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 13 ---

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 0.70 ALA 1 -1.26 GLY 39

GLY 25 1.23 ALA 2 -1.00 THR 47

GLY 101 0.43 PRO 3 -0.60 VAL 46

ARG 100 0.30 TYR 4 -0.31 VAL 42

TYR 4 0.23 GLU 5 -0.22 ASN 191

ASN 50 0.34 ASN 6 -0.34 ALA 1

ASN 50 0.28 LEU 7 -0.29 ALA 1

SER 43 0.28 MET 8 -0.37 ALA 1

SER 43 0.28 VAL 9 -0.30 ALA 1

SER 43 0.24 PRO 10 -0.31 ALA 1

GLY 244 0.24 SER 11 -0.37 ALA 1

GLY 244 0.22 PRO 12 -0.33 ALA 1

GLY 244 0.21 SER 13 -0.40 ALA 1

GLY 244 0.23 MET 14 -0.49 ALA 1

GLY 80 0.30 GLY 15 -0.45 ALA 1

GLY 244 0.25 ARG 16 -0.48 ALA 1

SER 43 0.27 ASP 17 -0.45 ALA 1

SER 43 0.33 ILE 18 -0.53 ALA 1

SER 43 0.37 PRO 19 -0.59 ALA 1

SER 43 0.32 VAL 20 -0.46 ALA 1

ASN 50 0.37 ALA 21 -0.42 ALA 1

ASN 50 0.27 PHE 22 -0.25 ASN 191

ALA 2 0.52 LEU 23 -0.26 ASN 191

ALA 2 0.85 ALA 24 -0.36 GLY 57

ALA 2 1.23 GLY 25 -0.37 ASN 191

ALA 2 1.02 GLY 26 -0.44 ASN 191

ALA 2 0.81 PRO 27 -0.46 ASN 191

ALA 2 0.66 HIS 28 -0.51 ASN 191

ALA 2 0.51 ALA 29 -0.37 ASN 191

ALA 2 0.28 VAL 30 -0.35 TRP 177

GLN 254 0.23 TYR 31 -0.33 HIS 178

GLN 254 0.29 LEU 32 -0.48 ALA 1

GLY 111 0.33 LEU 33 -0.67 ALA 1

GLY 244 0.28 ASP 34 -0.89 ALA 1

ASN 246 0.28 ALA 35 -1.00 ALA 1

ASN 246 0.26 PHE 36 -1.05 ALA 1

ALA 69 0.30 ASN 37 -1.25 ALA 1

GLY 244 0.30 ALA 38 -1.18 ALA 1

GLY 247 0.35 GLY 39 -1.26 ALA 1

GLY 244 0.29 PRO 40 -1.09 ALA 1

GLY 244 0.27 ASP 41 -0.98 ALA 1

PRO 19 0.27 VAL 42 -1.01 ALA 1

PRO 19 0.37 SER 43 -0.98 ALA 1

ALA 252 0.30 ASN 44 -1.12 ALA 1

VAL 20 0.31 TRP 45 -0.79 ALA 1

ALA 21 0.34 VAL 46 -0.79 ALA 1

ASN 6 0.32 THR 47 -1.08 ALA 1

PRO 19 0.25 ALA 48 -1.04 ALA 1

ALA 252 0.31 GLY 49 -0.71 ALA 1

ALA 21 0.37 ASN 50 -0.63 ALA 2

ALA 21 0.27 ALA 51 -0.40 GLY 111

ASN 53 0.25 MET 52 -0.37 PRO 3

GLY 25 0.29 ASN 53 -0.38 ALA 252

ALA 21 0.15 THR 54 -0.30 ALA 252

ALA 2 0.30 LEU 55 -0.28 HIS 178

ALA 2 0.61 ALA 56 -0.26 ALA 35

ALA 2 0.92 GLY 57 -0.36 ALA 24

ALA 2 0.72 LYS 58 -0.31 ASN 235

ALA 2 0.99 GLY 59 -0.40 ASN 191

ALA 2 0.80 ILE 60 -0.41 ASN 191

ALA 2 0.73 SER 61 -0.35 ASN 191

ALA 2 0.38 VAL 62 -0.29 TRP 177

ASN 50 0.22 VAL 63 -0.27 TRP 177

ALA 252 0.28 ALA 64 -0.51 ALA 1

ALA 252 0.28 PRO 65 -0.61 ALA 1

SER 43 0.33 ALA 66 -0.84 ALA 1

GLY 244 0.30 GLY 67 -0.91 ALA 1

GLY 244 0.26 GLY 68 -0.88 ALA 1

