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

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CA distance fluctuations for 2404032043392226964

--- normal mode 9 ---

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
SER 1038 0.47 ALA 1001 -0.61 LYS 1129

SER 1038 0.54 SER 1002 -0.46 CYS 1130

ASP 1125 0.55 GLY 1003 -0.38 CYS 1130

LYS 1127 0.63 LEU 1004 -0.32 SER 1002

LYS 1127 0.49 VAL 1005 -0.28 ALA 1132

LYS 1127 0.56 ALA 1006 -0.19 ASP 1134

LYS 1127 0.49 SER 1007 -0.15 SER 1038

LYS 1129 0.60 ASN 1008 -0.35 ASP 1037

LYS 1129 0.55 LEU 1009 -0.13 ASP 1037

LYS 1129 0.53 ASN 1010 -0.18 LYS 1036

LYS 1129 0.42 LEU 1011 -0.12 GLU 1015

CYS 1130 0.36 LYS 1012 -0.14 GLY 1053

CYS 1130 0.25 PRO 1013 -0.18 ALA 1075

CYS 1130 0.21 GLY 1014 -0.14 ALA 1075

CYS 1130 0.27 GLU 1015 -0.12 LEU 1011

VAL 1019 0.25 LEU 1017 -0.17 ASP 1134

GLU 1015 0.26 ARG 1018 -0.24 ALA 1001

ASN 1010 0.31 VAL 1019 -0.29 ALA 1001

ASN 1010 0.35 ARG 1020 -0.39 ALA 1001

ASN 1008 0.42 GLY 1021 -0.43 ALA 1001

ASN 1008 0.43 GLU 1022 -0.32 ALA 1001

LEU 1004 0.41 VAL 1023 -0.16 ASP 1102

LEU 1004 0.57 ALA 1024 -0.17 PRO 1078

LEU 1004 0.56 PRO 1025 -0.31 GLN 1080

GLY 1003 0.50 ASP 1026 -0.36 ASN 1056

GLY 1003 0.39 ALA 1027 -0.17 THR 1057

ALA 1001 0.35 LYS 1028 -0.22 TRP 1068

ALA 1001 0.30 SER 1029 -0.19 TRP 1068

ALA 1006 0.19 PHE 1030 -0.09 TRP 1068

ASP 1125 0.16 VAL 1031 -0.10 CYS 1130

ASP 1125 0.23 LEU 1032 -0.10 HIS 1052

SER 1002 0.23 ASN 1033 -0.18 HIS 1052

ASP 1125 0.23 LEU 1034 -0.18 HIS 1052

SER 1002 0.27 GLY 1035 -0.24 HIS 1052

SER 1002 0.33 LYS 1036 -0.29 ASN 1008

SER 1002 0.42 ASP 1037 -0.35 ASN 1008

SER 1002 0.54 SER 1038 -0.25 ASN 1008

SER 1002 0.46 ASN 1039 -0.33 HIS 1052

SER 1002 0.37 ASN 1040 -0.33 HIS 1052

SER 1002 0.32 LEU 1041 -0.31 HIS 1052

SER 1002 0.25 CYS 1042 -0.29 GLY 1053

SER 1002 0.21 LEU 1043 -0.23 GLY 1053

ALA 1001 0.25 HIS 1044 -0.24 HIS 1052

ALA 1001 0.15 PHE 1045 -0.13 HIS 1052

ALA 1001 0.21 ASN 1046 -0.13 TRP 1068

ALA 1001 0.15 PRO 1047 -0.18 TRP 1068

ALA 1001 0.26 ARG 1048 -0.26 TRP 1068

ALA 1001 0.23 PHE 1049 -0.32 ASP 1026

ALA 1001 0.30 ASN 1050 -0.36 TRP 1068

ALA 1001 0.35 ALA 1051 -0.43 TRP 1068

ALA 1001 0.32 HIS 1052 -0.64 TRP 1068

VAL 1076 0.27 GLY 1053 -0.62 TRP 1068

VAL 1076 0.29 ASP 1054 -0.43 TRP 1068

GLY 1053 0.24 ALA 1055 -0.38 THR 1070

ALA 1055 0.23 ASN 1056 -0.38 THR 1057

VAL 1076 0.25 THR 1057 -0.38 ASN 1056

ALA 1001 0.16 ILE 1058 -0.23 ASP 1026

ALA 1001 0.23 VAL 1059 -0.26 CYS 1060

ALA 1001 0.21 CYS 1060 -0.26 VAL 1059

ALA 1001 0.26 ASN 1061 -0.37 GLY 1053

ALA 1001 0.27 SER 1062 -0.41 GLY 1053

ALA 1001 0.32 LYS 1063 -0.45 HIS 1052

ALA 1001 0.32 ASP 1064 -0.45 GLY 1053

SER 1002 0.36 ASP 1065 -0.40 GLY 1053

ALA 1001 0.40 GLY 1066 -0.45 HIS 1052

ALA 1001 0.33 ALA 1067 -0.59 HIS 1052

