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

* 552ET3RZE *

CA strain for 22040500350481584

--- normal mode 9 ---

This graph displays the distance variation between successive pairs of CA atoms in the two extreme conformations that were computed for this mode (DQMIN/DQMAX). Large distance variations can be an indicator for residue pairs that support the important strain in that particular normal mode movement. Note that residue pairs between chain breaks or at flexible ends of the protein may also exhibit large CA-CA distance variations. If more than one residues ae grouped together into a rigid block (NRBL>1), CA-CA distance variations between CA atoms in the same block will be very low.

This feature is still experimental and will be further developped in the future.

CA i CA i+1 vari
MET 28 PRO 29 -0.0003

PRO 29 LEU 30 -0.0001

LEU 30 VAL 31 0.0003

VAL 31 VAL 32 0.0002

VAL 32 VAL 33 -0.0002

VAL 33 LEU 34 0.0001

LEU 34 SER 35 -0.0004

SER 35 THR 36 -0.0005

THR 36 ILE 37 0.0016

ILE 37 CYS 38 0.0003

CYS 38 LEU 39 -0.0001

LEU 39 VAL 40 0.0023

VAL 40 THR 41 0.0001

THR 41 VAL 42 -0.0001

VAL 42 GLY 43 0.0077

GLY 43 LEU 44 -0.0000

LEU 44 ASN 45 0.0002

ASN 45 LEU 46 -0.0040

LEU 46 LEU 47 -0.0001

LEU 47 VAL 48 -0.0001

VAL 48 LEU 49 0.0007

LEU 49 TYR 50 -0.0001

TYR 50 ALA 51 0.0001

ALA 51 VAL 52 -0.0047

VAL 52 ARG 53 -0.0000

ARG 53 SER 54 0.0004

SER 54 GLU 55 0.0036

GLU 55 ARG 56 0.0001

ARG 56 LYS 57 -0.0001

LYS 57 LEU 58 -0.0033

LEU 58 HIS 59 -0.0003

HIS 59 THR 60 -0.0002

THR 60 VAL 61 -0.0173

VAL 61 GLY 62 0.0001

GLY 62 ASN 63 -0.0001

ASN 63 LEU 64 0.0074

LEU 64 TYR 65 -0.0001

TYR 65 ILE 66 0.0003

ILE 66 VAL 67 0.0041

VAL 67 SER 68 0.0003

SER 68 LEU 69 -0.0002

LEU 69 SER 70 -0.0024

SER 70 VAL 71 -0.0001

VAL 71 ALA 72 -0.0002

ALA 72 ASP 73 -0.0007

ASP 73 LEU 74 0.0001

LEU 74 ILE 75 -0.0002

ILE 75 VAL 76 0.0013

VAL 76 GLY 77 0.0000

GLY 77 ALA 78 0.0001

ALA 78 VAL 79 0.0059

VAL 79 VAL 80 0.0001

VAL 80 MET 81 -0.0001

MET 81 PRO 82 -0.0001

PRO 82 MET 83 0.0002

MET 83 ASN 84 0.0003

ASN 84 ILE 85 -0.0005

ILE 85 LEU 86 -0.0002

LEU 86 TYR 87 0.0002

TYR 87 LEU 88 -0.0003

LEU 88 LEU 89 -0.0003

LEU 89 MET 90 -0.0001

MET 90 SER 91 0.0008

SER 91 LYS 92 0.0001

LYS 92 TRP 93 -0.0000

TRP 93 SER 94 -0.0009

SER 94 LEU 95 -0.0004

LEU 95 GLY 96 0.0004

