HPMV: sp|P05067|A4_HUMAN Amyloid beta A4 protein OS=Homo sapiens GN=APP PE=1 SV=3

Coloring:  Height:   Standalone-Viewer:
Width:

Click feature in cartoon to expand feature tree.

Mutation V123L has an uncertain/unknown affect on protein function.

Mutation T456M could potentially affect protein function. The mutation T456M has changed the extent/range/from-to of the coiled-coil region.

Feature Tree
▼ Query Mutations

User specified mutations of interest - differences between
the query protein and the wildtype reference protein.

123 V123L (p.Val123Leu) has an uncertain/unknown affect on protein function.
▼ 456 T456M (p.Thr456Met) could potentially affect protein function.
▼ T456M could potentially affect Coiled-Coil

The mutation T456M has changed the extent/range/from-to
of the coiled-coil region.

wt : 425 460 IMP-COIL
mut: 425 463 IMP-COIL
▼ T456M has an uncertain/unknown affect on Disorder

The mutation T456M has potentially disrupted an disorder region
but the general effects on function/stability are uncertain.

wt : 348 460 IUPred Long
mut: absent
▼ Known Variants

Known sequence variants from UniProt.
Red: specific annotation - usually disease variant.
Blue: dbSNP variant - without additional annotation.
Green: no information available.

▼ 501 E->K In dbSNP:rs45588932.
▼ 501 ( 501) E->K UniProt Natural Variant: In dbSNP:rs45588932.
▼ 665 E->D In a patient with late onset Alzheimer disease.
▼ 665 ( 665) E->D UniProt Natural Variant: In a patient with late onset Alzheimer disease.
▼ 670 671 KM->NL In AD1.
▼ 670 671 ( 670 671) KM->NL UniProt Natural Variant: In AD1.
▼ 678 D->N In AD1.
▼ 678 ( 678) D->N UniProt Natural Variant: In AD1.
▼ 692 A->G In AD1; Flemish mutation; increases the solubility of processed beta-amyloid peptides and increases the stability of peptide oligomers.
▼ 692 ( 692) A->G UniProt Natural Variant: In AD1; Flemish mutation; increases the solubility of processed beta-amyloid peptides and increases the stability of peptide oligomers.
▼ 693 complex variants
▼ 693 ( 693) E->G UniProt Natural Variant: In AD1.
▼ 693 ( 693) E->K UniProt Natural Variant: In CAA-APP; Italian type.
▼ 693 ( 693) E->Q UniProt Natural Variant: In CAA-APP; Dutch type.
▼ 694 D->N In CAA-APP; Iowa type.
▼ 694 ( 694) D->N UniProt Natural Variant: In CAA-APP; Iowa type.
▼ 705 L->V In CAA-APP; Italian type.
▼ 705 ( 705) L->V UniProt Natural Variant: In CAA-APP; Italian type.
▼ 713 complex variants
▼ 713 ( 713) A->T UniProt Natural Variant: In AD1.
▼ 713 ( 713) A->V UniProt Natural Variant: In one chronic schizophrenia patient; unknown pathological significance; dbSNP:rs1800557.
▼ 714 complex variants
▼ 714 ( 714) T->A UniProt Natural Variant: In AD1.
▼ 714 ( 714) T->I UniProt Natural Variant: In AD1; increased beta-APP42/beta-APP40 ratio.
▼ 715 V->M In AD1; decreased beta-APP40/total APP-beta.
▼ 715 ( 715) V->M UniProt Natural Variant: In AD1; decreased beta-APP40/total APP-beta.
▼ 716 I->V In AD1.
▼ 716 ( 716) I->V UniProt Natural Variant: In AD1.
▼ 717 complex variants
▼ 717 ( 717) V->F UniProt Natural Variant: In AD1.
▼ 717 ( 717) V->G UniProt Natural Variant: In AD1.
▼ 717 ( 717) V->I UniProt Natural Variant: In AD1.
▼ 717 ( 717) V->L UniProt Natural Variant: In AD1.
▼ 723 L->P In AD1.
▼ 723 ( 723) L->P UniProt Natural Variant: In AD1.
▼ Targeting Signals & Post-Translational Modifications

Targeting signals, post-translational modifications (PTMs)
and coiled-coil and transmembrane segments.

▼ 425 460 Coiled-Coil

Alpha-helices packed together in dimers, trimers, or tetramers.
Heptade repeat sequence: hydrophobic at 1st and 4th positions.
Generally too large to be affected by single mutations.

  425 460 IMP-COIL
▼ 553 577 Coiled-Coil

Alpha-helices packed together in dimers, trimers, or tetramers.
Heptade repeat sequence: hydrophobic at 1st and 4th positions.
Generally too large to be affected by single mutations.

  553 577 IMP-COIL
▼ 198 Modified Residue: Phosphoserine; by CK2

Residue with post-translational covalent modification.
Mutations potentially significant when modifications when
modifications have important function.

▼ 198 ( 198) S UniProt Modified Residue: Phosphoserine; by CK2 evidence=109
▼ 206 Modified Residue: Phosphoserine; by CK1

Residue with post-translational covalent modification.
Mutations potentially significant when modifications when
modifications have important function.

▼ 206 ( 206) S UniProt Modified Residue: Phosphoserine; by CK1 evidence=109
▼ 441 Modified Residue: Phosphoserine; by FAM20C

Residue with post-translational covalent modification.
Mutations potentially significant when modifications when
modifications have important function.

▼ 441 ( 441) S UniProt Modified Residue: Phosphoserine; by FAM20C evidence=91
▼ 497 Modified Residue: Phosphotyrosine

Residue with post-translational covalent modification.
Mutations potentially significant when modifications when
modifications have important function.

▼ 497 ( 497) Y UniProt Modified Residue: Phosphotyrosine evidence=91
▼ 729 Modified Residue: Phosphothreonine

Residue with post-translational covalent modification.
Mutations potentially significant when modifications when
modifications have important function.

▼ 729 ( 729) T UniProt Modified Residue: Phosphothreonine evidence=22
▼ 730 Modified Residue: Phosphoserine; by APP-kinase I

Residue with post-translational covalent modification.
Mutations potentially significant when modifications when
modifications have important function.

▼ 730 ( 730) S UniProt Modified Residue: Phosphoserine; by APP-kinase I evidence=21
▼ 743 Modified Residue: Phosphothreonine; by CDK5 and MAPK10

Residue with post-translational covalent modification.
Mutations potentially significant when modifications when
modifications have important function.

▼ 743 ( 743) T UniProt Modified Residue: Phosphothreonine; by CDK5 and MAPK10 evidence=20 96
▼ 757 Modified Residue: Phosphotyrosine

Residue with post-translational covalent modification.
Mutations potentially significant when modifications when
modifications have important function.

▼ 757 ( 757) Y UniProt Modified Residue: Phosphotyrosine evidence=52
▼ 724 734 Short Motif: Basolateral sorting signal

Short sequence motifs - based on UniProt annotations.

▼ 724 734 ( 724 734) Basolateral sorting signal
▼ 759 762 Short Motif: NPXY motif; contains endocytosis signal

Short sequence motifs - based on UniProt annotations.

▼ 759 762 ( 759 762) NPXY motif; contains endocytosis signal
▼ 1 18 Signal Peptide

Signals translocation across ER membrane.
Cleavage site can distinguish: anchors and secretory proteins.
Mutations that affect cleavage site are potentially significant.

  1 17 Phobius SIGNAL
  1 18 SignalP-3.0
▼ 1 17 ( 1 17) UniProt Signal Peptide
▼ 701 723 Transmembrane

Can be single anchor or multipass integral membrane protein.
Can be simple (general hydrophobic composition) or complex.
Single hydrophobic substitutions may be tolerated but
deletion of entire helix would be potentially significant.

  701 723 Phobius TRANSMEN
▼ Non-Globular Regions (Compositional Bias)

Non-globular features relating to sequence composition including
charge clusters, low complexity regions and disordered regions.

▼ 191 264 Negative Charge Cluster

Compositional bias: run of negatively charged residues.
Mutations of opposite/positive charge are likely to be significant.

  191 264 SAPS Negative Charge Cluster tvalue=8.20
▼ 219 295 Disorder

Unstructured: no well defined 3D structure - high mobility.
Missing electron density / high temperature facture.
Mutations in disordered regions are less likely to be significant.

