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

* *

CA distance fluctuations for 240531115742101615

--- normal mode 31 ---

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
VAL 960 0.29 PHE 939 -0.16 GLY 965

VAL 960 0.58 ARG 940 -0.19 GLY 965

TRP 959 0.40 ARG 941 -0.22 GLY 965

TRP 959 0.35 PHE 942 -0.21 HSD 963

PRO 949 0.39 GLN 943 -0.20 HSD 963

PRO 949 0.38 MET 944 -0.21 HSD 963

PRO 949 0.32 ILE 945 -0.22 SER 953

PRO 949 0.32 PRO 946 -0.24 SER 953

ARG 940 0.22 LEU 947 -0.19 SER 953

ARG 940 0.22 ASP 948 -0.18 THR 1035

GLN 943 0.39 PRO 949 -0.33 PRO 1034

ARG 941 0.29 LYS 950 -0.43 ASP 1031

SER 953 0.22 GLY 951 -0.32 PRO 949

GLU 999 0.25 THR 952 -0.18 PRO 949

GLY 951 0.22 SER 953 -0.28 ASP 956

ARG 940 0.28 GLN 954 -0.26 LYS 950

ARG 940 0.32 ASN 955 -0.25 TRP 1030

ARG 940 0.35 ASP 956 -0.28 SER 953

ARG 940 0.37 PRO 957 -0.24 SER 953

ARG 940 0.46 ASN 958 -0.19 HSD 963

ARG 940 0.53 TRP 959 -0.22 SER 953

ARG 940 0.58 VAL 960 -0.25 HSD 963

ARG 940 0.35 VAL 961 -0.24 ALA 979

ARG 940 0.39 ARG 962 -0.28 LEU 968

THR 1088 0.17 HSD 963 -0.25 VAL 960

LYS 966 0.26 GLN 964 -0.19 ARG 941

MET 1114 0.23 GLY 965 -0.25 ARG 962

GLN 964 0.26 LYS 966 -0.19 ARG 962

SER 1143 0.24 GLU 967 -0.26 ARG 962

ARG 940 0.34 LEU 968 -0.28 ARG 962

ARG 940 0.37 VAL 969 -0.21 ARG 962

ARG 940 0.39 GLN 970 -0.17 THR 1035

ARG 940 0.35 THR 971 -0.18 GLY 1110

ARG 940 0.33 VAL 972 -0.22 TRP 1030

ARG 940 0.29 ASN 973 -0.25 TRP 1030

ARG 940 0.29 CYS 974 -0.21 TRP 1030

ARG 940 0.22 ASP 975 -0.22 LYS 950

ARG 940 0.19 PRO 976 -0.17 HSD 963

PHE 942 0.23 GLY 977 -0.22 SER 953

PHE 942 0.25 LEU 978 -0.19 SER 953

PHE 942 0.31 ALA 979 -0.24 VAL 961

ALA 1115 0.25 VAL 980 -0.18 VAL 961

PRO 949 0.25 GLY 981 -0.13 VAL 961

PRO 949 0.31 TYR 982 -0.15 PRO 1152

PRO 949 0.24 ASP 983 -0.16 PRO 1152

PRO 949 0.20 GLU 984 -0.23 PRO 1152

LYS 1112 0.17 PHE 985 -0.16 PRO 1152

LYS 1112 0.18 ASN 986 -0.25 PRO 1152

LYS 1112 0.21 ALA 987 -0.17 LYS 1111

LYS 1112 0.22 VAL 988 -0.19 GLY 1110

LYS 1112 0.24 ASP 989 -0.23 GLY 1110

ILE 1113 0.24 PHE 990 -0.24 GLY 1110

ILE 1113 0.28 SER 991 -0.27 GLY 1110

