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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 15 ---

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
HSD 963 0.32 THR 937 -0.58 ASP 1151

HSD 963 0.40 ASP 938 -0.63 ASP 1151

HSD 963 0.55 PHE 939 -0.47 ASP 1151

HSD 963 0.66 ARG 940 -0.48 ASP 1151

HSD 963 0.61 ARG 941 -0.49 ASP 1151

HSD 963 0.64 PHE 942 -0.40 ASP 1151

HSD 963 0.47 GLN 943 -0.33 ASP 1151

HSD 963 0.50 MET 944 -0.26 ASP 1151

HSD 963 0.34 ILE 945 -0.25 LYS 966

HSD 963 0.32 PRO 946 -0.24 TRP 959

HSD 963 0.31 LEU 947 -0.15 TRP 959

HSD 963 0.27 ASP 948 -0.16 PRO 957

SER 1014 0.19 PRO 949 -0.32 ASP 956

HSD 963 0.16 LYS 950 -0.23 ASP 956

HSD 963 0.25 GLY 951 -0.13 ASP 1002

HSD 963 0.31 THR 952 -0.22 SER 953

HSD 963 0.34 SER 953 -0.22 THR 952

HSD 963 0.40 GLN 954 -0.21 ASP 1002

HSD 963 0.40 ASN 955 -0.20 ARG 1000

HSD 963 0.43 ASP 956 -0.32 PRO 949

HSD 963 0.54 PRO 957 -0.31 PRO 949

HSD 963 0.61 ASN 958 -0.29 PRO 949

HSD 963 0.84 TRP 959 -0.25 PRO 949

HSD 963 0.92 VAL 960 -0.22 ASP 1151

HSD 963 0.65 VAL 961 -0.26 ASP 1151

HSD 963 0.31 ARG 962 -0.26 ASP 1151

VAL 960 0.92 HSD 963 -0.09 PRO 1152

ARG 940 0.56 GLN 964 -0.17 PRO 1152

ASP 1144 0.46 GLY 965 -0.29 ASP 1151

ALA 1089 0.39 LYS 966 -0.36 ARG 940

HSD 963 0.54 GLU 967 -0.24 ASP 1151

HSD 963 0.84 LEU 968 -0.24 ASP 1151

HSD 963 0.72 VAL 969 -0.19 ILE 945

HSD 963 0.67 GLN 970 -0.21 PRO 949

HSD 963 0.54 THR 971 -0.23 PRO 949

HSD 963 0.47 VAL 972 -0.21 PRO 949

HSD 963 0.47 ASN 973 -0.18 ARG 1000

HSD 963 0.46 CYS 974 -0.24 PRO 949

HSD 963 0.42 ASP 975 -0.17 SER 1136

HSD 963 0.43 PRO 976 -0.12 PRO 949

HSD 963 0.45 GLY 977 -0.14 THR 1052

HSD 963 0.48 LEU 978 -0.17 ASP 1151

HSD 963 0.57 ALA 979 -0.24 ASP 1151

HSD 963 0.47 VAL 980 -0.31 ASP 1151

HSD 963 0.45 GLY 981 -0.44 ASP 1151

HSD 963 0.39 TYR 982 -0.59 ASP 1151

HSD 963 0.30 ASP 983 -0.70 ASP 1151

HSD 963 0.27 GLU 984 -0.66 ASP 1151

HSD 963 0.19 PHE 985 -0.49 ASP 1151

CYS 1149 0.22 ASN 986 -0.35 GLU 984

HSD 963 0.19 ALA 987 -0.22 ASP 938

HSD 963 0.23 VAL 988 -0.19 LYS 1111

HSD 963 0.29 ASP 989 -0.24 LYS 1111

HSD 963 0.36 PHE 990 -0.25 LYS 1111

HSD 963 0.41 SER 991 -0.29 LYS 1111

HSD 963 0.48 GLY 992 -0.23 LYS 1111

HSD 963 0.49 THR 993 -0.14 GLY 992

HSD 963 0.53 PHE 994 -0.15 PHE 995

HSD 963 0.47 PHE 995 -0.15 PHE 994

HSD 963 0.45 ILE 996 -0.16 PRO 949

HSD 963 0.38 ASN 997 -0.16 PRO 949

HSD 963 0.33 THR 998 -0.17 PRO 949

GLN 1027 0.30 GLU 999 -0.16 ASN 955

GLN 1027 0.36 ARG 1000 -0.20 ASN 955

HSD 963 0.39 ASP 1001 -0.20 GLN 954

HSD 963 0.40 ASP 1002 -0.21 GLN 954

HSD 963 0.45 ASP 1003 -0.17 GLN 954

HSD 963 0.47 TYR 1004 -0.12 ASP 975

HSD 963 0.51 ALA 1005 -0.11 PRO 949

HSD 963 0.49 GLY 1006 -0.12 LYS 1111

HSD 963 0.48 PHE 1007 -0.15 LYS 1111

HSD 963 0.41 VAL 1008 -0.15 LYS 1111

