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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 20 ---

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
CYS 1149 0.27 THR 937 -0.41 GLN 964

CYS 1149 0.25 ASP 938 -0.46 GLY 965

ASP 1151 0.15 PHE 939 -0.40 LEU 968

ASP 1151 0.17 ARG 940 -0.65 LEU 968

PRO 1152 0.19 ARG 941 -0.47 PRO 949

PRO 1152 0.14 PHE 942 -0.58 ILE 945

HSD 963 0.11 GLN 943 -0.44 ILE 945

ALA 979 0.24 MET 944 -0.70 ILE 945

ASP 956 0.07 ILE 945 -0.70 MET 944

SER 1013 0.10 PRO 946 -0.51 MET 944

LYS 1046 0.08 LEU 947 -0.46 PHE 942

PRO 949 0.18 ASP 948 -0.43 MET 944

ASP 948 0.18 PRO 949 -0.57 MET 944

PRO 1079 0.16 LYS 950 -0.43 MET 944

PRO 1079 0.16 GLY 951 -0.38 ARG 940

SER 953 0.20 THR 952 -0.44 ASN 955

THR 952 0.20 SER 953 -0.30 ARG 940

ASP 975 0.10 GLN 954 -0.32 ARG 940

PHE 1135 0.12 ASN 955 -0.44 THR 952

GLY 977 0.18 ASP 956 -0.39 ARG 940

VAL 1134 0.13 PRO 957 -0.41 PRO 949

PHE 1007 0.15 ASN 958 -0.44 ARG 940

LYS 1111 0.15 TRP 959 -0.54 ARG 940

LYS 1111 0.16 VAL 960 -0.58 ARG 940

LYS 1111 0.14 VAL 961 -0.62 ARG 940

LYS 1111 0.11 ARG 962 -0.50 ARG 940

ALA 979 0.15 HSD 963 -0.33 ARG 940

ARG 962 0.08 GLN 964 -0.46 ARG 940

ARG 962 0.06 GLY 965 -0.48 ARG 940

LYS 1111 0.08 LYS 966 -0.42 ARG 940

LYS 1111 0.16 GLU 967 -0.54 ARG 940

LYS 1111 0.16 LEU 968 -0.65 ARG 940

LYS 1111 0.19 VAL 969 -0.56 ARG 940

LYS 1111 0.17 GLN 970 -0.48 ARG 940

LYS 1111 0.16 THR 971 -0.42 ARG 940

VAL 1134 0.14 VAL 972 -0.36 ARG 940

SER 1117 0.13 ASN 973 -0.32 ARG 940

VAL 1020 0.11 CYS 974 -0.35 ARG 940

ASN 955 0.11 ASP 975 -0.37 ARG 940

ASP 956 0.11 PRO 976 -0.38 ARG 940

ASP 956 0.18 GLY 977 -0.38 ARG 940

PRO 957 0.11 LEU 978 -0.46 ALA 979

MET 944 0.24 ALA 979 -0.46 LEU 978

MET 944 0.12 VAL 980 -0.30 GLY 981

PRO 1152 0.13 GLY 981 -0.30 ILE 945

PRO 1152 0.25 TYR 982 -0.34 ILE 945

ASP 1151 0.30 ASP 983 -0.23 PRO 949

PRO 1152 0.31 GLU 984 -0.16 GLN 964

PRO 1152 0.25 PHE 985 -0.12 GLN 964

ALA 1126 0.26 ASN 986 -0.15 LYS 1099

LYS 1112 0.22 ALA 987 -0.09 GLN 964

LYS 1112 0.20 VAL 988 -0.09 GLN 964

LYS 1111 0.22 ASP 989 -0.14 PRO 1152

