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

* *

CA distance fluctuations for 240531115742101615

--- normal mode 22 ---

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
TYR 1147 0.21 PHE 939 -0.35 ASP 983

TYR 1147 0.17 ARG 940 -0.31 PRO 1152

TYR 1147 0.22 ARG 941 -0.27 PRO 1152

TYR 1147 0.19 PHE 942 -0.29 SER 1013

TYR 1147 0.15 GLN 943 -0.32 SER 1013

ASP 975 0.18 MET 944 -0.29 THR 1052

ARG 1129 0.13 ILE 945 -0.29 THR 1052

ASP 975 0.13 PRO 946 -0.31 THR 1052

SER 1014 0.11 LEU 947 -0.30 ASP 1031

GLY 951 0.16 ASP 948 -0.34 ASN 1033

SER 1014 0.15 PRO 949 -0.36 ASN 1033

SER 1014 0.13 LYS 950 -0.41 THR 1032

TRP 1030 0.38 GLY 951 -0.29 PRO 949

TRP 1030 0.45 THR 952 -0.21 PRO 949

SER 1028 0.28 SER 953 -0.22 ASN 958

SER 1028 0.24 GLN 954 -0.35 LYS 950

CYS 974 0.17 ASN 955 -0.40 LYS 950

MET 944 0.11 ASP 956 -0.33 LYS 950

ASN 955 0.12 PRO 957 -0.27 ASP 1031

LEU 968 0.14 ASN 958 -0.25 THR 1052

LEU 1145 0.13 TRP 959 -0.24 THR 1052

LEU 968 0.16 VAL 960 -0.21 THR 1052

VAL 960 0.15 VAL 961 -0.25 PHE 1087

ASP 956 0.11 ARG 962 -0.38 PHE 1087

ASP 956 0.09 HSD 963 -0.37 PHE 1087

ASN 955 0.08 GLN 964 -0.26 PHE 1087

VAL 960 0.15 GLY 965 -0.28 ASP 983

VAL 960 0.16 LYS 966 -0.33 ASP 983

VAL 960 0.15 GLU 967 -0.25 ASP 983

VAL 960 0.16 LEU 968 -0.20 PHE 1141

SER 1143 0.16 VAL 969 -0.26 ARG 962

GLY 992 0.12 GLN 970 -0.21 ASP 1031

GLN 1027 0.14 THR 971 -0.19 ASP 1031

GLN 1027 0.17 VAL 972 -0.22 ASP 1031

GLN 1027 0.19 ASN 973 -0.26 ASP 1031

THR 952 0.19 CYS 974 -0.34 ASP 1031

THR 952 0.34 ASP 975 -0.40 ASP 1031

THR 952 0.24 PRO 976 -0.35 ASP 1031

PRO 976 0.14 GLY 977 -0.27 ASP 1031

LEU 1130 0.09 LEU 978 -0.23 ASP 1031

GLY 1131 0.12 ALA 979 -0.21 SER 1015

LEU 1130 0.13 VAL 980 -0.23 SER 1013

TYR 1147 0.15 GLY 981 -0.30 PHE 939

PRO 949 0.15 TYR 982 -0.39 PRO 1152

PRO 949 0.14 ASP 983 -0.45 PRO 1152

PRO 949 0.15 GLU 984 -0.50 PRO 1152

PRO 949 0.10 PHE 985 -0.44 ASP 1151

PRO 949 0.08 ASN 986 -0.27 ASP 1151

PRO 949 0.09 ALA 987 -0.14 PRO 1069

GLY 981 0.11 VAL 988 -0.13 PRO 1069

ARG 941 0.14 ASP 989 -0.15 GLY 1042

ARG 941 0.15 PHE 990 -0.16 GLY 1110

VAL 960 0.12 SER 991 -0.20 TYR 1147

VAL 969 0.14 GLY 992 -0.22 TYR 1090

ARG 1091 0.20 THR 993 -0.21 LEU 1145

ARG 1091 0.13 PHE 994 -0.20 HSD 963

LYS 1111 0.17 PHE 995 -0.33 ARG 962

VAL 1025 0.17 ILE 996 -0.32 ARG 962

VAL 1025 0.24 ASN 997 -0.37 ARG 962

GLN 1027 0.29 THR 998 -0.27 ARG 962

GLN 1027 0.43 GLU 999 -0.28 ARG 962

VAL 1025 0.62 ARG 1000 -0.23 ARG 962

GLN 1027 0.37 ASP 1001 -0.11 ASP 1031

ARG 1000 0.33 ASP 1002 -0.12 ASP 1031

THR 952 0.31 ASP 1003 -0.24 ASP 1031

THR 952 0.24 TYR 1004 -0.22 ASP 1031

THR 952 0.17 ALA 1005 -0.21 ASP 1031

THR 952 0.13 GLY 1006 -0.19 ASP 1031

THR 952 0.11 PHE 1007 -0.18 ASP 1031

THR 952 0.09 VAL 1008 -0.18 ASP 1031

PRO 949 0.10 PHE 1009 -0.15 ASP 1031

PRO 949 0.11 GLY 1010 -0.18 GLY 1070

PRO 949 0.13 TYR 1011 -0.21 GLY 1070

SER 1013 0.18 GLN 1012 -0.23 PRO 1152

GLN 1012 0.18 SER 1013 -0.32 GLN 943

PRO 949 0.15 SER 1014 -0.31 SER 1015

GLY 1053 0.15 SER 1015 -0.31 SER 1014

PRO 1079 0.16 ARG 1016 -0.27 GLY 1070

ARG 1016 0.12 PHE 1017 -0.21 GLY 1070

PRO 1079 0.11 TYR 1018 -0.15 VAL 1047

THR 952 0.12 VAL 1019 -0.17 ASP 1031

THR 952 0.13 VAL 1020 -0.17 ASP 1031

THR 952 0.16 MET 1021 -0.17 TRP 1030

ARG 1000 0.19 TRP 1022 -0.19 TRP 1030

ARG 1000 0.27 LYS 1023 -0.17 TRP 1030

ARG 1000 0.37 GLN 1024 -0.15 LYS 1112

ARG 1000 0.62 VAL 1025 -0.17 TRP 1030

ARG 1000 0.50 THR 1026 -0.21 GLN 1027

ARG 1000 0.57 GLN 1027 -0.24 PRO 1079

ARG 1000 0.46 SER 1028 -0.24 TRP 1076

THR 952 0.40 TYR 1029 -0.20 TRP 1076

THR 952 0.45 TRP 1030 -0.20 LEU 1043

SER 1028 0.30 ASP 1031 -0.41 GLU 1056

ALA 1037 0.37 THR 1032 -0.41 LYS 950

ALA 1037 0.29 ASN 1033 -0.48 GLU 1056

ALA 1037 0.16 PRO 1034 -0.37 GLU 1056

PRO 1069 0.32 THR 1035 -0.17 GLU 1056

ALA 1037 0.53 ARG 1036 -0.19 TRP 1030

ARG 1036 0.53 ALA 1037 -0.20 TRP 1076

ARG 1000 0.44 GLN 1038 -0.26 TRP 1076

ARG 1000 0.40 GLY 1039 -0.22 TRP 1076

ARG 1000 0.40 TYR 1040 -0.25 LEU 1043

ARG 1000 0.34 SER 1041 -0.21 THR 1026

GLY 1083 0.33 GLY 1042 -0.25 ALA 1115

LYS 1085 0.25 LEU 1043 -0.25 TYR 1040

THR 1074 0.22 SER 1044 -0.23 TYR 1040

ARG 1000 0.17 VAL 1045 -0.16 TRP 1063

VAL 1047 0.22 LYS 1046 -0.17 TRP 1063

LYS 1046 0.22 VAL 1047 -0.15 TYR 1018

PRO 1079 0.19 VAL 1048 -0.17 PRO 1069

PRO 1079 0.23 ASN 1049 -0.30 GLY 1070

PRO 1079 0.21 SER 1050 -0.28 GLY 1070

PRO 1079 0.24 THR 1051 -0.29 GLY 1053

PRO 1079 0.17 THR 1052 -0.38 GLY 1053

SER 1015 0.15 GLY 1053 -0.38 THR 1052

GLY 1055 0.17 PRO 1054 -0.26 PRO 946

PRO 1054 0.17 GLY 1055 -0.37 ASN 1033

GLY 951 0.29 GLU 1056 -0.48 ASN 1033

THR 952 0.13 HSD 1057 -0.28 ASN 1033

ALA 1037 0.13 LEU 1058 -0.20 ASN 1033

THR 952 0.28 ARG 1059 -0.27 ASP 1031

THR 952 0.29 ASN 1060 -0.20 LEU 1062

ARG 1000 0.20 ALA 1061 -0.18 ASN 1060

THR 952 0.21 LEU 1062 -0.20 ASN 1060

THR 952 0.31 TRP 1063 -0.22 TRP 1076

ARG 1000 0.30 HSD 1064 -0.24 LEU 1075

SER 1041 0.34 THR 1065 -0.28 TRP 1076

ASN 1067 0.40 GLY 1066 -0.24 LEU 1075

PRO 1079 0.42 ASN 1067 -0.16 TYR 1121

GLY 1066 0.33 THR 1068 -0.14 ASP 1122

GLY 1066 0.37 PRO 1069 -0.26 THR 1124

PRO 1079 0.30 GLY 1070 -0.30 ASN 1049

PRO 1079 0.25 GLN 1071 -0.17 GLN 943

PRO 1079 0.28 VAL 1072 -0.15 VAL 1048

PRO 1079 0.31 ARG 1073 -0.17 ASN 1060

HSD 1077 0.40 THR 1074 -0.28 LEU 1075

PRO 1079 0.25 LEU 1075 -0.28 THR 1065

PRO 1079 0.26 TRP 1076 -0.28 THR 1065

THR 1074 0.40 HSD 1077 -0.28 SER 1117

ASN 1067 0.27 ASP 1078 -0.24 ASP 1116

ASN 1067 0.42 PRO 1079 -0.24 GLN 1027

ASN 1067 0.33 ARG 1080 -0.23 GLN 1027

ASN 1067 0.36 HSD 1081 -0.26 ALA 1115

ASN 1067 0.28 ILE 1082 -0.22 MET 1114

GLY 1042 0.33 GLY 1083 -0.19 LYS 1112

LYS 1085 0.25 TRP 1084 -0.17 HSD 963

ILE 1082 0.28 LYS 1085 -0.25 ARG 962

VAL 1025 0.30 ASP 1086 -0.31 ARG 962

VAL 1025 0.27 PHE 1087 -0.38 ARG 962

LEU 1043 0.20 THR 1088 -0.33 HSD 963

LYS 1111 0.21 ALA 1089 -0.29 HSD 963

SER 1117 0.19 TYR 1090 -0.22 GLY 992

THR 993 0.20 ARG 1091 -0.24 GLU 1109

VAL 1106 0.17 TRP 1092 -0.18 GLY 1042

PHE 1142 0.14 ARG 1093 -0.20 GLY 1042

PRO 1152 0.15 LEU 1094 -0.16 GLY 1042

PRO 1152 0.27 SER 1095 -0.16 TYR 1040

PRO 1152 0.28 HSD 1096 -0.14 GLY 1066

PRO 1152 0.38 ARG 1097 -0.14 PRO 1069

PRO 1152 0.22 PRO 1098 -0.17 PRO 1069

PRO 1152 0.30 LYS 1099 -0.11 ALA 987

PRO 1152 0.57 THR 1100 -0.13 PRO 1069

PRO 1152 0.38 GLY 1101 -0.16 PRO 1069

PRO 1152 0.44 PHE 1102 -0.16 GLY 1066

PRO 1152 0.31 ILE 1103 -0.16 GLY 1066

PRO 1152 0.32 ARG 1104 -0.19 HSD 1077

PRO 1152 0.22 VAL 1105 -0.19 TYR 1040

PRO 1152 0.23 VAL 1106 -0.22 GLY 1042

PRO 1119 0.21 MET 1107 -0.23 GLY 1042

GLY 1118 0.20 TYR 1108 -0.17 GLU 1148

GLY 1118 0.23 GLU 1109 -0.24 ARG 1091

LYS 1111 0.46 GLY 1110 -0.24 GLU 1148

GLY 1110 0.46 LYS 1111 -0.19 GLU 1148

GLY 1118 0.33 LYS 1112 -0.19 ILE 1082

GLY 1118 0.32 ILE 1113 -0.18 HSD 1081

ALA 1115 0.42 MET 1114 -0.22 ILE 1082

MET 1114 0.42 ALA 1115 -0.26 HSD 1081

SER 1117 0.37 ASP 1116 -0.24 ASP 1078

ASP 1116 0.37 SER 1117 -0.28 HSD 1077

PRO 1152 0.37 GLY 1118 -0.22 HSD 1077

PRO 1152 0.43 PRO 1119 -0.19 GLN 1038

PRO 1152 0.34 ILE 1120 -0.22 GLY 1066

PRO 1152 0.34 TYR 1121 -0.20 GLY 1066

PRO 1152 0.20 ASP 1122 -0.19 PRO 1069

PRO 1079 0.17 LYS 1123 -0.21 PRO 1069

PRO 1079 0.19 THR 1124 -0.26 PRO 1069

PRO 1079 0.14 TYR 1125 -0.21 PRO 1069

LYS 1099 0.11 ALA 1126 -0.18 PRO 1069

PRO 949 0.10 GLY 1127 -0.18 PRO 1069

PRO 949 0.13 GLY 1128 -0.29 PRO 1152

PRO 949 0.15 ARG 1129 -0.29 PRO 1152

VAL 980 0.13 LEU 1130 -0.18 ASP 1151

ALA 979 0.12 GLY 1131 -0.18 GLY 1070

ASN 955 0.10 LEU 1132 -0.19 ASP 1031

THR 952 0.12 PHE 1133 -0.23 ASP 1031

THR 952 0.16 VAL 1134 -0.25 ASP 1031

THR 952 0.26 PHE 1135 -0.30 ASP 1031

THR 952 0.31 SER 1136 -0.34 ASP 1031

THR 952 0.20 GLN 1137 -0.25 ASP 1031

GLN 1027 0.19 GLU 1138 -0.20 ASP 1031

GLN 1027 0.20 MET 1139 -0.29 ARG 962

GLN 1027 0.13 VAL 1140 -0.28 ARG 962

ARG 1091 0.15 PHE 1141 -0.36 ARG 962

ARG 1091 0.14 PHE 1142 -0.23 HSD 963

VAL 969 0.16 SER 1143 -0.25 HSD 963

VAL 969 0.13 ASP 1144 -0.25 ASP 983

VAL 960 0.14 LEU 1145 -0.24 ASP 983

PHE 939 0.15 LYS 1146 -0.26 TYR 1147

ARG 941 0.22 TYR 1147 -0.26 LYS 1146

ARG 941 0.19 GLU 1148 -0.33 CYS 1149

ARG 941 0.11 CYS 1149 -0.33 GLU 1148

ASP 1151 0.20 ARG 1150 -0.12 GLY 1110

THR 1100 0.31 ASP 1151 -0.44 PHE 985

THR 1100 0.57 PRO 1152 -0.50 GLU 984

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 240531115742101615

--- normal mode 22 ---

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

* *