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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 26 ---

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
LYS 1111 0.40 THR 937 -0.20 ASP 983

LYS 1111 0.34 ASP 938 -0.21 ASP 983

LYS 1111 0.35 PHE 939 -0.18 ASP 983

VAL 960 0.41 ARG 940 -0.15 ASP 983

LYS 1111 0.28 ARG 941 -0.15 ALA 1089

LYS 1111 0.24 PHE 942 -0.20 ALA 1089

LYS 1111 0.19 GLN 943 -0.19 ALA 1089

ILE 945 0.21 MET 944 -0.19 ALA 1089

MET 944 0.21 ILE 945 -0.21 THR 952

THR 1052 0.20 PRO 946 -0.26 THR 952

GLY 977 0.19 LEU 947 -0.17 THR 952

GLY 1055 0.21 ASP 948 -0.22 THR 952

ASP 956 0.42 PRO 949 -0.24 THR 952

ASN 955 0.38 LYS 950 -0.22 SER 1015

ARG 1000 0.25 GLY 951 -0.23 PRO 949

ARG 1000 0.32 THR 952 -0.26 PRO 946

ARG 1000 0.27 SER 953 -0.36 ASP 1031

ARG 1000 0.31 GLN 954 -0.49 ASN 955

LYS 950 0.38 ASN 955 -0.49 GLN 954

PRO 949 0.42 ASP 956 -0.28 GLN 954

PRO 949 0.33 PRO 957 -0.17 ASP 1031

ARG 940 0.31 ASN 958 -0.19 ASP 1086

ARG 940 0.36 TRP 959 -0.19 THR 1088

ARG 940 0.41 VAL 960 -0.19 PHE 1087

ARG 940 0.39 VAL 961 -0.20 THR 1088

VAL 960 0.34 ARG 962 -0.17 THR 1088

THR 971 0.26 HSD 963 -0.34 GLY 965

ARG 940 0.28 GLN 964 -0.20 THR 1088

LYS 1111 0.30 GLY 965 -0.34 HSD 963

LYS 1111 0.32 LYS 966 -0.21 ALA 1089

LYS 1111 0.37 GLU 967 -0.24 ALA 1089

ARG 940 0.33 LEU 968 -0.22 ALA 1089

ARG 940 0.30 VAL 969 -0.21 THR 1088

ARG 940 0.28 GLN 970 -0.20 ASP 1086

ARG 940 0.29 THR 971 -0.23 ASP 1086

PRO 949 0.25 VAL 972 -0.19 ASP 1086

LYS 950 0.26 ASN 973 -0.20 TRP 1030

LYS 950 0.31 CYS 974 -0.21 ASP 1031

LYS 950 0.23 ASP 975 -0.20 ASP 1031

ARG 940 0.18 PRO 976 -0.12 THR 1124

LEU 947 0.19 GLY 977 -0.12 ALA 1089

ALA 979 0.21 LEU 978 -0.17 ALA 1089

LEU 978 0.21 ALA 979 -0.23 ALA 1089

LYS 1111 0.20 VAL 980 -0.23 ALA 1089

LYS 1111 0.23 GLY 981 -0.21 ALA 1089

LYS 1111 0.23 TYR 982 -0.17 ALA 1089

LYS 1112 0.24 ASP 983 -0.21 ASP 938

LYS 1112 0.24 GLU 984 -0.17 ALA 1089

LYS 1112 0.27 PHE 985 -0.18 ALA 1089

LYS 1112 0.28 ASN 986 -0.21 ALA 1126

LYS 1112 0.34 ALA 987 -0.16 TYR 1090

LYS 1112 0.36 VAL 988 -0.19 TYR 1090

LYS 1112 0.44 ASP 989 -0.19 GLU 1109

