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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 17 ---

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
ASP 1151 0.39 THR 937 -0.52 GLN 964

ASP 1151 0.33 ASP 938 -0.80 GLY 965

HSD 963 0.55 PHE 939 -0.78 LYS 966

HSD 963 0.41 ARG 940 -1.22 LYS 966

HSD 963 0.46 ARG 941 -1.21 GLY 965

HSD 963 0.78 PHE 942 -0.78 GLY 965

HSD 963 0.72 GLN 943 -0.59 GLY 965

HSD 963 0.85 MET 944 -0.43 GLY 965

HSD 963 0.70 ILE 945 -0.36 GLY 965

HSD 963 0.66 PRO 946 -0.28 GLY 965

HSD 963 0.60 LEU 947 -0.24 GLY 965

HSD 963 0.52 ASP 948 -0.22 GLY 965

HSD 963 0.48 PRO 949 -0.24 GLY 965

HSD 963 0.41 LYS 950 -0.20 GLY 965

HSD 963 0.38 GLY 951 -0.20 PRO 946

HSD 963 0.32 THR 952 -0.26 PRO 946

HSD 963 0.38 SER 953 -0.17 ASP 1031

HSD 963 0.43 GLN 954 -0.27 ASN 955

HSD 963 0.48 ASN 955 -0.27 GLN 954

HSD 963 0.57 ASP 956 -0.21 GLY 965

HSD 963 0.77 PRO 957 -0.19 GLN 954

HSD 963 0.86 ASN 958 -0.17 LYS 966

HSD 963 1.21 TRP 959 -0.24 LYS 966

HSD 963 1.14 VAL 960 -0.25 ARG 940

HSD 963 0.65 VAL 961 -0.54 ARG 941

GLN 964 0.70 ARG 962 -0.52 ARG 941

TRP 959 1.21 HSD 963 0.00 THR 937

ARG 962 0.70 GLN 964 -0.68 ASP 938

ASN 997 0.34 GLY 965 -1.21 ARG 941

PHE 1087 0.42 LYS 966 -1.22 ARG 940

HSD 963 0.66 GLU 967 -0.52 ARG 940

HSD 963 1.13 LEU 968 -0.39 ARG 940

HSD 963 1.06 VAL 969 -0.28 ARG 940

HSD 963 1.01 GLN 970 -0.18 ARG 940

HSD 963 0.80 THR 971 -0.16 ARG 940

HSD 963 0.68 VAL 972 -0.13 ASP 1031

HSD 963 0.60 ASN 973 -0.14 ASP 1031

HSD 963 0.62 CYS 974 -0.17 ASP 1031

HSD 963 0.58 ASP 975 -0.15 GLY 965

HSD 963 0.65 PRO 976 -0.17 GLY 965

HSD 963 0.76 GLY 977 -0.23 GLY 965

HSD 963 0.82 LEU 978 -0.30 GLY 965

HSD 963 0.94 ALA 979 -0.39 GLY 965

HSD 963 0.75 VAL 980 -0.47 GLY 965

HSD 963 0.60 GLY 981 -0.61 GLY 965

HSD 963 0.38 TYR 982 -0.73 GLY 965

HSD 963 0.34 ASP 983 -0.58 GLY 965

HSD 963 0.33 GLU 984 -0.48 GLY 965

HSD 963 0.37 PHE 985 -0.33 GLY 965

HSD 963 0.34 ASN 986 -0.27 GLY 965

HSD 963 0.37 ALA 987 -0.19 GLY 965

HSD 963 0.43 VAL 988 -0.17 GLY 965

HSD 963 0.45 ASP 989 -0.14 VAL 1106

HSD 963 0.53 PHE 990 -0.13 GLY 965

HSD 963 0.54 SER 991 -0.12 THR 937

HSD 963 0.64 GLY 992 -0.15 THR 937

HSD 963 0.65 THR 993 -0.18 PHE 939

HSD 963 0.75 PHE 994 -0.15 ARG 940

HSD 963 0.68 PHE 995 -0.18 ARG 940

HSD 963 0.68 ILE 996 -0.14 ARG 940

ARG 962 0.64 ASN 997 -0.13 ARG 940

HSD 963 0.58 THR 998 -0.10 ARG 940

HSD 963 0.53 GLU 999 -0.14 VAL 1025

HSD 963 0.54 ARG 1000 -0.25 ASP 1001

HSD 963 0.54 ASP 1001 -0.25 ARG 1000

HSD 963 0.54 ASP 1002 -0.20 ARG 1000

HSD 963 0.59 ASP 1003 -0.18 ARG 1000

HSD 963 0.66 TYR 1004 -0.10 ARG 1000

HSD 963 0.75 ALA 1005 -0.10 ARG 1000

HSD 963 0.73 GLY 1006 -0.11 PHE 1007

HSD 963 0.74 PHE 1007 -0.14 GLY 965

HSD 963 0.66 VAL 1008 -0.21 GLY 965

HSD 963 0.58 PHE 1009 -0.23 GLY 965

