Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* 7D9Z Crystal structure of anti-basigin Fab fragment *

CA strain for 2608161417401737521

--- 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
ALA 1 ASP 2 0.0001

ASP 2 VAL 3 0.0002

VAL 3 VAL 4 -0.0626

VAL 4 MET 5 -0.0000

MET 5 THR 6 -0.0000

THR 6 GLN 7 -0.0411

GLN 7 THR 8 -0.0000

THR 8 PRO 9 0.0002

PRO 9 SER 10 0.0186

SER 10 SER 10 0.0137

SER 10 SER 11 0.0002

SER 11 VAL 12 0.0002

VAL 12 VAL 12 -0.0003

VAL 12 SER 13 -0.0264

SER 13 SER 13 0.0052

SER 13 ALA 14 0.0001

ALA 14 ALA 15 -0.0003

ALA 15 VAL 16 0.0093

VAL 16 GLY 17 -0.0002

GLY 17 GLY 18 -0.0001

GLY 18 THR 19 -0.0338

THR 19 VAL 20 -0.0004

VAL 20 THR 21 0.0002

THR 21 THR 21 0.0011

THR 21 ILE 22 -0.0223

ILE 22 ASN 23 -0.0001

ASN 23 CYS 24 -0.0000

CYS 24 CYS 24 0.0049

CYS 24 GLN 25 0.0005

GLN 25 GLN 25 0.0122

GLN 25 ALA 26 -0.0004

ALA 26 SER 27 0.0004

SER 27 GLN 28 -0.0218

GLN 28 SER 29 0.0004

SER 29 ILE 30 0.0003

ILE 30 SER 31 0.0059

SER 31 SER 31 0.0000

SER 31 ALA 32 -0.0003

ALA 32 TYR 33 0.0002

TYR 33 LEU 34 0.0130

LEU 34 ALA 35 0.0003

ALA 35 TRP 36 0.0002

TRP 36 TYR 37 0.0356

TYR 37 GLN 38 0.0002

GLN 38 GLN 39 0.0001

GLN 39 LYS 40 0.0617

LYS 40 PRO 41 -0.0003

PRO 41 GLY 42 0.0004

GLY 42 GLN 43 0.1584

GLN 43 PRO 44 0.0001

PRO 44 PRO 45 -0.0000

PRO 45 LYS 46 -0.0568

LYS 46 LEU 47 0.0000

LEU 47 LEU 48 0.0004

LEU 48 ILE 49 -0.0054

ILE 49 ILE 49 0.0059

ILE 49 TYR 50 0.0005

TYR 50 ASP 51 -0.0003

ASP 51 ALA 52 -0.0119

ALA 52 SER 53 0.0002

SER 53 ASP 54 -0.0002

ASP 54 LEU 55 -0.0004

LEU 55 ALA 56 0.0002

ALA 56 SER 57 -0.0002

SER 57 SER 57 0.0377

SER 57 GLY 58 0.0050

GLY 58 VAL 59 0.0000

VAL 59 SER 60 -0.0002

SER 60 SER 61 -0.0355

SER 61 ARG 62 -0.0003

ARG 62 PHE 63 0.0000

PHE 63 LYS 64 0.0122

LYS 64 GLY 65 -0.0002

GLY 65 SER 66 -0.0001

SER 66 GLY 67 0.0267

GLY 67 SER 68 0.0001

SER 68 GLY 69 0.0001

GLY 69 THR 70 -0.0020

THR 70 GLN 71 -0.0003

GLN 71 PHE 72 0.0000

PHE 72 THR 73 0.0202

THR 73 LEU 74 -0.0005

LEU 74 THR 75 0.0000

THR 75 ILE 76 0.0106

ILE 76 SER 77 -0.0000

SER 77 SER 77 -0.0268

SER 77 ASP 78 0.0001

ASP 78 LEU 79 0.0201

LEU 79 GLU 80 -0.0000

GLU 80 CYS 81 -0.0003

CYS 81 ALA 82 -0.0312

ALA 82 ASP 83 0.0003

ASP 83 ALA 84 -0.0002

ALA 84 ALA 85 -0.0268

ALA 85 THR 86 -0.0001

