pax_global_header00006660000000000000000000000064146127310260014514gustar00rootroot0000000000000052 comment=128e7837bdd908c293e889037f9ae3183a6c3785 prodigy-2.2.2/000077500000000000000000000000001461273102600131745ustar00rootroot00000000000000prodigy-2.2.2/.github/000077500000000000000000000000001461273102600145345ustar00rootroot00000000000000prodigy-2.2.2/.github/workflows/000077500000000000000000000000001461273102600165715ustar00rootroot00000000000000prodigy-2.2.2/.github/workflows/ci.yml000066400000000000000000000013321461273102600177060ustar00rootroot00000000000000name: ci on: push jobs: test: runs-on: ubuntu-latest steps: - uses: actions/checkout@v3 - uses: actions/setup-python@v4 with: python-version: "3.10" - uses: snok/install-poetry@v1 with: version: 1.3.2 virtualenvs-create: true virtualenvs-in-project: true - run: poetry install --no-interaction --no-root - run: poetry run pytest --cov --cov-report xml:coverage.xml --cov-append -vv --hypothesis-show-statistics - name: Run codacy-coverage-reporter uses: codacy/codacy-coverage-reporter-action@v1 with: project-token: ${{ secrets.CODACY_PROJECT_TOKEN }} coverage-reports: coverage.xml prodigy-2.2.2/.github/workflows/docker-publish.yml000066400000000000000000000033731461273102600222350ustar00rootroot00000000000000# name: Create and publish a Docker image on: push: # run only against tags tags: - "*" env: REGISTRY: ghcr.io IMAGE_NAME: ${{ github.repository }} # There is a single job in this workflow. It's configured to run on the latest available version of Ubuntu. jobs: build-and-push-image: runs-on: ubuntu-latest # Sets the permissions granted to the `GITHUB_TOKEN` for the actions in this job. permissions: contents: read packages: write steps: - name: Checkout repository uses: actions/checkout@v4 # Uses the `docker/login-action` action to log in to the Container registry registry using the account and password that will publish the packages. Once published, the packages are scoped to the account defined here. - name: Log in to the Container registry uses: docker/login-action@v3 with: registry: ${{ env.REGISTRY }} username: ${{ github.actor }} password: ${{ secrets.GITHUB_TOKEN }} # This step uses [docker/metadata-action](https://github.com/docker/metadata-action#about) to extract tags and labels that will be applied to the specified image. The `id` "meta" allows the output of this step to be referenced in a subsequent step. The `images` value provides the base name for the tags and labels. - name: Extract metadata (tags, labels) for Docker id: meta uses: docker/metadata-action@v5 with: images: ${{ env.REGISTRY }}/${{ env.IMAGE_NAME }} - name: Build and push uses: docker/build-push-action@v5 with: context: . push: ${{ github.event_name != 'pull_request' }} tags: ${{ steps.meta.outputs.tags }} labels: ${{ steps.meta.outputs.labels }} prodigy-2.2.2/.github/workflows/pypi-publish.yml000066400000000000000000000012071461273102600217410ustar00rootroot00000000000000name: publish to PyPI on: release: types: [published] jobs: pypi_release: name: Builds Using Poetry and Publishes to PyPI runs-on: ubuntu-latest steps: - uses: actions/checkout@v4 - uses: actions/setup-python@v4 with: python-version: "3.11" - uses: snok/install-poetry@v1 with: version: 1.3.2 virtualenvs-create: true virtualenvs-in-project: true - run: poetry install - run: poetry run pytest - run: poetry config pypi-token.pypi "${{ secrets.PYPI_API_KEY }}" - name: Publish package run: poetry publish --build prodigy-2.2.2/.gitignore000066400000000000000000000060361461273102600151710ustar00rootroot00000000000000# Byte-compiled / optimized / DLL files __pycache__/ *.py[cod] *$py.class # C extensions *.so # Distribution / packaging .Python build/ develop-eggs/ dist/ downloads/ eggs/ .eggs/ # lib/ lib64/ parts/ sdist/ var/ wheels/ share/python-wheels/ *.egg-info/ .installed.cfg *.egg MANIFEST # PyInstaller # Usually these files are written by a python script from a template # before PyInstaller builds the exe, so as to inject date/other infos into it. *.manifest *.spec # Installer logs pip-log.txt pip-delete-this-directory.txt # Unit test / coverage reports htmlcov/ .tox/ .nox/ .coverage .coverage.* .cache nosetests.xml coverage.xml *.cover *.py,cover .hypothesis/ .pytest_cache/ cover/ # Translations *.mo *.pot # Django stuff: *.log local_settings.py db.sqlite3 db.sqlite3-journal # Flask stuff: instance/ .webassets-cache # Scrapy stuff: .scrapy # Sphinx documentation docs/_build/ # PyBuilder .pybuilder/ target/ # Jupyter Notebook .ipynb_checkpoints # IPython profile_default/ ipython_config.py # pyenv # For a library or package, you might want to ignore these files since the code is # intended to run in multiple environments; otherwise, check them in: # .python-version # pipenv # According to pypa/pipenv#598, it is recommended to include Pipfile.lock in version control. # However, in case of collaboration, if having platform-specific dependencies or dependencies # having no cross-platform support, pipenv may install dependencies that don't work, or not # install all needed dependencies. #Pipfile.lock # poetry # Similar to Pipfile.lock, it is generally recommended to include poetry.lock in version control. # This is especially recommended for binary packages to ensure reproducibility, and is more # commonly ignored for libraries. # https://python-poetry.org/docs/basic-usage/#commit-your-poetrylock-file-to-version-control #poetry.lock # pdm # Similar to Pipfile.lock, it is generally recommended to include pdm.lock in version control. #pdm.lock # pdm stores project-wide configurations in .pdm.toml, but it is recommended to not include it # in version control. # https://pdm.fming.dev/#use-with-ide .pdm.toml # PEP 582; used by e.g. github.com/David-OConnor/pyflow and github.com/pdm-project/pdm __pypackages__/ # Celery stuff celerybeat-schedule celerybeat.pid # SageMath parsed files *.sage.py # Environments .env .venv env/ venv/ ENV/ env.bak/ venv.bak/ # Spyder project settings .spyderproject .spyproject # Rope project settings .ropeproject # mkdocs documentation /site # mypy .mypy_cache/ .dmypy.json dmypy.json # Pyre type checker .pyre/ # pytype static type analyzer .pytype/ # Cython debug symbols cython_debug/ # PyCharm # JetBrains specific template is maintained in a separate JetBrains.gitignore that can # be found at https://github.com/github/gitignore/blob/main/Global/JetBrains.gitignore # and can be added to the global gitignore or merged into this file. For a more nuclear # option (not recommended) you can uncomment the following to ignore the entire idea folder. #.idea/ .vscode/ poetry.lock prodigy-2.2.2/.howfairis.yml000066400000000000000000000006641461273102600157760ustar00rootroot00000000000000## Uncomment a line if you want to skip a given category of checks #skip_repository_checks_reason: #skip_license_checks_reason: #skip_registry_checks_reason: #skip_citation_checks_reason: skip_checklist_checks_reason: "I'm using the Codacy dashboard to guide my development" ignore_commented_badges: false prodigy-2.2.2/.trunk/000077500000000000000000000000001461273102600144155ustar00rootroot00000000000000prodigy-2.2.2/.trunk/.gitignore000066400000000000000000000001051461273102600164010ustar00rootroot00000000000000*out *logs *actions *notifications plugins user_trunk.yaml user.yaml prodigy-2.2.2/.trunk/configs/000077500000000000000000000000001461273102600160455ustar00rootroot00000000000000prodigy-2.2.2/.trunk/configs/.isort.cfg000066400000000000000000000000311461273102600177360ustar00rootroot00000000000000[settings] profile=black prodigy-2.2.2/.trunk/configs/.markdownlint.yaml000066400000000000000000000003311461273102600215150ustar00rootroot00000000000000# Autoformatter friendly markdownlint config (all formatting rules disabled) default: true blank_lines: false bullet: false html: false indentation: false line_length: false spaces: false url: false whitespace: false prodigy-2.2.2/.trunk/trunk.yaml000066400000000000000000000010371461273102600164450ustar00rootroot00000000000000version: 0.1 cli: version: 1.4.1 plugins: sources: - id: trunk ref: v0.0.9 uri: https://github.com/trunk-io/plugins lint: enabled: - gitleaks@8.15.3 - actionlint@1.6.23 - markdownlint@0.33.0 - git-diff-check - prettier@2.8.3 - taplo@0.7.0 - flake8@6.0.0 - black@23.1.0 - isort@5.12.0 runtimes: enabled: - go@1.18.3 - node@18.12.1 - python@3.10.8 actions: enabled: - trunk-announce - trunk-check-pre-push - trunk-fmt-pre-commit - trunk-upgrade-available prodigy-2.2.2/CITATION.cff000066400000000000000000000024661461273102600150760ustar00rootroot00000000000000# This CITATION.cff file was generated with cffinit. # Visit https://bit.ly/cffinit to generate yours today! cff-version: 1.2.0 title: Prodigy message: >- If you use this software, please cite it using the metadata from this file. type: software authors: - given-names: Anna family-names: Vangone affiliation: Utrecht University - given-names: Alexandre name-particle: MJJ family-names: Bonvin affiliation: Utrecht University - given-names: Joerg family-names: Schaarschmidt affiliation: Utrecht University - given-names: Rodrigo family-names: Vargas Honorato affiliation: Utrecht University - given-names: Brian family-names: Jimenez affiliation: Utrecht University - given-names: Joao family-names: Rodrigues affiliation: Utrecht University identifiers: - type: doi value: 10.1093/bioinformatics/btw514 description: DOI of the web service version - type: doi value: 10.7554/eLife.07454 - type: doi value: 10.1016/j.jmb.2014.04.017 repository-code: 'https://github.com/haddocking/prodigy' url: 'https://wenmr.science.uu.nl/prodigy' abstract: >- A tool to predict binding affinity values for protein-protein complexes from atomic structures. keywords: - binding affinity - computational biology - protein-protein license: Apache-2.0 prodigy-2.2.2/CODE_OF_CONDUCT.md000066400000000000000000000125661461273102600160050ustar00rootroot00000000000000# Contributor Covenant Code of Conduct ## Our Pledge We as members, contributors, and leaders pledge to make participation in our community a harassment-free experience for everyone, regardless of age, body size, visible or invisible disability, ethnicity, sex characteristics, gender identity and expression, level of experience, education, socio-economic status, nationality, personal appearance, race, caste, color, religion, or sexual identity and orientation. We pledge to act and interact in ways that contribute to an open, welcoming, diverse, inclusive, and healthy community. ## Our Standards Examples of behavior that contributes to a positive environment for our community include: - Demonstrating empathy and kindness toward other people - Being respectful of differing opinions, viewpoints, and experiences - Giving and gracefully accepting constructive feedback - Accepting responsibility and apologizing to those affected by our mistakes, and learning from the experience - Focusing on what is best not just for us as individuals, but for the overall community Examples of unacceptable behavior include: - The use of sexualized language or imagery, and sexual attention or advances of any kind - Trolling, insulting or derogatory comments, and personal or political attacks - Public or private harassment - Publishing others' private information, such as a physical or email address, without their explicit permission - Other conduct which could reasonably be considered inappropriate in a professional setting ## Enforcement Responsibilities Community leaders are responsible for clarifying and enforcing our standards of acceptable behavior and will take appropriate and fair corrective action in response to any behavior that they deem inappropriate, threatening, offensive, or harmful. Community leaders have the right and responsibility to remove, edit, or reject comments, commits, code, wiki edits, issues, and other contributions that are not aligned to this Code of Conduct, and will communicate reasons for moderation decisions when appropriate. ## Scope This Code of Conduct applies within all community spaces, and also applies when an individual is officially representing the community in public spaces. Examples of representing our community include using an official e-mail address, posting via an official social media account, or acting as an appointed representative at an online or offline event. ## Enforcement Instances of abusive, harassing, or otherwise unacceptable behavior may be reported to the community leaders responsible for enforcement at `prodigy.bonvinlab@gmail.com`. All complaints will be reviewed and investigated promptly and fairly. All community leaders are obligated to respect the privacy and security of the reporter of any incident. ## Enforcement Guidelines Community leaders will follow these Community Impact Guidelines in determining the consequences for any action they deem in violation of this Code of Conduct: ### 1. Correction **Community Impact**: Use of inappropriate language or other behavior deemed unprofessional or unwelcome in the community. **Consequence**: A private, written warning from community leaders, providing clarity around the nature of the violation and an explanation of why the behavior was inappropriate. A public apology may be requested. ### 2. Warning **Community Impact**: A violation through a single incident or series of actions. **Consequence**: A warning with consequences for continued behavior. No interaction with the people involved, including unsolicited interaction with those enforcing the Code of Conduct, for a specified period of time. This includes avoiding interactions in community spaces as well as external channels like social media. Violating these terms may lead to a temporary or permanent ban. ### 3. Temporary Ban **Community Impact**: A serious violation of community standards, including sustained inappropriate behavior. **Consequence**: A temporary ban from any sort of interaction or public communication with the community for a specified period of time. No public or private interaction with the people involved, including unsolicited interaction with those enforcing the Code of Conduct, is allowed during this period. Violating these terms may lead to a permanent ban. ### 4. Permanent Ban **Community Impact**: Demonstrating a pattern of violation of community standards, including sustained inappropriate behavior, harassment of an individual, or aggression toward or disparagement of classes of individuals. **Consequence**: A permanent ban from any sort of public interaction within the community. ## Attribution This Code of Conduct is adapted from the [Contributor Covenant][homepage], version 2.1, available at [https://www.contributor-covenant.org/version/2/1/code_of_conduct.html][v2.1]. Community Impact Guidelines were inspired by [Mozilla's code of conduct enforcement ladder][Mozilla CoC]. For answers to common questions about this code of conduct, see the FAQ at [https://www.contributor-covenant.org/faq][FAQ]. Translations are available at [https://www.contributor-covenant.org/translations][translations]. [homepage]: https://www.contributor-covenant.org [v2.1]: https://www.contributor-covenant.org/version/2/1/code_of_conduct.html [Mozilla CoC]: https://github.com/mozilla/diversity [FAQ]: https://www.contributor-covenant.org/faq [translations]: https://www.contributor-covenant.org/translations prodigy-2.2.2/CONTRIBUTING.md000066400000000000000000000010321461273102600154210ustar00rootroot00000000000000# Contributing with PRODIGY ## Reporting issues If you find a bug or have a feature request, please report it in the [issue tracker](https://github.com/haddocking/prodigy/issues) ## Contributing code We welcome contributions to PRODIGY. If you would like to contribute, please fork the repository and make a pull request. ## Development conventions Please refer to the [development guidelines](DEVELOPMENT.md) for more details. ## Contact If you have any questions, please contact us at [ask.bioexcel.eu](https://ask.bioexcel.eu) prodigy-2.2.2/DEVELOPMENT.md000066400000000000000000000013361461273102600153030ustar00rootroot00000000000000# PRODIGY Development ## Installation We use `poetry` to manage the dependencies and the virtual environment, so you need to install it first; check the [official documentation](https://python-poetry.org/docs/#installation) for more details. Clone the repository and install the dependencies: ```text git clone https://github.com/haddocking/prodigy.git && cd prodigy poetry install ``` ## Testing To run the tests, use the following command: ```text python -m unittest ``` ## Code style We use `trunk` as the "all-purpose" linting tool, check its [documentation](https://docs.trunk.io/docs/install). To check for code style issues, run: ```text trunk check ``` To automatically fix the issues, run: ```text trunk fmt ``` prodigy-2.2.2/Dockerfile000066400000000000000000000004511461273102600151660ustar00rootroot00000000000000#============================================================================================== FROM python:3.10 WORKDIR /opt/software COPY . . RUN pip install . WORKDIR /data ENTRYPOINT [ "prodigy" ] #============================================================================================== prodigy-2.2.2/LICENSE000066400000000000000000000250551461273102600142100ustar00rootroot00000000000000 Apache License Version 2.0, January 2004 http://www.apache.org/licenses/ TERMS AND CONDITIONS FOR USE, REPRODUCTION, AND DISTRIBUTION 1. Definitions. "License" shall mean the terms and conditions for use, reproduction, and distribution as defined by Sections 1 through 9 of this document. "Licensor" shall mean the copyright owner or entity authorized by the copyright owner that is granting the License. "Legal Entity" shall mean the union of the acting entity and all other entities that control, are controlled by, or are under common control with that entity. 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See the License for the specific language governing permissions and limitations under the License. prodigy-2.2.2/README.md000066400000000000000000000146651461273102600144670ustar00rootroot00000000000000# PRODIGY / Binding Affinity Prediction [![ci](https://github.com/haddocking/prodigy/actions/workflows/ci.yml/badge.svg)](https://github.com/haddocking/prodigy/actions/workflows/ci.yml) [![Codacy Badge](https://app.codacy.com/project/badge/Grade/98180cbac27d4a5aaf46a3dd72c3174d)](https://www.codacy.com/gh/haddocking/prodigy/dashboard?utm_source=github.com&utm_medium=referral&utm_content=haddocking/prodigy&utm_campaign=Badge_Grade) [![Codacy Badge](https://app.codacy.com/project/badge/Coverage/98180cbac27d4a5aaf46a3dd72c3174d)](https://www.codacy.com/gh/haddocking/prodigy/dashboard?utm_source=github.com&utm_medium=referral&utm_content=haddocking/prodigy&utm_campaign=Badge_Coverage) [![SQAaaS badge shields.io](https://img.shields.io/badge/sqaaas%20software-gold-yellow)](https://api.eu.badgr.io/public/assertions/w8HcpcH4Svi3-UZ93LHHMA "SQAaaS gold badge achieved") [![fair-software.eu](https://img.shields.io/badge/fair--software.eu-%E2%97%8F%20%20%E2%97%8F%20%20%E2%97%8B%20%20%E2%97%8F%20%20%E2%97%8F-yellow)](https://fair-software.eu) [![Contributor Covenant](https://img.shields.io/badge/Contributor%20Covenant-2.1-4baaaa.svg)](code_of_conduct.md) [![DOI](https://zenodo.org/badge/DOI/10.5281/zenodo.1193244.svg)](https://doi.org/10.5281/zenodo.1193244) [![SQAaaS badge](https://github.com/EOSC-synergy/SQAaaS/raw/master/badges/badges_150x116/badge_software_gold.png)](https://api.eu.badgr.io/public/assertions/w8HcpcH4Svi3-UZ93LHHMA "SQAaaS gold badge achieved") * * * PRODIGY is also available as a web service @ [wenmr.science.uu.nl/prodigy](https://wenmr.science.uu.nl/prodigy/) ## Installation ```text git clone https://github.com/haddocking/prodigy && cd prodigy pip install . ``` If you want to develop PRODIGY, check [DEVELOPMENT](DEVELOPMENT.md) for more details. ## Usage ```bash prodigy [--selection ] ``` To get a list of all the possible options. ```bash $ prodigy --help usage: prodigy [-h] [--distance-cutoff DISTANCE_CUTOFF] [--acc-threshold ACC_THRESHOLD] [--temperature TEMPERATURE] [--contact_list] [--pymol_selection] [-q] [-V] [--selection A B [A,B C ...]] structf Binding affinity predictor based on Intermolecular Contacts (ICs). Anna Vangone and Alexandre M.J.J. Bonvin, Contacts-based prediction of binding affinity in protein-protein complexes. eLife (2015) positional arguments: structf Structure to analyse in PDB or mmCIF format options: -h, --help show this help message and exit --distance-cutoff DISTANCE_CUTOFF Distance cutoff to calculate ICs --acc-threshold ACC_THRESHOLD Accessibility threshold for BSA analysis --temperature TEMPERATURE Temperature (C) for Kd prediction --contact_list Output a list of contacts --pymol_selection Output a script to highlight the interface (pymol) -q, --quiet Outputs only the predicted affinity value -V, --version Print the version and exit. Selection Options: By default, all intermolecular contacts are taken into consideration, a molecule being defined as an isolated group of amino acids sharing a common chain identifier. In specific cases, for example antibody-antigen complexes, some chains should be considered as a single molecule. Use the --selection option to provide collections of chains that should be considered for the calculation. Separate by a space the chains that are to be considered _different_ molecules. Use commas to include multiple chains as part of a single group: --selection A B => Contacts calculated (only) between chains A and B. --selection A,B C => Contacts calculated (only) between chains A and C; and B and C. --selection A B C => Contacts calculated (only) between chains A and B; B and C; and A and C. --selection A B [A,B C ...] ``` ## Example Download the PDB [3BZD](https://www.rcsb.org/structure/3bzd) and run PRODIGY on it. ```bash $ curl -o 3bzd.pdb https://files.rcsb.org/download/3BZD.pdb $ prodigy 3bzd.pdb [+] Reading structure file: /Users/rvhonorato/dbg/3bzd.pdb [+] Parsed structure file 3bzd (2 chains, 343 residues) [+] No. of intermolecular contacts: 51 [+] No. of charged-charged contacts: 4 [+] No. of charged-polar contacts: 7 [+] No. of charged-apolar contacts: 6 [+] No. of polar-polar contacts: 7 [+] No. of apolar-polar contacts: 15 [+] No. of apolar-apolar contacts: 12 [+] Percentage of apolar NIS residues: 29.48 [+] Percentage of charged NIS residues: 29.48 [++] Predicted binding affinity (kcal.mol-1): -9.4 [++] Predicted dissociation constant (M) at 25.0˚C: 1.3e-07 ``` Details of the binding affinity predictor implemented in PRODIGY can be found at [10.7554/elife.07454](https://doi.org/10.7554/elife.07454) ## Citing us If our tool is useful to you, please cite PRODIGY in your publications: - **Xue L, Rodrigues J, Kastritis P, Bonvin A.M.J.J, Vangone A.**: PRODIGY: a web server for predicting the binding affinity of protein-protein complexes. _Bioinformatics_ (2016) ([10.1093/bioinformatics/btw514](https://doi.org/10.1093/bioinformatics/btw514)) - **Anna Vangone and Alexandre M.J.J. Bonvin**: Contacts-based prediction of binding affinity in protein-protein complexes. _eLife_, e07454 (2015) ([10.7554/eLife.07454](https://doi.org/10.7554/elife.07454)) - **Panagiotis L. Kastritis , João P.G.L.M. Rodrigues, Gert E. Folkers, Rolf Boelens, Alexandre M.J.J. Bonvin**: Proteins Feel More Than They See: Fine-Tuning of Binding Affinity by Properties of the Non-Interacting Surface. _Journal of Molecular Biology_, 14, 2632–2652 (2014). ([10.1016/j.jmb.2014.04.017](https://doi.org/10.1016/j.jmb.2014.04.017)) ## Contact For questions about PRODIGY usage, please reach out the team at [ask.bioexcel.eu](https://ask.bioexcel.eu/) ## Information about dependencies The scripts rely on [Biopython](www.biopython.org) to validate the PDB structures and calculate interatomic distances. [freesasa](https://github.com/mittinatten/freesasa), with the parameter set used in NACCESS ([Chothia, 1976](http://www.ncbi.nlm.nih.gov/pubmed/994183)), is also required for calculating the buried surface area. **DISCLAIMER**: given the different software to calculate solvent accessiblity, predicted values might differ (very slightly) from those published in the reference implementations. The correlation of the actual atomic accessibilities is over 0.99, so we expect these differences to be very minor. --- prodigy-2.2.2/data/000077500000000000000000000000001461273102600141055ustar00rootroot00000000000000prodigy-2.2.2/data/dataset.json000066400000000000000000000640631461273102600164360ustar00rootroot00000000000000{ "1A2K": { "Interacting_chains": "C:AB", "Functional_class": "OG", "DG": -9.3, "ba_val": -9.0, "Experimental_method": "ITC", "iRMSD": 1.11, "BSA": 1603, "CC": 5, "CP": 4, "AC": 20, "PP": 2, "AP": 11, "AA": 25, "nis_p": 31.65, "nis_a": 41.77, "nis_c": 26.58 }, "1ACB": { "Interacting_chains": "E:I", "Functional_class": "EI", "DG": -13.1, "ba_val": -11.9, "Experimental_method": "spectroscopy", "iRMSD": 1.08, "BSA": 1544, "CC": 3, "CP": 2, "AC": 19, "PP": 4, "AP": 19, "AA": 25, "nis_p": 42.72, "nis_a": 38.5, "nis_c": 18.78 }, "1AK4": { "Interacting_chains": "A:D", "Functional_class": "OX", "DG": -6.4, "ba_val": -7.3, "Experimental_method": "ITC", "iRMSD": 1.33, "BSA": 1029, "CC": 0, "CP": 4, "AC": 14, "PP": 1, "AP": 10, "AA": 20, "nis_p": 27.95, "nis_a": 45.41, "nis_c": 26.64 }, "1AKJ": { "Interacting_chains": "AB:DE", "Functional_class": "OX", "DG": -5.3, "ba_val": -7.3, "Experimental_method": "SPR", "iRMSD": 1.14, "BSA": 1995, "CC": 8, "CP": 20, "AC": 7, "PP": 18, "AP": 18, "AA": 2, "nis_p": 35.18, "nis_a": 35.18, "nis_c": 29.64 }, "1ATN": { "Interacting_chains": "A:D", "Functional_class": "OX", "DG": -12.1, "ba_val": -10.9, "Experimental_method": "spectroscopy", "iRMSD": 3.28, "BSA": 1774, "CC": 9, "CP": 8, "AC": 20, "PP": 4, "AP": 15, "AA": 28, "nis_p": 36.32, "nis_a": 34.94, "nis_c": 28.74 }, "1AVZ": { "Interacting_chains": "B:C", "Functional_class": "NC", "DG": -6.5, "ba_val": -8.4, "Experimental_method": "ITC", "iRMSD": 0.73, "BSA": 1259, "CC": 5, "CP": 8, "AC": 9, "PP": 2, "AP": 14, "AA": 10, "nis_p": 30.6, "nis_a": 42.54, "nis_c": 26.87 }, "1B6C": { "Interacting_chains": "A:B", "Functional_class": "OX", "DG": -8.9, "ba_val": -9.4, "Experimental_method": "SPR", "iRMSD": 1.96, "BSA": 1752, "CC": 6, "CP": 11, "AC": 18, "PP": 1, "AP": 11, "AA": 21, "nis_p": 31.53, "nis_a": 35.35, "nis_c": 33.12 }, "1BJ1": { "Interacting_chains": "HL:VW", "Functional_class": "AB", "DG": -11.6, "ba_val": -12.2, "Experimental_method": "SPR", "iRMSD": 0.5, "BSA": 1731, "CC": 3, "CP": 8, "AC": 21, "PP": 7, "AP": 22, "AA": 19, "nis_p": 41.7, "nis_a": 35.68, "nis_c": 22.61 }, "1BUH": { "Interacting_chains": "A:B", "Functional_class": "EI", "DG": -9.7, "ba_val": -8.4, "Experimental_method": "SPR", "iRMSD": 0.75, "BSA": 1324, "CC": 12, "CP": 4, "AC": 20, "PP": 0, "AP": 5, "AA": 17, "nis_p": 28.83, "nis_a": 41.24, "nis_c": 29.93 }, "1BVK": { "Interacting_chains": "DE:F", "Functional_class": "A", "DG": -10.5, "ba_val": -11.3, "Experimental_method": "stopped-flow", "iRMSD": 1.24, "BSA": 1321, "CC": 2, "CP": 8, "AC": 18, "PP": 2, "AP": 14, "AA": 14, "nis_p": 43.75, "nis_a": 33.59, "nis_c": 22.66 }, "1BVN": { "Interacting_chains": "P:T", "Functional_class": "EI", "DG": -15.1, "ba_val": -13.3, "Experimental_method": "SPR", "iRMSD": 0.87, "BSA": 2222, "CC": 3, "CP": 12, "AC": 22, "PP": 0, "AP": 23, "AA": 33, "nis_p": 38.22, "nis_a": 36.78, "nis_c": 25 }, "1CBW": { "Interacting_chains": "ABC:D", "Functional_class": "NC", "DG": -10.7, "ba_val": -11.3, "Experimental_method": "spectroscopy", "iRMSD": 0.74, "BSA": 1457, "CC": 3, "CP": 10, "AC": 26, "PP": 1, "AP": 13, "AA": 28, "nis_p": 39.71, "nis_a": 39.71, "nis_c": 20.59 }, "1DE4": { "Interacting_chains": "AB:CF", "Functional_class": "OX", "DG": -9.8, "ba_val": -8.9, "Experimental_method": "SPR", "iRMSD": 2.59, "BSA": 2066, "CC": 5, "CP": 13, "AC": 17, "PP": 9, "AP": 14, "AA": 9, "nis_p": 35.21, "nis_a": 33.85, "nis_c": 30.94 }, "1DQJ": { "Interacting_chains": "AB:C", "Functional_class": "A", "DG": -11.7, "ba_val": -12.7, "Experimental_method": "SPR", "iRMSD": 0.75, "BSA": 1765, "CC": 2, "CP": 20, "AC": 18, "PP": 11, "AP": 25, "AA": 15, "nis_p": 47.79, "nis_a": 31.37, "nis_c": 20.83 }, "1E4K": { "Interacting_chains": "AB:C", "Functional_class": "OR", "DG": -7.9, "ba_val": -9.4, "Experimental_method": "SPR", "iRMSD": 2.59, "BSA": 1634, "CC": 3, "CP": 8, "AC": 26, "PP": 2, "AP": 5, "AA": 21, "nis_p": 38.88, "nis_a": 35.97, "nis_c": 25.16 }, "1E6E": { "Interacting_chains": "A:B", "Functional_class": "ES", "DG": -8.3, "ba_val": -8.6, "Experimental_method": "SPR", "iRMSD": 1.33, "BSA": 2315, "CC": 18, "CP": 15, "AC": 17, "PP": 5, "AP": 11, "AA": 11, "nis_p": 26.09, "nis_a": 42.75, "nis_c": 31.16 }, "1E6J": { "Interacting_chains": "HL:P", "Functional_class": "A", "DG": -10.3, "ba_val": -9.1, "Experimental_method": "SPR", "iRMSD": 1.05, "BSA": 1245, "CC": 0, "CP": 7, "AC": 8, "PP": 5, "AP": 15, "AA": 26, "nis_p": 40.76, "nis_a": 38.77, "nis_c": 20.48 }, "1E96": { "Interacting_chains": "A:B", "Functional_class": "OG", "DG": -7.4, "ba_val": -8.0, "Experimental_method": "ITC", "iRMSD": 0.71, "BSA": 1179, "CC": 4, "CP": 7, "AC": 16, "PP": 4, "AP": 11, "AA": 8, "nis_p": 28.74, "nis_a": 37.16, "nis_c": 34.1 }, "1EER": { "Interacting_chains": "A:BC", "Functional_class": "OR", "DG": -15.6, "ba_val": -13.6, "Experimental_method": "SPR", "iRMSD": 2.44, "BSA": 3347, "CC": 30, "CP": 19, "AC": 25, "PP": 12, "AP": 31, "AA": 19, "nis_p": 26.12, "nis_a": 43.75, "nis_c": 30.13 }, "1EFN": { "Interacting_chains": "B:A", "Functional_class": "OX", "DG": -10.1, "ba_val": -8.0, "Experimental_method": "SPR", "iRMSD": 0.9, "BSA": 1253, "CC": 5, "CP": 5, "AC": 12, "PP": 1, "AP": 12, "AA": 16, "nis_p": 27.48, "nis_a": 44.27, "nis_c": 28.24 }, "1EMV": { "Interacting_chains": "A:B", "Functional_class": "EI", "DG": -18.6, "ba_val": -11.0, "Experimental_method": "stopped-flow", "iRMSD": 1.28, "BSA": 1535, "CC": 4, "CP": 12, "AC": 11, "PP": 4, "AP": 24, "AA": 13, "nis_p": 29.7, "nis_a": 29.09, "nis_c": 41.21 }, "1EWY": { "Interacting_chains": "A:C", "Functional_class": "ES", "DG": -7.4, "ba_val": -8.3, "Experimental_method": "spectroscopy", "iRMSD": 0.8, "BSA": 1502, "CC": 9, "CP": 10, "AC": 15, "PP": 3, "AP": 9, "AA": 12, "nis_p": 29.83, "nis_a": 36.95, "nis_c": 33.22 }, "1EZU": { "Interacting_chains": "C:AB", "Functional_class": "EI", "DG": -13.8, "ba_val": -13.1, "Experimental_method": "spectroscopy", "iRMSD": 1.21, "BSA": 2751, "CC": 7, "CP": 9, "AC": 33, "PP": 8, "AP": 28, "AA": 42, "nis_p": 30.59, "nis_a": 40.43, "nis_c": 28.99 }, "1FC2": { "Interacting_chains": "C:D", "Functional_class": "OX", "DG": -10.4, "ba_val": -8.5, "Experimental_method": "stopped-flow", "iRMSD": 1.69, "BSA": 1307, "CC": 4, "CP": 4, "AC": 9, "PP": 8, "AP": 14, "AA": 11, "nis_p": 37.56, "nis_a": 35.61, "nis_c": 26.83 }, "1FFW": { "Interacting_chains": "A:B", "Functional_class": "OX", "DG": -8.1, "ba_val": -5.7, "Experimental_method": "ITC", "iRMSD": 1.43, "BSA": 1170, "CC": 7, "CP": 2, "AC": 16, "PP": 0, "AP": 2, "AA": 15, "nis_p": 21.85, "nis_a": 44.37, "nis_c": 33.77 }, "1FSK": { "Interacting_chains": "BC:A", "Functional_class": "AB", "DG": -13.1, "ba_val": -11.7, "Experimental_method": "SPR", "iRMSD": 0.45, "BSA": 1623, "CC": 7, "CP": 10, "AC": 22, "PP": 3, "AP": 15, "AA": 25, "nis_p": 40.61, "nis_a": 35.81, "nis_c": 23.58 }, "1GCQ": { "Interacting_chains": "B:C", "Functional_class": "OX", "DG": -6.5, "ba_val": -9.0, "Experimental_method": "SPR", "iRMSD": 0.92, "BSA": 1208, "CC": 5, "CP": 7, "AC": 11, "PP": 0, "AP": 12, "AA": 21, "nis_p": 33.33, "nis_a": 41.18, "nis_c": 25.49 }, "1GLA": { "Interacting_chains": "G:F", "Functional_class": "ER", "DG": -6.8, "ba_val": -8.1, "Experimental_method": "spectroscopy", "iRMSD": 0.98, "BSA": 1304, "CC": 5, "CP": 8, "AC": 13, "PP": 0, "AP": 11, "AA": 9, "nis_p": 26.35, "nis_a": 38.82, "nis_c": 34.82 }, "1GXD": { "Interacting_chains": "A:C", "Functional_class": "EI", "DG": -11.7, "ba_val": -12.6, "Experimental_method": "SPR", "iRMSD": 1.39, "BSA": 2445, "CC": 16, "CP": 6, "AC": 33, "PP": 0, "AP": 15, "AA": 35, "nis_p": 30.31, "nis_a": 40, "nis_c": 29.69 }, "1HE8": { "Interacting_chains": "B:A", "Functional_class": "OG", "DG": -7.4, "ba_val": -7.3, "Experimental_method": "stopped-flow", "iRMSD": 0.92, "BSA": 1305, "CC": 8, "CP": 15, "AC": 6, "PP": 5, "AP": 8, "AA": 6, "nis_p": 33.18, "nis_a": 33.33, "nis_c": 33.48 }, "1I2M": { "Interacting_chains": "A:B", "Functional_class": "OG", "DG": -15.8, "ba_val": -14.6, "Experimental_method": "stopped-flow", "iRMSD": 2.12, "BSA": 2779, "CC": 20, "CP": 17, "AC": 37, "PP": 7, "AP": 26, "AA": 12, "nis_p": 30.41, "nis_a": 38.63, "nis_c": 30.96 }, "1I4D": { "Interacting_chains": "D:AB", "Functional_class": "OG", "DG": -7.5, "ba_val": -9.3, "Experimental_method": "ITC", "iRMSD": 1.41, "BSA": 1657, "CC": 3, "CP": 9, "AC": 9, "PP": 7, "AP": 21, "AA": 18, "nis_p": 31.25, "nis_a": 35.1, "nis_c": 33.65 }, "1J2J": { "Interacting_chains": "A:B", "Functional_class": "OG", "DG": -8.1, "ba_val": -7.0, "Experimental_method": "SPR", "iRMSD": 0.63, "BSA": 1209, "CC": 3, "CP": 4, "AC": 12, "PP": 1, "AP": 3, "AA": 20, "nis_p": 31.79, "nis_a": 30.46, "nis_c": 37.75 }, "1JPS": { "Interacting_chains": "HL:T", "Functional_class": "A", "DG": -13.6, "ba_val": -12.9, "Experimental_method": "SPR", "iRMSD": 0.51, "BSA": 1852, "CC": 13, "CP": 16, "AC": 18, "PP": 4, "AP": 20, "AA": 12, "nis_p": 40.81, "nis_a": 34.83, "nis_c": 24.36 }, "1JTG": { "Interacting_chains": "B:A", "Functional_class": "EI", "DG": -12.8, "ba_val": -11.6, "Experimental_method": "SPR", "iRMSD": 0.49, "BSA": 2600, "CC": 11, "CP": 19, "AC": 34, "PP": 4, "AP": 15, "AA": 25, "nis_p": 32.18, "nis_a": 40.83, "nis_c": 26.99 }, "1JWH": { "Interacting_chains": "CD:A", "Functional_class": "ER", "DG": -11.1, "ba_val": -9.5, "Experimental_method": "ITC", "iRMSD": 1.27, "BSA": 1451, "CC": 2, "CP": 5, "AC": 20, "PP": 0, "AP": 10, "AA": 20, "nis_p": 33.27, "nis_a": 34.18, "nis_c": 32.55 }, "1K5D": { "Interacting_chains": "AB:C", "Functional_class": "OG", "DG": -12.8, "ba_val": -11.6, "Experimental_method": "stopped-flow", "iRMSD": 1.19, "BSA": 2527, "CC": 16, "CP": 15, "AC": 24, "PP": 6, "AP": 21, "AA": 27, "nis_p": 25.89, "nis_a": 33.61, "nis_c": 40.5 }, "1KAC": { "Interacting_chains": "A:B", "Functional_class": "OR", "DG": -10.7, "ba_val": -11.9, "Experimental_method": "SPR", "iRMSD": 0.95, "BSA": 1456, "CC": 7, "CP": 5, "AC": 13, "PP": 2, "AP": 18, "AA": 12, "nis_p": 42.86, "nis_a": 37.66, "nis_c": 19.48 }, "1KKL": { "Interacting_chains": "ABC:H", "Functional_class": "ES", "DG": -10, "ba_val": -9.1, "Experimental_method": "SPR", "iRMSD": 2.2, "BSA": 1641, "CC": 6, "CP": 9, "AC": 16, "PP": 4, "AP": 14, "AA": 22, "nis_p": 31.19, "nis_a": 38.1, "nis_c": 30.71 }, "1KTZ": { "Interacting_chains": "A:B", "Functional_class": "OR", "DG": -8.9, "ba_val": -8.1, "Experimental_method": "SPR", "iRMSD": 0.39, "BSA": 989, "CC": 5, "CP": 6, "AC": 7, "PP": 0, "AP": 5, "AA": 12, "nis_p": 38.18, "nis_a": 33.94, "nis_c": 27.88 }, "1KXQ": { "Interacting_chains": "H:A", "Functional_class": "AB", "DG": -11.5, "ba_val": -11.8, "Experimental_method": "SPR", "iRMSD": 0.72, "BSA": 2172, "CC": 7, "CP": 9, "AC": 18, "PP": 12, "AP": 25, "AA": 23, "nis_p": 40.46, "nis_a": 34.54, "nis_c": 25 }, "1LFD": { "Interacting_chains": "B:A", "Functional_class": "OG", "DG": -7.8, "ba_val": -8.4, "Experimental_method": "stopped-flow", "iRMSD": 1.79, "BSA": 1167, "CC": 9, "CP": 8, "AC": 9, "PP": 3, "AP": 9, "AA": 11, "nis_p": 32.46, "nis_a": 29.32, "nis_c": 38.22 }, "1M10": { "Interacting_chains": "A:B", "Functional_class": "ER", "DG": -11.2, "ba_val": -10.5, "Experimental_method": "SPR", "iRMSD": 2.1, "BSA": 2097, "CC": 16, "CP": 24, "AC": 24, "PP": 2, "AP": 8, "AA": 12, "nis_p": 35.08, "nis_a": 36.31, "nis_c": 28.62 }, "1MLC": { "Interacting_chains": "AB:E", "Functional_class": "NC", "DG": -9.6, "ba_val": -10.3, "Experimental_method": "SPR", "iRMSD": 0.6, "BSA": 1392, "CC": 5, "CP": 8, "AC": 15, "PP": 13, "AP": 18, "AA": 8, "nis_p": 45.63, "nis_a": 33.01, "nis_c": 21.36 }, "1MQ8": { "Interacting_chains": "A:B", "Functional_class": "OX", "DG": -7.5, "ba_val": -8.2, "Experimental_method": "SPR", "iRMSD": 1.76, "BSA": 1241, "CC": 3, "CP": 11, "AC": 10, "PP": 6, "AP": 15, "AA": 11, "nis_p": 31.79, "nis_a": 37.14, "nis_c": 31.07 }, "1P2C": { "Interacting_chains": "AB:C", "Functional_class": "A", "DG": -13.6, "ba_val": -11.4, "Experimental_method": "SPR", "iRMSD": 0.46, "BSA": 1456, "CC": 5, "CP": 8, "AC": 17, "PP": 13, "AP": 22, "AA": 10, "nis_p": 45.06, "nis_a": 32.66, "nis_c": 22.28 }, "1PPE": { "Interacting_chains": "E:I", "Functional_class": "EI", "DG": -15.6, "ba_val": -14.7, "Experimental_method": "spectroscopy", "iRMSD": 0.34, "BSA": 1688, "CC": 5, "CP": 10, "AC": 28, "PP": 0, "AP": 20, "AA": 24, "nis_p": 47.09, "nis_a": 34.88, "nis_c": 18.02 }, "1PVH": { "Interacting_chains": "A:B", "Functional_class": "OR", "DG": -9.5, "ba_val": -10.9, "Experimental_method": "ITC", "iRMSD": 0.34, "BSA": 1403, "CC": 5, "CP": 8, "AC": 8, "PP": 4, "AP": 21, "AA": 11, "nis_p": 38.13, "nis_a": 35.12, "nis_c": 26.76 }, "1QA9": { "Interacting_chains": "A:B", "Functional_class": "OX", "DG": -7.2, "ba_val": -9.6, "Experimental_method": "SPR", "iRMSD": 0.73, "BSA": 1353, "CC": 21, "CP": 10, "AC": 14, "PP": 0, "AP": 2, "AA": 3, "nis_p": 35.22, "nis_a": 25.79, "nis_c": 38.99 }, "1R0R": { "Interacting_chains": "E:I", "Functional_class": "EI", "DG": -14.2, "ba_val": -11.3, "Experimental_method": "spectroscopy", "iRMSD": 0.45, "BSA": 1409, "CC": 1, "CP": 13, "AC": 8, "PP": 6, "AP": 21, "AA": 31, "nis_p": 46.67, "nis_a": 37.14, "nis_c": 16.19 }, "1S1Q": { "Interacting_chains": "A:B", "Functional_class": "OX", "DG": -4.3, "ba_val": -9.0, "Experimental_method": "SPR", "iRMSD": 0.98, "BSA": 1288, "CC": 1, "CP": 4, "AC": 11, "PP": 6, "AP": 16, "AA": 16, "nis_p": 35.67, "nis_a": 35.67, "nis_c": 28.65 }, "1US7": { "Interacting_chains": "A:B", "Functional_class": "ER", "DG": -8.1, "ba_val": -6.8, "Experimental_method": "ITC", "iRMSD": 1.06, "BSA": 1106, "CC": 6, "CP": 6, "AC": 10, "PP": 1, "AP": 5, "AA": 14, "nis_p": 27.6, "nis_a": 33.77, "nis_c": 38.64 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ǕׂA&<[ h\5n6@} hus㥚RA,TѶhע\NF6ow[or|sf~ΨLK[!̆,URN!1#>ؔY@]Ez&$=D=V] Q ^ .zq| Df:d@U葜CM mF2˕Q3Dt]Br9MF"+OKmy CP3SKV6GѠ َb7!9O T:SBr|ގ5iD(cYHdQc۵;tPeWnF1̍4rUÍA]!IZyAºYsQ&>3G=C2{x G_{#~.$ H}0/%Yw N/(TȺo=+~x#qK1S,iQjT"c yK/^*ז% 7b,+ N~(& X] Ҏ|_?UKn"1tܺ3WL CeTU/RFF;Z[zIbFU4/C}c Qx4a)1D; P[x,dNcY8NgQiA*rg;? tqRzr|zKWaR@n8"덠^J)'1w+>ݴBΏ]D22 _7ȚqMs ߷5SI3MHurX%:k oF Q@lnZ"FmNL7-!/U5K5փDCuihvFtե M4LIJb3XSJ* WW!4pAt[ .A~k\GŒ{,$z`>8Hz߷"VATG\ķ ,wX" .cszo 9MXBqO'^e&kZL-*س5<>ܺd'dD>7R?DUJKtCD7 Dӆ(Ua˗Jџ $8 R4t/О9Pni `ЭXp"&5bȤƴJ~ߣ܍J(r@L!wpz(N }o$VR{Xq\'ktJxsx)EU.>m|ڿי_2;@DfmxNA$|>MSb:Wv-Q D^ Z {] Nȳ0p?vU!"v)l|IigwUC5_{jEt]==HL8k7"ļ_0ͪNaJnf3?U]?`b ߈Dt]ᖽg'\2-AR Dn2;7,JW4eWg7҃n|e-::K7Is|$C_ Al֌.]:7~]Gѭ#bLXu1PՍ[%](Ɵ phJ'N3gZųK:UQUdflA^i3N qխZ:Bfn?SZ5dF^0ÏLw|}WEƏ( H AX4$@zTB7(#q*7>0Dp7!Q mu6 y:arey.u:\!m9! 5t/ [jEp0it R$7#]?w<7 <, 㷅Iq" Qgaϗ;(jFV!~/MBAEVy@hY/'6b֊bh+FcXD $h CҾj*e{7U. 9"@a e$H[XC01aECd<*9^J,05s na !a&AW5<Eaf6cke"S+ho! }ƒ \@]KE:3PspJ\Xv"Z;g.'h)h,Y j:!WσФDdco s.Y-[UəF]ZDvWtZwNy,-/:/V;[/=#X rk=EU_]J:6Tj̜iՄTeஞI (7$d)u{Q_(յcC՘mn|Zf [e+u0-b04ط=p"jE?:}o#0A(,b!Ч6;ͦ_t/V{:>[8EP}pFo |B'T7A "rfFm:N=#e$9sT FHJN3DVbN+OjDQgcqKSSjs|]!%/aSӡ*_)AM!LÝ7RcV7u yiVDJz#7?{'u뭢h3+ieވkξ"KܦcM'YTI37+:CT]dr+BiVypz|25($Wt UZ+D2aYMP'VdR"#IDȬ]! 5,`5D:ffv,U %Q44.bJ61]H !(Ʒ\k&!?ݢb{[nQBGjʁR(/s:ڭb(¾o!ԕZn/ּB 1|"v(TF9;饶1|*.&)m5"`+ 1{"o$ꕆxβVL2A>HZo*.8@(lkcى8CvzBu} <5ŸAlb0? 9`D"#[ɠ# E9raZ杖g5Ov޵f aңVdw &2:>kE7uka7\G[E[O}?Hs7DԊ6mA$ݹ fq3NMG%b&m9NG3ġ:o)Z=uj.N(ivVz %t.93;# DU4<֮%M˦3% ~9RZ<6NSUwR]y ! EebW^UߖD!=+O/J}K|*_Oԓ45*_gl=VzИ_@GM}t(O~>D7%DɺnfkS 4 zh~N3Dzq=v#v 8Α]7΃2MS F]=ŝgcxEauLH#'{ 8l#Q@tpI҄i?ȓ#s>UNA"\}#gV;s1"X.:ᰏNT@{vZ/rXz\J5i[D\Px.kQ@|SfF}mxnV$V׃F#C)QD6kEg;vor_;"1,T{ڬ]!BUaaM]BMO'DvZQ@dsђCtaAȴBj ģH|eCoFpҠX.prodigy-2.2.2/examples/000077500000000000000000000000001461273102600150125ustar00rootroot00000000000000prodigy-2.2.2/examples/3BZD.ic_model000066400000000000000000000011311461273102600172050ustar00rootroot00000000000000[+] Reading structure file: /Users/joao/software/binding_affinity/examples/3BZD.pdb [+] Parsed structure file 3BZD (2 chains, 343 residues) [+] No. of intermolecular contacts: 51 [+] No. of charged-charged contacts: 4 [+] No. of charged-polar contacts: 7 [+] No. of charged-apolar contacts: 6 [+] No. of polar-polar contacts: 7 [+] No. of apolar-polar contacts: 15 [+] No. of apolar-apolar contacts: 12 [+] Percentage of apolar NIS residues: 29.48 [+] Percentage of charged NIS residues: 29.48 [++] Predicted binding affinity (kcal.mol-1): -9.373 [++] Predicted dissociation constant (M): 1.333e-07 prodigy-2.2.2/examples/3BZD.pdb000066400000000000000000005503061461273102600162140ustar00rootroot00000000000000ATOM 1 N ALA A 2 33.763 52.112 -44.090 1.00 25.34 ATOM 2 CA ALA A 2 33.403 52.722 -42.739 1.00 25.11 ATOM 3 C ALA A 2 31.960 53.249 -42.614 1.00 24.76 ATOM 4 O ALA A 2 31.694 54.512 -42.582 1.00 23.96 ATOM 5 CB ALA A 2 34.416 53.856 -42.420 1.00 25.90 ATOM 6 N ALA A 3 31.006 52.310 -42.598 1.00 22.94 ATOM 7 CA ALA A 3 29.599 52.628 -42.417 1.00 20.08 ATOM 8 C ALA A 3 29.149 54.015 -41.825 1.00 19.99 ATOM 9 O ALA A 3 28.776 54.906 -42.573 1.00 20.00 ATOM 10 CB ALA A 3 28.955 51.482 -41.644 1.00 23.26 ATOM 11 N VAL A 4 29.035 54.170 -40.506 1.00 18.40 ATOM 12 CA VAL A 4 28.549 55.423 -39.964 1.00 18.10 ATOM 13 C VAL A 4 29.576 56.081 -38.981 1.00 20.17 ATOM 14 O VAL A 4 30.137 55.401 -38.110 1.00 23.21 ATOM 15 CB VAL A 4 27.169 55.298 -39.311 1.00 17.65 ATOM 16 CG1 VAL A 4 26.698 56.664 -38.801 1.00 15.66 ATOM 17 CG2 VAL A 4 26.087 54.720 -40.311 1.00 13.28 ATOM 18 N THR A 5 29.873 57.358 -39.124 1.00 20.40 ATOM 19 CA THR A 5 30.874 57.978 -38.197 1.00 20.85 ATOM 20 C THR A 5 30.306 59.193 -37.579 1.00 20.88 ATOM 21 O THR A 5 29.679 59.984 -38.291 1.00 23.01 ATOM 22 CB THR A 5 32.105 58.415 -38.935 1.00 19.13 ATOM 23 OG1 THR A 5 31.701 59.319 -39.976 1.00 20.17 ATOM 24 CG2 THR A 5 32.793 57.235 -39.515 1.00 19.09 ATOM 25 N GLN A 6 30.516 59.359 -36.266 1.00 22.20 ATOM 26 CA GLN A 6 30.067 60.585 -35.579 1.00 23.92 ATOM 27 C GLN A 6 31.183 61.576 -35.350 1.00 24.16 ATOM 28 O GLN A 6 32.319 61.255 -35.567 1.00 24.44 ATOM 29 CB GLN A 6 29.374 60.216 -34.293 1.00 24.31 ATOM 30 CG GLN A 6 28.414 59.048 -34.567 1.00 26.83 ATOM 31 CD GLN A 6 27.650 58.653 -33.341 1.00 33.51 ATOM 32 OE1 GLN A 6 27.159 57.489 -33.222 1.00 29.01 ATOM 33 NE2 GLN A 6 27.551 59.606 -32.387 1.00 30.50 ATOM 34 N SER A 7 30.858 62.793 -34.915 1.00 24.73 ATOM 35 CA SER A 7 31.873 63.763 -34.592 1.00 24.61 ATOM 36 C SER A 7 31.252 64.844 -33.743 1.00 22.89 ATOM 37 O SER A 7 30.226 65.374 -34.175 1.00 23.88 ATOM 38 CB SER A 7 32.492 64.358 -35.868 1.00 24.52 ATOM 39 OG SER A 7 32.873 65.718 -35.598 1.00 29.35 ATOM 40 N PRO A 8 31.876 65.196 -32.575 1.00 21.61 ATOM 41 CA PRO A 8 33.116 64.595 -32.127 1.00 23.90 ATOM 42 C PRO A 8 32.855 63.370 -31.324 1.00 25.23 ATOM 43 O PRO A 8 31.723 63.054 -31.034 1.00 26.87 ATOM 44 CB PRO A 8 33.746 65.663 -31.273 1.00 21.34 ATOM 45 CG PRO A 8 32.608 66.338 -30.689 1.00 20.62 ATOM 46 CD PRO A 8 31.440 66.196 -31.594 1.00 21.05 ATOM 47 N ARG A 9 33.912 62.635 -31.030 1.00 30.32 ATOM 48 CA ARG A 9 33.769 61.344 -30.318 1.00 32.66 ATOM 49 C ARG A 9 33.547 61.556 -28.814 1.00 34.51 ATOM 50 O ARG A 9 32.676 60.886 -28.211 1.00 34.65 ATOM 51 CB ARG A 9 34.960 60.411 -30.594 1.00 33.97 ATOM 52 CG ARG A 9 34.579 58.965 -31.203 1.00 37.59 ATOM 53 CD ARG A 9 34.574 57.847 -30.146 1.00 41.10 ATOM 54 NE ARG A 9 33.525 57.998 -29.122 1.00 41.96 ATOM 55 CZ ARG A 9 33.148 57.018 -28.288 1.00 46.33 ATOM 56 NH1 ARG A 9 33.734 55.823 -28.351 1.00 46.04 ATOM 57 NH2 ARG A 9 32.191 57.226 -27.381 1.00 45.03 ATOM 58 N ASN A 10 34.255 62.538 -28.252 1.00 34.63 ATOM 59 CA ASN A 10 34.322 62.770 -26.841 1.00 36.87 ATOM 60 C ASN A 10 34.176 64.301 -26.619 1.00 37.49 ATOM 61 O ASN A 10 34.952 65.100 -27.222 1.00 37.87 ATOM 62 CB ASN A 10 35.728 62.350 -26.344 1.00 38.51 ATOM 63 CG ASN A 10 35.808 60.909 -25.778 1.00 40.50 ATOM 64 OD1 ASN A 10 35.289 60.621 -24.690 1.00 42.89 ATOM 65 ND2 ASN A 10 36.562 60.024 -26.478 1.00 45.07 ATOM 66 N LYS A 11 33.234 64.711 -25.756 1.00 37.13 ATOM 67 CA LYS A 11 32.988 66.146 -25.513 1.00 37.05 ATOM 68 C LYS A 11 32.611 66.551 -24.094 1.00 37.79 ATOM 69 O LYS A 11 31.611 66.081 -23.547 1.00 38.26 ATOM 70 CB LYS A 11 31.917 66.640 -26.461 1.00 36.57 ATOM 71 CG LYS A 11 31.671 68.085 -26.434 1.00 34.46 ATOM 72 CD LYS A 11 32.930 68.874 -26.804 1.00 34.83 ATOM 73 CE LYS A 11 32.640 70.397 -26.761 1.00 30.64 ATOM 74 NZ LYS A 11 31.514 70.805 -27.599 1.00 22.67 ATOM 75 N VAL A 12 33.386 67.505 -23.554 1.00 38.60 ATOM 76 CA VAL A 12 33.166 68.115 -22.222 1.00 38.63 ATOM 77 C VAL A 12 32.833 69.600 -22.304 1.00 37.84 ATOM 78 O VAL A 12 33.705 70.410 -22.575 1.00 37.68 ATOM 79 CB VAL A 12 34.436 68.044 -21.367 1.00 38.68 ATOM 80 CG1 VAL A 12 34.455 66.783 -20.594 1.00 36.81 ATOM 81 CG2 VAL A 12 35.698 68.267 -22.244 1.00 39.25 ATOM 82 N ALA A 13 31.582 69.958 -22.048 1.00 38.24 ATOM 83 CA ALA A 13 31.154 71.334 -22.244 1.00 37.91 ATOM 84 C ALA A 13 30.518 71.865 -20.969 1.00 38.80 ATOM 85 O ALA A 13 29.977 71.078 -20.172 1.00 40.28 ATOM 86 CB ALA A 13 30.206 71.429 -23.445 1.00 36.72 ATOM 87 N VAL A 14 30.572 73.184 -20.774 1.00 38.57 ATOM 88 CA VAL A 14 30.029 73.826 -19.562 1.00 37.61 ATOM 89 C VAL A 14 28.509 74.033 -19.608 1.00 37.37 ATOM 90 O VAL A 14 27.928 74.222 -20.657 1.00 37.41 ATOM 91 CB VAL A 14 30.786 75.122 -19.224 1.00 37.15 ATOM 92 CG1 VAL A 14 32.258 74.813 -18.990 1.00 39.31 ATOM 93 CG2 VAL A 14 30.659 76.145 -20.333 1.00 36.96 ATOM 94 N THR A 15 27.833 73.972 -18.484 1.00 37.50 ATOM 95 CA THR A 15 26.374 74.084 -18.570 1.00 38.08 ATOM 96 C THR A 15 26.081 75.446 -19.119 1.00 38.88 ATOM 97 O THR A 15 26.546 76.448 -18.589 1.00 38.13 ATOM 98 CB THR A 15 25.740 73.917 -17.219 1.00 38.28 ATOM 99 OG1 THR A 15 26.179 72.659 -16.708 1.00 37.16 ATOM 100 CG2 THR A 15 24.211 73.945 -17.270 1.00 33.98 ATOM 101 N GLY A 16 25.378 75.454 -20.243 1.00 40.38 ATOM 102 CA GLY A 16 25.006 76.708 -20.944 1.00 40.95 ATOM 103 C GLY A 16 25.235 76.682 -22.453 1.00 41.28 ATOM 104 O GLY A 16 24.284 76.759 -23.237 1.00 41.72 ATOM 105 N GLU A 17 26.507 76.545 -22.845 1.00 40.82 ATOM 106 CA GLU A 17 26.917 76.561 -24.222 1.00 39.97 ATOM 107 C GLU A 17 26.090 75.713 -25.162 1.00 39.45 ATOM 108 O GLU A 17 25.424 74.709 -24.773 1.00 41.25 ATOM 109 CB GLU A 17 28.383 76.194 -24.313 1.00 39.94 ATOM 110 CG GLU A 17 28.705 74.768 -24.699 1.00 42.31 ATOM 111 CD GLU A 17 30.173 74.663 -25.044 1.00 46.41 ATOM 112 OE1 GLU A 17 30.997 74.973 -24.160 1.00 50.97 ATOM 113 OE2 GLU A 17 30.528 74.333 -26.192 1.00 47.31 ATOM 114 N LYS A 18 26.162 76.106 -26.423 1.00 38.14 ATOM 115 CA LYS A 18 25.390 75.490 -27.489 1.00 36.59 ATOM 116 C LYS A 18 26.189 74.336 -28.077 1.00 35.70 ATOM 117 O LYS A 18 27.186 74.553 -28.726 1.00 35.80 ATOM 118 CB LYS A 18 25.078 76.547 -28.555 1.00 35.73 ATOM 119 CG LYS A 18 24.642 75.967 -29.873 1.00 35.86 ATOM 120 CD LYS A 18 24.304 77.030 -30.889 1.00 32.18 ATOM 121 CE LYS A 18 23.847 76.454 -32.203 1.00 30.56 ATOM 122 NZ LYS A 18 23.525 77.616 -33.110 1.00 28.09 ATOM 123 N VAL A 19 25.740 73.104 -27.883 1.00 34.54 ATOM 124 CA VAL A 19 26.489 72.024 -28.480 1.00 33.14 ATOM 125 C VAL A 19 25.814 71.336 -29.702 1.00 31.93 ATOM 126 O VAL A 19 24.659 70.939 -29.621 1.00 30.42 ATOM 127 CB VAL A 19 26.948 71.030 -27.399 1.00 32.22 ATOM 128 CG1 VAL A 19 27.930 70.120 -27.985 1.00 33.61 ATOM 129 CG2 VAL A 19 27.634 71.795 -26.270 1.00 32.41 ATOM 130 N THR A 20 26.586 71.154 -30.793 1.00 30.75 ATOM 131 CA THR A 20 26.129 70.433 -32.017 1.00 30.63 ATOM 132 C THR A 20 26.803 69.064 -32.325 1.00 29.61 ATOM 133 O THR A 20 28.002 68.986 -32.412 1.00 28.29 ATOM 134 CB THR A 20 26.358 71.321 -33.227 1.00 30.22 ATOM 135 OG1 THR A 20 26.098 72.665 -32.851 1.00 33.58 ATOM 136 CG2 THR A 20 25.454 70.942 -34.404 1.00 33.21 ATOM 137 N LEU A 21 26.040 67.994 -32.533 1.00 29.29 ATOM 138 CA LEU A 21 26.700 66.703 -32.864 1.00 27.84 ATOM 139 C LEU A 21 26.557 66.244 -34.315 1.00 27.04 ATOM 140 O LEU A 21 25.477 65.992 -34.733 1.00 27.86 ATOM 141 CB LEU A 21 26.195 65.601 -31.949 1.00 27.07 ATOM 142 CG LEU A 21 26.733 65.616 -30.538 1.00 26.22 ATOM 143 CD1 LEU A 21 26.467 64.263 -30.005 1.00 22.98 ATOM 144 CD2 LEU A 21 28.210 65.836 -30.545 1.00 24.93 ATOM 145 N SER A 22 27.666 66.097 -35.041 1.00 26.93 ATOM 146 CA SER A 22 27.686 65.831 -36.452 1.00 25.10 ATOM 147 C SER A 22 27.878 64.323 -36.752 1.00 25.45 ATOM 148 O SER A 22 28.824 63.705 -36.279 1.00 25.57 ATOM 149 CB SER A 22 28.845 66.590 -37.029 1.00 25.68 ATOM 150 OG SER A 22 30.064 66.188 -36.403 1.00 23.64 ATOM 151 N CYS A 23 26.991 63.763 -37.572 1.00 24.02 ATOM 152 CA CYS A 23 27.004 62.372 -37.923 1.00 22.83 ATOM 153 C CYS A 23 26.979 62.271 -39.446 1.00 23.31 ATOM 154 O CYS A 23 26.279 63.033 -40.098 1.00 23.51 ATOM 155 CB CYS A 23 25.766 61.690 -37.327 1.00 21.98 ATOM 156 SG CYS A 23 25.500 60.064 -38.017 1.00 27.28 ATOM 157 N GLN A 24 27.724 61.334 -40.069 1.00 24.11 ATOM 158 CA GLN A 24 27.667 61.306 -41.533 1.00 22.59 ATOM 159 C GLN A 24 27.779 59.925 -42.002 1.00 21.63 ATOM 160 O GLN A 24 28.489 59.172 -41.354 1.00 24.40 ATOM 161 CB GLN A 24 28.770 62.176 -42.143 1.00 21.88 ATOM 162 CG GLN A 24 30.159 61.762 -41.757 1.00 21.77 ATOM 163 CD GLN A 24 31.178 62.618 -42.429 1.00 26.24 ATOM 164 OE1 GLN A 24 31.091 63.863 -42.343 1.00 29.92 ATOM 165 NE2 GLN A 24 32.140 61.991 -43.145 1.00 24.42 ATOM 166 N GLN A 25 27.160 59.595 -43.134 1.00 20.02 ATOM 167 CA GLN A 25 27.124 58.224 -43.673 1.00 21.13 ATOM 168 C GLN A 25 27.819 58.088 -45.004 1.00 20.72 ATOM 169 O GLN A 25 28.362 59.074 -45.564 1.00 22.35 ATOM 170 CB GLN A 25 25.756 57.546 -43.767 1.00 19.39 ATOM 171 CG GLN A 25 24.519 58.524 -43.955 1.00 20.36 ATOM 172 CD GLN A 25 23.359 57.917 -44.753 1.00 23.09 ATOM 173 OE1 GLN A 25 22.679 56.907 -44.328 1.00 19.57 ATOM 174 NE2 GLN A 25 23.099 58.545 -45.937 1.00 16.66 ATOM 175 N THR A 26 27.877 56.829 -45.457 1.00 18.37 ATOM 176 CA THR A 26 28.528 56.500 -46.708 1.00 16.35 ATOM 177 C THR A 26 27.721 55.440 -47.431 1.00 17.39 ATOM 178 O THR A 26 27.938 55.242 -48.615 1.00 17.50 ATOM 179 CB THR A 26 29.959 56.011 -46.482 1.00 16.16 ATOM 180 OG1 THR A 26 29.910 54.845 -45.647 1.00 11.99 ATOM 181 CG2 THR A 26 30.757 57.080 -45.751 1.00 13.64 ATOM 182 N ASN A 27 26.734 54.815 -46.773 1.00 17.97 ATOM 183 CA ASN A 27 25.938 53.826 -47.485 1.00 18.36 ATOM 184 C ASN A 27 24.715 54.509 -47.983 1.00 18.04 ATOM 185 O ASN A 27 23.783 53.876 -48.453 1.00 18.57 ATOM 186 CB ASN A 27 25.558 52.683 -46.505 1.00 20.73 ATOM 187 CG ASN A 27 25.725 51.289 -47.098 1.00 24.04 ATOM 188 OD1 ASN A 27 26.831 50.715 -47.091 1.00 29.48 ATOM 189 ND2 ASN A 27 24.608 50.706 -47.571 1.00 30.58 ATOM 190 N ASN A 28 24.671 55.826 -47.792 1.00 20.40 ATOM 191 CA ASN A 28 23.537 56.642 -48.189 1.00 19.02 ATOM 192 C ASN A 28 22.188 55.904 -47.921 1.00 19.71 ATOM 193 O ASN A 28 21.534 55.410 -48.886 1.00 19.66 ATOM 194 CB ASN A 28 23.680 56.862 -49.657 1.00 20.31 ATOM 195 CG ASN A 28 24.155 58.217 -50.032 1.00 20.99 ATOM 196 OD1 ASN A 28 23.445 59.211 -49.917 1.00 27.80 ATOM 197 ND2 ASN A 28 25.368 58.270 -50.570 1.00 24.27 ATOM 198 N HIS A 29 21.795 55.744 -46.648 1.00 18.69 ATOM 199 CA HIS A 29 20.457 55.153 -46.346 1.00 18.06 ATOM 200 C HIS A 29 19.444 56.308 -46.121 1.00 16.73 ATOM 201 O HIS A 29 19.811 57.331 -45.565 1.00 20.04 ATOM 202 CB HIS A 29 20.507 54.337 -45.095 1.00 17.41 ATOM 203 CG HIS A 29 21.021 52.959 -45.269 1.00 19.31 ATOM 204 ND1 HIS A 29 20.203 51.888 -45.553 1.00 16.65 ATOM 205 CD2 HIS A 29 22.258 52.452 -45.058 1.00 21.43 ATOM 206 CE1 HIS A 29 20.941 50.796 -45.604 1.00 25.33 ATOM 207 NE2 HIS A 29 22.191 51.109 -45.304 1.00 22.12 ATOM 208 N ASN A 30 18.211 56.170 -46.565 1.00 16.43 ATOM 209 CA ASN A 30 17.159 57.197 -46.310 1.00 17.97 ATOM 210 C ASN A 30 17.031 57.559 -44.839 1.00 16.70 ATOM 211 O ASN A 30 17.239 58.757 -44.450 1.00 17.12 ATOM 212 CB ASN A 30 15.761 56.739 -46.736 1.00 17.02 ATOM 213 CG ASN A 30 15.515 56.891 -48.242 1.00 22.50 ATOM 214 OD1 ASN A 30 15.136 57.977 -48.709 1.00 18.29 ATOM 215 ND2 ASN A 30 15.689 55.759 -49.011 1.00 22.63 ATOM 216 N ASN A 31 16.761 56.515 -44.054 1.00 11.02 ATOM 217 CA ASN A 31 16.530 56.652 -42.671 1.00 9.90 ATOM 218 C ASN A 31 17.818 56.798 -41.902 1.00 6.58 ATOM 219 O ASN A 31 18.694 55.898 -41.955 1.00 4.85 ATOM 220 CB ASN A 31 15.760 55.424 -42.145 1.00 6.98 ATOM 221 CG ASN A 31 14.467 55.180 -42.966 1.00 14.28 ATOM 222 OD1 ASN A 31 13.762 56.123 -43.321 1.00 7.84 ATOM 223 ND2 ASN A 31 14.218 53.914 -43.341 1.00 16.55 ATOM 224 N MET A 32 17.807 57.813 -41.093 1.00 5.23 ATOM 225 CA MET A 32 18.898 58.140 -40.201 1.00 7.27 ATOM 226 C MET A 32 18.254 58.442 -38.836 1.00 8.07 ATOM 227 O MET A 32 17.211 58.997 -38.766 1.00 8.99 ATOM 228 CB MET A 32 19.672 59.387 -40.702 1.00 3.95 ATOM 229 CG MET A 32 20.577 59.136 -41.919 1.00 5.49 ATOM 230 SD MET A 32 21.698 60.644 -42.175 1.00 5.77 ATOM 231 CE MET A 32 22.930 60.281 -40.924 1.00 2.69 ATOM 232 N TYR A 33 18.939 58.049 -37.781 1.00 10.23 ATOM 233 CA TYR A 33 18.485 58.134 -36.453 1.00 11.65 ATOM 234 C TYR A 33 19.529 58.685 -35.519 1.00 13.00 ATOM 235 O TYR A 33 20.745 58.482 -35.738 1.00 14.80 ATOM 236 CB TYR A 33 18.183 56.755 -35.952 1.00 8.27 ATOM 237 CG TYR A 33 17.172 55.995 -36.797 1.00 9.16 ATOM 238 CD1 TYR A 33 17.567 55.372 -37.947 1.00 9.60 ATOM 239 CD2 TYR A 33 15.875 55.813 -36.394 1.00 8.35 ATOM 240 CE1 TYR A 33 16.726 54.629 -38.655 1.00 8.48 ATOM 241 CE2 TYR A 33 14.994 55.044 -37.161 1.00 4.06 ATOM 242 CZ TYR A 33 15.412 54.492 -38.272 1.00 2.00 ATOM 243 OH TYR A 33 14.651 53.753 -39.062 1.00 2.00 ATOM 244 N TRP A 34 19.017 59.313 -34.456 1.00 12.47 ATOM 245 CA TRP A 34 19.789 59.833 -33.397 1.00 14.01 ATOM 246 C TRP A 34 19.380 59.348 -32.091 1.00 14.80 ATOM 247 O TRP A 34 18.295 59.679 -31.673 1.00 13.65 ATOM 248 CB TRP A 34 19.719 61.354 -33.312 1.00 14.33 ATOM 249 CG TRP A 34 21.039 62.043 -33.708 1.00 14.58 ATOM 250 CD1 TRP A 34 21.164 63.184 -34.489 1.00 21.03 ATOM 251 CD2 TRP A 34 22.393 61.706 -33.337 1.00 21.37 ATOM 252 NE1 TRP A 34 22.489 63.581 -34.609 1.00 18.93 ATOM 253 CE2 TRP A 34 23.268 62.656 -33.967 1.00 22.46 ATOM 254 CE3 TRP A 34 22.966 60.679 -32.611 1.00 22.42 ATOM 255 CZ2 TRP A 34 24.640 62.626 -33.817 1.00 16.69 ATOM 256 CZ3 TRP A 34 24.360 60.669 -32.487 1.00 19.46 ATOM 257 CH2 TRP A 34 25.156 61.624 -33.089 1.00 16.75 ATOM 258 N TYR A 35 20.318 58.700 -31.373 1.00 16.59 ATOM 259 CA TYR A 35 20.025 58.048 -30.110 1.00 19.53 ATOM 260 C TYR A 35 20.770 58.434 -28.838 1.00 23.24 ATOM 261 O TYR A 35 21.798 59.136 -28.807 1.00 23.03 ATOM 262 CB TYR A 35 20.165 56.517 -30.238 1.00 19.62 ATOM 263 CG TYR A 35 19.116 55.815 -31.007 1.00 17.41 ATOM 264 CD1 TYR A 35 19.385 55.211 -32.233 1.00 24.24 ATOM 265 CD2 TYR A 35 17.824 55.757 -30.540 1.00 26.35 ATOM 266 CE1 TYR A 35 18.329 54.539 -32.996 1.00 23.20 ATOM 267 CE2 TYR A 35 16.774 55.105 -31.289 1.00 23.93 ATOM 268 CZ TYR A 35 17.047 54.502 -32.502 1.00 18.60 ATOM 269 OH TYR A 35 16.022 53.857 -33.132 1.00 18.41 ATOM 270 N ARG A 36 20.215 57.924 -27.745 1.00 26.23 ATOM 271 CA ARG A 36 20.751 58.211 -26.419 1.00 28.69 ATOM 272 C ARG A 36 20.212 57.170 -25.494 1.00 28.15 ATOM 273 O ARG A 36 19.027 56.836 -25.571 1.00 28.01 ATOM 274 CB ARG A 36 20.285 59.583 -25.939 1.00 27.85 ATOM 275 CG ARG A 36 20.493 59.755 -24.462 1.00 31.16 ATOM 276 CD ARG A 36 19.602 60.811 -23.864 1.00 33.89 ATOM 277 NE ARG A 36 20.211 61.355 -22.672 1.00 36.37 ATOM 278 CZ ARG A 36 19.768 62.446 -22.062 1.00 41.06 ATOM 279 NH1 ARG A 36 18.687 63.103 -22.518 1.00 39.15 ATOM 280 NH2 ARG A 36 20.414 62.881 -20.979 1.00 45.24 ATOM 281 N GLN A 37 21.052 56.654 -24.618 1.00 27.73 ATOM 282 CA GLN A 37 20.513 55.667 -23.666 1.00 29.93 ATOM 283 C GLN A 37 20.937 55.839 -22.220 1.00 32.10 ATOM 284 O GLN A 37 22.045 56.329 -21.956 1.00 31.45 ATOM 285 CB GLN A 37 20.940 54.259 -24.103 1.00 28.84 ATOM 286 CG GLN A 37 22.207 53.757 -23.477 1.00 28.69 ATOM 287 CD GLN A 37 23.398 54.608 -23.778 1.00 28.99 ATOM 288 OE1 GLN A 37 23.312 55.848 -23.782 1.00 31.15 ATOM 289 NE2 GLN A 37 24.542 53.954 -23.997 1.00 31.03 ATOM 290 N ASP A 38 20.091 55.359 -21.292 1.00 35.15 ATOM 291 CA ASP A 38 20.347 55.510 -19.830 1.00 37.59 ATOM 292 C ASP A 38 21.750 54.926 -19.513 1.00 39.77 ATOM 293 O ASP A 38 22.144 53.892 -20.107 1.00 39.61 ATOM 294 CB ASP A 38 19.246 54.830 -18.980 1.00 37.64 ATOM 295 CG ASP A 38 17.786 55.219 -19.403 1.00 40.45 ATOM 296 OD1 ASP A 38 16.827 54.657 -18.785 1.00 43.63 ATOM 297 OD2 ASP A 38 17.596 56.075 -20.341 1.00 42.66 ATOM 298 N THR A 39 22.522 55.610 -18.641 1.00 40.55 ATOM 299 CA THR A 39 23.847 55.118 -18.192 1.00 40.95 ATOM 300 C THR A 39 23.898 53.578 -18.042 1.00 40.92 ATOM 301 O THR A 39 23.483 53.036 -17.009 1.00 41.40 ATOM 302 CB THR A 39 24.208 55.719 -16.803 1.00 41.28 ATOM 303 OG1 THR A 39 23.294 55.208 -15.795 1.00 40.20 ATOM 304 CG2 THR A 39 24.172 57.241 -16.865 1.00 38.52 ATOM 305 N GLY A 40 24.365 52.867 -19.061 1.00 40.84 ATOM 306 CA GLY A 40 24.301 51.382 -19.003 1.00 39.24 ATOM 307 C GLY A 40 22.895 50.808 -18.952 1.00 39.07 ATOM 308 O GLY A 40 22.571 49.886 -18.168 1.00 38.71 ATOM 309 N HIS A 