GLY 96 ARG 97 -0.0009

ARG 97 PRO 98 -0.0001

PRO 98 LEU 99 0.0001

LEU 99 CYS 100 -0.0008

CYS 100 LEU 101 0.0001

LEU 101 PHE 102 -0.0003

PHE 102 TRP 103 -0.0008

TRP 103 LEU 104 0.0001

LEU 104 SER 105 -0.0001

SER 105 MET 106 0.0040

MET 106 ASP 107 0.0000

ASP 107 TYR 108 -0.0001

TYR 108 VAL 109 0.0058

VAL 109 ALA 110 0.0002

ALA 110 SER 111 0.0003

SER 111 THR 112 0.0010

THR 112 ALA 113 -0.0001

ALA 113 SER 114 0.0002

SER 114 ILE 115 -0.0043

ILE 115 PHE 116 0.0004

PHE 116 SER 117 0.0001

SER 117 VAL 118 -0.0010

VAL 118 PHE 119 0.0004

PHE 119 ILE 120 0.0002

ILE 120 LEU 121 0.0107

LEU 121 CYS 122 -0.0000

CYS 122 ILE 123 -0.0001

ILE 123 ASP 124 0.0147

ASP 124 ARG 125 0.0000

ARG 125 TYR 126 0.0003

TYR 126 ARG 127 -0.0314

ARG 127 SER 128 0.0001

SER 128 VAL 129 0.0001

VAL 129 GLN 130 0.0081

GLN 130 GLN 131 0.0003

GLN 131 PRO 132 -0.0001

PRO 132 LEU 133 0.0200

LEU 133 ARG 134 0.0001

ARG 134 TYR 135 -0.0000

TYR 135 LEU 136 0.0106

LEU 136 LYS 137 -0.0001

LYS 137 TYR 138 -0.0001

TYR 138 ARG 139 -0.0096

ARG 139 THR 140 0.0003

THR 140 LYS 141 -0.0002

LYS 141 THR 142 0.0054

THR 142 ARG 143 0.0003

ARG 143 ALA 144 -0.0003

ALA 144 SER 145 0.0044

SER 145 ALA 146 -0.0001

ALA 146 THR 147 -0.0003

THR 147 ILE 148 0.0078

ILE 148 LEU 149 0.0003

LEU 149 GLY 150 -0.0001

GLY 150 ALA 151 -0.0086

ALA 151 TRP 152 -0.0000

TRP 152 PHE 153 0.0003

PHE 153 LEU 154 0.0014

LEU 154 SER 155 0.0000

SER 155 PHE 156 0.0001

PHE 156 LEU 157 0.0018

LEU 157 TRP 158 -0.0002

TRP 158 VAL 159 0.0002

VAL 159 ILE 160 0.0016

ILE 160 PRO 161 -0.0001

PRO 161 ILE 162 -0.0001

ILE 162 LEU 163 -0.0006

LEU 163 GLY 164 0.0000

GLY 164 TRP 165 -0.0001

TRP 165 ASN 166 -0.0021

ASN 166 HIS 167 0.0001

HIS 167 ARG 175 0.0009

ARG 175 ARG 176 -0.0003

ARG 176 GLU 177 0.0003

GLU 177 ASP 178 -0.0009

ASP 178 LYS 179 -0.0000

LYS 179 CYS 180 -0.0001

CYS 180 GLU 181 -0.0015

GLU 181 THR 182 0.0000

THR 182 ASP 183 -0.0002

ASP 183 PHE 184 -0.0047

PHE 184 TYR 185 -0.0001

TYR 185 ASP 186 -0.0004

ASP 186 VAL 187 -0.0056

VAL 187 THR 188 0.0001

THR 188 TRP 189 -0.0002

TRP 189 PHE 190 0.0053

PHE 190 LYS 191 0.0002

LYS 191 VAL 192 0.0001

VAL 192 MET 193 0.0028

MET 193 THR 194 0.0001

THR 194 ALA 195 -0.0003

ALA 195 ILE 196 -0.0013

ILE 196 ILE 197 0.0001

ILE 197 ASN 198 0.0001

ASN 198 PHE 199 -0.0033

