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

* 4XFX_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *

CA distance fluctuations for 240220091228160354

--- normal mode 7 ---

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 89 0.22 PRO 1 -0.37 GLU 207

GLY 89 0.23 ILE 2 -0.35 GLU 207

GLY 89 0.14 VAL 3 -0.34 GLU 207

GLN 107 0.12 GLN 4 -0.28 GLU 207

GLN 107 0.03 MET 5 -0.28 GLU 207

GLN 4 0.02 VAL 6 -0.23 GLU 207

GLN 4 0.03 HIS 7 -0.21 GLU 207

ALA 9 0.02 GLN 8 -0.19 GLU 207

GLN 4 0.03 ALA 9 -0.15 GLU 207

GLY 41 0.03 ILE 10 -0.14 GLU 207

GLY 41 0.03 SER 11 -0.11 GLU 207

GLY 41 0.02 PRO 12 -0.07 GLU 207

ALA 172 0.03 ARG 13 -0.07 THR 211

ALA 172 0.03 THR 14 -0.10 GLU 207

THR 105 0.02 LEU 15 -0.07 GLU 207

ALA 172 0.03 ASN 16 -0.06 VAL 3

ALA 172 0.04 ALA 17 -0.08 VAL 3

ALA 172 0.03 TRP 18 -0.07 VAL 3

THR 102 0.03 VAL 19 -0.05 VAL 3

GLN 174 0.04 LYS 20 -0.07 VAL 3

GLN 174 0.05 VAL 21 -0.08 VAL 3

ARG 162 0.04 VAL 22 -0.06 VAL 3

ASP 161 0.08 GLU 23 -0.05 VAL 3

ASP 161 0.09 GLU 24 -0.07 PRO 1

LYS 165 0.08 LYS 25 -0.08 PRO 1

ARG 162 0.09 ALA 26 -0.06 VAL 3

ARG 162 0.07 PHE 27 -0.06 PRO 1

ARG 168 0.07 SER 28 -0.09 PRO 1

ALA 172 0.08 PRO 29 -0.11 PRO 1

GLN 174 0.10 GLU 30 -0.12 PRO 1

ALA 172 0.05 VAL 31 -0.10 PRO 1

ALA 172 0.04 ILE 32 -0.13 TYR 164

SER 173 0.08 PRO 33 -0.21 ASP 161

SER 173 0.06 MET 34 -0.16 ASP 161

ALA 172 0.02 PHE 35 -0.14 GLU 207

ALA 37 0.03 SER 36 -0.21 GLU 207

SER 173 0.04 ALA 37 -0.23 GLU 207

ALA 172 0.03 LEU 38 -0.17 GLU 207

ARG 127 0.02 SER 39 -0.19 GLU 207

ARG 127 0.02 GLU 40 -0.24 GLU 207

SER 11 0.03 GLY 41 -0.25 GLU 207

ILE 10 0.02 ALA 42 -0.20 GLU 207

GLN 58 0.02 THR 43 -0.19 THR 205

GLN 58 0.04 PRO 44 -0.17 THR 205

GLN 58 0.05 GLN 45 -0.14 THR 205

GLN 58 0.03 ASP 46 -0.14 GLU 207

GLN 58 0.02 LEU 47 -0.13 THR 205

GLN 58 0.05 ASN 48 -0.10 THR 205

THR 105 0.04 THR 49 -0.09 THR 205

PRO 142 0.03 MET 50 -0.08 THR 205

THR 102 0.05 LEU 51 -0.07 THR 205

THR 105 0.06 ASN 52 -0.06 GLN 174

THR 105 0.05 THR 53 -0.04 THR 205

GLY 151 0.06 VAL 54 -0.03 GLN 174

GLU 154 0.09 GLY 55 -0.03 LEU 133

GLU 154 0.12 GLY 56 -0.03 SER 173

GLU 154 0.12 HIS 57 -0.04 SER 173

GLY 151 0.12 GLN 58 -0.06 SER 173

GLY 151 0.14 ALA 59 -0.07 SER 173

GLY 151 0.11 ALA 60 -0.07 SER 173

THR 102 0.09 MET 61 -0.08 SER 173

GLY 151 0.10 GLN 62 -0.10 SER 173

THR 143 0.11 MET 63 -0.12 SER 173

THR 143 0.07 LEU 64 -0.12 GLN 174

SER 97 0.09 LYS 65 -0.13 GLN 174

THR 143 0.09 GLU 66 -0.15 SER 173

THR 143 0.08 THR 67 -0.18 GLN 174

THR 143 0.05 ILE 68 -0.18 GLN 174

THR 143 0.07 ASN 69 -0.18 GLN 174

THR 143 0.07 GLU 70 -0.20 GLN 174