ALA 1001 0.32 TRP 1068 -0.64 HIS 1052

ALA 1001 0.28 GLY 1069 -0.57 GLY 1053

ALA 1001 0.28 THR 1070 -0.56 GLY 1053

ALA 1001 0.30 GLU 1071 -0.43 GLY 1053

ALA 1001 0.23 GLN 1072 -0.32 ASN 1056

ALA 1001 0.20 ARG 1073 -0.31 ASN 1056

GLU 1105 0.15 GLU 1074 -0.29 PRO 1109

ASP 1054 0.29 ALA 1075 -0.34 LYS 1107

ASP 1054 0.29 VAL 1076 -0.28 LYS 1107

GLY 1053 0.21 PHE 1077 -0.30 ASP 1026

ASN 1056 0.21 PRO 1078 -0.31 GLN 1080

GLU 1086 0.21 PHE 1079 -0.26 PRO 1081

LEU 1004 0.24 GLN 1080 -0.31 PRO 1025

LEU 1004 0.35 PRO 1081 -0.31 PRO 1025

LEU 1004 0.38 GLY 1082 -0.27 PRO 1078

ASN 1008 0.32 SER 1083 -0.31 ASP 1102

ASN 1008 0.33 VAL 1084 -0.36 ASP 1102

ASN 1008 0.26 ALA 1085 -0.29 PRO 1101

ASN 1010 0.22 GLU 1086 -0.27 ALA 1001

ASN 1010 0.15 VAL 1087 -0.19 ALA 1001

GLU 1015 0.14 CYS 1088 -0.17 GLY 1003

ALA 1024 0.11 ILE 1089 -0.12 VAL 1005

CYS 1088 0.12 THR 1090 -0.10 VAL 1005

LYS 1129 0.17 PHE 1091 -0.17 ALA 1075

CYS 1130 0.15 ASP 1092 -0.23 ALA 1075

CYS 1130 0.18 GLN 1093 -0.27 ALA 1075

LEU 1112 0.16 ALA 1094 -0.34 ALA 1075

ARG 1111 0.13 ASN 1095 -0.31 ALA 1075

PRO 1109 0.09 LEU 1096 -0.20 ALA 1075

PHE 1108 0.12 THR 1097 -0.17 ALA 1075

THR 1070 0.10 VAL 1098 -0.11 VAL 1084

ASP 1054 0.10 LYS 1099 -0.17 VAL 1084

ASP 1054 0.12 LEU 1100 -0.24 VAL 1084

ASN 1056 0.15 PRO 1101 -0.33 VAL 1084

ALA 1055 0.16 ASP 1102 -0.36 VAL 1084

ASP 1054 0.15 GLY 1103 -0.30 VAL 1084

ASP 1054 0.17 TYR 1104 -0.24 VAL 1084

ARG 1073 0.16 GLU 1105 -0.21 VAL 1084

THR 1070 0.15 PHE 1106 -0.26 LYS 1107

PHE 1108 0.18 LYS 1107 -0.34 ALA 1075

LYS 1107 0.18 PHE 1108 -0.28 ALA 1075

SER 1002 0.16 PRO 1109 -0.31 ALA 1075

SER 1002 0.19 ASN 1110 -0.31 GLY 1053

SER 1002 0.23 ARG 1111 -0.40 ASN 1113

SER 1002 0.25 LEU 1112 -0.37 GLY 1053

SER 1002 0.24 ASN 1113 -0.40 ARG 1111

LYS 1129 0.23 LEU 1114 -0.28 GLY 1053

LYS 1129 0.30 GLU 1115 -0.27 ARG 1111

LYS 1129 0.35 ALA 1116 -0.20 GLY 1053

LYS 1129 0.35 ILE 1117 -0.18 HIS 1052

LYS 1129 0.42 ASN 1118 -0.19 ASN 1008

LYS 1127 0.38 TYR 1119 -0.16 HIS 1052

LYS 1127 0.37 MET 1120 -0.16 ASP 1134

ASP 1125 0.37 ALA 1121 -0.17 ALA 1132

ASP 1125 0.42 ALA 1122 -0.14 ALA 1132

ASP 1125 0.33 ASP 1123 -0.26 ILE 1128

GLY 1003 0.28 GLY 1124 -0.20 LYS 1127

GLY 1003 0.55 ASP 1125 -0.10 GLU 1022

LEU 1004 0.43 PHE 1126 -0.22 ALA 1001

LEU 1004 0.63 LYS 1127 -0.51 ALA 1001

ASN 1008 0.48 ILE 1128 -0.59 ALA 1001

ASN 1008 0.60 LYS 1129 -0.61 ALA 1001

ASN 1008 0.52 CYS 1130 -0.55 ALA 1001

ASN 1010 0.46 VAL 1131 -0.35 ALA 1001

PHE 1133 0.50 ALA 1132 -0.30 ALA 1001

ALA 1132 0.50 PHE 1133 -0.25 ASP 1134

PRO 1025 0.23 ASP 1134 -0.25 PHE 1133

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 ***

CA distance fluctuations for 2404032043392226964

--- normal mode 9 ---

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

* opt_a *