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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 21 ---

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 1146 0.19 THR 937 -0.31 ASN 958

LYS 1146 0.22 ASP 938 -0.34 ASN 958

GLY 965 0.34 PHE 939 -0.37 ASN 958

GLY 965 0.48 ARG 940 -0.41 TRP 959

GLY 965 0.54 ARG 941 -0.37 ASN 958

GLY 965 0.51 PHE 942 -0.46 PRO 957

GLY 965 0.39 GLN 943 -0.35 ASP 956

VAL 961 0.36 MET 944 -0.48 ASP 956

VAL 961 0.38 ILE 945 -0.30 TYR 982

TRP 959 0.37 PRO 946 -0.31 ASP 956

TRP 959 0.29 LEU 947 -0.28 ASP 1151

TRP 959 0.26 ASP 948 -0.25 ASP 1151

TRP 959 0.29 PRO 949 -0.24 ASP 1151

VAL 961 0.22 LYS 950 -0.21 ASP 1151

VAL 961 0.15 GLY 951 -0.24 ASP 1151

ASP 1031 0.21 THR 952 -0.27 PRO 946

ASP 1031 0.14 SER 953 -0.32 ARG 1000

ASN 955 0.21 GLN 954 -0.30 PHE 942

GLN 954 0.21 ASN 955 -0.36 MET 944

SER 1028 0.15 ASP 956 -0.48 MET 944

PRO 949 0.25 PRO 957 -0.46 PHE 942

PRO 949 0.23 ASN 958 -0.45 PHE 942

PRO 946 0.37 TRP 959 -0.41 ARG 940

PRO 946 0.29 VAL 960 -0.34 ARG 940

ILE 945 0.38 VAL 961 -0.18 HSD 963

ILE 945 0.34 ARG 962 -0.16 GLN 964

PHE 1087 0.11 HSD 963 -0.33 VAL 960

ASP 1144 0.40 GLN 964 -0.16 ARG 962

ARG 941 0.54 GLY 965 -0.15 ARG 962

GLU 967 0.66 LYS 966 -0.15 ARG 962

LYS 966 0.66 GLU 967 -0.18 ASP 1151

LYS 966 0.38 LEU 968 -0.23 THR 937

PRO 946 0.27 VAL 969 -0.24 TYR 1147

PRO 946 0.25 GLN 970 -0.31 PHE 939

TYR 1004 0.16 THR 971 -0.26 PHE 939

THR 1026 0.17 VAL 972 -0.31 PHE 942

THR 1026 0.18 ASN 973 -0.31 LEU 1132

SER 1136 0.19 CYS 974 -0.38 PHE 942

PRO 957 0.17 ASP 975 -0.34 GLY 977

TRP 959 0.23 PRO 976 -0.38 LEU 1130

VAL 961 0.29 GLY 977 -0.37 CYS 974

LYS 966 0.35 LEU 978 -0.39 LEU 1130

GLY 965 0.39 ALA 979 -0.39 PRO 957

GLY 965 0.39 VAL 980 -0.37 GLY 981

GLY 965 0.37 GLY 981 -0.37 VAL 980

GLY 965 0.32 TYR 982 -0.33 ASP 956

GLY 965 0.22 ASP 983 -0.31 LEU 978

GLY 965 0.20 GLU 984 -0.32 ASP 1151

GLY 965 0.15 PHE 985 -0.36 ASP 1151

GLY 965 0.13 ASN 986 -0.33 GLY 1010

GLN 964 0.14 ALA 987 -0.33 VAL 1019

GLN 964 0.16 VAL 988 -0.37 MET 1021

TYR 1147 0.27 ASP 989 -0.34 MET 1021

SER 1095 0.26 PHE 990 -0.41 GLY 1006

GLN 964 0.26 SER 991 -0.31 CYS 1149

GLN 964 0.30 GLY 992 -0.28 TYR 1004

LYS 966 0.33 THR 993 -0.23 CYS 1149

LYS 966 0.39 PHE 994 -0.23 CYS 1149

LYS 966 0.33 PHE 995 -0.19 CYS 1149

LYS 966 0.29 ILE 996 -0.21 TRP 1030

LYS 966 0.30 ASN 997 -0.21 TRP 1030

LYS 966 0.23 THR 998 -0.28 TRP 1030

ASP 1086 0.21 GLU 999 -0.39 TRP 1030

LYS 966 0.16 ARG 1000 -0.46 TRP 1030

LYS 966 0.15 ASP 1001 -0.41 TRP 1030

LYS 966 0.15 ASP 1002 -0.34 TRP 1030

GLN 1137 0.19 ASP 1003 -0.31 CYS 1149

LYS 966 0.22 TYR 1004 -0.37 PHE 1007

LYS 966 0.29 ALA 1005 -0.32 CYS 1149

LYS 966 0.31 GLY 1006 -0.41 PHE 990

LYS 966 0.37 PHE 1007 -0.45 PHE 1133

LYS 966 0.33 VAL 1008 -0.34 ASP 1151

