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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 22 ---

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
GLN 964 0.56 THR 937 -0.66 LYS 966

GLN 964 0.63 ASP 938 -0.74 LYS 966

GLN 964 0.66 PHE 939 -0.77 LYS 966

GLN 964 0.88 ARG 940 -0.94 LYS 966

GLN 964 0.63 ARG 941 -0.85 HSD 963

GLN 964 0.49 PHE 942 -0.78 HSD 963

GLN 964 0.37 GLN 943 -0.64 HSD 963

GLN 964 0.26 MET 944 -0.54 HSD 963

GLN 964 0.23 ILE 945 -0.41 HSD 963

PHE 942 0.17 PRO 946 -0.31 HSD 963

GLN 964 0.18 LEU 947 -0.25 HSD 963

LYS 1111 0.17 ASP 948 -0.20 HSD 963

LYS 1111 0.14 PRO 949 -0.23 HSD 963

PRO 1079 0.18 LYS 950 -0.19 HSD 963

PRO 1079 0.19 GLY 951 -0.15 HSD 963

PRO 1079 0.15 THR 952 -0.14 HSD 963

LYS 966 0.18 SER 953 -0.13 SER 1015

LYS 966 0.22 GLN 954 -0.14 THR 1124

LYS 966 0.18 ASN 955 -0.13 LYS 1099

LYS 966 0.15 ASP 956 -0.17 HSD 963

LYS 966 0.17 PRO 957 -0.20 HSD 963

VAL 961 0.18 ASN 958 -0.20 HSD 963

VAL 961 0.16 TRP 959 -0.30 HSD 963

VAL 961 0.40 VAL 960 -0.23 LEU 1145

VAL 960 0.40 VAL 961 -0.47 LEU 968

HSD 963 0.30 ARG 962 -0.31 LEU 1145

ARG 962 0.30 HSD 963 -0.85 ARG 941

ARG 940 0.88 GLN 964 -0.26 ARG 962

GLU 967 0.85 GLY 965 -0.64 HSD 963

GLU 967 0.63 LYS 966 -0.94 ARG 940

GLY 965 0.85 GLU 967 -0.46 SER 1143

GLY 965 0.53 LEU 968 -0.47 VAL 961

LYS 966 0.49 VAL 969 -0.24 GLY 992

LYS 966 0.33 GLN 970 -0.22 PHE 1007

LYS 966 0.40 THR 971 -0.20 PHE 1007

LYS 966 0.31 VAL 972 -0.17 PHE 1009

LYS 966 0.33 ASN 973 -0.14 THR 1124

LYS 966 0.25 CYS 974 -0.15 THR 1124

LYS 966 0.20 ASP 975 -0.14 THR 1124

GLY 965 0.19 PRO 976 -0.17 THR 1124

PHE 942 0.21 GLY 977 -0.27 HSD 963

GLN 964 0.28 LEU 978 -0.36 HSD 963

GLN 964 0.35 ALA 979 -0.50 HSD 963

GLN 964 0.40 VAL 980 -0.53 HSD 963

GLN 964 0.44 GLY 981 -0.62 HSD 963

GLN 964 0.42 TYR 982 -0.61 HSD 963

GLN 964 0.36 ASP 983 -0.56 HSD 963

GLN 964 0.30 GLU 984 -0.49 HSD 963

GLY 1127 0.25 PHE 985 -0.48 HSD 963

GLY 1127 0.27 ASN 986 -0.42 HSD 963

GLN 964 0.20 ALA 987 -0.40 HSD 963

GLN 964 0.23 VAL 988 -0.40 HSD 963

GLN 964 0.27 ASP 989 -0.34 HSD 963

GLN 964 0.29 PHE 990 -0.37 HSD 963

GLN 964 0.29 SER 991 -0.32 VAL 961

GLN 964 0.30 GLY 992 -0.36 VAL 961

GLY 965 0.37 THR 993 -0.29 VAL 961

GLY 965 0.41 PHE 994 -0.22 VAL 961

GLY 965 0.45 PHE 995 -0.16 ASP 1151

LYS 966 0.45 ILE 996 -0.15 ASP 1151

LYS 966 0.57 ASN 997 -0.15 ASP 1151

LYS 966 0.49 THR 998 -0.14 ASP 1151

LYS 966 0.41 GLU 999 -0.14 ILE 1082

LYS 966 0.38 ARG 1000 -0.13 ASP 1151

LYS 966 0.35 ASP 1001 -0.12 VAL 1045

LYS 966 0.32 ASP 1002 -0.13 VAL 1045

LYS 966 0.30 ASP 1003 -0.13 ASP 1002

GLY 965 0.30 TYR 1004 -0.15 VAL 1045

GLY 965 0.30 ALA 1005 -0.15 GLU 1138

GLY 965 0.26 GLY 1006 -0.21 HSD 963

GLN 964 0.27 PHE 1007 -0.32 HSD 963

GLN 964 0.28 VAL 1008 -0.35 HSD 963