LYS 1112 0.39 PHE 990 -0.23 TYR 1090

LYS 1112 0.42 SER 991 -0.25 GLU 1109

LYS 1111 0.45 GLY 992 -0.29 GLU 1109

LYS 1111 0.55 THR 993 -0.26 GLU 1109

LYS 1111 0.39 PHE 994 -0.27 ALA 1089

LYS 1111 0.34 PHE 995 -0.26 PHE 1141

LYS 1023 0.18 ILE 996 -0.29 LYS 1112

LYS 1111 0.20 ASN 997 -0.29 LYS 1112

ASP 1002 0.14 THR 998 -0.42 LYS 1112

THR 952 0.25 GLU 999 -0.65 LYS 1112

THR 952 0.32 ARG 1000 -0.58 LYS 1112

THR 952 0.27 ASP 1001 -0.43 LYS 1112

SER 953 0.22 ASP 1002 -0.41 LYS 1112

ARG 940 0.14 ASP 1003 -0.24 MET 1114

ALA 1005 0.24 TYR 1004 -0.17 MET 1114

TYR 1004 0.24 ALA 1005 -0.15 MET 1114

HSD 1064 0.21 GLY 1006 -0.27 PHE 1007

LYS 1111 0.20 PHE 1007 -0.27 GLY 1006

LYS 1111 0.18 VAL 1008 -0.18 TYR 1090

LYS 1112 0.22 PHE 1009 -0.21 TYR 1090

LYS 1112 0.22 GLY 1010 -0.17 TYR 1090

PRO 1069 0.18 TYR 1011 -0.18 ALA 1089

GLY 1070 0.21 GLN 1012 -0.16 ALA 1089

GLY 1070 0.24 SER 1013 -0.19 PRO 949

THR 1051 0.23 SER 1014 -0.23 PRO 949

GLY 1070 0.24 SER 1015 -0.27 GLY 1053

GLY 1070 0.25 ARG 1016 -0.20 THR 1124

PRO 1069 0.19 PHE 1017 -0.14 PRO 949

LYS 1112 0.19 TYR 1018 -0.17 VAL 1019

ARG 1036 0.20 VAL 1019 -0.17 TYR 1018

HSD 1064 0.20 VAL 1020 -0.16 MET 1021

GLY 1006 0.20 MET 1021 -0.16 VAL 1020

TYR 1040 0.20 TRP 1022 -0.25 ARG 1000

PHE 1087 0.21 LYS 1023 -0.25 LEU 1043

PHE 1087 0.25 GLN 1024 -0.39 MET 1114

ASP 1086 0.25 VAL 1025 -0.33 LYS 1112

GLY 1083 0.22 THR 1026 -0.26 ARG 1000

ASP 1031 0.19 GLN 1027 -0.22 ARG 1000

THR 1032 0.24 SER 1028 -0.19 ASN 973

ASP 1031 0.19 TYR 1029 -0.17 ARG 1036

ASP 1031 0.26 TRP 1030 -0.24 ASN 955

TRP 1030 0.26 ASP 1031 -0.36 SER 953

ASN 1067 0.27 THR 1032 -0.24 SER 953

GLY 1070 0.19 ASN 1033 -0.21 GLY 951

GLY 1070 0.22 PRO 1034 -0.13 LYS 950

GLN 1071 0.27 THR 1035 -0.13 GLY 951

ASN 1067 0.40 ARG 1036 -0.19 TRP 1030

THR 1032 0.24 ALA 1037 -0.12 ASN 955

THR 1032 0.22 GLN 1038 -0.12 ARG 1000

GLY 1083 0.19 GLY 1039 -0.16 ARG 1000

GLY 1083 0.30 TYR 1040 -0.21 ARG 1000

GLY 1083 0.37 SER 1041 -0.29 ARG 1000

GLU 1109 0.26 GLY 1042 -0.27 ARG 1000

GLU 1109 0.18 LEU 1043 -0.27 ARG 1000

THR 1065 0.20 SER 1044 -0.20 ARG 1000

LYS 1112 0.22 VAL 1045 -0.19 LYS 1023

