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

* Angio *

CA strain for 2404051739442459575

--- normal mode 7 ---

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
CYS 35 SER 36 -0.0003

SER 36 GLN 37 0.0003

GLN 37 LYS 38 0.0001

LYS 38 PRO 39 0.0004

PRO 39 SER 40 -0.0005

SER 40 ASP 41 0.0013

ASP 41 LYS 42 -0.0001

LYS 42 HIS 43 -0.0004

HIS 43 LEU 44 -0.0002

LEU 44 ASP 45 0.0011

ASP 45 ALA 46 0.0000

ALA 46 ILE 47 0.0000

ILE 47 PRO 48 -0.0001

PRO 48 ILE 49 -0.0003

ILE 49 LEU 50 -0.0002

LEU 50 TYR 51 0.0008

TYR 51 TYR 52 -0.0001

TYR 52 ILE 53 0.0005

ILE 53 ILE 54 0.0004

ILE 54 PHE 55 0.0011

PHE 55 VAL 56 0.0003

VAL 56 ILE 57 -0.0053

ILE 57 GLY 58 -0.0000

GLY 58 PHE 59 0.0002

PHE 59 LEU 60 -0.0001

LEU 60 VAL 61 -0.0057

VAL 61 ASN 62 0.0001

ASN 62 ILE 63 0.0012

ILE 63 VAL 64 -0.0002

VAL 64 VAL 65 -0.0016

VAL 65 VAL 66 0.0002

VAL 66 THR 67 -0.0008

THR 67 LEU 68 -0.0005

LEU 68 PHE 69 -0.0037

PHE 69 CYS 70 0.0001

CYS 70 CYS 71 0.0007

CYS 71 GLN 72 0.0004

GLN 72 LYS 73 0.0070

LYS 73 GLY 74 -0.0001

GLY 74 PRO 75 0.0115

PRO 75 LYS 76 -0.0001

LYS 76 LYS 77 -0.0176

LYS 77 VAL 78 -0.0001

VAL 78 SER 79 0.0025

SER 79 SER 80 0.0001

SER 80 ILE 81 -0.0048

ILE 81 TYR 82 -0.0001

TYR 82 ILE 83 -0.0010

ILE 83 PHE 84 -0.0002

PHE 84 ASN 85 -0.0045

ASN 85 LEU 86 -0.0002

LEU 86 ALA 87 0.0048

ALA 87 VAL 88 0.0001

VAL 88 ALA 89 -0.0048

ALA 89 ASP 90 0.0003

ASP 90 LEU 91 0.0028

LEU 91 LEU 92 -0.0001

LEU 92 LEU 93 -0.0001

LEU 93 LEU 94 0.0002

LEU 94 ALA 95 -0.0031

ALA 95 THR 96 0.0000

THR 96 LEU 97 0.0021

LEU 97 PRO 98 0.0001

PRO 98 LEU 99 -0.0062

LEU 99 TRP 100 0.0001

TRP 100 ALA 101 0.0027

ALA 101 THR 102 -0.0002

THR 102 TYR 103 -0.0012

TYR 103 TYR 104 0.0002

TYR 104 SER 105 0.0016

SER 105 TYR 106 -0.0002

TYR 106 ARG 107 0.0001

ARG 107 TYR 108 0.0000

TYR 108 ASP 109 0.0027

ASP 109 TRP 110 0.0003

TRP 110 LEU 111 -0.0011

LEU 111 PHE 112 0.0004

PHE 112 GLY 113 0.0011

GLY 113 PRO 114 0.0003

PRO 114 VAL 115 -0.0007

VAL 115 MET 116 0.0000

MET 116 CYS 117 -0.0000

CYS 117 LYS 118 0.0000

LYS 118 VAL 119 -0.0034

VAL 119 PHE 120 -0.0003

PHE 120 GLY 121 0.0028

GLY 121 SER 122 -0.0001

SER 122 PHE 123 -0.0055

PHE 123 LEU 124 0.0002

LEU 124 THR 125 0.0035

THR 125 LEU 126 -0.0002

LEU 126 ASN 127 -0.0061

ASN 127 MET 128 -0.0002

MET 128 PHE 129 0.0032

PHE 129 ALA 130 0.0002

ALA 130 SER 131 -0.0027

