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

* 1R88_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *

CA distance fluctuations for 240220085926145927

--- normal mode 11 ---

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 25 0.46 ALA 1 -0.50 THR 47

GLY 25 0.67 ALA 2 -0.31 PRO 253

GLY 101 0.32 PRO 3 -0.33 ALA 257

GLY 101 0.29 TYR 4 -0.32 ALA 56

GLY 101 0.23 GLU 5 -0.35 GLY 57

ASP 41 0.25 ASN 6 -0.27 ALA 1

ASP 41 0.23 LEU 7 -0.33 GLY 57

TRP 177 0.24 MET 8 -0.27 GLY 57

TRP 177 0.27 VAL 9 -0.29 GLY 57

TRP 177 0.32 PRO 10 -0.25 GLY 57

TRP 177 0.37 SER 11 -0.24 GLY 25

TRP 177 0.42 PRO 12 -0.21 TRP 95

TRP 177 0.45 SER 13 -0.22 ASP 94

TRP 177 0.37 MET 14 -0.25 ALA 1

TRP 177 0.36 GLY 15 -0.25 ALA 1

TRP 177 0.30 ARG 16 -0.29 ALA 1

TRP 177 0.28 ASP 17 -0.29 ALA 1

TRP 177 0.25 ILE 18 -0.31 ALA 1

ALA 38 0.21 PRO 19 -0.32 ALA 1

ALA 38 0.20 VAL 20 -0.27 ALA 1

SER 43 0.18 ALA 21 -0.25 VAL 20

GLY 101 0.19 PHE 22 -0.30 GLY 57

ALA 2 0.39 LEU 23 -0.34 GLY 57

ALA 2 0.47 ALA 24 -0.44 GLY 57

ALA 2 0.67 GLY 25 -0.39 ARG 100

ALA 2 0.50 GLY 26 -0.38 ARG 100

ALA 2 0.44 PRO 27 -0.34 LEU 102

ALA 2 0.37 HIS 28 -0.24 LEU 92

ALA 2 0.32 ALA 29 -0.25 LEU 92

ALA 2 0.21 VAL 30 -0.21 TRP 84

ALA 2 0.13 TYR 31 -0.22 TRP 84

SER 205 0.15 LEU 32 -0.22 THR 163

ALA 214 0.11 LEU 33 -0.26 THR 163

ALA 209 0.15 ASP 34 -0.31 ALA 169

ALA 66 0.15 ALA 35 -0.34 ALA 169

ILE 18 0.19 PHE 36 -0.45 ALA 169

ALA 208 0.20 ASN 37 -0.45 ALA 169

ALA 66 0.28 ALA 38 -0.38 ALA 169

ALA 208 0.20 GLY 39 -0.39 VAL 161

LEU 7 0.21 PRO 40 -0.37 VAL 161

ASN 6 0.25 ASP 41 -0.33 SER 81

ASN 6 0.19 VAL 42 -0.38 ALA 1

ALA 21 0.18 SER 43 -0.32 ALA 1

ASP 206 0.20 ASN 44 -0.35 ALA 1

ASP 206 0.16 TRP 45 -0.31 ALA 1

VAL 62 0.18 VAL 46 -0.42 ALA 1

GLY 25 0.18 THR 47 -0.50 ALA 1

SER 205 0.20 ALA 48 -0.41 ALA 1

SER 205 0.18 GLY 49 -0.36 ALA 1

GLY 25 0.21 ASN 50 -0.43 ALA 1

GLY 25 0.21 ALA 51 -0.34 ALA 257

GLY 25 0.28 MET 52 -0.34 ALA 257

GLY 25 0.32 ASN 53 -0.35 ALA 257

GLY 57 0.18 THR 54 -0.47 ALA 257

ARG 267 0.19 LEU 55 -0.34 ALA 257

GLY 25 0.34 ALA 56 -0.32 TYR 4

ALA 1 0.41 GLY 57 -0.44 ALA 24

ARG 267 0.26 LYS 58 -0.36 ALA 24

ALA 2 0.39 GLY 59 -0.31 ARG 100

ALA 2 0.37 ILE 60 -0.30 ARG 100

ALA 2 0.45 SER 61 -0.29 ILE 60

ALA 2 0.30 VAL 62 -0.25 SER 259

ALA 2 0.15 VAL 63 -0.23 SER 81

ASP 206 0.15 ALA 64 -0.23 SER 81

ALA 38 0.17 PRO 65 -0.25 SER 81

ALA 38 0.28 ALA 66 -0.31 ALA 1

ILE 18 0.20 GLY 67 -0.32 ALA 169

