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

* *

CA distance fluctuations for 2405021543434120385

--- normal mode 24 ---

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 0.66 THR 937 -0.42 GLN 964

LYS 966 0.92 ASP 938 -0.36 GLN 964

LYS 966 0.89 PHE 939 -0.51 GLN 964

LYS 966 1.47 ARG 940 -0.45 GLN 964

LYS 966 1.07 ARG 941 -0.27 GLY 1128

LYS 966 0.67 PHE 942 -0.29 GLN 964

HSD 963 0.55 GLN 943 -0.29 GLY 1128

HSD 963 0.38 MET 944 -0.37 ASN 958

HSD 963 0.29 ILE 945 -0.36 ASN 958

HSD 963 0.22 PRO 946 -0.32 PRO 957

LEU 1132 0.27 LEU 947 -0.29 SER 1015

LEU 1132 0.21 ASP 948 -0.23 PRO 1054

GLY 965 0.19 PRO 949 -0.28 ASP 956

LEU 1132 0.17 LYS 950 -0.19 ASN 955

LEU 1132 0.18 GLY 951 -0.14 LYS 1099

LEU 1132 0.15 THR 952 -0.17 ARG 1000

GLY 992 0.12 SER 953 -0.16 LYS 1099

ASN 955 0.12 GLN 954 -0.20 ARG 1000

GLN 954 0.12 ASN 955 -0.25 PRO 949

LEU 968 0.15 ASP 956 -0.30 PRO 946

LEU 968 0.16 PRO 957 -0.35 ILE 945

ALA 1089 0.13 ASN 958 -0.37 MET 944

LEU 968 0.12 TRP 959 -0.31 ALA 979

ALA 1089 0.13 VAL 960 -0.29 VAL 961

ARG 940 0.36 VAL 961 -0.29 VAL 960

ARG 941 0.34 ARG 962 -0.46 HSD 963

GLY 965 1.17 HSD 963 -0.46 ARG 962

ARG 962 0.32 GLN 964 -0.51 PHE 939

HSD 963 1.17 GLY 965 -0.69 GLU 967

ARG 940 1.47 LYS 966 -0.61 ASN 997

ARG 940 0.56 GLU 967 -0.69 GLY 965

ARG 940 0.33 LEU 968 -0.31 GLN 964

ALA 1089 0.14 VAL 969 -0.28 ALA 979

ALA 1089 0.14 GLN 970 -0.37 ALA 979

ALA 1089 0.12 THR 971 -0.32 ALA 979

ALA 1089 0.11 VAL 972 -0.30 GLY 977

TRP 1030 0.12 ASN 973 -0.27 ARG 1000

PHE 994 0.13 CYS 974 -0.32 GLY 977

SER 1143 0.17 ASP 975 -0.27 CYS 974

LEU 1132 0.23 PRO 976 -0.28 SER 1015

LEU 1132 0.23 GLY 977 -0.33 GLU 1138

LEU 1132 0.28 LEU 978 -0.35 GLU 1138

HSD 963 0.31 ALA 979 -0.37 GLN 970

LYS 966 0.41 VAL 980 -0.35 GLY 1128

LYS 966 0.53 GLY 981 -0.35 GLN 964

LYS 966 0.63 TYR 982 -0.37 GLY 1128

LYS 966 0.48 ASP 983 -0.37 PHE 985

LYS 966 0.37 GLU 984 -0.55 PHE 985

LYS 966 0.23 PHE 985 -0.55 GLU 984

LYS 966 0.20 ASN 986 -0.41 GLU 984

LYS 966 0.18 ALA 987 -0.29 GLN 964

LYS 966 0.21 VAL 988 -0.30 GLN 964

LYS 966 0.23 ASP 989 -0.26 GLN 964

TYR 1018 0.23 PHE 990 -0.29 GLN 964

PHE 939 0.25 SER 991 -0.24 GLN 964

PHE 939 0.34 GLY 992 -0.24 GLN 964

ARG 940 0.36 THR 993 -0.24 GLY 965

ARG 940 0.29 PHE 994 -0.34 PHE 995

ARG 940 0.20 PHE 995 -0.34 PHE 994

TYR 1029 0.13 ILE 996 -0.37 LYS 966

TYR 1029 0.11 ASN 997 -0.61 LYS 966

LYS 1112 0.10 THR 998 -0.55 LYS 966

ASP 1086 0.17 GLU 999 -0.49 LYS 966

VAL 1025 0.22 ARG 1000 -0.46 LYS 966

GLN 1027 0.17 ASP 1001 -0.29 LYS 966

LYS 1112 0.19 ASP 1002 -0.19 LYS 966

LYS 1112 0.19 ASP 1003 -0.21 TYR 1018

PHE 994 0.23 TYR 1004 -0.27 TYR 1018

PHE 1135 0.24 ALA 1005 -0.25 PHE 1007

LEU 1062 0.25 GLY 1006 -0.41 PHE 1007

LEU 1062 0.27 PHE 1007 -0.41 GLY 1006

LEU 1058 0.24 VAL 1008 -0.38 PHE 1009

PHE 1017 0.21 PHE 1009 -0.38 VAL 1008

LYS 966 0.20 GLY 1010 -0.34 LYS 1099

LYS 966 0.25 TYR 1011 -0.34 LYS 1099

LYS 966 0.24 GLN 1012 -0.36 LYS 1099

LYS 966 0.22 SER 1013 -0.29 LYS 1099

LYS 966 0.22 SER 1014 -0.31 PRO 957

LEU 1130 0.17 SER 1015 -0.29 LEU 947

PHE 1009 0.20 ARG 1016 -0.27 PRO 957

PHE 1009 0.21 PHE 1017 -0.30 PHE 1133

PHE 990 0.23 TYR 1018 -0.34 PHE 1133

SER 991 0.24 VAL 1019 -0.27 TYR 1018

SER 991 0.25 VAL 1020 -0.24 MET 1021

GLY 992 0.25 MET 1021 -0.24 VAL 1020

TRP 1063 0.25 TRP 1022 -0.16 PRO 1098

LYS 1112 0.24 LYS 1023 -0.20 VAL 1045

LYS 1112 0.25 GLN 1024 -0.16 TYR 1018

LYS 1112 0.24 VAL 1025 -0.15 VAL 1047

LYS 1112 0.22 THR 1026 -0.14 VAL 1047

LYS 1112 0.21 GLN 1027 -0.16 VAL 1047

LYS 1112 0.19 SER 1028 -0.15 THR 1124

LYS 1112 0.20 TYR 1029 -0.15 THR 1124

LYS 1112 0.17 TRP 1030 -0.14 THR 1124

LYS 1112 0.18 ASP 1031 -0.11 LYS 1099

LYS 1112 0.20 THR 1032 -0.10 LYS 1099

LYS 1112 0.20 ASN 1033 -0.09 LYS 1099

GLY 992 0.21 PRO 1034 -0.09 LYS 1099

SER 1044 0.21 THR 1035 -0.10 LYS 1099

LYS 1112 0.22 ARG 1036 -0.10 THR 1124

LYS 1112 0.22 ALA 1037 -0.13 THR 1124

GLY 1039 0.24 GLN 1038 -0.13 ARG 1073

GLN 1038 0.24 GLY 1039 -0.17 THR 1074

LYS 1112 0.24 TYR 1040 -0.13 THR 1074

LYS 1112 0.24 SER 1041 -0.12 VAL 1045

MET 1114 0.27 GLY 1042 -0.10 PRO 1098

HSD 1064 0.25 LEU 1043 -0.12 TRP 1084

ASN 1067 0.26 SER 1044 -0.16 LYS 1023