41 22.035 51.322 -19.806 1.00 38.93 ATOM 310 CA HIS A 41 20.732 50.721 -19.935 1.00 39.45 ATOM 311 C HIS A 41 20.433 50.476 -21.375 1.00 38.06 ATOM 312 O HIS A 41 21.288 49.913 -22.066 1.00 39.00 ATOM 313 CB HIS A 41 19.656 51.558 -19.295 1.00 40.24 ATOM 314 CG HIS A 41 19.886 51.795 -17.843 1.00 44.06 ATOM 315 ND1 HIS A 41 20.900 52.611 -17.378 1.00 44.73 ATOM 316 CD2 HIS A 41 19.210 51.352 -16.751 1.00 44.64 ATOM 317 CE1 HIS A 41 20.838 52.657 -16.056 1.00 48.20 ATOM 318 NE2 HIS A 41 19.828 51.897 -15.653 1.00 46.58 ATOM 319 N GLY A 42 19.234 50.901 -21.798 1.00 36.92 ATOM 320 CA GLY A 42 18.756 50.882 -23.205 1.00 33.98 ATOM 321 C GLY A 42 18.650 52.260 -23.892 1.00 32.32 ATOM 322 O GLY A 42 18.530 53.325 -23.203 1.00 30.64 ATOM 323 N LEU A 43 18.686 52.201 -25.244 1.00 30.24 ATOM 324 CA LEU A 43 18.813 53.349 -26.156 1.00 28.39 ATOM 325 C LEU A 43 17.429 53.821 -26.436 1.00 26.43 ATOM 326 O LEU A 43 16.610 53.017 -26.821 1.00 27.01 ATOM 327 CB LEU A 43 19.447 52.940 -27.507 1.00 26.17 ATOM 328 CG LEU A 43 20.808 52.296 -27.686 1.00 27.83 ATOM 329 CD1 LEU A 43 20.850 51.996 -29.120 1.00 20.60 ATOM 330 CD2 LEU A 43 22.063 53.200 -27.360 1.00 26.64 ATOM 331 N ARG A 44 17.190 55.112 -26.282 1.00 25.05 ATOM 332 CA ARG A 44 15.838 55.669 -26.456 1.00 21.42 ATOM 333 C ARG A 44 15.875 56.773 -27.502 1.00 18.53 ATOM 334 O ARG A 44 16.653 57.707 -27.355 1.00 15.20 ATOM 335 CB ARG A 44 15.350 56.296 -25.153 1.00 21.90 ATOM 336 CG ARG A 44 14.698 55.388 -24.124 1.00 25.18 ATOM 337 CD ARG A 44 14.147 56.223 -22.980 1.00 25.46 ATOM 338 NE ARG A 44 12.690 56.439 -23.148 1.00 32.69 ATOM 339 CZ ARG A 44 11.874 57.006 -22.248 1.00 31.77 ATOM 340 NH1 ARG A 44 12.363 57.448 -21.079 1.00 32.00 ATOM 341 NH2 ARG A 44 10.555 57.108 -22.503 1.00 30.75 ATOM 342 N LEU A 45 14.957 56.707 -28.469 1.00 16.07 ATOM 343 CA LEU A 45 14.820 57.706 -29.550 1.00 16.26 ATOM 344 C LEU A 45 14.482 59.159 -29.299 1.00 17.44 ATOM 345 O LEU A 45 13.280 59.517 -29.108 1.00 17.07 ATOM 346 CB LEU A 45 13.762 57.206 -30.568 1.00 16.13 ATOM 347 CG LEU A 45 13.630 57.726 -32.009 1.00 13.95 ATOM 348 CD1 LEU A 45 14.927 58.143 -32.676 1.00 9.54 ATOM 349 CD2 LEU A 45 12.942 56.649 -32.893 1.00 15.48 ATOM 350 N ILE A 46 15.475 60.026 -29.511 1.00 17.03 ATOM 351 CA ILE A 46 15.239 61.497 -29.465 1.00 17.15 ATOM 352 C ILE A 46 14.645 62.029 -30.738 1.00 17.84 ATOM 353 O ILE A 46 13.578 62.589 -30.728 1.00 16.66 ATOM 354 CB ILE A 46 16.535 62.247 -29.258 1.00 17.70 ATOM 355 CG1 ILE A 46 17.534 61.249 -28.731 1.00 17.56 ATOM 356 CG2 ILE A 46 16.338 63.315 -28.213 1.00 15.51 ATOM 357 CD1 ILE A 46 18.843 61.663 -29.077 1.00 31.46 ATOM 358 N HIS A 47 15.366 61.844 -31.845 1.00 18.47 ATOM 359 CA HIS A 47 14.915 62.350 -33.169 1.00 19.88 ATOM 360 C HIS A 47 15.342 61.473 -34.313 1.00 19.68 ATOM 361 O HIS A 47 16.442 60.924 -34.283 1.00 20.02 ATOM 362 CB HIS A 47 15.493 63.749 -33.415 1.00 18.60 ATOM 363 CG HIS A 47 14.717 64.794 -32.719 1.00 20.12 ATOM 364 ND1 HIS A 47 13.370 64.973 -32.962 1.00 19.16 ATOM 365 CD2 HIS A 47 15.052 65.676 -31.756 1.00 18.63 ATOM 366 CE1 HIS A 47 12.922 65.972 -32.223 1.00 21.23 ATOM 367 NE2 HIS A 47 13.925 66.433 -31.500 1.00 23.41 ATOM 368 N TYR A 48 14.499 61.385 -35.333 1.00 21.16 ATOM 369 CA TYR A 48 14.814 60.597 -36.549 1.00 20.65 ATOM 370 C TYR A 48 14.527 61.357 -37.816 1.00 21.75 ATOM 371 O TYR A 48 14.028 62.495 -37.743 1.00 23.47 ATOM 372 CB TYR A 48 14.078 59.310 -36.601 1.00 19.65 ATOM 373 CG TYR A 48 12.582 59.339 -36.698 1.00 15.57 ATOM 374 CD1 TYR A 48 11.852 59.965 -35.756 1.00 12.80 ATOM 375 CD2 TYR A 48 11.909 58.546 -37.644 1.00 13.82 ATOM 376 CE1 TYR A 48 10.495 59.958 -35.784 1.00 20.40 ATOM 377 CE2 TYR A 48 10.548 58.489 -37.674 1.00 20.23 ATOM 378 CZ TYR A 48 9.848 59.245 -36.721 1.00 21.09 ATOM 379 OH TYR A 48 8.507 59.262 -36.650 1.00 26.85 ATOM 380 N SER A 49 14.874 60.783 -38.965 1.00 21.01 ATOM 381 CA SER A 49 14.604 61.422 -40.248 1.00 21.90 ATOM 382 C SER A 49 14.467 60.424 -41.392 1.00 23.43 ATOM 383 O SER A 49 15.316 59.524 -41.525 1.00 25.88 ATOM 384 CB SER A 49 15.683 62.458 -40.535 1.00 20.33 ATOM 385 OG SER A 49 15.677 62.884 -41.871 1.00 20.71 ATOM 386 N TYR A 50 13.399 60.596 -42.210 1.00 25.27 ATOM 387 CA TYR A 50 13.154 59.850 -43.486 1.00 24.55 ATOM 388 C TYR A 50 13.955 60.321 -44.693 1.00 23.16 ATOM 389 O TYR A 50 14.199 59.547 -45.605 1.00 21.41 ATOM 390 CB TYR A 50 11.662 59.878 -43.843 1.00 25.93 ATOM 391 CG TYR A 50 10.801 59.254 -42.771 1.00 27.76 ATOM 392 CD1 TYR A 50 11.001 57.919 -42.349 1.00 23.84 ATOM 393 CD2 TYR A 50 9.786 60.020 -42.177 1.00 26.69 ATOM 394 CE1 TYR A 50 10.201 57.382 -41.364 1.00 29.67 ATOM 395 CE2 TYR A 50 9.017 59.535 -41.212 1.00 26.58 ATOM 396 CZ TYR A 50 9.186 58.226 -40.810 1.00 31.34 ATOM 397 OH TYR A 50 8.312 57.826 -39.836 1.00 30.53 ATOM 398 N GLY A 51 14.382 61.599 -44.667 1.00 24.09 ATOM 399 CA GLY A 51 15.044 62.217 -45.809 1.00 22.40 ATOM 400 C GLY A 51 15.515 63.611 -45.560 1.00 23.82 ATOM 401 O GLY A 51 14.961 64.313 -44.716 1.00 26.06 ATOM 402 N ALA A 52 16.553 64.051 -46.281 1.00 23.19 ATOM 403 CA ALA A 52 17.007 65.436 -46.141 1.00 23.91 ATOM 404 C ALA A 52 15.881 66.444 -46.162 1.00 24.25 ATOM 405 O ALA A 52 14.943 66.314 -46.916 1.00 25.89 ATOM 406 CB ALA A 52 18.151 65.807 -47.227 1.00 22.66 ATOM 407 N GLY A 53 16.015 67.459 -45.311 1.00 24.18 ATOM 408 CA GLY A 53 15.035 68.450 -45.106 1.00 22.02 ATOM 409 C GLY A 53 13.803 67.916 -44.403 1.00 22.81 ATOM 410 O GLY A 53 12.703 68.347 -44.689 1.00 21.34 ATOM 411 N SER A 54 13.971 66.935 -43.509 1.00 22.17 ATOM 412 CA SER A 54 12.877 66.527 -42.671 1.00 21.55 ATOM 413 C SER A 54 13.201 65.595 -41.507 1.00 21.71 ATOM 414 O SER A 54 13.686 64.487 -41.696 1.00 20.84 ATOM 415 CB SER A 54 11.802 65.882 -43.505 1.00 20.87 ATOM 416 OG SER A 54 10.948 65.235 -42.602 1.00 23.65 ATOM 417 N THR A 55 12.833 66.054 -40.303 1.00 22.12 ATOM 418 CA THR A 55 12.933 65.303 -39.070 1.00 21.61 ATOM 419 C THR A 55 11.540 65.066 -38.392 1.00 21.37 ATOM 420 O THR A 55 10.504 65.776 -38.677 1.00 18.29 ATOM 421 CB THR A 55 13.918 65.965 -38.099 1.00 21.00 ATOM 422 OG1 THR A 55 13.268 67.027 -37.418 1.00 22.30 ATOM 423 CG2 THR A 55 15.184 66.550 -38.840 1.00 24.47 ATOM 424 N GLU A 56 11.513 64.052 -37.523 1.00 21.59 ATOM 425 CA GLU A 56 10.357 63.828 -36.597 1.00 23.73 ATOM 426 C GLU A 56 10.811 63.516 -35.181 1.00 23.29 ATOM 427 O GLU A 56 11.898 62.891 -34.967 1.00 24.24 ATOM 428 CB GLU A 56 9.366 62.757 -37.097 1.00 22.89 ATOM 429 CG GLU A 56 8.972 62.899 -38.593 1.00 23.30 ATOM 430 CD GLU A 56 7.966 63.975 -38.767 1.00 24.59 ATOM 431 OE1 GLU A 56 6.975 63.962 -38.004 1.00 24.30 ATOM 432 OE2 GLU A 56 8.173 64.864 -39.630 1.00 22.90 ATOM 433 N LYS A 57 9.977 63.983 -34.260 1.00 21.97 ATOM 434 CA LYS A 57 10.125 63.815 -32.851 1.00 21.74 ATOM 435 C LYS A 57 10.046 62.357 -32.520 1.00 23.50 ATOM 436 O LYS A 57 9.113 61.660 -33.019 1.00 24.08 ATOM 437 CB LYS A 57 9.004 64.498 -32.131 1.00 21.29 ATOM 438 CG LYS A 57 9.092 66.030 -32.143 1.00 22.47 ATOM 439 CD LYS A 57 8.106 66.668 -31.228 1.00 17.06 ATOM 440 CE LYS A 57 6.736 66.528 -31.850 1.00 19.31 ATOM 441 NZ LYS A 57 5.969 67.741 -31.538 1.00 13.09 ATOM 442 N GLY A 58 11.013 61.945 -31.675 1.00 22.52 ATOM 443 CA GLY A 58 11.141 60.601 -31.144 1.00 23.14 ATOM 444 C GLY A 58 10.491 60.439 -29.804 1.00 23.00 ATOM 445 O GLY A 58 9.500 61.107 -29.477 1.00 25.96 ATOM 446 N ASP A 59 11.057 59.544 -29.011 1.00 22.81 ATOM 447 CA ASP A 59 10.479 59.219 -27.734 1.00 21.67 ATOM 448 C ASP A 59 10.615 60.410 -26.766 1.00 20.59 ATOM 449 O ASP A 59 9.570 60.910 -26.239 1.00 16.51 ATOM 450 CB ASP A 59 11.204 58.085 -27.102 1.00 21.61 ATOM 451 CG ASP A 59 10.902 56.820 -27.730 1.00 24.79 ATOM 452 OD1 ASP A 59 9.737 56.567 -28.095 1.00 31.31 ATOM 453 OD2 ASP A 59 11.864 56.042 -27.866 1.00 35.15 ATOM 454 N ILE A 60 11.906 60.748 -26.535 1.00 14.01 ATOM 455 CA ILE A 60 12.349 61.815 -25.704 1.00 12.85 ATOM 456 C ILE A 60 12.806 63.151 -26.431 1.00 13.38 ATOM 457 O ILE A 60 13.811 63.676 -26.085 1.00 7.88 ATOM 458 CB ILE A 60 13.442 61.322 -24.741 1.00 11.10 ATOM 459 CG1 ILE A 60 14.791 61.088 -25.491 1.00 7.48 ATOM 460 CG2 ILE A 60 12.981 60.093 -24.170 1.00 7.33 ATOM 461 CD1 ILE A 60 15.782 60.438 -24.619 1.00 6.63 ATOM 462 N PRO A 61 11.927 63.770 -27.291 1.00 15.12 ATOM 463 CA PRO A 61 12.273 64.920 -28.126 1.00 15.69 ATOM 464 C PRO A 61 12.844 66.019 -27.261 1.00 18.53 ATOM 465 O PRO A 61 14.033 66.465 -27.424 1.00 17.03 ATOM 466 CB PRO A 61 10.909 65.320 -28.776 1.00 18.22 ATOM 467 CG PRO A 61 9.837 64.631 -28.044 1.00 14.90 ATOM 468 CD PRO A 61 10.511 63.389 -27.425 1.00 15.95 ATOM 469 N ASP A 62 12.055 66.359 -26.241 1.00 19.16 ATOM 470 CA ASP A 62 12.335 67.506 -25.360 1.00 22.26 ATOM 471 C ASP A 62 13.779 67.849 -25.121 1.00 22.45 ATOM 472 O ASP A 62 14.600 66.976 -24.835 1.00 21.75 ATOM 473 CB ASP A 62 11.652 67.288 -24.035 1.00 22.99 ATOM 474 CG ASP A 62 10.145 67.026 -24.200 1.00 26.95 ATOM 475 OD1 ASP A 62 9.379 68.031 -24.343 1.00 27.55 ATOM 476 OD2 ASP A 62 9.751 65.812 -24.217 1.00 23.92 ATOM 477 N GLY A 63 14.084 69.127 -25.257 1.00 23.31 ATOM 478 CA GLY A 63 15.418 69.672 -24.964 1.00 23.00 ATOM 479 C GLY A 63 16.459 69.321 -26.028 1.00 25.36 ATOM 480 O GLY A 63 17.703 69.460 -25.831 1.00 24.68 ATOM 481 N TYR A 65 15.959 68.720 -27.420 1.00 19.63 ATOM 482 CA TYR A 65 16.878 68.607 -28.527 1.00 20.06 ATOM 483 C TYR A 65 16.368 69.227 -29.784 1.00 20.64 ATOM 484 O TYR A 65 15.126 69.419 -29.965 1.00 23.12 ATOM 485 CB TYR A 65 17.234 67.148 -28.747 1.00 19.26 ATOM 486 CG TYR A 65 18.014 66.628 -27.603 1.00 18.44 ATOM 487 CD1 TYR A 65 19.403 66.906 -27.457 1.00 16.23 ATOM 488 CD2 TYR A 65 17.393 65.948 -26.599 1.00 14.82 ATOM 489 CE1 TYR A 65 20.115 66.405 -26.338 1.00 17.23 ATOM 490 CE2 TYR A 65 18.076 65.465 -25.489 1.00 17.56 ATOM 491 CZ TYR A 65 19.409 65.684 -25.339 1.00 20.74 ATOM 492 OH TYR A 65 20.037 65.156 -24.211 1.00 24.31 ATOM 493 N LYS A 66 17.332 69.545 -30.665 1.00 20.59 ATOM 494 CA LYS A 66 17.100 70.052 -32.030 1.00 18.57 ATOM 495 C LYS A 66 17.852 69.194 -32.963 1.00 17.77 ATOM 496 O LYS A 66 18.948 68.800 -32.639 1.00 20.25 ATOM 497 CB LYS A 66 17.584 71.478 -32.191 1.00 18.01 ATOM 498 CG LYS A 66 16.390 72.410 -32.349 1.00 14.95 ATOM 499 CD LYS A 66 15.674 72.462 -31.017 1.00 14.01 ATOM 500 CE LYS A 66 14.751 73.705 -30.789 1.00 21.17 ATOM 501 NZ LYS A 66 15.542 75.062 -30.712 1.00 20.26 ATOM 502 N ALA A 67 17.283 68.861 -34.109 1.00 16.92 ATOM 503 CA ALA A 67 18.016 68.067 -35.075 1.00 16.23 ATOM 504 C ALA A 67 18.008 68.801 -36.409 1.00 15.26 ATOM 505 O ALA A 67 17.425 69.935 -36.527 1.00 15.93 ATOM 506 CB ALA A 67 17.514 66.589 -35.160 1.00 13.96 ATOM 507 N SER A 68 18.698 68.217 -37.398 1.00 12.50 ATOM 508 CA SER A 68 18.651 68.734 -38.754 1.00 10.06 ATOM 509 C SER A 68 19.205 67.806 -39.812 1.00 9.01 ATOM 510 O SER A 68 20.371 67.363 -39.695 1.00 9.10 ATOM 511 CB SER A 68 19.462 70.011 -38.820 1.00 8.25 ATOM 512 OG SER A 68 19.426 70.358 -40.171 1.00 9.36 ATOM 513 N ARG A 69 18.460 67.575 -40.888 1.00 7.32 ATOM 514 CA ARG A 69 18.987 66.675 -42.042 1.00 6.51 ATOM 515 C ARG A 69 19.050 67.470 -43.266 1.00 6.32 ATOM 516 O ARG A 69 18.025 67.776 -43.877 1.00 7.29 ATOM 517 CB ARG A 69 18.025 65.512 -42.346 1.00 7.56 ATOM 518 CG ARG A 69 18.425 64.404 -43.244 1.00 2.00 ATOM 519 CD ARG A 69 19.062 63.260 -42.459 1.00 7.87 ATOM 520 NE ARG A 69 19.565 62.159 -43.299 1.00 2.00 ATOM 521 CZ ARG A 69 18.724 61.367 -43.970 1.00 9.88 ATOM 522 NH1 ARG A 69 19.189 60.339 -44.719 1.00 2.65 ATOM 523 NH2 ARG A 69 17.380 61.594 -43.841 1.00 6.65 ATOM 524 N PRO A 70 20.233 67.879 -43.615 1.00 8.98 ATOM 525 CA PRO A 70 20.571 68.724 -44.742 1.00 8.76 ATOM 526 C PRO A 70 20.981 68.046 -45.986 1.00 8.00 ATOM 527 O PRO A 70 21.057 68.718 -47.017 1.00 8.50 ATOM 528 CB PRO A 70 21.709 69.611 -44.185 1.00 10.30 ATOM 529 CG PRO A 70 22.478 68.558 -43.262 1.00 10.69 ATOM 530 CD PRO A 70 21.396 67.681 -42.695 1.00 11.50 ATOM 531 N SER A 71 21.092 66.704 -45.949 1.00 10.22 ATOM 532 CA SER A 71 21.519 65.934 -47.038 1.00 7.07 ATOM 533 C SER A 71 21.439 64.413 -46.663 1.00 10.49 ATOM 534 O SER A 71 22.057 64.013 -45.654 1.00 12.31 ATOM 535 CB SER A 71 22.961 66.344 -47.335 1.00 9.69 ATOM 536 OG SER A 71 23.860 66.173 -46.280 1.00 6.34 ATOM 537 N GLN A 72 20.687 63.610 -47.418 1.00 7.39 ATOM 538 CA GLN A 72 20.667 62.122 -47.333 1.00 10.10 ATOM 539 C GLN A 72 21.697 61.453 -46.511 1.00 10.83 ATOM 540 O GLN A 72 21.357 60.718 -45.696 1.00 15.05 ATOM 541 CB GLN A 72 20.553 61.480 -48.729 1.00 8.55 ATOM 542 CG GLN A 72 19.132 60.903 -48.997 1.00 6.16 ATOM 543 CD GLN A 72 18.945 59.442 -48.739 1.00 4.96 ATOM 544 OE1 GLN A 72 19.928 58.648 -48.743 1.00 7.54 ATOM 545 NE2 GLN A 72 17.665 59.032 -48.424 1.00 4.14 ATOM 546 N GLU A 73 22.967 61.840 -46.616 1.00 18.10 ATOM 547 CA GLU A 73 24.014 61.227 -45.813 1.00 20.45 ATOM 548 C GLU A 73 24.460 62.009 -44.574 1.00 21.25 ATOM 549 O GLU A 73 25.455 61.657 -43.906 1.00 22.74 ATOM 550 CB GLU A 73 25.204 60.777 -46.715 1.00 21.37 ATOM 551 CG GLU A 73 26.107 61.919 -47.214 1.00 25.91 ATOM 552 CD GLU A 73 25.471 62.696 -48.296 1.00 30.33 ATOM 553 OE1 GLU A 73 25.819 63.890 -48.434 1.00 36.07 ATOM 554 OE2 GLU A 73 24.575 62.130 -48.985 1.00 37.75 ATOM 555 N GLN A 74 23.753 63.069 -44.218 1.00 21.10 ATOM 556 CA GLN A 74 24.223 63.914 -43.050 1.00 18.96 ATOM 557 C GLN A 74 23.063 64.248 -42.126 1.00 19.32 ATOM 558 O GLN A 74 21.965 64.539 -42.642 1.00 20.50 ATOM 559 CB GLN A 74 24.840 65.155 -43.538 1.00 16.28 ATOM 560 CG GLN A 74 25.188 66.134 -42.337 1.00 20.77 ATOM 561 CD GLN A 74 26.198 65.514 -41.271 1.00 18.29 ATOM 562 OE1 GLN A 74 26.127 65.828 -40.078 1.00 18.61 ATOM 563 NE2 GLN A 74 27.109 64.603 -41.728 1.00 22.03 ATOM 564 N PHE A 75 23.271 64.195 -40.802 1.00 20.12 ATOM 565 CA PHE A 75 22.225 64.478 -39.692 1.00 20.28 ATOM 566 C PHE A 75 23.044 65.020 -38.500 1.00 20.22 ATOM 567 O PHE A 75 24.233 64.606 -38.304 1.00 21.49 ATOM 568 CB PHE A 75 21.526 63.178 -39.228 1.00 19.63 ATOM 569 CG PHE A 75 20.143 63.339 -38.633 1.00 19.51 ATOM 570 CD1 PHE A 75 19.429 64.541 -38.725 1.00 17.91 ATOM 571 CD2 PHE A 75 19.501 62.247 -38.086 1.00 15.80 ATOM 572 CE1 PHE A 75 18.126 64.640 -38.263 1.00 18.24 ATOM 573 CE2 PHE A 75 18.170 62.395 -37.596 1.00 18.85 ATOM 574 CZ PHE A 75 17.509 63.600 -37.706 1.00 13.17 ATOM 575 N SER A 76 22.438 65.895 -37.724 1.00 18.33 ATOM 576 CA SER A 76 23.094 66.642 -36.635 1.00 19.06 ATOM 577 C SER A 76 22.195 66.909 -35.418 1.00 19.81 ATOM 578 O SER A 76 20.976 67.121 -35.561 1.00 21.88 ATOM 579 CB SER A 76 23.724 67.957 -37.150 1.00 17.55 ATOM 580 OG SER A 76 24.248 67.727 -38.459 1.00 15.12 ATOM 581 N LEU A 77 22.764 66.836 -34.218 1.00 19.96 ATOM 582 CA LEU A 77 21.937 66.978 -32.984 1.00 21.04 ATOM 583 C LEU A 77 22.306 68.335 -32.408 1.00 22.72 ATOM 584 O LEU A 77 23.515 68.564 -32.114 1.00 23.84 ATOM 585 CB LEU A 77 22.267 65.859 -31.972 1.00 19.71 ATOM 586 CG LEU A 77 21.254 65.468 -30.936 1.00 16.37 ATOM 587 CD1 LEU A 77 20.058 65.094 -31.704 1.00 23.34 ATOM 588 CD2 LEU A 77 21.653 64.259 -30.036 1.00 19.34 ATOM 589 N ILE A 78 21.331 69.241 -32.370 1.00 24.76 ATOM 590 CA ILE A 78 21.572 70.568 -31.829 1.00 28.07 ATOM 591 C ILE A 78 21.116 70.641 -30.376 1.00 29.24 ATOM 592 O ILE A 78 20.137 70.001 -29.992 1.00 29.48 ATOM 593 CB ILE A 78 21.083 71.747 -32.771 1.00 28.37 ATOM 594 CG1 ILE A 78 21.845 71.695 -34.109 1.00 30.48 ATOM 595 CG2 ILE A 78 21.437 73.125 -32.176 1.00 25.48 ATOM 596 CD1 ILE A 78 21.085 72.241 -35.308 1.00 32.11 ATOM 597 N LEU A 79 21.894 71.361 -29.572 1.00 31.09 ATOM 598 CA LEU A 79 21.646 71.560 -28.153 1.00 33.06 ATOM 599 C LEU A 79 21.943 72.998 -27.807 1.00 33.59 ATOM 600 O LEU A 79 23.115 73.408 -27.776 1.00 34.79 ATOM 601 CB LEU A 79 22.576 70.648 -27.361 1.00 33.63 ATOM 602 CG LEU A 79 22.018 69.218 -27.316 1.00 33.58 ATOM 603 CD1 LEU A 79 22.503 68.427 -28.455 1.00 35.82 ATOM 604 CD2 LEU A 79 22.473 68.540 -26.077 1.00 32.36 ATOM 605 N GLU A 80 20.890 73.777 -27.589 1.00 34.47 ATOM 606 CA GLU A 80 21.055 75.212 -27.578 1.00 34.81 ATOM 607 C GLU A 80 21.702 75.589 -26.248 1.00 35.80 ATOM 608 O GLU A 80 22.928 75.889 -26.179 1.00 37.02 ATOM 609 CB GLU A 80 19.721 75.882 -27.786 1.00 34.59 ATOM 610 CG GLU A 80 19.770 77.292 -28.411 1.00 34.90 ATOM 611 CD GLU A 80 19.674 77.291 -29.941 1.00 35.81 ATOM 612 OE1 GLU A 80 18.613 76.862 -30.493 1.00 33.77 ATOM 613 OE2 GLU A 80 20.666 77.723 -30.575 1.00 33.25 ATOM 614 N SER A 81 20.928 75.517 -25.170 1.00 34.67 ATOM 615 CA SER A 81 21.519 75.649 -23.834 1.00 33.28 ATOM 616 C SER A 81 21.590 74.271 -23.172 1.00 32.90 ATOM 617 O SER A 81 20.570 73.728 -22.759 1.00 32.83 ATOM 618 CB SER A 81 20.715 76.626 -22.949 1.00 34.47 ATOM 619 OG SER A 81 20.274 77.805 -23.635 1.00 33.38 ATOM 620 N ALA A 82 22.800 73.708 -23.122 1.00 32.67 ATOM 621 CA ALA A 82 23.068 72.434 -22.458 1.00 32.37 ATOM 622 C ALA A 82 22.717 72.504 -21.007 1.00 32.22 ATOM 623 O ALA A 82 22.595 73.598 -20.430 1.00 34.49 ATOM 624 CB ALA A 82 24.509 72.063 -22.586 1.00 31.35 ATOM 625 N THR A 83 22.610 71.333 -20.405 1.00 31.68 ATOM 626 CA THR A 83 22.424 71.174 -18.960 1.00 31.76 ATOM 627 C THR A 83 22.860 69.746 -18.549 1.00 31.96 ATOM 628 O THR A 83 22.633 68.790 -19.318 1.00 32.23 ATOM 629 CB THR A 83 20.925 71.301 -18.557 1.00 30.60 ATOM 630 OG1 THR A 83 20.235 70.118 -18.976 1.00 28.00 ATOM 631 CG2 THR A 83 20.285 72.495 -19.217 1.00 33.27 ATOM 632 N PRO A 84 23.476 69.604 -17.357 1.00 31.47 ATOM 633 CA PRO A 84 24.094 68.370 -16.921 1.00 30.69 ATOM 634 C PRO A 84 23.235 67.208 -17.192 1.00 30.90 ATOM 635 O PRO A 84 23.740 66.259 -17.733 1.00 32.14 ATOM 636 CB PRO A 84 24.305 68.597 -15.458 1.00 31.44 ATOM 637 CG PRO A 84 24.748 70.155 -15.443 1.00 30.69 ATOM 638 CD PRO A 84 23.703 70.712 -16.399 1.00 32.64 ATOM 639 N SER A 85 21.940 67.289 -16.909 1.00 30.74 ATOM 640 CA SER A 85 20.986 66.254 -17.312 1.00 30.68 ATOM 641 C SER A 85 21.299 65.585 -18.671 1.00 29.82 ATOM 642 O SER A 85 21.387 64.336 -18.758 1.00 29.59 ATOM 643 CB SER A 85 19.586 66.850 -17.402 1.00 31.56 ATOM 644 OG SER A 85 19.367 67.736 -16.333 1.00 34.84 ATOM 645 N GLN A 86 21.439 66.414 -19.717 1.00 27.94 ATOM 646 CA GLN A 86 21.732 65.966 -21.084 1.00 26.08 ATOM 647 C GLN A 86 23.091 65.288 -21.160 1.00 26.67 ATOM 648 O GLN A 86 23.608 64.988 -22.240 1.00 28.23 ATOM 649 CB GLN A 86 21.691 67.140 -22.047 1.00 25.17 ATOM 650 CG GLN A 86 20.319 67.829 -22.172 1.00 20.93 ATOM 651 CD GLN A 86 20.368 69.002 -23.076 1.00 21.62 ATOM 652 OE1 GLN A 86 21.401 69.744 -23.136 1.00 23.80 ATOM 653 NE2 GLN A 86 19.287 69.208 -23.820 1.00 23.26 ATOM 654 N THR A 87 23.683 64.999 -20.023 1.00 26.64 ATOM 655 CA THR A 87 25.012 64.384 -20.074 1.00 25.84 ATOM 656 C THR A 87 24.914 62.912 -20.298 1.00 24.76 ATOM 657 O THR A 87 24.318 62.224 -19.474 1.00 24.67 ATOM 658 CB THR A 87 25.758 64.614 -18.804 1.00 25.33 ATOM 659 OG1 THR A 87 26.164 65.997 -18.742 1.00 28.64 ATOM 660 CG2 THR A 87 26.982 63.731 -18.783 1.00 27.86 ATOM 661 N SER A 88 25.501 62.395 -21.391 1.00 24.36 ATOM 662 CA SER A 88 25.407 60.952 -21.684 1.00 21.73 ATOM 663 C SER A 88 26.274 60.418 -22.863 1.00 22.18 ATOM 664 O SER A 88 27.319 61.007 -23.207 1.00 19.63 ATOM 665 CB SER A 88 23.940 60.567 -21.884 1.00 20.91 ATOM 666 OG SER A 88 23.838 59.253 -22.405 1.00 24.54 ATOM 667 N VAL A 89 25.808 59.310 -23.478 1.00 21.23 ATOM 668 CA VAL A 89 26.430 58.712 -24.647 1.00 20.48 ATOM 669 C VAL A 89 25.371 58.628 -25.771 1.00 20.61 ATOM 670 O VAL A 89 24.345 57.912 -25.598 1.00 19.43 ATOM 671 CB VAL A 89 26.952 57.283 -24.320 1.00 19.60 ATOM 672 CG1 VAL A 89 27.430 56.704 -25.530 1.00 22.57 ATOM 673 CG2 VAL A 89 28.099 57.282 -23.399 1.00 17.69 ATOM 674 N TYR A 90 25.614 59.411 -26.856 1.00 20.59 ATOM 675 CA TYR A 90 24.821 59.476 -28.078 1.00 19.75 ATOM 676 C TYR A 90 25.227 58.495 -29.234 1.00 19.70 ATOM 677 O TYR A 90 26.435 58.282 -29.492 1.00 20.90 ATOM 678 CB TYR A 90 24.762 60.934 -28.553 1.00 21.37 ATOM 679 CG TYR A 90 24.112 61.839 -27.490 1.00 20.56 ATOM 680 CD1 TYR A 90 24.860 62.303 -26.407 1.00 19.91 ATOM 681 CD2 TYR A 90 22.802 62.251 -27.588 1.00 16.94 ATOM 682 CE1 TYR A 90 24.305 63.093 -25.447 1.00 17.31 ATOM 683 CE2 TYR A 90 22.245 63.063 -26.606 1.00 12.46 ATOM 684 CZ TYR A 90 22.998 63.423 -25.533 1.00 17.07 ATOM 685 OH TYR A 90 22.497 64.165 -24.526 1.00 18.29 ATOM 686 N PHE A 91 24.268 57.943 -29.983 1.00 18.99 ATOM 687 CA PHE A 91 24.676 56.971 -31.084 1.00 18.42 ATOM 688 C PHE A 91 23.810 57.255 -32.288 1.00 17.15 ATOM 689 O PHE A 91 22.624 57.554 -32.137 1.00 16.37 ATOM 690 CB PHE A 91 24.418 55.526 -30.739 1.00 16.98 ATOM 691 CG PHE A 91 25.403 54.914 -29.845 1.00 16.49 ATOM 692 CD1 PHE A 91 26.490 54.188 -30.362 1.00 19.19 ATOM 693 CD2 PHE A 91 25.190 54.910 -28.510 1.00 17.43 ATOM 694 CE1 PHE A 91 27.372 53.597 -29.593 1.00 15.02 ATOM 695 CE2 PHE A 91 26.066 54.366 -27.712 1.00 15.69 ATOM 696 CZ PHE A 91 27.241 53.687 -28.268 1.00 17.74 ATOM 697 N CYS A 92 24.399 57.129 -33.464 1.00 16.41 ATOM 698 CA CYS A 92 23.771 57.517 -34.705 1.00 16.96 ATOM 699 C CYS A 92 23.599 56.269 -35.504 1.00 15.72 ATOM 700 O CYS A 92 24.488 55.435 -35.526 1.00 16.29 ATOM 701 CB CYS A 92 24.678 58.472 -35.489 1.00 18.61 ATOM 702 SG CYS A 92 23.944 59.212 -37.011 1.00 23.63 ATOM 703 N ALA A 93 22.458 56.140 -36.165 1.00 13.99 ATOM 704 CA ALA A 93 22.243 55.027 -37.068 1.00 11.57 ATOM 705 C ALA A 93 21.548 55.415 -38.349 1.00 12.39 ATOM 706 O ALA A 93 20.745 56.401 -38.424 1.00 11.49 ATOM 707 CB ALA A 93 21.489 53.930 -36.413 1.00 10.15 ATOM 708 N SER A 94 21.759 54.539 -39.329 1.00 12.18 ATOM 709 CA SER A 94 21.044 54.576 -40.607 1.00 9.60 ATOM 710 C SER A 94 20.648 53.183 -40.926 1.00 9.12 ATOM 711 O SER A 94 21.406 52.166 -40.720 1.00 6.58 ATOM 712 CB SER A 94 22.023 55.019 -41.649 1.00 7.65 ATOM 713 OG SER A 94 23.207 54.268 -41.355 1.00 12.05 ATOM 714 N GLY A 95 19.505 53.169 -41.543 1.00 11.63 ATOM 715 CA GLY A 95 18.600 52.030 -41.608 1.00 12.49 ATOM 716 C GLY A 95 17.878 52.015 -42.984 1.00 14.87 ATOM 717 O GLY A 95 17.472 53.076 -43.480 1.00 14.59 ATOM 718 N GLY A 96 17.720 50.808 -43.601 1.00 15.93 ATOM 719 CA GLY A 96 17.256 50.745 -45.014 1.00 16.18 ATOM 720 C GLY A 96 17.464 49.438 -45.734 1.00 17.00 ATOM 721 O GLY A 96 18.383 48.692 -45.438 1.00 17.51 ATOM 722 N GLY A 97 16.588 49.132 -46.678 1.00 18.28 ATOM 723 CA GLY A 97 16.631 47.827 -47.309 1.00 17.77 ATOM 724 C GLY A 97 17.089 46.726 -46.412 1.00 18.83 ATOM 725 O GLY A 97 17.969 46.009 -46.752 1.00 20.47 ATOM 726 N GLY A 98 16.462 46.553 -45.261 1.00 21.86 ATOM 727 CA GLY A 98 16.840 45.474 -44.308 1.00 23.33 ATOM 728 C GLY A 98 18.162 45.786 -43.608 1.00 25.81 ATOM 729 O GLY A 98 19.022 44.886 -43.439 1.00 25.35 ATOM 730 N THR A 99 18.368 47.057 -43.204 1.00 24.75 ATOM 731 CA THR A 99 19.680 47.437 -42.682 1.00 25.00 ATOM 732 C THR A 99 19.548 48.550 -41.602 1.00 24.87 ATOM 733 O THR A 99 18.457 49.170 -41.491 1.00 24.41 ATOM 734 CB THR A 99 20.609 47.780 -43.897 1.00 26.72 ATOM 735 OG1 THR A 99 20.607 46.656 -44.794 1.00 29.51 ATOM 736 CG2 THR A 99 22.060 48.119 -43.519 1.00 24.08 ATOM 737 N LEU A 100 20.603 48.685 -40.770 1.00 22.07 ATOM 738 CA LEU A 100 20.668 49.552 -39.620 1.00 21.67 ATOM 739 C LEU A 100 22.149 49.677 -39.220 1.00 22.92 ATOM 740 O LEU A 100 22.780 48.691 -38.892 1.00 22.85 ATOM 741 CB LEU A 100 19.827 49.030 -38.442 1.00 22.58 ATOM 742 CG LEU A 100 19.595 49.844 -37.168 1.00 21.21 ATOM 743 CD1 LEU A 100 19.535 51.364 -37.409 1.00 25.83 ATOM 744 CD2 LEU A 100 18.396 49.373 -36.361 1.00 20.40 ATOM 745 N TYR A 101 22.715 50.878 -39.273 1.00 21.83 ATOM 746 CA TYR A 101 24.121 50.939 -38.988 1.00 21.69 ATOM 747 C TYR A 101 24.314 51.712 -37.736 1.00 20.75 ATOM 748 O TYR A 101 23.656 52.703 -37.532 1.00 19.76 ATOM 749 CB TYR A 101 24.890 51.480 -40.186 1.00 22.03 ATOM 750 CG TYR A 101 25.320 50.372 -41.087 1.00 22.85 ATOM 751 CD1 TYR A 101 25.923 50.635 -42.288 1.00 25.76 ATOM 752 CD2 TYR A 101 25.099 49.037 -40.731 1.00 28.10 ATOM 753 CE1 TYR A 101 26.322 49.615 -43.147 1.00 29.14 ATOM 754 CE2 TYR A 101 25.478 47.958 -41.570 1.00 27.04 ATOM 755 CZ TYR A 101 26.097 48.266 -42.799 1.00 28.81 ATOM 756 OH TYR A 101 26.508 47.282 -43.689 1.00 25.17 ATOM 757 N PHE A 108 25.796 51.509 -36.846 1.00 23.14 ATOM 758 CA PHE A 108 25.593 52.538 -35.802 1.00 22.74 ATOM 759 C PHE A 108 26.853 53.325 -35.788 1.00 23.97 ATOM 760 O PHE A 108 27.890 52.816 -36.196 1.00 25.37 ATOM 761 CB PHE A 108 25.475 51.881 -34.427 1.00 22.25 ATOM 762 CG PHE A 108 24.058 51.459 -34.040 1.00 16.70 ATOM 763 CD1 PHE A 108 23.678 50.130 -34.142 1.00 15.08 ATOM 764 CD2 PHE A 108 23.131 52.378 -33.574 1.00 18.12 ATOM 765 CE1 PHE A 108 22.438 49.732 -33.768 1.00 16.12 ATOM 766 CE2 PHE A 108 21.855 51.997 -33.209 1.00 7.42 ATOM 767 CZ PHE A 108 21.483 50.736 -33.298 1.00 12.82 ATOM 768 N GLY A 109 26.807 54.533 -35.273 1.00 23.99 ATOM 769 CA GLY A 109 28.025 55.292 -35.101 1.00 24.15 ATOM 770 C GLY A 109 28.791 54.785 -33.905 1.00 24.01 ATOM 771 O GLY A 109 28.454 53.768 -33.315 1.00 23.80 ATOM 772 N ALA A 110 29.861 55.467 -33.547 1.00 25.49 ATOM 773 CA ALA A 110 30.728 54.861 -32.550 1.00 25.77 ATOM 774 C ALA A 110 30.348 55.522 -31.280 1.00 26.56 ATOM 775 O ALA A 110 30.881 55.249 -30.243 1.00 28.13 ATOM 776 CB ALA A 110 32.212 55.059 -32.896 1.00 26.23 ATOM 777 N GLY A 111 29.351 56.381 -31.346 1.00 27.71 ATOM 778 CA GLY A 111 28.863 56.987 -30.135 1.00 27.86 ATOM 779 C GLY A 111 29.637 58.278 -29.814 1.00 27.73 ATOM 780 O GLY A 111 30.829 58.413 -30.117 1.00 26.03 ATOM 781 N THR A 112 28.935 59.222 -29.182 1.00 28.75 ATOM 782 CA THR A 112 29.537 60.467 -28.644 1.00 28.28 ATOM 783 C THR A 112 29.319 60.549 -27.147 1.00 28.92 ATOM 784 O THR A 112 28.196 60.439 -26.702 1.00 30.00 ATOM 785 CB THR A 112 28.947 61.626 -29.319 1.00 28.48 ATOM 786 OG1 THR A 112 29.185 61.457 -30.712 1.00 28.68 ATOM 787 CG2 THR A 112 29.594 62.918 -28.838 1.00 31.20 ATOM 788 N ARG A 113 30.403 60.636 -26.377 1.00 30.74 ATOM 789 CA ARG A 113 30.387 60.678 -24.924 1.00 32.03 ATOM 790 C ARG A 113 30.446 62.132 -24.544 1.00 31.11 ATOM 791 O ARG A 113 31.453 62.776 -24.809 1.00 32.54 ATOM 792 CB ARG A 113 31.630 59.986 -24.374 1.00 32.00 ATOM 793 CG ARG A 113 31.649 58.473 -24.550 1.00 35.71 ATOM 794 CD ARG A 113 32.988 57.842 -24.112 1.00 37.55 ATOM 795 NE ARG A 113 33.135 56.454 -24.554 1.00 44.07 ATOM 796 CZ ARG A 113 34.213 55.711 -24.329 1.00 48.18 ATOM 797 NH1 ARG A 113 34.232 54.447 -24.748 1.00 49.96 ATOM 798 NH2 ARG A 113 35.280 56.233 -23.702 1.00 51.15 ATOM 799 N LEU A 114 29.386 62.644 -23.908 1.00 30.65 ATOM 800 CA LEU A 114 29.223 64.073 -23.619 1.00 29.44 ATOM 801 C LEU A 114 29.274 64.390 -22.127 1.00 29.99 ATOM 802 O LEU A 114 29.050 63.498 -21.318 1.00 29.03 ATOM 803 CB LEU A 114 27.924 64.575 -24.216 1.00 29.38 ATOM 804 CG LEU A 114 27.736 66.059 -23.995 1.00 27.56 ATOM 805 CD1 LEU A 114 28.957 66.681 -24.544 1.00 27.56 ATOM 806 CD2 LEU A 114 26.492 66.543 -24.706 1.00 25.50 ATOM 807 N SER A 115 29.539 65.670 -21.765 1.00 30.00 ATOM 808 CA SER A 115 29.621 66.072 -20.353 1.00 27.94 ATOM 809 C SER A 115 29.199 67.512 -20.170 1.00 27.64 ATOM 810 O SER A 115 29.829 68.465 -20.669 1.00 25.16 ATOM 811 CB SER A 115 31.035 65.824 -19.800 1.00 27.42 ATOM 812 OG SER A 115 31.646 64.723 -20.470 1.00 27.25 ATOM 813 N VAL A 116 28.123 67.651 -19.401 1.00 28.68 ATOM 814 CA VAL A 116 27.453 68.912 -19.238 1.00 29.51 ATOM 815 C VAL A 116 27.605 69.348 -17.817 1.00 30.12 ATOM 816 O VAL A 116 26.847 68.922 -16.934 1.00 30.98 ATOM 817 CB VAL A 116 25.946 68.867 -19.510 1.00 29.62 ATOM 818 CG1 VAL A 116 25.479 70.293 -19.652 1.00 29.79 ATOM 819 CG2 VAL A 116 25.636 68.102 -20.793 1.00 30.72 ATOM 820 N LEU A 117 28.600 70.205 -17.611 1.00 30.29 ATOM 821 CA LEU A 117 29.021 70.664 -16.285 1.00 30.02 ATOM 822 C LEU A 117 28.991 72.211 -16.238 1.00 31.55 ATOM 823 O LEU A 117 28.115 72.739 -15.535 1.00 32.99 ATOM 824 CB LEU A 117 30.402 70.080 -15.927 1.00 27.75 ATOM 825 CG LEU A 117 31.582 70.437 -16.806 1.00 25.62 ATOM 826 CD1 LEU A 117 32.102 71.840 -16.433 1.00 25.56 ATOM 827 CD2 LEU A 117 32.699 69.428 -16.689 1.00 25.18 ATOM 828 OXT LEU A 117 29.765 72.971 -16.897 1.00 32.42 ATOM 830 N SER B 2 -12.922 87.868 -57.323 1.00 49.46 ATOM 831 CA SER B 2 -11.806 87.540 -56.402 1.00 48.79 ATOM 832 C SER B 2 -12.055 86.351 -55.422 1.00 49.31 ATOM 833 O SER B 2 -13.190 85.844 -55.322 1.00 48.83 ATOM 834 CB SER B 2 -11.469 88.790 -55.623 1.00 48.77 ATOM 835 OG SER B 2 -10.170 88.647 -55.125 1.00 48.31 ATOM 836 N GLN B 3 -10.986 85.888 -54.740 1.00 49.19 ATOM 837 CA GLN B 3 -11.064 84.920 -53.596 1.00 48.86 ATOM 838 C GLN B 3 -11.487 85.698 -52.298 1.00 49.55 ATOM 839 O GLN B 3 -10.695 86.513 -51.788 1.00 50.05 ATOM 840 CB GLN B 3 -9.707 84.192 -53.388 1.00 48.33 ATOM 841 CG GLN B 3 -9.746 82.913 -52.500 1.00 47.69 ATOM 842 CD GLN B 3 -8.367 82.248 -52.242 1.00 46.58 ATOM 843 OE1 GLN B 3 -8.265 81.026 -52.113 1.00 42.58 ATOM 844 NE2 GLN B 3 -7.321 83.060 -52.145 1.00 42.62 ATOM 845 N PRO B 4 -12.730 85.463 -51.772 1.00 49.48 ATOM 846 CA PRO B 4 -13.194 86.135 -50.554 1.00 49.75 ATOM 847 C PRO B 4 -12.220 85.975 -49.369 1.00 49.79 ATOM 848 O PRO B 4 -11.565 84.909 -49.257 1.00 50.72 ATOM 849 CB PRO B 4 -14.531 85.438 -50.253 1.00 49.38 ATOM 850 CG PRO B 4 -14.546 84.264 -51.047 1.00 49.06 ATOM 851 CD PRO B 4 -13.771 84.553 -52.267 1.00 49.45 ATOM 852 N ASP B 5 -12.093 87.039 -48.555 1.00 48.69 ATOM 853 CA ASP B 5 -11.260 87.080 -47.343 1.00 47.45 ATOM 854 C ASP B 5 -11.474 85.845 -46.457 1.00 47.10 ATOM 855 O ASP B 5 -12.635 85.374 -46.332 1.00 48.05 ATOM 856 CB ASP B 5 -11.551 88.375 -46.572 1.00 48.22 ATOM 857 CG ASP B 5 -10.393 89.390 -46.650 1.00 47.87 ATOM 858 OD1 ASP B 5 -10.500 90.526 -46.098 1.00 46.94 ATOM 859 OD2 ASP B 5 -9.356 89.014 -47.235 1.00 47.90 ATOM 860 N PRO B 6 -10.389 85.287 -45.865 1.00 45.35 ATOM 861 CA PRO B 6 -10.480 83.963 -45.209 1.00 44.40 ATOM 862 C PRO B 6 -11.416 84.024 -44.032 1.00 43.68 ATOM 863 O PRO B 6 -11.791 85.140 -43.617 1.00 43.26 ATOM 864 CB PRO B 6 -9.066 83.745 -44.672 1.00 44.87 ATOM 865 CG PRO B 6 -8.463 85.182 -44.538 1.00 45.39 ATOM 866 CD PRO B 6 -9.042 85.878 -45.734 1.00 45.51 ATOM 867 N MET B 7 -11.766 82.859 -43.482 1.00 43.29 ATOM 868 CA MET B 7 -12.558 82.791 -42.235 1.00 43.42 ATOM 869 C MET B 7 -11.817 82.205 -41.022 1.00 41.64 ATOM 870 O MET B 7 -11.003 81.338 -41.176 1.00 41.74 ATOM 871 CB MET B 7 -13.867 82.057 -42.472 1.00 43.12 ATOM 872 CG MET B 7 -14.881 82.876 -43.309 1.00 44.63 ATOM 873 SD MET B 7 -16.391 82.001 -43.780 1.00 46.00 ATOM 874 CE MET B 7 -16.086 81.536 -45.474 1.00 45.38 ATOM 875 N PRO B 8 -12.075 82.739 -39.824 1.00 40.58 ATOM 876 CA PRO B 8 -11.602 82.269 -38.537 1.00 39.41 ATOM 877 C PRO B 8 -11.354 80.759 -38.486 1.00 39.14 ATOM 878 O PRO B 8 -10.205 80.297 -38.461 1.00 35.97 ATOM 879 CB PRO B 8 -12.769 82.608 -37.614 1.00 40.15 ATOM 880 CG PRO B 8 -13.805 83.511 -38.512 1.00 41.93 ATOM 881 CD PRO B 8 -12.897 83.954 -39.673 1.00 40.17 ATOM 882 N ASP B 9 -12.459 80.012 -38.473 1.00 37.97 ATOM 883 CA ASP B 9 -12.404 78.567 -38.416 1.00 37.87 ATOM 884 C ASP B 9 -12.072 78.072 -39.838 1.00 35.74 ATOM 885 O ASP B 9 -12.058 76.906 -40.113 1.00 36.24 ATOM 886 CB ASP B 9 -13.761 78.077 -37.934 1.00 37.93 ATOM 887 CG ASP B 9 -14.883 78.722 -38.711 1.00 41.67 ATOM 888 OD1 ASP B 9 -15.393 79.807 -38.263 1.00 38.95 ATOM 889 OD2 ASP B 9 -15.217 78.135 -39.790 1.00 43.48 ATOM 890 N ASP B 10 -11.808 78.983 -40.757 1.00 34.01 ATOM 891 CA ASP B 10 -11.432 78.587 -42.104 1.00 31.00 ATOM 892 C ASP B 10 -9.941 78.590 -42.281 1.00 28.13 ATOM 893 O ASP B 10 -9.442 78.366 -43.405 1.00 27.56 ATOM 894 CB ASP B 10 -12.089 79.467 -43.162 1.00 31.03 ATOM 895 CG ASP B 10 -13.537 79.031 -43.497 1.00 34.41 ATOM 896 OD1 ASP B 10 -14.481 79.227 -42.651 1.00 34.30 ATOM 897 OD2 ASP B 10 -13.741 78.495 -44.632 1.00 35.04 ATOM 898 N LEU B 11 -9.251 78.865 -41.178 1.00 25.86 ATOM 899 CA LEU B 11 -7.741 78.964 -41.092 1.00 23.56 ATOM 900 C LEU B 11 -7.166 77.868 -40.181 1.00 23.57 ATOM 901 O LEU B 11 -7.882 77.367 -39.268 1.00 26.01 ATOM 902 CB LEU B 11 -7.290 80.355 -40.609 1.00 20.63 ATOM 903 CG LEU B 11 -7.653 81.528 -41.534 1.00 18.00 ATOM 904 CD1 LEU B 11 -7.544 82.846 -40.865 1.00 12.99 ATOM 905 CD2 LEU B 11 -6.781 81.594 -42.784 1.00 13.84 ATOM 906 N HIS B 12 -5.936 77.438 -40.442 1.00 21.48 ATOM 907 CA HIS B 12 -5.348 76.332 -39.727 1.00 20.33 ATOM 908 C HIS B 12 -4.675 76.904 -38.512 1.00 21.48 ATOM 909 O HIS B 12 -4.085 78.055 -38.515 1.00 25.05 ATOM 910 CB HIS B 12 -4.281 75.644 -40.576 1.00 20.41 ATOM 911 CG HIS B 12 -4.804 74.672 -41.605 1.00 17.84 ATOM 912 ND1 HIS B 12 -3.961 73.932 -42.413 1.00 16.88 ATOM 913 CD2 HIS B 12 -6.056 74.271 -41.914 1.00 14.19 ATOM 914 CE1 HIS B 12 -4.680 73.127 -43.182 1.00 19.53 ATOM 915 NE2 HIS B 12 -5.958 73.341 -42.930 1.00 11.77 ATOM 916 N LYS B 13 -4.684 76.094 -37.478 1.00 19.87 ATOM 917 CA LYS B 13 -4.274 76.539 -36.217 1.00 15.64 ATOM 918 C LYS B 13 -3.105 75.722 -35.836 1.00 14.91 ATOM 919 O LYS B 13 -3.162 74.456 -35.690 1.00 12.68 ATOM 920 CB LYS B 13 -5.357 76.258 -35.218 1.00 16.55 ATOM 921 CG LYS B 13 -6.629 77.068 -35.451 1.00 18.23 ATOM 922 CD LYS B 13 -7.676 76.703 -34.429 1.00 17.83 ATOM 923 CE LYS B 13 -9.096 77.253 -34.794 1.00 17.38 ATOM 924 NZ LYS B 13 -9.703 76.685 -36.027 1.00 19.74 ATOM 925 N SER B 14 -2.080 76.493 -35.533 1.00 9.93 ATOM 926 CA SER B 14 -0.873 76.010 -34.961 1.00 7.98 ATOM 927 C SER B 14 -1.060 75.122 -33.772 1.00 8.16 ATOM 928 O SER B 14 -0.506 74.034 -33.780 1.00 7.79 ATOM 929 CB SER B 14 -0.015 77.203 -34.554 1.00 7.92 ATOM 930 OG SER B 14 1.229 76.758 -34.063 1.00 11.22 ATOM 931 N SER B 15 -1.772 75.606 -32.717 1.00 9.50 ATOM 932 CA SER B 15 -2.182 74.794 -31.569 1.00 8.75 ATOM 933 C SER B 15 -2.690 73.367 -31.957 1.00 7.50 ATOM 934 O SER B 15 -2.784 72.491 -31.119 1.00 2.00 ATOM 935 CB SER B 15 -3.361 75.457 -30.840 1.00 10.06 ATOM 936 OG SER B 15 -4.501 75.523 -31.686 1.00 11.48 ATOM 937 N GLU B 16 -3.118 73.202 -33.202 1.00 8.28 ATOM 938 CA GLU B 16 -3.663 71.873 -33.584 1.00 8.32 ATOM 939 C GLU B 16 -2.693 70.973 -34.283 1.00 7.34 ATOM 940 O GLU B 16 -3.077 69.906 -34.819 1.00 9.72 ATOM 941 CB GLU B 16 -4.940 71.972 -34.384 1.00 6.90 ATOM 942 CG GLU B 16 -6.110 72.774 -33.611 1.00 13.03 ATOM 943 CD GLU B 16 -7.082 73.426 -34.592 1.00 15.44 ATOM 944 OE1 GLU B 16 -8.246 73.802 -34.204 1.00 14.49 ATOM 945 OE2 GLU B 16 -6.693 73.489 -35.802 1.00 15.33 ATOM 946 N PHE B 17 -1.447 71.346 -34.309 1.00 5.54 ATOM 947 CA PHE B 17 -0.477 70.537 -35.005 1.00 8.01 ATOM 948 C PHE B 17 0.634 70.002 -34.046 1.00 8.60 ATOM 949 O PHE B 17 1.639 70.697 -33.698 1.00 10.83 ATOM 950 CB PHE B 17 0.093 71.335 -36.173 1.00 9.38 ATOM 951 CG PHE B 17 1.388 70.796 -36.738 1.00 8.94 ATOM 952 CD1 PHE B 17 1.406 69.702 -37.581 1.00 8.04 ATOM 953 CD2 PHE B 17 2.592 71.437 -36.481 1.00 13.11 ATOM 954 CE1 PHE B 17 2.597 69.272 -38.139 1.00 3.89 ATOM 955 CE2 PHE B 17 3.797 70.956 -37.026 1.00 4.66 ATOM 956 CZ PHE B 17 3.789 69.927 -37.838 1.00 6.54 ATOM 957 N THR B 18 0.463 68.752 -33.636 1.00 5.37 ATOM 958 CA THR B 18 1.315 68.198 -32.667 1.00 5.33 ATOM 959 C THR B 18 2.629 67.818 -33.297 1.00 4.69 ATOM 960 O THR B 18 3.511 67.445 -32.597 1.00 4.77 ATOM 961 CB THR B 18 0.720 66.955 -32.010 1.00 6.54 ATOM 962 OG1 THR B 18 1.465 65.775 -32.431 1.00 3.09 ATOM 963 CG2 THR B 18 -0.787 66.747 -32.453 1.00 6.57 ATOM 964 N GLY B 19 2.715 68.028 -34.598 1.00 5.78 ATOM 965 CA GLY B 19 3.820 67.641 -35.507 1.00 6.84 ATOM 966 C GLY B 19 5.073 68.363 -35.118 1.00 8.48 ATOM 967 O GLY B 19 5.154 68.776 -33.959 1.00 10.21 ATOM 968 N THR B 20 6.004 68.575 -36.076 1.00 8.52 ATOM 969 CA THR B 20 7.187 69.354 -35.838 1.00 6.10 ATOM 970 C THR B 20 7.286 70.595 -36.787 1.00 4.47 ATOM 971 O THR B 20 7.777 70.493 -37.870 1.00 7.92 ATOM 972 CB THR B 20 8.422 68.486 -36.181 1.00 7.30 ATOM 973 OG1 THR B 20 8.455 67.268 -35.411 1.00 4.45 ATOM 974 CG2 THR B 20 9.736 69.308 -35.881 1.00 5.58 ATOM 975 N MET B 21 6.923 71.806 -36.425 1.00 7.84 ATOM 976 CA MET B 21 6.991 72.951 -37.374 1.00 6.25 ATOM 977 C MET B 21 8.347 73.215 -38.035 1.00 6.67 ATOM 978 O MET B 21 8.460 74.145 -38.823 1.00 9.47 ATOM 979 CB MET B 21 6.533 74.221 -36.666 1.00 9.03 ATOM 980 CG MET B 21 6.240 75.448 -37.531 1.00 2.99 ATOM 981 SD MET B 21 4.679 75.068 -38.286 1.00 12.32 ATOM 982 CE MET B 21 3.576 75.454 -36.948 1.00 2.00 ATOM 983 N GLY B 22 9.354 72.348 -37.848 1.00 5.67 ATOM 984 CA GLY B 22 10.657 72.569 -38.394 1.00 5.46 ATOM 985 C GLY B 22 10.691 72.137 -39.819 1.00 5.45 ATOM 986 O GLY B 22 11.374 72.766 -40.666 1.00 4.30 ATOM 987 N ASN B 23 9.894 71.108 -40.152 1.00 4.03 ATOM 988 CA ASN B 23 9.755 70.722 -41.544 1.00 2.32 ATOM 989 C ASN B 23 9.094 71.790 -42.450 1.00 3.97 ATOM 990 O ASN B 23 9.135 71.699 -43.717 1.00 4.25 ATOM 991 CB ASN B 23 8.988 69.480 -41.632 1.00 3.48 ATOM 992 CG ASN B 23 9.503 68.445 -40.683 1.00 4.51 ATOM 993 OD1 ASN B 23 8.951 67.398 -40.603 1.00 2.00 ATOM 994 ND2 ASN B 23 10.684 68.724 -40.048 1.00 8.89 ATOM 995 N MET B 24 8.413 72.746 -41.824 1.00 4.15 ATOM 996 CA MET B 24 7.869 73.871 -42.604 1.00 6.07 ATOM 997 C MET B 24 8.935 74.946 -42.606 1.00 8.10 ATOM 998 O MET B 24 9.056 75.652 -43.569 1.00 11.97 ATOM 999 CB MET B 24 6.585 74.375 -41.946 1.00 5.93 ATOM 1000 CG MET B 24 6.282 75.875 -42.155 1.00 6.16 ATOM 1001 SD MET B 24 5.399 76.020 -43.732 1.00 11.88 ATOM 1002 CE MET B 24 4.033 74.884 -43.653 1.00 12.63 ATOM 1003 N LYS B 25 9.591 75.196 -41.477 1.00 9.51 ATOM 1004 CA LYS B 25 10.632 76.225 -41.474 1.00 12.64 ATOM 1005 C LYS B 25 11.555 75.823 -42.623 1.00 12.16 ATOM 1006 O LYS B 25 11.972 76.666 -43.399 1.00 10.17 ATOM 1007 CB LYS B 25 11.449 76.210 -40.172 1.00 11.58 ATOM 1008 CG LYS B 25 12.314 77.417 -39.928 1.00 13.23 ATOM 1009 CD LYS B 25 13.033 77.369 -38.536 1.00 12.03 ATOM 1010 CE LYS B 25 14.389 78.062 -38.522 1.00 11.09 ATOM 1011 NZ LYS B 25 14.975 78.650 -37.246 1.00 9.14 ATOM 1012 N TYR B 26 11.729 74.508 -42.790 1.00 12.78 ATOM 1013 CA TYR B 26 12.779 73.942 -43.671 1.00 13.08 ATOM 1014 C TYR B 26 12.727 74.501 -45.052 1.00 14.82 ATOM 1015 O TYR B 26 13.768 74.870 -45.606 1.00 16.26 ATOM 1016 CB TYR B 26 12.662 72.412 -43.825 1.00 15.17 ATOM 1017 CG TYR B 26 13.626 71.883 -44.844 1.00 16.72 ATOM 1018 CD1 TYR B 26 14.993 72.051 -44.706 1.00 16.69 ATOM 1019 CD2 TYR B 26 13.154 71.284 -45.989 1.00 22.97 ATOM 1020 CE1 TYR B 26 15.922 71.599 -45.696 1.00 17.03 ATOM 1021 CE2 TYR B 26 14.042 70.807 -46.984 1.00 21.75 ATOM 1022 CZ TYR B 26 15.423 71.017 -46.822 1.00 20.28 ATOM 1023 OH TYR B 26 16.212 70.601 -47.826 1.00 22.50 ATOM 1024 N LEU B 27 11.513 74.577 -45.606 1.00 15.13 ATOM 1025 CA LEU B 27 11.258 74.998 -46.969 1.00 11.75 ATOM 1026 C LEU B 27 11.462 76.511 -47.238 1.00 12.61 ATOM 1027 O LEU B 27 11.363 76.924 -48.416 1.00 13.55 ATOM 1028 CB LEU B 27 9.793 74.655 -47.240 1.00 11.96 ATOM 1029 CG LEU B 27 9.249 73.293 -46.797 1.00 10.71 ATOM 1030 CD1 LEU B 27 7.846 73.236 -47.184 1.00 8.09 ATOM 1031 CD2 LEU B 27 10.048 72.234 -47.482 1.00 10.20 ATOM 1032 N TYR B 28 11.605 77.351 -46.192 1.00 10.51 ATOM 1033 CA TYR B 28 11.910 78.786 -46.430 1.00 12.26 ATOM 1034 C TYR B 28 13.061 79.521 -45.738 1.00 9.88 ATOM 1035 O TYR B 28 13.247 80.680 -45.994 1.00 9.05 ATOM 1036 CB TYR B 28 10.688 79.632 -46.251 1.00 12.47 ATOM 1037 CG TYR B 28 9.486 79.043 -46.815 1.00 16.52 ATOM 1038 CD1 TYR B 28 9.009 77.837 -46.342 1.00 17.14 ATOM 1039 CD2 TYR B 28 8.708 79.739 -47.700 1.00 17.99 ATOM 1040 CE1 TYR B 28 7.896 77.325 -46.807 1.00 19.39 ATOM 1041 CE2 TYR B 28 7.536 79.196 -48.149 1.00 18.75 ATOM 1042 CZ TYR B 28 7.138 78.013 -47.697 1.00 14.71 ATOM 1043 OH TYR B 28 5.988 77.435 -48.151 1.00 18.96 ATOM 1044 N ASP B 29 13.834 78.889 -44.865 1.00 11.42 ATOM 1045 CA ASP B 29 15.039 79.582 -44.329 1.00 12.07 ATOM 1046 C ASP B 29 16.120 79.506 -45.382 1.00 12.70 ATOM 1047 O ASP B 29 16.874 78.462 -45.477 1.00 13.45 ATOM 1048 CB ASP B 29 15.478 79.013 -42.972 1.00 12.05 ATOM 1049 CG ASP B 29 16.523 79.893 -42.233 1.00 20.40 ATOM 1050 OD1 ASP B 29 16.977 79.436 -41.118 1.00 25.56 ATOM 1051 OD2 ASP B 29 16.891 81.035 -42.722 1.00 21.98 ATOM 1052 N ASP B 30 16.145 80.510 -46.279 1.00 10.97 ATOM 1053 CA ASP B 30 17.227 80.571 -47.304 1.00 12.51 ATOM 1054 C ASP B 30 17.311 79.226 -48.096 1.00 13.06 ATOM 1055 O ASP B 30 18.435 78.724 -48.297 1.00 12.50 ATOM 1056 CB ASP B 30 18.607 80.840 -46.658 1.00 12.06 ATOM 1057 CG ASP B 30 19.697 81.234 -47.696 1.00 17.11 ATOM 1058 OD1 ASP B 30 19.489 82.195 -48.463 1.00 15.72 ATOM 1059 OD2 ASP B 30 20.774 80.600 -47.724 1.00 14.13 ATOM 1060 N HIS B 31 16.132 78.730 -48.546 1.00 9.50 ATOM 1061 CA HIS B 31 15.966 77.483 -49.319 1.00 11.12 ATOM 1062 C HIS B 31 15.071 77.866 -50.454 1.00 11.29 ATOM 1063 O HIS B 31 13.974 78.366 -50.185 1.00 16.56 ATOM 1064 CB HIS B 31 15.131 76.527 -48.447 1.00 9.99 ATOM 1065 CG HIS B 31 14.696 75.288 -49.095 1.00 7.73 ATOM 1066 ND1 HIS B 31 15.545 74.224 -49.295 1.00 2.00 ATOM 1067 CD2 HIS B 31 13.465 74.898 -49.547 1.00 14.99 ATOM 1068 CE1 HIS B 31 14.855 73.229 -49.825 1.00 11.39 ATOM 1069 NE2 HIS B 31 13.587 73.591 -49.959 1.00 5.47 ATOM 1070 N TYR B 32 15.557 77.760 -51.681 1.00 11.92 ATOM 1071 CA TYR B 32 14.771 77.896 -52.927 1.00 12.20 ATOM 1072 C TYR B 32 15.646 77.342 -54.070 1.00 12.61 ATOM 1073 O TYR B 32 16.857 77.145 -53.874 1.00 10.79 ATOM 1074 CB TYR B 32 14.534 79.343 -53.236 1.00 12.35 ATOM 1075 CG TYR B 32 15.805 80.063 -53.151 1.00 12.45 ATOM 1076 CD1 TYR B 32 16.803 79.780 -54.022 1.00 7.96 ATOM 1077 CD2 TYR B 32 16.029 81.005 -52.146 1.00 10.10 ATOM 1078 CE1 TYR B 32 18.015 80.430 -53.913 1.00 11.27 ATOM 1079 CE2 TYR B 32 17.196 81.659 -52.046 1.00 11.49 ATOM 1080 CZ TYR B 32 18.206 81.364 -52.904 1.00 13.57 ATOM 1081 OH TYR B 32 19.445 81.985 -52.705 1.00 15.12 ATOM 1082 N VAL B 33 15.053 77.207 -55.268 1.00 9.92 ATOM 1083 CA VAL B 33 15.792 76.815 -56.413 1.00 7.41 ATOM 1084 C VAL B 33 15.738 77.982 -57.313 1.00 9.49 ATOM 1085 O VAL B 33 14.617 78.528 -57.530 1.00 7.51 ATOM 1086 CB VAL B 33 15.069 75.631 -57.030 1.00 7.08 ATOM 1087 CG1 VAL B 33 15.556 75.285 -58.414 1.00 2.45 ATOM 1088 CG2 VAL B 33 15.150 74.529 -56.135 1.00 5.59 ATOM 1089 N SER B 34 16.898 78.390 -57.879 1.00 8.50 ATOM 1090 CA SER B 34 16.866 79.564 -58.721 1.00 9.28 ATOM 1091 C SER B 34 17.727 79.393 -59.896 1.00 10.37 ATOM 1092 O SER B 34 18.939 79.451 -59.788 1.00 14.13 ATOM 1093 CB SER B 34 17.181 80.861 -58.005 1.00 10.40 ATOM 1094 OG SER B 34 16.973 81.971 -58.909 1.00 9.49 ATOM 1095 N ALA B 35 17.098 79.261 -61.062 1.00 11.32 ATOM 1096 CA ALA B 35 17.828 79.044 -62.324 1.00 9.78 ATOM 1097 C ALA B 35 17.370 80.112 -63.260 1.00 8.82 ATOM 1098 O ALA B 35 16.275 80.511 -63.151 1.00 6.77 ATOM 1099 CB ALA B 35 17.474 77.737 -62.932 1.00 9.96 ATOM 1100 N THR B 36 18.220 80.489 -64.208 1.00 10.12 ATOM 1101 CA THR B 36 18.011 81.657 -65.118 1.00 11.05 ATOM 1102 C THR B 36 18.294 81.320 -66.544 1.00 12.61 ATOM 1103 O THR B 36 19.354 80.861 -66.853 1.00 10.92 ATOM 1104 CB THR B 36 18.942 82.743 -64.777 1.00 11.66 ATOM 1105 OG1 THR B 36 18.747 82.955 -63.382 1.00 15.75 ATOM 1106 CG2 THR B 36 18.594 84.074 -65.630 1.00 11.27 ATOM 1107 N LYS B 37 17.296 81.531 -67.430 1.00 14.89 ATOM 1108 CA LYS B 37 17.543 81.310 -68.814 1.00 13.99 ATOM 1109 C LYS B 37 17.984 79.844 -68.958 1.00 14.22 ATOM 1110 O LYS B 37 19.196 79.574 -69.047 1.00 11.92 ATOM 1111 CB LYS B 37 18.653 82.324 -69.197 1.00 14.69 ATOM 1112 CG LYS B 37 19.098 82.350 -70.666 1.00 14.92 ATOM 1113 CD LYS B 37 20.481 83.023 -70.818 1.00 15.90 ATOM 1114 CE LYS B 37 21.493 82.531 -69.826 1.00 18.89 ATOM 1115 NZ LYS B 37 22.701 83.497 -70.086 1.00 25.94 ATOM 1116 N VAL B 38 17.018 78.889 -68.941 1.00 14.33 ATOM 1117 CA VAL B 38 17.333 77.460 -69.217 1.00 8.47 ATOM 1118 C VAL B 38 16.156 76.741 -69.917 1.00 11.64 ATOM 1119 O VAL B 38 15.036 77.291 -70.018 1.00 11.70 ATOM 1120 CB VAL B 38 17.549 76.692 -67.969 1.00 9.41 ATOM 1121 CG1 VAL B 38 18.761 77.135 -67.216 1.00 5.49 ATOM 1122 CG2 VAL B 38 16.192 76.623 -66.976 1.00 3.34 ATOM 1123 N LYS B 39 16.348 75.481 -70.341 1.00 8.26 ATOM 1124 CA LYS B 39 15.260 74.869 -70.996 1.00 7.03 ATOM 1125 C LYS B 39 15.158 73.459 -70.546 1.00 7.23 ATOM 1126 O LYS B 39 16.188 72.769 -70.251 1.00 4.87 ATOM 1127 CB LYS B 39 15.431 74.849 -72.513 1.00 8.92 ATOM 1128 CG LYS B 39 14.042 74.528 -73.349 1.00 8.95 ATOM 1129 CD LYS B 39 14.417 74.176 -74.848 1.00 5.73 ATOM 1130 CE LYS B 39 15.312 75.405 -75.341 1.00 11.99 ATOM 1131 NZ LYS B 39 15.446 75.446 -76.803 1.00 16.06 ATOM 1132 N SER B 40 13.887 73.080 -70.432 1.00 4.91 ATOM 1133 CA SER B 40 13.521 71.755 -69.977 1.00 6.31 ATOM 1134 C SER B 40 14.456 70.798 -70.680 1.00 4.19 ATOM 1135 O SER B 40 14.844 71.105 -71.730 1.00 7.46 ATOM 1136 CB SER B 40 12.115 71.366 -70.441 1.00 3.16 ATOM 1137 OG SER B 40 12.137 69.930 -70.572 1.00 4.42 ATOM 1138 N VAL B 41 14.734 69.669 -70.124 1.00 4.68 ATOM 1139 CA VAL B 41 15.584 68.637 -70.775 1.00 5.16 ATOM 1140 C VAL B 41 15.081 67.212 -70.608 1.00 6.17 ATOM 1141 O VAL B 41 15.809 66.230 -70.835 1.00 8.77 ATOM 1142 CB VAL B 41 16.973 68.667 -70.217 1.00 3.62 ATOM 1143 CG1 VAL B 41 17.543 70.203 -70.141 1.00 2.00 ATOM 1144 CG2 VAL B 41 16.981 68.059 -68.909 1.00 2.37 ATOM 1145 N ASP B 42 13.868 67.049 -70.145 1.00 7.39 ATOM 1146 CA ASP B 42 13.306 65.666 -70.092 1.00 9.19 ATOM 1147 C ASP B 42 11.941 65.741 -69.522 1.00 8.29 ATOM 1148 O ASP B 42 11.325 66.848 -69.425 1.00 9.02 ATOM 1149 CB ASP B 42 14.161 64.741 -69.201 1.00 8.49 ATOM 1150 CG ASP B 42 13.714 63.283 -69.281 1.00 12.22 ATOM 1151 OD1 ASP B 42 14.480 62.410 -68.854 1.00 9.11 ATOM 1152 OD2 ASP B 42 12.595 62.983 -69.819 1.00 14.09 ATOM 1153 N LYS B 43 11.473 64.586 -69.038 1.00 8.95 ATOM 1154 CA LYS B 43 10.139 64.519 -68.495 1.00 7.59 ATOM 1155 C LYS B 43 9.684 63.146 -68.063 1.00 10.74 ATOM 1156 O LYS B 43 10.015 62.135 -68.714 1.00 10.33 ATOM 1157 CB LYS B 43 9.253 65.059 -69.569 1.00 5.57 ATOM 1158 CG LYS B 43 7.828 64.484 -69.586 1.00 10.36 ATOM 1159 CD LYS B 43 6.985 64.859 -70.881 1.00 3.92 ATOM 1160 CE LYS B 43 6.779 66.394 -71.226 1.00 11.54 ATOM 1161 NZ LYS B 43 5.771 67.268 -70.464 1.00 12.95 ATOM 1162 N PHE B 44 8.899 63.089 -66.973 1.00 13.77 ATOM 1163 CA PHE B 44 8.231 61.846 -66.431 1.00 13.20 ATOM 1164 C PHE B 44 6.713 61.771 -66.767 1.00 13.65 ATOM 1165 O PHE B 44 6.333 61.164 -67.764 1.00 14.30 ATOM 1166 CB PHE B 44 8.265 61.820 -64.913 1.00 15.36 ATOM 1167 CG PHE B 44 7.633 60.568 -64.303 1.00 18.19 ATOM 1168 CD1 PHE B 44 7.180 60.562 -63.004 1.00 25.22 ATOM 1169 CD2 PHE B 44 7.398 59.431 -65.070 1.00 23.88 ATOM 1170 CE1 PHE B 44 6.605 59.390 -62.409 1.00 26.02 ATOM 1171 CE2 PHE B 44 6.800 58.257 -64.475 1.00 24.48 ATOM 1172 CZ PHE B 44 6.431 58.275 -63.141 1.00 25.14 ATOM 1173 N LEU B 45 5.846 62.308 -65.937 1.00 10.95 ATOM 1174 CA LEU B 45 4.420 62.211 -66.290 1.00 13.95 ATOM 1175 C LEU B 45 4.007 63.403 -67.129 1.00 13.43 ATOM 1176 O LEU B 45 4.714 64.387 -67.080 1.00 13.44 ATOM 1177 CB LEU B 45 3.533 62.034 -65.052 1.00 12.98 ATOM 1178 CG LEU B 45 3.491 60.557 -64.573 1.00 17.93 ATOM 1179 CD1 LEU B 45 2.605 60.444 -63.348 1.00 15.62 ATOM 1180 CD2 LEU B 45 2.989 59.653 -65.701 1.00 18.26 ATOM 1181 N ALA B 46 2.807 63.332 -67.766 1.00 15.53 ATOM 1182 CA ALA B 46 2.294 64.222 -68.816 1.00 13.36 ATOM 1183 C ALA B 46 2.261 65.697 -68.384 1.00 14.37 ATOM 1184 O ALA B 46 1.548 66.560 -68.990 1.00 16.33 ATOM 1185 CB ALA B 46 0.974 63.805 -69.171 1.00 15.72 ATOM 1186 N HIS B 47 2.986 65.981 -67.335 1.00 11.62 ATOM 1187 CA HIS B 47 2.946 67.269 -66.763 1.00 12.15 ATOM 1188 C HIS B 47 4.089 67.604 -65.841 1.00 12.13 ATOM 1189 O HIS B 47 3.843 68.485 -65.023 1.00 16.78 ATOM 1190 CB HIS B 47 1.627 67.475 -65.997 1.00 11.30 ATOM 1191 CG HIS B 47 1.524 66.644 -64.769 1.00 8.04 ATOM 1192 ND1 HIS B 47 1.415 65.265 -64.818 1.00 11.28 ATOM 1193 CD2 HIS B 47 1.572 66.966 -63.462 1.00 9.91 ATOM 1194 CE1 HIS B 47 1.331 64.779 -63.591 1.00 12.14 ATOM 1195 NE2 HIS B 47 1.447 65.780 -62.744 1.00 11.10 ATOM 1196 N ASP B 48 5.329 67.095 -66.039 1.00 10.44 ATOM 1197 CA ASP B 48 6.482 67.608 -65.281 1.00 10.07 ATOM 1198 C ASP B 48 7.732 67.723 -66.130 1.00 11.73 ATOM 1199 O ASP B 48 8.044 66.806 -66.774 1.00 12.14 ATOM 1200 CB ASP B 48 6.804 66.628 -64.196 1.00 10.01 ATOM 1201 CG ASP B 48 7.151 65.308 -64.774 1.00 12.06 ATOM 1202 OD1 ASP B 48 6.255 64.716 -65.450 1.00 16.00 ATOM 1203 OD2 ASP B 48 8.334 64.933 -64.674 1.00 10.05 ATOM 1204 N LEU B 49 8.419 68.874 -66.147 1.00 14.01 ATOM 1205 CA LEU B 49 9.622 69.109 -66.936 1.00 11.39 ATOM 1206 C LEU B 49 10.864 69.134 -66.050 1.00 10.43 ATOM 1207 O LEU B 49 10.920 69.975 -65.207 1.00 8.63 ATOM 1208 CB LEU B 49 9.471 70.402 -67.733 1.00 14.66 ATOM 1209 CG LEU B 49 7.996 70.851 -67.931 1.00 11.19 ATOM 1210 CD1 LEU B 49 8.099 72.163 -68.333 1.00 10.92 ATOM 1211 CD2 LEU B 49 7.245 70.080 -68.995 1.00 11.02 ATOM 1212 N ILE B 50 11.770 68.146 -66.209 1.00 8.25 ATOM 1213 CA ILE B 50 13.045 68.051 -65.544 1.00 9.33 ATOM 1214 C ILE B 50 14.068 69.010 -66.171 1.00 10.09 ATOM 1215 O ILE B 50 14.155 69.097 -67.364 1.00 11.32 ATOM 1216 CB ILE B 50 13.693 66.661 -65.734 1.00 10.94 ATOM 1217 CG1 ILE B 50 12.772 65.492 -65.444 1.00 7.35 ATOM 1218 CG2 ILE B 50 15.055 66.522 -64.894 1.00 15.10 ATOM 1219 CD1 ILE B 50 12.196 65.557 -64.237 1.00 19.03 ATOM 1220 N TYR B 51 14.861 69.697 -65.394 1.00 10.16 ATOM 1221 CA TYR B 51 15.858 70.595 -65.925 1.00 10.62 ATOM 1222 C TYR B 51 17.190 70.100 -65.383 1.00 13.67 ATOM 1223 O TYR B 51 17.173 69.256 -64.457 1.00 13.15 ATOM 1224 CB TYR B 51 15.580 71.985 -65.381 1.00 9.74 ATOM 1225 CG TYR B 51 14.372 72.680 -66.007 1.00 4.41 ATOM 1226 CD1 TYR B 51 13.066 72.166 -65.865 1.00 9.42 ATOM 1227 CD2 TYR B 51 14.534 73.789 -66.752 1.00 2.00 ATOM 1228 CE1 TYR B 51 11.920 72.867 -66.435 1.00 3.76 ATOM 1229 CE2 TYR B 51 13.431 74.465 -67.376 1.00 3.37 ATOM 1230 CZ TYR B 51 12.132 73.991 -67.193 1.00 2.47 ATOM 1231 OH TYR B 51 11.103 74.610 -67.833 1.00 2.40 ATOM 1232 N ASN B 52 18.309 70.669 -65.826 1.00 11.97 ATOM 1233 CA ASN B 52 19.512 70.170 -65.302 1.00 16.18 ATOM 1234 C ASN B 52 20.011 71.357 -64.563 1.00 18.09 ATOM 1235 O ASN B 52 20.932 72.001 -65.058 1.00 16.56 ATOM 1236 CB ASN B 52 20.539 69.722 -66.381 1.00 14.82 ATOM 1237 CG ASN B 52 20.068 68.591 -67.201 1.00 18.24 ATOM 1238 OD1 ASN B 52 19.771 67.528 -66.662 1.00 22.02 ATOM 1239 ND2 ASN B 52 19.954 68.790 -68.538 1.00 15.48 ATOM 1240 N ILE B 53 19.397 71.620 -63.404 1.00 19.01 ATOM 1241 CA ILE B 53 19.784 72.713 -62.507 1.00 18.95 ATOM 1242 C ILE B 53 20.574 72.138 -61.328 1.00 19.83 ATOM 1243 O ILE B 53 20.063 71.356 -60.587 1.00 18.44 ATOM 1244 CB ILE B 53 18.514 73.413 -61.941 1.00 18.10 ATOM 1245 CG1 ILE B 53 17.650 74.111 -63.022 1.00 20.40 ATOM 1246 CG2 ILE B 53 18.850 74.429 -60.893 1.00 15.21 ATOM 1247 CD1 ILE B 53 18.495 74.743 -64.053 1.00 28.21 ATOM 1248 N SER B 54 21.773 72.639 -61.067 1.00 20.41 ATOM 1249 CA SER B 54 22.556 72.066 -59.997 1.00 19.93 ATOM 1250 C SER B 54 22.663 72.786 -58.690 1.00 21.74 ATOM 1251 O SER B 54 23.084 73.939 -58.644 1.00 22.49 ATOM 1252 CB SER B 54 24.016 71.951 -60.412 1.00 19.12 ATOM 1253 OG SER B 54 24.117 71.236 -61.577 1.00 19.90 ATOM 1254 N ASP B 55 22.484 72.032 -57.619 1.00 24.40 ATOM 1255 CA ASP B 55 22.631 72.525 -56.276 1.00 27.39 ATOM 1256 C ASP B 55 23.850 73.400 -56.170 1.00 28.79 ATOM 1257 O ASP B 55 24.937 72.900 -56.246 1.00 29.60 ATOM 1258 CB ASP B 55 22.775 71.310 -55.333 1.00 28.70 ATOM 1259 CG ASP B 55 22.622 71.670 -53.853 1.00 28.72 ATOM 1260 OD1 ASP B 55 22.728 70.776 -52.983 1.00 21.42 ATOM 1261 OD2 ASP B 55 22.423 72.871 -53.570 1.00 29.02 ATOM 1262 N LYS B 56 23.689 74.715 -55.947 1.00 30.83 ATOM 1263 CA LYS B 56 24.874 75.548 -55.684 1.00 30.73 ATOM 1264 C LYS B 56 25.373 75.552 -54.230 1.00 30.90 ATOM 1265 O LYS B 56 26.582 75.461 -53.950 1.00 32.61 ATOM 1266 CB LYS B 56 24.687 76.960 -56.247 1.00 31.60 ATOM 1267 CG LYS B 56 25.160 77.072 -57.720 1.00 32.82 ATOM 1268 CD LYS B 56 26.585 76.462 -57.886 1.00 37.24 ATOM 1269 CE LYS B 56 26.706 75.575 -59.119 1.00 35.70 ATOM 1270 NZ LYS B 56 26.428 76.315 -60.371 1.00 35.95 ATOM 1271 N LYS B 57 24.428 75.645 -53.310 1.00 31.60 ATOM 1272 CA LYS B 57 24.639 75.634 -51.870 1.00 31.24 ATOM 1273 C LYS B 57 25.322 74.360 -51.418 1.00 30.68 ATOM 1274 O LYS B 57 26.396 74.421 -50.916 1.00 28.36 ATOM 1275 CB LYS B 57 23.295 75.785 -51.152 1.00 31.97 ATOM 1276 CG LYS B 57 22.915 77.245 -50.724 1.00 33.43 ATOM 1277 CD LYS B 57 22.763 78.189 -51.967 1.00 38.46 ATOM 1278 CE LYS B 57 21.830 79.384 -51.702 1.00 38.33 ATOM 1279 NZ LYS B 57 20.614 78.991 -50.937 1.00 33.85 ATOM 1280 N LEU B 58 24.698 73.204 -51.613 1.00 31.37 ATOM 1281 CA LEU B 58 25.336 71.948 -51.168 1.00 31.93 ATOM 1282 C LEU B 58 25.752 71.059 -52.354 1.00 31.95 ATOM 1283 O LEU B 58 26.643 71.387 -53.145 1.00 32.26 ATOM 1284 CB LEU B 58 24.392 71.172 -50.259 1.00 32.96 ATOM 1285 CG LEU B 58 23.395 71.988 -49.404 1.00 32.02 ATOM 1286 CD1 LEU B 58 22.251 71.121 -48.917 1.00 36.53 ATOM 1287 CD2 LEU B 58 24.084 72.609 -48.210 1.00 34.80 ATOM 1288 N LYS B 59 25.098 69.921 -52.485 1.00 31.56 ATOM 1289 CA LYS B 59 25.498 68.925 -53.512 1.00 30.11 ATOM 1290 C LYS B 59 24.412 67.847 -53.648 1.00 27.60 ATOM 1291 O LYS B 59 24.633 66.702 -54.165 1.00 25.06 ATOM 1292 CB LYS B 59 26.889 68.313 -53.230 1.00 30.42 ATOM 1293 CG LYS B 59 27.120 67.821 -51.786 1.00 33.62 ATOM 1294 CD LYS B 59 28.487 67.027 -51.655 1.00 32.10 ATOM 1295 CE LYS B 59 28.596 66.317 -50.318 1.00 35.13 ATOM 1296 NZ LYS B 59 29.742 65.287 -50.286 1.00 37.19 ATOM 1297 N ASN B 60 23.215 68.265 -53.235 1.00 25.43 ATOM 1298 CA ASN B 60 22.065 67.375 -53.182 1.00 25.07 ATOM 1299 C ASN B 60 21.634 66.986 -54.603 1.00 23.02 ATOM 1300 O ASN B 60 21.571 65.851 -54.845 1.00 23.53 ATOM 1301 CB ASN B 60 20.943 67.975 -52.301 1.00 24.37 ATOM 1302 CG ASN B 60 21.513 68.539 -51.004 1.00 29.91 ATOM 1303 OD1 ASN B 60 22.355 67.865 -50.312 1.00 22.22 ATOM 1304 ND2 ASN B 60 21.158 69.825 -50.702 1.00 26.60 ATOM 1305 N TYR B 61 21.386 67.925 -55.539 1.00 22.28 ATOM 1306 CA TYR B 61 20.766 67.595 -56.850 1.00 21.25 ATOM 1307 C TYR B 61 21.603 68.088 -57.992 1.00 19.95 ATOM 1308 O TYR B 61 22.388 68.957 -57.803 1.00 22.42 ATOM 1309 CB TYR B 61 19.317 68.143 -56.927 1.00 20.47 ATOM 1310 CG TYR B 61 19.231 69.645 -56.725 1.00 22.50 ATOM 1311 CD1 TYR B 61 19.603 70.503 -57.744 1.00 17.96 ATOM 1312 CD2 TYR B 61 18.819 70.185 -55.508 1.00 22.53 ATOM 1313 CE1 TYR B 61 19.552 71.866 -57.543 1.00 21.42 ATOM 1314 CE2 TYR B 61 18.791 71.524 -55.288 1.00 18.08 ATOM 1315 CZ TYR B 61 19.175 72.338 -56.311 1.00 18.98 ATOM 1316 OH TYR B 61 19.158 73.620 -56.151 1.00 23.27 ATOM 1317 N ASP B 62 21.453 67.527 -59.165 1.00 18.98 ATOM 1318 CA ASP B 62 21.948 68.124 -60.410 1.00 18.61 ATOM 1319 C ASP B 62 20.707 68.334 -61.325 1.00 17.80 ATOM 1320 O ASP B 62 20.795 68.945 -62.349 1.00 17.30 ATOM 1321 CB ASP B 62 22.852 67.123 -61.091 1.00 19.51 ATOM 1322 CG ASP B 62 22.099 65.851 -61.414 1.00 18.23 ATOM 1323 OD1 ASP B 62 22.010 64.964 -60.565 1.00 16.70 ATOM 1324 OD2 ASP B 62 21.558 65.780 -62.505 1.00 24.79 ATOM 1325 N LYS B 63 19.526 67.848 -60.930 1.00 18.24 ATOM 1326 CA LYS B 63 18.277 67.989 -61.726 1.00 17.27 ATOM 1327 C LYS B 63 17.025 68.255 -60.877 1.00 16.44 ATOM 1328 O LYS B 63 17.022 68.000 -59.702 1.00 16.35 ATOM 1329 CB LYS B 63 18.004 66.723 -62.471 1.00 17.43 ATOM 1330 CG LYS B 63 18.989 66.354 -63.557 1.00 18.56 ATOM 1331 CD LYS B 63 18.273 65.328 -64.583 1.00 19.04 ATOM 1332 CE LYS B 63 19.232 64.535 -65.499 1.00 22.68 ATOM 1333 NZ LYS B 63 20.351 63.925 -64.725 1.00 20.82 ATOM 1334 N VAL B 64 15.956 68.762 -61.466 1.00 14.94 ATOM 1335 CA VAL B 64 14.918 69.428 -60.687 1.00 13.39 ATOM 1336 C VAL B 64 13.690 69.204 -61.470 1.00 14.07 ATOM 1337 O VAL B 64 13.659 69.610 -62.662 1.00 13.58 ATOM 1338 CB VAL B 64 15.129 70.881 -60.563 1.00 13.23 ATOM 1339 CG1 VAL B 64 14.106 71.459 -59.685 1.00 13.27 ATOM 1340 CG2 VAL B 64 16.539 71.163 -59.937 1.00 14.70 ATOM 1341 N LYS B 65 12.758 68.457 -60.862 1.00 11.22 ATOM 1342 CA LYS B 65 11.479 68.023 -61.513 1.00 10.59 ATOM 1343 C LYS B 65 10.399 68.943 -61.018 1.00 9.34 ATOM 1344 O LYS B 65 10.124 68.893 -59.864 1.00 10.41 ATOM 1345 CB LYS B 65 11.075 66.669 -61.027 1.00 9.02 ATOM 1346 CG LYS B 65 9.850 66.003 -61.721 1.00 12.54 ATOM 1347 CD LYS B 65 9.549 64.629 -60.972 1.00 10.08 ATOM 1348 CE LYS B 65 8.240 64.021 -61.369 1.00 15.90 ATOM 1349 NZ LYS B 65 6.934 64.371 -60.782 1.00 11.30 ATOM 1350 N THR B 66 9.829 69.785 -61.846 1.00 5.88 ATOM 1351 CA THR B 66 8.816 70.634 -61.359 1.00 7.32 ATOM 1352 C THR B 66 7.519 70.173 -61.946 1.00 6.50 ATOM 1353 O THR B 66 7.553 69.747 -63.109 1.00 7.78 ATOM 1354 CB THR B 66 8.992 72.105 -61.878 1.00 7.09 ATOM 1355 OG1 THR B 66 7.855 72.831 -61.412 1.00 8.11 ATOM 1356 CG2 THR B 66 8.875 72.163 -63.350 1.00 2.38 ATOM 1357 N GLU B 67 6.431 70.214 -61.200 1.00 4.69 ATOM 1358 CA GLU B 67 5.170 69.577 -61.684 1.00 7.90 ATOM 1359 C GLU B 67 4.184 70.675 -61.809 1.00 7.23 ATOM 1360 O GLU B 67 4.206 71.534 -60.958 1.00 10.86 ATOM 1361 CB GLU B 67 4.580 68.526 -60.696 1.00 7.73 ATOM 1362 CG GLU B 67 5.458 67.338 -60.426 1.00 8.95 ATOM 1363 CD GLU B 67 4.690 66.177 -59.888 1.00 11.55 ATOM 1364 OE1 GLU B 67 4.324 66.244 -58.729 1.00 16.77 ATOM 1365 OE2 GLU B 67 4.470 65.142 -60.591 1.00 16.26 ATOM 1366 N LEU B 68 3.365 70.693 -62.850 1.00 8.84 ATOM 1367 CA LEU B 68 2.462 71.833 -63.143 1.00 9.86 ATOM 1368 C LEU B 68 1.027 71.385 -62.992 1.00 10.53 ATOM 1369 O LEU B 68 0.791 70.184 -62.825 1.00 10.30 ATOM 1370 CB LEU B 68 2.716 72.295 -64.551 1.00 9.24 ATOM 1371 CG LEU B 68 4.027 73.070 -64.676 1.00 7.01 ATOM 1372 CD1 LEU B 68 5.248 72.234 -64.901 1.00 17.00 ATOM 1373 CD2 LEU B 68 4.025 74.132 -65.788 1.00 14.31 ATOM 1374 N LEU B 69 0.099 72.328 -63.029 1.00 11.18 ATOM 1375 CA LEU B 69 -1.315 72.050 -62.810 1.00 11.28 ATOM 1376 C LEU B 69 -1.819 70.892 -63.672 1.00 10.82 ATOM 1377 O LEU B 69 -2.476 69.979 -63.156 1.00 8.92 ATOM 1378 CB LEU B 69 -2.130 73.341 -62.923 1.00 12.67 ATOM 1379 CG LEU B 69 -3.627 73.149 -62.920 1.00 15.85 ATOM 1380 CD1 LEU B 69 -4.010 72.221 -61.839 1.00 18.69 ATOM 1381 CD2 LEU B 69 -4.286 74.471 -62.738 1.00 17.52 ATOM 1382 N ASN B 70 -1.508 70.919 -64.968 1.00 9.53 ATOM 1383 CA ASN B 70 -2.003 69.907 -65.903 1.00 9.06 ATOM 1384 C ASN B 70 -1.073 69.825 -67.089 1.00 9.38 ATOM 1385 O ASN B 70 -0.050 70.521 -67.152 1.00 10.04 ATOM 1386 CB ASN B 70 -3.409 70.182 -66.411 1.00 6.28 ATOM 1387 CG ASN B 70 -3.501 71.506 -66.983 1.00 13.91 ATOM 1388 OD1 ASN B 70 -2.579 71.916 -67.741 1.00 16.29 ATOM 1389 ND2 ASN B 70 -4.504 72.305 -66.529 1.00 11.11 ATOM 1390 N GLU B 71 -1.424 68.960 -68.016 1.00 7.89 ATOM 1391 CA GLU B 71 -0.676 68.737 -69.198 1.00 7.99 ATOM 1392 C GLU B 71 -0.468 69.933 -70.108 1.00 9.63 ATOM 1393 O GLU B 71 0.627 70.112 -70.552 1.00 8.93 ATOM 1394 CB GLU B 71 -1.268 67.546 -69.978 1.00 7.88 ATOM 1395 CG GLU B 71 -0.765 67.327 -71.345 1.00 8.94 ATOM 1396 CD GLU B 71 -1.738 66.502 -72.194 1.00 19.55 ATOM 1397 OE1 GLU B 71 -2.182 65.417 -71.711 1.00 21.09 ATOM 1398 OE2 GLU B 71 -2.064 66.942 -73.327 1.00 22.55 ATOM 1399 N ASP B 72 -1.517 70.679 -70.516 1.00 14.68 ATOM 1400 CA ASP B 72 -1.301 71.873 -71.390 1.00 13.93 ATOM 1401 C ASP B 72 -0.493 72.928 -70.793 1.00 14.66 ATOM 1402 O ASP B 72 0.170 73.716 -71.506 1.00 17.22 ATOM 1403 CB ASP B 72 -2.611 72.412 -71.915 1.00 17.39 ATOM 1404 CG ASP B 72 -3.429 71.314 -72.501 1.00 19.78 ATOM 1405 OD1 ASP B 72 -2.947 70.643 -73.464 1.00 21.01 ATOM 1406 OD2 ASP B 72 -4.467 71.078 -71.921 1.00 18.49 ATOM 1407 N LEU B 73 -0.450 72.988 -69.489 1.00 15.50 ATOM 1408 CA LEU B 73 0.356 74.077 -68.854 1.00 16.88 ATOM 1409 C LEU B 73 1.795 73.598 -68.994 1.00 17.13 ATOM 1410 O LEU B 73 2.713 74.421 -68.993 1.00 14.55 ATOM 1411 CB LEU B 73 0.041 74.280 -67.349 1.00 15.61 ATOM 1412 CG LEU B 73 0.738 75.289 -66.451 1.00 14.47 ATOM 1413 CD1 LEU B 73 0.660 76.606 -67.087 1.00 15.56 ATOM 1414 CD2 LEU B 73 -0.027 75.293 -65.170 1.00 12.77 ATOM 1415 N ALA B 74 1.958 72.262 -69.083 1.00 17.65 ATOM 1416 CA ALA B 74 3.328 71.583 -69.197 1.00 18.93 ATOM 1417 C ALA B 74 3.979 72.020 -70.515 1.00 17.88 ATOM 1418 O ALA B 74 5.065 72.519 -70.526 1.00 19.26 ATOM 1419 CB ALA B 74 3.180 70.088 -69.191 1.00 17.35 ATOM 1420 N LYS B 75 3.242 71.878 -71.613 1.00 16.67 ATOM 1421 CA LYS B 75 3.692 72.225 -72.929 1.00 14.00 ATOM 1422 C LYS B 75 3.926 73.707 -73.032 1.00 14.30 ATOM 1423 O LYS B 75 5.026 74.104 -73.441 1.00 15.59 ATOM 1424 CB LYS B 75 2.679 71.749 -73.934 1.00 14.96 ATOM 1425 CG LYS B 75 1.968 70.381 -73.562 1.00 14.40 ATOM 1426 CD LYS B 75 2.272 69.253 -74.608 1.00 12.43 ATOM 1427 CE LYS B 75 1.170 68.249 -74.842 1.00 15.68 ATOM 1428 NZ LYS B 75 -0.199 68.762 -75.093 1.00 13.37 ATOM 1429 N LYS B 76 2.984 74.553 -72.617 1.00 12.03 ATOM 1430 CA LYS B 76 3.311 75.984 -72.654 1.00 10.80 ATOM 1431 C LYS B 76 4.841 76.225 -72.391 1.00 10.78 ATOM 1432 O LYS B 76 5.448 77.124 -72.943 1.00 9.45 ATOM 1433 CB LYS B 76 2.462 76.752 -71.698 1.00 8.57 ATOM 1434 CG LYS B 76 2.749 78.209 -71.763 1.00 8.38 ATOM 1435 CD LYS B 76 1.966 78.906 -70.687 1.00 4.09 ATOM 1436 CE LYS B 76 2.484 80.347 -70.386 1.00 2.00 ATOM 1437 NZ LYS B 76 1.287 81.228 -69.885 1.00 6.42 ATOM 1438 N TYR B 77 5.491 75.393 -71.582 1.00 10.61 ATOM 1439 CA TYR B 77 6.872 75.670 -71.324 1.00 12.40 ATOM 1440 C TYR B 77 7.830 74.629 -71.793 1.00 12.88 ATOM 1441 O TYR B 77 9.057 74.842 -71.636 1.00 11.52 ATOM 1442 CB TYR B 77 7.130 75.839 -69.871 1.00 12.86 ATOM 1443 CG TYR B 77 6.508 77.058 -69.301 1.00 15.12 ATOM 1444 CD1 TYR B 77 5.163 77.019 -68.837 1.00 14.99 ATOM 1445 CD2 TYR B 77 7.157 78.239 -69.376 1.00 6.11 ATOM 1446 CE1 TYR B 77 4.582 78.144 -68.372 1.00 18.57 ATOM 1447 CE2 TYR B 77 6.584 79.388 -68.847 1.00 16.06 ATOM 1448 CZ TYR B 77 5.311 79.335 -68.345 1.00 7.39 ATOM 1449 OH TYR B 77 4.699 80.458 -67.889 1.00 14.02 ATOM 1450 N LYS B 78 7.263 73.504 -72.250 1.00 14.19 ATOM 1451 CA LYS B 78 8.003 72.249 -72.535 1.00 15.10 ATOM 1452 C LYS B 78 9.323 72.472 -73.139 1.00 15.39 ATOM 1453 O LYS B 78 10.278 71.866 -72.682 1.00 16.90 ATOM 1454 CB LYS B 78 7.264 71.344 -73.514 1.00 15.32 ATOM 1455 CG LYS B 78 7.999 69.995 -73.797 1.00 11.68 ATOM 1456 CD LYS B 78 7.232 69.281 -74.934 1.00 16.61 ATOM 1457 CE LYS B 78 8.095 68.285 -75.666 1.00 20.76 ATOM 1458 NZ LYS B 78 9.032 67.580 -74.703 1.00 11.20 ATOM 1459 N ASP B 79 9.423 73.322 -74.163 1.00 16.73 ATOM 1460 CA ASP B 79 10.788 73.702 -74.750 1.00 18.74 ATOM 1461 C ASP B 79 11.135 75.217 -74.946 1.00 20.66 ATOM 1462 O ASP B 79 11.712 75.641 -76.009 1.00 20.48 ATOM 1463 CB ASP B 79 10.968 73.054 -76.098 1.00 18.72 ATOM 1464 CG ASP B 79 9.662 72.840 -76.800 1.00 21.57 ATOM 1465 OD1 ASP B 79 9.419 71.711 -77.346 1.00 25.37 ATOM 1466 OD2 ASP B 79 8.851 73.809 -76.783 1.00 24.82 ATOM 1467 N GLU B 80 10.863 76.019 -73.924 1.00 19.44 ATOM 1468 CA GLU B 80 11.144 77.436 -73.999 1.00 19.33 ATOM 1469 C GLU B 80 12.226 77.796 -73.009 1.00 18.09 ATOM 1470 O GLU B 80 12.434 77.108 -72.022 1.00 16.55 ATOM 1471 CB GLU B 80 9.828 78.244 -73.719 1.00 20.36 ATOM 1472 CG GLU B 80 8.704 78.003 -74.707 1.00 21.54 ATOM 1473 CD GLU B 80 9.206 78.011 -76.179 1.00 30.53 ATOM 1474 OE1 GLU B 80 9.469 79.116 -76.782 1.00 31.76 ATOM 1475 OE2 GLU B 80 9.326 76.886 -76.746 1.00 31.31 ATOM 1476 N VAL B 81 12.878 78.937 -73.238 1.00 17.57 ATOM 1477 CA VAL B 81 13.940 79.359 -72.343 1.00 16.47 ATOM 1478 C VAL B 81 13.323 80.074 -71.207 1.00 15.80 ATOM 1479 O VAL B 81 12.771 81.152 -71.433 1.00 16.92 ATOM 1480 CB VAL B 81 15.086 80.195 -73.045 1.00 17.46 ATOM 1481 CG1 VAL B 81 16.185 80.500 -72.069 1.00 13.61 ATOM 1482 CG2 VAL B 81 15.671 79.426 -74.271 1.00 17.65 ATOM 1483 N VAL B 82 13.346 79.476 -69.990 1.00 14.23 ATOM 1484 CA VAL B 82 12.610 80.098 -68.904 1.00 13.60 ATOM 1485 C VAL B 82 13.534 80.375 -67.765 1.00 12.40 ATOM 1486 O VAL B 82 14.676 79.967 -67.895 1.00 14.07 ATOM 1487 CB VAL B 82 11.490 79.249 -68.382 1.00 12.61 ATOM 1488 CG1 VAL B 82 10.354 79.315 -69.282 1.00 10.09 ATOM 1489 CG2 VAL B 82 11.999 77.805 -68.150 1.00 11.70 ATOM 1490 N ASP B 83 13.039 81.043 -66.689 1.00 10.60 ATOM 1491 CA ASP B 83 13.762 81.172 -65.403 1.00 11.28 ATOM 1492 C ASP B 83 13.062 80.297 -64.387 1.00 9.47 ATOM 1493 O ASP B 83 11.936 79.906 -64.585 1.00 9.22 ATOM 1494 CB ASP B 83 13.768 82.602 -64.944 1.00 9.92 ATOM 1495 CG ASP B 83 14.390 83.537 -65.985 1.00 11.34 ATOM 1496 OD1 ASP B 83 15.623 83.444 -66.297 1.00 17.16 ATOM 1497 OD2 ASP B 83 13.664 84.379 -66.431 1.00 6.06 ATOM 1498 N VAL B 84 13.691 80.060 -63.267 1.00 8.77 ATOM 1499 CA VAL B 84 13.023 79.298 -62.188 1.00 10.37 ATOM 1500 C VAL B 84 13.117 79.876 -60.767 1.00 11.30 ATOM 1501 O VAL B 84 14.126 80.482 -60.456 1.00 13.92 ATOM 1502 CB VAL B 84 13.628 77.883 -62.165 1.00 10.76 ATOM 1503 CG1 VAL B 84 12.884 77.064 -61.176 1.00 5.69 ATOM 1504 CG2 VAL B 84 13.564 77.266 -63.594 1.00 4.66 ATOM 1505 N TYR B 85 12.108 79.666 -59.896 1.00 8.83 ATOM 1506 CA TYR B 85 12.136 80.156 -58.546 1.00 9.12 ATOM 1507 C TYR B 85 11.096 79.343 -57.815 1.00 10.75 ATOM 1508 O TYR B 85 9.841 79.621 -57.969 1.00 10.81 ATOM 1509 CB TYR B 85 11.767 81.683 -58.387 1.00 11.31 ATOM 1510 CG TYR B 85 12.501 82.121 -57.168 1.00 9.98 ATOM 1511 CD1 TYR B 85 13.853 82.362 -57.238 1.00 8.95 ATOM 1512 CD2 TYR B 85 11.896 82.151 -55.943 1.00 5.62 ATOM 1513 CE1 TYR B 85 14.571 82.620 -56.105 1.00 9.81 ATOM 1514 CE2 TYR B 85 12.609 82.444 -54.793 1.00 5.27 ATOM 1515 CZ TYR B 85 13.965 82.664 -54.887 1.00 10.35 ATOM 1516 OH TYR B 85 14.728 83.004 -53.767 1.00 11.66 ATOM 1517 N GLY B 86 11.541 78.354 -57.052 1.00 7.23 ATOM 1518 CA GLY B 86 10.644 77.587 -56.266 1.00 7.38 ATOM 1519 C GLY B 86 11.231 76.949 -55.037 1.00 6.94 ATOM 1520 O GLY B 86 12.435 76.891 -54.965 1.00 8.25 ATOM 1521 N SER B 87 10.382 76.472 -54.097 1.00 7.72 ATOM 1522 CA SER B 87 10.844 75.599 -52.995 1.00 8.44 ATOM 1523 C SER B 87 10.802 74.121 -53.322 1.00 8.90 ATOM 1524 O SER B 87 9.713 73.546 -53.513 1.00 9.26 ATOM 1525 CB SER B 87 9.983 75.747 -51.747 1.00 8.80 ATOM 1526 OG SER B 87 10.728 75.763 -50.525 1.00 7.70 ATOM 1527 N ASN B 88 11.982 73.491 -53.252 1.00 8.69 ATOM 1528 CA ASN B 88 12.165 72.144 -53.582 1.00 7.11 ATOM 1529 C ASN B 88 12.002 71.279 -52.338 1.00 8.13 ATOM 1530 O ASN B 88 12.130 71.771 -51.217 1.00 4.36 ATOM 1531 CB ASN B 88 13.499 71.970 -54.194 1.00 7.12 ATOM 1532 CG ASN B 88 14.642 72.413 -53.287 1.00 10.18 ATOM 1533 OD1 ASN B 88 14.774 73.557 -53.002 1.00 11.23 ATOM 1534 ND2 ASN B 88 15.541 71.479 -52.920 1.00 14.47 ATOM 1535 N TYR B 89 11.690 69.987 -52.544 1.00 6.65 ATOM 1536 CA TYR B 89 11.737 69.031 -51.411 1.00 8.82 ATOM 1537 C TYR B 89 12.318 67.674 -51.833 1.00 7.44 ATOM 1538 O TYR B 89 12.585 67.502 -52.994 1.00 11.07 ATOM 1539 CB TYR B 89 10.314 68.813 -50.904 1.00 8.27 ATOM 1540 CG TYR B 89 9.512 68.177 -51.942 1.00 11.68 ATOM 1541 CD1 TYR B 89 8.875 68.985 -52.869 1.00 15.37 ATOM 1542 CD2 TYR B 89 9.322 66.799 -51.994 1.00 12.69 ATOM 1543 CE1 TYR B 89 8.097 68.485 -53.860 1.00 17.48 ATOM 1544 CE2 TYR B 89 8.426 66.252 -52.973 1.00 17.91 ATOM 1545 CZ TYR B 89 7.807 67.121 -53.924 1.00 17.27 ATOM 1546 OH TYR B 89 6.978 66.738 -55.040 1.00 15.30 ATOM 1547 N TYR B 90 12.379 66.694 -50.953 1.00 6.70 ATOM 1548 CA TYR B 90 12.874 65.401 -51.307 1.00 9.56 ATOM 1549 C TYR B 90 11.972 64.287 -50.795 1.00 10.66 ATOM 1550 O TYR B 90 11.441 63.521 -51.556 1.00 9.30 ATOM 1551 CB TYR B 90 14.355 65.180 -50.866 1.00 11.84 ATOM 1552 CG TYR B 90 15.304 66.388 -51.055 1.00 6.94 ATOM 1553 CD1 TYR B 90 15.061 67.617 -50.466 1.00 11.94 ATOM 1554 CD2 TYR B 90 16.488 66.267 -51.848 1.00 13.00 ATOM 1555 CE1 TYR B 90 16.035 68.788 -50.710 1.00 13.14 ATOM 1556 CE2 TYR B 90 17.361 67.346 -52.107 1.00 6.85 ATOM 1557 CZ TYR B 90 17.158 68.564 -51.548 1.00 11.37 ATOM 1558 OH TYR B 90 18.112 69.535 -51.834 1.00 13.49 ATOM 1559 N VAL B 91 11.758 64.193 -49.511 1.00 12.20 ATOM 1560 CA VAL B 91 10.935 63.129 -49.007 1.00 12.35 ATOM 1561 C VAL B 91 9.624 63.043 -49.868 1.00 14.60 ATOM 1562 O VAL B 91 8.783 63.939 -49.828 1.00 15.23 ATOM 1563 CB VAL B 91 10.650 63.404 -47.531 1.00 11.92 ATOM 1564 CG1 VAL B 91 9.584 62.436 -46.988 1.00 15.42 ATOM 1565 CG2 VAL B 91 11.821 63.307 -46.758 1.00 10.19 ATOM 1566 N ASN B 92 9.518 61.970 -50.668 1.00 17.21 ATOM 1567 CA ASN B 92 8.487 61.746 -51.714 1.00 19.48 ATOM 1568 C ASN B 92 8.707 62.480 -53.062 1.00 18.45 ATOM 1569 O ASN B 92 7.691 62.951 -53.670 1.00 21.19 ATOM 1570 CB ASN B 92 7.082 62.037 -51.126 1.00 19.37 ATOM 1571 CG ASN B 92 7.038 61.674 -49.672 1.00 22.66 ATOM 1572 OD1 ASN B 92 7.620 60.637 -49.265 1.00 20.81 ATOM 1573 ND2 ASN B 92 6.391 62.518 -48.864 1.00 18.75 ATOM 1574 N CYS B 93 9.980 62.605 -53.491 1.00 15.78 ATOM 1575 CA CYS B 93 10.367 63.139 -54.805 1.00 13.75 ATOM 1576 C CYS B 93 10.644 61.980 -55.647 1.00 13.70 ATOM 1577 O CYS B 93 11.751 61.344 -55.527 1.00 10.79 ATOM 1578 CB CYS B 93 11.636 63.954 -54.782 1.00 13.51 ATOM 1579 SG CYS B 93 11.861 64.897 -56.272 1.00 14.61 ATOM 1580 N TYR B 94 9.653 61.678 -56.486 1.00 13.67 ATOM 1581 CA TYR B 94 9.621 60.421 -57.328 1.00 15.69 ATOM 1582 C TYR B 94 9.675 60.669 -58.829 1.00 15.27 ATOM 1583 O TYR B 94 9.286 61.762 -59.331 1.00 19.56 ATOM 1584 CB TYR B 94 8.305 59.659 -57.057 1.00 15.20 ATOM 1585 CG TYR B 94 7.031 60.478 -57.059 1.00 18.01 ATOM 1586 CD1 TYR B 94 7.022 61.873 -56.649 1.00 15.82 ATOM 1587 CD2 TYR B 94 5.785 59.875 -57.383 1.00 23.47 ATOM 1588 CE1 TYR B 94 5.877 62.615 -56.650 1.00 17.23 ATOM 1589 CE2 TYR B 94 4.621 60.606 -57.388 1.00 19.56 ATOM 1590 CZ TYR B 94 4.679 62.004 -56.987 1.00 19.32 ATOM 1591 OH TYR B 94 3.547 62.769 -56.927 1.00 17.22 ATOM 1592 N PHE B 95 9.970 59.607 -59.527 1.00 17.97 ATOM 1593 CA PHE B 95 10.083 59.509 -60.982 1.00 19.11 ATOM 1594 C PHE B 95 9.652 58.228 -61.591 1.00 21.85 ATOM 1595 O PHE B 95 10.132 57.878 -62.688 1.00 22.70 ATOM 1596 CB PHE B 95 11.560 59.673 -61.375 1.00 17.11 ATOM 1597 CG PHE B 95 12.114 61.023 -61.058 1.00 14.83 ATOM 1598 CD1 PHE B 95 12.667 61.299 -59.805 1.00 13.75 ATOM 1599 CD2 PHE B 95 12.203 61.974 -62.026 1.00 14.84 ATOM 1600 CE1 PHE B 95 13.252 62.604 -59.528 1.00 8.51 ATOM 1601 CE2 PHE B 95 12.822 63.262 -61.725 1.00 12.52 ATOM 1602 CZ PHE B 95 13.338 63.488 -60.464 1.00 6.47 ATOM 1603 N SER B 96 8.810 57.482 -60.875 1.00 25.99 ATOM 1604 CA SER B 96 8.347 56.176 -61.296 1.00 28.59 ATOM 1605 C SER B 96 7.024 55.902 -60.597 1.00 31.56 ATOM 1606 O SER B 96 6.234 56.815 -60.366 1.00 33.73 ATOM 1607 CB SER B 96 9.379 55.077 -60.951 1.00 29.62 ATOM 1608 OG SER B 96 9.536 54.957 -59.559 1.00 28.29 ATOM 1609 N SER B 97 6.788 54.675 -60.185 1.00 33.99 ATOM 1610 CA SER B 97 5.468 54.366 -59.653 1.00 38.04 ATOM 1611 C SER B 97 5.525 54.185 -58.124 1.00 39.63 ATOM 1612 O SER B 97 4.625 54.625 -57.400 1.00 40.35 ATOM 1613 CB SER B 97 4.880 53.118 -60.369 1.00 37.97 ATOM 1614 OG SER B 97 5.813 52.017 -60.388 1.00 40.53 ATOM 1615 N LYS B 98 6.578 53.505 -57.648 1.00 41.07 ATOM 1616 CA LYS B 98 6.788 53.287 -56.228 1.00 41.19 ATOM 1617 C LYS B 98 6.946 54.657 -55.566 1.00 40.42 ATOM 1618 O LYS B 98 7.752 55.497 -56.014 1.00 40.75 ATOM 1619 CB LYS B 98 8.019 52.418 -55.969 1.00 41.81 ATOM 1620 CG LYS B 98 8.231 52.130 -54.448 1.00 46.39 ATOM 1621 CD LYS B 98 8.799 50.694 -54.215 1.00 47.24 ATOM 1622 CE LYS B 98 9.540 50.525 -52.875 1.00 44.71 ATOM 1623 NZ LYS B 98 10.104 49.134 -52.858 1.00 43.05 ATOM 1624 N ASP B 99 6.189 54.810 -54.474 1.00 38.39 ATOM 1625 CA ASP B 99 5.901 56.066 -53.718 1.00 34.76 ATOM 1626 C ASP B 99 7.036 56.611 -52.805 1.00 32.59 ATOM 1627 O ASP B 99 7.281 57.835 -52.828 1.00 31.60 ATOM 1628 CB ASP B 99 4.584 55.829 -52.926 1.00 34.67 ATOM 1629 CG ASP B 99 4.399 54.356 -52.600 1.00 35.24 ATOM 1630 OD1 ASP B 99 5.420 53.669 -52.353 1.00 32.71 ATOM 1631 OD2 ASP B 99 3.253 53.869 -52.686 1.00 40.51 ATOM 1632 N ASN B 100 7.685 55.702 -52.026 1.00 31.93 ATOM 1633 CA ASN B 100 8.939 55.992 -51.232 1.00 30.10 ATOM 1634 C ASN B 100 10.162 55.208 -51.702 1.00 27.75 ATOM 1635 O ASN B 100 10.419 54.047 -51.296 1.00 26.05 ATOM 1636 CB ASN B 100 8.766 55.841 -49.718 1.00 30.15 ATOM 1637 CG ASN B 100 9.343 57.037 -48.930 1.00 33.53 ATOM 1638 OD1 ASN B 100 9.026 57.182 -47.760 1.00 37.67 ATOM 1639 ND2 ASN B 100 10.181 57.898 -49.571 1.00 36.67 ATOM 1640 N VAL B 101 10.896 55.889 -52.579 1.00 23.52 ATOM 1641 CA VAL B 101 12.030 55.317 -53.305 1.00 19.42 ATOM 1642 C VAL B 101 13.074 56.460 -53.430 1.00 17.45 ATOM 1643 O VAL B 101 12.697 57.638 -53.560 1.00 17.04 ATOM 1644 CB VAL B 101 11.655 54.932 -54.680 1.00 19.06 ATOM 1645 CG1 VAL B 101 12.769 55.233 -55.580 1.00 16.25 ATOM 1646 CG2 VAL B 101 11.246 53.482 -54.761 1.00 16.36 ATOM 1647 N TRP B 102 14.352 56.134 -53.434 1.00 13.17 ATOM 1648 CA TRP B 102 15.408 57.181 -53.580 1.00 11.54 ATOM 1649 C TRP B 102 16.058 57.307 -55.003 1.00 13.46 ATOM 1650 O TRP B 102 15.952 56.363 -55.838 1.00 12.67 ATOM 1651 CB TRP B 102 16.497 57.028 -52.477 1.00 10.48 ATOM 1652 CG TRP B 102 17.507 58.185 -52.433 1.00 5.07 ATOM 1653 CD1 TRP B 102 17.217 59.462 -52.217 1.00 7.38 ATOM 1654 CD2 TRP B 102 18.941 58.100 -52.532 1.00 6.91 ATOM 1655 NE1 TRP B 102 18.339 60.232 -52.206 1.00 12.31 ATOM 1656 CE2 TRP B 102 19.437 59.423 -52.400 1.00 11.59 ATOM 1657 CE3 TRP B 102 19.844 57.047 -52.618 1.00 2.04 ATOM 1658 CZ2 TRP B 102 20.804 59.745 -52.437 1.00 9.18 ATOM 1659 CZ3 TRP B 102 21.225 57.372 -52.720 1.00 12.39 ATOM 1660 CH2 TRP B 102 21.678 58.744 -52.650 1.00 5.74 ATOM 1661 N TRP B 103 16.737 58.440 -55.275 1.00 10.67 ATOM 1662 CA TRP B 103 17.389 58.659 -56.531 1.00 11.92 ATOM 1663 C TRP B 103 18.728 59.316 -56.402 1.00 12.65 ATOM 1664 O TRP B 103 19.762 58.621 -56.390 1.00 9.75 ATOM 1665 CB TRP B 103 16.594 59.594 -57.349 1.00 12.69 ATOM 1666 CG TRP B 103 15.126 59.184 -57.268 1.00 16.33 ATOM 1667 CD1 TRP B 103 14.267 59.483 -56.223 1.00 18.14 ATOM 1668 CD2 TRP B 103 14.374 58.378 -58.206 1.00 10.68 ATOM 1669 NE1 TRP B 103 12.989 58.940 -56.488 1.00 21.88 ATOM 1670 CE2 TRP B 103 13.016 58.269 -57.681 1.00 16.85 ATOM 1671 CE3 TRP B 103 14.674 57.779 -59.411 1.00 9.65 ATOM 1672 CZ2 TRP B 103 12.003 57.597 -58.327 1.00 5.83 ATOM 1673 CZ3 TRP B 103 13.686 57.072 -60.073 1.00 14.50 ATOM 1674 CH2 TRP B 103 12.327 56.970 -59.508 1.00 16.82 ATOM 1675 N HIS B 104 18.665 60.638 -56.254 1.00 12.02 ATOM 1676 CA HIS B 104 19.857 61.491 -56.132 1.00 16.75 ATOM 1677 C HIS B 104 20.012 62.383 -57.314 1.00 16.77 ATOM 1678 O HIS B 104 19.530 62.037 -58.414 1.00 18.99 ATOM 1679 CB HIS B 104 21.213 60.746 -55.925 1.00 16.62 ATOM 1680 CG HIS B 104 22.336 61.642 -55.459 1.00 25.28 ATOM 1681 ND1 HIS B 104 23.120 62.390 -56.337 1.00 29.30 ATOM 1682 CD2 HIS B 104 22.773 61.953 -54.208 1.00 29.34 ATOM 1683 CE1 HIS B 104 23.952 63.152 -55.647 1.00 29.76 ATOM 1684 NE2 HIS B 104 23.782 62.891 -54.358 1.00 36.11 ATOM 1685 N GLY B 105 20.739 63.493 -57.095 1.00 18.38 ATOM 1686 CA GLY B 105 20.819 64.653 -58.034 1.00 16.22 ATOM 1687 C GLY B 105 19.465 65.145 -58.513 1.00 16.19 ATOM 1688 O GLY B 105 19.368 65.887 -59.512 1.00 19.12 ATOM 1689 N LYS B 106 18.393 64.787 -57.799 1.00 14.02 ATOM 1690 CA LYS B 106 17.084 65.062 -58.255 1.00 12.47 ATOM 1691 C LYS B 106 16.345 65.731 -57.120 1.00 12.17 ATOM 1692 O LYS B 106 16.776 65.679 -56.013 1.00 11.55 ATOM 1693 CB LYS B 106 16.360 63.756 -58.710 1.00 13.14 ATOM 1694 CG LYS B 106 16.797 63.278 -60.111 1.00 8.35 ATOM 1695 CD LYS B 106 16.382 61.820 -60.425 1.00 11.82 ATOM 1696 CE LYS B 106 17.092 61.326 -61.692 1.00 15.57 ATOM 1697 NZ LYS B 106 18.235 60.490 -61.370 1.00 7.61 ATOM 1698 N THR B 107 15.234 66.428 -57.401 1.00 13.15 ATOM 1699 CA THR B 107 14.476 67.159 -56.381 1.00 8.49 ATOM 1700 C THR B 107 13.231 67.590 -57.055 1.00 6.30 ATOM 1701 O THR B 107 13.235 67.728 -58.277 1.00 5.01 ATOM 1702 CB THR B 107 15.275 68.272 -55.782 1.00 8.54 ATOM 1703 OG1 THR B 107 14.660 68.602 -54.511 1.00 14.67 ATOM 1704 CG2 THR B 107 15.330 69.521 -56.648 1.00 9.67 ATOM 1705 N CYS B 108 12.188 67.807 -56.306 1.00 4.27 ATOM 1706 CA CYS B 108 10.876 68.141 -56.923 1.00 6.58 ATOM 1707 C CYS B 108 10.353 69.553 -56.567 1.00 5.36 ATOM 1708 O CYS B 108 10.907 70.226 -55.725 1.00 5.29 ATOM 1709 CB CYS B 108 9.803 67.187 -56.465 1.00 6.72 ATOM 1710 SG CYS B 108 10.094 65.385 -57.069 1.00 9.90 ATOM 1711 N MET B 109 9.316 70.008 -57.246 1.00 5.12 ATOM 1712 CA MET B 109 8.679 71.251 -56.801 1.00 7.91 ATOM 1713 C MET B 109 7.433 71.379 -57.550 1.00 9.35 ATOM 1714 O MET B 109 6.863 70.371 -58.066 1.00 8.73 ATOM 1715 CB MET B 109 9.568 72.495 -57.063 1.00 4.69 ATOM 1716 CG MET B 109 10.500 72.430 -58.287 1.00 4.57 ATOM 1717 SD MET B 109 11.353 73.955 -58.699 1.00 14.05 ATOM 1718 CE MET B 109 10.059 75.050 -58.966 1.00 5.69 ATOM 1719 N TYR B 110 6.937 72.604 -57.591 1.00 9.58 ATOM 1720 CA TYR B 110 5.757 72.850 -58.404 1.00 10.15 ATOM 1721 C TYR B 110 5.902 74.323 -58.882 1.00 9.39 ATOM 1722 O TYR B 110 6.311 75.097 -58.125 1.00 9.09 ATOM 1723 CB TYR B 110 4.550 72.741 -57.565 1.00 7.44 ATOM 1724 CG TYR B 110 4.372 71.414 -56.868 1.00 9.66 ATOM 1725 CD1 TYR B 110 4.965 71.150 -55.616 1.00 6.00 ATOM 1726 CD2 TYR B 110 3.577 70.425 -57.453 1.00 3.96 ATOM 1727 CE1 TYR B 110 4.778 69.920 -54.962 1.00 12.85 ATOM 1728 CE2 TYR B 110 3.408 69.212 -56.844 1.00 15.12 ATOM 1729 CZ TYR B 110 3.977 68.950 -55.612 1.00 12.80 ATOM 1730 OH TYR B 110 3.699 67.763 -55.123 1.00 5.30 ATOM 1731 N GLY B 111 5.582 74.631 -60.131 1.00 8.70 ATOM 1732 CA GLY B 111 5.484 75.996 -60.610 1.00 9.13 ATOM 1733 C GLY B 111 6.866 76.655 -60.607 1.00 9.52 ATOM 1734 O GLY B 111 7.889 75.991 -60.731 1.00 8.14 ATOM 1735 N GLY B 112 6.873 77.960 -60.434 1.00 10.77 ATOM 1736 CA GLY B 112 8.144 78.748 -60.544 1.00 13.18 ATOM 1737 C GLY B 112 8.996 78.739 -61.797 1.00 11.17 ATOM 1738 O GLY B 112 10.105 78.204 -61.791 1.00 13.11 ATOM 1739 N ILE B 113 8.467 79.310 -62.878 1.00 11.24 ATOM 1740 CA ILE B 113 9.169 79.449 -64.171 1.00 9.56 ATOM 1741 C ILE B 113 8.519 80.518 -64.952 1.00 10.23 ATOM 1742 O ILE B 113 7.281 80.661 -64.867 1.00 10.06 ATOM 1743 CB ILE B 113 9.006 78.156 -64.984 1.00 8.61 ATOM 1744 CG1 ILE B 113 7.580 77.622 -64.832 1.00 8.65 ATOM 1745 CG2 ILE B 113 9.994 77.192 -64.406 1.00 6.90 ATOM 1746 CD1 ILE B 113 7.313 76.166 -65.516 1.00 12.96 ATOM 1747 N THR B 114 9.325 81.256 -65.725 1.00 10.16 ATOM 1748 CA THR B 114 8.774 82.257 -66.629 1.00 11.15 ATOM 1749 C THR B 114 9.670 82.465 -67.835 1.00 10.54 ATOM 1750 O THR B 114 10.912 82.234 -67.805 1.00 11.15 ATOM 1751 CB THR B 114 8.550 83.601 -65.914 1.00 13.35 ATOM 1752 OG1 THR B 114 9.843 84.078 -65.478 1.00 16.18 ATOM 1753 CG2 THR B 114 7.606 83.380 -64.728 1.00 7.66 ATOM 1754 N LYS B 115 9.050 82.879 -68.928 1.00 9.49 ATOM 1755 CA LYS B 115 9.785 83.011 -70.168 1.00 9.70 ATOM 1756 C LYS B 115 10.811 84.122 -69.895 1.00 9.23 ATOM 1757 O LYS B 115 10.503 85.183 -69.354 1.00 9.06 ATOM 1758 CB LYS B 115 8.908 83.301 -71.387 1.00 10.49 ATOM 1759 CG LYS B 115 8.038 82.187 -72.012 1.00 19.64 ATOM 1760 CD LYS B 115 8.699 80.880 -72.386 1.00 19.57 ATOM 1761 CE LYS B 115 9.221 80.970 -73.805 1.00 21.13 ATOM 1762 NZ LYS B 115 8.195 80.572 -74.876 1.00 17.94 ATOM 1763 N HIS B 116 12.071 83.790 -70.094 1.00 10.99 ATOM 1764 CA HIS B 116 13.201 84.707 -69.864 1.00 10.07 ATOM 1765 C HIS B 116 13.223 85.943 -70.791 1.00 12.52 ATOM 1766 O HIS B 116 13.477 87.033 -70.303 1.00 9.87 ATOM 1767 CB HIS B 116 14.447 83.988 -70.149 1.00 9.39 ATOM 1768 CG HIS B 116 15.634 84.874 -70.122 1.00 10.83 ATOM 1769 ND1 HIS B 116 15.658 86.065 -70.805 1.00 10.40 ATOM 1770 CD2 HIS B 116 16.854 84.727 -69.554 1.00 7.08 ATOM 1771 CE1 HIS B 116 16.851 86.627 -70.630 1.00 16.48 ATOM 1772 NE2 HIS B 116 17.600 85.809 -69.915 1.00 13.80 ATOM 1773 N GLU B 117 12.954 85.711 -72.095 1.00 14.09 ATOM 1774 CA GLU B 117 13.008 86.715 -73.119 1.00 18.84 ATOM 1775 C GLU B 117 12.160 87.878 -72.715 1.00 20.59 ATOM 1776 O GLU B 117 10.973 87.724 -72.412 1.00 18.17 ATOM 1777 CB GLU B 117 12.507 86.212 -74.453 1.00 19.37 ATOM 1778 CG GLU B 117 13.333 85.008 -74.997 1.00 25.78 ATOM 1779 CD GLU B 117 13.310 83.843 -74.035 1.00 27.77 ATOM 1780 OE1 GLU B 117 12.223 83.466 -73.482 1.00 32.69 ATOM 1781 OE2 GLU B 117 14.401 83.336 -73.758 1.00 33.27 ATOM 1782 N GLY B 118 12.817 89.041 -72.711 1.00 22.37 ATOM 1783 CA GLY B 118 12.149 90.322 -72.498 1.00 24.73 ATOM 1784 C GLY B 118 11.132 90.259 -71.360 1.00 26.71 ATOM 1785 O GLY B 118 9.886 90.422 -71.592 1.00 27.33 ATOM 1786 N ASN B 119 11.679 89.909 -70.183 1.00 27.51 ATOM 1787 CA ASN B 119 10.988 89.869 -68.887 1.00 29.14 ATOM 1788 C ASN B 119 11.884 90.374 -67.752 1.00 29.31 ATOM 1789 O ASN B 119 11.366 90.684 -66.681 1.00 30.05 ATOM 1790 CB ASN B 119 10.432 88.477 -68.527 1.00 28.85 ATOM 1791 CG ASN B 119 9.737 88.451 -67.164 1.00 29.52 ATOM 1792 OD1 ASN B 119 8.930 89.342 -66.828 1.00 26.52 ATOM 1793 ND2 ASN B 119 10.089 87.441 -66.339 1.00 26.90 ATOM 1794 N HIS B 120 13.196 90.450 -67.971 1.00 28.78 ATOM 1795 CA HIS B 120 14.067 91.078 -66.995 1.00 29.01 ATOM 1796 C HIS B 120 14.113 92.632 -67.214 1.00 29.57 ATOM 1797 O HIS B 120 13.477 93.145 -68.150 1.00 28.35 ATOM 1798 CB HIS B 120 15.447 90.446 -66.999 1.00 27.87 ATOM 1799 CG HIS B 120 15.452 88.993 -66.670 1.00 27.03 ATOM 1800 ND1 HIS B 120 16.619 88.308 -66.412 1.00 24.92 ATOM 1801 CD2 HIS B 120 14.451 88.070 -66.614 1.00 27.21 ATOM 1802 CE1 HIS B 120 16.339 87.035 -66.170 1.00 25.59 ATOM 1803 NE2 HIS B 120 15.024 86.861 -66.280 1.00 24.73 ATOM 1804 N PHE B 121 14.850 93.346 -66.342 1.00 30.72 ATOM 1805 CA PHE B 121 14.986 94.839 -66.354 1.00 30.52 ATOM 1806 C PHE B 121 16.146 95.390 -67.176 1.00 31.96 ATOM 1807 O PHE B 121 17.125 94.668 -67.533 1.00 28.89 ATOM 1808 CB PHE B 121 15.031 95.395 -64.915 1.00 30.37 ATOM 1809 CG PHE B 121 13.773 95.020 -64.070 1.00 32.98 ATOM 1810 CD1 PHE B 121 13.731 93.846 -63.346 1.00 29.42 ATOM 1811 CD2 PHE B 121 12.650 95.835 -64.060 1.00 31.22 ATOM 1812 CE1 PHE B 121 12.612 93.474 -62.648 1.00 29.11 ATOM 1813 CE2 PHE B 121 11.490 95.513 -63.325 1.00 31.61 ATOM 1814 CZ PHE B 121 11.449 94.340 -62.621 1.00 33.06 ATOM 1815 N ASP B 122 16.012 96.696 -67.433 1.00 33.06 ATOM 1816 CA ASP B 122 17.021 97.532 -68.102 1.00 35.47 ATOM 1817 C ASP B 122 18.478 97.100 -67.971 1.00 36.30 ATOM 1818 O ASP B 122 19.023 96.501 -68.922 1.00 36.41 ATOM 1819 CB ASP B 122 16.832 98.948 -67.623 1.00 35.80 ATOM 1820 CG ASP B 122 15.368 99.286 -67.473 1.00 37.96 ATOM 1821 OD1 ASP B 122 14.704 99.441 -68.516 1.00 33.41 ATOM 1822 OD2 ASP B 122 14.876 99.334 -66.319 1.00 41.53 ATOM 1823 N ASN B 123 19.109 97.411 -66.826 1.00 36.90 ATOM 1824 CA ASN B 123 20.581 97.164 -66.654 1.00 38.14 ATOM 1825 C ASN B 123 20.949 96.369 -65.397 1.00 37.63 ATOM 1826 O ASN B 123 21.938 96.646 -64.728 1.00 37.21 ATOM 1827 CB ASN B 123 21.380 98.488 -66.751 1.00 38.59 ATOM 1828 CG ASN B 123 20.858 99.394 -67.885 1.00 40.63 ATOM 1829 OD1 ASN B 123 20.748 98.955 -69.059 1.00 38.53 ATOM 1830 ND2 ASN B 123 20.479 100.644 -67.525 1.00 41.94 ATOM 1831 N GLY B 124 20.147 95.340 -65.127 1.00 38.07 ATOM 1832 CA GLY B 124 20.142 94.651 -63.830 1.00 36.81 ATOM 1833 C GLY B 124 19.411 95.286 -62.633 1.00 35.66 ATOM 1834 O GLY B 124 19.419 94.723 -61.534 1.00 36.43 ATOM 1835 N ASN B 125 18.789 96.454 -62.805 1.00 34.47 ATOM 1836 CA ASN B 125 17.963 97.006 -61.726 1.00 31.69 ATOM 1837 C ASN B 125 16.999 95.950 -61.192 1.00 30.35 ATOM 1838 O ASN B 125 16.532 95.069 -61.946 1.00 29.46 ATOM 1839 CB ASN B 125 17.196 98.203 -62.233 1.00 31.89 ATOM 1840 CG ASN B 125 18.067 99.117 -63.058 1.00 30.31 ATOM 1841 OD1 ASN B 125 19.126 99.578 -62.604 1.00 32.28 ATOM 1842 ND2 ASN B 125 17.651 99.357 -64.282 1.00 27.13 ATOM 1843 N LEU B 126 16.716 96.038 -59.894 1.00 28.25 ATOM 1844 CA LEU B 126 15.776 95.134 -59.194 1.00 25.70 ATOM 1845 C LEU B 126 14.576 95.936 -58.726 1.00 25.19 ATOM 1846 O LEU B 126 14.705 97.120 -58.351 1.00 24.59 ATOM 1847 CB LEU B 126 16.428 94.546 -57.965 1.00 22.39 ATOM 1848 CG LEU B 126 17.691 93.714 -58.205 1.00 25.21 ATOM 1849 CD1 LEU B 126 18.909 94.566 -57.829 1.00 21.63 ATOM 1850 CD2 LEU B 126 17.725 92.365 -57.395 1.00 14.86 ATOM 1851 N GLN B 127 13.438 95.266 -58.681 1.00 24.03 ATOM 1852 CA GLN B 127 12.162 95.869 -58.291 1.00 23.82 ATOM 1853 C GLN B 127 11.867 95.662 -56.816 1.00 21.33 ATOM 1854 O GLN B 127 12.310 94.690 -56.213 1.00 23.19 ATOM 1855 CB GLN B 127 11.088 95.236 -59.159 1.00 24.51 ATOM 1856 CG GLN B 127 9.693 95.720 -59.004 1.00 23.80 ATOM 1857 CD GLN B 127 9.518 97.090 -59.486 1.00 19.47 ATOM 1858 OE1 GLN B 127 9.931 97.432 -60.602 1.00 16.64 ATOM 1859 NE2 GLN B 127 8.884 97.934 -58.638 1.00 18.42 ATOM 1860 N ASN B 128 11.174 96.586 -56.197 1.00 18.24 ATOM 1861 CA ASN B 128 10.876 96.414 -54.808 1.00 16.74 ATOM 1862 C ASN B 128 9.400 96.250 -54.537 1.00 14.86 ATOM 1863 O ASN B 128 8.579 96.911 -55.087 1.00 13.35 ATOM 1864 CB ASN B 128 11.460 97.541 -54.027 1.00 17.06 ATOM 1865 CG ASN B 128 12.946 97.437 -53.892 1.00 22.92 ATOM 1866 OD1 ASN B 128 13.540 96.484 -53.243 1.00 27.41 ATOM 1867 ND2 ASN B 128 13.598 98.411 -54.478 1.00 23.80 ATOM 1868 N VAL B 129 9.079 95.342 -53.647 1.00 15.83 ATOM 1869 CA VAL B 129 7.672 94.996 -53.374 1.00 12.49 ATOM 1870 C VAL B 129 7.427 95.137 -51.888 1.00 12.76 ATOM 1871 O VAL B 129 8.068 94.511 -51.012 1.00 12.57 ATOM 1872 CB VAL B 129 7.312 93.651 -53.890 1.00 11.86 ATOM 1873 CG1 VAL B 129 5.859 93.312 -53.630 1.00 13.98 ATOM 1874 CG2 VAL B 129 7.557 93.552 -55.345 1.00 12.23 ATOM 1875 N LEU B 130 6.505 96.028 -51.600 1.00 12.53 ATOM 1876 CA LEU B 130 6.116 96.238 -50.255 1.00 14.17 ATOM 1877 C LEU B 130 5.396 95.053 -49.567 1.00 15.01 ATOM 1878 O LEU B 130 4.605 94.357 -50.183 1.00 12.94 ATOM 1879 CB LEU B 130 5.234 97.449 -50.208 1.00 13.01 ATOM 1880 CG LEU B 130 4.670 97.861 -48.845 1.00 13.37 ATOM 1881 CD1 LEU B 130 5.718 98.086 -47.935 1.00 17.50 ATOM 1882 CD2 LEU B 130 3.956 99.214 -49.054 1.00 14.42 ATOM 1883 N VAL B 131 5.654 94.887 -48.273 1.00 15.72 ATOM 1884 CA VAL B 131 4.900 93.944 -47.502 1.00 17.44 ATOM 1885 C VAL B 131 4.422 94.588 -46.227 1.00 17.65 ATOM 1886 O VAL B 131 5.232 94.875 -45.390 1.00 18.45 ATOM 1887 CB VAL B 131 5.732 92.787 -47.129 1.00 17.83 ATOM 1888 CG1 VAL B 131 4.857 91.621 -46.696 1.00 20.26 ATOM 1889 CG2 VAL B 131 6.479 92.304 -48.370 1.00 21.52 ATOM 1890 N ARG B 132 3.096 94.764 -46.065 1.00 17.10 ATOM 1891 CA ARG B 132 2.514 95.230 -44.837 1.00 16.49 ATOM 1892 C ARG B 132 2.250 94.041 -43.951 1.00 16.38 ATOM 1893 O ARG B 132 1.486 93.128 -44.288 1.00 17.66 ATOM 1894 CB ARG B 132 1.233 96.053 -45.158 1.00 17.64 ATOM 1895 CG ARG B 132 1.533 97.451 -45.817 1.00 19.05 ATOM 1896 CD ARG B 132 0.175 98.171 -46.138 1.00 22.16 ATOM 1897 NE ARG B 132 0.272 99.465 -46.820 1.00 26.61 ATOM 1898 CZ ARG B 132 1.090 100.473 -46.477 1.00 28.63 ATOM 1899 NH1 ARG B 132 1.978 100.343 -45.482 1.00 24.59 ATOM 1900 NH2 ARG B 132 1.025 101.621 -47.167 1.00 26.04 ATOM 1901 N VAL B 133 2.899 93.957 -42.793 1.00 17.40 ATOM 1902 CA VAL B 133 2.578 92.864 -41.856 1.00 17.03 ATOM 1903 C VAL B 133 1.515 93.263 -40.800 1.00 18.71 ATOM 1904 O VAL B 133 1.548 94.406 -40.251 1.00 20.36 ATOM 1905 CB VAL B 133 3.822 92.297 -41.244 1.00 16.70 ATOM 1906 CG1 VAL B 133 3.556 90.928 -40.665 1.00 16.96 ATOM 1907 CG2 VAL B 133 4.932 92.191 -42.356 1.00 16.40 ATOM 1908 N TYR B 134 0.524 92.392 -40.573 1.00 15.25 ATOM 1909 CA TYR B 134 -0.435 92.626 -39.494 1.00 14.39 ATOM 1910 C TYR B 134 -0.391 91.550 -38.377 1.00 14.65 ATOM 1911 O TYR B 134 -0.665 90.379 -38.641 1.00 16.82 ATOM 1912 CB TYR B 134 -1.813 92.708 -40.093 1.00 12.80 ATOM 1913 CG TYR B 134 -1.924 93.732 -41.220 1.00 11.35 ATOM 1914 CD1 TYR B 134 -1.179 93.601 -42.391 1.00 13.80 ATOM 1915 CD2 TYR B 134 -2.725 94.806 -41.095 1.00 9.74 ATOM 1916 CE1 TYR B 134 -1.221 94.530 -43.377 1.00 12.88 ATOM 1917 CE2 TYR B 134 -2.824 95.757 -42.071 1.00 12.15 ATOM 1918 CZ TYR B 134 -2.126 95.645 -43.251 1.00 15.95 ATOM 1919 OH TYR B 134 -2.229 96.681 -44.278 1.00 10.49 ATOM 1920 N GLU B 135 -0.109 91.959 -37.145 1.00 12.49 ATOM 1921 CA GLU B 135 -0.117 91.142 -35.939 1.00 11.29 ATOM 1922 C GLU B 135 -1.349 91.598 -35.210 1.00 11.63 ATOM 1923 O GLU B 135 -1.486 92.793 -34.824 1.00 11.38 ATOM 1924 CB GLU B 135 1.158 91.467 -35.102 1.00 6.45 ATOM 1925 CG GLU B 135 2.327 91.503 -35.961 1.00 9.85 ATOM 1926 CD GLU B 135 3.631 91.477 -35.138 1.00 15.83 ATOM 1927 OE1 GLU B 135 3.927 90.356 -34.611 1.00 17.06 ATOM 1928 OE2 GLU B 135 4.251 92.551 -34.974 1.00 8.29 ATOM 1929 N ASN B 136 -2.278 90.671 -35.064 1.00 13.39 ATOM 1930 CA ASN B 136 -3.520 90.942 -34.395 1.00 14.33 ATOM 1931 C ASN B 136 -4.244 92.175 -34.980 1.00 15.19 ATOM 1932 O ASN B 136 -4.798 92.970 -34.222 1.00 15.12 ATOM 1933 CB ASN B 136 -3.238 91.057 -32.887 1.00 13.00 ATOM 1934 CG ASN B 136 -2.793 89.706 -32.317 1.00 15.23 ATOM 1935 OD1 ASN B 136 -3.528 88.730 -32.438 1.00 16.81 ATOM 1936 ND2 ASN B 136 -1.577 89.630 -31.783 1.00 8.97 ATOM 1937 N LYS B 137 -4.207 92.305 -36.305 1.00 15.54 ATOM 1938 CA LYS B 137 -4.813 93.461 -36.993 1.00 16.83 ATOM 1939 C LYS B 137 -4.002 94.796 -36.861 1.00 17.35 ATOM 1940 O LYS B 137 -4.584 95.859 -36.880 1.00 17.81 ATOM 1941 CB LYS B 137 -6.211 93.705 -36.484 1.00 16.90 ATOM 1942 CG LYS B 137 -7.126 92.573 -36.869 1.00 17.32 ATOM 1943 CD LYS B 137 -8.365 92.709 -36.102 1.00 16.98 ATOM 1944 CE LYS B 137 -9.354 91.606 -36.404 1.00 13.15 ATOM 1945 NZ LYS B 137 -9.922 91.819 -37.745 1.00 15.50 ATOM 1946 N ARG B 138 -2.684 94.771 -36.745 1.00 16.45 ATOM 1947 CA ARG B 138 -2.027 96.073 -36.683 1.00 16.54 ATOM 1948 C ARG B 138 -0.818 96.168 -37.593 1.00 15.22 ATOM 1949 O ARG B 138 -0.110 95.183 -37.825 1.00 11.80 ATOM 1950 CB ARG B 138 -1.701 96.347 -35.235 1.00 18.53 ATOM 1951 CG ARG B 138 -2.889 96.118 -34.246 1.00 17.08 ATOM 1952 CD ARG B 138 -2.777 97.008 -32.987 1.00 23.06 ATOM 1953 NE ARG B 138 -3.823 96.655 -32.002 1.00 22.86 ATOM 1954 CZ ARG B 138 -4.245 97.403 -31.003 1.00 20.73 ATOM 1955 NH1 ARG B 138 -3.748 98.619 -30.789 1.00 28.49 ATOM 1956 NH2 ARG B 138 -5.168 96.938 -30.191 1.00 21.56 ATOM 1957 N ASN B 139 -0.613 97.325 -38.231 1.00 14.96 ATOM 1958 CA ASN B 139 0.519 97.337 -39.218 1.00 12.56 ATOM 1959 C ASN B 139 1.790 97.520 -38.443 1.00 12.18 ATOM 1960 O ASN B 139 2.277 98.658 -38.204 1.00 12.06 ATOM 1961 CB ASN B 139 0.269 98.289 -40.419 1.00 12.40 ATOM 1962 CG ASN B 139 1.417 98.285 -41.448 1.00 12.13 ATOM 1963 OD1 ASN B 139 1.525 99.198 -42.291 1.00 5.69 ATOM 1964 ND2 ASN B 139 2.212 97.187 -41.462 1.00 8.79 ATOM 1965 N THR B 140 2.331 96.396 -37.975 1.00 9.99 ATOM 1966 CA THR B 140 3.434 96.455 -37.026 1.00 10.22 ATOM 1967 C THR B 140 4.735 96.731 -37.764 1.00 10.78 ATOM 1968 O THR B 140 5.424 97.718 -37.508 1.00 10.37 ATOM 1969 CB THR B 140 3.592 95.116 -36.234 1.00 11.20 ATOM 1970 OG1 THR B 140 3.922 94.053 -37.120 1.00 10.26 ATOM 1971 CG2 THR B 140 2.394 94.746 -35.594 1.00 2.00 ATOM 1972 N ILE B 141 4.992 95.880 -38.747 1.00 11.81 ATOM 1973 CA ILE B 141 6.255 95.790 -39.452 1.00 10.72 ATOM 1974 C ILE B 141 5.875 95.830 -40.951 1.00 12.42 ATOM 1975 O ILE B 141 4.781 95.385 -41.355 1.00 7.30 ATOM 1976 CB ILE B 141 7.065 94.510 -39.006 1.00 11.91 ATOM 1977 CG1 ILE B 141 8.147 94.211 -40.039 1.00 8.86 ATOM 1978 CG2 ILE B 141 6.128 93.292 -38.739 1.00 12.28 ATOM 1979 CD1 ILE B 141 9.167 95.493 -40.257 1.00 3.62 ATOM 1980 N SER B 142 6.709 96.523 -41.742 1.00 14.48 ATOM 1981 CA SER B 142 6.628 96.591 -43.249 1.00 13.70 ATOM 1982 C SER B 142 8.025 96.659 -43.904 1.00 13.12 ATOM 1983 O SER B 142 8.828 97.511 -43.611 1.00 11.14 ATOM 1984 CB SER B 142 5.924 97.861 -43.653 1.00 15.53 ATOM 1985 OG SER B 142 4.702 98.005 -42.923 1.00 14.03 ATOM 1986 N PHE B 143 8.274 95.801 -44.875 1.00 11.99 ATOM 1987 CA PHE B 143 9.587 95.706 -45.468 1.00 11.37 ATOM 1988 C PHE B 143 9.326 95.531 -46.924 1.00 11.45 ATOM 1989 O PHE B 143 8.239 95.761 -47.315 1.00 12.79 ATOM 1990 CB PHE B 143 10.301 94.526 -44.890 1.00 10.71 ATOM 1991 CG PHE B 143 9.560 93.219 -45.002 1.00 9.49 ATOM 1992 CD1 PHE B 143 10.106 92.186 -45.648 1.00 18.65 ATOM 1993 CD2 PHE B 143 8.331 93.022 -44.396 1.00 19.43 ATOM 1994 CE1 PHE B 143 9.481 90.991 -45.773 1.00 12.40 ATOM 1995 CE2 PHE B 143 7.697 91.820 -44.463 1.00 19.98 ATOM 1996 CZ PHE B 143 8.272 90.796 -45.184 1.00 14.91 ATOM 1997 N GLU B 144 10.294 95.092 -47.693 1.00 13.00 ATOM 1998 CA GLU B 144 10.170 94.924 -49.116 1.00 14.00 ATOM 1999 C GLU B 144 10.976 93.757 -49.637 1.00 15.25 ATOM 2000 O GLU B 144 11.881 93.239 -49.002 1.00 15.56 ATOM 2001 CB GLU B 144 10.675 96.141 -49.862 1.00 15.88 ATOM 2002 CG GLU B 144 9.759 97.382 -49.850 1.00 16.61 ATOM 2003 CD GLU B 144 10.582 98.650 -50.076 1.00 25.88 ATOM 2004 OE1 GLU B 144 10.004 99.734 -50.402 1.00 24.45 ATOM 2005 OE2 GLU B 144 11.836 98.527 -49.921 1.00 27.33 ATOM 2006 N VAL B 145 10.655 93.342 -50.842 1.00 16.09 ATOM 2007 CA VAL B 145 11.274 92.161 -51.363 1.00 16.73 ATOM 2008 C VAL B 145 11.813 92.517 -52.690 1.00 16.25 ATOM 2009 O VAL B 145 11.346 93.406 -53.306 1.00 17.89 ATOM 2010 CB VAL B 145 10.275 91.022 -51.474 1.00 14.60 ATOM 2011 CG1 VAL B 145 9.897 90.667 -50.134 1.00 16.65 ATOM 2012 CG2 VAL B 145 8.988 91.435 -52.283 1.00 15.99 ATOM 2013 N GLN B 146 12.814 91.803 -53.152 1.00 17.11 ATOM 2014 CA GLN B 146 13.408 92.204 -54.403 1.00 15.52 ATOM 2015 C GLN B 146 13.434 91.066 -55.360 1.00 14.76 ATOM 2016 O GLN B 146 13.734 89.925 -54.991 1.00 12.62 ATOM 2017 CB GLN B 146 14.852 92.695 -54.164 1.00 15.29 ATOM 2018 CG GLN B 146 14.915 93.883 -53.203 1.00 15.56 ATOM 2019 CD GLN B 146 16.273 94.492 -53.179 1.00 18.50 ATOM 2020 OE1 GLN B 146 17.342 93.781 -53.079 1.00 18.79 ATOM 2021 NE2 GLN B 146 16.291 95.800 -53.332 1.00 18.71 ATOM 2022 N THR B 147 13.218 91.384 -56.629 1.00 14.53 ATOM 2023 CA THR B 147 13.246 90.289 -57.663 1.00 12.61 ATOM 2024 C THR B 147 13.786 90.853 -59.005 1.00 11.23 ATOM 2025 O THR B 147 13.910 92.079 -59.168 1.00 10.99 ATOM 2026 CB THR B 147 11.877 89.794 -57.949 1.00 11.13 ATOM 2027 OG1 THR B 147 11.982 88.639 -58.863 1.00 11.61 ATOM 2028 CG2 THR B 147 11.081 90.946 -58.616 1.00 5.83 ATOM 2029 N ASP B 148 14.115 89.978 -59.937 1.00 10.18 ATOM 2030 CA ASP B 148 14.563 90.373 -61.257 1.00 10.48 ATOM 2031 C ASP B 148 13.474 90.219 -62.298 1.00 11.60 ATOM 2032 O ASP B 148 13.622 90.804 -63.393 1.00 12.41 ATOM 2033 CB ASP B 148 15.841 89.592 -61.685 1.00 9.84 ATOM 2034 CG ASP B 148 15.558 88.075 -61.807 1.00 11.48 ATOM 2035 OD1 ASP B 148 16.421 87.265 -62.192 1.00 4.81 ATOM 2036 OD2 ASP B 148 14.466 87.683 -61.423 1.00 7.10 ATOM 2037 N LYS B 149 12.332 89.534 -61.997 1.00 11.88 ATOM 2038 CA LYS B 149 11.258 89.381 -62.974 1.00 10.08 ATOM 2039 C LYS B 149 10.382 90.661 -63.193 1.00 11.09 ATOM 2040 O LYS B 149 10.161 91.470 -62.235 1.00 12.10 ATOM 2041 CB LYS B 149 10.389 88.174 -62.594 1.00 11.55 ATOM 2042 CG LYS B 149 11.188 87.045 -61.819 1.00 7.50 ATOM 2043 CD LYS B 149 12.368 86.532 -62.637 1.00 2.00 ATOM 2044 CE LYS B 149 12.881 85.112 -62.243 1.00 3.24 ATOM 2045 NZ LYS B 149 13.152 84.927 -60.827 1.00 2.00 ATOM 2046 N LYS B 150 9.764 90.813 -64.379 1.00 10.58 ATOM 2047 CA LYS B 150 8.923 92.106 -64.677 1.00 9.53 ATOM 2048 C LYS B 150 7.539 91.632 -64.457 1.00 11.23 ATOM 2049 O LYS B 150 6.500 92.418 -64.529 1.00 10.14 ATOM 2050 CB LYS B 150 9.052 92.532 -66.136 1.00 4.52 ATOM 2051 CG LYS B 150 8.851 94.008 -66.451 1.00 13.20 ATOM 2052 CD LYS B 150 9.400 94.300 -67.839 1.00 9.55 ATOM 2053 CE LYS B 150 10.997 94.288 -67.822 1.00 4.98 ATOM 2054 NZ LYS B 150 11.424 94.556 -69.223 1.00 4.30 ATOM 2055 N SER B 151 7.503 90.300 -64.323 1.00 9.23 ATOM 2056 CA SER B 151 6.316 89.645 -63.928 1.00 10.30 ATOM 2057 C SER B 151 6.768 88.289 -63.338 1.00 11.72 ATOM 2058 O SER B 151 7.337 87.448 -64.084 1.00 8.10 ATOM 2059 CB SER B 151 5.377 89.450 -65.116 1.00 10.96 ATOM 2060 OG SER B 151 4.585 88.212 -64.909 1.00 14.65 ATOM 2061 N VAL B 152 6.455 88.057 -62.037 1.00 11.10 ATOM 2062 CA VAL B 152 7.048 86.941 -61.284 1.00 9.74 ATOM 2063 C VAL B 152 6.031 86.059 -60.641 1.00 10.99 ATOM 2064 O VAL B 152 4.885 86.505 -60.445 1.00 6.61 ATOM 2065 CB VAL B 152 7.801 87.481 -60.116 1.00 9.35 ATOM 2066 CG1 VAL B 152 6.878 88.376 -59.353 1.00 11.35 ATOM 2067 CG2 VAL B 152 8.253 86.384 -59.300 1.00 13.03 ATOM 2068 N THR B 153 6.510 84.848 -60.248 1.00 11.20 ATOM 2069 CA THR B 153 5.698 83.768 -59.709 1.00 11.26 ATOM 2070 C THR B 153 5.340 84.185 -58.299 1.00 12.21 ATOM 2071 O THR B 153 6.251 84.416 -57.503 1.00 12.96 ATOM 2072 CB THR B 153 6.433 82.432 -59.655 1.00 11.29 ATOM 2073 OG1 THR B 153 7.814 82.597 -59.311 1.00 11.34 ATOM 2074 CG2 THR B 153 6.466 81.805 -60.952 1.00 12.78 ATOM 2075 N ALA B 154 4.019 84.290 -57.955 1.00 12.08 ATOM 2076 CA ALA B 154 3.649 84.533 -56.565 1.00 9.26 ATOM 2077 C ALA B 154 4.533 83.702 -55.618 1.00 11.16 ATOM 2078 O ALA B 154 4.940 84.181 -54.553 1.00 12.36 ATOM 2079 CB ALA B 154 2.205 84.209 -56.320 1.00 9.88 ATOM 2080 N GLN B 155 4.785 82.440 -55.964 1.00 12.24 ATOM 2081 CA GLN B 155 5.619 81.588 -55.156 1.00 11.20 ATOM 2082 C GLN B 155 6.899 82.299 -54.858 1.00 11.78 ATOM 2083 O GLN B 155 7.191 82.525 -53.686 1.00 12.77 ATOM 2084 CB GLN B 155 5.908 80.251 -55.863 1.00 11.22 ATOM 2085 CG GLN B 155 6.855 79.389 -55.121 1.00 9.44 ATOM 2086 CD GLN B 155 6.851 78.024 -55.598 1.00 12.25 ATOM 2087 OE1 GLN B 155 7.563 77.137 -55.072 1.00 14.74 ATOM 2088 NE2 GLN B 155 6.021 77.785 -56.576 1.00 12.35 ATOM 2089 N GLU B 156 7.640 82.714 -55.879 1.00 12.68 ATOM 2090 CA GLU B 156 8.891 83.439 -55.654 1.00 11.50 ATOM 2091 C GLU B 156 8.637 84.443 -54.618 1.00 10.38 ATOM 2092 O GLU B 156 9.384 84.522 -53.634 1.00 12.43 ATOM 2093 CB GLU B 156 9.405 84.209 -56.862 1.00 11.73 ATOM 2094 CG GLU B 156 10.798 84.824 -56.532 1.00 10.22 ATOM 2095 CD GLU B 156 11.506 85.410 -57.710 1.00 10.70 ATOM 2096 OE1 GLU B 156 12.296 86.337 -57.499 1.00 10.68 ATOM 2097 OE2 GLU B 156 11.198 85.056 -58.862 1.00 10.69 ATOM 2098 N LEU B 157 7.605 85.247 -54.803 1.00 9.38 ATOM 2099 CA LEU B 157 7.452 86.402 -53.926 1.00 6.92 ATOM 2100 C LEU B 157 7.151 85.981 -52.523 1.00 9.33 ATOM 2101 O LEU B 157 7.821 86.443 -51.555 1.00 7.71 ATOM 2102 CB LEU B 157 6.296 87.275 -54.392 1.00 7.19 ATOM 2103 CG LEU B 157 6.432 88.273 -55.528 1.00 4.70 ATOM 2104 CD1 LEU B 157 5.233 89.109 -55.484 1.00 9.57 ATOM 2105 CD2 LEU B 157 7.750 89.060 -55.364 1.00 2.23 ATOM 2106 N ASP B 158 6.125 85.108 -52.393 1.00 6.81 ATOM 2107 CA ASP B 158 5.819 84.524 -51.116 1.00 9.26 ATOM 2108 C ASP B 158 7.054 84.005 -50.379 1.00 9.19 ATOM 2109 O ASP B 158 7.252 84.374 -49.231 1.00 8.82 ATOM 2110 CB ASP B 158 4.784 83.418 -51.365 1.00 11.98 ATOM 2111 CG ASP B 158 4.422 82.679 -50.145 1.00 16.30 ATOM 2112 OD1 ASP B 158 3.748 83.262 -49.219 1.00 14.32 ATOM 2113 OD2 ASP B 158 4.880 81.525 -50.123 1.00 19.46 ATOM 2114 N ILE B 159 7.863 83.122 -51.007 1.00 9.30 ATOM 2115 CA ILE B 159 8.998 82.477 -50.346 1.00 8.37 ATOM 2116 C ILE B 159 9.803 83.588 -49.644 1.00 10.33 ATOM 2117 O ILE B 159 9.997 83.623 -48.443 1.00 7.57 ATOM 2118 CB ILE B 159 9.929 81.735 -51.351 1.00 11.06 ATOM 2119 CG1 ILE B 159 9.363 80.388 -51.909 1.00 7.96 ATOM 2120 CG2 ILE B 159 11.177 81.314 -50.633 1.00 9.39 ATOM 2121 CD1 ILE B 159 7.844 80.183 -51.454 1.00 17.04 ATOM 2122 N LYS B 160 10.165 84.572 -50.452 1.00 11.82 ATOM 2123 CA LYS B 160 11.039 85.659 -50.114 1.00 11.64 ATOM 2124 C LYS B 160 10.470 86.359 -48.872 1.00 11.98 ATOM 2125 O LYS B 160 11.216 86.627 -47.920 1.00 12.74 ATOM 2126 CB LYS B 160 11.194 86.610 -51.340 1.00 12.67 ATOM 2127 CG LYS B 160 12.181 86.122 -52.431 1.00 9.61 ATOM 2128 CD LYS B 160 12.580 87.203 -53.487 1.00 11.23 ATOM 2129 CE LYS B 160 13.616 86.635 -54.541 1.00 9.99 ATOM 2130 NZ LYS B 160 14.115 87.376 -55.820 1.00 5.35 ATOM 2131 N ALA B 161 9.146 86.534 -48.838 1.00 12.01 ATOM 2132 CA ALA B 161 8.426 87.120 -47.715 1.00 11.13 ATOM 2133 C ALA B 161 8.716 86.295 -46.441 1.00 11.55 ATOM 2134 O ALA B 161 9.305 86.799 -45.452 1.00 9.66 ATOM 2135 CB ALA B 161 6.886 87.065 -48.056 1.00 12.32 ATOM 2136 N ARG B 162 8.197 85.055 -46.442 1.00 11.54 ATOM 2137 CA ARG B 162 8.422 84.079 -45.400 1.00 9.79 ATOM 2138 C ARG B 162 9.892 83.993 -44.978 1.00 9.42 ATOM 2139 O ARG B 162 10.168 84.068 -43.811 1.00 10.61 ATOM 2140 CB ARG B 162 7.896 82.740 -45.885 1.00 10.88 ATOM 2141 CG ARG B 162 6.352 82.681 -45.804 1.00 13.06 ATOM 2142 CD ARG B 162 5.850 81.273 -46.220 1.00 10.66 ATOM 2143 NE ARG B 162 4.394 81.194 -46.520 1.00 10.75 ATOM 2144 CZ ARG B 162 3.785 80.040 -46.788 1.00 9.56 ATOM 2145 NH1 ARG B 162 4.494 78.951 -46.798 1.00 8.33 ATOM 2146 NH2 ARG B 162 2.508 79.945 -47.064 1.00 10.35 ATOM 2147 N ASN B 163 10.835 83.795 -45.876 1.00 10.21 ATOM 2148 CA ASN B 163 12.235 83.716 -45.525 1.00 12.67 ATOM 2149 C ASN B 163 12.604 84.864 -44.587 1.00 15.05 ATOM 2150 O ASN B 163 13.316 84.622 -43.558 1.00 17.57 ATOM 2151 CB ASN B 163 13.070 83.786 -46.788 1.00 14.36 ATOM 2152 CG ASN B 163 14.512 83.980 -46.551 1.00 14.15 ATOM 2153 OD1 ASN B 163 15.211 83.055 -46.280 1.00 11.96 ATOM 2154 ND2 ASN B 163 15.004 85.206 -46.822 1.00 24.48 ATOM 2155 N PHE B 164 12.080 86.093 -44.849 1.00 15.44 ATOM 2156 CA PHE B 164 12.399 87.286 -44.019 1.00 15.88 ATOM 2157 C PHE B 164 11.749 87.102 -42.681 1.00 16.37 ATOM 2158 O PHE B 164 12.455 87.126 -41.657 1.00 16.67 ATOM 2159 CB PHE B 164 11.861 88.609 -44.588 1.00 17.00 ATOM 2160 CG PHE B 164 12.462 89.877 -43.968 1.00 14.90 ATOM 2161 CD1 PHE B 164 13.725 90.325 -44.338 1.00 13.56 ATOM 2162 CD2 PHE B 164 11.668 90.727 -43.203 1.00 15.63 ATOM 2163 CE1 PHE B 164 14.224 91.559 -43.866 1.00 13.87 ATOM 2164 CE2 PHE B 164 12.157 91.868 -42.730 1.00 19.60 ATOM 2165 CZ PHE B 164 13.479 92.294 -43.064 1.00 18.93 ATOM 2166 N LEU B 165 10.410 86.953 -42.669 1.00 15.37 ATOM 2167 CA LEU B 165 9.702 86.666 -41.401 1.00 13.55 ATOM 2168 C LEU B 165 10.424 85.562 -40.539 1.00 13.06 ATOM 2169 O LEU B 165 10.520 85.713 -39.307 1.00 11.08 ATOM 2170 CB LEU B 165 8.245 86.377 -41.674 1.00 13.17 ATOM 2171 CG LEU B 165 7.361 87.729 -41.740 1.00 13.02 ATOM 2172 CD1 LEU B 165 8.178 89.013 -41.878 1.00 11.78 ATOM 2173 CD2 LEU B 165 6.474 87.628 -42.851 1.00 6.61 ATOM 2174 N ILE B 166 10.884 84.469 -41.152 1.00 11.42 ATOM 2175 CA ILE B 166 11.692 83.493 -40.416 1.00 11.67 ATOM 2176 C ILE B 166 12.885 84.313 -39.938 1.00 10.13 ATOM 2177 O ILE B 166 13.040 84.607 -38.744 1.00 10.32 ATOM 2178 CB ILE B 166 12.252 82.345 -41.291 1.00 11.20 ATOM 2179 CG1 ILE B 166 11.249 81.284 -41.675 1.00 11.84 ATOM 2180 CG2 ILE B 166 13.248 81.641 -40.507 1.00 11.60 ATOM 2181 CD1 ILE B 166 9.884 81.831 -42.041 1.00 22.91 ATOM 2182 N ASN B 167 13.770 84.714 -40.837 1.00 11.87 ATOM 2183 CA ASN B 167 14.978 85.474 -40.340 1.00 14.05 ATOM 2184 C ASN B 167 14.829 86.695 -39.391 1.00 12.90 ATOM 2185 O ASN B 167 15.831 87.273 -38.896 1.00 13.51 ATOM 2186 CB ASN B 167 15.834 85.843 -41.520 1.00 14.78 ATOM 2187 CG ASN B 167 16.375 84.558 -42.230 1.00 19.05 ATOM 2188 OD1 ASN B 167 15.645 83.560 -42.347 1.00 14.46 ATOM 2189 ND2 ASN B 167 17.676 84.566 -42.610 1.00 19.30 ATOM 2190 N LYS B 168 13.615 87.148 -39.125 1.00 11.26 ATOM 2191 CA LYS B 168 13.500 88.395 -38.258 1.00 11.77 ATOM 2192 C LYS B 168 12.337 88.450 -37.256 1.00 12.15 ATOM 2193 O LYS B 168 12.322 89.311 -36.316 1.00 12.84 ATOM 2194 CB LYS B 168 13.505 89.680 -39.095 1.00 9.20 ATOM 2195 CG LYS B 168 14.681 89.812 -40.078 1.00 10.37 ATOM 2196 CD LYS B 168 15.794 90.757 -39.535 1.00 8.01 ATOM 2197 CE LYS B 168 17.213 90.346 -40.138 1.00 15.79 ATOM 2198 NZ LYS B 168 17.281 88.821 -40.091 1.00 16.18 ATOM 2199 N LYS B 169 11.339 87.613 -37.467 1.00 13.05 ATOM 2200 CA LYS B 169 10.094 87.567 -36.613 1.00 12.54 ATOM 2201 C LYS B 169 9.630 86.120 -36.246 1.00 13.48 ATOM 2202 O LYS B 169 8.418 85.868 -35.965 1.00 10.89 ATOM 2203 CB LYS B 169 8.916 88.327 -37.262 1.00 13.42 ATOM 2204 CG LYS B 169 8.749 89.804 -36.680 1.00 17.03 ATOM 2205 CD LYS B 169 7.947 89.896 -35.456 1.00 14.89 ATOM 2206 CE LYS B 169 7.454 91.335 -35.199 1.00 16.37 ATOM 2207 NZ LYS B 169 6.425 91.315 -34.085 1.00 15.63 ATOM 2208 N ASN B 170 10.593 85.201 -36.191 1.00 12.08 ATOM 2209 CA ASN B 170 10.322 83.812 -35.828 1.00 12.48 ATOM 2210 C ASN B 170 9.004 83.244 -36.324 1.00 12.71 ATOM 2211 O ASN B 170 8.240 82.589 -35.537 1.00 14.21 ATOM 2212 CB ASN B 170 10.468 83.548 -34.334 1.00 11.37 ATOM 2213 CG ASN B 170 11.920 83.693 -33.827 1.00 17.78 ATOM 2214 OD1 ASN B 170 12.516 84.844 -33.851 1.00 15.93 ATOM 2215 ND2 ASN B 170 12.530 82.540 -33.361 1.00 15.97 ATOM 2216 N LEU B 171 8.770 83.362 -37.618 1.00 12.00 ATOM 2217 CA LEU B 171 7.446 82.934 -38.152 1.00 13.94 ATOM 2218 C LEU B 171 7.249 81.443 -37.909 1.00 12.54 ATOM 2219 O LEU B 171 6.137 81.008 -37.725 1.00 12.15 ATOM 2220 CB LEU B 171 7.261 83.317 -39.637 1.00 13.40 ATOM 2221 CG LEU B 171 6.274 82.567 -40.512 1.00 14.34 ATOM 2222 CD1 LEU B 171 4.844 83.009 -40.145 1.00 7.49 ATOM 2223 CD2 LEU B 171 6.735 82.999 -41.949 1.00 8.00 ATOM 2224 N TYR B 172 8.341 80.728 -37.855 1.00 10.81 ATOM 2225 CA TYR B 172 8.365 79.256 -37.737 1.00 11.68 ATOM 2226 C TYR B 172 9.645 79.034 -36.906 1.00 12.20 ATOM 2227 O TYR B 172 10.677 79.740 -37.096 1.00 10.17 ATOM 2228 CB TYR B 172 8.570 78.541 -39.088 1.00 11.85 ATOM 2229 CG TYR B 172 7.468 78.762 -40.131 1.00 9.76 ATOM 2230 CD1 TYR B 172 7.741 79.149 -41.451 1.00 7.06 ATOM 2231 CD2 TYR B 172 6.145 78.621 -39.779 1.00 10.34 ATOM 2232 CE1 TYR B 172 6.648 79.451 -42.338 1.00 9.66 ATOM 2233 CE2 TYR B 172 5.073 78.813 -40.713 1.00 4.52 ATOM 2234 CZ TYR B 172 5.331 79.239 -41.922 1.00 7.82 ATOM 2235 OH TYR B 172 4.253 79.404 -42.710 1.00 8.43 ATOM 2236 N GLU B 173 9.500 78.171 -35.925 1.00 10.42 ATOM 2237 CA GLU B 173 10.576 77.696 -35.098 1.00 10.75 ATOM 2238 C GLU B 173 10.569 76.151 -35.102 1.00 8.85 ATOM 2239 O GLU B 173 9.491 75.561 -35.281 1.00 8.01 ATOM 2240 CB GLU B 173 10.446 78.222 -33.678 1.00 10.73 ATOM 2241 CG GLU B 173 11.265 79.448 -33.450 1.00 12.19 ATOM 2242 CD GLU B 173 11.168 80.039 -32.022 1.00 15.69 ATOM 2243 OE1 GLU B 173 10.013 80.268 -31.509 1.00 15.58 ATOM 2244 OE2 GLU B 173 12.274 80.389 -31.525 1.00 12.51 ATOM 2245 N PHE B 174 11.758 75.549 -34.925 1.00 6.15 ATOM 2246 CA PHE B 174 11.932 74.151 -34.929 1.00 8.07 ATOM 2247 C PHE B 174 10.870 73.308 -34.207 1.00 9.68 ATOM 2248 O PHE B 174 10.626 72.209 -34.646 1.00 9.78 ATOM 2249 CB PHE B 174 13.303 73.732 -34.570 1.00 7.52 ATOM 2250 CG PHE B 174 13.510 72.266 -34.568 1.00 5.79 ATOM 2251 CD1 PHE B 174 14.065 71.623 -35.663 1.00 14.25 ATOM 2252 CD2 PHE B 174 13.263 71.536 -33.446 1.00 9.44 ATOM 2253 CE1 PHE B 174 14.391 70.235 -35.653 1.00 10.77 ATOM 2254 CE2 PHE B 174 13.485 70.101 -33.390 1.00 10.57 ATOM 2255 CZ PHE B 174 14.040 69.450 -34.497 1.00 12.18 ATOM 2256 N ASN B 175 10.204 73.806 -33.170 1.00 12.47 ATOM 2257 CA ASN B 175 9.083 73.005 -32.528 1.00 13.00 ATOM 2258 C ASN B 175 7.697 73.473 -32.777 1.00 12.75 ATOM 2259 O ASN B 175 6.675 72.740 -32.556 1.00 16.51 ATOM 2260 CB ASN B 175 9.316 72.909 -31.030 1.00 12.93 ATOM 2261 CG ASN B 175 10.835 72.902 -30.648 1.00 19.64 ATOM 2262 OD1 ASN B 175 11.562 73.894 -30.895 1.00 24.36 ATOM 2263 ND2 ASN B 175 11.309 71.787 -30.048 1.00 18.24 ATOM 2264 N SER B 176 7.597 74.751 -33.083 1.00 12.74 ATOM 2265 CA SER B 176 6.358 75.376 -33.393 1.00 12.21 ATOM 2266 C SER B 176 6.504 76.858 -33.733 1.00 12.97 ATOM 2267 O SER B 176 7.577 77.313 -34.215 1.00 13.11 ATOM 2268 CB SER B 176 5.358 75.164 -32.278 1.00 14.14 ATOM 2269 OG SER B 176 4.137 75.662 -32.658 1.00 7.94 ATOM 2270 N SER B 177 5.427 77.594 -33.519 1.00 10.45 ATOM 2271 CA SER B 177 5.393 79.010 -33.915 1.00 12.73 ATOM 2272 C SER B 177 4.541 79.885 -32.965 1.00 12.63 ATOM 2273 O SER B 177 3.448 79.464 -32.507 1.00 11.87 ATOM 2274 CB SER B 177 4.833 79.114 -35.350 1.00 12.31 ATOM 2275 OG SER B 177 5.052 80.370 -35.936 1.00 11.70 ATOM 2276 N PRO B 178 5.080 81.076 -32.644 1.00 12.02 ATOM 2277 CA PRO B 178 4.547 82.091 -31.802 1.00 9.04 ATOM 2278 C PRO B 178 3.199 82.494 -32.270 1.00 8.64 ATOM 2279 O PRO B 178 2.496 83.197 -31.526 1.00 10.15 ATOM 2280 CB PRO B 178 5.504 83.279 -32.044 1.00 6.82 ATOM 2281 CG PRO B 178 6.732 82.693 -32.542 1.00 10.75 ATOM 2282 CD PRO B 178 6.362 81.497 -33.266 1.00 10.69 ATOM 2283 N TYR B 179 2.828 82.127 -33.485 1.00 8.35 ATOM 2284 CA TYR B 179 1.535 82.531 -34.083 1.00 7.55 ATOM 2285 C TYR B 179 0.545 81.338 -34.147 1.00 9.22 ATOM 2286 O TYR B 179 0.978 80.119 -34.091 1.00 7.45 ATOM 2287 CB TYR B 179 1.749 83.185 -35.439 1.00 7.94 ATOM 2288 CG TYR B 179 2.835 84.308 -35.407 1.00 9.55 ATOM 2289 CD1 TYR B 179 4.125 84.015 -35.696 1.00 4.63 ATOM 2290 CD2 TYR B 179 2.489 85.691 -35.052 1.00 5.68 ATOM 2291 CE1 TYR B 179 5.148 85.040 -35.661 1.00 9.84 ATOM 2292 CE2 TYR B 179 3.437 86.672 -35.060 1.00 10.92 ATOM 2293 CZ TYR B 179 4.731 86.347 -35.363 1.00 7.69 ATOM 2294 OH TYR B 179 5.601 87.296 -35.362 1.00 11.82 ATOM 2295 N GLU B 180 -0.758 81.659 -34.154 1.00 7.58 ATOM 2296 CA GLU B 180 -1.771 80.611 -34.103 1.00 8.20 ATOM 2297 C GLU B 180 -2.225 80.392 -35.524 1.00 9.69 ATOM 2298 O GLU B 180 -2.495 79.213 -35.937 1.00 12.55 ATOM 2299 CB GLU B 180 -2.968 81.073 -33.226 1.00 9.88 ATOM 2300 CG GLU B 180 -4.214 80.055 -33.074 1.00 7.74 ATOM 2301 CD GLU B 180 -3.815 78.698 -32.652 1.00 14.00 ATOM 2302 OE1 GLU B 180 -4.718 77.859 -32.381 1.00 13.19 ATOM 2303 OE2 GLU B 180 -2.594 78.441 -32.539 1.00 14.28 ATOM 2304 N THR B 181 -2.340 81.495 -36.291 1.00 7.35 ATOM 2305 CA THR B 181 -2.758 81.443 -37.668 1.00 5.80 ATOM 2306 C THR B 181 -2.063 82.479 -38.501 1.00 8.40 ATOM 2307 O THR B 181 -1.553 83.505 -37.992 1.00 8.91 ATOM 2308 CB THR B 181 -4.217 81.805 -37.857 1.00 6.75 ATOM 2309 OG1 THR B 181 -4.375 83.227 -37.709 1.00 3.57 ATOM 2310 CG2 THR B 181 -5.036 81.183 -36.781 1.00 9.08 ATOM 2311 N GLY B 182 -2.142 82.311 -39.822 1.00 10.56 ATOM 2312 CA GLY B 182 -1.544 83.286 -40.758 1.00 10.08 ATOM 2313 C GLY B 182 -1.610 82.947 -42.226 1.00 9.33 ATOM 2314 O GLY B 182 -1.493 81.779 -42.637 1.00 11.90 ATOM 2315 N TYR B 183 -1.868 83.965 -43.020 1.00 10.65 ATOM 2316 CA TYR B 183 -2.120 83.795 -44.454 1.00 9.89 ATOM 2317 C TYR B 183 -1.543 84.942 -45.226 1.00 8.57 ATOM 2318 O TYR B 183 -1.530 86.077 -44.750 1.00 9.83 ATOM 2319 CB TYR B 183 -3.624 83.631 -44.720 1.00 9.39 ATOM 2320 CG TYR B 183 -4.399 84.770 -44.286 1.00 8.52 ATOM 2321 CD1 TYR B 183 -4.479 85.875 -45.086 1.00 11.80 ATOM 2322 CD2 TYR B 183 -5.080 84.771 -43.095 1.00 10.88 ATOM 2323 CE1 TYR B 183 -5.115 86.953 -44.720 1.00 6.52 ATOM 2324 CE2 TYR B 183 -5.779 85.899 -42.704 1.00 12.75 ATOM 2325 CZ TYR B 183 -5.731 87.021 -43.535 1.00 11.06 ATOM 2326 OH TYR B 183 -6.374 88.211 -43.253 1.00 7.67 ATOM 2327 N ILE B 184 -1.031 84.654 -46.405 1.00 9.90 ATOM 2328 CA ILE B 184 -0.388 85.700 -47.205 1.00 10.65 ATOM 2329 C ILE B 184 -1.317 86.012 -48.368 1.00 11.31 ATOM 2330 O ILE B 184 -1.555 85.121 -49.199 1.00 11.43 ATOM 2331 CB ILE B 184 1.035 85.376 -47.623 1.00 9.55 ATOM 2332 CG1 ILE B 184 1.540 86.523 -48.481 1.00 11.59 ATOM 2333 CG2 ILE B 184 1.133 84.079 -48.420 1.00 7.45 ATOM 2334 CD1 ILE B 184 3.055 86.502 -48.734 1.00 2.00 ATOM 2335 N LYS B 185 -1.922 87.214 -48.352 1.00 11.47 ATOM 2336 CA LYS B 185 -2.835 87.668 -49.404 1.00 10.17 ATOM 2337 C LYS B 185 -2.159 88.672 -50.310 1.00 10.31 ATOM 2338 O LYS B 185 -1.532 89.563 -49.758 1.00 9.95 ATOM 2339 CB LYS B 185 -4.051 88.357 -48.798 1.00 9.79 ATOM 2340 CG LYS B 185 -4.768 89.267 -49.747 1.00 6.30 ATOM 2341 CD LYS B 185 -5.563 90.327 -48.982 1.00 10.91 ATOM 2342 CE LYS B 185 -6.862 89.796 -48.284 1.00 7.86 ATOM 2343 NZ LYS B 185 -7.989 89.703 -49.318 1.00 5.30 ATOM 2344 N PHE B 186 -2.414 88.522 -51.635 1.00 9.12 ATOM 2345 CA PHE B 186 -1.964 89.335 -52.784 1.00 10.62 ATOM 2346 C PHE B 186 -3.098 90.156 -53.455 1.00 12.24 ATOM 2347 O PHE B 186 -4.298 89.748 -53.549 1.00 10.76 ATOM 2348 CB PHE B 186 -1.213 88.516 -53.906 1.00 9.75 ATOM 2349 CG PHE B 186 0.022 87.762 -53.438 1.00 9.80 ATOM 2350 CD1 PHE B 186 -0.134 86.622 -52.682 1.00 11.65 ATOM 2351 CD2 PHE B 186 1.306 88.160 -53.817 1.00 3.11 ATOM 2352 CE1 PHE B 186 0.994 85.877 -52.255 1.00 16.27 ATOM 2353 CE2 PHE B 186 2.389 87.450 -53.410 1.00 15.26 ATOM 2354 CZ PHE B 186 2.244 86.292 -52.600 1.00 6.63 ATOM 2355 N ILE B 187 -2.700 91.335 -53.942 1.00 11.90 ATOM 2356 CA ILE B 187 -3.582 92.250 -54.580 1.00 12.57 ATOM 2357 C ILE B 187 -3.041 92.600 -55.941 1.00 14.79 ATOM 2358 O ILE B 187 -1.846 93.039 -56.077 1.00 16.42 ATOM 2359 CB ILE B 187 -3.715 93.431 -53.735 1.00 13.01 ATOM 2360 CG1 ILE B 187 -4.226 93.007 -52.311 1.00 16.00 ATOM 2361 CG2 ILE B 187 -4.758 94.386 -54.373 1.00 15.42 ATOM 2362 CD1 ILE B 187 -4.528 94.141 -51.308 1.00 10.51 ATOM 2363 N GLU B 188 -3.836 92.355 -56.982 1.00 15.05 ATOM 2364 CA GLU B 188 -3.408 92.707 -58.334 1.00 14.95 ATOM 2365 C GLU B 188 -4.027 94.071 -58.816 1.00 19.36 ATOM 2366 O GLU B 188 -5.206 94.374 -58.606 1.00 18.43 ATOM 2367 CB GLU B 188 -3.804 91.576 -59.273 1.00 17.01 ATOM 2368 CG GLU B 188 -2.806 90.476 -59.373 1.00 12.13 ATOM 2369 CD GLU B 188 -3.221 89.365 -60.378 1.00 13.05 ATOM 2370 OE1 GLU B 188 -4.321 88.737 -60.229 1.00 10.21 ATOM 2371 OE2 GLU B 188 -2.443 89.176 -61.327 1.00 10.67 ATOM 2372 N ASN B 189 -3.182 94.892 -59.418 1.00 19.45 ATOM 2373 CA ASN B 189 -3.527 96.195 -59.949 1.00 20.35 ATOM 2374 C ASN B 189 -4.976 96.278 -60.436 1.00 20.82 ATOM 2375 O ASN B 189 -5.691 97.232 -60.105 1.00 20.40 ATOM 2376 CB ASN B 189 -2.462 96.539 -61.019 1.00 20.40 ATOM 2377 CG ASN B 189 -2.371 97.982 -61.313 1.00 22.90 ATOM 2378 OD1 ASN B 189 -1.446 98.399 -62.053 1.00 19.48 ATOM 2379 ND2 ASN B 189 -3.348 98.783 -60.807 1.00 20.53 ATOM 2380 N ASN B 190 -5.448 95.201 -61.065 1.00 22.20 ATOM 2381 CA ASN B 190 -6.825 95.098 -61.558 1.00 24.24 ATOM 2382 C ASN B 190 -7.914 95.023 -60.459 1.00 24.69 ATOM 2383 O ASN B 190 -9.077 95.542 -60.629 1.00 25.12 ATOM 2384 CB ASN B 190 -6.974 93.922 -62.575 1.00 22.98 ATOM 2385 CG ASN B 190 -6.899 92.603 -61.943 1.00 24.78 ATOM 2386 OD1 ASN B 190 -7.526 92.379 -60.912 1.00 22.45 ATOM 2387 ND2 ASN B 190 -6.111 91.662 -62.565 1.00 29.35 ATOM 2388 N GLY B 191 -7.535 94.384 -59.353 1.00 23.82 ATOM 2389 CA GLY B 191 -8.432 94.063 -58.212 1.00 23.15 ATOM 2390 C GLY B 191 -8.493 92.564 -57.899 1.00 22.31 ATOM 2391 O GLY B 191 -9.385 92.085 -57.250 1.00 22.97 ATOM 2392 N ASN B 192 -7.533 91.811 -58.346 1.00 21.65 ATOM 2393 CA ASN B 192 -7.634 90.412 -58.000 1.00 22.72 ATOM 2394 C ASN B 192 -6.888 90.259 -56.722 1.00 21.77 ATOM 2395 O ASN B 192 -5.828 90.871 -56.502 1.00 22.82 ATOM 2396 CB ASN B 192 -7.213 89.485 -59.140 1.00 22.16 ATOM 2397 CG ASN B 192 -7.340 88.019 -58.780 1.00 23.83 ATOM 2398 OD1 ASN B 192 -8.445 87.499 -58.582 1.00 28.16 ATOM 2399 ND2 ASN B 192 -6.202 87.341 -58.688 1.00 15.99 ATOM 2400 N THR B 193 -7.516 89.556 -55.813 1.00 22.25 ATOM 2401 CA THR B 193 -6.939 89.344 -54.528 1.00 23.00 ATOM 2402 C THR B 193 -7.088 87.890 -54.172 1.00 22.98 ATOM 2403 O THR B 193 -8.237 87.347 -54.187 1.00 23.92 ATOM 2404 CB THR B 193 -7.653 90.154 -53.441 1.00 24.01 ATOM 2405 OG1 THR B 193 -9.071 89.922 -53.495 1.00 27.20 ATOM 2406 CG2 THR B 193 -7.330 91.673 -53.524 1.00 25.14 ATOM 2407 N PHE B 194 -5.977 87.264 -53.775 1.00 20.38 ATOM 2408 CA PHE B 194 -6.001 85.844 -53.397 1.00 19.18 ATOM 2409 C PHE B 194 -5.067 85.592 -52.208 1.00 18.89 ATOM 2410 O PHE B 194 -4.134 86.334 -51.997 1.00 21.99 ATOM 2411 CB PHE B 194 -5.628 84.944 -54.586 1.00 17.29 ATOM 2412 CG PHE B 194 -4.247 85.218 -55.194 1.00 18.77 ATOM 2413 CD1 PHE B 194 -3.169 84.380 -54.924 1.00 12.76 ATOM 2414 CD2 PHE B 194 -4.047 86.286 -56.084 1.00 13.96 ATOM 2415 CE1 PHE B 194 -1.951 84.623 -55.515 1.00 11.06 ATOM 2416 CE2 PHE B 194 -2.787 86.529 -56.635 1.00 12.71 ATOM 2417 CZ PHE B 194 -1.763 85.671 -56.366 1.00 8.39 ATOM 2418 N TRP B 195 -5.338 84.619 -51.381 1.00 17.64 ATOM 2419 CA TRP B 195 -4.539 84.404 -50.150 1.00 16.18 ATOM 2420 C TRP B 195 -4.153 82.918 -50.037 1.00 15.37 ATOM 2421 O TRP B 195 -4.823 82.064 -50.592 1.00 17.63 ATOM 2422 CB TRP B 195 -5.301 84.892 -48.904 1.00 15.52 ATOM 2423 CG TRP B 195 -6.663 84.153 -48.565 1.00 13.57 ATOM 2424 CD1 TRP B 195 -7.938 84.485 -48.996 1.00 16.11 ATOM 2425 CD2 TRP B 195 -6.810 83.005 -47.748 1.00 13.94 ATOM 2426 NE1 TRP B 195 -8.883 83.587 -48.487 1.00 12.09 ATOM 2427 CE2 TRP B 195 -8.210 82.663 -47.730 1.00 11.99 ATOM 2428 CE3 TRP B 195 -5.912 82.179 -47.097 1.00 11.60 ATOM 2429 CZ2 TRP B 195 -8.672 81.627 -47.067 1.00 11.51 ATOM 2430 CZ3 TRP B 195 -6.395 81.122 -46.421 1.00 17.58 ATOM 2431 CH2 TRP B 195 -7.790 80.877 -46.369 1.00 14.64 ATOM 2432 N TYR B 196 -3.187 82.614 -49.215 1.00 14.57 ATOM 2433 CA TYR B 196 -2.660 81.260 -49.076 1.00 12.19 ATOM 2434 C TYR B 196 -2.391 81.016 -47.588 1.00 13.35 ATOM 2435 O TYR B 196 -1.703 81.832 -46.938 1.00 13.23 ATOM 2436 CB TYR B 196 -1.325 81.064 -49.838 1.00 12.78 ATOM 2437 CG TYR B 196 -1.362 81.122 -51.385 1.00 11.28 ATOM 2438 CD1 TYR B 196 -0.232 81.508 -52.105 1.00 7.94 ATOM 2439 CD2 TYR B 196 -2.517 80.777 -52.105 1.00 10.80 ATOM 2440 CE1 TYR B 196 -0.243 81.564 -53.451 1.00 9.77 ATOM 2441 CE2 TYR B 196 -2.571 80.869 -53.487 1.00 8.96 ATOM 2442 CZ TYR B 196 -1.388 81.261 -54.156 1.00 14.65 ATOM 2443 OH TYR B 196 -1.393 81.334 -55.542 1.00 12.98 ATOM 2444 N ASP B 197 -2.894 79.903 -47.033 1.00 11.14 ATOM 2445 CA ASP B 197 -2.708 79.655 -45.619 1.00 11.60 ATOM 2446 C ASP B 197 -1.246 79.357 -45.326 1.00 11.07 ATOM 2447 O ASP B 197 -0.588 78.761 -46.133 1.00 12.24 ATOM 2448 CB ASP B 197 -3.616 78.517 -45.132 1.00 10.08 ATOM 2449 CG ASP B 197 -3.393 78.176 -43.664 1.00 14.64 ATOM 2450 OD1 ASP B 197 -2.209 78.129 -43.204 1.00 19.92 ATOM 2451 OD2 ASP B 197 -4.376 77.867 -42.955 1.00 18.48 ATOM 2452 N MET B 198 -0.742 79.757 -44.170 1.00 12.07 ATOM 2453 CA MET B 198 0.727 79.527 -43.850 1.00 11.16 ATOM 2454 C MET B 198 0.926 78.434 -42.884 1.00 11.82 ATOM 2455 O MET B 198 2.065 77.960 -42.729 1.00 9.95 ATOM 2456 CB MET B 198 1.388 80.779 -43.383 1.00 7.16 ATOM 2457 CG MET B 198 0.996 81.883 -44.351 1.00 8.30 ATOM 2458 SD MET B 198 1.492 83.513 -43.744 1.00 9.06 ATOM 2459 CE MET B 198 3.287 83.563 -43.783 1.00 2.00 ATOM 2460 N MET B 199 -0.184 78.031 -42.249 1.00 12.91 ATOM 2461 CA MET B 199 -0.064 77.067 -41.224 1.00 15.02 ATOM 2462 C MET B 199 -0.478 75.681 -41.652 1.00 16.65 ATOM 2463 O MET B 199 -1.454 75.492 -42.412 1.00 19.44 ATOM 2464 CB MET B 199 -0.720 77.528 -39.935 1.00 13.49 ATOM 2465 CG MET B 199 -0.201 78.796 -39.427 1.00 11.97 ATOM 2466 SD MET B 199 1.350 78.591 -38.589 1.00 13.57 ATOM 2467 CE MET B 199 1.680 80.312 -38.301 1.00 8.73 ATOM 2468 N PRO B 200 0.288 74.679 -41.195 1.00 17.16 ATOM 2469 CA PRO B 200 0.032 73.273 -41.338 1.00 16.01 ATOM 2470 C PRO B 200 -1.377 72.760 -41.071 1.00 17.27 ATOM 2471 O PRO B 200 -2.319 73.473 -40.633 1.00 17.12 ATOM 2472 CB PRO B 200 1.001 72.626 -40.355 1.00 16.46 ATOM 2473 CG PRO B 200 2.214 73.558 -40.387 1.00 14.67 ATOM 2474 CD PRO B 200 1.551 74.971 -40.464 1.00 17.02 ATOM 2475 N ALA B 201 -1.540 71.493 -41.378 1.00 15.58 ATOM 2476 CA ALA B 201 -2.863 70.939 -41.396 1.00 17.17 ATOM 2477 C ALA B 201 -3.114 70.473 -39.966 1.00 18.46 ATOM 2478 O ALA B 201 -2.181 69.919 -39.361 1.00 20.88 ATOM 2479 CB ALA B 201 -2.815 69.737 -42.273 1.00 17.09 ATOM 2480 N PRO B 202 -4.355 70.567 -39.454 1.00 16.86 ATOM 2481 CA PRO B 202 -4.566 70.282 -38.124 1.00 16.02 ATOM 2482 C PRO B 202 -4.383 68.790 -37.988 1.00 16.82 ATOM 2483 O PRO B 202 -5.291 68.064 -38.297 1.00 17.69 ATOM 2484 CB PRO B 202 -6.027 70.705 -37.918 1.00 12.96 ATOM 2485 CG PRO B 202 -6.672 70.356 -39.075 1.00 13.52 ATOM 2486 CD PRO B 202 -5.649 70.868 -40.091 1.00 20.01 ATOM 2487 N GLY B 203 -3.168 68.355 -37.621 1.00 18.95 ATOM 2488 CA GLY B 203 -2.881 66.987 -37.126 1.00 19.31 ATOM 2489 C GLY B 203 -1.470 66.626 -36.655 1.00 20.74 ATOM 2490 O GLY B 203 -0.637 67.490 -36.252 1.00 21.35 ATOM 2491 N ASP B 204 -1.169 65.332 -36.660 1.00 21.37 ATOM 2492 CA ASP B 204 0.117 64.865 -36.115 1.00 22.31 ATOM 2493 C ASP B 204 1.356 65.057 -36.952 1.00 21.10 ATOM 2494 O ASP B 204 2.421 65.302 -36.395 1.00 20.39 ATOM 2495 CB ASP B 204 0.038 63.364 -35.820 1.00 23.43 ATOM 2496 CG ASP B 204 1.406 62.788 -35.466 1.00 29.29 ATOM 2497 OD1 ASP B 204 2.103 63.400 -34.634 1.00 25.43 ATOM 2498 OD2 ASP B 204 1.788 61.713 -36.016 1.00 35.50 ATOM 2499 N LYS B 205 1.253 64.780 -38.266 1.00 21.26 ATOM 2500 CA LYS B 205 2.385 64.893 -39.228 1.00 19.07 ATOM 2501 C LYS B 205 2.184 65.936 -40.311 1.00 16.65 ATOM 2502 O LYS B 205 1.121 66.441 -40.483 1.00 14.45 ATOM 2503 CB LYS B 205 2.831 63.549 -39.839 1.00 20.05 ATOM 2504 CG LYS B 205 1.670 62.561 -40.116 1.00 24.18 ATOM 2505 CD LYS B 205 1.331 61.766 -38.850 1.00 21.21 ATOM 2506 CE LYS B 205 0.100 60.838 -39.050 1.00 23.66 ATOM 2507 NZ LYS B 205 0.010 59.948 -37.824 1.00 18.16 ATOM 2508 N PHE B 206 3.242 66.235 -41.061 1.00 14.82 ATOM 2509 CA PHE B 206 3.137 67.215 -42.131 1.00 13.57 ATOM 2510 C PHE B 206 3.690 66.705 -43.463 1.00 13.13 ATOM 2511 O PHE B 206 4.897 66.556 -43.586 1.00 14.61 ATOM 2512 CB PHE B 206 3.972 68.471 -41.702 1.00 11.00 ATOM 2513 CG PHE B 206 4.048 69.531 -42.709 1.00 10.52 ATOM 2514 CD1 PHE B 206 2.886 70.012 -43.328 1.00 5.52 ATOM 2515 CD2 PHE B 206 5.278 70.093 -43.038 1.00 8.57 ATOM 2516 CE1 PHE B 206 2.972 71.070 -44.134 1.00 9.40 ATOM 2517 CE2 PHE B 206 5.354 71.122 -43.857 1.00 5.77 ATOM 2518 CZ PHE B 206 4.172 71.631 -44.437 1.00 4.76 ATOM 2519 N ASP B 207 2.852 66.444 -44.474 1.00 14.31 ATOM 2520 CA ASP B 207 3.382 66.066 -45.781 1.00 12.10 ATOM 2521 C ASP B 207 3.919 67.366 -46.431 1.00 13.28 ATOM 2522 O ASP B 207 3.152 68.192 -46.951 1.00 11.62 ATOM 2523 CB ASP B 207 2.239 65.477 -46.568 1.00 11.84 ATOM 2524 CG ASP B 207 2.604 65.072 -47.969 1.00 14.12 ATOM 2525 OD1 ASP B 207 3.819 65.021 -48.280 1.00 20.54 ATOM 2526 OD2 ASP B 207 1.653 64.838 -48.794 1.00 16.80 ATOM 2527 N GLN B 208 5.249 67.519 -46.462 1.00 12.94 ATOM 2528 CA GLN B 208 5.846 68.678 -47.079 1.00 12.07 ATOM 2529 C GLN B 208 5.292 68.909 -48.441 1.00 14.28 ATOM 2530 O GLN B 208 4.488 69.855 -48.699 1.00 16.38 ATOM 2531 CB GLN B 208 7.343 68.518 -47.118 1.00 13.83 ATOM 2532 CG GLN B 208 8.076 69.250 -45.963 1.00 8.93 ATOM 2533 CD GLN B 208 9.522 68.700 -45.880 1.00 7.81 ATOM 2534 OE1 GLN B 208 10.449 69.331 -45.329 1.00 2.00 ATOM 2535 NE2 GLN B 208 9.706 67.572 -46.534 1.00 7.76 ATOM 2536 N SER B 209 5.549 67.949 -49.281 1.00 13.28 ATOM 2537 CA SER B 209 4.976 67.974 -50.609 1.00 14.95 ATOM 2538 C SER B 209 3.596 68.558 -50.733 1.00 15.05 ATOM 2539 O SER B 209 3.413 69.708 -51.100 1.00 15.66 ATOM 2540 CB SER B 209 4.884 66.623 -51.212 1.00 14.51 ATOM 2541 OG SER B 209 4.184 66.790 -52.450 1.00 20.02 ATOM 2542 N LYS B 210 2.629 67.688 -50.540 1.00 13.77 ATOM 2543 CA LYS B 210 1.213 68.094 -50.713 1.00 12.46 ATOM 2544 C LYS B 210 0.881 69.486 -50.315 1.00 8.67 ATOM 2545 O LYS B 210 -0.174 69.981 -50.687 1.00 8.86 ATOM 2546 CB LYS B 210 0.316 67.149 -49.895 1.00 10.27 ATOM 2547 CG LYS B 210 -1.092 67.083 -50.390 1.00 10.90 ATOM 2548 CD LYS B 210 -2.095 66.676 -49.232 1.00 11.44 ATOM 2549 CE LYS B 210 -3.580 66.439 -49.764 1.00 14.70 ATOM 2550 NZ LYS B 210 -4.473 66.155 -48.636 1.00 13.56 ATOM 2551 N TYR B 211 1.706 70.096 -49.468 1.00 10.54 ATOM 2552 CA TYR B 211 1.443 71.515 -49.057 1.00 7.88 ATOM 2553 C TYR B 211 1.711 72.318 -50.290 1.00 8.59 ATOM 2554 O TYR B 211 0.925 73.263 -50.746 1.00 11.87 ATOM 2555 CB TYR B 211 2.347 71.974 -47.907 1.00 7.91 ATOM 2556 CG TYR B 211 2.248 73.541 -47.516 1.00 9.48 ATOM 2557 CD1 TYR B 211 1.033 74.114 -47.060 1.00 2.42 ATOM 2558 CD2 TYR B 211 3.315 74.389 -47.688 1.00 5.30 ATOM 2559 CE1 TYR B 211 0.899 75.421 -46.669 1.00 2.05 ATOM 2560 CE2 TYR B 211 3.187 75.795 -47.393 1.00 7.64 ATOM 2561 CZ TYR B 211 1.964 76.276 -46.875 1.00 8.61 ATOM 2562 OH TYR B 211 1.790 77.577 -46.600 1.00 7.48 ATOM 2563 N LEU B 212 2.870 72.048 -50.850 1.00 7.58 ATOM 2564 CA LEU B 212 3.405 72.839 -51.971 1.00 5.40 ATOM 2565 C LEU B 212 2.632 72.655 -53.177 1.00 8.42 ATOM 2566 O LEU B 212 2.670 73.494 -54.063 1.00 12.22 ATOM 2567 CB LEU B 212 4.817 72.454 -52.247 1.00 4.90 ATOM 2568 CG LEU B 212 5.906 72.763 -51.202 1.00 2.14 ATOM 2569 CD1 LEU B 212 7.193 72.208 -51.542 1.00 10.84 ATOM 2570 CD2 LEU B 212 6.169 74.388 -51.135 1.00 5.79 ATOM 2571 N MET B 213 1.842 71.572 -53.271 1.00 9.17 ATOM 2572 CA MET B 213 1.198 71.298 -54.517 1.00 5.98 ATOM 2573 C MET B 213 0.358 72.535 -54.882 1.00 6.67 ATOM 2574 O MET B 213 -0.136 72.676 -55.997 1.00 8.57 ATOM 2575 CB MET B 213 0.327 70.158 -54.313 1.00 2.70 ATOM 2576 CG MET B 213 -0.485 69.890 -55.450 1.00 5.38 ATOM 2577 SD MET B 213 -1.040 68.218 -55.292 1.00 10.00 ATOM 2578 CE MET B 213 0.675 67.411 -55.231 1.00 7.05 ATOM 2579 N MET B 214 0.114 73.410 -53.931 1.00 6.76 ATOM 2580 CA MET B 214 -0.600 74.596 -54.245 1.00 5.62 ATOM 2581 C MET B 214 0.100 75.546 -55.204 1.00 8.62 ATOM 2582 O MET B 214 -0.545 76.605 -55.666 1.00 7.46 ATOM 2583 CB MET B 214 -0.940 75.403 -53.004 1.00 7.43 ATOM 2584 CG MET B 214 0.189 75.926 -52.127 1.00 5.09 ATOM 2585 SD MET B 214 -0.177 76.922 -50.685 1.00 3.90 ATOM 2586 CE MET B 214 0.893 78.406 -51.057 1.00 7.67 ATOM 2587 N TYR B 215 1.355 75.241 -55.536 1.00 6.55 ATOM 2588 CA TYR B 215 2.067 76.214 -56.352 1.00 8.24 ATOM 2589 C TYR B 215 2.055 75.738 -57.767 1.00 10.44 ATOM 2590 O TYR B 215 2.719 76.301 -58.669 1.00 9.45 ATOM 2591 CB TYR B 215 3.489 76.556 -55.873 1.00 9.46 ATOM 2592 CG TYR B 215 3.640 77.347 -54.574 1.00 9.98 ATOM 2593 CD1 TYR B 215 4.463 76.871 -53.521 1.00 13.26 ATOM 2594 CD2 TYR B 215 2.891 78.498 -54.349 1.00 12.80 ATOM 2595 CE1 TYR B 215 4.586 77.611 -52.313 1.00 11.10 ATOM 2596 CE2 TYR B 215 3.009 79.237 -53.144 1.00 7.24 ATOM 2597 CZ TYR B 215 3.863 78.800 -52.158 1.00 6.83 ATOM 2598 OH TYR B 215 3.966 79.535 -50.972 1.00 6.01 ATOM 2599 N ASN B 216 1.207 74.743 -58.027 1.00 10.11 ATOM 2600 CA ASN B 216 1.243 74.184 -59.366 1.00 10.42 ATOM 2601 C ASN B 216 0.340 74.921 -60.396 1.00 11.37 ATOM 2602 O ASN B 216 0.157 74.494 -61.556 1.00 12.14 ATOM 2603 CB ASN B 216 1.003 72.660 -59.234 1.00 10.99 ATOM 2604 CG ASN B 216 -0.493 72.295 -58.845 1.00 7.94 ATOM 2605 OD1 ASN B 216 -0.880 71.187 -59.046 1.00 8.88 ATOM 2606 ND2 ASN B 216 -1.276 73.223 -58.348 1.00 7.90 ATOM 2607 N ASP B 217 -0.208 76.049 -59.971 1.00 13.41 ATOM 2608 CA ASP B 217 -1.109 76.814 -60.818 1.00 13.47 ATOM 2609 C ASP B 217 -0.190 77.876 -61.500 1.00 13.44 ATOM 2610 O ASP B 217 -0.605 78.774 -62.232 1.00 8.95 ATOM 2611 CB ASP B 217 -2.173 77.474 -59.928 1.00 14.77 ATOM 2612 CG ASP B 217 -1.604 78.561 -59.073 1.00 18.29 ATOM 2613 OD1 ASP B 217 -0.357 78.599 -59.004 1.00 25.18 ATOM 2614 OD2 ASP B 217 -2.360 79.387 -58.522 1.00 15.38 ATOM 2615 N ASN B 218 1.119 77.716 -61.246 1.00 13.79 ATOM 2616 CA ASN B 218 2.083 78.640 -61.731 1.00 11.63 ATOM 2617 C ASN B 218 1.623 80.062 -61.868 1.00 14.18 ATOM 2618 O ASN B 218 1.977 80.681 -62.792 1.00 16.15 ATOM 2619 CB ASN B 218 2.554 78.205 -63.054 1.00 12.01 ATOM 2620 CG ASN B 218 3.987 78.680 -63.272 1.00 13.18 ATOM 2621 OD1 ASN B 218 4.903 78.223 -62.578 1.00 10.21 ATOM 2622 ND2 ASN B 218 4.161 79.674 -64.107 1.00 7.20 ATOM 2623 N LYS B 219 0.784 80.555 -60.967 1.00 13.83 ATOM 2624 CA LYS B 219 0.125 81.773 -61.130 1.00 13.39 ATOM 2625 C LYS B 219 1.207 82.778 -60.997 1.00 14.08 ATOM 2626 O LYS B 219 2.116 82.609 -60.161 1.00 16.86 ATOM 2627 CB LYS B 219 -0.855 82.027 -59.962 1.00 13.32 ATOM 2628 CG LYS B 219 -1.266 83.523 -59.806 1.00 10.67 ATOM 2629 CD LYS B 219 -1.971 84.122 -61.071 1.00 2.64 ATOM 2630 CE LYS B 219 -2.428 85.720 -60.820 1.00 6.33 ATOM 2631 NZ LYS B 219 -3.811 85.804 -60.273 1.00 9.10 ATOM 2632 N THR B 220 1.132 83.796 -61.845 1.00 12.34 ATOM 2633 CA THR B 220 2.051 84.948 -61.885 1.00 13.14 ATOM 2634 C THR B 220 1.331 86.328 -61.557 1.00 11.83 ATOM 2635 O THR B 220 0.035 86.521 -61.610 1.00 6.57 ATOM 2636 CB THR B 220 2.628 85.189 -63.283 1.00 11.29 ATOM 2637 OG1 THR B 220 1.735 84.675 -64.246 1.00 16.36 ATOM 2638 CG2 THR B 220 4.031 84.648 -63.482 1.00 15.28 ATOM 2639 N VAL B 221 2.205 87.279 -61.336 1.00 9.47 ATOM 2640 CA VAL B 221 1.804 88.642 -60.939 1.00 8.96 ATOM 2641 C VAL B 221 2.805 89.735 -61.425 1.00 9.26 ATOM 2642 O VAL B 221 3.969 89.454 -61.744 1.00 7.29 ATOM 2643 CB VAL B 221 1.740 88.729 -59.432 1.00 8.07 ATOM 2644 CG1 VAL B 221 0.413 88.178 -58.892 1.00 6.23 ATOM 2645 CG2 VAL B 221 2.885 88.058 -58.844 1.00 8.07 ATOM 2646 N ASP B 222 2.354 90.999 -61.458 1.00 11.10 ATOM 2647 CA ASP B 222 3.230 92.030 -62.042 1.00 11.38 ATOM 2648 C ASP B 222 3.928 92.799 -60.967 1.00 10.59 ATOM 2649 O ASP B 222 3.290 93.658 -60.236 1.00 10.88 ATOM 2650 CB ASP B 222 2.458 92.942 -62.994 1.00 11.31 ATOM 2651 CG ASP B 222 3.159 94.290 -63.216 1.00 18.61 ATOM 2652 OD1 ASP B 222 4.402 94.328 -63.651 1.00 12.76 ATOM 2653 OD2 ASP B 222 2.437 95.315 -62.949 1.00 20.55 ATOM 2654 N SER B 223 5.202 92.484 -60.775 1.00 11.01 ATOM 2655 CA SER B 223 6.008 93.167 -59.706 1.00 10.81 ATOM 2656 C SER B 223 5.680 94.662 -59.588 1.00 13.01 ATOM 2657 O SER B 223 4.861 95.098 -58.779 1.00 12.28 ATOM 2658 CB SER B 223 7.431 92.954 -60.035 1.00 12.80 ATOM 2659 OG SER B 223 7.714 93.692 -61.198 1.00 17.99 ATOM 2660 N LYS B 224 6.293 95.493 -60.391 1.00 16.57 ATOM 2661 CA LYS B 224 6.027 96.970 -60.347 1.00 18.61 ATOM 2662 C LYS B 224 4.662 97.474 -59.806 1.00 17.45 ATOM 2663 O LYS B 224 4.496 98.671 -59.496 1.00 22.39 ATOM 2664 CB LYS B 224 6.328 97.627 -61.715 1.00 17.57 ATOM 2665 CG LYS B 224 5.840 99.108 -61.832 1.00 22.56 ATOM 2666 CD LYS B 224 6.607 100.035 -60.888 1.00 30.04 ATOM 2667 CE LYS B 224 8.134 99.942 -61.100 1.00 30.69 ATOM 2668 NZ LYS B 224 8.574 100.785 -62.276 1.00 30.96 ATOM 2669 N SER B 225 3.700 96.620 -59.636 1.00 15.93 ATOM 2670 CA SER B 225 2.383 97.129 -59.155 1.00 16.39 ATOM 2671 C SER B 225 1.743 96.430 -58.047 1.00 13.02 ATOM 2672 O SER B 225 1.368 97.084 -57.074 1.00 16.98 ATOM 2673 CB SER B 225 1.304 97.240 -60.229 1.00 15.75 ATOM 2674 OG SER B 225 0.888 95.949 -60.640 1.00 23.80 ATOM 2675 N VAL B 226 1.532 95.163 -58.206 1.00 12.07 ATOM 2676 CA VAL B 226 1.080 94.194 -57.144 1.00 12.12 ATOM 2677 C VAL B 226 1.634 94.647 -55.829 1.00 13.26 ATOM 2678 O VAL B 226 2.795 95.206 -55.740 1.00 15.27 ATOM 2679 CB VAL B 226 1.664 92.740 -57.401 1.00 10.62 ATOM 2680 CG1 VAL B 226 3.105 92.644 -57.014 1.00 12.40 ATOM 2681 CG2 VAL B 226 0.975 91.629 -56.666 1.00 12.97 ATOM 2682 N LYS B 227 0.829 94.417 -54.801 1.00 14.79 ATOM 2683 CA LYS B 227 1.127 94.757 -53.375 1.00 13.32 ATOM 2684 C LYS B 227 0.797 93.482 -52.514 1.00 11.92 ATOM 2685 O LYS B 227 -0.144 92.773 -52.855 1.00 9.07 ATOM 2686 CB LYS B 227 0.244 95.971 -52.941 1.00 10.36 ATOM 2687 CG LYS B 227 -1.236 95.816 -53.245 1.00 12.29 ATOM 2688 CD LYS B 227 -2.001 97.269 -53.303 1.00 16.29 ATOM 2689 CE LYS B 227 -1.117 98.384 -54.076 1.00 17.98 ATOM 2690 NZ LYS B 227 -1.848 99.652 -54.281 1.00 21.46 ATOM 2691 N ILE B 228 1.511 93.278 -51.387 1.00 12.84 ATOM 2692 CA ILE B 228 1.363 92.065 -50.474 1.00 12.66 ATOM 2693 C ILE B 228 0.868 92.391 -49.090 1.00 11.62 ATOM 2694 O ILE B 228 1.163 93.494 -48.570 1.00 9.82 ATOM 2695 CB ILE B 228 2.649 91.385 -50.356 1.00 11.44 ATOM 2696 CG1 ILE B 228 3.085 91.087 -51.804 1.00 17.05 ATOM 2697 CG2 ILE B 228 2.432 90.020 -49.796 1.00 14.63 ATOM 2698 CD1 ILE B 228 4.582 90.906 -51.983 1.00 27.71 ATOM 2699 N GLU B 229 0.051 91.488 -48.552 1.00 8.09 ATOM 2700 CA GLU B 229 -0.319 91.548 -47.203 1.00 8.55 ATOM 2701 C GLU B 229 -0.230 90.210 -46.470 1.00 10.16 ATOM 2702 O GLU B 229 -0.815 89.166 -46.918 1.00 8.76 ATOM 2703 CB GLU B 229 -1.793 92.008 -47.080 1.00 8.11 ATOM 2704 CG GLU B 229 -1.987 93.457 -47.591 1.00 5.95 ATOM 2705 CD GLU B 229 -3.473 94.015 -47.374 1.00 9.38 ATOM 2706 OE1 GLU B 229 -4.138 93.522 -46.464 1.00 4.16 ATOM 2707 OE2 GLU B 229 -3.928 94.948 -48.149 1.00 5.72 ATOM 2708 N VAL B 230 0.441 90.271 -45.317 1.00 9.23 ATOM 2709 CA VAL B 230 0.472 89.129 -44.411 1.00 10.18 ATOM 2710 C VAL B 230 -0.299 89.382 -43.165 1.00 10.18 ATOM 2711 O VAL B 230 -0.392 90.540 -42.669 1.00 7.88 ATOM 2712 CB VAL B 230 1.900 88.713 -44.098 1.00 9.33 ATOM 2713 CG1 VAL B 230 1.911 87.345 -43.637 1.00 11.38 ATOM 2714 CG2 VAL B 230 2.678 88.721 -45.378 1.00 6.10 ATOM 2715 N HIS B 231 -0.999 88.328 -42.715 1.00 10.47 ATOM 2716 CA HIS B 231 -1.878 88.492 -41.562 1.00 7.93 ATOM 2717 C HIS B 231 -1.788 87.438 -40.479 1.00 9.90 ATOM 2718 O HIS B 231 -2.104 86.235 -40.706 1.00 7.96 ATOM 2719 CB HIS B 231 -3.308 88.687 -42.003 1.00 10.05 ATOM 2720 CG HIS B 231 -3.514 89.873 -42.884 1.00 4.45 ATOM 2721 ND1 HIS B 231 -3.540 91.167 -42.386 1.00 14.17 ATOM 2722 CD2 HIS B 231 -3.743 89.978 -44.205 1.00 8.07 ATOM 2723 CE1 HIS B 231 -3.814 92.023 -43.367 1.00 11.46 ATOM 2724 NE2 HIS B 231 -3.921 91.338 -44.496 1.00 9.52 ATOM 2725 N LEU B 232 -1.347 87.908 -39.281 1.00 9.33 ATOM 2726 CA LEU B 232 -1.211 87.048 -38.168 1.00 10.79 ATOM 2727 C LEU B 232 -1.990 87.322 -36.867 1.00 11.53 ATOM 2728 O LEU B 232 -2.351 88.432 -36.581 1.00 9.61 ATOM 2729 CB LEU B 232 0.289 86.905 -37.838 1.00 6.58 ATOM 2730 CG LEU B 232 1.204 87.014 -39.059 1.00 6.26 ATOM 2731 CD1 LEU B 232 2.639 87.509 -38.690 1.00 2.00 ATOM 2732 CD2 LEU B 232 1.300 85.699 -39.770 1.00 8.32 ATOM 2733 N THR B 233 -2.050 86.274 -36.041 1.00 13.55 ATOM 2734 CA THR B 233 -2.766 86.244 -34.802 1.00 17.69 ATOM 2735 C THR B 233 -1.963 85.429 -33.839 1.00 18.51 ATOM 2736 O THR B 233 -1.586 84.272 -34.110 1.00 18.86 ATOM 2737 CB THR B 233 -4.114 85.683 -34.921 1.00 15.29 ATOM 2738 OG1 THR B 233 -4.012 84.454 -35.648 1.00 22.65 ATOM 2739 CG2 THR B 233 -5.033 86.635 -35.675 1.00 16.54 ATOM 2740 N THR B 234 -1.686 86.088 -32.721 1.00 21.39 ATOM 2741 CA THR B 234 -0.809 85.565 -31.717 1.00 24.25 ATOM 2742 C THR B 234 -1.483 84.491 -30.955 1.00 24.47 ATOM 2743 O THR B 234 -2.715 84.347 -30.992 1.00 26.05 ATOM 2744 CB THR B 234 -0.389 86.652 -30.788 1.00 24.84 ATOM 2745 OG1 THR B 234 0.167 87.710 -31.570 1.00 25.92 ATOM 2746 CG2 THR B 234 0.698 86.127 -29.884 1.00 31.82 ATOM 2747 N LYS B 235 -0.671 83.665 -30.317 1.00 26.23 ATOM 2748 CA LYS B 235 -1.160 82.497 -29.579 1.00 25.36 ATOM 2749 C LYS B 235 -1.798 83.077 -28.343 1.00 26.05 ATOM 2750 O LYS B 235 -2.684 83.934 -28.437 1.00 26.41 ATOM 2751 CB LYS B 235 0.022 81.665 -29.110 1.00 24.60 ATOM 2752 CG LYS B 235 0.453 80.518 -30.001 1.00 28.91 ATOM 2753 CD LYS B 235 -0.485 79.259 -29.947 1.00 27.15 ATOM 2754 CE LYS B 235 0.151 78.062 -30.780 1.00 23.19 ATOM 2755 NZ LYS B 235 1.588 77.709 -30.374 1.00 24.48 prodigy-2.2.2/examples/3bzd.cif000066400000000000000000012407201461273102600163450ustar00rootroot00000000000000data_3BZD # _entry.id 3BZD # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 4.007 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3BZD RCSB RCSB046146 # _database_PDB_rev.num 1 _database_PDB_rev.date 2009-05-12 _database_PDB_rev.date_original 2008-01-17 _database_PDB_rev.mod_type 0 _database_PDB_rev.replaces 3BZD _database_PDB_rev.status ? # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3BYY . unspecified PDB 3BYT . unspecified PDB 3BVG . unspecified PDB 3BVM . unspecified PDB 3BVZ . unspecified # _pdbx_database_status.entry_id 3BZD _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? # _audit_author.name 'Cho, S.' _audit_author.pdbx_ordinal 1 # _citation.id primary _citation.title 'Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex' _citation.journal_abbrev 'To be Published' _citation.journal_volume ? _citation.page_first ? _citation.page_last ? _citation.year ? _citation.journal_id_ASTM ? _citation.country ? _citation.journal_id_ISSN ? _citation.journal_id_CSD 0353 _citation.book_publisher ? _citation.pdbx_database_id_PubMed ? _citation.pdbx_database_id_DOI ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Cho, S.' 1 primary 'Swaminathan, C.P.' 2 primary 'Kerzic, M.C.' 3 primary 'Guan, R.' 4 primary 'Yang, J.' 5 primary 'Kieke, M.C.' 6 primary 'Andersen, P.S.' 7 primary 'Krantz, D.M.' 8 primary 'Mariuzza, R.A.' 9 primary 'Eric, S.J.' 10 # _cell.length_a 96.970 _cell.length_b 96.970 _cell.length_c 92.510 _cell.angle_alpha 90.000 _cell.angle_beta 90.000 _cell.angle_gamma 120.000 _cell.entry_id 3BZD _cell.pdbx_unique_axis ? _cell.Z_PDB 6 _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.space_group_name_H-M 'P 65' _symmetry.entry_id 3BZD _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.Int_Tables_number ? _symmetry.cell_setting ? _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.details _entity.pdbx_mutation _entity.pdbx_fragment _entity.pdbx_ec 1 polymer man 'T cell receptor beta chain 8.2' 11766.051 1 ? ? 'Variable domain' ? 2 polymer man 'Enterotoxin type C-3' 27690.242 1 ? ? ? ? 3 non-polymer syn 'SULFATE ION' 96.058 2 ? ? ? ? 4 water nat water 18.015 85 ? ? ? ? # loop_ _entity_keywords.entity_id _entity_keywords.text 1 ? 2 ? 3 ? 4 ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 ? 2 SEC3 3 ? 4 ? # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id 1 'polypeptide(L)' no no ;AAVTQSPRNKVAVTGEKVTLSCQQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIPDGYKASRPSQEQFSLILESA TPSQTSVYFCASGGGGTLYFGAGTRLSVL ; ;AAVTQSPRNKVAVTGEKVTLSCQQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIPDGYKASRPSQEQFSLILESA TPSQTSVYFCASGGGGTLYFGAGTRLSVL ; A 2 'polypeptide(L)' no no ;ESQPDPMPDDLHKSSEFTGTMGNMKYLYDDHYVSATKVKSVDKFLAHDLIYNISDKKLKNYDKVKTELLNEDLAKKYKDE VVDVYGSNYYVNCYFSSKDNVWWHGKTCMYGGITKHEGNHFDNGNLQNVLVRVYENKRNTISFEVQTDKKSVTAQELDIK ARNFLINKKNLYEFNSSPYETGYIKFIENNGNTFWYDMMPAPGDKFDQSKYLMMYNDNKTVDSKSVKIEVHLTTKNG ; ;ESQPDPMPDDLHKSSEFTGTMGNMKYLYDDHYVSATKVKSVDKFLAHDLIYNISDKKLKNYDKVKTELLNEDLAKKYKDE VVDVYGSNYYVNCYFSSKDNVWWHGKTCMYGGITKHEGNHFDNGNLQNVLVRVYENKRNTISFEVQTDKKSVTAQELDIK ARNFLINKKNLYEFNSSPYETGYIKFIENNGNTFWYDMMPAPGDKFDQSKYLMMYNDNKTVDSKSVKIEVHLTTKNG ; B # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ALA n 1 2 ALA n 1 3 VAL n 1 4 THR n 1 5 GLN n 1 6 SER n 1 7 PRO n 1 8 ARG n 1 9 ASN n 1 10 LYS n 1 11 VAL n 1 12 ALA n 1 13 VAL n 1 14 THR n 1 15 GLY n 1 16 GLU n 1 17 LYS n 1 18 VAL n 1 19 THR n 1 20 LEU n 1 21 SER n 1 22 CYS n 1 23 GLN n 1 24 GLN n 1 25 THR n 1 26 ASN n 1 27 ASN n 1 28 HIS n 1 29 ASN n 1 30 ASN n 1 31 MET n 1 32 TYR n 1 33 TRP n 1 34 TYR n 1 35 ARG n 1 36 GLN n 1 37 ASP n 1 38 THR n 1 39 GLY n 1 40 HIS n 1 41 GLY n 1 42 LEU n 1 43 ARG n 1 44 LEU n 1 45 ILE n 1 46 HIS n 1 47 TYR n 1 48 SER n 1 49 TYR n 1 50 GLY n 1 51 ALA n 1 52 GLY n 1 53 SER n 1 54 THR n 1 55 GLU n 1 56 LYS n 1 57 GLY n 1 58 ASP n 1 59 ILE n 1 60 PRO n 1 61 ASP n 1 62 GLY n 1 63 TYR n 1 64 LYS n 1 65 ALA n 1 66 SER n 1 67 ARG n 1 68 PRO n 1 69 SER n 1 70 GLN n 1 71 GLU n 1 72 GLN n 1 73 PHE n 1 74 SER n 1 75 LEU n 1 76 ILE n 1 77 LEU n 1 78 GLU n 1 79 SER n 1 80 ALA n 1 81 THR n 1 82 PRO n 1 83 SER n 1 84 GLN n 1 85 THR n 1 86 SER n 1 87 VAL n 1 88 TYR n 1 89 PHE n 1 90 CYS n 1 91 ALA n 1 92 SER n 1 93 GLY n 1 94 GLY n 1 95 GLY n 1 96 GLY n 1 97 THR n 1 98 LEU n 1 99 TYR n 1 100 PHE n 1 101 GLY n 1 102 ALA n 1 103 GLY n 1 104 THR n 1 105 ARG n 1 106 LEU n 1 107 SER n 1 108 VAL n 1 109 LEU n 2 1 GLU n 2 2 SER n 2 3 GLN n 2 4 PRO n 2 5 ASP n 2 6 PRO n 2 7 MET n 2 8 PRO n 2 9 ASP n 2 10 ASP n 2 11 LEU n 2 12 HIS n 2 13 LYS n 2 14 SER n 2 15 SER n 2 16 GLU n 2 17 PHE n 2 18 THR n 2 19 GLY n 2 20 THR n 2 21 MET n 2 22 GLY n 2 23 ASN n 2 24 MET n 2 25 LYS n 2 26 TYR n 2 27 LEU n 2 28 TYR n 2 29 ASP n 2 30 ASP n 2 31 HIS n 2 32 TYR n 2 33 VAL n 2 34 SER n 2 35 ALA n 2 36 THR n 2 37 LYS n 2 38 VAL n 2 39 LYS n 2 40 SER n 2 41 VAL n 2 42 ASP n 2 43 LYS n 2 44 PHE n 2 45 LEU n 2 46 ALA n 2 47 HIS n 2 48 ASP n 2 49 LEU n 2 50 ILE n 2 51 TYR n 2 52 ASN n 2 53 ILE n 2 54 SER n 2 55 ASP n 2 56 LYS n 2 57 LYS n 2 58 LEU n 2 59 LYS n 2 60 ASN n 2 61 TYR n 2 62 ASP n 2 63 LYS n 2 64 VAL n 2 65 LYS n 2 66 THR n 2 67 GLU n 2 68 LEU n 2 69 LEU n 2 70 ASN n 2 71 GLU n 2 72 ASP n 2 73 LEU n 2 74 ALA n 2 75 LYS n 2 76 LYS n 2 77 TYR n 2 78 LYS n 2 79 ASP n 2 80 GLU n 2 81 VAL n 2 82 VAL n 2 83 ASP n 2 84 VAL n 2 85 TYR n 2 86 GLY n 2 87 SER n 2 88 ASN n 2 89 TYR n 2 90 TYR n 2 91 VAL n 2 92 ASN n 2 93 CYS n 2 94 TYR n 2 95 PHE n 2 96 SER n 2 97 SER n 2 98 LYS n 2 99 ASP n 2 100 ASN n 2 101 VAL n 2 102 TRP n 2 103 TRP n 2 104 HIS n 2 105 GLY n 2 106 LYS n 2 107 THR n 2 108 CYS n 2 109 MET n 2 110 TYR n 2 111 GLY n 2 112 GLY n 2 113 ILE n 2 114 THR n 2 115 LYS n 2 116 HIS n 2 117 GLU n 2 118 GLY n 2 119 ASN n 2 120 HIS n 2 121 PHE n 2 122 ASP n 2 123 ASN n 2 124 GLY n 2 125 ASN n 2 126 LEU n 2 127 GLN n 2 128 ASN n 2 129 VAL n 2 130 LEU n 2 131 VAL n 2 132 ARG n 2 133 VAL n 2 134 TYR n 2 135 GLU n 2 136 ASN n 2 137 LYS n 2 138 ARG n 2 139 ASN n 2 140 THR n 2 141 ILE n 2 142 SER n 2 143 PHE n 2 144 GLU n 2 145 VAL n 2 146 GLN n 2 147 THR n 2 148 ASP n 2 149 LYS n 2 150 LYS n 2 151 SER n 2 152 VAL n 2 153 THR n 2 154 ALA n 2 155 GLN n 2 156 GLU n 2 157 LEU n 2 158 ASP n 2 159 ILE n 2 160 LYS n 2 161 ALA n 2 162 ARG n 2 163 ASN n 2 164 PHE n 2 165 LEU n 2 166 ILE n 2 167 ASN n 2 168 LYS n 2 169 LYS n 2 170 ASN n 2 171 LEU n 2 172 TYR n 2 173 GLU n 2 174 PHE n 2 175 ASN n 2 176 SER n 2 177 SER n 2 178 PRO n 2 179 TYR n 2 180 GLU n 2 181 THR n 2 182 GLY n 2 183 TYR n 2 184 ILE n 2 185 LYS n 2 186 PHE n 2 187 ILE n 2 188 GLU n 2 189 ASN n 2 190 ASN n 2 191 GLY n 2 192 ASN n 2 193 THR n 2 194 PHE n 2 195 TRP n 2 196 TYR n 2 197 ASP n 2 198 MET n 2 199 MET n 2 200 PRO n 2 201 ALA n 2 202 PRO n 2 203 GLY n 2 204 ASP n 2 205 LYS n 2 206 PHE n 2 207 ASP n 2 208 GLN n 2 209 SER n 2 210 LYS n 2 211 TYR n 2 212 LEU n 2 213 MET n 2 214 MET n 2 215 TYR n 2 216 ASN n 2 217 ASP n 2 218 ASN n 2 219 LYS n 2 220 THR n 2 221 VAL n 2 222 ASP n 2 223 SER n 2 224 LYS n 2 225 SER n 2 226 VAL n 2 227 LYS n 2 228 ILE n 2 229 GLU n 2 230 VAL n 2 231 HIS n 2 232 LEU n 2 233 THR n 2 234 THR n 2 235 LYS n 2 236 ASN n 2 237 GLY n # loop_ _entity_src_gen.entity_id _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _entity_src_gen.gene_src_tissue _entity_src_gen.gene_src_tissue_fraction _entity_src_gen.gene_src_details _entity_src_gen.pdbx_gene_src_fragment _entity_src_gen.pdbx_gene_src_scientific_name _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _entity_src_gen.pdbx_host_org_organelle _entity_src_gen.pdbx_host_org_cellular_location _entity_src_gen.pdbx_host_org_vector_type _entity_src_gen.pdbx_host_org_vector _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 ? ? ? ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? 'BL21(DE3)' ? ? ? ? ? ? ? ? ? PT7-7 ? ? 2 ? ? entC3 ? ? ? ? ? ? 'Staphylococcus aureus' 1280 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? 'BL21(DE3)' ? ? ? ? ? ? ? ? ? PET26b+ ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.biol_id 1 PDB 3BZD 3BZD 1 ' AAVTQSPRNKVAVTGEKVTLSCQQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIPDGYKASRPSQEQFSLILESA TPSQTSVYFCASGGGGTLYFGAGTRLSVL' 1 . 2 UNP ENTC3_STAAU P0A0L5 2 ;eSQPDPMPDDLHKSSEFTGTMGNMKYLYDDHYVSATKVKSVDKFLAHDLIYNISDKKLKNYDKVKTELLNEDLAKKYKDEVVDVYGSNYYVNCYFSSKDNVGKVTGGKTCMYGGITKHEGNHFDNGNLQNVLVRVYENKRNTISFEVQTDKKSVTAQELDIKARNFLINKKNLYEFNSSPYETGYIKFIENNGNTFWYDMMPAPGDKFDQSKYLMMYNDNKTVDSKSVKIEVHLTTKng ; 28 . # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 3BZD A 1 ? 109 ? 3BZD 2 117 2 117 2 2 3BZD B 1 ? 237 ? P0A0L5 28 266 1 237 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 2 3BZD ? B ? ? UNP P0A0L5 GLY 129 'SEE REMARK 999' ? 1 2 3BZD ? B ? ? UNP P0A0L5 LYS 130 'SEE REMARK 999' ? 2 2 3BZD TRP B 102 ? UNP P0A0L5 VAL 131 'SEE REMARK 999' 102 3 2 3BZD TRP B 103 ? UNP P0A0L5 THR 132 'SEE REMARK 999' 103 4 2 3BZD HIS B 104 ? UNP P0A0L5 GLY 133 'SEE REMARK 999' 104 5 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.094 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.147 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.120 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.146 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.132 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.210 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.119 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.197 GLY 'PEPTIDE LINKING' y GLYCINE ? 'C2 H5 N O2' 75.067 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.130 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.174 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.154 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.164 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.207 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.191 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.228 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.104 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.174 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.191 SO4 NON-POLYMER . 'SULFATE ION' ? 'O4 S -2' 96.058 HOH NON-POLYMER . WATER ? 'H2 O' 18.015 # _exptl.crystals_number 1 _exptl.entry_id 3BZD _exptl.method 'X-RAY DIFFRACTION' # _exptl_crystal.id 1 _exptl_crystal.density_Matthews 3.21 _exptl_crystal.density_meas ? _exptl_crystal.density_percent_sol 61.64 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.pH 7.0 _exptl_crystal_grow.temp 298 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pdbx_details '2.0 M ammonium sulfate, 0.1 M Tris-Cl pH 7.0, 0.3 % 1,6-diaminohexane, VAPOR DIFFUSION, HANGING DROP, temperature 298K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type 'RIGAKU RAXIS IV++' _diffrn_detector.pdbx_collection_date 2007-03-15 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'RIGAKU RU200' _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.5418 _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? # _reflns.entry_id 3BZD _reflns.observed_criterion_sigma_F 2 _reflns.observed_criterion_sigma_I 2 _reflns.d_resolution_high 2.3 _reflns.d_resolution_low 30 _reflns.number_all 23532 _reflns.number_obs 21938 _reflns.percent_possible_obs 99.7 _reflns.pdbx_Rmerge_I_obs 0.058 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate 31.3 _reflns.pdbx_redundancy ? _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 2.30 _reflns_shell.d_res_low 2.36 _reflns_shell.percent_possible_obs ? _reflns_shell.percent_possible_all 93.3 _reflns_shell.Rmerge_I_obs 0.356 _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.pdbx_redundancy ? _reflns_shell.number_unique_all 1518 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _computing.entry_id 3BZD _computing.pdbx_data_reduction_ii CrystalClear _computing.pdbx_data_reduction_ds CrystalClear _computing.data_collection CrystalClear _computing.structure_solution MOLREP _computing.structure_refinement 'REFMAC 5.2.0019' _computing.pdbx_structure_refinement_method ? # _refine.entry_id 3BZD _refine.ls_d_res_high 2.300 _refine.ls_d_res_low 27.990 _refine.pdbx_ls_sigma_F 0.00 _refine.ls_percent_reflns_obs 100.000 _refine.ls_number_reflns_obs 21938 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.pdbx_R_Free_selection_details RANDOM _refine.details ? _refine.ls_R_factor_obs 0.213 _refine.ls_R_factor_R_work 0.210 _refine.ls_R_factor_R_free 0.258 _refine.ls_percent_reflns_R_free 4.900 _refine.ls_number_reflns_R_free 1073 _refine.B_iso_mean 18.380 _refine.aniso_B[1][1] 1.510 _refine.aniso_B[2][2] 1.510 _refine.aniso_B[3][3] -2.270 _refine.aniso_B[1][2] 0.760 _refine.aniso_B[1][3] 0.000 _refine.aniso_B[2][3] 0.000 _refine.correlation_coeff_Fo_to_Fc 0.903 _refine.correlation_coeff_Fo_to_Fc_free 0.865 _refine.pdbx_overall_ESU_R 0.270 _refine.pdbx_overall_ESU_R_Free 0.223 _refine.overall_SU_ML 0.217 _refine.overall_SU_B 9.004 _refine.solvent_model_details MASK _refine.pdbx_solvent_vdw_probe_radii 1.400 _refine.pdbx_solvent_ion_probe_radii 0.800 _refine.pdbx_solvent_shrinkage_radii 0.800 _refine.pdbx_method_to_determine_struct ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_ls_sigma_I ? _refine.ls_number_reflns_all ? _refine.ls_R_factor_all ? _refine.ls_redundancy_reflns_obs ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.pdbx_starting_model ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.solvent_model_param_bsol ? _refine.solvent_model_param_ksol ? _refine.occupancy_max ? _refine.occupancy_min ? _refine.pdbx_isotropic_thermal_model ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_overall_phase_error ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2754 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 10 _refine_hist.number_atoms_solvent 85 _refine_hist.number_atoms_total 2849 _refine_hist.d_res_high 2.300 _refine_hist.d_res_low 27.990 # loop_ _refine_ls_restr.type _refine_ls_restr.number _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.pdbx_refine_id r_bond_refined_d 2827 0.031 0.022 ? 'X-RAY DIFFRACTION' r_angle_refined_deg 3819 2.359 1.944 ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 339 5.887 5.000 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 139 44.201 25.108 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 491 18.367 15.000 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 8 19.678 15.000 ? 'X-RAY DIFFRACTION' r_chiral_restr 401 0.158 0.200 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 2151 0.013 0.020 ? 'X-RAY DIFFRACTION' r_nbd_refined 1494 0.326 0.200 ? 'X-RAY DIFFRACTION' r_nbtor_refined 1900 0.343 0.200 ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_refined 184 0.244 0.200 ? 'X-RAY DIFFRACTION' r_symmetry_vdw_refined 43 0.299 0.200 ? 'X-RAY DIFFRACTION' r_symmetry_hbond_refined 6 0.123 0.200 ? 'X-RAY DIFFRACTION' r_mcbond_it 1759 1.663 1.500 ? 'X-RAY DIFFRACTION' r_mcangle_it 2739 2.435 2.000 ? 'X-RAY DIFFRACTION' r_scbond_it 1271 3.911 3.000 ? 'X-RAY DIFFRACTION' r_scangle_it 1080 4.760 4.500 ? 'X-RAY DIFFRACTION' # _refine_ls_shell.d_res_high 2.300 _refine_ls_shell.d_res_low 2.359 _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.percent_reflns_obs 100.000 _refine_ls_shell.number_reflns_R_work 1518 _refine_ls_shell.R_factor_all ? _refine_ls_shell.R_factor_R_work 0.310 _refine_ls_shell.R_factor_R_free 0.327 _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 75 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.number_reflns_all 1593 _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 3BZD _struct.title 'Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex' _struct.pdbx_descriptor 'Variable domain of the murine T cell receptor beta chain 8.2, Enterotoxin type C-3' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3BZD _struct_keywords.pdbx_keywords TOXIN _struct_keywords.text 'Superantigen, Secreted, TOXIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 4 ? F N N 4 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 THR A 81 ? THR A 85 ? THR A 83 THR A 87 5 ? 5 HELX_P HELX_P2 2 MET B 7 ? LEU B 11 ? MET B 7 LEU B 11 5 ? 5 HELX_P HELX_P3 3 LYS B 13 ? PHE B 17 ? LYS B 13 PHE B 17 5 ? 5 HELX_P HELX_P4 4 MET B 21 ? TYR B 26 ? MET B 21 TYR B 26 1 ? 6 HELX_P HELX_P5 5 ASN B 70 ? ASP B 79 ? ASN B 70 ASP B 79 1 ? 10 HELX_P HELX_P6 6 ALA B 154 ? ASN B 170 ? ALA B 154 ASN B 170 1 ? 17 HELX_P HELX_P7 7 ASP B 207 ? MET B 213 ? ASP B 207 MET B 213 1 ? 7 HELX_P HELX_P8 8 MET B 214 ? ASN B 216 ? MET B 214 ASN B 216 5 ? 3 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? A CYS 22 SG ? ? ? 1_555 A CYS 90 SG ? ? A CYS 23 A CYS 92 1_555 ? ? ? ? ? ? ? 2.039 ? disulf2 disulf ? B CYS 93 SG ? ? ? 1_555 B CYS 108 SG ? ? B CYS 93 B CYS 108 1_555 ? ? ? ? ? ? ? 1.999 ? # _struct_conn_type.id disulf _struct_conn_type.criteria ? _struct_conn_type.reference ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id SER _struct_mon_prot_cis.label_seq_id 6 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id SER _struct_mon_prot_cis.auth_seq_id 7 _struct_mon_prot_cis.auth_asym_id A _struct_mon_prot_cis.pdbx_label_comp_id_2 PRO _struct_mon_prot_cis.pdbx_label_seq_id_2 7 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PRO _struct_mon_prot_cis.pdbx_auth_seq_id_2 8 _struct_mon_prot_cis.pdbx_auth_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle 1.06 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 6 ? C ? 4 ? D ? 3 ? E ? 4 ? F ? 5 ? G ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel B 1 2 ? parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel B 5 6 ? anti-parallel C 1 2 ? parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? parallel F 1 2 ? anti-parallel F 2 3 ? parallel F 3 4 ? anti-parallel F 4 5 ? anti-parallel G 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.symmetry _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 VAL A 3 ? SER A 6 ? ? VAL A 4 SER A 7 A 2 VAL A 18 ? GLN A 24 ? ? VAL A 19 GLN A 25 A 3 GLN A 72 ? LEU A 77 ? ? GLN A 74 LEU A 79 A 4 LYS A 64 ? SER A 69 ? ? LYS A 66 SER A 71 B 1 ASN A 9 ? ALA A 12 ? ? ASN A 10 ALA A 13 B 2 THR A 104 ? VAL A 108 ? ? THR A 112 VAL A 116 B 3 VAL A 87 ? GLY A 93 ? ? VAL A 89 GLY A 95 B 4 ASN A 30 ? GLN A 36 ? ? ASN A 31 GLN A 37 B 5 LEU A 42 ? GLY A 50 ? ? LEU A 43 GLY A 51 B 6 SER A 53 ? LYS A 56 ? ? SER A 54 LYS A 57 C 1 ASN A 9 ? ALA A 12 ? ? ASN A 10 ALA A 13 C 2 THR A 104 ? VAL A 108 ? ? THR A 112 VAL A 116 C 3 VAL A 87 ? GLY A 93 ? ? VAL A 89 GLY A 95 C 4 LEU A 98 ? PHE A 100 ? ? LEU A 100 PHE A 108 D 1 VAL B 33 ? VAL B 38 ? ? VAL B 33 VAL B 38 D 2 VAL B 82 ? GLY B 86 ? ? VAL B 82 GLY B 86 D 3 ILE B 113 ? LYS B 115 ? ? ILE B 113 LYS B 115 E 1 ASP B 42 ? LYS B 43 ? ? ASP B 42 LYS B 43 E 2 ASP B 48 ? TYR B 51 ? ? ASP B 48 TYR B 51 E 3 VAL B 64 ? GLU B 67 ? ? VAL B 64 GLU B 67 E 4 CYS B 108 ? TYR B 110 ? ? CYS B 108 TYR B 110 F 1 ASN B 139 ? THR B 147 ? ? ASN B 139 THR B 147 F 2 GLN B 127 ? GLU B 135 ? ? GLN B 127 GLU B 135 F 3 LYS B 227 ? THR B 234 ? ? LYS B 227 THR B 234 F 4 TYR B 179 ? GLU B 188 ? ? TYR B 179 GLU B 188 F 5 ASN B 192 ? ASP B 197 ? ? ASN B 192 ASP B 197 G 1 VAL B 152 ? THR B 153 ? ? VAL B 152 THR B 153 G 2 THR B 220 ? VAL B 221 ? ? THR B 220 VAL B 221 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N THR A 4 ? N THR A 5 O GLN A 23 ? O GLN A 24 A 2 3 N LEU A 20 ? N LEU A 21 O LEU A 75 ? O LEU A 77 A 3 4 O GLN A 72 ? O GLN A 74 N SER A 69 ? N SER A 71 B 1 2 N LYS A 10 ? N LYS A 11 O ARG A 105 ? O ARG A 113 B 2 3 O THR A 104 ? O THR A 112 N TYR A 88 ? N TYR A 90 B 3 4 O ALA A 91 ? O ALA A 93 N TYR A 32 ? N TYR A 33 B 4 5 N ARG A 35 ? N ARG A 36 O ARG A 43 ? O ARG A 44 B 5 6 N TYR A 47 ? N TYR A 48 O GLU A 55 ? O GLU A 56 C 1 2 N LYS A 10 ? N LYS A 11 O ARG A 105 ? O ARG A 113 C 2 3 O THR A 104 ? O THR A 112 N TYR A 88 ? N TYR A 90 C 3 4 N SER A 92 ? N SER A 94 O TYR A 99 ? O TYR A 101 D 1 2 N ALA B 35 ? N ALA B 35 O VAL B 84 ? O VAL B 84 D 2 3 N ASP B 83 ? N ASP B 83 O THR B 114 ? O THR B 114 E 1 2 N ASP B 42 ? N ASP B 42 O ILE B 50 ? O ILE B 50 E 2 3 N TYR B 51 ? N TYR B 51 O VAL B 64 ? O VAL B 64 E 3 4 N GLU B 67 ? N GLU B 67 O MET B 109 ? O MET B 109 F 1 2 O ILE B 141 ? O ILE B 141 N VAL B 133 ? N VAL B 133 F 2 3 N TYR B 134 ? N TYR B 134 O LEU B 232 ? O LEU B 232 F 3 4 O GLU B 229 ? O GLU B 229 N LYS B 185 ? N LYS B 185 F 4 5 N GLU B 188 ? N GLU B 188 O ASN B 192 ? O ASN B 192 G 1 2 N VAL B 152 ? N VAL B 152 O VAL B 221 ? O VAL B 221 # loop_ _struct_site.id _struct_site.details _struct_site.pdbx_evidence_code AC1 'BINDING SITE FOR RESIDUE SO4 B 500' ? AC2 'BINDING SITE FOR RESIDUE SO4 B 501' ? AC3 'BINDING SITE FOR RESIDUE SO4 B 500' SOFTWARE AC4 'BINDING SITE FOR RESIDUE SO4 B 501' SOFTWARE # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 3 LYS B 75 ? LYS B 75 . . 1_555 ? 2 AC1 3 LYS B 98 ? LYS B 98 . . 1_555 ? 3 AC1 3 ARG B 138 ? ARG B 138 . . 1_555 ? 4 AC2 3 LYS B 25 ? LYS B 25 . . 1_555 ? 5 AC2 3 GLU B 173 ? GLU B 173 . . 1_555 ? 6 AC2 3 PHE B 174 ? PHE B 174 . . 1_555 ? 7 AC3 3 LYS B 75 ? LYS B 75 . . 4_675 ? 8 AC3 3 LYS B 98 ? LYS B 98 . . 5_565 ? 9 AC3 3 ARG B 138 ? ARG B 138 . . 1_555 ? 10 AC4 3 LYS B 25 ? LYS B 25 . . 1_555 ? 11 AC4 3 GLU B 173 ? GLU B 173 . . 1_555 ? 12 AC4 3 PHE B 174 ? PHE B 174 . . 1_555 ? # _atom_sites.entry_id 3BZD _atom_sites.Cartn_transform_axes ? _atom_sites.fract_transf_matrix[1][1] 0.010312 _atom_sites.fract_transf_matrix[1][2] 0.005954 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.011908 _atom_sites.fract_transf_matrix[2][3] 0.000000 _atom_sites.fract_transf_matrix[3][1] 0.000000 _atom_sites.fract_transf_matrix[3][2] 0.000000 _atom_sites.fract_transf_matrix[3][3] 0.010810 _atom_sites.fract_transf_vector[1] 0.000000 _atom_sites.fract_transf_vector[2] 0.000000 _atom_sites.fract_transf_vector[3] 0.000000 # loop_ _atom_type.symbol N C O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.Cartn_x_esd _atom_site.Cartn_y_esd _atom_site.Cartn_z_esd _atom_site.occupancy_esd _atom_site.B_iso_or_equiv_esd _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ALA A 1 1 ? 33.763 52.112 -44.090 1.00 25.34 ? ? ? ? ? ? 2 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? 33.403 52.722 -42.739 1.00 25.11 ? ? ? ? ? ? 2 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 31.960 53.249 -42.614 1.00 24.76 ? ? ? ? ? ? 2 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? 31.694 54.512 -42.582 1.00 23.96 ? ? ? ? ? ? 2 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 34.416 53.856 -42.420 1.00 25.90 ? ? ? ? ? ? 2 ALA A CB 1 ATOM 6 N N . ALA A 1 2 ? 31.006 52.310 -42.598 1.00 22.94 ? ? ? ? ? ? 3 ALA A N 1 ATOM 7 C CA . ALA A 1 2 ? 29.599 52.628 -42.417 1.00 20.08 ? ? ? ? ? ? 3 ALA A CA 1 ATOM 8 C C . ALA A 1 2 ? 29.149 54.015 -41.825 1.00 19.99 ? ? ? ? ? ? 3 ALA A C 1 ATOM 9 O O . ALA A 1 2 ? 28.776 54.906 -42.573 1.00 20.00 ? ? ? ? ? ? 3 ALA A O 1 ATOM 10 C CB . ALA A 1 2 ? 28.955 51.482 -41.644 1.00 23.26 ? ? ? ? ? ? 3 ALA A CB 1 ATOM 11 N N . VAL A 1 3 ? 29.035 54.170 -40.506 1.00 18.40 ? ? ? ? ? ? 4 VAL A N 1 ATOM 12 C CA . VAL A 1 3 ? 28.549 55.423 -39.964 1.00 18.10 ? ? ? ? ? ? 4 VAL A CA 1 ATOM 13 C C . VAL A 1 3 ? 29.576 56.081 -38.981 1.00 20.17 ? ? ? ? ? ? 4 VAL A C 1 ATOM 14 O O . VAL A 1 3 ? 30.137 55.401 -38.110 1.00 23.21 ? ? ? ? ? ? 4 VAL A O 1 ATOM 15 C CB . VAL A 1 3 ? 27.169 55.298 -39.311 1.00 17.65 ? ? ? ? ? ? 4 VAL A CB 1 ATOM 16 C CG1 . VAL A 1 3 ? 26.698 56.664 -38.801 1.00 15.66 ? ? ? ? ? ? 4 VAL A CG1 1 ATOM 17 C CG2 . VAL A 1 3 ? 26.087 54.720 -40.311 1.00 13.28 ? ? ? ? ? ? 4 VAL A CG2 1 ATOM 18 N N . THR A 1 4 ? 29.873 57.358 -39.124 1.00 20.40 ? ? ? ? ? ? 5 THR A N 1 ATOM 19 C CA . THR A 1 4 ? 30.874 57.978 -38.197 1.00 20.85 ? ? ? ? ? ? 5 THR A CA 1 ATOM 20 C C . THR A 1 4 ? 30.306 59.193 -37.579 1.00 20.88 ? ? ? ? ? ? 5 THR A C 1 ATOM 21 O O . THR A 1 4 ? 29.679 59.984 -38.291 1.00 23.01 ? ? ? ? ? ? 5 THR A O 1 ATOM 22 C CB . THR A 1 4 ? 32.105 58.415 -38.935 1.00 19.13 ? ? ? ? ? ? 5 THR A CB 1 ATOM 23 O OG1 . THR A 1 4 ? 31.701 59.319 -39.976 1.00 20.17 ? ? ? ? ? ? 5 THR A OG1 1 ATOM 24 C CG2 . THR A 1 4 ? 32.793 57.235 -39.515 1.00 19.09 ? ? ? ? ? ? 5 THR A CG2 1 ATOM 25 N N . GLN A 1 5 ? 30.516 59.359 -36.266 1.00 22.20 ? ? ? ? ? ? 6 GLN A N 1 ATOM 26 C CA . GLN A 1 5 ? 30.067 60.585 -35.579 1.00 23.92 ? ? ? ? ? ? 6 GLN A CA 1 ATOM 27 C C . GLN A 1 5 ? 31.183 61.576 -35.350 1.00 24.16 ? ? ? ? ? ? 6 GLN A C 1 ATOM 28 O O . GLN A 1 5 ? 32.319 61.255 -35.567 1.00 24.44 ? ? ? ? ? ? 6 GLN A O 1 ATOM 29 C CB . GLN A 1 5 ? 29.374 60.216 -34.293 1.00 24.31 ? ? ? ? ? ? 6 GLN A CB 1 ATOM 30 C CG . GLN A 1 5 ? 28.414 59.048 -34.567 1.00 26.83 ? ? ? ? ? ? 6 GLN A CG 1 ATOM 31 C CD . GLN A 1 5 ? 27.650 58.653 -33.341 1.00 33.51 ? ? ? ? ? ? 6 GLN A CD 1 ATOM 32 O OE1 . GLN A 1 5 ? 27.159 57.489 -33.222 1.00 29.01 ? ? ? ? ? ? 6 GLN A OE1 1 ATOM 33 N NE2 . GLN A 1 5 ? 27.551 59.606 -32.387 1.00 30.50 ? ? ? ? ? ? 6 GLN A NE2 1 ATOM 34 N N . SER A 1 6 ? 30.858 62.793 -34.915 1.00 24.73 ? ? ? ? ? ? 7 SER A N 1 ATOM 35 C CA . SER A 1 6 ? 31.873 63.763 -34.592 1.00 24.61 ? ? ? ? ? ? 7 SER A CA 1 ATOM 36 C C . SER A 1 6 ? 31.252 64.844 -33.743 1.00 22.89 ? ? ? ? ? ? 7 SER A C 1 ATOM 37 O O . SER A 1 6 ? 30.226 65.374 -34.175 1.00 23.88 ? ? ? ? ? ? 7 SER A O 1 ATOM 38 C CB . SER A 1 6 ? 32.492 64.358 -35.868 1.00 24.52 ? ? ? ? ? ? 7 SER A CB 1 ATOM 39 O OG . SER A 1 6 ? 32.873 65.718 -35.598 1.00 29.35 ? ? ? ? ? ? 7 SER A OG 1 ATOM 40 N N . PRO A 1 7 ? 31.876 65.196 -32.575 1.00 21.61 ? ? ? ? ? ? 8 PRO A N 1 ATOM 41 C CA . PRO A 1 7 ? 33.116 64.595 -32.127 1.00 23.90 ? ? ? ? ? ? 8 PRO A CA 1 ATOM 42 C C . PRO A 1 7 ? 32.855 63.370 -31.324 1.00 25.23 ? ? ? ? ? ? 8 PRO A C 1 ATOM 43 O O . PRO A 1 7 ? 31.723 63.054 -31.034 1.00 26.87 ? ? ? ? ? ? 8 PRO A O 1 ATOM 44 C CB . PRO A 1 7 ? 33.746 65.663 -31.273 1.00 21.34 ? ? ? ? ? ? 8 PRO A CB 1 ATOM 45 C CG . PRO A 1 7 ? 32.608 66.338 -30.689 1.00 20.62 ? ? ? ? ? ? 8 PRO A CG 1 ATOM 46 C CD . PRO A 1 7 ? 31.440 66.196 -31.594 1.00 21.05 ? ? ? ? ? ? 8 PRO A CD 1 ATOM 47 N N . ARG A 1 8 ? 33.912 62.635 -31.030 1.00 30.32 ? ? ? ? ? ? 9 ARG A N 1 ATOM 48 C CA . ARG A 1 8 ? 33.769 61.344 -30.318 1.00 32.66 ? ? ? ? ? ? 9 ARG A CA 1 ATOM 49 C C . ARG A 1 8 ? 33.547 61.556 -28.814 1.00 34.51 ? ? ? ? ? ? 9 ARG A C 1 ATOM 50 O O . ARG A 1 8 ? 32.676 60.886 -28.211 1.00 34.65 ? ? ? ? ? ? 9 ARG A O 1 ATOM 51 C CB . ARG A 1 8 ? 34.960 60.411 -30.594 1.00 33.97 ? ? ? ? ? ? 9 ARG A CB 1 ATOM 52 C CG . ARG A 1 8 ? 34.579 58.965 -31.203 1.00 37.59 ? ? ? ? ? ? 9 ARG A CG 1 ATOM 53 C CD . ARG A 1 8 ? 34.574 57.847 -30.146 1.00 41.10 ? ? ? ? ? ? 9 ARG A CD 1 ATOM 54 N NE . ARG A 1 8 ? 33.525 57.998 -29.122 1.00 41.96 ? ? ? ? ? ? 9 ARG A NE 1 ATOM 55 C CZ . ARG A 1 8 ? 33.148 57.018 -28.288 1.00 46.33 ? ? ? ? ? ? 9 ARG A CZ 1 ATOM 56 N NH1 . ARG A 1 8 ? 33.734 55.823 -28.351 1.00 46.04 ? ? ? ? ? ? 9 ARG A NH1 1 ATOM 57 N NH2 . ARG A 1 8 ? 32.191 57.226 -27.381 1.00 45.03 ? ? ? ? ? ? 9 ARG A NH2 1 ATOM 58 N N . ASN A 1 9 ? 34.255 62.538 -28.252 1.00 34.63 ? ? ? ? ? ? 10 ASN A N 1 ATOM 59 C CA . ASN A 1 9 ? 34.322 62.770 -26.841 1.00 36.87 ? ? ? ? ? ? 10 ASN A CA 1 ATOM 60 C C . ASN A 1 9 ? 34.176 64.301 -26.619 1.00 37.49 ? ? ? ? ? ? 10 ASN A C 1 ATOM 61 O O . ASN A 1 9 ? 34.952 65.100 -27.222 1.00 37.87 ? ? ? ? ? ? 10 ASN A O 1 ATOM 62 C CB . ASN A 1 9 ? 35.728 62.350 -26.344 1.00 38.51 ? ? ? ? ? ? 10 ASN A CB 1 ATOM 63 C CG . ASN A 1 9 ? 35.808 60.909 -25.778 1.00 40.50 ? ? ? ? ? ? 10 ASN A CG 1 ATOM 64 O OD1 . ASN A 1 9 ? 35.289 60.621 -24.690 1.00 42.89 ? ? ? ? ? ? 10 ASN A OD1 1 ATOM 65 N ND2 . ASN A 1 9 ? 36.562 60.024 -26.478 1.00 45.07 ? ? ? ? ? ? 10 ASN A ND2 1 ATOM 66 N N . LYS A 1 10 ? 33.234 64.711 -25.756 1.00 37.13 ? ? ? ? ? ? 11 LYS A N 1 ATOM 67 C CA . LYS A 1 10 ? 32.988 66.146 -25.513 1.00 37.05 ? ? ? ? ? ? 11 LYS A CA 1 ATOM 68 C C . LYS A 1 10 ? 32.611 66.551 -24.094 1.00 37.79 ? ? ? ? ? ? 11 LYS A C 1 ATOM 69 O O . LYS A 1 10 ? 31.611 66.081 -23.547 1.00 38.26 ? ? ? ? ? ? 11 LYS A O 1 ATOM 70 C CB . LYS A 1 10 ? 31.917 66.640 -26.461 1.00 36.57 ? ? ? ? ? ? 11 LYS A CB 1 ATOM 71 C CG . LYS A 1 10 ? 31.671 68.085 -26.434 1.00 34.46 ? ? ? ? ? ? 11 LYS A CG 1 ATOM 72 C CD . LYS A 1 10 ? 32.930 68.874 -26.804 1.00 34.83 ? ? ? ? ? ? 11 LYS A CD 1 ATOM 73 C CE . LYS A 1 10 ? 32.640 70.397 -26.761 1.00 30.64 ? ? ? ? ? ? 11 LYS A CE 1 ATOM 74 N NZ . LYS A 1 10 ? 31.514 70.805 -27.599 1.00 22.67 ? ? ? ? ? ? 11 LYS A NZ 1 ATOM 75 N N . VAL A 1 11 ? 33.386 67.505 -23.554 1.00 38.60 ? ? ? ? ? ? 12 VAL A N 1 ATOM 76 C CA . VAL A 1 11 ? 33.166 68.115 -22.222 1.00 38.63 ? ? ? ? ? ? 12 VAL A CA 1 ATOM 77 C C . VAL A 1 11 ? 32.833 69.600 -22.304 1.00 37.84 ? ? ? ? ? ? 12 VAL A C 1 ATOM 78 O O . VAL A 1 11 ? 33.705 70.410 -22.575 1.00 37.68 ? ? ? ? ? ? 12 VAL A O 1 ATOM 79 C CB . VAL A 1 11 ? 34.436 68.044 -21.367 1.00 38.68 ? ? ? ? ? ? 12 VAL A CB 1 ATOM 80 C CG1 . VAL A 1 11 ? 34.455 66.783 -20.594 1.00 36.81 ? ? ? ? ? ? 12 VAL A CG1 1 ATOM 81 C CG2 . VAL A 1 11 ? 35.698 68.267 -22.244 1.00 39.25 ? ? ? ? ? ? 12 VAL A CG2 1 ATOM 82 N N . ALA A 1 12 ? 31.582 69.958 -22.048 1.00 38.24 ? ? ? ? ? ? 13 ALA A N 1 ATOM 83 C CA . ALA A 1 12 ? 31.154 71.334 -22.244 1.00 37.91 ? ? ? ? ? ? 13 ALA A CA 1 ATOM 84 C C . ALA A 1 12 ? 30.518 71.865 -20.969 1.00 38.80 ? ? ? ? ? ? 13 ALA A C 1 ATOM 85 O O . ALA A 1 12 ? 29.977 71.078 -20.172 1.00 40.28 ? ? ? ? ? ? 13 ALA A O 1 ATOM 86 C CB . ALA A 1 12 ? 30.206 71.429 -23.445 1.00 36.72 ? ? ? ? ? ? 13 ALA A CB 1 ATOM 87 N N . VAL A 1 13 ? 30.572 73.184 -20.774 1.00 38.57 ? ? ? ? ? ? 14 VAL A N 1 ATOM 88 C CA . VAL A 1 13 ? 30.029 73.826 -19.562 1.00 37.61 ? ? ? ? ? ? 14 VAL A CA 1 ATOM 89 C C . VAL A 1 13 ? 28.509 74.033 -19.608 1.00 37.37 ? ? ? ? ? ? 14 VAL A C 1 ATOM 90 O O . VAL A 1 13 ? 27.928 74.222 -20.657 1.00 37.41 ? ? ? ? ? ? 14 VAL A O 1 ATOM 91 C CB . VAL A 1 13 ? 30.786 75.122 -19.224 1.00 37.15 ? ? ? ? ? ? 14 VAL A CB 1 ATOM 92 C CG1 . VAL A 1 13 ? 32.258 74.813 -18.990 1.00 39.31 ? ? ? ? ? ? 14 VAL A CG1 1 ATOM 93 C CG2 . VAL A 1 13 ? 30.659 76.145 -20.333 1.00 36.96 ? ? ? ? ? ? 14 VAL A CG2 1 ATOM 94 N N . THR A 1 14 ? 27.833 73.972 -18.484 1.00 37.50 ? ? ? ? ? ? 15 THR A N 1 ATOM 95 C CA . THR A 1 14 ? 26.374 74.084 -18.570 1.00 38.08 ? ? ? ? ? ? 15 THR A CA 1 ATOM 96 C C . THR A 1 14 ? 26.081 75.446 -19.119 1.00 38.88 ? ? ? ? ? ? 15 THR A C 1 ATOM 97 O O . THR A 1 14 ? 26.546 76.448 -18.589 1.00 38.13 ? ? ? ? ? ? 15 THR A O 1 ATOM 98 C CB . THR A 1 14 ? 25.740 73.917 -17.219 1.00 38.28 ? ? ? ? ? ? 15 THR A CB 1 ATOM 99 O OG1 . THR A 1 14 ? 26.179 72.659 -16.708 1.00 37.16 ? ? ? ? ? ? 15 THR A OG1 1 ATOM 100 C CG2 . THR A 1 14 ? 24.211 73.945 -17.270 1.00 33.98 ? ? ? ? ? ? 15 THR A CG2 1 ATOM 101 N N . GLY A 1 15 ? 25.378 75.454 -20.243 1.00 40.38 ? ? ? ? ? ? 16 GLY A N 1 ATOM 102 C CA . GLY A 1 15 ? 25.006 76.708 -20.944 1.00 40.95 ? ? ? ? ? ? 16 GLY A CA 1 ATOM 103 C C . GLY A 1 15 ? 25.235 76.682 -22.453 1.00 41.28 ? ? ? ? ? ? 16 GLY A C 1 ATOM 104 O O . GLY A 1 15 ? 24.284 76.759 -23.237 1.00 41.72 ? ? ? ? ? ? 16 GLY A O 1 ATOM 105 N N . GLU A 1 16 ? 26.507 76.545 -22.845 1.00 40.82 ? ? ? ? ? ? 17 GLU A N 1 ATOM 106 C CA . GLU A 1 16 ? 26.917 76.561 -24.222 1.00 39.97 ? ? ? ? ? ? 17 GLU A CA 1 ATOM 107 C C . GLU A 1 16 ? 26.090 75.713 -25.162 1.00 39.45 ? ? ? ? ? ? 17 GLU A C 1 ATOM 108 O O . GLU A 1 16 ? 25.424 74.709 -24.773 1.00 41.25 ? ? ? ? ? ? 17 GLU A O 1 ATOM 109 C CB . GLU A 1 16 ? 28.383 76.194 -24.313 1.00 39.94 ? ? ? ? ? ? 17 GLU A CB 1 ATOM 110 C CG . GLU A 1 16 ? 28.705 74.768 -24.699 1.00 42.31 ? ? ? ? ? ? 17 GLU A CG 1 ATOM 111 C CD . GLU A 1 16 ? 30.173 74.663 -25.044 1.00 46.41 ? ? ? ? ? ? 17 GLU A CD 1 ATOM 112 O OE1 . GLU A 1 16 ? 30.997 74.973 -24.160 1.00 50.97 ? ? ? ? ? ? 17 GLU A OE1 1 ATOM 113 O OE2 . GLU A 1 16 ? 30.528 74.333 -26.192 1.00 47.31 ? ? ? ? ? ? 17 GLU A OE2 1 ATOM 114 N N . LYS A 1 17 ? 26.162 76.106 -26.423 1.00 38.14 ? ? ? ? ? ? 18 LYS A N 1 ATOM 115 C CA . LYS A 1 17 ? 25.390 75.490 -27.489 1.00 36.59 ? ? ? ? ? ? 18 LYS A CA 1 ATOM 116 C C . LYS A 1 17 ? 26.189 74.336 -28.077 1.00 35.70 ? ? ? ? ? ? 18 LYS A C 1 ATOM 117 O O . LYS A 1 17 ? 27.186 74.553 -28.726 1.00 35.80 ? ? ? ? ? ? 18 LYS A O 1 ATOM 118 C CB . LYS A 1 17 ? 25.078 76.547 -28.555 1.00 35.73 ? ? ? ? ? ? 18 LYS A CB 1 ATOM 119 C CG . LYS A 1 17 ? 24.642 75.967 -29.873 1.00 35.86 ? ? ? ? ? ? 18 LYS A CG 1 ATOM 120 C CD . LYS A 1 17 ? 24.304 77.030 -30.889 1.00 32.18 ? ? ? ? ? ? 18 LYS A CD 1 ATOM 121 C CE . LYS A 1 17 ? 23.847 76.454 -32.203 1.00 30.56 ? ? ? ? ? ? 18 LYS A CE 1 ATOM 122 N NZ . LYS A 1 17 ? 23.525 77.616 -33.110 1.00 28.09 ? ? ? ? ? ? 18 LYS A NZ 1 ATOM 123 N N . VAL A 1 18 ? 25.740 73.104 -27.883 1.00 34.54 ? ? ? ? ? ? 19 VAL A N 1 ATOM 124 C CA . VAL A 1 18 ? 26.489 72.024 -28.480 1.00 33.14 ? ? ? ? ? ? 19 VAL A CA 1 ATOM 125 C C . VAL A 1 18 ? 25.814 71.336 -29.702 1.00 31.93 ? ? ? ? ? ? 19 VAL A C 1 ATOM 126 O O . VAL A 1 18 ? 24.659 70.939 -29.621 1.00 30.42 ? ? ? ? ? ? 19 VAL A O 1 ATOM 127 C CB . VAL A 1 18 ? 26.948 71.030 -27.399 1.00 32.22 ? ? ? ? ? ? 19 VAL A CB 1 ATOM 128 C CG1 . VAL A 1 18 ? 27.930 70.120 -27.985 1.00 33.61 ? ? ? ? ? ? 19 VAL A CG1 1 ATOM 129 C CG2 . VAL A 1 18 ? 27.634 71.795 -26.270 1.00 32.41 ? ? ? ? ? ? 19 VAL A CG2 1 ATOM 130 N N . THR A 1 19 ? 26.586 71.154 -30.793 1.00 30.75 ? ? ? ? ? ? 20 THR A N 1 ATOM 131 C CA . THR A 1 19 ? 26.129 70.433 -32.017 1.00 30.63 ? ? ? ? ? ? 20 THR A CA 1 ATOM 132 C C . THR A 1 19 ? 26.803 69.064 -32.325 1.00 29.61 ? ? ? ? ? ? 20 THR A C 1 ATOM 133 O O . THR A 1 19 ? 28.002 68.986 -32.412 1.00 28.29 ? ? ? ? ? ? 20 THR A O 1 ATOM 134 C CB . THR A 1 19 ? 26.358 71.321 -33.227 1.00 30.22 ? ? ? ? ? ? 20 THR A CB 1 ATOM 135 O OG1 . THR A 1 19 ? 26.098 72.665 -32.851 1.00 33.58 ? ? ? ? ? ? 20 THR A OG1 1 ATOM 136 C CG2 . THR A 1 19 ? 25.454 70.942 -34.404 1.00 33.21 ? ? ? ? ? ? 20 THR A CG2 1 ATOM 137 N N . LEU A 1 20 ? 26.040 67.994 -32.533 1.00 29.29 ? ? ? ? ? ? 21 LEU A N 1 ATOM 138 C CA . LEU A 1 20 ? 26.700 66.703 -32.864 1.00 27.84 ? ? ? ? ? ? 21 LEU A CA 1 ATOM 139 C C . LEU A 1 20 ? 26.557 66.244 -34.315 1.00 27.04 ? ? ? ? ? ? 21 LEU A C 1 ATOM 140 O O . LEU A 1 20 ? 25.477 65.992 -34.733 1.00 27.86 ? ? ? ? ? ? 21 LEU A O 1 ATOM 141 C CB . LEU A 1 20 ? 26.195 65.601 -31.949 1.00 27.07 ? ? ? ? ? ? 21 LEU A CB 1 ATOM 142 C CG . LEU A 1 20 ? 26.733 65.616 -30.538 1.00 26.22 ? ? ? ? ? ? 21 LEU A CG 1 ATOM 143 C CD1 . LEU A 1 20 ? 26.467 64.263 -30.005 1.00 22.98 ? ? ? ? ? ? 21 LEU A CD1 1 ATOM 144 C CD2 . LEU A 1 20 ? 28.210 65.836 -30.545 1.00 24.93 ? ? ? ? ? ? 21 LEU A CD2 1 ATOM 145 N N . SER A 1 21 ? 27.666 66.097 -35.041 1.00 26.93 ? ? ? ? ? ? 22 SER A N 1 ATOM 146 C CA . SER A 1 21 ? 27.686 65.831 -36.452 1.00 25.10 ? ? ? ? ? ? 22 SER A CA 1 ATOM 147 C C . SER A 1 21 ? 27.878 64.323 -36.752 1.00 25.45 ? ? ? ? ? ? 22 SER A C 1 ATOM 148 O O . SER A 1 21 ? 28.824 63.705 -36.279 1.00 25.57 ? ? ? ? ? ? 22 SER A O 1 ATOM 149 C CB . SER A 1 21 ? 28.845 66.590 -37.029 1.00 25.68 ? ? ? ? ? ? 22 SER A CB 1 ATOM 150 O OG . SER A 1 21 ? 30.064 66.188 -36.403 1.00 23.64 ? ? ? ? ? ? 22 SER A OG 1 ATOM 151 N N . CYS A 1 22 ? 26.991 63.763 -37.572 1.00 24.02 ? ? ? ? ? ? 23 CYS A N 1 ATOM 152 C CA . CYS A 1 22 ? 27.004 62.372 -37.923 1.00 22.83 ? ? ? ? ? ? 23 CYS A CA 1 ATOM 153 C C . CYS A 1 22 ? 26.979 62.271 -39.446 1.00 23.31 ? ? ? ? ? ? 23 CYS A C 1 ATOM 154 O O . CYS A 1 22 ? 26.279 63.033 -40.098 1.00 23.51 ? ? ? ? ? ? 23 CYS A O 1 ATOM 155 C CB . CYS A 1 22 ? 25.766 61.690 -37.327 1.00 21.98 ? ? ? ? ? ? 23 CYS A CB 1 ATOM 156 S SG . CYS A 1 22 ? 25.500 60.064 -38.017 1.00 27.28 ? ? ? ? ? ? 23 CYS A SG 1 ATOM 157 N N . GLN A 1 23 ? 27.724 61.334 -40.069 1.00 24.11 ? ? ? ? ? ? 24 GLN A N 1 ATOM 158 C CA . GLN A 1 23 ? 27.667 61.306 -41.533 1.00 22.59 ? ? ? ? ? ? 24 GLN A CA 1 ATOM 159 C C . GLN A 1 23 ? 27.779 59.925 -42.002 1.00 21.63 ? ? ? ? ? ? 24 GLN A C 1 ATOM 160 O O . GLN A 1 23 ? 28.489 59.172 -41.354 1.00 24.40 ? ? ? ? ? ? 24 GLN A O 1 ATOM 161 C CB . GLN A 1 23 ? 28.770 62.176 -42.143 1.00 21.88 ? ? ? ? ? ? 24 GLN A CB 1 ATOM 162 C CG . GLN A 1 23 ? 30.159 61.762 -41.757 1.00 21.77 ? ? ? ? ? ? 24 GLN A CG 1 ATOM 163 C CD . GLN A 1 23 ? 31.178 62.618 -42.429 1.00 26.24 ? ? ? ? ? ? 24 GLN A CD 1 ATOM 164 O OE1 . GLN A 1 23 ? 31.091 63.863 -42.343 1.00 29.92 ? ? ? ? ? ? 24 GLN A OE1 1 ATOM 165 N NE2 . GLN A 1 23 ? 32.140 61.991 -43.145 1.00 24.42 ? ? ? ? ? ? 24 GLN A NE2 1 ATOM 166 N N . GLN A 1 24 ? 27.160 59.595 -43.134 1.00 20.02 ? ? ? ? ? ? 25 GLN A N 1 ATOM 167 C CA . GLN A 1 24 ? 27.124 58.224 -43.673 1.00 21.13 ? ? ? ? ? ? 25 GLN A CA 1 ATOM 168 C C . GLN A 1 24 ? 27.819 58.088 -45.004 1.00 20.72 ? ? ? ? ? ? 25 GLN A C 1 ATOM 169 O O . GLN A 1 24 ? 28.362 59.074 -45.564 1.00 22.35 ? ? ? ? ? ? 25 GLN A O 1 ATOM 170 C CB . GLN A 1 24 ? 25.756 57.546 -43.767 1.00 19.39 ? ? ? ? ? ? 25 GLN A CB 1 ATOM 171 C CG . GLN A 1 24 ? 24.519 58.524 -43.955 1.00 20.36 ? ? ? ? ? ? 25 GLN A CG 1 ATOM 172 C CD . GLN A 1 24 ? 23.359 57.917 -44.753 1.00 23.09 ? ? ? ? ? ? 25 GLN A CD 1 ATOM 173 O OE1 . GLN A 1 24 ? 22.679 56.907 -44.328 1.00 19.57 ? ? ? ? ? ? 25 GLN A OE1 1 ATOM 174 N NE2 . GLN A 1 24 ? 23.099 58.545 -45.937 1.00 16.66 ? ? ? ? ? ? 25 GLN A NE2 1 ATOM 175 N N . THR A 1 25 ? 27.877 56.829 -45.457 1.00 18.37 ? ? ? ? ? ? 26 THR A N 1 ATOM 176 C CA . THR A 1 25 ? 28.528 56.500 -46.708 1.00 16.35 ? ? ? ? ? ? 26 THR A CA 1 ATOM 177 C C . THR A 1 25 ? 27.721 55.440 -47.431 1.00 17.39 ? ? ? ? ? ? 26 THR A C 1 ATOM 178 O O . THR A 1 25 ? 27.938 55.242 -48.615 1.00 17.50 ? ? ? ? ? ? 26 THR A O 1 ATOM 179 C CB . THR A 1 25 ? 29.959 56.011 -46.482 1.00 16.16 ? ? ? ? ? ? 26 THR A CB 1 ATOM 180 O OG1 . THR A 1 25 ? 29.910 54.845 -45.647 1.00 11.99 ? ? ? ? ? ? 26 THR A OG1 1 ATOM 181 C CG2 . THR A 1 25 ? 30.757 57.080 -45.751 1.00 13.64 ? ? ? ? ? ? 26 THR A CG2 1 ATOM 182 N N . ASN A 1 26 ? 26.734 54.815 -46.773 1.00 17.97 ? ? ? ? ? ? 27 ASN A N 1 ATOM 183 C CA . ASN A 1 26 ? 25.938 53.826 -47.485 1.00 18.36 ? ? ? ? ? ? 27 ASN A CA 1 ATOM 184 C C . ASN A 1 26 ? 24.715 54.509 -47.983 1.00 18.04 ? ? ? ? ? ? 27 ASN A C 1 ATOM 185 O O . ASN A 1 26 ? 23.783 53.876 -48.453 1.00 18.57 ? ? ? ? ? ? 27 ASN A O 1 ATOM 186 C CB . ASN A 1 26 ? 25.558 52.683 -46.505 1.00 20.73 ? ? ? ? ? ? 27 ASN A CB 1 ATOM 187 C CG . ASN A 1 26 ? 25.725 51.289 -47.098 1.00 24.04 ? ? ? ? ? ? 27 ASN A CG 1 ATOM 188 O OD1 . ASN A 1 26 ? 26.831 50.715 -47.091 1.00 29.48 ? ? ? ? ? ? 27 ASN A OD1 1 ATOM 189 N ND2 . ASN A 1 26 ? 24.608 50.706 -47.571 1.00 30.58 ? ? ? ? ? ? 27 ASN A ND2 1 ATOM 190 N N . ASN A 1 27 ? 24.671 55.826 -47.792 1.00 20.40 ? ? ? ? ? ? 28 ASN A N 1 ATOM 191 C CA . ASN A 1 27 ? 23.537 56.642 -48.189 1.00 19.02 ? ? ? ? ? ? 28 ASN A CA 1 ATOM 192 C C . ASN A 1 27 ? 22.188 55.904 -47.921 1.00 19.71 ? ? ? ? ? ? 28 ASN A C 1 ATOM 193 O O . ASN A 1 27 ? 21.534 55.410 -48.886 1.00 19.66 ? ? ? ? ? ? 