  219 295 IUPred Long
▼ 348 460 Disorder

Unstructured: no well defined 3D structure - high mobility.
Missing electron density / high temperature facture.
Mutations in disordered regions are less likely to be significant.

  348 460 IUPred Long
▼ 624 663 Disorder

Unstructured: no well defined 3D structure - high mobility.
Missing electron density / high temperature facture.
Mutations in disordered regions are less likely to be significant.

  624 663 IUPred Long
▼ 2 30 Low Complexity

Regions that have a compositional bias (non-random composition).
They are common in natural sequences and are associated with
disordered and fibrillar regions (i.e. non-globular regions).
The precise order of the amino acids is less important.
These regions are generally less sensitve to mutations.

  2 18 SEG [12/2.5/2.2] complexity=2.25
  2 30 SEG [25/3.3/3.0] complexity=2.89
▼ 190 297 Low Complexity

Regions that have a compositional bias (non-random composition).
They are common in natural sequences and are associated with
disordered and fibrillar regions (i.e. non-globular regions).
The precise order of the amino acids is less important.
These regions are generally less sensitve to mutations.

  190 208 SEG [12/2.5/2.2] complexity=2.40
  190 297 SEG [25/3.3/3.0] complexity=3.12
▼ 222 290 Low Complexity

Regions that have a compositional bias (non-random composition).
They are common in natural sequences and are associated with
disordered and fibrillar regions (i.e. non-globular regions).
The precise order of the amino acids is less important.
These regions are generally less sensitve to mutations.

  222 290 SEG [12/2.5/2.2] complexity=2.74
▼ 700 723 Low Complexity

Regions that have a compositional bias (non-random composition).
They are common in natural sequences and are associated with
disordered and fibrillar regions (i.e. non-globular regions).
The precise order of the amino acids is less important.
These regions are generally less sensitve to mutations.

  706 723 SEG [12/2.5/2.2] complexity=2.60
  700 722 SEG [25/3.3/3.0] complexity=2.65
▼ Conserved Domains

Conserved domains with significant similarity to the query.

▼ 31 131 PF02177.12 APP_N Amyloid A4 N-terminal heparin-binding D

This N-terminal domain of APP, amyloid precursor protein, is
the heparin-binding domain of the protein. this region is also
responsible for stimulation of neurite outgrowth. The structure
reveals both a highly charged basic surface that may interact
with glycosaminoglycans in the brain and an abutting hydrophobic
surface that is proposed to play an important functional role
such as in dimerisation or ligand-binding. Structural similarities
with cysteine-rich growth factors, taken together with its known
growth-promoting properties, suggest the APP N-terminal domain
could function as a growth factor in vivo [1].
HMM-range=1-100 HMM-length=100

  31 131 HMMER3 E-value=2.2E-47
(max 30 seqs)
▼ 132 188 PF12924.3 APP_Cu_bd Copper-binding of amyloid precursor, CuBD D

This short domain, part of the extra-cellular N-terminus of the
amyloid precursor protein, APP, can bind both copper and zinc,
CuBD. The structure of Cu2+-bound CuBD reveals that the metal
ligands are His147, His151, Tyr168 and two water molecules,
which are arranged in a square pyramidal geometry. The structure
of Cu+-bound CuBD is almost identical to the Cu2+-bound structure
except for the loss of one of the water ligands. The geometry
of the site is unfavourable for Cu+, thus providing a mechanism
by which CuBD could readily transfer Cu ions to other proteins.
HMM-range=1-57 HMM-length=57

  132 188 HMMER3 E-value=6.2E-29
(max 30 seqs)
▼ 290 341 PF00014.19 Kunitz_BPTI Kunitz/Bovine pancreatic trypsin inhibitor domain D

Indicative of a protease inhibitor, usually a serine protease
inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI
(bovine pancreatic trypsin inhibitor) is an extensively studied
model structure. Certain family members are similar to the tick
anticoagulant peptide (TAP, Swiss:P17726). This is a highly
selective inhibitor of factor Xa in the blood coagulation pathways
[1]. TAP molecules are highly dipolar [2], and are arranged
to form a twisted two- stranded antiparallel beta-sheet followed
by an alpha helix [1].
HMM-range=1-52 HMM-length=53

