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

* Angio *

CA distance fluctuations for 2404051739442459575

--- 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
ASN 288 0.84 CYS 35 -1.35 ILE 54

SER 289 0.59 SER 36 -1.09 LEU 306

GLU 291 0.23 GLN 37 -0.38 PHE 302

GLU 291 0.14 LYS 38 -0.21 PHE 302

VAL 292 0.05 PRO 39 -0.28 SER 36

ASP 41 0.05 SER 40 -0.20 SER 36

SER 40 0.05 ASP 41 -0.27 SER 36

VAL 292 0.02 LYS 42 -0.33 CYS 35

VAL 292 0.03 HIS 43 -0.49 SER 36

SER 40 0.03 LEU 44 -0.52 SER 36

SER 40 0.02 ASP 45 -0.54 CYS 35

ASN 288 0.01 ALA 46 -0.72 CYS 35

ASN 288 0.01 ILE 47 -0.77 CYS 35

SER 40 0.01 PRO 48 -0.81 CYS 35

ASN 288 0.01 ILE 49 -0.95 CYS 35

ILE 287 0.01 LEU 50 -1.07 CYS 35

ASP 297 0.01 TYR 51 -1.07 CYS 35

SER 105 0.01 TYR 52 -1.08 CYS 35

SER 105 0.01 ILE 53 -1.26 CYS 35

ASP 297 0.01 ILE 54 -1.35 CYS 35

ASP 297 0.01 PHE 55 -1.18 CYS 35

TYR 106 0.01 VAL 56 -1.20 CYS 35

THR 102 0.01 ILE 57 -1.32 CYS 35

ASP 297 0.01 GLY 58 -1.28 CYS 35

ASP 297 0.01 PHE 59 -1.16 CYS 35

THR 102 0.01 LEU 60 -1.22 CYS 35

THR 102 0.01 VAL 61 -1.23 CYS 35

ASP 297 0.01 ASN 62 -1.11 CYS 35

ASP 297 0.01 ILE 63 -1.04 CYS 35

PHE 112 0.01 VAL 64 -1.03 CYS 35

ASP 297 0.01 VAL 65 -0.98 CYS 35

ASP 297 0.01 VAL 66 -0.91 CYS 35

ASP 297 0.01 THR 67 -0.89 CYS 35

PHE 112 0.01 LEU 68 -0.87 CYS 35

ASP 297 0.01 PHE 69 -0.81 CYS 35

ASP 297 0.01 CYS 70 -0.76 CYS 35

ASP 297 0.01 CYS 71 -0.70 CYS 35

ASP 297 0.01 GLN 72 -0.67 CYS 35

ASP 297 0.01 LYS 73 -0.61 CYS 35

PRO 157 0.01 GLY 74 -0.57 CYS 35

PHE 320 0.01 PRO 75 -0.56 CYS 35

PHE 320 0.01 LYS 76 -0.61 CYS 35

LEU 68 0.01 LYS 77 -0.66 CYS 35

GLY 233 0.01 VAL 78 -0.61 CYS 35

PHE 320 0.01 SER 79 -0.67 CYS 35

ASP 297 0.01 SER 80 -0.73 CYS 35

GLY 233 0.01 ILE 81 -0.68 CYS 35

GLY 233 0.01 TYR 82 -0.70 CYS 35

ASP 297 0.01 ILE 83 -0.81 CYS 35

ASP 297 0.01 PHE 84 -0.80 CYS 35

ASP 297 0.01 ASN 85 -0.74 CYS 35

ASP 297 0.01 LEU 86 -0.81 CYS 35

ASP 297 0.01 ALA 87 -0.91 CYS 35

ASP 297 0.01 VAL 88 -0.83 CYS 35

ASP 297 0.01 ALA 89 -0.78 CYS 35

ASP 297 0.01 ASP 90 -0.92 CYS 35

ASP 297 0.01 LEU 91 -0.95 CYS 35

ASP 297 0.02 LEU 92 -0.83 CYS 35

ASP 297 0.02 LEU 93 -0.85 CYS 35

ASP 297 0.02 LEU 94 -0.98 CYS 35

ASP 297 0.02 ALA 95 -0.88 CYS 35

ASP 297 0.02 THR 96 -0.77 CYS 35

