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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 13 ---

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 0.18 THR 937 -0.24 LYS 1146

PRO 949 0.21 ASP 938 -0.26 ASP 1144

PRO 949 0.21 PHE 939 -0.35 ASP 1144

PRO 949 0.27 ARG 940 -0.53 GLY 965

GLN 943 0.31 ARG 941 -0.58 GLY 965

GLN 943 0.43 PHE 942 -0.45 GLN 964

PHE 942 0.43 GLN 943 -0.32 GLN 964

ILE 945 0.33 MET 944 -0.25 GLN 964

PHE 942 0.35 ILE 945 -0.14 GLN 964

MET 944 0.29 PRO 946 -0.14 SER 1014

PHE 942 0.25 LEU 947 -0.15 SER 1015

MET 944 0.26 ASP 948 -0.16 SER 1015

MET 944 0.32 PRO 949 -0.14 SER 1015

PHE 942 0.25 LYS 950 -0.15 LYS 1099

PHE 942 0.24 GLY 951 -0.16 THR 1124

PHE 942 0.25 THR 952 -0.13 SER 953

ASN 1033 0.18 SER 953 -0.14 THR 1124

TRP 959 0.20 GLN 954 -0.11 SER 1015

THR 952 0.23 ASN 955 -0.11 SER 1015

TRP 959 0.25 ASP 956 -0.12 SER 1015

ASP 956 0.23 PRO 957 -0.12 ILE 945

TRP 959 0.26 ASN 958 -0.14 ILE 945

ASN 958 0.26 TRP 959 -0.15 HSD 963

VAL 961 0.24 VAL 960 -0.20 HSD 963

VAL 960 0.24 VAL 961 -0.18 ASN 997

THR 952 0.23 ARG 962 -0.18 ASN 997

THR 937 0.15 HSD 963 -0.24 PHE 942

THR 952 0.14 GLN 964 -0.58 ARG 941

THR 952 0.12 GLY 965 -0.58 ARG 941

LYS 1111 0.17 LYS 966 -0.40 ARG 940

LYS 1111 0.22 GLU 967 -0.25 ARG 941

LEU 1145 0.23 LEU 968 -0.19 ARG 941

LYS 1111 0.26 VAL 969 -0.16 HSD 963

LYS 1111 0.23 GLN 970 -0.12 HSD 963

LYS 1111 0.27 THR 971 -0.11 ILE 945

LYS 1111 0.23 VAL 972 -0.10 ILE 945

LYS 1111 0.22 ASN 973 -0.08 SER 1015

ASP 1031 0.19 CYS 974 -0.10 SER 1015

PHE 942 0.19 ASP 975 -0.11 SER 1015

PHE 942 0.19 PRO 976 -0.11 SER 1015

PHE 942 0.20 GLY 977 -0.09 PRO 957

PHE 942 0.21 LEU 978 -0.15 GLN 964

PHE 942 0.18 ALA 979 -0.23 GLN 964

PRO 949 0.14 VAL 980 -0.25 GLN 964

PRO 949 0.16 GLY 981 -0.30 GLN 964

PRO 949 0.18 TYR 982 -0.36 GLN 964

ALA 1126 0.14 ASP 983 -0.24 GLN 964

ALA 1126 0.19 GLU 984 -0.21 GLN 964

LYS 1099 0.13 PHE 985 -0.22 GLY 1128

LYS 1099 0.19 ASN 986 -0.40 GLY 1127

SER 991 0.16 ALA 987 -0.26 GLY 1070

SER 991 0.22 VAL 988 -0.19 PRO 1069

ASP 1151 0.24 ASP 989 -0.18 TYR 1147

SER 991 0.31 PHE 990 -0.17 TYR 1147

