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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 29 ---

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
CYS 1149 0.67 THR 937 -0.36 GLY 965

CYS 1149 0.47 ASP 938 -0.28 GLY 965

CYS 1149 0.35 PHE 939 -0.27 VAL 960

CYS 1149 0.33 ARG 940 -0.43 VAL 960

CYS 1149 0.25 ARG 941 -0.36 GLN 943

GLY 965 0.21 PHE 942 -0.48 GLN 943

HSD 963 0.13 GLN 943 -0.48 PHE 942

HSD 963 0.18 MET 944 -0.35 PHE 942

HSD 963 0.10 ILE 945 -0.36 SER 1117

HSD 963 0.09 PRO 946 -0.39 SER 1044

GLN 1137 0.12 LEU 947 -0.38 SER 1044

PRO 1054 0.10 ASP 948 -0.34 SER 1044

GLU 984 0.02 PRO 949 -0.33 SER 1044

GLU 984 0.05 LYS 950 -0.28 HSD 1077

GLU 984 0.05 GLY 951 -0.29 HSD 1077

GLY 951 0.00 THR 952 -0.30 LEU 1043

SER 1015 0.06 SER 953 -0.27 LEU 1043

SER 1015 0.07 GLN 954 -0.31 LEU 1043

SER 1015 0.00 ASN 955 -0.33 LEU 1043

GLN 964 0.02 ASP 956 -0.38 LEU 1043

HSD 963 0.08 PRO 957 -0.37 ALA 1115

HSD 963 0.08 ASN 958 -0.37 ARG 940

HSD 963 0.11 TRP 959 -0.41 ARG 940

VAL 961 0.13 VAL 960 -0.43 ARG 940

VAL 960 0.13 VAL 961 -0.37 ARG 940

MET 944 0.11 ARG 962 -0.37 ARG 940

MET 944 0.18 HSD 963 -0.35 ARG 940

PHE 942 0.19 GLN 964 -0.29 THR 937

PHE 942 0.21 GLY 965 -0.36 THR 937

PHE 942 0.17 LYS 966 -0.27 ASP 1144

LEU 1062 0.18 GLU 967 -0.23 SER 1143

ALA 979 0.18 LEU 968 -0.25 SER 1143

LEU 1062 0.18 VAL 969 -0.29 PHE 994

PRO 976 0.16 GLN 970 -0.32 ALA 1115

PRO 976 0.14 THR 971 -0.27 ALA 1115

PRO 976 0.13 VAL 972 -0.29 ALA 1115

PRO 976 0.14 ASN 973 -0.30 ALA 1115

ASP 975 0.13 CYS 974 -0.36 LEU 1043

CYS 974 0.13 ASP 975 -0.41 LEU 1043

GLN 1137 0.17 PRO 976 -0.48 MET 1021

GLN 970 0.14 GLY 977 -0.41 MET 1021

VAL 969 0.16 LEU 978 -0.41 PHE 1007

LEU 968 0.18 ALA 979 -0.37 PHE 1007

ASN 997 0.13 VAL 980 -0.34 VAL 1105

PHE 995 0.14 GLY 981 -0.24 LYS 1112

PHE 942 0.18 TYR 982 -0.23 LYS 1112

GLY 1070 0.19 ASP 983 -0.25 LYS 1112

GLN 1012 0.27 GLU 984 -0.32 PRO 1152

THR 937 0.25 PHE 985 -0.27 GLU 984

THR 937 0.27 ASN 986 -0.33 PRO 1152

THR 937 0.39 ALA 987 -0.24 LYS 1112

THR 937 0.47 VAL 988 -0.28 LYS 1112

THR 937 0.40 ASP 989 -0.33 LYS 1112