ASP 297 0.02 LEU 97 -0.87 CYS 35

ALA 294 0.02 PRO 98 -0.83 CYS 35

ALA 294 0.03 LEU 99 -0.69 CYS 35

VAL 295 0.03 TRP 100 -0.67 CYS 35

VAL 295 0.02 ALA 101 -0.75 CYS 35

VAL 295 0.02 THR 102 -0.65 CYS 35

VAL 295 0.03 TYR 103 -0.53 CYS 35

GLU 291 0.02 TYR 104 -0.55 CYS 35

GLU 291 0.02 SER 105 -0.57 CYS 35

GLU 291 0.03 TYR 106 -0.46 CYS 35

GLU 291 0.03 ARG 107 -0.36 CYS 35

GLU 291 0.04 TYR 108 -0.24 CYS 35

VAL 295 0.05 ASP 109 -0.25 CYS 35

ALA 294 0.05 TRP 110 -0.31 CYS 35

ALA 294 0.04 LEU 111 -0.39 CYS 35

ALA 294 0.05 PHE 112 -0.40 CYS 35

ALA 294 0.05 GLY 113 -0.35 CYS 35

ALA 294 0.06 PRO 114 -0.32 CYS 35

ALA 294 0.05 VAL 115 -0.40 CYS 35

ALA 294 0.05 MET 116 -0.45 CYS 35

ALA 294 0.06 CYS 117 -0.37 CYS 35

ALA 294 0.06 LYS 118 -0.37 CYS 35

ALA 294 0.05 VAL 119 -0.48 CYS 35

ALA 294 0.05 PHE 120 -0.47 CYS 35

ALA 294 0.06 GLY 121 -0.37 CYS 35

ALA 294 0.05 SER 122 -0.43 CYS 35

ALA 294 0.04 PHE 123 -0.57 CYS 35

ALA 294 0.03 LEU 124 -0.61 CYS 35

ALA 294 0.03 THR 125 -0.49 CYS 35

ALA 294 0.03 LEU 126 -0.51 CYS 35

ALA 294 0.02 ASN 127 -0.65 CYS 35

ASP 297 0.02 MET 128 -0.65 CYS 35

ALA 294 0.02 PHE 129 -0.51 CYS 35

ALA 294 0.01 ALA 130 -0.58 CYS 35

ASP 297 0.01 SER 131 -0.71 CYS 35

ASP 297 0.01 ILE 132 -0.64 CYS 35

THR 229 0.01 PHE 133 -0.55 CYS 35

THR 229 0.01 PHE 134 -0.65 CYS 35

THR 229 0.00 ILE 135 -0.72 CYS 35

THR 229 0.01 THR 136 -0.59 CYS 35

THR 229 0.01 CYS 137 -0.57 CYS 35

GLY 233 0.01 MET 138 -0.67 CYS 35

GLY 233 0.01 SER 139 -0.64 CYS 35

GLY 233 0.01 VAL 140 -0.53 CYS 35

GLY 233 0.01 ASP 141 -0.57 CYS 35

ARG 155 0.00 ARG 142 -0.63 CYS 35

ARG 155 0.01 TYR 143 -0.53 CYS 35

ARG 155 0.01 GLN 144 -0.50 CYS 35

ILE 147 0.00 SER 145 -0.56 CYS 35

ILE 147 0.01 VAL 146 -0.53 CYS 35

HIS 237 0.01 ILE 147 -0.46 CYS 35

HIS 237 0.01 TYR 148 -0.48 CYS 35

VAL 146 0.01 PRO 149 -0.53 CYS 35

PHE 320 0.01 PHE 150 -0.50 CYS 35

PHE 320 0.01 LEU 151 -0.49 CYS 35

PHE 320 0.01 SER 152 -0.51 CYS 35

PHE 320 0.01 GLN 153 -0.53 CYS 35

GLY 233 0.01 ARG 154 -0.49 CYS 35

GLY 233 0.02 ARG 155 -0.45 CYS 35

LYS 236 0.02 ASN 156 -0.40 CYS 35

LYS 236 0.02 PRO 157 -0.38 CYS 35

LYS 236 0.02 TRP 158 -0.39 CYS 35

GLY 233 0.02 GLN 159 -0.46 CYS 35

GLY 233 0.01 ALA 160 -0.49 CYS 35

GLY 233 0.01 SER 161 -0.56 CYS 35