  290 341 HMMER3 E-value=8.5E-23
(max 30 seqs)
▼ 366 548 PF12925.3 APP_E2 E2 domain of amyloid precursor protein D

The E2 domain is the largest of the conserved domains of the
amyloid precursor protein. The structure of E2 consists of two
coiled-coil sub-structures connected through a continuous helix,
and bears an unexpected resemblance to the spectrin family of
protein structures.E 2 can reversibly dimerise in solution,
and the dimerisation occurs along the longest dimension of the
molecule in an antiparallel orientation, which enables the N-terminal
substructure of one monomer to pack against the C-terminal substructure
of a second monomer. The high degree of conservation of residues
at the putative dimer interface suggests that the E2 dimer observed
in the crystal could be physiologically relevant. Heparin sulfate
proteoglycans, the putative ligands for the precursor present
in extracellular matrix, bind to E2 at a conserved and positively
charged site near the dimer interface [1].
HMM-range=1-190 HMM-length=190

  366 548 HMMER3 E-value=2.0E-77
(max 30 seqs)
▼ 675 713 PF03494.9 Beta-APP Beta-amyloid peptide (beta-APP) F

HMM-range=1-39 HMM-length=39

  675 713 HMMER3 E-value=6.8E-30
(max 30 seqs)
▼ 716 766 PF10515.5 APP_amyloid beta-amyloid precursor protein C-terminus F

This is the amyloid, C-terminal, protein of the beta-Amyloid
precursor protein (APP) which is a conserved and ubiquitous
transmembrane glycoprotein strongly implicated in the pathogenesis
of Alzheimer's disease but whose normal biological function
is unknown. The C-terminal 100 residues are released and aggregate
into amyloid deposits which are strongly implicated in the pathology
of Alzheimer's disease plaque-formation. The domain is associated
with family A4_EXTRA, Pfam:PF02177, further towards the N-terminus.
HMM-range=1-52 HMM-length=52

  716 766 HMMER3 E-value=2.2E-28
(max 30 seqs)
▼ 3D Structures

PDB structures with significant similarity to the query sequence.

▼ 18 199 4pwq_A Amyloid beta A4 protein

PDB-range=2-183 PDB-length=191

  18 199 ssearchE-value=5.0E-75
▼ 131 188 2m05_A Beta-amyloid-like protein

PDB-range=1-64 PDB-length=65

  131 188 ssearchE-value=2.0E-5
▼ 269 345 1co7_I BOVINE PANCREATIC TRYPSIN INHIBITOR

PDB-range=17-93 PDB-length=99

  269 345 ssearchE-value=2.0E-7
▼ 274 341 4bqd_A TISSUE FACTOR PATHWAY INHIBITOR (LIPOPROTEIN-

PDB-range=9-76 PDB-length=79

  274 341 ssearchE-value=1.2E-6
▼ 287 344 1aap_A ALZHEIMER'S DISEASE AMYLOID A4 PROTEIN

PDB-range=1-58 PDB-length=58

  287 344 ssearchE-value=4.1E-22
▼ 288 341 2m01_A Protease inhibitor LmKTT-1a

PDB-range=1-54 PDB-length=59

  288 341 ssearchE-value=9.1E-5
▼ 289 341 1kun_A ALPHA3-CHAIN TYPE VI COLLAGEN

PDB-range=3-55 PDB-length=58

  289 341 ssearchE-value=4.0E-7
▼ 289 341 1yc0_I Kunitz-type protease inhibitor 1

PDB-range=20-72 PDB-length=75

  289 341 ssearchE-value=1.8E-6
▼ 289 341 1zr0_B Tissue factor pathway inhibitor 2

PDB-range=7-59 PDB-length=63

  289 341 ssearchE-value=2.7E-6
▼ 289 341 2ddi_A WAP, follistatin/kazal, immunoglobulin, kunit