LYS 1146 0.32 PHE 990 -0.34 LYS 1112

SER 1095 0.34 SER 991 -0.34 LYS 1112

THR 993 0.39 GLY 992 -0.26 LYS 1112

GLY 992 0.39 THR 993 -0.30 PHE 1142

PHE 1007 0.34 PHE 994 -0.30 GLN 970

PHE 1007 0.34 PHE 995 -0.20 LYS 1111

PHE 1007 0.30 ILE 996 -0.16 VAL 972

LEU 1062 0.25 ASN 997 -0.10 LYS 1111

LEU 1062 0.25 THR 998 -0.07 THR 952

VAL 1025 0.32 GLU 999 -0.07 ASN 955

ASP 1001 0.45 ARG 1000 -0.08 ASN 955

ARG 1000 0.45 ASP 1001 -0.12 ALA 1115

ARG 1000 0.34 ASP 1002 -0.18 ASN 973

ARG 1000 0.36 ASP 1003 -0.38 LYS 1023

ALA 1005 0.35 TYR 1004 -0.40 TRP 1022

TYR 1004 0.35 ALA 1005 -0.39 ALA 1115

PHE 1007 0.48 GLY 1006 -0.44 ALA 1115

GLY 1006 0.48 PHE 1007 -0.41 LEU 978

GLY 1006 0.27 VAL 1008 -0.40 VAL 1105

TYR 1018 0.26 PHE 1009 -0.28 VAL 1105

PRO 1069 0.23 GLY 1010 -0.33 TYR 1011

GLN 1071 0.21 TYR 1011 -0.33 GLY 1010

GLU 984 0.27 GLN 1012 -0.27 PRO 1152

GLU 984 0.25 SER 1013 -0.21 SER 1117

GLU 984 0.19 SER 1014 -0.26 SER 1117

THR 1035 0.26 SER 1015 -0.20 ILE 1120

THR 1035 0.26 ARG 1016 -0.20 ASP 1122

LEU 1130 0.24 PHE 1017 -0.25 SER 1014

GLY 1006 0.31 TYR 1018 -0.30 ILE 1120

GLY 1006 0.35 VAL 1019 -0.37 PRO 946

MET 1021 0.35 VAL 1020 -0.40 SER 1117

VAL 1020 0.35 MET 1021 -0.48 PRO 976

THR 1074 0.27 TRP 1022 -0.44 PHE 1135

THR 1065 0.34 LYS 1023 -0.38 ASP 1003

THR 1065 0.28 GLN 1024 -0.23 CYS 974

GLU 999 0.32 VAL 1025 -0.16 GLN 954

ARG 1000 0.27 THR 1026 -0.16 ASP 975

ARG 1000 0.34 GLN 1027 -0.17 PRO 1079

ARG 1000 0.26 SER 1028 -0.15 PRO 1079

ARG 1000 0.24 TYR 1029 -0.21 GLY 1039

SER 1050 0.18 TRP 1030 -0.15 HSD 1077

SER 1050 0.18 ASP 1031 -0.16 HSD 1077

SER 1050 0.24 THR 1032 -0.10 SER 953

THR 1051 0.23 ASN 1033 -0.15 SER 953

THR 1051 0.30 PRO 1034 -0.11 HSD 1077

SER 1050 0.33 THR 1035 -0.09 GLY 951

GLN 1071 0.30 ARG 1036 -0.09 SER 953

GLN 1071 0.28 ALA 1037 -0.15 PRO 1079

ARG 1000 0.27 GLN 1038 -0.17 PRO 1079

ASN 1067 0.27 GLY 1039 -0.25 ASP 975

ASN 1067 0.26 TYR 1040 -0.24 ASP 975

THR 1065 0.26 SER 1041 -0.29 SER 1136

THR 1074 0.25 GLY 1042 -0.37 PHE 1135

LYS 1085 0.23 LEU 1043 -0.47 PRO 976

THR 1074 0.33 SER 1044 -0.48 PRO 976

TRP 1092 0.30 VAL 1045 -0.39 PRO 976

