rewire.itbenchmarks
Configuration

ESM-IF1

ESM-IF1 designs protein sequences conditioned on backbone coordinates.

Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models

1 evaluation · 5 results

How it worksESM-IF1 workflow
ESM-IF1 workflow1. Backbone coordinates. Then: 2. Geometric processing. Then: 3. Sequence transformer. Then: 4. Designed sequence or likelihoodESM-IF1 workflow1. Backbone coordinates. Then: 2. Geometric processing. Then: 3. Sequence transformer. Then: 4. Designed sequence or likelihoodESM-IF1 workflow1. Backbone coordinates. Then: 2. Geometric processing. Then: 3. Sequence transformer. Then: 4. Designed sequence or likelihood

Conceptual summary of the documented data flow; optional inputs and configured downstream stages must be reported for a reproducible evaluation.

Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models

Overview

Model type

Geometric encoder and inverse-folding transformer

Inputs

Protein backbone atom coordinates; the model supports missing backbone spans.

Outputs

Sampled protein sequences or conditional sequence likelihoods.

Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models

limited source coverage · Automated source review, 2026-09-16. All specifications and missing details

Evaluations and results

1 evaluation · 5 results. Different protocols are not a single leaderboard.

Filter evaluations

Applied filters: All linked evaluations

Exact evaluated configurations and original reported results
Tested configurationProtocol and datasetFindingEvidence and details
Configuration: ESM-IF1Task: ProteinGym ZS-SUB-AUC: Zero-shot substitutions, AUC
Dataset subset: ProteinGym substitution DMS assays (ProteinGym split)
0.73 auc
fraction · higher

Uncertainty: Not reported

Coverage: Not reported scored / Not reported eligible

Author-reported evaluation · Source checked
Methods, coverage and source

ESM-IF1 on ProteinGym ZS-SUB-AUC: Zero-shot substitutions, AUC

Zero-shot scoring of substitution assays, averaged over assays with the correction the paper describes.

Aggregation: Not reported

ProteinGym: Large-Scale Benchmarks for Protein Fitness Prediction and Design · Table 2, row(Inverse ESM-IF1), column(Zero-shot substitutions, AUC)
Configuration: ESM-IF1Task: ProteinGym ZS-SUB-MCC: Zero-shot substitutions, MCC
Dataset subset: ProteinGym substitution DMS assays (ProteinGym split)
0.331 mcc
correlation · higher

Uncertainty: Not reported

Coverage: Not reported scored / Not reported eligible

Author-reported evaluation · Source checked
Methods, coverage and source

ESM-IF1 on ProteinGym ZS-SUB-MCC: Zero-shot substitutions, MCC

Zero-shot scoring of substitution assays, averaged over assays with the correction the paper describes.

Aggregation: Not reported

ProteinGym: Large-Scale Benchmarks for Protein Fitness Prediction and Design · Table 2, row(Inverse ESM-IF1), column(Zero-shot substitutions, MCC)
Configuration: ESM-IF1Task: ProteinGym ZS-SUB-NDCG: Zero-shot substitutions, NDCG@10%
Dataset subset: ProteinGym substitution DMS assays (ProteinGym split)
0.748 ndcg
fraction · higher

Uncertainty: Not reported

Coverage: Not reported scored / Not reported eligible

Author-reported evaluation · Source checked
Methods, coverage and source

ESM-IF1 on ProteinGym ZS-SUB-NDCG: Zero-shot substitutions, NDCG@10%

Zero-shot scoring of substitution assays, averaged over assays with the correction the paper describes.

Aggregation: Not reported

ProteinGym: Large-Scale Benchmarks for Protein Fitness Prediction and Design · Table 2, row(Inverse ESM-IF1), column(Zero-shot substitutions, NDCG@10%)
Configuration: ESM-IF1Task: ProteinGym ZS-SUB-RECALL: Zero-shot substitutions, top 10% recall
Dataset subset: ProteinGym substitution DMS assays (ProteinGym split)
0.223 recall
fraction · higher

Uncertainty: Not reported

Coverage: Not reported scored / Not reported eligible

Author-reported evaluation · Source checked
Methods, coverage and source

ESM-IF1 on ProteinGym ZS-SUB-RECALL: Zero-shot substitutions, top 10% recall

Zero-shot scoring of substitution assays, averaged over assays with the correction the paper describes.

Aggregation: Not reported

ProteinGym: Large-Scale Benchmarks for Protein Fitness Prediction and Design · Table 2, row(Inverse ESM-IF1), column(Zero-shot substitutions, top 10% recall)
Configuration: ESM-IF1Task: ProteinGym ZS-SUB-SPEARMAN: Zero-shot substitutions, Spearman
Dataset subset: ProteinGym substitution DMS assays (ProteinGym split)
0.422 spearman
correlation · higher

Uncertainty: Not reported

Coverage: Not reported scored / Not reported eligible

Author-reported evaluation · Source checked
Methods, coverage and source

ESM-IF1 on ProteinGym ZS-SUB-SPEARMAN: Zero-shot substitutions, Spearman

Zero-shot scoring of substitution assays, averaged over assays with the correction the paper describes.

Aggregation: Not reported

ProteinGym: Large-Scale Benchmarks for Protein Fitness Prediction and Design · Table 2, row(Inverse ESM-IF1), column(Zero-shot substitutions, Spearman)

Source checking is not independent reproduction. Release 2026-09-29-06401fd5b220.

