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

* 2QLE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *

CA distance fluctuations for 240220090021146876

--- normal mode 16 ---

This matrix displays the maximum distance fluctuations between all pairs of CA atoms and between the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Distance increases are plotted in blue and decreases in red for the strongest 10% of the residue pair distance changes. Every pixel corresponds to a single residue. Grey lines are drawn every 10 residues, yellow lines every 100 residues (counting from the upper left corner).

The following table indicates for every residue the two corresponding residues with the strongest CA distance fluctuations.

[HELP on distance fluctuations]

GD ok

largest increase ref largest decrease
GLY 183 0.53 GLY 1 -0.50 GLY 226

GLY 183 0.40 GLU 2 -0.48 GLY 226

GLY 185 0.45 GLU 3 -0.42 GLY 226

GLY 183 0.39 LEU 4 -0.38 GLY 226

GLY 183 0.34 PHE 5 -0.36 GLY 226

GLY 183 0.31 THR 6 -0.32 PRO 205

GLY 183 0.28 GLY 7 -0.34 PRO 205

GLY 183 0.25 VAL 8 -0.36 PRO 205

GLY 183 0.25 VAL 9 -0.31 PRO 205

ASP 174 0.24 PRO 10 -0.27 GLY 226

THR 59 0.25 ILE 11 -0.33 GLY 226

TYR 100 0.25 LEU 12 -0.34 GLY 226

TYR 100 0.25 VAL 13 -0.39 GLY 226

LEU 119 0.30 GLU 14 -0.38 GLY 226

LEU 119 0.25 LEU 15 -0.50 ALA 104

LYS 120 0.20 ASP 16 -0.48 ALA 104

ASP 16 0.19 GLY 17 -0.53 GLU 89

HIS 133 0.21 ASP 18 -0.48 LYS 152

HIS 133 0.22 VAL 19 -0.41 GLN 151

HIS 133 0.21 ASN 20 -0.35 GLN 151

HIS 133 0.28 GLY 21 -0.41 GLN 151

HIS 133 0.37 HIS 22 -0.42 LYS 152

HIS 133 0.28 LYS 23 -0.49 LYS 152

GLU 136 0.26 PHE 24 -0.45 LYS 152

GLU 136 0.21 SER 25 -0.42 ALA 104

GLU 136 0.17 VAL 26 -0.39 GLY 226

LEU 119 0.16 SER 27 -0.37 GLY 226

ARG 162 0.17 GLY 28 -0.38 GLY 226

VAL 58 0.19 GLU 29 -0.32 GLY 226

ILE 161 0.20 GLY 30 -0.35 PRO 205

ILE 161 0.24 GLU 31 -0.41 PRO 205

ASP 174 0.25 GLY 32 -0.41 PRO 205

GLY 183 0.24 ASP 33 -0.44 PRO 205

GLY 183 0.27 ALA 34 -0.41 PRO 205

GLY 183 0.27 THR 35 -0.43 PRO 205

GLY 183 0.22 TYR 36 -0.49 PRO 205

PHE 159 0.23 GLY 37 -0.46 PRO 205

SER 141 0.24 LYS 38 -0.53 PRO 205

SER 141 0.25 LEU 39 -0.48 PRO 205

VAL 199 0.27 THR 40 -0.56 PRO 205

ARG 162 0.17 LEU 41 -0.38 PHE 65

LEU 201 0.15 LYS 42 -0.34 GLY 226