HSD 963 0.50 GLY 1010 -0.25 GLY 965

HSD 963 0.54 TYR 1011 -0.30 GLY 965

HSD 963 0.47 GLN 1012 -0.31 GLY 965

HSD 963 0.51 SER 1013 -0.30 GLY 965

HSD 963 0.54 SER 1014 -0.28 GLY 965

HSD 963 0.50 SER 1015 -0.29 GLY 1053

HSD 963 0.50 ARG 1016 -0.24 LYS 1099

HSD 963 0.54 PHE 1017 -0.22 GLY 965

HSD 963 0.56 TYR 1018 -0.18 PRO 1152

HSD 963 0.62 VAL 1019 -0.15 PRO 1152

HSD 963 0.62 VAL 1020 -0.15 PRO 1152

HSD 963 0.64 MET 1021 -0.14 PRO 1152

HSD 963 0.62 TRP 1022 -0.13 PRO 1152

HSD 963 0.58 LYS 1023 -0.13 PRO 1152

HSD 963 0.55 GLN 1024 -0.14 ARG 1000

HSD 963 0.49 VAL 1025 -0.17 ARG 1000

HSD 963 0.46 THR 1026 -0.16 ARG 1000

HSD 963 0.43 GLN 1027 -0.21 ARG 1000

HSD 963 0.41 SER 1028 -0.17 ARG 1000

HSD 963 0.41 TYR 1029 -0.12 ARG 1000

HSD 963 0.35 TRP 1030 -0.14 ASN 973

HSD 963 0.33 ASP 1031 -0.18 ASN 955

HSD 963 0.33 THR 1032 -0.13 ASN 955

HSD 963 0.33 ASN 1033 -0.13 GLY 965

HSD 963 0.35 PRO 1034 -0.13 GLY 965

HSD 963 0.37 THR 1035 -0.11 GLY 965

HSD 963 0.37 ARG 1036 -0.12 ARG 1000

HSD 963 0.42 ALA 1037 -0.12 ARG 1000

HSD 963 0.43 GLN 1038 -0.14 ARG 1000

HSD 963 0.49 GLY 1039 -0.15 ARG 1000

HSD 963 0.48 TYR 1040 -0.14 ARG 1000

HSD 963 0.51 SER 1041 -0.14 PRO 1152

HSD 963 0.53 GLY 1042 -0.16 PRO 1152

HSD 963 0.55 LEU 1043 -0.17 PRO 1152

HSD 963 0.54 SER 1044 -0.18 PRO 1152

HSD 963 0.54 VAL 1045 -0.19 PRO 1152

HSD 963 0.53 LYS 1046 -0.19 PRO 1152

HSD 963 0.51 VAL 1047 -0.19 PRO 1152

HSD 963 0.51 VAL 1048 -0.19 LYS 1099

HSD 963 0.48 ASN 1049 -0.25 LYS 1099

HSD 963 0.47 SER 1050 -0.21 LYS 1099

HSD 963 0.44 THR 1051 -0.25 LYS 1099

HSD 963 0.44 THR 1052 -0.23 LYS 1099

HSD 963 0.47 GLY 1053 -0.29 SER 1015

HSD 963 0.51 PRO 1054 -0.24 GLY 1055

HSD 963 0.45 GLY 1055 -0.24 PRO 1054

HSD 963 0.42 GLU 1056 -0.17 GLY 965

HSD 963 0.44 HSD 1057 -0.15 LYS 1099

HSD 963 0.49 LEU 1058 -0.16 LYS 1099

HSD 963 0.50 ARG 1059 -0.16 GLY 965

HSD 963 0.46 ASN 1060 -0.12 GLY 965

HSD 963 0.48 ALA 1061 -0.13 PRO 1152

HSD 963 0.55 LEU 1062 -0.13 PRO 1152

HSD 963 0.53 TRP 1063 -0.12 PRO 1152

HSD 963 0.48 HSD 1064 -0.12 PRO 1152

HSD 963 0.48 THR 1065 -0.14 PRO 1152

HSD 963 0.46 GLY 1066 -0.17 ASN 1067

HSD 963 0.44 ASN 1067 -0.17 GLY 1066

HSD 963 0.43 THR 1068 -0.14 PRO 1152

HSD 963 0.41 PRO 1069 -0.13 PRO 1152

HSD 963 0.43 GLY 1070 -0.17 LYS 1099

HSD 963 0.46 GLN 1071 -0.17 LYS 1099

HSD 963 0.49 VAL 1072 -0.16 PRO 1152

HSD 963 0.47 ARG 1073 -0.17 PRO 1152

HSD 963 0.48 THR 1074 -0.18 PRO 1152

HSD 963 0.47 LEU 1075 -0.22 PRO 1152

HSD 963 0.47 TRP 1076 -0.22 PRO 1152

HSD 963 0.49 HSD 1077 -0.20 PRO 1152

HSD 963 0.47 ASP 1078 -0.20 PRO 1152

HSD 963 0.44 PRO 1079 -0.21 PRO 1152

HSD 963 0.43 ARG 1080 -0.19 PRO 1152

HSD 963 0.47 HSD 1081 -0.17 PRO 1152

HSD 963 0.48 ILE 1082 -0.16 PRO 1152

HSD 963 0.51 GLY 1083 -0.14 PRO 1152