PHE 990 0.31 SER 991 -0.17 PHE 939

PHE 1142 0.24 GLY 992 -0.24 PHE 939

LYS 1111 0.23 THR 993 -0.26 ARG 940

LYS 1111 0.28 PHE 994 -0.22 ARG 940

LYS 1111 0.45 PHE 995 -0.20 ARG 940

LYS 1111 0.40 ILE 996 -0.16 VAL 961

LYS 1111 0.46 ASN 997 -0.18 VAL 961

LYS 1111 0.40 THR 998 -0.14 HSD 963

LYS 1111 0.37 GLU 999 -0.14 HSD 963

LYS 1111 0.31 ARG 1000 -0.11 HSD 963

LYS 1111 0.26 ASP 1001 -0.09 HSD 963

LYS 1111 0.22 ASP 1002 -0.09 HSD 963

LYS 1111 0.18 ASP 1003 -0.08 HSD 963

LYS 1111 0.15 TYR 1004 -0.09 HSD 963

LYS 1111 0.17 ALA 1005 -0.11 HSD 963

GLY 1110 0.10 GLY 1006 -0.11 GLY 965

PHE 1133 0.12 PHE 1007 -0.13 GLN 964

ALA 1126 0.08 VAL 1008 -0.14 GLN 964

ALA 1126 0.12 PHE 1009 -0.14 GLN 964

ALA 1126 0.16 GLY 1010 -0.24 ASN 986

TYR 982 0.14 TYR 1011 -0.23 ASN 986

TYR 982 0.18 GLN 1012 -0.27 PRO 1152

TYR 982 0.18 SER 1013 -0.25 PRO 1152

TYR 982 0.18 SER 1014 -0.20 PRO 1152

TYR 982 0.15 SER 1015 -0.24 PRO 1152

TYR 982 0.13 ARG 1016 -0.28 PRO 1152

TYR 982 0.12 PHE 1017 -0.22 ASN 986

HSD 1077 0.08 TYR 1018 -0.17 ASN 986

ARG 1016 0.05 VAL 1019 -0.12 GLN 964

ALA 1126 0.08 VAL 1020 -0.11 GLN 964

GLY 1110 0.07 MET 1021 -0.10 GLY 965

GLY 1110 0.09 TRP 1022 -0.10 HSD 963

GLY 1110 0.11 LYS 1023 -0.10 HSD 963

LYS 1111 0.16 GLN 1024 -0.10 HSD 963

LYS 1111 0.12 VAL 1025 -0.09 HSD 963

PRO 1069 0.10 THR 1026 -0.09 LYS 1112

GLY 1110 0.09 GLN 1027 -0.09 PRO 1079

ARG 1036 0.11 SER 1028 -0.14 LEU 1075

ASP 1001 0.13 TYR 1029 -0.16 LEU 1075

ARG 1000 0.15 TRP 1030 -0.14 ARG 1073

CYS 974 0.19 ASP 1031 -0.19 ARG 1073

CYS 974 0.14 THR 1032 -0.24 ARG 1073

SER 953 0.18 ASN 1033 -0.24 ARG 1073

MET 944 0.15 PRO 1034 -0.28 THR 1124

MET 944 0.13 THR 1035 -0.28 ARG 1073

MET 944 0.11 ARG 1036 -0.28 ARG 1073

PRO 1069 0.09 ALA 1037 -0.24 LEU 1075

PRO 1069 0.12 GLN 1038 -0.19 TRP 1076

PRO 1069 0.11 GLY 1039 -0.13 TRP 1076

PRO 1069 0.10 TYR 1040 -0.14 LYS 1112

PRO 1069 0.08 SER 1041 -0.13 LYS 1112

ALA 1126 0.07 GLY 1042 -0.18 LYS 1112

ALA 1126 0.08 LEU 1043 -0.15 LYS 1112

VAL 1045 0.09 SER 1044 -0.14 ARG 1036

SER 1044 0.09 VAL 1045 -0.15 ARG 1036