ARG 1036 0.23 LYS 1046 -0.16 THR 1051

ARG 1036 0.24 VAL 1047 -0.18 THR 1051

VAL 1072 0.25 VAL 1048 -0.24 GLY 1053

PRO 1069 0.34 ASN 1049 -0.28 THR 1124

GLY 1070 0.29 SER 1050 -0.26 THR 1052

SER 1014 0.23 THR 1051 -0.30 THR 1124

GLY 1053 0.33 THR 1052 -0.26 SER 1050

THR 1052 0.33 GLY 1053 -0.27 SER 1015

THR 1052 0.21 PRO 1054 -0.26 SER 1015

ASP 948 0.21 GLY 1055 -0.21 SER 1015

GLU 999 0.15 GLU 1056 -0.12 ARG 1073

PRO 1034 0.17 HSD 1057 -0.19 THR 1068

LEU 1132 0.17 LEU 1058 -0.16 ARG 1073

LEU 1132 0.17 ARG 1059 -0.13 ALA 1061

LEU 1132 0.18 ASN 1060 -0.07 HSD 1064

ARG 1036 0.28 ALA 1061 -0.13 THR 1065

LEU 1132 0.21 LEU 1062 -0.11 LEU 1075

GLY 1006 0.20 TRP 1063 -0.11 GLY 1039

ALA 1037 0.22 HSD 1064 -0.10 HSD 1057

ARG 1036 0.21 THR 1065 -0.14 GLY 1070

ARG 1036 0.31 GLY 1066 -0.21 GLY 1070

ARG 1036 0.40 ASN 1067 -0.23 GLY 1070

ARG 1036 0.38 THR 1068 -0.19 HSD 1057

ASN 1049 0.34 PRO 1069 -0.18 HSD 1057

ASN 1049 0.31 GLY 1070 -0.30 ARG 1073

ASN 1049 0.28 GLN 1071 -0.23 ARG 1073

ARG 1036 0.31 VAL 1072 -0.39 ARG 1073

ARG 1036 0.31 ARG 1073 -0.39 VAL 1072

ARG 1036 0.26 THR 1074 -0.22 VAL 1072

LYS 1112 0.24 LEU 1075 -0.23 THR 1051

LYS 1112 0.24 TRP 1076 -0.19 ARG 1000

GLU 1109 0.23 HSD 1077 -0.20 ARG 1000

GLU 1109 0.32 ASP 1078 -0.24 ARG 1000

GLU 1109 0.33 PRO 1079 -0.23 ARG 1000

GLU 1109 0.43 ARG 1080 -0.27 ARG 1000

GLU 1109 0.33 HSD 1081 -0.30 ARG 1000

GLU 1109 0.43 ILE 1082 -0.37 ARG 1000

SER 1041 0.37 GLY 1083 -0.50 MET 1114

THR 1088 0.29 TRP 1084 -0.61 MET 1114

ILE 1082 0.28 LYS 1085 -0.67 LYS 1112

VAL 1025 0.25 ASP 1086 -0.55 LYS 1112

TRP 1084 0.26 PHE 1087 -0.46 LYS 1112

ILE 1082 0.34 THR 1088 -0.43 LYS 1112

LYS 1111 0.44 ALA 1089 -0.28 PHE 1142

LYS 1111 0.47 TYR 1090 -0.28 ARG 1091

LYS 1111 0.54 ARG 1091 -0.49 GLU 1109

LYS 1111 0.38 TRP 1092 -0.25 GLU 1109

LYS 1112 0.50 ARG 1093 -0.26 GLU 1109

LYS 1112 0.44 LEU 1094 -0.19 TYR 1090

LYS 1112 0.45 SER 1095 -0.17 TRP 1084

LYS 1112 0.37 HSD 1096 -0.15 TRP 1084

LYS 1112 0.37 ARG 1097 -0.14 TRP 1084

LYS 1112 0.31 PRO 1098 -0.13 THR 1051

LYS 1112 0.32 LYS 1099 -0.17 THR 1051

LYS 1112 0.36 THR 1100 -0.20 THR 1051

