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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 18 ---

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
ASP 1144 0.47 THR 937 -0.27 PHE 985

GLN 964 0.51 ASP 938 -0.29 PHE 985

SER 1143 0.55 PHE 939 -0.19 GLY 1128

GLN 964 0.74 ARG 940 -0.21 GLY 1128

GLN 964 0.45 ARG 941 -0.21 GLY 1128

ASP 1151 0.30 PHE 942 -0.19 GLN 943

ASP 1151 0.28 GLN 943 -0.20 ARG 941

ASP 1151 0.23 MET 944 -0.22 ASP 956

ASP 1151 0.20 ILE 945 -0.21 ASP 956

ASP 1151 0.17 PRO 946 -0.24 ASP 956

ASP 1151 0.12 LEU 947 -0.16 SER 1014

PRO 957 0.12 ASP 948 -0.17 THR 952

PRO 957 0.16 PRO 949 -0.22 THR 952

PRO 957 0.14 LYS 950 -0.19 SER 1015

ASN 955 0.13 GLY 951 -0.16 ARG 1000

ASN 1033 0.17 THR 952 -0.22 PRO 946

ASN 1033 0.16 SER 953 -0.21 ARG 1000

ASN 1033 0.12 GLN 954 -0.22 ARG 1000

ASN 1033 0.14 ASN 955 -0.21 ARG 1000

LYS 950 0.14 ASP 956 -0.24 PRO 946

PRO 949 0.16 PRO 957 -0.21 MET 944

PRO 949 0.15 ASN 958 -0.21 MET 944

ASP 1151 0.15 TRP 959 -0.18 ARG 962

ARG 940 0.21 VAL 960 -0.21 ARG 962

HSD 963 0.33 VAL 961 -0.15 VAL 960

HSD 963 0.34 ARG 962 -0.21 VAL 960

GLU 967 0.39 HSD 963 -0.07 MET 944

ARG 940 0.74 GLN 964 -0.08 ARG 962

GLN 964 0.68 GLY 965 -0.17 ARG 962

GLU 967 0.60 LYS 966 -0.10 VAL 960

LYS 966 0.60 GLU 967 -0.08 VAL 960

ARG 940 0.47 LEU 968 -0.11 LYS 1111

ARG 940 0.35 VAL 969 -0.16 GLY 1110

ARG 940 0.22 GLN 970 -0.17 GLY 1110

ARG 940 0.19 THR 971 -0.15 GLY 1110

ASN 973 0.14 VAL 972 -0.15 ARG 1000

ARG 940 0.14 ASN 973 -0.24 ARG 1000

SER 1028 0.11 CYS 974 -0.20 PRO 946

ASP 1151 0.11 ASP 975 -0.19 ARG 1000

ASP 1151 0.12 PRO 976 -0.16 LYS 1111

ASP 1151 0.16 GLY 977 -0.18 CYS 974

ASP 1151 0.19 LEU 978 -0.17 LYS 1111

ASP 1151 0.23 ALA 979 -0.16 LYS 1111

ASP 1151 0.29 VAL 980 -0.14 LYS 1111

ASP 1151 0.34 GLY 981 -0.19 GLY 1128

ASP 1151 0.45 TYR 982 -0.33 GLY 1128

ASP 1151 0.56 ASP 983 -0.30 GLY 1128

ASP 1151 0.63 GLU 984 -0.39 GLY 1128

ASP 1151 0.56 PHE 985 -0.29 ASP 938

GLY 1127 0.41 ASN 986 -0.22 ASP 938

ILE 1113 0.26 ALA 987 -0.19 THR 937

ARG 1093 0.29 VAL 988 -0.19 THR 937

ARG 1093 0.29 ASP 989 -0.17 PRO 1119