ILE 18 0.24 GLY 68 -0.34 ALA 169

ILE 18 0.25 ALA 69 -0.41 ALA 169

ILE 18 0.19 TYR 70 -0.51 ALA 169

GLY 159 0.21 SER 71 -0.40 THR 163

PHE 139 0.27 MET 72 -0.31 ALA 169

PHE 139 0.23 TYR 73 -0.24 MET 166

HIS 178 0.35 THR 74 -0.20 ARG 129

HIS 178 0.46 ASN 75 -0.22 ASP 85

PRO 142 0.37 TRP 76 -0.24 GLY 165

SER 230 0.31 GLU 77 -0.23 GLY 105

ASN 148 0.35 GLN 78 -0.25 ALA 1

ASN 148 0.32 ASP 79 -0.29 PRO 40

TRP 177 0.32 GLY 80 -0.26 ALA 1

HIS 178 0.28 SER 81 -0.33 ASP 41

HIS 178 0.32 LYS 82 -0.28 ALA 1

HIS 178 0.42 GLN 83 -0.23 GLN 78

HIS 178 0.38 TRP 84 -0.22 TYR 31

HIS 178 0.45 ASP 85 -0.22 ASN 75

TRP 177 0.46 THR 86 -0.23 GLN 78

TRP 177 0.38 PHE 87 -0.22 GLY 80

TRP 177 0.31 LEU 88 -0.21 ALA 29

PHE 125 0.33 SER 89 -0.24 GLY 105

TRP 177 0.33 ALA 90 -0.24 PRO 104

TRP 177 0.36 GLU 91 -0.21 ASP 94

TRP 177 0.30 LEU 92 -0.25 ALA 29

HIS 126 0.28 PRO 93 -0.22 HIS 28

HIS 126 0.29 ASP 94 -0.22 SER 13

TRP 177 0.28 TRP 95 -0.22 SER 11

TRP 177 0.22 LEU 96 -0.29 PRO 27

ALA 2 0.26 ALA 97 -0.22 PRO 27

TRP 177 0.24 ALA 98 -0.19 PRO 27

TRP 177 0.22 ASN 99 -0.29 GLY 25

ALA 2 0.24 ARG 100 -0.39 GLY 25

ALA 2 0.37 GLY 101 -0.29 PRO 27

ALA 2 0.37 LEU 102 -0.34 PRO 27

ALA 2 0.37 ALA 103 -0.20 GLN 78

ALA 2 0.29 PRO 104 -0.24 ALA 90

ALA 2 0.28 GLY 105 -0.24 SER 89

ALA 2 0.26 GLY 106 -0.20 GLU 77

ALA 2 0.25 HIS 107 -0.20 ASN 75

ALA 2 0.17 ALA 108 -0.19 TRP 84

ALA 2 0.11 ALA 109 -0.18 MET 166

TRP 251 0.12 VAL 110 -0.17 THR 163

PRO 93 0.10 GLY 111 -0.20 ALA 169

ALA 214 0.12 ALA 112 -0.23 ALA 169

ALA 214 0.14 ALA 113 -0.27 ALA 169

ALA 217 0.21 GLN 114 -0.31 ALA 169

MET 8 0.14 GLY 115 -0.26 ALA 169

LEU 88 0.13 GLY 116 -0.16 ALA 169

ASP 85 0.19 TYR 117 -0.15 ALA 169

LEU 88 0.24 GLY 118 -0.18 ALA 169

LEU 88 0.14 ALA 119 -0.16 THR 163

LEU 88 0.19 MET 120 -0.08 LEU 186

ASP 85 0.25 ALA 121 -0.12 ALA 152

LEU 88 0.28 LEU 122 -0.17 MET 166

PRO 93 0.20 ALA 123 -0.11 GLU 77

SER 89 0.29 ALA 124 -0.09 ALA 152

SER 89 0.33 PHE 125 -0.12 ALA 152

ASP 94 0.29 HIS 126 -0.20 GLU 77

ASP 94 0.23 PRO 127 -0.14 GLU 77

ASP 94 0.23 ASP 128 -0.21 GLU 77

ALA 2 0.21 ARG 129 -0.22 GLU 77

ALA 2 0.19 PHE 130 -0.19 GLU 77

GLN 171 0.18 GLY 131 -0.14 GLU 77

GLN 171 0.17 PHE 132 -0.14 ALA 108

GLN 171 0.16 ALA 133 -0.11 ALA 188

GLN 171 0.12 GLY 134 -0.13 GLY 233

GLN 171 0.10 SER 135 -0.15 ALA 1

ALA 214 0.08 MET 136 -0.20 ALA 1

ASP 85 0.11 SER 137 -0.18 ALA 1

ASP 85 0.16 GLY 138 -0.16 ALA 1