TRP 1092 0.27 LYS 1046 -0.38 LEU 947

LYS 1023 0.30 VAL 1047 -0.27 ILE 1120

VAL 1072 0.28 VAL 1048 -0.30 PRO 1054

GLN 1071 0.31 ASN 1049 -0.19 ASP 1122

THR 1035 0.33 SER 1050 -0.21 GLY 1053

THR 1035 0.32 THR 1051 -0.12 ILE 1120

PRO 1034 0.25 THR 1052 -0.16 LEU 1075

GLU 984 0.19 GLY 1053 -0.25 VAL 1048

GLU 984 0.14 PRO 1054 -0.33 LYS 1046

GLU 984 0.13 GLY 1055 -0.30 LYS 1046

GLU 984 0.13 GLU 1056 -0.28 HSD 1077

PRO 1034 0.23 HSD 1057 -0.26 THR 1068

SER 1015 0.25 LEU 1058 -0.29 TRP 1076

SER 1015 0.23 ARG 1059 -0.35 HSD 1077

SER 1050 0.25 ASN 1060 -0.30 HSD 1077

ALA 1037 0.28 ALA 1061 -0.25 TRP 1076

ALA 1005 0.30 LEU 1062 -0.38 HSD 1077

ARG 1000 0.28 TRP 1063 -0.35 HSD 1077

ARG 1000 0.28 HSD 1064 -0.30 THR 1065

LYS 1023 0.34 THR 1065 -0.30 HSD 1064

ASN 1067 0.43 GLY 1066 -0.24 ARG 1059

GLY 1066 0.43 ASN 1067 -0.21 GLY 1055

ASN 1049 0.27 THR 1068 -0.26 HSD 1057

ASN 1049 0.26 PRO 1069 -0.26 HSD 1057

THR 1035 0.31 GLY 1070 -0.14 GLY 1055

ASN 1049 0.31 GLN 1071 -0.20 GLY 1055

LYS 1023 0.29 VAL 1072 -0.39 ARG 1073

LYS 1023 0.29 ARG 1073 -0.39 VAL 1072

SER 1044 0.33 THR 1074 -0.30 LEU 1062

TRP 1092 0.25 LEU 1075 -0.33 LEU 947

TRP 1092 0.21 TRP 1076 -0.38 PRO 976

LYS 1085 0.16 HSD 1077 -0.43 PRO 976

LYS 1085 0.13 ASP 1078 -0.40 PRO 976

GLU 999 0.10 PRO 1079 -0.35 PRO 976

GLU 999 0.11 ARG 1080 -0.31 PRO 976

ASN 1067 0.16 HSD 1081 -0.30 PRO 976

ASN 1067 0.15 ILE 1082 -0.29 PHE 1135

THR 1074 0.27 GLY 1083 -0.24 CYS 974

THR 1074 0.27 TRP 1084 -0.23 GLN 1137

THR 1074 0.26 LYS 1085 -0.18 ASN 973

VAL 1020 0.26 ASP 1086 -0.12 ASN 973

VAL 1020 0.25 PHE 1087 -0.09 ASN 955

VAL 1020 0.26 THR 1088 -0.13 VAL 972

PRO 1152 0.26 ALA 1089 -0.18 LYS 1111

ARG 1091 0.36 TYR 1090 -0.27 VAL 1140

TYR 1090 0.36 ARG 1091 -0.32 LYS 1112

VAL 1045 0.30 TRP 1092 -0.42 LYS 1112

ARG 1104 0.31 ARG 1093 -0.37 LYS 1112

ILE 1103 0.31 LEU 1094 -0.33 LYS 1112

SER 991 0.34 SER 1095 -0.28 LYS 1112

THR 937 0.32 HSD 1096 -0.23 LYS 1112

THR 937 0.34 ARG 1097 -0.21 LYS 1112

THR 937 0.29 PRO 1098 -0.18 LYS 1112

THR 937 0.31 LYS 1099 -0.19 TYR 1125

THR 937 0.30 THR 1100 -0.16 PRO 949

THR 937 0.28 GLY 1101 -0.18 PRO 946

THR 937 0.29 PHE 1102 -0.21 PRO 946

LEU 1094 0.31 ILE 1103 -0.26 TYR 1018

ARG 1093 0.31 ARG 1104 -0.30 LEU 978

ARG 1104 0.24 VAL 1105 -0.40 VAL 1008

PRO 1152 0.20 VAL 1106 -0.38 LEU 1132

PRO 1152 0.21 MET 1107 -0.39 LEU 1132

GLU 1109 0.32 TYR 1108 -0.35 LYS 1112

TYR 1108 0.32 GLU 1109 -0.21 PRO 957

PRO 1152 0.27 GLY 1110 -0.33 LYS 1111

PRO 1152 0.20 LYS 1111 -0.33 GLY 1110

LYS 1085 0.14 LYS 1112 -0.42 TRP 1092

LYS 1111 0.19 ILE 1113 -0.40 LYS 1112

PRO 1152 0.14 MET 1114 -0.34 VAL 1134

PRO 1152 0.14 ALA 1115 -0.44 GLY 1006

PRO 1152 0.15 ASP 1116 -0.42 PHE 1133

PRO 1152 0.16 SER 1117 -0.41 PRO 976

PRO 1152 0.22 GLY 1118 -0.34 PRO 976

PRO 1152 0.29 PRO 1119 -0.29 PRO 976

ARG 1093 0.23 ILE 1120 -0.30 TYR 1018

SER 991 0.25 TYR 1121 -0.24 LEU 947

LEU 1094 0.26 ASP 1122 -0.22 PRO 1054

THR 937 0.25 LYS 1123 -0.17 LYS 1099

PRO 1069 0.25 THR 1124 -0.17 ARG 1016

PRO 1069 0.26 TYR 1125 -0.24 PRO 1152

PRO 1069 0.22 ALA 1126 -0.36 PRO 1152

PRO 1069 0.23 GLY 1127 -0.34 PRO 1152

GLU 984 0.23 GLY 1128 -0.30 PRO 1152

PHE 1017 0.21 ARG 1129 -0.26 VAL 1105

PHE 1017 0.24 LEU 1130 -0.31 VAL 1105

LEU 1130 0.22 GLY 1131 -0.36 VAL 1105

PHE 1133 0.22 LEU 1132 -0.39 MET 1107

LEU 1132 0.22 PHE 1133 -0.43 ALA 1115

GLN 1137 0.21 VAL 1134 -0.44 LEU 1043

GLN 1137 0.29 PHE 1135 -0.45 LEU 1043

GLN 1137 0.25 SER 1136 -0.36 LEU 1043

PHE 1135 0.29 GLN 1137 -0.30 ALA 1115

SER 1136 0.20 GLU 1138 -0.26 ALA 1115

LEU 1062 0.22 MET 1139 -0.21 ALA 1115

LEU 1062 0.25 VAL 1140 -0.28 ALA 1115

LEU 1062 0.23 PHE 1141 -0.29 PHE 994

PHE 1007 0.24 PHE 1142 -0.30 ARG 1091

TYR 1018 0.23 SER 1143 -0.26 VAL 961

PRO 1152 0.27 ASP 1144 -0.27 LYS 966

ASP 1151 0.26 LEU 1145 -0.22 LYS 1112

ASP 1151 0.34 LYS 1146 -0.24 LYS 1112

THR 937 0.56 TYR 1147 -0.30 LYS 1112

THR 937 0.66 GLU 1148 -0.28 LYS 1112

THR 937 0.67 CYS 1149 -0.24 LYS 1112

ASP 1151 0.65 ARG 1150 -0.21 LYS 1112

ARG 1150 0.65 ASP 1151 -0.22 GLU 984

ARG 1150 0.45 PRO 1152 -0.36 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 29 ---

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

* *