THR 86 TYR 87 0.0001

TYR 87 TYR 88 -0.0157

TYR 88 CYS 89 -0.0003

CYS 89 CYS 89 0.0051

CYS 89 GLN 90 0.0001

GLN 90 THR 91 0.0150

THR 91 TYR 92 0.0000

TYR 92 TYR 93 -0.0003

TYR 93 ALA 94 0.0452

ALA 94 ILE 95 -0.0003

ILE 95 ILE 96 -0.0001

ILE 96 THR 97 -0.0498

THR 97 TYR 98 -0.0001

TYR 98 GLY 99 -0.0002

GLY 99 ALA 100 0.0223

ALA 100 ALA 101 0.0002

ALA 101 PHE 102 -0.0002

PHE 102 GLY 103 -0.0684

GLY 103 GLY 104 -0.0001

GLY 104 GLY 105 -0.0000

GLY 105 THR 106 -0.0585

THR 106 GLU 107 -0.0004

GLU 107 GLU 107 -0.0369

GLU 107 VAL 108 0.0003

VAL 108 VAL 109 0.0080

VAL 109 VAL 110 0.0002

VAL 110 LYS 111 -0.0002

LYS 111 ARG 112 -0.1001

ARG 112 THR 113 -0.0004

THR 113 VAL 114 0.0001

VAL 114 ALA 115 -0.0368

ALA 115 ALA 116 0.0004

ALA 116 PRO 117 -0.0004

PRO 117 SER 118 0.0009

SER 118 SER 118 -0.0367

SER 118 VAL 119 0.0002

VAL 119 PHE 120 0.0001

PHE 120 ILE 121 -0.0299

ILE 121 PHE 122 -0.0003

PHE 122 PRO 123 -0.0001

PRO 123 PRO 124 0.0523

PRO 124 SER 125 0.0001

SER 125 ASP 126 0.0001

ASP 126 GLU 127 0.0340

GLU 127 GLN 128 0.0001

GLN 128 LEU 129 -0.0001

LEU 129 LYS 130 0.0025

LYS 130 SER 131 -0.0000

SER 131 GLY 132 0.0001

GLY 132 THR 133 -0.0055

THR 133 ALA 134 0.0002

ALA 134 SER 135 -0.0000

SER 135 VAL 136 0.0699

VAL 136 VAL 137 0.0001

VAL 137 CYS 138 -0.0004

CYS 138 LEU 139 -0.0093

LEU 139 LEU 140 -0.0004

LEU 140 ASN 141 0.0002

ASN 141 ASN 142 -0.0023

ASN 142 ASN 142 -0.0115

ASN 142 PHE 143 0.0002

PHE 143 TYR 144 -0.0002

TYR 144 PRO 145 0.0353

PRO 145 ARG 146 0.0000

ARG 146 GLU 147 -0.0004

GLU 147 ALA 148 0.0449

ALA 148 LYS 149 -0.0003

LYS 149 VAL 150 0.0001

VAL 150 GLN 151 0.0590

GLN 151 TRP 152 0.0004

TRP 152 LYS 153 0.0001

LYS 153 VAL 154 0.0045

VAL 154 ASP 155 -0.0002

ASP 155 ASN 156 -0.0004

ASN 156 ALA 157 0.0169

ALA 157 LEU 158 0.0002

LEU 158 GLN 159 -0.0003

GLN 159 SER 160 0.0326

SER 160 GLY 161 -0.0002

GLY 161 ASN 162 0.0000

ASN 162 SER 163 0.0595

SER 163 GLN 164 0.0004

GLN 164 GLU 165 -0.0000

GLU 165 SER 166 0.0723

SER 166 SER 166 -0.0060

SER 166 VAL 167 0.0003

VAL 167 VAL 167 0.0001

VAL 167 THR 168 0.0000

THR 168 GLU 169 0.1814

GLU 169 GLU 169 0.0019

GLU 169 GLN 170 -0.0001

GLN 170 ASP 171 -0.0002

ASP 171 SER 172 0.0262

SER 172 LYS 173 0.0003

LYS 173 ASP 174 -0.0003

ASP 174 CYS 175 0.0345

