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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 23 ---

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 0.45 THR 937 -0.80 LYS 966

CYS 1149 0.27 ASP 938 -0.75 LYS 966

ASP 1144 0.41 PHE 939 -0.85 LYS 966

ASP 1144 0.50 ARG 940 -0.69 HSD 963

ASP 1144 0.38 ARG 941 -0.47 GLN 943

ASP 1144 0.28 PHE 942 -0.49 GLN 943

GLY 992 0.21 GLN 943 -0.49 PHE 942

ALA 979 0.31 MET 944 -0.39 ILE 945

LEU 1132 0.29 ILE 945 -0.39 MET 944

GLY 977 0.34 PRO 946 -0.24 ARG 940

PHE 1007 0.29 LEU 947 -0.27 PHE 942

MET 1021 0.23 ASP 948 -0.21 ARG 940

PHE 1007 0.28 PRO 949 -0.19 THR 1052

PHE 1007 0.22 LYS 950 -0.19 PRO 1069

TYR 1004 0.20 GLY 951 -0.18 PRO 1069

SER 1136 0.25 THR 952 -0.13 PRO 1069

ASP 1002 0.21 SER 953 -0.18 ARG 940

ASP 1002 0.28 GLN 954 -0.20 ARG 940

GLN 1137 0.28 ASN 955 -0.21 ARG 940

GLN 1137 0.27 ASP 956 -0.23 ARG 940

PHE 994 0.27 PRO 957 -0.25 ARG 940

PHE 994 0.22 ASN 958 -0.28 ARG 940

ALA 1089 0.16 TRP 959 -0.30 PHE 1135

ALA 1089 0.12 VAL 960 -0.44 ARG 962

HSD 963 0.13 VAL 961 -0.43 PHE 939

HSD 963 0.40 ARG 962 -0.44 ARG 940

ARG 962 0.40 HSD 963 -0.69 ARG 940

GLY 965 0.20 GLN 964 -0.27 THR 937

GLU 967 0.21 GLY 965 -0.71 PHE 939

ARG 962 0.17 LYS 966 -0.85 PHE 939

GLY 965 0.21 GLU 967 -0.39 PHE 1007

SER 1143 0.14 LEU 968 -0.40 PHE 1133

ALA 1089 0.17 VAL 969 -0.31 TYR 1004

PHE 994 0.23 GLN 970 -0.33 PHE 1135

MET 1139 0.20 THR 971 -0.28 SER 1136

GLU 1138 0.27 VAL 972 -0.34 ASN 973

GLN 1137 0.30 ASN 973 -0.34 VAL 972

GLN 1137 0.27 CYS 974 -0.25 ASP 1031

SER 1136 0.29 ASP 975 -0.24 ARG 962

ALA 1005 0.30 PRO 976 -0.29 ARG 962

PRO 946 0.34 GLY 977 -0.31 PHE 942

LEU 1132 0.33 LEU 978 -0.43 PHE 942

MET 944 0.31 ALA 979 -0.45 LYS 966

GLY 992 0.22 VAL 980 -0.52 LYS 966

GLY 992 0.20 GLY 981 -0.58 LYS 966

GLY 992 0.15 TYR 982 -0.47 LYS 966

PRO 949 0.15 ASP 983 -0.53 LYS 966

PRO 949 0.17 GLU 984 -0.46 LYS 966

PRO 949 0.10 PHE 985 -0.46 LYS 966

LYS 1099 0.11 ASN 986 -0.40 LYS 966

THR 937 0.20 ALA 987 -0.35 LYS 966

THR 937 0.24 VAL 988 -0.37 LYS 966

ASP 1151 0.27 ASP 989 -0.36 LYS 966

ILE 945 0.22 PHE 990 -0.43 LYS 966

PHE 939 0.25 SER 991 -0.39 LYS 966

PHE 939 0.27 GLY 992 -0.40 LYS 966

MET 944 0.26 THR 993 -0.26 LYS 966

PRO 946 0.27 PHE 994 -0.22 LYS 1023

PRO 957 0.23 PHE 995 -0.23 GLN 1027

VAL 972 0.25 ILE 996 -0.27 GLN 1027

VAL 972 0.19 ASN 997 -0.27 GLN 1027

VAL 972 0.19 THR 998 -0.30 GLN 1027

ASP 1086 0.25 GLU 999 -0.31 GLN 1027

ASN 955 0.20 ARG 1000 -0.37 GLN 1027

GLN 954 0.24 ASP 1001 -0.35 GLN 1027

GLN 954 0.28 ASP 1002 -0.35 GLN 1027

GLN 954 0.26 ASP 1003 -0.29 VAL 1140

ASP 975 0.28 TYR 1004 -0.35 LEU 968

VAL 1134 0.34 ALA 1005 -0.31 LEU 968

PHE 1133 0.30 GLY 1006 -0.39 LYS 966

PHE 1133 0.30 PHE 1007 -0.50 LYS 966

SER 1014 0.26 VAL 1008 -0.50 LYS 966