28 ASN A O 1 ATOM 194 C CB . ASN A 1 27 ? 23.680 56.862 -49.657 1.00 20.31 ? ? ? ? ? ? 28 ASN A CB 1 ATOM 195 C CG . ASN A 1 27 ? 24.155 58.217 -50.032 1.00 20.99 ? ? ? ? ? ? 28 ASN A CG 1 ATOM 196 O OD1 . ASN A 1 27 ? 23.445 59.211 -49.917 1.00 27.80 ? ? ? ? ? ? 28 ASN A OD1 1 ATOM 197 N ND2 . ASN A 1 27 ? 25.368 58.270 -50.570 1.00 24.27 ? ? ? ? ? ? 28 ASN A ND2 1 ATOM 198 N N . HIS A 1 28 ? 21.795 55.744 -46.648 1.00 18.69 ? ? ? ? ? ? 29 HIS A N 1 ATOM 199 C CA . HIS A 1 28 ? 20.457 55.153 -46.346 1.00 18.06 ? ? ? ? ? ? 29 HIS A CA 1 ATOM 200 C C . HIS A 1 28 ? 19.444 56.308 -46.121 1.00 16.73 ? ? ? ? ? ? 29 HIS A C 1 ATOM 201 O O . HIS A 1 28 ? 19.811 57.331 -45.565 1.00 20.04 ? ? ? ? ? ? 29 HIS A O 1 ATOM 202 C CB . HIS A 1 28 ? 20.507 54.337 -45.095 1.00 17.41 ? ? ? ? ? ? 29 HIS A CB 1 ATOM 203 C CG . HIS A 1 28 ? 21.021 52.959 -45.269 1.00 19.31 ? ? ? ? ? ? 29 HIS A CG 1 ATOM 204 N ND1 . HIS A 1 28 ? 20.203 51.888 -45.553 1.00 16.65 ? ? ? ? ? ? 29 HIS A ND1 1 ATOM 205 C CD2 . HIS A 1 28 ? 22.258 52.452 -45.058 1.00 21.43 ? ? ? ? ? ? 29 HIS A CD2 1 ATOM 206 C CE1 . HIS A 1 28 ? 20.941 50.796 -45.604 1.00 25.33 ? ? ? ? ? ? 29 HIS A CE1 1 ATOM 207 N NE2 . HIS A 1 28 ? 22.191 51.109 -45.304 1.00 22.12 ? ? ? ? ? ? 29 HIS A NE2 1 ATOM 208 N N . ASN A 1 29 ? 18.211 56.170 -46.565 1.00 16.43 ? ? ? ? ? ? 30 ASN A N 1 ATOM 209 C CA . ASN A 1 29 ? 17.159 57.197 -46.310 1.00 17.97 ? ? ? ? ? ? 30 ASN A CA 1 ATOM 210 C C . ASN A 1 29 ? 17.031 57.559 -44.839 1.00 16.70 ? ? ? ? ? ? 30 ASN A C 1 ATOM 211 O O . ASN A 1 29 ? 17.239 58.757 -44.450 1.00 17.12 ? ? ? ? ? ? 30 ASN A O 1 ATOM 212 C CB . ASN A 1 29 ? 15.761 56.739 -46.736 1.00 17.02 ? ? ? ? ? ? 30 ASN A CB 1 ATOM 213 C CG . ASN A 1 29 ? 15.515 56.891 -48.242 1.00 22.50 ? ? ? ? ? ? 30 ASN A CG 1 ATOM 214 O OD1 . ASN A 1 29 ? 15.136 57.977 -48.709 1.00 18.29 ? ? ? ? ? ? 30 ASN A OD1 1 ATOM 215 N ND2 . ASN A 1 29 ? 15.689 55.759 -49.011 1.00 22.63 ? ? ? ? ? ? 30 ASN A ND2 1 ATOM 216 N N . ASN A 1 30 ? 16.761 56.515 -44.054 1.00 11.02 ? ? ? ? ? ? 31 ASN A N 1 ATOM 217 C CA . ASN A 1 30 ? 16.530 56.652 -42.671 1.00 9.90 ? ? ? ? ? ? 31 ASN A CA 1 ATOM 218 C C . ASN A 1 30 ? 17.818 56.798 -41.902 1.00 6.58 ? ? ? ? ? ? 31 ASN A C 1 ATOM 219 O O . ASN A 1 30 ? 18.694 55.898 -41.955 1.00 4.85 ? ? ? ? ? ? 31 ASN A O 1 ATOM 220 C CB . ASN A 1 30 ? 15.760 55.424 -42.145 1.00 6.98 ? ? ? ? ? ? 31 ASN A CB 1 ATOM 221 C CG . ASN A 1 30 ? 14.467 55.180 -42.966 1.00 14.28 ? ? ? ? ? ? 31 ASN A CG 1 ATOM 222 O OD1 . ASN A 1 30 ? 13.762 56.123 -43.321 1.00 7.84 ? ? ? ? ? ? 31 ASN A OD1 1 ATOM 223 N ND2 . ASN A 1 30 ? 14.218 53.914 -43.341 1.00 16.55 ? ? ? ? ? ? 31 ASN A ND2 1 ATOM 224 N N . MET A 1 31 ? 17.807 57.813 -41.093 1.00 5.23 ? ? ? ? ? ? 32 MET A N 1 ATOM 225 C CA . MET A 1 31 ? 18.898 58.140 -40.201 1.00 7.27 ? ? ? ? ? ? 32 MET A CA 1 ATOM 226 C C . MET A 1 31 ? 18.254 58.442 -38.836 1.00 8.07 ? ? ? ? ? ? 32 MET A C 1 ATOM 227 O O . MET A 1 31 ? 17.211 58.997 -38.766 1.00 8.99 ? ? ? ? ? ? 32 MET A O 1 ATOM 228 C CB . MET A 1 31 ? 19.672 59.387 -40.702 1.00 3.95 ? ? ? ? ? ? 32 MET A CB 1 ATOM 229 C CG . MET A 1 31 ? 20.577 59.136 -41.919 1.00 5.49 ? ? ? ? ? ? 32 MET A CG 1 ATOM 230 S SD . MET A 1 31 ? 21.698 60.644 -42.175 1.00 5.77 ? ? ? ? ? ? 32 MET A SD 1 ATOM 231 C CE . MET A 1 31 ? 22.930 60.281 -40.924 1.00 2.69 ? ? ? ? ? ? 32 MET A CE 1 ATOM 232 N N . TYR A 1 32 ? 18.939 58.049 -37.781 1.00 10.23 ? ? ? ? ? ? 33 TYR A N 1 ATOM 233 C CA . TYR A 1 32 ? 18.485 58.134 -36.453 1.00 11.65 ? ? ? ? ? ? 33 TYR A CA 1 ATOM 234 C C . TYR A 1 32 ? 19.529 58.685 -35.519 1.00 13.00 ? ? ? ? ? ? 33 TYR A C 1 ATOM 235 O O . TYR A 1 32 ? 20.745 58.482 -35.738 1.00 14.80 ? ? ? ? ? ? 33 TYR A O 1 ATOM 236 C CB . TYR A 1 32 ? 18.183 56.755 -35.952 1.00 8.27 ? ? ? ? ? ? 33 TYR A CB 1 ATOM 237 C CG . TYR A 1 32 ? 17.172 55.995 -36.797 1.00 9.16 ? ? ? ? ? ? 33 TYR A CG 1 ATOM 238 C CD1 . TYR A 1 32 ? 17.567 55.372 -37.947 1.00 9.60 ? ? ? ? ? ? 33 TYR A CD1 1 ATOM 239 C CD2 . TYR A 1 32 ? 15.875 55.813 -36.394 1.00 8.35 ? ? ? ? ? ? 33 TYR A CD2 1 ATOM 240 C CE1 . TYR A 1 32 ? 16.726 54.629 -38.655 1.00 8.48 ? ? ? ? ? ? 33 TYR A CE1 1 ATOM 241 C CE2 . TYR A 1 32 ? 14.994 55.044 -37.161 1.00 4.06 ? ? ? ? ? ? 33 TYR A CE2 1 ATOM 242 C CZ . TYR A 1 32 ? 15.412 54.492 -38.272 1.00 2.00 ? ? ? ? ? ? 33 TYR A CZ 1 ATOM 243 O OH . TYR A 1 32 ? 14.651 53.753 -39.062 1.00 2.00 ? ? ? ? ? ? 33 TYR A OH 1 ATOM 244 N N . TRP A 1 33 ? 19.017 59.313 -34.456 1.00 12.47 ? ? ? ? ? ? 34 TRP A N 1 ATOM 245 C CA . TRP A 1 33 ? 19.789 59.833 -33.397 1.00 14.01 ? ? ? ? ? ? 34 TRP A CA 1 ATOM 246 C C . TRP A 1 33 ? 19.380 59.348 -32.091 1.00 14.80 ? ? ? ? ? ? 34 TRP A C 1 ATOM 247 O O . TRP A 1 33 ? 18.295 59.679 -31.673 1.00 13.65 ? ? ? ? ? ? 34 TRP A O 1 ATOM 248 C CB . TRP A 1 33 ? 19.719 61.354 -33.312 1.00 14.33 ? ? ? ? ? ? 34 TRP A CB 1 ATOM 249 C CG . TRP A 1 33 ? 21.039 62.043 -33.708 1.00 14.58 ? ? ? ? ? ? 34 TRP A CG 1 ATOM 250 C CD1 . TRP A 1 33 ? 21.164 63.184 -34.489 1.00 21.03 ? ? ? ? ? ? 34 TRP A CD1 1 ATOM 251 C CD2 . TRP A 1 33 ? 22.393 61.706 -33.337 1.00 21.37 ? ? ? ? ? ? 34 TRP A CD2 1 ATOM 252 N NE1 . TRP A 1 33 ? 22.489 63.581 -34.609 1.00 18.93 ? ? ? ? ? ? 34 TRP A NE1 1 ATOM 253 C CE2 . TRP A 1 33 ? 23.268 62.656 -33.967 1.00 22.46 ? ? ? ? ? ? 34 TRP A CE2 1 ATOM 254 C CE3 . TRP A 1 33 ? 22.966 60.679 -32.611 1.00 22.42 ? ? ? ? ? ? 34 TRP A CE3 1 ATOM 255 C CZ2 . TRP A 1 33 ? 24.640 62.626 -33.817 1.00 16.69 ? ? ? ? ? ? 34 TRP A CZ2 1 ATOM 256 C CZ3 . TRP A 1 33 ? 24.360 60.669 -32.487 1.00 19.46 ? ? ? ? ? ? 34 TRP A CZ3 1 ATOM 257 C CH2 . TRP A 1 33 ? 25.156 61.624 -33.089 1.00 16.75 ? ? ? ? ? ? 34 TRP A CH2 1 ATOM 258 N N . TYR A 1 34 ? 20.318 58.700 -31.373 1.00 16.59 ? ? ? ? ? ? 35 TYR A N 1 ATOM 259 C CA . TYR A 1 34 ? 20.025 58.048 -30.110 1.00 19.53 ? ? ? ? ? ? 35 TYR A CA 1 ATOM 260 C C . TYR A 1 34 ? 20.770 58.434 -28.838 1.00 23.24 ? ? ? ? ? ? 35 TYR A C 1 ATOM 261 O O . TYR A 1 34 ? 21.798 59.136 -28.807 1.00 23.03 ? ? ? ? ? ? 35 TYR A O 1 ATOM 262 C CB . TYR A 1 34 ? 20.165 56.517 -30.238 1.00 19.62 ? ? ? ? ? ? 35 TYR A CB 1 ATOM 263 C CG . TYR A 1 34 ? 19.116 55.815 -31.007 1.00 17.41 ? ? ? ? ? ? 35 TYR A CG 1 ATOM 264 C CD1 . TYR A 1 34 ? 19.385 55.211 -32.233 1.00 24.24 ? ? ? ? ? ? 35 TYR A CD1 1 ATOM 265 C CD2 . TYR A 1 34 ? 17.824 55.757 -30.540 1.00 26.35 ? ? ? ? ? ? 35 TYR A CD2 1 ATOM 266 C CE1 . TYR A 1 34 ? 18.329 54.539 -32.996 1.00 23.20 ? ? ? ? ? ? 35 TYR A CE1 1 ATOM 267 C CE2 . TYR A 1 34 ? 16.774 55.105 -31.289 1.00 23.93 ? ? ? ? ? ? 35 TYR A CE2 1 ATOM 268 C CZ . TYR A 1 34 ? 17.047 54.502 -32.502 1.00 18.60 ? ? ? ? ? ? 35 TYR A CZ 1 ATOM 269 O OH . TYR A 1 34 ? 16.022 53.857 -33.132 1.00 18.41 ? ? ? ? ? ? 35 TYR A OH 1 ATOM 270 N N . ARG A 1 35 ? 20.215 57.924 -27.745 1.00 26.23 ? ? ? ? ? ? 36 ARG A N 1 ATOM 271 C CA . ARG A 1 35 ? 20.751 58.211 -26.419 1.00 28.69 ? ? ? ? ? ? 36 ARG A CA 1 ATOM 272 C C . ARG A 1 35 ? 20.212 57.170 -25.494 1.00 28.15 ? ? ? ? ? ? 36 ARG A C 1 ATOM 273 O O . ARG A 1 35 ? 19.027 56.836 -25.571 1.00 28.01 ? ? ? ? ? ? 36 ARG A O 1 ATOM 274 C CB . ARG A 1 35 ? 20.285 59.583 -25.939 1.00 27.85 ? ? ? ? ? ? 36 ARG A CB 1 ATOM 275 C CG . ARG A 1 35 ? 20.493 59.755 -24.462 1.00 31.16 ? ? ? ? ? ? 36 ARG A CG 1 ATOM 276 C CD . ARG A 1 35 ? 19.602 60.811 -23.864 1.00 33.89 ? ? ? ? ? ? 36 ARG A CD 1 ATOM 277 N NE . ARG A 1 35 ? 20.211 61.355 -22.672 1.00 36.37 ? ? ? ? ? ? 36 ARG A NE 1 ATOM 278 C CZ . ARG A 1 35 ? 19.768 62.446 -22.062 1.00 41.06 ? ? ? ? ? ? 36 ARG A CZ 1 ATOM 279 N NH1 . ARG A 1 35 ? 18.687 63.103 -22.518 1.00 39.15 ? ? ? ? ? ? 36 ARG A NH1 1 ATOM 280 N NH2 . ARG A 1 35 ? 20.414 62.881 -20.979 1.00 45.24 ? ? ? ? ? ? 36 ARG A NH2 1 ATOM 281 N N . GLN A 1 36 ? 21.052 56.654 -24.618 1.00 27.73 ? ? ? ? ? ? 37 GLN A N 1 ATOM 282 C CA . GLN A 1 36 ? 20.513 55.667 -23.666 1.00 29.93 ? ? ? ? ? ? 37 GLN A CA 1 ATOM 283 C C . GLN A 1 36 ? 20.937 55.839 -22.220 1.00 32.10 ? ? ? ? ? ? 37 GLN A C 1 ATOM 284 O O . GLN A 1 36 ? 22.045 56.329 -21.956 1.00 31.45 ? ? ? ? ? ? 37 GLN A O 1 ATOM 285 C CB . GLN A 1 36 ? 20.940 54.259 -24.103 1.00 28.84 ? ? ? ? ? ? 37 GLN A CB 1 ATOM 286 C CG . GLN A 1 36 ? 22.207 53.757 -23.477 1.00 28.69 ? ? ? ? ? ? 37 GLN A CG 1 ATOM 287 C CD . GLN A 1 36 ? 23.398 54.608 -23.778 1.00 28.99 ? ? ? ? ? ? 37 GLN A CD 1 ATOM 288 O OE1 . GLN A 1 36 ? 23.312 55.848 -23.782 1.00 31.15 ? ? ? ? ? ? 37 GLN A OE1 1 ATOM 289 N NE2 . GLN A 1 36 ? 24.542 53.954 -23.997 1.00 31.03 ? ? ? ? ? ? 37 GLN A NE2 1 ATOM 290 N N . ASP A 1 37 ? 20.091 55.359 -21.292 1.00 35.15 ? ? ? ? ? ? 38 ASP A N 1 ATOM 291 C CA . ASP A 1 37 ? 20.347 55.510 -19.830 1.00 37.59 ? ? ? ? ? ? 38 ASP A CA 1 ATOM 292 C C . ASP A 1 37 ? 21.750 54.926 -19.513 1.00 39.77 ? ? ? ? ? ? 38 ASP A C 1 ATOM 293 O O . ASP A 1 37 ? 22.144 53.892 -20.107 1.00 39.61 ? ? ? ? ? ? 38 ASP A O 1 ATOM 294 C CB . ASP A 1 37 ? 19.246 54.830 -18.980 1.00 37.64 ? ? ? ? ? ? 38 ASP A CB 1 ATOM 295 C CG . ASP A 1 37 ? 17.786 55.219 -19.403 1.00 40.45 ? ? ? ? ? ? 38 ASP A CG 1 ATOM 296 O OD1 . ASP A 1 37 ? 16.827 54.657 -18.785 1.00 43.63 ? ? ? ? ? ? 38 ASP A OD1 1 ATOM 297 O OD2 . ASP A 1 37 ? 17.596 56.075 -20.341 1.00 42.66 ? ? ? ? ? ? 38 ASP A OD2 1 ATOM 298 N N . THR A 1 38 ? 22.522 55.610 -18.641 1.00 40.55 ? ? ? ? ? ? 39 THR A N 1 ATOM 299 C CA . THR A 1 38 ? 23.847 55.118 -18.192 1.00 40.95 ? ? ? ? ? ? 39 THR A CA 1 ATOM 300 C C . THR A 1 38 ? 23.898 53.578 -18.042 1.00 40.92 ? ? ? ? ? ? 39 THR A C 1 ATOM 301 O O . THR A 1 38 ? 23.483 53.036 -17.009 1.00 41.40 ? ? ? ? ? ? 39 THR A O 1 ATOM 302 C CB . THR A 1 38 ? 24.208 55.719 -16.803 1.00 41.28 ? ? ? ? ? ? 39 THR A CB 1 ATOM 303 O OG1 . THR A 1 38 ? 23.294 55.208 -15.795 1.00 40.20 ? ? ? ? ? ? 39 THR A OG1 1 ATOM 304 C CG2 . THR A 1 38 ? 24.172 57.241 -16.865 1.00 38.52 ? ? ? ? ? ? 39 THR A CG2 1 ATOM 305 N N . GLY A 1 39 ? 24.365 52.867 -19.061 1.00 40.84 ? ? ? ? ? ? 40 GLY A N 1 ATOM 306 C CA . GLY A 1 39 ? 24.301 51.382 -19.003 1.00 39.24 ? ? ? ? ? ? 40 GLY A CA 1 ATOM 307 C C . GLY A 1 39 ? 22.895 50.808 -18.952 1.00 39.07 ? ? ? ? ? ? 40 GLY A C 1 ATOM 308 O O . GLY A 1 39 ? 22.571 49.886 -18.168 1.00 38.71 ? ? ? ? ? ? 40 GLY A O 1 ATOM 309 N N . HIS A 1 40 ? 22.035 51.322 -19.806 1.00 38.93 ? ? ? ? ? ? 41 HIS A N 1 ATOM 310 C CA . HIS A 1 40 ? 20.732 50.721 -19.935 1.00 39.45 ? ? ? ? ? ? 41 HIS A CA 1 ATOM 311 C C . HIS A 1 40 ? 20.433 50.476 -21.375 1.00 38.06 ? ? ? ? ? ? 41 HIS A C 1 ATOM 312 O O . HIS A 1 40 ? 21.288 49.913 -22.066 1.00 39.00 ? ? ? ? ? ? 41 HIS A O 1 ATOM 313 C CB . HIS A 1 40 ? 19.656 51.558 -19.295 1.00 40.24 ? ? ? ? ? ? 41 HIS A CB 1 ATOM 314 C CG . HIS A 1 40 ? 19.886 51.795 -17.843 1.00 44.06 ? ? ? ? ? ? 41 HIS A CG 1 ATOM 315 N ND1 . HIS A 1 40 ? 20.900 52.611 -17.378 1.00 44.73 ? ? ? ? ? ? 41 HIS A ND1 1 ATOM 316 C CD2 . HIS A 1 40 ? 19.210 51.352 -16.751 1.00 44.64 ? ? ? ? ? ? 41 HIS A CD2 1 ATOM 317 C CE1 . HIS A 1 40 ? 20.838 52.657 -16.056 1.00 48.20 ? ? ? ? ? ? 41 HIS A CE1 1 ATOM 318 N NE2 . HIS A 1 40 ? 19.828 51.897 -15.653 1.00 46.58 ? ? ? ? ? ? 41 HIS A NE2 1 ATOM 319 N N . GLY A 1 41 ? 19.234 50.901 -21.798 1.00 36.92 ? ? ? ? ? ? 42 GLY A N 1 ATOM 320 C CA . GLY A 1 41 ? 18.756 50.882 -23.205 1.00 33.98 ? ? ? ? ? ? 42 GLY A CA 1 ATOM 321 C C . GLY A 1 41 ? 18.650 52.260 -23.892 1.00 32.32 ? ? ? ? ? ? 42 GLY A C 1 ATOM 322 O O . GLY A 1 41 ? 18.530 53.325 -23.203 1.00 30.64 ? ? ? ? ? ? 42 GLY A O 1 ATOM 323 N N . LEU A 1 42 ? 18.686 52.201 -25.244 1.00 30.24 ? ? ? ? ? ? 43 LEU A N 1 ATOM 324 C CA . LEU A 1 42 ? 18.813 53.349 -26.156 1.00 28.39 ? ? ? ? ? ? 43 LEU A CA 1 ATOM 325 C C . LEU A 1 42 ? 17.429 53.821 -26.436 1.00 26.43 ? ? ? ? ? ? 43 LEU A C 1 ATOM 326 O O . LEU A 1 42 ? 16.610 53.017 -26.821 1.00 27.01 ? ? ? ? ? ? 43 LEU A O 1 ATOM 327 C CB . LEU A 1 42 ? 19.447 52.940 -27.507 1.00 26.17 ? ? ? ? ? ? 43 LEU A CB 1 ATOM 328 C CG . LEU A 1 42 ? 20.808 52.296 -27.686 1.00 27.83 ? ? ? ? ? ? 43 LEU A CG 1 ATOM 329 C CD1 . LEU A 1 42 ? 20.850 51.996 -29.120 1.00 20.60 ? ? ? ? ? ? 43 LEU A CD1 1 ATOM 330 C CD2 . LEU A 1 42 ? 22.063 53.200 -27.360 1.00 26.64 ? ? ? ? ? ? 43 LEU A CD2 1 ATOM 331 N N . ARG A 1 43 ? 17.190 55.112 -26.282 1.00 25.05 ? ? ? ? ? ? 44 ARG A N 1 ATOM 332 C CA . ARG A 1 43 ? 15.838 55.669 -26.456 1.00 21.42 ? ? ? ? ? ? 44 ARG A CA 1 ATOM 333 C C . ARG A 1 43 ? 15.875 56.773 -27.502 1.00 18.53 ? ? ? ? ? ? 44 ARG A C 1 ATOM 334 O O . ARG A 1 43 ? 16.653 57.707 -27.355 1.00 15.20 ? ? ? ? ? ? 44 ARG A O 1 ATOM 335 C CB . ARG A 1 43 ? 15.350 56.296 -25.153 1.00 21.90 ? ? ? ? ? ? 44 ARG A CB 1 ATOM 336 C CG . ARG A 1 43 ? 14.698 55.388 -24.124 1.00 25.18 ? ? ? ? ? ? 44 ARG A CG 1 ATOM 337 C CD . ARG A 1 43 ? 14.147 56.223 -22.980 1.00 25.46 ? ? ? ? ? ? 44 ARG A CD 1 ATOM 338 N NE . ARG A 1 43 ? 12.690 56.439 -23.148 1.00 32.69 ? ? ? ? ? ? 44 ARG A NE 1 ATOM 339 C CZ . ARG A 1 43 ? 11.874 57.006 -22.248 1.00 31.77 ? ? ? ? ? ? 44 ARG A CZ 1 ATOM 340 N NH1 . ARG A 1 43 ? 12.363 57.448 -21.079 1.00 32.00 ? ? ? ? ? ? 44 ARG A NH1 1 ATOM 341 N NH2 . ARG A 1 43 ? 10.555 57.108 -22.503 1.00 30.75 ? ? ? ? ? ? 44 ARG A NH2 1 ATOM 342 N N . LEU A 1 44 ? 14.957 56.707 -28.469 1.00 16.07 ? ? ? ? ? ? 45 LEU A N 1 ATOM 343 C CA . LEU A 1 44 ? 14.820 57.706 -29.550 1.00 16.26 ? ? ? ? ? ? 45 LEU A CA 1 ATOM 344 C C . LEU A 1 44 ? 14.482 59.159 -29.299 1.00 17.44 ? ? ? ? ? ? 45 LEU A C 1 ATOM 345 O O . LEU A 1 44 ? 13.280 59.517 -29.108 1.00 17.07 ? ? ? ? ? ? 45 LEU A O 1 ATOM 346 C CB . LEU A 1 44 ? 13.762 57.206 -30.568 1.00 16.13 ? ? ? ? ? ? 45 LEU A CB 1 ATOM 347 C CG . LEU A 1 44 ? 13.630 57.726 -32.009 1.00 13.95 ? ? ? ? ? ? 45 LEU A CG 1 ATOM 348 C CD1 . LEU A 1 44 ? 14.927 58.143 -32.676 1.00 9.54 ? ? ? ? ? ? 45 LEU A CD1 1 ATOM 349 C CD2 . LEU A 1 44 ? 12.942 56.649 -32.893 1.00 15.48 ? ? ? ? ? ? 45 LEU A CD2 1 ATOM 350 N N . ILE A 1 45 ? 15.475 60.026 -29.511 1.00 17.03 ? ? ? ? ? ? 46 ILE A N 1 ATOM 351 C CA . ILE A 1 45 ? 15.239 61.497 -29.465 1.00 17.15 ? ? ? ? ? ? 46 ILE A CA 1 ATOM 352 C C . ILE A 1 45 ? 14.645 62.029 -30.738 1.00 17.84 ? ? ? ? ? ? 46 ILE A C 1 ATOM 353 O O . ILE A 1 45 ? 13.578 62.589 -30.728 1.00 16.66 ? ? ? ? ? ? 46 ILE A O 1 ATOM 354 C CB . ILE A 1 45 ? 16.535 62.247 -29.258 1.00 17.70 ? ? ? ? ? ? 46 ILE A CB 1 ATOM 355 C CG1 . ILE A 1 45 ? 17.534 61.249 -28.731 1.00 17.56 ? ? ? ? ? ? 46 ILE A CG1 1 ATOM 356 C CG2 . ILE A 1 45 ? 16.338 63.315 -28.213 1.00 15.51 ? ? ? ? ? ? 46 ILE A CG2 1 ATOM 357 C CD1 . ILE A 1 45 ? 18.843 61.663 -29.077 1.00 31.46 ? ? ? ? ? ? 46 ILE A CD1 1 ATOM 358 N N . HIS A 1 46 ? 15.366 61.844 -31.845 1.00 18.47 ? ? ? ? ? ? 47 HIS A N 1 ATOM 359 C CA . HIS A 1 46 ? 14.915 62.350 -33.169 1.00 19.88 ? ? ? ? ? ? 47 HIS A CA 1 ATOM 360 C C . HIS A 1 46 ? 15.342 61.473 -34.313 1.00 19.68 ? ? ? ? ? ? 47 HIS A C 1 ATOM 361 O O . HIS A 1 46 ? 16.442 60.924 -34.283 1.00 20.02 ? ? ? ? ? ? 47 HIS A O 1 ATOM 362 C CB . HIS A 1 46 ? 15.493 63.749 -33.415 1.00 18.60 ? ? ? ? ? ? 47 HIS A CB 1 ATOM 363 C CG . HIS A 1 46 ? 14.717 64.794 -32.719 1.00 20.12 ? ? ? ? ? ? 47 HIS A CG 1 ATOM 364 N ND1 . HIS A 1 46 ? 13.370 64.973 -32.962 1.00 19.16 ? ? ? ? ? ? 47 HIS A ND1 1 ATOM 365 C CD2 . HIS A 1 46 ? 15.052 65.676 -31.756 1.00 18.63 ? ? ? ? ? ? 47 HIS A CD2 1 ATOM 366 C CE1 . HIS A 1 46 ? 12.922 65.972 -32.223 1.00 21.23 ? ? ? ? ? ? 47 HIS A CE1 1 ATOM 367 N NE2 . HIS A 1 46 ? 13.925 66.433 -31.500 1.00 23.41 ? ? ? ? ? ? 47 HIS A NE2 1 ATOM 368 N N . TYR A 1 47 ? 14.499 61.385 -35.333 1.00 21.16 ? ? ? ? ? ? 48 TYR A N 1 ATOM 369 C CA . TYR A 1 47 ? 14.814 60.597 -36.549 1.00 20.65 ? ? ? ? ? ? 48 TYR A CA 1 ATOM 370 C C . TYR A 1 47 ? 14.527 61.357 -37.816 1.00 21.75 ? ? ? ? ? ? 48 TYR A C 1 ATOM 371 O O . TYR A 1 47 ? 14.028 62.495 -37.743 1.00 23.47 ? ? ? ? ? ? 48 TYR A O 1 ATOM 372 C CB . TYR A 1 47 ? 14.078 59.310 -36.601 1.00 19.65 ? ? ? ? ? ? 48 TYR A CB 1 ATOM 373 C CG . TYR A 1 47 ? 12.582 59.339 -36.698 1.00 15.57 ? ? ? ? ? ? 48 TYR A CG 1 ATOM 374 C CD1 . TYR A 1 47 ? 11.852 59.965 -35.756 1.00 12.80 ? ? ? ? ? ? 48 TYR A CD1 1 ATOM 375 C CD2 . TYR A 1 47 ? 11.909 58.546 -37.644 1.00 13.82 ? ? ? ? ? ? 48 TYR A CD2 1 ATOM 376 C CE1 . TYR A 1 47 ? 10.495 59.958 -35.784 1.00 20.40 ? ? ? ? ? ? 48 TYR A CE1 1 ATOM 377 C CE2 . TYR A 1 47 ? 10.548 58.489 -37.674 1.00 20.23 ? ? ? ? ? ? 48 TYR A CE2 1 ATOM 378 C CZ . TYR A 1 47 ? 9.848 59.245 -36.721 1.00 21.09 ? ? ? ? ? ? 48 TYR A CZ 1 ATOM 379 O OH . TYR A 1 47 ? 8.507 59.262 -36.650 1.00 26.85 ? ? ? ? ? ? 48 TYR A OH 1 ATOM 380 N N . SER A 1 48 ? 14.874 60.783 -38.965 1.00 21.01 ? ? ? ? ? ? 49 SER A N 1 ATOM 381 C CA . SER A 1 48 ? 14.604 61.422 -40.248 1.00 21.90 ? ? ? ? ? ? 49 SER A CA 1 ATOM 382 C C . SER A 1 48 ? 14.467 60.424 -41.392 1.00 23.43 ? ? ? ? ? ? 49 SER A C 1 ATOM 383 O O . SER A 1 48 ? 15.316 59.524 -41.525 1.00 25.88 ? ? ? ? ? ? 49 SER A O 1 ATOM 384 C CB . SER A 1 48 ? 15.683 62.458 -40.535 1.00 20.33 ? ? ? ? ? ? 49 SER A CB 1 ATOM 385 O OG . SER A 1 48 ? 15.677 62.884 -41.871 1.00 20.71 ? ? ? ? ? ? 49 SER A OG 1 ATOM 386 N N . TYR A 1 49 ? 13.399 60.596 -42.210 1.00 25.27 ? ? ? ? ? ? 50 TYR A N 1 ATOM 387 C CA . TYR A 1 49 ? 13.154 59.850 -43.486 1.00 24.55 ? ? ? ? ? ? 50 TYR A CA 1 ATOM 388 C C . TYR A 1 49 ? 13.955 60.321 -44.693 1.00 23.16 ? ? ? ? ? ? 50 TYR A C 1 ATOM 389 O O . TYR A 1 49 ? 14.199 59.547 -45.605 1.00 21.41 ? ? ? ? ? ? 50 TYR A O 1 ATOM 390 C CB . TYR A 1 49 ? 11.662 59.878 -43.843 1.00 25.93 ? ? ? ? ? ? 50 TYR A CB 1 ATOM 391 C CG . TYR A 1 49 ? 10.801 59.254 -42.771 1.00 27.76 ? ? ? ? ? ? 50 TYR A CG 1 ATOM 392 C CD1 . TYR A 1 49 ? 11.001 57.919 -42.349 1.00 23.84 ? ? ? ? ? ? 50 TYR A CD1 1 ATOM 393 C CD2 . TYR A 1 49 ? 9.786 60.020 -42.177 1.00 26.69 ? ? ? ? ? ? 50 TYR A CD2 1 ATOM 394 C CE1 . TYR A 1 49 ? 10.201 57.382 -41.364 1.00 29.67 ? ? ? ? ? ? 50 TYR A CE1 1 ATOM 395 C CE2 . TYR A 1 49 ? 9.017 59.535 -41.212 1.00 26.58 ? ? ? ? ? ? 50 TYR A CE2 1 ATOM 396 C CZ . TYR A 1 49 ? 9.186 58.226 -40.810 1.00 31.34 ? ? ? ? ? ? 50 TYR A CZ 1 ATOM 397 O OH . TYR A 1 49 ? 8.312 57.826 -39.836 1.00 30.53 ? ? ? ? ? ? 50 TYR A OH 1 ATOM 398 N N . GLY A 1 50 ? 14.382 61.599 -44.667 1.00 24.09 ? ? ? ? ? ? 51 GLY A N 1 ATOM 399 C CA . GLY A 1 50 ? 15.044 62.217 -45.809 1.00 22.40 ? ? ? ? ? ? 51 GLY A CA 1 ATOM 400 C C . GLY A 1 50 ? 15.515 63.611 -45.560 1.00 23.82 ? ? ? ? ? ? 51 GLY A C 1 ATOM 401 O O . GLY A 1 50 ? 14.961 64.313 -44.716 1.00 26.06 ? ? ? ? ? ? 51 GLY A O 1 ATOM 402 N N . ALA A 1 51 ? 16.553 64.051 -46.281 1.00 23.19 ? ? ? ? ? ? 52 ALA A N 1 ATOM 403 C CA . ALA A 1 51 ? 17.007 65.436 -46.141 1.00 23.91 ? ? ? ? ? ? 52 ALA A CA 1 ATOM 404 C C . ALA A 1 51 ? 15.881 66.444 -46.162 1.00 24.25 ? ? ? ? ? ? 52 ALA A C 1 ATOM 405 O O . ALA A 1 51 ? 14.943 66.314 -46.916 1.00 25.89 ? ? ? ? ? ? 52 ALA A O 1 ATOM 406 C CB . ALA A 1 51 ? 18.151 65.807 -47.227 1.00 22.66 ? ? ? ? ? ? 52 ALA A CB 1 ATOM 407 N N . GLY A 1 52 ? 16.015 67.459 -45.311 1.00 24.18 ? ? ? ? ? ? 53 GLY A N 1 ATOM 408 C CA . GLY A 1 52 ? 15.035 68.450 -45.106 1.00 22.02 ? ? ? ? ? ? 53 GLY A CA 1 ATOM 409 C C . GLY A 1 52 ? 13.803 67.916 -44.403 1.00 22.81 ? ? ? ? ? ? 53 GLY A C 1 ATOM 410 O O . GLY A 1 52 ? 12.703 68.347 -44.689 1.00 21.34 ? ? ? ? ? ? 53 GLY A O 1 ATOM 411 N N . SER A 1 53 ? 13.971 66.935 -43.509 1.00 22.17 ? ? ? ? ? ? 54 SER A N 1 ATOM 412 C CA . SER A 1 53 ? 12.877 66.527 -42.671 1.00 21.55 ? ? ? ? ? ? 54 SER A CA 1 ATOM 413 C C . SER A 1 53 ? 13.201 65.595 -41.507 1.00 21.71 ? ? ? ? ? ? 54 SER A C 1 ATOM 414 O O . SER A 1 53 ? 13.686 64.487 -41.696 1.00 20.84 ? ? ? ? ? ? 54 SER A O 1 ATOM 415 C CB . SER A 1 53 ? 11.802 65.882 -43.505 1.00 20.87 ? ? ? ? ? ? 54 SER A CB 1 ATOM 416 O OG . SER A 1 53 ? 10.948 65.235 -42.602 1.00 23.65 ? ? ? ? ? ? 54 SER A OG 1 ATOM 417 N N . THR A 1 54 ? 12.833 66.054 -40.303 1.00 22.12 ? ? ? ? ? ? 55 THR A N 1 ATOM 418 C CA . THR A 1 54 ? 12.933 65.303 -39.070 1.00 21.61 ? ? ? ? ? ? 55 THR A CA 1 ATOM 419 C C . THR A 1 54 ? 11.540 65.066 -38.392 1.00 21.37 ? ? ? ? ? ? 55 THR A C 1 ATOM 420 O O . THR A 1 54 ? 10.504 65.776 -38.677 1.00 18.29 ? ? ? ? ? ? 55 THR A O 1 ATOM 421 C CB . THR A 1 54 ? 13.918 65.965 -38.099 1.00 21.00 ? ? ? ? ? ? 55 THR A CB 1 ATOM 422 O OG1 . THR A 1 54 ? 13.268 67.027 -37.418 1.00 22.30 ? ? ? ? ? ? 55 THR A OG1 1 ATOM 423 C CG2 . THR A 1 54 ? 15.184 66.550 -38.840 1.00 24.47 ? ? ? ? ? ? 55 THR A CG2 1 ATOM 424 N N . GLU A 1 55 ? 11.513 64.052 -37.523 1.00 21.59 ? ? ? ? ? ? 56 GLU A N 1 ATOM 425 C CA . GLU A 1 55 ? 10.357 63.828 -36.597 1.00 23.73 ? ? ? ? ? ? 56 GLU A CA 1 ATOM 426 C C . GLU A 1 55 ? 10.811 63.516 -35.181 1.00 23.29 ? ? ? ? ? ? 56 GLU A C 1 ATOM 427 O O . GLU A 1 55 ? 11.898 62.891 -34.967 1.00 24.24 ? ? ? ? ? ? 56 GLU A O 1 ATOM 428 C CB . GLU A 1 55 ? 9.366 62.757 -37.097 1.00 22.89 ? ? ? ? ? ? 56 GLU A CB 1 ATOM 429 C CG . GLU A 1 55 ? 8.972 62.899 -38.593 1.00 23.30 ? ? ? ? ? ? 56 GLU A CG 1 ATOM 430 C CD . GLU A 1 55 ? 7.966 63.975 -38.767 1.00 24.59 ? ? ? ? ? ? 56 GLU A CD 1 ATOM 431 O OE1 . GLU A 1 55 ? 6.975 63.962 -38.004 1.00 24.30 ? ? ? ? ? ? 56 GLU A OE1 1 ATOM 432 O OE2 . GLU A 1 55 ? 8.173 64.864 -39.630 1.00 22.90 ? ? ? ? ? ? 56 GLU A OE2 1 ATOM 433 N N . LYS A 1 56 ? 9.977 63.983 -34.260 1.00 21.97 ? ? ? ? ? ? 57 LYS A N 1 ATOM 434 C CA . LYS A 1 56 ? 10.125 63.815 -32.851 1.00 21.74 ? ? ? ? ? ? 57 LYS A CA 1 ATOM 435 C C . LYS A 1 56 ? 10.046 62.357 -32.520 1.00 23.50 ? ? ? ? ? ? 57 LYS A C 1 ATOM 436 O O . LYS A 1 56 ? 9.113 61.660 -33.019 1.00 24.08 ? ? ? ? ? ? 57 LYS A O 1 ATOM 437 C CB . LYS A 1 56 ? 9.004 64.498 -32.131 1.00 21.29 ? ? ? ? ? ? 57 LYS A CB 1 ATOM 438 C CG . LYS A 1 56 ? 9.092 66.030 -32.143 1.00 22.47 ? ? ? ? ? ? 57 LYS A CG 1 ATOM 439 C CD . LYS A 1 56 ? 8.106 66.668 -31.228 1.00 17.06 ? ? ? ? ? ? 57 LYS A CD 1 ATOM 440 C CE . LYS A 1 56 ? 6.736 66.528 -31.850 1.00 19.31 ? ? ? ? ? ? 57 LYS A CE 1 ATOM 441 N NZ . LYS A 1 56 ? 5.969 67.741 -31.538 1.00 13.09 ? ? ? ? ? ? 57 LYS A NZ 1 ATOM 442 N N . GLY A 1 57 ? 11.013 61.945 -31.675 1.00 22.52 ? ? ? ? ? ? 58 GLY A N 1 ATOM 443 C CA . GLY A 1 57 ? 11.141 60.601 -31.144 1.00 23.14 ? ? ? ? ? ? 58 GLY A CA 1 ATOM 444 C C . GLY A 1 57 ? 10.491 60.439 -29.804 1.00 23.00 ? ? ? ? ? ? 58 GLY A C 1 ATOM 445 O O . GLY A 1 57 ? 9.500 61.107 -29.477 1.00 25.96 ? ? ? ? ? ? 58 GLY A O 1 ATOM 446 N N . ASP A 1 58 ? 11.057 59.544 -29.011 1.00 22.81 ? ? ? ? ? ? 59 ASP A N 1 ATOM 447 C CA . ASP A 1 58 ? 10.479 59.219 -27.734 1.00 21.67 ? ? ? ? ? ? 59 ASP A CA 1 ATOM 448 C C . ASP A 1 58 ? 10.615 60.410 -26.766 1.00 20.59 ? ? ? ? ? ? 59 ASP A C 1 ATOM 449 O O . ASP A 1 58 ? 9.570 60.910 -26.239 1.00 16.51 ? ? ? ? ? ? 59 ASP A O 1 ATOM 450 C CB . ASP A 1 58 ? 11.204 58.085 -27.102 1.00 21.61 ? ? ? ? ? ? 59 ASP A CB 1 ATOM 451 C CG . ASP A 1 58 ? 10.902 56.820 -27.730 1.00 24.79 ? ? ? ? ? ? 59 ASP A CG 1 ATOM 452 O OD1 . ASP A 1 58 ? 9.737 56.567 -28.095 1.00 31.31 ? ? ? ? ? ? 59 ASP A OD1 1 ATOM 453 O OD2 . ASP A 1 58 ? 11.864 56.042 -27.866 1.00 35.15 ? ? ? ? ? ? 59 ASP A OD2 1 ATOM 454 N N . ILE A 1 59 ? 11.906 60.748 -26.535 1.00 14.01 ? ? ? ? ? ? 60 ILE A N 1 ATOM 455 C CA . ILE A 1 59 ? 12.349 61.815 -25.704 1.00 12.85 ? ? ? ? ? ? 60 ILE A CA 1 ATOM 456 C C . ILE A 1 59 ? 12.806 63.151 -26.431 1.00 13.38 ? ? ? ? ? ? 60 ILE A C 1 ATOM 457 O O . ILE A 1 59 ? 13.811 63.676 -26.085 1.00 7.88 ? ? ? ? ? ? 60 ILE A O 1 ATOM 458 C CB . ILE A 1 59 ? 13.442 61.322 -24.741 1.00 11.10 ? ? ? ? ? ? 60 ILE A CB 1 ATOM 459 C CG1 . ILE A 1 59 ? 14.791 61.088 -25.491 1.00 7.48 ? ? ? ? ? ? 60 ILE A CG1 1 ATOM 460 C CG2 . ILE A 1 59 ? 12.981 60.093 -24.170 1.00 7.33 ? ? ? ? ? ? 60 ILE A CG2 1 ATOM 461 C CD1 . ILE A 1 59 ? 15.782 60.438 -24.619 1.00 6.63 ? ? ? ? ? ? 60 ILE A CD1 1 ATOM 462 N N . PRO A 1 60 ? 11.927 63.770 -27.291 1.00 15.12 ? ? ? ? ? ? 61 PRO A N 1 ATOM 463 C CA . PRO A 1 60 ? 12.273 64.920 -28.126 1.00 15.69 ? ? ? ? ? ? 61 PRO A CA 1 ATOM 464 C C . PRO A 1 60 ? 12.844 66.019 -27.261 1.00 18.53 ? ? ? ? ? ? 61 PRO A C 1 ATOM 465 O O . PRO A 1 60 ? 14.033 66.465 -27.424 1.00 17.03 ? ? ? ? ? ? 61 PRO A O 1 ATOM 466 C CB . PRO A 1 60 ? 10.909 65.320 -28.776 1.00 18.22 ? ? ? ? ? ? 61 PRO A CB 1 ATOM 467 C CG . PRO A 1 60 ? 9.837 64.631 -28.044 1.00 14.90 ? ? ? ? ? ? 61 PRO A CG 1 ATOM 468 C CD . PRO A 1 60 ? 10.511 63.389 -27.425 1.00 15.95 ? ? ? ? ? ? 61 PRO A CD 1 ATOM 469 N N . ASP A 1 61 ? 12.055 66.359 -26.241 1.00 19.16 ? ? ? ? ? ? 62 ASP A N 1 ATOM 470 C CA . ASP A 1 61 ? 12.335 67.506 -25.360 1.00 22.26 ? ? ? ? ? ? 62 ASP A CA 1 ATOM 471 C C . ASP A 1 61 ? 13.779 67.849 -25.121 1.00 22.45 ? ? ? ? ? ? 62 ASP A C 1 ATOM 472 O O . ASP A 1 61 ? 14.600 66.976 -24.835 1.00 21.75 ? ? ? ? ? ? 62 ASP A O 1 ATOM 473 C CB . ASP A 1 61 ? 11.652 67.288 -24.035 1.00 22.99 ? ? ? ? ? ? 62 ASP A CB 1 ATOM 474 C CG . ASP A 1 61 ? 10.145 67.026 -24.200 1.00 26.95 ? ? ? ? ? ? 62 ASP A CG 1 ATOM 475 O OD1 . ASP A 1 61 ? 9.379 68.031 -24.343 1.00 27.55 ? ? ? ? ? ? 62 ASP A OD1 1 ATOM 476 O OD2 . ASP A 1 61 ? 9.751 65.812 -24.217 1.00 23.92 ? ? ? ? ? ? 62 ASP A OD2 1 ATOM 477 N N . GLY A 1 62 ? 14.084 69.127 -25.257 1.00 23.31 ? ? ? ? ? ? 63 GLY A N 1 ATOM 478 C CA . GLY A 1 62 ? 15.418 69.672 -24.964 1.00 23.00 ? ? ? ? ? ? 63 GLY A CA 1 ATOM 479 C C . GLY A 1 62 ? 16.459 69.321 -26.028 1.00 25.36 ? ? ? ? ? ? 63 GLY A C 1 ATOM 480 O O . GLY A 1 62 ? 17.703 69.460 -25.831 1.00 24.68 ? ? ? ? ? ? 63 GLY A O 1 ATOM 481 N N . TYR A 1 63 ? 15.959 68.720 -27.420 1.00 19.63 ? ? ? ? ? ? 65 TYR A N 1 ATOM 482 C CA . TYR A 1 63 ? 16.878 68.607 -28.527 1.00 20.06 ? ? ? ? ? ? 65 TYR A CA 1 ATOM 483 C C . TYR A 1 63 ? 16.368 69.227 -29.784 1.00 20.64 ? ? ? ? ? ? 65 TYR A C 1 ATOM 484 O O . TYR A 1 63 ? 15.126 69.419 -29.965 1.00 23.12 ? ? ? ? ? ? 65 TYR A O 1 ATOM 485 C CB . TYR A 1 63 ? 17.234 67.148 -28.747 1.00 19.26 ? ? ? ? ? ? 65 TYR A CB 1 ATOM 486 C CG . TYR A 1 63 ? 18.014 66.628 -27.603 1.00 18.44 ? ? ? ? ? ? 65 TYR A CG 1 ATOM 487 C CD1 . TYR A 1 63 ? 19.403 66.906 -27.457 1.00 16.23 ? ? ? ? ? ? 65 TYR A CD1 1 ATOM 488 C CD2 . TYR A 1 63 ? 17.393 65.948 -26.599 1.00 14.82 ? ? ? ? ? ? 65 TYR A CD2 1 ATOM 489 C CE1 . TYR A 1 63 ? 20.115 66.405 -26.338 1.00 17.23 ? ? ? ? ? ? 65 TYR A CE1 1 ATOM 490 C CE2 . TYR A 1 63 ? 18.076 65.465 -25.489 1.00 17.56 ? ? ? ? ? ? 65 TYR A CE2 1 ATOM 491 C CZ . TYR A 1 63 ? 19.409 65.684 -25.339 1.00 20.74 ? ? ? ? ? ? 65 TYR A CZ 1 ATOM 492 O OH . TYR A 1 63 ? 20.037 65.156 -24.211 1.00 24.31 ? ? ? ? ? ? 65 TYR A OH 1 ATOM 493 N N . LYS A 1 64 ? 17.332 69.545 -30.665 1.00 20.59 ? ? ? ? ? ? 66 LYS A N 1 ATOM 494 C CA . LYS A 1 64 ? 17.100 70.052 -32.030 1.00 18.57 ? ? ? ? ? ? 66 LYS A CA 1 ATOM 495 C C . LYS A 1 64 ? 17.852 69.194 -32.963 1.00 17.77 ? ? ? ? ? ? 66 LYS A C 1 ATOM 496 O O . LYS A 1 64 ? 18.948 68.800 -32.639 1.00 20.25 ? ? ? ? ? ? 66 LYS A O 1 ATOM 497 C CB . LYS A 1 64 ? 17.584 71.478 -32.191 1.00 18.01 ? ? ? ? ? ? 66 LYS A CB 1 ATOM 498 C CG . LYS A 1 64 ? 16.390 72.410 -32.349 1.00 14.95 ? ? ? ? ? ? 66 LYS A CG 1 ATOM 499 C CD . LYS A 1 64 ? 15.674 72.462 -31.017 1.00 14.01 ? ? ? ? ? ? 66 LYS A CD 1 ATOM 500 C CE . LYS A 1 64 ? 14.751 73.705 -30.789 1.00 21.17 ? ? ? ? ? ? 66 LYS A CE 1 ATOM 501 N NZ . LYS A 1 64 ? 15.542 75.062 -30.712 1.00 20.26 ? ? ? ? ? ? 66 LYS A NZ 1 ATOM 502 N N . ALA A 1 65 ? 17.283 68.861 -34.109 1.00 16.92 ? ? ? ? ? ? 67 ALA A N 1 ATOM 503 C CA . ALA A 1 65 ? 18.016 68.067 -35.075 1.00 16.23 ? ? ? ? ? ? 67 ALA A CA 1 ATOM 504 C C . ALA A 1 65 ? 18.008 68.801 -36.409 1.00 15.26 ? ? ? ? ? ? 67 ALA A C 1 ATOM 505 O O . ALA A 1 65 ? 17.425 69.935 -36.527 1.00 15.93 ? ? ? ? ? ? 67 ALA A O 1 ATOM 506 C CB . ALA A 1 65 ? 17.514 66.589 -35.160 1.00 13.96 ? ? ? ? ? ? 67 ALA A CB 1 ATOM 507 N N . SER A 1 66 ? 18.698 68.217 -37.398 1.00 12.50 ? ? ? ? ? ? 68 SER A N 1 ATOM 508 C CA . SER A 1 66 ? 18.651 68.734 -38.754 1.00 10.06 ? ? ? ? ? ? 68 SER A CA 1 ATOM 509 C C . SER A 1 66 ? 19.205 67.806 -39.812 1.00 9.01 ? ? ? ? ? ? 68 SER A C 1 ATOM 510 O O . SER A 1 66 ? 20.371 67.363 -39.695 1.00 9.10 ? ? ? ? ? ? 68 SER A O 1 ATOM 511 C CB . SER A 1 66 ? 19.462 70.011 -38.820 1.00 8.25 ? ? ? ? ? ? 68 SER A CB 1 ATOM 512 O OG . SER A 1 66 ? 19.426 70.358 -40.171 1.00 9.36 ? ? ? ? ? ? 68 SER A OG 1 ATOM 513 N N . ARG A 1 67 ? 18.460 67.575 -40.888 1.00 7.32 ? ? ? ? ? ? 69 ARG A N 1 ATOM 514 C CA . ARG A 1 67 ? 18.987 66.675 -42.042 1.00 6.51 ? ? ? ? ? ? 69 ARG A CA 1 ATOM 515 C C . ARG A 1 67 ? 19.050 67.470 -43.266 1.00 6.32 ? ? ? ? ? ? 69 ARG A C 1 ATOM 516 O O . ARG A 1 67 ? 18.025 67.776 -43.877 1.00 7.29 ? ? ? ? ? ? 69 ARG A O 1 ATOM 517 C CB . ARG A 1 67 ? 18.025 65.512 -42.346 1.00 7.56 ? ? ? ? ? ? 69 ARG A CB 1 ATOM 518 C CG . ARG A 1 67 ? 18.425 64.404 -43.244 1.00 2.00 ? ? ? ? ? ? 69 ARG A CG 1 ATOM 519 C CD . ARG A 1 67 ? 19.062 63.260 -42.459 1.00 7.87 ? ? ? ? ? ? 69 ARG A CD 1 ATOM 520 N NE . ARG A 1 67 ? 19.565 62.159 -43.299 1.00 2.00 ? ? ? ? ? ? 69 ARG A NE 1 ATOM 521 C CZ . ARG A 1 67 ? 18.724 61.367 -43.970 1.00 9.88 ? ? ? ? ? ? 69 ARG A CZ 1 ATOM 522 N NH1 . ARG A 1 67 ? 19.189 60.339 -44.719 1.00 2.65 ? ? ? ? ? ? 69 ARG A NH1 1 ATOM 523 N NH2 . ARG A 1 67 ? 17.380 61.594 -43.841 1.00 6.65 ? ? ? ? ? ? 69 ARG A NH2 1 ATOM 524 N N . PRO A 1 68 ? 20.233 67.879 -43.615 1.00 8.98 ? ? ? ? ? ? 70 PRO A N 1 ATOM 525 C CA . PRO A 1 68 ? 20.571 68.724 -44.742 1.00 8.76 ? ? ? ? ? ? 70 PRO A CA 1 ATOM 526 C C . PRO A 1 68 ? 20.981 68.046 -45.986 1.00 8.00 ? ? ? ? ? ? 70 PRO A C 1 ATOM 527 O O . PRO A 1 68 ? 21.057 68.718 -47.017 1.00 8.50 ? ? ? ? ? ? 70 PRO A O 1 ATOM 528 C CB . PRO A 1 68 ? 21.709 69.611 -44.185 1.00 10.30 ? ? ? ? ? ? 70 PRO A CB 1 ATOM 529 C CG . PRO A 1 68 ? 22.478 68.558 -43.262 1.00 10.69 ? ? ? ? ? ? 70 PRO A CG 1 ATOM 530 C CD . PRO A 1 68 ? 21.396 67.681 -42.695 1.00 11.50 ? ? ? ? ? ? 70 PRO A CD 1 ATOM 531 N N . SER A 1 69 ? 21.092 66.704 -45.949 1.00 10.22 ? ? ? ? ? ? 71 SER A N 1 ATOM 532 C CA . SER A 1 69 ? 21.519 65.934 -47.038 1.00 7.07 ? ? ? ? ? ? 71 SER A CA 1 ATOM 533 C C . SER A 1 69 ? 21.439 64.413 -46.663 1.00 10.49 ? ? ? ? ? ? 71 SER A C 1 ATOM 534 O O . SER A 1 69 ? 22.057 64.013 -45.654 1.00 12.31 ? ? ? ? ? ? 71 SER A O 1 ATOM 535 C CB . SER A 1 69 ? 22.961 66.344 -47.335 1.00 9.69 ? ? ? ? ? ? 71 SER A CB 1 ATOM 536 O OG . SER A 1 69 ? 23.860 66.173 -46.280 1.00 6.34 ? ? ? ? ? ? 71 SER A OG 1 ATOM 537 N N . GLN A 1 70 ? 20.687 63.610 -47.418 1.00 7.39 ? ? ? ? ? ? 72 GLN A N 1 ATOM 538 C CA . GLN A 1 70 ? 20.667 62.122 -47.333 1.00 10.10 ? ? ? ? ? ? 72 GLN A CA 1 ATOM 539 C C . GLN A 1 70 ? 21.697 61.453 -46.511 1.00 10.83 ? ? ? ? ? ? 72 GLN A C 1 ATOM 540 O O . GLN A 1 70 ? 21.357 60.718 -45.696 1.00 15.05 ? ? ? ? ? ? 72 GLN A O 1 ATOM 541 C CB . GLN A 1 70 ? 20.553 61.480 -48.729 1.00 8.55 ? ? ? ? ? ? 72 GLN A CB 1 ATOM 542 C CG . GLN A 1 70 ? 19.132 60.903 -48.997 1.00 6.16 ? ? ? ? ? ? 72 GLN A CG 1 ATOM 543 C CD . GLN A 1 70 ? 18.945 59.442 -48.739 1.00 4.96 ? ? ? ? ? ? 72 GLN A CD 1 ATOM 544 O OE1 . GLN A 1 70 ? 19.928 58.648 -48.743 1.00 7.54 ? ? ? ? ? ? 72 GLN A OE1 1 ATOM 545 N NE2 . GLN A 1 70 ? 17.665 59.032 -48.424 1.00 4.14 ? ? ? ? ? ? 72 GLN A NE2 1 ATOM 546 N N . GLU A 1 71 ? 22.967 61.840 -46.616 1.00 18.10 ? ? ? ? ? ? 73 GLU A N 1 ATOM 547 C CA . GLU A 1 71 ? 24.014 61.227 -45.813 1.00 20.45 ? ? ? ? ? ? 73 GLU A CA 1 ATOM 548 C C . GLU A 1 71 ? 24.460 62.009 -44.574 1.00 21.25 ? ? ? ? ? ? 73 GLU A C 1 ATOM 549 O O . GLU A 1 71 ? 25.455 61.657 -43.906 1.00 22.74 ? ? ? ? ? ? 73 GLU A O 1 ATOM 550 C CB . GLU A 1 71 ? 25.204 60.777 -46.715 1.00 21.37 ? ? ? ? ? ? 73 GLU A CB 1 ATOM 551 C CG . GLU A 1 71 ? 26.107 61.919 -47.214 1.00 25.91 ? ? ? ? ? ? 73 GLU A CG 1 ATOM 552 C CD . GLU A 1 71 ? 25.471 62.696 -48.296 1.00 30.33 ? ? ? ? ? ? 73 GLU A CD 1 ATOM 553 O OE1 . GLU A 1 71 ? 25.819 63.890 -48.434 1.00 36.07 ? ? ? ? ? ? 73 GLU A OE1 1 ATOM 554 O OE2 . GLU A 1 71 ? 24.575 62.130 -48.985 1.00 37.75 ? ? ? ? ? ? 73 GLU A OE2 1 ATOM 555 N N . GLN A 1 72 ? 23.753 63.069 -44.218 1.00 21.10 ? ? ? ? ? ? 74 GLN A N 1 ATOM 556 C CA . GLN A 1 72 ? 24.223 63.914 -43.050 1.00 18.96 ? ? ? ? ? ? 74 GLN A CA 1 ATOM 557 C C . GLN A 1 72 ? 23.063 64.248 -42.126 1.00 19.32 ? ? ? ? ? ? 74 GLN A C 1 ATOM 558 O O . GLN A 1 72 ? 21.965 64.539 -42.642 1.00 20.50 ? ? ? ? ? ? 74 GLN A O 1 ATOM 559 C CB . GLN A 1 72 ? 24.840 65.155 -43.538 1.00 16.28 ? ? ? ? ? ? 74 GLN A CB 1 ATOM 560 C CG . GLN A 1 72 ? 25.188 66.134 -42.337 1.00 20.77 ? ? ? ? ? ? 74 GLN A CG 1 ATOM 561 C CD . GLN A 1 72 ? 26.198 65.514 -41.271 1.00 18.29 ? ? ? ? ? ? 74 GLN A CD 1 ATOM 562 O OE1 . GLN A 1 72 ? 26.127 65.828 -40.078 1.00 18.61 ? ? ? ? ? ? 74 GLN A OE1 1 ATOM 563 N NE2 . GLN A 1 72 ? 27.109 64.603 -41.728 1.00 22.03 ? ? ? ? ? ? 74 GLN A NE2 1 ATOM 564 N N . PHE A 1 73 ? 23.271 64.195 -40.802 1.00 20.12 ? ? ? ? ? ? 75 PHE A N 1 ATOM 565 C CA . PHE A 1 73 ? 22.225 64.478 -39.692 1.00 20.28 ? ? ? ? ? ? 75 PHE A CA 1 ATOM 566 C C . PHE A 1 73 ? 23.044 65.020 -38.500 1.00 20.22 ? ? ? ? ? ? 75 PHE A C 1 ATOM 567 O O . PHE A 1 73 ? 24.233 64.606 -38.304 1.00 21.49 ? ? ? ? ? ? 75 PHE A O 1 ATOM 568 C CB . PHE A 1 73 ? 21.526 63.178 -39.228 1.00 19.63 ? ? ? ? ? ? 75 PHE A CB 1 ATOM 569 C CG . PHE A 1 73 ? 20.143 63.339 -38.633 1.00 19.51 ? ? ? ? ? ? 75 PHE A CG 1 ATOM 570 C CD1 . PHE A 1 73 ? 19.429 64.541 -38.725 1.00 17.91 ? ? ? ? ? ? 75 PHE A CD1 1 ATOM 571 C CD2 . PHE A 1 73 ? 19.501 62.247 -38.086 1.00 15.80 ? ? ? ? ? ? 75 PHE A CD2 1 ATOM 572 C CE1 . PHE A 1 73 ? 18.126 64.640 -38.263 1.00 18.24 ? ? ? ? ? ? 75 PHE A CE1 1 ATOM 573 C CE2 . PHE A 1 73 ? 18.170 62.395 -37.596 1.00 18.85 ? ? ? ? ? ? 75 PHE A CE2 1 ATOM 574 C CZ . PHE A 1 73 ? 17.509 63.600 -37.706 1.00 13.17 ? ? ? ? ? ? 75 PHE A CZ 1 ATOM 575 N N . SER A 1 74 ? 22.438 65.895 -37.724 1.00 18.33 ? ? ? ? ? ? 76 SER A N 1 ATOM 576 C CA . SER A 1 74 ? 23.094 66.642 -36.635 1.00 19.06 ? ? ? ? ? ? 76 SER A CA 1 ATOM 577 C C . SER A 1 74 ? 22.195 66.909 -35.418 1.00 19.81 ? ? ? ? ? ? 76 SER A C 1 ATOM 578 O O . SER A 1 74 ? 20.976 67.121 -35.561 1.00 21.88 ? ? ? ? ? ? 76 SER A O 1 ATOM 579 C CB . SER A 1 74 ? 23.724 67.957 -37.150 1.00 17.55 ? ? ? ? ? ? 76 SER A CB 1 ATOM 580 O OG . SER A 1 74 ? 24.248 67.727 -38.459 1.00 15.12 ? ? ? ? ? ? 76 SER A OG 1 ATOM 581 N N . LEU A 1 75 ? 22.764 66.836 -34.218 1.00 19.96 ? ? ? ? ? ? 77 LEU A N 1 ATOM 582 C CA . LEU A 1 75 ? 21.937 66.978 -32.984 1.00 21.04 ? ? ? ? ? ? 77 LEU A CA 1 ATOM 583 C C . LEU A 1 75 ? 22.306 68.335 -32.408 1.00 22.72 ? ? ? ? ? ? 77 LEU A C 1 ATOM 584 O O . LEU A 1 75 ? 23.515 68.564 -32.114 1.00 23.84 ? ? ? ? ? ? 77 LEU A O 1 ATOM 585 C CB . LEU A 1 75 ? 22.267 65.859 -31.972 1.00 19.71 ? ? ? ? ? ? 77 LEU A CB 1 ATOM 586 C CG . LEU A 1 75 ? 21.254 65.468 -30.936 1.00 16.37 ? ? ? ? ? ? 77 LEU A CG 1 ATOM 587 C CD1 . LEU A 1 75 ? 20.058 65.094 -31.704 1.00 23.34 ? ? ? ? ? ? 77 LEU A CD1 1 ATOM 588 C CD2 . LEU A 1 75 ? 21.653 64.259 -30.036 1.00 19.34 ? ? ? ? ? ? 77 LEU A CD2 1 ATOM 589 N N . ILE A 1 76 ? 21.331 69.241 -32.370 1.00 24.76 ? ? ? ? ? ? 78 ILE A N 1 ATOM 590 C CA . ILE A 1 76 ? 21.572 70.568 -31.829 1.00 28.07 ? ? ? ? ? ? 78 ILE A CA 1 ATOM 591 C C . ILE A 1 76 ? 21.116 70.641 -30.376 1.00 29.24 ? ? ? ? ? ? 78 ILE A C 1 ATOM 592 O O . ILE A 1 76 ? 20.137 70.001 -29.992 1.00 29.48 ? ? ? ? ? ? 78 ILE A O 1 ATOM 593 C CB . ILE A 1 76 ? 21.083 71.747 -32.771 1.00 28.37 ? ? ? ? ? ? 78 ILE A CB 1 ATOM 594 C CG1 . ILE A 1 76 ? 21.845 71.695 -34.109 1.00 30.48 ? ? ? ? ? ? 78 ILE A CG1 1 ATOM 595 C CG2 . ILE A 1 76 ? 21.437 73.125 -32.176 1.00 25.48 ? ? ? ? ? ? 78 ILE A CG2 1 ATOM 596 C CD1 . ILE A 1 76 ? 21.085 72.241 -35.308 1.00 32.11 ? ? ? ? ? ? 78 ILE A CD1 1 ATOM 597 N N . LEU A 1 77 ? 21.894 71.361 -29.572 1.00 31.09 ? ? ? ? ? ? 79 LEU A N 1 ATOM 598 C CA . LEU A 1 77 ? 21.646 71.560 -28.153 1.00 33.06 ? ? ? ? ? ? 79 LEU A CA 1 ATOM 599 C C . LEU A 1 77 ? 21.943 72.998 -27.807 1.00 33.59 ? ? ? ? ? ? 79 LEU A C 1 ATOM 600 O O . LEU A 1 77 ? 23.115 73.408 -27.776 1.00 34.79 ? ? ? ? ? ? 79 LEU A O 1 ATOM 601 C CB . LEU A 1 77 ? 22.576 70.648 -27.361 1.00 33.63 ? ? ? ? ? ? 79 LEU A CB 1 ATOM 602 C CG . LEU A 1 77 ? 22.018 69.218 -27.316 1.00 33.58 ? ? ? ? ? ? 79 LEU A CG 1 ATOM 603 C CD1 . LEU A 1 77 ? 22.503 68.427 -28.455 1.00 35.82 ? ? ? ? ? ? 79 LEU A CD1 1 ATOM 604 C CD2 . LEU A 1 77 ? 22.473 68.540 -26.077 1.00 32.36 ? ? ? ? ? ? 79 LEU A CD2 1 ATOM 605 N N . GLU A 1 78 ? 20.890 73.777 -27.589 1.00 34.47 ? ? ? ? ? ? 80 GLU A N 1 ATOM 606 C CA . GLU A 1 78 ? 21.055 75.212 -27.578 1.00 34.81 ? ? ? ? ? ? 80 GLU A CA 1 ATOM 607 C C . GLU A 1 78 ? 21.702 75.589 -26.248 1.00 35.80 ? ? ? ? ? ? 80 GLU A C 1 ATOM 608 O O . GLU A 1 78 ? 22.928 75.889 -26.179 1.00 37.02 ? ? ? ? ? ? 80 GLU A O 1 ATOM 609 C CB . GLU A 1 78 ? 19.721 75.882 -27.786 1.00 34.59 ? ? ? ? ? ? 80 GLU A CB 1 ATOM 610 C CG . GLU A 1 78 ? 19.770 77.292 -28.411 1.00 34.90 ? ? ? ? ? ? 80 GLU A CG 1 ATOM 611 C CD . GLU A 1 78 ? 19.674 77.291 -29.941 1.00 35.81 ? ? ? ? ? ? 80 GLU A CD 1 ATOM 612 O OE1 . GLU A 1 78 ? 18.613 76.862 -30.493 1.00 33.77 ? ? ? ? ? ? 80 GLU A OE1 1 ATOM 613 O OE2 . GLU A 1 78 ? 20.666 77.723 -30.575 1.00 33.25 ? ? ? ? ? ? 80 GLU A OE2 1 ATOM 614 N N . SER A 1 79 ? 20.928 75.517 -25.170 1.00 34.67 ? ? ? ? ? ? 81 SER A N 1 ATOM 615 C CA . SER A 1 79 ? 21.519 75.649 -23.834 1.00 33.28 ? ? ? ? ? ? 81 SER A CA 1 ATOM 616 C C . SER A 1 79 ? 21.590 74.271 -23.172 1.00 32.90 ? ? ? ? ? ? 81 SER A C 1 ATOM 617 O O . SER A 1 79 ? 20.570 73.728 -22.759 1.00 32.83 ? ? ? ? ? ? 81 SER A O 1 ATOM 618 C CB . SER A 1 79 ? 20.715 76.626 -22.949 1.00 34.47 ? ? ? ? ? ? 81 SER A CB 1 ATOM 619 O OG . SER A 1 79 ? 20.274 77.805 -23.635 1.00 33.38 ? ? ? ? ? ? 81 SER A OG 1 ATOM 620 N N . ALA A 1 80 ? 22.800 73.708 -23.122 1.00 32.67 ? ? ? ? ? ? 82 ALA A N 1 ATOM 621 C CA . ALA A 1 80 ? 23.068 72.434 -22.458 1.00 32.37 ? ? ? ? ? ? 82 ALA A CA 1 ATOM 622 C C . ALA A 1 80 ? 22.717 72.504 -21.007 1.00 32.22 ? ? ? ? ? ? 82 ALA A C 1 ATOM 623 O O . ALA A 1 80 ? 22.595 73.598 -20.430 1.00 34.49 ? ? ? ? ? ? 82 ALA A O 1 ATOM 624 C CB . ALA A 1 80 ? 24.509 72.063 -22.586 1.00 31.35 ? ? ? ? ? ? 82 ALA A CB 1 ATOM 625 N N . THR A 1 81 ? 22.610 71.333 -20.405 1.00 31.68 ? ? ? ? ? ? 83 THR A N 1 ATOM 626 C CA . THR A 1 81 ? 22.424 71.174 -18.960 1.00 31.76 ? ? ? ? ? ? 83 THR A CA 1 ATOM 627 C C . THR A 1 81 ? 22.860 69.746 -18.549 1.00 31.96 ? ? ? ? ? ? 83 THR A C 1 ATOM 628 O O . THR A 1 81 ? 22.633 68.790 -19.318 1.00 32.23 ? ? ? ? ? ? 83 THR A O 1 ATOM 629 C CB . THR A 1 81 ? 20.925 71.301 -18.557 1.00 30.60 ? ? ? ? ? ? 83 THR A CB 1 ATOM 630 O OG1 . THR A 1 81 ? 20.235 70.118 -18.976 1.00 28.00 ? ? ? ? ? ? 83 THR A OG1 1 ATOM 631 C CG2 . THR A 1 81 ? 20.285 72.495 -19.217 1.00 33.27 ? ? ? ? ? ? 83 THR A CG2 1 ATOM 632 N N . PRO A 1 82 ? 23.476 69.604 -17.357 1.00 31.47 ? ? ? ? ? ? 84 PRO A N 1 ATOM 633 C CA . PRO A 1 82 ? 24.094 68.370 -16.921 1.00 30.69 ? ? ? ? ? ? 84 PRO A CA 1 ATOM 634 C C . PRO A 1 82 ? 23.235 67.208 -17.192 1.00 30.90 ? ? ? ? ? ? 84 PRO A C 1 ATOM 635 O O . PRO A 1 82 ? 23.740 66.259 -17.733 1.00 32.14 ? ? ? ? ? ? 84 PRO A O 1 ATOM 636 C CB . PRO A 1 82 ? 24.305 68.597 -15.458 1.00 31.44 ? ? ? ? ? ? 84 PRO A CB 1 ATOM 637 C CG . PRO A 1 82 ? 24.748 70.155 -15.443 1.00 30.69 ? ? ? ? ? ? 84 PRO A CG 1 ATOM 638 C CD . PRO A 1 82 ? 23.703 70.712 -16.399 1.00 32.64 ? ? ? ? ? ? 84 PRO A CD 1 ATOM 639 N N . SER A 1 83 ? 21.940 67.289 -16.909 1.00 30.74 ? ? ? ? ? ? 85 SER A N 1 ATOM 640 C CA . SER A 1 83 ? 20.986 66.254 -17.312 1.00 30.68 ? ? ? ? ? ? 85 SER A CA 1 ATOM 641 C C . SER A 1 83 ? 21.299 65.585 -18.671 1.00 29.82 ? ? ? ? ? ? 85 SER A C 1 ATOM 642 O O . SER A 1 83 ? 21.387 64.336 -18.758 1.00 29.59 ? ? ? ? ? ? 85 SER A O 1 ATOM 643 C CB . SER A 1 83 ? 19.586 66.850 -17.402 1.00 31.56 ? ? ? ? ? ? 85 SER A CB 1 ATOM 644 O OG . SER A 1 83 ? 19.367 67.736 -16.333 1.00 34.84 ? ? ? ? ? ? 85 SER A OG 1 ATOM 645 N N . GLN A 1 84 ? 21.439 66.414 -19.717 1.00 27.94 ? ? ? ? ? ? 86 GLN A N 1 ATOM 646 C CA . GLN A 1 84 ? 21.732 65.966 -21.084 1.00 26.08 ? ? ? ? ? ? 86 GLN A CA 1 ATOM 647 C C . GLN A 1 84 ? 23.091 65.288 -21.160 1.00 26.67 ? ? ? ? ? ? 86 GLN A C 1 ATOM 648 O O . GLN A 1 84 ? 23.608 64.988 -22.240 1.00 28.23 ? ? ? ? ? ? 86 GLN A O 1 ATOM 649 C CB . GLN A 1 84 ? 21.691 67.140 -22.047 1.00 25.17 ? ? ? ? ? ? 86 GLN A CB 1 ATOM 650 C CG . GLN A 1 84 ? 20.319 67.829 -22.172 1.00 20.93 ? ? ? ? ? ? 86 GLN A CG 1 ATOM 651 C CD . GLN A 1 84 ? 20.368 69.002 -23.076 1.00 21.62 ? ? ? ? ? ? 86 GLN A CD 1 ATOM 652 O OE1 . GLN A 1 84 ? 21.401 69.744 -23.136 1.00 23.80 ? ? ? ? ? ? 86 GLN A OE1 1 ATOM 653 N NE2 . GLN A 1 84 ? 19.287 69.208 -23.820 1.00 23.26 ? ? ? ? ? ? 86 GLN A NE2 1 ATOM 654 N N . THR A 1 85 ? 23.683 64.999 -20.023 1.00 26.64 ? ? ? ? ? ? 87 THR A N 1 ATOM 655 C CA . THR A 1 85 ? 25.012 64.384 -20.074 1.00 25.84 ? ? ? ? ? ? 87 THR A CA 1 ATOM 656 C C . THR A 1 85 ? 24.914 62.912 -20.298 1.00 24.76 ? ? ? ? ? ? 87 THR A C 1 ATOM 657 O O . THR A 1 85 ? 24.318 62.224 -19.474 1.00 24.67 ? ? ? ? ? ? 87 THR A O 1 ATOM 658 C CB . THR A 1 85 ? 25.758 64.614 -18.804 1.00 25.33 ? ? ? ? ? ? 87 THR A CB 1 ATOM 659 O OG1 . THR A 1 85 ? 26.164 65.997 -18.742 1.00 28.64 ? ? ? ? ? ? 87 THR A OG1 1 ATOM 660 C CG2 . THR A 1 85 ? 26.982 63.731 -18.783 1.00 27.86 ? ? ? ? ? ? 87 THR A CG2 1 ATOM 661 N N . SER A 1 86 ? 25.501 62.395 -21.391 1.00 24.36 ? ? ? ? ? ? 88 SER A N 1 ATOM 662 C CA . SER A 1 86 ? 25.407 60.952 -21.684 1.00 21.73 ? ? ? ? ? ? 88 SER A CA 1 ATOM 663 C C . SER A 1 86 ? 26.274 60.418 -22.863 1.00 22.18 ? ? ? ? ? ? 88 SER A C 1 ATOM 664 O O . SER A 1 86 ? 27.319 61.007 -23.207 1.00 19.63 ? ? ? ? ? ? 88 SER A O 1 ATOM 665 C CB . SER A 1 86 ? 23.940 60.567 -21.884 1.00 20.91 ? ? ? ? ? ? 88 SER A CB 1 ATOM 666 O OG . SER A 1 86 ? 23.838 59.253 -22.405 1.00 24.54 ? ? ? ? ? ? 88 SER A OG 1 ATOM 667 N N . VAL A 1 87 ? 25.808 59.310 -23.478 1.00 21.23 ? ? ? ? ? ? 89 VAL A N 1 ATOM 668 C CA . VAL A 1 87 ? 26.430 58.712 -24.647 1.00 20.48 ? ? ? ? ? ? 89 VAL A CA 1 ATOM 669 C C . VAL A 1 87 ? 25.371 58.628 -25.771 1.00 20.61 ? ? ? ? ? ? 89 VAL A C 1 ATOM 670 O O . VAL A 1 87 ? 24.345 57.912 -25.598 1.00 19.43 ? ? ? ? ? ? 89 VAL A O 1 ATOM 671 C CB . VAL A 1 87 ? 26.952 57.283 -24.320 1.00 19.60 ? ? ? ? ? ? 89 VAL A CB 1 ATOM 672 C CG1 . VAL A 1 87 ? 27.430 56.704 -25.530 1.00 22.57 ? ? ? ? ? ? 89 VAL A CG1 1 ATOM 673 C CG2 . VAL A 1 87 ? 28.099 57.282 -23.399 1.00 17.69 ? ? ? ? ? ? 89 VAL A CG2 1 ATOM 674 N N . TYR A 1 88 ? 25.614 59.411 -26.856 1.00 20.59 ? ? ? ? ? ? 90 TYR A N 1 ATOM 675 C CA . TYR A 1 88 ? 24.821 59.476 -28.078 1.00 19.75 ? ? ? ? ? ? 90 TYR A CA 1 ATOM 676 C C . TYR A 1 88 ? 25.227 58.495 -29.234 1.00 19.70 ? ? ? ? ? ? 90 TYR A C 1 ATOM 677 O O . TYR A 1 88 ? 26.435 58.282 -29.492 1.00 20.90 ? ? ? ? ? ? 90 TYR A O 1 ATOM 678 C CB . TYR A 1 88 ? 24.762 60.934 -28.553 1.00 21.37 ? ? ? ? ? ? 90 TYR A CB 1 ATOM 679 C CG . TYR A 1 88 ? 24.112 61.839 -27.490 1.00 20.56 ? ? ? ? ? ? 90 TYR A CG 1 ATOM 680 C CD1 . TYR A 1 88 ? 24.860 62.303 -26.407 1.00 19.91 ? ? ? ? ? ? 90 TYR A CD1 1 ATOM 681 C CD2 . TYR A 1 88 ? 22.802 62.251 -27.588 1.00 16.94 ? ? ? ? ? ? 90 TYR A CD2 1 ATOM 682 C CE1 . TYR A 1 88 ? 24.305 63.093 -25.447 1.00 17.31 ? ? ? ? ? ? 90 TYR A CE1 1 ATOM 683 C CE2 . TYR A 1 88 ? 22.245 63.063 -26.606 1.00 12.46 ? ? ? ? ? ? 90 TYR A CE2 1 ATOM 684 C CZ . TYR A 1 88 ? 22.998 63.423 -25.533 1.00 17.07 ? ? ? ? ? ? 90 TYR A CZ 1 ATOM 685 O OH . TYR A 1 88 ? 22.497 64.165 -24.526 1.00 18.29 ? ? ? ? ? ? 90 TYR A OH 1 ATOM 686 N N . PHE A 1 89 ? 24.268 57.943 -29.983 1.00 18.99 ? ? ? ? ? ? 91 PHE A N 1 ATOM 687 C CA . PHE A 1 89 ? 24.676 56.971 -31.084 1.00 18.42 ? ? ? ? ? ? 91 PHE A CA 1 ATOM 688 C C . PHE A 1 89 ? 23.810 57.255 -32.288 1.00 17.15 ? ? ? ? ? ? 91 PHE A C 1 ATOM 689 O O . PHE A 1 89 ? 22.624 57.554 -32.137 1.00 16.37 ? ? ? ? ? ? 91 PHE A O 1 ATOM 690 C CB . PHE A 1 89 ? 24.418 55.526 -30.739 1.00 16.98 ? ? ? ? ? ? 91 PHE A CB 1 ATOM 691 C CG . PHE A 1 89 ? 25.403 54.914 -29.845 1.00 16.49 ? ? ? ? ? ? 91 PHE A CG 1 ATOM 692 C CD1 . PHE A 1 89 ? 26.490 54.188 -30.362 1.00 19.19 ? ? ? ? ? ? 91 PHE A CD1 1 ATOM 693 C CD2 . PHE A 1 89 ? 25.190 54.910 -28.510 1.00 17.43 ? ? ? ? ? ? 91 PHE A CD2 1 ATOM 694 C CE1 . PHE A 1 89 ? 27.372 53.597 -29.593 1.00 15.02 ? ? ? ? ? ? 91 PHE A CE1 1 ATOM 695 C CE2 . PHE A 1 89 ? 26.066 54.366 -27.712 1.00 15.69 ? ? ? ? ? ? 91 PHE A CE2 1 ATOM 696 C CZ . PHE A 1 89 ? 27.241 53.687 -28.268 1.00 17.74 ? ? ? ? ? ? 91 PHE A CZ 1 ATOM 697 N N . CYS A 1 90 ? 24.399 57.129 -33.464 1.00 16.41 ? ? ? ? ? ? 92 CYS A N 1 ATOM 698 C CA . CYS A 1 90 ? 23.771 57.517 -34.705 1.00 16.96 ? ? ? ? ? ? 92 CYS A CA 1 ATOM 699 C C . CYS A 1 90 ? 23.599 56.269 -35.504 1.00 15.72 ? ? ? ? ? ? 92 CYS A C 1 ATOM 700 O O . CYS A 1 90 ? 24.488 55.435 -35.526 1.00 16.29 ? ? ? ? ? ? 92 CYS A O 1 ATOM 701 C CB . CYS A 1 90 ? 24.678 58.472 -35.489 1.00 18.61 ? ? ? ? ? ? 92 CYS A CB 1 ATOM 702 S SG . CYS A 1 90 ? 23.944 59.212 -37.011 1.00 23.63 ? ? ? ? ? ? 92 CYS A SG 1 ATOM 703 N N . ALA A 1 91 ? 22.458 56.140 -36.165 1.00 13.99 ? ? ? ? ? ? 93 ALA A N 1 ATOM 704 C CA . ALA A 1 91 ? 22.243 55.027 -37.068 1.00 11.57 ? ? ? ? ? ? 93 ALA A CA 1 ATOM 705 C C . ALA A 1 91 ? 21.548 55.415 -38.349 1.00 12.39 ? ? ? ? ? ? 93 ALA A C 1 ATOM 706 O O . ALA A 1 91 ? 20.745 56.401 -38.424 1.00 11.49 ? ? ? ? ? ? 93 ALA A O 1 ATOM 707 C CB . ALA A 1 91 ? 21.489 53.930 -36.413 1.00 10.15 ? ? ? ? ? ? 93 ALA A CB 1 ATOM 708 N N . SER A 1 92 ? 21.759 54.539 -39.329 1.00 12.18 ? ? ? ? ? ? 94 SER A N 1 ATOM 709 C CA . SER A 1 92 ? 21.044 54.576 -40.607 1.00 9.60 ? ? ? ? ? ? 94 SER A CA 1 ATOM 710 C C . SER A 1 92 ? 20.648 53.183 -40.926 1.00 9.12 ? ? ? ? ? ? 94 SER A C 1 ATOM 711 O O . SER A 1 92 ? 21.406 52.166 -40.720 1.00 6.58 ? ? ? ? ? ? 94 SER A O 1 ATOM 712 C CB . SER A 1 92 ? 22.023 55.019 -41.649 1.00 7.65 ? ? ? ? ? ? 94 SER A CB 1 ATOM 713 O OG . SER A 1 92 ? 23.207 54.268 -41.355 1.00 12.05 ? ? ? ? ? ? 94 SER A OG 1 ATOM 714 N N . GLY A 1 93 ? 19.505 53.169 -41.543 1.00 11.63 ? ? ? ? ? ? 95 GLY A N 1 ATOM 715 C CA . GLY A 1 93 ? 18.600 52.030 -41.608 1.00 12.49 ? ? ? ? ? ? 95 GLY A CA 1 ATOM 716 C C . GLY A 1 93 ? 17.878 52.015 -42.984 1.00 14.87 ? ? ? ? ? ? 95 GLY A C 1 ATOM 717 O O . GLY A 1 93 ? 17.472 53.076 -43.480 1.00 14.59 ? ? ? ? ? ? 95 GLY A O 1 ATOM 718 N N . GLY A 1 94 ? 17.720 50.808 -43.601 1.00 15.93 ? ? ? ? ? ? 96 GLY A N 1 ATOM 719 C CA . GLY A 1 94 ? 17.256 50.745 -45.014 1.00 16.18 ? ? ? ? ? ? 96 GLY A CA 1 ATOM 720 C C . GLY A 1 94 ? 17.464 49.438 -45.734 1.00 17.00 ? ? ? ? ? ? 96 GLY A C 1 ATOM 721 O O . GLY A 1 94 ? 18.383 48.692 -45.438 1.00 17.51 ? ? ? ? ? ? 96 GLY A O 1 ATOM 722 N N . GLY A 1 95 ? 16.588 49.132 -46.678 1.00 18.28 ? ? ? ? ? ? 97 GLY A N 1 ATOM 723 C CA . GLY A 1 95 ? 16.631 47.827 -47.309 1.00 17.77 ? ? ? ? ? ? 97 GLY A CA 1 ATOM 724 C C . GLY A 1 95 ? 17.089 46.726 -46.412 1.00 18.83 ? ? ? ? ? ? 97 GLY A C 1 ATOM 725 O O . GLY A 1 95 ? 17.969 46.009 -46.752 1.00 20.47 ? ? ? ? ? ? 97 GLY A O 1 ATOM 726 N N . GLY A 1 96 ? 16.462 46.553 -45.261 1.00 21.86 ? ? ? ? ? ? 98 GLY A N 1 ATOM 727 C CA . GLY A 1 96 ? 16.840 45.474 -44.308 1.00 23.33 ? ? ? ? ? ? 98 GLY A CA 1 ATOM 728 C C . GLY A 1 96 ? 18.162 45.786 -43.608 1.00 25.81 ? ? ? ? ? ? 98 GLY A C 1 ATOM 729 O O . GLY A 1 96 ? 19.022 44.886 -43.439 1.00 25.35 ? ? ? ? ? ? 98 GLY A O 1 ATOM 730 N N . THR A 1 97 ? 18.368 47.057 -43.204 1.00 24.75 ? ? ? ? ? ? 99 THR A N 1 ATOM 731 C CA . THR A 1 97 ? 19.680 47.437 -42.682 1.00 25.00 ? ? ? ? ? ? 99 THR A CA 1 ATOM 732 C C . THR A 1 97 ? 19.548 48.550 -41.602 1.00 24.87 ? ? ? ? ? ? 99 THR A C 1 ATOM 733 O O . THR A 1 97 ? 18.457 49.170 -41.491 1.00 24.41 ? ? ? ? ? ? 99 THR A O 1 ATOM 734 C CB . THR A 1 97 ? 20.609 47.780 -43.897 1.00 26.72 ? ? ? ? ? ? 99 THR A CB 1 ATOM 735 O OG1 . THR A 1 97 ? 20.607 46.656 -44.794 1.00 29.51 ? ? ? ? ? ? 99 THR A OG1 1 ATOM 736 C CG2 . THR A 1 97 ? 22.060 48.119 -43.519 1.00 24.08 ? ? ? ? ? ? 99 THR A CG2 1 ATOM 737 N N . LEU A 1 98 ? 20.603 48.685 -40.770 1.00 22.07 ? ? ? ? ? ? 100 LEU A N 1 ATOM 738 C CA . LEU A 1 98 ? 20.668 49.552 -39.620 1.00 21.67 ? ? ? ? ? ? 100 LEU A CA 1 ATOM 739 C C . LEU A 1 98 ? 22.149 49.677 -39.220 1.00 22.92 ? ? ? ? ? ? 100 LEU A C 1 ATOM 740 O O . LEU A 1 98 ? 22.780 48.691 -38.892 1.00 22.85 ? ? ? ? ? ? 100 LEU A O 1 ATOM 741 C CB . LEU A 1 98 ? 19.827 49.030 -38.442 1.00 22.58 ? ? ? ? ? ? 100 LEU A CB 1 ATOM 742 C CG . LEU A 1 98 ? 19.595 49.844 -37.168 1.00 21.21 ? ? ? ? ? ? 100 LEU A CG 1 ATOM 743 C CD1 . LEU A 1 98 ? 19.535 51.364 -37.409 1.00 25.83 ? ? ? ? ? ? 100 LEU A CD1 1 ATOM 744 C CD2 . LEU A 1 98 ? 18.396 49.373 -36.361 1.00 20.40 ? ? ? ? ? ? 100 LEU A CD2 1 ATOM 745 N N . TYR A 1 99 ? 22.715 50.878 -39.273 1.00 21.83 ? ? ? ? ? ? 101 TYR A N 1 ATOM 746 C CA . TYR A 1 99 ? 24.121 50.939 -38.988 1.00 21.69 ? ? ? ? ? ? 101 TYR A CA 1 ATOM 747 C C . TYR A 1 99 ? 24.314 51.712 -37.736 1.00 20.75 ? ? ? ? ? ? 101 TYR A C 1 ATOM 748 O O . TYR A 1 99 ? 23.656 52.703 -37.532 1.00 19.76 ? ? ? ? ? ? 101 TYR A O 1 ATOM 749 C CB . TYR A 1 99 ? 24.890 51.480 -40.186 1.00 22.03 ? ? ? ? ? ? 101 TYR A CB 1 ATOM 750 C CG . TYR A 1 99 ? 25.320 50.372 -41.087 1.00 22.85 ? ? ? ? ? ? 101 TYR A CG 1 ATOM 751 C CD1 . TYR A 1 99 ? 25.923 50.635 -42.288 1.00 25.76 ? ? ? ? ? ? 101 TYR A CD1 1 ATOM 752 C CD2 . TYR A 1 99 ? 25.099 49.037 -40.731 1.00 28.10 ? ? ? ? ? ? 101 TYR A CD2 1 ATOM 753 C CE1 . TYR A 1 99 ? 26.322 49.615 -43.147 1.00 29.14 ? ? ? ? ? ? 101 TYR A CE1 1 ATOM 754 C CE2 . TYR A 1 99 ? 25.478 47.958 -41.570 1.00 27.04 ? ? ? ? ? ? 101 TYR A CE2 1 ATOM 755 C CZ . TYR A 1 99 ? 26.097 48.266 -42.799 1.00 28.81 ? ? ? ? ? ? 101 TYR A CZ 1 ATOM 756 O OH . TYR A 1 99 ? 26.508 47.282 -43.689 1.00 25.17 ? ? ? ? ? ? 101 TYR A OH 1 ATOM 757 N N . PHE A 1 100 ? 25.796 51.509 -36.846 1.00 23.14 ? ? ? ? ? ? 108 PHE A N 1 ATOM 758 C CA . PHE A 1 100 ? 25.593 52.538 -35.802 1.00 22.74 ? ? ? ? ? ? 108 PHE A CA 1 ATOM 759 C C . PHE A 1 100 ? 26.853 53.325 -35.788 1.00 23.97 ? ? ? ? ? ? 108 PHE A C 1 ATOM 760 O O . PHE A 1 100 ? 27.890 52.816 -36.196 1.00 25.37 ? ? ? ? ? ? 108 PHE A O 1 ATOM 761 C CB . PHE A 1 100 ? 25.475 51.881 -34.427 1.00 22.25 ? ? ? ? ? ? 108 PHE A CB 1 ATOM 762 C CG . PHE A 1 100 ? 24.058 51.459 -34.040 1.00 16.70 ? ? ? ? ? ? 108 PHE A CG 1 ATOM 763 C CD1 . PHE A 1 100 ? 23.678 50.130 -34.142 1.00 15.08 ? ? ? ? ? ? 108 PHE A CD1 1 ATOM 764 C CD2 . PHE A 1 100 ? 23.131 52.378 -33.574 1.00 18.12 ? ? ? ? ? ? 108 PHE A CD2 1 ATOM 765 C CE1 . PHE A 1 100 ? 22.438 49.732 -33.768 1.00 16.12 ? ? ? ? ? ? 108 PHE A CE1 1 ATOM 766 C CE2 . PHE A 1 100 ? 21.855 51.997 -33.209 1.00 7.42 ? ? ? ? ? ? 108 PHE A CE2 1 ATOM 767 C CZ . PHE A 1 100 ? 21.483 50.736 -33.298 1.00 12.82 ? ? ? ? ? ? 108 PHE A CZ 1 ATOM 768 N N . GLY A 1 101 ? 26.807 54.533 -35.273 1.00 23.99 ? ? ? ? ? ? 109 GLY A N 1 ATOM 769 C CA . GLY A 1 101 ? 28.025 55.292 -35.101 1.00 24.15 ? ? ? ? ? ? 109 GLY A CA 1 ATOM 770 C C . GLY A 1 101 ? 28.791 54.785 -33.905 1.00 24.01 ? ? ? ? ? ? 109 GLY A C 1 ATOM 771 O O . GLY A 1 101 ? 28.454 53.768 -33.315 1.00 23.80 ? ? ? ? ? ? 109 GLY A O 1 ATOM 772 N N . ALA A 1 102 ? 29.861 55.467 -33.547 1.00 25.49 ? ? ? ? ? ? 110 ALA A N 1 ATOM 773 C CA . ALA A 1 102 ? 30.728 54.861 -32.550 1.00 25.77 ? ? ? ? ? ? 110 ALA A CA 1 ATOM 774 C C . ALA A 1 102 ? 30.348 55.522 -31.280 1.00 26.56 ? ? ? ? ? ? 110 ALA A C 1 ATOM 775 O O . ALA A 1 102 ? 30.881 55.249 -30.243 1.00 28.13 ? ? ? ? ? ? 110 ALA A O 1 ATOM 776 C CB . ALA A 1 102 ? 32.212 55.059 -32.896 1.00 26.23 ? ? ? ? ? ? 110 ALA A CB 1 ATOM 777 N N . GLY A 1 103 ? 29.351 56.381 -31.346 1.00 27.71 ? ? ? ? ? ? 111 GLY A N 1 ATOM 778 C CA . GLY A 1 103 ? 28.863 56.987 -30.135 1.00 27.86 ? ? ? ? ? ? 111 GLY A CA 1 ATOM 779 C C . GLY A 1 103 ? 29.637 58.278 -29.814 1.00 27.73 ? ? ? ? ? ? 111 GLY A C 1 ATOM 780 O O . GLY A 1 103 ? 30.829 58.413 -30.117 1.00 26.03 ? ? ? ? ? ? 111 GLY A O 1 ATOM 781 N N . THR A 1 104 ? 28.935 59.222 -29.182 1.00 28.75 ? ? ? ? ? ? 112 THR A N 1 ATOM 782 C CA . THR A 1 104 ? 29.537 60.467 -28.644 1.00 28.28 ? ? ? ? ? ? 112 THR A CA 1 ATOM 783 C C . THR A 1 104 ? 29.319 60.549 -27.147 1.00 28.92 ? ? ? ? ? ? 112 THR A C 1 ATOM 784 O O . THR A 1 104 ? 28.196 60.439 -26.702 1.00 30.00 ? ? ? ? ? ? 112 THR A O 1 ATOM 785 C CB . THR A 1 104 ? 28.947 61.626 -29.319 1.00 28.48 ? ? ? ? ? ? 112 THR A CB 1 ATOM 786 O OG1 . THR A 1 104 ? 29.185 61.457 -30.712 1.00 28.68 ? ? ? ? ? ? 112 THR A OG1 1 ATOM 787 C CG2 . THR A 1 104 ? 29.594 62.918 -28.838 1.00 31.20 ? ? ? ? ? ? 112 THR A CG2 1 ATOM 788 N N . ARG A 1 105 ? 30.403 60.636 -26.377 1.00 30.74 ? ? ? ? ? ? 113 ARG A N 1 ATOM 789 C CA . ARG A 1 105 ? 30.387 60.678 -24.924 1.00 32.03 ? ? ? ? ? ? 113 ARG A CA 1 ATOM 790 C C . ARG A 1 105 ? 30.446 62.132 -24.544 1.00 31.11 ? ? ? ? ? ? 113 ARG A C 1 ATOM 791 O O . ARG A 1 105 ? 31.453 62.776 -24.809 1.00 32.54 ? ? ? ? ? ? 113 ARG A O 1 ATOM 792 C CB . ARG A 1 105 ? 31.630 59.986 -24.374 1.00 32.00 ? ? ? ? ? ? 113 ARG A CB 1 ATOM 793 C CG . ARG A 1 105 ? 31.649 58.473 -24.550 1.00 35.71 ? ? ? ? ? ? 113 ARG A CG 1 ATOM 794 C CD . ARG A 1 105 ? 32.988 57.842 -24.112 1.00 37.55 ? ? ? ? ? ? 113 ARG A CD 1 ATOM 795 N NE . ARG A 1 105 ? 33.135 56.454 -24.554 1.00 44.07 ? ? ? ? ? ? 113 ARG A NE 1 ATOM 796 C CZ . ARG A 1 105 ? 34.213 55.711 -24.329 1.00 48.18 ? ? ? ? ? ? 113 ARG A CZ 1 ATOM 797 N NH1 . ARG A 1 105 ? 34.232 54.447 -24.748 1.00 49.96 ? ? ? ? ? ? 113 ARG A NH1 1 ATOM 798 N NH2 . ARG A 1 105 ? 35.280 56.233 -23.702 1.00 51.15 ? ? ? ? ? ? 113 ARG A NH2 1 ATOM 799 N N . LEU A 1 106 ? 29.386 62.644 -23.908 1.00 30.65 ? ? ? ? ? ? 114 LEU A N 1 ATOM 800 C CA . LEU A 1 106 ? 29.223 64.073 -23.619 1.00 29.44 ? ? ? ? ? ? 114 LEU A CA 1 ATOM 801 C C . LEU A 1 106 ? 29.274 64.390 -22.127 1.00 29.99 ? ? ? ? ? ? 114 LEU A C 1 ATOM 802 O O . LEU A 1 106 ? 29.050 63.498 -21.318 1.00 29.03 ? ? ? ? ? ? 114 LEU A O 1 ATOM 803 C CB . LEU A 1 106 ? 27.924 64.575 -24.216 1.00 29.38 ? ? ? ? ? ? 114 LEU A CB 1 ATOM 804 C CG . LEU A 1 106 ? 27.736 66.059 -23.995 1.00 27.56 ? ? ? ? ? ? 114 LEU A CG 1 ATOM 805 C CD1 . LEU A 1 106 ? 28.957 66.681 -24.544 1.00 27.56 ? ? ? ? ? ? 114 LEU A CD1 1 ATOM 806 C CD2 . LEU A 1 106 ? 26.492 66.543 -24.706 1.00 25.50 ? ? ? ? ? ? 114 LEU A CD2 1 ATOM 807 N N . SER A 1 107 ? 29.539 65.670 -21.765 1.00 30.00 ? ? ? ? ? ? 115 SER A N 1 ATOM 808 C CA . SER A 1 107 ? 29.621 66.072 -20.353 1.00 27.94 ? ? ? ? ? ? 115 SER A CA 1 ATOM 809 C C . SER A 1 107 ? 29.199 67.512 -20.170 1.00 27.64 ? ? ? ? ? ? 115 SER A C 1 ATOM 810 O O . SER A 1 107 ? 29.829 68.465 -20.669 1.00 25.16 ? ? ? ? ? ? 115 SER A O 1 ATOM 811 C CB . SER A 1 107 ? 31.035 65.824 -19.800 1.00 27.42 ? ? ? ? ? ? 115 SER A CB 1 ATOM 812 O OG . SER A 1 107 ? 31.646 64.723 -20.470 1.00 27.25 ? ? ? ? ? ? 115 SER A OG 1 ATOM 813 N N . VAL A 1 108 ? 28.123 67.651 -19.401 1.00 28.68 ? ? ? ? ? ? 116 VAL A N 1 ATOM 814 C CA . VAL A 1 108 ? 27.453 68.912 -19.238 1.00 29.51 ? ? ? ? ? ? 116 VAL A CA 1 ATOM 815 C C . VAL A 1 108 ? 27.605 69.348 -17.817 1.00 30.12 ? ? ? ? ? ? 116 VAL A C 1 ATOM 816 O O . VAL A 1 108 ? 26.847 68.922 -16.934 1.00 30.98 ? ? ? ? ? ? 116 VAL A O 1 ATOM 817 C CB . VAL A 1 108 ? 25.946 68.867 -19.510 1.00 29.62 ? ? ? ? ? ? 116 VAL A CB 1 ATOM 818 C CG1 . VAL A 1 108 ? 25.479 70.293 -19.652 1.00 29.79 ? ? ? ? ? ? 116 VAL A CG1 1 ATOM 819 C CG2 . VAL A 1 108 ? 25.636 68.102 -20.793 1.00 30.72 ? ? ? ? ? ? 116 VAL A CG2 1 ATOM 820 N N . LEU A 1 109 ? 28.600 70.205 -17.611 1.00 30.29 ? ? ? ? ? ? 117 LEU A N 1 ATOM 821 C CA . LEU A 1 109 ? 29.021 70.664 -16.285 1.00 30.02 ? ? ? ? ? ? 117 LEU A CA 1 ATOM 822 C C . LEU A 1 109 ? 28.991 72.211 -16.238 1.00 31.55 ? ? ? ? ? ? 117 LEU A C 1 ATOM 823 O O . LEU A 1 109 ? 28.115 72.739 -15.535 1.00 32.99 ? ? ? ? ? ? 117 LEU A O 1 ATOM 824 C CB . LEU A 1 109 ? 30.402 70.080 -15.927 1.00 27.75 ? ? ? ? ? ? 117 LEU A CB 1 ATOM 825 C CG . LEU A 1 109 ? 31.582 70.437 -16.806 1.00 25.62 ? ? ? ? ? ? 117 LEU A CG 1 ATOM 826 C CD1 . LEU A 1 109 ? 32.102 71.840 -16.433 1.00 25.56 ? ? ? ? ? ? 117 LEU A CD1 1 ATOM 827 C CD2 . LEU A 1 109 ? 32.699 69.428 -16.689 1.00 25.18 ? ? ? ? ? ? 117 LEU A CD2 1 ATOM 828 O OXT . LEU A 1 109 ? 29.765 72.971 -16.897 1.00 32.42 ? ? ? ? ? ? 117 LEU A OXT 1 ATOM 829 N N . SER B 2 2 ? -12.922 87.868 -57.323 1.00 49.46 ? ? ? ? ? ? 2 SER B N 1 ATOM 830 C CA . SER B 2 2 ? -11.806 87.540 -56.402 1.00 48.79 ? ? ? ? ? ? 2 SER B CA 1 ATOM 831 C C . SER B 2 2 ? -12.055 86.351 -55.422 1.00 49.31 ? ? ? ? ? ? 2 SER B C 1 ATOM 832 O O . SER B 2 2 ? -13.190 85.844 -55.322 1.00 48.83 ? ? ? ? ? ? 2 SER B O 1 ATOM 833 C CB . SER B 2 2 ? -11.469 88.790 -55.623 1.00 48.77 ? ? ? ? ? ? 2 SER B CB 1 ATOM 834 O OG . SER B 2 2 ? -10.170 88.647 -55.125 1.00 48.31 ? ? ? ? ? ? 2 SER B OG 1 ATOM 835 N N . GLN B 2 3 ? -10.986 85.888 -54.740 1.00 49.19 ? ? ? ? ? ? 3 GLN B N 1 ATOM 836 C CA . GLN B 2 3 ? -11.064 84.920 -53.596 1.00 48.86 ? ? ? ? ? ? 3 GLN B CA 1 ATOM 837 C C . GLN B 2 3 ? -11.487 85.698 -52.298 1.00 49.55 ? ? ? ? ? ? 3 GLN B C 1 ATOM 838 O O . GLN B 2 3 ? -10.695 86.513 -51.788 1.00 50.05 ? ? ? ? ? ? 3 GLN B O 1 ATOM 839 C CB . GLN B 2 3 ? -9.707 84.192 -53.388 1.00 48.33 ? ? ? ? ? ? 3 GLN B CB 1 ATOM 840 C CG . GLN B 2 3 ? -9.746 82.913 -52.500 1.00 47.69 ? ? ? ? ? ? 3 GLN B CG 1 ATOM 841 C CD . GLN B 2 3 ? -8.367 82.248 -52.242 1.00 46.58 ? ? ? ? ? ? 3 GLN B CD 1 ATOM 842 O OE1 . GLN B 2 3 ? -8.265 81.026 -52.113 1.00 42.58 ? ? ? ? ? ? 3 GLN B OE1 1 ATOM 843 N NE2 . GLN B 2 3 ? -7.321 83.060 -52.145 1.00 42.62 ? ? ? ? ? ? 3 GLN B NE2 1 ATOM 844 N N . PRO B 2 4 ? -12.730 85.463 -51.772 1.00 49.48 ? ? ? ? ? ? 4 PRO B N 1 ATOM 845 C CA . PRO B 2 4 ? -13.194 86.135 -50.554 1.00 49.75 ? ? ? ? ? ? 4 PRO B CA 1 ATOM 846 C C . PRO B 2 4 ? -12.220 85.975 -49.369 1.00 49.79 ? ? ? ? ? ? 