ASN 37 0.30 ALA 69 -1.04 ALA 1

ALA 209 0.21 TYR 70 -0.96 ALA 1

LYS 82 0.21 SER 71 -0.81 ALA 1

PHE 139 0.23 MET 72 -0.77 ALA 1

TRP 84 0.23 TYR 73 -0.68 ALA 1

PRO 180 0.20 THR 74 -0.60 ALA 1

ASP 179 0.20 ASN 75 -0.55 ALA 1

GLY 15 0.17 TRP 76 -0.59 ALA 1

GLY 15 0.17 GLU 77 -0.54 ALA 1

GLY 15 0.23 GLN 78 -0.55 ALA 1

GLY 15 0.24 ASP 79 -0.59 ALA 1

GLY 15 0.30 GLY 80 -0.52 ALA 1

GLY 15 0.29 SER 81 -0.59 ALA 1

ASN 246 0.22 LYS 82 -0.63 ALA 1

GLY 118 0.20 GLN 83 -0.54 ALA 1

GLY 118 0.27 TRP 84 -0.56 ALA 1

GLY 118 0.32 ASP 85 -0.47 ALA 1

GLY 118 0.23 THR 86 -0.38 ALA 1

GLY 111 0.26 PHE 87 -0.40 ALA 1

GLY 111 0.29 LEU 88 -0.38 ALA 1

ALA 119 0.25 SER 89 -0.32 ARG 174

ALA 2 0.21 ALA 90 -0.26 ARG 174

GLY 111 0.21 GLU 91 -0.24 ALA 1

ALA 252 0.22 LEU 92 -0.23 ALA 1

ALA 2 0.34 PRO 93 -0.26 ARG 174

ALA 2 0.36 ASP 94 -0.23 ASN 190

ALA 2 0.34 TRP 95 -0.22 ASN 190

ALA 2 0.44 LEU 96 -0.28 ASN 191

ALA 2 0.53 ALA 97 -0.34 ASN 190

ALA 2 0.47 ALA 98 -0.28 ASN 191

ALA 2 0.44 ASN 99 -0.28 ASN 191

ALA 2 0.59 ARG 100 -0.34 ASN 191

ALA 2 0.71 GLY 101 -0.39 ASN 191

ALA 2 0.68 LEU 102 -0.43 ASN 191

ALA 2 0.63 ALA 103 -0.47 ASN 191

ALA 2 0.49 PRO 104 -0.40 ASN 190

ALA 2 0.42 GLY 105 -0.48 ASN 190

ALA 2 0.43 GLY 106 -0.61 ASN 190

ALA 2 0.37 HIS 107 -0.43 THR 192

ALA 2 0.23 ALA 108 -0.42 TRP 177

SER 89 0.23 ALA 109 -0.36 HIS 178

LEU 88 0.22 VAL 110 -0.40 ALA 1

LEU 33 0.33 GLY 111 -0.60 ALA 1

ILE 18 0.24 ALA 112 -0.71 ALA 1

SER 137 0.41 ALA 113 -0.80 ALA 1

GLY 138 0.24 GLN 114 -0.80 ALA 1

TRP 84 0.27 GLY 115 -0.72 ALA 1

TRP 84 0.23 GLY 116 -0.62 ALA 1

ASP 85 0.22 TYR 117 -0.62 ALA 1

ASP 85 0.32 GLY 118 -0.60 ALA 1

LEU 88 0.25 ALA 119 -0.47 ALA 1

ASP 85 0.19 MET 120 -0.44 HIS 178

ASP 85 0.21 ALA 121 -0.58 HIS 178

MET 120 0.19 LEU 122 -0.45 TRP 177

HIS 126 0.22 ALA 123 -0.50 TRP 177

HIS 126 0.14 ALA 124 -0.64 TRP 177

ALA 121 0.11 PHE 125 -0.63 TRP 177

ALA 133 0.22 HIS 126 -0.47 ARG 174

ALA 133 0.25 PRO 127 -0.52 TRP 177

GLY 131 0.30 ASP 128 -0.43 ARG 174

ALA 2 0.27 ARG 129 -0.42 TRP 177

ALA 133 0.25 PHE 130 -0.47 TRP 177

ASP 128 0.30 GLY 131 -0.50 THR 192

ASP 128 0.24 PHE 132 -0.43 TRP 177

PRO 127 0.25 ALA 133 -0.39 PRO 180

LEU 88 0.23 GLY 134 -0.33 ALA 1

LEU 88 0.25 SER 135 -0.46 ALA 1

LEU 88 0.24 MET 136 -0.52 ALA 1

ALA 113 0.41 SER 137 -0.61 ALA 1

