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

* gal1_monomer_wt *

CA distance fluctuations for 2405021233474105405

--- normal mode 10 ---

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
ASP 1026 0.88 ALA 1001 -0.96 ASN 1008

TRP 1068 0.52 SER 1002 -0.58 VAL 1005

ALA 1067 0.46 GLY 1003 -0.41 ASP 1125

GLY 1066 0.41 LEU 1004 -0.44 PHE 1133

CYS 1130 0.41 VAL 1005 -0.59 ALA 1001

CYS 1130 0.55 ALA 1006 -0.76 ALA 1001

CYS 1130 0.47 SER 1007 -0.90 ALA 1001

ALA 1132 0.43 ASN 1008 -0.96 ALA 1001

LEU 1017 0.35 LEU 1009 -0.81 ALA 1001

GLY 1103 0.31 ASN 1010 -0.77 ALA 1001

GLY 1103 0.33 LEU 1011 -0.60 ALA 1001

GLY 1103 0.35 LYS 1012 -0.53 ALA 1001

GLU 1105 0.34 PRO 1013 -0.39 ALA 1001

GLU 1105 0.45 GLY 1014 -0.33 ALA 1001

GLY 1103 0.50 GLU 1015 -0.40 ALA 1001

LEU 1009 0.35 LEU 1017 -0.29 LEU 1004

ASN 1008 0.33 ARG 1018 -0.27 THR 1090

SER 1007 0.33 VAL 1019 -0.19 GLY 1003

ALA 1006 0.34 ARG 1020 -0.19 GLU 1086

ALA 1001 0.30 GLY 1021 -0.18 PRO 1101

ALA 1001 0.48 GLU 1022 -0.19 ASP 1102

ALA 1001 0.60 VAL 1023 -0.20 GLY 1003

ALA 1001 0.77 ALA 1024 -0.29 GLY 1003

ALA 1001 0.78 PRO 1025 -0.27 GLY 1003

ALA 1001 0.88 ASP 1026 -0.35 SER 1038

ALA 1001 0.86 ALA 1027 -0.37 SER 1038

ALA 1001 0.85 LYS 1028 -0.55 SER 1038

ALA 1001 0.73 SER 1029 -0.52 SER 1038

ALA 1001 0.55 PHE 1030 -0.39 SER 1038

ALA 1001 0.31 VAL 1031 -0.35 SER 1038

LYS 1127 0.21 LEU 1032 -0.27 ALA 1051

CYS 1130 0.25 ASN 1033 -0.44 HIS 1052

CYS 1130 0.23 LEU 1034 -0.39 HIS 1052

CYS 1130 0.23 GLY 1035 -0.47 HIS 1052

CYS 1130 0.24 LYS 1036 -0.53 HIS 1052

CYS 1130 0.31 ASP 1037 -0.69 HIS 1052

VAL 1005 0.39 SER 1038 -0.87 HIS 1052

VAL 1005 0.36 ASN 1039 -0.89 HIS 1052

CYS 1130 0.24 ASN 1040 -0.67 HIS 1052

CYS 1130 0.22 LEU 1041 -0.54 HIS 1052

CYS 1130 0.13 CYS 1042 -0.36 HIS 1052

SER 1002 0.16 LEU 1043 -0.30 HIS 1052

SER 1002 0.31 HIS 1044 -0.37 HIS 1052

ALA 1001 0.24 PHE 1045 -0.21 SER 1038

ALA 1001 0.43 ASN 1046 -0.37 SER 1038

ALA 1001 0.51 PRO 1047 -0.34 SER 1038

ALA 1001 0.63 ARG 1048 -0.50 SER 1038

ALA 1001 0.66 PHE 1049 -0.44 SER 1038

ALA 1001 0.68 ASN 1050 -0.60 SER 1038

ALA 1001 0.71 ALA 1051 -0.77 SER 1038

ALA 1001 0.64 HIS 1052 -0.89 ASN 1039

ALA 1001 0.56 GLY 1053 -0.72 GLY 1066

ALA 1001 0.57 ASP 1054 -0.56 ASN 1039

ALA 1001 0.55 ALA 1055 -0.47 SER 1038

ALA 1001 0.56 ASN 1056 -0.36 SER 1038

ALA 1001 0.52 THR 1057 -0.32 ASN 1039

ALA 1001 0.46 ILE 1058 -0.27 SER 1038

ALA 1001 0.45 VAL 1059 -0.32 ASN 1039

ALA 1001 0.32 CYS 1060 -0.23 ASN 1061

SER 1002 0.38 ASN 1061 -0.25 HIS 1052

SER 1002 0.32 SER 1062 -0.38 HIS 1052

GLY 1003 0.36 LYS 1063 -0.60 HIS 1052

GLY 1003 0.28 ASP 1064 -0.56 HIS 1052

GLY 1003 0.28 ASP 1065 -0.70 HIS 1052

GLY 1003 0.43 GLY 1066 -0.84 HIS 1052

SER 1002 0.48 ALA 1067 -0.67 HIS 1052

SER 1002 0.52 TRP 1068 -0.60 HIS 1052

SER 1002 0.45 GLY 1069 -0.28 HIS 1052

SER 1002 0.45 THR 1070 -0.24 GLU 1074

SER 1002 0.42 GLU 1071 -0.29 GLU 1074

ALA 1001 0.37 GLN 1072 -0.27 GLU 1074

ALA 1001 0.41 ARG 1073 -0.32 TRP 1068

ALA 1001 0.37 GLU 1074 -0.29 GLU 1071

ALA 1001 0.39 ALA 1075 -0.27 TRP 1068

ALA 1001 0.41 VAL 1076 -0.23 TRP 1068

ALA 1001 0.45 PHE 1077 -0.23 TRP 1068

ALA 1001 0.42 PRO 1078 -0.25 VAL 1084

ALA 1001 0.48 PHE 1079 -0.16 SER 1038

ALA 1001 0.54 GLN 1080 -0.18 SER 1038

ALA 1001 0.65 PRO 1081 -0.22 SER 1038

ALA 1001 0.63 GLY 1082 -0.19 GLY 1003

ALA 1001 0.52 SER 1083 -0.19 PRO 1078

ALA 1001 0.43 VAL 1084 -0.28 ASP 1102

ALA 1001 0.36 ALA 1085 -0.26 PRO 1101

ALA 1085 0.28 GLU 1086 -0.19 ARG 1020

LEU 1009 0.23 VAL 1087 -0.16 VAL 1098

ASP 1134 0.34 CYS 1088 -0.22 THR 1097

LYS 1099 0.29 ILE 1089 -0.17 ARG 1018

GLU 1105 0.38 THR 1090 -0.27 ARG 1018

GLU 1105 0.35 PHE 1091 -0.26 ALA 1001

GLU 1105 0.29 ASP 1092 -0.24 ALA 1001

ALA 1075 0.23 GLN 1093 -0.25 ALA 1001

ALA 1075 0.25 ALA 1094 -0.14 ARG 1018

ALA 1075 0.26 ASN 1095 -0.16 ARG 1018

ALA 1075 0.23 LEU 1096 -0.17 ARG 1018

ALA 1075 0.30 THR 1097 -0.22 CYS 1088

GLU 1015 0.28 VAL 1098 -0.17 CYS 1088

GLU 1015 0.42 LYS 1099 -0.18 GLU 1086

ASP 1134 0.35 LEU 1100 -0.18 VAL 1084

ASP 1134 0.38 PRO 1101 -0.26 ALA 1085

ASP 1134 0.42 ASP 1102 -0.28 VAL 1084

GLU 1015 0.50 GLY 1103 -0.22 VAL 1084

GLU 1015 0.44 TYR 1104 -0.23 GLN 1072

GLY 1014 0.45 GLU 1105 -0.20 THR 1070

ALA 1075 0.35 PHE 1106 -0.22 THR 1070

ALA 1075 0.32 LYS 1107 -0.17 CYS 1088

ARG 1073 0.28 PHE 1108 -0.13 LYS 1107

ARG 1073 0.21 PRO 1109 -0.11 CYS 1088

ARG 1073 0.12 ASN 1110 -0.17 HIS 1052

SER 1002 0.16 ARG 1111 -0.20 HIS 1052

GLY 1003 0.10 LEU 1112 -0.33 HIS 1052

GLY 1103 0.09 ASN 1113 -0.26 HIS 1052

GLY 1103 0.14 LEU 1114 -0.35 ALA 1001

GLY 1103 0.21 GLU 1115 -0.45 ALA 1001

GLY 1103 0.24 ALA 1116 -0.53 ALA 1001

GLY 1103 0.24 ILE 1117 -0.51 ALA 1001

LEU 1017 0.30 ASN 1118 -0.68 ALA 1001

CYS 1130 0.37 TYR 1119 -0.59 ALA 1001

CYS 1130 0.35 MET 1120 -0.41 ALA 1001

GLY 1066 0.32 ALA 1121 -0.44 ASP 1123

TRP 1068 0.33 ALA 1122 -0.35 ASP 1125

THR 1070 0.35 ASP 1123 -0.46 VAL 1005

ALA 1001 0.55 GLY 1124 -0.41 VAL 1005

ALA 1001 0.76 ASP 1125 -0.41 GLY 1003

ALA 1001 0.50 PHE 1126 -0.27 GLY 1003

ALA 1001 0.37 LYS 1127 -0.19 VAL 1131

GLY 1066 0.27 ILE 1128 -0.23 VAL 1131

ALA 1006 0.40 LYS 1129 -0.16 GLY 1103

ALA 1006 0.55 CYS 1130 -0.18 GLY 1014

SER 1007 0.46 VAL 1131 -0.31 GLY 1003

ASN 1008 0.43 ALA 1132 -0.33 GLY 1003

ASN 1008 0.36 PHE 1133 -0.48 ALA 1001

GLY 1103 0.49 ASP 1134 -0.46 ALA 1001

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.

*** gal1_monomer_wt ***

CA distance fluctuations for 2405021233474105405

--- normal mode 10 ---

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

* gal1_monomer_wt *