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

* *

CA strain for 2404082132133069958

--- 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 1 LEU 2 -0.0002

LEU 2 PHE 3 0.0154

PHE 3 GLU 4 0.0000

GLU 4 LEU 5 -0.0650

LEU 5 GLY 6 0.0000

GLY 6 LYS 7 -0.1072

LYS 7 MET 8 -0.0001

MET 8 ILE 9 0.0753

ILE 9 LEU 10 -0.0001

LEU 10 GLN 11 -0.2544

GLN 11 GLU 12 -0.0002

GLU 12 THR 13 0.0610

THR 13 GLY 14 -0.0003

GLY 14 LYS 15 -0.0516

LYS 15 ASN 16 -0.0001

ASN 16 PRO 17 0.0111

PRO 17 ALA 18 0.0002

ALA 18 LYS 19 0.0010

LYS 19 SER 20 0.0000

SER 20 TYR 21 -0.0190

TYR 21 GLY 22 0.0000

GLY 22 ALA 23 0.0348

ALA 23 TYR 24 -0.0003

TYR 24 GLY 25 -0.0751

GLY 25 CYS 26 0.0001

CYS 26 ASN 27 0.0044

ASN 27 CYS 28 0.0003

CYS 28 GLY 29 0.0221

GLY 29 VAL 30 -0.0001

VAL 30 LEU 31 -0.0331

LEU 31 GLY 32 0.0001

GLY 32 ARG 33 -0.0398

ARG 33 GLY 34 -0.0001

GLY 34 LYS 35 0.0639

LYS 35 PRO 36 0.0000

PRO 36 LYS 37 -0.0281

LYS 37 ASP 38 -0.0001

ASP 38 ALA 39 0.0579

ALA 39 THR 40 -0.0001

THR 40 ASP 41 0.0174

ASP 41 ARG 42 -0.0000

ARG 42 CYS 43 0.0217

CYS 43 CYS 44 -0.0001

CYS 44 TYR 45 0.0113

TYR 45 VAL 46 0.0001

VAL 46 HIS 47 -0.0340

HIS 47 LYS 48 -0.0004

LYS 48 CYS 49 -0.0004

CYS 49 CYS 50 -0.0001

CYS 50 TYR 51 -0.0361

TYR 51 LYS 52 -0.0002

LYS 52 LYS 53 0.1642

LYS 53 LEU 54 0.0004

LEU 54 THR 55 -0.0364

THR 55 GLY 56 0.0001

GLY 56 CYS 57 0.0180

CYS 57 ASP 58 0.0002

ASP 58 PRO 59 -0.0278

PRO 59 LYS 60 -0.0003

LYS 60 LYS 61 -0.0338

LYS 61 ASP 62 -0.0001

ASP 62 ARG 63 -0.0230

ARG 63 TYR 64 -0.0004

TYR 64 SER 65 -0.0837

SER 65 TYR 66 0.0002

TYR 66 SER 67 -0.1262

SER 67 TRP 68 0.0003

TRP 68 LYS 69 -0.2759

LYS 69 ASP 70 0.0000

ASP 70 LYS 71 -0.0028

LYS 71 THR 72 -0.0001

THR 72 ILE 73 0.1240

ILE 73 VAL 74 0.0000

VAL 74 CYS 75 0.1262

CYS 75 GLY 76 0.0000

GLY 76 GLU 77 -0.0046

GLU 77 ASN 78 0.0000

ASN 78 ASN 79 -0.0111

ASN 79 PRO 80 -0.0001

PRO 80 CYS 81 0.0250

CYS 81 LEU 82 -0.0001

LEU 82 LYS 83 -0.0115

LYS 83 GLU 84 -0.0001

GLU 84 LEU 85 -0.0250

LEU 85 CYS 86 -0.0001

CYS 86 GLU 87 -0.0466

GLU 87 CYS 88 -0.0002

CYS 88 ASP 89 -0.0378

ASP 89 LYS 90 -0.0003

LYS 90 ALA 91 0.1837

ALA 91 VAL 92 0.0001

VAL 92 ALA 93 0.0251

ALA 93 ILE 94 -0.0000

ILE 94 CYS 95 0.1532

CYS 95 LEU 96 -0.0001

LEU 96 ARG 97 0.0153

ARG 97 GLU 98 0.0000

GLU 98 ASN 99 0.1148

ASN 99 LEU 100 0.0003

LEU 100 GLY 101 -0.0123

GLY 101 THR 102 0.0001

THR 102 TYR 103 0.0107

TYR 103 ASN 104 0.0001

ASN 104 LYS 105 0.0281

LYS 105 LYS 106 0.0001

LYS 106 TYR 107 -0.0161

TYR 107 ARG 108 0.0002

ARG 108 TYR 109 0.2460

TYR 109 HIS 110 0.0002

HIS 110 LEU 111 0.1903

LEU 111 LYS 112 -0.0003

LYS 112 PRO 113 0.1781

PRO 113 PHE 114 0.0004

PHE 114 CYS 115 -0.0094

CYS 115 LYS 116 -0.0003

LYS 116 LYS 117 -0.0396

LYS 117 ALA 118 -0.0000

ALA 118 ASP 119 -0.0075

ASP 119 PRO 120 -0.0003

PRO 120 CYS 121 -0.2100

CYS 121 SER 122 0.0000

SER 122 LEU 123 -0.0389

LEU 123 PHE 124 0.0001

PHE 124 GLU 125 0.0950