ALA 113 0.25 GLY 138 -0.63 ALA 1

MET 72 0.23 PHE 139 -0.66 ALA 1

ASP 85 0.20 LEU 140 -0.54 ALA 1

GLN 227 0.17 TYR 141 -0.55 ALA 1

ASN 75 0.17 PRO 142 -0.62 ALA 1

LYS 176 0.13 SER 143 -0.58 ALA 1

SER 230 0.18 ASN 144 -0.58 ALA 1

GLY 173 0.22 THR 145 -0.62 ALA 1

SER 230 0.29 THR 146 -0.67 ALA 1

GLN 227 0.24 THR 147 -0.69 ALA 1

GLY 173 0.20 ASN 148 -0.70 ALA 1

GLY 173 0.23 GLY 149 -0.74 ALA 1

ASN 226 0.25 ALA 150 -0.80 ALA 1

MET 223 0.21 ILE 151 -0.82 ALA 1

ALA 169 0.33 ALA 152 -0.82 ALA 1

GLN 171 0.31 ALA 153 -0.88 ALA 1

ALA 169 0.25 GLY 154 -0.97 ALA 1

ALA 169 0.28 MET 155 -0.95 ALA 1

ALA 169 0.38 GLN 156 -0.94 ALA 1

GLN 171 0.32 GLN 157 -1.04 ALA 1

ALA 169 0.27 PHE 158 -1.15 ALA 1

ALA 208 0.33 GLY 159 -1.07 ALA 1

ALA 169 0.31 GLY 160 -0.97 ALA 1

GLY 159 0.28 VAL 161 -0.85 ALA 1

ALA 169 0.36 ASP 162 -0.77 ALA 1

ALA 169 0.29 THR 163 -0.72 ALA 1

ASP 162 0.28 ASN 164 -0.64 ALA 1

LEU 172 0.19 GLY 165 -0.62 ALA 1

GLY 15 0.15 MET 166 -0.64 ALA 1

GLY 15 0.14 TRP 167 -0.58 ALA 1

GLN 156 0.24 GLY 168 -0.56 ALA 1

GLN 156 0.38 ALA 169 -0.55 ALA 1

ALA 152 0.31 PRO 170 -0.58 ALA 1

GLN 156 0.36 GLN 171 -0.55 VAL 182

GLN 156 0.31 LEU 172 -0.58 GLY 173

ALA 152 0.27 GLY 173 -0.58 LEU 172

ALA 152 0.19 ARG 174 -0.56 PHE 125

GLN 156 0.13 TRP 175 -0.56 ALA 1

TRP 177 0.14 LYS 176 -0.55 GLN 171

LYS 176 0.14 TRP 177 -0.64 ALA 124

ASN 75 0.15 HIS 178 -0.58 ALA 121

ASN 75 0.20 ASP 179 -0.50 ALA 1

ASP 85 0.21 PRO 180 -0.45 ALA 1

THR 74 0.16 TRP 181 -0.44 GLN 171

THR 146 0.13 VAL 182 -0.55 GLN 171

PRO 180 0.17 HIS 183 -0.49 GLN 171

LEU 140 0.19 ALA 184 -0.40 ALA 265

LEU 140 0.17 SER 185 -0.42 LEU 172

LEU 140 0.14 LEU 186 -0.46 LEU 172

MET 218 0.13 LEU 187 -0.45 ARG 267

PHE 224 0.19 ALA 188 -0.51 ARG 267

PHE 224 0.15 GLN 189 -0.49 ARG 267

HIS 237 0.16 ASN 190 -0.61 GLY 106

HIS 237 0.20 ASN 191 -0.70 ARG 267

HIS 237 0.18 THR 192 -0.62 ILE 266

PRO 127 0.22 ARG 193 -0.54 ALA 265

PRO 127 0.21 VAL 194 -0.37 GLN 171

PRO 127 0.21 TRP 195 -0.32 GLN 171

LEU 88 0.21 VAL 196 -0.32 ALA 1

LEU 88 0.23 TRP 197 -0.36 ALA 1

ALA 113 0.28 SER 198 -0.44 ALA 1

GLY 39 0.25 PRO 199 -0.42 ALA 1

PHE 240 0.24 THR 200 -0.42 ALA 1

PRO 207 0.23 ASN 201 -0.52 ALA 1

PRO 207 0.24 PRO 202 -0.62 ALA 1

PRO 207 0.29 GLY 203 -0.74 ALA 1

PRO 207 0.27 ALA 204 -0.85 ALA 1

GLY 39 0.23 SER 205 -0.93 ALA 1