PHE 199 TYR 200 -0.0002

TYR 200 LEU 201 0.0001

LEU 201 PRO 202 0.0026

PRO 202 THR 203 0.0001

THR 203 LEU 204 0.0005

LEU 204 LEU 205 0.0104

LEU 205 MET 206 -0.0001

MET 206 LEU 207 -0.0001

LEU 207 TRP 208 0.0026

TRP 208 PHE 209 0.0001

PHE 209 TYR 210 0.0000

TYR 210 ALA 211 -0.0062

ALA 211 LYS 212 -0.0001

LYS 212 ILE 213 -0.0003

ILE 213 TYR 214 -0.0284

TYR 214 LYS 215 0.0000

LYS 215 ALA 216 0.0003

ALA 216 VAL 217 -0.0493

VAL 217 ARG 218 -0.0000

ARG 218 GLN 219 0.0001

GLN 219 HIS 220 -0.0363

HIS 220 CYS 221 -0.0001

CYS 221 ASN 1002 -0.0393

ASN 1002 ILE 1003 -0.0003

ILE 1003 PHE 1004 0.0002

PHE 1004 GLU 1005 -0.0053

GLU 1005 MET 1006 -0.0000

MET 1006 LEU 1007 -0.0003

LEU 1007 ARG 1008 0.0102

ARG 1008 ILE 1009 -0.0002

ILE 1009 ASP 1010 0.0003

ASP 1010 GLU 1011 0.0263

GLU 1011 GLY 1012 -0.0001

GLY 1012 LEU 1013 -0.0002

LEU 1013 ARG 1014 -0.0007

ARG 1014 LEU 1015 0.0002

LEU 1015 LYS 1016 0.0001

LYS 1016 ILE 1017 -0.0043

ILE 1017 TYR 1018 -0.0001

TYR 1018 LYS 1019 0.0001

LYS 1019 ASP 1020 -0.0002

ASP 1020 THR 1021 -0.0002

THR 1021 GLU 1022 0.0001

GLU 1022 GLY 1023 -0.0017

GLY 1023 TYR 1024 -0.0003

TYR 1024 TYR 1025 0.0003

TYR 1025 THR 1026 0.0019

THR 1026 ILE 1027 -0.0001

ILE 1027 GLY 1028 0.0001

GLY 1028 ILE 1029 0.0056

ILE 1029 GLY 1030 0.0002

GLY 1030 HIS 1031 0.0003

HIS 1031 LEU 1032 0.0043

LEU 1032 LEU 1033 -0.0001

LEU 1033 THR 1034 -0.0002

THR 1034 LYS 1035 0.0020

LYS 1035 SER 1036 -0.0001

SER 1036 PRO 1037 -0.0001

PRO 1037 SER 1038 0.0008

SER 1038 LEU 1039 -0.0003

LEU 1039 ASN 1040 -0.0003

ASN 1040 ALA 1041 0.0016

ALA 1041 ALA 1042 0.0000

ALA 1042 LYS 1043 -0.0002

LYS 1043 SER 1044 0.0011

SER 1044 GLU 1045 -0.0003

GLU 1045 LEU 1046 -0.0005

LEU 1046 ASP 1047 0.0013

ASP 1047 LYS 1048 0.0001

LYS 1048 ALA 1049 -0.0003

ALA 1049 ILE 1050 -0.0004

ILE 1050 GLY 1051 0.0001

GLY 1051 ARG 1052 0.0002

ARG 1052 ASN 1053 0.0026

ASN 1053 THR 1054 0.0000

THR 1054 ASN 1055 -0.0001

ASN 1055 GLY 1056 0.0021

GLY 1056 VAL 1057 -0.0004

VAL 1057 ILE 1058 0.0000

ILE 1058 THR 1059 -0.0074

THR 1059 LYS 1060 0.0000

LYS 1060 ASP 1061 -0.0001

ASP 1061 GLU 1062 -0.0040

GLU 1062 ALA 1063 -0.0000

ALA 1063 GLU 1064 -0.0003

GLU 1064 LYS 1065 -0.0094

LYS 1065 LEU 1066 -0.0003

LEU 1066 PHE 1067 -0.0003

PHE 1067 ASN 1068 0.0052

ASN 1068 GLN 1069 0.0002

