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

* *

CA distance fluctuations for 240531115742101615

--- normal mode 19 ---

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
TYR 1147 0.31 PHE 939 -0.19 GLN 954

ASP 983 0.31 ARG 940 -0.31 VAL 960

ASP 983 0.17 ARG 941 -0.20 GLN 954

VAL 961 0.12 PHE 942 -0.21 ILE 945

ASP 1031 0.08 GLN 943 -0.20 ARG 940

ASN 958 0.10 MET 944 -0.25 ILE 945

ASP 1031 0.15 ILE 945 -0.25 MET 944

ASP 1031 0.18 PRO 946 -0.23 ARG 940

ASP 1031 0.24 LEU 947 -0.20 MET 944

ASP 1031 0.31 ASP 948 -0.28 SER 953

ASP 1031 0.33 PRO 949 -0.32 SER 953

ASP 1031 0.38 LYS 950 -0.35 SER 953

PRO 949 0.20 GLY 951 -0.32 PRO 1034

GLU 999 0.14 THR 952 -0.27 PRO 1034

GLU 999 0.16 SER 953 -0.35 LYS 950

GLU 999 0.20 GLN 954 -0.37 ARG 962

GLU 999 0.19 ASN 955 -0.36 ARG 962

GLU 999 0.13 ASP 956 -0.36 ARG 962

MET 1139 0.11 PRO 957 -0.32 ARG 962

MET 944 0.10 ASN 958 -0.46 ARG 962

VAL 969 0.13 TRP 959 -0.30 ARG 940

LEU 968 0.12 VAL 960 -0.45 ARG 962

GLU 967 0.21 VAL 961 -0.45 VAL 960

GLY 965 0.30 ARG 962 -0.47 THR 971

GLY 965 0.38 HSD 963 -0.43 THR 971

TYR 1147 0.33 GLN 964 -0.35 MET 1139

HSD 963 0.38 GLY 965 -0.27 MET 1139

LEU 1145 0.26 LYS 966 -0.28 GLU 967

ARG 962 0.25 GLU 967 -0.28 LYS 966

VAL 960 0.12 LEU 968 -0.25 ARG 940

TRP 959 0.13 VAL 969 -0.31 GLN 964

PHE 1141 0.11 GLN 970 -0.34 VAL 961

PHE 1141 0.09 THR 971 -0.47 ARG 962

MET 1139 0.17 VAL 972 -0.53 ARG 1000

GLU 999 0.23 ASN 973 -0.49 ARG 1000

GLU 999 0.20 CYS 974 -0.32 ARG 962

GLU 999 0.23 ASP 975 -0.27 ARG 962

GLU 999 0.21 PRO 976 -0.22 ARG 962

GLU 999 0.15 GLY 977 -0.20 ARG 940

ASP 1031 0.11 LEU 978 -0.16 ARG 940

ASN 958 0.09 ALA 979 -0.16 ARG 940

VAL 961 0.09 VAL 980 -0.13 THR 1035

GLN 964 0.17 GLY 981 -0.13 PRO 1152

GLN 964 0.17 TYR 982 -0.17 PRO 1152

ARG 940 0.31 ASP 983 -0.23 PRO 1152

ARG 940 0.23 GLU 984 -0.24 PRO 1152

ARG 940 0.25 PHE 985 -0.23 ASP 1151

ARG 940 0.21 ASN 986 -0.14 PRO 1152

GLN 964 0.22 ALA 987 -0.08 THR 993

GLN 964 0.24 VAL 988 -0.10 THR 993

GLN 964 0.25 ASP 989 -0.10 THR 993

GLN 964 0.25 PHE 990 -0.14 SER 991

GLN 964 0.23 SER 991 -0.14 PHE 990

LYS 966 0.20 GLY 992 -0.20 THR 993

ARG 962 0.16 THR 993 -0.21 LYS 1111

ARG 1000 0.16 PHE 994 -0.23 LYS 1111

ARG 1000 0.21 PHE 995 -0.38 LYS 1111

ARG 1000 0.21 ILE 996 -0.32 LYS 1111

ARG 1000 0.18 ASN 997 -0.37 LYS 1111

ASN 973 0.16 THR 998 -0.33 HSD 963

ASP 1001 0.32 GLU 999 -0.36 HSD 963

LYS 1085 0.57 ARG 1000 -0.53 VAL 972

GLU 999 0.32 ASP 1001 -0.32 ARG 962

ARG 1000 0.28 ASP 1002 -0.23 ARG 962

GLU 999 0.26 ASP 1003 -0.22 ARG 962

ARG 1000 0.19 TYR 1004 -0.17 ARG 962

ARG 1000 0.16 ALA 1005 -0.12 ARG 940

ARG 1000 0.16 GLY 1006 -0.09 GLY 1110

ARG 1000 0.12 PHE 1007 -0.10 ARG 1036

ARG 1000 0.10 VAL 1008 -0.12 ARG 1036

GLN 964 0.15 PHE 1009 -0.12 ARG 1036

GLN 964 0.15 GLY 1010 -0.12 ARG 1036

GLN 964 0.12 TYR 1011 -0.13 ARG 1036

ASP 1031 0.13 GLN 1012 -0.13 ARG 1036

ASP 1031 0.16 SER 1013 -0.13 ARG 1036

ASP 1031 0.18 SER 1014 -0.15 THR 1035

ASP 1031 0.21 SER 1015 -0.15 ARG 1036

ASP 1031 0.15 ARG 1016 -0.16 ARG 1036

ASP 1031 0.12 PHE 1017 -0.15 ARG 1036

ARG 1000 0.13 TYR 1018 -0.15 ARG 1036

ARG 1000 0.15 VAL 1019 -0.15 ARG 1036

ARG 1000 0.19 VAL 1020 -0.12 ARG 1036

ARG 1000 0.23 MET 1021 -0.11 ARG 1036

ARG 1000 0.32 TRP 1022 -0.12 THR 1032

ARG 1000 0.36 LYS 1023 -0.13 ARG 962

ARG 1000 0.54 GLN 1024 -0.15 THR 1032

ARG 1000 0.51 VAL 1025 -0.20 THR 1032

ARG 1000 0.34 THR 1026 -0.32 THR 1032

ARG 1000 0.27 GLN 1027 -0.31 ASP 1031

ARG 1036 0.45 SER 1028 -0.54 ASP 1031

ARG 1036 0.45 TYR 1029 -0.36 ASP 1031

ARG 1036 0.34 TRP 1030 -0.24 SER 1028

GLU 1056 0.50 ASP 1031 -0.54 SER 1028

GLU 1056 0.32 THR 1032 -0.46 GLN 1038

HSD 1057 0.29 ASN 1033 -0.21 SER 1028

THR 1068 0.23 PRO 1034 -0.32 GLY 951

GLU 999 0.20 THR 1035 -0.33 ASN 1060

TYR 1029 0.45 ARG 1036 -0.46 GLY 1066

ARG 1000 0.15 ALA 1037 -0.42 THR 1032

ARG 1000 0.20 GLN 1038 -0.46 THR 1032

ARG 1000 0.23 GLY 1039 -0.28 THR 1032

ARG 1000 0.29 TYR 1040 -0.32 THR 1032

ARG 1000 0.38 SER 1041 -0.25 THR 1032

ARG 1000 0.35 GLY 1042 -0.22 THR 1032

ARG 1000 0.31 LEU 1043 -0.16 THR 1032

ARG 1000 0.26 SER 1044 -0.16 THR 1032

ARG 1000 0.21 VAL 1045 -0.16 ARG 1036

ARG 1000 0.18 LYS 1046 -0.20 ARG 1036

ARG 1000 0.15 VAL 1047 -0.19 ARG 1036

PRO 1034 0.13 VAL 1048 -0.20 ARG 1036

ASP 1031 0.14 ASN 1049 -0.20 ARG 1036

ASP 1031 0.20 SER 1050 -0.19 ARG 1036

ASP 1031 0.22 THR 1051 -0.18 ARG 1036

ASP 1031 0.29 THR 1052 -0.15 THR 1035

ASP 1031 0.27 GLY 1053 -0.15 THR 1035

ASP 1031 0.30 PRO 1054 -0.17 THR 1035

ASP 1031 0.40 GLY 1055 -0.23 SER 953

ASP 1031 0.50 GLU 1056 -0.26 SER 953

ASP 1031 0.39 HSD 1057 -0.24 THR 1035

ASP 1031 0.28 LEU 1058 -0.23 THR 1035

ASP 1031 0.27 ARG 1059 -0.24 SER 953

GLU 999 0.21 ASN 1060 -0.33 THR 1035

PRO 1034 0.17 ALA 1061 -0.32 ARG 1036

ASP 1002 0.17 LEU 1062 -0.22 ARG 1036

GLU 999 0.17 TRP 1063 -0.20 SER 953

ARG 1000 0.17 HSD 1064 -0.35 ARG 1036

ARG 1000 0.20 THR 1065 -0.34 ARG 1036

ARG 1000 0.17 GLY 1066 -0.46 ARG 1036

PRO 1034 0.18 ASN 1067 -0.40 ARG 1036

PRO 1034 0.23 THR 1068 -0.41 ARG 1036

PRO 1034 0.19 PRO 1069 -0.36 ARG 1036

PRO 1034 0.19 GLY 1070 -0.26 ARG 1036

PRO 1034 0.19 GLN 1071 -0.26 ARG 1036

PRO 1034 0.16 VAL 1072 -0.28 ARG 1036

PRO 1034 0.16 ARG 1073 -0.28 ARG 1036

ARG 1000 0.19 THR 1074 -0.26 ARG 1036

ARG 1000 0.19 LEU 1075 -0.19 ARG 1036

ARG 1000 0.23 TRP 1076 -0.17 ARG 1036

ARG 1000 0.25 HSD 1077 -0.22 THR 1032

ARG 1000 0.28 ASP 1078 -0.23 THR 1032

ARG 1000 0.26 PRO 1079 -0.31 THR 1032

ARG 1000 0.30 ARG 1080 -0.28 THR 1032

ARG 1000 0.35 HSD 1081 -0.29 THR 1032

ARG 1000 0.42 ILE 1082 -0.23 THR 1032

ARG 1000 0.50 GLY 1083 -0.18 THR 1032

ARG 1000 0.50 TRP 1084 -0.16 LYS 1111

ARG 1000 0.57 LYS 1085 -0.29 LYS 1111

ARG 1000 0.54 ASP 1086 -0.35 LYS 1111

ARG 1000 0.37 PHE 1087 -0.49 LYS 1111

ARG 1000 0.35 THR 1088 -0.56 LYS 1111

ARG 1000 0.23 ALA 1089 -0.52 LYS 1111

ARG 1000 0.24 TYR 1090 -0.32 LYS 1111

ASP 1144 0.19 ARG 1091 -0.18 LYS 1111

ARG 1000 0.18 TRP 1092 -0.14 ARG 1093

GLN 964 0.20 ARG 1093 -0.14 TRP 1092

GLN 964 0.20 LEU 1094 -0.10 TYR 1090

GLN 964 0.21 SER 1095 -0.10 TYR 1090

GLN 964 0.19 HSD 1096 -0.09 ARG 1036

PRO 1152 0.26 ARG 1097 -0.08 TYR 1090

GLN 964 0.17 PRO 1098 -0.09 ARG 1036

PRO 1152 0.19 LYS 1099 -0.07 TYR 1090

PRO 1152 0.34 THR 1100 -0.07 TYR 1090

PRO 1152 0.25 GLY 1101 -0.09 ARG 1036

PRO 1152 0.29 PHE 1102 -0.09 ARG 1036

PRO 1152 0.22 ILE 1103 -0.10 ARG 1036

PRO 1152 0.21 ARG 1104 -0.09 ARG 1036

LYS 1111 0.20 VAL 1105 -0.10 TYR 1090

LYS 1111 0.27 VAL 1106 -0.11 TYR 1090

ARG 1000 0.25 MET 1107 -0.11 TYR 1090

ARG 1000 0.22 TYR 1108 -0.19 THR 1088

ARG 1000 0.19 GLU 1109 -0.34 LYS 1111

ARG 1000 0.09 GLY 1110 -0.83 LYS 1111

ILE 1113 0.40 LYS 1111 -0.83 GLY 1110

MET 1114 0.29 LYS 1112 -0.14 THR 1088

LYS 1111 0.40 ILE 1113 -0.15 THR 1088

ARG 1000 0.31 MET 1114 -0.12 THR 1032

ARG 1000 0.28 ALA 1115 -0.14 THR 1032

LYS 1111 0.32 ASP 1116 -0.12 THR 1032

LYS 1111 0.25 SER 1117 -0.13 THR 1032

LYS 1111 0.29 GLY 1118 -0.12 THR 1032

PRO 1152 0.29 PRO 1119 -0.10 ARG 1036

PRO 1152 0.24 ILE 1120 -0.12 ARG 1036

PRO 1152 0.24 TYR 1121 -0.11 ARG 1036

PRO 1152 0.18 ASP 1122 -0.13 ARG 1036

LYS 1099 0.17 LYS 1123 -0.12 ARG 1036

PRO 1034 0.15 THR 1124 -0.14 ARG 1036

GLN 964 0.13 TYR 1125 -0.13 ARG 1036

GLN 964 0.15 ALA 1126 -0.12 ARG 1036

GLN 964 0.17 GLY 1127 -0.11 ARG 1036

GLN 964 0.18 GLY 1128 -0.15 PRO 1152

GLN 964 0.17 ARG 1129 -0.15 PRO 1152

GLN 964 0.18 LEU 1130 -0.11 ASP 1151

GLN 964 0.13 GLY 1131 -0.10 THR 1035

ASP 1031 0.06 LEU 1132 -0.11 THR 1035

GLU 999 0.08 PHE 1133 -0.12 ARG 940

GLU 999 0.13 VAL 1134 -0.17 ARG 940

GLU 999 0.20 PHE 1135 -0.20 ARG 962

GLU 999 0.26 SER 1136 -0.27 ARG 962

SER 1136 0.20 GLN 1137 -0.29 ARG 962

ASN 973 0.18 GLU 1138 -0.41 ARG 962

ASN 973 0.20 MET 1139 -0.40 HSD 963

VAL 972 0.10 VAL 1140 -0.27 HSD 963

GLN 970 0.11 PHE 1141 -0.23 LYS 1111

VAL 960 0.11 PHE 1142 -0.17 LYS 1111

ARG 962 0.19 SER 1143 -0.17 PHE 1141

ARG 962 0.24 ASP 1144 -0.14 LEU 1145

LYS 966 0.26 LEU 1145 -0.14 PHE 1142

GLN 964 0.33 LYS 1146 -0.12 ASP 1144

GLN 964 0.33 TYR 1147 -0.11 THR 993

GLN 964 0.31 GLU 1148 -0.13 CYS 1149

GLN 964 0.26 CYS 1149 -0.15 ASP 1151

GLN 964 0.22 ARG 1150 -0.08 PHE 995

PRO 1119 0.22 ASP 1151 -0.23 PHE 985

THR 1100 0.34 PRO 1152 -0.24 GLU 984

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 19 ---

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

* *