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 10 ---

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 57 0.57 ALA 1 -0.64 THR 47

GLY 57 0.63 ALA 2 -0.51 SER 243

GLY 25 0.30 PRO 3 -0.43 SER 243

ASN 190 0.22 TYR 4 -0.38 SER 243

GLY 160 0.25 GLU 5 -0.31 SER 243

GLY 160 0.32 ASN 6 -0.22 ALA 1

GLY 160 0.35 LEU 7 -0.21 SER 243

GLY 160 0.42 MET 8 -0.21 ALA 1

GLY 160 0.38 VAL 9 -0.17 GLY 244

GLY 160 0.39 PRO 10 -0.16 ALA 1

GLY 160 0.34 SER 11 -0.19 ASP 41

GLY 160 0.30 PRO 12 -0.19 LEU 172

GLY 160 0.24 SER 13 -0.23 ASP 41

GLY 160 0.33 MET 14 -0.30 ASP 41

GLY 160 0.40 GLY 15 -0.26 ASP 41

GLY 160 0.46 ARG 16 -0.31 ASP 41

GLY 160 0.48 ASP 17 -0.23 ALA 1

GLY 160 0.46 ILE 18 -0.27 ALA 1

GLY 160 0.41 PRO 19 -0.29 ALA 1

ALA 69 0.33 VAL 20 -0.25 ALA 1

GLY 159 0.25 ALA 21 -0.27 GLY 244

GLY 160 0.22 PHE 22 -0.33 SER 243

ALA 2 0.29 LEU 23 -0.40 SER 243

ALA 2 0.36 ALA 24 -0.42 SER 243

ALA 2 0.54 GLY 25 -0.46 SER 243

ALA 2 0.40 GLY 26 -0.44 SER 243

ALA 2 0.32 PRO 27 -0.37 SER 243

ALA 2 0.33 HIS 28 -0.37 SER 243

ALA 2 0.33 ALA 29 -0.36 SER 243

ASN 190 0.28 VAL 30 -0.37 SER 243

ASN 190 0.22 TYR 31 -0.30 GLY 244

THR 192 0.21 LEU 32 -0.31 GLY 244

PHE 132 0.16 LEU 33 -0.23 GLY 244

GLY 134 0.15 ASP 34 -0.25 ALA 1

GLN 171 0.19 ALA 35 -0.26 ALA 1

GLN 171 0.22 PHE 36 -0.23 ALA 1

PHE 158 0.22 ASN 37 -0.27 ALA 1

ALA 66 0.29 ALA 38 -0.28 ALA 1

PHE 158 0.30 GLY 39 -0.32 ALA 1

GLY 159 0.43 PRO 40 -0.41 SER 81

GLY 159 0.34 ASP 41 -0.36 SER 81

GLY 159 0.26 VAL 42 -0.36 ALA 1

GLY 159 0.20 SER 43 -0.33 ALA 1

ARG 193 0.19 ASN 44 -0.41 ALA 1

ARG 193 0.22 TRP 45 -0.35 ALA 1

ARG 193 0.22 VAL 46 -0.47 ALA 1

ASP 261 0.22 THR 47 -0.64 ALA 1

GLY 256 0.25 ALA 48 -0.57 ALA 1

GLY 256 0.29 GLY 49 -0.42 ALA 1

SER 259 0.30 ASN 50 -0.49 ALA 1

ILE 262 0.27 ALA 51 -0.51 ALA 252

THR 192 0.26 MET 52 -0.47 SER 243

ILE 262 0.28 ASN 53 -0.57 SER 243

SER 259 0.36 THR 54 -0.63 SER 243

ILE 262 0.33 LEU 55 -0.58 SER 243

ALA 2 0.52 ALA 56 -0.55 SER 243

ALA 2 0.63 GLY 57 -0.56 SER 243

ALA 2 0.44 LYS 58 -0.58 SER 243

ALA 2 0.48 GLY 59 -0.53 SER 243

ALA 2 0.44 ILE 60 -0.47 SER 243

ALA 2 0.40 SER 61 -0.43 SER 243

ALA 2 0.29 VAL 62 -0.41 SER 243

ASN 190 0.21 VAL 63 -0.32 GLY 244

ALA 69 0.23 ALA 64 -0.29 GLY 244

ALA 69 0.32 PRO 65 -0.23 ALA 1

ALA 69 0.41 ALA 66 -0.30 ALA 1

ALA 69 0.44 GLY 67 -0.32 SER 81

ALA 69 0.45 GLY 68 -0.26 LYS 82