SER 131 ILE 132 -0.0000

ILE 132 PHE 133 0.0010

PHE 133 PHE 134 -0.0001

PHE 134 ILE 135 -0.0041

ILE 135 THR 136 0.0005

THR 136 CYS 137 -0.0017

CYS 137 MET 138 0.0001

MET 138 SER 139 0.0001

SER 139 VAL 140 -0.0001

VAL 140 ASP 141 -0.0085

ASP 141 ARG 142 -0.0000

ARG 142 TYR 143 -0.0453

TYR 143 GLN 144 -0.0001

GLN 144 SER 145 0.0014

SER 145 VAL 146 -0.0000

VAL 146 ILE 147 -0.0036

ILE 147 TYR 148 -0.0000

TYR 148 PRO 149 0.0059

PRO 149 PHE 150 0.0002

PHE 150 LEU 151 0.0175

LEU 151 SER 152 0.0004

SER 152 GLN 153 0.0030

GLN 153 ARG 154 0.0004

ARG 154 ARG 155 -0.0020

ARG 155 ASN 156 -0.0003

ASN 156 PRO 157 -0.0021

PRO 157 TRP 158 0.0000

TRP 158 GLN 159 -0.0013

GLN 159 ALA 160 -0.0002

ALA 160 SER 161 0.0057

SER 161 TYR 162 -0.0002

TYR 162 ILE 163 -0.0055

ILE 163 VAL 164 0.0000

VAL 164 PRO 165 0.0009

PRO 165 LEU 166 0.0000

LEU 166 VAL 167 0.0094

VAL 167 TRP 168 -0.0001

TRP 168 CYS 169 -0.0029

CYS 169 MET 170 0.0000

MET 170 ALA 171 0.0025

ALA 171 CYS 172 -0.0000

CYS 172 LEU 173 -0.0018

LEU 173 SER 174 -0.0001

SER 174 SER 175 0.0028

SER 175 LEU 176 -0.0004

LEU 176 PRO 177 -0.0007

PRO 177 THR 178 -0.0004

THR 178 PHE 179 -0.0001

PHE 179 TYR 180 0.0001

TYR 180 PHE 181 0.0011

PHE 181 ARG 182 0.0001

ARG 182 ASP 183 0.0028

ASP 183 VAL 184 -0.0001

VAL 184 ARG 185 -0.0003

ARG 185 THR 186 -0.0002

THR 186 ILE 187 -0.0011

ILE 187 GLU 188 0.0003

GLU 188 TYR 189 0.0001

TYR 189 LEU 190 0.0002

LEU 190 GLY 191 -0.0003

GLY 191 VAL 192 0.0000

VAL 192 ASN 193 -0.0003

ASN 193 ALA 194 0.0002

ALA 194 CYS 195 0.0032

CYS 195 ILE 196 0.0000

ILE 196 MET 197 0.0039

MET 197 ALA 198 0.0001

ALA 198 PHE 199 -0.0027

PHE 199 PRO 200 -0.0002

PRO 200 PRO 201 0.0003

PRO 201 GLU 202 -0.0003

GLU 202 LYS 203 0.0008

LYS 203 TYR 204 0.0001

TYR 204 ALA 205 0.0002

ALA 205 GLN 206 0.0003

GLN 206 TRP 207 -0.0020

TRP 207 SER 208 0.0001

SER 208 ALA 209 0.0024

ALA 209 GLY 210 0.0004

GLY 210 ILE 211 -0.0007

ILE 211 ALA 212 0.0003

ALA 212 LEU 213 0.0008

LEU 213 MET 214 -0.0001

MET 214 LYS 215 -0.0039

LYS 215 ASN 216 -0.0000

ASN 216 ILE 217 0.0064

ILE 217 LEU 218 0.0001

LEU 218 GLY 219 -0.0057

GLY 219 PHE 220 0.0002

PHE 220 ILE 221 0.0040

ILE 221 ILE 222 0.0001

ILE 222 PRO 223 0.0002

PRO 223 LEU 224 0.0001

LEU 224 ILE 225 0.0039

ILE 225 PHE 226 0.0004

PHE 226 ILE 227 -0.0057

ILE 227 ALA 228 0.0001

ALA 228 THR 229 0.0029

