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 9 ---

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
THR 91 0.13 GLY 1 -0.50 ASN 206

ARG 67 0.14 GLU 2 -0.52 ASN 206

ARG 67 0.13 GLU 3 -0.59 ASN 206

ARG 67 0.10 LEU 4 -0.64 ASN 206

CYS 64 0.09 PHE 5 -0.63 ASN 206

ARG 67 0.08 THR 6 -0.66 ASN 206

ASP 111 0.13 GLY 7 -0.73 ASN 206

VAL 9 0.12 VAL 8 -0.82 ASN 206

VAL 8 0.12 VAL 9 -0.77 ASN 206

ASN 115 0.10 PRO 10 -0.83 ASN 206

GLU 31 0.14 ILE 11 -0.62 ASN 206

LEU 39 0.08 LEU 12 -0.53 ASN 206

GLY 30 0.09 VAL 13 -0.34 ASN 206

THR 40 0.07 GLU 14 -0.24 ASN 206

GLY 222 0.07 LEU 15 -0.12 ASN 206

LYS 208 0.11 ASP 16 -0.11 GLY 17

ARG 103 0.17 GLY 17 -0.11 ASP 16

GLN 151 0.24 ASP 18 -0.07 GLY 98

GLN 151 0.28 VAL 19 -0.08 SER 27

GLN 151 0.32 ASN 20 -0.07 SER 27

GLN 151 0.28 GLY 21 -0.06 SER 27

GLN 151 0.23 HIS 22 -0.08 SER 27

LYS 208 0.19 LYS 23 -0.08 HIS 22

LYS 208 0.20 PHE 24 -0.13 SER 25

LYS 208 0.13 SER 25 -0.13 PHE 24

LYS 208 0.07 VAL 26 -0.15 THR 112

LEU 215 0.05 SER 27 -0.24 ASN 206

LEU 215 0.07 GLY 28 -0.36 ASN 206

THR 40 0.12 GLU 29 -0.59 ASN 206

THR 40 0.10 GLY 30 -0.73 ASN 206

ILE 11 0.14 GLU 31 -0.76 ASN 206

ASN 115 0.10 GLY 32 -0.62 ASN 206

LEU 113 0.09 ASP 33 -0.63 ASN 206

PHE 65 0.09 ALA 34 -0.52 ASN 206

ASP 111 0.08 THR 35 -0.53 ASN 206

ASP 111 0.07 TYR 36 -0.47 ASN 206

ASP 33 0.07 GLY 37 -0.41 ARG 67

GLY 32 0.08 LYS 38 -0.45 ASN 206

GLY 30 0.09 LEU 39 -0.44 ASN 206

GLU 29 0.12 THR 40 -0.58 ASP 204

GLU 29 0.11 LEU 41 -0.42 GLU 31

LEU 214 0.15 LYS 42 -0.52 GLY 30

ALA 200 0.07 PHE 43 -0.31 PRO 10

SER 141 0.07 ILE 44 -0.29 PRO 10

LYS 208 0.16 CYS 45 -0.21 PRO 10

LYS 208 0.11 THR 46 -0.22 GLY 110

LYS 208 0.20 THR 47 -0.17 GLY 110

LYS 208 0.35 GLY 48 -0.19 PRO 10

LYS 208 0.42 LYS 49 -0.20 PRO 10

LYS 208 0.32 LEU 50 -0.17 PRO 10

LYS 208 0.30 PRO 51 -0.14 PRO 10

LYS 208 0.27 VAL 52 -0.14 GLU 31

PRO 205 0.32 PRO 53 -0.15 THR 40

PRO 205 0.22 TRP 54 -0.19 GLU 31

PRO 205 0.22 PRO 55 -0.18 LEU 215

GLN 177 0.24 THR 56 -0.12 LEU 41

GLN 177 0.20 LEU 57 -0.10 LEU 41

GLN 177 0.13 VAL 58 -0.11 LEU 41

GLY 222 0.15 THR 59 -0.09 LEU 41

GLN 177 0.12 THR 60 -0.08 LEU 41

GLY 222 0.08 PHE 61 -0.19 ASN 206

GLY 32 0.10 VAL 62 -0.28 ASN 206

ALA 34 0.09 GLN 63 -0.29 ASN 206

PHE 5 0.09 CYS 64 -0.40 ASN 206

ALA 34 0.09 PHE 65 -0.45 ASN 206

PHE 159 0.09 SER 66 -0.36 ASN 206

GLU 2 0.14 ARG 67 -0.41 GLY 37

PHE 159 0.13 TYR 68 -0.37 ASN 206

PHE 159 0.13 PRO 69 -0.40 ASN 206

PHE 159 0.14 ASP 70 -0.45 ASN 206

PHE 159 0.18 HIS 71 -0.37 ASN 206

PHE 159 0.21 MET 72 -0.34 ASN 206

PHE 159 0.17 LYS 73 -0.41 ASN 206

TYR 176 0.19 ARG 74 -0.55 GLY 226

TYR 176 0.23 HIS 75 -0.40 GLY 226

TYR 176 0.19 ASP 76 -0.36 ASN 206

TYR 176 0.20 PHE 77 -0.32 ASN 206

THR 91 0.15 PHE 78 -0.36 ASN 206

THR 91 0.14 LYS 79 -0.45 ASN 206

THR 91 0.16 SER 80 -0.42 ASN 206

THR 91 0.17 ALA 81 -0.39 ASN 206

THR 91 0.12 MET 82 -0.48 ASN 206

LYS 101 0.10 PRO 83 -0.51 ASN 206

LYS 101 0.13 GLU 84 -0.44 ASN 206

LYS 101 0.12 GLY 85 -0.40 ASN 206

LYS 101 0.19 TYR 86 -0.30 ASN 206

LYS 120 0.19 VAL 87 -0.22 ASN 206

LYS 101 0.22 GLN 88 -0.16 ASN 206

LYS 101 0.33 GLU 89 -0.13 GLN 177

TYR 100 0.35 ARG 90 -0.09 TYR 176

GLN 178 0.45 THR 91 -0.10 THR 102

LYS 156 0.39 ILE 92 -0.08 LEU 41

LYS 156 0.41 PHE 93 -0.14 ALA 173

ASP 149 0.34 PHE 94 -0.09 ARG 162

ASP 149 0.37 LYS 95 -0.09 ILE 122

GLN 151 0.41 ASP 96 -0.09 VAL 170

GLN 151 0.39 ASP 97 -0.10 LEU 215

GLN 151 0.40 GLY 98 -0.10 ILE 122

GLN 151 0.40 ASN 99 -0.09 PHE 94

GLN 178 0.36 TYR 100 -0.08 LEU 41

GLN 178 0.36 LYS 101 -0.09 GLU 118

GLU 89 0.27 THR 102 -0.10 THR 91

LYS 120 0.26 ARG 103 -0.09 ASN 206

GLU 105 0.13 ALA 104 -0.18 ASN 206

LYS 120 0.13 GLU 105 -0.26 ASN 206

LYS 107 0.13 VAL 106 -0.35 ASN 206

VAL 106 0.13 LYS 107 -0.44 ASN 206

GLY 7 0.10 PHE 108 -0.55 ASN 206

GLY 7 0.10 GLU 109 -0.58 ASN 206

GLY 7 0.11 GLY 110 -0.68 ASN 206

GLY 7 0.13 ASP 111 -0.75 ASN 206

VAL 8 0.11 THR 112 -0.71 ASN 206

THR 112 0.11 LEU 113 -0.57 ASN 206

ASN 115 0.09 VAL 114 -0.47 ASN 206

GLY 32 0.10 ASN 115 -0.33 ASN 206

GLY 32 0.08 ARG 116 -0.25 ASN 206

GLY 32 0.07 ILE 117 -0.14 ASN 206

GLY 17 0.14 GLU 118 -0.09 LYS 101

ARG 103 0.25 LEU 119 -0.06 TYR 100

LYS 152 0.30 LYS 120 -0.07 ASP 16

GLN 151 0.34 GLY 121 -0.08 LEU 41

GLN 151 0.40 ILE 122 -0.10 GLY 98

GLN 151 0.43 ASP 123 -0.07 LEU 41

GLN 151 0.36 PHE 124 -0.10 LEU 215

GLN 151 0.36 LYS 125 -0.10 LEU 215

GLN 151 0.31 GLU 126 -0.11 LEU 215

GLN 151 0.30 ASP 127 -0.13 LEU 215

GLN 151 0.32 GLY 128 -0.11 LEU 215

PRO 205 0.31 ASN 129 -0.14 LEU 215

PRO 205 0.29 ILE 130 -0.14 LEU 215

PRO 205 0.29 LEU 131 -0.13 LEU 215

PRO 205 0.34 GLY 132 -0.14 LEU 215

PRO 205 0.39 HIS 133 -0.16 LEU 215

PRO 205 0.40 LYS 134 -0.17 LEU 215

PRO 205 0.40 LEU 135 -0.17 LEU 215

PRO 205 0.45 GLU 136 -0.22 ALA 200

PRO 205 0.41 TYR 137 -0.21 LEU 215

PRO 205 0.27 ASN 138 -0.30 ALA 200

PRO 205 0.22 TYR 139 -0.19 VAL 199

THR 224 0.22 ASN 140 -0.16 GLN 198

THR 224 0.22 SER 141 -0.11 GLN 198

THR 224 0.29 HIS 142 -0.07 LYS 160

THR 224 0.29 ASN 143 -0.03 GLN 178

ILE 223 0.25 VAL 144 -0.06 ASN 206

PHE 159 0.46 TYR 145 -0.07 GLN 178

PHE 159 0.35 ILE 146 -0.13 ASN 206

TYR 176 0.36 MET 147 -0.14 ASN 206

TYR 176 0.36 ALA 148 -0.22 GLY 226

TYR 176 0.43 ASP 149 -0.22 GLY 226

ASP 123 0.36 LYS 150 -0.31 GLY 226

ASP 123 0.43 GLN 151 -0.27 GLY 226

ASP 123 0.39 LYS 152 -0.25 GLY 226

THR 91 0.32 ASN 153 -0.31 GLY 226

THR 91 0.34 GLY 154 -0.25 GLY 226

TYR 176 0.37 ILE 155 -0.17 ASN 206

TYR 176 0.58 LYS 156 -0.09 ASN 206

TYR 176 0.29 VAL 157 -0.10 GLN 178

ASP 174 0.41 ASN 158 -0.11 GLU 89

TYR 145 0.46 PHE 159 -0.04 TYR 176

THR 224 0.33 LYS 160 -0.07 HIS 142

THR 224 0.30 ILE 161 -0.09 PHE 93

THR 224 0.29 ARG 162 -0.13 LEU 172

PRO 205 0.27 HIS 163 -0.14 LEU 215

PRO 205 0.33 ASN 164 -0.17 ALA 200

PRO 205 0.37 ILE 165 -0.17 ALA 200

PRO 205 0.45 GLU 166 -0.18 ALA 200

PRO 205 0.40 ASP 167 -0.16 ALA 200

PRO 205 0.36 GLY 168 -0.15 ALA 200

PRO 205 0.31 SER 169 -0.13 LEU 215

GLY 226 0.29 VAL 170 -0.12 LEU 215

PRO 205 0.27 GLN 171 -0.12 LEU 215

THR 224 0.32 LEU 172 -0.13 ARG 162

LYS 156 0.29 ALA 173 -0.14 PHE 93

ASN 158 0.41 ASP 174 -0.08 LEU 41

LYS 156 0.38 HIS 175 -0.08 LEU 41

LYS 156 0.58 TYR 176 -0.09 ARG 90

THR 91 0.41 GLN 177 -0.13 GLU 89

THR 91 0.45 GLN 178 -0.10 VAL 157

THR 91 0.31 ASN 179 -0.18 ASN 206

LYS 101 0.27 THR 180 -0.22 ASN 206

LYS 101 0.23 PRO 181 -0.29 ASN 206

LYS 101 0.20 ILE 182 -0.31 ASN 206

ASP 123 0.18 GLY 183 -0.37 ASN 206

ASP 123 0.23 ASP 184 -0.35 GLY 226

ASP 123 0.19 GLY 185 -0.40 GLY 226

THR 91 0.24 PRO 186 -0.46 GLY 226

THR 91 0.23 VAL 187 -0.43 GLY 226

TYR 176 0.24 LEU 188 -0.47 GLY 226

TYR 176 0.28 LEU 189 -0.41 GLY 226

TYR 176 0.27 PRO 190 -0.34 GLY 226

ASP 174 0.30 ASP 191 -0.25 GLY 226

ASP 174 0.36 ASN 192 -0.13 ASN 206

ILE 223 0.34 HIS 193 -0.14 ASN 206

PHE 159 0.33 TYR 194 -0.11 ASN 206

THR 224 0.17 LEU 195 -0.14 ASN 206

THR 224 0.20 SER 196 -0.10 ASN 206

THR 224 0.15 THR 197 -0.10 ASN 206

THR 224 0.12 GLN 198 -0.16 ASN 140

THR 224 0.11 VAL 199 -0.19 TYR 139

LYS 42 0.12 ALA 200 -0.30 ASN 138

SER 141 0.15 LEU 201 -0.31 LEU 215

TYR 139 0.13 SER 202 -0.32 THR 40

TYR 137 0.25 LYS 203 -0.44 GLU 31

TYR 137 0.16 ASP 204 -0.66 GLU 31

GLU 166 0.45 PRO 205 -0.75 VAL 8

GLU 166 0.32 ASN 206 -0.83 PRO 10

ARG 209 0.22 GLU 207 -0.63 PRO 10

LYS 49 0.42 LYS 208 -0.46 PRO 10

LYS 208 0.32 ARG 209 -0.35 PRO 10

LYS 208 0.34 ASP 210 -0.28 PRO 10

PRO 205 0.13 HIS 211 -0.30 PRO 10

TYR 139 0.13 MET 212 -0.31 GLU 31

ALA 200 0.10 VAL 213 -0.39 THR 40

LYS 42 0.15 LEU 214 -0.29 THR 40

GLU 29 0.10 LEU 215 -0.31 LEU 201

GLU 29 0.09 GLU 216 -0.23 ASN 206

GLY 32 0.09 PHE 217 -0.26 ASN 206

GLY 32 0.06 VAL 218 -0.24 ASN 206

PHE 159 0.08 THR 219 -0.26 ASN 206

PHE 159 0.17 ALA 220 -0.23 ASN 206

THR 224 0.22 ALA 221 -0.18 ASN 206

PHE 159 0.35 GLY 222 -0.11 ASN 206

PHE 159 0.35 ILE 223 -0.16 ASN 206

PHE 159 0.34 THR 224 -0.17 ARG 74

LYS 95 0.28 HIS 225 -0.36 ARG 74

LYS 95 0.29 GLY 226 -0.55 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 9 ---

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

* 2QLE_unrelaxed_rank_001_alphafold2_ptm_model_5_seed_000 *