ASN 164 0.13 PHE 43 -0.37 GLY 226

HIS 211 0.13 ILE 44 -0.35 GLY 226

GLU 136 0.20 CYS 45 -0.37 GLY 226

LYS 208 0.30 THR 46 -0.36 GLY 226

LYS 208 0.29 THR 47 -0.38 LYS 152

PRO 205 0.36 GLY 48 -0.42 GLU 126

PRO 205 0.32 LYS 49 -0.50 GLU 126

GLU 136 0.32 LEU 50 -0.43 GLU 126

GLU 166 0.29 PRO 51 -0.42 GLU 126

LEU 135 0.33 VAL 52 -0.38 GLN 177

GLU 136 0.26 PRO 53 -0.39 LEU 131

GLU 136 0.23 TRP 54 -0.39 GLY 226

VAL 26 0.15 PRO 55 -0.43 VAL 144

GLU 14 0.18 THR 56 -0.41 GLN 177

VAL 13 0.19 LEU 57 -0.47 GLN 177

LEU 12 0.23 VAL 58 -0.46 VAL 144

PHE 61 0.32 THR 59 -0.44 GLY 226

VAL 114 0.27 THR 60 -0.45 GLY 226

THR 59 0.32 PHE 61 -0.43 GLY 226

ASP 174 0.32 VAL 62 -0.46 GLY 226

PHE 159 0.27 GLN 63 -0.44 GLY 226

GLY 183 0.26 CYS 64 -0.46 GLY 226

PHE 159 0.24 PHE 65 -0.40 PRO 205

GLY 183 0.23 SER 66 -0.43 PRO 205

GLY 183 0.22 ARG 67 -0.46 PRO 205

GLY 183 0.21 TYR 68 -0.42 GLY 226

GLY 183 0.18 PRO 69 -0.43 PRO 205

LYS 150 0.21 ASP 70 -0.40 PRO 205

LYS 150 0.21 HIS 71 -0.45 GLY 226

LYS 150 0.21 MET 72 -0.65 GLY 226

LYS 150 0.22 LYS 73 -0.64 GLY 226

LYS 150 0.28 ARG 74 -0.87 GLY 226

LYS 150 0.25 HIS 75 -0.82 GLY 226

GLY 183 0.23 ASP 76 -0.64 GLY 226

GLY 183 0.27 PHE 77 -0.64 GLY 226

GLY 183 0.31 PHE 78 -0.54 GLY 226

GLY 183 0.38 LYS 79 -0.52 GLY 226

GLY 183 0.47 SER 80 -0.60 GLY 226

GLY 183 0.61 ALA 81 -0.54 GLY 226

GLY 183 0.60 MET 82 -0.49 GLY 226

GLY 183 0.44 PRO 83 -0.43 GLY 226

GLY 183 0.36 GLU 84 -0.46 GLY 226

GLY 183 0.38 GLY 85 -0.46 GLY 226

TYR 176 0.19 TYR 86 -0.47 GLY 226

GLU 89 0.19 VAL 87 -0.49 ILE 117

GLU 89 0.33 GLN 88 -0.47 ILE 117

GLN 88 0.33 GLU 89 -0.60 LEU 119

THR 91 0.39 ARG 90 -0.47 GLN 177

ARG 90 0.39 THR 91 -0.43 GLN 151

VAL 62 0.30 ILE 92 -0.35 GLY 226

VAL 62 0.28 PHE 93 -0.29 GLY 226

GLY 128 0.25 PHE 94 -0.26 GLY 226

ASP 174 0.28 LYS 95 -0.17 LYS 208

ASP 174 0.24 ASP 96 -0.25 LYS 208

GLY 128 0.25 ASP 97 -0.25 LYS 208

ASN 99 0.25 GLY 98 -0.25 GLY 226

ARG 116 0.26 ASN 99 -0.32 GLN 151

ARG 116 0.33 TYR 100 -0.40 GLN 151

ARG 103 0.32 LYS 101 -0.48 GLN 151

ARG 103 0.41 THR 102 -0.59 LEU 119

THR 102 0.41 ARG 103 -0.50 LYS 152

THR 91 0.30 ALA 104 -0.62 ILE 117

THR 91 0.33 GLU 105 -0.41 GLY 226

THR 91 0.30 VAL 106 -0.42 GLY 226

THR 91 0.28 LYS 107 -0.41 GLY 226

