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Update README.md

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Added UI compatibility

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  1. README.md +16 -0
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@@ -121,6 +121,22 @@ Example response:
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  {"choices":[{"finish_reason":"stop","index":0,"logprobs":null,"message":{"content":" Protein misfolding and aggregation are central to many diseases, including neurodegenerative disorders like Alzheimer's Disease (AD), Parkinson\u2019s Disease (PD), Huntington\u2019s Disease (HD) etc.\n\nIn these conditions, proteins fail to fold into their correct three-dimensional structures and instead aggregate or misfold in the cellular environment leading to formation of insoluble protein aggregates known as amyloid fibrils which are highly resistant to degradation by lysosomal enzymes.\n\nThese aberrant proteins can disrupt normal physiological processes, interfere with neuronal communication and eventually lead to cell death or apoptosis in the affected tissues/organs thereby causing disease symptoms associated with these conditions like memory loss (in Alzheimer\u2019s), movement difficulties etc.\n\nTherefore understanding protein folding pathways is crucial for developing therapeutic strategies aimed at preventing misfolding or promoting proper refolding of aberrant proteins back into their native conformations thereby restoring normal cellular function and alleviating disease symptoms associated with these conditions.","role":"assistant"}}],"created":null,"id":"rkllm_chat","object":"rkllm_chat","usage":{"completion_tokens":null,"prompt_tokens":null,"total_tokens":null}}
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  ```
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  # License
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  This conversion follows the license of the source model: [mit license](https://huggingface.co/datasets/choosealicense/licenses/blob/main/markdown/mit.md)
 
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  {"choices":[{"finish_reason":"stop","index":0,"logprobs":null,"message":{"content":" Protein misfolding and aggregation are central to many diseases, including neurodegenerative disorders like Alzheimer's Disease (AD), Parkinson\u2019s Disease (PD), Huntington\u2019s Disease (HD) etc.\n\nIn these conditions, proteins fail to fold into their correct three-dimensional structures and instead aggregate or misfold in the cellular environment leading to formation of insoluble protein aggregates known as amyloid fibrils which are highly resistant to degradation by lysosomal enzymes.\n\nThese aberrant proteins can disrupt normal physiological processes, interfere with neuronal communication and eventually lead to cell death or apoptosis in the affected tissues/organs thereby causing disease symptoms associated with these conditions like memory loss (in Alzheimer\u2019s), movement difficulties etc.\n\nTherefore understanding protein folding pathways is crucial for developing therapeutic strategies aimed at preventing misfolding or promoting proper refolding of aberrant proteins back into their native conformations thereby restoring normal cellular function and alleviating disease symptoms associated with these conditions.","role":"assistant"}}],"created":null,"id":"rkllm_chat","object":"rkllm_chat","usage":{"completion_tokens":null,"prompt_tokens":null,"total_tokens":null}}
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  ```
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+ ### 4) UI compatibility
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+
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+ This server exposes an **OpenAI-compatible Chat Completions API**.
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+
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+ You can connect it to any OpenAI-compatible client or UI (for example: [Open WebUI](https://github.com/open-webui/open-webui?utm_source=chatgpt.com))
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+ - Configure your client with the API base: `http://<SERVER_IP_ADDRESS>:8080` and use the endpoint: `/rkllm_chat`
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+ - Make sure the `model` field matches the converted model’s name, for example:
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+
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+ ```json
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+ {
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+ "model": "llama-3.1-8b-instruct",
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+ "messages": [{"role":"user","content":"Hello!"}],
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+ "stream": false
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+ }
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+ ```
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+
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  # License
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  This conversion follows the license of the source model: [mit license](https://huggingface.co/datasets/choosealicense/licenses/blob/main/markdown/mit.md)