GLN 964 0.26 PHE 1009 -0.40 HSD 963

GLN 964 0.25 GLY 1010 -0.40 HSD 963

GLN 964 0.28 TYR 1011 -0.40 HSD 963

GLN 964 0.26 GLN 1012 -0.39 HSD 963

GLN 964 0.25 SER 1013 -0.36 HSD 963

GLN 964 0.23 SER 1014 -0.34 HSD 963

GLN 964 0.21 SER 1015 -0.29 HSD 963

GLN 964 0.23 ARG 1016 -0.31 HSD 963

GLN 964 0.24 PHE 1017 -0.33 HSD 963

LYS 1111 0.23 TYR 1018 -0.30 HSD 963

LYS 1111 0.24 VAL 1019 -0.26 HSD 963

LYS 1111 0.28 VAL 1020 -0.24 HSD 963

LYS 1111 0.28 MET 1021 -0.18 HSD 963

LYS 1111 0.26 TRP 1022 -0.14 HSD 963

GLU 1109 0.28 LYS 1023 -0.16 VAL 1045

GLU 1109 0.27 GLN 1024 -0.13 SER 1044

LYS 1085 0.27 VAL 1025 -0.16 THR 1074

GLN 1027 0.31 THR 1026 -0.19 THR 1074

THR 1026 0.31 GLN 1027 -0.19 ARG 1073

THR 1032 0.34 SER 1028 -0.20 ARG 1073

ARG 1080 0.30 TYR 1029 -0.18 ALA 1061

ARG 1080 0.26 TRP 1030 -0.14 ALA 1061

PRO 1079 0.29 ASP 1031 -0.15 SER 1050

PRO 1079 0.37 THR 1032 -0.18 SER 1050

PRO 1079 0.37 ASN 1033 -0.15 THR 1051

PRO 1079 0.37 PRO 1034 -0.19 THR 1051

PRO 1079 0.41 THR 1035 -0.21 GLY 1070

PRO 1079 0.46 ARG 1036 -0.20 GLY 1070

PRO 1079 0.39 ALA 1037 -0.18 ASN 1067

ARG 1080 0.43 GLN 1038 -0.21 ARG 1073

ARG 1036 0.35 GLY 1039 -0.22 THR 1065

HSD 1081 0.41 TYR 1040 -0.18 THR 1074

GLN 1038 0.33 SER 1041 -0.13 LEU 1075

ARG 1036 0.29 GLY 1042 -0.13 GLN 1024

HSD 1064 0.26 LEU 1043 -0.15 HSD 963

HSD 1064 0.25 SER 1044 -0.17 HSD 963

LYS 1111 0.27 VAL 1045 -0.21 HSD 963

LYS 1111 0.24 LYS 1046 -0.21 HSD 963

LYS 1111 0.22 VAL 1047 -0.25 HSD 963

LYS 1111 0.21 VAL 1048 -0.25 HSD 963

GLN 964 0.20 ASN 1049 -0.24 HSD 963

LYS 1111 0.19 SER 1050 -0.22 HSD 963

GLN 964 0.19 THR 1051 -0.20 THR 1035

PRO 1079 0.20 THR 1052 -0.20 HSD 963

GLN 964 0.18 GLY 1053 -0.24 HSD 963

LYS 1111 0.18 PRO 1054 -0.24 HSD 963

PRO 1079 0.20 GLY 1055 -0.22 PRO 1054

PRO 1079 0.26 GLU 1056 -0.15 SER 1015

PRO 1079 0.29 HSD 1057 -0.16 PRO 1034

PRO 1079 0.24 LEU 1058 -0.17 HSD 963

PRO 1079 0.22 ARG 1059 -0.17 SER 1015

PRO 1079 0.32 ASN 1060 -0.15 SER 1050

PRO 1079 0.30 ALA 1061 -0.18 TYR 1029

LYS 1111 0.25 LEU 1062 -0.17 TRP 1063

LYS 1111 0.25 TRP 1063 -0.18 ARG 1073

PRO 1079 0.38 HSD 1064 -0.22 ARG 1073

PRO 1079 0.38 THR 1065 -0.22 GLY 1039

PRO 1079 0.41 GLY 1066 -0.20 ARG 1073

PRO 1079 0.38 ASN 1067 -0.21 GLN 1038

PRO 1079 0.34 THR 1068 -0.16 ARG 1036

PRO 1079 0.30 PRO 1069 -0.19 ARG 1036

PRO 1079 0.25 GLY 1070 -0.21 THR 1035

PRO 1079 0.23 GLN 1071 -0.19 ARG 1036

PRO 1079 0.24 VAL 1072 -0.18 HSD 963

LYS 1111 0.20 ARG 1073 -0.22 HSD 1064

LYS 1111 0.22 THR 1074 -0.20 GLY 1039

LYS 1111 0.20 LEU 1075 -0.20 HSD 963

ASN 1067 0.28 TRP 1076 -0.18 HSD 963

GLY 1066 0.31 HSD 1077 -0.14 HSD 963

ARG 1036 0.31 ASP 1078 -0.15 HSD 963

ARG 1036 0.46 PRO 1079 -0.16 LYS 1085

ARG 1036 0.43 ARG 1080 -0.22 LYS 1085

GLN 1038 0.41 HSD 1081 -0.20 GLY 1083

