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

* *

CA distance fluctuations for 240531115742101615

--- normal mode 17 ---

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 0.10 PHE 939 -0.23 PRO 1152

GLY 951 0.11 ARG 940 -0.26 PRO 1152

ARG 962 0.17 ARG 941 -0.28 PRO 1152

GLY 951 0.14 PHE 942 -0.24 PRO 1152

GLY 951 0.19 GLN 943 -0.26 PRO 1152

GLY 951 0.21 MET 944 -0.20 PRO 1152

GLY 951 0.24 ILE 945 -0.22 THR 1035

ASP 1031 0.29 PRO 946 -0.24 THR 1035

ASP 1031 0.33 LEU 947 -0.27 THR 1035

ASP 1031 0.45 ASP 948 -0.29 THR 1035

ASP 1031 0.49 PRO 949 -0.33 SER 953

ASP 1031 0.57 LYS 950 -0.44 SER 953

PRO 949 0.27 GLY 951 -0.67 PRO 1034

ARG 962 0.22 THR 952 -0.60 PRO 1034

ARG 962 0.26 SER 953 -0.49 PRO 1034

ARG 1000 0.26 GLN 954 -0.36 PRO 1034

ARG 1000 0.26 ASN 955 -0.28 PRO 1034

ASP 1031 0.22 ASP 956 -0.23 PRO 1034

ARG 1000 0.19 PRO 957 -0.17 PRO 1034

SER 953 0.21 ASN 958 -0.15 PRO 1034

GLY 951 0.18 TRP 959 -0.13 PRO 1152

SER 953 0.19 VAL 960 -0.13 PRO 1152

SER 953 0.16 VAL 961 -0.17 GLU 967

SER 953 0.26 ARG 962 -0.30 GLU 967

SER 953 0.19 HSD 963 -0.41 GLY 965

MET 1139 0.14 GLN 964 -0.23 PRO 1152

LYS 1111 0.16 GLY 965 -0.41 HSD 963

LYS 1111 0.14 LYS 966 -0.22 HSD 963

LYS 1111 0.14 GLU 967 -0.30 ARG 962

LYS 1111 0.14 LEU 968 -0.18 ARG 962

LYS 1111 0.14 VAL 969 -0.09 THR 1035

LYS 1111 0.14 GLN 970 -0.12 PRO 1034

ARG 1000 0.19 THR 971 -0.15 PRO 1034

ARG 1000 0.30 VAL 972 -0.19 PRO 1034

ARG 1000 0.35 ASN 973 -0.23 PRO 1034

ARG 1000 0.25 CYS 974 -0.24 PRO 1034

ASP 1031 0.26 ASP 975 -0.25 PRO 1034

ASP 1031 0.22 PRO 976 -0.20 THR 1035

ASP 1031 0.18 GLY 977 -0.21 THR 1035

ASP 1031 0.14 LEU 978 -0.19 THR 1035

GLY 951 0.14 ALA 979 -0.17 PRO 1152

GLY 951 0.13 VAL 980 -0.23 PRO 1152

GLY 951 0.12 GLY 981 -0.29 PRO 1152

GLY 951 0.12 TYR 982 -0.39 PRO 1152

GLY 951 0.10 ASP 983 -0.46 PRO 1152

GLY 951 0.09 GLU 984 -0.50 PRO 1152

LYS 1099 0.06 PHE 985 -0.39 ASP 1151

LYS 1099 0.07 ASN 986 -0.28 PRO 1152

PRO 1034 0.10 ALA 987 -0.13 ARG 1036

PRO 1034 0.10 VAL 988 -0.12 GLN 964

PRO 1152 0.16 ASP 989 -0.13 GLN 964

PRO 1034 0.09 PHE 990 -0.14 HSD 963

PRO 1152 0.09 SER 991 -0.17 ARG 962

LYS 1111 0.12 GLY 992 -0.20 ARG 962

LYS 1111 0.24 THR 993 -0.22 ARG 962

LYS 1111 0.23 PHE 994 -0.18 ARG 962

LYS 1111 0.31 PHE 995 -0.17 ARG 962

LYS 1111 0.26 ILE 996 -0.17 ARG 1000

LYS 1111 0.27 ASN 997 -0.16 ARG 1000

LYS 1111 0.21 THR 998 -0.18 ASP 1031

LYS 1111 0.18 GLU 999 -0.25 ASP 1031

ASN 973 0.35 ARG 1000 -0.41 LYS 1085

ARG 1000 0.20 ASP 1001 -0.27 ASP 1031

ARG 1036 0.19 ASP 1002 -0.31 ASP 1031

GLN 1027 0.19 ASP 1003 -0.20 TRP 1030

GLY 1110 0.10 TYR 1004 -0.14 TRP 1030

GLY 1110 0.11 ALA 1005 -0.09 TRP 1030

GLY 1110 0.10 GLY 1006 -0.09 ARG 1000

GLY 1110 0.07 PHE 1007 -0.10 THR 1035

PRO 1034 0.08 VAL 1008 -0.14 THR 1035

PRO 1034 0.10 PHE 1009 -0.14 ARG 1036

PRO 1034 0.11 GLY 1010 -0.20 ASN 986

ASP 1031 0.11 TYR 1011 -0.25 PRO 1152

ASP 1031 0.15 GLN 1012 -0.32 PRO 1152

ASP 1031 0.20 SER 1013 -0.30 PRO 1152

ASP 1031 0.24 SER 1014 -0.27 THR 1035

ASP 1031 0.26 SER 1015 -0.29 THR 1035

ASP 1031 0.18 ARG 1016 -0.27 ARG 1036

PRO 1034 0.14 PHE 1017 -0.23 ARG 1036

PRO 1034 0.18 TYR 1018 -0.20 ARG 1036

PRO 1034 0.16 VAL 1019 -0.14 ARG 1036

PRO 1034 0.16 VAL 1020 -0.11 ARG 1000

PRO 1034 0.14 MET 1021 -0.12 ARG 1000

PRO 1034 0.12 TRP 1022 -0.19 ARG 1000

GLU 1109 0.13 LYS 1023 -0.22 ASP 1031

ARG 1036 0.21 GLN 1024 -0.31 ARG 1000

ARG 1036 0.26 VAL 1025 -0.45 ASP 1031

ARG 1036 0.34 THR 1026 -0.49 ASP 1031

ARG 1036 0.39 GLN 1027 -0.54 ASP 1031

ARG 1036 0.57 SER 1028 -0.65 ASP 1031

ARG 1036 0.49 TYR 1029 -0.37 ASP 1031

ARG 1036 0.32 TRP 1030 -0.33 GLN 1027

GLU 1056 0.67 ASP 1031 -0.65 SER 1028

GLU 1056 0.37 THR 1032 -0.62 SER 1028

PRO 1069 0.36 ASN 1033 -0.34 GLY 951

THR 1068 0.65 PRO 1034 -0.67 GLY 951

ALA 1037 0.30 THR 1035 -0.59 HSD 1057

SER 1028 0.57 ARG 1036 -0.58 THR 1068

PRO 1034 0.31 ALA 1037 -0.33 THR 1032

THR 1026 0.22 GLN 1038 -0.48 THR 1032

GLN 1038 0.19 GLY 1039 -0.31 THR 1032

PRO 1034 0.21 TYR 1040 -0.33 THR 1032

ARG 1036 0.19 SER 1041 -0.31 ASP 1031

PRO 1034 0.18 GLY 1042 -0.23 ASP 1031

PRO 1034 0.19 LEU 1043 -0.21 ARG 1000

PRO 1034 0.25 SER 1044 -0.16 THR 1032

PRO 1034 0.24 VAL 1045 -0.13 TYR 1029