THR 143 0.04 GLU 71 -0.24 GLN 174

THR 143 0.04 ALA 72 -0.21 GLN 174

THR 143 0.05 ALA 73 -0.21 GLN 174

THR 143 0.03 GLU 74 -0.26 GLN 174

ASN 69 0.02 TRP 75 -0.27 GLN 174

ASN 69 0.04 ASP 76 -0.23 GLN 174

ILE 2 0.03 ARG 77 -0.25 GLN 174

PRO 117 0.02 LEU 78 -0.29 GLN 174

ILE 2 0.03 HIS 79 -0.26 GLN 174

ILE 2 0.05 PRO 80 -0.23 GLN 174

ILE 2 0.07 VAL 81 -0.21 GLN 174

PRO 1 0.08 HIS 82 -0.22 GLY 203

PRO 1 0.08 ALA 83 -0.21 GLY 203

PRO 1 0.10 GLY 84 -0.21 GLY 203

PRO 1 0.12 PRO 85 -0.20 GLY 203

PRO 1 0.13 ILE 86 -0.21 GLY 203

PRO 1 0.16 ALA 87 -0.23 GLY 203

PRO 1 0.20 PRO 88 -0.21 GLY 203

ILE 2 0.23 GLY 89 -0.22 THR 205

ILE 2 0.18 GLN 90 -0.23 THR 205

ILE 2 0.16 MET 91 -0.22 THR 205

ILE 2 0.12 ARG 92 -0.21 THR 205

ILE 2 0.08 GLU 93 -0.23 THR 205

ILE 2 0.07 PRO 94 -0.21 THR 205

ILE 2 0.05 ARG 95 -0.21 GLN 174

LYS 65 0.06 GLY 96 -0.21 GLN 174

LYS 65 0.09 SER 97 -0.17 GLN 174

LYS 65 0.07 ASP 98 -0.17 GLN 174

LYS 65 0.05 ILE 99 -0.19 GLN 174

LYS 65 0.07 ALA 100 -0.16 GLN 174

GLN 58 0.07 GLY 101 -0.14 THR 205

GLN 62 0.10 THR 102 -0.13 GLN 174

GLN 58 0.09 THR 103 -0.14 GLN 174

ILE 2 0.09 SER 104 -0.15 THR 205

ILE 2 0.11 THR 105 -0.15 THR 205

ILE 2 0.10 LEU 106 -0.16 THR 205

ILE 2 0.15 GLN 107 -0.18 THR 205

ILE 2 0.13 GLU 108 -0.19 THR 205

ILE 2 0.08 GLN 109 -0.20 THR 205

ILE 2 0.08 ILE 110 -0.22 THR 205

ILE 2 0.14 GLY 111 -0.23 THR 205

ILE 2 0.07 TRP 112 -0.25 THR 205

GLN 58 0.02 MET 113 -0.27 THR 205

VAL 3 0.03 THR 114 -0.28 THR 205

VAL 3 0.06 HIS 115 -0.28 THR 205

VAL 3 0.04 ASN 116 -0.31 THR 205

HIS 79 0.02 PRO 117 -0.33 THR 205

HIS 79 0.02 PRO 118 -0.31 THR 205

LYS 65 0.02 ILE 119 -0.28 THR 205

THR 43 0.02 PRO 120 -0.28 THR 205

LYS 65 0.03 VAL 121 -0.24 THR 205

LYS 65 0.02 GLY 122 -0.23 THR 205

TYR 125 0.02 GLU 123 -0.26 THR 205

LYS 65 0.02 ILE 124 -0.26 GLN 174

LYS 65 0.02 TYR 125 -0.20 GLN 174

ARG 127 0.02 LYS 126 -0.20 THR 205

GLU 40 0.02 ARG 127 -0.25 GLN 174

GLU 40 0.01 TRP 128 -0.23 GLN 174

SER 144 0.03 ILE 129 -0.16 GLN 174

LEU 131 0.03 ILE 130 -0.16 THR 205

ALA 37 0.03 LEU 131 -0.22 GLN 174

SER 144 0.05 GLY 132 -0.15 GLN 174

SER 144 0.04 LEU 133 -0.09 ARG 168

SER 144 0.04 ASN 134 -0.13 ARG 168

SER 144 0.08 LYS 135 -0.13 SER 173

THR 143 0.08 ILE 136 -0.07 SER 173

GLY 151 0.05 VAL 137 -0.07 PRO 1

SER 144 0.11 ARG 138 -0.08 MET 139

THR 143 0.15 MET 139 -0.08 ARG 138

ARG 162 0.17 TYR 140 -0.06 PRO 1

TYR 140 0.16 SER 141 -0.08 PRO 1

THR 143 0.17 PRO 142 -0.07 PRO 1

PRO 142 0.17 THR 143 -0.09 PRO 1

MET 139 0.11 SER 144 -0.09 PRO 1

TYR 140 0.09 ILE 145 -0.13 PRO 1

MET 139 0.07 LEU 146 -0.12 PRO 1

MET 139 0.11 ASP 147 -0.11 PRO 1