THR 229 CYS 230 -0.0001

CYS 230 TYR 231 -0.0006

TYR 231 PHE 232 -0.0003

PHE 232 GLY 233 -0.0202

GLY 233 ILE 234 0.0002

ILE 234 ARG 235 -0.0011

ARG 235 LYS 236 0.0003

LYS 236 HIS 237 0.0117

HIS 237 LEU 238 0.0000

LEU 238 LEU 239 -0.0093

LEU 239 LYS 240 -0.0001

LYS 240 THR 241 0.0115

THR 241 ASN 242 -0.0003

ASN 242 ALA 1001 -0.0106

ALA 1001 ASP 1002 -0.0001

ASP 1002 LEU 1003 0.0035

LEU 1003 GLU 1004 -0.0000

GLU 1004 ASP 1005 -0.0148

ASP 1005 ASN 1006 0.0004

ASN 1006 TRP 1007 0.0116

TRP 1007 GLU 1008 -0.0001

GLU 1008 THR 1009 -0.0112

THR 1009 LEU 1010 -0.0002

LEU 1010 ASN 1011 0.0002

ASN 1011 ASP 1012 0.0002

ASP 1012 ASN 1013 -0.0021

ASN 1013 LEU 1014 -0.0002

LEU 1014 LYS 1015 -0.0016

LYS 1015 VAL 1016 0.0003

VAL 1016 ILE 1017 0.0004

ILE 1017 GLU 1018 -0.0001

GLU 1018 LYS 1019 -0.0037

LYS 1019 ALA 1020 -0.0001

ALA 1020 ASP 1021 0.0004

ASP 1021 ASN 1022 -0.0000

ASN 1022 ALA 1023 0.0001

ALA 1023 ALA 1024 0.0005

ALA 1024 GLN 1025 -0.0009

GLN 1025 VAL 1026 -0.0001

VAL 1026 LYS 1027 -0.0002

LYS 1027 ASP 1028 0.0000

ASP 1028 ALA 1029 -0.0019

ALA 1029 LEU 1030 -0.0004

LEU 1030 THR 1031 0.0017

THR 1031 LYS 1032 -0.0000

LYS 1032 MET 1033 -0.0016

MET 1033 ARG 1034 0.0002

ARG 1034 ALA 1035 0.0050

ALA 1035 ALA 1036 -0.0000

ALA 1036 ALA 1037 -0.0002

ALA 1037 LEU 1038 0.0002

LEU 1038 ASP 1039 0.0193

ASP 1039 ALA 1040 -0.0000

ALA 1040 GLN 1041 -0.0021

GLN 1041 LYS 1042 -0.0002

LYS 1042 ALA 1043 0.0104

ALA 1043 THR 1044 -0.0003

THR 1044 PRO 1045 0.0023

PRO 1045 ASP 1060 -0.0323

ASP 1060 PHE 1061 0.0003

PHE 1061 ARG 1062 0.0052

ARG 1062 HIS 1063 0.0001

HIS 1063 GLY 1064 -0.0075

GLY 1064 PHE 1065 -0.0004

PHE 1065 ASP 1066 -0.0017

ASP 1066 ILE 1067 -0.0003

ILE 1067 LEU 1068 0.0022

LEU 1068 VAL 1069 0.0000

VAL 1069 GLY 1070 0.0020

GLY 1070 GLN 1071 0.0003

GLN 1071 ILE 1072 -0.0017

ILE 1072 ASP 1073 0.0001

ASP 1073 ASP 1074 0.0046

ASP 1074 ALA 1075 0.0001

ALA 1075 LEU 1076 -0.0021

LEU 1076 LYS 1077 0.0003

LYS 1077 LEU 1078 0.0027

LEU 1078 ALA 1079 0.0001

ALA 1079 ASN 1080 -0.0006

ASN 1080 GLU 1081 -0.0000

GLU 1081 GLY 1082 0.0003

GLY 1082 LYS 1083 0.0001

LYS 1083 VAL 1084 0.0021

VAL 1084 LYS 1085 0.0000

LYS 1085 GLU 1086 -0.0013

GLU 1086 ALA 1087 0.0001

ALA 1087 GLN 1088 0.0006

GLN 1088 ALA 1089 -0.0001

ALA 1089 ALA 1090 -0.0010

ALA 1090 ALA 1091 0.0004

ALA 1091 GLU 1092 0.0000