PRO 1034 0.29 LYS 1046 -0.20 ARG 1036

PRO 1034 0.26 VAL 1047 -0.27 ARG 1036

PRO 1034 0.23 VAL 1048 -0.30 ARG 1036

PRO 1034 0.23 ASN 1049 -0.35 ARG 1036

ASP 1031 0.28 SER 1050 -0.36 ARG 1036

ASP 1031 0.32 THR 1051 -0.37 ARG 1036

ASP 1031 0.41 THR 1052 -0.38 THR 1035

ASP 1031 0.37 GLY 1053 -0.34 THR 1035

ASP 1031 0.41 PRO 1054 -0.34 THR 1035

ASP 1031 0.55 GLY 1055 -0.38 THR 1035

ASP 1031 0.67 GLU 1056 -0.46 THR 1035

ASP 1031 0.54 HSD 1057 -0.59 THR 1035

ASP 1031 0.37 LEU 1058 -0.45 THR 1035

ASP 1031 0.33 ARG 1059 -0.38 THR 1035

ASP 1031 0.24 ASN 1060 -0.50 THR 1035

PRO 1034 0.36 ALA 1061 -0.43 ARG 1036

PRO 1034 0.21 LEU 1062 -0.24 ARG 1036

PRO 1034 0.21 TRP 1063 -0.17 TYR 1029

PRO 1034 0.44 HSD 1064 -0.30 ARG 1036

PRO 1034 0.45 THR 1065 -0.21 SER 1028

PRO 1034 0.57 GLY 1066 -0.39 ARG 1036

PRO 1034 0.56 ASN 1067 -0.49 ARG 1036

PRO 1034 0.65 THR 1068 -0.58 ARG 1036

PRO 1034 0.58 PRO 1069 -0.56 ARG 1036

PRO 1034 0.41 GLY 1070 -0.45 ARG 1036

PRO 1034 0.35 GLN 1071 -0.44 ARG 1036

PRO 1034 0.36 VAL 1072 -0.39 ARG 1036

PRO 1034 0.43 ARG 1073 -0.36 ARG 1036

PRO 1034 0.39 THR 1074 -0.27 ARG 1036

PRO 1034 0.36 LEU 1075 -0.21 ARG 1036

PRO 1034 0.33 TRP 1076 -0.20 HSD 1077

PRO 1034 0.32 HSD 1077 -0.20 TRP 1076

PRO 1034 0.26 ASP 1078 -0.21 THR 1032

PRO 1034 0.31 PRO 1079 -0.23 THR 1032

PRO 1034 0.24 ARG 1080 -0.25 ASP 1031

PRO 1034 0.21 HSD 1081 -0.29 ASP 1031

ARG 1036 0.18 ILE 1082 -0.31 ARG 1000

ARG 1036 0.20 GLY 1083 -0.33 ARG 1000

LYS 1111 0.19 TRP 1084 -0.35 ARG 1000

LYS 1111 0.25 LYS 1085 -0.41 ARG 1000

LYS 1111 0.27 ASP 1086 -0.41 ARG 1000

LYS 1111 0.36 PHE 1087 -0.27 ARG 1000

LYS 1111 0.43 THR 1088 -0.25 ARG 1000

LYS 1111 0.44 ALA 1089 -0.17 ARG 962

LYS 1111 0.30 TYR 1090 -0.17 ARG 1000

LYS 1111 0.19 ARG 1091 -0.18 ARG 962

PRO 1152 0.14 TRP 1092 -0.15 ARG 962

PRO 1152 0.19 ARG 1093 -0.15 LYS 1111

PRO 1152 0.17 LEU 1094 -0.16 LYS 1111

PRO 1152 0.27 SER 1095 -0.22 LYS 1111

PRO 1152 0.22 HSD 1096 -0.20 LYS 1111

PRO 1152 0.24 ARG 1097 -0.19 LYS 1111

PRO 1034 0.16 PRO 1098 -0.18 ARG 1036

PRO 1034 0.17 LYS 1099 -0.19 LYS 1111

PRO 1152 0.31 THR 1100 -0.25 LYS 1111