HSD 963 0.35 PHE 1009 -0.17 LYS 1111

HSD 963 0.29 GLY 1010 -0.19 PHE 985

HSD 963 0.30 TYR 1011 -0.22 ASP 1151

HSD 963 0.23 GLN 1012 -0.27 ASP 1151

HSD 963 0.21 SER 1013 -0.25 THR 1051

HSD 963 0.23 SER 1014 -0.25 THR 1051

GLY 1053 0.21 SER 1015 -0.21 GLY 1070

HSD 963 0.23 ARG 1016 -0.22 GLY 1070

HSD 963 0.29 PHE 1017 -0.17 TYR 1011

HSD 963 0.32 TYR 1018 -0.13 PHE 985

HSD 963 0.38 VAL 1019 -0.13 LYS 1111

HSD 963 0.41 VAL 1020 -0.13 LYS 1111

HSD 963 0.43 MET 1021 -0.10 LYS 1111

HSD 963 0.42 TRP 1022 -0.09 GLN 954

HSD 963 0.41 LYS 1023 -0.13 GLN 954

HSD 963 0.39 GLN 1024 -0.17 GLN 954

HSD 963 0.37 VAL 1025 -0.18 SER 953

HSD 963 0.35 THR 1026 -0.19 GLN 1027

HSD 963 0.37 GLN 1027 -0.19 THR 1026

HSD 963 0.35 SER 1028 -0.15 TYR 1029

HSD 963 0.37 TYR 1029 -0.15 GLY 1039

HSD 963 0.37 TRP 1030 -0.14 THR 952

HSD 963 0.35 ASP 1031 -0.11 GLN 1038

HSD 963 0.30 THR 1032 -0.14 ASN 1067

HSD 963 0.27 ASN 1033 -0.09 ASN 1067

HSD 963 0.24 PRO 1034 -0.09 PHE 985

HSD 963 0.26 THR 1035 -0.14 THR 1068

HSD 963 0.29 ARG 1036 -0.20 ASN 1067

HSD 963 0.32 ALA 1037 -0.15 GLY 1066

HSD 963 0.33 GLN 1038 -0.14 TYR 1029

HSD 963 0.35 GLY 1039 -0.15 TYR 1029

HSD 963 0.35 TYR 1040 -0.16 GLN 1027

HSD 963 0.36 SER 1041 -0.15 SER 953

HSD 963 0.36 GLY 1042 -0.11 SER 953

HSD 963 0.38 LEU 1043 -0.09 GLN 1027

HSD 963 0.36 SER 1044 -0.09 GLN 1038

HSD 963 0.35 VAL 1045 -0.10 LYS 1111

HSD 963 0.32 LYS 1046 -0.11 PHE 985

HSD 963 0.29 VAL 1047 -0.14 GLY 1128

HSD 963 0.27 VAL 1048 -0.17 VAL 1072

HSD 963 0.21 ASN 1049 -0.24 GLY 1070

HSD 963 0.18 SER 1050 -0.24 GLY 1070

ARG 1073 0.20 THR 1051 -0.25 SER 1014

SER 1050 0.17 THR 1052 -0.29 GLY 1053

SER 1015 0.21 GLY 1053 -0.29 THR 1052

SER 1015 0.20 PRO 1054 -0.19 TRP 959

HSD 963 0.20 GLY 1055 -0.15 TRP 959

HSD 963 0.24 GLU 1056 -0.07 ASP 1151

HSD 963 0.22 HSD 1057 -0.09 GLN 943

HSD 963 0.25 LEU 1058 -0.10 PHE 985

HSD 963 0.31 ARG 1059 -0.07 PHE 985

HSD 963 0.31 ASN 1060 -0.09 ALA 1061

HSD 963 0.29 ALA 1061 -0.12 ARG 1036

HSD 963 0.34 LEU 1062 -0.10 PHE 985

HSD 963 0.36 TRP 1063 -0.09 PHE 985

HSD 963 0.32 HSD 1064 -0.11 PHE 985

HSD 963 0.33 THR 1065 -0.13 ALA 1037

ASN 1067 0.29 GLY 1066 -0.18 ARG 1036

GLY 1066 0.29 ASN 1067 -0.20 ARG 1036

HSD 963 0.24 THR 1068 -0.17 ARG 1036

GLY 1066 0.21 PRO 1069 -0.22 ASN 1049

ARG 1073 0.21 GLY 1070 -0.24 SER 1050

HSD 963 0.21 GLN 1071 -0.18 ASN 1049

HSD 963 0.26 VAL 1072 -0.17 VAL 1048

HSD 963 0.26 ARG 1073 -0.16 ARG 1036

HSD 963 0.30 THR 1074 -0.14 ARG 1036

PRO 1152 0.30 LEU 1075 -0.12 ARG 1036

PRO 1152 0.34 TRP 1076 -0.11 GLN 1038

HSD 963 0.32 HSD 1077 -0.11 GLN 1038

PRO 1152 0.34 ASP 1078 -0.12 GLN 1027

PRO 1152 0.35 PRO 1079 -0.15 GLN 1027

PRO 1152 0.34 ARG 1080 -0.16 GLN 1027

HSD 963 0.33 HSD 1081 -0.15 GLN 1027

HSD 963 0.34 ILE 1082 -0.13 SER 953