TRP 1092 0.30 PHE 990 -0.17 LYS 1111

TYR 1147 0.37 SER 991 -0.27 LYS 1111

THR 993 0.34 GLY 992 -0.25 LYS 1111

PHE 939 0.44 THR 993 -0.27 LYS 1111

ARG 940 0.41 PHE 994 -0.22 GLY 1110

LYS 966 0.50 PHE 995 -0.20 GLY 1110

LYS 966 0.45 ILE 996 -0.12 GLY 1110

LYS 966 0.56 ASN 997 -0.10 VAL 972

LYS 966 0.42 THR 998 -0.13 ASN 973

LYS 966 0.40 GLU 999 -0.20 ASP 1001

LYS 966 0.31 ARG 1000 -0.24 ASN 973

LYS 966 0.27 ASP 1001 -0.20 GLU 999

LYS 966 0.25 ASP 1002 -0.14 TYR 1029

LYS 966 0.21 ASP 1003 -0.14 LYS 1085

ARG 940 0.21 TYR 1004 -0.13 GLY 1110

ARG 940 0.24 ALA 1005 -0.18 LYS 1111

PHE 1007 0.23 GLY 1006 -0.24 LYS 1111

GLY 1006 0.23 PHE 1007 -0.23 LYS 1111

ASN 986 0.22 VAL 1008 -0.22 LYS 1111

ASN 986 0.28 PHE 1009 -0.18 LEU 1130

ASN 986 0.32 GLY 1010 -0.23 ARG 1129

ASP 1151 0.26 TYR 1011 -0.24 TYR 982

ASP 1151 0.29 GLN 1012 -0.31 TYR 982

ASP 1151 0.24 SER 1013 -0.24 TYR 982

ASP 1151 0.19 SER 1014 -0.21 PRO 949

ASP 1151 0.15 SER 1015 -0.30 GLY 1053

ASP 1151 0.14 ARG 1016 -0.23 THR 1124

ASN 986 0.20 PHE 1017 -0.19 TYR 982

ASN 986 0.19 TYR 1018 -0.20 LYS 1111

ASN 986 0.21 VAL 1019 -0.23 LYS 1111

ASN 986 0.22 VAL 1020 -0.27 LYS 1111

ASN 986 0.22 MET 1021 -0.22 LYS 1111

ASN 986 0.22 TRP 1022 -0.17 LYS 1111

LYS 966 0.21 LYS 1023 -0.13 TRP 1063

LYS 966 0.25 GLN 1024 -0.17 LYS 1085

SER 1117 0.22 VAL 1025 -0.14 LYS 1085

PRO 1119 0.21 THR 1026 -0.15 GLN 1038

TRP 1076 0.18 GLN 1027 -0.13 LYS 1085

TRP 1076 0.17 SER 1028 -0.17 ARG 1036

THR 1074 0.13 TYR 1029 -0.16 ARG 1000

GLY 1066 0.11 TRP 1030 -0.18 ARG 1000

ASN 1067 0.11 ASP 1031 -0.16 ARG 1000

ASN 1067 0.14 THR 1032 -0.14 ARG 1000

THR 952 0.17 ASN 1033 -0.13 THR 1032

THR 952 0.16 PRO 1034 -0.17 ALA 1037

SER 953 0.12 THR 1035 -0.16 ALA 1037

ASN 1067 0.19 ARG 1036 -0.17 SER 1028

GLY 1066 0.16 ALA 1037 -0.17 PRO 1034

LEU 1075 0.19 GLN 1038 -0.15 THR 1026

TRP 1076 0.20 GLY 1039 -0.20 HSD 1064

TRP 1076 0.24 TYR 1040 -0.17 PRO 1069

PRO 1119 0.23 SER 1041 -0.19 HSD 1064

SER 1117 0.30 GLY 1042 -0.19 ASN 1067

GLY 1042 0.25 LEU 1043 -0.22 LYS 1111

ASN 986 0.20 SER 1044 -0.23 LYS 1111

ASN 986 0.19 VAL 1045 -0.27 LYS 1111

