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

* opt_a_lac *

CA distance fluctuations for 2406061849031399629

--- 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
LYS 1129 0.71 ALA 1001 -1.44 HIS 1052

LYS 1127 0.69 SER 1002 -1.27 HIS 1052

ILE 1128 0.36 GLY 1003 -0.82 HIS 1052

GLY 1003 0.34 LEU 1004 -0.61 HIS 1052

PRO 1025 0.18 VAL 1005 -0.57 HIS 1052

GLY 1003 0.14 ALA 1006 -0.46 HIS 1052

PRO 1025 0.12 SER 1007 -0.44 HIS 1052

PRO 1025 0.10 ASN 1008 -0.39 HIS 1052

GLY 1003 0.13 LEU 1009 -0.34 HIS 1052

PHE 1133 0.10 ASN 1010 -0.31 HIS 1052

PHE 1133 0.12 LEU 1011 -0.26 HIS 1052

PHE 1133 0.17 LYS 1012 -0.22 HIS 1052

ARG 1018 0.16 PRO 1013 -0.17 HIS 1052

ASP 1134 0.18 GLY 1014 -0.12 HIS 1052

ASP 1134 0.21 GLU 1015 -0.15 HIS 1052

GLY 1003 0.22 LEU 1017 -0.20 HIS 1052

ALA 1001 0.29 ARG 1018 -0.18 HIS 1052

ALA 1001 0.35 VAL 1019 -0.22 HIS 1052

ALA 1001 0.47 ARG 1020 -0.21 VAL 1031

ALA 1001 0.58 GLY 1021 -0.29 ASP 1125

ALA 1001 0.67 GLU 1022 -0.37 ASP 1125

ALA 1001 0.49 VAL 1023 -0.19 VAL 1084

SER 1002 0.56 ALA 1024 -0.27 GLU 1022

SER 1002 0.61 PRO 1025 -0.23 GLN 1080

SER 1002 0.34 ASP 1026 -0.21 ASN 1056

PHE 1030 0.13 ALA 1027 -0.32 LYS 1127

PRO 1047 0.14 LYS 1028 -0.48 LYS 1127

ASN 1046 0.15 SER 1029 -0.68 GLY 1124

ASP 1125 0.20 PHE 1030 -0.50 LYS 1127

ASP 1125 0.19 VAL 1031 -0.42 HIS 1052

ALA 1024 0.15 LEU 1032 -0.38 HIS 1052

PRO 1025 0.12 ASN 1033 -0.46 HIS 1052

PRO 1025 0.09 LEU 1034 -0.40 HIS 1052

ILE 1089 0.08 GLY 1035 -0.43 SER 1002

ILE 1117 0.08 LYS 1036 -0.49 SER 1002

PRO 1025 0.06 ASP 1037 -0.66 SER 1002

LEU 1041 0.06 SER 1038 -0.95 SER 1002

ASN 1040 0.06 ASN 1039 -1.08 SER 1002

CYS 1042 0.07 ASN 1040 -0.78 SER 1002

LEU 1043 0.07 LEU 1041 -0.63 SER 1002

ASP 1064 0.09 CYS 1042 -0.47 SER 1002

TRP 1068 0.08 LEU 1043 -0.40 SER 1002

ALA 1024 0.08 HIS 1044 -0.49 SER 1002

ASP 1125 0.11 PHE 1045 -0.30 SER 1002

SER 1029 0.15 ASN 1046 -0.35 SER 1002

LYS 1028 0.14 PRO 1047 -0.25 LYS 1127

LYS 1028 0.13 ARG 1048 -0.49 GLY 1124

ASN 1050 0.28 PHE 1049 -0.35 GLY 1124

GLN 1080 0.29 ASN 1050 -0.63 ALA 1001

VAL 1076 0.25 ALA 1051 -0.97 ALA 1001

ALA 1075 0.34 HIS 1052 -1.44 ALA 1001

ALA 1075 0.47 GLY 1053 -1.26 ALA 1001

ALA 1075 0.46 ASP 1054 -0.81 ALA 1001

VAL 1076 0.44 ALA 1055 -0.56 ALA 1001

ALA 1055 0.38 ASN 1056 -0.32 THR 1057

ASP 1054 0.37 THR 1057 -0.34 ALA 1001

ASP 1054 0.24 ILE 1058 -0.27 ALA 1001

LYS 1028 0.09 VAL 1059 -0.43 ALA 1001

LYS 1028 0.08 CYS 1060 -0.41 SER 1002

ASP 1125 0.04 ASN 1061 -0.54 SER 1002

TRP 1068 0.11 SER 1062 -0.61 SER 1002

CYS 1042 0.09 LYS 1063 -0.83 SER 1002

ARG 1111 0.15 ASP 1064 -0.83 SER 1002

LEU 1112 0.17 ASP 1065 -0.98 SER 1002

ARG 1111 0.12 GLY 1066 -1.17 SER 1002

ARG 1111 0.16 ALA 1067 -1.09 ALA 1001

GLY 1069 0.11 TRP 1068 -0.92 ALA 1001