ALA 294 0.01 TYR 162 -0.56 CYS 35

THR 229 0.01 ILE 163 -0.54 CYS 35

ALA 294 0.02 VAL 164 -0.53 CYS 35

ALA 294 0.02 PRO 165 -0.44 CYS 35

THR 229 0.02 LEU 166 -0.44 CYS 35

ALA 294 0.02 VAL 167 -0.44 CYS 35

ALA 294 0.03 TRP 168 -0.42 CYS 35

ALA 294 0.03 CYS 169 -0.33 CYS 35

ALA 294 0.03 MET 170 -0.30 CYS 35

ALA 294 0.03 ALA 171 -0.36 CYS 35

ALA 294 0.04 CYS 172 -0.29 CYS 35

ALA 294 0.04 LEU 173 -0.22 CYS 35

ALA 294 0.04 SER 174 -0.26 CYS 35

ALA 294 0.05 SER 175 -0.35 CYS 35

ALA 294 0.05 LEU 176 -0.34 CYS 35

ALA 294 0.06 PRO 177 -0.24 CYS 35

ALA 294 0.07 THR 178 -0.27 CYS 35

ALA 294 0.06 PHE 179 -0.34 CYS 35

ALA 294 0.06 TYR 180 -0.27 CYS 35

ALA 294 0.07 PHE 181 -0.19 CYS 35

ALA 294 0.07 ARG 182 -0.23 CYS 35

ALA 294 0.08 ASP 183 -0.21 CYS 35

ALA 294 0.07 VAL 184 -0.21 CYS 35

ALA 294 0.08 ARG 185 -0.14 SER 36

ALA 294 0.07 THR 186 -0.11 SER 36

ALA 294 0.08 ILE 187 -0.06 SER 36

LYS 38 0.07 GLU 188 -0.03 SER 36

CYS 35 0.12 TYR 189 -0.03 TRP 283

LYS 38 0.09 LEU 190 -0.03 TRP 283

LYS 38 0.07 GLY 191 -0.06 SER 36

GLU 291 0.06 VAL 192 -0.13 SER 36

ALA 294 0.06 ASN 193 -0.17 CYS 35

ALA 294 0.08 ALA 194 -0.19 SER 36

ALA 294 0.08 CYS 195 -0.24 CYS 35

ALA 294 0.10 ILE 196 -0.17 SER 36

ALA 294 0.10 MET 197 -0.15 SER 36

ALA 294 0.09 ALA 198 -0.12 SER 36

ALA 294 0.08 PHE 199 -0.11 SER 36

ALA 294 0.07 PRO 200 -0.08 SER 36

ALA 294 0.08 PRO 201 -0.04 SER 36

CYS 35 0.08 GLU 202 -0.02 LYS 1077

CYS 35 0.08 LYS 203 -0.03 SER 36

ALA 294 0.09 TYR 204 -0.04 SER 36

CYS 35 0.12 ALA 205 -0.02 TYR 189

CYS 35 0.11 GLN 206 -0.02 LYS 1077

ALA 294 0.07 TRP 207 -0.07 SER 36

ALA 294 0.09 SER 208 -0.08 SER 36

CYS 35 0.07 ALA 209 -0.04 SER 36

ALA 294 0.05 GLY 210 -0.09 SER 36

ALA 294 0.06 ILE 211 -0.16 SER 36

ALA 294 0.06 ALA 212 -0.13 SER 36

ALA 294 0.04 LEU 213 -0.11 SER 36

ALA 294 0.04 MET 214 -0.18 SER 36

ALA 294 0.04 LYS 215 -0.25 SER 36

ALA 294 0.02 ASN 216 -0.22 SER 36

ALA 294 0.02 ILE 217 -0.18 SER 36

ALA 294 0.02 LEU 218 -0.27 CYS 35

ALA 294 0.01 GLY 219 -0.37 CYS 35

ASP 297 0.01 PHE 220 -0.31 CYS 35

ALA 259 0.01 ILE 221 -0.22 SER 36

ALA 259 0.01 ILE 222 -0.26 CYS 35

ALA 259 0.01 PRO 223 -0.39 CYS 35

ALA 259 0.01 LEU 224 -0.31 CYS 35

ALA 259 0.02 ILE 225 -0.24 CYS 35

