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Peptide·map backed

ATLPC0017292

ATLPC0017292

SQLGDLGSGAGQGGGGGGSIRAAGGAFGKLEAAREEEFFYKKQKEQLERLKNDQIHQAEFHHQQIKEHEEAIQRHKDFLN…

Compare in workbenchDownload releaseAPI JSON
  • Length
    84 aa
  • Monoisotopic mass
    9332.7 Da
  • Net charge @ pH 7.4
    -0.40
  • Isoelectric point
    7.18
  • GRAVY
    -1.093
On this page
  • 01 Sequence & molecular identity
  • 02 Physicochemical profile
  • 03 Evidence landscape
  • 04 Product context
  • 05 Identity & reference map
  • 06 Data access & reproducibility
Coveragecounts only · not riskATLPC0017292
  • Measurements
    0
  • Endpoints
    0
  • Domains
    0/5
  • Products
    —
  • No matrix stability evidence
  • No clearance evidence
  • No immunogenicity context
  • No sequence liability cues
Jump to domain

Open the matching evidence section below

All evidence index
Exposure / Absorption
No evidence
Distribution / Barrier
No evidence
Metabolic & Proteolytic Stability
No evidence
Excretion / Persistence
No evidence
Toxicity / Safety
No evidence
01

Sequence & molecular identity

1 forms

Reviewed sequence, peptidoform forms, chemical representation, 3D references, and covalent topology used to interpret this peptide identity.

Sequence & peptidoform

·
Identity summarySpecific molecular form represented
Identity status
Specific molecular form represented
Residues
84
Peptidoform features
0
Documented molecular forms
1
Representations
4
Documented molecular forms1 form linked to this peptide identity
FormTopologyModificationsConnectionsRepresentationsMeasurements
ATLPF0018907———Notation only—
Residue view
Residue display
84 residues
S1Q2L3G4D5L6G7S8G9A10G11Q12G13G14G15G16G17G18S19I20R21A22A23G24G25A26F27G28K29L30E31A32A33R34E35E36E37F38F39Y40K41K42Q43K44E45Q46L47E48R49L50K51N52D53Q54I55H56Q57A58E59F60H61H62Q63Q64I65K66E67H68E69E70A71I72Q73R74H75K76D77F78L79N80N81L82H83K84
Side-chain classNonpolarPolarBasic (+)Acidic (−)Modified

Soft tints mark standard side-chain classes for scanning. Primary emphasis is reserved for reported modifications, termini, secondary-structure tracks, and topology links.

Peptidoform features

Features are shown only when a reported notation or topology record supports them.

No terminal modification, residue-level marker, disulfide, staple, coordination, or other topology signal is currently available.

Structure & chemistry

·
Chemical representationSMILES available
2D structure·RDKit.js
rendering molecule…
Canonical SMILES
CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](C)NC(=O)CNC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)CNC(=O)CNC(=O)CNC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(=O)O)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CO)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CCCCN)C(=O)O
Representation class

How the current release can interpret this identity chemically.

map backed
Parent-residue sequence

Residue string used for positional interpretation when available.

SQLGDLGSGAGQGGGGGGSIRAAGGAFGKLEAAREEEFFYKKQKEQLERLKNDQIHQAEFHHQQIKEHEEAIQRHKDFLNNLHK
HELM

Polymer notation for modified peptide representation when available.

SQLGDLGSGAGQGGGGGGSIRAAGGAFGKLEAAREEEFFYKKQKEQLERLKNDQIHQAEFHHQQIKEHEEAIQRHKDFLNNLHK
SMILES

Chemical graph string used for atom-level 2D depiction when available.

CC[C@H](C)[C@H](NC(=O)[C@H](C)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)CNC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](C)NC(=O)CNC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)CNC(=O)CNC(=O)CNC(=O)CNC(=O)CNC(=O)CNC(=O)[C@H](CCC(N)=O)NC(=O)CNC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CO)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(=O)O)NC(=O)CNC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](N)CO)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)CC)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CCCCN)C(=O)O
3D structure referencesnone attached
3D structure not available

A 3D structure isn't available for this peptide in the current release. Chemistry and topology fields remain available when represented by sequence, HELM, or SMILES.

