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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 8 ---

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 0.65 THR 937 -0.07 SER 1143

HSD 963 0.56 ASP 938 -0.11 SER 1143

HSD 963 0.48 PHE 939 -0.15 SER 1143

ARG 962 0.59 ARG 940 -0.37 LYS 966

ARG 962 0.32 ARG 941 -0.43 LYS 966

TRP 959 0.21 PHE 942 -0.39 GLY 965

ASN 958 0.14 GLN 943 -0.46 GLY 965

ASN 958 0.17 MET 944 -0.47 GLY 965

ASP 956 0.08 ILE 945 -0.46 HSD 963

ASP 956 0.09 PRO 946 -0.55 HSD 963

GLN 954 0.03 LEU 947 -0.45 HSD 963

SER 953 0.04 ASP 948 -0.53 HSD 963

SER 953 0.04 PRO 949 -0.64 HSD 963

ARG 1000 0.03 LYS 950 -0.60 HSD 963

ARG 1000 0.04 GLY 951 -0.58 HSD 963

ARG 1000 0.04 THR 952 -0.64 HSD 963

ARG 1000 0.05 SER 953 -0.56 HSD 963

PRO 946 0.06 GLN 954 -0.60 HSD 963

MET 944 0.07 ASN 955 -0.71 HSD 963

MET 944 0.09 ASP 956 -0.72 HSD 963

MET 944 0.15 PRO 957 -0.63 HSD 963

PHE 942 0.18 ASN 958 -0.76 HSD 963

ARG 940 0.25 TRP 959 -0.54 HSD 963

ARG 940 0.34 VAL 960 -0.54 VAL 961

ARG 940 0.41 VAL 961 -0.54 VAL 960

ARG 940 0.59 ARG 962 -0.54 ASN 958

THR 937 0.65 HSD 963 -0.76 ASN 958

ASP 1144 0.69 GLN 964 -0.50 PRO 949

ASP 1144 0.87 GLY 965 -0.47 MET 944

ASP 1144 0.72 LYS 966 -0.43 ARG 941

LYS 966 0.45 GLU 967 -0.22 ARG 940

PHE 1142 0.21 LEU 968 -0.13 GLN 943

LYS 1111 0.12 VAL 969 -0.18 HSD 963

THR 971 0.10 GLN 970 -0.37 HSD 963

PHE 942 0.11 THR 971 -0.48 HSD 963

MET 944 0.10 VAL 972 -0.54 HSD 963

MET 944 0.07 ASN 973 -0.48 HSD 963

MET 944 0.09 CYS 974 -0.54 HSD 963

PRO 946 0.06 ASP 975 -0.52 HSD 963

PRO 946 0.03 PRO 976 -0.42 HSD 963

CYS 974 0.08 GLY 977 -0.42 HSD 963

ASN 958 0.07 LEU 978 -0.29 HSD 963

ASN 958 0.14 ALA 979 -0.25 GLY 965

ASN 958 0.11 VAL 980 -0.17 GLY 965

ARG 962 0.20 GLY 981 -0.13 LYS 966

ARG 962 0.20 TYR 982 -0.18 LYS 966

HSD 963 0.24 ASP 983 -0.07 LYS 966

ARG 962 0.18 GLU 984 -0.03 LYS 966

HSD 963 0.23 PHE 985 -0.03 ILE 1113

HSD 963 0.21 ASN 986 -0.04 ILE 1113

HSD 963 0.25 ALA 987 -0.04 ILE 1113

HSD 963 0.30 VAL 988 -0.05 VAL 1106

GLY 965 0.39 ASP 989 -0.07 ARG 1093

GLY 965 0.40 PHE 990 -0.06 TRP 1092

GLY 965 0.51 SER 991 -0.07 TYR 1090

GLY 965 0.54 GLY 992 -0.06 PHE 995

LYS 966 0.60 THR 993 -0.09 LEU 1145

LYS 966 0.50 PHE 994 -0.10 PHE 995

LYS 966 0.49 PHE 995 -0.10 PHE 994

LYS 966 0.34 ILE 996 -0.06 ARG 962

LYS 966 0.33 ASN 997 -0.09 ARG 962

LYS 966 0.23 THR 998 -0.16 ARG 962

LYS 966 0.22 GLU 999 -0.14 HSD 963

LYS 966 0.15 ARG 1000 -0.24 HSD 963

LYS 966 0.13 ASP 1001 -0.26 HSD 963

LYS 966 0.17 ASP 1002 -0.20 HSD 963

LYS 966 0.14 ASP 1003 -0.23 HSD 963

LYS 966 0.15 TYR 1004 -0.19 HSD 963

LYS 966 0.19 ALA 1005 -0.12 HSD 963

LYS 966 0.20 GLY 1006 -0.03 HSD 963

LYS 966 0.16 PHE 1007 -0.03 GLY 1006

LYS 966 0.09 VAL 1008 -0.02 THR 1088