GLN 1069 ASP 1070 0.0005

ASP 1070 VAL 1071 0.0064

VAL 1071 ASP 1072 -0.0001

ASP 1072 ALA 1073 0.0001

ALA 1073 ALA 1074 0.0079

ALA 1074 VAL 1075 -0.0000

VAL 1075 ARG 1076 0.0003

ARG 1076 GLY 1077 -0.0008

GLY 1077 ILE 1078 -0.0001

ILE 1078 LEU 1079 0.0003

LEU 1079 ARG 1080 0.0004

ARG 1080 ASN 1081 0.0001

ASN 1081 ALA 1082 -0.0001

ALA 1082 LYS 1083 0.0004

LYS 1083 LEU 1084 -0.0001

LEU 1084 LYS 1085 -0.0000

LYS 1085 PRO 1086 0.0014

PRO 1086 VAL 1087 -0.0004

VAL 1087 TYR 1088 0.0002

TYR 1088 ASP 1089 0.0001

ASP 1089 SER 1090 0.0002

SER 1090 LEU 1091 -0.0001

LEU 1091 ASP 1092 -0.0024

ASP 1092 ALA 1093 0.0003

ALA 1093 VAL 1094 -0.0002

VAL 1094 ARG 1095 -0.0041

ARG 1095 ARG 1096 0.0001

ARG 1096 ALA 1097 -0.0000

ALA 1097 ALA 1098 -0.0112

ALA 1098 LEU 1099 -0.0003

LEU 1099 ILE 1100 -0.0001

ILE 1100 ASN 1101 0.0042

ASN 1101 MET 1102 -0.0003

MET 1102 VAL 1103 -0.0002

VAL 1103 PHE 1104 0.0051

PHE 1104 GLN 1105 -0.0002

GLN 1105 MET 1106 -0.0001

MET 1106 GLY 1107 0.0083

GLY 1107 GLU 1108 0.0004

GLU 1108 THR 1109 0.0003

THR 1109 GLY 1110 0.0008

GLY 1110 VAL 1111 -0.0000

VAL 1111 ALA 1112 0.0002

ALA 1112 GLY 1113 -0.0005

GLY 1113 PHE 1114 -0.0002

PHE 1114 THR 1115 -0.0001

THR 1115 ASN 1116 0.0018

ASN 1116 SER 1117 0.0003

SER 1117 LEU 1118 -0.0004

LEU 1118 ARG 1119 -0.0009

ARG 1119 MET 1120 0.0000

MET 1120 LEU 1121 -0.0001

LEU 1121 GLN 1122 0.0022

GLN 1122 GLN 1123 -0.0002

GLN 1123 LYS 1124 0.0001

LYS 1124 ARG 1125 0.0006

ARG 1125 TRP 1126 -0.0001

TRP 1126 ASP 1127 0.0002

ASP 1127 GLU 1128 0.0004

GLU 1128 ALA 1129 -0.0002

ALA 1129 ALA 1130 0.0002

ALA 1130 VAL 1131 0.0009

VAL 1131 ASN 1132 -0.0005

ASN 1132 LEU 1133 0.0002

LEU 1133 ALA 1134 -0.0002

ALA 1134 LYS 1135 0.0002

LYS 1135 SER 1136 0.0001

SER 1136 ARG 1137 -0.0023

ARG 1137 TRP 1138 -0.0003

TRP 1138 TYR 1139 -0.0000

TYR 1139 ASN 1140 -0.0002

ASN 1140 GLN 1141 -0.0001

GLN 1141 THR 1142 -0.0003

THR 1142 PRO 1143 0.0032

PRO 1143 ASN 1144 0.0002

ASN 1144 ARG 1145 0.0004

ARG 1145 ALA 1146 -0.0045

ALA 1146 LYS 1147 -0.0001

LYS 1147 ARG 1148 -0.0003

ARG 1148 VAL 1149 0.0047

VAL 1149 ILE 1150 0.0003

ILE 1150 THR 1151 -0.0001

THR 1151 THR 1152 -0.0085

THR 1152 PHE 1153 0.0003

PHE 1153 ARG 1154 0.0000

ARG 1154 THR 1155 0.0040

THR 1155 GLY 1156 0.0001

GLY 1156 THR 1157 -0.0000

THR 1157 TRP 1158 -0.0057