GLY 68 0.45 ALA 69 -0.26 ASN 37

ILE 18 0.32 TYR 70 -0.19 ALA 1

ILE 18 0.24 SER 71 -0.21 ALA 1

ILE 18 0.16 MET 72 -0.19 ALA 1

PHE 139 0.14 TYR 73 -0.19 ALA 1

ALA 217 0.14 THR 74 -0.24 ARG 174

ASP 179 0.14 ASN 75 -0.21 LEU 172

ALA 153 0.16 TRP 76 -0.28 GLU 77

GLY 149 0.18 GLU 77 -0.28 TRP 76

ALA 153 0.17 GLN 78 -0.20 PRO 40

ASP 162 0.27 ASP 79 -0.27 PRO 40

ASP 162 0.20 GLY 80 -0.32 PRO 40

VAL 161 0.34 SER 81 -0.41 PRO 40

VAL 161 0.27 LYS 82 -0.33 PRO 40

VAL 161 0.19 GLN 83 -0.24 PRO 40

GLY 160 0.19 TRP 84 -0.21 PRO 40

PRO 180 0.16 ASP 85 -0.28 ARG 174

GLY 160 0.14 THR 86 -0.28 ARG 174

GLY 160 0.23 PHE 87 -0.21 ARG 174

ALA 69 0.18 LEU 88 -0.23 ARG 174

ALA 184 0.17 SER 89 -0.31 ARG 174

GLY 160 0.16 ALA 90 -0.28 LEU 172

GLY 160 0.23 GLU 91 -0.22 LEU 172

GLY 160 0.24 LEU 92 -0.20 GLY 244

ALA 69 0.19 PRO 93 -0.22 GLY 244

GLY 160 0.21 ASP 94 -0.21 LEU 172

GLY 160 0.27 TRP 95 -0.20 SER 243

GLY 160 0.24 LEU 96 -0.26 SER 243

GLY 160 0.20 ALA 97 -0.27 SER 243

GLY 160 0.24 ALA 98 -0.24 SER 243

GLY 160 0.26 ASN 99 -0.26 SER 243

GLY 160 0.23 ARG 100 -0.31 SER 243

ALA 2 0.21 GLY 101 -0.31 SER 243

ALA 2 0.24 LEU 102 -0.32 SER 243

ALA 2 0.27 ALA 103 -0.29 SER 243

ALA 2 0.21 PRO 104 -0.24 LEU 172

ALA 2 0.25 GLY 105 -0.27 ARG 174

ASN 190 0.36 GLY 106 -0.27 SER 243

ASN 190 0.31 HIS 107 -0.29 SER 243

ASN 190 0.30 ALA 108 -0.30 SER 243

ASN 190 0.20 ALA 109 -0.26 TRP 177

ALA 133 0.21 VAL 110 -0.28 GLY 244

GLY 134 0.19 GLY 111 -0.23 GLY 244

GLN 171 0.17 ALA 112 -0.21 ALA 1

GLN 171 0.25 ALA 113 -0.21 ALA 1

GLN 171 0.19 GLN 114 -0.19 ALA 1

GLN 171 0.11 GLY 115 -0.18 ALA 1

GLN 171 0.11 GLY 116 -0.18 HIS 178

LEU 140 0.13 TYR 117 -0.20 HIS 178

ALA 184 0.12 GLY 118 -0.23 HIS 178

ALA 184 0.14 ALA 119 -0.27 TRP 177

ALA 184 0.18 MET 120 -0.31 HIS 178

ALA 184 0.21 ALA 121 -0.40 TRP 177

ALA 184 0.21 LEU 122 -0.40 TRP 177

ALA 184 0.19 ALA 123 -0.45 TRP 177

ALA 184 0.29 ALA 124 -0.58 TRP 177

ALA 184 0.24 PHE 125 -0.60 TRP 177

LEU 186 0.26 HIS 126 -0.45 ARG 174

LEU 186 0.29 PRO 127 -0.46 TRP 177

LEU 186 0.24 ASP 128 -0.39 ARG 174

LEU 186 0.24 ARG 129 -0.32 ARG 174

ASN 190 0.24 PHE 130 -0.34 TRP 177

ASN 190 0.37 GLY 131 -0.34 TRP 177

THR 192 0.31 PHE 132 -0.30 TRP 177

VAL 110 0.21 ALA 133 -0.30 TRP 177

GLY 111 0.19 GLY 134 -0.23 ALA 108

TRP 195 0.12 SER 135 -0.19 HIS 178

GLN 171 0.18 MET 136 -0.19 GLY 244

GLN 171 0.29 SER 137 -0.21 ALA 1

