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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 14 ---

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
SER 1013 0.25 THR 937 -0.62 LYS 1111

SER 1013 0.29 ASP 938 -0.54 LYS 1111

SER 1014 0.20 PHE 939 -0.54 LYS 1111

GLN 943 0.24 ARG 940 -0.75 LYS 966

GLN 943 0.34 ARG 941 -0.50 GLY 965

GLN 943 0.47 PHE 942 -0.35 LYS 1111

PHE 942 0.47 GLN 943 -0.27 LYS 1111

ILE 945 0.29 MET 944 -0.24 LYS 1111

PHE 942 0.33 ILE 945 -0.19 LYS 1111

PHE 942 0.24 PRO 946 -0.17 SER 1014

PHE 942 0.24 LEU 947 -0.16 LYS 1111

PHE 942 0.21 ASP 948 -0.14 LYS 1111

PHE 942 0.25 PRO 949 -0.13 LYS 1111

PHE 942 0.21 LYS 950 -0.12 LYS 1111

PHE 942 0.16 GLY 951 -0.11 LYS 1111

PHE 942 0.11 THR 952 -0.11 LYS 1111

PHE 942 0.08 SER 953 -0.10 LYS 1111

LYS 1112 0.05 GLN 954 -0.11 LYS 1111

MET 1114 0.06 ASN 955 -0.12 LYS 1111

PHE 942 0.07 ASP 956 -0.14 LYS 1111

PRO 949 0.07 PRO 957 -0.17 LYS 1111

PRO 949 0.08 ASN 958 -0.17 LYS 1111

PRO 949 0.12 TRP 959 -0.22 LYS 1111

PRO 949 0.10 VAL 960 -0.29 ARG 940

PRO 949 0.11 VAL 961 -0.40 ARG 940

PRO 949 0.12 ARG 962 -0.26 ARG 940

ASP 1144 0.20 HSD 963 -0.21 LYS 1111

ASP 1144 0.20 GLN 964 -0.34 ARG 941

ASP 1144 0.29 GLY 965 -0.62 ARG 940

GLU 967 0.16 LYS 966 -0.75 ARG 940

LYS 966 0.16 GLU 967 -0.62 ARG 940

PRO 949 0.10 LEU 968 -0.48 ARG 940

PRO 949 0.08 VAL 969 -0.36 ARG 940

ASN 958 0.07 GLN 970 -0.23 ARG 940

ALA 1115 0.08 THR 971 -0.23 ARG 940

GLU 1138 0.08 VAL 972 -0.16 ARG 940

ALA 1115 0.07 ASN 973 -0.14 ARG 940

MET 1114 0.06 CYS 974 -0.14 LYS 1111

PHE 942 0.08 ASP 975 -0.14 LYS 1111

PHE 942 0.12 PRO 976 -0.16 LYS 1111

PHE 942 0.15 GLY 977 -0.18 LYS 1111

PHE 942 0.19 LEU 978 -0.22 LYS 1111

PHE 942 0.18 ALA 979 -0.28 LYS 1111

PHE 939 0.19 VAL 980 -0.30 LYS 1111

SER 1014 0.25 GLY 981 -0.39 LYS 1111

SER 1013 0.43 TYR 982 -0.39 LYS 1111

SER 1013 0.35 ASP 983 -0.42 LYS 1111

GLN 1012 0.37 GLU 984 -0.36 LYS 1111

THR 1051 0.24 PHE 985 -0.35 LYS 1111

ALA 1126 0.26 ASN 986 -0.28 LYS 1111

PRO 1069 0.19 ALA 987 -0.29 LYS 1111

GLY 1070 0.14 VAL 988 -0.39 LYS 1111

PHE 1017 0.08 ASP 989 -0.46 LYS 1111

THR 1052 0.07 PHE 990 -0.51 LYS 1111

GLY 965 0.13 SER 991 -0.64 LYS 1111

GLY 965 0.17 GLY 992 -0.67 LYS 1111

GLY 965 0.15 THR 993 -0.62 LYS 1111

LYS 966 0.11 PHE 994 -0.41 LYS 1111

SER 1117 0.10 PHE 995 -0.32 ARG 940

ALA 1115 0.11 ILE 996 -0.28 ARG 940

ALA 1115 0.10 ASN 997 -0.33 ARG 940

SER 1117 0.11 THR 998 -0.27 ARG 940

ILE 1082 0.13 GLU 999 -0.24 ARG 940

ILE 1082 0.13 ARG 1000 -0.21 ARG 940

TYR 1121 0.10 ASP 1001 -0.18 ARG 940

TYR 1121 0.13 ASP 1002 -0.16 ARG 940

TYR 1121 0.11 ASP 1003 -0.13 GLY 1110

TYR 1121 0.10 TYR 1004 -0.17 LYS 1111

SER 1117 0.08 ALA 1005 -0.22 LYS 1111

MET 1114 0.08 GLY 1006 -0.26 LYS 1111

ASP 1144 0.08 PHE 1007 -0.29 LYS 1111

THR 937 0.10 VAL 1008 -0.26 LYS 1111

THR 937 0.12 PHE 1009 -0.28 LYS 1111

PHE 985 0.20 GLY 1010 -0.23 LYS 1111

ARG 1129 0.25 TYR 1011 -0.23 LYS 1111

GLU 984 0.37 GLN 1012 -0.20 ALA 1126

TYR 982 0.43 SER 1013 -0.19 LYS 1111

TYR 982 0.38 SER 1014 -0.17 LYS 1111

TYR 982 0.35 SER 1015 -0.16 LYS 1111

GLU 984 0.31 ARG 1016 -0.17 LYS 1111

GLU 984 0.24 PHE 1017 -0.18 LYS 1111

ASN 986 0.14 TYR 1018 -0.18 LYS 1111

TYR 982 0.11 VAL 1019 -0.19 LYS 1111

MET 1114 0.10 VAL 1020 -0.19 LYS 1111

TYR 1121 0.10 MET 1021 -0.18 LYS 1111

TYR 1121 0.13 TRP 1022 -0.15 LYS 1111

TYR 1121 0.16 LYS 1023 -0.14 GLY 1110

TYR 1121 0.16 GLN 1024 -0.15 ARG 940

TYR 1121 0.18 VAL 1025 -0.15 LYS 1085

TYR 1121 0.20 THR 1026 -0.13 GLY 1083

TYR 1121 0.18 GLN 1027 -0.13 LYS 1085

LYS 1123 0.18 SER 1028 -0.14 ARG 1036

LYS 1123 0.15 TYR 1029 -0.13 ASP 1001

LYS 1123 0.13 TRP 1030 -0.15 ASP 1001

LYS 1123 0.12 ASP 1031 -0.12 ASP 1001

LYS 1123 0.17 THR 1032 -0.11 SER 1028

TYR 982 0.16 ASN 1033 -0.10 LYS 1111

TYR 982 0.20 PRO 1034 -0.13 ALA 1037

ASN 1049 0.20 THR 1035 -0.15 ALA 1037

LYS 1123 0.22 ARG 1036 -0.14 SER 1028

LYS 1123 0.21 ALA 1037 -0.15 THR 1035

LYS 1123 0.22 GLN 1038 -0.13 GLY 1039

TYR 1121 0.20 GLY 1039 -0.13 ARG 1036

TYR 1121 0.22 TYR 1040 -0.12 SER 1041

TYR 1121 0.20 SER 1041 -0.13 ARG 1091

TYR 1121 0.21 GLY 1042 -0.14 ARG 1091

LYS 1112 0.19 LEU 1043 -0.12 ASN 1067

TYR 1121 0.20 SER 1044 -0.14 ASN 1067

TYR 1121 0.16 VAL 1045 -0.12 LYS 1111

PRO 1098 0.19 LYS 1046 -0.12 LYS 1111

PRO 1152 0.19 VAL 1047 -0.14 LYS 1111

GLU 984 0.22 VAL 1048 -0.14 LYS 1111

GLY 1070 0.28 ASN 1049 -0.14 LYS 1111

TYR 982 0.30 SER 1050 -0.15 GLY 1053

TYR 982 0.35 THR 1051 -0.18 ARG 1073

TYR 982 0.35 THR 1052 -0.14 ARG 1073

TYR 982 0.36 GLY 1053 -0.15 SER 1050

TYR 982 0.30 PRO 1054 -0.14 LYS 1111

TYR 982 0.26 GLY 1055 -0.12 LYS 1111

TYR 982 0.21 GLU 1056 -0.12 LYS 1111

TYR 982 0.23 HSD 1057 -0.12 LYS 1111

TYR 982 0.25 LEU 1058 -0.13 LYS 1111

TYR 982 0.19 ARG 1059 -0.13 LYS 1111

TYR 982 0.17 ASN 1060 -0.12 LYS 1111

TYR 982 0.18 ALA 1061 -0.12 LYS 1111

TYR 982 0.15 LEU 1062 -0.14 LYS 1111

LYS 1123 0.14 TRP 1063 -0.12 LYS 1111

ARG 1073 0.21 HSD 1064 -0.12 PRO 1079

LYS 1123 0.23 THR 1065 -0.12 PRO 1079

LYS 1123 0.28 GLY 1066 -0.15 THR 1068

LYS 1123 0.27 ASN 1067 -0.17 HSD 1077

LYS 1123 0.23 THR 1068 -0.15 GLY 1066

TYR 1125 0.27 PRO 1069 -0.15 PRO 1079

GLU 984 0.29 GLY 1070 -0.19 ARG 1073

ASN 1049 0.26 GLN 1071 -0.13 ARG 1073

VAL 1048 0.22 VAL 1072 -0.20 ARG 1073

LYS 1123 0.25 ARG 1073 -0.20 VAL 1072

LYS 1123 0.26 THR 1074 -0.15 GLY 1070

ASP 1122 0.25 LEU 1075 -0.15 THR 1051

HSD 1077 0.38 TRP 1076 -0.15 ASN 1067

TRP 1076 0.38 HSD 1077 -0.17 ASN 1067

TYR 1121 0.26 ASP 1078 -0.13 ASN 1067

TYR 1121 0.27 PRO 1079 -0.16 ASN 1067

LYS 1112 0.29 ARG 1080 -0.13 ASN 1067

LYS 1112 0.22 HSD 1081 -0.12 ARG 1091

LYS 1112 0.25 ILE 1082 -0.15 ARG 1091

LYS 1112 0.21 GLY 1083 -0.15 ARG 1091

LYS 1112 0.17 TRP 1084 -0.17 ARG 940

LYS 1112 0.18 LYS 1085 -0.20 ARG 940

SER 1117 0.13 ASP 1086 -0.23 ARG 940

SER 1117 0.12 PHE 1087 -0.29 ARG 940

SER 1117 0.13 THR 1088 -0.27 ARG 940

TYR 1108 0.11 ALA 1089 -0.38 LYS 1111

TYR 1108 0.15 TYR 1090 -0.44 LYS 1111

GLY 965 0.16 ARG 1091 -0.70 LYS 1111

GLY 965 0.13 TRP 1092 -0.49 LYS 1111

GLY 965 0.11 ARG 1093 -0.45 LYS 1111

GLY 965 0.08 LEU 1094 -0.32 LYS 1111

PRO 1152 0.09 SER 1095 -0.28 LYS 1111

PRO 1152 0.16 HSD 1096 -0.23 LYS 1111

PRO 1152 0.27 ARG 1097 -0.19 LYS 1111

PRO 1152 0.28 PRO 1098 -0.19 GLY 1127

ASP 1122 0.27 LYS 1099 -0.20 ASN 986

PRO 1152 0.26 THR 1100 -0.17 GLY 1127

PRO 1152 0.27 GLY 1101 -0.15 TYR 1125

PRO 1152 0.24 PHE 1102 -0.11 TYR 1125

PRO 1152 0.20 ILE 1103 -0.11 LYS 1111

MET 1114 0.18 ARG 1104 -0.09 LYS 1111

MET 1114 0.14 VAL 1105 -0.17 LYS 1111

MET 1114 0.15 VAL 1106 -0.14 LYS 1111

LYS 1112 0.14 MET 1107 -0.21 LYS 1111

TYR 1090 0.15 TYR 1108 -0.31 LYS 1111

GLY 1118 0.12 GLU 1109 -0.31 ARG 1091

ILE 1113 0.13 GLY 1110 -0.47 ASP 1144

ILE 1113 0.16 LYS 1111 -0.71 ASP 1144

ILE 1113 0.48 LYS 1112 -0.33 THR 937

LYS 1112 0.48 ILE 1113 -0.17 THR 937

ALA 1115 0.45 MET 1114 -0.13 ARG 1091

MET 1114 0.45 ALA 1115 -0.10 TYR 1147

LYS 1112 0.32 ASP 1116 -0.11 VAL 1106

LYS 1112 0.30 SER 1117 -0.12 ASN 1067

LYS 1112 0.30 GLY 1118 -0.11 GLY 1070

ASP 1116 0.25 PRO 1119 -0.09 THR 1051

HSD 1077 0.24 ILE 1120 -0.12 THR 1051

HSD 1077 0.30 TYR 1121 -0.11 TYR 1125

LYS 1099 0.27 ASP 1122 -0.12 THR 1124

GLY 1066 0.28 LYS 1123 -0.24 TYR 1125

PRO 1152 0.27 THR 1124 -0.16 ARG 1016

PRO 1069 0.27 TYR 1125 -0.24 LYS 1123

PRO 1152 0.30 ALA 1126 -0.21 TYR 1011

GLY 1070 0.25 GLY 1127 -0.23 LYS 1111

GLY 1070 0.27 GLY 1128 -0.30 ARG 1129

SER 1013 0.26 ARG 1129 -0.31 LYS 1111

THR 1051 0.16 LEU 1130 -0.35 LYS 1111

THR 937 0.12 GLY 1131 -0.32 LYS 1111

ASP 1144 0.11 LEU 1132 -0.31 LYS 1111

ASP 1144 0.08 PHE 1133 -0.24 LYS 1111

MET 1114 0.07 VAL 1134 -0.20 LYS 1111

MET 1114 0.06 PHE 1135 -0.17 LYS 1111

TYR 1121 0.06 SER 1136 -0.14 LYS 1111

SER 1117 0.08 GLN 1137 -0.16 ARG 940

ALA 1115 0.08 GLU 1138 -0.22 ARG 940

ALA 1115 0.09 MET 1139 -0.28 ARG 940

ALA 1115 0.09 VAL 1140 -0.28 ARG 940

PHE 994 0.11 PHE 1141 -0.37 ARG 940

LYS 966 0.11 PHE 1142 -0.40 LYS 1111

GLY 965 0.21 SER 1143 -0.52 LYS 1111

GLY 965 0.29 ASP 1144 -0.71 LYS 1111

GLY 965 0.17 LEU 1145 -0.67 LYS 1111

SER 1014 0.13 LYS 1146 -0.69 LYS 1111

SER 1013 0.15 TYR 1147 -0.62 LYS 1111

GLN 1012 0.17 GLU 1148 -0.57 LYS 1111

THR 1051 0.18 CYS 1149 -0.48 LYS 1111

ALA 1126 0.15 ARG 1150 -0.38 LYS 1111

ALA 1126 0.24 ASP 1151 -0.33 LYS 1111

ALA 1126 0.30 PRO 1152 -0.26 LYS 1111

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 14 ---

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

* *