LYS 1111 0.22 PHE 990 -0.13 ASP 1078

LYS 1111 0.26 SER 991 -0.18 ARG 1080

LYS 1111 0.25 GLY 992 -0.19 ARG 1080

LYS 1111 0.32 THR 993 -0.25 ARG 940

LYS 1111 0.27 PHE 994 -0.35 ARG 940

LYS 1111 0.33 PHE 995 -0.40 ARG 940

LYS 1111 0.25 ILE 996 -0.39 ARG 940

LYS 1111 0.30 ASN 997 -0.39 ARG 940

SER 1117 0.26 THR 998 -0.35 ARG 940

VAL 1025 0.36 GLU 999 -0.33 ARG 940

ASP 1001 0.25 ARG 1000 -0.29 ARG 940

ARG 1000 0.25 ASP 1001 -0.27 ARG 940

GLU 999 0.26 ASP 1002 -0.26 ARG 940

ARG 1000 0.19 ASP 1003 -0.28 ARG 940

TYR 1121 0.18 TYR 1004 -0.30 ARG 940

VAL 1020 0.18 ALA 1005 -0.31 ARG 940

VAL 1020 0.20 GLY 1006 -0.24 ARG 940

VAL 1140 0.15 PHE 1007 -0.18 ARG 940

LYS 1111 0.14 VAL 1008 -0.14 VAL 1019

LYS 1111 0.16 PHE 1009 -0.09 GLN 1071

GLY 1128 0.16 GLY 1010 -0.14 THR 1100

LYS 1111 0.13 TYR 1011 -0.14 THR 1052

PRO 1152 0.15 GLN 1012 -0.18 THR 1051

PRO 946 0.10 SER 1013 -0.24 THR 1051

PRO 946 0.10 SER 1014 -0.31 PHE 942

PRO 1079 0.13 SER 1015 -0.26 PHE 942

PRO 1079 0.13 ARG 1016 -0.17 THR 1124

LYS 1111 0.12 PHE 1017 -0.14 ARG 940

VAL 1019 0.20 TYR 1018 -0.10 ARG 940

TYR 1018 0.20 VAL 1019 -0.15 ARG 940

GLY 1006 0.20 VAL 1020 -0.15 ARG 940

VAL 1045 0.20 MET 1021 -0.23 ARG 940

TYR 1121 0.25 TRP 1022 -0.25 ARG 940

TYR 1121 0.24 LYS 1023 -0.27 ARG 940

GLU 999 0.29 GLN 1024 -0.26 ARG 940

GLU 999 0.36 VAL 1025 -0.23 ARG 940

GLU 999 0.26 THR 1026 -0.23 ARG 940

GLU 999 0.26 GLN 1027 -0.23 ARG 940

THR 1032 0.22 SER 1028 -0.25 ARG 940

GLY 1039 0.15 TYR 1029 -0.27 ARG 940

GLY 951 0.15 TRP 1030 -0.26 ARG 940

PRO 1079 0.17 ASP 1031 -0.30 ARG 940

PRO 1079 0.24 THR 1032 -0.27 ARG 940

ALA 1037 0.30 ASN 1033 -0.30 ARG 940

ALA 1037 0.34 PRO 1034 -0.30 PHE 942

PRO 1079 0.34 THR 1035 -0.28 PHE 942

PRO 1079 0.33 ARG 1036 -0.26 PHE 942

PRO 1034 0.34 ALA 1037 -0.24 ARG 940

ARG 1036 0.28 GLN 1038 -0.24 ARG 940

PRO 1034 0.25 GLY 1039 -0.25 ARG 940

ARG 1036 0.26 TYR 1040 -0.23 ARG 940

GLU 999 0.26 SER 1041 -0.23 ARG 940

TYR 1121 0.29 GLY 1042 -0.22 ARG 940

TRP 1084 0.33 LEU 1043 -0.18 ARG 940

TYR 1121 0.27 SER 1044 -0.16 ARG 940

TRP 1084 0.25 VAL 1045 -0.12 ARG 940