Use this model

How it works, versions and access

Related profile: ESM-IF1. This page retains the exact record and its evaluation context.

This configuration

Fitness prediction model evaluated by the ProteinGym authors under their harness.

record
ESM-IF1
configuration
Not reported
entity type
Configuration

How it works

How it works

ESM-IF1 designs protein sequences conditioned on backbone coordinates. Geometric-vector-perceptron input processing followed by a sequence-to-sequence transformer. The documented inputs are protein backbone atom coordinates; the model supports missing backbone spans. The output consists of sampled protein sequences or conditional sequence likelihoods.

Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
Versions and reproducibility

esm_if1_gvp4_t16_142M_UR50. The applicable input limits require configuration-specific checking.

Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
Strengths, limitations and unresolved questions

Strengths and limitations

Strengths and considerations

  • Structure-conditioned design can use partially missing backbones because training included span masking.
    Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models

Limitations and conditions

  • The public checkpoint name contains 142M but the README parameter table reports 124M. This discrepancy is retained rather than silently selecting a total.
    Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
Profile review details

Inspected pinned official documentation, relevant implementation files and named primary-paper sections. Claims are limited to those artifacts. Remaining field extraction and identity conflicts are explicit; no new performance claims, model runs or human review are implied.

Stable record: discovery-model-esm-if1

Specifications

Inputs, training, access and other details

Explanatory profile: limited source coverage · Automated source review, 2026-09-16. Review applies to the cited claims; unresolved fields are listed below. Numerical results retain their own review status.

Inputs, outputs and configuration
PropertyDescription and evidence
Model typeGeometric encoder and inverse-folding transformer
Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
ArchitectureGeometric-vector-perceptron input processing followed by a sequence-to-sequence transformer.
Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
InputsProtein backbone atom coordinates; the model supports missing backbone spans.
Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
OutputsSampled protein sequences or conditional sequence likelihoods.
Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
ParametersThe official checkpoint identifier contains 142M but the same repository model table states 124M. Both values are retained as a source discrepancy, without choosing a total.
Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
Known versionsesm_if1_gvp4_t16_142M_UR50.
Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
Training dataCATH 4.3 and predicted UniRef50 structures; README reports 12M structures predicted by AlphaFold2.
Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
Training cutoffThe official model table identifies CATH 4.3 and predicted UniRef50 structures, but does not state a common latest-structure or sequence date. · Not reported in inspected sources
Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
Context limitsThe reviewed inverse-folding usage and model table do not establish a universal maximum backbone length; the structural graph and selected inference configuration determine resource use. · Not reported in inspected sources
Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
Weights licenceSeparate checkpoint-distribution terms are not stated in the inspected release documentation and licence material. The source-code licence alone is not recorded as an explicit weight grant. · Not reported in inspected sources
Sources (2)facebookresearch/esm: README.md; facebookresearch/esm: LICENSE · README.md: Inverse folding and Pre-trained Models; LICENSE: licence text
AccessOfficial project documentation and implementation: https://github.com/facebookresearch/esm
Sourcesfacebookresearch/esm: README.md · README.md: Inverse folding and Pre-trained Models
Code licenceMIT
Sourcesfacebookresearch/esm: LICENSE · LICENSE: licence text

Evidence

Source checking verifies the cited claim or transcription. It does not establish independent reproduction.

Evidence table

Inspect claims, sources and review details

Trace each statement to its source and review. A context-only reference supports the record generally; it does not verify an individual field. Source checking does not reproduce an experiment.

One row per statement and cited source. Multiple citations are not independent evaluations. Shared locators are labelled explicitly.

1 evidence row matching the loaded filters

Claims, original sources and review scope · Release 2026-09-29-06401fd5b220
Property and statementOriginal source and locationReview and provenance
Relationship: family
discovery-model-esm-if1
Individual claims
ProteinGym: Large-Scale Benchmarks for Protein Fitness Prediction and Design

Original source ↗

Section 4.1 Zero-shot benchmarks; Table 2 named model row

Version: Primary full-text snapshot retrieved 2026-09-17; exact bytes pinned by SHA-256
Retrieved: 2026-09-17T08:06:28.522924+00:00

source checked

automated source review · 2026-09-23

Audit details

Source review establishes this relationship only. Exact evaluated configurations and original numerical review status remain unchanged. The primary table and baseline descriptions identify the evaluated family. ESM-1v remains an ensemble; ESM-2 remains 15B; inverse-folding conditions remain distinct.

Field: links:family:discovery-model-esm-if1

Claim: model-evaluation-identity-41267a3a1f7abb612d10

Source artifact SHA-256: a3b08cc4a6befd64620cf0f287d78d55a36dc2639955f52c5655f83833c50104

Hash scope: Exact retrieved primary paper artifact bytes.

Inspected artifact

Sources and history

View linked audit checks and correction history

Release 2026-09-29-06401fd5b220 · Record review: source checked

1 source records and release historyDownload this release
Technical metadata and extraction receipts

Stable ID: proteingym-method-esm-if1

areas
proteins-complexes
source locator
Table 2, row(Inverse ESM-IF1)
missing metadata
checkpoint revision: unreported; parameters: unextracted
Related records

Suggest a correction