MET 72 0.27 PHE 139 -0.20 TYR 141

THR 74 0.27 LEU 140 -0.18 HIS 183

ASN 164 0.35 TYR 141 -0.20 PHE 139

ASN 164 0.40 PRO 142 -0.23 LYS 176

ASN 164 0.49 SER 143 -0.42 LYS 176

ASN 164 0.49 ASN 144 -0.31 LYS 176

ASN 164 0.53 THR 145 -0.48 GLY 173

ASP 162 0.44 THR 146 -0.38 GLY 173

ASP 162 0.44 THR 147 -0.30 GLY 173

THR 163 0.57 ASN 148 -0.46 GLY 173

ASP 162 0.58 GLY 149 -0.67 GLY 173

ASP 162 0.40 ALA 150 -0.49 GLY 173

ASP 162 0.35 ILE 151 -0.56 PRO 170

ASP 162 0.51 ALA 152 -0.90 PRO 170

ALA 215 0.31 ALA 153 -0.87 GLN 171

GLN 213 0.29 GLY 154 -0.65 GLN 171

GLU 216 0.25 MET 155 -0.70 ALA 169

GLU 216 0.24 GLN 156 -0.80 ALA 169

PRO 202 0.21 GLN 157 -0.75 GLN 171

ILE 18 0.21 PHE 158 -0.58 GLN 171

LYS 82 0.25 GLY 159 -0.52 ALA 169

SER 81 0.23 GLY 160 -0.55 GLN 171

GLY 149 0.39 VAL 161 -0.47 ALA 169

GLY 149 0.58 ASP 162 -0.60 ALA 169

ASN 148 0.57 THR 163 -0.57 ALA 169

ASN 148 0.56 ASN 164 -0.40 ASP 162

ASN 148 0.43 GLY 165 -0.34 PRO 40

ASN 148 0.40 MET 166 -0.30 SER 71

TRP 175 0.39 TRP 167 -0.26 TYR 70

SER 230 0.44 GLY 168 -0.42 GLN 156

SER 230 0.51 ALA 169 -0.80 GLN 156

SER 230 0.61 PRO 170 -0.90 ALA 152

SER 230 0.90 GLN 171 -0.87 ALA 153

SER 230 0.78 LEU 172 -0.71 ALA 153

VAL 231 0.77 GLY 173 -0.67 GLY 149

VAL 231 0.55 ARG 174 -0.50 ALA 152

SER 230 0.43 TRP 175 -0.37 ALA 152

VAL 182 0.67 LYS 176 -0.42 THR 145

HIS 183 0.49 TRP 177 -0.36 THR 145

ASN 75 0.46 HIS 178 -0.16 ALA 152

ASN 75 0.40 ASP 179 -0.14 THR 145

GLN 171 0.37 PRO 180 -0.13 LEU 140

GLN 171 0.57 TRP 181 -0.20 HIS 183

GLN 171 0.71 VAL 182 -0.19 GLU 216

GLY 173 0.61 HIS 183 -0.20 TRP 181

GLN 171 0.56 ALA 184 -0.19 SER 185

GLN 171 0.64 SER 185 -0.21 PHE 224

GLY 173 0.50 LEU 186 -0.16 ALA 184

GLN 171 0.43 LEU 187 -0.12 ARG 267

GLN 171 0.52 ALA 188 -0.18 GLY 264

GLN 171 0.50 GLN 189 -0.16 GLY 264

GLN 171 0.37 ASN 190 -0.14 ARG 267

GLN 171 0.39 ASN 191 -0.23 ARG 267

GLN 171 0.32 THR 192 -0.18 ARG 267

GLN 171 0.28 ARG 193 -0.24 ALA 265

GLN 171 0.30 VAL 194 -0.16 THR 54

GLN 171 0.24 TRP 195 -0.21 THR 54

GLN 171 0.24 VAL 196 -0.19 THR 54

GLN 171 0.16 TRP 197 -0.23 ALA 1

ALA 153 0.15 SER 198 -0.22 ALA 1

ALA 215 0.18 PRO 199 -0.25 ALA 1

ALA 215 0.30 THR 200 -0.22 ALA 1

ALA 153 0.22 ASN 201 -0.21 ASN 226

ALA 153 0.30 PRO 202 -0.24 MET 223

ALA 153 0.15 GLY 203 -0.22 GLN 171

GLY 247 0.17 ALA 204 -0.28 ALA 169

ALA 48 0.20 SER 205 -0.32 ALA 169

ASN 44 0.20 ASP 206 -0.38 ALA 169

GLY 39 0.19 PRO 207 -0.44 GLN 171