ARG 962 0.11 PHE 1009 -0.02 THR 1088

ARG 962 0.09 GLY 1010 -0.02 LYS 1112

ASN 958 0.05 TYR 1011 -0.07 GLN 964

ASN 958 0.04 GLN 1012 -0.13 GLN 964

ASP 1151 0.04 SER 1013 -0.23 GLN 964

GLN 954 0.03 SER 1014 -0.29 HSD 963

GLY 1053 0.03 SER 1015 -0.25 HSD 963

ASN 986 0.03 ARG 1016 -0.16 HSD 963

GLU 967 0.03 PHE 1017 -0.10 HSD 963

LYS 966 0.07 TYR 1018 -0.04 HSD 963

LYS 966 0.10 VAL 1019 -0.06 HSD 963

LYS 966 0.18 VAL 1020 -0.03 TRP 959

LYS 966 0.18 MET 1021 -0.07 HSD 963

LYS 966 0.23 TRP 1022 -0.05 HSD 963

LYS 966 0.20 LYS 1023 -0.12 HSD 963

LYS 966 0.22 GLN 1024 -0.10 HSD 963

LYS 966 0.18 VAL 1025 -0.14 HSD 963

LYS 966 0.15 THR 1026 -0.17 HSD 963

LYS 966 0.10 GLN 1027 -0.23 HSD 963

LYS 966 0.06 SER 1028 -0.27 HSD 963

GLU 999 0.04 TYR 1029 -0.33 HSD 963

ARG 1000 0.05 TRP 1030 -0.37 HSD 963

ARG 1000 0.04 ASP 1031 -0.40 HSD 963

GLU 999 0.04 THR 1032 -0.36 HSD 963

ARG 1000 0.03 ASN 1033 -0.39 HSD 963

ARG 1000 0.03 PRO 1034 -0.38 HSD 963

GLU 999 0.03 THR 1035 -0.32 HSD 963

SER 1028 0.03 ARG 1036 -0.29 HSD 963

GLU 967 0.05 ALA 1037 -0.27 HSD 963

LYS 966 0.08 GLN 1038 -0.23 HSD 963

LYS 966 0.11 GLY 1039 -0.20 HSD 963

LYS 966 0.15 TYR 1040 -0.14 HSD 963

LYS 966 0.20 SER 1041 -0.10 HSD 963

LYS 966 0.23 GLY 1042 -0.04 TRP 959

LYS 966 0.24 LEU 1043 -0.04 PRO 1152

LYS 966 0.19 SER 1044 -0.04 TRP 959

LYS 966 0.16 VAL 1045 -0.03 TRP 959

LYS 966 0.10 LYS 1046 -0.08 HSD 963

LYS 966 0.06 VAL 1047 -0.09 HSD 963

GLU 967 0.03 VAL 1048 -0.16 HSD 963

ASN 986 0.02 ASN 1049 -0.18 HSD 963

ASN 986 0.02 SER 1050 -0.26 HSD 963

ALA 1037 0.02 THR 1051 -0.28 HSD 963

ASN 986 0.02 THR 1052 -0.35 HSD 963

SER 1015 0.03 GLY 1053 -0.36 HSD 963

PHE 985 0.03 PRO 1054 -0.43 HSD 963

ARG 1000 0.03 GLY 1055 -0.47 HSD 963

ARG 1000 0.03 GLU 1056 -0.45 HSD 963

ARG 1000 0.03 HSD 1057 -0.38 HSD 963

ARG 1000 0.02 LEU 1058 -0.35 HSD 963

ARG 1000 0.03 ARG 1059 -0.38 HSD 963

ARG 1000 0.03 ASN 1060 -0.34 HSD 963

GLU 967 0.03 ALA 1061 -0.27 HSD 963

GLU 967 0.04 LEU 1062 -0.25 HSD 963

GLU 967 0.06 TRP 1063 -0.26 HSD 963

LYS 966 0.07 HSD 1064 -0.22 HSD 963

LYS 966 0.11 THR 1065 -0.15 HSD 963

LYS 966 0.09 GLY 1066 -0.14 HSD 963

LYS 966 0.06 ASN 1067 -0.16 HSD 963

GLU 967 0.04 THR 1068 -0.22 HSD 963

GLY 1066 0.03 PRO 1069 -0.23 HSD 963

GLY 1066 0.02 GLY 1070 -0.23 HSD 963

ARG 1000 0.02 GLN 1071 -0.25 HSD 963

GLU 967 0.04 VAL 1072 -0.19 HSD 963

LYS 966 0.06 ARG 1073 -0.13 HSD 963

LYS 966 0.10 THR 1074 -0.09 HSD 963

LYS 966 0.13 LEU 1075 -0.04 TRP 959

LYS 966 0.17 TRP 1076 -0.04 PRO 1152

LYS 966 0.19 HSD 1077 -0.04 PRO 1152

LYS 966 0.23 ASP 1078 -0.05 PRO 1152

LYS 966 0.21 PRO 1079 -0.05 PRO 1152

LYS 966 0.24 ARG 1080 -0.05 PRO 1152

LYS 966 0.22 HSD 1081 -0.04 PRO 1152

LYS 966 0.27 ILE 1082 -0.04 PRO 1152