GLN 1038 0.33 ILE 1082 -0.25 GLY 1083

GLN 1027 0.27 GLY 1083 -0.25 ILE 1082

GLU 1109 0.31 TRP 1084 -0.24 ILE 1082

GLY 965 0.28 LYS 1085 -0.22 ILE 1082

LYS 966 0.36 ASP 1086 -0.17 ILE 1082

LYS 966 0.43 PHE 1087 -0.16 ARG 1080

GLY 965 0.35 THR 1088 -0.17 ARG 1080

GLY 965 0.38 ALA 1089 -0.16 VAL 961

GLY 965 0.31 TYR 1090 -0.19 VAL 961

LYS 1111 0.38 ARG 1091 -0.26 VAL 961

LYS 1111 0.35 TRP 1092 -0.25 VAL 961

LYS 1111 0.35 ARG 1093 -0.28 VAL 961

LYS 1111 0.27 LEU 1094 -0.32 HSD 963

LYS 1111 0.24 SER 1095 -0.32 HSD 963

LYS 1111 0.21 HSD 1096 -0.35 HSD 963

LYS 1111 0.18 ARG 1097 -0.35 HSD 963

LYS 1111 0.16 PRO 1098 -0.39 HSD 963

LYS 1111 0.15 LYS 1099 -0.38 HSD 963

LYS 1111 0.20 THR 1100 -0.33 HSD 963

LYS 1111 0.20 GLY 1101 -0.32 HSD 963

LYS 1111 0.23 PHE 1102 -0.30 HSD 963

LYS 1111 0.25 ILE 1103 -0.30 HSD 963

LYS 1111 0.29 ARG 1104 -0.27 HSD 963

LYS 1111 0.32 VAL 1105 -0.26 HSD 963

LYS 1111 0.39 VAL 1106 -0.23 ARG 1150

LYS 1111 0.38 MET 1107 -0.21 VAL 961

LYS 1111 0.57 TYR 1108 -0.22 VAL 961

TRP 1084 0.31 GLU 1109 -0.15 PRO 1152

GLY 965 0.29 GLY 1110 -0.13 VAL 961

TYR 1108 0.57 LYS 1111 -0.10 VAL 961

VAL 1025 0.22 LYS 1112 -0.22 PRO 1152

GLN 1038 0.23 ILE 1113 -0.25 GLU 1148

GLN 1038 0.28 MET 1114 -0.21 ASP 1151

ARG 1036 0.25 ALA 1115 -0.20 ARG 1150

LYS 1111 0.24 ASP 1116 -0.23 ARG 1150

LYS 1111 0.24 SER 1117 -0.21 HSD 963

LYS 1111 0.22 GLY 1118 -0.23 ARG 1150

LYS 1111 0.23 PRO 1119 -0.24 HSD 963

LYS 1111 0.22 ILE 1120 -0.25 HSD 963

LYS 1111 0.22 TYR 1121 -0.26 HSD 963

LYS 1111 0.21 ASP 1122 -0.28 HSD 963

LYS 1111 0.19 LYS 1123 -0.30 HSD 963

ASN 986 0.19 THR 1124 -0.31 HSD 963

ASN 986 0.20 TYR 1125 -0.35 HSD 963

ASN 986 0.23 ALA 1126 -0.38 HSD 963

ASN 986 0.27 GLY 1127 -0.40 HSD 963

GLN 964 0.24 GLY 1128 -0.47 HSD 963

GLN 964 0.32 ARG 1129 -0.48 HSD 963

GLN 964 0.32 LEU 1130 -0.49 HSD 963

GLN 964 0.39 GLY 1131 -0.44 HSD 963

GLN 964 0.34 LEU 1132 -0.37 HSD 963

GLN 964 0.29 PHE 1133 -0.25 HSD 963

GLY 965 0.27 VAL 1134 -0.18 HSD 963

GLY 965 0.26 PHE 1135 -0.16 THR 1124

LYS 966 0.30 SER 1136 -0.14 THR 1124

LYS 966 0.33 GLN 1137 -0.15 PHE 1007

LYS 966 0.41 GLU 1138 -0.17 PHE 1007

LYS 966 0.52 MET 1139 -0.16 ASP 1151

LYS 966 0.46 VAL 1140 -0.20 PHE 1007

GLY 965 0.50 PHE 1141 -0.20 GLY 992

GLY 965 0.56 PHE 1142 -0.30 GLY 992

GLY 965 0.60 SER 1143 -0.46 GLU 967

GLN 964 0.43 ASP 1144 -0.39 GLU 967

GLN 964 0.43 LEU 1145 -0.45 GLU 967

GLN 964 0.40 LYS 1146 -0.47 LYS 966

GLN 964 0.35 TYR 1147 -0.46 LYS 966

GLN 964 0.32 GLU 1148 -0.42 LYS 966

GLN 964 0.23 CYS 1149 -0.45 LYS 966

GLN 964 0.21 ARG 1150 -0.36 LYS 966

ALA 1126 0.18 ASP 1151 -0.41 LYS 966

ALA 1126 0.22 PRO 1152 -0.37 LYS 966

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 22 ---

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

* *