CYS 175 THR 176 -0.0003

THR 176 TYR 177 -0.0001

TYR 177 SER 178 0.0496

SER 178 LEU 179 0.0001

LEU 179 SER 180 0.0001

SER 180 SER 181 0.0499

SER 181 THR 182 -0.0001

THR 182 LEU 183 -0.0000

LEU 183 THR 184 0.0459

THR 184 LEU 185 -0.0000

LEU 185 SER 186 0.0000

SER 186 LYS 187 -0.0037

LYS 187 ALA 188 -0.0001

ALA 188 ASP 189 0.0002

ASP 189 TYR 190 -0.0306

TYR 190 GLU 191 -0.0001

GLU 191 LYS 192 0.0001

LYS 192 HIS 193 -0.0069

HIS 193 LYS 194 0.0000

LYS 194 LYS 194 0.0307

LYS 194 VAL 195 0.0001

VAL 195 TYR 196 0.0275

TYR 196 ALA 197 -0.0002

ALA 197 CYS 198 -0.0000

CYS 198 CYS 198 -0.0091

CYS 198 GLU 199 -0.0063

GLU 199 VAL 200 0.0002

VAL 200 THR 201 -0.0002

THR 201 HIS 202 -0.0074

HIS 202 GLN 203 0.0002

GLN 203 GLY 204 -0.0002

GLY 204 LEU 205 -0.0448

LEU 205 SER 206 -0.0001

SER 206 SER 207 -0.0002

SER 207 PRO 208 -0.0063

PRO 208 VAL 209 0.0003

VAL 209 THR 210 -0.0001

THR 210 LYS 211 0.0029

LYS 211 SER 212 -0.0001

SER 212 PHE 213 0.0003

PHE 213 ASN 214 -0.0555

ASN 214 ARG 215 0.0001

ARG 215 GLY 216 0.0002

GLY 216 GLU 217 0.0462

GLU 217 SER 2 0.0923

SER 2 VAL 3 -0.0002

VAL 3 GLU 4 -0.0000

GLU 4 GLU 5 0.0294

GLU 5 SER 6 0.0002

SER 6 GLY 7 -0.0001

GLY 7 GLY 8 0.1269

GLY 8 ARG 9 -0.0000

ARG 9 LEU 10 -0.0000

LEU 10 VAL 11 0.0254

VAL 11 THR 12 -0.0001

THR 12 PRO 13 0.0001

PRO 13 GLY 14 -0.0235

GLY 14 THR 15 0.0001

THR 15 PRO 16 -0.0002

PRO 16 LEU 17 -0.0143

LEU 17 THR 18 -0.0002

THR 18 LEU 19 -0.0001

LEU 19 THR 20 0.0288

THR 20 CYS 21 0.0000

CYS 21 THR 22 0.0002

THR 22 VAL 23 0.0192

VAL 23 SER 24 0.0001

SER 24 GLY 25 -0.0001

GLY 25 PHE 26 -0.0244

PHE 26 SER 27 0.0003

SER 27 LEU 28 -0.0002

LEU 28 SER 29 0.0196

SER 29 SER 29 0.0001

SER 29 ASP 30 0.0001

ASP 30 TYR 31 -0.0003

TYR 31 ALA 32 -0.0058

ALA 32 MET 33 0.0000

MET 33 SER 34 -0.0001

SER 34 TRP 35 0.0555

TRP 35 VAL 36 0.0003

VAL 36 ARG 37 -0.0001

ARG 37 GLN 38 -0.0055

GLN 38 ALA 39 -0.0004

ALA 39 PRO 40 0.0002

PRO 40 GLY 41 -0.0110

GLY 41 LYS 42 0.0001

LYS 42 GLY 43 0.0002

GLY 43 LEU 44 -0.0047

LEU 44 GLU 45 0.0004

GLU 45 TRP 46 -0.0002

TRP 46 ILE 47 -0.0583

ILE 47 GLY 48 0.0003

GLY 48 ILE 49 -0.0003

ILE 49 ILE 50 -0.0092

ILE 50 TYR 51 -0.0002

TYR 51 ALA 52 0.0001

ALA 52 SER 53 0.0065

SER 53 GLY 54 0.0001

GLY 54 SER 55 0.0000