MET 1114 0.28 GLY 992 -0.30 THR 993

ILE 1082 0.24 THR 993 -0.30 GLY 992

ILE 1082 0.25 PHE 994 -0.24 GLY 1110

LEU 968 0.22 PHE 995 -0.31 GLY 1110

ARG 940 0.25 ILE 996 -0.31 LYS 1112

ARG 940 0.23 ASN 997 -0.40 LYS 1112

ARG 940 0.25 THR 998 -0.33 LYS 1112

ASN 973 0.29 GLU 999 -0.42 LYS 1112

THR 998 0.23 ARG 1000 -0.50 GLN 1027

ARG 940 0.20 ASP 1001 -0.41 ARG 1000

PHE 942 0.20 ASP 1002 -0.34 ARG 1000

PHE 942 0.19 ASP 1003 -0.26 ARG 1000

PHE 942 0.23 TYR 1004 -0.25 ASN 1060

PHE 942 0.27 ALA 1005 -0.25 ARG 1059

TRP 1022 0.29 GLY 1006 -0.22 ARG 1059

ALA 1115 0.27 PHE 1007 -0.19 ARG 1059

ALA 1115 0.25 VAL 1008 -0.16 THR 1035

ALA 1115 0.22 PHE 1009 -0.15 VAL 1008

LYS 1112 0.19 GLY 1010 -0.18 PRO 1152

ALA 1115 0.19 TYR 1011 -0.16 PRO 1152

THR 1051 0.17 GLN 1012 -0.17 PRO 1152

THR 1051 0.21 SER 1013 -0.12 THR 1035

THR 1052 0.19 SER 1014 -0.14 SER 953

SER 1013 0.18 SER 1015 -0.20 THR 1035

GLY 1070 0.14 ARG 1016 -0.16 LYS 1099

THR 1065 0.15 PHE 1017 -0.19 LYS 1099

VAL 1045 0.18 TYR 1018 -0.19 LYS 1099

TYR 1040 0.19 VAL 1019 -0.20 GLY 1006

VAL 1008 0.24 VAL 1020 -0.21 THR 1035

ALA 979 0.24 MET 1021 -0.23 ASN 1060

GLY 1006 0.29 TRP 1022 -0.27 TRP 1063

VAL 1134 0.26 LYS 1023 -0.26 TRP 1063

PHE 942 0.23 GLN 1024 -0.32 GLU 999

PHE 942 0.20 VAL 1025 -0.40 GLU 999

PHE 942 0.21 THR 1026 -0.35 ARG 1000

PHE 942 0.17 GLN 1027 -0.50 ARG 1000

GLY 1066 0.19 SER 1028 -0.44 ARG 1000

ARG 1036 0.28 TYR 1029 -0.40 ARG 1000

ARG 1036 0.22 TRP 1030 -0.41 LYS 950

THR 1035 0.09 ASP 1031 -0.43 LYS 950

ARG 940 0.05 THR 1032 -0.38 LYS 950

TRP 1030 0.07 ASN 1033 -0.38 LYS 950

TRP 1030 0.06 PRO 1034 -0.49 HSD 1057

TRP 1030 0.16 THR 1035 -0.49 HSD 1057

TYR 1029 0.28 ARG 1036 -0.44 ALA 1037

ASN 1067 0.12 ALA 1037 -0.44 ARG 1036

GLY 1066 0.21 GLN 1038 -0.38 ARG 1000

PHE 942 0.19 GLY 1039 -0.34 ARG 1000

PHE 942 0.22 TYR 1040 -0.27 GLN 1038

PHE 942 0.23 SER 1041 -0.29 GLN 1038

GLY 1006 0.28 GLY 1042 -0.29 HSD 1064

LEU 1132 0.27 LEU 1043 -0.26 ASN 1067

VAL 1008 0.22 SER 1044 -0.32 ASN 1067

TYR 1018 0.18 VAL 1045 -0.22 TYR 1090

TYR 1018 0.17 LYS 1046 -0.24 VAL 1072

