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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 19 ---

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
LYS 966 0.61 THR 937 -0.77 ASP 1151

LYS 966 0.80 ASP 938 -0.71 ASP 1151

GLU 967 0.78 PHE 939 -0.50 ASP 1151

VAL 961 1.16 ARG 940 -0.51 ASP 1151

HSD 963 0.77 ARG 941 -0.45 ASP 1151

VAL 960 0.44 PHE 942 -0.27 ASP 1151

TYR 982 0.27 GLN 943 -0.25 PHE 942

ASN 958 0.20 MET 944 -0.14 GLN 964

GLU 1138 0.11 ILE 945 -0.11 GLY 965

THR 1052 0.14 PRO 946 -0.13 THR 952

THR 1052 0.12 LEU 947 -0.11 THR 952

ARG 1000 0.16 ASP 948 -0.18 GLY 951

ASP 956 0.24 PRO 949 -0.17 SER 1014

ARG 1000 0.23 LYS 950 -0.21 SER 1015

ARG 1000 0.24 GLY 951 -0.20 SER 1015

ARG 1000 0.31 THR 952 -0.17 ASP 948

ARG 1000 0.29 SER 953 -0.12 SER 1015

ARG 1000 0.35 GLN 954 -0.13 ASN 955

ARG 940 0.29 ASN 955 -0.13 GLN 954

ARG 940 0.28 ASP 956 -0.10 GLN 954

ARG 940 0.38 PRO 957 -0.08 LYS 966

ARG 940 0.52 ASN 958 -0.09 GLN 1027

ARG 940 0.67 TRP 959 -0.10 VAL 961

ARG 940 0.90 VAL 960 -0.09 VAL 961

ARG 940 1.16 VAL 961 -0.10 TRP 959

ARG 940 0.94 ARG 962 -0.15 HSD 963

ARG 940 0.77 HSD 963 -0.15 ARG 962

ARG 940 0.44 GLN 964 -0.33 ASP 1144

ARG 940 0.79 GLY 965 -0.41 ASP 1144

ARG 940 1.11 LYS 966 -0.49 GLU 967

ARG 940 1.01 GLU 967 -0.49 LYS 966

ARG 940 1.03 LEU 968 -0.29 GLY 965

ARG 940 0.84 VAL 969 -0.17 LYS 966

ARG 940 0.64 GLN 970 -0.11 GLN 1027

ARG 940 0.62 THR 971 -0.14 GLN 1027

ARG 940 0.48 VAL 972 -0.14 GLN 1027

ARG 940 0.39 ASN 973 -0.14 GLN 1027

ARG 940 0.34 CYS 974 -0.12 SER 1028

ARG 940 0.23 ASP 975 -0.07 GLY 965

ARG 940 0.19 PRO 976 -0.11 GLY 965

ARG 940 0.18 GLY 977 -0.14 GLY 965

ARG 940 0.14 LEU 978 -0.16 GLY 965

GLU 1138 0.19 ALA 979 -0.19 GLY 965

GLU 984 0.21 VAL 980 -0.19 ARG 941

VAL 960 0.32 GLY 981 -0.33 ASP 1151

HSD 963 0.47 TYR 982 -0.51 GLY 1128

HSD 963 0.35 ASP 983 -0.59 ASP 1151

HSD 963 0.29 GLU 984 -0.60 GLY 1127

CYS 1149 0.22 PHE 985 -0.56 GLU 984

CYS 1149 0.28 ASN 986 -0.48 GLU 984

ALA 1126 0.17 ALA 987 -0.34 ASP 938

GLU 967 0.16 VAL 988 -0.28 THR 937

LYS 1146 0.21 ASP 989 -0.41 LEU 1094

LEU 1145 0.22 PHE 990 -0.41 ARG 1093

SER 1095 0.37 SER 991 -0.31 TYR 1147

SER 1095 0.27 GLY 992 -0.24 GLY 965

ARG 940 0.27 THR 993 -0.28 GLY 965

ARG 940 0.38 PHE 994 -0.24 GLY 965

ARG 940 0.45 PHE 995 -0.19 LYS 966

ARG 940 0.45 ILE 996 -0.15 LYS 966

ARG 940 0.53 ASN 997 -0.15 VAL 1025

ARG 940 0.48 THR 998 -0.18 VAL 1025

ARG 940 0.40 GLU 999 -0.23 VAL 1025

ARG 940 0.40 ARG 1000 -0.27 VAL 1025

ARG 940 0.32 ASP 1001 -0.18 GLN 1027

ARG 940 0.26 ASP 1002 -0.21 ARG 1000

ARG 940 0.24 ASP 1003 -0.14 LYS 966

ARG 940 0.22 TYR 1004 -0.16 GLY 965

ARG 940 0.27 ALA 1005 -0.18 GLY 965

TYR 1121 0.21 GLY 1006 -0.19 GLY 965

PRO 1098 0.15 PHE 1007 -0.16 GLY 965

PRO 1098 0.17 VAL 1008 -0.18 TYR 982

GLY 1131 0.17 PHE 1009 -0.28 TYR 982

ASN 986 0.20 GLY 1010 -0.41 TYR 982

ASN 986 0.16 TYR 1011 -0.39 TYR 982

ASN 986 0.14 GLN 1012 -0.46 TYR 982

GLU 1138 0.09 SER 1013 -0.33 TYR 982

THR 1051 0.10 SER 1014 -0.22 TYR 982

PRO 1152 0.09 SER 1015 -0.38 GLY 1053

PRO 1152 0.12 ARG 1016 -0.30 TYR 982

PRO 1152 0.15 PHE 1017 -0.31 TYR 982

VAL 1019 0.19 TYR 1018 -0.25 TYR 982

TYR 1018 0.19 VAL 1019 -0.19 TYR 982

TYR 1121 0.20 VAL 1020 -0.15 GLU 1148

TYR 1121 0.20 MET 1021 -0.16 GLY 965

TYR 1121 0.20 TRP 1022 -0.17 GLY 965

TYR 1121 0.18 LYS 1023 -0.16 GLY 965

ARG 940 0.21 GLN 1024 -0.16 TYR 1040

TRP 1030 0.22 VAL 1025 -0.27 ARG 1000

GLN 1027 0.30 THR 1026 -0.23 ARG 1000

THR 1026 0.30 GLN 1027 -0.22 ARG 1000

ASP 1031 0.15 SER 1028 -0.14 GLN 1137

VAL 1025 0.19 TYR 1029 -0.10 GLY 965

VAL 1025 0.22 TRP 1030 -0.09 CYS 974

VAL 1025 0.19 ASP 1031 -0.10 SER 1050

SER 1028 0.14 THR 1032 -0.12 THR 1068

VAL 1025 0.12 ASN 1033 -0.16 ARG 1073

ASP 1001 0.09 PRO 1034 -0.22 GLN 1071

PRO 1152 0.08 THR 1035 -0.18 ARG 1073

PRO 1152 0.10 ARG 1036 -0.12 ARG 1073

PRO 1152 0.12 ALA 1037 -0.11 GLY 965

PRO 1152 0.14 GLN 1038 -0.13 ARG 1000

LYS 1099 0.15 GLY 1039 -0.14 ARG 1000

LYS 1123 0.17 TYR 1040 -0.19 ARG 1000

GLN 1027 0.22 SER 1041 -0.15 ARG 1000

TYR 1121 0.22 GLY 1042 -0.17 GLU 1148

TYR 1121 0.23 LEU 1043 -0.21 GLU 1148

TYR 1121 0.24 SER 1044 -0.17 GLU 1148

LYS 1123 0.23 VAL 1045 -0.18 GLU 984

PRO 1152 0.23 LYS 1046 -0.23 VAL 1072

PRO 1152 0.23 VAL 1047 -0.23 TYR 982

PRO 1152 0.18 VAL 1048 -0.22 TYR 982

PRO 1152 0.14 ASN 1049 -0.36 THR 1124

PRO 1152 0.11 SER 1050 -0.27 THR 1124

GLY 1053 0.21 THR 1051 -0.40 THR 1124

GLY 1053 0.20 THR 1052 -0.32 THR 1124

THR 1051 0.21 GLY 1053 -0.38 SER 1015

THR 1052 0.16 PRO 1054 -0.24 SER 1015

ARG 1000 0.14 GLY 1055 -0.25 SER 1015

ARG 1000 0.15 GLU 1056 -0.18 SER 1015

ARG 1059 0.11 HSD 1057 -0.18 THR 1124

ARG 1000 0.07 LEU 1058 -0.16 THR 1124

HSD 1057 0.11 ARG 1059 -0.11 THR 1124

GLY 1039 0.10 ASN 1060 -0.10 GLY 965

PRO 1152 0.12 ALA 1061 -0.15 PRO 1034

PRO 1152 0.12 LEU 1062 -0.12 GLY 965

LYS 1099 0.13 TRP 1063 -0.13 GLY 965

PRO 1152 0.15 HSD 1064 -0.12 GLY 965

PRO 1152 0.18 THR 1065 -0.13 GLY 965

PRO 1152 0.21 GLY 1066 -0.13 ASN 1067

PRO 1152 0.20 ASN 1067 -0.22 LEU 1075

PRO 1152 0.16 THR 1068 -0.24 ARG 1073

PRO 1152 0.12 PRO 1069 -0.33 ARG 1073

PRO 1152 0.12 GLY 1070 -0.33 ASP 1122

PRO 1152 0.13 GLN 1071 -0.22 PRO 1034

PRO 1152 0.17 VAL 1072 -0.24 ARG 1073

PRO 1152 0.25 ARG 1073 -0.33 PRO 1069

PRO 1152 0.24 THR 1074 -0.21 PRO 1069

LYS 1123 0.31 LEU 1075 -0.28 PRO 1069

PRO 1152 0.26 TRP 1076 -0.22 ASN 1067

TYR 1121 0.26 HSD 1077 -0.18 GLU 1148

TYR 1121 0.25 ASP 1078 -0.22 GLU 1148

TYR 1121 0.21 PRO 1079 -0.20 GLU 1148

GLN 1027 0.19 ARG 1080 -0.23 GLU 1148

GLN 1027 0.21 HSD 1081 -0.19 GLU 1148

GLN 1027 0.22 ILE 1082 -0.22 GLU 1148

TYR 1121 0.18 GLY 1083 -0.16 HSD 1081

MET 1114 0.23 TRP 1084 -0.16 GLY 965

ARG 940 0.27 LYS 1085 -0.18 ILE 1082

ARG 940 0.35 ASP 1086 -0.13 ILE 1082

ARG 940 0.40 PHE 1087 -0.12 ILE 1082

ARG 940 0.32 THR 1088 -0.14 GLY 965

ARG 940 0.33 ALA 1089 -0.18 GLY 965

PRO 1119 0.25 TYR 1090 -0.20 GLY 965

ARG 1104 0.27 ARG 1091 -0.23 GLU 1148

ARG 1104 0.35 TRP 1092 -0.29 GLU 1148

ARG 1104 0.30 ARG 1093 -0.44 GLU 1148

PHE 1102 0.28 LEU 1094 -0.41 ASP 989

SER 991 0.37 SER 1095 -0.29 ARG 1104

PRO 1152 0.32 HSD 1096 -0.34 GLU 984

PRO 1152 0.52 ARG 1097 -0.38 GLU 984

PRO 1152 0.51 PRO 1098 -0.52 GLU 984

PRO 1152 0.66 LYS 1099 -0.49 GLU 984

PRO 1152 0.72 THR 1100 -0.42 GLU 984

PRO 1152 0.59 GLY 1101 -0.42 GLU 984

PRO 1152 0.51 PHE 1102 -0.35 GLU 984

PRO 1152 0.36 ILE 1103 -0.31 GLU 984

VAL 1105 0.39 ARG 1104 -0.29 SER 1095

ARG 1104 0.39 VAL 1105 -0.38 ASP 989

MET 1107 0.32 VAL 1106 -0.40 GLU 1148

VAL 1106 0.32 MET 1107 -0.34 GLU 1148

PRO 1119 0.24 TYR 1108 -0.35 GLU 1148

PRO 1119 0.21 GLU 1109 -0.25 GLU 1148

PRO 1119 0.22 GLY 1110 -0.52 LYS 1111

PRO 1119 0.35 LYS 1111 -0.52 GLY 1110

THR 1088 0.23 LYS 1112 -0.39 GLU 1148

LYS 1111 0.27 ILE 1113 -0.41 GLU 1148

TRP 1084 0.23 MET 1114 -0.34 GLU 1148

TRP 1084 0.21 ALA 1115 -0.34 GLU 1148

PRO 1119 0.28 ASP 1116 -0.34 GLU 1148

TYR 1121 0.23 SER 1117 -0.27 GLU 1148

LYS 1111 0.32 GLY 1118 -0.25 GLU 1148

LYS 1111 0.35 PRO 1119 -0.25 GLU 984

PRO 1152 0.39 ILE 1120 -0.29 PRO 1069

PRO 1152 0.47 TYR 1121 -0.31 GLU 984

PRO 1152 0.48 ASP 1122 -0.34 THR 1051

PRO 1152 0.48 LYS 1123 -0.45 GLU 984

PRO 1152 0.42 THR 1124 -0.40 THR 1051

PRO 1152 0.31 TYR 1125 -0.45 GLU 984

PRO 1152 0.37 ALA 1126 -0.58 GLU 984

ASN 986 0.27 GLY 1127 -0.60 GLU 984

ASN 986 0.19 GLY 1128 -0.57 GLU 984

HSD 963 0.15 ARG 1129 -0.46 TYR 982

GLY 1131 0.20 LEU 1130 -0.20 TYR 982

LEU 1130 0.20 GLY 1131 -0.16 GLY 965

ARG 940 0.19 LEU 1132 -0.22 GLY 965

ARG 940 0.19 PHE 1133 -0.19 GLY 965

ARG 940 0.28 VAL 1134 -0.16 GLY 965

ARG 940 0.24 PHE 1135 -0.13 GLY 965

ARG 940 0.29 SER 1136 -0.12 SER 1028

ARG 940 0.38 GLN 1137 -0.17 GLN 1027

ARG 940 0.50 GLU 1138 -0.16 GLN 1027

ARG 940 0.60 MET 1139 -0.15 GLN 1027

ARG 940 0.56 VAL 1140 -0.16 LYS 966

ARG 940 0.66 PHE 1141 -0.21 LYS 966

ARG 940 0.59 PHE 1142 -0.31 GLY 965

ARG 940 0.51 SER 1143 -0.40 GLY 965

THR 937 0.30 ASP 1144 -0.41 GLY 965

SER 1095 0.24 LEU 1145 -0.27 GLY 965

SER 1095 0.22 LYS 1146 -0.28 ASP 1151

GLU 967 0.19 TYR 1147 -0.38 ARG 1093

GLU 984 0.23 GLU 1148 -0.53 CYS 1149

ASN 986 0.28 CYS 1149 -0.54 THR 937

ALA 1126 0.15 ARG 1150 -0.35 THR 937

THR 1100 0.34 ASP 1151 -0.77 THR 937

THR 1100 0.72 PRO 1152 -0.69 THR 937

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 19 ---

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

* *