HSD 963 0.36 GLY 1083 -0.14 GLN 954

HSD 963 0.39 TRP 1084 -0.13 GLN 954

HSD 963 0.34 LYS 1085 -0.15 ASN 973

HSD 963 0.34 ASP 1086 -0.17 ASN 973

HSD 963 0.34 PHE 1087 -0.14 PRO 949

HSD 963 0.36 THR 1088 -0.12 ALA 1089

HSD 963 0.41 ALA 1089 -0.12 THR 1088

HSD 963 0.42 TYR 1090 -0.11 ARG 1091

HSD 963 0.42 ARG 1091 -0.28 LYS 1111

HSD 963 0.41 TRP 1092 -0.27 LYS 1111

HSD 963 0.37 ARG 1093 -0.34 LYS 1111

HSD 963 0.35 LEU 1094 -0.26 LYS 1111

PRO 1152 0.39 SER 1095 -0.24 LYS 1111

PRO 1152 0.34 HSD 1096 -0.20 LYS 1111

PRO 1152 0.45 ARG 1097 -0.17 LYS 1111

PRO 1152 0.25 PRO 1098 -0.18 GLU 984

PRO 1152 0.33 LYS 1099 -0.18 GLU 984

PRO 1152 0.57 THR 1100 -0.16 LYS 1111

PRO 1152 0.43 GLY 1101 -0.16 LYS 1111

PRO 1152 0.61 PHE 1102 -0.18 LYS 1111

PRO 1152 0.49 ILE 1103 -0.19 LYS 1111

PRO 1152 0.52 ARG 1104 -0.21 LYS 1111

PRO 1152 0.40 VAL 1105 -0.23 LYS 1111

PRO 1152 0.40 VAL 1106 -0.25 LYS 1111

HSD 963 0.38 MET 1107 -0.19 LYS 1111

HSD 963 0.36 TYR 1108 -0.24 LYS 1111

HSD 963 0.33 GLU 1109 -0.09 ASN 973

LYS 1111 0.30 GLY 1110 -0.17 ARG 1091

GLY 1110 0.30 LYS 1111 -0.34 ARG 1093

PRO 1152 0.31 LYS 1112 -0.07 THR 1088

PRO 1152 0.39 ILE 1113 -0.10 LYS 1111

PRO 1152 0.36 MET 1114 -0.09 TRP 1084

PRO 1152 0.39 ALA 1115 -0.08 GLN 1027

PRO 1152 0.48 ASP 1116 -0.13 LYS 1111

PRO 1152 0.47 SER 1117 -0.11 LYS 1111

PRO 1152 0.59 GLY 1118 -0.13 LYS 1111

PRO 1152 0.66 PRO 1119 -0.15 LYS 1111

PRO 1152 0.53 ILE 1120 -0.14 LYS 1111

PRO 1152 0.48 TYR 1121 -0.14 LYS 1111

PRO 1152 0.32 ASP 1122 -0.16 GLU 984

PRO 1152 0.22 LYS 1123 -0.22 GLY 1127

HSD 963 0.22 THR 1124 -0.19 GLU 984

HSD 963 0.22 TYR 1125 -0.20 GLU 984

HSD 963 0.21 ALA 1126 -0.22 ASN 986

HSD 963 0.24 GLY 1127 -0.24 ASN 986

HSD 963 0.25 GLY 1128 -0.33 ASP 1151

HSD 963 0.32 ARG 1129 -0.39 ASP 1151

HSD 963 0.38 LEU 1130 -0.27 ASP 1151

HSD 963 0.50 GLY 1131 -0.25 ASP 1151

HSD 963 0.55 LEU 1132 -0.17 ASP 1151

HSD 963 0.52 PHE 1133 -0.11 LYS 1111

HSD 963 0.53 VAL 1134 -0.12 PRO 949

HSD 963 0.48 PHE 1135 -0.13 PRO 949

HSD 963 0.48 SER 1136 -0.17 ASP 975

HSD 963 0.48 GLN 1137 -0.18 PRO 949

HSD 963 0.49 GLU 1138 -0.21 PRO 949

HSD 963 0.49 MET 1139 -0.19 PRO 949

HSD 963 0.56 VAL 1140 -0.17 PRO 949

HSD 963 0.58 PHE 1141 -0.15 CYS 1149

HSD 963 0.63 PHE 1142 -0.18 CYS 1149

HSD 963 0.57 SER 1143 -0.19 ASP 1151

HSD 963 0.50 ASP 1144 -0.20 CYS 1149

HSD 963 0.48 LEU 1145 -0.22 ASP 1151

HSD 963 0.39 LYS 1146 -0.27 CYS 1149

HSD 963 0.30 TYR 1147 -0.28 CYS 1149

HSD 963 0.24 GLU 1148 -0.31 CYS 1149

ASN 986 0.22 CYS 1149 -0.45 THR 937

ARG 1104 0.22 ARG 1150 -0.29 THR 937

PRO 1119 0.43 ASP 1151 -0.70 ASP 983

PRO 1119 0.66 PRO 1152 -0.61 ASP 983

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 15 ---

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

* *