Covalent topology & modifications1 signal
FeaturePositionsInterpretationLink
Form-level topologyATLPF0018907Open-chain form. Residue-level connection endpoints are shown separately when available.Not linked
02

Physicochemical profile

10 descriptors

Computed sequence-derived descriptors and any measured physicochemical evidence such as lipophilicity. Computed values are interpretation aids, not experimental ADMET measurements.

·
Core descriptors84 aa · pI 7.2 · GRAVY -1.09
Length
84 aa
Monoisotopic mass
9332.69 Da
Average mass
9338.27 Da
Net charge at pH 7.4
-0.40
Estimated pI
7.18
GRAVY
-1.093
KD-positive residues
28.6%
Aromatic residues
7.1%
Developability interpretation
Ionization context
pH 7.4 close to pI
Hydrophobicity balance
Leans hydrophilic
Amphipathic moment (μH)
0.50
Computation boundary
Standard-sequence only
Charge & residue composition
pH charge context

Modeled net charge across common formulation and assay pH checkpoints.

pH 2
18.86
pH 5
6.19
pH 6
3.71
pH 7.4
-0.39
pH 9
-1.90
pH 12
-11.47
Residue-class composition

Grouped composition is often more interpretable than a long amino-acid list.

Acidic (D,E)
13 · 15.5%
Basic (K,R,H)
18 · 21.4%
Polar uncharged (N,Q,S,T)
15 · 17.9%
Hydrophobic aliphatic (A,V,I,L,M)
19 · 22.6%
Aromatic (F,W,Y)
6 · 7.1%
Conformational / sulfur (G,P,C)
13 · 15.5%
Top residues
G1315.5%E1011.9%Q910.7%A89.5%K89.5%L78.3%H67.1%F56.0%
Hydropathy & amphipathic windows
Hydropathy windows

Seven-residue sliding windows expose local patches hidden by whole-sequence GRAVY.

Most hydrophobic window
22-28
AAGGAFG
GRAVY 1.000
Most hydrophilic window
40-46
YKKQKEQ
GRAVY -3.357
78 local hydropathy windows scanned. A local patch is context for solubility, adsorption, and membrane interaction review, not a standalone endpoint.
Amphipathic-window scan

Top alpha-helix hydrophobic-moment windows across 12, 15, 18, and 21 residues.

15 aa window
70-84
EAIQRHKDFLNNLHK
μH 1.79 · charge 1.2
12 aa window
71-82
AIQRHKDFLNNL
μH 1.75 · charge 1.1
12 aa window
70-81
EAIQRHKDFLNN
μH 1.74 · charge 0.1
12 aa window
73-84
QRHKDFLNNLHK
μH 1.73 · charge 2.2
12 aa window
63-74
QQIKEHEEAIQR
μH 1.66 · charge -0.9
Sequence-liability cues
Sequence-liability notes

Motifs are review prompts for formulation or CMC interpretation; they are not degradation predictions.