GLU 1092 GLN 1093 0.0003

GLN 1093 LEU 1094 0.0020

LEU 1094 LYS 1095 -0.0001

LYS 1095 THR 1096 0.0046

THR 1096 THR 1097 -0.0002

THR 1097 ARG 1098 -0.0002

ARG 1098 ASN 1099 -0.0002

ASN 1099 ALA 1100 -0.0010

ALA 1100 TYR 1101 0.0000

TYR 1101 ILE 1102 0.0014

ILE 1102 GLN 1103 0.0004

GLN 1103 LYS 1104 0.0058

LYS 1104 TYR 1105 -0.0002

TYR 1105 LEU 1106 0.0134

LEU 1106 LYS 246 0.0029

LYS 246 ASN 247 -0.0002

ASN 247 ARG 248 0.0098

ARG 248 ILE 249 0.0001

ILE 249 THR 250 0.0158

THR 250 ARG 251 0.0004

ARG 251 ASP 252 -0.0135

ASP 252 GLN 253 0.0004

GLN 253 VAL 254 0.0055

VAL 254 LEU 255 0.0000

LEU 255 LYS 256 0.0009

LYS 256 MET 257 0.0003

MET 257 ALA 258 -0.0035

ALA 258 ALA 259 -0.0004

ALA 259 ALA 260 0.0097

ALA 260 VAL 261 0.0002

VAL 261 VAL 262 -0.0597

VAL 262 LEU 263 0.0000

LEU 263 ALA 264 0.0023

ALA 264 PHE 265 0.0004

PHE 265 ILE 266 0.0099

ILE 266 ILE 267 0.0000

ILE 267 CYS 268 -0.0088

CYS 268 TRP 269 0.0002

TRP 269 LEU 270 0.0056

LEU 270 PRO 271 -0.0002

PRO 271 PHE 272 -0.0034

PHE 272 HIS 273 -0.0002

HIS 273 VAL 274 -0.0001

VAL 274 LEU 275 0.0003

LEU 275 THR 276 0.0002

THR 276 PHE 277 -0.0000

PHE 277 LEU 278 0.0047

LEU 278 ASP 279 -0.0004

ASP 279 ALA 280 0.0026

ALA 280 LEU 281 0.0001

LEU 281 ALA 282 0.0008

ALA 282 TRP 283 -0.0002

TRP 283 MET 284 -0.0008

MET 284 GLY 285 -0.0000

GLY 285 VAL 286 -0.0007

VAL 286 ILE 287 0.0002

ILE 287 ASN 288 0.0002

ASN 288 SER 289 -0.0003

SER 289 CYS 290 -0.0007

CYS 290 GLU 291 0.0002

GLU 291 VAL 292 -0.0000

VAL 292 ILE 293 0.0003

ILE 293 ALA 294 0.0021

ALA 294 VAL 295 -0.0003

VAL 295 ILE 296 0.0008

ILE 296 ASP 297 -0.0001

ASP 297 LEU 298 0.0017

LEU 298 ALA 299 -0.0001

ALA 299 LEU 300 -0.0013

LEU 300 PRO 301 0.0002

PRO 301 PHE 302 -0.0002

PHE 302 ALA 303 -0.0000

ALA 303 ILE 304 0.0000

ILE 304 LEU 305 -0.0001

LEU 305 LEU 306 -0.0096

LEU 306 GLY 307 -0.0002

GLY 307 PHE 308 -0.0007

PHE 308 THR 309 0.0002

THR 309 ASN 310 -0.0097

ASN 310 SER 311 0.0003

SER 311 CYS 312 0.0029

CYS 312 VAL 313 -0.0000

VAL 313 ASN 314 -0.0028

ASN 314 PRO 315 0.0001

PRO 315 PHE 316 0.0047

PHE 316 LEU 317 0.0000

LEU 317 TYR 318 -0.0124

TYR 318 CYS 319 -0.0001

CYS 319 PHE 320 0.0012

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.

*** Angio ***

CA strain for 2404051739442459575

--- normal mode 7 ---

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

* Angio *