4 PRO B C 1 ATOM 847 O O . PRO B 2 4 ? -11.565 84.909 -49.257 1.00 50.72 ? ? ? ? ? ? 4 PRO B O 1 ATOM 848 C CB . PRO B 2 4 ? -14.531 85.438 -50.253 1.00 49.38 ? ? ? ? ? ? 4 PRO B CB 1 ATOM 849 C CG . PRO B 2 4 ? -14.546 84.264 -51.047 1.00 49.06 ? ? ? ? ? ? 4 PRO B CG 1 ATOM 850 C CD . PRO B 2 4 ? -13.771 84.553 -52.267 1.00 49.45 ? ? ? ? ? ? 4 PRO B CD 1 ATOM 851 N N . ASP B 2 5 ? -12.093 87.039 -48.555 1.00 48.69 ? ? ? ? ? ? 5 ASP B N 1 ATOM 852 C CA . ASP B 2 5 ? -11.260 87.080 -47.343 1.00 47.45 ? ? ? ? ? ? 5 ASP B CA 1 ATOM 853 C C . ASP B 2 5 ? -11.474 85.845 -46.457 1.00 47.10 ? ? ? ? ? ? 5 ASP B C 1 ATOM 854 O O . ASP B 2 5 ? -12.635 85.374 -46.332 1.00 48.05 ? ? ? ? ? ? 5 ASP B O 1 ATOM 855 C CB . ASP B 2 5 ? -11.551 88.375 -46.572 1.00 48.22 ? ? ? ? ? ? 5 ASP B CB 1 ATOM 856 C CG . ASP B 2 5 ? -10.393 89.390 -46.650 1.00 47.87 ? ? ? ? ? ? 5 ASP B CG 1 ATOM 857 O OD1 . ASP B 2 5 ? -10.500 90.526 -46.098 1.00 46.94 ? ? ? ? ? ? 5 ASP B OD1 1 ATOM 858 O OD2 . ASP B 2 5 ? -9.356 89.014 -47.235 1.00 47.90 ? ? ? ? ? ? 5 ASP B OD2 1 ATOM 859 N N . PRO B 2 6 ? -10.389 85.287 -45.865 1.00 45.35 ? ? ? ? ? ? 6 PRO B N 1 ATOM 860 C CA . PRO B 2 6 ? -10.480 83.963 -45.209 1.00 44.40 ? ? ? ? ? ? 6 PRO B CA 1 ATOM 861 C C . PRO B 2 6 ? -11.416 84.024 -44.032 1.00 43.68 ? ? ? ? ? ? 6 PRO B C 1 ATOM 862 O O . PRO B 2 6 ? -11.791 85.140 -43.617 1.00 43.26 ? ? ? ? ? ? 6 PRO B O 1 ATOM 863 C CB . PRO B 2 6 ? -9.066 83.745 -44.672 1.00 44.87 ? ? ? ? ? ? 6 PRO B CB 1 ATOM 864 C CG . PRO B 2 6 ? -8.463 85.182 -44.538 1.00 45.39 ? ? ? ? ? ? 6 PRO B CG 1 ATOM 865 C CD . PRO B 2 6 ? -9.042 85.878 -45.734 1.00 45.51 ? ? ? ? ? ? 6 PRO B CD 1 ATOM 866 N N . MET B 2 7 ? -11.766 82.859 -43.482 1.00 43.29 ? ? ? ? ? ? 7 MET B N 1 ATOM 867 C CA . MET B 2 7 ? -12.558 82.791 -42.235 1.00 43.42 ? ? ? ? ? ? 7 MET B CA 1 ATOM 868 C C . MET B 2 7 ? -11.817 82.205 -41.022 1.00 41.64 ? ? ? ? ? ? 7 MET B C 1 ATOM 869 O O . MET B 2 7 ? -11.003 81.338 -41.176 1.00 41.74 ? ? ? ? ? ? 7 MET B O 1 ATOM 870 C CB . MET B 2 7 ? -13.867 82.057 -42.472 1.00 43.12 ? ? ? ? ? ? 7 MET B CB 1 ATOM 871 C CG . MET B 2 7 ? -14.881 82.876 -43.309 1.00 44.63 ? ? ? ? ? ? 7 MET B CG 1 ATOM 872 S SD . MET B 2 7 ? -16.391 82.001 -43.780 1.00 46.00 ? ? ? ? ? ? 7 MET B SD 1 ATOM 873 C CE . MET B 2 7 ? -16.086 81.536 -45.474 1.00 45.38 ? ? ? ? ? ? 7 MET B CE 1 ATOM 874 N N . PRO B 2 8 ? -12.075 82.739 -39.824 1.00 40.58 ? ? ? ? ? ? 8 PRO B N 1 ATOM 875 C CA . PRO B 2 8 ? -11.602 82.269 -38.537 1.00 39.41 ? ? ? ? ? ? 8 PRO B CA 1 ATOM 876 C C . PRO B 2 8 ? -11.354 80.759 -38.486 1.00 39.14 ? ? ? ? ? ? 8 PRO B C 1 ATOM 877 O O . PRO B 2 8 ? -10.205 80.297 -38.461 1.00 35.97 ? ? ? ? ? ? 8 PRO B O 1 ATOM 878 C CB . PRO B 2 8 ? -12.769 82.608 -37.614 1.00 40.15 ? ? ? ? ? ? 8 PRO B CB 1 ATOM 879 C CG . PRO B 2 8 ? -13.805 83.511 -38.512 1.00 41.93 ? ? ? ? ? ? 8 PRO B CG 1 ATOM 880 C CD . PRO B 2 8 ? -12.897 83.954 -39.673 1.00 40.17 ? ? ? ? ? ? 8 PRO B CD 1 ATOM 881 N N . ASP B 2 9 ? -12.459 80.012 -38.473 1.00 37.97 ? ? ? ? ? ? 9 ASP B N 1 ATOM 882 C CA . ASP B 2 9 ? -12.404 78.567 -38.416 1.00 37.87 ? ? ? ? ? ? 9 ASP B CA 1 ATOM 883 C C . ASP B 2 9 ? -12.072 78.072 -39.838 1.00 35.74 ? ? ? ? ? ? 9 ASP B C 1 ATOM 884 O O . ASP B 2 9 ? -12.058 76.906 -40.113 1.00 36.24 ? ? ? ? ? ? 9 ASP B O 1 ATOM 885 C CB . ASP B 2 9 ? -13.761 78.077 -37.934 1.00 37.93 ? ? ? ? ? ? 9 ASP B CB 1 ATOM 886 C CG . ASP B 2 9 ? -14.883 78.722 -38.711 1.00 41.67 ? ? ? ? ? ? 9 ASP B CG 1 ATOM 887 O OD1 . ASP B 2 9 ? -15.393 79.807 -38.263 1.00 38.95 ? ? ? ? ? ? 9 ASP B OD1 1 ATOM 888 O OD2 . ASP B 2 9 ? -15.217 78.135 -39.790 1.00 43.48 ? ? ? ? ? ? 9 ASP B OD2 1 ATOM 889 N N . ASP B 2 10 ? -11.808 78.983 -40.757 1.00 34.01 ? ? ? ? ? ? 10 ASP B N 1 ATOM 890 C CA . ASP B 2 10 ? -11.432 78.587 -42.104 1.00 31.00 ? ? ? ? ? ? 10 ASP B CA 1 ATOM 891 C C . ASP B 2 10 ? -9.941 78.590 -42.281 1.00 28.13 ? ? ? ? ? ? 10 ASP B C 1 ATOM 892 O O . ASP B 2 10 ? -9.442 78.366 -43.405 1.00 27.56 ? ? ? ? ? ? 10 ASP B O 1 ATOM 893 C CB . ASP B 2 10 ? -12.089 79.467 -43.162 1.00 31.03 ? ? ? ? ? ? 10 ASP B CB 1 ATOM 894 C CG . ASP B 2 10 ? -13.537 79.031 -43.497 1.00 34.41 ? ? ? ? ? ? 10 ASP B CG 1 ATOM 895 O OD1 . ASP B 2 10 ? -14.481 79.227 -42.651 1.00 34.30 ? ? ? ? ? ? 10 ASP B OD1 1 ATOM 896 O OD2 . ASP B 2 10 ? -13.741 78.495 -44.632 1.00 35.04 ? ? ? ? ? ? 10 ASP B OD2 1 ATOM 897 N N . LEU B 2 11 ? -9.251 78.865 -41.178 1.00 25.86 ? ? ? ? ? ? 11 LEU B N 1 ATOM 898 C CA . LEU B 2 11 ? -7.741 78.964 -41.092 1.00 23.56 ? ? ? ? ? ? 11 LEU B CA 1 ATOM 899 C C . LEU B 2 11 ? -7.166 77.868 -40.181 1.00 23.57 ? ? ? ? ? ? 11 LEU B C 1 ATOM 900 O O . LEU B 2 11 ? -7.882 77.367 -39.268 1.00 26.01 ? ? ? ? ? ? 11 LEU B O 1 ATOM 901 C CB . LEU B 2 11 ? -7.290 80.355 -40.609 1.00 20.63 ? ? ? ? ? ? 11 LEU B CB 1 ATOM 902 C CG . LEU B 2 11 ? -7.653 81.528 -41.534 1.00 18.00 ? ? ? ? ? ? 11 LEU B CG 1 ATOM 903 C CD1 . LEU B 2 11 ? -7.544 82.846 -40.865 1.00 12.99 ? ? ? ? ? ? 11 LEU B CD1 1 ATOM 904 C CD2 . LEU B 2 11 ? -6.781 81.594 -42.784 1.00 13.84 ? ? ? ? ? ? 11 LEU B CD2 1 ATOM 905 N N . HIS B 2 12 ? -5.936 77.438 -40.442 1.00 21.48 ? ? ? ? ? ? 12 HIS B N 1 ATOM 906 C CA . HIS B 2 12 ? -5.348 76.332 -39.727 1.00 20.33 ? ? ? ? ? ? 12 HIS B CA 1 ATOM 907 C C . HIS B 2 12 ? -4.675 76.904 -38.512 1.00 21.48 ? ? ? ? ? ? 12 HIS B C 1 ATOM 908 O O . HIS B 2 12 ? -4.085 78.055 -38.515 1.00 25.05 ? ? ? ? ? ? 12 HIS B O 1 ATOM 909 C CB . HIS B 2 12 ? -4.281 75.644 -40.576 1.00 20.41 ? ? ? ? ? ? 12 HIS B CB 1 ATOM 910 C CG . HIS B 2 12 ? -4.804 74.672 -41.605 1.00 17.84 ? ? ? ? ? ? 12 HIS B CG 1 ATOM 911 N ND1 . HIS B 2 12 ? -3.961 73.932 -42.413 1.00 16.88 ? ? ? ? ? ? 12 HIS B ND1 1 ATOM 912 C CD2 . HIS B 2 12 ? -6.056 74.271 -41.914 1.00 14.19 ? ? ? ? ? ? 12 HIS B CD2 1 ATOM 913 C CE1 . HIS B 2 12 ? -4.680 73.127 -43.182 1.00 19.53 ? ? ? ? ? ? 12 HIS B CE1 1 ATOM 914 N NE2 . HIS B 2 12 ? -5.958 73.341 -42.930 1.00 11.77 ? ? ? ? ? ? 12 HIS B NE2 1 ATOM 915 N N . LYS B 2 13 ? -4.684 76.094 -37.478 1.00 19.87 ? ? ? ? ? ? 13 LYS B N 1 ATOM 916 C CA . LYS B 2 13 ? -4.274 76.539 -36.217 1.00 15.64 ? ? ? ? ? ? 13 LYS B CA 1 ATOM 917 C C . LYS B 2 13 ? -3.105 75.722 -35.836 1.00 14.91 ? ? ? ? ? ? 13 LYS B C 1 ATOM 918 O O . LYS B 2 13 ? -3.162 74.456 -35.690 1.00 12.68 ? ? ? ? ? ? 13 LYS B O 1 ATOM 919 C CB . LYS B 2 13 ? -5.357 76.258 -35.218 1.00 16.55 ? ? ? ? ? ? 13 LYS B CB 1 ATOM 920 C CG . LYS B 2 13 ? -6.629 77.068 -35.451 1.00 18.23 ? ? ? ? ? ? 13 LYS B CG 1 ATOM 921 C CD . LYS B 2 13 ? -7.676 76.703 -34.429 1.00 17.83 ? ? ? ? ? ? 13 LYS B CD 1 ATOM 922 C CE . LYS B 2 13 ? -9.096 77.253 -34.794 1.00 17.38 ? ? ? ? ? ? 13 LYS B CE 1 ATOM 923 N NZ . LYS B 2 13 ? -9.703 76.685 -36.027 1.00 19.74 ? ? ? ? ? ? 13 LYS B NZ 1 ATOM 924 N N . SER B 2 14 ? -2.080 76.493 -35.533 1.00 9.93 ? ? ? ? ? ? 14 SER B N 1 ATOM 925 C CA . SER B 2 14 ? -0.873 76.010 -34.961 1.00 7.98 ? ? ? ? ? ? 14 SER B CA 1 ATOM 926 C C . SER B 2 14 ? -1.060 75.122 -33.772 1.00 8.16 ? ? ? ? ? ? 14 SER B C 1 ATOM 927 O O . SER B 2 14 ? -0.506 74.034 -33.780 1.00 7.79 ? ? ? ? ? ? 14 SER B O 1 ATOM 928 C CB . SER B 2 14 ? -0.015 77.203 -34.554 1.00 7.92 ? ? ? ? ? ? 14 SER B CB 1 ATOM 929 O OG . SER B 2 14 ? 1.229 76.758 -34.063 1.00 11.22 ? ? ? ? ? ? 14 SER B OG 1 ATOM 930 N N . SER B 2 15 ? -1.772 75.606 -32.717 1.00 9.50 ? ? ? ? ? ? 15 SER B N 1 ATOM 931 C CA . SER B 2 15 ? -2.182 74.794 -31.569 1.00 8.75 ? ? ? ? ? ? 15 SER B CA 1 ATOM 932 C C . SER B 2 15 ? -2.690 73.367 -31.957 1.00 7.50 ? ? ? ? ? ? 15 SER B C 1 ATOM 933 O O . SER B 2 15 ? -2.784 72.491 -31.119 1.00 2.00 ? ? ? ? ? ? 15 SER B O 1 ATOM 934 C CB . SER B 2 15 ? -3.361 75.457 -30.840 1.00 10.06 ? ? ? ? ? ? 15 SER B CB 1 ATOM 935 O OG . SER B 2 15 ? -4.501 75.523 -31.686 1.00 11.48 ? ? ? ? ? ? 15 SER B OG 1 ATOM 936 N N . GLU B 2 16 ? -3.118 73.202 -33.202 1.00 8.28 ? ? ? ? ? ? 16 GLU B N 1 ATOM 937 C CA . GLU B 2 16 ? -3.663 71.873 -33.584 1.00 8.32 ? ? ? ? ? ? 16 GLU B CA 1 ATOM 938 C C . GLU B 2 16 ? -2.693 70.973 -34.283 1.00 7.34 ? ? ? ? ? ? 16 GLU B C 1 ATOM 939 O O . GLU B 2 16 ? -3.077 69.906 -34.819 1.00 9.72 ? ? ? ? ? ? 16 GLU B O 1 ATOM 940 C CB . GLU B 2 16 ? -4.940 71.972 -34.384 1.00 6.90 ? ? ? ? ? ? 16 GLU B CB 1 ATOM 941 C CG . GLU B 2 16 ? -6.110 72.774 -33.611 1.00 13.03 ? ? ? ? ? ? 16 GLU B CG 1 ATOM 942 C CD . GLU B 2 16 ? -7.082 73.426 -34.592 1.00 15.44 ? ? ? ? ? ? 16 GLU B CD 1 ATOM 943 O OE1 . GLU B 2 16 ? -8.246 73.802 -34.204 1.00 14.49 ? ? ? ? ? ? 16 GLU B OE1 1 ATOM 944 O OE2 . GLU B 2 16 ? -6.693 73.489 -35.802 1.00 15.33 ? ? ? ? ? ? 16 GLU B OE2 1 ATOM 945 N N . PHE B 2 17 ? -1.447 71.346 -34.309 1.00 5.54 ? ? ? ? ? ? 17 PHE B N 1 ATOM 946 C CA . PHE B 2 17 ? -0.477 70.537 -35.005 1.00 8.01 ? ? ? ? ? ? 17 PHE B CA 1 ATOM 947 C C . PHE B 2 17 ? 0.634 70.002 -34.046 1.00 8.60 ? ? ? ? ? ? 17 PHE B C 1 ATOM 948 O O . PHE B 2 17 ? 1.639 70.697 -33.698 1.00 10.83 ? ? ? ? ? ? 17 PHE B O 1 ATOM 949 C CB . PHE B 2 17 ? 0.093 71.335 -36.173 1.00 9.38 ? ? ? ? ? ? 17 PHE B CB 1 ATOM 950 C CG . PHE B 2 17 ? 1.388 70.796 -36.738 1.00 8.94 ? ? ? ? ? ? 17 PHE B CG 1 ATOM 951 C CD1 . PHE B 2 17 ? 1.406 69.702 -37.581 1.00 8.04 ? ? ? ? ? ? 17 PHE B CD1 1 ATOM 952 C CD2 . PHE B 2 17 ? 2.592 71.437 -36.481 1.00 13.11 ? ? ? ? ? ? 17 PHE B CD2 1 ATOM 953 C CE1 . PHE B 2 17 ? 2.597 69.272 -38.139 1.00 3.89 ? ? ? ? ? ? 17 PHE B CE1 1 ATOM 954 C CE2 . PHE B 2 17 ? 3.797 70.956 -37.026 1.00 4.66 ? ? ? ? ? ? 17 PHE B CE2 1 ATOM 955 C CZ . PHE B 2 17 ? 3.789 69.927 -37.838 1.00 6.54 ? ? ? ? ? ? 17 PHE B CZ 1 ATOM 956 N N . THR B 2 18 ? 0.463 68.752 -33.636 1.00 5.37 ? ? ? ? ? ? 18 THR B N 1 ATOM 957 C CA . THR B 2 18 ? 1.315 68.198 -32.667 1.00 5.33 ? ? ? ? ? ? 18 THR B CA 1 ATOM 958 C C . THR B 2 18 ? 2.629 67.818 -33.297 1.00 4.69 ? ? ? ? ? ? 18 THR B C 1 ATOM 959 O O . THR B 2 18 ? 3.511 67.445 -32.597 1.00 4.77 ? ? ? ? ? ? 18 THR B O 1 ATOM 960 C CB . THR B 2 18 ? 0.720 66.955 -32.010 1.00 6.54 ? ? ? ? ? ? 18 THR B CB 1 ATOM 961 O OG1 . THR B 2 18 ? 1.465 65.775 -32.431 1.00 3.09 ? ? ? ? ? ? 18 THR B OG1 1 ATOM 962 C CG2 . THR B 2 18 ? -0.787 66.747 -32.453 1.00 6.57 ? ? ? ? ? ? 18 THR B CG2 1 ATOM 963 N N . GLY B 2 19 ? 2.715 68.028 -34.598 1.00 5.78 ? ? ? ? ? ? 19 GLY B N 1 ATOM 964 C CA . GLY B 2 19 ? 3.820 67.641 -35.507 1.00 6.84 ? ? ? ? ? ? 19 GLY B CA 1 ATOM 965 C C . GLY B 2 19 ? 5.073 68.363 -35.118 1.00 8.48 ? ? ? ? ? ? 19 GLY B C 1 ATOM 966 O O . GLY B 2 19 ? 5.154 68.776 -33.959 1.00 10.21 ? ? ? ? ? ? 19 GLY B O 1 ATOM 967 N N . THR B 2 20 ? 6.004 68.575 -36.076 1.00 8.52 ? ? ? ? ? ? 20 THR B N 1 ATOM 968 C CA . THR B 2 20 ? 7.187 69.354 -35.838 1.00 6.10 ? ? ? ? ? ? 20 THR B CA 1 ATOM 969 C C . THR B 2 20 ? 7.286 70.595 -36.787 1.00 4.47 ? ? ? ? ? ? 20 THR B C 1 ATOM 970 O O . THR B 2 20 ? 7.777 70.493 -37.870 1.00 7.92 ? ? ? ? ? ? 20 THR B O 1 ATOM 971 C CB . THR B 2 20 ? 8.422 68.486 -36.181 1.00 7.30 ? ? ? ? ? ? 20 THR B CB 1 ATOM 972 O OG1 . THR B 2 20 ? 8.455 67.268 -35.411 1.00 4.45 ? ? ? ? ? ? 20 THR B OG1 1 ATOM 973 C CG2 . THR B 2 20 ? 9.736 69.308 -35.881 1.00 5.58 ? ? ? ? ? ? 20 THR B CG2 1 ATOM 974 N N . MET B 2 21 ? 6.923 71.806 -36.425 1.00 7.84 ? ? ? ? ? ? 21 MET B N 1 ATOM 975 C CA . MET B 2 21 ? 6.991 72.951 -37.374 1.00 6.25 ? ? ? ? ? ? 21 MET B CA 1 ATOM 976 C C . MET B 2 21 ? 8.347 73.215 -38.035 1.00 6.67 ? ? ? ? ? ? 21 MET B C 1 ATOM 977 O O . MET B 2 21 ? 8.460 74.145 -38.823 1.00 9.47 ? ? ? ? ? ? 21 MET B O 1 ATOM 978 C CB . MET B 2 21 ? 6.533 74.221 -36.666 1.00 9.03 ? ? ? ? ? ? 21 MET B CB 1 ATOM 979 C CG . MET B 2 21 ? 6.240 75.448 -37.531 1.00 2.99 ? ? ? ? ? ? 21 MET B CG 1 ATOM 980 S SD . MET B 2 21 ? 4.679 75.068 -38.286 1.00 12.32 ? ? ? ? ? ? 21 MET B SD 1 ATOM 981 C CE . MET B 2 21 ? 3.576 75.454 -36.948 1.00 2.00 ? ? ? ? ? ? 21 MET B CE 1 ATOM 982 N N . GLY B 2 22 ? 9.354 72.348 -37.848 1.00 5.67 ? ? ? ? ? ? 22 GLY B N 1 ATOM 983 C CA . GLY B 2 22 ? 10.657 72.569 -38.394 1.00 5.46 ? ? ? ? ? ? 22 GLY B CA 1 ATOM 984 C C . GLY B 2 22 ? 10.691 72.137 -39.819 1.00 5.45 ? ? ? ? ? ? 22 GLY B C 1 ATOM 985 O O . GLY B 2 22 ? 11.374 72.766 -40.666 1.00 4.30 ? ? ? ? ? ? 22 GLY B O 1 ATOM 986 N N . ASN B 2 23 ? 9.894 71.108 -40.152 1.00 4.03 ? ? ? ? ? ? 23 ASN B N 1 ATOM 987 C CA . ASN B 2 23 ? 9.755 70.722 -41.544 1.00 2.32 ? ? ? ? ? ? 23 ASN B CA 1 ATOM 988 C C . ASN B 2 23 ? 9.094 71.790 -42.450 1.00 3.97 ? ? ? ? ? ? 23 ASN B C 1 ATOM 989 O O . ASN B 2 23 ? 9.135 71.699 -43.717 1.00 4.25 ? ? ? ? ? ? 23 ASN B O 1 ATOM 990 C CB . ASN B 2 23 ? 8.988 69.480 -41.632 1.00 3.48 ? ? ? ? ? ? 23 ASN B CB 1 ATOM 991 C CG . ASN B 2 23 ? 9.503 68.445 -40.683 1.00 4.51 ? ? ? ? ? ? 23 ASN B CG 1 ATOM 992 O OD1 . ASN B 2 23 ? 8.951 67.398 -40.603 1.00 2.00 ? ? ? ? ? ? 23 ASN B OD1 1 ATOM 993 N ND2 . ASN B 2 23 ? 10.684 68.724 -40.048 1.00 8.89 ? ? ? ? ? ? 23 ASN B ND2 1 ATOM 994 N N . MET B 2 24 ? 8.413 72.746 -41.824 1.00 4.15 ? ? ? ? ? ? 24 MET B N 1 ATOM 995 C CA . MET B 2 24 ? 7.869 73.871 -42.604 1.00 6.07 ? ? ? ? ? ? 24 MET B CA 1 ATOM 996 C C . MET B 2 24 ? 8.935 74.946 -42.606 1.00 8.10 ? ? ? ? ? ? 24 MET B C 1 ATOM 997 O O . MET B 2 24 ? 9.056 75.652 -43.569 1.00 11.97 ? ? ? ? ? ? 24 MET B O 1 ATOM 998 C CB . MET B 2 24 ? 6.585 74.375 -41.946 1.00 5.93 ? ? ? ? ? ? 24 MET B CB 1 ATOM 999 C CG . MET B 2 24 ? 6.282 75.875 -42.155 1.00 6.16 ? ? ? ? ? ? 24 MET B CG 1 ATOM 1000 S SD . MET B 2 24 ? 5.399 76.020 -43.732 1.00 11.88 ? ? ? ? ? ? 24 MET B SD 1 ATOM 1001 C CE . MET B 2 24 ? 4.033 74.884 -43.653 1.00 12.63 ? ? ? ? ? ? 24 MET B CE 1 ATOM 1002 N N . LYS B 2 25 ? 9.591 75.196 -41.477 1.00 9.51 ? ? ? ? ? ? 25 LYS B N 1 ATOM 1003 C CA . LYS B 2 25 ? 10.632 76.225 -41.474 1.00 12.64 ? ? ? ? ? ? 25 LYS B CA 1 ATOM 1004 C C . LYS B 2 25 ? 11.555 75.823 -42.623 1.00 12.16 ? ? ? ? ? ? 25 LYS B C 1 ATOM 1005 O O . LYS B 2 25 ? 11.972 76.666 -43.399 1.00 10.17 ? ? ? ? ? ? 25 LYS B O 1 ATOM 1006 C CB . LYS B 2 25 ? 11.449 76.210 -40.172 1.00 11.58 ? ? ? ? ? ? 25 LYS B CB 1 ATOM 1007 C CG . LYS B 2 25 ? 12.314 77.417 -39.928 1.00 13.23 ? ? ? ? ? ? 25 LYS B CG 1 ATOM 1008 C CD . LYS B 2 25 ? 13.033 77.369 -38.536 1.00 12.03 ? ? ? ? ? ? 25 LYS B CD 1 ATOM 1009 C CE . LYS B 2 25 ? 14.389 78.062 -38.522 1.00 11.09 ? ? ? ? ? ? 25 LYS B CE 1 ATOM 1010 N NZ . LYS B 2 25 ? 14.975 78.650 -37.246 1.00 9.14 ? ? ? ? ? ? 25 LYS B NZ 1 ATOM 1011 N N . TYR B 2 26 ? 11.729 74.508 -42.790 1.00 12.78 ? ? ? ? ? ? 26 TYR B N 1 ATOM 1012 C CA . TYR B 2 26 ? 12.779 73.942 -43.671 1.00 13.08 ? ? ? ? ? ? 26 TYR B CA 1 ATOM 1013 C C . TYR B 2 26 ? 12.727 74.501 -45.052 1.00 14.82 ? ? ? ? ? ? 26 TYR B C 1 ATOM 1014 O O . TYR B 2 26 ? 13.768 74.870 -45.606 1.00 16.26 ? ? ? ? ? ? 26 TYR B O 1 ATOM 1015 C CB . TYR B 2 26 ? 12.662 72.412 -43.825 1.00 15.17 ? ? ? ? ? ? 26 TYR B CB 1 ATOM 1016 C CG . TYR B 2 26 ? 13.626 71.883 -44.844 1.00 16.72 ? ? ? ? ? ? 26 TYR B CG 1 ATOM 1017 C CD1 . TYR B 2 26 ? 14.993 72.051 -44.706 1.00 16.69 ? ? ? ? ? ? 26 TYR B CD1 1 ATOM 1018 C CD2 . TYR B 2 26 ? 13.154 71.284 -45.989 1.00 22.97 ? ? ? ? ? ? 26 TYR B CD2 1 ATOM 1019 C CE1 . TYR B 2 26 ? 15.922 71.599 -45.696 1.00 17.03 ? ? ? ? ? ? 26 TYR B CE1 1 ATOM 1020 C CE2 . TYR B 2 26 ? 14.042 70.807 -46.984 1.00 21.75 ? ? ? ? ? ? 26 TYR B CE2 1 ATOM 1021 C CZ . TYR B 2 26 ? 15.423 71.017 -46.822 1.00 20.28 ? ? ? ? ? ? 26 TYR B CZ 1 ATOM 1022 O OH . TYR B 2 26 ? 16.212 70.601 -47.826 1.00 22.50 ? ? ? ? ? ? 26 TYR B OH 1 ATOM 1023 N N . LEU B 2 27 ? 11.513 74.577 -45.606 1.00 15.13 ? ? ? ? ? ? 27 LEU B N 1 ATOM 1024 C CA . LEU B 2 27 ? 11.258 74.998 -46.969 1.00 11.75 ? ? ? ? ? ? 27 LEU B CA 1 ATOM 1025 C C . LEU B 2 27 ? 11.462 76.511 -47.238 1.00 12.61 ? ? ? ? ? ? 27 LEU B C 1 ATOM 1026 O O . LEU B 2 27 ? 11.363 76.924 -48.416 1.00 13.55 ? ? ? ? ? ? 27 LEU B O 1 ATOM 1027 C CB . LEU B 2 27 ? 9.793 74.655 -47.240 1.00 11.96 ? ? ? ? ? ? 27 LEU B CB 1 ATOM 1028 C CG . LEU B 2 27 ? 9.249 73.293 -46.797 1.00 10.71 ? ? ? ? ? ? 27 LEU B CG 1 ATOM 1029 C CD1 . LEU B 2 27 ? 7.846 73.236 -47.184 1.00 8.09 ? ? ? ? ? ? 27 LEU B CD1 1 ATOM 1030 C CD2 . LEU B 2 27 ? 10.048 72.234 -47.482 1.00 10.20 ? ? ? ? ? ? 27 LEU B CD2 1 ATOM 1031 N N . TYR B 2 28 ? 11.605 77.351 -46.192 1.00 10.51 ? ? ? ? ? ? 28 TYR B N 1 ATOM 1032 C CA . TYR B 2 28 ? 11.910 78.786 -46.430 1.00 12.26 ? ? ? ? ? ? 28 TYR B CA 1 ATOM 1033 C C . TYR B 2 28 ? 13.061 79.521 -45.738 1.00 9.88 ? ? ? ? ? ? 28 TYR B C 1 ATOM 1034 O O . TYR B 2 28 ? 13.247 80.680 -45.994 1.00 9.05 ? ? ? ? ? ? 28 TYR B O 1 ATOM 1035 C CB . TYR B 2 28 ? 10.688 79.632 -46.251 1.00 12.47 ? ? ? ? ? ? 28 TYR B CB 1 ATOM 1036 C CG . TYR B 2 28 ? 9.486 79.043 -46.815 1.00 16.52 ? ? ? ? ? ? 28 TYR B CG 1 ATOM 1037 C CD1 . TYR B 2 28 ? 9.009 77.837 -46.342 1.00 17.14 ? ? ? ? ? ? 28 TYR B CD1 1 ATOM 1038 C CD2 . TYR B 2 28 ? 8.708 79.739 -47.700 1.00 17.99 ? ? ? ? ? ? 28 TYR B CD2 1 ATOM 1039 C CE1 . TYR B 2 28 ? 7.896 77.325 -46.807 1.00 19.39 ? ? ? ? ? ? 28 TYR B CE1 1 ATOM 1040 C CE2 . TYR B 2 28 ? 7.536 79.196 -48.149 1.00 18.75 ? ? ? ? ? ? 28 TYR B CE2 1 ATOM 1041 C CZ . TYR B 2 28 ? 7.138 78.013 -47.697 1.00 14.71 ? ? ? ? ? ? 28 TYR B CZ 1 ATOM 1042 O OH . TYR B 2 28 ? 5.988 77.435 -48.151 1.00 18.96 ? ? ? ? ? ? 28 TYR B OH 1 ATOM 1043 N N . ASP B 2 29 ? 13.834 78.889 -44.865 1.00 11.42 ? ? ? ? ? ? 29 ASP B N 1 ATOM 1044 C CA . ASP B 2 29 ? 15.039 79.582 -44.329 1.00 12.07 ? ? ? ? ? ? 29 ASP B CA 1 ATOM 1045 C C . ASP B 2 29 ? 16.120 79.506 -45.382 1.00 12.70 ? ? ? ? ? ? 29 ASP B C 1 ATOM 1046 O O . ASP B 2 29 ? 16.874 78.462 -45.477 1.00 13.45 ? ? ? ? ? ? 29 ASP B O 1 ATOM 1047 C CB . ASP B 2 29 ? 15.478 79.013 -42.972 1.00 12.05 ? ? ? ? ? ? 29 ASP B CB 1 ATOM 1048 C CG . ASP B 2 29 ? 16.523 79.893 -42.233 1.00 20.40 ? ? ? ? ? ? 29 ASP B CG 1 ATOM 1049 O OD1 . ASP B 2 29 ? 16.977 79.436 -41.118 1.00 25.56 ? ? ? ? ? ? 29 ASP B OD1 1 ATOM 1050 O OD2 . ASP B 2 29 ? 16.891 81.035 -42.722 1.00 21.98 ? ? ? ? ? ? 29 ASP B OD2 1 ATOM 1051 N N . ASP B 2 30 ? 16.145 80.510 -46.279 1.00 10.97 ? ? ? ? ? ? 30 ASP B N 1 ATOM 1052 C CA . ASP B 2 30 ? 17.227 80.571 -47.304 1.00 12.51 ? ? ? ? ? ? 30 ASP B CA 1 ATOM 1053 C C . ASP B 2 30 ? 17.311 79.226 -48.096 1.00 13.06 ? ? ? ? ? ? 30 ASP B C 1 ATOM 1054 O O . ASP B 2 30 ? 18.435 78.724 -48.297 1.00 12.50 ? ? ? ? ? ? 30 ASP B O 1 ATOM 1055 C CB . ASP B 2 30 ? 18.607 80.840 -46.658 1.00 12.06 ? ? ? ? ? ? 30 ASP B CB 1 ATOM 1056 C CG . ASP B 2 30 ? 19.697 81.234 -47.696 1.00 17.11 ? ? ? ? ? ? 30 ASP B CG 1 ATOM 1057 O OD1 . ASP B 2 30 ? 19.489 82.195 -48.463 1.00 15.72 ? ? ? ? ? ? 30 ASP B OD1 1 ATOM 1058 O OD2 . ASP B 2 30 ? 20.774 80.600 -47.724 1.00 14.13 ? ? ? ? ? ? 30 ASP B OD2 1 ATOM 1059 N N . HIS B 2 31 ? 16.132 78.730 -48.546 1.00 9.50 ? ? ? ? ? ? 31 HIS B N 1 ATOM 1060 C CA . HIS B 2 31 ? 15.966 77.483 -49.319 1.00 11.12 ? ? ? ? ? ? 31 HIS B CA 1 ATOM 1061 C C . HIS B 2 31 ? 15.071 77.866 -50.454 1.00 11.29 ? ? ? ? ? ? 31 HIS B C 1 ATOM 1062 O O . HIS B 2 31 ? 13.974 78.366 -50.185 1.00 16.56 ? ? ? ? ? ? 31 HIS B O 1 ATOM 1063 C CB . HIS B 2 31 ? 15.131 76.527 -48.447 1.00 9.99 ? ? ? ? ? ? 31 HIS B CB 1 ATOM 1064 C CG . HIS B 2 31 ? 14.696 75.288 -49.095 1.00 7.73 ? ? ? ? ? ? 31 HIS B CG 1 ATOM 1065 N ND1 . HIS B 2 31 ? 15.545 74.224 -49.295 1.00 2.00 ? ? ? ? ? ? 31 HIS B ND1 1 ATOM 1066 C CD2 . HIS B 2 31 ? 13.465 74.898 -49.547 1.00 14.99 ? ? ? ? ? ? 31 HIS B CD2 1 ATOM 1067 C CE1 . HIS B 2 31 ? 14.855 73.229 -49.825 1.00 11.39 ? ? ? ? ? ? 31 HIS B CE1 1 ATOM 1068 N NE2 . HIS B 2 31 ? 13.587 73.591 -49.959 1.00 5.47 ? ? ? ? ? ? 31 HIS B NE2 1 ATOM 1069 N N . TYR B 2 32 ? 15.557 77.760 -51.681 1.00 11.92 ? ? ? ? ? ? 32 TYR B N 1 ATOM 1070 C CA . TYR B 2 32 ? 14.771 77.896 -52.927 1.00 12.20 ? ? ? ? ? ? 32 TYR B CA 1 ATOM 1071 C C . TYR B 2 32 ? 15.646 77.342 -54.070 1.00 12.61 ? ? ? ? ? ? 32 TYR B C 1 ATOM 1072 O O . TYR B 2 32 ? 16.857 77.145 -53.874 1.00 10.79 ? ? ? ? ? ? 32 TYR B O 1 ATOM 1073 C CB . TYR B 2 32 ? 14.534 79.343 -53.236 1.00 12.35 ? ? ? ? ? ? 32 TYR B CB 1 ATOM 1074 C CG . TYR B 2 32 ? 15.805 80.063 -53.151 1.00 12.45 ? ? ? ? ? ? 32 TYR B CG 1 ATOM 1075 C CD1 . TYR B 2 32 ? 16.803 79.780 -54.022 1.00 7.96 ? ? ? ? ? ? 32 TYR B CD1 1 ATOM 1076 C CD2 . TYR B 2 32 ? 16.029 81.005 -52.146 1.00 10.10 ? ? ? ? ? ? 32 TYR B CD2 1 ATOM 1077 C CE1 . TYR B 2 32 ? 18.015 80.430 -53.913 1.00 11.27 ? ? ? ? ? ? 32 TYR B CE1 1 ATOM 1078 C CE2 . TYR B 2 32 ? 17.196 81.659 -52.046 1.00 11.49 ? ? ? ? ? ? 32 TYR B CE2 1 ATOM 1079 C CZ . TYR B 2 32 ? 18.206 81.364 -52.904 1.00 13.57 ? ? ? ? ? ? 32 TYR B CZ 1 ATOM 1080 O OH . TYR B 2 32 ? 19.445 81.985 -52.705 1.00 15.12 ? ? ? ? ? ? 32 TYR B OH 1 ATOM 1081 N N . VAL B 2 33 ? 15.053 77.207 -55.268 1.00 9.92 ? ? ? ? ? ? 33 VAL B N 1 ATOM 1082 C CA . VAL B 2 33 ? 15.792 76.815 -56.413 1.00 7.41 ? ? ? ? ? ? 33 VAL B CA 1 ATOM 1083 C C . VAL B 2 33 ? 15.738 77.982 -57.313 1.00 9.49 ? ? ? ? ? ? 33 VAL B C 1 ATOM 1084 O O . VAL B 2 33 ? 14.617 78.528 -57.530 1.00 7.51 ? ? ? ? ? ? 33 VAL B O 1 ATOM 1085 C CB . VAL B 2 33 ? 15.069 75.631 -57.030 1.00 7.08 ? ? ? ? ? ? 33 VAL B CB 1 ATOM 1086 C CG1 . VAL B 2 33 ? 15.556 75.285 -58.414 1.00 2.45 ? ? ? ? ? ? 33 VAL B CG1 1 ATOM 1087 C CG2 . VAL B 2 33 ? 15.150 74.529 -56.135 1.00 5.59 ? ? ? ? ? ? 33 VAL B CG2 1 ATOM 1088 N N . SER B 2 34 ? 16.898 78.390 -57.879 1.00 8.50 ? ? ? ? ? ? 34 SER B N 1 ATOM 1089 C CA . SER B 2 34 ? 16.866 79.564 -58.721 1.00 9.28 ? ? ? ? ? ? 34 SER B CA 1 ATOM 1090 C C . SER B 2 34 ? 17.727 79.393 -59.896 1.00 10.37 ? ? ? ? ? ? 34 SER B C 1 ATOM 1091 O O . SER B 2 34 ? 18.939 79.451 -59.788 1.00 14.13 ? ? ? ? ? ? 34 SER B O 1 ATOM 1092 C CB . SER B 2 34 ? 17.181 80.861 -58.005 1.00 10.40 ? ? ? ? ? ? 34 SER B CB 1 ATOM 1093 O OG . SER B 2 34 ? 16.973 81.971 -58.909 1.00 9.49 ? ? ? ? ? ? 34 SER B OG 1 ATOM 1094 N N . ALA B 2 35 ? 17.098 79.261 -61.062 1.00 11.32 ? ? ? ? ? ? 35 ALA B N 1 ATOM 1095 C CA . ALA B 2 35 ? 17.828 79.044 -62.324 1.00 9.78 ? ? ? ? ? ? 35 ALA B CA 1 ATOM 1096 C C . ALA B 2 35 ? 17.370 80.112 -63.260 1.00 8.82 ? ? ? ? ? ? 35 ALA B C 1 ATOM 1097 O O . ALA B 2 35 ? 16.275 80.511 -63.151 1.00 6.77 ? ? ? ? ? ? 35 ALA B O 1 ATOM 1098 C CB . ALA B 2 35 ? 17.474 77.737 -62.932 1.00 9.96 ? ? ? ? ? ? 35 ALA B CB 1 ATOM 1099 N N . THR B 2 36 ? 18.220 80.489 -64.208 1.00 10.12 ? ? ? ? ? ? 36 THR B N 1 ATOM 1100 C CA . THR B 2 36 ? 18.011 81.657 -65.118 1.00 11.05 ? ? ? ? ? ? 36 THR B CA 1 ATOM 1101 C C . THR B 2 36 ? 18.294 81.320 -66.544 1.00 12.61 ? ? ? ? ? ? 36 THR B C 1 ATOM 1102 O O . THR B 2 36 ? 19.354 80.861 -66.853 1.00 10.92 ? ? ? ? ? ? 36 THR B O 1 ATOM 1103 C CB . THR B 2 36 ? 18.942 82.743 -64.777 1.00 11.66 ? ? ? ? ? ? 36 THR B CB 1 ATOM 1104 O OG1 . THR B 2 36 ? 18.747 82.955 -63.382 1.00 15.75 ? ? ? ? ? ? 36 THR B OG1 1 ATOM 1105 C CG2 . THR B 2 36 ? 18.594 84.074 -65.630 1.00 11.27 ? ? ? ? ? ? 36 THR B CG2 1 ATOM 1106 N N . LYS B 2 37 ? 17.296 81.531 -67.430 1.00 14.89 ? ? ? ? ? ? 37 LYS B N 1 ATOM 1107 C CA . LYS B 2 37 ? 17.543 81.310 -68.814 1.00 13.99 ? ? ? ? ? ? 37 LYS B CA 1 ATOM 1108 C C . LYS B 2 37 ? 17.984 79.844 -68.958 1.00 14.22 ? ? ? ? ? ? 37 LYS B C 1 ATOM 1109 O O . LYS B 2 37 ? 19.196 79.574 -69.047 1.00 11.92 ? ? ? ? ? ? 37 LYS B O 1 ATOM 1110 C CB . LYS B 2 37 ? 18.653 82.324 -69.197 1.00 14.69 ? ? ? ? ? ? 37 LYS B CB 1 ATOM 1111 C CG . LYS B 2 37 ? 19.098 82.350 -70.666 1.00 14.92 ? ? ? ? ? ? 37 LYS B CG 1 ATOM 1112 C CD . LYS B 2 37 ? 20.481 83.023 -70.818 1.00 15.90 ? ? ? ? ? ? 37 LYS B CD 1 ATOM 1113 C CE . LYS B 2 37 ? 21.493 82.531 -69.826 1.00 18.89 ? ? ? ? ? ? 37 LYS B CE 1 ATOM 1114 N NZ . LYS B 2 37 ? 22.701 83.497 -70.086 1.00 25.94 ? ? ? ? ? ? 37 LYS B NZ 1 ATOM 1115 N N . VAL B 2 38 ? 17.018 78.889 -68.941 1.00 14.33 ? ? ? ? ? ? 38 VAL B N 1 ATOM 1116 C CA . VAL B 2 38 ? 17.333 77.460 -69.217 1.00 8.47 ? ? ? ? ? ? 38 VAL B CA 1 ATOM 1117 C C . VAL B 2 38 ? 16.156 76.741 -69.917 1.00 11.64 ? ? ? ? ? ? 38 VAL B C 1 ATOM 1118 O O . VAL B 2 38 ? 15.036 77.291 -70.018 1.00 11.70 ? ? ? ? ? ? 38 VAL B O 1 ATOM 1119 C CB . VAL B 2 38 ? 17.549 76.692 -67.969 1.00 9.41 ? ? ? ? ? ? 38 VAL B CB 1 ATOM 1120 C CG1 . VAL B 2 38 ? 18.761 77.135 -67.216 1.00 5.49 ? ? ? ? ? ? 38 VAL B CG1 1 ATOM 1121 C CG2 . VAL B 2 38 ? 16.192 76.623 -66.976 1.00 3.34 ? ? ? ? ? ? 38 VAL B CG2 1 ATOM 1122 N N . LYS B 2 39 ? 16.348 75.481 -70.341 1.00 8.26 ? ? ? ? ? ? 39 LYS B N 1 ATOM 1123 C CA . LYS B 2 39 ? 15.260 74.869 -70.996 1.00 7.03 ? ? ? ? ? ? 39 LYS B CA 1 ATOM 1124 C C . LYS B 2 39 ? 15.158 73.459 -70.546 1.00 7.23 ? ? ? ? ? ? 39 LYS B C 1 ATOM 1125 O O . LYS B 2 39 ? 16.188 72.769 -70.251 1.00 4.87 ? ? ? ? ? ? 39 LYS B O 1 ATOM 1126 C CB . LYS B 2 39 ? 15.431 74.849 -72.513 1.00 8.92 ? ? ? ? ? ? 39 LYS B CB 1 ATOM 1127 C CG . LYS B 2 39 ? 14.042 74.528 -73.349 1.00 8.95 ? ? ? ? ? ? 39 LYS B CG 1 ATOM 1128 C CD . LYS B 2 39 ? 14.417 74.176 -74.848 1.00 5.73 ? ? ? ? ? ? 39 LYS B CD 1 ATOM 1129 C CE . LYS B 2 39 ? 15.312 75.405 -75.341 1.00 11.99 ? ? ? ? ? ? 39 LYS B CE 1 ATOM 1130 N NZ . LYS B 2 39 ? 15.446 75.446 -76.803 1.00 16.06 ? ? ? ? ? ? 39 LYS B NZ 1 ATOM 1131 N N . SER B 2 40 ? 13.887 73.080 -70.432 1.00 4.91 ? ? ? ? ? ? 40 SER B N 1 ATOM 1132 C CA . SER B 2 40 ? 13.521 71.755 -69.977 1.00 6.31 ? ? ? ? ? ? 40 SER B CA 1 ATOM 1133 C C . SER B 2 40 ? 14.456 70.798 -70.680 1.00 4.19 ? ? ? ? ? ? 40 SER B C 1 ATOM 1134 O O . SER B 2 40 ? 14.844 71.105 -71.730 1.00 7.46 ? ? ? ? ? ? 40 SER B O 1 ATOM 1135 C CB . SER B 2 40 ? 12.115 71.366 -70.441 1.00 3.16 ? ? ? ? ? ? 40 SER B CB 1 ATOM 1136 O OG . SER B 2 40 ? 12.137 69.930 -70.572 1.00 4.42 ? ? ? ? ? ? 40 SER B OG 1 ATOM 1137 N N . VAL B 2 41 ? 14.734 69.669 -70.124 1.00 4.68 ? ? ? ? ? ? 41 VAL B N 1 ATOM 1138 C CA . VAL B 2 41 ? 15.584 68.637 -70.775 1.00 5.16 ? ? ? ? ? ? 41 VAL B CA 1 ATOM 1139 C C . VAL B 2 41 ? 15.081 67.212 -70.608 1.00 6.17 ? ? ? ? ? ? 41 VAL B C 1 ATOM 1140 O O . VAL B 2 41 ? 15.809 66.230 -70.835 1.00 8.77 ? ? ? ? ? ? 41 VAL B O 1 ATOM 1141 C CB . VAL B 2 41 ? 16.973 68.667 -70.217 1.00 3.62 ? ? ? ? ? ? 41 VAL B CB 1 ATOM 1142 C CG1 . VAL B 2 41 ? 17.543 70.203 -70.141 1.00 2.00 ? ? ? ? ? ? 41 VAL B CG1 1 ATOM 1143 C CG2 . VAL B 2 41 ? 16.981 68.059 -68.909 1.00 2.37 ? ? ? ? ? ? 41 VAL B CG2 1 ATOM 1144 N N . ASP B 2 42 ? 13.868 67.049 -70.145 1.00 7.39 ? ? ? ? ? ? 42 ASP B N 1 ATOM 1145 C CA . ASP B 2 42 ? 13.306 65.666 -70.092 1.00 9.19 ? ? ? ? ? ? 42 ASP B CA 1 ATOM 1146 C C . ASP B 2 42 ? 11.941 65.741 -69.522 1.00 8.29 ? ? ? ? ? ? 42 ASP B C 1 ATOM 1147 O O . ASP B 2 42 ? 11.325 66.848 -69.425 1.00 9.02 ? ? ? ? ? ? 42 ASP B O 1 ATOM 1148 C CB . ASP B 2 42 ? 14.161 64.741 -69.201 1.00 8.49 ? ? ? ? ? ? 42 ASP B CB 1 ATOM 1149 C CG . ASP B 2 42 ? 13.714 63.283 -69.281 1.00 12.22 ? ? ? ? ? ? 42 ASP B CG 1 ATOM 1150 O OD1 . ASP B 2 42 ? 14.480 62.410 -68.854 1.00 9.11 ? ? ? ? ? ? 42 ASP B OD1 1 ATOM 1151 O OD2 . ASP B 2 42 ? 12.595 62.983 -69.819 1.00 14.09 ? ? ? ? ? ? 42 ASP B OD2 1 ATOM 1152 N N . LYS B 2 43 ? 11.473 64.586 -69.038 1.00 8.95 ? ? ? ? ? ? 43 LYS B N 1 ATOM 1153 C CA . LYS B 2 43 ? 10.139 64.519 -68.495 1.00 7.59 ? ? ? ? ? ? 43 LYS B CA 1 ATOM 1154 C C . LYS B 2 43 ? 9.684 63.146 -68.063 1.00 10.74 ? ? ? ? ? ? 43 LYS B C 1 ATOM 1155 O O . LYS B 2 43 ? 10.015 62.135 -68.714 1.00 10.33 ? ? ? ? ? ? 43 LYS B O 1 ATOM 1156 C CB . LYS B 2 43 ? 9.253 65.059 -69.569 1.00 5.57 ? ? ? ? ? ? 43 LYS B CB 1 ATOM 1157 C CG . LYS B 2 43 ? 7.828 64.484 -69.586 1.00 10.36 ? ? ? ? ? ? 43 LYS B CG 1 ATOM 1158 C CD . LYS B 2 43 ? 6.985 64.859 -70.881 1.00 3.92 ? ? ? ? ? ? 43 LYS B CD 1 ATOM 1159 C CE . LYS B 2 43 ? 6.779 66.394 -71.226 1.00 11.54 ? ? ? ? ? ? 43 LYS B CE 1 ATOM 1160 N NZ . LYS B 2 43 ? 5.771 67.268 -70.464 1.00 12.95 ? ? ? ? ? ? 43 LYS B NZ 1 ATOM 1161 N N . PHE B 2 44 ? 8.899 63.089 -66.973 1.00 13.77 ? ? ? ? ? ? 44 PHE B N 1 ATOM 1162 C CA . PHE B 2 44 ? 8.231 61.846 -66.431 1.00 13.20 ? ? ? ? ? ? 44 PHE B CA 1 ATOM 1163 C C . PHE B 2 44 ? 6.713 61.771 -66.767 1.00 13.65 ? ? ? ? ? ? 44 PHE B C 1 ATOM 1164 O O . PHE B 2 44 ? 6.333 61.164 -67.764 1.00 14.30 ? ? ? ? ? ? 44 PHE B O 1 ATOM 1165 C CB . PHE B 2 44 ? 8.265 61.820 -64.913 1.00 15.36 ? ? ? ? ? ? 44 PHE B CB 1 ATOM 1166 C CG . PHE B 2 44 ? 7.633 60.568 -64.303 1.00 18.19 ? ? ? ? ? ? 44 PHE B CG 1 ATOM 1167 C CD1 . PHE B 2 44 ? 7.180 60.562 -63.004 1.00 25.22 ? ? ? ? ? ? 44 PHE B CD1 1 ATOM 1168 C CD2 . PHE B 2 44 ? 7.398 59.431 -65.070 1.00 23.88 ? ? ? ? ? ? 44 PHE B CD2 1 ATOM 1169 C CE1 . PHE B 2 44 ? 6.605 59.390 -62.409 1.00 26.02 ? ? ? ? ? ? 44 PHE B CE1 1 ATOM 1170 C CE2 . PHE B 2 44 ? 6.800 58.257 -64.475 1.00 24.48 ? ? ? ? ? ? 44 PHE B CE2 1 ATOM 1171 C CZ . PHE B 2 44 ? 6.431 58.275 -63.141 1.00 25.14 ? ? ? ? ? ? 44 PHE B CZ 1 ATOM 1172 N N . LEU B 2 45 ? 5.846 62.308 -65.937 1.00 10.95 ? ? ? ? ? ? 45 LEU B N 1 ATOM 1173 C CA . LEU B 2 45 ? 4.420 62.211 -66.290 1.00 13.95 ? ? ? ? ? ? 45 LEU B CA 1 ATOM 1174 C C . LEU B 2 45 ? 4.007 63.403 -67.129 1.00 13.43 ? ? ? ? ? ? 45 LEU B C 1 ATOM 1175 O O . LEU B 2 45 ? 4.714 64.387 -67.080 1.00 13.44 ? ? ? ? ? ? 45 LEU B O 1 ATOM 1176 C CB . LEU B 2 45 ? 3.533 62.034 -65.052 1.00 12.98 ? ? ? ? ? ? 45 LEU B CB 1 ATOM 1177 C CG . LEU B 2 45 ? 3.491 60.557 -64.573 1.00 17.93 ? ? ? ? ? ? 45 LEU B CG 1 ATOM 1178 C CD1 . LEU B 2 45 ? 2.605 60.444 -63.348 1.00 15.62 ? ? ? ? ? ? 45 LEU B CD1 1 ATOM 1179 C CD2 . LEU B 2 45 ? 2.989 59.653 -65.701 1.00 18.26 ? ? ? ? ? ? 45 LEU B CD2 1 ATOM 1180 N N . ALA B 2 46 ? 2.807 63.332 -67.766 1.00 15.53 ? ? ? ? ? ? 46 ALA B N 1 ATOM 1181 C CA . ALA B 2 46 ? 2.294 64.222 -68.816 1.00 13.36 ? ? ? ? ? ? 46 ALA B CA 1 ATOM 1182 C C . ALA B 2 46 ? 2.261 65.697 -68.384 1.00 14.37 ? ? ? ? ? ? 46 ALA B C 1 ATOM 1183 O O . ALA B 2 46 ? 1.548 66.560 -68.990 1.00 16.33 ? ? ? ? ? ? 46 ALA B O 1 ATOM 1184 C CB . ALA B 2 46 ? 0.974 63.805 -69.171 1.00 15.72 ? ? ? ? ? ? 46 ALA B CB 1 ATOM 1185 N N . HIS B 2 47 ? 2.986 65.981 -67.335 1.00 11.62 ? ? ? ? ? ? 47 HIS B N 1 ATOM 1186 C CA . HIS B 2 47 ? 2.946 67.269 -66.763 1.00 12.15 ? ? ? ? ? ? 47 HIS B CA 1 ATOM 1187 C C . HIS B 2 47 ? 4.089 67.604 -65.841 1.00 12.13 ? ? ? ? ? ? 47 HIS B C 1 ATOM 1188 O O . HIS B 2 47 ? 3.843 68.485 -65.023 1.00 16.78 ? ? ? ? ? ? 47 HIS B O 1 ATOM 1189 C CB . HIS B 2 47 ? 1.627 67.475 -65.997 1.00 11.30 ? ? ? ? ? ? 47 HIS B CB 1 ATOM 1190 C CG . HIS B 2 47 ? 1.524 66.644 -64.769 1.00 8.04 ? ? ? ? ? ? 47 HIS B CG 1 ATOM 1191 N ND1 . HIS B 2 47 ? 1.415 65.265 -64.818 1.00 11.28 ? ? ? ? ? ? 47 HIS B ND1 1 ATOM 1192 C CD2 . HIS B 2 47 ? 1.572 66.966 -63.462 1.00 9.91 ? ? ? ? ? ? 47 HIS B CD2 1 ATOM 1193 C CE1 . HIS B 2 47 ? 1.331 64.779 -63.591 1.00 12.14 ? ? ? ? ? ? 47 HIS B CE1 1 ATOM 1194 N NE2 . HIS B 2 47 ? 1.447 65.780 -62.744 1.00 11.10 ? ? ? ? ? ? 47 HIS B NE2 1 ATOM 1195 N N . ASP B 2 48 ? 5.329 67.095 -66.039 1.00 10.44 ? ? ? ? ? ? 48 ASP B N 1 ATOM 1196 C CA . ASP B 2 48 ? 6.482 67.608 -65.281 1.00 10.07 ? ? ? ? ? ? 48 ASP B CA 1 ATOM 1197 C C . ASP B 2 48 ? 7.732 67.723 -66.130 1.00 11.73 ? ? ? ? ? ? 48 ASP B C 1 ATOM 1198 O O . ASP B 2 48 ? 8.044 66.806 -66.774 1.00 12.14 ? ? ? ? ? ? 48 ASP B O 1 ATOM 1199 C CB . ASP B 2 48 ? 6.804 66.628 -64.196 1.00 10.01 ? ? ? ? ? ? 48 ASP B CB 1 ATOM 1200 C CG . ASP B 2 48 ? 7.151 65.308 -64.774 1.00 12.06 ? ? ? ? ? ? 48 ASP B CG 1 ATOM 1201 O OD1 . ASP B 2 48 ? 6.255 64.716 -65.450 1.00 16.00 ? ? ? ? ? ? 48 ASP B OD1 1 ATOM 1202 O OD2 . ASP B 2 48 ? 8.334 64.933 -64.674 1.00 10.05 ? ? ? ? ? ? 48 ASP B OD2 1 ATOM 1203 N N . LEU B 2 49 ? 8.419 68.874 -66.147 1.00 14.01 ? ? ? ? ? ? 49 LEU B N 1 ATOM 1204 C CA . LEU B 2 49 ? 9.622 69.109 -66.936 1.00 11.39 ? ? ? ? ? ? 49 LEU B CA 1 ATOM 1205 C C . LEU B 2 49 ? 10.864 69.134 -66.050 1.00 10.43 ? ? ? ? ? ? 49 LEU B C 1 ATOM 1206 O O . LEU B 2 49 ? 10.920 69.975 -65.207 1.00 8.63 ? ? ? ? ? ? 49 LEU B O 1 ATOM 1207 C CB . LEU B 2 49 ? 9.471 70.402 -67.733 1.00 14.66 ? ? ? ? ? ? 49 LEU B CB 1 ATOM 1208 C CG . LEU B 2 49 ? 7.996 70.851 -67.931 1.00 11.19 ? ? ? ? ? ? 49 LEU B CG 1 ATOM 1209 C CD1 . LEU B 2 49 ? 8.099 72.163 -68.333 1.00 10.92 ? ? ? ? ? ? 49 LEU B CD1 1 ATOM 1210 C CD2 . LEU B 2 49 ? 7.245 70.080 -68.995 1.00 11.02 ? ? ? ? ? ? 49 LEU B CD2 1 ATOM 1211 N N . ILE B 2 50 ? 11.770 68.146 -66.209 1.00 8.25 ? ? ? ? ? ? 50 ILE B N 1 ATOM 1212 C CA . ILE B 2 50 ? 13.045 68.051 -65.544 1.00 9.33 ? ? ? ? ? ? 50 ILE B CA 1 ATOM 1213 C C . ILE B 2 50 ? 14.068 69.010 -66.171 1.00 10.09 ? ? ? ? ? ? 50 ILE B C 1 ATOM 1214 O O . ILE B 2 50 ? 14.155 69.097 -67.364 1.00 11.32 ? ? ? ? ? ? 50 ILE B O 1 ATOM 1215 C CB . ILE B 2 50 ? 13.693 66.661 -65.734 1.00 10.94 ? ? ? ? ? ? 50 ILE B CB 1 ATOM 1216 C CG1 . ILE B 2 50 ? 12.772 65.492 -65.444 1.00 7.35 ? ? ? ? ? ? 50 ILE B CG1 1 ATOM 1217 C CG2 . ILE B 2 50 ? 15.055 66.522 -64.894 1.00 15.10 ? ? ? ? ? ? 50 ILE B CG2 1 ATOM 1218 C CD1 . ILE B 2 50 ? 12.196 65.557 -64.237 1.00 19.03 ? ? ? ? ? ? 50 ILE B CD1 1 ATOM 1219 N N . TYR B 2 51 ? 14.861 69.697 -65.394 1.00 10.16 ? ? ? ? ? ? 51 TYR B N 1 ATOM 1220 C CA . TYR B 2 51 ? 15.858 70.595 -65.925 1.00 10.62 ? ? ? ? ? ? 51 TYR B CA 1 ATOM 1221 C C . TYR B 2 51 ? 17.190 70.100 -65.383 1.00 13.67 ? ? ? ? ? ? 51 TYR B C 1 ATOM 1222 O O . TYR B 2 51 ? 17.173 69.256 -64.457 1.00 13.15 ? ? ? ? ? ? 51 TYR B O 1 ATOM 1223 C CB . TYR B 2 51 ? 15.580 71.985 -65.381 1.00 9.74 ? ? ? ? ? ? 51 TYR B CB 1 ATOM 1224 C CG . TYR B 2 51 ? 14.372 72.680 -66.007 1.00 4.41 ? ? ? ? ? ? 51 TYR B CG 1 ATOM 1225 C CD1 . TYR B 2 51 ? 13.066 72.166 -65.865 1.00 9.42 ? ? ? ? ? ? 51 TYR B CD1 1 ATOM 1226 C CD2 . TYR B 2 51 ? 14.534 73.789 -66.752 1.00 2.00 ? ? ? ? ? ? 51 TYR B CD2 1 ATOM 1227 C CE1 . TYR B 2 51 ? 11.920 72.867 -66.435 1.00 3.76 ? ? ? ? ? ? 51 TYR B CE1 1 ATOM 1228 C CE2 . TYR B 2 51 ? 13.431 74.465 -67.376 1.00 3.37 ? ? ? ? ? ? 51 TYR B CE2 1 ATOM 1229 C CZ . TYR B 2 51 ? 12.132 73.991 -67.193 1.00 2.47 ? ? ? ? ? ? 51 TYR B CZ 1 ATOM 1230 O OH . TYR B 2 51 ? 11.103 74.610 -67.833 1.00 2.40 ? ? ? ? ? ? 51 TYR B OH 1 ATOM 1231 N N . ASN B 2 52 ? 18.309 70.669 -65.826 1.00 11.97 ? ? ? ? ? ? 52 ASN B N 1 ATOM 1232 C CA . ASN B 2 52 ? 19.512 70.170 -65.302 1.00 16.18 ? ? ? ? ? ? 52 ASN B CA 1 ATOM 1233 C C . ASN B 2 52 ? 20.011 71.357 -64.563 1.00 18.09 ? ? ? ? ? ? 52 ASN B C 1 ATOM 1234 O O . ASN B 2 52 ? 20.932 72.001 -65.058 1.00 16.56 ? ? ? ? ? ? 52 ASN B O 1 ATOM 1235 C CB . ASN B 2 52 ? 20.539 69.722 -66.381 1.00 14.82 ? ? ? ? ? ? 52 ASN B CB 1 ATOM 1236 C CG . ASN B 2 52 ? 20.068 68.591 -67.201 1.00 18.24 ? ? ? ? ? ? 52 ASN B CG 1 ATOM 1237 O OD1 . ASN B 2 52 ? 19.771 67.528 -66.662 1.00 22.02 ? ? ? ? ? ? 52 ASN B OD1 1 ATOM 1238 N ND2 . ASN B 2 52 ? 19.954 68.790 -68.538 1.00 15.48 ? ? ? ? ? ? 52 ASN B ND2 1 ATOM 1239 N N . ILE B 2 53 ? 19.397 71.620 -63.404 1.00 19.01 ? ? ? ? ? ? 53 ILE B N 1 ATOM 1240 C CA . ILE B 2 53 ? 19.784 72.713 -62.507 1.00 18.95 ? ? ? ? ? ? 53 ILE B CA 1 ATOM 1241 C C . ILE B 2 53 ? 20.574 72.138 -61.328 1.00 19.83 ? ? ? ? ? ? 53 ILE B C 1 ATOM 1242 O O . ILE B 2 53 ? 20.063 71.356 -60.587 1.00 18.44 ? ? ? ? ? ? 53 ILE B O 1 ATOM 1243 C CB . ILE B 2 53 ? 18.514 73.413 -61.941 1.00 18.10 ? ? ? ? ? ? 53 ILE B CB 1 ATOM 1244 C CG1 . ILE B 2 53 ? 17.650 74.111 -63.022 1.00 20.40 ? ? ? ? ? ? 53 ILE B CG1 1 ATOM 1245 C CG2 . ILE B 2 53 ? 18.850 74.429 -60.893 1.00 15.21 ? ? ? ? ? ? 53 ILE B CG2 1 ATOM 1246 C CD1 . ILE B 2 53 ? 18.495 74.743 -64.053 1.00 28.21 ? ? ? ? ? ? 53 ILE B CD1 1 ATOM 1247 N N . SER B 2 54 ? 21.773 72.639 -61.067 1.00 20.41 ? ? ? ? ? ? 54 SER B N 1 ATOM 1248 C CA . SER B 2 54 ? 22.556 72.066 -59.997 1.00 19.93 ? ? ? ? ? ? 54 SER B CA 1 ATOM 1249 C C . SER B 2 54 ? 22.663 72.786 -58.690 1.00 21.74 ? ? ? ? ? ? 54 SER B C 1 ATOM 1250 O O . SER B 2 54 ? 23.084 73.939 -58.644 1.00 22.49 ? ? ? ? ? ? 54 SER B O 1 ATOM 1251 C CB . SER B 2 54 ? 24.016 71.951 -60.412 1.00 19.12 ? ? ? ? ? ? 54 SER B CB 1 ATOM 1252 O OG . SER B 2 54 ? 24.117 71.236 -61.577 1.00 19.90 ? ? ? ? ? ? 54 SER B OG 1 ATOM 1253 N N . ASP B 2 55 ? 22.484 72.032 -57.619 1.00 24.40 ? ? ? ? ? ? 55 ASP B N 1 ATOM 1254 C CA . ASP B 2 55 ? 22.631 72.525 -56.276 1.00 27.39 ? ? ? ? ? ? 55 ASP B CA 1 ATOM 1255 C C . ASP B 2 55 ? 23.850 73.400 -56.170 1.00 28.79 ? ? ? ? ? ? 55 ASP B C 1 ATOM 1256 O O . ASP B 2 55 ? 24.937 72.900 -56.246 1.00 29.60 ? ? ? ? ? ? 55 ASP B O 1 ATOM 1257 C CB . ASP B 2 55 ? 22.775 71.310 -55.333 1.00 28.70 ? ? ? ? ? ? 55 ASP B CB 1 ATOM 1258 C CG . ASP B 2 55 ? 22.622 71.670 -53.853 1.00 28.72 ? ? ? ? ? ? 55 ASP B CG 1 ATOM 1259 O OD1 . ASP B 2 55 ? 22.728 70.776 -52.983 1.00 21.42 ? ? ? ? ? ? 55 ASP B OD1 1 ATOM 1260 O OD2 . ASP B 2 55 ? 22.423 72.871 -53.570 1.00 29.02 ? ? ? ? ? ? 55 ASP B OD2 1 ATOM 1261 N N . LYS B 2 56 ? 23.689 74.715 -55.947 1.00 30.83 ? ? ? ? ? ? 56 LYS B N 1 ATOM 1262 C CA . LYS B 2 56 ? 24.874 75.548 -55.684 1.00 30.73 ? ? ? ? ? ? 56 LYS B CA 1 ATOM 1263 C C . LYS B 2 56 ? 25.373 75.552 -54.230 1.00 30.90 ? ? ? ? ? ? 56 LYS B C 1 ATOM 1264 O O . LYS B 2 56 ? 26.582 75.461 -53.950 1.00 32.61 ? ? ? ? ? ? 56 LYS B O 1 ATOM 1265 C CB . LYS B 2 56 ? 24.687 76.960 -56.247 1.00 31.60 ? ? ? ? ? ? 56 LYS B CB 1 ATOM 1266 C CG . LYS B 2 56 ? 25.160 77.072 -57.720 1.00 32.82 ? ? ? ? ? ? 56 LYS B CG 1 ATOM 1267 C CD . LYS B 2 56 ? 26.585 76.462 -57.886 1.00 37.24 ? ? ? ? ? ? 56 LYS B CD 1 ATOM 1268 C CE . LYS B 2 56 ? 26.706 75.575 -59.119 1.00 35.70 ? ? ? ? ? ? 56 LYS B CE 1 ATOM 1269 N NZ . LYS B 2 56 ? 26.428 76.315 -60.371 1.00 35.95 ? ? ? ? ? ? 56 LYS B NZ 1 ATOM 1270 N N . LYS B 2 57 ? 24.428 75.645 -53.310 1.00 31.60 ? ? ? ? ? ? 57 LYS B N 1 ATOM 1271 C CA . LYS B 2 57 ? 24.639 75.634 -51.870 1.00 31.24 ? ? ? ? ? ? 57 LYS B CA 1 ATOM 1272 C C . LYS B 2 57 ? 25.322 74.360 -51.418 1.00 30.68 ? ? ? ? ? ? 57 LYS B C 1 ATOM 1273 O O . LYS B 2 57 ? 26.396 74.421 -50.916 1.00 28.36 ? ? ? ? ? ? 57 LYS B O 1 ATOM 1274 C CB . LYS B 2 57 ? 23.295 75.785 -51.152 1.00 31.97 ? ? ? ? ? ? 57 LYS B CB 1 ATOM 1275 C CG . LYS B 2 57 ? 22.915 77.245 -50.724 1.00 33.43 ? ? ? ? ? ? 57 LYS B CG 1 ATOM 1276 C CD . LYS B 2 57 ? 22.763 78.189 -51.967 1.00 38.46 ? ? ? ? ? ? 57 LYS B CD 1 ATOM 1277 C CE . LYS B 2 57 ? 21.830 79.384 -51.702 1.00 38.33 ? ? ? ? ? ? 57 LYS B CE 1 ATOM 1278 N NZ . LYS B 2 57 ? 20.614 78.991 -50.937 1.00 33.85 ? ? ? ? ? ? 57 LYS B NZ 1 ATOM 1279 N N . LEU B 2 58 ? 24.698 73.204 -51.613 1.00 31.37 ? ? ? ? ? ? 58 LEU B N 1 ATOM 1280 C CA . LEU B 2 58 ? 25.336 71.948 -51.168 1.00 31.93 ? ? ? ? ? ? 58 LEU B CA 1 ATOM 1281 C C . LEU B 2 58 ? 25.752 71.059 -52.354 1.00 31.95 ? ? ? ? ? ? 58 LEU B C 1 ATOM 1282 O O . LEU B 2 58 ? 26.643 71.387 -53.145 1.00 32.26 ? ? ? ? ? ? 58 LEU B O 1 ATOM 1283 C CB . LEU B 2 58 ? 24.392 71.172 -50.259 1.00 32.96 ? ? ? ? ? ? 58 LEU B CB 1 ATOM 1284 C CG . LEU B 2 58 ? 23.395 71.988 -49.404 1.00 32.02 ? ? ? ? ? ? 58 LEU B CG 1 ATOM 1285 C CD1 . LEU B 2 58 ? 22.251 71.121 -48.917 1.00 36.53 ? ? ? ? ? ? 58 LEU B CD1 1 ATOM 1286 C CD2 . LEU B 2 58 ? 24.084 72.609 -48.210 1.00 34.80 ? ? ? ? ? ? 58 LEU B CD2 1 ATOM 1287 N N . LYS B 2 59 ? 25.098 69.921 -52.485 1.00 31.56 ? ? ? ? ? ? 59 LYS B N 1 ATOM 1288 C CA . LYS B 2 59 ? 25.498 68.925 -53.512 1.00 30.11 ? ? ? ? ? ? 59 LYS B CA 1 ATOM 1289 C C . LYS B 2 59 ? 24.412 67.847 -53.648 1.00 27.60 ? ? ? ? ? ? 59 LYS B C 1 ATOM 1290 O O . LYS B 2 59 ? 24.633 66.702 -54.165 1.00 25.06 ? ? ? ? ? ? 59 LYS B O 1 ATOM 1291 C CB . LYS B 2 59 ? 26.889 68.313 -53.230 1.00 30.42 ? ? ? ? ? ? 59 LYS B CB 1 ATOM 1292 C CG . LYS B 2 59 ? 27.120 67.821 -51.786 1.00 33.62 ? ? ? ? ? ? 59 LYS B CG 1 ATOM 1293 C CD . LYS B 2 59 ? 28.487 67.027 -51.655 1.00 32.10 ? ? ? ? ? ? 59 LYS B CD 1 ATOM 1294 C CE . LYS B 2 59 ? 28.596 66.317 -50.318 1.00 35.13 ? ? ? ? ? ? 59 LYS B CE 1 ATOM 1295 N NZ . LYS B 2 59 ? 29.742 65.287 -50.286 1.00 37.19 ? ? ? ? ? ? 59 LYS B NZ 1 ATOM 1296 N N . ASN B 2 60 ? 23.215 68.265 -53.235 1.00 25.43 ? ? ? ? ? ? 60 ASN B N 1 ATOM 1297 C CA . ASN B 2 60 ? 22.065 67.375 -53.182 1.00 25.07 ? ? ? ? ? ? 60 ASN B CA 1 ATOM 1298 C C . ASN B 2 60 ? 21.634 66.986 -54.603 1.00 23.02 ? ? ? ? ? ? 60 ASN B C 1 ATOM 1299 O O . ASN B 2 60 ? 21.571 65.851 -54.845 1.00 23.53 ? ? ? ? ? ? 60 ASN B O 1 ATOM 1300 C CB . ASN B 2 60 ? 20.943 67.975 -52.301 1.00 24.37 ? ? ? ? ? ? 60 ASN B CB 1 ATOM 1301 C CG . ASN B 2 60 ? 21.513 68.539 -51.004 1.00 29.91 ? ? ? ? ? ? 60 ASN B CG 1 ATOM 1302 O OD1 . ASN B 2 60 ? 22.355 67.865 -50.312 1.00 22.22 ? ? ? ? ? ? 60 ASN B OD1 1 ATOM 1303 N ND2 . ASN B 2 60 ? 21.158 69.825 -50.702 1.00 26.60 ? ? ? ? ? ? 60 ASN B ND2 1 ATOM 1304 N N . TYR B 2 61 ? 21.386 67.925 -55.539 1.00 22.28 ? ? ? ? ? ? 61 TYR B N 1 ATOM 1305 C CA . TYR B 2 61 ? 20.766 67.595 -56.850 1.00 21.25 ? ? ? ? ? ? 61 TYR B CA 1 ATOM 1306 C C . TYR B 2 61 ? 21.603 68.088 -57.992 1.00 19.95 ? ? ? ? ? ? 61 TYR B C 1 ATOM 1307 O O . TYR B 2 61 ? 22.388 68.957 -57.803 1.00 22.42 ? ? ? ? ? ? 61 TYR B O 1 ATOM 1308 C CB . TYR B 2 61 ? 19.317 68.143 -56.927 1.00 20.47 ? ? ? ? ? ? 61 TYR B CB 1 ATOM 1309 C CG . TYR B 2 61 ? 19.231 69.645 -56.725 1.00 22.50 ? ? ? ? ? ? 61 TYR B CG 1 ATOM 1310 C CD1 . TYR B 2 61 ? 19.603 70.503 -57.744 1.00 17.96 ? ? ? ? ? ? 61 TYR B CD1 1 ATOM 1311 C CD2 . TYR B 2 61 ? 18.819 70.185 -55.508 1.00 22.53 ? ? ? ? ? ? 61 TYR B CD2 1 ATOM 1312 C CE1 . TYR B 2 61 ? 19.552 71.866 -57.543 1.00 21.42 ? ? ? ? ? ? 61 TYR B CE1 1 ATOM 1313 C CE2 . TYR B 2 61 ? 18.791 71.524 -55.288 1.00 18.08 ? ? ? ? ? ? 61 TYR B CE2 1 ATOM 1314 C CZ . TYR B 2 61 ? 19.175 72.338 -56.311 1.00 18.98 ? ? ? ? ? ? 61 TYR B CZ 1 ATOM 1315 O OH . TYR B 2 61 ? 19.158 73.620 -56.151 1.00 23.27 ? ? ? ? ? ? 61 TYR B OH 1 ATOM 1316 N N . ASP B 2 62 ? 21.453 67.527 -59.165 1.00 18.98 ? ? ? ? ? ? 62 ASP B N 1 ATOM 1317 C CA . ASP B 2 62 ? 21.948 68.124 -60.410 1.00 18.61 ? ? ? ? ? ? 62 ASP B CA 1 ATOM 1318 C C . ASP B 2 62 ? 20.707 68.334 -61.325 1.00 17.80 ? ? ? ? ? ? 62 ASP B C 1 ATOM 1319 O O . ASP B 2 62 ? 20.795 68.945 -62.349 1.00 17.30 ? ? ? ? ? ? 62 ASP B O 1 ATOM 1320 C CB . ASP B 2 62 ? 22.852 67.123 -61.091 1.00 19.51 ? ? ? ? ? ? 62 ASP B CB 1 ATOM 1321 C CG . ASP B 2 62 ? 22.099 65.851 -61.414 1.00 18.23 ? ? ? ? ? ? 62 ASP B CG 1 ATOM 1322 O OD1 . ASP B 2 62 ? 22.010 64.964 -60.565 1.00 16.70 ? ? ? ? ? ? 62 ASP B OD1 1 ATOM 1323 O OD2 . ASP B 2 62 ? 21.558 65.780 -62.505 1.00 24.79 ? ? ? ? ? ? 62 ASP B OD2 1 ATOM 1324 N N . LYS B 2 63 ? 19.526 67.848 -60.930 1.00 18.24 ? ? ? ? ? ? 63 LYS B N 1 ATOM 1325 C CA . LYS B 2 63 ? 18.277 67.989 -61.726 1.00 17.27 ? ? ? ? ? ? 63 LYS B CA 1 ATOM 1326 C C . LYS B 2 63 ? 17.025 68.255 -60.877 1.00 16.44 ? ? ? ? ? ? 63 LYS B C 1 ATOM 1327 O O . LYS B 2 63 ? 17.022 68.000 -59.702 1.00 16.35 ? ? ? ? ? ? 63 LYS B O 1 ATOM 1328 C CB . LYS B 2 63 ? 18.004 66.723 -62.471 1.00 17.43 ? ? ? ? ? ? 63 LYS B CB 1 ATOM 1329 C CG . LYS B 2 63 ? 18.989 66.354 -63.557 1.00 18.56 ? ? ? ? ? ? 63 LYS B CG 1 ATOM 1330 C CD . LYS B 2 63 ? 18.273 65.328 -64.583 1.00 19.04 ? ? ? ? ? ? 63 LYS B CD 1 ATOM 1331 C CE . LYS B 2 63 ? 19.232 64.535 -65.499 1.00 22.68 ? ? ? ? ? ? 63 LYS B CE 1 ATOM 1332 N NZ . LYS B 2 63 ? 20.351 63.925 -64.725 1.00 20.82 ? ? ? ? ? ? 63 LYS B NZ 1 ATOM 1333 N N . VAL B 2 64 ? 15.956 68.762 -61.466 1.00 14.94 ? ? ? ? ? ? 64 VAL B N 1 ATOM 1334 C CA . VAL B 2 64 ? 14.918 69.428 -60.687 1.00 13.39 ? ? ? ? ? ? 64 VAL B CA 1 ATOM 1335 C C . VAL B 2 64 ? 13.690 69.204 -61.470 1.00 14.07 ? ? ? ? ? ? 64 VAL B C 1 ATOM 1336 O O . VAL B 2 64 ? 13.659 69.610 -62.662 1.00 13.58 ? ? ? ? ? ? 64 VAL B O 1 ATOM 1337 C CB . VAL B 2 64 ? 15.129 70.881 -60.563 1.00 13.23 ? ? ? ? ? ? 64 VAL B CB 1 ATOM 1338 C CG1 . VAL B 2 64 ? 14.106 71.459 -59.685 1.00 13.27 ? ? ? ? ? ? 64 VAL B CG1 1 ATOM 1339 C CG2 . VAL B 2 64 ? 16.539 71.163 -59.937 1.00 14.70 ? ? ? ? ? ? 64 VAL B CG2 1 ATOM 1340 N N . LYS B 2 65 ? 12.758 68.457 -60.862 1.00 11.22 ? ? ? ? ? ? 65 LYS B N 1 ATOM 1341 C CA . LYS B 2 65 ? 11.479 68.023 -61.513 1.00 10.59 ? ? ? ? ? ? 65 LYS B CA 1 ATOM 1342 C C . LYS B 2 65 ? 10.399 68.943 -61.018 1.00 9.34 ? ? ? ? ? ? 65 LYS B C 1 ATOM 1343 O O . LYS B 2 65 ? 10.124 68.893 -59.864 1.00 10.41 ? ? ? ? ? ? 65 LYS B O 1 ATOM 1344 C CB . LYS B 2 65 ? 11.075 66.669 -61.027 1.00 9.02 ? ? ? ? ? ? 65 LYS B CB 1 ATOM 1345 C CG . LYS B 2 65 ? 9.850 66.003 -61.721 1.00 12.54 ? ? ? ? ? ? 65 LYS B CG 1 ATOM 1346 C CD . LYS B 2 65 ? 9.549 64.629 -60.972 1.00 10.08 ? ? ? ? ? ? 65 LYS B CD 1 ATOM 1347 C CE . LYS B 2 65 ? 8.240 64.021 -61.369 1.00 15.90 ? ? ? ? ? ? 65 LYS B CE 1 ATOM 1348 N NZ . LYS B 2 65 ? 6.934 64.371 -60.782 1.00 11.30 ? ? ? ? ? ? 65 LYS B NZ 1 ATOM 1349 N N . THR B 2 66 ? 9.829 69.785 -61.846 1.00 5.88 ? ? ? ? ? ? 66 THR B N 1 ATOM 1350 C CA . THR B 2 66 ? 8.816 70.634 -61.359 1.00 7.32 ? ? ? ? ? ? 66 THR B CA 1 ATOM 1351 C C . THR B 2 66 ? 7.519 70.173 -61.946 1.00 6.50 ? ? ? ? ? ? 66 THR B C 1 ATOM 1352 O O . THR B 2 66 ? 7.553 69.747 -63.109 1.00 7.78 ? ? ? ? ? ? 66 THR B O 1 ATOM 1353 C CB . THR B 2 66 ? 8.992 72.105 -61.878 1.00 7.09 ? ? ? ? ? ? 66 THR B CB 1 ATOM 1354 O OG1 . THR B 2 66 ? 7.855 72.831 -61.412 1.00 8.11 ? ? ? ? ? ? 66 THR B OG1 1 ATOM 1355 C CG2 . THR B 2 66 ? 8.875 72.163 -63.350 1.00 2.38 ? ? ? ? ? ? 66 THR B CG2 1 ATOM 1356 N N . GLU B 2 67 ? 6.431 70.214 -61.200 1.00 4.69 ? ? ? ? ? ? 67 GLU B N 1 ATOM 1357 C CA . GLU B 2 67 ? 5.170 69.577 -61.684 1.00 7.90 ? ? ? ? ? ? 67 GLU B CA 1 ATOM 1358 C C . GLU B 2 67 ? 4.184 70.675 -61.809 1.00 7.23 ? ? ? ? ? ? 67 GLU B C 1 ATOM 1359 O O . GLU B 2 67 ? 4.206 71.534 -60.958 1.00 10.86 ? ? ? ? ? ? 67 GLU B O 1 ATOM 1360 C CB . GLU B 2 67 ? 4.580 68.526 -60.696 1.00 7.73 ? ? ? ? ? ? 67 GLU B CB 1 ATOM 1361 C CG . GLU B 2 67 ? 5.458 67.338 -60.426 1.00 8.95 ? ? ? ? ? ? 67 GLU B CG 1 ATOM 1362 C CD . GLU B 2 67 ? 4.690 66.177 -59.888 1.00 11.55 ? ? ? ? ? ? 67 GLU B CD 1 ATOM 1363 O OE1 . GLU B 2 67 ? 4.324 66.244 -58.729 1.00 16.77 ? ? ? ? ? ? 67 GLU B OE1 1 ATOM 1364 O OE2 . GLU B 2 67 ? 4.470 65.142 -60.591 1.00 16.26 ? ? ? ? ? ? 67 GLU B OE2 1 ATOM 1365 N N . LEU B 2 68 ? 3.365 70.693 -62.850 1.00 8.84 ? ? ? ? ? ? 68 LEU B N 1 ATOM 1366 C CA . LEU B 2 68 ? 2.462 71.833 -63.143 1.00 9.86 ? ? ? ? ? ? 68 LEU B CA 1 ATOM 1367 C C . LEU B 2 68 ? 1.027 71.385 -62.992 1.00 10.53 ? ? ? ? ? ? 68 LEU B C 1 ATOM 1368 O O . LEU B 2 68 ? 0.791 70.184 -62.825 1.00 10.30 ? ? ? ? ? ? 68 LEU B O 1 ATOM 1369 C CB . LEU B 2 68 ? 2.716 72.295 -64.551 1.00 9.24 ? ? ? ? ? ? 68 LEU B CB 1 ATOM 1370 C CG . LEU B 2 68 ? 4.027 73.070 -64.676 1.00 7.01 ? ? ? ? ? ? 68 LEU B CG 1 ATOM 1371 C CD1 . LEU B 2 68 ? 5.248 72.234 -64.901 1.00 17.00 ? ? ? ? ? ? 68 LEU B CD1 1 ATOM 1372 C CD2 . LEU B 2 68 ? 4.025 74.132 -65.788 1.00 14.31 ? ? ? ? ? ? 68 LEU B CD2 1 ATOM 1373 N N . LEU B 2 69 ? 0.099 72.328 -63.029 1.00 11.18 ? ? ? ? ? ? 69 LEU B N 1 ATOM 1374 C CA . LEU B 2 69 ? -1.315 72.050 -62.810 1.00 11.28 ? ? ? ? ? ? 69 LEU B CA 1 ATOM 1375 C C . LEU B 2 69 ? -1.819 70.892 -63.672 1.00 10.82 ? ? ? ? ? ? 69 LEU B C 1 ATOM 1376 O O . LEU B 2 69 ? -2.476 69.979 -63.156 1.00 8.92 ? ? ? ? ? ? 69 LEU B O 1 ATOM 1377 C CB . LEU B 2 69 ? -2.130 73.341 -62.923 1.00 12.67 ? ? ? ? ? ? 69 LEU B CB 1 ATOM 1378 C CG . LEU B 2 69 ? -3.627 73.149 -62.920 1.00 15.85 ? ? ? ? ? ? 69 LEU B CG 1 ATOM 1379 C CD1 . LEU B 2 69 ? -4.010 72.221 -61.839 1.00 18.69 ? ? ? ? ? ? 69 LEU B CD1 1 ATOM 1380 C CD2 . LEU B 2 69 ? -4.286 74.471 -62.738 1.00 17.52 ? ? ? ? ? ? 69 LEU B CD2 1 ATOM 1381 N N . ASN B 2 70 ? -1.508 70.919 -64.968 1.00 9.53 ? ? ? ? ? ? 70 ASN B N 1 ATOM 1382 C CA . ASN B 2 70 ? -2.003 69.907 -65.903 1.00 9.06 ? ? ? ? ? ? 70 ASN B CA 1 ATOM 1383 C C . ASN B 2 70 ? -1.073 69.825 -67.089 1.00 9.38 ? ? ? ? ? ? 70 ASN B C 1 ATOM 1384 O O . ASN B 2 70 ? -0.050 70.521 -67.152 1.00 10.04 ? ? ? ? ? ? 70 ASN B O 1 ATOM 1385 C CB . ASN B 2 70 ? -3.409 70.182 -66.411 1.00 6.28 ? ? ? ? ? ? 70 ASN B CB 1 ATOM 1386 C CG . ASN B 2 70 ? -3.501 71.506 -66.983 1.00 13.91 ? ? ? ? ? ? 70 ASN B CG 1 ATOM 1387 O OD1 . ASN B 2 70 ? -2.579 71.916 -67.741 1.00 16.29 ? ? ? ? ? ? 70 ASN B OD1 1 ATOM 1388 N ND2 . ASN B 2 70 ? -4.504 72.305 -66.529 1.00 11.11 ? ? ? ? ? ? 70 ASN B ND2 1 ATOM 1389 N N . GLU B 2 71 ? -1.424 68.960 -68.016 1.00 7.89 ? ? ? ? ? ? 71 GLU B N 1 ATOM 1390 C CA . GLU B 2 71 ? -0.676 68.737 -69.198 1.00 7.99 ? ? ? ? ? ? 71 GLU B CA 1 ATOM 1391 C C . GLU B 2 71 ? -0.468 69.933 -70.108 1.00 9.63 ? ? ? ? ? ? 71 GLU B C 1 ATOM 1392 O O . GLU B 2 71 ? 0.627 70.112 -70.552 1.00 8.93 ? ? ? ? ? ? 71 GLU B O 1 ATOM 1393 C CB . GLU B 2 71 ? -1.268 67.546 -69.978 1.00 7.88 ? ? ? ? ? ? 71 GLU B CB 1 ATOM 1394 C CG . GLU B 2 71 ? -0.765 67.327 -71.345 1.00 8.94 ? ? ? ? ? ? 71 GLU B CG 1 ATOM 1395 C CD . GLU B 2 71 ? -1.738 66.502 -72.194 1.00 19.55 ? ? ? ? ? ? 71 GLU B CD 1 ATOM 1396 O OE1 . GLU B 2 71 ? -2.182 65.417 -71.711 1.00 21.09 ? ? ? ? ? ? 71 GLU B OE1 1 ATOM 1397 O OE2 . GLU B 2 71 ? -2.064 66.942 -73.327 1.00 22.55 ? ? ? ? ? ? 71 GLU B OE2 1 ATOM 1398 N N . ASP B 2 72 ? -1.517 70.679 -70.516 1.00 14.68 ? ? ? ? ? ? 72 ASP B N 1 ATOM 1399 C CA . ASP B 2 72 ? -1.301 71.873 -71.390 1.00 13.93 ? ? ? ? ? ? 72 ASP B CA 1 ATOM 1400 C C . ASP B 2 72 ? -0.493 72.928 -70.793 1.00 14.66 ? ? ? ? ? ? 72 ASP B C 1 ATOM 1401 O O . ASP B 2 72 ? 0.170 73.716 -71.506 1.00 17.22 ? ? ? ? ? ? 72 ASP B O 1 ATOM 1402 C CB . ASP B 2 72 ? -2.611 72.412 -71.915 1.00 17.39 ? ? ? ? ? ? 72 ASP B CB 1 ATOM 1403 C CG . ASP B 2 72 ? -3.429 71.314 -72.501 1.00 19.78 ? ? ? ? ? ? 72 ASP B CG 1 ATOM 1404 O OD1 . ASP B 2 72 ? -2.947 70.643 -73.464 1.00 21.01 ? ? ? ? ? ? 72 ASP B OD1 1 ATOM 1405 O OD2 . ASP B 2 72 ? -4.467 71.078 -71.921 1.00 18.49 ? ? ? ? ? ? 72 ASP B OD2 1 ATOM 1406 N N . LEU B 2 73 ? -0.450 72.988 -69.489 1.00 15.50 ? ? ? ? ? ? 73 LEU B N 1 ATOM 1407 C CA . LEU B 2 73 ? 0.356 74.077 -68.854 1.00 16.88 ? ? ? ? ? ? 73 LEU B CA 1 ATOM 1408 C C . LEU B 2 73 ? 1.795 73.598 -68.994 1.00 17.13 ? ? ? ? ? ? 73 LEU B C 1 ATOM 1409 O O . LEU B 2 73 ? 2.713 74.421 -68.993 1.00 14.55 ? ? ? ? ? ? 73 LEU B O 1 ATOM 1410 C CB . LEU B 2 73 ? 0.041 74.280 -67.349 1.00 15.61 ? ? ? ? ? ? 73 LEU B CB 1 ATOM 1411 C CG . LEU B 2 73 ? 0.738 75.289 -66.451 1.00 14.47 ? ? ? ? ? ? 73 LEU B CG 1 ATOM 1412 C CD1 . LEU B 2 73 ? 0.660 76.606 -67.087 1.00 15.56 ? ? ? ? ? ? 73 LEU B CD1 1 ATOM 1413 C CD2 . LEU B 2 73 ? -0.027 75.293 -65.170 1.00 12.77 ? ? ? ? ? ? 73 LEU B CD2 1 ATOM 1414 N N . ALA B 2 74 ? 1.958 72.262 -69.083 1.00 17.65 ? ? ? ? ? ? 74 ALA B N 1 ATOM 1415 C CA . ALA B 2 74 ? 3.328 71.583 -69.197 1.00 18.93 ? ? ? ? ? ? 74 ALA B CA 1 ATOM 1416 C C . ALA B 2 74 ? 3.979 72.020 -70.515 1.00 17.88 ? ? ? ? ? ? 74 ALA B C 1 ATOM 1417 O O . ALA B 2 74 ? 5.065 72.519 -70.526 1.00 19.26 ? ? ? ? ? ? 74 ALA B O 1 ATOM 1418 C CB . ALA B 2 74 ? 3.180 70.088 -69.191 1.00 17.35 ? ? ? ? ? ? 74 ALA B CB 1 ATOM 1419 N N . LYS B 2 75 ? 3.242 71.878 -71.613 1.00 16.67 ? ? ? ? ? ? 75 LYS B N 1 ATOM 1420 C CA . LYS B 2 75 ? 3.692 72.225 -72.929 1.00 14.00 ? ? ? ? ? ? 75 LYS B CA 1 ATOM 1421 C C . LYS B 2 75 ? 3.926 73.707 -73.032 1.00 14.30 ? ? ? ? ? ? 75 LYS B C 1 ATOM 1422 O O . LYS B 2 75 ? 5.026 74.104 -73.441 1.00 15.59 ? ? ? ? ? ? 75 LYS B O 1 ATOM 1423 C CB . LYS B 2 75 ? 2.679 71.749 -73.934 1.00 14.96 ? ? ? ? ? ? 75 LYS B CB 1 ATOM 1424 C CG . LYS B 2 75 ? 1.968 70.381 -73.562 1.00 14.40 ? ? ? ? ? ? 75 LYS B CG 1 ATOM 1425 C CD . LYS B 2 75 ? 2.272 69.253 -74.608 1.00 12.43 ? ? ? ? ? ? 75 LYS B CD 1 ATOM 1426 C CE . LYS B 2 75 ? 1.170 68.249 -74.842 1.00 15.68 ? ? ? ? ? ? 75 LYS B CE 1 ATOM 1427 N NZ . LYS B 2 75 ? -0.199 68.762 -75.093 1.00 13.37 ? ? ? ? ? ? 75 LYS B NZ 1 ATOM 1428 N N . LYS B 2 76 ? 2.984 74.553 -72.617 1.00 12.03 ? ? ? ? ? ? 76 LYS B N 1 ATOM 1429 C CA . LYS B 2 76 ? 3.311 75.984 -72.654 1.00 10.80 ? ? ? ? ? ? 76 LYS B CA 1 ATOM 1430 C C . LYS B 2 76 ? 4.841 76.225 -72.391 1.00 10.78 ? ? ? ? ? ? 76 LYS B C 1 ATOM 1431 O O . LYS B 2 76 ? 5.448 77.124 -72.943 1.00 9.45 ? ? ? ? ? ? 76 LYS B O 1 ATOM 1432 C CB . LYS B 2 76 ? 2.462 76.752 -71.698 1.00 8.57 ? ? ? ? ? ? 76 LYS B CB 1 ATOM 1433 C CG . LYS B 2 76 ? 2.749 78.209 -71.763 1.00 8.38 ? ? ? ? ? ? 76 LYS B CG 1 ATOM 1434 C CD . LYS B 2 76 ? 1.966 78.906 -70.687 1.00 4.09 ? ? ? ? ? ? 76 LYS B CD 1 ATOM 1435 C CE . LYS B 2 76 ? 2.484 80.347 -70.386 1.00 2.00 ? ? ? ? ? ? 76 LYS B CE 1 ATOM 1436 N NZ . LYS B 2 76 ? 1.287 81.228 -69.885 1.00 6.42 ? ? ? ? ? ? 76 LYS B NZ 1 ATOM 1437 N N . TYR B 2 77 ? 5.491 75.393 -71.582 1.00 10.61 ? ? ? ? ? ? 77 TYR B N 1 ATOM 1438 C CA . TYR B 2 77 ? 6.872 75.670 -71.324 1.00 12.40 ? ? ? ? ? ? 77 TYR B CA 1 ATOM 1439 C C . TYR B 2 77 ? 7.830 74.629 -71.793 1.00 12.88 ? ? ? ? ? ? 77 TYR B C 1 ATOM 1440 O O . TYR B 2 77 ? 9.057 74.842 -71.636 1.00 11.52 ? ? ? ? ? ? 77 TYR B O 1 ATOM 1441 C CB . TYR B 2 77 ? 7.130 75.839 -69.871 1.00 12.86 ? ? ? ? ? ? 77 TYR B CB 1 ATOM 1442 C CG . TYR B 2 77 ? 6.508 77.058 -69.301 1.00 15.12 ? ? ? ? ? ? 77 TYR B CG 1 ATOM 1443 C CD1 . TYR B 2 77 ? 5.163 77.019 -68.837 1.00 14.99 ? ? ? ? ? ? 77 TYR B CD1 1 ATOM 1444 C CD2 . TYR B 2 77 ? 7.157 78.239 -69.376 1.00 6.11 ? ? ? ? ? ? 77 TYR B CD2 1 ATOM 1445 C CE1 . TYR B 2 77 ? 4.582 78.144 -68.372 1.00 18.57 ? ? ? ? ? ? 77 TYR B CE1 1 ATOM 1446 C CE2 . TYR B 2 77 ? 6.584 79.388 -68.847 1.00 16.06 ? ? ? ? ? ? 77 TYR B CE2 1 ATOM 1447 C CZ . TYR B 2 77 ? 5.311 79.335 -68.345 1.00 7.39 ? ? ? ? ? ? 77 TYR B CZ 1 ATOM 1448 O OH . TYR B 2 77 ? 4.699 80.458 -67.889 1.00 14.02 ? ? ? ? ? ? 77 TYR B OH 1 ATOM 1449 N N . LYS B 2 78 ? 7.263 73.504 -72.250 1.00 14.19 ? ? ? ? ? ? 78 LYS B N 1 ATOM 1450 C CA . LYS B 2 78 ? 8.003 72.249 -72.535 1.00 15.10 ? ? ? ? ? ? 78 LYS B CA 1 ATOM 1451 C C . LYS B 2 78 ? 9.323 72.472 -73.139 1.00 15.39 ? ? ? ? ? ? 78 LYS B C 1 ATOM 1452 O O . LYS B 2 78 ? 10.278 71.866 -72.682 1.00 16.90 ? ? ? ? ? ? 78 LYS B O 1 ATOM 1453 C CB . LYS B 2 78 ? 7.264 71.344 -73.514 1.00 15.32 ? ? ? ? ? ? 78 LYS B CB 1 ATOM 1454 C CG . LYS B 2 78 ? 7.999 69.995 -73.797 1.00 11.68 ? ? ? ? ? ? 78 LYS B CG 1 ATOM 1455 C CD . LYS B 2 78 ? 7.232 69.281 -74.934 1.00 16.61 ? ? ? ? ? ? 78 LYS B CD 1 ATOM 1456 C CE . LYS B 2 78 ? 8.095 68.285 -75.666 1.00 20.76 ? ? ? ? ? ? 78 LYS B CE 1 ATOM 1457 N NZ . LYS B 2 78 ? 9.032 67.580 -74.703 1.00 11.20 ? ? ? ? ? ? 78 LYS B NZ 1 ATOM 1458 N N . ASP B 2 79 ? 9.423 73.322 -74.163 1.00 16.73 ? ? ? ? ? ? 79 ASP B N 1 ATOM 1459 C CA . ASP B 2 79 ? 10.788 73.702 -74.750 1.00 18.74 ? ? ? ? ? ? 79 ASP B CA 1 ATOM 1460 C C . ASP B 2 79 ? 11.135 75.217 -74.946 1.00 20.66 ? ? ? ? ? ? 79 ASP B C 1 ATOM 1461 O O . ASP B 2 79 ? 11.712 75.641 -76.009 1.00 20.48 ? ? ? ? ? ? 79 ASP B O 1 ATOM 1462 C CB . ASP B 2 79 ? 10.968 73.054 -76.098 1.00 18.72 ? ? ? ? ? ? 79 ASP B CB 1 ATOM 1463 C CG . ASP B 2 79 ? 9.662 72.840 -76.800 1.00 21.57 ? ? ? ? ? ? 79 ASP B CG 1 ATOM 1464 O OD1 . ASP B 2 79 ? 9.419 71.711 -77.346 1.00 25.37 ? ? ? ? ? ? 79 ASP B OD1 1 ATOM 1465 O OD2 . ASP B 2 79 ? 8.851 73.809 -76.783 1.00 24.82 ? ? ? ? ? ? 79 ASP B OD2 1 ATOM 1466 N N . GLU B 2 80 ? 10.863 76.019 -73.924 1.00 19.44 ? ? ? ? ? ? 80 GLU B N 1 ATOM 1467 C CA . GLU B 2 80 ? 11.144 77.436 -73.999 1.00 19.33 ? ? ? ? ? ? 80 GLU B CA 1 ATOM 1468 C C . GLU B 2 80 ? 12.226 77.796 -73.009 1.00 18.09 ? ? ? ? ? ? 80 GLU B C 1 ATOM 1469 O O . GLU B 2 80 ? 12.434 77.108 -72.022 1.00 16.55 ? ? ? ? ? ? 80 GLU B O 1 ATOM 1470 C CB . GLU B 2 80 ? 9.828 78.244 -73.719 1.00 20.36 ? ? ? ? ? ? 80 GLU B CB 1 ATOM 1471 C CG . GLU B 2 80 ? 8.704 78.003 -74.707 1.00 21.54 ? ? ? ? ? ? 80 GLU B CG 1 ATOM 1472 C CD . GLU B 2 80 ? 9.206 78.011 -76.179 1.00 30.53 ? ? ? ? ? ? 80 GLU B CD 1 ATOM 1473 O OE1 . GLU B 2 80 ? 9.469 79.116 -76.782 1.00 31.76 ? ? ? ? ? ? 80 GLU B OE1 1 ATOM 1474 O OE2 . GLU B 2 80 ? 9.326 76.886 -76.746 1.00 31.31 ? ? ? ? ? ? 80 GLU B OE2 1 ATOM 1475 N N . VAL B 2 81 ? 12.878 78.937 -73.238 1.00 17.57 ? ? ? ? ? ? 81 VAL B N 1 ATOM 1476 C CA . VAL B 2 81 ? 13.940 79.359 -72.343 1.00 16.47 ? ? ? ? ? ? 81 VAL B CA 1 ATOM 1477 C C . VAL B 2 81 ? 13.323 80.074 -71.207 1.00 15.80 ? ? ? ? ? ? 81 VAL B C 1 ATOM 1478 O O . VAL B 2 81 ? 12.771 81.152 -71.433 1.00 16.92 ? ? ? ? ? ? 81 VAL B O 1 ATOM 1479 C CB . VAL B 2 81 ? 15.086 80.195 -73.045 1.00 17.46 ? ? ? ? ? ? 81 VAL B CB 1 ATOM 1480 C CG1 . VAL B 2 81 ? 16.185 80.500 -72.069 1.00 13.61 ? ? ? ? ? ? 81 VAL B CG1 1 ATOM 1481 C CG2 . VAL B 2 81 ? 15.671 79.426 -74.271 1.00 17.65 ? ? ? ? ? ? 81 VAL B CG2 1 ATOM 1482 N N . VAL B 2 82 ? 13.346 79.476 -69.990 1.00 14.23 ? ? ? ? ? ? 82 VAL B N 1 ATOM 1483 C CA . VAL B 2 82 ? 12.610 80.098 -68.904 1.00 13.60 ? ? ? ? ? ? 82 VAL B CA 1 ATOM 1484 C C . VAL B 2 82 ? 13.534 80.375 -67.765 1.00 12.40 ? ? ? ? ? ? 82 VAL B C 1 ATOM 1485 O O . VAL B 2 82 ? 14.676 79.967 -67.895 1.00 14.07 ? ? ? ? ? ? 82 VAL B O 1 ATOM 1486 C CB . VAL B 2 82 ? 11.490 79.249 -68.382 1.00 12.61 ? ? ? ? ? ? 82 VAL B CB 1 ATOM 1487 C CG1 . VAL B 2 82 ? 10.354 79.315 -69.282 1.00 10.09 ? ? ? ? ? ? 82 VAL B CG1 1 ATOM 1488 C CG2 . VAL B 2 82 ? 11.999 77.805 -68.150 1.00 11.70 ? ? ? ? ? ? 82 VAL B CG2 1 ATOM 1489 N N . ASP B 2 83 ? 13.039 81.043 -66.689 1.00 10.60 ? ? ? ? ? ? 83 ASP B N 1 ATOM 1490 C CA . ASP B 2 83 ? 13.762 81.172 -65.403 1.00 11.28 ? ? ? ? ? ? 83 ASP B CA 1 ATOM 1491 C C . ASP B 2 83 ? 13.062 80.297 -64.387 1.00 9.47 ? ? ? ? ? ? 83 ASP B C 1 ATOM 1492 O O . ASP B 2 83 ? 11.936 79.906 -64.585 1.00 9.22 ? ? ? ? ? ? 83 ASP B O 1 ATOM 1493 C CB . ASP B 2 83 ? 13.768 82.602 -64.944 1.00 9.92 ? ? ? ? ? ? 83 ASP B CB 1 ATOM 1494 C CG . ASP B 2 83 ? 14.390 83.537 -65.985 1.00 11.34 ? ? ? ? ? ? 83 ASP B CG 1 ATOM 1495 O OD1 . ASP B 2 83 ? 15.623 83.444 -66.297 1.00 17.16 ? ? ? ? ? ? 83 ASP B OD1 1 ATOM 1496 O OD2 . ASP B 2 83 ? 13.664 84.379 -66.431 1.00 6.06 ? ? ? ? ? ? 83 ASP B OD2 1 ATOM 1497 N N . VAL B 2 84 ? 13.691 80.060 -63.267 1.00 8.77 ? ? ? ? ? ? 84 VAL B N 1 ATOM 1498 C CA . VAL B 2 84 ? 13.023 79.298 -62.188 1.00 10.37 ? ? ? ? ? ? 84 VAL B CA 1 ATOM 1499 C C . VAL B 2 84 ? 13.117 79.876 -60.767 1.00 11.30 ? ? ? ? ? ? 84 VAL B C 1 ATOM 1500 O O . VAL B 2 84 ? 14.126 80.482 -60.456 1.00 13.92 ? ? ? ? ? ? 84 VAL B O 1 ATOM 1501 C CB . VAL B 2 84 ? 13.628 77.883 -62.165 1.00 10.76 ? ? ? ? ? ? 84 VAL B CB 1 ATOM 1502 C CG1 . VAL B 2 84 ? 12.884 77.064 -61.176 1.00 5.69 ? ? ? ? ? ? 84 VAL B CG1 1 ATOM 1503 C CG2 . VAL B 2 84 ? 13.564 77.266 -63.594 1.00 4.66 ? ? ? ? ? ? 84 VAL B CG2 1 ATOM 1504 N N . TYR B 2 85 ? 12.108 79.666 -59.896 1.00 8.83 ? ? ? ? ? ? 85 TYR B N 1 ATOM 1505 C CA . TYR B 2 85 ? 12.136 80.156 -58.546 1.00 9.12 ? ? ? ? ? ? 85 TYR B CA 1 ATOM 1506 C C . TYR B 2 85 ? 11.096 79.343 -57.815 1.00 10.75 ? ? ? ? ? ? 85 TYR B C 1 ATOM 1507 O O . TYR B 2 85 ? 9.841 79.621 -57.969 1.00 10.81 ? ? ? ? ? ? 85 TYR B O 1 ATOM 1508 C CB . TYR B 2 85 ? 11.767 81.683 -58.387 1.00 11.31 ? ? ? ? ? ? 85 TYR B CB 1 ATOM 1509 C CG . TYR B 2 85 ? 12.501 82.121 -57.168 1.00 9.98 ? ? ? ? ? ? 85 TYR B CG 1 ATOM 1510 C CD1 . TYR B 2 85 ? 13.853 82.362 -57.238 1.00 8.95 ? ? ? ? ? ? 85 TYR B CD1 1 ATOM 1511 C CD2 . TYR B 2 85 ? 11.896 82.151 -55.943 1.00 5.62 ? ? ? ? ? ? 85 TYR B CD2 1 ATOM 1512 C CE1 . TYR B 2 85 ? 14.571 82.620 -56.105 1.00 9.81 ? ? ? ? ? ? 85 TYR B CE1 1 ATOM 1513 C CE2 . TYR B 2 85 ? 12.609 82.444 -54.793 1.00 5.27 ? ? ? ? ? ? 85 TYR B CE2 1 ATOM 1514 C CZ . TYR B 2 85 ? 13.965 82.664 -54.887 1.00 10.35 ? ? ? ? ? ? 85 TYR B CZ 1 ATOM 1515 O OH . TYR B 2 85 ? 14.728 83.004 -53.767 1.00 11.66 ? ? ? ? ? ? 85 TYR B OH 1 ATOM 1516 N N . GLY B 2 86 ? 11.541 78.354 -57.052 1.00 7.23 ? ? ? ? ? ? 86 GLY B N 1 ATOM 1517 C CA . GLY B 2 86 ? 10.644 77.587 -56.266 1.00 7.38 ? ? ? ? ? ? 86 GLY B CA 1 ATOM 1518 C C . GLY B 2 86 ? 11.231 76.949 -55.037 1.00 6.94 ? ? ? ? ? ? 86 GLY B C 1 ATOM 1519 O O . GLY B 2 86 ? 12.435 76.891 -54.965 1.00 8.25 ? ? ? ? ? ? 86 GLY B O 1 ATOM 1520 N N . SER B 2 87 ? 10.382 76.472 -54.097 1.00 7.72 ? ? ? ? ? ? 87 SER B N 1 ATOM 1521 C CA . SER B 2 87 ? 10.844 75.599 -52.995 1.00 8.44 ? ? ? ? ? ? 87 SER B CA 1 ATOM 1522 C C . SER B 2 87 ? 10.802 74.121 -53.322 1.00 8.90 ? ? ? ? ? ? 87 SER B C 1 ATOM 1523 O O . SER B 2 87 ? 9.713 73.546 -53.513 1.00 9.26 ? ? ? ? ? ? 87 SER B O 1 ATOM 1524 C CB . SER B 2 87 ? 9.983 75.747 -51.747 1.00 8.80 ? ? ? ? ? ? 87 SER B CB 1 ATOM 1525 O OG . SER B 2 87 ? 10.728 75.763 -50.525 1.00 7.70 ? ? ? ? ? ? 87 SER B OG 1 ATOM 1526 N N . ASN B 2 88 ? 11.982 73.491 -53.252 1.00 8.69 ? ? ? ? ? ? 88 ASN B N 1 ATOM 1527 C CA . ASN B 2 88 ? 12.165 72.144 -53.582 1.00 7.11 ? ? ? ? ? ? 88 ASN B CA 1 ATOM 1528 C C . ASN B 2 88 ? 12.002 71.279 -52.338 1.00 8.13 ? ? ? ? ? ? 88 ASN B C 1 ATOM 1529 O O . ASN B 2 88 ? 12.130 71.771 -51.217 1.00 4.36 ? ? ? ? ? ? 88 ASN B O 1 ATOM 1530 C CB . ASN B 2 88 ? 13.499 71.970 -54.194 1.00 7.12 ? ? ? ? ? ? 88 ASN B CB 1 ATOM 1531 C CG . ASN B 2 88 ? 14.642 72.413 -53.287 1.00 10.18 ? ? ? ? ? ? 88 ASN B CG 1 ATOM 1532 O OD1 . ASN B 2 88 ? 14.774 73.557 -53.002 1.00 11.23 ? ? ? ? ? ? 88 ASN B OD1 1 ATOM 1533 N ND2 . ASN B 2 88 ? 15.541 71.479 -52.920 1.00 14.47 ? ? ? ? ? ? 88 ASN B ND2 1 ATOM 1534 N N . TYR B 2 89 ? 11.690 69.987 -52.544 1.00 6.65 ? ? ? ? ? ? 89 TYR B N 1 ATOM 1535 C CA . TYR B 2 89 ? 11.737 69.031 -51.411 1.00 8.82 ? ? ? ? ? ? 89 TYR B CA 1 ATOM 1536 C C . TYR B 2 89 ? 12.318 67.674 -51.833 1.00 7.44 ? ? ? ? ? ? 89 TYR B C 1 ATOM 1537 O O . TYR B 2 89 ? 12.585 67.502 -52.994 1.00 11.07 ? ? ? ? ? ? 89 TYR B O 1 ATOM 1538 C CB . TYR B 2 89 ? 10.314 68.813 -50.904 1.00 8.27 ? ? ? ? ? ? 89 TYR B CB 1 ATOM 1539 C CG . TYR B 2 89 ? 9.512 68.177 -51.942 1.00 11.68 ? ? ? ? ? ? 89 TYR B CG 1 ATOM 1540 C CD1 . TYR B 2 89 ? 8.875 68.985 -52.869 1.00 15.37 ? ? ? ? ? ? 89 TYR B CD1 1 ATOM 1541 C CD2 . TYR B 2 89 ? 9.322 66.799 -51.994 1.00 12.69 ? ? ? ? ? ? 89 TYR B CD2 1 ATOM 1542 C CE1 . TYR B 2 89 ? 8.097 68.485 -53.860 1.00 17.48 ? ? ? ? ? ? 89 TYR B CE1 1 ATOM 1543 C CE2 . TYR B 2 89 ? 8.426 66.252 -52.973 1.00 17.91 ? ? ? ? ? ? 89 TYR B CE2 1 ATOM 1544 C CZ . TYR B 2 89 ? 7.807 67.121 -53.924 1.00 17.27 ? ? ? ? ? ? 89 TYR B CZ 1 ATOM 1545 O OH . TYR B 2 89 ? 6.978 66.738 -55.040 1.00 15.30 ? ? ? ? ? ? 89 TYR B OH 1 ATOM 1546 N N . TYR B 2 90 ? 12.379 66.694 -50.953 1.00 6.70 ? ? ? ? ? ? 90 TYR B N 1 ATOM 1547 C CA . TYR B 2 90 ? 12.874 65.401 -51.307 1.00 9.56 ? ? ? ? ? ? 90 TYR B CA 1 ATOM 1548 C C . TYR B 2 90 ? 11.972 64.287 -50.795 1.00 10.66 ? ? ? ? ? ? 90 TYR B C 1 ATOM 1549 O O . TYR B 2 90 ? 11.441 63.521 -51.556 1.00 9.30 ? ? ? ? ? ? 90 TYR B O 1 ATOM 1550 C CB . TYR B 2 90 ? 14.355 65.180 -50.866 1.00 11.84 ? ? ? ? ? ? 90 TYR B CB 1 ATOM 1551 C CG . TYR B 2 90 ? 15.304 66.388 -51.055 1.00 6.94 ? ? ? ? ? ? 90 TYR B CG 1 ATOM 1552 C CD1 . TYR B 2 90 ? 15.061 67.617 -50.466 1.00 11.94 ? ? ? ? ? ? 90 TYR B CD1 1 ATOM 1553 C CD2 . TYR B 2 90 ? 16.488 66.267 -51.848 1.00 13.00 ? ? ? ? ? ? 90 TYR B CD2 1 ATOM 1554 C CE1 . TYR B 2 90 ? 16.035 68.788 -50.710 1.00 13.14 ? ? ? ? ? ? 90 TYR B CE1 1 ATOM 1555 C CE2 . TYR B 2 90 ? 17.361 67.346 -52.107 1.00 6.85 ? ? ? ? ? ? 90 TYR B CE2 1 ATOM 1556 C CZ . TYR B 2 90 ? 17.158 68.564 -51.548 1.00 11.37 ? ? ? ? ? ? 90 TYR B CZ 1 ATOM 1557 O OH . TYR B 2 90 ? 18.112 69.535 -51.834 1.00 13.49 ? ? ? ? ? ? 90 TYR B OH 1 ATOM 1558 N N . VAL B 2 91 ? 11.758 64.193 -49.511 1.00 12.20 ? ? ? ? ? ? 91 VAL B N 1 ATOM 1559 C CA . VAL B 2 91 ? 10.935 63.129 -49.007 1.00 12.35 ? ? ? ? ? ? 91 VAL B CA 1 ATOM 1560 C C . VAL B 2 91 ? 9.624 63.043 -49.868 1.00 14.60 ? ? ? ? ? ? 91 VAL B C 1 ATOM 1561 O O . VAL B 2 91 ? 8.783 63.939 -49.828 1.00 15.23 ? ? ? ? ? ? 91 VAL B O 1 ATOM 1562 C CB . VAL B 2 91 ? 10.650 63.404 -47.531 1.00 11.92 ? ? ? ? ? ? 91 VAL B CB 1 ATOM 1563 C CG1 . VAL B 2 91 ? 9.584 62.436 -46.988 1.00 15.42 ? ? ? ? ? ? 91 VAL B CG1 1 ATOM 1564 C CG2 . VAL B 2 91 ? 11.821 63.307 -46.758 1.00 10.19 ? ? ? ? ? ? 91 VAL B CG2 1 ATOM 1565 N N . ASN B 2 92 ? 9.518 61.970 -50.668 1.00 17.21 ? ? ? ? ? ? 92 ASN B N 1 ATOM 1566 C CA . ASN B 2 92 ? 8.487 61.746 -51.714 1.00 19.48 ? ? ? ? ? ? 92 ASN B CA 1 ATOM 1567 C C . ASN B 2 92 ? 8.707 62.480 -53.062 1.00 18.45 ? ? ? ? ? ? 92 ASN B C 1 ATOM 1568 O O . ASN B 2 92 ? 7.691 62.951 -53.670 1.00 21.19 ? ? ? ? ? ? 92 ASN B O 1 ATOM 1569 C CB . ASN B 2 92 ? 7.082 62.037 -51.126 1.00 19.37 ? ? ? ? ? ? 92 ASN B CB 1 ATOM 1570 C CG . ASN B 2 92 ? 7.038 61.674 -49.672 1.00 22.66 ? ? ? ? ? ? 92 ASN B CG 1 ATOM 1571 O OD1 . ASN B 2 92 ? 7.620 60.637 -49.265 1.00 20.81 ? ? ? ? ? ? 92 ASN B OD1 1 ATOM 1572 N ND2 . ASN B 2 92 ? 6.391 62.518 -48.864 1.00 18.75 ? ? ? ? ? ? 92 ASN B ND2 1 ATOM 1573 N N . CYS B 2 93 ? 9.980 62.605 -53.491 1.00 15.78 ? ? ? ? ? ? 93 CYS B N 1 ATOM 1574 C CA . CYS B 2 93 ? 10.367 63.139 -54.805 1.00 13.75 ? ? ? ? ? ? 93 CYS B CA 1 ATOM 1575 C C . CYS B 2 93 ? 10.644 61.980 -55.647 1.00 13.70 ? ? ? ? ? ? 93 CYS B C 1 ATOM 1576 O O . CYS B 2 93 ? 11.751 61.344 -55.527 1.00 10.79 ? ? ? ? ? ? 93 CYS B O 1 ATOM 1577 C CB . CYS B 2 93 ? 11.636 63.954 -54.782 1.00 13.51 ? ? ? ? ? ? 93 CYS B CB 1 ATOM 1578 S SG . CYS B 2 93 ? 11.861 64.897 -56.272 1.00 14.61 ? ? ? ? ? ? 93 CYS B SG 1 ATOM 1579 N N . TYR B 2 94 ? 9.653 61.678 -56.486 1.00 13.67 ? ? ? ? ? ? 94 TYR B N 1 ATOM 1580 C CA . TYR B 2 94 ? 9.621 60.421 -57.328 1.00 15.69 ? ? ? ? ? ? 94 TYR B CA 1 ATOM 1581 C C . TYR B 2 94 ? 9.675 60.669 -58.829 1.00 15.27 ? ? ? ? ? ? 94 TYR B C 1 ATOM 1582 O O . TYR B 2 94 ? 9.286 61.762 -59.331 1.00 19.56 ? ? ? ? ? ? 94 TYR B O 1 ATOM 1583 C CB . TYR B 2 94 ? 8.305 59.659 -57.057 1.00 15.20 ? ? ? ? ? ? 94 TYR B CB 1 ATOM 1584 C CG . TYR B 2 94 ? 7.031 60.478 -57.059 1.00 18.01 ? ? ? ? ? ? 94 TYR B CG 1 ATOM 1585 C CD1 . TYR B 2 94 ? 7.022 61.873 -56.649 1.00 15.82 ? ? ? ? ? ? 94 TYR B CD1 1 ATOM 1586 C CD2 . TYR B 2 94 ? 5.785 59.875 -57.383 1.00 23.47 ? ? ? ? ? ? 94 TYR B CD2 1 ATOM 1587 C CE1 . TYR B 2 94 ? 5.877 62.615 -56.650 1.00 17.23 ? ? ? ? ? ? 94 TYR B CE1 1 ATOM 1588 C CE2 . TYR B 2 94 ? 4.621 60.606 -57.388 1.00 19.56 ? ? ? ? ? ? 94 TYR B CE2 1 ATOM 1589 C CZ . TYR B 2 94 ? 4.679 62.004 -56.987 1.00 19.32 ? ? ? ? ? ? 94 TYR B CZ 1 ATOM 1590 O OH . TYR B 2 94 ? 3.547 62.769 -56.927 1.00 17.22 ? ? ? ? ? ? 94 TYR B OH 1 ATOM 1591 N N . PHE B 2 95 ? 9.970 59.607 -59.527 1.00 17.97 ? ? ? ? ? ? 95 PHE B N 1 ATOM 1592 C CA . PHE B 2 95 ? 10.083 59.509 -60.982 1.00 19.11 ? ? ? ? ? ? 95 PHE B CA 1 ATOM 1593 C C . PHE B 2 95 ? 9.652 58.228 -61.591 1.00 21.85 ? ? ? ? ? ? 95 PHE B C 1 ATOM 1594 O O . PHE B 2 95 ? 10.132 57.878 -62.688 1.00 22.70 ? ? ? ? ? ? 95 PHE B O 1 ATOM 1595 C CB . PHE B 2 95 ? 11.560 59.673 -61.375 1.00 17.11 ? ? ? ? ? ? 95 PHE B CB 1 ATOM 1596 C CG . PHE B 2 95 ? 12.114 61.023 -61.058 1.00 14.83 ? ? ? ? ? ? 95 PHE B CG 1 ATOM 1597 C CD1 . PHE B 2 95 ? 12.667 61.299 -59.805 1.00 13.75 ? ? ? ? ? ? 95 PHE B CD1 1 ATOM 1598 C CD2 . PHE B 2 95 ? 12.203 61.974 -62.026 1.00 14.84 ? ? ? ? ? ? 95 PHE B CD2 1 ATOM 1599 C CE1 . PHE B 2 95 ? 13.252 62.604 -59.528 1.00 8.51 ? ? ? ? ? ? 95 PHE B CE1 1 ATOM 1600 C CE2 . PHE B 2 95 ? 12.822 63.262 -61.725 1.00 12.52 ? ? ? ? ? ? 95 PHE B CE2 1 ATOM 1601 C CZ . PHE B 2 95 ? 13.338 63.488 -60.464 1.00 6.47 ? ? ? ? ? ? 95 PHE B CZ 1 ATOM 1602 N N . SER B 2 96 ? 8.810 57.482 -60.875 1.00 25.99 ? ? ? ? ? ? 96 SER B N 1 ATOM 1603 C CA . SER B 2 96 ? 8.347 56.176 -61.296 1.00 28.59 ? ? ? ? ? ? 96 SER B CA 1 ATOM 1604 C C . SER B 2 96 ? 7.024 55.902 -60.597 1.00 31.56 ? ? ? ? ? ? 96 SER B C 1 ATOM 1605 O O . SER B 2 96 ? 6.234 56.815 -60.366 1.00 33.73 ? ? ? ? ? ? 96 SER B O 1 ATOM 1606 C CB . SER B 2 96 ? 9.379 55.077 -60.951 1.00 29.62 ? ? ? ? ? ? 96 SER B CB 1 ATOM 1607 O OG . SER B 2 96 ? 9.536 54.957 -59.559 1.00 28.29 ? ? ? ? ? ? 96 SER B OG 1 ATOM 1608 N N . SER B 2 97 ? 6.788 54.675 -60.185 1.00 33.99 ? ? ? ? ? ? 97 SER B N 1 ATOM 1609 C CA . SER B 2 97 ? 5.468 54.366 -59.653 1.00 38.04 ? ? ? ? ? ? 97 SER B CA 1 ATOM 1610 C C . SER B 2 97 ? 5.525 54.185 -58.124 1.00 39.63 ? ? ? ? ? ? 97 SER B C 1 ATOM 1611 O O . SER B 2 97 ? 4.625 54.625 -57.400 1.00 40.35 ? ? ? ? ? ? 97 SER B O 1 ATOM 1612 C CB . SER B 2 97 ? 4.880 53.118 -60.369 1.00 37.97 ? ? ? ? ? ? 97 SER B CB 1 ATOM 1613 O OG . SER B 2 97 ? 5.813 52.017 -60.388 1.00 40.53 ? ? ? ? ? ? 97 SER B OG 1 ATOM 1614 N N . LYS B 2 98 ? 6.578 53.505 -57.648 1.00 41.07 ? ? ? ? ? ? 98 LYS B N 1 ATOM 1615 C CA . LYS B 2 98 ? 6.788 53.287 -56.228 1.00 41.19 ? ? ? ? ? ? 98 LYS B CA 1 ATOM 1616 C C . LYS B 2 98 ? 6.946 54.657 -55.566 1.00 40.42 ? ? ? ? ? ? 98 LYS B C 1 ATOM 1617 O O . LYS B 2 98 ? 7.752 55.497 -56.014 1.00 40.75 ? ? ? ? ? ? 98 LYS B O 1 ATOM 1618 C CB . LYS B 2 98 ? 8.019 52.418 -55.969 1.00 41.81 ? ? ? ? ? ? 98 LYS B CB 1 ATOM 1619 C CG . LYS B 2 98 ? 8.231 52.130 -54.448 1.00 46.39 ? ? ? ? ? ? 98 LYS B CG 1 ATOM 1620 C CD . LYS B 2 98 ? 8.799 50.694 -54.215 1.00 47.24 ? ? ? ? ? ? 98 LYS B CD 1 ATOM 1621 C CE . LYS B 2 98 ? 9.540 50.525 -52.875 1.00 44.71 ? ? ? ? ? ? 98 LYS B CE 1 ATOM 1622 N NZ . LYS B 2 98 ? 10.104 49.134 -52.858 1.00 43.05 ? ? ? ? ? ? 98 LYS B NZ 1 ATOM 1623 N N . ASP B 2 99 ? 6.189 54.810 -54.474 1.00 38.39 ? ? ? ? ? ? 99 ASP B N 1 ATOM 1624 C CA . ASP B 2 99 ? 5.901 56.066 -53.718 1.00 34.76 ? ? ? ? ? ? 99 ASP B CA 1 ATOM 1625 C C . ASP B 2 99 ? 7.036 56.611 -52.805 1.00 32.59 ? ? ? ? ? ? 99 ASP B C 1 ATOM 1626 O O . ASP B 2 99 ? 7.281 57.835 -52.828 1.00 31.60 ? ? ? ? ? ? 99 ASP B O 1 ATOM 1627 C CB . ASP B 2 99 ? 4.584 55.829 -52.926 1.00 34.67 ? ? ? ? ? ? 99 ASP B CB 1 ATOM 1628 C CG . ASP B 2 99 ? 4.399 54.356 -52.600 1.00 35.24 ? ? ? ? ? ? 99 ASP B CG 1 ATOM 1629 O OD1 . ASP B 2 99 ? 5.420 53.669 -52.353 1.00 32.71 ? ? ? ? ? ? 99 ASP B OD1 1 ATOM 1630 O OD2 . ASP B 2 99 ? 3.253 53.869 -52.686 1.00 40.51 ? ? ? ? ? ? 99 ASP B OD2 1 ATOM 1631 N N . ASN B 2 100 ? 7.685 55.702 -52.026 1.00 31.93 ? ? ? ? ? ? 100 ASN B N 1 ATOM 1632 C CA . ASN B 2 100 ? 8.939 55.992 -51.232 1.00 30.10 ? ? ? ? ? ? 100 ASN B CA 1 ATOM 1633 C C . ASN B 2 100 ? 10.162 55.208 -51.702 1.00 27.75 ? ? ? ? ? ? 100 ASN B C 1 ATOM 1634 O O . ASN B 2 100 ? 10.419 54.047 -51.296 1.00 26.05 ? ? ? ? ? ? 100 ASN B O 1 ATOM 1635 C CB . ASN B 2 100 ? 8.766 55.841 -49.718 1.00 30.15 ? ? ? ? ? ? 100 ASN B CB 1 ATOM 1636 C CG . ASN B 2 100 ? 9.343 57.037 -48.930 1.00 33.53 ? ? ? ? ? ? 100 ASN B CG 1 ATOM 1637 O OD1 . ASN B 2 100 ? 9.026 57.182 -47.760 1.00 37.67 ? ? ? ? ? ? 100 ASN B OD1 1 ATOM 1638 N ND2 . ASN B 2 100 ? 10.181 57.898 -49.571 1.00 36.67 ? ? ? ? ? ? 100 ASN B ND2 1 ATOM 1639 N N . VAL B 2 101 ? 10.896 55.889 -52.579 1.00 23.52 ? ? ? ? ? ? 101 VAL B N 1 ATOM 1640 C CA . VAL B 2 101 ? 12.030 55.317 -53.305 1.00 19.42 ? ? ? ? ? ? 101 VAL B CA 1 ATOM 1641 C C . VAL B 2 101 ? 13.074 56.460 -53.430 1.00 17.45 ? ? ? ? ? ? 101 VAL B C 1 ATOM 1642 O O . VAL B 2 101 ? 12.697 57.638 -53.560 1.00 17.04 ? ? ? ? ? ? 101 VAL B O 1 ATOM 1643 C CB . VAL B 2 101 ? 11.655 54.932 -54.680 1.00 19.06 ? ? ? ? ? ? 101 VAL B CB 1 ATOM 1644 C CG1 . VAL B 2 101 ? 12.769 55.233 -55.580 1.00 16.25 ? ? ? ? ? ? 101 VAL B CG1 1 ATOM 1645 C CG2 . VAL B 2 101 ? 11.246 53.482 -54.761 1.00 16.36 ? ? ? ? ? ? 101 VAL B CG2 1 ATOM 1646 N N . TRP B 2 102 ? 14.352 56.134 -53.434 1.00 13.17 ? ? ? ? ? ? 102 TRP B N 1 ATOM 1647 C CA . TRP B 2 102 ? 15.408 57.181 -53.580 1.00 11.54 ? ? ? ? ? ? 102 TRP B CA 1 ATOM 1648 C C . TRP B 2 102 ? 16.058 57.307 -55.003 1.00 13.46 ? ? ? ? ? ? 102 TRP B C 1 ATOM 1649 O O . TRP B 2 102 ? 15.952 56.363 -55.838 1.00 12.67 ? ? ? ? ? ? 102 TRP B O 1 ATOM 1650 C CB . TRP B 2 102 ? 16.497 57.028 -52.477 1.00 10.48 ? ? ? ? ? ? 102 TRP B CB 1 ATOM 1651 C CG . TRP B 2 102 ? 17.507 58.185 -52.433 1.00 5.07 ? ? ? ? ? ? 102 TRP B CG 1 ATOM 1652 C CD1 . TRP B 2 102 ? 17.217 59.462 -52.217 1.00 7.38 ? ? ? ? ? ? 102 TRP B CD1 1 ATOM 1653 C CD2 . TRP B 2 102 ? 18.941 58.100 -52.532 1.00 6.91 ? ? ? ? ? ? 102 TRP B CD2 1 ATOM 1654 N NE1 . TRP B 2 102 ? 18.339 60.232 -52.206 1.00 12.31 ? ? ? ? ? ? 102 TRP B NE1 1 ATOM 1655 C CE2 . TRP B 2 102 ? 19.437 59.423 -52.400 1.00 11.59 ? ? ? ? ? ? 102 TRP B CE2 1 ATOM 1656 C CE3 . TRP B 2 102 ? 19.844 57.047 -52.618 1.00 2.04 ? ? ? ? ? ? 102 TRP B CE3 1 ATOM 1657 C CZ2 . TRP B 2 102 ? 20.804 59.745 -52.437 1.00 9.18 ? ? ? ? ? ? 102 TRP B CZ2 1 ATOM 1658 C CZ3 . TRP B 2 102 ? 21.225 57.372 -52.720 1.00 12.39 ? ? ? ? ? ? 102 TRP B CZ3 1 ATOM 1659 C CH2 . TRP B 2 102 ? 21.678 58.744 -52.650 1.00 5.74 ? ? ? ? ? ? 102 TRP B CH2 1 ATOM 1660 N N . TRP B 2 103 ? 16.737 58.440 -55.275 1.00 10.67 ? ? ? ? ? ? 103 TRP B N 1 ATOM 1661 C CA . TRP B 2 103 ? 17.389 58.659 -56.531 1.00 11.92 ? ? ? ? ? ? 103 TRP B CA 1 ATOM 1662 C C . TRP B 2 103 ? 18.728 59.316 -56.402 1.00 12.65 ? ? ? ? ? ? 103 TRP B C 1 ATOM 1663 O O . TRP B 2 103 ? 19.762 58.621 -56.390 1.00 9.75 ? ? ? ? ? ? 103 TRP B O 1 ATOM 1664 C CB . TRP B 2 103 ? 16.594 59.594 -57.349 1.00 12.69 ? ? ? ? ? ? 103 TRP B CB 1 ATOM 1665 C CG . TRP B 2 103 ? 15.126 59.184 -57.268 1.00 16.33 ? ? ? ? ? ? 103 TRP B CG 1 ATOM 1666 C CD1 . TRP B 2 103 ? 14.267 59.483 -56.223 1.00 18.14 ? ? ? ? ? ? 103 TRP B CD1 1 ATOM 1667 C CD2 . TRP B 2 103 ? 14.374 58.378 -58.206 1.00 10.68 ? ? ? ? ? ? 103 TRP B CD2 1 ATOM 1668 N NE1 . TRP B 2 103 ? 12.989 58.940 -56.488 1.00 21.88 ? ? ? ? ? ? 103 TRP B NE1 1 ATOM 1669 C CE2 . TRP B 2 103 ? 13.016 58.269 -57.681 1.00 16.85 ? ? ? ? ? ? 103 TRP B CE2 1 ATOM 1670 C CE3 . TRP B 2 103 ? 14.674 57.779 -59.411 1.00 9.65 ? ? ? ? ? ? 103 TRP B CE3 1 ATOM 1671 C CZ2 . TRP B 2 103 ? 12.003 57.597 -58.327 1.00 5.83 ? ? ? ? ? ? 103 TRP B CZ2 1 ATOM 1672 C CZ3 . TRP B 2 103 ? 13.686 57.072 -60.073 1.00 14.50 ? ? ? ? ? ? 103 TRP B CZ3 1 ATOM 1673 C CH2 . TRP B 2 103 ? 12.327 56.970 -59.508 1.00 16.82 ? ? ? ? ? ? 103 TRP B CH2 1 ATOM 1674 N N . HIS B 2 104 ? 18.665 60.638 -56.254 1.00 12.02 ? ? ? ? ? ? 104 HIS B N 1 ATOM 1675 C CA . HIS B 2 104 ? 19.857 61.491 -56.132 1.00 16.75 ? ? ? ? ? ? 104 HIS B CA 1 ATOM 1676 C C . HIS B 2 104 ? 20.012 62.383 -57.314 1.00 16.77 ? ? ? ? ? ? 104 HIS B C 1 ATOM 1677 O O . HIS B 2 104 ? 19.530 62.037 -58.414 1.00 18.99 ? ? ? ? ? ? 104 HIS B O 1 ATOM 1678 C CB . HIS B 2 104 ? 21.213 60.746 -55.925 1.00 16.62 ? ? ? ? ? ? 104 HIS B CB 1 ATOM 1679 C CG . HIS B 2 104 ? 22.336 61.642 -55.459 1.00 25.28 ? ? ? ? ? ? 104 HIS B CG 1 ATOM 1680 N ND1 . HIS B 2 104 ? 23.120 62.390 -56.337 1.00 29.30 ? ? ? ? ? ? 104 HIS B ND1 1 ATOM 1681 C CD2 . HIS B 2 104 ? 22.773 61.953 -54.208 1.00 29.34 ? ? ? ? ? ? 104 HIS B CD2 1 ATOM 1682 C CE1 . HIS B 2 104 ? 23.952 63.152 -55.647 1.00 29.76 ? ? ? ? ? ? 104 HIS B CE1 1 ATOM 1683 N NE2 . HIS B 2 104 ? 23.782 62.891 -54.358 1.00 36.11 ? ? ? ? ? ? 104 HIS B NE2 1 ATOM 1684 N N . GLY B 2 105 ? 20.739 63.493 -57.095 1.00 18.38 ? ? ? ? ? ? 105 GLY B N 1 ATOM 1685 C CA . GLY B 2 105 ? 20.819 64.653 -58.034 1.00 16.22 ? ? ? ? ? ? 105 GLY B CA 1 ATOM 1686 C C . GLY B 2 105 ? 19.465 65.145 -58.513 1.00 16.19 ? ? ? ? ? ? 105 GLY B C 1 ATOM 1687 O O . GLY B 2 105 ? 19.368 65.887 -59.512 1.00 19.12 ? ? ? ? ? ? 105 GLY B O 1 ATOM 1688 N N . LYS B 2 106 ? 18.393 64.787 -57.799 1.00 14.02 ? ? ? ? ? ? 106 LYS B N 1 ATOM 1689 C CA . LYS B 2 106 ? 17.084 65.062 -58.255 1.00 12.47 ? ? ? ? ? ? 106 LYS B CA 1 ATOM 1690 C C . LYS B 2 106 ? 16.345 65.731 -57.120 1.00 12.17 ? ? ? ? ? ? 106 LYS B C 1 ATOM 1691 O O . LYS B 2 106 ? 16.776 65.679 -56.013 1.00 11.55 ? ? ? ? ? ? 106 LYS B O 1 ATOM 1692 C CB . LYS B 2 106 ? 16.360 63.756 -58.710 1.00 13.14 ? ? ? ? ? ? 106 LYS B CB 1 ATOM 1693 C CG . LYS B 2 106 ? 16.797 63.278 -60.111 1.00 8.35 ? ? ? ? ? ? 106 LYS B CG 1 ATOM 1694 C CD . LYS B 2 106 ? 16.382 61.820 -60.425 1.00 11.82 ? ? ? ? ? ? 106 LYS B CD 1 ATOM 1695 C CE . LYS B 2 106 ? 17.092 61.326 -61.692 1.00 15.57 ? ? ? ? ? ? 106 LYS B CE 1 ATOM 1696 N NZ . LYS B 2 106 ? 18.235 60.490 -61.370 1.00 7.61 ? ? ? ? ? ? 106 LYS B NZ 1 ATOM 1697 N N . THR B 2 107 ? 15.234 66.428 -57.401 1.00 13.15 ? ? ? ? ? ? 107 THR B N 1 ATOM 1698 C CA . THR B 2 107 ? 14.476 67.159 -56.381 1.00 8.49 ? ? ? ? ? ? 107 THR B CA 1 ATOM 1699 C C . THR B 2 107 ? 13.231 67.590 -57.055 1.00 6.30 ? ? ? ? ? ? 107 THR B C 1 ATOM 1700 O O . THR B 2 107 ? 13.235 67.728 -58.277 1.00 5.01 ? ? ? ? ? ? 107 THR B O 1 ATOM 1701 C CB . THR B 2 107 ? 15.275 68.272 -55.782 1.00 8.54 ? ? ? ? ? ? 107 THR B CB 1 ATOM 1702 O OG1 . THR B 2 107 ? 14.660 68.602 -54.511 1.00 14.67 ? ? ? ? ? ? 107 THR B OG1 1 ATOM 1703 C CG2 . THR B 2 107 ? 15.330 69.521 -56.648 1.00 9.67 ? ? ? ? ? ? 107 THR B CG2 1 ATOM 1704 N N . CYS B 2 108 ? 12.188 67.807 -56.306 1.00 4.27 ? ? ? ? ? ? 108 CYS B N 1 ATOM 1705 C CA . CYS B 2 108 ? 10.876 68.141 -56.923 1.00 6.58 ? ? ? ? ? ? 108 CYS B CA 1 ATOM 1706 C C . CYS B 2 108 ? 10.353 69.553 -56.567 1.00 5.36 ? ? ? ? ? ? 108 CYS B C 1 ATOM 1707 O O . CYS B 2 108 ? 10.907 70.226 -55.725 1.00 5.29 ? ? ? ? ? ? 108 CYS B O 1 ATOM 1708 C CB . CYS B 2 108 ? 9.803 67.187 -56.465 1.00 6.72 ? ? ? ? ? ? 108 CYS B CB 1 ATOM 1709 S SG . CYS B 2 108 ? 10.094 65.385 -57.069 1.00 9.90 ? ? ? ? ? ? 108 CYS B SG 1 ATOM 1710 N N . MET B 2 109 ? 9.316 70.008 -57.246 1.00 5.12 ? ? ? ? ? ? 109 MET B N 1 ATOM 1711 C CA . MET B 2 109 ? 8.679 71.251 -56.801 1.00 7.91 ? ? ? ? ? ? 109 MET B CA 1 ATOM 1712 C C . MET B 2 109 ? 7.433 71.379 -57.550 1.00 9.35 ? ? ? ? ? ? 109 MET B C 1 ATOM 1713 O O . MET B 2 109 ? 6.863 70.371 -58.066 1.00 8.73 ? ? ? ? ? ? 109 MET B O 1 ATOM 1714 C CB . MET B 2 109 ? 9.568 72.495 -57.063 1.00 4.69 ? ? ? ? ? ? 109 MET B CB 1 ATOM 1715 C CG . MET B 2 109 ? 10.500 72.430 -58.287 1.00 4.57 ? ? ? ? ? ? 109 MET B CG 1 ATOM 1716 S SD . MET B 2 109 ? 11.353 73.955 -58.699 1.00 14.05 ? ? ? ? ? ? 109 MET B SD 1 ATOM 1717 C CE . MET B 2 109 ? 10.059 75.050 -58.966 1.00 5.69 ? ? ? ? ? ? 109 MET B CE 1 ATOM 1718 N N . TYR B 2 110 ? 6.937 72.604 -57.591 1.00 9.58 ? ? ? ? ? ? 110 TYR B N 1 ATOM 1719 C CA . TYR B 2 110 ? 5.757 72.850 -58.404 1.00 10.15 ? ? ? ? ? ? 110 TYR B CA 1 ATOM 1720 C C . TYR B 2 110 ? 5.902 74.323 -58.882 1.00 9.39 ? ? ? ? ? ? 110 TYR B C 1 ATOM 1721 O O . TYR B 2 110 ? 6.311 75.097 -58.125 1.00 9.09 ? ? ? ? ? ? 110 TYR B O 1 ATOM 1722 C CB . TYR B 2 110 ? 4.550 72.741 -57.565 1.00 7.44 ? ? ? ? ? ? 110 TYR B CB 1 ATOM 1723 C CG . TYR B 2 110 ? 4.372 71.414 -56.868 1.00 9.66 ? ? ? ? ? ? 110 TYR B CG 1 ATOM 1724 C CD1 . TYR B 2 110 ? 4.965 71.150 -55.616 1.00 6.00 ? ? ? ? ? ? 110 TYR B CD1 1 ATOM 1725 C CD2 . TYR B 2 110 ? 3.577 70.425 -57.453 1.00 3.96 ? ? ? ? ? ? 110 TYR B CD2 1 ATOM 1726 C CE1 . TYR B 2 110 ? 4.778 69.920 -54.962 1.00 12.85 ? ? ? ? ? ? 110 TYR B CE1 1 ATOM 1727 C CE2 . TYR B 2 110 ? 3.408 69.212 -56.844 1.00 15.12 ? ? ? ? ? ? 110 TYR B CE2 1 ATOM 1728 C CZ . TYR B 2 110 ? 3.977 68.950 -55.612 1.00 12.80 ? ? ? ? ? ? 110 TYR B CZ 1 ATOM 1729 O OH . TYR B 2 110 ? 3.699 67.763 -55.123 1.00 5.30 ? ? ? ? ? ? 110 TYR B OH 1 ATOM 1730 N N . GLY B 2 111 ? 5.582 74.631 -60.131 1.00 8.70 ? ? ? ? ? ? 111 GLY B N 1 ATOM 1731 C CA . GLY B 2 111 ? 5.484 75.996 -60.610 1.00 9.13 ? ? ? ? ? ? 111 GLY B CA 1 ATOM 1732 C C . GLY B 2 111 ? 6.866 76.655 -60.607 1.00 9.52 ? ? ? ? ? ? 111 GLY B C 1 ATOM 1733 O O . GLY B 2 111 ? 7.889 75.991 -60.731 1.00 8.14 ? ? ? ? ? ? 111 GLY B O 1 ATOM 1734 N N . GLY B 2 112 ? 6.873 77.960 -60.434 1.00 10.77 ? ? ? ? ? ? 112 GLY B N 1 ATOM 1735 C CA . GLY B 2 112 ? 8.144 78.748 -60.544 1.00 13.18 ? ? ? ? ? ? 112 GLY B CA 1 ATOM 1736 C C . GLY B 2 112 ? 8.996 78.739 -61.797 1.00 11.17 ? ? ? ? ? ? 112 GLY B C 1 ATOM 1737 O O . GLY B 2 112 ? 10.105 78.204 -61.791 1.00 13.11 ? ? ? ? ? ? 112 GLY B O 1 ATOM 1738 N N . ILE B 2 113 ? 8.467 79.310 -62.878 1.00 11.24 ? ? ? ? ? ? 113 ILE B N 1 ATOM 1739 C CA . ILE B 2 113 ? 9.169 79.449 -64.171 1.00 9.56 ? ? ? ? ? ? 113 ILE B CA 1 ATOM 1740 C C . ILE B 2 113 ? 8.519 80.518 -64.952 1.00 10.23 ? ? ? ? ? ? 113 ILE B C 1 ATOM 1741 O O . ILE B 2 113 ? 7.281 80.661 -64.867 1.00 10.06 ? ? ? ? ? ? 113 ILE B O 1 ATOM 1742 C CB . ILE B 2 113 ? 9.006 78.156 -64.984 1.00 8.61 ? ? ? ? ? ? 113 ILE B CB 1 ATOM 1743 C CG1 . ILE B 2 113 ? 7.580 77.622 -64.832 1.00 8.65 ? ? ? ? ? ? 113 ILE B CG1 1 ATOM 1744 C CG2 . ILE B 2 113 ? 9.994 77.192 -64.406 1.00 6.90 ? ? ? ? ? ? 113 ILE B CG2 1 ATOM 1745 C CD1 . ILE B 2 113 ? 7.313 76.166 -65.516 1.00 12.96 ? ? ? ? ? ? 113 ILE B CD1 1 ATOM 1746 N N . THR B 2 114 ? 9.325 81.256 -65.725 1.00 10.16 ? ? ? ? ? ? 114 THR B N 1 ATOM 1747 C CA . THR B 2 114 ? 8.774 82.257 -66.629 1.00 11.15 ? ? ? ? ? ? 114 THR B CA 1 ATOM 1748 C C . THR B 2 114 ? 9.670 82.465 -67.835 1.00 10.54 ? ? ? ? ? ? 114 THR B C 1 ATOM 1749 O O . THR B 2 114 ? 10.912 82.234 -67.805 1.00 11.15 ? ? ? ? ? ? 114 THR B O 1 ATOM 1750 C CB . THR B 2 114 ? 8.550 83.601 -65.914 1.00 13.35 ? ? ? ? ? ? 114 THR B CB 1 ATOM 1751 O OG1 . THR B 2 114 ? 9.843 84.078 -65.478 1.00 16.18 ? ? ? ? ? ? 114 THR B OG1 1 ATOM 1752 C CG2 . THR B 2 114 ? 7.606 83.380 -64.728 1.00 7.66 ? ? ? ? ? ? 114 THR B CG2 1 ATOM 1753 N N . LYS B 2 115 ? 9.050 82.879 -68.928 1.00 9.49 ? ? ? ? ? ? 115 LYS B N 1 ATOM 1754 C CA . LYS B 2 115 ? 9.785 83.011 -70.168 1.00 9.70 ? ? ? ? ? ? 115 LYS B CA 1 ATOM 1755 C C . LYS B 2 115 ? 10.811 84.122 -69.895 1.00 9.23 ? ? ? ? ? ? 115 LYS B C 1 ATOM 1756 O O . LYS B 2 115 ? 10.503 85.183 -69.354 1.00 9.06 ? ? ? ? ? ? 115 LYS B O 1 ATOM 1757 C CB . LYS B 2 115 ? 8.908 83.301 -71.387 1.00 10.49 ? ? ? ? ? ? 115 LYS B CB 1 ATOM 1758 C CG . LYS B 2 115 ? 8.038 82.187 -72.012 1.00 19.64 ? ? ? ? ? ? 115 LYS B CG 1 ATOM 1759 C CD . LYS B 2 115 ? 8.699 80.880 -72.386 1.00 19.57 ? ? ? ? ? ? 115 LYS B CD 1 ATOM 1760 C CE . LYS B 2 115 ? 9.221 80.970 -73.805 1.00 21.13 ? ? ? ? ? ? 115 LYS B CE 1 ATOM 1761 N NZ . LYS B 2 115 ? 8.195 80.572 -74.876 1.00 17.94 ? ? ? ? ? ? 115 LYS B NZ 1 ATOM 1762 N N . HIS B 2 116 ? 12.071 83.790 -70.094 1.00 10.99 ? ? ? ? ? ? 116 HIS B N 1 ATOM 1763 C CA . HIS B 2 116 ? 13.201 84.707 -69.864 1.00 10.07 ? ? ? ? ? ? 116 HIS B CA 1 ATOM 1764 C C . HIS B 2 116 ? 13.223 85.943 -70.791 1.00 12.52 ? ? ? ? ? ? 116 HIS B C 1 ATOM 1765 O O . HIS B 2 116 ? 13.477 87.033 -70.303 1.00 9.87 ? ? ? ? ? ? 116 HIS B O 1 ATOM 1766 C CB . HIS B 2 116 ? 14.447 83.988 -70.149 1.00 9.39 ? ? ? ? ? ? 116 HIS B CB 1 ATOM 1767 C CG . HIS B 2 116 ? 15.634 84.874 -70.122 1.00 10.83 ? ? ? ? ? ? 116 HIS B CG 1 ATOM 1768 N ND1 . HIS B 2 116 ? 15.658 86.065 -70.805 1.00 10.40 ? ? ? ? ? ? 116 HIS B ND1 1 ATOM 1769 C CD2 . HIS B 2 116 ? 16.854 84.727 -69.554 1.00 7.08 ? ? ? ? ? ? 116 HIS B CD2 1 ATOM 1770 C CE1 . HIS B 2 116 ? 16.851 86.627 -70.630 1.00 16.48 ? ? ? ? ? ? 116 HIS B CE1 1 ATOM 1771 N NE2 . HIS B 2 116 ? 17.600 85.809 -69.915 1.00 13.80 ? ? ? ? ? ? 116 HIS B NE2 1 ATOM 1772 N N . GLU B 2 117 ? 12.954 85.711 -72.095 1.00 14.09 ? ? ? ? ? ? 117 GLU B N 1 ATOM 1773 C CA . GLU B 2 117 ? 13.008 86.715 -73.119 1.00 18.84 ? ? ? ? ? ? 117 GLU B CA 1 ATOM 1774 C C . GLU B 2 117 ? 12.160 87.878 -72.715 1.00 20.59 ? ? ? ? ? ? 117 GLU B C 1 ATOM 1775 O O . GLU B 2 117 ? 10.973 87.724 -72.412 1.00 18.17 ? ? ? ? ? ? 117 GLU B O 1 ATOM 1776 C CB . GLU B 2 117 ? 12.507 86.212 -74.453 1.00 19.37 ? ? ? ? ? ? 117 GLU B CB 1 ATOM 1777 C CG . GLU B 2 117 ? 13.333 85.008 -74.997 1.00 25.78 ? ? ? ? ? ? 117 GLU B CG 1 ATOM 1778 C CD . GLU B 2 117 ? 13.310 83.843 -74.035 1.00 27.77 ? ? ? ? ? ? 117 GLU B CD 1 ATOM 1779 O OE1 . GLU B 2 117 ? 12.223 83.466 -73.482 1.00 32.69 ? ? ? ? ? ? 117 GLU B OE1 1 ATOM 1780 O OE2 . GLU B 2 117 ? 14.401 83.336 -73.758 1.00 33.27 ? ? ? ? ? ? 117 GLU B OE2 1 ATOM 1781 N N . GLY B 2 118 ? 12.817 89.041 -72.711 1.00 22.37 ? ? ? ? ? ? 118 GLY B N 1 ATOM 1782 C CA . GLY B 2 118 ? 12.149 90.322 -72.498 1.00 24.73 ? ? ? ? ? ? 118 GLY B CA 1 ATOM 1783 C C . GLY B 2 118 ? 11.132 90.259 -71.360 1.00 26.71 ? ? ? ? ? ? 118 GLY B C 1 ATOM 1784 O O . GLY B 2 118 ? 9.886 90.422 -71.592 1.00 27.33 ? ? ? ? ? ? 118 GLY B O 1 ATOM 1785 N N . ASN B 2 119 ? 11.679 89.909 -70.183 1.00 27.51 ? ? ? ? ? ? 119 ASN B N 1 ATOM 1786 C CA . ASN B 2 119 ? 10.988 89.869 -68.887 1.00 29.14 ? ? ? ? ? ? 119 ASN B CA 1 ATOM 1787 C C . ASN B 2 119 ? 11.884 90.374 -67.752 1.00 29.31 ? ? ? ? ? ? 119 ASN B C 1 ATOM 1788 O O . ASN B 2 119 ? 11.366 90.684 -66.681 1.00 30.05 ? ? ? ? ? ? 119 ASN B O 1 ATOM 1789 C CB . ASN B 2 119 ? 10.432 88.477 -68.527 1.00 28.85 ? ? ? ? ? ? 119 ASN B CB 1 ATOM 1790 C CG . ASN B 2 119 ? 9.737 88.451 -67.164 1.00 29.52 ? ? ? ? ? ? 119 ASN B CG 1 ATOM 1791 O OD1 . ASN B 2 119 ? 8.930 89.342 -66.828 1.00 26.52 ? ? ? ? ? ? 119 ASN B OD1 1 ATOM 1792 N ND2 . ASN B 2 119 ? 10.089 87.441 -66.339 1.00 26.90 ? ? ? ? ? ? 119 ASN B ND2 1 ATOM 1793 N N . HIS B 2 120 ? 13.196 90.450 -67.971 1.00 28.78 ? ? ? ? ? ? 120 HIS B N 1 ATOM 1794 C CA . HIS B 2 120 ? 14.067 91.078 -66.995 1.00 29.01 ? ? ? ? ? ? 120 HIS B CA 1 ATOM 1795 C C . HIS B 2 120 ? 14.113 92.632 -67.214 1.00 29.57 ? ? ? ? ? ? 120 HIS B C 1 ATOM 1796 O O . HIS B 2 120 ? 13.477 93.145 -68.150 1.00 28.35 ? ? ? ? ? ? 120 HIS B O 1 ATOM 1797 C CB . HIS B 2 120 ? 15.447 90.446 -66.999 1.00 27.87 ? ? ? ? ? ? 120 HIS B CB 1 ATOM 1798 C CG . HIS B 2 120 ? 15.452 88.993 -66.670 1.00 27.03 ? ? ? ? ? ? 120 HIS B CG 1 ATOM 1799 N ND1 . HIS B 2 120 ? 16.619 88.308 -66.412 1.00 24.92 ? ? ? ? ? ? 120 HIS B ND1 1 ATOM 1800 C CD2 . HIS B 2 120 ? 14.451 88.070 -66.614 1.00 27.21 ? ? ? ? ? ? 120 HIS B CD2 1 ATOM 1801 C CE1 . HIS B 2 120 ? 16.339 87.035 -66.170 1.00 25.59 ? ? ? ? ? ? 120 HIS B CE1 1 ATOM 1802 N NE2 . HIS B 2 120 ? 15.024 86.861 -66.280 1.00 24.73 ? ? ? ? ? ? 120 HIS B NE2 1 ATOM 1803 N N . PHE B 2 121 ? 14.850 93.346 -66.342 1.00 30.72 ? ? ? ? ? ? 121 PHE B N 1 ATOM 1804 C CA . PHE B 2 121 ? 14.986 94.839 -66.354 1.00 30.52 ? ? ? ? ? ? 121 PHE B CA 1 ATOM 1805 C C . PHE B 2 121 ? 16.146 95.390 -67.176 1.00 31.96 ? ? ? ? ? ? 121 PHE B C 1 ATOM 1806 O O . PHE B 2 121 ? 17.125 94.668 -67.533 1.00 28.89 ? ? ? ? ? ? 121 PHE B O 1 ATOM 1807 C CB . PHE B 2 121 ? 15.031 95.395 -64.915 1.00 30.37 ? ? ? ? ? ? 121 PHE B CB 1 ATOM 1808 C CG . PHE B 2 121 ? 13.773 95.020 -64.070 1.00 32.98 ? ? ? ? ? ? 121 PHE B CG 1 ATOM 1809 C CD1 . PHE B 2 121 ? 13.731 93.846 -63.346 1.00 29.42 ? ? ? ? ? ? 121 PHE B CD1 1 ATOM 1810 C CD2 . PHE B 2 121 ? 12.650 95.835 -64.060 1.00 31.22 ? ? ? ? ? ? 121 PHE B CD2 1 ATOM 1811 C CE1 . PHE B 2 121 ? 12.612 93.474 -62.648 1.00 29.11 ? ? ? ? ? ? 121 PHE B CE1 1 ATOM 1812 C CE2 . PHE B 2 121 ? 11.490 95.513 -63.325 1.00 31.61 ? ? ? ? ? ? 121 PHE B CE2 1 ATOM 1813 C CZ . PHE B 2 121 ? 11.449 94.340 -62.621 1.00 33.06 ? ? ? ? ? ? 121 PHE B CZ 1 ATOM 1814 N N . ASP B 2 122 ? 16.012 96.696 -67.433 1.00 33.06 ? ? ? ? ? ? 122 ASP B N 1 ATOM 1815 C CA . ASP B 2 122 ? 17.021 97.532 -68.102 1.00 35.47 ? ? ? ? ? ? 122 ASP B CA 1 ATOM 1816 C C . ASP B 2 122 ? 18.478 97.100 -67.971 1.00 36.30 ? ? ? ? ? ? 122 ASP B C 1 ATOM 1817 O O . ASP B 2 122 ? 19.023 96.501 -68.922 1.00 36.41 ? ? ? ? ? ? 122 ASP B O 1 ATOM 1818 C CB . ASP B 2 122 ? 16.832 98.948 -67.623 1.00 35.80 ? ? ? ? ? ? 122 ASP B CB 1 ATOM 1819 C CG . ASP B 2 122 ? 15.368 99.286 -67.473 1.00 37.96 ? ? ? ? ? ? 122 ASP B CG 1 ATOM 1820 O OD1 . ASP B 2 122 ? 14.704 99.441 -68.516 1.00 33.41 ? ? ? ? ? ? 122 ASP B OD1 1 ATOM 1821 O OD2 . ASP B 2 122 ? 14.876 99.334 -66.319 1.00 41.53 ? ? ? ? ? ? 122 ASP B OD2 1 ATOM 1822 N N . ASN B 2 123 ? 19.109 97.411 -66.826 1.00 36.90 ? ? ? ? ? ? 123 ASN B N 1 ATOM 1823 C CA . ASN B 2 123 ? 20.581 97.164 -66.654 1.00 38.14 ? ? ? ? ? ? 123 ASN B CA 1 ATOM 1824 C C . ASN B 2 123 ? 20.949 96.369 -65.397 1.00 37.63 ? ? ? ? ? ? 123 ASN B C 1 ATOM 1825 O O . ASN B 2 123 ? 21.938 96.646 -64.728 1.00 37.21 ? ? ? ? ? ? 123 ASN B O 1 ATOM 1826 C CB . ASN B 2 123 ? 21.380 98.488 -66.751 1.00 38.59 ? ? ? ? ? ? 123 ASN B CB 1 ATOM 1827 C CG . ASN B 2 123 ? 20.858 99.394 -67.885 1.00 40.63 ? ? ? ? ? ? 123 ASN B CG 1 ATOM 1828 O OD1 . ASN B 2 123 ? 20.748 98.955 -69.059 1.00 38.53 ? ? ? ? ? ? 123 ASN B OD1 1 ATOM 1829 N ND2 . ASN B 2 123 ? 20.479 100.644 -67.525 1.00 41.94 ? ? ? ? ? ? 123 ASN B ND2 1 ATOM 1830 N N . GLY B 2 124 ? 20.147 95.340 -65.127 1.00 38.07 ? ? ? ? ? ? 124 GLY B N 1 ATOM 1831 C CA . GLY B 2 124 ? 20.142 94.651 -63.830 1.00 36.81 ? ? ? ? ? ? 124 GLY B CA 1 ATOM 1832 C C . GLY B 2 124 ? 19.411 95.286 -62.633 1.00 35.66 ? ? ? ? ? ? 124 GLY B C 1 ATOM 1833 O O . GLY B 2 124 ? 19.419 94.723 -61.534 1.00 36.43 ? ? ? ? ? ? 124 GLY B O 1 ATOM 1834 N N . ASN B 2 125 ? 18.789 96.454 -62.805 1.00 34.47 ? ? ? ? ? ? 125 ASN B N 1 ATOM 1835 C CA . ASN B 2 125 ? 17.963 97.006 -61.726 1.00 31.69 ? ? ? ? ? ? 125 ASN B CA 1 ATOM 1836 C C . ASN B 2 125 ? 16.999 95.950 -61.192 1.00 30.35 ? ? ? ? ? ? 125 ASN B C 1 ATOM 1837 O O . ASN B 2 125 ? 16.532 95.069 -61.946 1.00 29.46 ? ? ? ? ? ? 125 ASN B O 1 ATOM 1838 C CB . ASN B 2 125 ? 17.196 98.203 -62.233 1.00 31.89 ? ? ? ? ? ? 125 ASN B CB 1 ATOM 1839 C CG . ASN B 2 125 ? 18.067 99.117 -63.058 1.00 30.31 ? ? ? ? ? ? 125 ASN B CG 1 ATOM 1840 O OD1 . ASN B 2 125 ? 19.126 99.578 -62.604 1.00 32.28 ? ? ? ? ? ? 125 ASN B OD1 1 ATOM 1841 N ND2 . ASN B 2 125 ? 17.651 99.357 -64.282 1.00 27.13 ? ? ? ? ? ? 125 ASN B ND2 1 ATOM 1842 N N . LEU B 2 126 ? 16.716 96.038 -59.894 1.00 28.25 ? ? ? ? ? ? 126 LEU B N 1 ATOM 1843 C CA . LEU B 2 126 ? 15.776 95.134 -59.194 1.00 25.70 ? ? ? ? ? ? 126 LEU B CA 1 ATOM 1844 C C . LEU B 2 126 ? 14.576 95.936 -58.726 1.00 25.19 ? ? ? ? ? ? 126 LEU B C 1 ATOM 1845 O O . LEU B 2 126 ? 14.705 97.120 -58.351 1.00 24.59 ? ? ? ? ? ? 126 LEU B O 1 ATOM 1846 C CB . LEU B 2 126 ? 16.428 94.546 -57.965 1.00 22.39 ? ? ? ? ? ? 126 LEU B CB 1 ATOM 1847 C CG . LEU B 2 126 ? 17.691 93.714 -58.205 1.00 25.21 ? ? ? ? ? ? 126 LEU B CG 1 ATOM 1848 C CD1 . LEU B 2 126 ? 18.909 94.566 -57.829 1.00 21.63 ? ? ? ? ? ? 126 LEU B CD1 1 ATOM 1849 C CD2 . LEU B 2 126 ? 17.725 92.365 -57.395 1.00 14.86 ? ? ? ? ? ? 126 LEU B CD2 1 ATOM 1850 N N . GLN B 2 127 ? 13.438 95.266 -58.681 1.00 24.03 ? ? ? ? ? ? 127 GLN B N 1 ATOM 1851 C CA . GLN B 2 127 ? 12.162 95.869 -58.291 1.00 23.82 ? ? ? ? ? ? 127 GLN B CA 1 ATOM 1852 C C . GLN B 2 127 ? 11.867 95.662 -56.816 1.00 21.33 ? ? ? ? ? ? 127 GLN B C 1 ATOM 1853 O O . GLN B 2 127 ? 12.310 94.690 -56.213 1.00 23.19 ? ? ? ? ? ? 127 GLN B O 1 ATOM 1854 C CB . GLN B 2 127 ? 11.088 95.236 -59.159 1.00 24.51 ? ? ? ? ? ? 127 GLN B CB 1 ATOM 1855 C CG . GLN B 2 127 ? 9.693 95.720 -59.004 1.00 23.80 ? ? ? ? ? ? 127 GLN B CG 1 ATOM 1856 C CD . GLN B 2 127 ? 9.518 97.090 -59.486 1.00 19.47 ? ? ? ? ? ? 127 GLN B CD 1 ATOM 1857 O OE1 . GLN B 2 127 ? 9.931 97.432 -60.602 1.00 16.64 ? ? ? ? ? ? 127 GLN B OE1 1 ATOM 1858 N NE2 . GLN B 2 127 ? 8.884 97.934 -58.638 1.00 18.42 ? ? ? ? ? ? 127 GLN B NE2 1 ATOM 1859 N N . ASN B 2 128 ? 11.174 96.586 -56.197 1.00 18.24 ? ? ? ? ? ? 128 ASN B N 1 ATOM 1860 C CA . ASN B 2 128 ? 10.876 96.414 -54.808 1.00 16.74 ? ? ? ? ? ? 128 ASN B CA 1 ATOM 1861 C C . ASN B 2 128 ? 9.400 96.250 -54.537 1.00 14.86 ? ? ? ? ? ? 128 ASN B C 1 ATOM 1862 O O . ASN B 2 128 ? 8.579 96.911 -55.087 1.00 13.35 ? ? ? ? ? ? 128 ASN B O 1 ATOM 1863 C CB . ASN B 2 128 ? 11.460 97.541 -54.027 1.00 17.06 ? ? ? ? ? ? 128 ASN B CB 1 ATOM 1864 C CG . ASN B 2 128 ? 12.946 97.437 -53.892 1.00 22.92 ? ? ? ? ? ? 128 ASN B CG 1 ATOM 1865 O OD1 . ASN B 2 128 ? 13.540 96.484 -53.243 1.00 27.41 ? ? ? ? ? ? 128 ASN B OD1 1 ATOM 1866 N ND2 . ASN B 2 128 ? 13.598 98.411 -54.478 1.00 23.80 ? ? ? ? ? ? 128 ASN B ND2 1 ATOM 1867 N N . VAL B 2 129 ? 9.079 95.342 -53.647 1.00 15.83 ? ? ? ? ? ? 129 VAL B N 1 ATOM 1868 C CA . VAL B 2 129 ? 7.672 94.996 -53.374 1.00 12.49 ? ? ? ? ? ? 129 VAL B CA 1 ATOM 1869 C C . VAL B 2 129 ? 7.427 95.137 -51.888 1.00 12.76 ? ? ? ? ? ? 129 VAL B C 1 ATOM 1870 O O . VAL B 2 129 ? 8.068 94.511 -51.012 1.00 12.57 ? ? ? ? ? ? 129 VAL B O 1 ATOM 1871 C CB . VAL B 2 129 ? 7.312 93.651 -53.890 1.00 11.86 ? ? ? ? ? ? 129 VAL B CB 1 ATOM 1872 C CG1 . VAL B 2 129 ? 5.859 93.312 -53.630 1.00 13.98 ? ? ? ? ? ? 129 VAL B CG1 1 ATOM 1873 C CG2 . VAL B 2 129 ? 7.557 93.552 -55.345 1.00 12.23 ? ? ? ? ? ? 129 VAL B CG2 1 ATOM 1874 N N . LEU B 2 130 ? 6.505 96.028 -51.600 1.00 12.53 ? ? ? ? ? ? 130 LEU B N 1 ATOM 1875 C CA . LEU B 2 130 ? 6.116 96.238 -50.255 1.00 14.17 ? ? ? ? ? ? 130 LEU B CA 1 ATOM 1876 C C . LEU B 2 130 ? 5.396 95.053 -49.567 1.00 15.01 ? ? ? ? ? ? 130 LEU B C 1 ATOM 1877 O O . LEU B 2 130 ? 4.605 94.357 -50.183 1.00 12.94 ? ? ? ? ? ? 130 LEU B O 1 ATOM 1878 C CB . LEU B 2 130 ? 5.234 97.449 -50.208 1.00 13.01 ? ? ? ? ? ? 130 LEU B CB 1 ATOM 1879 C CG . LEU B 2 130 ? 4.670 97.861 -48.845 1.00 13.37 ? ? ? ? ? ? 130 LEU B CG 1 ATOM 1880 C CD1 . LEU B 2 130 ? 5.718 98.086 -47.935 1.00 17.50 ? ? ? ? ? ? 130 LEU B CD1 1 ATOM 1881 C CD2 . LEU B 2 130 ? 3.956 99.214 -49.054 1.00 14.42 ? ? ? ? ? ? 130 LEU B CD2 1 ATOM 1882 N N . VAL B 2 131 ? 5.654 94.887 -48.273 1.00 15.72 ? ? ? ? ? ? 131 VAL B N 1 ATOM 1883 C CA . VAL B 2 131 ? 4.900 93.944 -47.502 1.00 17.44 ? ? ? ? ? ? 131 VAL B CA 1 ATOM 1884 C C . VAL B 2 131 ? 4.422 94.588 -46.227 1.00 17.65 ? ? ? ? ? ? 131 VAL B C 1 ATOM 1885 O O . VAL B 2 131 ? 5.232 94.875 -45.390 1.00 18.45 ? ? ? ? ? ? 131 VAL B O 1 ATOM 1886 C CB . VAL B 2 131 ? 5.732 92.787 -47.129 1.00 17.83 ? ? ? ? ? ? 131 VAL B CB 1 ATOM 1887 C CG1 . VAL B 2 131 ? 4.857 91.621 -46.696 1.00 20.26 ? ? ? ? ? ? 131 VAL B CG1 1 ATOM 1888 C CG2 . VAL B 2 131 ? 6.479 92.304 -48.370 1.00 21.52 ? ? ? ? ? ? 131 VAL B CG2 1 ATOM 1889 N N . ARG B 2 132 ? 3.096 94.764 -46.065 1.00 17.10 ? ? ? ? ? ? 132 ARG B N 1 ATOM 1890 C CA . ARG B 2 132 ? 2.514 95.230 -44.837 1.00 16.49 ? ? ? ? ? ? 132 ARG B CA 1 ATOM 1891 C C . ARG B 2 132 ? 2.250 94.041 -43.951 1.00 16.38 ? ? ? ? ? ? 132 ARG B C 1 ATOM 1892 O O . ARG B 2 132 ? 1.486 93.128 -44.288 1.00 17.66 ? ? ? ? ? ? 132 ARG B O 1 ATOM 1893 C CB . ARG B 2 132 ? 1.233 96.053 -45.158 1.00 17.64 ? ? ? ? ? ? 132 ARG B CB 1 ATOM 1894 C CG . ARG B 2 132 ? 1.533 97.451 -45.817 1.00 19.05 ? ? ? ? ? ? 132 ARG B CG 1 ATOM 1895 C CD . ARG B 2 132 ? 0.175 98.171 -46.138 1.00 22.16 ? ? ? ? ? ? 132 ARG B CD 1 ATOM 1896 N NE . ARG B 2 132 ? 0.272 99.465 -46.820 1.00 26.61 ? ? ? ? ? ? 132 ARG B NE 1 ATOM 1897 C CZ . ARG B 2 132 ? 1.090 100.473 -46.477 1.00 28.63 ? ? ? ? ? ? 132 ARG B CZ 1 ATOM 1898 N NH1 . ARG B 2 132 ? 1.978 100.343 -45.482 1.00 24.59 ? ? ? ? ? ? 132 ARG B NH1 1 ATOM 1899 N NH2 . ARG B 2 132 ? 1.025 101.621 -47.167 1.00 26.04 ? ? ? ? ? ? 132 ARG B NH2 1 ATOM 1900 N N . VAL B 2 133 ? 2.899 93.957 -42.793 1.00 17.40 ? ? ? ? ? ? 133 VAL B N 1 ATOM 1901 C CA . VAL B 2 133 ? 2.578 92.864 -41.856 1.00 17.03 ? ? ? ? ? ? 133 VAL B CA 1 ATOM 1902 C C . VAL B 2 133 ? 1.515 93.263 -40.800 1.00 18.71 ? ? ? ? ? ? 133 VAL B C 1 ATOM 1903 O O . VAL B 2 133 ? 1.548 94.406 -40.251 1.00 20.36 ? ? ? ? ? ? 133 VAL B O 1 ATOM 1904 C CB . VAL B 2 133 ? 3.822 92.297 -41.244 1.00 16.70 ? ? ? ? ? ? 133 VAL B CB 1 ATOM 1905 C CG1 . VAL B 2 133 ? 3.556 90.928 -40.665 1.00 16.96 ? ? ? ? ? ? 133 VAL B CG1 1 ATOM 1906 C CG2 . VAL B 2 133 ? 4.932 92.191 -42.356 1.00 16.40 ? ? ? ? ? ? 133 VAL B CG2 1 ATOM 1907 N N . TYR B 2 134 ? 0.524 92.392 -40.573 1.00 15.25 ? ? ? ? ? ? 134 TYR B N 1 ATOM 1908 C CA . TYR B 2 134 ? -0.435 92.626 -39.494 1.00 14.39 ? ? ? ? ? ? 134 TYR B CA 1 ATOM 1909 C C . TYR B 2 134 ? -0.391 91.550 -38.377 1.00 14.65 ? ? ? ? ? ? 134 TYR B C 1 ATOM 1910 O O . TYR B 2 134 ? -0.665 90.379 -38.641 1.00 16.82 ? ? ? ? ? ? 134 TYR B O 1 ATOM 1911 C CB . TYR B 2 134 ? -1.813 92.708 -40.093 1.00 12.80 ? ? ? ? ? ? 134 TYR B CB 1 ATOM 1912 C CG . TYR B 2 134 ? -1.924 93.732 -41.220 1.00 11.35 ? ? ? ? ? ? 134 TYR B CG 1 ATOM 1913 C CD1 . TYR B 2 134 ? -1.179 93.601 -42.391 1.00 13.80 ? ? ? ? ? ? 134 TYR B CD1 1 ATOM 1914 C CD2 . TYR B 2 134 ? -2.725 94.806 -41.095 1.00 9.74 ? ? ? ? ? ? 134 TYR B CD2 1 ATOM 1915 C CE1 . TYR B 2 134 ? -1.221 94.530 -43.377 1.00 12.88 ? ? ? ? ? ? 134 TYR B CE1 1 ATOM 1916 C CE2 . TYR B 2 134 ? -2.824 95.757 -42.071 1.00 12.15 ? ? ? ? ? ? 134 TYR B CE2 1 ATOM 1917 C CZ . TYR B 2 134 ? -2.126 95.645 -43.251 1.00 15.95 ? ? ? ? ? ? 134 TYR B CZ 1 ATOM 1918 O OH . TYR B 2 134 ? -2.229 96.681 -44.278 1.00 10.49 ? ? ? ? ? ? 134 TYR B OH 1 ATOM 1919 N N . GLU B 2 135 ? -0.109 91.959 -37.145 1.00 12.49 ? ? ? ? ? ? 135 GLU B N 1 ATOM 1920 C CA . GLU B 2 135 ? -0.117 91.142 -35.939 1.00 11.29 ? ? ? ? ? ? 135 GLU B CA 1 ATOM 1921 C C . GLU B 2 135 ? -1.349 91.598 -35.210 1.00 11.63 ? ? ? ? ? ? 135 GLU B C 1 ATOM 1922 O O . GLU B 2 135 ? -1.486 92.793 -34.824 1.00 11.38 ? ? ? ? ? ? 135 GLU B O 1 ATOM 1923 C CB . GLU B 2 135 ? 1.158 91.467 -35.102 1.00 6.45 ? ? ? ? ? ? 135 GLU B CB 1 ATOM 1924 C CG . GLU B 2 135 ? 2.327 91.503 -35.961 1.00 9.85 ? ? ? ? ? ? 135 GLU B CG 1 ATOM 1925 C CD . GLU B 2 135 ? 3.631 91.477 -35.138 1.00 15.83 ? ? ? ? ? ? 135 GLU B CD 1 ATOM 1926 O OE1 . GLU B 2 135 ? 3.927 90.356 -34.611 1.00 17.06 ? ? ? ? ? ? 135 GLU B OE1 1 ATOM 1927 O OE2 . GLU B 2 135 ? 4.251 92.551 -34.974 1.00 8.29 ? ? ? ? ? ? 135 GLU B OE2 1 ATOM 1928 N N . ASN B 2 136 ? -2.278 90.671 -35.064 1.00 13.39 ? ? ? ? ? ? 136 ASN B N 1 ATOM 1929 C CA . ASN B 2 136 ? -3.520 90.942 -34.395 1.00 14.33 ? ? ? ? ? ? 136 ASN B CA 1 ATOM 1930 C C . ASN B 2 136 ? -4.244 92.175 -34.980 1.00 15.19 ? ? ? ? ? ? 136 ASN B C 1 ATOM 1931 O O . ASN B 2 136 ? -4.798 92.970 -34.222 1.00 15.12 ? ? ? ? ? ? 136 ASN B O 1 ATOM 1932 C CB . ASN B 2 136 ? -3.238 91.057 -32.887 1.00 13.00 ? ? ? ? ? ? 136 ASN B CB 1 ATOM 1933 C CG . ASN B 2 136 ? -2.793 89.706 -32.317 1.00 15.23 ? ? ? ? ? ? 136 ASN B CG 1 ATOM 1934 O OD1 . ASN B 2 136 ? -3.528 88.730 -32.438 1.00 16.81 ? ? ? ? ? ? 136 ASN B OD1 1 ATOM 1935 N ND2 . ASN B 2 136 ? -1.577 89.630 -31.783 1.00 8.97 ? ? ? ? ? ? 136 ASN B ND2 1 ATOM 1936 N N . LYS B 2 137 ? -4.207 92.305 -36.305 1.00 15.54 ? ? ? ? ? ? 137 LYS B N 1 ATOM 1937 C CA . LYS B 2 137 ? -4.813 93.461 -36.993 1.00 16.83 ? ? ? ? ? ? 137 LYS B CA 1 ATOM 1938 C C . LYS B 2 137 ? -4.002 94.796 -36.861 1.00 17.35 ? ? ? ? ? ? 137 LYS B C 1 ATOM 1939 O O . LYS B 2 137 ? -4.584 95.859 -36.880 1.00 17.81 ? ? ? ? ? ? 137 LYS B O 1 ATOM 1940 C CB . LYS B 2 137 ? -6.211 93.705 -36.484 1.00 16.90 ? ? ? ? ? ? 137 LYS B CB 1 ATOM 1941 C CG . LYS B 2 137 ? -7.126 92.573 -36.869 1.00 17.32 ? ? ? ? ? ? 137 LYS B CG 1 ATOM 1942 C CD . LYS B 2 137 ? -8.365 92.709 -36.102 1.00 16.98 ? ? ? ? ? ? 137 LYS B CD 1 ATOM 1943 C CE . LYS B 2 137 ? -9.354 91.606 -36.404 1.00 13.15 ? ? ? ? ? ? 137 LYS B CE 1 ATOM 1944 N NZ . LYS B 2 137 ? -9.922 91.819 -37.745 1.00 15.50 ? ? ? ? ? ? 137 LYS B NZ 1 ATOM 1945 N N . ARG B 2 138 ? -2.684 94.771 -36.745 1.00 16.45 ? ? ? ? ? ? 138 ARG B N 1 ATOM 1946 C CA . ARG B 2 138 ? -2.027 96.073 -36.683 1.00 16.54 ? ? ? ? ? ? 138 ARG B CA 1 ATOM 1947 C C . ARG B 2 138 ? -0.818 96.168 -37.593 1.00 15.22 ? ? ? ? ? ? 138 ARG B C 1 ATOM 1948 O O . ARG B 2 138 ? -0.110 95.183 -37.825 1.00 11.80 ? ? ? ? ? ? 138 ARG B O 1 ATOM 1949 C CB . ARG B 2 138 ? -1.701 96.347 -35.235 1.00 18.53 ? ? ? ? ? ? 138 ARG B CB 1 ATOM 1950 C CG . ARG B 2 138 ? -2.889 96.118 -34.246 1.00 17.08 ? ? ? ? ? ? 138 ARG B CG 1 ATOM 1951 C CD . ARG B 2 138 ? -2.777 97.008 -32.987 1.00 23.06 ? ? ? ? ? ? 138 ARG B CD 1 ATOM 1952 N NE . ARG B 2 138 ? -3.823 96.655 -32.002 1.00 22.86 ? ? ? ? ? ? 138 ARG B NE 1 ATOM 1953 C CZ . ARG B 2 138 ? -4.245 97.403 -31.003 1.00 20.73 ? ? ? ? ? ? 138 ARG B CZ 1 ATOM 1954 N NH1 . ARG B 2 138 ? -3.748 98.619 -30.789 1.00 28.49 ? ? ? ? ? ? 138 ARG B NH1 1 ATOM 1955 N NH2 . ARG B 2 138 ? -5.168 96.938 -30.191 1.00 21.56 ? ? ? ? ? ? 138 ARG B NH2 1 ATOM 1956 N N . ASN B 2 139 ? -0.613 97.325 -38.231 1.00 14.96 ? ? ? ? ? ? 139 ASN B N 1 ATOM 1957 C CA . ASN B 2 139 ? 0.519 97.337 -39.218 1.00 12.56 ? ? ? ? ? ? 139 ASN B CA 1 ATOM 1958 C C . ASN B 2 139 ? 1.790 97.520 -38.443 1.00 12.18 ? ? ? ? ? ? 139 ASN B C 1 ATOM 1959 O O . ASN B 2 139 ? 2.277 98.658 -38.204 1.00 12.06 ? ? ? ? ? ? 139 ASN B O 1 ATOM 1960 C CB . ASN B 2 139 ? 0.269 98.289 -40.419 1.00 12.40 ? ? ? ? ? ? 139 ASN B CB 1 ATOM 1961 C CG . ASN B 2 139 ? 1.417 98.285 -41.448 1.00 12.13 ? ? ? ? ? ? 139 ASN B CG 1 ATOM 1962 O OD1 . ASN B 2 139 ? 1.525 99.198 -42.291 1.00 5.69 ? ? ? ? ? ? 139 ASN B OD1 1 ATOM 1963 N ND2 . ASN B 2 139 ? 2.212 97.187 -41.462 1.00 8.79 ? ? ? ? ? ? 139 ASN B ND2 1 ATOM 1964 N N . THR B 2 140 ? 2.331 96.396 -37.975 1.00 9.99 ? ? ? ? ? ? 140 THR B N 1 ATOM 1965 C CA . THR B 2 140 ? 3.434 96.455 -37.026 1.00 10.22 ? ? ? ? ? ? 140 THR B CA 1 ATOM 1966 C C . THR B 2 140 ? 4.735 96.731 -37.764 1.00 10.78 ? ? ? ? ? ? 140 THR B C 1 ATOM 1967 O O . THR B 2 140 ? 5.424 97.718 -37.508 1.00 10.37 ? ? ? ? ? ? 140 THR B O 1 ATOM 1968 C CB . THR B 2 140 ? 3.592 95.116 -36.234 1.00 11.20 ? ? ? ? ? ? 140 THR B CB 1 ATOM 1969 O OG1 . THR B 2 140 ? 3.922 94.053 -37.120 1.00 10.26 ? ? ? ? ? ? 140 THR B OG1 1 ATOM 1970 C CG2 . THR B 2 140 ? 2.394 94.746 -35.594 1.00 2.00 ? ? ? ? ? ? 140 THR B CG2 1 ATOM 1971 N N . ILE B 2 141 ? 4.992 95.880 -38.747 1.00 11.81 ? ? ? ? ? ? 141 ILE B N 1 ATOM 1972 C CA . ILE B 2 141 ? 6.255 95.790 -39.452 1.00 10.72 ? ? ? ? ? ? 141 ILE B CA 1 ATOM 1973 C C . ILE B 2 141 ? 5.875 95.830 -40.951 1.00 12.42 ? ? ? ? ? ? 141 ILE B C 1 ATOM 1974 O O . ILE B 2 141 ? 4.781 95.385 -41.355 1.00 7.30 ? ? ? ? ? ? 141 ILE B O 1 ATOM 1975 C CB . ILE B 2 141 ? 7.065 94.510 -39.006 1.00 11.91 ? ? ? ? ? ? 141 ILE B CB 1 ATOM 1976 C CG1 . ILE B 2 141 ? 8.147 94.211 -40.039 1.00 8.86 ? ? ? ? ? ? 141 ILE B CG1 1 ATOM 1977 C CG2 . ILE B 2 141 ? 6.128 93.292 -38.739 1.00 12.28 ? ? ? ? ? ? 141 ILE B CG2 1 ATOM 1978 C CD1 . ILE B 2 141 ? 9.167 95.493 -40.257 1.00 3.62 ? ? ? ? ? ? 141 ILE B CD1 1 ATOM 1979 N N . SER B 2 142 ? 6.709 96.523 -41.742 1.00 14.48 ? ? ? ? ? ? 142 SER B N 1 ATOM 1980 C CA . SER B 2 142 ? 6.628 96.591 -43.249 1.00 13.70 ? ? ? ? ? ? 142 SER B CA 1 ATOM 1981 C C . SER B 2 142 ? 8.025 96.659 -43.904 1.00 13.12 ? ? ? ? ? ? 142 SER B C 1 ATOM 1982 O O . SER B 2 142 ? 8.828 97.511 -43.611 1.00 11.14 ? ? ? ? ? ? 142 SER B O 1 ATOM 1983 C CB . SER B 2 142 ? 5.924 97.861 -43.653 1.00 15.53 ? ? ? ? ? ? 142 SER B CB 1 ATOM 1984 O OG . SER B 2 142 ? 4.702 98.005 -42.923 1.00 14.03 ? ? ? ? ? ? 142 SER B OG 1 ATOM 1985 N N . PHE B 2 143 ? 8.274 95.801 -44.875 1.00 11.99 ? ? ? ? ? ? 143 PHE B N 1 ATOM 1986 C CA . PHE B 2 143 ? 9.587 95.706 -45.468 1.00 11.37 ? ? ? ? ? ? 143 PHE B CA 1 ATOM 1987 C C . PHE B 2 143 ? 9.326 95.531 -46.924 1.00 11.45 ? ? ? ? ? ? 143 PHE B C 1 ATOM 1988 O O . PHE B 2 143 ? 8.239 95.761 -47.315 1.00 12.79 ? ? ? ? ? ? 143 PHE B O 1 ATOM 1989 C CB . PHE B 2 143 ? 10.301 94.526 -44.890 1.00 10.71 ? ? ? ? ? ? 143 PHE B CB 1 ATOM 1990 C CG . PHE B 2 143 ? 9.560 93.219 -45.002 1.00 9.49 ? ? ? ? ? ? 143 PHE B CG 1 ATOM 1991 C CD1 . PHE B 2 143 ? 10.106 92.186 -45.648 1.00 18.65 ? ? ? ? ? ? 143 PHE B CD1 1 ATOM 1992 C CD2 . PHE B 2 143 ? 8.331 93.022 -44.396 1.00 19.43 ? ? ? ? ? ? 143 PHE B CD2 1 ATOM 1993 C CE1 . PHE B 2 143 ? 9.481 90.991 -45.773 1.00 12.40 ? ? ? ? ? ? 143 PHE B CE1 1 ATOM 1994 C CE2 . PHE B 2 143 ? 7.697 91.820 -44.463 1.00 19.98 ? ? ? ? ? ? 143 PHE B CE2 1 ATOM 1995 C CZ . PHE B 2 143 ? 8.272 90.796 -45.184 1.00 14.91 ? ? ? ? ? ? 143 PHE B CZ 1 ATOM 1996 N N . GLU B 2 144 ? 10.294 95.092 -47.693 1.00 13.00 ? ? ? ? ? ? 144 GLU B N 1 ATOM 1997 C CA . GLU B 2 144 ? 10.170 94.924 -49.116 1.00 14.00 ? ? ? ? ? ? 144 GLU B CA 1 ATOM 1998 C C . GLU B 2 144 ? 10.976 93.757 -49.637 1.00 15.25 ? ? ? ? ? ? 144 GLU B C 1 ATOM 1999 O O . GLU B 2 144 ? 11.881 93.239 -49.002 1.00 15.56 ? ? ? ? ? ? 144 GLU B O 1 ATOM 2000 C CB . GLU B 2 144 ? 10.675 96.141 -49.862 1.00 15.88 ? ? ? ? ? ? 144 GLU B CB 1 ATOM 2001 C CG . GLU B 2 144 ? 9.759 97.382 -49.850 1.00 16.61 ? ? ? ? ? ? 144 GLU B CG 1 ATOM 2002 C CD . GLU B 2 144 ? 10.582 98.650 -50.076 1.00 25.88 ? ? ? ? ? ? 144 GLU B CD 1 ATOM 2003 O OE1 . GLU B 2 144 ? 10.004 99.734 -50.402 1.00 24.45 ? ? ? ? ? ? 144 GLU B OE1 1 ATOM 2004 O OE2 . GLU B 2 144 ? 11.836 98.527 -49.921 1.00 27.33 ? ? ? ? ? ? 144 GLU B OE2 1 ATOM 2005 N N . VAL B 2 145 ? 10.655 93.342 -50.842 1.00 16.09 ? ? ? ? ? ? 145 VAL B N 1 ATOM 2006 C CA . VAL B 2 145 ? 11.274 92.161 -51.363 1.00 16.73 ? ? ? ? ? ? 145 VAL B CA 1 ATOM 2007 C C . VAL B 2 145 ? 11.813 92.517 -52.690 1.00 16.25 ? ? ? ? ? ? 145 VAL B C 1 ATOM 2008 O O . VAL B 2 145 ? 11.346 93.406 -53.306 1.00 17.89 ? ? ? ? ? ? 145 VAL B O 1 ATOM 2009 C CB . VAL B 2 145 ? 10.275 91.022 -51.474 1.00 14.60 ? ? ? ? ? ? 145 VAL B CB 1 ATOM 2010 C CG1 . VAL B 2 145 ? 9.897 90.667 -50.134 1.00 16.65 ? ? ? ? ? ? 145 VAL B CG1 1 ATOM 2011 C CG2 . VAL B 2 145 ? 8.988 91.435 -52.283 1.00 15.99 ? ? ? ? ? ? 145 VAL B CG2 1 ATOM 2012 N N . GLN B 2 146 ? 12.814 91.803 -53.152 1.00 17.11 ? ? ? ? ? ? 146 GLN B N 1 ATOM 2013 C CA . GLN B 2 146 ? 13.408 92.204 -54.403 1.00 15.52 ? ? ? ? ? ? 146 GLN B CA 1 ATOM 2014 C C . GLN B 2 146 ? 13.434 91.066 -55.360 1.00 14.76 ? ? ? ? ? ? 146 GLN B C 1 ATOM 2015 O O . GLN B 2 146 ? 13.734 89.925 -54.991 1.00 12.62 ? ? ? ? ? ? 146 GLN B O 1 ATOM 2016 C CB . GLN B 2 146 ? 14.852 92.695 -54.164 1.00 15.29 ? ? ? ? ? ? 146 GLN B CB 1 ATOM 2017 C CG . GLN B 2 146 ? 14.915 93.883 -53.203 1.00 15.56 ? ? ? ? ? ? 146 GLN B CG 1 ATOM 2018 C CD . GLN B 2 146 ? 16.273 94.492 -53.179 1.00 18.50 ? ? ? ? ? ? 146 GLN B CD 1 ATOM 2019 O OE1 . GLN B 2 146 ? 17.342 93.781 -53.079 1.00 18.79 ? ? ? ? ? ? 146 GLN B OE1 1 ATOM 2020 N NE2 . GLN B 2 146 ? 16.291 95.800 -53.332 1.00 18.71 ? ? ? ? ? ? 146 GLN B NE2 1 ATOM 2021 N N . THR B 2 147 ? 13.218 91.384 -56.629 1.00 14.53 ? ? ? ? ? ? 147 THR B N 1 ATOM 2022 C CA . THR B 2 147 ? 13.246 90.289 -57.663 1.00 12.61 ? ? ? ? ? ? 147 THR B CA 1 ATOM 2023 C C . THR B 2 147 ? 13.786 90.853 -59.005 1.00 11.23 ? ? ? ? ? ? 147 THR B C 1 ATOM 2024 O O . THR B 2 147 ? 13.910 92.079 -59.168 1.00 10.99 ? ? ? ? ? ? 147 THR B O 1 ATOM 2025 C CB . THR B 2 147 ? 11.877 89.794 -57.949 1.00 11.13 ? ? ? ? ? ? 147 THR B CB 1 ATOM 2026 O OG1 . THR B 2 147 ? 11.982 88.639 -58.863 1.00 11.61 ? ? ? ? ? ? 147 THR B OG1 1 ATOM 2027 C CG2 . THR B 2 147 ? 11.081 90.946 -58.616 1.00 5.83 ? ? ? ? ? ? 147 THR B CG2 1 ATOM 2028 N N . ASP B 2 148 ? 14.115 89.978 -59.937 1.00 10.18 ? ? ? ? ? ? 148 ASP B N 1 ATOM 2029 C CA . ASP B 2 148 ? 14.563 90.373 -61.257 1.00 10.48 ? ? ? ? ? ? 148 ASP B CA 1 ATOM 2030 C C . ASP B 2 148 ? 13.474 90.219 -62.298 1.00 11.60 ? ? ? ? ? ? 148 ASP B C 1 ATOM 2031 O O . ASP B 2 148 ? 13.622 90.804 -63.393 1.00 12.41 ? ? ? ? ? ? 148 ASP B O 1 ATOM 2032 C CB . ASP B 2 148 ? 15.841 89.592 -61.685 1.00 9.84 ? ? ? ? ? ? 148 ASP B CB 1 ATOM 2033 C CG . ASP B 2 148 ? 15.558 88.075 -61.807 1.00 11.48 ? ? ? ? ? ? 148 ASP B CG 1 ATOM 2034 O OD1 . ASP B 2 148 ? 16.421 87.265 -62.192 1.00 4.81 ? ? ? ? ? ? 148 ASP B OD1 1 ATOM 2035 O OD2 . ASP B 2 148 ? 14.466 87.683 -61.423 1.00 7.10 ? ? ? ? ? ? 148 ASP B OD2 1 ATOM 2036 N N . LYS B 2 149 ? 12.332 89.534 -61.997 1.00 11.88 ? ? ? ? ? ? 149 LYS B N 1 ATOM 2037 C CA . LYS B 2 149 ? 11.258 89.381 -62.974 1.00 10.08 ? ? ? ? ? ? 149 LYS B CA 1 ATOM 2038 C C . LYS B 2 149 ? 10.382 90.661 -63.193 1.00 11.09 ? ? ? ? ? ? 149 LYS B C 1 ATOM 2039 O O . LYS B 2 149 ? 10.161 91.470 -62.235 1.00 12.10 ? ? ? ? ? ? 149 LYS B O 1 ATOM 2040 C CB . LYS B 2 149 ? 10.389 88.174 -62.594 1.00 11.55 ? ? ? ? ? ? 149 LYS B CB 1 ATOM 2041 C CG . LYS B 2 149 ? 11.188 87.045 -61.819 1.00 7.50 ? ? ? ? ? ? 149 LYS B CG 1 ATOM 2042 C CD . LYS B 2 149 ? 12.368 86.532 -62.637 1.00 2.00 ? ? ? ? ? ? 149 LYS B CD 1 ATOM 2043 C CE . LYS B 2 149 ? 12.881 85.112 -62.243 1.00 3.24 ? ? ? ? ? ? 149 LYS B CE 1 ATOM 2044 N NZ . LYS B 2 149 ? 13.152 84.927 -60.827 1.00 2.00 ? ? ? ? ? ? 149 LYS B NZ 1 ATOM 2045 N N . LYS B 2 150 ? 9.764 90.813 -64.379 1.00 10.58 ? ? ? ? ? ? 150 LYS B N 1 ATOM 2046 C CA . LYS B 2 150 ? 8.923 92.106 -64.677 1.00 9.53 ? ? ? ? ? ? 150 LYS B CA 1 ATOM 2047 C C . LYS B 2 150 ? 7.539 91.632 -64.457 1.00 11.23 ? ? ? ? ? ? 150 LYS B C 1 ATOM 2048 O O . LYS B 2 150 ? 6.500 92.418 -64.529 1.00 10.14 ? ? ? ? ? ? 150 LYS B O 1 ATOM 2049 C CB . LYS B 2 150 ? 9.052 92.532 -66.136 1.00 4.52 ? ? ? ? ? ? 150 LYS B CB 1 ATOM 2050 C CG . LYS B 2 150 ? 8.851 94.008 -66.451 1.00 13.20 ? ? ? ? ? ? 150 LYS B CG 1 ATOM 2051 C CD . LYS B 2 150 ? 9.400 94.300 -67.839 1.00 9.55 ? ? ? ? ? ? 150 LYS B CD 1 ATOM 2052 C CE . LYS B 2 150 ? 10.997 94.288 -67.822 1.00 4.98 ? ? ? ? ? ? 150 LYS B CE 1 ATOM 2053 N NZ . LYS B 2 150 ? 11.424 94.556 -69.223 1.00 4.30 ? ? ? ? ? ? 150 LYS B NZ 1 ATOM 2054 N N . SER B 2 151 ? 7.503 90.300 -64.323 1.00 9.23 ? ? ? ? ? ? 151 SER B N 1 ATOM 2055 C CA . SER B 2 151 ? 6.316 89.645 -63.928 1.00 10.30 ? ? ? ? ? ? 151 SER B CA 1 ATOM 2056 C C . SER B 2 151 ? 6.768 88.289 -63.338 1.00 11.72 ? ? ? ? ? ? 151 SER B C 1 ATOM 2057 O O . SER B 2 151 ? 7.337 87.448 -64.084 1.00 8.10 ? ? ? ? ? ? 151 SER B O 1 ATOM 2058 C CB . SER B 2 151 ? 5.377 89.450 -65.116 1.00 10.96 ? ? ? ? ? ? 151 SER B CB 1 ATOM 2059 O OG . SER B 2 151 ? 4.585 88.212 -64.909 1.00 14.65 ? ? ? ? ? ? 151 SER B OG 1 ATOM 2060 N N . VAL B 2 152 ? 6.455 88.057 -62.037 1.00 11.10 ? ? ? ? ? ? 152 VAL B N 1 ATOM 2061 C CA . VAL B 2 152 ? 7.048 86.941 -61.284 1.00 9.74 ? ? ? ? ? ? 152 VAL B CA 1 ATOM 2062 C C . VAL B 2 152 ? 6.031 86.059 -60.641 1.00 10.99 ? ? ? ? ? ? 152 VAL B C 1 ATOM 2063 O O . VAL B 2 152 ? 4.885 86.505 -60.445 1.00 6.61 ? ? ? ? ? ? 152 VAL B O 1 ATOM 2064 C CB . VAL B 2 152 ? 7.801 87.481 -60.116 1.00 9.35 ? ? ? ? ? ? 152 VAL B CB 1 ATOM 2065 C CG1 . VAL B 2 152 ? 6.878 88.376 -59.353 1.00 11.35 ? ? ? ? ? ? 152 VAL B CG1 1 ATOM 2066 C CG2 . VAL B 2 152 ? 8.253 86.384 -59.300 1.00 13.03 ? ? ? ? ? ? 152 VAL B CG2 1 ATOM 2067 N N . THR B 2 153 ? 6.510 84.848 -60.248 1.00 11.20 ? ? ? ? ? ? 153 THR B N 1 ATOM 2068 C CA . THR B 2 153 ? 5.698 83.768 -59.709 1.00 11.26 ? ? ? ? ? ? 153 THR B CA 1 ATOM 2069 C C . THR B 2 153 ? 5.340 84.185 -58.299 1.00 12.21 ? ? ? ? ? ? 153 THR B C 1 ATOM 2070 O O . THR B 2 153 ? 6.251 84.416 -57.503 1.00 12.96 ? ? ? ? ? ? 153 THR B O 1 ATOM 2071 C CB . THR B 2 153 ? 6.433 82.432 -59.655 1.00 11.29 ? ? ? ? ? ? 153 THR B CB 1 ATOM 2072 O OG1 . THR B 2 153 ? 7.814 82.597 -59.311 1.00 11.34 ? ? ? ? ? ? 153 THR B OG1 1 ATOM 2073 C CG2 . THR B 2 153 ? 6.466 81.805 -60.952 1.00 12.78 ? ? ? ? ? ? 153 THR B CG2 1 ATOM 2074 N N . ALA B 2 154 ? 4.019 84.290 -57.955 1.00 12.08 ? ? ? ? ? ? 154 ALA B N 1 ATOM 2075 C CA . ALA B 2 154 ? 3.649 84.533 -56.565 1.00 9.26 ? ? ? ? ? ? 154 ALA B CA 1 ATOM 2076 C C . ALA B 2 154 ? 4.533 83.702 -55.618 1.00 11.16 ? ? ? ? ? ? 154 ALA B C 1 ATOM 2077 O O . ALA B 2 154 ? 4.940 84.181 -54.553 1.00 12.36 ? ? ? ? ? ? 154 ALA B O 1 ATOM 2078 C CB . ALA B 2 154 ? 2.205 84.209 -56.320 1.00 9.88 ? ? ? ? ? ? 154 ALA B CB 1 ATOM 2079 N N . GLN B 2 155 ? 4.785 82.440 -55.964 1.00 12.24 ? ? ? ? ? ? 155 GLN B N 1 ATOM 2080 C CA . GLN B 2 155 ? 5.619 81.588 -55.156 1.00 11.20 ? ? ? ? ? ? 155 GLN B CA 1 ATOM 2081 C C . GLN B 2 155 ? 6.899 82.299 -54.858 1.00 11.78 ? ? ? ? ? ? 155 GLN B C 1 ATOM 2082 O O . GLN B 2 155 ? 7.191 82.525 -53.686 1.00 12.77 ? ? ? ? ? ? 155 GLN B O 1 ATOM 2083 C CB . GLN B 2 155 ? 5.908 80.251 -55.863 1.00 11.22 ? ? ? ? ? ? 155 GLN B CB 1 ATOM 2084 C CG . GLN B 2 155 ? 6.855 79.389 -55.121 1.00 9.44 ? ? ? ? ? ? 155 GLN B CG 1 ATOM 2085 C CD . GLN B 2 155 ? 6.851 78.024 -55.598 1.00 12.25 ? ? ? ? ? ? 155 GLN B CD 1 ATOM 2086 O OE1 . GLN B 2 155 ? 7.563 77.137 -55.072 1.00 14.74 ? ? ? ? ? ? 155 GLN B OE1 1 ATOM 2087 N NE2 . GLN B 2 155 ? 6.021 77.785 -56.576 1.00 12.35 ? ? ? ? ? ? 155 GLN B NE2 1 ATOM 2088 N N . GLU B 2 156 ? 7.640 82.714 -55.879 1.00 12.68 ? ? ? ? ? ? 156 GLU B N 1 ATOM 2089 C CA . GLU B 2 156 ? 8.891 83.439 -55.654 1.00 11.50 ? ? ? ? ? ? 156 GLU B CA 1 ATOM 2090 C C . GLU B 2 156 ? 8.637 84.443 -54.618 1.00 10.38 ? ? ? ? ? ? 156 GLU B C 1 ATOM 2091 O O . GLU B 2 156 ? 9.384 84.522 -53.634 1.00 12.43 ? ? ? ? ? ? 156 GLU B O 1 ATOM 2092 C CB . GLU B 2 156 ? 9.405 84.209 -56.862 1.00 11.73 ? ? ? ? ? ? 156 GLU B CB 1 ATOM 2093 C CG . GLU B 2 156 ? 10.798 84.824 -56.532 1.00 10.22 ? ? ? ? ? ? 156 GLU B CG 1 ATOM 2094 C CD . GLU B 2 156 ? 11.506 85.410 -57.710 1.00 10.70 ? ? ? ? ? ? 156 GLU B CD 1 ATOM 2095 O OE1 . GLU B 2 156 ? 12.296 86.337 -57.499 1.00 10.68 ? ? ? ? ? ? 156 GLU B OE1 1 ATOM 2096 O OE2 . GLU B 2 156 ? 11.198 85.056 -58.862 1.00 10.69 ? ? ? ? ? ? 156 GLU B OE2 1 ATOM 2097 N N . LEU B 2 157 ? 7.605 85.247 -54.803 1.00 9.38 ? ? ? ? ? ? 157 LEU B N 1 ATOM 2098 C CA . LEU B 2 157 ? 7.452 86.402 -53.926 1.00 6.92 ? ? ? ? ? ? 157 LEU B CA 1 ATOM 2099 C C . LEU B 2 157 ? 7.151 85.981 -52.523 1.00 9.33 ? ? ? ? ? ? 157 LEU B C 1 ATOM 2100 O O . LEU B 2 157 ? 7.821 86.443 -51.555 1.00 7.71 ? ? ? ? ? ? 157 LEU B O 1 ATOM 2101 C CB . LEU B 2 157 ? 6.296 87.275 -54.392 1.00 7.19 ? ? ? ? ? ? 157 LEU B CB 1 ATOM 2102 C CG . LEU B 2 157 ? 6.432 88.273 -55.528 1.00 4.70 ? ? ? ? ? ? 157 LEU B CG 1 ATOM 2103 C CD1 . LEU B 2 157 ? 5.233 89.109 -55.484 1.00 9.57 ? ? ? ? ? ? 157 LEU B CD1 1 ATOM 2104 C CD2 . LEU B 2 157 ? 7.750 89.060 -55.364 1.00 2.23 ? ? ? ? ? ? 157 LEU B CD2 1 ATOM 2105 N N . ASP B 2 158 ? 6.125 85.108 -52.393 1.00 6.81 ? ? ? ? ? ? 158 ASP B N 1 ATOM 2106 C CA . ASP B 2 158 ? 5.819 84.524 -51.116 1.00 9.26 ? ? ? ? ? ? 158 ASP B CA 1 ATOM 2107 C C . ASP B 2 158 ? 7.054 84.005 -50.379 1.00 9.19 ? ? ? ? ? ? 158 ASP B C 1 ATOM 2108 O O . ASP B 2 158 ? 7.252 84.374 -49.231 1.00 8.82 ? ? ? ? ? ? 158 ASP B O 1 ATOM 2109 C CB . ASP B 2 158 ? 4.784 83.418 -51.365 1.00 11.98 ? ? ? ? ? ? 158 ASP B CB 1 ATOM 2110 C CG . ASP B 2 158 ? 4.422 82.679 -50.145 1.00 16.30 ? ? ? ? ? ? 158 ASP B CG 1 ATOM 2111 O OD1 . ASP B 2 158 ? 3.748 83.262 -49.219 1.00 14.32 ? ? ? ? ? ? 158 ASP B OD1 1 ATOM 2112 O OD2 . ASP B 2 158 ? 4.880 81.525 -50.123 1.00 19.46 ? ? ? ? ? ? 158 ASP B OD2 1 ATOM 2113 N N . ILE B 2 159 ? 7.863 83.122 -51.007 1.00 9.30 ? ? ? ? ? ? 159 ILE B N 1 ATOM 2114 C CA . ILE B 2 159 ? 8.998 82.477 -50.346 1.00 8.37 ? ? ? ? ? ? 159 ILE B CA 1 ATOM 2115 C C . ILE B 2 159 ? 9.803 83.588 -49.644 1.00 10.33 ? ? ? ? ? ? 159 ILE B C 1 ATOM 2116 O O . ILE B 2 159 ? 9.997 83.623 -48.443 1.00 7.57 ? ? ? ? ? ? 159 ILE B O 1 ATOM 2117 C CB . ILE B 2 159 ? 9.929 81.735 -51.351 1.00 11.06 ? ? ? ? ? ? 159 ILE B CB 1 ATOM 2118 C CG1 . ILE B 2 159 ? 9.363 80.388 -51.909 1.00 7.96 ? ? ? ? ? ? 159 ILE B CG1 1 ATOM 2119 C CG2 . ILE B 2 159 ? 11.177 81.314 -50.633 1.00 9.39 ? ? ? ? ? ? 159 ILE B CG2 1 ATOM 2120 C CD1 . ILE B 2 159 ? 7.844 80.183 -51.454 1.00 17.04 ? ? ? ? ? ? 159 ILE B CD1 1 ATOM 2121 N N . LYS B 2 160 ? 10.165 84.572 -50.452 1.00 11.82 ? ? ? ? ? ? 160 LYS B N 1 ATOM 2122 C CA . LYS B 2 160 ? 11.039 85.659 -50.114 1.00 11.64 ? ? ? ? ? ? 160 LYS B CA 1 ATOM 2123 C C . LYS B 2 160 ? 10.470 86.359 -48.872 1.00 11.98 ? ? ? ? ? ? 160 LYS B C 1 ATOM 2124 O O . LYS B 2 160 ? 11.216 86.627 -47.920 1.00 12.74 ? ? ? ? ? ? 160 LYS B O 1 ATOM 2125 C CB . LYS B 2 160 ? 11.194 86.610 -51.340 1.00 12.67 ? ? ? ? ? ? 160 LYS B CB 1 ATOM 2126 C CG . LYS B 2 160 ? 12.181 86.122 -52.431 1.00 9.61 ? ? ? ? ? ? 160 LYS B CG 1 ATOM 2127 C CD . LYS B 2 160 ? 12.580 87.203 -53.487 1.00 11.23 ? ? ? ? ? ? 160 LYS B CD 1 ATOM 2128 C CE . LYS B 2 160 ? 13.616 86.635 -54.541 1.00 9.99 ? ? ? ? ? ? 160 LYS B CE 1 ATOM 2129 N NZ . LYS B 2 160 ? 14.115 87.376 -55.820 1.00 5.35 ? ? ? ? ? ? 160 LYS B NZ 1 ATOM 2130 N N . ALA B 2 161 ? 9.146 86.534 -48.838 1.00 12.01 ? ? ? ? ? ? 161 ALA B N 1 ATOM 2131 C CA . ALA B 2 161 ? 8.426 87.120 -47.715 1.00 11.13 ? ? ? ? ? ? 161 ALA B CA 1 ATOM 2132 C C . ALA B 2 161 ? 8.716 86.295 -46.441 1.00 11.55 ? ? ? ? ? ? 161 ALA B C 1 ATOM 2133 O O . ALA B 2 161 ? 9.305 86.799 -45.452 1.00 9.66 ? ? ? ? ? ? 161 ALA B O 1 ATOM 2134 C CB . ALA B 2 161 ? 6.886 87.065 -48.056 1.00 12.32 ? ? ? ? ? ? 161 ALA B CB 1 ATOM 2135 N N . ARG B 2 162 ? 8.197 85.055 -46.442 1.00 11.54 ? ? ? ? ? ? 162 ARG B N 1 ATOM 2136 C CA . ARG B 2 162 ? 8.422 84.079 -45.400 1.00 9.79 ? ? ? ? ? ? 162 ARG B CA 1 ATOM 2137 C C . ARG B 2 162 ? 9.892 83.993 -44.978 1.00 9.42 ? ? ? ? ? ? 162 ARG B C 1 ATOM 2138 O O . ARG B 2 162 ? 10.168 84.068 -43.811 1.00 10.61 ? ? ? ? ? ? 162 ARG B O 1 ATOM 2139 C CB . ARG B 2 162 ? 