TYR 140 0.12 ILE 148 -0.14 PRO 1

PRO 142 0.12 ARG 149 -0.16 PRO 1

TYR 140 0.12 GLN 150 -0.18 PRO 1

ALA 59 0.14 GLY 151 -0.17 PRO 1

ALA 59 0.13 PRO 152 -0.18 PRO 1

ALA 59 0.13 LYS 153 -0.19 PRO 1

ALA 59 0.13 GLU 154 -0.20 PRO 1

TYR 140 0.12 PRO 155 -0.23 PRO 1

TYR 140 0.11 PHE 156 -0.25 PRO 1

TYR 140 0.11 ARG 157 -0.26 PRO 1

TYR 140 0.14 ASP 158 -0.22 PRO 1

TYR 140 0.13 TYR 159 -0.21 PRO 1

TYR 140 0.11 VAL 160 -0.24 PRO 1

TYR 140 0.13 ASP 161 -0.23 PRO 1

TYR 140 0.17 ARG 162 -0.18 PRO 1

TYR 140 0.13 PHE 163 -0.19 PRO 1

TYR 140 0.10 TYR 164 -0.21 PRO 1

TYR 140 0.12 LYS 165 -0.17 PRO 1

TYR 140 0.14 THR 166 -0.14 PRO 1

TYR 140 0.08 LEU 167 -0.17 PRO 1

SER 28 0.07 ARG 168 -0.18 ARG 127

SER 28 0.07 ALA 169 -0.12 PRO 1

ALA 172 0.05 GLU 170 -0.12 PRO 1

GLU 30 0.08 GLN 171 -0.13 LEU 131

GLU 30 0.09 ALA 172 -0.16 LEU 78

GLU 30 0.10 SER 173 -0.26 LEU 78

GLU 30 0.10 GLN 174 -0.29 LEU 78

GLU 30 0.07 GLU 175 -0.27 LEU 78

GLU 30 0.06 VAL 176 -0.20 LEU 78

GLU 24 0.06 LYS 177 -0.20 LEU 78

GLU 24 0.07 ASN 178 -0.24 PRO 117

GLU 24 0.05 TRP 179 -0.21 PRO 1

GLU 24 0.05 MET 180 -0.20 PRO 1

GLU 24 0.07 THR 181 -0.24 PRO 1

GLU 24 0.06 GLU 182 -0.25 PRO 1

GLU 24 0.05 THR 183 -0.22 PRO 1

TYR 140 0.05 LEU 184 -0.19 PRO 1

TYR 140 0.07 LEU 185 -0.22 PRO 1

TYR 140 0.07 VAL 186 -0.23 PRO 1

TYR 140 0.06 GLN 187 -0.19 PRO 1

TYR 140 0.08 ASN 188 -0.18 PRO 1

TYR 140 0.09 ALA 189 -0.20 PRO 1

TYR 140 0.10 ASN 190 -0.20 PRO 1

ALA 59 0.08 PRO 191 -0.20 PRO 1

ALA 59 0.08 ASP 192 -0.23 PRO 1

TYR 140 0.08 CYS 193 -0.24 PRO 1

TYR 140 0.07 LYS 194 -0.23 PRO 1

TYR 140 0.06 THR 195 -0.24 PRO 1

TYR 140 0.06 ILE 196 -0.27 PRO 1

TYR 140 0.06 LEU 197 -0.27 PRO 1

TYR 140 0.05 LYS 198 -0.26 PRO 1

TYR 140 0.05 ALA 199 -0.28 PRO 1

GLU 24 0.05 LEU 200 -0.31 PRO 1

GLU 24 0.05 GLY 201 -0.30 PRO 1

GLU 24 0.06 PRO 202 -0.30 PRO 1

GLU 24 0.06 GLY 203 -0.34 PRO 1

GLU 24 0.07 ALA 204 -0.34 PRO 1

GLU 24 0.07 THR 205 -0.37 PRO 1

GLU 24 0.08 LEU 206 -0.34 PRO 1

GLU 24 0.09 GLU 207 -0.37 PRO 1

GLU 24 0.07 GLU 208 -0.36 PRO 1

GLU 24 0.07 MET 209 -0.32 PRO 1

GLU 24 0.08 MET 210 -0.32 PRO 1

GLU 24 0.07 THR 211 -0.34 PRO 1

TYR 140 0.07 ALA 212 -0.32 PRO 1

TYR 140 0.08 CYS 213 -0.29 PRO 1

TYR 140 0.08 GLN 214 -0.30 PRO 1

TYR 140 0.09 GLY 215 -0.27 PRO 1

ALA 59 0.09 VAL 216 -0.25 PRO 1

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.

*** 4XFX_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 ***

CA distance fluctuations for 240220091228160354

--- normal mode 7 ---

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

* 4XFX_unrelaxed_rank_001_alphafold2_ptm_model_4_seed_000 *