ASN 986 0.17 LYS 1046 -0.23 LYS 1111

ASN 986 0.13 VAL 1047 -0.22 LYS 1111

ASN 986 0.13 VAL 1048 -0.19 LYS 1111

ASN 986 0.08 ASN 1049 -0.28 THR 1124

GLY 1070 0.12 SER 1050 -0.20 THR 1124

GLY 1053 0.18 THR 1051 -0.28 THR 1124

GLY 1053 0.20 THR 1052 -0.24 THR 1124

THR 1052 0.20 GLY 1053 -0.30 SER 1015

THR 1052 0.16 PRO 1054 -0.25 GLY 1055

PRO 957 0.10 GLY 1055 -0.25 PRO 1054

ASP 956 0.12 GLU 1056 -0.15 SER 1015

PRO 1069 0.12 HSD 1057 -0.16 ALA 1037

PRO 1069 0.10 LEU 1058 -0.17 LYS 1111

PRO 957 0.10 ARG 1059 -0.16 LYS 1111

ASN 1067 0.10 ASN 1060 -0.15 LYS 1111

ASN 986 0.10 ALA 1061 -0.18 PRO 1079

ASN 986 0.13 LEU 1062 -0.19 LYS 1111

ASN 986 0.14 TRP 1063 -0.15 LYS 1111

THR 1074 0.16 HSD 1064 -0.20 GLY 1039

LEU 1075 0.20 THR 1065 -0.21 HSD 1081

ALA 1037 0.16 GLY 1066 -0.37 ASN 1067

ARG 1036 0.19 ASN 1067 -0.37 GLY 1066

ARG 1036 0.13 THR 1068 -0.27 PRO 1079

HSD 1057 0.12 PRO 1069 -0.29 PRO 1079

SER 1050 0.12 GLY 1070 -0.27 ARG 1073

GLN 964 0.09 GLN 1071 -0.19 PRO 1079

ASN 986 0.10 VAL 1072 -0.22 LYS 1111

HSD 1064 0.14 ARG 1073 -0.27 GLY 1070

GLN 1038 0.18 THR 1074 -0.23 LYS 1111

THR 1065 0.20 LEU 1075 -0.29 PRO 1152

HSD 1077 0.28 TRP 1076 -0.27 PRO 1152

TRP 1076 0.28 HSD 1077 -0.28 ASN 1067

PRO 1119 0.34 ASP 1078 -0.23 ASN 1067

PRO 1119 0.32 PRO 1079 -0.33 ASN 1067

PRO 1119 0.31 ARG 1080 -0.27 ASN 1067

PRO 1119 0.29 HSD 1081 -0.24 ASN 1067

SER 1117 0.28 ILE 1082 -0.19 ASN 1067

SER 1117 0.26 GLY 1083 -0.17 HSD 1064

LYS 966 0.29 TRP 1084 -0.12 HSD 1064

LYS 966 0.34 LYS 1085 -0.17 GLN 1024

LYS 966 0.42 ASP 1086 -0.14 ASP 1003

LYS 966 0.51 PHE 1087 -0.13 ASP 1003

LYS 966 0.44 THR 1088 -0.11 ASP 1003

ARG 940 0.40 ALA 1089 -0.20 PHE 995

ARG 1091 0.56 TYR 1090 -0.26 GLY 1110

TYR 1090 0.56 ARG 1091 -0.38 LYS 1111

CYS 1149 0.30 TRP 1092 -0.39 LYS 1111

CYS 1149 0.30 ARG 1093 -0.36 LYS 1111

VAL 988 0.28 LEU 1094 -0.28 LYS 1111

VAL 1106 0.35 SER 1095 -0.31 PRO 1152

VAL 1105 0.28 HSD 1096 -0.31 PRO 1152

ILE 1113 0.28 ARG 1097 -0.50 PRO 1152

VAL 1105 0.24 PRO 1098 -0.30 GLU 984

ILE 1113 0.26 LYS 1099 -0.38 PRO 1152

ILE 1113 0.28 THR 1100 -0.68 PRO 1152