ASN 37 0.20 ALA 208 -0.48 ALA 169

ALA 66 0.18 ALA 209 -0.42 ALA 169

PRO 202 0.17 MET 210 -0.38 ALA 169

PRO 202 0.19 ILE 211 -0.49 ALA 169

PRO 202 0.25 GLY 212 -0.48 GLN 171

GLY 154 0.29 GLN 213 -0.33 GLN 171

THR 200 0.20 ALA 214 -0.21 GLY 173

ALA 153 0.31 ALA 215 -0.19 GLY 203

ASP 162 0.34 GLU 216 -0.19 VAL 182

ASP 162 0.28 ALA 217 -0.16 GLY 203

ASP 162 0.26 MET 218 -0.21 GLN 227

ASP 162 0.34 GLY 219 -0.23 PRO 202

ASP 162 0.32 ASN 220 -0.18 SER 185

GLN 171 0.30 SER 221 -0.20 MET 218

GLN 171 0.42 ARG 222 -0.25 GLN 227

GLN 171 0.52 MET 223 -0.24 PRO 202

GLN 171 0.51 PHE 224 -0.21 SER 185

GLN 171 0.56 TYR 225 -0.21 PRO 202

GLN 171 0.72 ASN 226 -0.24 ARG 222

GLN 171 0.79 GLN 227 -0.25 ARG 222

GLN 171 0.66 TYR 228 -0.18 PRO 202

GLN 171 0.74 ARG 229 -0.20 THR 54

GLN 171 0.90 SER 230 -0.21 PRO 202

GLN 171 0.86 VAL 231 -0.20 ARG 222

GLN 171 0.73 GLY 232 -0.23 GLY 264

GLN 171 0.63 GLY 233 -0.26 GLY 264

GLN 171 0.55 HIS 234 -0.31 GLY 264

GLN 171 0.42 ASN 235 -0.33 GLY 264

GLN 171 0.41 GLY 236 -0.26 GLY 260

GLN 171 0.34 HIS 237 -0.29 THR 54

GLN 171 0.35 PHE 238 -0.28 THR 54

GLN 171 0.27 ASP 239 -0.28 THR 54

GLN 171 0.26 PHE 240 -0.26 ALA 1

THR 146 0.24 PRO 241 -0.32 ALA 1

THR 146 0.26 ALA 242 -0.30 ALA 1

ALA 215 0.16 SER 243 -0.32 ALA 1

ALA 257 0.16 GLY 244 -0.30 ALA 1

ALA 257 0.15 ASP 245 -0.24 GLY 244

ALA 257 0.11 ASN 246 -0.21 ALA 169

ALA 204 0.17 GLY 247 -0.28 ALA 169

SER 205 0.18 TRP 248 -0.28 ALA 1

SER 259 0.19 GLY 249 -0.32 ALA 1

ALA 257 0.18 SER 250 -0.30 ALA 1

VAL 263 0.16 TRP 251 -0.26 ALA 1

VAL 263 0.20 ALA 252 -0.33 ALA 1

SER 259 0.24 PRO 253 -0.38 ALA 1

MET 258 0.17 GLN 254 -0.31 ALA 51

VAL 263 0.19 LEU 255 -0.28 ALA 51

PRO 253 0.23 GLY 256 -0.45 THR 54

SER 250 0.18 ALA 257 -0.47 THR 54

GLN 254 0.17 MET 258 -0.35 THR 54

PRO 253 0.24 SER 259 -0.27 LEU 55

PRO 253 0.22 GLY 260 -0.30 ASP 261

GLN 171 0.16 ASP 261 -0.30 GLY 260

PRO 253 0.17 ILE 262 -0.27 SER 61

PRO 253 0.21 VAL 263 -0.26 ARG 100

PRO 253 0.19 GLY 264 -0.33 ASN 235

GLN 171 0.16 ALA 265 -0.32 ASN 235

ALA 2 0.21 ILE 266 -0.22 ASN 235

ALA 2 0.30 ARG 267 -0.26 ASN 235

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.

*** 1R88_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 ***

CA distance fluctuations for 240220085926145927

--- normal mode 11 ---

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

* 1R88_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *