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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 31 ---

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
GLN 964 0.37 THR 937 -0.56 GLU 1148

GLN 964 0.41 ASP 938 -0.45 CYS 1149

VAL 961 0.38 PHE 939 -0.29 VAL 988

VAL 961 0.63 ARG 940 -0.30 CYS 1149

VAL 960 0.24 ARG 941 -0.23 PHE 985

GLN 943 0.31 PHE 942 -0.25 GLY 965

PHE 942 0.31 GLN 943 -0.16 GLY 965

ILE 945 0.32 MET 944 -0.15 PHE 1135

MET 944 0.32 ILE 945 -0.14 GLU 984

ARG 940 0.27 PRO 946 -0.13 ASP 975

ARG 940 0.21 LEU 947 -0.16 GLU 984

ARG 940 0.20 ASP 948 -0.16 PRO 1069

ARG 940 0.24 PRO 949 -0.17 PRO 1069

ARG 940 0.20 LYS 950 -0.21 PRO 1069

ARG 940 0.20 GLY 951 -0.31 ASN 1033

ARG 940 0.27 THR 952 -0.50 ASN 1033

ARG 940 0.17 SER 953 -0.42 ASN 1033

ARG 940 0.18 GLN 954 -0.34 ASN 955

ARG 940 0.26 ASN 955 -0.34 GLN 954

ARG 940 0.29 ASP 956 -0.23 ASP 1031

ARG 940 0.33 PRO 957 -0.20 ASP 1031

ARG 940 0.44 ASN 958 -0.20 ASP 1031

ARG 940 0.53 TRP 959 -0.14 ASP 1031

ARG 940 0.61 VAL 960 -0.13 ASP 1031

ARG 940 0.63 VAL 961 -0.12 PHE 1087

ARG 940 0.58 ARG 962 -0.10 PHE 1087

ARG 940 0.41 HSD 963 -0.28 GLY 965

ARG 940 0.50 GLN 964 -0.14 PHE 1087

THR 937 0.32 GLY 965 -0.28 HSD 963

THR 937 0.23 LYS 966 -0.20 PHE 942

ARG 940 0.32 GLU 967 -0.17 PHE 995

ARG 940 0.47 LEU 968 -0.13 PHE 995

ARG 940 0.42 VAL 969 -0.14 ASP 1031

ARG 940 0.37 GLN 970 -0.17 ASP 1031

ARG 940 0.39 THR 971 -0.23 ASP 1031

ARG 940 0.32 VAL 972 -0.30 ASP 1031

ARG 1000 0.26 ASN 973 -0.33 ASP 1031

ARG 940 0.23 CYS 974 -0.29 ASP 1031

ARG 940 0.20 ASP 975 -0.23 ASP 1031

ARG 940 0.19 PRO 976 -0.19 GLY 977

ARG 940 0.25 GLY 977 -0.19 PRO 976

ARG 940 0.26 LEU 978 -0.20 PHE 1135

ARG 940 0.30 ALA 979 -0.19 PHE 1135

ARG 940 0.16 VAL 980 -0.20 PHE 1135

ASP 1151 0.14 GLY 981 -0.17 TYR 1004

ASP 1151 0.15 TYR 982 -0.23 PHE 985

ASP 1151 0.22 ASP 983 -0.34 PHE 985

ASP 1151 0.32 GLU 984 -0.40 GLY 1128

ASP 1151 0.38 PHE 985 -0.39 ASP 938

PRO 1079 0.25 ASN 986 -0.33 THR 937

PRO 1079 0.27 ALA 987 -0.42 THR 937

ASP 1151 0.28 VAL 988 -0.49 THR 937

CYS 1149 0.36 ASP 989 -0.40 THR 937

CYS 1149 0.25 PHE 990 -0.29 THR 937

CYS 1149 0.24 SER 991 -0.25 LYS 1112

PHE 1142 0.21 GLY 992 -0.27 LYS 1111

ARG 1091 0.23 THR 993 -0.28 LYS 1111

VAL 1020 0.24 PHE 994 -0.22 LYS 1111

ALA 1089 0.35 PHE 995 -0.19 PHE 1142

LYS 1112 0.24 ILE 996 -0.17 PHE 1141

ALA 1089 0.39 ASN 997 -0.17 GLU 999

LYS 1112 0.28 THR 998 -0.24 GLU 999

ASP 1001 0.31 GLU 999 -0.28 ARG 1080

VAL 972 0.28 ARG 1000 -0.63 ILE 1082

GLU 999 0.31 ASP 1001 -0.49 ARG 1000

GLU 999 0.29 ASP 1002 -0.57 ILE 1082

GLU 999 0.21 ASP 1003 -0.34 ARG 1080

LEU 1062 0.22 TYR 1004 -0.29 PHE 1007

LEU 1062 0.26 ALA 1005 -0.21 LEU 1132

VAL 1072 0.24 GLY 1006 -0.29 PHE 1007

PHE 1142 0.20 PHE 1007 -0.29 GLY 1006

LEU 1132 0.18 VAL 1008 -0.22 TYR 1004

ASP 1151 0.14 PHE 1009 -0.19 TYR 1004

PRO 1079 0.15 GLY 1010 -0.20 GLU 984

GLY 1131 0.12 TYR 1011 -0.22 GLU 984

PRO 1079 0.11 GLN 1012 -0.33 GLU 984

PHE 942 0.14 SER 1013 -0.27 GLU 984

MET 944 0.18 SER 1014 -0.20 GLU 984

PRO 1034 0.19 SER 1015 -0.19 GLU 984

LEU 1132 0.17 ARG 1016 -0.21 GLU 984

LEU 1132 0.17 PHE 1017 -0.21 GLU 984

LEU 1132 0.17 TYR 1018 -0.15 PRO 1152

PHE 994 0.20 VAL 1019 -0.17 GLY 1039

PHE 994 0.24 VAL 1020 -0.20 GLY 1039

VAL 1072 0.26 MET 1021 -0.19 PHE 1007

ASN 1067 0.28 TRP 1022 -0.38 LYS 1023

ASN 1067 0.30 LYS 1023 -0.38 TRP 1022

LYS 1085 0.32 GLN 1024 -0.55 ILE 1082

ASN 1067 0.26 VAL 1025 -0.61 ARG 1000

ASN 1067 0.29 THR 1026 -0.50 ARG 1080

ASN 1067 0.19 GLN 1027 -0.47 ARG 1080

ASN 1067 0.16 SER 1028 -0.35 ARG 1080

THR 1051 0.14 TYR 1029 -0.31 ARG 1080

THR 1051 0.14 TRP 1030 -0.34 ARG 1080

THR 1051 0.19 ASP 1031 -0.39 SER 953

THR 1051 0.28 THR 1032 -0.34 THR 952

THR 1051 0.31 ASN 1033 -0.50 THR 952

THR 1051 0.41 PRO 1034 -0.40 THR 952

THR 1051 0.35 THR 1035 -0.31 THR 952

GLY 1070 0.26 ARG 1036 -0.25 THR 952

GLY 1070 0.19 ALA 1037 -0.18 THR 952

ASN 1067 0.21 GLN 1038 -0.27 PRO 1079

ASN 1067 0.27 GLY 1039 -0.26 TYR 1029

ASN 1067 0.33 TYR 1040 -0.39 PRO 1079

GLY 1083 0.40 SER 1041 -0.50 ARG 1000

ASN 1067 0.34 GLY 1042 -0.39 ARG 1000

THR 1088 0.29 LEU 1043 -0.28 ARG 1000

PRO 1069 0.30 SER 1044 -0.19 ARG 1000

PRO 1069 0.28 VAL 1045 -0.16 PRO 1152

PRO 1069 0.32 LYS 1046 -0.19 PRO 1152

PRO 1069 0.28 VAL 1047 -0.20 PRO 1152

PRO 1034 0.22 VAL 1048 -0.17 PRO 1152

THR 1124 0.26 ASN 1049 -0.15 GLU 984

PRO 1034 0.35 SER 1050 -0.16 GLU 984

PRO 1034 0.41 THR 1051 -0.18 GLY 1053

PRO 1034 0.35 THR 1052 -0.21 PRO 1069

PRO 1034 0.23 GLY 1053 -0.18 THR 1051

ARG 940 0.18 PRO 1054 -0.18 PRO 1069

ARG 940 0.19 GLY 1055 -0.25 PRO 1069

ARG 940 0.15 GLU 1056 -0.24 PRO 1069

PRO 1034 0.32 HSD 1057 -0.32 PRO 1069

PRO 1034 0.19 LEU 1058 -0.21 PRO 1069

LYS 1085 0.17 ARG 1059 -0.15 GLU 984

LYS 1085 0.17 ASN 1060 -0.13 GLU 984

LYS 1085 0.23 ALA 1061 -0.13 GLU 984

ALA 1005 0.26 LEU 1062 -0.16 GLU 984

LYS 1085 0.24 TRP 1063 -0.18 ARG 1129

LYS 1085 0.26 HSD 1064 -0.15 PRO 1152

GLY 1083 0.35 THR 1065 -0.15 PRO 1152

ASN 1067 0.70 GLY 1066 -0.15 PRO 1152

GLY 1066 0.70 ASN 1067 -0.18 VAL 1072

ARG 1073 0.37 THR 1068 -0.20 HSD 1057

ARG 1073 0.58 PRO 1069 -0.32 HSD 1057

ARG 1073 0.41 GLY 1070 -0.15 GLY 1053

PRO 1034 0.34 GLN 1071 -0.14 ASN 1067

LYS 1046 0.29 VAL 1072 -0.18 ASN 1067

PRO 1069 0.58 ARG 1073 -0.21 PRO 1152

HSD 1077 0.43 THR 1074 -0.18 PRO 1152

PRO 1069 0.45 LEU 1075 -0.22 PRO 1152

PRO 1079 0.51 TRP 1076 -0.16 ARG 1000

TRP 1076 0.48 HSD 1077 -0.25 ARG 1000

TRP 1076 0.38 ASP 1078 -0.35 ARG 1000

PRO 1119 0.55 PRO 1079 -0.49 ARG 1000

PRO 1119 0.45 ARG 1080 -0.60 ARG 1000

ASN 1067 0.40 HSD 1081 -0.57 ARG 1000

ASN 1067 0.32 ILE 1082 -0.65 GLY 1083

SER 1041 0.40 GLY 1083 -0.65 ILE 1082

ASN 1067 0.31 TRP 1084 -0.43 ARG 1000

GLN 1024 0.32 LYS 1085 -0.35 ARG 1000

LYS 1112 0.26 ASP 1086 -0.23 ARG 1000

LYS 1112 0.37 PHE 1087 -0.15 GLU 967

LYS 1112 0.44 THR 1088 -0.19 LYS 1111

ASN 997 0.39 ALA 1089 -0.35 LYS 1111

GLU 1109 0.28 TYR 1090 -0.37 LYS 1111

THR 993 0.23 ARG 1091 -0.34 LYS 1111

CYS 1149 0.21 TRP 1092 -0.23 LYS 1023

CYS 1149 0.29 ARG 1093 -0.30 LYS 1112

CYS 1149 0.29 LEU 1094 -0.24 PHE 1102

ARG 1104 0.30 SER 1095 -0.33 THR 937

PRO 1079 0.29 HSD 1096 -0.35 THR 937

PRO 1079 0.33 ARG 1097 -0.60 PRO 1152

PRO 1079 0.30 PRO 1098 -0.56 PRO 1152

PRO 1079 0.30 LYS 1099 -0.84 PRO 1152

PRO 1079 0.38 THR 1100 -1.06 PRO 1152

PRO 1079 0.38 GLY 1101 -0.74 PRO 1152

PRO 1079 0.42 PHE 1102 -0.60 PRO 1152

PRO 1079 0.36 ILE 1103 -0.32 PRO 1152

PRO 1079 0.31 ARG 1104 -0.22 LYS 1112

CYS 1149 0.27 VAL 1105 -0.22 LYS 1023

CYS 1149 0.28 VAL 1106 -0.25 LYS 1023

TYR 1090 0.20 MET 1107 -0.25 GLN 1024

ASN 997 0.20 TYR 1108 -0.22 GLY 1083

PHE 995 0.30 GLU 1109 -0.38 LYS 1111

ASN 997 0.29 GLY 1110 -1.17 LYS 1111

ILE 1113 0.53 LYS 1111 -1.17 GLY 1110

THR 1088 0.44 LYS 1112 -0.30 ARG 1093

LYS 1111 0.53 ILE 1113 -0.20 ARG 1000

LYS 1112 0.23 MET 1114 -0.30 ARG 1000

LYS 1111 0.23 ALA 1115 -0.32 ARG 1000

ARG 1150 0.29 ASP 1116 -0.28 ARG 1000

ARG 1080 0.33 SER 1117 -0.21 ARG 1000

PRO 1079 0.42 GLY 1118 -0.19 ARG 1000

PRO 1079 0.55 PRO 1119 -0.33 PRO 1152

PRO 1079 0.55 ILE 1120 -0.37 PRO 1152

PRO 1079 0.52 TYR 1121 -0.59 PRO 1152

PRO 1069 0.47 ASP 1122 -0.52 PRO 1152

PRO 1069 0.41 LYS 1123 -0.62 PRO 1152

GLY 1070 0.35 THR 1124 -0.41 PRO 1152

PRO 1079 0.25 TYR 1125 -0.28 PRO 1152

PRO 1079 0.26 ALA 1126 -0.32 GLU 984

PRO 1079 0.19 GLY 1127 -0.30 GLU 984

ASP 1151 0.17 GLY 1128 -0.40 GLU 984

ASP 1151 0.20 ARG 1129 -0.21 PHE 1135

ASP 1151 0.20 LEU 1130 -0.23 PHE 1133

ARG 1016 0.15 GLY 1131 -0.22 PHE 1133

VAL 1019 0.20 LEU 1132 -0.24 TYR 1004

VAL 1072 0.17 PHE 1133 -0.23 LEU 1130

ARG 940 0.19 VAL 1134 -0.27 PHE 1135

GLN 1137 0.18 PHE 1135 -0.27 VAL 1134

GLU 999 0.19 SER 1136 -0.24 ARG 1080

PHE 1135 0.18 GLN 1137 -0.25 ARG 1080

ARG 940 0.29 GLU 1138 -0.26 ASP 1031

ARG 940 0.31 MET 1139 -0.23 ASP 1031

ARG 940 0.23 VAL 1140 -0.15 ASP 1031

GLU 1109 0.23 PHE 1141 -0.17 ILE 996

VAL 1020 0.21 PHE 1142 -0.19 PHE 995

GLU 967 0.25 SER 1143 -0.21 LYS 1111

GLU 967 0.25 ASP 1144 -0.28 LYS 1111

GLU 967 0.21 LEU 1145 -0.26 LYS 1111

ASP 1151 0.18 LYS 1146 -0.24 SER 1095

ASP 1151 0.23 TYR 1147 -0.47 THR 937

ASP 1151 0.32 GLU 1148 -0.56 THR 937

ASP 1151 0.52 CYS 1149 -0.53 THR 937

ASP 1116 0.29 ARG 1150 -0.44 THR 937

CYS 1149 0.52 ASP 1151 -0.62 THR 1100

CYS 1149 0.32 PRO 1152 -1.06 THR 1100

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 31 ---

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

* *