GLY 965 0.33 PHE 1009 -0.33 ASP 1151

GLY 965 0.28 GLY 1010 -0.33 ASN 986

GLY 965 0.32 TYR 1011 -0.30 ASP 1151

GLY 965 0.28 GLN 1012 -0.26 ASP 1151

GLY 965 0.30 SER 1013 -0.25 ASP 1151

LYS 966 0.30 SER 1014 -0.24 ASP 1151

LYS 966 0.29 SER 1015 -0.19 ASP 1151

GLY 965 0.29 ARG 1016 -0.22 ASN 986

LYS 966 0.31 PHE 1017 -0.30 ASN 986

LYS 966 0.31 TYR 1018 -0.30 TRP 1063

LYS 966 0.32 VAL 1019 -0.34 VAL 988

LYS 966 0.32 VAL 1020 -0.34 VAL 988

LYS 966 0.29 MET 1021 -0.37 VAL 988

LYS 966 0.27 TRP 1022 -0.43 LYS 1023

LYS 966 0.20 LYS 1023 -0.43 TRP 1022

LYS 966 0.19 GLN 1024 -0.28 CYS 1149

ASN 973 0.16 VAL 1025 -0.28 CYS 1149

CYS 974 0.18 THR 1026 -0.29 SER 1095

CYS 974 0.19 GLN 1027 -0.30 SER 1095

CYS 974 0.18 SER 1028 -0.34 THR 1032

ASN 955 0.11 TYR 1029 -0.37 ARG 1000

THR 952 0.12 TRP 1030 -0.46 ARG 1000

THR 952 0.21 ASP 1031 -0.41 ARG 1000

THR 952 0.16 THR 1032 -0.36 ARG 1000

THR 952 0.14 ASN 1033 -0.31 ARG 1000

LYS 966 0.13 PRO 1034 -0.25 ARG 1000

LYS 966 0.14 THR 1035 -0.22 ARG 1000

THR 952 0.13 ARG 1036 -0.26 LEU 1075

LYS 966 0.13 ALA 1037 -0.29 SER 1095

CYS 974 0.15 GLN 1038 -0.32 SER 1095

CYS 974 0.18 GLY 1039 -0.33 SER 1095

LYS 966 0.18 TYR 1040 -0.34 LEU 1043

LYS 966 0.20 SER 1041 -0.29 SER 1095

LYS 966 0.22 GLY 1042 -0.34 LEU 1043

LYS 966 0.28 LEU 1043 -0.34 TYR 1040

LYS 966 0.27 SER 1044 -0.35 SER 1095

LYS 966 0.29 VAL 1045 -0.35 HSD 1096

LYS 966 0.28 LYS 1046 -0.31 HSD 1096

LYS 966 0.29 VAL 1047 -0.25 ASN 986

LYS 966 0.28 VAL 1048 -0.24 ASN 986

LYS 966 0.27 ASN 1049 -0.18 ASN 986

LYS 966 0.26 SER 1050 -0.16 ASP 1151

LYS 966 0.25 THR 1051 -0.12 ASP 1151

LYS 966 0.24 THR 1052 -0.14 ASP 1151

VAL 961 0.26 GLY 1053 -0.19 ASP 1151

VAL 961 0.27 PRO 1054 -0.22 ASP 1151

VAL 961 0.23 GLY 1055 -0.22 ASP 1151

VAL 961 0.18 GLU 1056 -0.22 ASP 1151

LYS 966 0.20 HSD 1057 -0.20 ASP 1151

LYS 966 0.23 LEU 1058 -0.23 ASP 1151

LYS 966 0.19 ARG 1059 -0.28 ASP 1151

LYS 966 0.16 ASN 1060 -0.28 VAL 988

LYS 966 0.20 ALA 1061 -0.26 ASN 986

LYS 966 0.23 LEU 1062 -0.30 VAL 988

LYS 966 0.19 TRP 1063 -0.33 VAL 988

LYS 966 0.18 HSD 1064 -0.31 SER 1095

LYS 966 0.22 THR 1065 -0.31 LEU 1075

LYS 966 0.22 GLY 1066 -0.31 LEU 1075

LYS 966 0.23 ASN 1067 -0.22 TYR 1121

LYS 966 0.21 THR 1068 -0.19 ALA 987

LYS 966 0.21 PRO 1069 -0.15 ASN 986

LYS 966 0.23 GLY 1070 -0.14 ASN 986

LYS 966 0.24 GLN 1071 -0.19 ASN 986

LYS 966 0.25 VAL 1072 -0.23 ASN 986

LYS 966 0.25 ARG 1073 -0.23 ARG 1036

LYS 966 0.26 THR 1074 -0.31 LEU 1075

LYS 966 0.26 LEU 1075 -0.31 THR 1065

LYS 966 0.26 TRP 1076 -0.31 THR 1065

LYS 966 0.25 HSD 1077 -0.32 ARG 1104

LYS 966 0.24 ASP 1078 -0.33 SER 1117

LYS 966 0.22 PRO 1079 -0.29 GLY 1118

GLY 1083 0.24 ARG 1080 -0.22 SER 1095

GLY 1083 0.23 HSD 1081 -0.27 SER 1095

GLY 1083 0.38 ILE 1082 -0.24 CYS 1149