GLN 171 0.23 GLY 138 -0.16 ALA 1

GLN 171 0.28 PHE 139 -0.20 GLY 154

THR 200 0.18 LEU 140 -0.17 GLY 154

THR 200 0.26 TYR 141 -0.29 ALA 150

GLY 173 0.32 PRO 142 -0.31 ILE 151

GLY 173 0.41 SER 143 -0.31 SER 185

GLY 173 0.59 ASN 144 -0.34 VAL 231

GLY 173 0.88 THR 145 -0.33 VAL 231

GLN 171 0.90 THR 146 -0.34 VAL 231

GLN 171 0.59 THR 147 -0.37 ALA 150

GLN 171 0.63 ASN 148 -0.28 ALA 152

GLN 171 0.98 GLY 149 -0.35 ALA 153

GLN 171 0.74 ALA 150 -0.37 THR 147

GLN 171 0.51 ILE 151 -0.31 PRO 142

GLN 171 0.50 ALA 152 -0.29 PRO 142

GLN 171 0.56 ALA 153 -0.36 THR 147

GLN 171 0.45 GLY 154 -0.27 THR 147

ASP 17 0.31 MET 155 -0.26 PRO 142

ASP 17 0.36 GLN 156 -0.31 GLY 149

ASP 17 0.34 GLN 157 -0.26 GLY 149

PRO 40 0.40 PHE 158 -0.17 PRO 142

PRO 40 0.43 GLY 159 -0.19 PRO 142

ASP 17 0.48 GLY 160 -0.24 GLY 149

ARG 16 0.42 VAL 161 -0.20 PRO 142

ARG 16 0.34 ASP 162 -0.27 THR 163

ALA 153 0.27 THR 163 -0.27 ASP 162

ALA 153 0.33 ASN 164 -0.26 GLN 189

ALA 153 0.25 GLY 165 -0.17 GLN 189

PRO 202 0.19 MET 166 -0.17 ALA 1

GLY 149 0.26 TRP 167 -0.27 ASN 190

GLY 149 0.42 GLY 168 -0.29 GLN 189

GLY 149 0.63 ALA 169 -0.39 LEU 186

GLY 149 0.79 PRO 170 -0.43 LEU 186

GLY 149 0.98 GLN 171 -0.49 GLN 189

THR 145 0.76 LEU 172 -0.53 GLN 189

THR 145 0.88 GLY 173 -0.56 LEU 186

THR 145 0.54 ARG 174 -0.53 LEU 186

THR 200 0.28 TRP 175 -0.39 LEU 186

SER 143 0.33 LYS 176 -0.54 LEU 186

LYS 176 0.30 TRP 177 -0.60 PHE 125

ASN 75 0.13 HIS 178 -0.39 ALA 121

THR 200 0.17 ASP 179 -0.27 LEU 186

ALA 121 0.18 PRO 180 -0.27 LEU 187

ALA 242 0.16 TRP 181 -0.24 ALA 150

ALA 242 0.16 VAL 182 -0.36 PRO 170

PHE 125 0.22 HIS 183 -0.49 LYS 176

ALA 124 0.29 ALA 184 -0.30 LYS 176

SER 230 0.24 SER 185 -0.47 LYS 176

PRO 127 0.29 LEU 186 -0.56 TRP 177

ARG 267 0.27 LEU 187 -0.49 TRP 177

ARG 267 0.31 ALA 188 -0.41 GLY 173

ARG 267 0.39 GLN 189 -0.54 GLY 173

ARG 267 0.48 ASN 190 -0.54 TRP 177

ALA 265 0.47 ASN 191 -0.46 TRP 177

ALA 265 0.39 THR 192 -0.43 TRP 177

LEU 55 0.31 ARG 193 -0.33 TRP 177

ASN 50 0.22 VAL 194 -0.28 TRP 177

GLY 49 0.21 TRP 195 -0.21 ASP 239

MET 136 0.15 VAL 196 -0.17 ALA 108

GLN 171 0.19 TRP 197 -0.28 MET 258

GLN 171 0.32 SER 198 -0.27 ALA 257

GLN 171 0.43 PRO 199 -0.45 ALA 257

GLN 171 0.58 THR 200 -0.39 ALA 257

GLN 171 0.56 ASN 201 -0.35 ALA 1

GLN 171 0.66 PRO 202 -0.31 ALA 1

GLN 171 0.56 GLY 203 -0.33 ALA 1

GLN 171 0.45 ALA 204 -0.34 ALA 1

