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

* cd1d *

CA strain for 2402011637291200144

--- 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
GLN 5 ARG 6 -0.0002

ARG 6 LEU 7 -0.0083

LEU 7 PHE 8 -0.0001

PHE 8 PRO 9 -0.0575

PRO 9 LEU 10 -0.0002

LEU 10 ARG 11 -0.0030

ARG 11 CYS 12 0.0001

CYS 12 LEU 13 -0.0064

LEU 13 GLN 14 -0.0000

GLN 14 ILE 15 0.0089

ILE 15 SER 16 0.0001

SER 16 SER 17 0.0070

SER 17 PHE 18 0.0001

PHE 18 ALA 19 -0.0006

ALA 19 ASN 20 0.0000

ASN 20 SER 21 -0.0033

SER 21 SER 22 -0.0000

SER 22 TRP 23 0.0081

TRP 23 THR 24 0.0003

THR 24 ARG 25 0.0138

ARG 25 THR 26 0.0000

THR 26 ASP 27 0.0318

ASP 27 GLY 28 0.0001

GLY 28 LEU 29 0.0334

LEU 29 ALA 30 0.0001

ALA 30 TRP 31 0.0017

TRP 31 LEU 32 0.0000

LEU 32 GLY 33 -0.0090

GLY 33 GLU 34 0.0001

GLU 34 LEU 35 -0.0330

LEU 35 GLN 36 -0.0002

GLN 36 THR 37 0.0148

THR 37 HIS 38 0.0003

HIS 38 SER 39 0.0105

SER 39 TRP 40 -0.0002

TRP 40 SER 41 0.0204

SER 41 ASN 42 -0.0002

ASN 42 ASP 43 0.0031

ASP 43 SER 44 -0.0000

SER 44 ASP 45 -0.0113

ASP 45 THR 46 0.0002

THR 46 VAL 47 0.0145

VAL 47 ARG 48 -0.0002

ARG 48 SER 49 0.0278

SER 49 LEU 50 0.0000

LEU 50 LYS 51 0.0222

LYS 51 PRO 52 -0.0002

PRO 52 TRP 53 -0.0038

TRP 53 SER 54 0.0001

SER 54 GLN 55 0.0331

GLN 55 GLY 56 0.0003

GLY 56 THR 57 0.0127

THR 57 PHE 58 -0.0001

PHE 58 SER 59 -0.0083

SER 59 ASP 60 0.0001

ASP 60 GLN 61 0.0009

GLN 61 GLN 62 0.0002

GLN 62 TRP 63 0.0079

TRP 63 GLU 64 0.0004

GLU 64 THR 65 0.0140

THR 65 LEU 66 -0.0001

LEU 66 GLN 67 -0.0091

GLN 67 HIS 68 -0.0002

HIS 68 ILE 69 0.0047

ILE 69 PHE 70 0.0002

PHE 70 ARG 71 -0.0078

ARG 71 VAL 72 0.0003

VAL 72 TYR 73 0.0077

TYR 73 ARG 74 -0.0001

ARG 74 SER 75 0.0103

SER 75 SER 76 -0.0001

SER 76 PHE 77 0.0004

PHE 77 THR 78 0.0001

THR 78 ARG 79 0.0142

ARG 79 ASP 80 -0.0004

ASP 80 VAL 81 -0.0058

VAL 81 LYS 82 -0.0001

LYS 82 GLU 83 0.0018

GLU 83 PHE 84 0.0000

PHE 84 ALA 85 -0.0067

ALA 85 LYS 86 0.0002

LYS 86 MET 87 -0.0054

MET 87 LEU 88 -0.0002

LEU 88 ARG 89 -0.0091

ARG 89 LEU 90 0.0001

LEU 90 SER 91 -0.0030

SER 91 TYR 92 -0.0001

TYR 92 PRO 93 -0.0012

PRO 93 LEU 94 0.0000

LEU 94 GLU 95 0.0070

GLU 95 LEU 96 0.0001

LEU 96 GLN 97 0.0099

GLN 97 VAL 98 -0.0000

VAL 98 SER 99 0.0027

SER 99 ALA 100 -0.0001

ALA 100 GLY 101 -0.0072

GLY 101 CYS 102 0.0000

CYS 102 GLU 103 -0.0310

GLU 103 VAL 104 -0.0002

VAL 104 HIS 105 0.0157

HIS 105 PRO 106 0.0002

PRO 106 GLY 107 -0.0378

GLY 107 ASN 108 0.0002

ASN 108 ALA 109 0.0104

ALA 109 SER 110 -0.0001

SER 110 ASN 111 0.0073

ASN 111 ASN 112 0.0006

ASN 112 PHE 113 -0.0015

PHE 113 PHE 114 -0.0002

PHE 114 HIS 115 0.0042

HIS 115 VAL 116 0.0000

VAL 116 ALA 117 0.0081

ALA 117 PHE 118 -0.0002

PHE 118 GLN 119 0.0030

GLN 119 GLY 120 -0.0001

GLY 120 LYS 121 -0.0048

LYS 121 ASP 122 0.0004

ASP 122 ILE 123 0.0016

ILE 123 LEU 124 -0.0001

LEU 124 SER 125 0.0029

SER 125 PHE 126 -0.0004

PHE 126 GLN 127 0.0063

GLN 127 GLY 128 0.0001

GLY 128 THR 129 -0.0152

THR 129 SER 130 -0.0002

SER 130 TRP 131 0.0067

TRP 131 GLU 132 0.0002

GLU 132 PRO 133 0.0122

PRO 133 THR 134 0.0001

THR 134 GLN 135 0.0010

GLN 135 GLU 136 -0.0005

GLU 136 ALA 137 0.0031

ALA 137 PRO 138 -0.0004

PRO 138 LEU 139 -0.0022

LEU 139 TRP 140 0.0000

TRP 140 VAL 141 -0.0019

VAL 141 ASN 142 -0.0004

ASN 142 LEU 143 0.0018

LEU 143 ALA 144 -0.0002

ALA 144 ILE 145 -0.0059

ILE 145 GLN 146 -0.0000

GLN 146 VAL 147 0.0041

VAL 147 LEU 148 -0.0000

LEU 148 ASN 149 -0.0066

ASN 149 GLN 150 0.0004

GLN 150 ASP 151 0.0104

ASP 151 LYS 152 -0.0000

LYS 152 TRP 153 0.0162

TRP 153 THR 154 0.0001

THR 154 ARG 155 0.0016

ARG 155 GLU 156 0.0002

GLU 156 THR 157 0.0106

THR 157 VAL 158 -0.0001

VAL 158 GLN 159 0.0015

GLN 159 TRP 160 -0.0002

TRP 160 LEU 161 -0.0023

LEU 161 LEU 162 0.0001

LEU 162 ASN 163 0.0124

ASN 163 GLY 164 0.0003

GLY 164 THR 165 0.0032

THR 165 CYS 166 -0.0003

CYS 166 PRO 167 -0.0088

PRO 167 GLN 168 0.0001

GLN 168 PHE 169 0.0084

PHE 169 VAL 170 -0.0003

VAL 170 SER 171 0.0066

SER 171 GLY 172 0.0002

GLY 172 LEU 173 -0.0002

LEU 173 LEU 174 0.0002

LEU 174 GLU 175 0.0138

GLU 175 SER 176 0.0002

SER 176 GLY 177 0.0074

GLY 177 LYS 178 -0.0001

LYS 178 SER 179 -0.0298

SER 179 GLU 180 -0.0004

GLU 180 LEU 181 0.0223

LEU 181 LYS 182 -0.0002

LYS 182 LYS 183 -0.1370

LYS 183 GLN 184 -0.0005

GLN 184 VAL 185 -0.0778

VAL 185 LYS 186 -0.0001

LYS 186 PRO 187 -0.0428

PRO 187 LYS 188 0.0000

LYS 188 ALA 189 -0.0047

ALA 189 TRP 190 0.0003

TRP 190 LEU 191 -0.0112

LEU 191 SER 192 -0.0001

SER 192 ARG 193 -0.0287

ARG 193 GLY 194 -0.0002

GLY 194 PRO 195 0.0014

PRO 195 SER 196 -0.0003

SER 196 PRO 197 -0.0090

PRO 197 GLY 198 -0.0001

GLY 198 PRO 199 0.0143

PRO 199 GLY 200 0.0002

GLY 200 ARG 201 -0.0170

ARG 201 LEU 202 -0.0001

LEU 202 LEU 203 0.0072

LEU 203 LEU 204 -0.0001

LEU 204 VAL 205 0.0212

VAL 205 CYS 206 0.0000

CYS 206 HIS 207 0.0159

HIS 207 VAL 208 0.0002

VAL 208 SER 209 0.0574

SER 209 GLY 210 0.0001

GLY 210 PHE 211 -0.0098

PHE 211 TYR 212 -0.0002

TYR 212 PRO 213 -0.0417

PRO 213 LYS 214 -0.0002

LYS 214 PRO 215 -0.0216

PRO 215 VAL 216 0.0001

VAL 216 TRP 217 -0.1219

TRP 217 VAL 218 0.0000

VAL 218 LYS 219 -0.0244

LYS 219 TRP 220 0.0001

TRP 220 MET 221 0.0032

MET 221 ARG 222 0.0001

ARG 222 GLY 223 0.0053

GLY 223 GLU 224 0.0001

GLU 224 GLN 225 -0.0048

GLN 225 GLU 226 0.0001

GLU 226 GLN 227 0.0027

GLN 227 GLN 228 -0.0002

GLN 228 GLY 229 -0.0109

GLY 229 THR 230 0.0002

THR 230 GLN 231 -0.0174

GLN 231 PRO 232 -0.0001

PRO 232 GLY 233 -0.0414

GLY 233 ASP 234 0.0000

ASP 234 ILE 235 0.0018

ILE 235 LEU 236 0.0002

LEU 236 PRO 237 -0.0202

PRO 237 ASN 238 0.0001

ASN 238 ALA 239 0.0273

ALA 239 ASP 240 0.0002

ASP 240 GLU 241 0.0455

GLU 241 THR 242 -0.0000

THR 242 TRP 243 0.0110

TRP 243 TYR 244 -0.0003

TYR 244 LEU 245 0.0071

LEU 245 ARG 246 -0.0001

ARG 246 ALA 247 0.0018

ALA 247 THR 248 -0.0003

THR 248 LEU 249 0.0042

LEU 249 ASP 250 0.0001

ASP 250 VAL 251 0.0004

VAL 251 VAL 252 -0.0001

VAL 252 ALA 253 0.0024

ALA 253 GLY 254 0.0002

GLY 254 GLU 255 -0.0076

GLU 255 ALA 256 0.0000

ALA 256 ALA 257 -0.0046

ALA 257 GLY 258 -0.0001

GLY 258 LEU 259 -0.0034

LEU 259 SER 260 0.0003

SER 260 CYS 261 -0.0086

CYS 261 ARG 262 -0.0003

ARG 262 VAL 263 -0.0159

VAL 263 LYS 264 -0.0003

LYS 264 HIS 265 -0.0552

HIS 265 SER 266 -0.0000

SER 266 SER 267 -0.0355

SER 267 LEU 268 -0.0005

LEU 268 GLU 269 0.0089

GLU 269 GLY 270 -0.0001

GLY 270 GLN 271 -0.0124

GLN 271 ASP 272 0.0000

ASP 272 ILE 273 -0.0170

ILE 273 VAL 274 0.0005

VAL 274 LEU 275 -0.0322

LEU 275 TYR 276 0.0002

TYR 276 TRP 277 -0.0423

TRP 277 HIS 278 -0.0000

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 25th, 2023.

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

*** cd1d ***

CA strain for 2402011637291200144

--- normal mode 9 ---

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

* cd1d *