ARG 1016 0.10 LYS 1046 -0.18 ARG 1036

ARG 1016 0.12 VAL 1047 -0.25 LYS 1099

ARG 1016 0.12 VAL 1048 -0.25 LYS 1099

ARG 1073 0.15 ASN 1049 -0.36 THR 1124

ASN 1067 0.14 SER 1050 -0.29 LYS 1099

ARG 941 0.13 THR 1051 -0.35 LYS 1099

PHE 942 0.17 THR 1052 -0.27 LYS 1099

PHE 942 0.18 GLY 1053 -0.24 PRO 1152

PHE 942 0.23 PRO 1054 -0.19 SER 1015

PHE 942 0.23 GLY 1055 -0.19 LYS 1099

PHE 942 0.21 GLU 1056 -0.20 LYS 1099

PHE 942 0.17 HSD 1057 -0.24 LYS 1099

PHE 942 0.17 LEU 1058 -0.23 LYS 1099

PHE 942 0.18 ARG 1059 -0.19 LYS 1099

PHE 942 0.13 ASN 1060 -0.22 ARG 1073

PHE 942 0.11 ALA 1061 -0.24 LYS 1099

PHE 942 0.10 LEU 1062 -0.18 LYS 1099

PHE 942 0.09 TRP 1063 -0.16 LYS 1099

PRO 1069 0.11 HSD 1064 -0.23 LEU 1075

GLY 1070 0.10 THR 1065 -0.21 TRP 1076

VAL 1072 0.13 GLY 1066 -0.26 LEU 1075

VAL 1072 0.15 ASN 1067 -0.29 ASP 1122

PRO 1069 0.14 THR 1068 -0.31 LYS 1099

THR 1068 0.14 PRO 1069 -0.42 LYS 1123

ASN 1067 0.14 GLY 1070 -0.43 THR 1124

ASN 1067 0.14 GLN 1071 -0.34 THR 1124

ASN 1067 0.15 VAL 1072 -0.31 LYS 1099

ASN 1049 0.15 ARG 1073 -0.31 THR 1068

HSD 1077 0.11 THR 1074 -0.33 LEU 1075

PRO 1079 0.11 LEU 1075 -0.33 THR 1074

PRO 1079 0.13 TRP 1076 -0.25 GLY 1066

THR 1074 0.11 HSD 1077 -0.19 LYS 1112

TRP 1076 0.13 ASP 1078 -0.23 LYS 1112

TRP 1076 0.13 PRO 1079 -0.23 LYS 1112

TRP 1076 0.10 ARG 1080 -0.24 LYS 1112

THR 1074 0.09 HSD 1081 -0.21 LYS 1112

SER 1117 0.11 ILE 1082 -0.21 LYS 1112

GLU 1109 0.10 GLY 1083 -0.11 LYS 1112

LYS 1111 0.23 TRP 1084 -0.14 ARG 940

LYS 1111 0.33 LYS 1085 -0.15 ARG 940

LYS 1111 0.42 ASP 1086 -0.15 ARG 940

LYS 1111 0.53 PHE 1087 -0.19 ARG 940

LYS 1111 0.62 THR 1088 -0.22 ARG 940

LYS 1111 0.60 ALA 1089 -0.26 ARG 940

LYS 1111 0.37 TYR 1090 -0.22 ARG 940

PRO 1152 0.22 ARG 1091 -0.21 ARG 940

ARG 1093 0.24 TRP 1092 -0.16 PHE 939

TRP 1092 0.24 ARG 1093 -0.16 THR 937

SER 1095 0.27 LEU 1094 -0.16 TYR 1147

LEU 1094 0.27 SER 1095 -0.18 PRO 1069

LEU 1094 0.15 HSD 1096 -0.23 PRO 1069

LEU 1094 0.16 ARG 1097 -0.29 PRO 1069

ASN 986 0.15 PRO 1098 -0.35 GLY 1070

ASN 986 0.19 LYS 1099 -0.41 PRO 1069

ILE 1113 0.14 THR 1100 -0.37 PRO 1069