No conservative sequence-liability motifs from the current rule set are present.
Alpha-helix amphipathic projection
Helical wheel · Edmundson projection
μH = 0.50100°/residue · 84 aa
μH1: S (Ser) · Polar · K-D -0.8S12: Q (Gln) · Polar · K-D -3.5Q3: L (Leu) · Hydrophobic · K-D 3.8L4: G (Gly) · Special · K-D -0.4G5: D (Asp) · Acidic − · K-D -3.5D56: L (Leu) · Hydrophobic · K-D 3.8L7: G (Gly) · Special · K-D -0.4G8: S (Ser) · Polar · K-D -0.8S9: G (Gly) · Special · K-D -0.4G10: A (Ala) · Hydrophobic · K-D 1.8A1011: G (Gly) · Special · K-D -0.4G12: Q (Gln) · Polar · K-D -3.5Q13: G (Gly) · Special · K-D -0.4G14: G (Gly) · Special · K-D -0.4G15: G (Gly) · Special · K-D -0.4G1516: G (Gly) · Special · K-D -0.4G17: G (Gly) · Special · K-D -0.4G18: G (Gly) · Special · K-D -0.4G19: S (Ser) · Polar · K-D -0.8S20: I (Ile) · Hydrophobic · K-D 4.5I2021: R (Arg) · Basic + · K-D -4.5R22: A (Ala) · Hydrophobic · K-D 1.8A23: A (Ala) · Hydrophobic · K-D 1.8A24: G (Gly) · Special · K-D -0.4G25: G (Gly) · Special · K-D -0.4G2526: A (Ala) · Hydrophobic · K-D 1.8A27: F (Phe) · Aromatic · K-D 2.8F28: G (Gly) · Special · K-D -0.4G29: K (Lys) · Basic + · K-D -3.9K30: L (Leu) · Hydrophobic · K-D 3.8L3031: E (Glu) · Acidic − · K-D -3.5E32: A (Ala) · Hydrophobic · K-D 1.8A33: A (Ala) · Hydrophobic · K-D 1.8A34: R (Arg) · Basic + · K-D -4.5R35: E (Glu) · Acidic − · K-D -3.5E3536: E (Glu) · Acidic − · K-D -3.5E37: E (Glu) · Acidic − · K-D -3.5E38: F (Phe) · Aromatic · K-D 2.8F39: F (Phe) · Aromatic · K-D 2.8F40: Y (Tyr) · Aromatic · K-D -1.3Y4041: K (Lys) · Basic + · K-D -3.9K42: K (Lys) · Basic + · K-D -3.9K43: Q (Gln) · Polar · K-D -3.5Q44: K (Lys) · Basic + · K-D -3.9K45: E (Glu) · Acidic − · K-D -3.5E4546: Q (Gln) · Polar · K-D -3.5Q47: L (Leu) · Hydrophobic · K-D 3.8L48: E (Glu) · Acidic − · K-D -3.5E49: R (Arg) · Basic + · K-D -4.5R50: L (Leu) · Hydrophobic · K-D 3.8L5051: K (Lys) · Basic + · K-D -3.9K52: N (Asn) · Polar · K-D -3.5N53: D (Asp) · Acidic − · K-D -3.5D54: Q (Gln) · Polar · K-D -3.5Q55: I (Ile) · Hydrophobic · K-D 4.5I5556: H (His) · Basic + · K-D -3.2H57: Q (Gln) · Polar · K-D -3.5Q58: A (Ala) · Hydrophobic · K-D 1.8A59: E (Glu) · Acidic − · K-D -3.5E60: F (Phe) · Aromatic · K-D 2.8F6061: H (His) · Basic + · K-D -3.2H62: H (His) · Basic + · K-D -3.2H63: Q (Gln) · Polar · K-D -3.5Q64: Q (Gln) · Polar · K-D -3.5Q65: I (Ile) · Hydrophobic · K-D 4.5I6566: K (Lys) · Basic + · K-D -3.9K67: E (Glu) · Acidic − · K-D -3.5E68: H (His) · Basic + · K-D -3.2H69: E (Glu) · Acidic − · K-D -3.5E70: E (Glu) · Acidic − · K-D -3.5E7071: A (Ala) · Hydrophobic · K-D 1.8A72: I (Ile) · Hydrophobic · K-D 4.5I73: Q (Gln) · Polar · K-D -3.5Q74: R (Arg) · Basic + · K-D -4.5R75: H (His) · Basic + · K-D -3.2H7576: K (Lys) · Basic + · K-D -3.9K77: D (Asp) · Acidic − · K-D -3.5D78: F (Phe) · Aromatic · K-D 2.8F79: L (Leu) · Hydrophobic · K-D 3.8L80: N (Asn) · Polar · K-D -3.5N8081: N (Asn) · Polar · K-D -3.5N82: L (Leu) · Hydrophobic · K-D 3.8L83: H (His) · Basic + · K-D -3.2H84: K (Lys) · Basic + · K-D -3.9K84
Hydrophobic moment0.50
Mean K-D hydropathy-1.09
Approx. net charge-1
Projection angle100° / residue
The pale sector marks the direction of the hydrophobic face inferred from μH. This is a projection assumption, not a measured fold.
HydrophobicAromaticPolarBasic +Acidic −Specialhydrophobic faceμH arrow → hydrophobic face

The projection assumes an α-helix conformation; a long μH arrow indicates an amphipathic helix, common in antimicrobial peptides.Sequence > 30 aa — only termini and every fifth position are numbered because later turns share earlier wheel angles.

Method notes

Charge model: side-chain pKa D 3.9, E 4.1, C 8.5, Y 10.1, H 6.5, K 10.8, R 12.5 with EMBOSS termini. pI is estimated by binary search on modeled net charge. Hydropathy uses Kyte-Doolittle values; hydrophobic moment follows the Eisenberg alpha-helix vector-sum convention. When the basis is a parent-residue sequence, modified chemistry is intentionally not inferred.

Computed developability descriptors

Deterministic descriptors computed from the reviewed sequence or chemical structure (RDKit), each anchored to a literature method. These are computed estimates for developability interpretation — not experimental measurements — and are validated against independent reference implementations.

Sequence-derived

Computed from the standard parent-residue sequence; protein-origin metrics defined at any length.

Aliphatic index
60.60
Instability index
45.5

Above 40 — predicted unstable in vitro.

Boman index
2.51 kcal/mol

Above 2.48 — elevated potential protein-binding.

Molar extinction coefficient (280 nm)
1,490 M⁻¹·cm⁻¹

A280 (1 g/L) ≈ 0.16

Structure-derived (developability)

Computed from the representative peptidoform's chemical structure. Rule-of-5 / beyond-Ro5 framing per Lipinski/Doak.

Topological polar surface area
4189.4 Ų
Computed logP (Crippen)
-47.38

Computed logP — distinct from the measured logD endpoint.

Hydrogen-bond donors
140
Hydrogen-bond acceptors
132
Rotatable bonds
333
Rule-of-5 / beyond-Ro5 flags
Beyond bRo5

3 Ro5 violations · MW 9,338.29 Da

03

Evidence landscape

Cross-domain evidence distribution and measurement-level detail. No assay-level evidence is available for this peptide in the current release.

No endpoint-level measurements returned

No ADMET endpoint evidence is attached to this peptide yet.

/evidence/drilldown
04

Product context

Product-level route, label, and clinical context that frames peptide-level evidence. A peptide-level summary only; product pages keep the full drilldown.

No product association in this release

This peptide is currently interpreted from sequence, structure, physicochemical, and ADMET evidence only.

Browse products
05

Identity & reference map

Reference-level support for checking reported names, sequence notation, and peptide identity agreement.

No identity references available

No reported identity references are available for this peptide in the current release.

06

Data access & reproducibility

Stable record access, analysis-ready files, and scripted retrieval for reproducing this profile view.

·
Record scopePublic release
ATL peptide ID
ATLPC0017292
Identity type
canonical sequence
ADMET endpoints
0
Evidence records
0
Reference groups
1
Release view
Public release
Data access

Structured peptide profile

JSON

Peptide-specific profile used by this page, including identity and evidence context.

Open JSON

Peptide catalogue

TSV

Complete frozen peptide table. Filter the ATL peptide ID column locally to isolate this record.

Download catalogue

Measurement catalogue

TSV

Complete frozen measurement table. Join or filter by ATL peptide ID for peptide-level analysis.

Download measurements
Programmatic access

The request returns the same structured peptide record used by this profile. The tabular downloads are complete frozen release tables and should be filtered locally by ATL peptide ID.

Open endpoint
GET /api/v1/peptides/ATLPC0017292
open
curl -sS 'https://admetatlas.scbdd.com/api/v1/peptides/ATLPC0017292' \
  -H 'accept: application/json' \
  -H 'X-Visibility: public_release'
ADMETatlas
peptide evidence atlas

ADMETatlas is an open, curated atlas of ADMET evidence for therapeutic peptides — spanning developability, membrane permeability and blood–brain-barrier transport, immune-recognition context, and approved-product context. Every measurement stays linked to its original source, with stable identifiers and transparent curation, so results can be traced, cited, and reproduced.

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