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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 10 ---

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 1111 0.62 THR 937 -0.20 GLU 967

LYS 1111 0.59 ASP 938 -0.18 GLU 967

LYS 1111 0.65 PHE 939 -0.21 LEU 968

LYS 1111 0.64 ARG 940 -0.23 VAL 960

LYS 1111 0.56 ARG 941 -0.17 VAL 960

LYS 1111 0.52 PHE 942 -0.14 TRP 959

LYS 1111 0.45 GLN 943 -0.12 ASP 1151

LYS 1111 0.42 MET 944 -0.11 PRO 957

LYS 1111 0.35 ILE 945 -0.08 ASP 956

LYS 1111 0.31 PRO 946 -0.06 ASP 956

LYS 1111 0.25 LEU 947 -0.08 MET 1114

LYS 1111 0.22 ASP 948 -0.08 MET 1114

LYS 1111 0.25 PRO 949 -0.06 MET 1114

LYS 1111 0.20 LYS 950 -0.07 MET 1114

LYS 1111 0.17 GLY 951 -0.08 MET 1114

LYS 1111 0.19 THR 952 -0.07 MET 1114

LYS 1111 0.16 SER 953 -0.08 LYS 1112

LYS 1111 0.20 GLN 954 -0.08 ARG 940

LYS 1111 0.25 ASN 955 -0.09 ARG 940

LYS 1111 0.29 ASP 956 -0.10 MET 944

LYS 1111 0.35 PRO 957 -0.11 ARG 940

LYS 1111 0.40 ASN 958 -0.15 ARG 940

LYS 1111 0.47 TRP 959 -0.19 ARG 940

LYS 1111 0.53 VAL 960 -0.23 ARG 940

LYS 1111 0.63 VAL 961 -0.22 ARG 940

LYS 1111 0.59 ARG 962 -0.16 ARG 940

LYS 1111 0.59 HSD 963 -0.07 ASP 1151

LYS 1111 0.63 GLN 964 -0.10 THR 998

LYS 1111 0.72 GLY 965 -0.09 ASP 1151

LYS 1111 0.78 LYS 966 -0.12 THR 937

LYS 1111 0.78 GLU 967 -0.20 THR 937

LYS 1111 0.66 LEU 968 -0.21 ARG 940

LYS 1111 0.57 VAL 969 -0.19 ARG 940

LYS 1111 0.46 GLN 970 -0.16 ARG 940

LYS 1111 0.41 THR 971 -0.16 ARG 940

LYS 1111 0.33 VAL 972 -0.13 ARG 940

LYS 1111 0.26 ASN 973 -0.11 ARG 940

LYS 1111 0.26 CYS 974 -0.10 ARG 940

LYS 1111 0.23 ASP 975 -0.08 MET 1114

LYS 1111 0.25 PRO 976 -0.09 MET 1114

LYS 1111 0.32 GLY 977 -0.06 MET 1114

LYS 1111 0.37 LEU 978 -0.07 PHE 985

LYS 1111 0.46 ALA 979 -0.10 ASN 958

LYS 1111 0.45 VAL 980 -0.11 ASP 1151

LYS 1111 0.49 GLY 981 -0.13 ASP 1151

LYS 1111 0.45 TYR 982 -0.15 ASP 1151

LYS 1111 0.42 ASP 983 -0.17 ASP 1151

LYS 1111 0.35 GLU 984 -0.17 ASP 1151

LYS 1111 0.30 PHE 985 -0.14 GLU 984

LYS 1111 0.23 ASN 986 -0.10 GLU 984

LYS 1111 0.20 ALA 987 -0.09 GLU 967

LYS 1111 0.28 VAL 988 -0.10 PHE 1142

LYS 1111 0.33 ASP 989 -0.10 LYS 1146

LYS 1111 0.45 PHE 990 -0.11 PHE 1142

LYS 1111 0.59 SER 991 -0.11 PHE 995

LYS 1111 0.73 GLY 992 -0.17 THR 993

LYS 1111 0.81 THR 993 -0.17 GLY 992

LYS 1111 0.62 PHE 994 -0.23 PHE 995

LYS 1111 0.55 PHE 995 -0.23 PHE 994

LYS 1111 0.39 ILE 996 -0.12 LEU 1145

LYS 1111 0.40 ASN 997 -0.14 LEU 1145

LYS 1111 0.28 THR 998 -0.12 ARG 940

LYS 1111 0.17 GLU 999 -0.10 THR 998

LYS 1111 0.17 ARG 1000 -0.11 ARG 940

GLY 1110 0.14 ASP 1001 -0.11 LYS 1112

GLY 1110 0.10 ASP 1002 -0.19 LYS 1112

GLY 1110 0.14 ASP 1003 -0.17 LYS 1112

LYS 1111 0.18 TYR 1004 -0.14 LYS 1112

LYS 1111 0.30 ALA 1005 -0.10 MET 1114

LYS 1111 0.32 GLY 1006 -0.12 MET 1114

LYS 1111 0.36 PHE 1007 -0.09 MET 1114

LYS 1111 0.30 VAL 1008 -0.09 MET 1114

LYS 1111 0.29 PHE 1009 -0.08 GLY 1131

LYS 1111 0.23 GLY 1010 -0.07 MET 1114

LYS 1111 0.28 TYR 1011 -0.08 ALA 1126

LYS 1111 0.25 GLN 1012 -0.08 ALA 1126

LYS 1111 0.25 SER 1013 -0.07 MET 1114

LYS 1111 0.24 SER 1014 -0.08 MET 1114

LYS 1111 0.18 SER 1015 -0.10 MET 1114

LYS 1111 0.18 ARG 1016 -0.10 MET 1114

LYS 1111 0.20 PHE 1017 -0.10 MET 1114

LYS 1111 0.16 TYR 1018 -0.13 MET 1114

LYS 1111 0.18 VAL 1019 -0.15 MET 1114

LYS 1111 0.16 VAL 1020 -0.19 MET 1114

LYS 1111 0.16 MET 1021 -0.20 MET 1114

GLY 1110 0.12 TRP 1022 -0.25 LYS 1112

TRP 1076 0.10 LYS 1023 -0.28 LYS 1112

TRP 1076 0.09 GLN 1024 -0.30 LYS 1112

TRP 1076 0.11 VAL 1025 -0.34 LYS 1112

LEU 1075 0.13 THR 1026 -0.36 LYS 1112

LEU 1075 0.11 GLN 1027 -0.29 LYS 1112

TYR 1121 0.11 SER 1028 -0.27 LYS 1112

ARG 1073 0.09 TYR 1029 -0.22 LYS 1112

TYR 1121 0.08 TRP 1030 -0.19 LYS 1112

GLY 1110 0.07 ASP 1031 -0.17 LYS 1112

LYS 1123 0.09 THR 1032 -0.20 LYS 1112

HSD 963 0.08 ASN 1033 -0.18 LYS 1112

HSD 963 0.09 PRO 1034 -0.18 LYS 1112

LYS 1123 0.10 THR 1035 -0.22 LYS 1112

LYS 1123 0.11 ARG 1036 -0.25 LYS 1112

ARG 1073 0.12 ALA 1037 -0.26 LYS 1112

TYR 1121 0.13 GLN 1038 -0.31 LYS 1112

LEU 1075 0.14 GLY 1039 -0.31 LYS 1112

LEU 1075 0.15 TYR 1040 -0.39 LYS 1112

TRP 1076 0.12 SER 1041 -0.41 LYS 1112

SER 1117 0.11 GLY 1042 -0.47 LYS 1112

SER 1117 0.09 LEU 1043 -0.40 LYS 1112

TYR 1121 0.11 SER 1044 -0.33 LYS 1112

PRO 1152 0.10 VAL 1045 -0.27 LYS 1112

PRO 1152 0.10 LYS 1046 -0.22 LYS 1112

HSD 963 0.09 VAL 1047 -0.18 LYS 1112

HSD 963 0.11 VAL 1048 -0.14 MET 1114

HSD 963 0.11 ASN 1049 -0.14 MET 1114

HSD 963 0.13 SER 1050 -0.13 MET 1114

HSD 963 0.13 THR 1051 -0.13 MET 1114

HSD 963 0.15 THR 1052 -0.11 MET 1114

LYS 1111 0.17 GLY 1053 -0.10 MET 1114

LYS 1111 0.20 PRO 1054 -0.10 MET 1114

LYS 1111 0.17 GLY 1055 -0.10 MET 1114

LYS 1111 0.13 GLU 1056 -0.12 MET 1114

HSD 963 0.12 HSD 1057 -0.15 LYS 1112

HSD 963 0.13 LEU 1058 -0.14 MET 1114

LYS 1111 0.13 ARG 1059 -0.13 MET 1114

HSD 963 0.10 ASN 1060 -0.19 LYS 1112

HSD 963 0.10 ALA 1061 -0.21 LYS 1112

HSD 963 0.10 LEU 1062 -0.19 LYS 1112

ARG 1073 0.09 TRP 1063 -0.22 LYS 1112

ARG 1073 0.14 HSD 1064 -0.28 LYS 1112

LEU 1075 0.15 THR 1065 -0.34 LYS 1112

ASP 1122 0.16 GLY 1066 -0.33 LYS 1112

LYS 1123 0.14 ASN 1067 -0.30 LYS 1112

LYS 1123 0.13 THR 1068 -0.25 LYS 1112

THR 1124 0.13 PRO 1069 -0.23 LYS 1112

HSD 963 0.11 GLY 1070 -0.19 LYS 1112

HSD 963 0.11 GLN 1071 -0.18 LYS 1112

THR 1124 0.10 VAL 1072 -0.21 LYS 1112

HSD 1064 0.14 ARG 1073 -0.24 LYS 1112

ASP 1122 0.14 THR 1074 -0.30 LYS 1112

THR 1065 0.15 LEU 1075 -0.29 LYS 1112

HSD 1077 0.21 TRP 1076 -0.37 LYS 1112

TRP 1076 0.21 HSD 1077 -0.44 LYS 1112

PRO 1119 0.16 ASP 1078 -0.57 LYS 1112

PRO 1119 0.20 PRO 1079 -0.53 LYS 1112

GLY 1118 0.15 ARG 1080 -0.62 LYS 1112

PRO 1119 0.13 HSD 1081 -0.54 LYS 1112

GLY 1083 0.15 ILE 1082 -0.60 LYS 1112

ILE 1082 0.15 GLY 1083 -0.43 LYS 1112

ILE 1082 0.10 TRP 1084 -0.29 LYS 1112

ALA 1115 0.12 LYS 1085 -0.16 LYS 1112

GLY 1110 0.18 ASP 1086 -0.09 GLY 992

LYS 1111 0.30 PHE 1087 -0.12 GLY 992

GLY 1110 0.35 THR 1088 -0.12 ALA 1089

GLY 1110 0.64 ALA 1089 -0.13 ARG 1091

GLY 1110 0.52 TYR 1090 -0.21 ARG 1091

LYS 1111 0.69 ARG 1091 -0.21 TYR 1090

LYS 1111 0.44 TRP 1092 -0.11 ARG 1093

LYS 1111 0.33 ARG 1093 -0.11 TRP 1092

LYS 1111 0.23 LEU 1094 -0.07 PHE 995

LYS 1111 0.16 SER 1095 -0.09 SER 991

LYS 1111 0.14 HSD 1096 -0.06 PHE 1142

PRO 1152 0.18 ARG 1097 -0.07 LYS 1146

PRO 1152 0.13 PRO 1098 -0.09 GLY 1127

PRO 1152 0.14 LYS 1099 -0.08 ARG 1129

PRO 1152 0.17 THR 1100 -0.09 LYS 1112