HSD 963 0.55 TRP 1084 -0.12 PRO 1152

HSD 963 0.53 LYS 1085 -0.11 ARG 1091

HSD 963 0.55 ASP 1086 -0.11 ARG 1091

HSD 963 0.55 PHE 1087 -0.11 THR 937

HSD 963 0.54 THR 1088 -0.16 ALA 1089

HSD 963 0.58 ALA 1089 -0.16 THR 1088

HSD 963 0.58 TYR 1090 -0.21 ARG 1091

HSD 963 0.56 ARG 1091 -0.21 TYR 1090

HSD 963 0.56 TRP 1092 -0.11 THR 937

HSD 963 0.50 ARG 1093 -0.15 TYR 1147

HSD 963 0.51 LEU 1094 -0.15 PRO 1152

HSD 963 0.46 SER 1095 -0.23 PRO 1152

HSD 963 0.44 HSD 1096 -0.29 PRO 1152

HSD 963 0.39 ARG 1097 -0.44 PRO 1152

HSD 963 0.37 PRO 1098 -0.35 PRO 1152

HSD 963 0.33 LYS 1099 -0.37 PRO 1152

HSD 963 0.36 THR 1100 -0.46 PRO 1152

HSD 963 0.40 GLY 1101 -0.37 PRO 1152

HSD 963 0.41 PHE 1102 -0.42 PRO 1152

HSD 963 0.46 ILE 1103 -0.34 PRO 1152

HSD 963 0.47 ARG 1104 -0.30 PRO 1152

HSD 963 0.50 VAL 1105 -0.23 PRO 1152

HSD 963 0.49 VAL 1106 -0.21 PRO 1152

HSD 963 0.52 MET 1107 -0.15 PRO 1152

HSD 963 0.49 TYR 1108 -0.13 THR 937

HSD 963 0.50 GLU 1109 -0.11 THR 937

HSD 963 0.45 GLY 1110 -0.34 LYS 1111

HSD 963 0.37 LYS 1111 -0.34 GLY 1110

HSD 963 0.41 LYS 1112 -0.16 PRO 1152

HSD 963 0.43 ILE 1113 -0.19 PRO 1152

HSD 963 0.47 MET 1114 -0.18 PRO 1152

HSD 963 0.48 ALA 1115 -0.20 PRO 1152

HSD 963 0.46 ASP 1116 -0.25 PRO 1152

HSD 963 0.46 SER 1117 -0.26 PRO 1152

HSD 963 0.42 GLY 1118 -0.31 PRO 1152

HSD 963 0.41 PRO 1119 -0.35 PRO 1152

HSD 963 0.43 ILE 1120 -0.32 PRO 1152

HSD 963 0.42 TYR 1121 -0.33 PRO 1152

HSD 963 0.43 ASP 1122 -0.28 PRO 1152

HSD 963 0.42 LYS 1123 -0.27 PRO 1152

HSD 963 0.42 THR 1124 -0.26 LYS 1099

HSD 963 0.43 TYR 1125 -0.33 LYS 1099

HSD 963 0.39 ALA 1126 -0.36 LYS 1099

HSD 963 0.40 GLY 1127 -0.27 GLY 965

HSD 963 0.44 GLY 1128 -0.33 GLY 965

HSD 963 0.51 ARG 1129 -0.39 GLY 965

HSD 963 0.60 LEU 1130 -0.35 GLY 965

HSD 963 0.75 GLY 1131 -0.33 GLY 965

HSD 963 0.87 LEU 1132 -0.23 LYS 966

HSD 963 0.81 PHE 1133 -0.17 GLY 965

HSD 963 0.80 VAL 1134 -0.11 GLY 965

HSD 963 0.68 PHE 1135 -0.11 LEU 1132

HSD 963 0.61 SER 1136 -0.12 ARG 940

HSD 963 0.68 GLN 1137 -0.12 ARG 940

HSD 963 0.73 GLU 1138 -0.12 ARG 940

HSD 963 0.78 MET 1139 -0.14 ARG 940

HSD 963 0.84 VAL 1140 -0.18 ARG 940

HSD 963 0.86 PHE 1141 -0.24 ARG 940

HSD 963 0.87 PHE 1142 -0.29 ARG 940

HSD 963 0.71 SER 1143 -0.31 ARG 940

HSD 963 0.56 ASP 1144 -0.24 ASP 938

HSD 963 0.63 LEU 1145 -0.20 LYS 966

HSD 963 0.49 LYS 1146 -0.21 GLN 964

HSD 963 0.48 TYR 1147 -0.19 GLN 964

HSD 963 0.38 GLU 1148 -0.22 GLN 964

HSD 963 0.38 CYS 1149 -0.18 GLN 964

HSD 963 0.36 ARG 1150 -0.15 GLN 964

THR 937 0.39 ASP 1151 -0.28 ARG 1097

THR 937 0.36 PRO 1152 -0.46 THR 1100

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.

*** ***

CA distance fluctuations for 2405021543434120385

--- normal mode 17 ---

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

* *