ILE 1103 0.22 GLY 1101 -0.54 PRO 1152

ASP 1116 0.27 PHE 1102 -0.67 PRO 1152

GLY 1101 0.22 ILE 1103 -0.44 PRO 1152

ASP 1116 0.28 ARG 1104 -0.39 PRO 1152

SER 1095 0.32 VAL 1105 -0.35 LYS 1111

SER 1095 0.35 VAL 1106 -0.43 LYS 1111

SER 1095 0.31 MET 1107 -0.38 LYS 1111

CYS 1149 0.29 TYR 1108 -0.47 LYS 1111

CYS 1149 0.28 GLU 1109 -0.23 TYR 1090

LYS 1111 0.46 GLY 1110 -0.26 TYR 1090

GLY 1110 0.46 LYS 1111 -0.47 TYR 1108

CYS 1149 0.27 LYS 1112 -0.13 TYR 1090

SER 1095 0.32 ILE 1113 -0.32 LYS 1111

SER 1095 0.32 MET 1114 -0.16 ASN 1067

MET 1114 0.30 ALA 1115 -0.25 LYS 1111

PRO 1119 0.29 ASP 1116 -0.33 LYS 1111

ASP 1078 0.31 SER 1117 -0.32 PRO 1152

ARG 1080 0.30 GLY 1118 -0.48 PRO 1152

ASP 1078 0.34 PRO 1119 -0.67 PRO 1152

ASP 1078 0.28 ILE 1120 -0.54 PRO 1152

ASP 1078 0.26 TYR 1121 -0.59 PRO 1152

LYS 1123 0.22 ASP 1122 -0.40 PRO 1152

ASP 1122 0.22 LYS 1123 -0.32 PRO 1152

ASP 1078 0.09 THR 1124 -0.28 ASN 1049

ASN 986 0.14 TYR 1125 -0.27 GLU 984

VAL 1105 0.17 ALA 1126 -0.38 GLU 984

ASN 986 0.41 GLY 1127 -0.35 GLU 984

ASP 1151 0.39 GLY 1128 -0.39 GLU 984

ASP 1151 0.41 ARG 1129 -0.23 GLY 1128

ASP 1151 0.32 LEU 1130 -0.18 PHE 1009

ASP 1151 0.27 GLY 1131 -0.18 LYS 1111

ASP 1151 0.21 LEU 1132 -0.21 LYS 1111

ASP 1151 0.17 PHE 1133 -0.22 LYS 1111

ARG 940 0.16 VAL 1134 -0.18 LYS 1111

ARG 940 0.14 PHE 1135 -0.14 LYS 1111

ARG 940 0.15 SER 1136 -0.20 ARG 1000

LYS 966 0.20 GLN 1137 -0.12 GLY 977

LYS 966 0.22 GLU 1138 -0.13 GLY 1110

LYS 966 0.31 MET 1139 -0.15 GLY 1110

ARG 940 0.35 VAL 1140 -0.19 GLY 1110

ARG 940 0.45 PHE 1141 -0.20 GLY 1110

ARG 940 0.51 PHE 1142 -0.19 LYS 1111

ARG 940 0.61 SER 1143 -0.16 LYS 1111

ARG 940 0.52 ASP 1144 -0.16 LYS 1111

THR 993 0.41 LEU 1145 -0.13 LYS 1111

THR 937 0.36 LYS 1146 -0.13 PRO 1119

SER 991 0.37 TYR 1147 -0.12 PRO 1119

ASP 1151 0.36 GLU 1148 -0.15 PRO 1119

ASP 1151 0.43 CYS 1149 -0.17 ASN 986

ILE 1113 0.24 ARG 1150 -0.22 PRO 1119

GLU 984 0.63 ASP 1151 -0.45 THR 1100

GLU 984 0.53 PRO 1152 -0.68 THR 1100

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 18 ---

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

* *