TYR 1011 0.24 PHE 1009 -0.52 LYS 966

SER 1013 0.20 GLY 1010 -0.47 LYS 966

PHE 1009 0.24 TYR 1011 -0.47 LYS 966

SER 1013 0.29 GLN 1012 -0.43 LYS 966

GLN 1012 0.29 SER 1013 -0.43 PHE 942

VAL 1008 0.26 SER 1014 -0.39 PHE 942

PRO 1034 0.21 SER 1015 -0.38 PHE 942

PHE 1017 0.19 ARG 1016 -0.40 LYS 966

ARG 1016 0.19 PHE 1017 -0.44 LYS 966

VAL 1105 0.20 TYR 1018 -0.44 LYS 966

PRO 1054 0.23 VAL 1019 -0.45 LYS 966

PRO 1054 0.20 VAL 1020 -0.40 LYS 966

PRO 976 0.27 MET 1021 -0.37 LYS 966

PRO 976 0.28 TRP 1022 -0.27 LYS 966

ASP 975 0.25 LYS 1023 -0.27 GLU 967

GLN 954 0.24 GLN 1024 -0.26 VAL 1025

GLN 954 0.23 VAL 1025 -0.26 GLN 1024

GLN 954 0.17 THR 1026 -0.22 LEU 968

SER 953 0.14 GLN 1027 -0.37 ARG 1000

THR 1051 0.13 SER 1028 -0.31 ARG 1000

THR 1051 0.15 TYR 1029 -0.34 GLN 1137

THR 1051 0.14 TRP 1030 -0.32 ARG 1000

THR 1051 0.17 ASP 1031 -0.27 VAL 972

THR 1051 0.25 THR 1032 -0.26 ARG 1000

THR 1051 0.24 ASN 1033 -0.19 ARG 962

THR 1051 0.31 PRO 1034 -0.18 LYS 966

THR 1051 0.33 THR 1035 -0.21 LYS 966

GLY 1070 0.27 ARG 1036 -0.25 ARG 1000

THR 1051 0.17 ALA 1037 -0.27 VAL 961

THR 1051 0.13 GLN 1038 -0.27 LEU 968

TRP 1063 0.13 GLY 1039 -0.28 LEU 968

GLN 954 0.11 TYR 1040 -0.24 LEU 968

GLN 954 0.19 SER 1041 -0.21 GLU 967

ASP 975 0.19 GLY 1042 -0.21 LYS 966

PRO 976 0.19 LEU 1043 -0.26 LYS 966

PRO 1054 0.14 SER 1044 -0.32 LYS 966

MET 1114 0.14 VAL 1045 -0.36 LYS 966

VAL 1048 0.15 LYS 1046 -0.39 LYS 966

MET 1114 0.13 VAL 1047 -0.41 LYS 966

MET 1114 0.15 VAL 1048 -0.39 LYS 966

THR 1035 0.19 ASN 1049 -0.36 LYS 966

THR 1035 0.26 SER 1050 -0.32 PHE 942

THR 1035 0.33 THR 1051 -0.27 LYS 966

PRO 1034 0.30 THR 1052 -0.22 LYS 966

PRO 1034 0.25 GLY 1053 -0.25 THR 1051

GLY 1055 0.31 PRO 1054 -0.23 ARG 940

PRO 1054 0.31 GLY 1055 -0.23 PRO 1069

PRO 1054 0.17 GLU 1056 -0.20 PRO 1069

PRO 1034 0.22 HSD 1057 -0.26 PRO 1069

GLY 1053 0.18 LEU 1058 -0.26 PHE 942

MET 1021 0.22 ARG 1059 -0.25 PHE 942

GLY 1053 0.17 ASN 1060 -0.26 VAL 961

SER 1050 0.15 ALA 1061 -0.28 LYS 966

MET 1021 0.17 LEU 1062 -0.32 LYS 966

SER 1041 0.14 TRP 1063 -0.32 VAL 961

SER 1050 0.11 HSD 1064 -0.29 LYS 966

LYS 1112 0.09 THR 1065 -0.30 LYS 966

LYS 1112 0.09 GLY 1066 -0.30 LYS 966

GLN 1038 0.09 ASN 1067 -0.30 LYS 966

ARG 1036 0.15 THR 1068 -0.29 LYS 966

ARG 1036 0.25 PRO 1069 -0.29 LYS 966

THR 1035 0.29 GLY 1070 -0.30 LYS 966

THR 1035 0.24 GLN 1071 -0.31 LYS 966

ARG 1036 0.12 VAL 1072 -0.35 LYS 966

LYS 1112 0.10 ARG 1073 -0.35 LYS 966

LYS 1112 0.11 THR 1074 -0.34 LYS 966

LYS 1112 0.12 LEU 1075 -0.33 LYS 966

LYS 1112 0.15 TRP 1076 -0.29 LYS 966

LYS 1112 0.16 HSD 1077 -0.26 LYS 966

LYS 1112 0.20 ASP 1078 -0.20 LYS 966

LYS 1112 0.22 PRO 1079 -0.21 PRO 1119

LYS 1112 0.23 ARG 1080 -0.18 PRO 1119

GLN 954 0.15 HSD 1081 -0.16 ARG 1036

GLY 1083 0.22 ILE 1082 -0.12 ARG 1036