GLY 159 0.26 ASP 206 -1.11 ALA 1

GLY 203 0.29 PRO 207 -1.11 ALA 1

GLY 159 0.33 ALA 208 -1.22 ALA 1

ALA 69 0.27 ALA 209 -1.14 ALA 1

SER 221 0.22 MET 210 -0.97 ALA 1

ALA 217 0.25 ILE 211 -1.03 ALA 1

GLY 219 0.28 GLY 212 -0.98 ALA 1

GLY 219 0.28 GLN 213 -0.86 ALA 1

GLY 212 0.26 ALA 214 -0.78 ALA 1

ASN 226 0.33 ALA 215 -0.69 ALA 1

GLY 219 0.34 GLU 216 -0.68 ALA 1

ILE 211 0.25 ALA 217 -0.65 ALA 1

ARG 222 0.27 MET 218 -0.54 ALA 1

ASN 226 0.34 GLY 219 -0.51 ALA 1

ASN 226 0.29 ASN 220 -0.52 ALA 1

ALA 113 0.28 SER 221 -0.44 ALA 1

ALA 215 0.33 ARG 222 -0.38 ALA 1

ASN 226 0.31 MET 223 -0.40 ALA 1

TYR 228 0.24 PHE 224 -0.38 ALA 1

GLY 219 0.29 TYR 225 -0.31 GLN 171

GLY 219 0.34 ASN 226 -0.33 GLN 171

GLU 216 0.27 GLN 227 -0.37 GLN 171

PHE 224 0.24 TYR 228 -0.37 ALA 265

GLY 219 0.28 ARG 229 -0.39 ALA 265

THR 146 0.29 SER 230 -0.35 ARG 267

THR 146 0.24 VAL 231 -0.39 ARG 267

ALA 215 0.23 GLY 232 -0.44 ARG 267

GLY 219 0.24 GLY 233 -0.49 ALA 265

ARG 222 0.26 HIS 234 -0.55 GLY 264

HIS 237 0.18 ASN 235 -0.63 ALA 265

HIS 237 0.34 GLY 236 -0.46 ALA 265

GLY 236 0.34 HIS 237 -0.28 GLY 260

ASP 239 0.22 PHE 238 -0.27 GLN 171

GLY 236 0.23 ASP 239 -0.24 GLN 171

THR 200 0.24 PHE 240 -0.29 ALA 1

GLY 39 0.24 PRO 241 -0.23 ALA 1

GLY 39 0.25 ALA 242 -0.25 GLY 219

GLY 39 0.28 SER 243 -0.28 ALA 1

ASP 245 0.36 GLY 244 -0.40 ALA 1

GLY 244 0.36 ASP 245 -0.61 ALA 1

GLY 39 0.30 ASN 246 -0.71 ALA 1

GLY 39 0.35 GLY 247 -0.82 ALA 1

GLY 39 0.34 TRP 248 -0.82 ALA 1

GLY 39 0.32 GLY 249 -0.65 ALA 1

GLY 244 0.30 SER 250 -0.51 ALA 1

ALA 66 0.30 TRP 251 -0.55 ALA 1

ALA 66 0.31 ALA 252 -0.48 ALA 1

GLY 49 0.28 PRO 253 -0.30 ALA 2

LEU 32 0.29 GLN 254 -0.26 ALA 1

LEU 32 0.27 LEU 255 -0.27 TYR 141

SER 243 0.20 GLY 256 -0.25 THR 54

SER 243 0.25 ALA 257 -0.22 GLN 171

SER 243 0.19 MET 258 -0.26 GLN 171

ALA 2 0.18 SER 259 -0.28 ASN 235

ALA 2 0.26 GLY 260 -0.33 ASN 235

ALA 2 0.18 ASP 261 -0.33 ASN 235

ALA 2 0.25 ILE 262 -0.36 ASN 235

ALA 2 0.47 VAL 263 -0.47 ASN 235

ALA 2 0.43 GLY 264 -0.60 ASN 235

ALA 2 0.35 ALA 265 -0.63 ASN 235

ALA 2 0.46 ILE 266 -0.67 ASN 191

ALA 2 0.66 ARG 267 -0.70 ASN 191

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 13 ---

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

* 1R88_unrelaxed_rank_001_alphafold2_ptm_model_3_seed_000 *