PRO 1034 0.23 GLY 1101 -0.22 LYS 1111

PRO 1152 0.30 PHE 1102 -0.27 LYS 1111

PRO 1152 0.24 ILE 1103 -0.24 LYS 1111

PRO 1152 0.29 ARG 1104 -0.31 LYS 1111

PRO 1152 0.23 VAL 1105 -0.24 LYS 1111

PRO 1152 0.26 VAL 1106 -0.32 LYS 1111

PRO 1152 0.19 MET 1107 -0.18 ARG 1000

PRO 1152 0.19 TYR 1108 -0.16 ARG 1000

LYS 1111 0.31 GLU 1109 -0.13 LYS 1112

LYS 1111 0.78 GLY 1110 -0.13 GLY 1118

GLY 1110 0.78 LYS 1111 -0.39 GLY 1118

PRO 1152 0.20 LYS 1112 -0.26 ILE 1113

PRO 1152 0.24 ILE 1113 -0.32 LYS 1111

PRO 1152 0.20 MET 1114 -0.23 ARG 1000

PRO 1152 0.22 ALA 1115 -0.23 ARG 1000

PRO 1152 0.27 ASP 1116 -0.33 LYS 1111

PRO 1152 0.25 SER 1117 -0.30 LYS 1111

PRO 1152 0.34 GLY 1118 -0.39 LYS 1111

PRO 1152 0.37 PRO 1119 -0.36 LYS 1111

PRO 1034 0.28 ILE 1120 -0.27 LYS 1111

PRO 1034 0.28 TYR 1121 -0.26 LYS 1111

PRO 1034 0.28 ASP 1122 -0.22 ARG 1036

PRO 1034 0.24 LYS 1123 -0.24 ARG 1036

PRO 1034 0.25 THR 1124 -0.27 ARG 1036

PRO 1034 0.17 TYR 1125 -0.25 ARG 1036

PRO 1034 0.15 ALA 1126 -0.22 PRO 1152

PRO 1034 0.10 GLY 1127 -0.26 ASN 986

ARG 1129 0.10 GLY 1128 -0.34 PRO 1152

GLY 1128 0.10 ARG 1129 -0.31 PRO 1152

GLY 951 0.08 LEU 1130 -0.18 PRO 1152

GLY 951 0.09 GLY 1131 -0.14 PRO 1152

GLY 1110 0.08 LEU 1132 -0.13 THR 1035

GLY 1110 0.08 PHE 1133 -0.14 THR 1035

GLN 1027 0.10 VAL 1134 -0.13 THR 1035

GLN 1027 0.13 PHE 1135 -0.15 THR 1035

GLN 1027 0.19 SER 1136 -0.18 PRO 1034

GLN 1027 0.15 GLN 1137 -0.16 PRO 1034

ARG 1000 0.18 GLU 1138 -0.17 PRO 1034

LYS 1111 0.20 MET 1139 -0.14 ASN 1033

LYS 1111 0.20 VAL 1140 -0.10 ASN 1033

LYS 1111 0.21 PHE 1141 -0.18 ARG 962

LYS 1111 0.18 PHE 1142 -0.20 ARG 962

LYS 1111 0.20 SER 1143 -0.29 ARG 962

LYS 1111 0.20 ASP 1144 -0.28 ARG 962

LYS 1111 0.13 LEU 1145 -0.21 ARG 962

GLY 1110 0.08 LYS 1146 -0.17 HSD 963

SER 991 0.09 TYR 1147 -0.17 GLN 964

ILE 1113 0.08 GLU 1148 -0.16 GLN 964

VAL 1106 0.09 CYS 1149 -0.18 ASP 983

ASP 1151 0.37 ARG 1150 -0.17 ASP 983

ARG 1150 0.37 ASP 1151 -0.46 GLU 984

PRO 1119 0.37 PRO 1152 -0.50 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 17 ---

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

* *