LYS 1112 0.34 GLY 1101 -0.20 THR 1051

LYS 1112 0.41 PHE 1102 -0.17 THR 1051

LYS 1112 0.40 ILE 1103 -0.17 ARG 1000

LYS 1112 0.48 ARG 1104 -0.21 GLY 1083

LYS 1112 0.41 VAL 1105 -0.22 TRP 1084

LYS 1112 0.52 VAL 1106 -0.29 TRP 1084

TRP 1092 0.30 MET 1107 -0.30 TRP 1084

LYS 1111 0.31 TYR 1108 -0.29 GLU 1109

ARG 1080 0.43 GLU 1109 -0.49 ARG 1091

LYS 1111 0.41 GLY 1110 -0.25 ARG 1091

THR 993 0.55 LYS 1111 -0.31 ILE 1113

GLY 1118 0.54 LYS 1112 -0.67 LYS 1085

LYS 1112 0.45 ILE 1113 -0.40 ARG 1000

ALA 1115 0.37 MET 1114 -0.61 TRP 1084

MET 1114 0.37 ALA 1115 -0.40 GLY 1083

LYS 1112 0.44 ASP 1116 -0.30 GLY 1083

LYS 1112 0.43 SER 1117 -0.25 ARG 1000

LYS 1112 0.54 GLY 1118 -0.22 ARG 1000

LYS 1112 0.53 PRO 1119 -0.18 ARG 1000

LYS 1112 0.42 ILE 1120 -0.20 THR 1051

LYS 1112 0.39 TYR 1121 -0.25 THR 1051

LYS 1112 0.32 ASP 1122 -0.29 THR 1051

LYS 1112 0.29 LYS 1123 -0.26 THR 1051

LYS 1112 0.23 THR 1124 -0.30 THR 1051

LYS 1112 0.22 TYR 1125 -0.15 GLY 1053

LYS 1112 0.24 ALA 1126 -0.21 ASN 986

LYS 1112 0.24 GLY 1127 -0.17 TYR 1090

LYS 1112 0.20 GLY 1128 -0.20 ALA 1089

LYS 1112 0.21 ARG 1129 -0.20 ALA 1089

LYS 1112 0.20 LEU 1130 -0.24 ALA 1089

LYS 1111 0.23 GLY 1131 -0.21 ALA 1089

PHE 1133 0.29 LEU 1132 -0.24 PHE 994

LEU 1132 0.29 PHE 1133 -0.14 ALA 1089

ARG 940 0.19 VAL 1134 -0.13 ASP 1086

ARG 940 0.18 PHE 1135 -0.12 MET 1114

LYS 950 0.19 SER 1136 -0.16 MET 1114

LYS 950 0.19 GLN 1137 -0.22 MET 1114

ARG 940 0.25 GLU 1138 -0.23 ASP 1086

ARG 940 0.23 MET 1139 -0.28 ASP 1086

LYS 1111 0.24 VAL 1140 -0.22 ASP 1086

LYS 1111 0.32 PHE 1141 -0.26 PHE 995

LYS 1111 0.39 PHE 1142 -0.28 ALA 1089

LYS 1111 0.47 SER 1143 -0.24 ALA 1089

LYS 1111 0.53 ASP 1144 -0.23 GLU 1109

LYS 1111 0.43 LEU 1145 -0.22 GLU 1109

LYS 1111 0.41 LYS 1146 -0.19 GLU 1109

LYS 1112 0.38 TYR 1147 -0.20 GLU 1109

LYS 1112 0.40 GLU 1148 -0.22 CYS 1149

LYS 1112 0.33 CYS 1149 -0.22 GLU 1148

LYS 1112 0.40 ARG 1150 -0.15 GLY 1110

LYS 1112 0.39 ASP 1151 -0.16 CYS 1149

LYS 1112 0.45 PRO 1152 -0.15 ASN 986

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 26 ---

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

* *