THR 229 0.02 PHE 226 -0.34 CYS 35

ALA 259 0.01 ILE 227 -0.40 CYS 35

ALA 259 0.02 ALA 228 -0.29 CYS 35

LEU 166 0.02 THR 229 -0.29 CYS 35

CYS 137 0.01 CYS 230 -0.41 CYS 35

PHE 226 0.01 TYR 231 -0.40 CYS 35

PHE 226 0.02 PHE 232 -0.30 CYS 35

ASN 156 0.02 GLY 233 -0.35 CYS 35

ASN 156 0.01 ILE 234 -0.43 CYS 35

ASN 156 0.02 ARG 235 -0.35 CYS 35

ASN 156 0.02 LYS 236 -0.31 CYS 35

ASN 156 0.02 HIS 237 -0.39 CYS 35

ASN 156 0.01 LEU 238 -0.39 CYS 35

ASN 156 0.02 LEU 239 -0.31 CYS 35

ASN 156 0.02 LYS 240 -0.34 CYS 35

ASN 156 0.01 THR 241 -0.40 CYS 35

LYS 236 0.01 ASN 242 -0.35 CYS 35

ASN 156 0.02 ALA 1001 -0.28 CYS 35

ASN 156 0.02 ASP 1002 -0.28 CYS 35

ASN 156 0.01 LEU 1003 -0.33 CYS 35

ALA 1001 0.01 GLU 1004 -0.31 CYS 35

ASN 156 0.01 ASP 1005 -0.26 CYS 35

PRO 157 0.01 ASN 1006 -0.29 CYS 35

ALA 1001 0.01 TRP 1007 -0.31 CYS 35

ALA 1001 0.01 GLU 1008 -0.26 CYS 35

PRO 157 0.01 THR 1009 -0.25 CYS 35

ALA 1001 0.01 LEU 1010 -0.29 CYS 35

ALA 1001 0.01 ASN 1011 -0.27 CYS 35

ALA 1001 0.01 ASP 1012 -0.23 CYS 35

ALA 1001 0.01 ASN 1013 -0.23 CYS 35

ALA 1001 0.01 LEU 1014 -0.26 CYS 35

ALA 1001 0.01 LYS 1015 -0.23 CYS 35

ALA 1001 0.01 VAL 1016 -0.20 CYS 35

ALA 1001 0.01 ILE 1017 -0.23 CYS 35

ALA 1001 0.01 GLU 1018 -0.22 CYS 35

ALA 1001 0.01 LYS 1019 -0.19 CYS 35

ALA 1001 0.00 ALA 1020 -0.18 CYS 35

ALA 1001 0.00 ASP 1021 -0.19 CYS 35

ASN 1080 0.00 ASN 1022 -0.18 CYS 35

ALA 1100 0.00 ALA 1023 -0.20 CYS 35

ALA 1100 0.00 ALA 1024 -0.19 CYS 35

LEU 1076 0.00 GLN 1025 -0.18 CYS 35

LYS 1027 0.00 VAL 1026 -0.21 CYS 35

ALA 1100 0.00 LYS 1027 -0.22 CYS 35

ASP 1073 0.00 ASP 1028 -0.21 CYS 35

THR 1031 0.00 ALA 1029 -0.22 CYS 35

ALA 1100 0.00 LEU 1030 -0.26 CYS 35

ALA 1100 0.00 THR 1031 -0.25 CYS 35

ASP 1066 0.00 LYS 1032 -0.24 CYS 35

LYS 1032 0.00 MET 1033 -0.28 CYS 35

ALA 1100 0.01 ARG 1034 -0.30 CYS 35

ASP 1066 0.01 ALA 1035 -0.28 CYS 35

ASP 1066 0.01 ALA 1036 -0.30 CYS 35

ASP 1066 0.00 ALA 1037 -0.34 CYS 35

ASP 1066 0.01 LEU 1038 -0.34 CYS 35

HIS 1063 0.01 ASP 1039 -0.33 CYS 35

HIS 1063 0.01 ALA 1040 -0.36 CYS 35

ARG 1062 0.01 GLN 1041 -0.41 CYS 35

ARG 1062 0.01 LYS 1042 -0.40 CYS 35

ASP 1060 0.01 ALA 1043 -0.44 CYS 35

PRO 1045 0.01 THR 1044 -0.51 CYS 35

LYS 1042 0.01 PRO 1045 -0.57 CYS 35

LYS 1042 0.01 ASP 1060 -0.58 CYS 35