GLN 171 0.38 SER 205 -0.40 ALA 1

GLN 171 0.34 ASP 206 -0.35 ALA 1

GLN 171 0.40 PRO 207 -0.28 ALA 1

GLN 171 0.32 ALA 208 -0.24 ALA 1

GLN 171 0.29 ALA 209 -0.28 ALA 1

GLN 171 0.39 MET 210 -0.25 ALA 1

GLN 171 0.42 ILE 211 -0.21 ALA 1

GLN 171 0.51 GLY 212 -0.23 ALA 1

GLN 171 0.61 GLN 213 -0.24 GLY 219

GLN 171 0.55 ALA 214 -0.24 ALA 1

GLN 171 0.62 ALA 215 -0.35 GLY 219

GLN 171 0.65 GLU 216 -0.27 GLY 219

GLN 171 0.49 ALA 217 -0.21 GLY 219

GLN 171 0.51 MET 218 -0.22 ALA 1

GLN 171 0.50 GLY 219 -0.35 ALA 215

GLN 171 0.37 ASN 220 -0.20 GLY 154

GLN 171 0.27 SER 221 -0.19 ALA 215

MET 223 0.38 ARG 222 -0.25 ALA 215

ARG 222 0.38 MET 223 -0.26 GLU 216

ALA 242 0.18 PHE 224 -0.22 ALA 150

ALA 242 0.16 TYR 225 -0.19 ALA 215

ALA 242 0.18 ASN 226 -0.24 ALA 215

ALA 242 0.17 GLN 227 -0.32 THR 146

HIS 126 0.14 TYR 228 -0.25 THR 146

ALA 2 0.14 ARG 229 -0.24 THR 146

SER 185 0.24 SER 230 -0.32 THR 146

ARG 267 0.23 VAL 231 -0.35 GLN 171

GLY 264 0.25 GLY 232 -0.31 GLN 171

GLY 264 0.26 GLY 233 -0.29 LYS 176

GLY 260 0.26 HIS 234 -0.26 TRP 177

GLY 260 0.30 ASN 235 -0.30 TRP 177

MET 258 0.24 GLY 236 -0.24 TRP 177

GLN 254 0.24 HIS 237 -0.24 ALA 265

SER 250 0.20 PHE 238 -0.19 ASP 261

GLN 171 0.20 ASP 239 -0.40 ASP 261

GLN 171 0.32 PHE 240 -0.37 ALA 257

GLN 171 0.39 PRO 241 -0.67 ALA 257

GLN 171 0.52 ALA 242 -0.57 ALA 257

GLN 171 0.48 SER 243 -0.69 ALA 257

GLN 171 0.36 GLY 244 -0.64 PRO 253

GLN 171 0.37 ASP 245 -0.41 ALA 1

GLN 171 0.38 ASN 246 -0.34 ALA 1

GLN 171 0.30 GLY 247 -0.37 ALA 1

GLN 171 0.23 TRP 248 -0.45 ALA 1

GLN 171 0.26 GLY 249 -0.54 ALA 1

GLN 171 0.25 SER 250 -0.59 GLY 244

HIS 237 0.21 TRP 251 -0.48 GLY 244

HIS 237 0.22 ALA 252 -0.51 ALA 51

ALA 48 0.20 PRO 253 -0.67 SER 243

HIS 237 0.24 GLN 254 -0.55 SER 243

GLY 49 0.28 LEU 255 -0.51 SER 243

GLY 49 0.29 GLY 256 -0.65 SER 243

ASN 235 0.25 ALA 257 -0.69 SER 243

ASN 235 0.28 MET 258 -0.51 PRO 241

THR 54 0.36 SER 259 -0.53 SER 243

ASN 191 0.32 GLY 260 -0.55 SER 243

THR 54 0.34 ASP 261 -0.44 PRO 241

LEU 55 0.33 ILE 262 -0.39 SER 243

ASN 191 0.38 VAL 263 -0.45 SER 243

ASN 191 0.47 GLY 264 -0.42 SER 243

ASN 191 0.47 ALA 265 -0.32 SER 243

ASN 190 0.46 ILE 266 -0.32 SER 243

ASN 190 0.48 ARG 267 -0.38 SER 243

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 10 ---

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

* 1R88_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *