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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 12 ---

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 1151 0.19 THR 937 -0.10 LYS 966

HSD 963 0.25 ASP 938 -0.12 ALA 1126

HSD 963 0.27 PHE 939 -0.14 LYS 966

HSD 963 0.38 ARG 940 -0.11 ALA 1126

HSD 963 0.41 ARG 941 -0.12 LYS 966

HSD 963 0.38 PHE 942 -0.13 GLN 1012

HSD 963 0.31 GLN 943 -0.19 SER 1013

ASP 956 0.35 MET 944 -0.19 SER 1013

PHE 985 0.30 ILE 945 -0.11 GLN 970

THR 952 0.32 PRO 946 -0.11 ASN 958

PHE 985 0.28 LEU 947 -0.10 PRO 1054

HSD 963 0.25 ASP 948 -0.14 CYS 974

PHE 985 0.29 PRO 949 -0.26 ASP 956

PHE 985 0.26 LYS 950 -0.21 ASN 955

HSD 963 0.28 GLY 951 -0.14 ARG 1000

HSD 963 0.34 THR 952 -0.21 SER 953

HSD 963 0.29 SER 953 -0.21 THR 952

HSD 963 0.32 GLN 954 -0.18 ARG 1000

HSD 963 0.35 ASN 955 -0.21 LYS 950

HSD 963 0.38 ASP 956 -0.26 PRO 949

HSD 963 0.36 PRO 957 -0.16 PRO 949

HSD 963 0.43 ASN 958 -0.13 PRO 949

HSD 963 0.43 TRP 959 -0.11 SER 1013

HSD 963 0.41 VAL 960 -0.11 SER 1013

VAL 960 0.24 VAL 961 -0.10 SER 1013

VAL 960 0.28 ARG 962 -0.08 GLU 967

ASN 958 0.43 HSD 963 -0.00 LYS 966

ASN 958 0.27 GLN 964 -0.11 LYS 966

THR 952 0.14 GLY 965 -0.12 SER 1013

THR 952 0.10 LYS 966 -0.17 SER 1143

GLY 1110 0.11 GLU 967 -0.10 SER 1013

HSD 963 0.21 LEU 968 -0.11 SER 1013

HSD 963 0.20 VAL 969 -0.11 SER 1013

HSD 963 0.28 GLN 970 -0.11 ILE 945

HSD 963 0.25 THR 971 -0.14 PRO 949

HSD 963 0.26 VAL 972 -0.17 PRO 949

HSD 963 0.25 ASN 973 -0.16 PRO 949

HSD 963 0.29 CYS 974 -0.21 PRO 949

HSD 963 0.29 ASP 975 -0.16 LYS 950

GLY 977 0.26 PRO 976 -0.12 PRO 949

PRO 976 0.26 GLY 977 -0.08 PRO 946

PHE 985 0.24 LEU 978 -0.10 SER 1013

HSD 963 0.27 ALA 979 -0.14 SER 1013

ASP 1151 0.28 VAL 980 -0.14 LYS 966

ASP 1151 0.29 GLY 981 -0.14 LYS 966

ASP 1151 0.36 TYR 982 -0.18 ALA 1126

ASP 1151 0.42 ASP 983 -0.18 ALA 1126

ASP 1151 0.49 GLU 984 -0.25 ALA 1126

ARG 1129 0.43 PHE 985 -0.10 PRO 1098

GLY 1127 0.43 ASN 986 -0.12 ARG 1104

SER 1013 0.27 ALA 987 -0.18 ARG 1104

SER 1013 0.20 VAL 988 -0.20 VAL 1105

LYS 1111 0.17 ASP 989 -0.25 LEU 1094

LYS 1111 0.21 PHE 990 -0.15 ARG 1093

LYS 1111 0.28 SER 991 -0.15 TYR 1147

LYS 1111 0.25 GLY 992 -0.11 LYS 966

LYS 1111 0.20 THR 993 -0.10 GLY 992

HSD 963 0.10 PHE 994 -0.08 ARG 1150

ILE 1082 0.07 PHE 995 -0.09 PRO 1152

ILE 1082 0.09 ILE 996 -0.10 LYS 950

ILE 1082 0.09 ASN 997 -0.11 LYS 950

ILE 1082 0.10 THR 998 -0.13 LYS 950

VAL 1025 0.12 GLU 999 -0.16 LYS 1111

VAL 1025 0.12 ARG 1000 -0.18 GLN 954

HSD 963 0.15 ASP 1001 -0.17 GLN 954

HSD 963 0.14 ASP 1002 -0.16 SER 953

HSD 963 0.17 ASP 1003 -0.13 SER 953

HSD 963 0.17 TYR 1004 -0.10 LYS 950

HSD 963 0.16 ALA 1005 -0.08 LYS 950

HSD 963 0.15 GLY 1006 -0.07 PHE 990

HSD 963 0.15 PHE 1007 -0.10 LYS 966

LYS 1111 0.15 VAL 1008 -0.11 LYS 966

LYS 1111 0.16 PHE 1009 -0.13 LEU 1130

ASN 986 0.30 GLY 1010 -0.15 TYR 982

ASN 986 0.36 TYR 1011 -0.13 LYS 966

ASN 986 0.43 GLN 1012 -0.13 PHE 942

ASN 986 0.42 SER 1013 -0.19 MET 944

ASN 986 0.33 SER 1014 -0.12 MET 944

ASN 986 0.29 SER 1015 -0.11 MET 944

ASN 986 0.31 ARG 1016 -0.13 GLN 943

ASN 986 0.27 PHE 1017 -0.11 LYS 966

ASN 986 0.15 TYR 1018 -0.09 LYS 966

HSD 963 0.13 VAL 1019 -0.08 LYS 966

HSD 963 0.13 VAL 1020 -0.11 PRO 1152

HSD 963 0.14 MET 1021 -0.11 SER 1095

HSD 963 0.13 TRP 1022 -0.15 PRO 1152

HSD 963 0.14 LYS 1023 -0.18 MET 1114

HSD 963 0.11 GLN 1024 -0.20 LYS 1112

HSD 963 0.13 VAL 1025 -0.23 LYS 1112

HSD 963 0.14 THR 1026 -0.23 GLN 1027

HSD 963 0.17 GLN 1027 -0.23 THR 1026

HSD 963 0.19 SER 1028 -0.17 MET 1114

HSD 963 0.21 TYR 1029 -0.18 GLY 1039

HSD 963 0.22 TRP 1030 -0.16 MET 1114

HSD 963 0.25 ASP 1031 -0.16 SER 1028

HSD 963 0.21 THR 1032 -0.18 TRP 1076

HSD 963 0.21 ASN 1033 -0.16 TRP 1076

HSD 963 0.20 PRO 1034 -0.15 TRP 1076

HSD 963 0.18 THR 1035 -0.17 TRP 1076

HSD 963 0.18 ARG 1036 -0.22 TRP 1076

HSD 963 0.17 ALA 1037 -0.21 TRP 1076

HSD 963 0.16 GLN 1038 -0.22 TRP 1076

HSD 963 0.16 GLY 1039 -0.18 TYR 1029

HSD 963 0.13 TYR 1040 -0.21 MET 1114

HSD 963 0.12 SER 1041 -0.22 MET 1114

HSD 963 0.10 GLY 1042 -0.26 MET 1114

HSD 963 0.11 LEU 1043 -0.23 PRO 1152

HSD 963 0.11 SER 1044 -0.21 PRO 1152

HSD 963 0.11 VAL 1045 -0.19 PRO 1152

HSD 963 0.11 LYS 1046 -0.11 SER 1095

LYS 1111 0.12 VAL 1047 -0.08 LYS 966

ASN 986 0.17 VAL 1048 -0.08 LYS 966

ASN 986 0.20 ASN 1049 -0.09 SER 1015

ASN 986 0.22 SER 1050 -0.09 PRO 946

ASN 986 0.24 THR 1051 -0.14 GLY 1053

ASN 986 0.26 THR 1052 -0.11 ASP 956

ASN 986 0.30 GLY 1053 -0.14 THR 1051

GLY 1055 0.31 PRO 1054 -0.12 PRO 957

PRO 1054 0.31 GLY 1055 -0.11 CYS 974

HSD 963 0.22 GLU 1056 -0.10 TRP 1076

HSD 963 0.18 HSD 1057 -0.10 TRP 1076

PHE 985 0.19 LEU 1058 -0.08 ARG 1073

HSD 963 0.22 ARG 1059 -0.09 TRP 1076

HSD 963 0.20 ASN 1060 -0.15 TRP 1076

HSD 963 0.16 ALA 1061 -0.13 LEU 1075

HSD 963 0.17 LEU 1062 -0.11 LEU 1075

HSD 963 0.18 TRP 1063 -0.15 TRP 1076

HSD 963 0.16 HSD 1064 -0.21 TRP 1076

HSD 963 0.14 THR 1065 -0.24 TRP 1076

ASN 1067 0.14 GLY 1066 -0.23 TRP 1076

GLY 1066 0.14 ASN 1067 -0.22 TYR 1121

HSD 963 0.13 THR 1068 -0.16 TYR 1121

HSD 963 0.11 PRO 1069 -0.16 TYR 1121

ASN 986 0.12 GLY 1070 -0.09 TYR 1121

ASN 986 0.15 GLN 1071 -0.09 TYR 1121

HSD 963 0.12 VAL 1072 -0.13 TYR 1121

HSD 963 0.10 ARG 1073 -0.17 TYR 1121

HSD 1077 0.11 THR 1074 -0.27 LEU 1075

LYS 1111 0.11 LEU 1075 -0.27 THR 1074

LYS 1111 0.09 TRP 1076 -0.27 PRO 1152

THR 1074 0.11 HSD 1077 -0.28 PRO 1152

LYS 1085 0.11 ASP 1078 -0.33 PRO 1152

LYS 1085 0.11 PRO 1079 -0.34 PRO 1152

LYS 1085 0.15 ARG 1080 -0.33 PRO 1152

GLY 1083 0.16 HSD 1081 -0.28 PRO 1152

GLY 1083 0.21 ILE 1082 -0.28 LYS 1112

ILE 1082 0.21 GLY 1083 -0.24 LYS 1112

ILE 1082 0.14 TRP 1084 -0.21 GLU 1109

ILE 1082 0.16 LYS 1085 -0.21 LYS 1111

ILE 1082 0.14 ASP 1086 -0.19 LYS 1111

ILE 1082 0.10 PHE 1087 -0.16 LYS 1111

ARG 1080 0.08 THR 1088 -0.19 LYS 1111

PRO 1119 0.07 ALA 1089 -0.15 PRO 1152

PRO 1119 0.08 TYR 1090 -0.19 ARG 1091

LYS 1111 0.28 ARG 1091 -0.19 PRO 1152

LYS 1111 0.28 TRP 1092 -0.21 PRO 1152

LYS 1111 0.33 ARG 1093 -0.27 PRO 1152

LYS 1111 0.25 LEU 1094 -0.25 PRO 1152

LYS 1111 0.24 SER 1095 -0.32 PRO 1152

LYS 1111 0.20 HSD 1096 -0.22 PRO 1152

LYS 1111 0.17 ARG 1097 -0.27 PRO 1152

ALA 1126 0.24 PRO 1098 -0.12 GLU 984

ALA 1126 0.23 LYS 1099 -0.15 PRO 1152

LYS 1111 0.19 THR 1100 -0.28 PRO 1152