GLY 1083 0.18 LYS 1046 -0.13 ARG 940

HSD 1077 0.18 VAL 1047 -0.12 ARG 940

PRO 1079 0.17 VAL 1048 -0.17 ARG 940

PRO 1079 0.21 ASN 1049 -0.18 PHE 942

PRO 1079 0.22 SER 1050 -0.26 PHE 942

PRO 1079 0.26 THR 1051 -0.29 PHE 942

PRO 1079 0.23 THR 1052 -0.36 MET 944

PRO 1079 0.17 GLY 1053 -0.36 PHE 942

PRO 1079 0.15 PRO 1054 -0.45 MET 944

PRO 1079 0.18 GLY 1055 -0.46 MET 944

PRO 1079 0.22 GLU 1056 -0.38 PHE 942

PRO 1079 0.27 HSD 1057 -0.33 PHE 942

PRO 1079 0.22 LEU 1058 -0.34 PHE 942

PRO 1079 0.18 ARG 1059 -0.36 PHE 942

PRO 1079 0.24 ASN 1060 -0.30 PHE 942

PRO 1079 0.27 ALA 1061 -0.25 PHE 942

PRO 1079 0.18 LEU 1062 -0.26 ARG 940

PRO 1079 0.17 TRP 1063 -0.28 ARG 940

PRO 1079 0.29 HSD 1064 -0.23 ARG 940

PRO 1079 0.31 THR 1065 -0.20 ARG 940

ASN 1067 0.49 GLY 1066 -0.18 ARG 940

PRO 1079 0.49 ASN 1067 -0.18 PHE 942

PRO 1079 0.39 THR 1068 -0.22 PHE 942

PRO 1079 0.42 PRO 1069 -0.22 PHE 942

PRO 1079 0.35 GLY 1070 -0.23 PHE 942

PRO 1079 0.28 GLN 1071 -0.26 PHE 942

ARG 1073 0.33 VAL 1072 -0.20 PHE 942

VAL 1072 0.33 ARG 1073 -0.14 ARG 940

HSD 1077 0.39 THR 1074 -0.13 ARG 940

LYS 1123 0.33 LEU 1075 -0.08 ARG 940

HSD 1077 0.41 TRP 1076 -0.10 ARG 940

ASN 1067 0.41 HSD 1077 -0.14 ARG 940

TYR 1121 0.36 ASP 1078 -0.20 VAL 1106

ASN 1067 0.49 PRO 1079 -0.27 ALA 1115

ASN 1067 0.36 ARG 1080 -0.35 LYS 1112

ASN 1067 0.32 HSD 1081 -0.27 LYS 1112

PRO 1119 0.34 ILE 1082 -0.34 LYS 1112

SER 1117 0.35 GLY 1083 -0.26 LYS 1112

SER 1117 0.39 TRP 1084 -0.26 ARG 940

ALA 1115 0.40 LYS 1085 -0.29 ARG 940

SER 1117 0.33 ASP 1086 -0.33 ARG 940

SER 1117 0.30 PHE 1087 -0.38 LYS 966

LYS 1111 0.36 THR 1088 -0.38 LYS 966

LYS 1111 0.42 ALA 1089 -0.36 LYS 966

LYS 1111 0.39 TYR 1090 -0.27 ARG 940

LYS 1111 0.38 ARG 1091 -0.26 MET 1114

LYS 1111 0.28 TRP 1092 -0.22 ARG 1080

LYS 1111 0.31 ARG 1093 -0.18 PRO 1079

LYS 1111 0.24 LEU 1094 -0.12 ASP 1078

LYS 1112 0.33 SER 1095 -0.20 PRO 1152

LYS 1112 0.29 HSD 1096 -0.11 PRO 1152

LYS 1112 0.32 ARG 1097 -0.16 PRO 1152

LYS 1112 0.28 PRO 1098 -0.21 GLY 1127

LYS 1112 0.31 LYS 1099 -0.21 GLY 1127

LYS 1112 0.39 THR 1100 -0.24 ALA 1126