PDB-range=8-60 PDB-length=70

  289 341 ssearchE-value=1.2E-5
▼ 289 341 1adz_A TISSUE FACTOR PATHWAY INHIBITOR

PDB-range=12-64 PDB-length=71

  289 341 ssearchE-value=5.4E-5
▼ 289 344 2jot_A Huwentoxin-11

PDB-range=2-55 PDB-length=55

  289 344 ssearchE-value=6.8E-7
▼ 290 345 4bd9_B CARBOXYPEPTIDASE INHIBITOR SMCI

PDB-range=3-58 PDB-length=165

  290 345 ssearchE-value=3.6E-6
▼ 291 341 4bd9_B CARBOXYPEPTIDASE INHIBITOR SMCI

PDB-range=115-165 PDB-length=165

  291 341 ssearchE-value=2.1E-7
▼ 291 341 1irh_A tissue factor pathway inhibitor

PDB-range=8-58 PDB-length=61

  291 341 ssearchE-value=1.2E-6
▼ 291 341 1bf0_A CALCICLUDINE

PDB-range=7-57 PDB-length=60

  291 341 ssearchE-value=5.9E-5
▼ 291 342 1bik_A BIKUNIN

PDB-range=82-133 PDB-length=147

  291 342 ssearchE-value=1.3E-6
▼ 291 348 1jc6_A VENOM BASIC PROTEASE INHIBITORS IX AND VIIIB

PDB-range=7-64 PDB-length=65

  291 348 ssearchE-value=9.3E-6
▼ 291 358 2ody_E Boophilin

PDB-range=6-78 PDB-length=127

  291 358 ssearchE-value=4.5E-8
▼ 296 341 2ody_E Boophilin

PDB-range=79-124 PDB-length=127

  296 341 ssearchE-value=1.2E-6
▼ 369 592 4yn0_B Amyloid beta A4 protein

PDB-range=2-225 PDB-length=233

  369 592 ssearchE-value=3.1E-87
▼ 376 595 3k66_A Beta-amyloid-like protein

PDB-range=3-222 PDB-length=239

  376 595 ssearchE-value=4.8E-20
▼ 671 770 2lp1_A C99

PDB-range=1-100 PDB-length=122

  671 770 ssearchE-value=5.6E-36
▼ 672 699 1nmj_A amyloid beta-peptide from Alzheimer's disease

PDB-range=1-28 PDB-length=28

  672 699 ssearchE-value=2.7E-5
▼ 739 770 2yt0_A Amyloid beta A4 protein and Amyloid beta A4 p

PDB-range=8-39 PDB-length=176

  739 770 ssearchE-value=1.4E-7
▼ 739 770 2ysz_A Amyloid beta A4 precursor protein-binding fam

PDB-range=154-185 PDB-length=185

  739 770 ssearchE-value=1.5E-7
▼ 739 770 2yt1_A Amyloid beta A4 protein and Amyloid beta A4 p

PDB-range=8-39 PDB-length=185

  739 770 ssearchE-value=1.5E-7
▼ Sequence Information

Information relating to sequence residues.

▼ 1 770 Individual Residues

Information relating to each individual residue.