GLY 1127 0.19 GLY 1101 -0.37 PRO 1069

MET 1114 0.13 PHE 1102 -0.30 PRO 1069

ALA 1126 0.14 ILE 1103 -0.23 PRO 1069

MET 1114 0.14 ARG 1104 -0.18 PRO 1069

ARG 1097 0.14 VAL 1105 -0.17 LYS 1111

PRO 1152 0.20 VAL 1106 -0.22 LYS 1111

PRO 1152 0.20 MET 1107 -0.15 ARG 940

PRO 1152 0.23 TYR 1108 -0.18 ARG 940

LYS 1111 0.35 GLU 1109 -0.22 ARG 940

LYS 1111 0.88 GLY 1110 -0.19 ARG 940

GLY 1110 0.88 LYS 1111 -0.33 ILE 1113

PRO 1152 0.25 LYS 1112 -0.40 ILE 1113

PRO 1152 0.25 ILE 1113 -0.40 LYS 1112

PRO 1152 0.20 MET 1114 -0.31 LYS 1112

MET 1114 0.16 ALA 1115 -0.23 LYS 1112

PRO 1152 0.16 ASP 1116 -0.27 LYS 1111

MET 1114 0.12 SER 1117 -0.21 LYS 1111

ASP 1116 0.15 GLY 1118 -0.25 LYS 1111

ASP 1116 0.15 PRO 1119 -0.20 PRO 1069

ALA 1126 0.13 ILE 1120 -0.25 PRO 1069

ILE 1120 0.13 TYR 1121 -0.34 PRO 1069

ALA 1126 0.14 ASP 1122 -0.40 PRO 1069

ALA 1126 0.26 LYS 1123 -0.42 PRO 1069

TYR 982 0.12 THR 1124 -0.43 GLY 1070

LYS 1123 0.21 TYR 1125 -0.35 PRO 1152

LYS 1123 0.26 ALA 1126 -0.46 PRO 1152

ALA 1126 0.25 GLY 1127 -0.40 ASN 986

GLU 984 0.19 GLY 1128 -0.27 ASN 986

LYS 1123 0.14 ARG 1129 -0.20 PHE 985

ALA 1126 0.11 LEU 1130 -0.17 GLN 964

LEU 978 0.11 GLY 1131 -0.18 GLN 964

PRO 976 0.11 LEU 1132 -0.16 GLN 964

PHE 1007 0.12 PHE 1133 -0.12 GLN 964

LYS 1111 0.15 VAL 1134 -0.09 HSD 963

LYS 1111 0.15 PHE 1135 -0.07 SER 1015

LYS 1111 0.18 SER 1136 -0.07 ASN 955

LYS 1111 0.23 GLN 1137 -0.08 HSD 963

LYS 1111 0.28 GLU 1138 -0.10 HSD 963

LYS 1111 0.32 MET 1139 -0.14 HSD 963

LYS 1111 0.31 VAL 1140 -0.14 HSD 963

LYS 1111 0.32 PHE 1141 -0.18 ARG 941

GLY 992 0.24 PHE 1142 -0.20 ARG 940

VAL 969 0.23 SER 1143 -0.36 ARG 940

TYR 1147 0.23 ASP 1144 -0.39 ARG 940

LEU 968 0.23 LEU 1145 -0.29 PHE 939

TYR 1147 0.35 LYS 1146 -0.24 THR 937

LYS 1146 0.35 TYR 1147 -0.18 ASP 989

CYS 1149 0.32 GLU 1148 -0.15 SER 1095

GLU 1148 0.32 CYS 1149 -0.17 PRO 1069

ASP 1151 0.33 ARG 1150 -0.22 PRO 1069

ARG 1150 0.33 ASP 1151 -0.36 ALA 1126

ILE 1113 0.25 PRO 1152 -0.46 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 2405021543434120385

--- normal mode 13 ---

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

* *