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

* *

CA distance fluctuations for 240531115742101615

--- 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
GLU 1109 0.36 PHE 939 -0.16 ASP 983

GLU 1109 0.33 ARG 940 -0.13 TRP 959

GLU 1109 0.31 ARG 941 -0.11 GLU 999

SER 953 0.29 PHE 942 -0.12 GLU 999

SER 953 0.35 GLN 943 -0.11 SER 1013

SER 953 0.43 MET 944 -0.10 SER 1013

SER 953 0.47 ILE 945 -0.12 CYS 974

SER 953 0.65 PRO 946 -0.12 SER 1015

SER 953 0.60 LEU 947 -0.14 ASN 1033

SER 953 0.75 ASP 948 -0.18 ASN 1033

SER 953 0.60 PRO 949 -0.31 ASN 1033

SER 953 0.45 LYS 950 -0.37 ASN 1033

GLU 1056 0.38 GLY 951 -0.16 PRO 949

GLU 1056 0.39 THR 952 -0.02 SER 953

ASP 948 0.75 SER 953 -0.02 THR 952

ASP 956 0.37 GLN 954 -0.05 LYS 950

LYS 1112 0.33 ASN 955 -0.29 LYS 950

SER 953 0.41 ASP 956 -0.13 LYS 950

SER 953 0.42 PRO 957 -0.10 ARG 940

LYS 1112 0.35 ASN 958 -0.13 ARG 940

SER 953 0.33 TRP 959 -0.13 ARG 940

GLU 1109 0.36 VAL 960 -0.13 ARG 940

GLU 1109 0.38 VAL 961 -0.16 GLU 999

GLU 1109 0.28 ARG 962 -0.22 GLU 999

GLU 1109 0.35 HSD 963 -0.19 GLY 965

GLU 1109 0.44 GLN 964 -0.11 GLU 999

GLU 1109 0.50 GLY 965 -0.22 ARG 962

GLU 1109 0.49 LYS 966 -0.15 ASP 983

GLU 1109 0.51 GLU 967 -0.15 ARG 962

GLU 1109 0.43 LEU 968 -0.16 GLU 999

GLU 1109 0.41 VAL 969 -0.17 GLU 999

LYS 1112 0.38 GLN 970 -0.14 GLU 999

LYS 1112 0.41 THR 971 -0.16 ARG 962

LYS 1112 0.39 VAL 972 -0.16 LYS 950

LYS 1112 0.36 ASN 973 -0.23 LYS 950

SER 953 0.37 CYS 974 -0.26 LYS 950

SER 953 0.60 ASP 975 -0.27 LYS 950

SER 953 0.54 PRO 976 -0.15 LYS 950

SER 953 0.54 GLY 977 -0.11 ASN 973

SER 953 0.44 LEU 978 -0.12 GLU 999

SER 953 0.38 ALA 979 -0.14 GLU 999

SER 953 0.34 VAL 980 -0.13 GLU 999

SER 953 0.29 GLY 981 -0.13 GLU 999

SER 953 0.28 TYR 982 -0.14 PRO 1152

SER 953 0.24 ASP 983 -0.16 PHE 939

SER 953 0.24 GLU 984 -0.27 PRO 1152

SER 953 0.21 PHE 985 -0.20 PRO 1152

SER 953 0.17 ASN 986 -0.30 PRO 1152

SER 953 0.19 ALA 987 -0.27 LYS 1112

SER 953 0.23 VAL 988 -0.25 LYS 1112

SER 953 0.24 ASP 989 -0.28 LYS 1112

SER 953 0.26 PHE 990 -0.16 PHE 995

SER 953 0.27 SER 991 -0.19 PHE 995

GLU 1109 0.40 GLY 992 -0.24 PHE 995

GLU 1109 0.62 THR 993 -0.24 LYS 1111

GLU 1109 0.46 PHE 994 -0.39 PHE 995

LYS 1112 0.54 PHE 995 -0.39 PHE 994

LYS 1112 0.52 ILE 996 -0.27 ARG 1000

LYS 1112 0.52 ASN 997 -0.27 ARG 1000

LYS 1112 0.46 THR 998 -0.27 ARG 1000

LYS 1112 0.44 GLU 999 -0.24 MET 1139

LYS 1112 0.29 ARG 1000 -0.31 ASP 1086

LYS 1112 0.35 ASP 1001 -0.19 LYS 950

LYS 1112 0.34 ASP 1002 -0.17 LYS 950

SER 953 0.34 ASP 1003 -0.17 ASP 1002

SER 953 0.38 TYR 1004 -0.16 ARG 1059

SER 953 0.37 ALA 1005 -0.14 ARG 1000

SER 953 0.36 GLY 1006 -0.24 PHE 1007

SER 953 0.35 PHE 1007 -0.24 GLY 1006

SER 953 0.34 VAL 1008 -0.15 ASN 986

SER 953 0.30 PHE 1009 -0.17 ASN 986

SER 953 0.26 GLY 1010 -0.26 PRO 1152

SER 953 0.29 TYR 1011 -0.24 PRO 1152

SER 953 0.28 GLN 1012 -0.29 PRO 1152

SER 953 0.30 SER 1013 -0.22 PRO 1152

SER 953 0.36 SER 1014 -0.18 PRO 1152

SER 953 0.32 SER 1015 -0.20 PRO 1152

SER 953 0.28 ARG 1016 -0.24 PRO 1152

SER 953 0.30 PHE 1017 -0.23 PRO 1152

SER 953 0.29 TYR 1018 -0.20 LYS 1099

SER 953 0.34 VAL 1019 -0.18 LYS 1099

SER 953 0.33 VAL 1020 -0.18 MET 1021

SER 953 0.36 MET 1021 -0.18 VAL 1020

SER 953 0.35 TRP 1022 -0.15 LYS 1085

SER 953 0.32 LYS 1023 -0.17 ASN 1060

LYS 1112 0.36 GLN 1024 -0.20 LYS 1085

LYS 1112 0.28 VAL 1025 -0.18 LYS 1085

SER 953 0.27 THR 1026 -0.20 GLN 1027

SER 953 0.32 GLN 1027 -0.20 THR 1026

SER 953 0.32 SER 1028 -0.15 PRO 1079

SER 953 0.33 TYR 1029 -0.15 PRO 1079

THR 952 0.34 TRP 1030 -0.16 LYS 950

THR 952 0.19 ASP 1031 -0.29 LYS 950

SER 1028 0.16 THR 1032 -0.33 LYS 950

THR 1035 0.20 ASN 1033 -0.37 GLU 1056

SER 953 0.16 PRO 1034 -0.39 GLU 1056

SER 953 0.20 THR 1035 -0.33 GLU 1056

SER 953 0.25 ARG 1036 -0.19 GLU 1056

SER 953 0.31 ALA 1037 -0.16 PRO 1079

SER 953 0.32 GLN 1038 -0.17 PRO 1079

SER 953 0.34 GLY 1039 -0.15 ASN 1060

SER 953 0.31 TYR 1040 -0.18 GLU 1109

SER 953 0.29 SER 1041 -0.21 GLU 1109

SER 953 0.30 GLY 1042 -0.25 GLU 1109

SER 953 0.32 LEU 1043 -0.21 GLU 1109

SER 953 0.31 SER 1044 -0.17 LYS 1099

SER 953 0.31 VAL 1045 -0.19 LYS 1099

SER 953 0.31 LYS 1046 -0.23 LYS 1099

SER 953 0.29 VAL 1047 -0.27 LYS 1099

SER 953 0.31 VAL 1048 -0.23 LYS 1099

SER 953 0.28 ASN 1049 -0.26 LYS 1099

SER 953 0.30 SER 1050 -0.22 PRO 1152

SER 953 0.28 THR 1051 -0.22 PRO 1152

SER 953 0.32 THR 1052 -0.21 PRO 1034

SER 953 0.36 GLY 1053 -0.18 PRO 1034

SER 953 0.45 PRO 1054 -0.19 PRO 1034

SER 953 0.50 GLY 1055 -0.30 PRO 1034

SER 953 0.51 GLU 1056 -0.39 PRO 1034

SER 953 0.41 HSD 1057 -0.33 PRO 1034

SER 953 0.42 LEU 1058 -0.19 THR 1035

SER 953 0.46 ARG 1059 -0.17 LYS 1099

SER 953 0.39 ASN 1060 -0.19 LYS 1099

SER 953 0.37 ALA 1061 -0.21 LYS 1099

SER 953 0.40 LEU 1062 -0.19 LYS 1099

SER 953 0.41 TRP 1063 -0.18 ASN 1060

SER 953 0.35 HSD 1064 -0.19 LYS 1099

SER 953 0.32 THR 1065 -0.23 PRO 1079

SER 953 0.30 GLY 1066 -0.24 PRO 1079

SER 953 0.30 ASN 1067 -0.27 LYS 1099

SER 953 0.31 THR 1068 -0.25 LYS 1099

SER 953 0.31 PRO 1069 -0.33 LYS 1099

SER 953 0.29 GLY 1070 -0.30 LYS 1099

SER 953 0.32 GLN 1071 -0.24 LYS 1099

SER 953 0.32 VAL 1072 -0.26 LYS 1099

SER 953 0.29 ARG 1073 -0.28 LYS 1099

SER 953 0.30 THR 1074 -0.24 LYS 1099

SER 953 0.26 LEU 1075 -0.26 LYS 1099

SER 953 0.27 TRP 1076 -0.19 LYS 1099

SER 953 0.28 HSD 1077 -0.20 ASN 1067

SER 953 0.28 ASP 1078 -0.24 GLU 1109

SER 953 0.24 PRO 1079 -0.24 GLY 1066

SER 953 0.25 ARG 1080 -0.22 GLU 1109

SER 953 0.26 HSD 1081 -0.26 GLU 1109

GLY 1083 0.39 ILE 1082 -0.33 GLU 1109

LYS 1112 0.41 GLY 1083 -0.23 GLU 1109

LYS 1112 0.54 TRP 1084 -0.17 GLY 1110

LYS 1112 0.71 LYS 1085 -0.25 ARG 1000

LYS 1112 0.60 ASP 1086 -0.31 ARG 1000

LYS 1112 0.63 PHE 1087 -0.32 LYS 1111

LYS 1112 0.78 THR 1088 -0.36 LYS 1111

LYS 1112 0.55 ALA 1089 -0.50 LYS 1111

LYS 1112 0.44 TYR 1090 -0.41 LYS 1111

GLU 1109 0.50 ARG 1091 -0.32 TYR 1090

SER 953 0.28 TRP 1092 -0.17 PHE 1087

SER 953 0.27 ARG 1093 -0.26 LYS 1112

SER 953 0.27 LEU 1094 -0.25 LYS 1112

SER 953 0.25 SER 1095 -0.37 LYS 1112

SER 953 0.23 HSD 1096 -0.32 LYS 1112

SER 953 0.20 ARG 1097 -0.32 LYS 1112

SER 953 0.18 PRO 1098 -0.30 PRO 1152

ALA 987 0.15 LYS 1099 -0.46 LYS 1123

SER 953 0.17 THR 1100 -0.33 LYS 1112

SER 953 0.20 GLY 1101 -0.39 LYS 1099

SER 953 0.22 PHE 1102 -0.35 LYS 1112

SER 953 0.24 ILE 1103 -0.32 LYS 1112

SER 953 0.26 ARG 1104 -0.39 LYS 1112

SER 953 0.27 VAL 1105 -0.28 LYS 1112

SER 953 0.27 VAL 1106 -0.38 LYS 1112

SER 953 0.28 MET 1107 -0.15 SER 1095

ASP 1144 0.30 TYR 1108 -0.13 GLY 1110

THR 993 0.62 GLU 1109 -0.39 MET 1114

ASP 1144 0.56 GLY 1110 -0.79 LYS 1111

ILE 1113 0.58 LYS 1111 -0.79 GLY 1110

THR 1088 0.78 LYS 1112 -0.44 GLY 1118

LYS 1111 0.58 ILE 1113 -0.30 GLY 1118

LYS 1112 0.30 MET 1114 -0.41 ALA 1115

SER 953 0.28 ALA 1115 -0.41 MET 1114

LYS 1111 0.28 ASP 1116 -0.33 SER 1117

SER 953 0.26 SER 1117 -0.33 ASP 1116

SER 953 0.24 GLY 1118 -0.44 LYS 1112

SER 953 0.23 PRO 1119 -0.42 LYS 1112

SER 953 0.24 ILE 1120 -0.32 LYS 1112

SER 953 0.22 TYR 1121 -0.30 LYS 1112

SER 953 0.22 ASP 1122 -0.39 LYS 1099

SER 953 0.21 LYS 1123 -0.46 LYS 1099

SER 953 0.22 THR 1124 -0.39 LYS 1099

SER 953 0.22 TYR 1125 -0.35 PRO 1152

SER 953 0.21 ALA 1126 -0.47 PRO 1152

SER 953 0.22 GLY 1127 -0.37 PRO 1152

SER 953 0.24 GLY 1128 -0.31 PRO 1152

SER 953 0.29 ARG 1129 -0.22 PRO 1152

SER 953 0.30 LEU 1130 -0.25 GLY 1131

SER 953 0.34 GLY 1131 -0.25 LEU 1130

SER 953 0.37 LEU 1132 -0.15 VAL 1140

SER 953 0.41 PHE 1133 -0.13 ASN 986

SER 953 0.42 VAL 1134 -0.17 GLN 1137

SER 953 0.45 PHE 1135 -0.17 GLN 1137

SER 953 0.42 SER 1136 -0.21 LYS 950

LYS 1112 0.36 GLN 1137 -0.17 VAL 1134

LYS 1112 0.40 GLU 1138 -0.15 LYS 950

LYS 1112 0.45 MET 1139 -0.24 GLU 999

LYS 1112 0.46 VAL 1140 -0.18 GLU 999

ALA 1089 0.45 PHE 1141 -0.20 GLU 999

GLU 1109 0.48 PHE 1142 -0.16 ARG 1000

GLU 1109 0.57 SER 1143 -0.19 ARG 1000

GLU 1109 0.59 ASP 1144 -0.16 ARG 1000

GLU 1109 0.42 LEU 1145 -0.15 ARG 1000

GLY 1110 0.31 LYS 1146 -0.14 ARG 1000

SER 953 0.25 TYR 1147 -0.13 ARG 1000

ASP 1151 0.26 GLU 1148 -0.22 LYS 1112

GLU 1148 0.26 CYS 1149 -0.21 LYS 1112

ASP 1151 0.47 ARG 1150 -0.27 LYS 1112

ARG 1150 0.47 ASP 1151 -0.28 ALA 1126

ARG 1150 0.36 PRO 1152 -0.47 ALA 1126

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 240531115742101615

--- normal mode 26 ---

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

* *