  1 M
  2 L
  3 P
  4 G
  5 L
  6 A
  7 L
  8 L
  9 L
  10 L
  11 A
  12 A
  13 W
  14 T
  15 A
  16 R
  17 A
  18 L
  19 E
  20 V
  21 P
  22 T
  23 D
  24 G
  25 N
  26 A
  27 G
  28 L
  29 L
  30 A
  31 E
  32 P
  33 Q
  34 I
  35 A
  36 M
  37 F
  38 C
  39 G
  40 R
  41 L
  42 N
  43 M
  44 H
  45 M
  46 N
  47 V
  48 Q
  49 N
  50 G
  51 K
  52 W
  53 D
  54 S
  55 D
  56 P
  57 S
  58 G
  59 T
  60 K
  61 T
  62 C
  63 I
  64 D
  65 T
  66 K
  67 E
  68 G
  69 I
  70 L
  71 Q
  72 Y
  73 C
  74 Q
  75 E
  76 V
  77 Y
  78 P
  79 E
  80 L
  81 Q
  82 I
  83 T
  84 N
  85 V
  86 V
  87 E
  88 A
  89 N
  90 Q
  91 P
  92 V
  93 T
  94 I
  95 Q
  96 N
  97 W
  98 C
  99 K
  100 R
  101 G
  102 R
  103 K
  104 Q
  105 C
  106 K
  107 T
  108 H
  109 P
  110 H
  111 F
  112 V
  113 I
  114 P
  115 Y
  116 R
  117 C
  118 L
  119 V
  120 G
  121 E
  122 F
  123 V
  124 S
  125 D
  126 A
  127 L
  128 L
  129 V
  130 P
  131 D
  132 K
  133 C
  134 K
  135 F
  136 L
  137 H
  138 Q
  139 E
  140 R
  141 M
  142 D
  143 V
  144 C
  145 E
  146 T
  147 H
  148 L
  149 H
  150 W
  151 H
  152 T
  153 V
  154 A
  155 K
  156 E
  157 T
  158 C
  159 S
  160 E
  161 K
  162 S
  163 T
  164 N
  165 L
  166 H
  167 D
  168 Y
  169 G
  170 M
  171 L
  172 L
  173 P
  174 C
  175 G
  176 I
  177 D
  178 K
  179 F
  180 R
  181 G
  182 V
  183 E
  184 F
  185 V
  186 C
  187 C
  188 P
  189 L
  190 A
  191 E
  192 E
  193 S
  194 D
  195 N
  196 V
  197 D
  198 S
  199 A
  200 D
  201 A
  202 E
  203 E
  204 D
  205 D
  206 S
  207 D
  208 V
  209 W
  210 W
  211 G
  212 G
  213 A
  214 D
  215 T
  216 D
  217 Y
  218 A
  219 D
  220 G
  221 S
  222 E
  223 D
  224 K
  225 V
  226 V
  227 E
  228 V
  229 A
  230 E
  231 E
  232 E
  233 E
  234 V
  235 A
  236 E
  237 V
  238 E
  239 E
  240 E
  241 E
  242 A
  243 D
  244 D
  245 D
  246 E
  247 D
  248 D
  249 E
  250 D
  251 G
  252 D
  253 E
  254 V
  255 E
  256 E
  257 E
  258 A
  259 E
  260 E
  261 P
  262 Y
  263 E
  264 E
  265 A
  266 T
  267 E
  268 R
  269 T
  270 T
  271 S
  272 I
  273 A
  274 T
  275 T
  276 T
  277 T
  278 T
  279 T
  280 T
  281 E
  282 S
  283 V
  284 E
  285 E
  286 V
  287 V
  288 R
  289 E
  290 V
  291 C
  292 S
  293 E
  294 Q
  295 A
  296 E
  297 T
  298 G
  299 P
  300 C
  301 R
  302 A
  303 M
  304 I
  305 S
  306 R
  307 W
  308 Y
  309 F
  310 D
  311 V
  312 T
  313 E
  314 G
  315 K
  316 C
  317 A
  318 P
  319 F
  320 F
  321 Y
  322 G
  323 G
  324 C
  325 G
  326 G
  327 N
  328 R
  329 N
  330 N
  331 F
  332 D
  333 T
  334 E
  335 E
  336 Y
  337 C
  338 M
  339 A
  340 V
  341 C
  342 G
  343 S
  344 A
  345 M
  346 S
  347 Q
  348 S
  349 L
  350 L
  351 K
  352 T
  353 T
  354 Q
  355 E
  356 P
  357 L
  358 A
  359 R
  360 D
  361 P
  362 V
  363 K
  364 L
  365 P
  366 T
  367 T
  368 A
  369 A
  370 S
  371 T
  372 P
  373 D
  374 A
  375 V
  376 D
  377 K
  378 Y
  379 L
  380 E
  381 T
  382 P
  383 G
  384 D
  385 E
  386 N
  387 E
  388 H
  389 A
  390 H
  391 F
  392 Q
  393 K
  394 A
  395 K
  396 E
  397 R
  398 L
  399 E
  400 A
  401 K
  402 H
  403 R
  404 E
  405 R
  406 M
  407 S
  408 Q
  409 V
  410 M
  411 R
  412 E
  413 W
  414 E
  415 E
  416 A
  417 E
  418 R
  419 Q
  420 A
  421 K
  422 N
  423 L
  424 P
  425 K
  426 A
  427 D
  428 K
  429 K
  430 A
  431 V
  432 I
  433 Q
  434 H
  435 F
  436 Q
  437 E
  438 K
  439 V
  440 E
  441 S
  442 L
  443 E
  444 Q
  445 E
  446 A
  447 A
  448 N
  449 E
  450 R
  451 Q
  452 Q
  453 L
  454 V
  455 E
  456 T
  457 H
  458 M
  459 A
  460 R
  461 V
  462 E
  463 A
  464 M
  465 L
  466 N
  467 D
  468 R
  469 R
  470 R
  471 L
  472 A
  473 L
  474 E
  475 N
  476 Y
  477 I
  478 T
  479 A
  480 L
  481 Q
  482 A
  483 V
  484 P
  485 P
  486 R
  487 P
  488 R
  489 H
  490 V
  491 F
  492 N
  493 M
  494 L
  495 K
  496 K
  497 Y
  498 V
  499 R
  500 A
  501 E
  502 Q
  503 K
  504 D
  505 R
  506 Q
  507 H
  508 T
  509 L
  510 K
  511 H
  512 F
  513 E
  514 H
  515 V
  516 R
  517 M
  518 V
  519 D
  520 P
  521 K
  522 K
  523 A
  524 A
  525 Q
  526 I
  527 R
  528 S
  529 Q
  530 V
  531 M
  532 T
  533 H
  534 L
  535 R
  536 V
  537 I
  538 Y
  539 E
  540 R
  541 M
  542 N
  543 Q
  544 S
  545 L
  546 S
  547 L
  548 L
  549 Y
  550 N
  551 V
  552 P
  553 A
  554 V
  555 A
  556 E
  557 E
  558 I
  559 Q
  560 D
  561 E
  562 V
  563 D
  564 E
  565 L
  566 L
  567 Q
  568 K
  569 E
  570 Q
  571 N
  572 Y
  573 S
  574 D
  575 D
  576 V
  577 L
  578 A
  579 N
  580 M
  581 I
  582 S
  583 E
  584 P
  585 R
  586 I
  587 S
  588 Y
  589 G
  590 N
  591 D
  592 A
  593 L
  594 M
  595 P
  596 S
  597 L
  598 T
  599 E
  600 T
  601 K
  602 T
  603 T
  604 V
  605 E
  606 L
  607 L
  608 P
  609 V
  610 N
  611 G
  612 E
  613 F
  614 S
  615 L
  616 D
  617 D
  618 L
  619 Q
  620 P
  621 W
  622 H
  623 S
  624 F
  625 G
  626 A
  627 D
  628 S
  629 V
  630 P
  631 A
  632 N
  633 T
  634 E
  635 N
  636 E
  637 V
  638 E
  639 P
  640 V
  641 D
  642 A
  643 R
  644 P
  645 A
  646 A
  647 D
  648 R
  649 G
  650 L
  651 T
  652 T
  653 R
  654 P
  655 G
  656 S
  657 G
  658 L
  659 T
  660 N
  661 I
  662 K
  663 T
  664 E
  665 E
  666 I
  667 S
  668 E
  669 V
  670 K
  671 M
  672 D
  673 A
  674 E
  675 F
  676 R
  677 H
  678 D
  679 S
  680 G
  681 Y
  682 E
  683 V
  684 H
  685 H
  686 Q
  687 K
  688 L
  689 V
  690 F
  691 F
  692 A
  693 E
  694 D
  695 V
  696 G
  697 S
  698 N
  699 K
  700 G
  701 A
  702 I
  703 I
  704 G
  705 L
  706 M
  707 V
  708 G
  709 G
  710 V
  711 V
  712 I
  713 A
  714 T
  715 V
  716 I
  717 V
  718 I
  719 T
  720 L
  721 V
  722 M
  723 L
  724 K
  725 K
  726 K
  727 Q
  728 Y
  729 T
  730 S
  731 I
  732 H
  733 H
  734 G
  735 V
  736 V
  737 E
  738 V
  739 D
  740 A
  741 A
  742 V
  743 T
  744 P
  745 E
  746 E
  747 R
  748 H
  749 L
  750 S
  751 K
  752 M
  753 Q
  754 Q
  755 N
  756 G
  757 Y
  758 E
  759 N
  760 P
  761 T
  762 Y
  763 K
  764 F
  765 F
  766 E
  767 Q
  768 M
  769 Q
  770 N

Click on Feature Tree nodes to expand/close them.