THR 1065 0.17 VAL 1047 -0.23 LYS 1099

THR 1065 0.14 VAL 1048 -0.20 THR 1035

ARG 1016 0.12 ASN 1049 -0.21 LYS 1099

GLY 1070 0.21 SER 1050 -0.26 THR 1035

SER 1013 0.21 THR 1051 -0.33 THR 1035

GLN 943 0.22 THR 1052 -0.36 THR 1035

THR 1052 0.22 GLY 1053 -0.27 THR 1035

ARG 940 0.21 PRO 1054 -0.25 PRO 1034

ARG 940 0.20 GLY 1055 -0.33 PRO 1034

THR 952 0.22 GLU 1056 -0.44 THR 1035

ARG 940 0.14 HSD 1057 -0.49 THR 1035

ARG 940 0.13 LEU 1058 -0.34 THR 1035

THR 952 0.13 ARG 1059 -0.25 ALA 1005

THR 952 0.11 ASN 1060 -0.32 THR 1035

PHE 942 0.12 ALA 1061 -0.35 THR 1035

TRP 1063 0.20 LEU 1062 -0.24 THR 1035

LEU 1062 0.20 TRP 1063 -0.29 ARG 1000

GLN 1038 0.17 HSD 1064 -0.31 PRO 1079

THR 1074 0.19 THR 1065 -0.37 PRO 1079

GLN 1038 0.21 GLY 1066 -0.44 PRO 1079

GLN 1038 0.14 ASN 1067 -0.45 PRO 1079

SER 1014 0.12 THR 1068 -0.38 PRO 1079

SER 1050 0.15 PRO 1069 -0.39 PRO 1079

SER 1050 0.21 GLY 1070 -0.29 PRO 1079

SER 1014 0.17 GLN 1071 -0.31 THR 1035

SER 1014 0.14 VAL 1072 -0.26 LEU 1075

GLN 1038 0.17 ARG 1073 -0.30 PRO 1069

THR 1065 0.19 THR 1074 -0.34 ASN 1067

LYS 1112 0.18 LEU 1075 -0.34 ASN 1067

LYS 1112 0.22 TRP 1076 -0.38 ASN 1067

LYS 1112 0.24 HSD 1077 -0.43 ASN 1067

LYS 1112 0.32 ASP 1078 -0.34 ASN 1067

LYS 1112 0.41 PRO 1079 -0.45 ASN 1067

LYS 1112 0.42 ARG 1080 -0.35 ASN 1067

GLU 1109 0.27 HSD 1081 -0.31 THR 1065

GLU 1109 0.34 ILE 1082 -0.26 GLN 1038

ILE 1082 0.26 GLY 1083 -0.26 GLU 999

PHE 942 0.24 TRP 1084 -0.26 GLU 999

ARG 940 0.22 LYS 1085 -0.44 LYS 1112

ARG 940 0.23 ASP 1086 -0.46 LYS 1112

ARG 940 0.20 PHE 1087 -0.54 LYS 1112

GLN 964 0.21 THR 1088 -0.64 LYS 1112

ILE 1082 0.21 ALA 1089 -0.39 LYS 1112

ILE 1082 0.24 TYR 1090 -0.27 ARG 1093

MET 1114 0.31 ARG 1091 -0.37 GLY 1110

MET 1107 0.49 TRP 1092 -0.33 ARG 1093

LYS 1112 0.28 ARG 1093 -0.33 TRP 1092

LYS 1112 0.29 LEU 1094 -0.27 TRP 1092

LYS 1112 0.29 SER 1095 -0.27 LYS 1111

LYS 1112 0.25 HSD 1096 -0.22 LYS 1111

LYS 1112 0.23 ARG 1097 -0.20 LYS 1111

LYS 1112 0.20 PRO 1098 -0.22 PRO 1152

LYS 1112 0.21 LYS 1099 -0.40 LYS 1123

LYS 1112 0.22 THR 1100 -0.20 PRO 1152

LYS 1112 0.21 GLY 1101 -0.28 LYS 1099