LYS 966 0.27 GLY 1083 -0.05 MET 1114

LYS 966 0.33 TRP 1084 -0.04 MET 1114

LYS 966 0.34 LYS 1085 -0.05 ARG 1091

LYS 966 0.33 ASP 1086 -0.06 ARG 1091

LYS 966 0.42 PHE 1087 -0.06 ARG 1091

LYS 966 0.50 THR 1088 -0.08 ARG 1091

LYS 966 0.63 ALA 1089 -0.08 THR 1088

LYS 966 0.55 TYR 1090 -0.14 ARG 1091

LYS 966 0.56 ARG 1091 -0.14 TYR 1090

GLY 965 0.44 TRP 1092 -0.06 TYR 1090

GLY 965 0.45 ARG 1093 -0.07 ASP 989

GLY 965 0.35 LEU 1094 -0.06 ASP 989

GLY 965 0.33 SER 1095 -0.07 VAL 1105

GLY 965 0.24 HSD 1096 -0.04 VAL 1105

GLY 965 0.22 ARG 1097 -0.05 PRO 1152

GLY 965 0.15 PRO 1098 -0.03 LYS 1112

GLY 965 0.16 LYS 1099 -0.03 PRO 1152

GLY 965 0.18 THR 1100 -0.05 PRO 1152

GLY 965 0.15 GLY 1101 -0.03 PRO 1152

GLY 965 0.21 PHE 1102 -0.06 PRO 1152

GLY 965 0.22 ILE 1103 -0.05 PRO 1152

GLY 965 0.28 ARG 1104 -0.06 PRO 1152

GLY 965 0.31 VAL 1105 -0.07 SER 1095

GLY 965 0.37 VAL 1106 -0.06 PRO 1152

LYS 966 0.40 MET 1107 -0.06 ASP 989

LYS 966 0.48 TYR 1108 -0.06 ARG 1150

LYS 966 0.52 GLU 1109 -0.05 ARG 1150

LYS 966 0.62 GLY 1110 -0.05 ARG 1150

GLY 965 0.62 LYS 1111 -0.07 PRO 1152

GLY 965 0.50 LYS 1112 -0.11 ILE 1113

GLY 965 0.43 ILE 1113 -0.11 LYS 1112

LYS 966 0.38 MET 1114 -0.07 LYS 1112

LYS 966 0.33 ALA 1115 -0.06 LYS 1112

GLY 965 0.32 ASP 1116 -0.07 PRO 1152

GLY 965 0.26 SER 1117 -0.06 PRO 1152

GLY 965 0.27 GLY 1118 -0.07 PRO 1152

GLY 965 0.25 PRO 1119 -0.06 PRO 1152

GLY 965 0.20 ILE 1120 -0.05 PRO 1152

GLY 965 0.16 TYR 1121 -0.04 PRO 1152

GLY 965 0.11 ASP 1122 -0.02 PRO 1152

GLY 965 0.08 LYS 1123 -0.02 LYS 1112

GLU 967 0.04 THR 1124 -0.02 HSD 963

ARG 962 0.05 TYR 1125 -0.02 LYS 1112

ARG 962 0.08 ALA 1126 -0.03 LYS 1112

ARG 962 0.11 GLY 1127 -0.03 LYS 1112

ARG 962 0.11 GLY 1128 -0.02 LYS 1112

ARG 962 0.13 ARG 1129 -0.03 LYS 966

ARG 962 0.16 LEU 1130 -0.03 TYR 1090

ARG 962 0.11 GLY 1131 -0.03 PHE 995

ASN 958 0.08 LEU 1132 -0.04 HSD 963

GLU 967 0.07 PHE 1133 -0.16 HSD 963

GLU 967 0.06 VAL 1134 -0.26 HSD 963

GLU 967 0.05 PHE 1135 -0.33 HSD 963

GLU 967 0.04 SER 1136 -0.39 HSD 963

LYS 966 0.09 GLN 1137 -0.31 HSD 963

LYS 966 0.07 GLU 1138 -0.36 HSD 963

LYS 966 0.14 MET 1139 -0.25 HSD 963

LYS 966 0.22 VAL 1140 -0.14 HSD 963

LYS 966 0.35 PHE 1141 -0.06 ARG 940

LYS 966 0.39 PHE 1142 -0.11 ARG 940

LYS 966 0.69 SER 1143 -0.17 ARG 940

GLY 965 0.87 ASP 1144 -0.10 ARG 940

GLY 965 0.62 LEU 1145 -0.09 THR 993

GLY 965 0.61 LYS 1146 -0.06 THR 993

GLY 965 0.47 TYR 1147 -0.06 TYR 1090

HSD 963 0.46 GLU 1148 -0.05 TYR 1090

HSD 963 0.40 CYS 1149 -0.05 ILE 1113

HSD 963 0.35 ARG 1150 -0.06 ILE 1113

HSD 963 0.33 ASP 1151 -0.06 ILE 1113

HSD 963 0.31 PRO 1152 -0.07 ILE 1113

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 8 ---

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

* *