TRP 1068 0.11 GLY 1069 -0.73 ALA 1001

ILE 1089 0.05 THR 1070 -0.63 ALA 1001

LYS 1028 0.06 GLU 1071 -0.58 ALA 1001

HIS 1052 0.09 GLN 1072 -0.43 ALA 1001

LYS 1107 0.21 ARG 1073 -0.40 ALA 1001

ASP 1054 0.34 GLU 1074 -0.24 ALA 1001

GLY 1053 0.47 ALA 1075 -0.18 ALA 1001

ASP 1054 0.46 VAL 1076 -0.15 PRO 1025

ALA 1055 0.37 PHE 1077 -0.17 PRO 1081

ALA 1055 0.35 PRO 1078 -0.19 GLN 1080

VAL 1084 0.24 PHE 1079 -0.20 GLN 1080

ALA 1001 0.30 GLN 1080 -0.23 PRO 1025

ALA 1001 0.38 PRO 1081 -0.21 PRO 1025

ALA 1001 0.65 GLY 1082 -0.20 VAL 1084

ALA 1001 0.60 SER 1083 -0.19 GLY 1082

ALA 1001 0.57 VAL 1084 -0.25 ALA 1024

ALA 1001 0.44 ALA 1085 -0.17 SER 1083

ALA 1001 0.38 GLU 1086 -0.14 SER 1083

ALA 1001 0.24 VAL 1087 -0.11 VAL 1031

ALA 1001 0.21 CYS 1088 -0.10 VAL 1031

GLY 1003 0.17 ILE 1089 -0.10 HIS 1052

ARG 1018 0.20 THR 1090 -0.10 ASN 1033

ARG 1018 0.18 PHE 1091 -0.15 HIS 1052

ARG 1018 0.14 ASP 1092 -0.15 SER 1002

ASP 1092 0.14 GLN 1093 -0.23 SER 1002

ASP 1065 0.12 ALA 1094 -0.25 SER 1002

LEU 1112 0.12 ASN 1095 -0.24 SER 1002

CYS 1088 0.12 LEU 1096 -0.18 SER 1002

ARG 1073 0.15 THR 1097 -0.10 SER 1002

THR 1057 0.17 VAL 1098 -0.08 VAL 1031

ARG 1020 0.18 LYS 1099 -0.11 VAL 1031

ARG 1020 0.23 LEU 1100 -0.12 ASN 1046

ALA 1001 0.30 PRO 1101 -0.13 GLY 1082

ALA 1055 0.27 ASP 1102 -0.15 PRO 1025

LYS 1129 0.26 GLY 1103 -0.10 PRO 1025

ASP 1054 0.26 TYR 1104 -0.10 PRO 1025

ASP 1054 0.24 GLU 1105 -0.09 VAL 1031

ASP 1054 0.23 PHE 1106 -0.11 SER 1002

ARG 1073 0.21 LYS 1107 -0.18 SER 1002

ARG 1073 0.15 PHE 1108 -0.27 SER 1002

ASP 1064 0.10 PRO 1109 -0.33 SER 1002

LEU 1112 0.14 ASN 1110 -0.37 SER 1002

ALA 1067 0.16 ARG 1111 -0.46 SER 1002

ASP 1065 0.17 LEU 1112 -0.52 SER 1002

ASP 1065 0.15 ASN 1113 -0.41 SER 1002

ASP 1065 0.14 LEU 1114 -0.38 SER 1002

ASP 1065 0.10 GLU 1115 -0.29 HIS 1052

PHE 1133 0.10 ALA 1116 -0.31 HIS 1052

LEU 1017 0.09 ILE 1117 -0.34 HIS 1052

PRO 1025 0.09 ASN 1118 -0.40 HIS 1052

PRO 1025 0.11 TYR 1119 -0.45 HIS 1052

PRO 1025 0.13 MET 1120 -0.45 HIS 1052

PRO 1025 0.18 ALA 1121 -0.55 HIS 1052

PRO 1025 0.22 ALA 1122 -0.57 HIS 1052

ALA 1024 0.41 ASP 1123 -0.82 HIS 1052

ALA 1024 0.36 GLY 1124 -0.79 ALA 1051

GLY 1124 0.29 ASP 1125 -0.78 LYS 1127

SER 1002 0.40 PHE 1126 -0.53 LYS 1127

ALA 1001 0.70 LYS 1127 -0.78 ASP 1125

ALA 1001 0.60 ILE 1128 -0.41 HIS 1052

ALA 1001 0.71 LYS 1129 -0.37 ASP 1125

ALA 1001 0.60 CYS 1130 -0.31 HIS 1052

ALA 1001 0.46 VAL 1131 -0.28 HIS 1052

ALA 1001 0.40 ALA 1132 -0.23 HIS 1052

ALA 1001 0.29 PHE 1133 -0.22 HIS 1052

ALA 1001 0.29 ASP 1134 -0.17 HIS 1052

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.

*** opt_a_lac ***

CA distance fluctuations for 2406061849031399629

--- normal mode 10 ---

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

* opt_a_lac *