THR 91 0.25 PHE 108 -0.38 GLY 226

THR 102 0.27 GLU 109 -0.34 GLY 226

ASP 184 0.28 GLY 110 -0.32 GLY 226

ASP 184 0.29 ASP 111 -0.31 GLY 226

THR 102 0.25 THR 112 -0.32 GLY 226

THR 91 0.26 LEU 113 -0.37 GLY 226

THR 102 0.32 VAL 114 -0.36 GLY 226

THR 102 0.32 ASN 115 -0.41 GLY 226

ILE 117 0.41 ARG 116 -0.39 GLY 226

ARG 116 0.41 ILE 117 -0.62 ALA 104

TYR 100 0.28 GLU 118 -0.48 LYS 152

GLU 14 0.30 LEU 119 -0.60 GLU 89

GLU 14 0.21 LYS 120 -0.50 GLN 151

ARG 116 0.21 GLY 121 -0.40 GLN 151

ARG 116 0.20 ILE 122 -0.33 GLN 151

ARG 103 0.21 ASP 123 -0.23 GLY 226

GLY 128 0.14 PHE 124 -0.29 LYS 208

ASN 99 0.16 LYS 125 -0.41 LYS 208

ASP 167 0.15 GLU 126 -0.53 LYS 208

ASP 97 0.21 ASP 127 -0.63 LYS 208

PHE 94 0.25 GLY 128 -0.43 LYS 208

HIS 22 0.20 ASN 129 -0.37 LYS 208

HIS 22 0.25 ILE 130 -0.34 LYS 208

HIS 22 0.24 LEU 131 -0.47 LYS 208

ASP 167 0.26 GLY 132 -0.60 LYS 208

HIS 22 0.37 HIS 133 -0.54 LYS 208

ASP 167 0.29 LYS 134 -0.48 TYR 137

VAL 52 0.33 LEU 135 -0.32 GLY 222

LYS 49 0.32 GLU 136 -0.39 TYR 139

LYS 49 0.23 TYR 137 -0.48 LYS 134

LYS 49 0.15 ASN 138 -0.41 SER 196

THR 40 0.19 TYR 139 -0.39 ASN 143

THR 40 0.21 ASN 140 -0.54 SER 141

GLN 198 0.37 SER 141 -0.54 ASN 140

LYS 160 0.26 HIS 142 -0.60 ASN 143

VAL 218 0.20 ASN 143 -0.60 HIS 142

SER 66 0.20 VAL 144 -0.46 VAL 58

SER 66 0.16 TYR 145 -0.44 GLY 226

THR 35 0.13 ILE 146 -0.52 GLY 226

THR 35 0.15 MET 147 -0.56 GLY 226

ASP 149 0.24 ALA 148 -0.56 GLY 226

ALA 148 0.24 ASP 149 -0.49 LEU 119

ARG 74 0.28 LYS 150 -0.43 LEU 119

ARG 74 0.25 GLN 151 -0.50 LYS 120

ARG 74 0.17 LYS 152 -0.51 LEU 119

SER 80 0.19 ASN 153 -0.48 GLY 226

GLY 1 0.15 GLY 154 -0.51 GLY 226

THR 35 0.14 ILE 155 -0.51 GLY 226

THR 35 0.11 LYS 156 -0.46 GLY 226

PHE 65 0.15 VAL 157 -0.46 GLY 226

GLN 63 0.21 ASN 158 -0.41 GLY 226

GLN 63 0.27 PHE 159 -0.37 GLY 226

VAL 62 0.28 LYS 160 -0.31 GLY 226

VAL 62 0.28 ILE 161 -0.34 GLY 226

ILE 11 0.23 ARG 162 -0.30 GLY 226

LEU 12 0.19 HIS 163 -0.33 GLY 222

TRP 54 0.19 ASN 164 -0.33 GLY 222

VAL 52 0.24 ILE 165 -0.29 GLY 222

PRO 51 0.29 GLU 166 -0.31 THR 224

LYS 134 0.29 ASP 167 -0.28 THR 224

LYS 49 0.23 GLY 168 -0.31 THR 224

LYS 134 0.19 SER 169 -0.24 THR 224

LEU 12 0.17 VAL 170 -0.25 THR 224

GLY 128 0.19 GLN 171 -0.25 GLY 226