SER 991 0.25 VAL 1045 -0.22 MET 1021

VAL 1072 0.28 LYS 1046 -0.21 ASP 1122

PHE 990 0.22 VAL 1047 -0.27 PHE 1135

SER 991 0.20 VAL 1048 -0.28 PHE 1135

PHE 990 0.19 ASN 1049 -0.22 PRO 976

VAL 1008 0.19 SER 1050 -0.20 CYS 974

SER 991 0.17 THR 1051 -0.16 ASP 956

VAL 1008 0.19 THR 1052 -0.17 ASP 956

VAL 1008 0.23 GLY 1053 -0.19 ASP 956

LEU 1132 0.23 PRO 1054 -0.25 ASP 956

LEU 1132 0.23 GLY 1055 -0.16 ASN 955

LEU 1132 0.22 GLU 1056 -0.13 LYS 1099

PHE 1007 0.21 HSD 1057 -0.13 LYS 1099

PHE 1007 0.26 LEU 1058 -0.19 ARG 1059

LEU 1132 0.26 ARG 1059 -0.19 LEU 1058

GLY 1006 0.24 ASN 1060 -0.15 THR 1124

GLY 992 0.22 ALA 1061 -0.17 THR 1124

PHE 1007 0.27 LEU 1062 -0.24 TRP 1063

TRP 1022 0.25 TRP 1063 -0.24 LEU 1062

LEU 1043 0.25 HSD 1064 -0.20 ARG 1073

SER 1044 0.24 THR 1065 -0.16 THR 1074

ASN 1067 0.24 GLY 1066 -0.14 ARG 1073

HSD 1077 0.26 ASN 1067 -0.11 HSD 1064

SER 1044 0.24 THR 1068 -0.12 LYS 1099

ARG 1073 0.24 PRO 1069 -0.11 LYS 1099

ARG 1073 0.24 GLY 1070 -0.13 LYS 1099

SER 991 0.20 GLN 1071 -0.17 THR 1124

LYS 1046 0.28 VAL 1072 -0.18 THR 1124

GLY 1070 0.24 ARG 1073 -0.21 TRP 1063

ASN 1067 0.23 THR 1074 -0.17 GLY 1039

PRO 1069 0.21 LEU 1075 -0.17 TYR 1004

ASN 1067 0.26 TRP 1076 -0.13 LYS 1023

ASN 1067 0.26 HSD 1077 -0.11 TRP 1076

LYS 1112 0.22 ASP 1078 -0.10 PRO 1152

ASN 1067 0.23 PRO 1079 -0.09 PRO 1152

LYS 1112 0.19 ARG 1080 -0.09 GLY 965

LYS 1112 0.23 HSD 1081 -0.09 PRO 1152

LYS 1112 0.28 ILE 1082 -0.12 GLY 965

LYS 1112 0.28 GLY 1083 -0.13 GLY 965

LYS 1112 0.28 TRP 1084 -0.17 GLY 965

LYS 1112 0.22 LYS 1085 -0.24 GLY 965

GLU 999 0.17 ASP 1086 -0.35 LYS 966

ARG 940 0.12 PHE 1087 -0.44 LYS 966

ARG 940 0.20 THR 1088 -0.30 GLY 965

ARG 940 0.29 ALA 1089 -0.27 GLY 965

ARG 940 0.29 TYR 1090 -0.19 GLY 965

ARG 940 0.30 ARG 1091 -0.19 GLY 965

LEU 1062 0.25 TRP 1092 -0.25 ARG 1093

VAL 1045 0.22 ARG 1093 -0.25 TRP 1092

VAL 1045 0.23 LEU 1094 -0.21 GLN 964

LYS 966 0.16 SER 1095 -0.23 GLN 964

LYS 1123 0.15 HSD 1096 -0.26 GLN 964

LYS 966 0.13 ARG 1097 -0.32 PRO 1152

LYS 966 0.10 PRO 1098 -0.46 GLY 1127

LYS 966 0.09 LYS 1099 -0.49 ALA 1126

LYS 966 0.10 THR 1100 -0.36 PRO 1152

LYS 966 0.09 GLY 1101 -0.28 PRO 1152

LYS 966 0.10 PHE 1102 -0.30 PRO 1152

ASP 989 0.14 ILE 1103 -0.23 GLY 1006

ASN 1067 0.15 ARG 1104 -0.18 GLY 1006

VAL 1045 0.23 VAL 1105 -0.16 PHE 995

ASN 1067 0.20 VAL 1106 -0.12 MET 1107

ARG 940 0.23 MET 1107 -0.12 VAL 1106

ARG 940 0.25 TYR 1108 -0.14 GLY 965

ARG 940 0.27 GLU 1109 -0.17 GLY 965

ARG 940 0.28 GLY 1110 -0.20 GLY 965

ILE 1113 0.25 LYS 1111 -0.22 GLY 965

ILE 1082 0.28 LYS 1112 -0.16 GLY 965

LYS 1112 0.27 ILE 1113 -0.12 GLY 965

GLY 1042 0.27 MET 1114 -0.12 GLY 965

LYS 1112 0.23 ALA 1115 -0.09 GLY 965

ASN 1067 0.20 ASP 1116 -0.11 PRO 1152

ASN 1067 0.20 SER 1117 -0.13 PRO 1152

ASN 1067 0.15 GLY 1118 -0.17 PRO 1152

LYS 1111 0.13 PRO 1119 -0.24 PRO 1152

PRO 1069 0.11 ILE 1120 -0.22 PRO 1152

LYS 1111 0.09 TYR 1121 -0.25 PRO 1152

ASP 989 0.13 ASP 1122 -0.23 PHE 1133

HSD 1096 0.15 LYS 1123 -0.24 LYS 1099

ASP 989 0.14 THR 1124 -0.27 PHE 1133

ASP 989 0.14 TYR 1125 -0.38 LYS 1099

LYS 966 0.13 ALA 1126 -0.49 LYS 1099

PHE 985 0.20 GLY 1127 -0.47 LYS 1099

LYS 966 0.21 GLY 1128 -0.51 ARG 1129

LYS 966 0.32 ARG 1129 -0.51 GLY 1128

LYS 966 0.28 LEU 1130 -0.50 GLY 1131

LYS 966 0.34 GLY 1131 -0.50 LEU 1130

PHE 1133 0.35 LEU 1132 -0.33 VAL 1140

LEU 1132 0.35 PHE 1133 -0.34 PHE 1009

PRO 976 0.21 VAL 1134 -0.36 GLN 1137

ALA 1005 0.24 PHE 1135 -0.28 TYR 1018

PHE 994 0.16 SER 1136 -0.23 THR 1124

TYR 1029 0.15 GLN 1137 -0.36 VAL 1134

TRP 1030 0.13 GLU 1138 -0.35 VAL 1134

TYR 1029 0.12 MET 1139 -0.46 LYS 966

TYR 1029 0.14 VAL 1140 -0.34 PHE 1007

ARG 940 0.23 PHE 1141 -0.37 GLY 965

ARG 940 0.31 PHE 1142 -0.30 GLY 965

ARG 940 0.52 SER 1143 -0.43 GLY 965

ARG 940 0.56 ASP 1144 -0.33 GLY 965

PHE 939 0.43 LEU 1145 -0.38 GLN 964

LYS 966 0.38 LYS 1146 -0.34 GLN 964

LYS 966 0.32 TYR 1147 -0.35 GLN 964

LYS 966 0.32 GLU 1148 -0.29 GLN 964

LYS 966 0.29 CYS 1149 -0.28 GLN 964

LYS 966 0.23 ARG 1150 -0.24 GLN 964

LYS 966 0.27 ASP 1151 -0.20 GLN 964

LYS 966 0.25 PRO 1152 -0.36 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 24 ---

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

* *