THR 250 0.01 PHE 1061 -0.52 CYS 35

GLN 1041 0.01 ARG 1062 -0.48 CYS 35

LEU 1038 0.01 HIS 1063 -0.48 CYS 35

LYS 1104 0.01 GLY 1064 -0.46 CYS 35

LEU 1038 0.01 PHE 1065 -0.42 CYS 35

ALA 1035 0.01 ASP 1066 -0.42 CYS 35

LYS 1104 0.01 ILE 1067 -0.41 CYS 35

ALA 1100 0.01 LEU 1068 -0.38 CYS 35

ALA 1100 0.01 VAL 1069 -0.35 CYS 35

ALA 1100 0.01 GLY 1070 -0.36 CYS 35

ALA 1100 0.01 GLN 1071 -0.35 CYS 35

ALA 1100 0.01 ILE 1072 -0.31 CYS 35

ALA 1100 0.01 ASP 1073 -0.31 CYS 35

ALA 1100 0.01 ASP 1074 -0.31 CYS 35

ALA 1100 0.01 ALA 1075 -0.29 CYS 35

ALA 1100 0.01 LEU 1076 -0.27 CYS 35

ALA 1100 0.01 LYS 1077 -0.28 CYS 35

ALA 1100 0.01 LEU 1078 -0.27 CYS 35

ALA 1100 0.01 ALA 1079 -0.24 CYS 35

ALA 1100 0.01 ASN 1080 -0.23 CYS 35

ALA 1100 0.01 GLU 1081 -0.23 CYS 35

ALA 1100 0.00 GLY 1082 -0.22 CYS 35

ALA 1100 0.01 LYS 1083 -0.24 CYS 35

ALA 1100 0.00 VAL 1084 -0.23 CYS 35

GLU 1018 0.00 LYS 1085 -0.23 CYS 35

GLU 1092 0.01 GLU 1086 -0.26 CYS 35

ALA 1090 0.01 ALA 1087 -0.27 CYS 35

ASN 1011 0.00 GLN 1088 -0.25 CYS 35

GLU 1086 0.01 ALA 1089 -0.27 CYS 35

LEU 1078 0.01 ALA 1090 -0.29 CYS 35

ALA 1001 0.01 ALA 1091 -0.29 CYS 35

ALA 1001 0.01 GLU 1092 -0.31 CYS 35

GLN 1103 0.01 GLN 1093 -0.34 CYS 35

ALA 1075 0.01 LEU 1094 -0.34 CYS 35

ALA 1001 0.01 LYS 1095 -0.33 CYS 35

GLN 1103 0.01 THR 1096 -0.37 CYS 35

ALA 1100 0.02 THR 1097 -0.39 CYS 35

ALA 1001 0.01 ARG 1098 -0.38 CYS 35

ASP 252 0.01 ASN 1099 -0.38 CYS 35

THR 1097 0.02 ALA 1100 -0.43 CYS 35

LEU 1068 0.01 TYR 1101 -0.44 CYS 35

ASN 1099 0.01 ILE 1102 -0.42 CYS 35

ASP 252 0.01 GLN 1103 -0.47 CYS 35

ILE 1067 0.01 LYS 1104 -0.50 CYS 35

TYR 1101 0.01 TYR 1105 -0.46 CYS 35

ASP 252 0.01 LEU 1106 -0.47 CYS 35

ASP 252 0.01 LYS 246 -0.54 CYS 35

THR 250 0.01 ASN 247 -0.52 CYS 35

ASP 252 0.01 ARG 248 -0.48 CYS 35

ASP 252 0.02 ILE 249 -0.55 CYS 35

ASN 247 0.01 THR 250 -0.54 CYS 35

ARG 235 0.01 ARG 251 -0.46 CYS 35

ILE 249 0.02 ASP 252 -0.51 CYS 35

ILE 249 0.01 GLN 253 -0.60 CYS 35

ILE 147 0.01 VAL 254 -0.53 CYS 35

ALA 228 0.02 LEU 255 -0.47 CYS 35

ALA 228 0.01 LYS 256 -0.58 CYS 35

ALA 228 0.01 MET 257 -0.59 CYS 35

ALA 228 0.01 ALA 258 -0.46 CYS 35

ALA 228 0.02 ALA 259 -0.48 CYS 35

ILE 225 0.01 ALA 260 -0.61 CYS 35

ILE 225 0.00 VAL 261 -0.69 CYS 35

ILE 225 0.00 VAL 262 -0.72 CYS 35

LEU 224 0.01 LEU 263 -0.74 CYS 35

ILE 222 0.00 ALA 264 -0.95 CYS 35

ILE 222 0.00 PHE 265 -0.90 CYS 35

ILE 221 0.01 ILE 266 -0.69 CYS 35

ILE 221 0.00 ILE 267 -0.74 CYS 35

ILE 221 0.00 CYS 268 -0.89 CYS 35

LEU 270 0.00 TRP 269 -0.69 SER 36

LEU 306 0.01 LEU 270 -0.55 SER 36

LEU 305 0.01 PRO 271 -0.68 SER 36

ILE 304 0.01 PHE 272 -0.62 SER 36

HIS 43 0.01 HIS 273 -0.42 SER 36

HIS 43 0.01 VAL 274 -0.27 SER 36

HIS 43 0.01 LEU 275 -0.27 SER 36

ALA 294 0.02 THR 276 -0.26 SER 36

HIS 43 0.01 PHE 277 -0.12 SER 36

CYS 35 0.15 LEU 278 -0.04 PHE 277

CYS 35 0.08 ASP 279 -0.05 SER 36

CYS 35 0.09 ALA 280 -0.04 SER 36

CYS 35 0.25 LEU 281 -0.02 LYS 1077

CYS 35 0.32 ALA 282 -0.02 LEU 190

CYS 35 0.28 TRP 283 -0.03 LEU 190

CYS 35 0.37 MET 284 -0.02 TYR 189

CYS 35 0.48 GLY 285 -0.02 LEU 190

CYS 35 0.58 VAL 286 -0.02 LYS 1077

CYS 35 0.65 ILE 287 -0.03 ALA 228

CYS 35 0.84 ASN 288 -0.04 ALA 228

CYS 35 0.76 SER 289 -0.05 ALA 228

CYS 35 0.59 CYS 290 -0.04 PRO 271

CYS 35 0.50 GLU 291 -0.06 PRO 271

CYS 35 0.38 VAL 292 -0.06 VAL 274

CYS 35 0.27 ILE 293 -0.04 PRO 271

CYS 35 0.27 ALA 294 -0.04 PRO 271

ILE 196 0.09 VAL 295 -0.05 PRO 39

ILE 196 0.04 ILE 296 -0.13 SER 36

VAL 295 0.06 ASP 297 -0.27 SER 36

ILE 196 0.03 LEU 298 -0.33 SER 36

VAL 292 0.02 ALA 299 -0.47 SER 36

HIS 43 0.01 LEU 300 -0.59 SER 36

HIS 43 0.01 PRO 301 -0.79 SER 36

HIS 43 0.02 PHE 302 -1.06 SER 36

VAL 274 0.01 ALA 303 -0.96 SER 36

PHE 272 0.01 ILE 304 -0.92 SER 36

VAL 274 0.01 LEU 305 -1.06 SER 36

LEU 270 0.01 LEU 306 -1.09 CYS 35

LEU 270 0.00 GLY 307 -1.00 CYS 35

ASP 297 0.01 PHE 308 -1.10 CYS 35

LEU 270 0.00 THR 309 -1.33 CYS 35

ILE 221 0.00 ASN 310 -1.25 CYS 35

ASP 297 0.01 SER 311 -1.15 CYS 35

ASP 297 0.01 CYS 312 -1.32 CYS 35

THR 102 0.00 VAL 313 -1.32 CYS 35

ASP 297 0.00 ASN 314 -1.15 CYS 35

ASP 297 0.01 PRO 315 -1.06 CYS 35

LYS 76 0.01 PHE 316 -1.13 CYS 35

SER 152 0.01 LEU 317 -1.12 CYS 35

SER 152 0.01 TYR 318 -0.97 CYS 35

LYS 76 0.01 CYS 319 -0.97 CYS 35

LYS 76 0.01 PHE 320 -1.01 CYS 35

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.

*** Angio ***

CA distance fluctuations for 2404051739442459575

--- normal mode 10 ---

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

* Angio *