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

* *

CA strain for 2404082132133069958

--- normal mode 8 ---

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 1 LEU 2 0.0003

LEU 2 PHE 3 -0.0166

PHE 3 GLU 4 0.0001

GLU 4 LEU 5 0.0102

LEU 5 GLY 6 0.0001

GLY 6 LYS 7 0.0362

LYS 7 MET 8 0.0003

MET 8 ILE 9 0.0137

ILE 9 LEU 10 -0.0000

LEU 10 GLN 11 0.1614

GLN 11 GLU 12 0.0002

GLU 12 THR 13 0.0197

THR 13 GLY 14 0.0001

GLY 14 LYS 15 0.0744

LYS 15 ASN 16 -0.0001

ASN 16 PRO 17 -0.0084

PRO 17 ALA 18 0.0004

ALA 18 LYS 19 -0.0579

LYS 19 SER 20 -0.0001

SER 20 TYR 21 0.1050

TYR 21 GLY 22 0.0002

GLY 22 ALA 23 -0.0067

ALA 23 TYR 24 0.0002

TYR 24 GLY 25 0.0064

GLY 25 CYS 26 -0.0002

CYS 26 ASN 27 0.0276

ASN 27 CYS 28 0.0002

CYS 28 GLY 29 -0.0648

GLY 29 VAL 30 0.0001

VAL 30 LEU 31 -0.0170

LEU 31 GLY 32 0.0001

GLY 32 ARG 33 -0.2115

ARG 33 GLY 34 -0.0000

GLY 34 LYS 35 -0.0713

LYS 35 PRO 36 0.0000

PRO 36 LYS 37 0.0299

LYS 37 ASP 38 -0.0001

ASP 38 ALA 39 -0.0554

ALA 39 THR 40 -0.0003

THR 40 ASP 41 -0.0260

ASP 41 ARG 42 -0.0001

ARG 42 CYS 43 -0.0169

CYS 43 CYS 44 0.0002

CYS 44 TYR 45 0.0109

TYR 45 VAL 46 0.0002

VAL 46 HIS 47 -0.0272

HIS 47 LYS 48 -0.0002

LYS 48 CYS 49 0.0155

CYS 49 CYS 50 0.0001

CYS 50 TYR 51 -0.0232

TYR 51 LYS 52 -0.0002

LYS 52 LYS 53 -0.0421

LYS 53 LEU 54 -0.0001

LEU 54 THR 55 0.0390

THR 55 GLY 56 -0.0004

GLY 56 CYS 57 -0.0313

CYS 57 ASP 58 -0.0001

ASP 58 PRO 59 -0.0168

PRO 59 LYS 60 0.0003

LYS 60 LYS 61 0.1290

LYS 61 ASP 62 -0.0000

ASP 62 ARG 63 -0.0041

ARG 63 TYR 64 -0.0001

TYR 64 SER 65 0.0258

SER 65 TYR 66 -0.0001

TYR 66 SER 67 0.0228

SER 67 TRP 68 -0.0002

TRP 68 LYS 69 0.1170

LYS 69 ASP 70 0.0002

ASP 70 LYS 71 0.0091

LYS 71 THR 72 -0.0004

THR 72 ILE 73 -0.0590

ILE 73 VAL 74 -0.0001

VAL 74 CYS 75 -0.0381

CYS 75 GLY 76 -0.0003

GLY 76 GLU 77 0.0219

GLU 77 ASN 78 0.0001

ASN 78 ASN 79 0.0045

ASN 79 PRO 80 -0.0001

PRO 80 CYS 81 -0.0282

CYS 81 LEU 82 -0.0001

LEU 82 LYS 83 -0.0242

LYS 83 GLU 84 0.0002

GLU 84 LEU 85 -0.0495

LEU 85 CYS 86 -0.0000

CYS 86 GLU 87 -0.0240

GLU 87 CYS 88 0.0002

CYS 88 ASP 89 0.0186

ASP 89 LYS 90 0.0000

LYS 90 ALA 91 -0.0699

ALA 91 VAL 92 -0.0000

VAL 92 ALA 93 0.0026

ALA 93 ILE 94 0.0001

ILE 94 CYS 95 -0.0654

CYS 95 LEU 96 0.0001

LEU 96 ARG 97 -0.0053

ARG 97 GLU 98 0.0002

GLU 98 ASN 99 -0.0647

ASN 99 LEU 100 0.0001

LEU 100 GLY 101 0.0120

GLY 101 THR 102 -0.0002

THR 102 TYR 103 0.0494

TYR 103 ASN 104 0.0002

ASN 104 LYS 105 0.0335

LYS 105 LYS 106 0.0003

LYS 106 TYR 107 -0.0131

TYR 107 ARG 108 0.0001

ARG 108 TYR 109 0.0598

TYR 109 HIS 110 -0.0000

HIS 110 LEU 111 -0.0533

LEU 111 LYS 112 0.0001

LYS 112 PRO 113 -0.0370

PRO 113 PHE 114 -0.0001

PHE 114 CYS 115 0.0355

CYS 115 LYS 116 0.0003

LYS 116 LYS 117 0.0284

LYS 117 ALA 118 0.0002

ALA 118 ASP 119 -0.0100

ASP 119 PRO 120 -0.0001

PRO 120 CYS 121 0.1785

CYS 121 SER 122 -0.0000

SER 122 LEU 123 -0.0160

LEU 123 PHE 124 0.0001

PHE 124 GLU 125 0.0039

GLU 125 LEU 126 -0.0000

LEU 126 GLY 127 0.0308

GLY 127 LYS 128 -0.0000

LYS 128 MET 129 0.0040

MET 129 ILE 130 -0.0001

ILE 130 LEU 131 -0.0011

LEU 131 GLN 132 -0.0000

GLN 132 GLU 133 -0.0710

GLU 133 THR 134 -0.0002

THR 134 GLY 135 0.0277

GLY 135 LYS 136 -0.0000

LYS 136 ASN 137 0.0278

ASN 137 PRO 138 0.0003

PRO 138 ALA 139 0.0413

ALA 139 LYS 140 -0.0001

LYS 140 SER 141 0.0841

SER 141 TYR 142 -0.0001

TYR 142 GLY 143 0.0421

GLY 143 ALA 144 0.0001

ALA 144 TYR 145 0.0460

TYR 145 GLY 146 0.0002

GLY 146 CYS 147 -0.0363

CYS 147 ASN 148 -0.0001

ASN 148 CYS 149 0.0116

CYS 149 GLY 150 0.0001

GLY 150 VAL 151 -0.0255

VAL 151 LEU 152 -0.0004

LEU 152 GLY 153 -0.1915

GLY 153 ARG 154 0.0002

ARG 154 GLY 155 0.0342

GLY 155 LYS 156 -0.0003

LYS 156 PRO 157 -0.1257

PRO 157 LYS 158 0.0003

LYS 158 ASP 159 -0.1141

ASP 159 ALA 160 -0.0001

ALA 160 THR 161 0.0068

THR 161 ASP 162 -0.0004

ASP 162 ARG 163 0.0444

ARG 163 CYS 164 0.0004

CYS 164 CYS 165 -0.0225

CYS 165 TYR 166 0.0001

TYR 166 VAL 167 -0.0345

VAL 167 HIS 168 -0.0003

HIS 168 LYS 169 -0.0427

LYS 169 CYS 170 -0.0001

CYS 170 CYS 171 -0.0232

CYS 171 TYR 172 -0.0002

TYR 172 LYS 173 0.0373

LYS 173 LYS 174 -0.0000

LYS 174 LEU 175 0.0630

LEU 175 THR 176 0.0001

THR 176 GLY 177 0.0061

GLY 177 CYS 178 0.0001

CYS 178 ASP 179 -0.2630

ASP 179 PRO 180 0.0001

PRO 180 LYS 181 -0.1240

LYS 181 LYS 182 0.0001

LYS 182 ASP 183 -0.1384

ASP 183 ARG 184 -0.0000

ARG 184 TYR 185 -0.0094

TYR 185 SER 186 0.0001

SER 186 TYR 187 0.0207

TYR 187 SER 188 -0.0003

SER 188 TRP 189 0.0061

TRP 189 LYS 190 -0.0001

LYS 190 ASP 191 0.0296

ASP 191 LYS 192 0.0002

LYS 192 THR 193 -0.1113

THR 193 ILE 194 0.0001

ILE 194 VAL 195 0.0632

VAL 195 CYS 196 -0.0001

CYS 196 GLY 197 0.0685

GLY 197 GLU 198 -0.0001

GLU 198 ASN 199 -0.0125

ASN 199 ASN 200 -0.0002

ASN 200 PRO 201 0.0084

PRO 201 CYS 202 0.0002

CYS 202 LEU 203 0.0286

LEU 203 LYS 204 0.0000

LYS 204 GLU 205 -0.0324

GLU 205 LEU 206 -0.0004

LEU 206 CYS 207 -0.0442

CYS 207 GLU 208 -0.0000

GLU 208 CYS 209 -0.0488

CYS 209 ASP 210 -0.0000

ASP 210 LYS 211 -0.0531

LYS 211 ALA 212 0.0001

ALA 212 VAL 213 -0.0185

VAL 213 ALA 214 0.0000

ALA 214 ILE 215 -0.0056

ILE 215 CYS 216 0.0003

CYS 216 LEU 217 0.0325

LEU 217 ARG 218 0.0005

ARG 218 GLU 219 -0.0749

GLU 219 ASN 220 -0.0001

ASN 220 LEU 221 -0.0276

LEU 221 GLY 222 0.0001

GLY 222 THR 223 -0.0595

THR 223 TYR 224 -0.0001

TYR 224 ASN 225 0.0077

ASN 225 LYS 226 0.0004

LYS 226 LYS 227 -0.0132

LYS 227 TYR 228 0.0001

TYR 228 ARG 229 0.0000

ARG 229 TYR 230 -0.0002

TYR 230 HIS 231 0.0216

HIS 231 LEU 232 -0.0000

LEU 232 LYS 233 -0.0446

LYS 233 PRO 234 -0.0001

PRO 234 PHE 235 0.0445

PHE 235 CYS 236 -0.0000

CYS 236 LYS 237 0.1143

LYS 237 LYS 238 -0.0002

LYS 238 ALA 239 0.0193

ALA 239 ASP 240 -0.0003

ASP 240 PRO 241 0.0845

PRO 241 CYS 242 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.

*** ***

CA strain for 2404082132133069958

--- normal mode 8 ---

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

* *