LYS 1112 0.24 PHE 1102 -0.23 LYS 1111

LYS 1112 0.25 ILE 1103 -0.24 LYS 1111

LYS 1112 0.31 ARG 1104 -0.27 LYS 1111

LYS 1112 0.32 VAL 1105 -0.27 LYS 1111

LYS 1112 0.42 VAL 1106 -0.34 LYS 1111

TRP 1092 0.49 MET 1107 -0.32 VAL 1106

MET 1114 0.30 TYR 1108 -0.27 THR 1088

ARG 1080 0.40 GLU 1109 -0.37 THR 1088

LYS 1111 1.07 GLY 1110 -0.37 ARG 1091

GLY 1110 1.07 LYS 1111 -0.34 VAL 1106

ILE 1113 0.72 LYS 1112 -0.64 THR 1088

LYS 1112 0.72 ILE 1113 -0.32 THR 1088

TRP 1092 0.42 MET 1114 -0.33 LYS 1085

LYS 1112 0.41 ALA 1115 -0.25 LYS 1085

LYS 1112 0.48 ASP 1116 -0.23 LYS 1111

LYS 1112 0.39 SER 1117 -0.25 ASN 1067

LYS 1112 0.43 GLY 1118 -0.22 ASN 1067

LYS 1112 0.33 PRO 1119 -0.24 LYS 1111

LYS 1112 0.27 ILE 1120 -0.22 PRO 1069

LYS 1112 0.23 TYR 1121 -0.21 PRO 1069

LYS 1112 0.19 ASP 1122 -0.30 LYS 1099

LYS 1112 0.18 LYS 1123 -0.40 LYS 1099

LYS 1112 0.15 THR 1124 -0.32 LYS 1099

LYS 1112 0.17 TYR 1125 -0.29 LYS 1099

LYS 1112 0.19 ALA 1126 -0.31 PRO 1152

LYS 1112 0.19 GLY 1127 -0.25 PRO 1152

LYS 1112 0.18 GLY 1128 -0.20 PRO 1152

ALA 1115 0.21 ARG 1129 -0.16 PRO 1152

ALA 1115 0.26 LEU 1130 -0.19 GLY 1131

ALA 1115 0.28 GLY 1131 -0.19 LEU 1130

ALA 1115 0.27 LEU 1132 -0.17 VAL 961

TRP 1022 0.26 PHE 1133 -0.18 ARG 1059

LYS 1023 0.26 VAL 1134 -0.20 ARG 1059

GLY 977 0.20 PHE 1135 -0.20 ARG 1059

ARG 940 0.21 SER 1136 -0.19 VAL 972

ARG 940 0.26 GLN 1137 -0.20 ASN 1060

ARG 940 0.29 GLU 1138 -0.19 TYR 1029

ARG 940 0.30 MET 1139 -0.25 LYS 1112

ARG 940 0.28 VAL 1140 -0.21 GLY 1110

ARG 940 0.28 PHE 1141 -0.22 GLY 1110

ILE 1082 0.24 PHE 1142 -0.18 GLY 1110

GLN 964 0.26 SER 1143 -0.18 GLY 1110

GLN 964 0.26 ASP 1144 -0.20 GLY 1110

MET 1114 0.25 LEU 1145 -0.21 GLY 1110

MET 1114 0.22 LYS 1146 -0.23 GLY 1110

ILE 1113 0.20 TYR 1147 -0.22 GLY 1110

LYS 1112 0.17 GLU 1148 -0.23 GLY 1110

LYS 1112 0.18 CYS 1149 -0.18 GLY 1110

ASP 1151 0.36 ARG 1150 -0.18 LYS 1111

ARG 1150 0.36 ASP 1151 -0.16 ALA 1126

ARG 1150 0.30 PRO 1152 -0.31 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 240531115742101615

--- normal mode 31 ---

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

* *