LYS 1112 0.33 GLY 1101 -0.15 TYR 1125

LYS 1112 0.40 PHE 1102 -0.17 PRO 1152

LYS 1112 0.32 ILE 1103 -0.17 PRO 1119

LYS 1112 0.39 ARG 1104 -0.16 PRO 1152

ARG 1104 0.37 VAL 1105 -0.14 ASP 1116

MET 1107 0.47 VAL 1106 -0.31 ASP 1116

VAL 1106 0.47 MET 1107 -0.25 ARG 1080

PRO 1119 0.34 TYR 1108 -0.24 MET 1114

PRO 1119 0.38 GLU 1109 -0.25 LYS 966

LYS 1111 0.55 GLY 1110 -0.19 GLN 964

GLY 1110 0.55 LYS 1111 -0.24 ARG 1080

PRO 1119 0.46 LYS 1112 -0.35 ARG 1080

PRO 1119 0.51 ILE 1113 -0.27 ARG 1080

GLY 1118 0.52 MET 1114 -0.26 ARG 1080

MET 1114 0.49 ALA 1115 -0.27 PRO 1079

GLY 1118 0.59 ASP 1116 -0.31 VAL 1106

MET 1114 0.46 SER 1117 -0.13 PRO 1152

ASP 1116 0.59 GLY 1118 -0.18 PRO 1152

ASP 1116 0.56 PRO 1119 -0.24 PRO 1152

TYR 1121 0.43 ILE 1120 -0.11 PRO 1152

ILE 1120 0.43 TYR 1121 -0.09 PRO 1152

LYS 1123 0.34 ASP 1122 -0.08 TYR 1011

ASP 1122 0.34 LYS 1123 -0.25 TYR 1125

PRO 1079 0.23 THR 1124 -0.17 ARG 1016

ASN 986 0.19 TYR 1125 -0.25 LYS 1123

ASN 986 0.26 ALA 1126 -0.24 THR 1100

ASN 986 0.24 GLY 1127 -0.21 LYS 1099

PRO 1152 0.19 GLY 1128 -0.15 LYS 1099

PRO 1152 0.14 ARG 1129 -0.18 THR 1052

LYS 1111 0.15 LEU 1130 -0.17 THR 1052

MET 944 0.13 GLY 1131 -0.20 ARG 1059

LYS 1111 0.13 LEU 1132 -0.34 PHE 1133

ASN 958 0.12 PHE 1133 -0.34 LEU 1132

VAL 972 0.14 VAL 1134 -0.35 ARG 940

ASN 955 0.12 PHE 1135 -0.35 ARG 940

ASN 955 0.11 SER 1136 -0.33 ARG 940

SER 1117 0.16 GLN 1137 -0.33 ARG 940

LYS 1111 0.16 GLU 1138 -0.36 ARG 940

LYS 1111 0.21 MET 1139 -0.41 ARG 940

LYS 1111 0.22 VAL 1140 -0.42 ARG 940

LYS 1111 0.24 PHE 1141 -0.48 ARG 940

LYS 1111 0.22 PHE 1142 -0.45 ARG 940

LYS 1111 0.22 SER 1143 -0.37 ARG 940

LYS 1111 0.23 ASP 1144 -0.27 THR 937

LYS 1111 0.19 LEU 1145 -0.22 THR 993

LYS 1111 0.20 LYS 1146 -0.21 TYR 1147

THR 937 0.23 TYR 1147 -0.21 LYS 1146

THR 937 0.26 GLU 1148 -0.16 GLN 964

THR 937 0.27 CYS 1149 -0.12 GLN 964

THR 937 0.21 ARG 1150 -0.30 ASP 1151

ASP 983 0.30 ASP 1151 -0.30 ARG 1150

GLU 984 0.31 PRO 1152 -0.24 PRO 1119

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 20 ---

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

* *