PRO 1152 0.15 GLY 1101 -0.11 LYS 1112

PRO 1152 0.18 PHE 1102 -0.12 LYS 1112

PRO 1152 0.16 ILE 1103 -0.14 LYS 1112

PRO 1152 0.15 ARG 1104 -0.18 LYS 1112

PRO 1152 0.11 VAL 1105 -0.15 LYS 1112

GLY 965 0.11 VAL 1106 -0.20 LYS 1112

GLY 965 0.13 MET 1107 -0.19 LYS 1112

ARG 1091 0.22 TYR 1108 -0.10 GLY 1042

TYR 1090 0.38 GLU 1109 -0.08 ILE 1082

THR 993 0.67 GLY 1110 -0.15 ILE 1113

ASP 1144 0.96 LYS 1111 -0.32 ARG 1080

ASP 1144 0.41 LYS 1112 -0.62 ARG 1080

LYS 966 0.19 ILE 1113 -0.56 LYS 1112

GLY 965 0.12 MET 1114 -0.54 LYS 1112

LYS 1085 0.12 ALA 1115 -0.58 LYS 1112

PRO 1152 0.13 ASP 1116 -0.44 LYS 1112

PRO 1079 0.16 SER 1117 -0.39 LYS 1112

PRO 1079 0.19 GLY 1118 -0.35 LYS 1112

PRO 1079 0.20 PRO 1119 -0.26 LYS 1112

HSD 1077 0.17 ILE 1120 -0.24 LYS 1112

HSD 1077 0.16 TYR 1121 -0.20 LYS 1112

GLY 1066 0.16 ASP 1122 -0.17 LYS 1112

GLY 1066 0.15 LYS 1123 -0.13 LYS 1112

PRO 1069 0.13 THR 1124 -0.12 LYS 1112

LYS 1111 0.11 TYR 1125 -0.10 LYS 1123

LYS 1111 0.13 ALA 1126 -0.10 GLY 1101

LYS 1111 0.21 GLY 1127 -0.09 PRO 1098

LYS 1111 0.27 GLY 1128 -0.11 ARG 1129

LYS 1111 0.35 ARG 1129 -0.12 PHE 985

LYS 1111 0.41 LEU 1130 -0.16 GLY 1131

LYS 1111 0.44 GLY 1131 -0.16 LEU 1130

LYS 1111 0.45 LEU 1132 -0.08 ASP 1151

LYS 1111 0.35 PHE 1133 -0.08 MET 1114

LYS 1111 0.33 VAL 1134 -0.07 MET 1114

LYS 1111 0.23 PHE 1135 -0.10 MET 1114

LYS 1111 0.21 SER 1136 -0.08 MET 1114

LYS 1111 0.26 GLN 1137 -0.10 ARG 940

LYS 1111 0.32 GLU 1138 -0.13 ARG 940

LYS 1111 0.41 MET 1139 -0.15 ARG 940

LYS 1111 0.46 VAL 1140 -0.13 PHE 939

LYS 1111 0.62 PHE 1141 -0.13 PHE 939

LYS 1111 0.70 PHE 1142 -0.17 LEU 1145

LYS 1111 0.87 SER 1143 -0.15 LEU 1145

LYS 1111 0.96 ASP 1144 -0.14 TYR 1147

LYS 1111 0.78 LEU 1145 -0.17 PHE 1142

LYS 1111 0.70 LYS 1146 -0.19 TYR 1147

LYS 1111 0.54 TYR 1147 -0.19 LYS 1146

LYS 1111 0.44 GLU 1148 -0.15 CYS 1149

LYS 1111 0.32 CYS 1149 -0.15 GLU 1148

LYS 1111 0.24 ARG 1150 -0.12 LYS 1146

LYS 1111 0.21 ASP 1151 -0.17 ASP 983

PHE 1102 0.18 PRO 1152 -0.16 ASP 983

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 10 ---

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

* *