LYS 1111 0.19 GLY 1101 -0.20 PRO 1152

LYS 1111 0.23 PHE 1102 -0.37 PRO 1152

LYS 1111 0.23 ILE 1103 -0.34 PRO 1152

LYS 1111 0.26 ARG 1104 -0.41 PRO 1152

LYS 1111 0.24 VAL 1105 -0.35 PRO 1152

LYS 1111 0.27 VAL 1106 -0.38 PRO 1152

LYS 1111 0.17 MET 1107 -0.29 PRO 1152

LYS 1111 0.19 TYR 1108 -0.28 PRO 1152

THR 993 0.08 GLU 1109 -0.24 PRO 1152

THR 993 0.15 GLY 1110 -0.33 LYS 1111

ARG 1093 0.33 LYS 1111 -0.33 GLY 1110

ARG 1091 0.12 LYS 1112 -0.29 PRO 1152

PRO 1119 0.09 ILE 1113 -0.37 PRO 1152

THR 1088 0.07 MET 1114 -0.34 PRO 1152

LYS 1085 0.08 ALA 1115 -0.36 PRO 1152

LYS 1111 0.16 ASP 1116 -0.43 PRO 1152

LYS 1111 0.17 SER 1117 -0.40 PRO 1152

LYS 1111 0.22 GLY 1118 -0.49 PRO 1152

LYS 1111 0.26 PRO 1119 -0.49 PRO 1152

LYS 1111 0.21 ILE 1120 -0.36 PRO 1152

LYS 1111 0.21 TYR 1121 -0.27 PRO 1152

LYS 1111 0.18 ASP 1122 -0.16 ASN 1067

LYS 1111 0.17 LYS 1123 -0.15 GLU 984

LYS 1111 0.15 THR 1124 -0.14 GLU 984

ASN 986 0.18 TYR 1125 -0.16 GLU 984

PRO 1098 0.24 ALA 1126 -0.26 GLY 1127

ASN 986 0.43 GLY 1127 -0.26 ALA 1126

ASN 986 0.43 GLY 1128 -0.22 GLU 984

PHE 985 0.43 ARG 1129 -0.15 ALA 1126

ASP 1151 0.21 LEU 1130 -0.13 PHE 1009

HSD 963 0.20 GLY 1131 -0.13 LYS 966

HSD 963 0.20 LEU 1132 -0.11 LYS 966

HSD 963 0.20 PHE 1133 -0.08 SER 1013

HSD 963 0.22 VAL 1134 -0.08 PRO 949

HSD 963 0.23 PHE 1135 -0.12 LYS 950

HSD 963 0.24 SER 1136 -0.15 LYS 950

HSD 963 0.20 GLN 1137 -0.15 PRO 949

HSD 963 0.20 GLU 1138 -0.15 PRO 949

HSD 963 0.14 MET 1139 -0.13 PRO 949

HSD 963 0.15 VAL 1140 -0.10 PRO 949

HSD 963 0.10 PHE 1141 -0.08 SER 1013

LYS 1111 0.13 PHE 1142 -0.11 LYS 966

LYS 1111 0.17 SER 1143 -0.17 LYS 966

LYS 1111 0.22 ASP 1144 -0.17 LYS 966

LYS 1111 0.21 LEU 1145 -0.17 LYS 966

LYS 1111 0.22 LYS 1146 -0.13 LYS 966

LYS 1111 0.16 TYR 1147 -0.15 SER 991

ILE 945 0.15 GLU 1148 -0.17 VAL 1106

GLU 984 0.28 CYS 1149 -0.22 ASP 1116

SER 1013 0.25 ARG 1150 -0.32 ASP 1116

GLU 984 0.49 ASP 1151 -0.38 GLY 1118

GLU 984 0.44 PRO 1152 -0.49 GLY 1118

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 12 ---

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

* *