ASP 975 0.22 GLY 1083 -0.16 SER 1041

ASP 975 0.24 TRP 1084 -0.18 VAL 1025

ASN 973 0.25 LYS 1085 -0.23 VAL 1025

ASN 973 0.26 ASP 1086 -0.24 VAL 1025

VAL 972 0.20 PHE 1087 -0.24 GLN 1027

ASP 956 0.22 THR 1088 -0.19 VAL 1025

PRO 957 0.24 ALA 1089 -0.17 VAL 1025

PRO 946 0.27 TYR 1090 -0.14 VAL 1025

PRO 946 0.25 ARG 1091 -0.18 LYS 966

PRO 946 0.26 TRP 1092 -0.26 LYS 966

PRO 946 0.23 ARG 1093 -0.29 LYS 966

PRO 949 0.21 LEU 1094 -0.35 LYS 966

THR 937 0.18 SER 1095 -0.31 LYS 966

SER 1014 0.14 HSD 1096 -0.35 LYS 966

THR 937 0.17 ARG 1097 -0.31 LYS 966

THR 937 0.10 PRO 1098 -0.34 LYS 966

THR 937 0.17 LYS 1099 -0.37 LYS 1123

THR 937 0.16 THR 1100 -0.26 LYS 966

THR 937 0.09 GLY 1101 -0.31 LYS 966

THR 937 0.13 PHE 1102 -0.28 LYS 966

ARG 1016 0.13 ILE 1103 -0.31 LYS 966

TYR 1018 0.15 ARG 1104 -0.27 LYS 966

LEU 947 0.20 VAL 1105 -0.28 LYS 966

PRO 946 0.21 VAL 1106 -0.20 LYS 966

PRO 946 0.25 MET 1107 -0.16 LYS 966

PRO 946 0.24 TYR 1108 -0.08 LYS 966

PRO 946 0.24 GLU 1109 -0.10 VAL 1025

PRO 1152 0.24 GLY 1110 -0.12 LYS 1111

PRO 1152 0.23 LYS 1111 -0.12 GLY 1110

ILE 1113 0.32 LYS 1112 -0.05 GLY 1110

LYS 1112 0.32 ILE 1113 -0.05 LYS 966

LYS 1112 0.27 MET 1114 -0.06 LYS 966

LYS 1112 0.25 ALA 1115 -0.13 LYS 966

LYS 1112 0.19 ASP 1116 -0.17 LYS 966

LYS 1112 0.17 SER 1117 -0.23 LYS 966

LYS 1112 0.17 GLY 1118 -0.19 LYS 966

THR 937 0.14 PRO 1119 -0.21 PRO 1079

LYS 1112 0.11 ILE 1120 -0.27 LYS 966

LYS 1112 0.10 TYR 1121 -0.29 LYS 966

LYS 1112 0.09 ASP 1122 -0.34 LYS 966

ALA 1126 0.11 LYS 1123 -0.37 LYS 1099

ILE 1103 0.09 THR 1124 -0.37 LYS 966

ILE 1103 0.11 TYR 1125 -0.39 LYS 966

LYS 1123 0.11 ALA 1126 -0.52 PRO 1152

SER 1013 0.10 GLY 1127 -0.42 LYS 966

SER 1013 0.15 GLY 1128 -0.48 LYS 966

PRO 949 0.19 ARG 1129 -0.51 LYS 966

ILE 945 0.23 LEU 1130 -0.58 LYS 966

ILE 945 0.29 GLY 1131 -0.57 LYS 966

LEU 978 0.33 LEU 1132 -0.50 LYS 966

PHE 1007 0.30 PHE 1133 -0.43 LYS 966

ALA 1005 0.34 VAL 1134 -0.35 VAL 961

ASP 975 0.29 PHE 1135 -0.34 VAL 961

ASP 975 0.29 SER 1136 -0.32 GLN 970

ASN 973 0.30 GLN 1137 -0.34 TYR 1029

VAL 972 0.27 GLU 1138 -0.29 TYR 1029

VAL 972 0.23 MET 1139 -0.28 TYR 1029

PRO 957 0.23 VAL 1140 -0.33 TYR 1004

ALA 1089 0.20 PHE 1141 -0.31 TYR 1004

MET 944 0.21 PHE 1142 -0.37 GLU 967

ARG 940 0.33 SER 1143 -0.38 LYS 966

ARG 940 0.50 ASP 1144 -0.45 LYS 966

PHE 939 0.40 LEU 1145 -0.67 LYS 966

PHE 939 0.39 LYS 1146 -0.57 LYS 966

THR 937 0.33 TYR 1147 -0.49 LYS 966

ASP 1151 0.46 GLU 1148 -0.40 LYS 966

THR 937 0.45 CYS 1149 -0.31 LYS 966

ASP 1151 0.53 ARG 1150 -0.26 LYS 966

ARG 1150 0.53 ASP 1151 -0.33 ALA 1126

ARG 1150 0.38 PRO 1152 -0.52 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 2405021543434120385

--- normal mode 23 ---

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

* *