GLU 125 LEU 126 0.0001

LEU 126 GLY 127 0.0370

GLY 127 LYS 128 0.0002

LYS 128 MET 129 -0.0021

MET 129 ILE 130 -0.0004

ILE 130 LEU 131 -0.0183

LEU 131 GLN 132 -0.0002

GLN 132 GLU 133 -0.0620

GLU 133 THR 134 -0.0000

THR 134 GLY 135 0.0419

GLY 135 LYS 136 -0.0003

LYS 136 ASN 137 0.0843

ASN 137 PRO 138 -0.0002

PRO 138 ALA 139 0.0192

ALA 139 LYS 140 -0.0000

LYS 140 SER 141 0.0231

SER 141 TYR 142 0.0002

TYR 142 GLY 143 0.0313

GLY 143 ALA 144 0.0000

ALA 144 TYR 145 0.0127

TYR 145 GLY 146 -0.0001

GLY 146 CYS 147 -0.0159

CYS 147 ASN 148 -0.0000

ASN 148 CYS 149 0.0204

CYS 149 GLY 150 -0.0003

GLY 150 VAL 151 0.0776

VAL 151 LEU 152 -0.0001

LEU 152 GLY 153 -0.0471

GLY 153 ARG 154 0.0001

ARG 154 GLY 155 0.0575

GLY 155 LYS 156 -0.0001

LYS 156 PRO 157 -0.1028

PRO 157 LYS 158 -0.0002

LYS 158 ASP 159 -0.2302

ASP 159 ALA 160 -0.0001

ALA 160 THR 161 0.0306

THR 161 ASP 162 0.0002

ASP 162 ARG 163 0.0470

ARG 163 CYS 164 0.0002

CYS 164 CYS 165 -0.0248

CYS 165 TYR 166 -0.0002

TYR 166 VAL 167 -0.1050

VAL 167 HIS 168 -0.0005

HIS 168 LYS 169 -0.0375

LYS 169 CYS 170 -0.0001

CYS 170 CYS 171 -0.1532

CYS 171 TYR 172 0.0001

TYR 172 LYS 173 -0.0159

LYS 173 LYS 174 -0.0002

LYS 174 LEU 175 -0.0123

LEU 175 THR 176 0.0003

THR 176 GLY 177 0.0170

GLY 177 CYS 178 -0.0001

CYS 178 ASP 179 0.0349

ASP 179 PRO 180 -0.0001

PRO 180 LYS 181 -0.0307

LYS 181 LYS 182 -0.0002

LYS 182 ASP 183 0.3013

ASP 183 ARG 184 0.0003

ARG 184 TYR 185 0.1174

TYR 185 SER 186 -0.0004

SER 186 TYR 187 0.1039

TYR 187 SER 188 0.0004

SER 188 TRP 189 0.0395

TRP 189 LYS 190 -0.0001

LYS 190 ASP 191 0.1213

ASP 191 LYS 192 -0.0002

LYS 192 THR 193 -0.1432

THR 193 ILE 194 0.0002

ILE 194 VAL 195 -0.0082

VAL 195 CYS 196 -0.0001

CYS 196 GLY 197 -0.0551

GLY 197 GLU 198 0.0003

GLU 198 ASN 199 -0.0058

ASN 199 ASN 200 -0.0001

ASN 200 PRO 201 -0.0281

PRO 201 CYS 202 -0.0000

CYS 202 LEU 203 -0.0096

LEU 203 LYS 204 -0.0000

LYS 204 GLU 205 -0.0916

GLU 205 LEU 206 -0.0004

LEU 206 CYS 207 0.0099

CYS 207 GLU 208 0.0001

GLU 208 CYS 209 -0.1327

CYS 209 ASP 210 0.0000

ASP 210 LYS 211 0.0470

LYS 211 ALA 212 -0.0000

ALA 212 VAL 213 -0.1482

VAL 213 ALA 214 -0.0002

ALA 214 ILE 215 0.0536

ILE 215 CYS 216 0.0002

CYS 216 LEU 217 0.0320

LEU 217 ARG 218 0.0000

ARG 218 GLU 219 -0.0391

GLU 219 ASN 220 -0.0002

ASN 220 LEU 221 0.0232

LEU 221 GLY 222 0.0004

GLY 222 THR 223 -0.0481

THR 223 TYR 224 0.0000

TYR 224 ASN 225 -0.0507

ASN 225 LYS 226 -0.0000

LYS 226 LYS 227 -0.0011

LYS 227 TYR 228 -0.0002

TYR 228 ARG 229 0.0186

ARG 229 TYR 230 -0.0002

TYR 230 HIS 231 0.1067

HIS 231 LEU 232 -0.0001

LEU 232 LYS 233 0.0562

LYS 233 PRO 234 0.0006

PRO 234 PHE 235 -0.1071

PHE 235 CYS 236 -0.0001

CYS 236 LYS 237 0.0590

LYS 237 LYS 238 -0.0001

LYS 238 ALA 239 -0.0500

ALA 239 ASP 240 -0.0002

ASP 240 PRO 241 0.0393

PRO 241 CYS 242 -0.0002

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 9 ---

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

* *