SER 55 THR 56 -0.0048

THR 56 THR 56 -0.0396

THR 56 TYR 57 -0.0000

TYR 57 TYR 58 0.0001

TYR 58 ALA 59 -0.0291

ALA 59 SER 60 0.0001

SER 60 TRP 61 -0.0002

TRP 61 ALA 62 0.0146

ALA 62 LYS 63 0.0003

LYS 63 GLY 64 -0.0001

GLY 64 ARG 65 0.0209

ARG 65 PHE 66 0.0005

PHE 66 THR 67 -0.0001

THR 67 ILE 68 -0.0225

ILE 68 SER 69 -0.0001

SER 69 LYS 70 -0.0000

LYS 70 THR 71 -0.0263

THR 71 SER 72 -0.0002

SER 72 THR 73 0.0003

THR 73 THR 74 0.0183

THR 74 VAL 75 0.0001

VAL 75 ASP 76 0.0002

ASP 76 LEU 77 -0.0073

LEU 77 LYS 78 0.0001

LYS 78 ILE 79 -0.0002

ILE 79 THR 80 -0.0189

THR 80 SER 81 -0.0004

SER 81 PRO 82 0.0000

PRO 82 THR 83 -0.0075

THR 83 THR 84 0.0001

THR 84 GLU 85 0.0003

GLU 85 ASP 86 0.0100

ASP 86 THR 87 -0.0000

THR 87 ALA 88 -0.0001

ALA 88 THR 89 -0.0189

THR 89 TYR 90 0.0000

TYR 90 PHE 91 0.0003

PHE 91 CYS 92 0.0918

CYS 92 CYS 92 0.0007

CYS 92 ALA 93 -0.0001

ALA 93 ARG 94 0.0002

ARG 94 TYR 95 0.0038

TYR 95 TYR 96 0.0001

TYR 96 TYR 96 -0.0036

TYR 96 ALA 97 -0.0003

ALA 97 GLY 98 -0.0057

GLY 98 SER 99 0.0000

SER 99 ASP 100 -0.0000

ASP 100 ILE 101 -0.0181

ILE 101 ILE 101 -0.0186

ILE 101 TRP 102 0.0003

TRP 102 GLY 103 -0.0003

GLY 103 PRO 104 0.0060

PRO 104 GLY 105 -0.0001

GLY 105 THR 106 0.0002

THR 106 LEU 107 0.1850

LEU 107 LEU 107 0.0276

LEU 107 VAL 108 0.0002

VAL 108 THR 109 -0.0001

THR 109 VAL 110 0.0088

VAL 110 SER 111 0.0003

SER 111 SER 112 0.0000

SER 112 ALA 113 -0.0440

ALA 113 SER 114 -0.0002

SER 114 THR 115 0.0001

THR 115 LYS 116 0.1273

LYS 116 GLY 117 0.0002

GLY 117 PRO 118 0.0000

PRO 118 SER 119 0.2409

SER 119 VAL 120 -0.0004

VAL 120 PHE 121 0.0004

PHE 121 PRO 122 0.1037

PRO 122 LEU 123 -0.0000

LEU 123 ALA 124 0.0003

ALA 124 PRO 125 0.0623

PRO 125 SER 126 -0.0001

SER 126 GLY 133 -0.0099

GLY 133 THR 134 0.0001

THR 134 THR 134 0.0150

THR 134 ALA 135 0.0000

ALA 135 ALA 136 0.0060

ALA 136 LEU 137 0.0002

LEU 137 GLY 138 -0.0002

GLY 138 CYS 139 0.0476

CYS 139 CYS 139 -0.0050

CYS 139 LEU 140 -0.0001

LEU 140 VAL 141 0.0002

VAL 141 LYS 142 -0.0119

LYS 142 ASP 143 -0.0004

ASP 143 TYR 144 0.0003

TYR 144 PHE 145 0.2559

PHE 145 PRO 146 0.0000

PRO 146 GLU 147 -0.0001

GLU 147 GLU 147 -0.0069

GLU 147 PRO 148 -0.0648

PRO 148 VAL 149 0.0002

VAL 149 THR 150 0.0000

THR 150 VAL 151 -0.0672

VAL 151 SER 152 0.0000

SER 152 TRP 153 0.0001

TRP 153 ASN 154 0.0065

ASN 154 SER 155 -0.0001

SER 155 GLY 156 -0.0001

GLY 156 ALA 157 -0.0090

ALA 157 LEU 158 0.0000

LEU 158 THR 159 -0.0001

THR 159 SER 160 0.0056

SER 160 SER 160 0.0109

SER 160 GLY 161 0.0003

GLY 161 VAL 162 0.0001

VAL 162 HIS 163 0.0231

HIS 163 THR 164 0.0001

THR 164 PHE 165 0.0000

PHE 165 PRO 166 -0.0156

PRO 166 ALA 167 -0.0002

ALA 167 VAL 168 -0.0001

VAL 168 VAL 168 -0.0168

VAL 168 LEU 169 -0.0748

LEU 169 GLN 170 0.0001

GLN 170 SER 171 0.0001

SER 171 SER 172 -0.0030

SER 172 GLY 173 0.0002

GLY 173 LEU 174 0.0002

LEU 174 TYR 175 -0.0028

TYR 175 SER 176 -0.0002

SER 176 SER 176 0.0089

SER 176 LEU 177 -0.0002

LEU 177 SER 178 -0.0019

SER 178 SER 178 0.0029

SER 178 SER 179 0.0001

SER 179 VAL 180 0.0001

VAL 180 VAL 181 -0.0013

VAL 181 THR 182 -0.0003

THR 182 VAL 183 -0.0001

VAL 183 PRO 184 0.0027

PRO 184 SER 185 0.0000

SER 185 SER 185 -0.0246

SER 185 SER 186 -0.0001

SER 186 SER 187 0.0000

SER 187 LEU 188 -0.0002

LEU 188 GLY 189 0.0000

GLY 189 THR 190 -0.0178

THR 190 GLN 191 0.0005

GLN 191 GLN 191 -0.0172

GLN 191 THR 192 0.0000

THR 192 TYR 193 0.0196

TYR 193 ILE 194 0.0004

ILE 194 CYS 195 -0.0001

CYS 195 CYS 195 -0.0121

CYS 195 ASN 196 -0.0110

ASN 196 VAL 197 -0.0004

VAL 197 ASN 198 -0.0002

ASN 198 ASN 198 -0.0006

ASN 198 HIS 199 -0.0060

HIS 199 LYS 200 0.0003

LYS 200 PRO 201 -0.0000

PRO 201 SER 202 0.0656

SER 202 ASN 203 -0.0002

ASN 203 THR 204 -0.0002

THR 204 LYS 205 0.0312

LYS 205 VAL 206 0.0003

VAL 206 ASP 207 0.0002

ASP 207 LYS 208 -0.0045

LYS 208 LYS 209 0.0001

LYS 209 VAL 210 -0.0001

VAL 210 GLU 211 0.0489

GLU 211 PRO 212 -0.0002

PRO 212 LYS 213 0.0001

LYS 213 SER 214 0.0087

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).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.

Should you encounter any unexpected behaviour, please let us know. elNémo has been relocated. **Some cleaning from time to time** Sorry for the inconvenience.

*** 7D9Z Crystal structure of anti-basigin Fab fragment ***

CA strain for 2608161417401737521

--- normal mode 9 ---

Should you encounter any unexpected behaviour,
please let us know.
elNémo has been relocated.
Some cleaning from time to time
Sorry for the inconvenience.

* 7D9Z Crystal structure of anti-basigin Fab fragment *