VAL 62 0.24 LEU 172 -0.25 GLY 226

VAL 62 0.30 ALA 173 -0.29 GLY 226

VAL 62 0.32 ASP 174 -0.31 GLY 226

VAL 62 0.31 HIS 175 -0.37 GLY 226

GLN 63 0.26 TYR 176 -0.43 ASP 149

TYR 176 0.21 GLN 177 -0.47 LEU 119

ASN 179 0.18 GLN 178 -0.54 LEU 119

GLN 178 0.18 ASN 179 -0.47 GLY 226

ASP 96 0.11 THR 180 -0.47 GLY 226

GLY 183 0.23 PRO 181 -0.48 GLY 226

GLU 3 0.11 ILE 182 -0.44 GLY 226

ALA 81 0.61 GLY 183 -0.34 LYS 23

GLY 1 0.45 ASP 184 -0.44 GLY 226

GLY 1 0.48 GLY 185 -0.45 GLY 226

GLU 3 0.32 PRO 186 -0.54 GLY 226

GLY 183 0.28 VAL 187 -0.61 GLY 226

LYS 150 0.23 LEU 188 -0.72 GLY 226

LYS 150 0.27 LEU 189 -0.70 GLY 226

LYS 150 0.24 PRO 190 -0.79 GLY 226

LYS 150 0.20 ASP 191 -0.83 GLY 226

ASP 149 0.12 ASN 192 -0.60 GLY 226

GLY 183 0.10 HIS 193 -0.55 GLY 226

GLY 183 0.13 TYR 194 -0.44 VAL 58

THR 35 0.15 LEU 195 -0.45 VAL 58

ASN 143 0.17 SER 196 -0.49 THR 197

LYS 160 0.24 THR 197 -0.49 SER 196

SER 141 0.37 GLN 198 -0.51 VAL 199

LEU 215 0.31 VAL 199 -0.51 GLN 198

ASN 140 0.20 ALA 200 -0.42 PRO 205

LYS 42 0.15 LEU 201 -0.41 GLN 198

LYS 42 0.10 SER 202 -0.42 LYS 203

GLY 48 0.12 LYS 203 -0.44 HIS 133

GLY 48 0.11 ASP 204 -0.51 LEU 215

ARG 209 0.39 PRO 205 -0.60 LEU 215

LYS 208 0.24 ASN 206 -0.48 THR 40

THR 47 0.16 GLU 207 -0.48 ASP 127

THR 46 0.30 LYS 208 -0.63 ASP 127

PRO 205 0.39 ARG 209 -0.51 ASP 127

PRO 205 0.38 ASP 210 -0.53 ASP 127

PRO 205 0.15 HIS 211 -0.43 ASP 127

ILE 44 0.12 MET 212 -0.37 GLY 226

LEU 201 0.14 VAL 213 -0.38 ASP 204

TYR 139 0.15 LEU 214 -0.41 THR 219

VAL 199 0.31 LEU 215 -0.60 PRO 205

SER 141 0.28 GLU 216 -0.47 PRO 205

SER 141 0.23 PHE 217 -0.51 PRO 205

PHE 159 0.23 VAL 218 -0.45 THR 219

GLY 183 0.18 THR 219 -0.45 PRO 205

GLY 183 0.17 ALA 220 -0.41 PRO 205

GLY 183 0.14 ALA 221 -0.40 PRO 205

GLY 183 0.11 GLY 222 -0.45 HIS 142

LYS 150 0.14 ILE 223 -0.41 HIS 142

LYS 150 0.14 THR 224 -0.39 HIS 142

THR 224 0.00 HIS 225 -0.44 MET 72

THR 224 0.05 GLY 226 -0.87 ARG 74

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.

*** 2QLE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 ***

CA distance fluctuations for 240220090021146876

--- normal mode 16 ---

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

* 2QLE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *