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

* *

CA distance fluctuations for 240531115742101615

--- 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
ARG 941 0.17 PHE 939 -0.33 GLY 981

PHE 1087 0.14 ARG 940 -0.32 TYR 982

TYR 1147 0.18 ARG 941 -0.28 SER 953

TYR 1147 0.14 PHE 942 -0.28 SER 953

PRO 1034 0.16 GLN 943 -0.28 PHE 942

PRO 1034 0.18 MET 944 -0.32 SER 953

PRO 1034 0.23 ILE 945 -0.25 SER 953

PRO 1034 0.26 PRO 946 -0.28 THR 952

PRO 1034 0.30 LEU 947 -0.27 TRP 1030

PRO 1034 0.32 ASP 948 -0.32 TRP 1030

PRO 1034 0.34 PRO 949 -0.27 TRP 1030

SER 953 0.34 LYS 950 -0.29 TRP 1030

PRO 1034 0.42 GLY 951 -0.25 PRO 946

PRO 1034 0.38 THR 952 -0.28 PRO 946

LYS 950 0.34 SER 953 -0.32 MET 944

GLU 1056 0.30 GLN 954 -0.19 MET 944

GLU 1056 0.36 ASN 955 -0.22 TRP 1030

LYS 950 0.33 ASP 956 -0.22 SER 953

GLU 1056 0.30 PRO 957 -0.21 SER 953

GLU 1056 0.25 ASN 958 -0.17 SER 953

GLU 1056 0.22 TRP 959 -0.18 SER 953

GLU 1056 0.19 VAL 960 -0.13 SER 953

GLU 1056 0.15 VAL 961 -0.13 SER 953

THR 971 0.24 ARG 962 -0.17 GLY 965

ASN 997 0.27 HSD 963 -0.16 ARG 941

PHE 1087 0.25 GLN 964 -0.23 ASP 983

PHE 1087 0.25 GLY 965 -0.17 ARG 962

THR 1088 0.18 LYS 966 -0.14 SER 953

PHE 995 0.17 GLU 967 -0.13 SER 953

ARG 1059 0.15 LEU 968 -0.14 SER 953

GLU 1056 0.21 VAL 969 -0.12 SER 953

GLU 1056 0.26 GLN 970 -0.13 GLN 1027

GLU 1056 0.27 THR 971 -0.13 GLN 1027

GLU 1056 0.32 VAL 972 -0.16 ARG 1000

GLU 1056 0.35 ASN 973 -0.20 GLN 1027

GLU 1056 0.41 CYS 974 -0.23 TRP 1030

GLU 1056 0.41 ASP 975 -0.32 TRP 1030

GLU 1056 0.33 PRO 976 -0.30 TRP 1030

PRO 1034 0.23 GLY 977 -0.25 TRP 1030

PRO 1034 0.21 LEU 978 -0.20 TRP 1030

PRO 1034 0.17 ALA 979 -0.21 SER 953

THR 1035 0.16 VAL 980 -0.24 ARG 940

LYS 1099 0.16 GLY 981 -0.33 PHE 939

ASP 983 0.21 TYR 982 -0.32 ARG 940

LYS 1099 0.25 ASP 983 -0.25 ARG 940

LYS 1099 0.30 GLU 984 -0.27 GLY 1070

ASP 983 0.25 PHE 985 -0.33 GLY 1128

LYS 1099 0.31 ASN 986 -0.53 GLY 1127

LYS 1099 0.15 ALA 987 -0.32 GLY 1070

ARG 941 0.14 VAL 988 -0.24 GLY 1070

ASP 1151 0.22 ASP 989 -0.17 GLY 1070

ASP 1151 0.15 PHE 990 -0.13 GLY 1070

ASP 1151 0.18 SER 991 -0.10 SER 953

ASP 1151 0.15 GLY 992 -0.11 SER 953

ASP 1144 0.15 THR 993 -0.12 ARG 1036

ARG 1059 0.17 PHE 994 -0.14 ARG 1036

HSD 963 0.23 PHE 995 -0.16 ARG 1036

ARG 1059 0.23 ILE 996 -0.18 ARG 1036

HSD 963 0.27 ASN 997 -0.19 ARG 1036

ARG 1059 0.25 THR 998 -0.20 ARG 1036

GLU 1056 0.26 GLU 999 -0.23 THR 1032

ARG 1059 0.21 ARG 1000 -0.32 THR 1032

ARG 1059 0.29 ASP 1001 -0.27 THR 1032

ARG 1059 0.27 ASP 1002 -0.31 ARG 1036

ARG 1059 0.32 ASP 1003 -0.28 GLN 1027

ARG 1059 0.31 TYR 1004 -0.22 ARG 1036

ARG 1059 0.28 ALA 1005 -0.16 ARG 1036

ARG 1059 0.19 GLY 1006 -0.14 TYR 1029

THR 1035 0.13 PHE 1007 -0.14 TRP 1030

THR 1035 0.17 VAL 1008 -0.14 TRP 1030

THR 1035 0.16 PHE 1009 -0.18 GLY 1070

ALA 1126 0.20 GLY 1010 -0.33 ASN 986

THR 1035 0.22 TYR 1011 -0.27 PRO 1152

THR 1035 0.26 GLN 1012 -0.36 PRO 1152

THR 1035 0.31 SER 1013 -0.29 PRO 1152

THR 1035 0.34 SER 1014 -0.23 PRO 1152

THR 1035 0.46 SER 1015 -0.31 PRO 1152

THR 1035 0.37 ARG 1016 -0.35 PRO 1152

THR 1035 0.26 PHE 1017 -0.28 PRO 1152

THR 1035 0.20 TYR 1018 -0.24 ASN 986

THR 1035 0.17 VAL 1019 -0.16 ASN 986

THR 1035 0.10 VAL 1020 -0.13 TRP 1030

LEU 1062 0.13 MET 1021 -0.17 ARG 1036

ARG 1059 0.15 TRP 1022 -0.26 ARG 1036

ARG 1059 0.21 LYS 1023 -0.30 ARG 1036

PRO 1069 0.17 GLN 1024 -0.39 ARG 1036

PRO 1069 0.22 VAL 1025 -0.48 ARG 1036

PRO 1069 0.25 THR 1026 -0.63 ARG 1036

PRO 1069 0.31 GLN 1027 -0.59 ARG 1036

PRO 1069 0.40 SER 1028 -0.79 ARG 1036

PRO 1069 0.46 TYR 1029 -0.31 ARG 1036

PRO 1069 0.34 TRP 1030 -0.44 ASP 1031

PRO 1069 0.45 ASP 1031 -0.44 TRP 1030

PRO 1069 0.68 THR 1032 -0.63 SER 1028

HSD 1057 0.59 ASN 1033 -0.47 THR 1035

HSD 1057 0.84 PRO 1034 -0.31 ALA 1037

PRO 1069 0.96 THR 1035 -0.47 ASN 1033

PRO 1069 0.91 ARG 1036 -0.79 SER 1028

PRO 1069 0.62 ALA 1037 -0.31 PRO 1034

PRO 1069 0.44 GLN 1038 -0.59 ARG 1036

PRO 1069 0.30 GLY 1039 -0.47 ARG 1036

PRO 1069 0.23 TYR 1040 -0.50 ARG 1036

PRO 1069 0.18 SER 1041 -0.46 ARG 1036

LYS 1112 0.15 GLY 1042 -0.36 ARG 1036

LYS 1112 0.13 LEU 1043 -0.27 ARG 1036

THR 1068 0.10 SER 1044 -0.21 ARG 1036

THR 1035 0.06 VAL 1045 -0.18 LYS 1099

THR 1035 0.16 LYS 1046 -0.23 LYS 1099

THR 1035 0.24 VAL 1047 -0.26 ASN 986

THR 1035 0.37 VAL 1048 -0.28 PRO 1152

THR 1035 0.49 ASN 1049 -0.39 PRO 1152

THR 1035 0.63 SER 1050 -0.35 PRO 1152

THR 1035 0.79 THR 1051 -0.40 PRO 1152

PRO 1034 0.74 THR 1052 -0.31 PRO 1152

THR 1035 0.56 GLY 1053 -0.26 PRO 1152

PRO 1034 0.47 PRO 1054 -0.19 PRO 1152

PRO 1034 0.50 GLY 1055 -0.17 PRO 1152

PRO 1034 0.52 GLU 1056 -0.16 PRO 1152

PRO 1034 0.84 HSD 1057 -0.21 PRO 1152

THR 1035 0.66 LEU 1058 -0.21 PRO 1152

PHE 1135 0.39 ARG 1059 -0.22 ALA 1061

THR 1035 0.47 ASN 1060 -0.20 HSD 1064

THR 1035 0.58 ALA 1061 -0.22 ARG 1059

THR 1035 0.31 LEU 1062 -0.17 LYS 1099

ASP 1002 0.22 TRP 1063 -0.19 LYS 1099

PRO 1069 0.30 HSD 1064 -0.21 LYS 1099

PRO 1069 0.22 THR 1065 -0.23 LYS 1099

PRO 1069 0.22 GLY 1066 -0.26 LYS 1099

ARG 1036 0.31 ASN 1067 -0.31 LYS 1099

THR 1035 0.64 THR 1068 -0.30 LYS 1099

THR 1035 0.96 PRO 1069 -0.46 LYS 1099

THR 1035 0.88 GLY 1070 -0.45 PRO 1152

THR 1035 0.73 GLN 1071 -0.33 PRO 1152

THR 1035 0.48 VAL 1072 -0.29 LYS 1099

THR 1035 0.29 ARG 1073 -0.33 LYS 1099

THR 1035 0.11 THR 1074 -0.28 LYS 1099

ASN 1049 0.07 LEU 1075 -0.28 LYS 1099

ASN 1049 0.06 TRP 1076 -0.21 LYS 1099

LYS 1112 0.11 HSD 1077 -0.25 ARG 1036

LYS 1112 0.16 ASP 1078 -0.30 ARG 1036

LYS 1112 0.17 PRO 1079 -0.37 ARG 1036

LYS 1112 0.23 ARG 1080 -0.40 ARG 1036

LYS 1112 0.20 HSD 1081 -0.45 ARG 1036

LYS 1112 0.24 ILE 1082 -0.42 ARG 1036

LYS 1112 0.15 GLY 1083 -0.37 ARG 1036

ARG 1059 0.16 TRP 1084 -0.30 ARG 1036

HSD 963 0.18 LYS 1085 -0.29 ARG 1036

HSD 963 0.22 ASP 1086 -0.25 ARG 1036

HSD 963 0.27 PHE 1087 -0.21 ARG 1036

GLY 965 0.24 THR 1088 -0.22 ARG 1036

GLY 965 0.22 ALA 1089 -0.18 ARG 1036

GLY 965 0.16 TYR 1090 -0.18 ARG 1036

PRO 1152 0.15 ARG 1091 -0.14 ARG 1036

ASP 1151 0.14 TRP 1092 -0.13 ARG 1036

ASP 1151 0.18 ARG 1093 -0.14 LYS 1111

ASP 1151 0.13 LEU 1094 -0.11 LYS 1111

ASP 1151 0.17 SER 1095 -0.13 PRO 1069

GLU 984 0.14 HSD 1096 -0.21 PRO 1069

GLU 984 0.21 ARG 1097 -0.29 PRO 1069

GLU 984 0.28 PRO 1098 -0.40 PRO 1069

ASN 986 0.31 LYS 1099 -0.51 LYS 1123

GLY 1127 0.25 THR 1100 -0.33 PRO 1069

GLY 1127 0.30 GLY 1101 -0.40 LYS 1099

GLY 1127 0.23 PHE 1102 -0.24 PRO 1069

GLY 1127 0.11 ILE 1103 -0.18 PRO 1069

PRO 1152 0.11 ARG 1104 -0.14 LYS 1111

ASP 1151 0.12 VAL 1105 -0.13 ARG 1036

PRO 1152 0.18 VAL 1106 -0.15 ARG 1036

PRO 1152 0.14 MET 1107 -0.18 ARG 1036

PRO 1152 0.17 TYR 1108 -0.17 ARG 1036

PRO 1152 0.16 GLU 1109 -0.17 ARG 1036

PRO 1152 0.19 GLY 1110 -0.15 ARG 1036

ILE 1082 0.17 LYS 1111 -0.15 PRO 1119

MET 1114 0.26 LYS 1112 -0.13 ARG 1036

PRO 1152 0.19 ILE 1113 -0.18 ARG 1036

LYS 1112 0.26 MET 1114 -0.21 ARG 1036

PRO 1152 0.14 ALA 1115 -0.23 ARG 1036

PRO 1152 0.15 ASP 1116 -0.19 ARG 1036

PRO 1152 0.10 SER 1117 -0.18 ARG 1036

PRO 1152 0.15 GLY 1118 -0.16 ASP 1116

PRO 1152 0.14 PRO 1119 -0.15 ASP 1116

TYR 1125 0.12 ILE 1120 -0.20 LYS 1099

TYR 1125 0.15 TYR 1121 -0.27 LYS 1099

TYR 1125 0.18 ASP 1122 -0.43 LYS 1099

TYR 1125 0.34 LYS 1123 -0.51 LYS 1099

THR 1035 0.21 THR 1124 -0.45 PRO 1069

LYS 1123 0.34 TYR 1125 -0.45 PRO 1152

GLY 1101 0.26 ALA 1126 -0.60 PRO 1152

GLY 1101 0.30 GLY 1127 -0.53 ASN 986

GLY 1101 0.21 GLY 1128 -0.35 PRO 1152

GLY 1128 0.20 ARG 1129 -0.24 GLY 1070

THR 1035 0.14 LEU 1130 -0.18 GLY 1070

THR 1035 0.15 GLY 1131 -0.17 PHE 939

THR 1035 0.15 LEU 1132 -0.15 SER 953

ARG 1059 0.21 PHE 1133 -0.17 TRP 1030

ARG 1059 0.30 VAL 1134 -0.20 TRP 1030

ARG 1059 0.39 PHE 1135 -0.26 TRP 1030

ARG 1059 0.35 SER 1136 -0.30 TRP 1030

ARG 1059 0.37 GLN 1137 -0.19 GLN 1027

GLU 1056 0.31 GLU 1138 -0.15 GLN 1027

GLU 1056 0.27 MET 1139 -0.14 ARG 1036

ARG 1059 0.25 VAL 1140 -0.14 ARG 1036

HSD 963 0.23 PHE 1141 -0.12 ARG 1036

ARG 1059 0.18 PHE 1142 -0.12 SER 953

PHE 995 0.18 SER 1143 -0.11 SER 953

ALA 1089 0.20 ASP 1144 -0.12 SER 953

ALA 1089 0.14 LEU 1145 -0.12 SER 953

ASP 1151 0.17 LYS 1146 -0.13 GLY 1070

ARG 941 0.18 TYR 1147 -0.16 GLY 1070

CYS 1149 0.29 GLU 1148 -0.19 GLY 1070

GLU 1148 0.29 CYS 1149 -0.25 GLY 1070

ASP 1151 0.52 ARG 1150 -0.27 ALA 1126

ARG 1150 0.52 ASP 1151 -0.47 ALA 1126

ARG 1150 0.36 PRO 1152 -0.60 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 20 ---

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

* *