TRP 1158 ASP 1159 -0.0000

ASP 1159 ALA 1160 -0.0003

ALA 1160 TYR 1161 0.0009

TYR 1161 LEU 405 0.0695

LEU 405 HIS 406 0.0002

HIS 406 MET 407 0.0002

MET 407 ASN 408 -0.0434

ASN 408 ARG 409 -0.0000

ARG 409 GLU 410 -0.0002

GLU 410 ARG 411 -0.0073

ARG 411 LYS 412 -0.0003

LYS 412 ALA 413 -0.0002

ALA 413 ALA 414 0.0178

ALA 414 LYS 415 0.0003

LYS 415 GLN 416 -0.0001

GLN 416 LEU 417 -0.0065

LEU 417 GLY 418 0.0001

GLY 418 PHE 419 0.0000

PHE 419 ILE 420 -0.0110

ILE 420 MET 421 -0.0002

MET 421 ALA 422 -0.0002

ALA 422 ALA 423 0.0061

ALA 423 PHE 424 0.0000

PHE 424 ILE 425 -0.0000

ILE 425 LEU 426 0.0107

LEU 426 CYS 427 0.0002

CYS 427 TRP 428 -0.0000

TRP 428 ILE 429 0.0023

ILE 429 PRO 430 -0.0001

PRO 430 TYR 431 -0.0002

TYR 431 PHE 432 0.0004

PHE 432 ILE 433 0.0002

ILE 433 PHE 434 0.0000

PHE 434 PHE 435 -0.0013

PHE 435 MET 436 0.0002

MET 436 VAL 437 0.0000

VAL 437 ILE 438 -0.0009

ILE 438 ALA 439 0.0001

ALA 439 PHE 440 -0.0001

PHE 440 CYS 441 0.0020

CYS 441 LYS 442 0.0002

LYS 442 ASN 443 0.0001

ASN 443 CYS 444 0.0009

CYS 444 CYS 445 -0.0001

CYS 445 ASN 446 -0.0002

ASN 446 GLU 447 0.0016

GLU 447 HIS 448 -0.0000

HIS 448 LEU 449 -0.0004

LEU 449 HIS 450 0.0004

HIS 450 MET 451 0.0002

MET 451 PHE 452 0.0003

PHE 452 THR 453 0.0020

THR 453 ILE 454 -0.0003

ILE 454 TRP 455 0.0002

TRP 455 LEU 456 -0.0005

LEU 456 GLY 457 0.0000

GLY 457 TYR 458 0.0001

TYR 458 ILE 459 -0.0004

ILE 459 ASN 460 -0.0002

ASN 460 SER 461 0.0000

SER 461 THR 462 0.0015

THR 462 LEU 463 0.0004

LEU 463 ASN 464 -0.0001

ASN 464 PRO 465 -0.0036

PRO 465 LEU 466 0.0004

LEU 466 ILE 467 -0.0001

ILE 467 TYR 468 -0.0052

TYR 468 PRO 469 -0.0004

PRO 469 LEU 470 0.0003

LEU 470 CYS 471 -0.0032

CYS 471 ASN 472 -0.0000

ASN 472 GLU 473 0.0000

GLU 473 ASN 474 0.0209

ASN 474 PHE 475 -0.0002

PHE 475 LYS 476 -0.0001

LYS 476 LYS 477 -0.0030

LYS 477 THR 478 -0.0000

THR 478 PHE 479 -0.0002

PHE 479 LYS 480 -0.0015

LYS 480 ARG 481 -0.0001

ARG 481 ILE 482 -0.0002

ILE 482 LEU 483 -0.0053

LEU 483 HIS 484 -0.0003

HIS 484 ILE 485 -0.0000

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: October 18th, 2018.

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

*** 552ET3RZE ***

CA strain for 22040500350481584

--- normal mode 9 ---

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

* 552ET3RZE *