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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 11 ---

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
GLY 965 0.30 THR 937 -0.10 SER 1095

GLN 964 0.23 ASP 938 -0.13 PRO 1152

GLY 965 0.27 PHE 939 -0.09 ASP 1144

GLN 964 0.23 ARG 940 -0.13 SER 1143

GLN 943 0.12 ARG 941 -0.14 PRO 1152

GLN 943 0.18 PHE 942 -0.15 PRO 1152

PHE 942 0.18 GLN 943 -0.18 PRO 1152

ILE 945 0.10 MET 944 -0.15 HSD 963

PHE 942 0.11 ILE 945 -0.15 PRO 1152

PHE 942 0.08 PRO 946 -0.12 PRO 1152

PHE 942 0.08 LEU 947 -0.11 PRO 1152

PHE 942 0.07 ASP 948 -0.11 PRO 1152

PHE 942 0.07 PRO 949 -0.13 PRO 1152

PHE 942 0.06 LYS 950 -0.12 PRO 1152

PHE 942 0.06 GLY 951 -0.11 GLY 1110

ARG 940 0.05 THR 952 -0.13 LYS 1111

PHE 942 0.05 SER 953 -0.15 LYS 1111

ASN 955 0.05 GLN 954 -0.18 LYS 1111

GLN 954 0.05 ASN 955 -0.18 LYS 1111

ARG 940 0.06 ASP 956 -0.14 LYS 1111

ARG 940 0.05 PRO 957 -0.15 LYS 1111

ARG 940 0.05 ASN 958 -0.18 LYS 1111

ARG 940 0.06 TRP 959 -0.17 LYS 1111

LEU 1145 0.08 VAL 960 -0.20 LYS 1111

LEU 1145 0.15 VAL 961 -0.18 LYS 1111

LEU 1145 0.15 ARG 962 -0.19 VAL 960

THR 937 0.18 HSD 963 -0.18 ASN 958

THR 937 0.30 GLN 964 -0.13 VAL 960

LEU 1145 0.32 GLY 965 -0.08 VAL 960

ASP 1144 0.32 LYS 966 -0.12 LYS 1111

LYS 966 0.20 GLU 967 -0.22 LYS 1111

LEU 1145 0.10 LEU 968 -0.18 LYS 1111

LEU 1145 0.06 VAL 969 -0.25 LYS 1111

PHE 990 0.05 GLN 970 -0.23 LYS 1111

PHE 990 0.05 THR 971 -0.28 LYS 1111

PHE 990 0.04 VAL 972 -0.26 LYS 1111

GLN 1027 0.04 ASN 973 -0.26 LYS 1111

SER 1028 0.05 CYS 974 -0.19 LYS 1111

PHE 942 0.04 ASP 975 -0.14 GLY 1110

PHE 942 0.05 PRO 976 -0.13 GLY 1110

PHE 942 0.06 GLY 977 -0.11 GLY 1110

PHE 942 0.07 LEU 978 -0.11 PHE 985

PHE 942 0.07 ALA 979 -0.11 PHE 985

LYS 1111 0.09 VAL 980 -0.15 PHE 985

LYS 1111 0.13 GLY 981 -0.16 PRO 1152

LYS 1111 0.16 TYR 982 -0.23 PRO 1152

LYS 1111 0.26 ASP 983 -0.26 ASP 1151

LYS 1111 0.33 GLU 984 -0.32 ASP 1151

LYS 1111 0.45 PHE 985 -0.28 ARG 1129

LYS 1111 0.54 ASN 986 -0.28 GLY 1127

LYS 1111 0.66 ALA 987 -0.14 ARG 1129

LYS 1111 0.65 VAL 988 -0.09 ARG 1129

LYS 1111 0.68 ASP 989 -0.16 SER 1095

LYS 1111 0.48 PHE 990 -0.12 ARG 1104

LYS 1111 0.36 SER 991 -0.12 VAL 1105

GLY 965 0.20 GLY 992 -0.07 VAL 1105

ARG 1150 0.19 THR 993 -0.12 LYS 1111

ARG 1150 0.14 PHE 994 -0.25 LYS 1111

ARG 1150 0.15 PHE 995 -0.45 LYS 1111

ARG 1150 0.12 ILE 996 -0.46 LYS 1111

ARG 1150 0.12 ASN 997 -0.53 LYS 1111

ARG 1150 0.11 THR 998 -0.50 LYS 1111

ARG 1150 0.12 GLU 999 -0.50 LYS 1111

ARG 1150 0.09 ARG 1000 -0.41 LYS 1111

ARG 1150 0.07 ASP 1001 -0.36 LYS 1111

ARG 1150 0.08 ASP 1002 -0.33 LYS 1111

ARG 1150 0.06 ASP 1003 -0.26 LYS 1111

SER 1095 0.06 TYR 1004 -0.21 GLU 1109

LYS 966 0.07 ALA 1005 -0.20 GLY 1110

LYS 966 0.09 GLY 1006 -0.13 GLU 1109

GLY 965 0.11 PHE 1007 -0.06 GLY 1110

LYS 1111 0.17 VAL 1008 -0.09 PHE 985

LYS 1111 0.29 PHE 1009 -0.10 PHE 985

LYS 1111 0.32 GLY 1010 -0.19 ASN 986

LYS 1111 0.23 TYR 1011 -0.21 ASN 986

LYS 1111 0.23 GLN 1012 -0.26 PRO 1152

LYS 1111 0.16 SER 1013 -0.24 PRO 1152

LYS 1111 0.10 SER 1014 -0.18 PRO 1152

LYS 1111 0.12 SER 1015 -0.17 PRO 1152

LYS 1111 0.19 ARG 1016 -0.18 PRO 1152

LYS 1111 0.21 PHE 1017 -0.16 ASN 986

LYS 1111 0.24 TYR 1018 -0.11 ASN 986

LYS 1111 0.15 VAL 1019 -0.08 ASN 986

LYS 1111 0.14 VAL 1020 -0.08 GLU 1109

SER 1095 0.08 MET 1021 -0.15 GLU 1109

PRO 1152 0.11 TRP 1022 -0.22 GLU 1109

PRO 1152 0.10 LYS 1023 -0.26 GLU 1109

PRO 1152 0.12 GLN 1024 -0.31 LYS 1111

PRO 1152 0.10 VAL 1025 -0.29 LYS 1111

PRO 1152 0.08 THR 1026 -0.22 GLU 1109

SER 1095 0.05 GLN 1027 -0.21 LYS 1111

CYS 974 0.05 SER 1028 -0.17 GLU 1109

GLN 1038 0.04 TYR 1029 -0.17 GLU 1109

PHE 942 0.03 TRP 1030 -0.18 LYS 1111

PHE 942 0.04 ASP 1031 -0.14 GLU 1109

PHE 942 0.04 THR 1032 -0.14 GLU 1109

PHE 942 0.04 ASN 1033 -0.12 GLU 1109

PHE 942 0.05 PRO 1034 -0.11 GLU 1109

PHE 942 0.04 THR 1035 -0.12 GLU 1109

PHE 942 0.04 ARG 1036 -0.13 GLU 1109

GLY 1118 0.04 ALA 1037 -0.14 GLU 1109

GLY 1118 0.04 GLN 1038 -0.17 GLU 1109

SER 1095 0.05 GLY 1039 -0.18 GLU 1109

PRO 1152 0.08 TYR 1040 -0.21 GLU 1109

PRO 1152 0.10 SER 1041 -0.25 GLU 1109

PRO 1152 0.14 GLY 1042 -0.25 GLU 1109

PRO 1152 0.14 LEU 1043 -0.20 GLU 1109

LYS 1111 0.10 SER 1044 -0.14 GLU 1109

LYS 1111 0.20 VAL 1045 -0.07 GLU 1109

LYS 1111 0.17 LYS 1046 -0.07 GLU 1109

LYS 1111 0.21 VAL 1047 -0.09 LYS 1099

LYS 1111 0.15 VAL 1048 -0.12 ASN 986

LYS 1111 0.16 ASN 1049 -0.14 PRO 1152

LYS 1111 0.11 SER 1050 -0.14 PRO 1152

LYS 1111 0.10 THR 1051 -0.16 PRO 1152

ARG 941 0.07 THR 1052 -0.15 PRO 1152

PHE 942 0.08 GLY 1053 -0.16 PRO 1152

PHE 942 0.08 PRO 1054 -0.14 PRO 1152

PHE 942 0.07 GLY 1055 -0.12 PRO 1152

PHE 942 0.06 GLU 1056 -0.10 GLU 1109

PHE 942 0.06 HSD 1057 -0.10 GLU 1109

PHE 942 0.06 LEU 1058 -0.10 ASN 986

PHE 942 0.06 ARG 1059 -0.12 GLU 1109

PHE 942 0.04 ASN 1060 -0.13 GLU 1109

PHE 942 0.04 ALA 1061 -0.12 GLU 1109

PHE 942 0.04 LEU 1062 -0.13 GLU 1109

LYS 966 0.04 TRP 1063 -0.15 GLU 1109

LYS 966 0.04 HSD 1064 -0.14 GLU 1109

GLY 965 0.04 THR 1065 -0.15 GLU 1109

LYS 1111 0.06 GLY 1066 -0.12 GLU 1109

LYS 1111 0.09 ASN 1067 -0.10 GLU 1109

LYS 1111 0.06 THR 1068 -0.10 GLU 1109

LYS 1111 0.08 PRO 1069 -0.09 LYS 1099

LYS 1111 0.10 GLY 1070 -0.11 LYS 1099

LYS 1111 0.09 GLN 1071 -0.10 LYS 1099

LYS 1111 0.11 VAL 1072 -0.09 LYS 1099

LYS 1111 0.15 ARG 1073 -0.08 LYS 1099

LYS 1111 0.15 THR 1074 -0.09 GLU 1109

LYS 1111 0.23 LEU 1075 -0.05 MET 1114

LYS 1111 0.21 TRP 1076 -0.08 GLU 1109

LYS 1111 0.11 HSD 1077 -0.13 GLU 1109

PRO 1152 0.16 ASP 1078 -0.16 GLU 1109

PRO 1152 0.15 PRO 1079 -0.14 GLU 1109

PRO 1152 0.17 ARG 1080 -0.18 GLU 1109

PRO 1152 0.14 HSD 1081 -0.21 GLU 1109

PRO 1152 0.18 ILE 1082 -0.28 GLU 1109

ILE 1082 0.17 GLY 1083 -0.31 GLU 1109

PRO 1152 0.17 TRP 1084 -0.40 GLU 1109

PRO 1152 0.20 LYS 1085 -0.51 LYS 1111

PRO 1152 0.16 ASP 1086 -0.57 LYS 1111

PRO 1152 0.17 PHE 1087 -0.68 LYS 1111

PRO 1152 0.21 THR 1088 -0.74 LYS 1111

PRO 1152 0.22 ALA 1089 -0.58 LYS 1111

PRO 1152 0.25 TYR 1090 -0.31 GLY 1110

ARG 1150 0.27 ARG 1091 -0.07 ILE 1113

ARG 1150 0.27 TRP 1092 -0.08 ASP 1116

LYS 1111 0.55 ARG 1093 -0.16 VAL 1105

LYS 1111 0.51 LEU 1094 -0.12 ARG 1104

LYS 1111 0.71 SER 1095 -0.16 ASP 989

LYS 1111 0.61 HSD 1096 -0.09 GLU 1148

LYS 1111 0.67 ARG 1097 -0.07 GLY 1010

LYS 1111 0.55 PRO 1098 -0.14 TYR 1125

LYS 1111 0.60 LYS 1099 -0.22 ALA 1126

LYS 1111 0.60 THR 1100 -0.09 LYS 1123

LYS 1111 0.51 GLY 1101 -0.07 THR 1100

LYS 1111 0.60 PHE 1102 -0.09 GLU 1148

LYS 1111 0.53 ILE 1103 -0.10 TYR 1147

LYS 1111 0.58 ARG 1104 -0.12 PHE 990

LYS 1111 0.45 VAL 1105 -0.16 ARG 1093

LYS 1111 0.49 VAL 1106 -0.12 ASP 1116

PRO 1152 0.30 MET 1107 -0.15 MET 1114

PRO 1152 0.37 TYR 1108 -0.11 ILE 1113

PRO 1152 0.35 GLU 1109 -0.40 TRP 1084

PRO 1152 0.43 GLY 1110 -0.54 LYS 1111

PRO 1152 0.88 LYS 1111 -0.74 THR 1088

PRO 1152 0.51 LYS 1112 -0.15 THR 1088

LYS 1112 0.42 ILE 1113 -0.11 TYR 1108

PRO 1152 0.27 MET 1114 -0.16 LEU 1043

PRO 1152 0.25 ALA 1115 -0.15 MET 1114

LYS 1111 0.40 ASP 1116 -0.12 VAL 1106

LYS 1111 0.38 SER 1117 -0.09 ARG 1093

LYS 1111 0.52 GLY 1118 -0.11 LYS 1146

LYS 1111 0.56 PRO 1119 -0.12 TYR 1147

LYS 1111 0.46 ILE 1120 -0.09 TYR 1147

LYS 1111 0.46 TYR 1121 -0.07 GLU 1148

LYS 1111 0.39 ASP 1122 -0.11 LYS 1099

LYS 1111 0.41 LYS 1123 -0.18 LYS 1099

LYS 1111 0.33 THR 1124 -0.17 LYS 1099

LYS 1111 0.36 TYR 1125 -0.18 PRO 1152

LYS 1111 0.42 ALA 1126 -0.27 PRO 1152

LYS 1111 0.41 GLY 1127 -0.28 ASN 986

LYS 1111 0.34 GLY 1128 -0.25 ASN 986

LYS 1111 0.26 ARG 1129 -0.28 PHE 985

LYS 1111 0.24 LEU 1130 -0.12 PHE 985

LYS 1111 0.12 GLY 1131 -0.11 PHE 985

GLY 965 0.10 LEU 1132 -0.08 GLY 1110

GLY 965 0.07 PHE 1133 -0.11 GLY 1110

LYS 966 0.05 VAL 1134 -0.16 GLY 1110

LYS 966 0.04 PHE 1135 -0.16 GLY 1110

SER 1028 0.04 SER 1136 -0.21 LYS 1111

PHE 990 0.05 GLN 1137 -0.27 LYS 1111

PHE 990 0.05 GLU 1138 -0.32 LYS 1111

ARG 1150 0.07 MET 1139 -0.36 LYS 1111

ARG 1150 0.08 VAL 1140 -0.32 LYS 1111

ARG 1150 0.09 PHE 1141 -0.32 LYS 1111

LYS 966 0.17 PHE 1142 -0.20 LYS 1111

LYS 966 0.29 SER 1143 -0.15 LYS 1111

LYS 966 0.32 ASP 1144 -0.12 ARG 940

GLY 965 0.32 LEU 1145 -0.09 ARG 1104

GLY 965 0.29 LYS 1146 -0.12 ARG 1104

LYS 1111 0.44 TYR 1147 -0.14 SER 1095

LYS 1111 0.59 GLU 1148 -0.14 SER 1095

LYS 1111 0.69 CYS 1149 -0.20 ASP 983

LYS 1111 0.85 ARG 1150 -0.16 GLU 984

LYS 1111 0.83 ASP 1151 -0.32 GLU 984

LYS 1111 0.88 PRO 1152 -0.32 GLU 984

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 11 ---

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

* *