.0004

LEU 101 PHE 102 -0.0000

PHE 102 GLN 103 -0.0008

GLN 103 GLN 104 0.0000

GLN 104 ALA 105 -0.0002

ALA 105 ASN 106 -0.0003

ASN 106 THR 107 0.0003

THR 107 LYS 108 -0.0000

LYS 108 CYS 109 -0.0004

CYS 109 PRO 110 0.0000

PRO 110 ASP 111 -0.0008

ASP 111 ALA 112 -0.0000

ALA 112 THR 113 -0.0002

THR 113 LEU 114 -0.0001

LEU 114 ILE 115 -0.0023

ILE 115 ALA 116 0.0001

ALA 116 GLY 117 -0.0031

GLY 117 GLY 118 0.0001

GLY 118 TYR 119 -0.0076

TYR 119 SER 120 -0.0002

SER 120 GLN 121 0.0016

GLN 121 GLY 122 -0.0000

GLY 122 ALA 123 0.0006

ALA 123 ALA 124 -0.0000

ALA 124 LEU 125 0.0018

LEU 125 ALA 126 0.0003

ALA 126 ALA 127 0.0004

ALA 127 ALA 128 0.0003

ALA 128 SER 129 0.0021

SER 129 ILE 130 -0.0002

ILE 130 GLU 131 0.0002

GLU 131 ASP 132 0.0001

ASP 132 LEU 133 0.0035

LEU 133 ASP 134 -0.0003

ASP 134 SER 135 -0.0002

SER 135 ALA 136 0.0002

ALA 136 ILE 137 -0.0012

ILE 137 ARG 138 -0.0000

ARG 138 ASP 139 0.0010

ASP 139 LYS 140 0.0001

LYS 140 ILE 141 -0.0012

ILE 141 ALA 142 -0.0002

ALA 142 GLY 143 -0.0008

GLY 143 THR 144 -0.0001

THR 144 VAL 145 -0.0033

VAL 145 LEU 146 -0.0001

LEU 146 PHE 147 -0.0052

PHE 147 GLY 148 -0.0001

GLY 148 TYR 149 -0.0107

TYR 149 THR 150 -0.0001

THR 150 LYS 151 -0.0035

LYS 151 ASN 152 -0.0001

ASN 152 LEU 153 -0.0031

LEU 153 GLN 154 0.0004

GLN 154 ASN 155 0.0159

ASN 155 ARG 156 -0.0001

ARG 156 GLY 157 -0.0019

GLY 157 ARG 158 -0.0000

ARG 158 ILE 159 -0.0014

ILE 159 PRO 160 -0.0002

PRO 160 ASN 161 0.0071

ASN 161 TYR 162 -0.0002

TYR 162 PRO 163 -0.0031

PRO 163 ALA 164 -0.0001

ALA 164 ASP 165 0.0032

ASP 165 ARG 166 -0.0000

ARG 166 THR 167 -0.0007

THR 167 LYS 168 0.0001

LYS 168 VAL 169 -0.0011

VAL 169 PHE 170 0.0001

PHE 170 CYS 171 0.0020

CYS 171 ASN 172 0.0001

ASN 172 THR 173 0.0018

THR 173 GLY 174 -0.0003

GLY 174 ASP 175 -0.0030

ASP 175 LEU 176 0.0001

LEU 176 VAL 177 0.0136

VAL 177 CYS 178 0.0003

CYS 178 THR 179 -0.0031

THR 179 GLY 180 -0.0001

GLY 180 SER 181 0.0318

SER 181 LEU 182 0.0001

LEU 182 ILE 183 0.0367

ILE 183 VAL 184 -0.0002

VAL 184 ALA 185 0.0060

ALA 185 ALA 186 0.0001

ALA 186 PRO 187 -0.0539

PRO 187 HIS 188 -0.0004

HIS 188 LEU 189 0.0134

LEU 189 ALA 190 -0.0000

ALA 190 TYR 191 -0.0213

TYR 191 GLY 192 -0.0002

GLY 192 PRO 193 0.0012

PRO 193 ASP 194 -0.0001

ASP 194 ALA 195 0.0012

ALA 195 ARG 196 -0.0001

ARG 196 GLY 197 0.0031

GLY 197 PRO 198 0.0001

PRO 198 ALA 199 0.0023

ALA 199 PRO 200 -0.0001

PRO 200 GLU 201 0.0012

GLU 201 PHE 202 0.0003

PHE 202 LEU 203 -0.0003

LEU 203 ILE 204 0.0001

ILE 204 GLU 205 0.0032

GLU 205 LYS 206 -0.0001

LYS 206 VAL 207 0.0020

VAL 207 ARG 208 -0.0002

ARG 208 ALA 209 0.0004

ALA 209 VAL 210 -0.0000

VAL 210 ARG 211 0.0019

ARG 211 GLY 212 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 8th, 2025.

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

*** 1oxm ***

CA strain for 2502181843402299115

--- normal mode 7 ---

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

* 1oxm *