ILE 1082 0.38 GLY 1083 -0.27 CYS 1149

ILE 1082 0.23 TRP 1084 -0.26 CYS 1149

LYS 966 0.22 LYS 1085 -0.27 TRP 1030

LYS 966 0.24 ASP 1086 -0.28 TRP 1030

LYS 966 0.28 PHE 1087 -0.25 TRP 1030

GLN 964 0.27 THR 1088 -0.21 TRP 1030

GLN 964 0.31 ALA 1089 -0.19 TRP 1030

LYS 966 0.28 TYR 1090 -0.20 CYS 1149

GLN 964 0.30 ARG 1091 -0.24 LYS 1023

GLN 964 0.27 TRP 1092 -0.31 LYS 1023

GLN 964 0.26 ARG 1093 -0.31 LYS 1023

ARG 1104 0.26 LEU 1094 -0.34 MET 1021

PHE 990 0.26 SER 1095 -0.39 VAL 1105

GLY 965 0.24 HSD 1096 -0.35 VAL 1045

GLY 965 0.19 ARG 1097 -0.30 VAL 1045

GLY 965 0.19 PRO 1098 -0.26 TRP 1063

PRO 1152 0.25 LYS 1099 -0.22 TRP 1063

PRO 1152 0.30 THR 1100 -0.22 GLN 1038

GLY 965 0.23 GLY 1101 -0.25 HSD 1064

GLY 965 0.24 PHE 1102 -0.27 THR 1065

GLY 965 0.27 ILE 1103 -0.29 VAL 1045

LYS 966 0.28 ARG 1104 -0.32 HSD 1077

LYS 966 0.27 VAL 1105 -0.39 SER 1095

GLN 964 0.26 VAL 1106 -0.30 GLY 1042

LYS 966 0.26 MET 1107 -0.28 LYS 1023

GLN 964 0.26 TYR 1108 -0.22 GLN 1027

GLN 964 0.25 GLU 1109 -0.21 GLN 1027

GLN 964 0.23 GLY 1110 -0.19 TRP 1030

GLN 964 0.19 LYS 1111 -0.23 CYS 1149

GLN 964 0.21 LYS 1112 -0.18 GLN 1027

GLN 964 0.22 ILE 1113 -0.20 GLN 1027

ALA 1115 0.23 MET 1114 -0.23 ILE 1082

LYS 966 0.24 ALA 1115 -0.30 GLY 1042

LYS 966 0.24 ASP 1116 -0.26 GLY 1042

LYS 966 0.26 SER 1117 -0.33 ASP 1078

LYS 966 0.25 GLY 1118 -0.29 PRO 1079

LYS 966 0.26 PRO 1119 -0.28 HSD 1077

LYS 966 0.27 ILE 1120 -0.27 HSD 1077

GLY 965 0.25 TYR 1121 -0.25 GLY 1066

GLY 965 0.25 ASP 1122 -0.24 HSD 1064

GLY 965 0.25 LYS 1123 -0.19 HSD 1064

GLY 965 0.25 THR 1124 -0.17 HSD 1064

GLY 965 0.26 TYR 1125 -0.19 TRP 1063

GLY 965 0.23 ALA 1126 -0.18 TRP 1063

GLY 965 0.23 GLY 1127 -0.32 ASN 986

GLY 965 0.26 GLY 1128 -0.30 ASP 1151

GLY 965 0.28 ARG 1129 -0.33 PRO 976

GLY 965 0.31 LEU 1130 -0.47 PHE 1133

GLY 965 0.34 GLY 1131 -0.40 PHE 1133

LYS 966 0.36 LEU 1132 -0.44 PHE 1133

LYS 966 0.33 PHE 1133 -0.47 LEU 1130

LYS 966 0.27 VAL 1134 -0.40 LEU 1132

LYS 966 0.19 PHE 1135 -0.40 PHE 1007

CYS 974 0.19 SER 1136 -0.33 LEU 1132

ASP 1003 0.19 GLN 1137 -0.33 LEU 1132

LYS 966 0.15 GLU 1138 -0.29 TYR 1147

LYS 966 0.21 MET 1139 -0.22 ASP 1151

LYS 966 0.27 VAL 1140 -0.27 TYR 1147

LYS 966 0.40 PHE 1141 -0.21 ASP 1151

LYS 966 0.45 PHE 1142 -0.26 LEU 1145

LYS 966 0.44 SER 1143 -0.19 ASP 1151

GLN 964 0.40 ASP 1144 -0.23 ASP 1151

GLN 964 0.30 LEU 1145 -0.26 PHE 1142

PHE 939 0.26 LYS 1146 -0.30 ASP 1151

ASP 989 0.27 TYR 1147 -0.39 PHE 1133

GLN 964 0.12 GLU 1148 -0.42 CYS 1149

THR 1100 0.08 CYS 1149 -0.42 ASP 1151

GLN 964 0.09 ARG 1150 -0.33 MET 1021

THR 1100 0.18 ASP 1151 -0.42 CYS 1149

THR 1100 0.30 PRO 1152 -0.31 GLU 1148

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 21 ---

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

* *