7.896 82.740 -45.885 1.00 10.88 ? ? ? ? ? ? 162 ARG B CB 1 ATOM 2140 C CG . ARG B 2 162 ? 6.352 82.681 -45.804 1.00 13.06 ? ? ? ? ? ? 162 ARG B CG 1 ATOM 2141 C CD . ARG B 2 162 ? 5.850 81.273 -46.220 1.00 10.66 ? ? ? ? ? ? 162 ARG B CD 1 ATOM 2142 N NE . ARG B 2 162 ? 4.394 81.194 -46.520 1.00 10.75 ? ? ? ? ? ? 162 ARG B NE 1 ATOM 2143 C CZ . ARG B 2 162 ? 3.785 80.040 -46.788 1.00 9.56 ? ? ? ? ? ? 162 ARG B CZ 1 ATOM 2144 N NH1 . ARG B 2 162 ? 4.494 78.951 -46.798 1.00 8.33 ? ? ? ? ? ? 162 ARG B NH1 1 ATOM 2145 N NH2 . ARG B 2 162 ? 2.508 79.945 -47.064 1.00 10.35 ? ? ? ? ? ? 162 ARG B NH2 1 ATOM 2146 N N . ASN B 2 163 ? 10.835 83.795 -45.876 1.00 10.21 ? ? ? ? ? ? 163 ASN B N 1 ATOM 2147 C CA . ASN B 2 163 ? 12.235 83.716 -45.525 1.00 12.67 ? ? ? ? ? ? 163 ASN B CA 1 ATOM 2148 C C . ASN B 2 163 ? 12.604 84.864 -44.587 1.00 15.05 ? ? ? ? ? ? 163 ASN B C 1 ATOM 2149 O O . ASN B 2 163 ? 13.316 84.622 -43.558 1.00 17.57 ? ? ? ? ? ? 163 ASN B O 1 ATOM 2150 C CB . ASN B 2 163 ? 13.070 83.786 -46.788 1.00 14.36 ? ? ? ? ? ? 163 ASN B CB 1 ATOM 2151 C CG . ASN B 2 163 ? 14.512 83.980 -46.551 1.00 14.15 ? ? ? ? ? ? 163 ASN B CG 1 ATOM 2152 O OD1 . ASN B 2 163 ? 15.211 83.055 -46.280 1.00 11.96 ? ? ? ? ? ? 163 ASN B OD1 1 ATOM 2153 N ND2 . ASN B 2 163 ? 15.004 85.206 -46.822 1.00 24.48 ? ? ? ? ? ? 163 ASN B ND2 1 ATOM 2154 N N . PHE B 2 164 ? 12.080 86.093 -44.849 1.00 15.44 ? ? ? ? ? ? 164 PHE B N 1 ATOM 2155 C CA . PHE B 2 164 ? 12.399 87.286 -44.019 1.00 15.88 ? ? ? ? ? ? 164 PHE B CA 1 ATOM 2156 C C . PHE B 2 164 ? 11.749 87.102 -42.681 1.00 16.37 ? ? ? ? ? ? 164 PHE B C 1 ATOM 2157 O O . PHE B 2 164 ? 12.455 87.126 -41.657 1.00 16.67 ? ? ? ? ? ? 164 PHE B O 1 ATOM 2158 C CB . PHE B 2 164 ? 11.861 88.609 -44.588 1.00 17.00 ? ? ? ? ? ? 164 PHE B CB 1 ATOM 2159 C CG . PHE B 2 164 ? 12.462 89.877 -43.968 1.00 14.90 ? ? ? ? ? ? 164 PHE B CG 1 ATOM 2160 C CD1 . PHE B 2 164 ? 13.725 90.325 -44.338 1.00 13.56 ? ? ? ? ? ? 164 PHE B CD1 1 ATOM 2161 C CD2 . PHE B 2 164 ? 11.668 90.727 -43.203 1.00 15.63 ? ? ? ? ? ? 164 PHE B CD2 1 ATOM 2162 C CE1 . PHE B 2 164 ? 14.224 91.559 -43.866 1.00 13.87 ? ? ? ? ? ? 164 PHE B CE1 1 ATOM 2163 C CE2 . PHE B 2 164 ? 12.157 91.868 -42.730 1.00 19.60 ? ? ? ? ? ? 164 PHE B CE2 1 ATOM 2164 C CZ . PHE B 2 164 ? 13.479 92.294 -43.064 1.00 18.93 ? ? ? ? ? ? 164 PHE B CZ 1 ATOM 2165 N N . LEU B 2 165 ? 10.410 86.953 -42.669 1.00 15.37 ? ? ? ? ? ? 165 LEU B N 1 ATOM 2166 C CA . LEU B 2 165 ? 9.702 86.666 -41.401 1.00 13.55 ? ? ? ? ? ? 165 LEU B CA 1 ATOM 2167 C C . LEU B 2 165 ? 10.424 85.562 -40.539 1.00 13.06 ? ? ? ? ? ? 165 LEU B C 1 ATOM 2168 O O . LEU B 2 165 ? 10.520 85.713 -39.307 1.00 11.08 ? ? ? ? ? ? 165 LEU B O 1 ATOM 2169 C CB . LEU B 2 165 ? 8.245 86.377 -41.674 1.00 13.17 ? ? ? ? ? ? 165 LEU B CB 1 ATOM 2170 C CG . LEU B 2 165 ? 7.361 87.729 -41.740 1.00 13.02 ? ? ? ? ? ? 165 LEU B CG 1 ATOM 2171 C CD1 . LEU B 2 165 ? 8.178 89.013 -41.878 1.00 11.78 ? ? ? ? ? ? 165 LEU B CD1 1 ATOM 2172 C CD2 . LEU B 2 165 ? 6.474 87.628 -42.851 1.00 6.61 ? ? ? ? ? ? 165 LEU B CD2 1 ATOM 2173 N N . ILE B 2 166 ? 10.884 84.469 -41.152 1.00 11.42 ? ? ? ? ? ? 166 ILE B N 1 ATOM 2174 C CA . ILE B 2 166 ? 11.692 83.493 -40.416 1.00 11.67 ? ? ? ? ? ? 166 ILE B CA 1 ATOM 2175 C C . ILE B 2 166 ? 12.885 84.313 -39.938 1.00 10.13 ? ? ? ? ? ? 166 ILE B C 1 ATOM 2176 O O . ILE B 2 166 ? 13.040 84.607 -38.744 1.00 10.32 ? ? ? ? ? ? 166 ILE B O 1 ATOM 2177 C CB . ILE B 2 166 ? 12.252 82.345 -41.291 1.00 11.20 ? ? ? ? ? ? 166 ILE B CB 1 ATOM 2178 C CG1 . ILE B 2 166 ? 11.249 81.284 -41.675 1.00 11.84 ? ? ? ? ? ? 166 ILE B CG1 1 ATOM 2179 C CG2 . ILE B 2 166 ? 13.248 81.641 -40.507 1.00 11.60 ? ? ? ? ? ? 166 ILE B CG2 1 ATOM 2180 C CD1 . ILE B 2 166 ? 9.884 81.831 -42.041 1.00 22.91 ? ? ? ? ? ? 166 ILE B CD1 1 ATOM 2181 N N . ASN B 2 167 ? 13.770 84.714 -40.837 1.00 11.87 ? ? ? ? ? ? 167 ASN B N 1 ATOM 2182 C CA . ASN B 2 167 ? 14.978 85.474 -40.340 1.00 14.05 ? ? ? ? ? ? 167 ASN B CA 1 ATOM 2183 C C . ASN B 2 167 ? 14.829 86.695 -39.391 1.00 12.90 ? ? ? ? ? ? 167 ASN B C 1 ATOM 2184 O O . ASN B 2 167 ? 15.831 87.273 -38.896 1.00 13.51 ? ? ? ? ? ? 167 ASN B O 1 ATOM 2185 C CB . ASN B 2 167 ? 15.834 85.843 -41.520 1.00 14.78 ? ? ? ? ? ? 167 ASN B CB 1 ATOM 2186 C CG . ASN B 2 167 ? 16.375 84.558 -42.230 1.00 19.05 ? ? ? ? ? ? 167 ASN B CG 1 ATOM 2187 O OD1 . ASN B 2 167 ? 15.645 83.560 -42.347 1.00 14.46 ? ? ? ? ? ? 167 ASN B OD1 1 ATOM 2188 N ND2 . ASN B 2 167 ? 17.676 84.566 -42.610 1.00 19.30 ? ? ? ? ? ? 167 ASN B ND2 1 ATOM 2189 N N . LYS B 2 168 ? 13.615 87.148 -39.125 1.00 11.26 ? ? ? ? ? ? 168 LYS B N 1 ATOM 2190 C CA . LYS B 2 168 ? 13.500 88.395 -38.258 1.00 11.77 ? ? ? ? ? ? 168 LYS B CA 1 ATOM 2191 C C . LYS B 2 168 ? 12.337 88.450 -37.256 1.00 12.15 ? ? ? ? ? ? 168 LYS B C 1 ATOM 2192 O O . LYS B 2 168 ? 12.322 89.311 -36.316 1.00 12.84 ? ? ? ? ? ? 168 LYS B O 1 ATOM 2193 C CB . LYS B 2 168 ? 13.505 89.680 -39.095 1.00 9.20 ? ? ? ? ? ? 168 LYS B CB 1 ATOM 2194 C CG . LYS B 2 168 ? 14.681 89.812 -40.078 1.00 10.37 ? ? ? ? ? ? 168 LYS B CG 1 ATOM 2195 C CD . LYS B 2 168 ? 15.794 90.757 -39.535 1.00 8.01 ? ? ? ? ? ? 168 LYS B CD 1 ATOM 2196 C CE . LYS B 2 168 ? 17.213 90.346 -40.138 1.00 15.79 ? ? ? ? ? ? 168 LYS B CE 1 ATOM 2197 N NZ . LYS B 2 168 ? 17.281 88.821 -40.091 1.00 16.18 ? ? ? ? ? ? 168 LYS B NZ 1 ATOM 2198 N N . LYS B 2 169 ? 11.339 87.613 -37.467 1.00 13.05 ? ? ? ? ? ? 169 LYS B N 1 ATOM 2199 C CA . LYS B 2 169 ? 10.094 87.567 -36.613 1.00 12.54 ? ? ? ? ? ? 169 LYS B CA 1 ATOM 2200 C C . LYS B 2 169 ? 9.630 86.120 -36.246 1.00 13.48 ? ? ? ? ? ? 169 LYS B C 1 ATOM 2201 O O . LYS B 2 169 ? 8.418 85.868 -35.965 1.00 10.89 ? ? ? ? ? ? 169 LYS B O 1 ATOM 2202 C CB . LYS B 2 169 ? 8.916 88.327 -37.262 1.00 13.42 ? ? ? ? ? ? 169 LYS B CB 1 ATOM 2203 C CG . LYS B 2 169 ? 8.749 89.804 -36.680 1.00 17.03 ? ? ? ? ? ? 169 LYS B CG 1 ATOM 2204 C CD . LYS B 2 169 ? 7.947 89.896 -35.456 1.00 14.89 ? ? ? ? ? ? 169 LYS B CD 1 ATOM 2205 C CE . LYS B 2 169 ? 7.454 91.335 -35.199 1.00 16.37 ? ? ? ? ? ? 169 LYS B CE 1 ATOM 2206 N NZ . LYS B 2 169 ? 6.425 91.315 -34.085 1.00 15.63 ? ? ? ? ? ? 169 LYS B NZ 1 ATOM 2207 N N . ASN B 2 170 ? 10.593 85.201 -36.191 1.00 12.08 ? ? ? ? ? ? 170 ASN B N 1 ATOM 2208 C CA . ASN B 2 170 ? 10.322 83.812 -35.828 1.00 12.48 ? ? ? ? ? ? 170 ASN B CA 1 ATOM 2209 C C . ASN B 2 170 ? 9.004 83.244 -36.324 1.00 12.71 ? ? ? ? ? ? 170 ASN B C 1 ATOM 2210 O O . ASN B 2 170 ? 8.240 82.589 -35.537 1.00 14.21 ? ? ? ? ? ? 170 ASN B O 1 ATOM 2211 C CB . ASN B 2 170 ? 10.468 83.548 -34.334 1.00 11.37 ? ? ? ? ? ? 170 ASN B CB 1 ATOM 2212 C CG . ASN B 2 170 ? 11.920 83.693 -33.827 1.00 17.78 ? ? ? ? ? ? 170 ASN B CG 1 ATOM 2213 O OD1 . ASN B 2 170 ? 12.516 84.844 -33.851 1.00 15.93 ? ? ? ? ? ? 170 ASN B OD1 1 ATOM 2214 N ND2 . ASN B 2 170 ? 12.530 82.540 -33.361 1.00 15.97 ? ? ? ? ? ? 170 ASN B ND2 1 ATOM 2215 N N . LEU B 2 171 ? 8.770 83.362 -37.618 1.00 12.00 ? ? ? ? ? ? 171 LEU B N 1 ATOM 2216 C CA . LEU B 2 171 ? 7.446 82.934 -38.152 1.00 13.94 ? ? ? ? ? ? 171 LEU B CA 1 ATOM 2217 C C . LEU B 2 171 ? 7.249 81.443 -37.909 1.00 12.54 ? ? ? ? ? ? 171 LEU B C 1 ATOM 2218 O O . LEU B 2 171 ? 6.137 81.008 -37.725 1.00 12.15 ? ? ? ? ? ? 171 LEU B O 1 ATOM 2219 C CB . LEU B 2 171 ? 7.261 83.317 -39.637 1.00 13.40 ? ? ? ? ? ? 171 LEU B CB 1 ATOM 2220 C CG . LEU B 2 171 ? 6.274 82.567 -40.512 1.00 14.34 ? ? ? ? ? ? 171 LEU B CG 1 ATOM 2221 C CD1 . LEU B 2 171 ? 4.844 83.009 -40.145 1.00 7.49 ? ? ? ? ? ? 171 LEU B CD1 1 ATOM 2222 C CD2 . LEU B 2 171 ? 6.735 82.999 -41.949 1.00 8.00 ? ? ? ? ? ? 171 LEU B CD2 1 ATOM 2223 N N . TYR B 2 172 ? 8.341 80.728 -37.855 1.00 10.81 ? ? ? ? ? ? 172 TYR B N 1 ATOM 2224 C CA . TYR B 2 172 ? 8.365 79.256 -37.737 1.00 11.68 ? ? ? ? ? ? 172 TYR B CA 1 ATOM 2225 C C . TYR B 2 172 ? 9.645 79.034 -36.906 1.00 12.20 ? ? ? ? ? ? 172 TYR B C 1 ATOM 2226 O O . TYR B 2 172 ? 10.677 79.740 -37.096 1.00 10.17 ? ? ? ? ? ? 172 TYR B O 1 ATOM 2227 C CB . TYR B 2 172 ? 8.570 78.541 -39.088 1.00 11.85 ? ? ? ? ? ? 172 TYR B CB 1 ATOM 2228 C CG . TYR B 2 172 ? 7.468 78.762 -40.131 1.00 9.76 ? ? ? ? ? ? 172 TYR B CG 1 ATOM 2229 C CD1 . TYR B 2 172 ? 7.741 79.149 -41.451 1.00 7.06 ? ? ? ? ? ? 172 TYR B CD1 1 ATOM 2230 C CD2 . TYR B 2 172 ? 6.145 78.621 -39.779 1.00 10.34 ? ? ? ? ? ? 172 TYR B CD2 1 ATOM 2231 C CE1 . TYR B 2 172 ? 6.648 79.451 -42.338 1.00 9.66 ? ? ? ? ? ? 172 TYR B CE1 1 ATOM 2232 C CE2 . TYR B 2 172 ? 5.073 78.813 -40.713 1.00 4.52 ? ? ? ? ? ? 172 TYR B CE2 1 ATOM 2233 C CZ . TYR B 2 172 ? 5.331 79.239 -41.922 1.00 7.82 ? ? ? ? ? ? 172 TYR B CZ 1 ATOM 2234 O OH . TYR B 2 172 ? 4.253 79.404 -42.710 1.00 8.43 ? ? ? ? ? ? 172 TYR B OH 1 ATOM 2235 N N . GLU B 2 173 ? 9.500 78.171 -35.925 1.00 10.42 ? ? ? ? ? ? 173 GLU B N 1 ATOM 2236 C CA . GLU B 2 173 ? 10.576 77.696 -35.098 1.00 10.75 ? ? ? ? ? ? 173 GLU B CA 1 ATOM 2237 C C . GLU B 2 173 ? 10.569 76.151 -35.102 1.00 8.85 ? ? ? ? ? ? 173 GLU B C 1 ATOM 2238 O O . GLU B 2 173 ? 9.491 75.561 -35.281 1.00 8.01 ? ? ? ? ? ? 173 GLU B O 1 ATOM 2239 C CB . GLU B 2 173 ? 10.446 78.222 -33.678 1.00 10.73 ? ? ? ? ? ? 173 GLU B CB 1 ATOM 2240 C CG . GLU B 2 173 ? 11.265 79.448 -33.450 1.00 12.19 ? ? ? ? ? ? 173 GLU B CG 1 ATOM 2241 C CD . GLU B 2 173 ? 11.168 80.039 -32.022 1.00 15.69 ? ? ? ? ? ? 173 GLU B CD 1 ATOM 2242 O OE1 . GLU B 2 173 ? 10.013 80.268 -31.509 1.00 15.58 ? ? ? ? ? ? 173 GLU B OE1 1 ATOM 2243 O OE2 . GLU B 2 173 ? 12.274 80.389 -31.525 1.00 12.51 ? ? ? ? ? ? 173 GLU B OE2 1 ATOM 2244 N N . PHE B 2 174 ? 11.758 75.549 -34.925 1.00 6.15 ? ? ? ? ? ? 174 PHE B N 1 ATOM 2245 C CA . PHE B 2 174 ? 11.932 74.151 -34.929 1.00 8.07 ? ? ? ? ? ? 174 PHE B CA 1 ATOM 2246 C C . PHE B 2 174 ? 10.870 73.308 -34.207 1.00 9.68 ? ? ? ? ? ? 174 PHE B C 1 ATOM 2247 O O . PHE B 2 174 ? 10.626 72.209 -34.646 1.00 9.78 ? ? ? ? ? ? 174 PHE B O 1 ATOM 2248 C CB . PHE B 2 174 ? 13.303 73.732 -34.570 1.00 7.52 ? ? ? ? ? ? 174 PHE B CB 1 ATOM 2249 C CG . PHE B 2 174 ? 13.510 72.266 -34.568 1.00 5.79 ? ? ? ? ? ? 174 PHE B CG 1 ATOM 2250 C CD1 . PHE B 2 174 ? 14.065 71.623 -35.663 1.00 14.25 ? ? ? ? ? ? 174 PHE B CD1 1 ATOM 2251 C CD2 . PHE B 2 174 ? 13.263 71.536 -33.446 1.00 9.44 ? ? ? ? ? ? 174 PHE B CD2 1 ATOM 2252 C CE1 . PHE B 2 174 ? 14.391 70.235 -35.653 1.00 10.77 ? ? ? ? ? ? 174 PHE B CE1 1 ATOM 2253 C CE2 . PHE B 2 174 ? 13.485 70.101 -33.390 1.00 10.57 ? ? ? ? ? ? 174 PHE B CE2 1 ATOM 2254 C CZ . PHE B 2 174 ? 14.040 69.450 -34.497 1.00 12.18 ? ? ? ? ? ? 174 PHE B CZ 1 ATOM 2255 N N . ASN B 2 175 ? 10.204 73.806 -33.170 1.00 12.47 ? ? ? ? ? ? 175 ASN B N 1 ATOM 2256 C CA . ASN B 2 175 ? 9.083 73.005 -32.528 1.00 13.00 ? ? ? ? ? ? 175 ASN B CA 1 ATOM 2257 C C . ASN B 2 175 ? 7.697 73.473 -32.777 1.00 12.75 ? ? ? ? ? ? 175 ASN B C 1 ATOM 2258 O O . ASN B 2 175 ? 6.675 72.740 -32.556 1.00 16.51 ? ? ? ? ? ? 175 ASN B O 1 ATOM 2259 C CB . ASN B 2 175 ? 9.316 72.909 -31.030 1.00 12.93 ? ? ? ? ? ? 175 ASN B CB 1 ATOM 2260 C CG . ASN B 2 175 ? 10.835 72.902 -30.648 1.00 19.64 ? ? ? ? ? ? 175 ASN B CG 1 ATOM 2261 O OD1 . ASN B 2 175 ? 11.562 73.894 -30.895 1.00 24.36 ? ? ? ? ? ? 175 ASN B OD1 1 ATOM 2262 N ND2 . ASN B 2 175 ? 11.309 71.787 -30.048 1.00 18.24 ? ? ? ? ? ? 175 ASN B ND2 1 ATOM 2263 N N . SER B 2 176 ? 7.597 74.751 -33.083 1.00 12.74 ? ? ? ? ? ? 176 SER B N 1 ATOM 2264 C CA . SER B 2 176 ? 6.358 75.376 -33.393 1.00 12.21 ? ? ? ? ? ? 176 SER B CA 1 ATOM 2265 C C . SER B 2 176 ? 6.504 76.858 -33.733 1.00 12.97 ? ? ? ? ? ? 176 SER B C 1 ATOM 2266 O O . SER B 2 176 ? 7.577 77.313 -34.215 1.00 13.11 ? ? ? ? ? ? 176 SER B O 1 ATOM 2267 C CB . SER B 2 176 ? 5.358 75.164 -32.278 1.00 14.14 ? ? ? ? ? ? 176 SER B CB 1 ATOM 2268 O OG . SER B 2 176 ? 4.137 75.662 -32.658 1.00 7.94 ? ? ? ? ? ? 176 SER B OG 1 ATOM 2269 N N . SER B 2 177 ? 5.427 77.594 -33.519 1.00 10.45 ? ? ? ? ? ? 177 SER B N 1 ATOM 2270 C CA . SER B 2 177 ? 5.393 79.010 -33.915 1.00 12.73 ? ? ? ? ? ? 177 SER B CA 1 ATOM 2271 C C . SER B 2 177 ? 4.541 79.885 -32.965 1.00 12.63 ? ? ? ? ? ? 177 SER B C 1 ATOM 2272 O O . SER B 2 177 ? 3.448 79.464 -32.507 1.00 11.87 ? ? ? ? ? ? 177 SER B O 1 ATOM 2273 C CB . SER B 2 177 ? 4.833 79.114 -35.350 1.00 12.31 ? ? ? ? ? ? 177 SER B CB 1 ATOM 2274 O OG . SER B 2 177 ? 5.052 80.370 -35.936 1.00 11.70 ? ? ? ? ? ? 177 SER B OG 1 ATOM 2275 N N . PRO B 2 178 ? 5.080 81.076 -32.644 1.00 12.02 ? ? ? ? ? ? 178 PRO B N 1 ATOM 2276 C CA . PRO B 2 178 ? 4.547 82.091 -31.802 1.00 9.04 ? ? ? ? ? ? 178 PRO B CA 1 ATOM 2277 C C . PRO B 2 178 ? 3.199 82.494 -32.270 1.00 8.64 ? ? ? ? ? ? 178 PRO B C 1 ATOM 2278 O O . PRO B 2 178 ? 2.496 83.197 -31.526 1.00 10.15 ? ? ? ? ? ? 178 PRO B O 1 ATOM 2279 C CB . PRO B 2 178 ? 5.504 83.279 -32.044 1.00 6.82 ? ? ? ? ? ? 178 PRO B CB 1 ATOM 2280 C CG . PRO B 2 178 ? 6.732 82.693 -32.542 1.00 10.75 ? ? ? ? ? ? 178 PRO B CG 1 ATOM 2281 C CD . PRO B 2 178 ? 6.362 81.497 -33.266 1.00 10.69 ? ? ? ? ? ? 178 PRO B CD 1 ATOM 2282 N N . TYR B 2 179 ? 2.828 82.127 -33.485 1.00 8.35 ? ? ? ? ? ? 179 TYR B N 1 ATOM 2283 C CA . TYR B 2 179 ? 1.535 82.531 -34.083 1.00 7.55 ? ? ? ? ? ? 179 TYR B CA 1 ATOM 2284 C C . TYR B 2 179 ? 0.545 81.338 -34.147 1.00 9.22 ? ? ? ? ? ? 179 TYR B C 1 ATOM 2285 O O . TYR B 2 179 ? 0.978 80.119 -34.091 1.00 7.45 ? ? ? ? ? ? 179 TYR B O 1 ATOM 2286 C CB . TYR B 2 179 ? 1.749 83.185 -35.439 1.00 7.94 ? ? ? ? ? ? 179 TYR B CB 1 ATOM 2287 C CG . TYR B 2 179 ? 2.835 84.308 -35.407 1.00 9.55 ? ? ? ? ? ? 179 TYR B CG 1 ATOM 2288 C CD1 . TYR B 2 179 ? 4.125 84.015 -35.696 1.00 4.63 ? ? ? ? ? ? 179 TYR B CD1 1 ATOM 2289 C CD2 . TYR B 2 179 ? 2.489 85.691 -35.052 1.00 5.68 ? ? ? ? ? ? 179 TYR B CD2 1 ATOM 2290 C CE1 . TYR B 2 179 ? 5.148 85.040 -35.661 1.00 9.84 ? ? ? ? ? ? 179 TYR B CE1 1 ATOM 2291 C CE2 . TYR B 2 179 ? 3.437 86.672 -35.060 1.00 10.92 ? ? ? ? ? ? 179 TYR B CE2 1 ATOM 2292 C CZ . TYR B 2 179 ? 4.731 86.347 -35.363 1.00 7.69 ? ? ? ? ? ? 179 TYR B CZ 1 ATOM 2293 O OH . TYR B 2 179 ? 5.601 87.296 -35.362 1.00 11.82 ? ? ? ? ? ? 179 TYR B OH 1 ATOM 2294 N N . GLU B 2 180 ? -0.758 81.659 -34.154 1.00 7.58 ? ? ? ? ? ? 180 GLU B N 1 ATOM 2295 C CA . GLU B 2 180 ? -1.771 80.611 -34.103 1.00 8.20 ? ? ? ? ? ? 180 GLU B CA 1 ATOM 2296 C C . GLU B 2 180 ? -2.225 80.392 -35.524 1.00 9.69 ? ? ? ? ? ? 180 GLU B C 1 ATOM 2297 O O . GLU B 2 180 ? -2.495 79.213 -35.937 1.00 12.55 ? ? ? ? ? ? 180 GLU B O 1 ATOM 2298 C CB . GLU B 2 180 ? -2.968 81.073 -33.226 1.00 9.88 ? ? ? ? ? ? 180 GLU B CB 1 ATOM 2299 C CG . GLU B 2 180 ? -4.214 80.055 -33.074 1.00 7.74 ? ? ? ? ? ? 180 GLU B CG 1 ATOM 2300 C CD . GLU B 2 180 ? -3.815 78.698 -32.652 1.00 14.00 ? ? ? ? ? ? 180 GLU B CD 1 ATOM 2301 O OE1 . GLU B 2 180 ? -4.718 77.859 -32.381 1.00 13.19 ? ? ? ? ? ? 180 GLU B OE1 1 ATOM 2302 O OE2 . GLU B 2 180 ? -2.594 78.441 -32.539 1.00 14.28 ? ? ? ? ? ? 180 GLU B OE2 1 ATOM 2303 N N . THR B 2 181 ? -2.340 81.495 -36.291 1.00 7.35 ? ? ? ? ? ? 181 THR B N 1 ATOM 2304 C CA . THR B 2 181 ? -2.758 81.443 -37.668 1.00 5.80 ? ? ? ? ? ? 181 THR B CA 1 ATOM 2305 C C . THR B 2 181 ? -2.063 82.479 -38.501 1.00 8.40 ? ? ? ? ? ? 181 THR B C 1 ATOM 2306 O O . THR B 2 181 ? -1.553 83.505 -37.992 1.00 8.91 ? ? ? ? ? ? 181 THR B O 1 ATOM 2307 C CB . THR B 2 181 ? -4.217 81.805 -37.857 1.00 6.75 ? ? ? ? ? ? 181 THR B CB 1 ATOM 2308 O OG1 . THR B 2 181 ? -4.375 83.227 -37.709 1.00 3.57 ? ? ? ? ? ? 181 THR B OG1 1 ATOM 2309 C CG2 . THR B 2 181 ? -5.036 81.183 -36.781 1.00 9.08 ? ? ? ? ? ? 181 THR B CG2 1 ATOM 2310 N N . GLY B 2 182 ? -2.142 82.311 -39.822 1.00 10.56 ? ? ? ? ? ? 182 GLY B N 1 ATOM 2311 C CA . GLY B 2 182 ? -1.544 83.286 -40.758 1.00 10.08 ? ? ? ? ? ? 182 GLY B CA 1 ATOM 2312 C C . GLY B 2 182 ? -1.610 82.947 -42.226 1.00 9.33 ? ? ? ? ? ? 182 GLY B C 1 ATOM 2313 O O . GLY B 2 182 ? -1.493 81.779 -42.637 1.00 11.90 ? ? ? ? ? ? 182 GLY B O 1 ATOM 2314 N N . TYR B 2 183 ? -1.868 83.965 -43.020 1.00 10.65 ? ? ? ? ? ? 183 TYR B N 1 ATOM 2315 C CA . TYR B 2 183 ? -2.120 83.795 -44.454 1.00 9.89 ? ? ? ? ? ? 183 TYR B CA 1 ATOM 2316 C C . TYR B 2 183 ? -1.543 84.942 -45.226 1.00 8.57 ? ? ? ? ? ? 183 TYR B C 1 ATOM 2317 O O . TYR B 2 183 ? -1.530 86.077 -44.750 1.00 9.83 ? ? ? ? ? ? 183 TYR B O 1 ATOM 2318 C CB . TYR B 2 183 ? -3.624 83.631 -44.720 1.00 9.39 ? ? ? ? ? ? 183 TYR B CB 1 ATOM 2319 C CG . TYR B 2 183 ? -4.399 84.770 -44.286 1.00 8.52 ? ? ? ? ? ? 183 TYR B CG 1 ATOM 2320 C CD1 . TYR B 2 183 ? -4.479 85.875 -45.086 1.00 11.80 ? ? ? ? ? ? 183 TYR B CD1 1 ATOM 2321 C CD2 . TYR B 2 183 ? -5.080 84.771 -43.095 1.00 10.88 ? ? ? ? ? ? 183 TYR B CD2 1 ATOM 2322 C CE1 . TYR B 2 183 ? -5.115 86.953 -44.720 1.00 6.52 ? ? ? ? ? ? 183 TYR B CE1 1 ATOM 2323 C CE2 . TYR B 2 183 ? -5.779 85.899 -42.704 1.00 12.75 ? ? ? ? ? ? 183 TYR B CE2 1 ATOM 2324 C CZ . TYR B 2 183 ? -5.731 87.021 -43.535 1.00 11.06 ? ? ? ? ? ? 183 TYR B CZ 1 ATOM 2325 O OH . TYR B 2 183 ? -6.374 88.211 -43.253 1.00 7.67 ? ? ? ? ? ? 183 TYR B OH 1 ATOM 2326 N N . ILE B 2 184 ? -1.031 84.654 -46.405 1.00 9.90 ? ? ? ? ? ? 184 ILE B N 1 ATOM 2327 C CA . ILE B 2 184 ? -0.388 85.700 -47.205 1.00 10.65 ? ? ? ? ? ? 184 ILE B CA 1 ATOM 2328 C C . ILE B 2 184 ? -1.317 86.012 -48.368 1.00 11.31 ? ? ? ? ? ? 184 ILE B C 1 ATOM 2329 O O . ILE B 2 184 ? -1.555 85.121 -49.199 1.00 11.43 ? ? ? ? ? ? 184 ILE B O 1 ATOM 2330 C CB . ILE B 2 184 ? 1.035 85.376 -47.623 1.00 9.55 ? ? ? ? ? ? 184 ILE B CB 1 ATOM 2331 C CG1 . ILE B 2 184 ? 1.540 86.523 -48.481 1.00 11.59 ? ? ? ? ? ? 184 ILE B CG1 1 ATOM 2332 C CG2 . ILE B 2 184 ? 1.133 84.079 -48.420 1.00 7.45 ? ? ? ? ? ? 184 ILE B CG2 1 ATOM 2333 C CD1 . ILE B 2 184 ? 3.055 86.502 -48.734 1.00 2.00 ? ? ? ? ? ? 184 ILE B CD1 1 ATOM 2334 N N . LYS B 2 185 ? -1.922 87.214 -48.352 1.00 11.47 ? ? ? ? ? ? 185 LYS B N 1 ATOM 2335 C CA . LYS B 2 185 ? -2.835 87.668 -49.404 1.00 10.17 ? ? ? ? ? ? 185 LYS B CA 1 ATOM 2336 C C . LYS B 2 185 ? -2.159 88.672 -50.310 1.00 10.31 ? ? ? ? ? ? 185 LYS B C 1 ATOM 2337 O O . LYS B 2 185 ? -1.532 89.563 -49.758 1.00 9.95 ? ? ? ? ? ? 185 LYS B O 1 ATOM 2338 C CB . LYS B 2 185 ? -4.051 88.357 -48.798 1.00 9.79 ? ? ? ? ? ? 185 LYS B CB 1 ATOM 2339 C CG . LYS B 2 185 ? -4.768 89.267 -49.747 1.00 6.30 ? ? ? ? ? ? 185 LYS B CG 1 ATOM 2340 C CD . LYS B 2 185 ? -5.563 90.327 -48.982 1.00 10.91 ? ? ? ? ? ? 185 LYS B CD 1 ATOM 2341 C CE . LYS B 2 185 ? -6.862 89.796 -48.284 1.00 7.86 ? ? ? ? ? ? 185 LYS B CE 1 ATOM 2342 N NZ . LYS B 2 185 ? -7.989 89.703 -49.318 1.00 5.30 ? ? ? ? ? ? 185 LYS B NZ 1 ATOM 2343 N N . PHE B 2 186 ? -2.414 88.522 -51.635 1.00 9.12 ? ? ? ? ? ? 186 PHE B N 1 ATOM 2344 C CA . PHE B 2 186 ? -1.964 89.335 -52.784 1.00 10.62 ? ? ? ? ? ? 186 PHE B CA 1 ATOM 2345 C C . PHE B 2 186 ? -3.098 90.156 -53.455 1.00 12.24 ? ? ? ? ? ? 186 PHE B C 1 ATOM 2346 O O . PHE B 2 186 ? -4.298 89.748 -53.549 1.00 10.76 ? ? ? ? ? ? 186 PHE B O 1 ATOM 2347 C CB . PHE B 2 186 ? -1.213 88.516 -53.906 1.00 9.75 ? ? ? ? ? ? 186 PHE B CB 1 ATOM 2348 C CG . PHE B 2 186 ? 0.022 87.762 -53.438 1.00 9.80 ? ? ? ? ? ? 186 PHE B CG 1 ATOM 2349 C CD1 . PHE B 2 186 ? -0.134 86.622 -52.682 1.00 11.65 ? ? ? ? ? ? 186 PHE B CD1 1 ATOM 2350 C CD2 . PHE B 2 186 ? 1.306 88.160 -53.817 1.00 3.11 ? ? ? ? ? ? 186 PHE B CD2 1 ATOM 2351 C CE1 . PHE B 2 186 ? 0.994 85.877 -52.255 1.00 16.27 ? ? ? ? ? ? 186 PHE B CE1 1 ATOM 2352 C CE2 . PHE B 2 186 ? 2.389 87.450 -53.410 1.00 15.26 ? ? ? ? ? ? 186 PHE B CE2 1 ATOM 2353 C CZ . PHE B 2 186 ? 2.244 86.292 -52.600 1.00 6.63 ? ? ? ? ? ? 186 PHE B CZ 1 ATOM 2354 N N . ILE B 2 187 ? -2.700 91.335 -53.942 1.00 11.90 ? ? ? ? ? ? 187 ILE B N 1 ATOM 2355 C CA . ILE B 2 187 ? -3.582 92.250 -54.580 1.00 12.57 ? ? ? ? ? ? 187 ILE B CA 1 ATOM 2356 C C . ILE B 2 187 ? -3.041 92.600 -55.941 1.00 14.79 ? ? ? ? ? ? 187 ILE B C 1 ATOM 2357 O O . ILE B 2 187 ? -1.846 93.039 -56.077 1.00 16.42 ? ? ? ? ? ? 187 ILE B O 1 ATOM 2358 C CB . ILE B 2 187 ? -3.715 93.431 -53.735 1.00 13.01 ? ? ? ? ? ? 187 ILE B CB 1 ATOM 2359 C CG1 . ILE B 2 187 ? -4.226 93.007 -52.311 1.00 16.00 ? ? ? ? ? ? 187 ILE B CG1 1 ATOM 2360 C CG2 . ILE B 2 187 ? -4.758 94.386 -54.373 1.00 15.42 ? ? ? ? ? ? 187 ILE B CG2 1 ATOM 2361 C CD1 . ILE B 2 187 ? -4.528 94.141 -51.308 1.00 10.51 ? ? ? ? ? ? 187 ILE B CD1 1 ATOM 2362 N N . GLU B 2 188 ? -3.836 92.355 -56.982 1.00 15.05 ? ? ? ? ? ? 188 GLU B N 1 ATOM 2363 C CA . GLU B 2 188 ? -3.408 92.707 -58.334 1.00 14.95 ? ? ? ? ? ? 188 GLU B CA 1 ATOM 2364 C C . GLU B 2 188 ? -4.027 94.071 -58.816 1.00 19.36 ? ? ? ? ? ? 188 GLU B C 1 ATOM 2365 O O . GLU B 2 188 ? -5.206 94.374 -58.606 1.00 18.43 ? ? ? ? ? ? 188 GLU B O 1 ATOM 2366 C CB . GLU B 2 188 ? -3.804 91.576 -59.273 1.00 17.01 ? ? ? ? ? ? 188 GLU B CB 1 ATOM 2367 C CG . GLU B 2 188 ? -2.806 90.476 -59.373 1.00 12.13 ? ? ? ? ? ? 188 GLU B CG 1 ATOM 2368 C CD . GLU B 2 188 ? -3.221 89.365 -60.378 1.00 13.05 ? ? ? ? ? ? 188 GLU B CD 1 ATOM 2369 O OE1 . GLU B 2 188 ? -4.321 88.737 -60.229 1.00 10.21 ? ? ? ? ? ? 188 GLU B OE1 1 ATOM 2370 O OE2 . GLU B 2 188 ? -2.443 89.176 -61.327 1.00 10.67 ? ? ? ? ? ? 188 GLU B OE2 1 ATOM 2371 N N . ASN B 2 189 ? -3.182 94.892 -59.418 1.00 19.45 ? ? ? ? ? ? 189 ASN B N 1 ATOM 2372 C CA . ASN B 2 189 ? -3.527 96.195 -59.949 1.00 20.35 ? ? ? ? ? ? 189 ASN B CA 1 ATOM 2373 C C . ASN B 2 189 ? -4.976 96.278 -60.436 1.00 20.82 ? ? ? ? ? ? 189 ASN B C 1 ATOM 2374 O O . ASN B 2 189 ? -5.691 97.232 -60.105 1.00 20.40 ? ? ? ? ? ? 189 ASN B O 1 ATOM 2375 C CB . ASN B 2 189 ? -2.462 96.539 -61.019 1.00 20.40 ? ? ? ? ? ? 189 ASN B CB 1 ATOM 2376 C CG . ASN B 2 189 ? -2.371 97.982 -61.313 1.00 22.90 ? ? ? ? ? ? 189 ASN B CG 1 ATOM 2377 O OD1 . ASN B 2 189 ? -1.446 98.399 -62.053 1.00 19.48 ? ? ? ? ? ? 189 ASN B OD1 1 ATOM 2378 N ND2 . ASN B 2 189 ? -3.348 98.783 -60.807 1.00 20.53 ? ? ? ? ? ? 189 ASN B ND2 1 ATOM 2379 N N . ASN B 2 190 ? -5.448 95.201 -61.065 1.00 22.20 ? ? ? ? ? ? 190 ASN B N 1 ATOM 2380 C CA . ASN B 2 190 ? -6.825 95.098 -61.558 1.00 24.24 ? ? ? ? ? ? 190 ASN B CA 1 ATOM 2381 C C . ASN B 2 190 ? -7.914 95.023 -60.459 1.00 24.69 ? ? ? ? ? ? 190 ASN B C 1 ATOM 2382 O O . ASN B 2 190 ? -9.077 95.542 -60.629 1.00 25.12 ? ? ? ? ? ? 190 ASN B O 1 ATOM 2383 C CB . ASN B 2 190 ? -6.974 93.922 -62.575 1.00 22.98 ? ? ? ? ? ? 190 ASN B CB 1 ATOM 2384 C CG . ASN B 2 190 ? -6.899 92.603 -61.943 1.00 24.78 ? ? ? ? ? ? 190 ASN B CG 1 ATOM 2385 O OD1 . ASN B 2 190 ? -7.526 92.379 -60.912 1.00 22.45 ? ? ? ? ? ? 190 ASN B OD1 1 ATOM 2386 N ND2 . ASN B 2 190 ? -6.111 91.662 -62.565 1.00 29.35 ? ? ? ? ? ? 190 ASN B ND2 1 ATOM 2387 N N . GLY B 2 191 ? -7.535 94.384 -59.353 1.00 23.82 ? ? ? ? ? ? 191 GLY B N 1 ATOM 2388 C CA . GLY B 2 191 ? -8.432 94.063 -58.212 1.00 23.15 ? ? ? ? ? ? 191 GLY B CA 1 ATOM 2389 C C . GLY B 2 191 ? -8.493 92.564 -57.899 1.00 22.31 ? ? ? ? ? ? 191 GLY B C 1 ATOM 2390 O O . GLY B 2 191 ? -9.385 92.085 -57.250 1.00 22.97 ? ? ? ? ? ? 191 GLY B O 1 ATOM 2391 N N . ASN B 2 192 ? -7.533 91.811 -58.346 1.00 21.65 ? ? ? ? ? ? 192 ASN B N 1 ATOM 2392 C CA . ASN B 2 192 ? -7.634 90.412 -58.000 1.00 22.72 ? ? ? ? ? ? 192 ASN B CA 1 ATOM 2393 C C . ASN B 2 192 ? -6.888 90.259 -56.722 1.00 21.77 ? ? ? ? ? ? 192 ASN B C 1 ATOM 2394 O O . ASN B 2 192 ? -5.828 90.871 -56.502 1.00 22.82 ? ? ? ? ? ? 192 ASN B O 1 ATOM 2395 C CB . ASN B 2 192 ? -7.213 89.485 -59.140 1.00 22.16 ? ? ? ? ? ? 192 ASN B CB 1 ATOM 2396 C CG . ASN B 2 192 ? -7.340 88.019 -58.780 1.00 23.83 ? ? ? ? ? ? 192 ASN B CG 1 ATOM 2397 O OD1 . ASN B 2 192 ? -8.445 87.499 -58.582 1.00 28.16 ? ? ? ? ? ? 192 ASN B OD1 1 ATOM 2398 N ND2 . ASN B 2 192 ? -6.202 87.341 -58.688 1.00 15.99 ? ? ? ? ? ? 192 ASN B ND2 1 ATOM 2399 N N . THR B 2 193 ? -7.516 89.556 -55.813 1.00 22.25 ? ? ? ? ? ? 193 THR B N 1 ATOM 2400 C CA . THR B 2 193 ? -6.939 89.344 -54.528 1.00 23.00 ? ? ? ? ? ? 193 THR B CA 1 ATOM 2401 C C . THR B 2 193 ? -7.088 87.890 -54.172 1.00 22.98 ? ? ? ? ? ? 193 THR B C 1 ATOM 2402 O O . THR B 2 193 ? -8.237 87.347 -54.187 1.00 23.92 ? ? ? ? ? ? 193 THR B O 1 ATOM 2403 C CB . THR B 2 193 ? -7.653 90.154 -53.441 1.00 24.01 ? ? ? ? ? ? 193 THR B CB 1 ATOM 2404 O OG1 . THR B 2 193 ? -9.071 89.922 -53.495 1.00 27.20 ? ? ? ? ? ? 193 THR B OG1 1 ATOM 2405 C CG2 . THR B 2 193 ? -7.330 91.673 -53.524 1.00 25.14 ? ? ? ? ? ? 193 THR B CG2 1 ATOM 2406 N N . PHE B 2 194 ? -5.977 87.264 -53.775 1.00 20.38 ? ? ? ? ? ? 194 PHE B N 1 ATOM 2407 C CA . PHE B 2 194 ? -6.001 85.844 -53.397 1.00 19.18 ? ? ? ? ? ? 194 PHE B CA 1 ATOM 2408 C C . PHE B 2 194 ? -5.067 85.592 -52.208 1.00 18.89 ? ? ? ? ? ? 194 PHE B C 1 ATOM 2409 O O . PHE B 2 194 ? -4.134 86.334 -51.997 1.00 21.99 ? ? ? ? ? ? 194 PHE B O 1 ATOM 2410 C CB . PHE B 2 194 ? -5.628 84.944 -54.586 1.00 17.29 ? ? ? ? ? ? 194 PHE B CB 1 ATOM 2411 C CG . PHE B 2 194 ? -4.247 85.218 -55.194 1.00 18.77 ? ? ? ? ? ? 194 PHE B CG 1 ATOM 2412 C CD1 . PHE B 2 194 ? -3.169 84.380 -54.924 1.00 12.76 ? ? ? ? ? ? 194 PHE B CD1 1 ATOM 2413 C CD2 . PHE B 2 194 ? -4.047 86.286 -56.084 1.00 13.96 ? ? ? ? ? ? 194 PHE B CD2 1 ATOM 2414 C CE1 . PHE B 2 194 ? -1.951 84.623 -55.515 1.00 11.06 ? ? ? ? ? ? 194 PHE B CE1 1 ATOM 2415 C CE2 . PHE B 2 194 ? -2.787 86.529 -56.635 1.00 12.71 ? ? ? ? ? ? 194 PHE B CE2 1 ATOM 2416 C CZ . PHE B 2 194 ? -1.763 85.671 -56.366 1.00 8.39 ? ? ? ? ? ? 194 PHE B CZ 1 ATOM 2417 N N . TRP B 2 195 ? -5.338 84.619 -51.381 1.00 17.64 ? ? ? ? ? ? 195 TRP B N 1 ATOM 2418 C CA . TRP B 2 195 ? -4.539 84.404 -50.150 1.00 16.18 ? ? ? ? ? ? 195 TRP B CA 1 ATOM 2419 C C . TRP B 2 195 ? -4.153 82.918 -50.037 1.00 15.37 ? ? ? ? ? ? 195 TRP B C 1 ATOM 2420 O O . TRP B 2 195 ? -4.823 82.064 -50.592 1.00 17.63 ? ? ? ? ? ? 195 TRP B O 1 ATOM 2421 C CB . TRP B 2 195 ? -5.301 84.892 -48.904 1.00 15.52 ? ? ? ? ? ? 195 TRP B CB 1 ATOM 2422 C CG . TRP B 2 195 ? -6.663 84.153 -48.565 1.00 13.57 ? ? ? ? ? ? 195 TRP B CG 1 ATOM 2423 C CD1 . TRP B 2 195 ? -7.938 84.485 -48.996 1.00 16.11 ? ? ? ? ? ? 195 TRP B CD1 1 ATOM 2424 C CD2 . TRP B 2 195 ? -6.810 83.005 -47.748 1.00 13.94 ? ? ? ? ? ? 195 TRP B CD2 1 ATOM 2425 N NE1 . TRP B 2 195 ? -8.883 83.587 -48.487 1.00 12.09 ? ? ? ? ? ? 195 TRP B NE1 1 ATOM 2426 C CE2 . TRP B 2 195 ? -8.210 82.663 -47.730 1.00 11.99 ? ? ? ? ? ? 195 TRP B CE2 1 ATOM 2427 C CE3 . TRP B 2 195 ? -5.912 82.179 -47.097 1.00 11.60 ? ? ? ? ? ? 195 TRP B CE3 1 ATOM 2428 C CZ2 . TRP B 2 195 ? -8.672 81.627 -47.067 1.00 11.51 ? ? ? ? ? ? 195 TRP B CZ2 1 ATOM 2429 C CZ3 . TRP B 2 195 ? -6.395 81.122 -46.421 1.00 17.58 ? ? ? ? ? ? 195 TRP B CZ3 1 ATOM 2430 C CH2 . TRP B 2 195 ? -7.790 80.877 -46.369 1.00 14.64 ? ? ? ? ? ? 195 TRP B CH2 1 ATOM 2431 N N . TYR B 2 196 ? -3.187 82.614 -49.215 1.00 14.57 ? ? ? ? ? ? 196 TYR B N 1 ATOM 2432 C CA . TYR B 2 196 ? -2.660 81.260 -49.076 1.00 12.19 ? ? ? ? ? ? 196 TYR B CA 1 ATOM 2433 C C . TYR B 2 196 ? -2.391 81.016 -47.588 1.00 13.35 ? ? ? ? ? ? 196 TYR B C 1 ATOM 2434 O O . TYR B 2 196 ? -1.703 81.832 -46.938 1.00 13.23 ? ? ? ? ? ? 196 TYR B O 1 ATOM 2435 C CB . TYR B 2 196 ? -1.325 81.064 -49.838 1.00 12.78 ? ? ? ? ? ? 196 TYR B CB 1 ATOM 2436 C CG . TYR B 2 196 ? -1.362 81.122 -51.385 1.00 11.28 ? ? ? ? ? ? 196 TYR B CG 1 ATOM 2437 C CD1 . TYR B 2 196 ? -0.232 81.508 -52.105 1.00 7.94 ? ? ? ? ? ? 196 TYR B CD1 1 ATOM 2438 C CD2 . TYR B 2 196 ? -2.517 80.777 -52.105 1.00 10.80 ? ? ? ? ? ? 196 TYR B CD2 1 ATOM 2439 C CE1 . TYR B 2 196 ? -0.243 81.564 -53.451 1.00 9.77 ? ? ? ? ? ? 196 TYR B CE1 1 ATOM 2440 C CE2 . TYR B 2 196 ? -2.571 80.869 -53.487 1.00 8.96 ? ? ? ? ? ? 196 TYR B CE2 1 ATOM 2441 C CZ . TYR B 2 196 ? -1.388 81.261 -54.156 1.00 14.65 ? ? ? ? ? ? 196 TYR B CZ 1 ATOM 2442 O OH . TYR B 2 196 ? -1.393 81.334 -55.542 1.00 12.98 ? ? ? ? ? ? 196 TYR B OH 1 ATOM 2443 N N . ASP B 2 197 ? -2.894 79.903 -47.033 1.00 11.14 ? ? ? ? ? ? 197 ASP B N 1 ATOM 2444 C CA . ASP B 2 197 ? -2.708 79.655 -45.619 1.00 11.60 ? ? ? ? ? ? 197 ASP B CA 1 ATOM 2445 C C . ASP B 2 197 ? -1.246 79.357 -45.326 1.00 11.07 ? ? ? ? ? ? 197 ASP B C 1 ATOM 2446 O O . ASP B 2 197 ? -0.588 78.761 -46.133 1.00 12.24 ? ? ? ? ? ? 197 ASP B O 1 ATOM 2447 C CB . ASP B 2 197 ? -3.616 78.517 -45.132 1.00 10.08 ? ? ? ? ? ? 197 ASP B CB 1 ATOM 2448 C CG . ASP B 2 197 ? -3.393 78.176 -43.664 1.00 14.64 ? ? ? ? ? ? 197 ASP B CG 1 ATOM 2449 O OD1 . ASP B 2 197 ? -2.209 78.129 -43.204 1.00 19.92 ? ? ? ? ? ? 197 ASP B OD1 1 ATOM 2450 O OD2 . ASP B 2 197 ? -4.376 77.867 -42.955 1.00 18.48 ? ? ? ? ? ? 197 ASP B OD2 1 ATOM 2451 N N . MET B 2 198 ? -0.742 79.757 -44.170 1.00 12.07 ? ? ? ? ? ? 198 MET B N 1 ATOM 2452 C CA . MET B 2 198 ? 0.727 79.527 -43.850 1.00 11.16 ? ? ? ? ? ? 198 MET B CA 1 ATOM 2453 C C . MET B 2 198 ? 0.926 78.434 -42.884 1.00 11.82 ? ? ? ? ? ? 198 MET B C 1 ATOM 2454 O O . MET B 2 198 ? 2.065 77.960 -42.729 1.00 9.95 ? ? ? ? ? ? 198 MET B O 1 ATOM 2455 C CB . MET B 2 198 ? 1.388 80.779 -43.383 1.00 7.16 ? ? ? ? ? ? 198 MET B CB 1 ATOM 2456 C CG . MET B 2 198 ? 0.996 81.883 -44.351 1.00 8.30 ? ? ? ? ? ? 198 MET B CG 1 ATOM 2457 S SD . MET B 2 198 ? 1.492 83.513 -43.744 1.00 9.06 ? ? ? ? ? ? 198 MET B SD 1 ATOM 2458 C CE . MET B 2 198 ? 3.287 83.563 -43.783 1.00 2.00 ? ? ? ? ? ? 198 MET B CE 1 ATOM 2459 N N . MET B 2 199 ? -0.184 78.031 -42.249 1.00 12.91 ? ? ? ? ? ? 199 MET B N 1 ATOM 2460 C CA . MET B 2 199 ? -0.064 77.067 -41.224 1.00 15.02 ? ? ? ? ? ? 199 MET B CA 1 ATOM 2461 C C . MET B 2 199 ? -0.478 75.681 -41.652 1.00 16.65 ? ? ? ? ? ? 199 MET B C 1 ATOM 2462 O O . MET B 2 199 ? -1.454 75.492 -42.412 1.00 19.44 ? ? ? ? ? ? 199 MET B O 1 ATOM 2463 C CB . MET B 2 199 ? -0.720 77.528 -39.935 1.00 13.49 ? ? ? ? ? ? 199 MET B CB 1 ATOM 2464 C CG . MET B 2 199 ? -0.201 78.796 -39.427 1.00 11.97 ? ? ? ? ? ? 199 MET B CG 1 ATOM 2465 S SD . MET B 2 199 ? 1.350 78.591 -38.589 1.00 13.57 ? ? ? ? ? ? 199 MET B SD 1 ATOM 2466 C CE . MET B 2 199 ? 1.680 80.312 -38.301 1.00 8.73 ? ? ? ? ? ? 199 MET B CE 1 ATOM 2467 N N . PRO B 2 200 ? 0.288 74.679 -41.195 1.00 17.16 ? ? ? ? ? ? 200 PRO B N 1 ATOM 2468 C CA . PRO B 2 200 ? 0.032 73.273 -41.338 1.00 16.01 ? ? ? ? ? ? 200 PRO B CA 1 ATOM 2469 C C . PRO B 2 200 ? -1.377 72.760 -41.071 1.00 17.27 ? ? ? ? ? ? 200 PRO B C 1 ATOM 2470 O O . PRO B 2 200 ? -2.319 73.473 -40.633 1.00 17.12 ? ? ? ? ? ? 200 PRO B O 1 ATOM 2471 C CB . PRO B 2 200 ? 1.001 72.626 -40.355 1.00 16.46 ? ? ? ? ? ? 200 PRO B CB 1 ATOM 2472 C CG . PRO B 2 200 ? 2.214 73.558 -40.387 1.00 14.67 ? ? ? ? ? ? 200 PRO B CG 1 ATOM 2473 C CD . PRO B 2 200 ? 1.551 74.971 -40.464 1.00 17.02 ? ? ? ? ? ? 200 PRO B CD 1 ATOM 2474 N N . ALA B 2 201 ? -1.540 71.493 -41.378 1.00 15.58 ? ? ? ? ? ? 201 ALA B N 1 ATOM 2475 C CA . ALA B 2 201 ? -2.863 70.939 -41.396 1.00 17.17 ? ? ? ? ? ? 201 ALA B CA 1 ATOM 2476 C C . ALA B 2 201 ? -3.114 70.473 -39.966 1.00 18.46 ? ? ? ? ? ? 201 ALA B C 1 ATOM 2477 O O . ALA B 2 201 ? -2.181 69.919 -39.361 1.00 20.88 ? ? ? ? ? ? 201 ALA B O 1 ATOM 2478 C CB . ALA B 2 201 ? -2.815 69.737 -42.273 1.00 17.09 ? ? ? ? ? ? 201 ALA B CB 1 ATOM 2479 N N . PRO B 2 202 ? -4.355 70.567 -39.454 1.00 16.86 ? ? ? ? ? ? 202 PRO B N 1 ATOM 2480 C CA . PRO B 2 202 ? -4.566 70.282 -38.124 1.00 16.02 ? ? ? ? ? ? 202 PRO B CA 1 ATOM 2481 C C . PRO B 2 202 ? -4.383 68.790 -37.988 1.00 16.82 ? ? ? ? ? ? 202 PRO B C 1 ATOM 2482 O O . PRO B 2 202 ? -5.291 68.064 -38.297 1.00 17.69 ? ? ? ? ? ? 202 PRO B O 1 ATOM 2483 C CB . PRO B 2 202 ? -6.027 70.705 -37.918 1.00 12.96 ? ? ? ? ? ? 202 PRO B CB 1 ATOM 2484 C CG . PRO B 2 202 ? -6.672 70.356 -39.075 1.00 13.52 ? ? ? ? ? ? 202 PRO B CG 1 ATOM 2485 C CD . PRO B 2 202 ? -5.649 70.868 -40.091 1.00 20.01 ? ? ? ? ? ? 202 PRO B CD 1 ATOM 2486 N N . GLY B 2 203 ? -3.168 68.355 -37.621 1.00 18.95 ? ? ? ? ? ? 203 GLY B N 1 ATOM 2487 C CA . GLY B 2 203 ? -2.881 66.987 -37.126 1.00 19.31 ? ? ? ? ? ? 203 GLY B CA 1 ATOM 2488 C C . GLY B 2 203 ? -1.470 66.626 -36.655 1.00 20.74 ? ? ? ? ? ? 203 GLY B C 1 ATOM 2489 O O . GLY B 2 203 ? -0.637 67.490 -36.252 1.00 21.35 ? ? ? ? ? ? 203 GLY B O 1 ATOM 2490 N N . ASP B 2 204 ? -1.169 65.332 -36.660 1.00 21.37 ? ? ? ? ? ? 204 ASP B N 1 ATOM 2491 C CA . ASP B 2 204 ? 0.117 64.865 -36.115 1.00 22.31 ? ? ? ? ? ? 204 ASP B CA 1 ATOM 2492 C C . ASP B 2 204 ? 1.356 65.057 -36.952 1.00 21.10 ? ? ? ? ? ? 204 ASP B C 1 ATOM 2493 O O . ASP B 2 204 ? 2.421 65.302 -36.395 1.00 20.39 ? ? ? ? ? ? 204 ASP B O 1 ATOM 2494 C CB . ASP B 2 204 ? 0.038 63.364 -35.820 1.00 23.43 ? ? ? ? ? ? 204 ASP B CB 1 ATOM 2495 C CG . ASP B 2 204 ? 1.406 62.788 -35.466 1.00 29.29 ? ? ? ? ? ? 204 ASP B CG 1 ATOM 2496 O OD1 . ASP B 2 204 ? 2.103 63.400 -34.634 1.00 25.43 ? ? ? ? ? ? 204 ASP B OD1 1 ATOM 2497 O OD2 . ASP B 2 204 ? 1.788 61.713 -36.016 1.00 35.50 ? ? ? ? ? ? 204 ASP B OD2 1 ATOM 2498 N N . LYS B 2 205 ? 1.253 64.780 -38.266 1.00 21.26 ? ? ? ? ? ? 205 LYS B N 1 ATOM 2499 C CA . LYS B 2 205 ? 2.385 64.893 -39.228 1.00 19.07 ? ? ? ? ? ? 205 LYS B CA 1 ATOM 2500 C C . LYS B 2 205 ? 2.184 65.936 -40.311 1.00 16.65 ? ? ? ? ? ? 205 LYS B C 1 ATOM 2501 O O . LYS B 2 205 ? 1.121 66.441 -40.483 1.00 14.45 ? ? ? ? ? ? 205 LYS B O 1 ATOM 2502 C CB . LYS B 2 205 ? 2.831 63.549 -39.839 1.00 20.05 ? ? ? ? ? ? 205 LYS B CB 1 ATOM 2503 C CG . LYS B 2 205 ? 1.670 62.561 -40.116 1.00 24.18 ? ? ? ? ? ? 205 LYS B CG 1 ATOM 2504 C CD . LYS B 2 205 ? 1.331 61.766 -38.850 1.00 21.21 ? ? ? ? ? ? 205 LYS B CD 1 ATOM 2505 C CE . LYS B 2 205 ? 0.100 60.838 -39.050 1.00 23.66 ? ? ? ? ? ? 205 LYS B CE 1 ATOM 2506 N NZ . LYS B 2 205 ? 0.010 59.948 -37.824 1.00 18.16 ? ? ? ? ? ? 205 LYS B NZ 1 ATOM 2507 N N . PHE B 2 206 ? 3.242 66.235 -41.061 1.00 14.82 ? ? ? ? ? ? 206 PHE B N 1 ATOM 2508 C CA . PHE B 2 206 ? 3.137 67.215 -42.131 1.00 13.57 ? ? ? ? ? ? 206 PHE B CA 1 ATOM 2509 C C . PHE B 2 206 ? 3.690 66.705 -43.463 1.00 13.13 ? ? ? ? ? ? 206 PHE B C 1 ATOM 2510 O O . PHE B 2 206 ? 4.897 66.556 -43.586 1.00 14.61 ? ? ? ? ? ? 206 PHE B O 1 ATOM 2511 C CB . PHE B 2 206 ? 3.972 68.471 -41.702 1.00 11.00 ? ? ? ? ? ? 206 PHE B CB 1 ATOM 2512 C CG . PHE B 2 206 ? 4.048 69.531 -42.709 1.00 10.52 ? ? ? ? ? ? 206 PHE B CG 1 ATOM 2513 C CD1 . PHE B 2 206 ? 2.886 70.012 -43.328 1.00 5.52 ? ? ? ? ? ? 206 PHE B CD1 1 ATOM 2514 C CD2 . PHE B 2 206 ? 5.278 70.093 -43.038 1.00 8.57 ? ? ? ? ? ? 206 PHE B CD2 1 ATOM 2515 C CE1 . PHE B 2 206 ? 2.972 71.070 -44.134 1.00 9.40 ? ? ? ? ? ? 206 PHE B CE1 1 ATOM 2516 C CE2 . PHE B 2 206 ? 5.354 71.122 -43.857 1.00 5.77 ? ? ? ? ? ? 206 PHE B CE2 1 ATOM 2517 C CZ . PHE B 2 206 ? 4.172 71.631 -44.437 1.00 4.76 ? ? ? ? ? ? 206 PHE B CZ 1 ATOM 2518 N N . ASP B 2 207 ? 2.852 66.444 -44.474 1.00 14.31 ? ? ? ? ? ? 207 ASP B N 1 ATOM 2519 C CA . ASP B 2 207 ? 3.382 66.066 -45.781 1.00 12.10 ? ? ? ? ? ? 207 ASP B CA 1 ATOM 2520 C C . ASP B 2 207 ? 3.919 67.366 -46.431 1.00 13.28 ? ? ? ? ? ? 207 ASP B C 1 ATOM 2521 O O . ASP B 2 207 ? 3.152 68.192 -46.951 1.00 11.62 ? ? ? ? ? ? 207 ASP B O 1 ATOM 2522 C CB . ASP B 2 207 ? 2.239 65.477 -46.568 1.00 11.84 ? ? ? ? ? ? 207 ASP B CB 1 ATOM 2523 C CG . ASP B 2 207 ? 2.604 65.072 -47.969 1.00 14.12 ? ? ? ? ? ? 207 ASP B CG 1 ATOM 2524 O OD1 . ASP B 2 207 ? 3.819 65.021 -48.280 1.00 20.54 ? ? ? ? ? ? 207 ASP B OD1 1 ATOM 2525 O OD2 . ASP B 2 207 ? 1.653 64.838 -48.794 1.00 16.80 ? ? ? ? ? ? 207 ASP B OD2 1 ATOM 2526 N N . GLN B 2 208 ? 5.249 67.519 -46.462 1.00 12.94 ? ? ? ? ? ? 208 GLN B N 1 ATOM 2527 C CA . GLN B 2 208 ? 5.846 68.678 -47.079 1.00 12.07 ? ? ? ? ? ? 208 GLN B CA 1 ATOM 2528 C C . GLN B 2 208 ? 5.292 68.909 -48.441 1.00 14.28 ? ? ? ? ? ? 208 GLN B C 1 ATOM 2529 O O . GLN B 2 208 ? 4.488 69.855 -48.699 1.00 16.38 ? ? ? ? ? ? 208 GLN B O 1 ATOM 2530 C CB . GLN B 2 208 ? 7.343 68.518 -47.118 1.00 13.83 ? ? ? ? ? ? 208 GLN B CB 1 ATOM 2531 C CG . GLN B 2 208 ? 8.076 69.250 -45.963 1.00 8.93 ? ? ? ? ? ? 208 GLN B CG 1 ATOM 2532 C CD . GLN B 2 208 ? 9.522 68.700 -45.880 1.00 7.81 ? ? ? ? ? ? 208 GLN B CD 1 ATOM 2533 O OE1 . GLN B 2 208 ? 10.449 69.331 -45.329 1.00 2.00 ? ? ? ? ? ? 208 GLN B OE1 1 ATOM 2534 N NE2 . GLN B 2 208 ? 9.706 67.572 -46.534 1.00 7.76 ? ? ? ? ? ? 208 GLN B NE2 1 ATOM 2535 N N . SER B 2 209 ? 5.549 67.949 -49.281 1.00 13.28 ? ? ? ? ? ? 209 SER B N 1 ATOM 2536 C CA . SER B 2 209 ? 4.976 67.974 -50.609 1.00 14.95 ? ? ? ? ? ? 209 SER B CA 1 ATOM 2537 C C . SER B 2 209 ? 3.596 68.558 -50.733 1.00 15.05 ? ? ? ? ? ? 209 SER B C 1 ATOM 2538 O O . SER B 2 209 ? 3.413 69.708 -51.100 1.00 15.66 ? ? ? ? ? ? 209 SER B O 1 ATOM 2539 C CB . SER B 2 209 ? 4.884 66.623 -51.212 1.00 14.51 ? ? ? ? ? ? 209 SER B CB 1 ATOM 2540 O OG . SER B 2 209 ? 4.184 66.790 -52.450 1.00 20.02 ? ? ? ? ? ? 209 SER B OG 1 ATOM 2541 N N . LYS B 2 210 ? 2.629 67.688 -50.540 1.00 13.77 ? ? ? ? ? ? 210 LYS B N 1 ATOM 2542 C CA . LYS B 2 210 ? 1.213 68.094 -50.713 1.00 12.46 ? ? ? ? ? ? 210 LYS B CA 1 ATOM 2543 C C . LYS B 2 210 ? 0.881 69.486 -50.315 1.00 8.67 ? ? ? ? ? ? 210 LYS B C 1 ATOM 2544 O O . LYS B 2 210 ? -0.174 69.981 -50.687 1.00 8.86 ? ? ? ? ? ? 210 LYS B O 1 ATOM 2545 C CB . LYS B 2 210 ? 0.316 67.149 -49.895 1.00 10.27 ? ? ? ? ? ? 210 LYS B CB 1 ATOM 2546 C CG . LYS B 2 210 ? -1.092 67.083 -50.390 1.00 10.90 ? ? ? ? ? ? 210 LYS B CG 1 ATOM 2547 C CD . LYS B 2 210 ? -2.095 66.676 -49.232 1.00 11.44 ? ? ? ? ? ? 210 LYS B CD 1 ATOM 2548 C CE . LYS B 2 210 ? -3.580 66.439 -49.764 1.00 14.70 ? ? ? ? ? ? 210 LYS B CE 1 ATOM 2549 N NZ . LYS B 2 210 ? -4.473 66.155 -48.636 1.00 13.56 ? ? ? ? ? ? 210 LYS B NZ 1 ATOM 2550 N N . TYR B 2 211 ? 1.706 70.096 -49.468 1.00 10.54 ? ? ? ? ? ? 211 TYR B N 1 ATOM 2551 C CA . TYR B 2 211 ? 1.443 71.515 -49.057 1.00 7.88 ? ? ? ? ? ? 211 TYR B CA 1 ATOM 2552 C C . TYR B 2 211 ? 1.711 72.318 -50.290 1.00 8.59 ? ? ? ? ? ? 211 TYR B C 1 ATOM 2553 O O . TYR B 2 211 ? 0.925 73.263 -50.746 1.00 11.87 ? ? ? ? ? ? 211 TYR B O 1 ATOM 2554 C CB . TYR B 2 211 ? 2.347 71.974 -47.907 1.00 7.91 ? ? ? ? ? ? 211 TYR B CB 1 ATOM 2555 C CG . TYR B 2 211 ? 2.248 73.541 -47.516 1.00 9.48 ? ? ? ? ? ? 211 TYR B CG 1 ATOM 2556 C CD1 . TYR B 2 211 ? 1.033 74.114 -47.060 1.00 2.42 ? ? ? ? ? ? 211 TYR B CD1 1 ATOM 2557 C CD2 . TYR B 2 211 ? 3.315 74.389 -47.688 1.00 5.30 ? ? ? ? ? ? 211 TYR B CD2 1 ATOM 2558 C CE1 . TYR B 2 211 ? 0.899 75.421 -46.669 1.00 2.05 ? ? ? ? ? ? 211 TYR B CE1 1 ATOM 2559 C CE2 . TYR B 2 211 ? 3.187 75.795 -47.393 1.00 7.64 ? ? ? ? ? ? 211 TYR B CE2 1 ATOM 2560 C CZ . TYR B 2 211 ? 1.964 76.276 -46.875 1.00 8.61 ? ? ? ? ? ? 211 TYR B CZ 1 ATOM 2561 O OH . TYR B 2 211 ? 1.790 77.577 -46.600 1.00 7.48 ? ? ? ? ? ? 211 TYR B OH 1 ATOM 2562 N N . LEU B 2 212 ? 2.870 72.048 -50.850 1.00 7.58 ? ? ? ? ? ? 212 LEU B N 1 ATOM 2563 C CA . LEU B 2 212 ? 3.405 72.839 -51.971 1.00 5.40 ? ? ? ? ? ? 212 LEU B CA 1 ATOM 2564 C C . LEU B 2 212 ? 2.632 72.655 -53.177 1.00 8.42 ? ? ? ? ? ? 212 LEU B C 1 ATOM 2565 O O . LEU B 2 212 ? 2.670 73.494 -54.063 1.00 12.22 ? ? ? ? ? ? 212 LEU B O 1 ATOM 2566 C CB . LEU B 2 212 ? 4.817 72.454 -52.247 1.00 4.90 ? ? ? ? ? ? 212 LEU B CB 1 ATOM 2567 C CG . LEU B 2 212 ? 5.906 72.763 -51.202 1.00 2.14 ? ? ? ? ? ? 212 LEU B CG 1 ATOM 2568 C CD1 . LEU B 2 212 ? 7.193 72.208 -51.542 1.00 10.84 ? ? ? ? ? ? 212 LEU B CD1 1 ATOM 2569 C CD2 . LEU B 2 212 ? 6.169 74.388 -51.135 1.00 5.79 ? ? ? ? ? ? 212 LEU B CD2 1 ATOM 2570 N N . MET B 2 213 ? 1.842 71.572 -53.271 1.00 9.17 ? ? ? ? ? ? 213 MET B N 1 ATOM 2571 C CA . MET B 2 213 ? 1.198 71.298 -54.517 1.00 5.98 ? ? ? ? ? ? 213 MET B CA 1 ATOM 2572 C C . MET B 2 213 ? 0.358 72.535 -54.882 1.00 6.67 ? ? ? ? ? ? 213 MET B C 1 ATOM 2573 O O . MET B 2 213 ? -0.136 72.676 -55.997 1.00 8.57 ? ? ? ? ? ? 213 MET B O 1 ATOM 2574 C CB . MET B 2 213 ? 0.327 70.158 -54.313 1.00 2.70 ? ? ? ? ? ? 213 MET B CB 1 ATOM 2575 C CG . MET B 2 213 ? -0.485 69.890 -55.450 1.00 5.38 ? ? ? ? ? ? 213 MET B CG 1 ATOM 2576 S SD . MET B 2 213 ? -1.040 68.218 -55.292 1.00 10.00 ? ? ? ? ? ? 213 MET B SD 1 ATOM 2577 C CE . MET B 2 213 ? 0.675 67.411 -55.231 1.00 7.05 ? ? ? ? ? ? 213 MET B CE 1 ATOM 2578 N N . MET B 2 214 ? 0.114 73.410 -53.931 1.00 6.76 ? ? ? ? ? ? 214 MET B N 1 ATOM 2579 C CA . MET B 2 214 ? -0.600 74.596 -54.245 1.00 5.62 ? ? ? ? ? ? 214 MET B CA 1 ATOM 2580 C C . MET B 2 214 ? 0.100 75.546 -55.204 1.00 8.62 ? ? ? ? ? ? 214 MET B C 1 ATOM 2581 O O . MET B 2 214 ? -0.545 76.605 -55.666 1.00 7.46 ? ? ? ? ? ? 214 MET B O 1 ATOM 2582 C CB . MET B 2 214 ? -0.940 75.403 -53.004 1.00 7.43 ? ? ? ? ? ? 214 MET B CB 1 ATOM 2583 C CG . MET B 2 214 ? 0.189 75.926 -52.127 1.00 5.09 ? ? ? ? ? ? 214 MET B CG 1 ATOM 2584 S SD . MET B 2 214 ? -0.177 76.922 -50.685 1.00 3.90 ? ? ? ? ? ? 214 MET B SD 1 ATOM 2585 C CE . MET B 2 214 ? 0.893 78.406 -51.057 1.00 7.67 ? ? ? ? ? ? 214 MET B CE 1 ATOM 2586 N N . TYR B 2 215 ? 1.355 75.241 -55.536 1.00 6.55 ? ? ? ? ? ? 215 TYR B N 1 ATOM 2587 C CA . TYR B 2 215 ? 2.067 76.214 -56.352 1.00 8.24 ? ? ? ? ? ? 215 TYR B CA 1 ATOM 2588 C C . TYR B 2 215 ? 2.055 75.738 -57.767 1.00 10.44 ? ? ? ? ? ? 215 TYR B C 1 ATOM 2589 O O . TYR B 2 215 ? 2.719 76.301 -58.669 1.00 9.45 ? ? ? ? ? ? 215 TYR B O 1 ATOM 2590 C CB . TYR B 2 215 ? 3.489 76.556 -55.873 1.00 9.46 ? ? ? ? ? ? 215 TYR B CB 1 ATOM 2591 C CG . TYR B 2 215 ? 3.640 77.347 -54.574 1.00 9.98 ? ? ? ? ? ? 215 TYR B CG 1 ATOM 2592 C CD1 . TYR B 2 215 ? 4.463 76.871 -53.521 1.00 13.26 ? ? ? ? ? ? 215 TYR B CD1 1 ATOM 2593 C CD2 . TYR B 2 215 ? 2.891 78.498 -54.349 1.00 12.80 ? ? ? ? ? ? 215 TYR B CD2 1 ATOM 2594 C CE1 . TYR B 2 215 ? 4.586 77.611 -52.313 1.00 11.10 ? ? ? ? ? ? 215 TYR B CE1 1 ATOM 2595 C CE2 . TYR B 2 215 ? 3.009 79.237 -53.144 1.00 7.24 ? ? ? ? ? ? 215 TYR B CE2 1 ATOM 2596 C CZ . TYR B 2 215 ? 3.863 78.800 -52.158 1.00 6.83 ? ? ? ? ? ? 215 TYR B CZ 1 ATOM 2597 O OH . TYR B 2 215 ? 3.966 79.535 -50.972 1.00 6.01 ? ? ? ? ? ? 215 TYR B OH 1 ATOM 2598 N N . ASN B 2 216 ? 1.207 74.743 -58.027 1.00 10.11 ? ? ? ? ? ? 216 ASN B N 1 ATOM 2599 C CA . ASN B 2 216 ? 1.243 74.184 -59.366 1.00 10.42 ? ? ? ? ? ? 216 ASN B CA 1 ATOM 2600 C C . ASN B 2 216 ? 0.340 74.921 -60.396 1.00 11.37 ? ? ? ? ? ? 216 ASN B C 1 ATOM 2601 O O . ASN B 2 216 ? 0.157 74.494 -61.556 1.00 12.14 ? ? ? ? ? ? 216 ASN B O 1 ATOM 2602 C CB . ASN B 2 216 ? 1.003 72.660 -59.234 1.00 10.99 ? ? ? ? ? ? 216 ASN B CB 1 ATOM 2603 C CG . ASN B 2 216 ? -0.493 72.295 -58.845 1.00 7.94 ? ? ? ? ? ? 216 ASN B CG 1 ATOM 2604 O OD1 . ASN B 2 216 ? -0.880 71.187 -59.046 1.00 8.88 ? ? ? ? ? ? 216 ASN B OD1 1 ATOM 2605 N ND2 . ASN B 2 216 ? -1.276 73.223 -58.348 1.00 7.90 ? ? ? ? ? ? 216 ASN B ND2 1 ATOM 2606 N N . ASP B 2 217 ? -0.208 76.049 -59.971 1.00 13.41 ? ? ? ? ? ? 217 ASP B N 1 ATOM 2607 C CA . ASP B 2 217 ? -1.109 76.814 -60.818 1.00 13.47 ? ? ? ? ? ? 217 ASP B CA 1 ATOM 2608 C C . ASP B 2 217 ? -0.190 77.876 -61.500 1.00 13.44 ? ? ? ? ? ? 217 ASP B C 1 ATOM 2609 O O . ASP B 2 217 ? -0.605 78.774 -62.232 1.00 8.95 ? ? ? ? ? ? 217 ASP B O 1 ATOM 2610 C CB . ASP B 2 217 ? -2.173 77.474 -59.928 1.00 14.77 ? ? ? ? ? ? 217 ASP B CB 1 ATOM 2611 C CG . ASP B 2 217 ? -1.604 78.561 -59.073 1.00 18.29 ? ? ? ? ? ? 217 ASP B CG 1 ATOM 2612 O OD1 . ASP B 2 217 ? -0.357 78.599 -59.004 1.00 25.18 ? ? ? ? ? ? 217 ASP B OD1 1 ATOM 2613 O OD2 . ASP B 2 217 ? -2.360 79.387 -58.522 1.00 15.38 ? ? ? ? ? ? 217 ASP B OD2 1 ATOM 2614 N N . ASN B 2 218 ? 1.119 77.716 -61.246 1.00 13.79 ? ? ? ? ? ? 218 ASN B N 1 ATOM 2615 C CA . ASN B 2 218 ? 2.083 78.640 -61.731 1.00 11.63 ? ? ? ? ? ? 218 ASN B CA 1 ATOM 2616 C C . ASN B 2 218 ? 1.623 80.062 -61.868 1.00 14.18 ? ? ? ? ? ? 218 ASN B C 1 ATOM 2617 O O . ASN B 2 218 ? 1.977 80.681 -62.792 1.00 16.15 ? ? ? ? ? ? 218 ASN B O 1 ATOM 2618 C CB . ASN B 2 218 ? 2.554 78.205 -63.054 1.00 12.01 ? ? ? ? ? ? 218 ASN B CB 1 ATOM 2619 C CG . ASN B 2 218 ? 3.987 78.680 -63.272 1.00 13.18 ? ? ? ? ? ? 218 ASN B CG 1 ATOM 2620 O OD1 . ASN B 2 218 ? 4.903 78.223 -62.578 1.00 10.21 ? ? ? ? ? ? 218 ASN B OD1 1 ATOM 2621 N ND2 . ASN B 2 218 ? 4.161 79.674 -64.107 1.00 7.20 ? ? ? ? ? ? 218 ASN B ND2 1 ATOM 2622 N N . LYS B 2 219 ? 0.784 80.555 -60.967 1.00 13.83 ? ? ? ? ? ? 219 LYS B N 1 ATOM 2623 C CA . LYS B 2 219 ? 0.125 81.773 -61.130 1.00 13.39 ? ? ? ? ? ? 219 LYS B CA 1 ATOM 2624 C C . LYS B 2 219 ? 1.207 82.778 -60.997 1.00 14.08 ? ? ? ? ? ? 219 LYS B C 1 ATOM 2625 O O . LYS B 2 219 ? 2.116 82.609 -60.161 1.00 16.86 ? ? ? ? ? ? 219 LYS B O 1 ATOM 2626 C CB . LYS B 2 219 ? -0.855 82.027 -59.962 1.00 13.32 ? ? ? ? ? ? 219 LYS B CB 1 ATOM 2627 C CG . LYS B 2 219 ? -1.266 83.523 -59.806 1.00 10.67 ? ? ? ? ? ? 219 LYS B CG 1 ATOM 2628 C CD . LYS B 2 219 ? -1.971 84.122 -61.071 1.00 2.64 ? ? ? ? ? ? 219 LYS B CD 1 ATOM 2629 C CE . LYS B 2 219 ? -2.428 85.720 -60.820 1.00 6.33 ? ? ? ? ? ? 219 LYS B CE 1 ATOM 2630 N NZ . LYS B 2 219 ? -3.811 85.804 -60.273 1.00 9.10 ? ? ? ? ? ? 219 LYS B NZ 1 ATOM 2631 N N . THR B 2 220 ? 1.132 83.796 -61.845 1.00 12.34 ? ? ? ? ? ? 220 THR B N 1 ATOM 2632 C CA . THR B 2 220 ? 2.051 84.948 -61.885 1.00 13.14 ? ? ? ? ? ? 220 THR B CA 1 ATOM 2633 C C . THR B 2 220 ? 1.331 86.328 -61.557 1.00 11.83 ? ? ? ? ? ? 220 THR B C 1 ATOM 2634 O O . THR B 2 220 ? 0.035 86.521 -61.610 1.00 6.57 ? ? ? ? ? ? 220 THR B O 1 ATOM 2635 C CB . THR B 2 220 ? 2.628 85.189 -63.283 1.00 11.29 ? ? ? ? ? ? 220 THR B CB 1 ATOM 2636 O OG1 . THR B 2 220 ? 1.735 84.675 -64.246 1.00 16.36 ? ? ? ? ? ? 220 THR B OG1 1 ATOM 2637 C CG2 . THR B 2 220 ? 4.031 84.648 -63.482 1.00 15.28 ? ? ? ? ? ? 220 THR B CG2 1 ATOM 2638 N N . VAL B 2 221 ? 2.205 87.279 -61.336 1.00 9.47 ? ? ? ? ? ? 221 VAL B N 1 ATOM 2639 C CA . VAL B 2 221 ? 1.804 88.642 -60.939 1.00 8.96 ? ? ? ? ? ? 221 VAL B CA 1 ATOM 2640 C C . VAL B 2 221 ? 2.805 89.735 -61.425 1.00 9.26 ? ? ? ? ? ? 221 VAL B C 1 ATOM 2641 O O . VAL B 2 221 ? 3.969 89.454 -61.744 1.00 7.29 ? ? ? ? ? ? 221 VAL B O 1 ATOM 2642 C CB . VAL B 2 221 ? 1.740 88.729 -59.432 1.00 8.07 ? ? ? ? ? ? 221 VAL B CB 1 ATOM 2643 C CG1 . VAL B 2 221 ? 0.413 88.178 -58.892 1.00 6.23 ? ? ? ? ? ? 221 VAL B CG1 1 ATOM 2644 C CG2 . VAL B 2 221 ? 2.885 88.058 -58.844 1.00 8.07 ? ? ? ? ? ? 221 VAL B CG2 1 ATOM 2645 N N . ASP B 2 222 ? 2.354 90.999 -61.458 1.00 11.10 ? ? ? ? ? ? 222 ASP B N 1 ATOM 2646 C CA . ASP B 2 222 ? 3.230 92.030 -62.042 1.00 11.38 ? ? ? ? ? ? 222 ASP B CA 1 ATOM 2647 C C . ASP B 2 222 ? 3.928 92.799 -60.967 1.00 10.59 ? ? ? ? ? ? 222 ASP B C 1 ATOM 2648 O O . ASP B 2 222 ? 3.290 93.658 -60.236 1.00 10.88 ? ? ? ? ? ? 222 ASP B O 1 ATOM 2649 C CB . ASP B 2 222 ? 2.458 92.942 -62.994 1.00 11.31 ? ? ? ? ? ? 222 ASP B CB 1 ATOM 2650 C CG . ASP B 2 222 ? 3.159 94.290 -63.216 1.00 18.61 ? ? ? ? ? ? 222 ASP B CG 1 ATOM 2651 O OD1 . ASP B 2 222 ? 4.402 94.328 -63.651 1.00 12.76 ? ? ? ? ? ? 222 ASP B OD1 1 ATOM 2652 O OD2 . ASP B 2 222 ? 2.437 95.315 -62.949 1.00 20.55 ? ? ? ? ? ? 222 ASP B OD2 1 ATOM 2653 N N . SER B 2 223 ? 5.202 92.484 -60.775 1.00 11.01 ? ? ? ? ? ? 223 SER B N 1 ATOM 2654 C CA . SER B 2 223 ? 6.008 93.167 -59.706 1.00 10.81 ? ? ? ? ? ? 223 SER B CA 1 ATOM 2655 C C . SER B 2 223 ? 5.680 94.662 -59.588 1.00 13.01 ? ? ? ? ? ? 223 SER B C 1 ATOM 2656 O O . SER B 2 223 ? 4.861 95.098 -58.779 1.00 12.28 ? ? ? ? ? ? 223 SER B O 1 ATOM 2657 C CB . SER B 2 223 ? 7.431 92.954 -60.035 1.00 12.80 ? ? ? ? ? ? 223 SER B CB 1 ATOM 2658 O OG . SER B 2 223 ? 7.714 93.692 -61.198 1.00 17.99 ? ? ? ? ? ? 223 SER B OG 1 ATOM 2659 N N . LYS B 2 224 ? 6.293 95.493 -60.391 1.00 16.57 ? ? ? ? ? ? 224 LYS B N 1 ATOM 2660 C CA . LYS B 2 224 ? 6.027 96.970 -60.347 1.00 18.61 ? ? ? ? ? ? 224 LYS B CA 1 ATOM 2661 C C . LYS B 2 224 ? 4.662 97.474 -59.806 1.00 17.45 ? ? ? ? ? ? 224 LYS B C 1 ATOM 2662 O O . LYS B 2 224 ? 4.496 98.671 -59.496 1.00 22.39 ? ? ? ? ? ? 224 LYS B O 1 ATOM 2663 C CB . LYS B 2 224 ? 6.328 97.627 -61.715 1.00 17.57 ? ? ? ? ? ? 224 LYS B CB 1 ATOM 2664 C CG . LYS B 2 224 ? 5.840 99.108 -61.832 1.00 22.56 ? ? ? ? ? ? 224 LYS B CG 1 ATOM 2665 C CD . LYS B 2 224 ? 6.607 100.035 -60.888 1.00 30.04 ? ? ? ? ? ? 224 LYS B CD 1 ATOM 2666 C CE . LYS B 2 224 ? 8.134 99.942 -61.100 1.00 30.69 ? ? ? ? ? ? 224 LYS B CE 1 ATOM 2667 N NZ . LYS B 2 224 ? 8.574 100.785 -62.276 1.00 30.96 ? ? ? ? ? ? 224 LYS B NZ 1 ATOM 2668 N N . SER B 2 225 ? 3.700 96.620 -59.636 1.00 15.93 ? ? ? ? ? ? 225 SER B N 1 ATOM 2669 C CA . SER B 2 225 ? 2.383 97.129 -59.155 1.00 16.39 ? ? ? ? ? ? 225 SER B CA 1 ATOM 2670 C C . SER B 2 225 ? 1.743 96.430 -58.047 1.00 13.02 ? ? ? ? ? ? 225 SER B C 1 ATOM 2671 O O . SER B 2 225 ? 1.368 97.084 -57.074 1.00 16.98 ? ? ? ? ? ? 225 SER B O 1 ATOM 2672 C CB . SER B 2 225 ? 1.304 97.240 -60.229 1.00 15.75 ? ? ? ? ? ? 225 SER B CB 1 ATOM 2673 O OG . SER B 2 225 ? 0.888 95.949 -60.640 1.00 23.80 ? ? ? ? ? ? 225 SER B OG 1 ATOM 2674 N N . VAL B 2 226 ? 1.532 95.163 -58.206 1.00 12.07 ? ? ? ? ? ? 226 VAL B N 1 ATOM 2675 C CA . VAL B 2 226 ? 1.080 94.194 -57.144 1.00 12.12 ? ? ? ? ? ? 226 VAL B CA 1 ATOM 2676 C C . VAL B 2 226 ? 1.634 94.647 -55.829 1.00 13.26 ? ? ? ? ? ? 226 VAL B C 1 ATOM 2677 O O . VAL B 2 226 ? 2.795 95.206 -55.740 1.00 15.27 ? ? ? ? ? ? 226 VAL B O 1 ATOM 2678 C CB . VAL B 2 226 ? 1.664 92.740 -57.401 1.00 10.62 ? ? ? ? ? ? 226 VAL B CB 1 ATOM 2679 C CG1 . VAL B 2 226 ? 3.105 92.644 -57.014 1.00 12.40 ? ? ? ? ? ? 226 VAL B CG1 1 ATOM 2680 C CG2 . VAL B 2 226 ? 0.975 91.629 -56.666 1.00 12.97 ? ? ? ? ? ? 226 VAL B CG2 1 ATOM 2681 N N . LYS B 2 227 ? 0.829 94.417 -54.801 1.00 14.79 ? ? ? ? ? ? 227 LYS B N 1 ATOM 2682 C CA . LYS B 2 227 ? 1.127 94.757 -53.375 1.00 13.32 ? ? ? ? ? ? 227 LYS B CA 1 ATOM 2683 C C . LYS B 2 227 ? 0.797 93.482 -52.514 1.00 11.92 ? ? ? ? ? ? 227 LYS B C 1 ATOM 2684 O O . LYS B 2 227 ? -0.144 92.773 -52.855 1.00 9.07 ? ? ? ? ? ? 227 LYS B O 1 ATOM 2685 C CB . LYS B 2 227 ? 0.244 95.971 -52.941 1.00 10.36 ? ? ? ? ? ? 227 LYS B CB 1 ATOM 2686 C CG . LYS B 2 227 ? -1.236 95.816 -53.245 1.00 12.29 ? ? ? ? ? ? 227 LYS B CG 1 ATOM 2687 C CD . LYS B 2 227 ? -2.001 97.269 -53.303 1.00 16.29 ? ? ? ? ? ? 227 LYS B CD 1 ATOM 2688 C CE . LYS B 2 227 ? -1.117 98.384 -54.076 1.00 17.98 ? ? ? ? ? ? 227 LYS B CE 1 ATOM 2689 N NZ . LYS B 2 227 ? -1.848 99.652 -54.281 1.00 21.46 ? ? ? ? ? ? 227 LYS B NZ 1 ATOM 2690 N N . ILE B 2 228 ? 1.511 93.278 -51.387 1.00 12.84 ? ? ? ? ? ? 228 ILE B N 1 ATOM 2691 C CA . ILE B 2 228 ? 1.363 92.065 -50.474 1.00 12.66 ? ? ? ? ? ? 228 ILE B CA 1 ATOM 2692 C C . ILE B 2 228 ? 0.868 92.391 -49.090 1.00 11.62 ? ? ? ? ? ? 228 ILE B C 1 ATOM 2693 O O . ILE B 2 228 ? 1.163 93.494 -48.570 1.00 9.82 ? ? ? ? ? ? 228 ILE B O 1 ATOM 2694 C CB . ILE B 2 228 ? 2.649 91.385 -50.356 1.00 11.44 ? ? ? ? ? ? 228 ILE B CB 1 ATOM 2695 C CG1 . ILE B 2 228 ? 3.085 91.087 -51.804 1.00 17.05 ? ? ? ? ? ? 228 ILE B CG1 1 ATOM 2696 C CG2 . ILE B 2 228 ? 2.432 90.020 -49.796 1.00 14.63 ? ? ? ? ? ? 228 ILE B CG2 1 ATOM 2697 C CD1 . ILE B 2 228 ? 4.582 90.906 -51.983 1.00 27.71 ? ? ? ? ? ? 228 ILE B CD1 1 ATOM 2698 N N . GLU B 2 229 ? 0.051 91.488 -48.552 1.00 8.09 ? ? ? ? ? ? 229 GLU B N 1 ATOM 2699 C CA . GLU B 2 229 ? -0.319 91.548 -47.203 1.00 8.55 ? ? ? ? ? ? 229 GLU B CA 1 ATOM 2700 C C . GLU B 2 229 ? -0.230 90.210 -46.470 1.00 10.16 ? ? ? ? ? ? 229 GLU B C 1 ATOM 2701 O O . GLU B 2 229 ? -0.815 89.166 -46.918 1.00 8.76 ? ? ? ? ? ? 229 GLU B O 1 ATOM 2702 C CB . GLU B 2 229 ? -1.793 92.008 -47.080 1.00 8.11 ? ? ? ? ? ? 229 GLU B CB 1 ATOM 2703 C CG . GLU B 2 229 ? -1.987 93.457 -47.591 1.00 5.95 ? ? ? ? ? ? 229 GLU B CG 1 ATOM 2704 C CD . GLU B 2 229 ? -3.473 94.015 -47.374 1.00 9.38 ? ? ? ? ? ? 229 GLU B CD 1 ATOM 2705 O OE1 . GLU B 2 229 ? -4.138 93.522 -46.464 1.00 4.16 ? ? ? ? ? ? 229 GLU B OE1 1 ATOM 2706 O OE2 . GLU B 2 229 ? -3.928 94.948 -48.149 1.00 5.72 ? ? ? ? ? ? 229 GLU B OE2 1 ATOM 2707 N N . VAL B 2 230 ? 0.441 90.271 -45.317 1.00 9.23 ? ? ? ? ? ? 230 VAL B N 1 ATOM 2708 C CA . VAL B 2 230 ? 0.472 89.129 -44.411 1.00 10.18 ? ? ? ? ? ? 230 VAL B CA 1 ATOM 2709 C C . VAL B 2 230 ? -0.299 89.382 -43.165 1.00 10.18 ? ? ? ? ? ? 230 VAL B C 1 ATOM 2710 O O . VAL B 2 230 ? -0.392 90.540 -42.669 1.00 7.88 ? ? ? ? ? ? 230 VAL B O 1 ATOM 2711 C CB . VAL B 2 230 ? 1.900 88.713 -44.098 1.00 9.33 ? ? ? ? ? ? 230 VAL B CB 1 ATOM 2712 C CG1 . VAL B 2 230 ? 1.911 87.345 -43.637 1.00 11.38 ? ? ? ? ? ? 230 VAL B CG1 1 ATOM 2713 C CG2 . VAL B 2 230 ? 2.678 88.721 -45.378 1.00 6.10 ? ? ? ? ? ? 230 VAL B CG2 1 ATOM 2714 N N . HIS B 2 231 ? -0.999 88.328 -42.715 1.00 10.47 ? ? ? ? ? ? 231 HIS B N 1 ATOM 2715 C CA . HIS B 2 231 ? -1.878 88.492 -41.562 1.00 7.93 ? ? ? ? ? ? 231 HIS B CA 1 ATOM 2716 C C . HIS B 2 231 ? -1.788 87.438 -40.479 1.00 9.90 ? ? ? ? ? ? 231 HIS B C 1 ATOM 2717 O O . HIS B 2 231 ? -2.104 86.235 -40.706 1.00 7.96 ? ? ? ? ? ? 231 HIS B O 1 ATOM 2718 C CB . HIS B 2 231 ? -3.308 88.687 -42.003 1.00 10.05 ? ? ? ? ? ? 231 HIS B CB 1 ATOM 2719 C CG . HIS B 2 231 ? -3.514 89.873 -42.884 1.00 4.45 ? ? ? ? ? ? 231 HIS B CG 1 ATOM 2720 N ND1 . HIS B 2 231 ? -3.540 91.167 -42.386 1.00 14.17 ? ? ? ? ? ? 231 HIS B ND1 1 ATOM 2721 C CD2 . HIS B 2 231 ? -3.743 89.978 -44.205 1.00 8.07 ? ? ? ? ? ? 231 HIS B CD2 1 ATOM 2722 C CE1 . HIS B 2 231 ? -3.814 92.023 -43.367 1.00 11.46 ? ? ? ? ? ? 231 HIS B CE1 1 ATOM 2723 N NE2 . HIS B 2 231 ? -3.921 91.338 -44.496 1.00 9.52 ? ? ? ? ? ? 231 HIS B NE2 1 ATOM 2724 N N . LEU B 2 232 ? -1.347 87.908 -39.281 1.00 9.33 ? ? ? ? ? ? 232 LEU B N 1 ATOM 2725 C CA . LEU B 2 232 ? -1.211 87.048 -38.168 1.00 10.79 ? ? ? ? ? ? 232 LEU B CA 1 ATOM 2726 C C . LEU B 2 232 ? -1.990 87.322 -36.867 1.00 11.53 ? ? ? ? ? ? 232 LEU B C 1 ATOM 2727 O O . LEU B 2 232 ? -2.351 88.432 -36.581 1.00 9.61 ? ? ? ? ? ? 232 LEU B O 1 ATOM 2728 C CB . LEU B 2 232 ? 0.289 86.905 -37.838 1.00 6.58 ? ? ? ? ? ? 232 LEU B CB 1 ATOM 2729 C CG . LEU B 2 232 ? 1.204 87.014 -39.059 1.00 6.26 ? ? ? ? ? ? 232 LEU B CG 1 ATOM 2730 C CD1 . LEU B 2 232 ? 2.639 87.509 -38.690 1.00 2.00 ? ? ? ? ? ? 232 LEU B CD1 1 ATOM 2731 C CD2 . LEU B 2 232 ? 1.300 85.699 -39.770 1.00 8.32 ? ? ? ? ? ? 232 LEU B CD2 1 ATOM 2732 N N . THR B 2 233 ? -2.050 86.274 -36.041 1.00 13.55 ? ? ? ? ? ? 233 THR B N 1 ATOM 2733 C CA . THR B 2 233 ? -2.766 86.244 -34.802 1.00 17.69 ? ? ? ? ? ? 233 THR B CA 1 ATOM 2734 C C . THR B 2 233 ? -1.963 85.429 -33.839 1.00 18.51 ? ? ? ? ? ? 233 THR B C 1 ATOM 2735 O O . THR B 2 233 ? -1.586 84.272 -34.110 1.00 18.86 ? ? ? ? ? ? 233 THR B O 1 ATOM 2736 C CB . THR B 2 233 ? -4.114 85.683 -34.921 1.00 15.29 ? ? ? ? ? ? 233 THR B CB 1 ATOM 2737 O OG1 . THR B 2 233 ? -4.012 84.454 -35.648 1.00 22.65 ? ? ? ? ? ? 233 THR B OG1 1 ATOM 2738 C CG2 . THR B 2 233 ? -5.033 86.635 -35.675 1.00 16.54 ? ? ? ? ? ? 233 THR B CG2 1 ATOM 2739 N N . THR B 2 234 ? -1.686 86.088 -32.721 1.00 21.39 ? ? ? ? ? ? 234 THR B N 1 ATOM 2740 C CA . THR B 2 234 ? -0.809 85.565 -31.717 1.00 24.25 ? ? ? ? ? ? 234 THR B CA 1 ATOM 2741 C C . THR B 2 234 ? -1.483 84.491 -30.955 1.00 24.47 ? ? ? ? ? ? 234 THR B C 1 ATOM 2742 O O . THR B 2 234 ? -2.715 84.347 -30.992 1.00 26.05 ? ? ? ? ? ? 234 THR B O 1 ATOM 2743 C CB . THR B 2 234 ? -0.389 86.652 -30.788 1.00 24.84 ? ? ? ? ? ? 234 THR B CB 1 ATOM 2744 O OG1 . THR B 2 234 ? 0.167 87.710 -31.570 1.00 25.92 ? ? ? ? ? ? 234 THR B OG1 1 ATOM 2745 C CG2 . THR B 2 234 ? 0.698 86.127 -29.884 1.00 31.82 ? ? ? ? ? ? 234 THR B CG2 1 ATOM 2746 N N . LYS B 2 235 ? -0.671 83.665 -30.317 1.00 26.23 ? ? ? ? ? ? 235 LYS B N 1 ATOM 2747 C CA . LYS B 2 235 ? -1.160 82.497 -29.579 1.00 25.36 ? ? ? ? ? ? 235 LYS B CA 1 ATOM 2748 C C . LYS B 2 235 ? -1.798 83.077 -28.343 1.00 26.05 ? ? ? ? ? ? 235 LYS B C 1 ATOM 2749 O O . LYS B 2 235 ? -2.684 83.934 -28.437 1.00 26.41 ? ? ? ? ? ? 235 LYS B O 1 ATOM 2750 C CB . LYS B 2 235 ? 0.022 81.665 -29.110 1.00 24.60 ? ? ? ? ? ? 235 LYS B CB 1 ATOM 2751 C CG . LYS B 2 235 ? 0.453 80.518 -30.001 1.00 28.91 ? ? ? ? ? ? 235 LYS B CG 1 ATOM 2752 C CD . LYS B 2 235 ? -0.485 79.259 -29.947 1.00 27.15 ? ? ? ? ? ? 235 LYS B CD 1 ATOM 2753 C CE . LYS B 2 235 ? 0.151 78.062 -30.780 1.00 23.19 ? ? ? ? ? ? 235 LYS B CE 1 ATOM 2754 N NZ . LYS B 2 235 ? 1.588 77.709 -30.374 1.00 24.48 ? ? ? ? ? ? 235 LYS B NZ 1 HETATM 2755 S S . SO4 C 3 . ? -1.075 100.089 -33.487 1.00 99.64 ? ? ? ? ? ? 500 SO4 B S 1 HETATM 2756 O O1 . SO4 C 3 . ? -0.224 101.290 -33.591 1.00 99.90 ? ? ? ? ? ? 500 SO4 B O1 1 HETATM 2757 O O2 . SO4 C 3 . ? -1.262 99.737 -32.069 1.00 99.56 ? ? ? ? ? ? 500 SO4 B O2 1 HETATM 2758 O O3 . SO4 C 3 . ? -2.395 100.374 -34.074 1.00 99.56 ? ? ? ? ? ? 500 SO4 B O3 1 HETATM 2759 O O4 . SO4 C 3 . ? -0.437 98.962 -34.198 1.00 99.00 ? ? ? ? ? ? 500 SO4 B O4 1 HETATM 2760 S S . SO4 D 3 . ? 14.376 77.820 -33.996 1.00 37.06 ? ? ? ? ? ? 501 SO4 B S 1 HETATM 2761 O O1 . SO4 D 3 . ? 15.095 78.791 -33.134 1.00 35.90 ? ? ? ? ? ? 501 SO4 B O1 1 HETATM 2762 O O2 . SO4 D 3 . ? 13.804 78.561 -35.114 1.00 38.01 ? ? ? ? ? ? 501 SO4 B O2 1 HETATM 2763 O O3 . SO4 D 3 . ? 15.347 76.831 -34.508 1.00 35.71 ? ? ? ? ? ? 501 SO4 B O3 1 HETATM 2764 O O4 . SO4 D 3 . ? 13.262 77.055 -33.412 1.00 31.43 ? ? ? ? ? ? 501 SO4 B O4 1 HETATM 2765 O O . HOH E 4 . ? 25.335 49.764 -30.273 1.00 2.00 ? ? ? ? ? ? 118 HOH A O 1 HETATM 2766 O O . HOH E 4 . ? 36.444 63.698 -31.174 1.00 9.23 ? ? ? ? ? ? 119 HOH A O 1 HETATM 2767 O O . HOH E 4 . ? 3.750 68.956 -28.729 1.00 7.77 ? ? ? ? ? ? 120 HOH A O 1 HETATM 2768 O O . HOH E 4 . ? 31.648 49.989 -40.728 1.00 21.48 ? ? ? ? ? ? 121 HOH A O 1 HETATM 2769 O O . HOH E 4 . ? 31.925 71.810 -11.999 1.00 6.98 ? ? ? ? ? ? 122 HOH A O 1 HETATM 2770 O O . HOH E 4 . ? 28.661 77.529 -14.550 1.00 18.14 ? ? ? ? ? ? 123 HOH A O 1 HETATM 2771 O O . HOH E 4 . ? 31.932 78.903 -23.497 1.00 3.10 ? ? ? ? ? ? 124 HOH A O 1 HETATM 2772 O O . HOH E 4 . ? 30.451 71.843 -30.785 1.00 8.12 ? ? ? ? ? ? 125 HOH A O 1 HETATM 2773 O O . HOH E 4 . ? 23.987 46.263 -36.414 1.00 10.69 ? ? ? ? ? ? 126 HOH A O 1 HETATM 2774 O O . HOH E 4 . ? 6.908 68.915 -22.223 1.00 13.35 ? ? ? ? ? ? 127 HOH A O 1 HETATM 2775 O O . HOH E 4 . ? 22.876 80.106 -35.648 1.00 22.53 ? ? ? ? ? ? 128 HOH A O 1 HETATM 2776 O O . HOH E 4 . ? 25.967 77.266 -36.524 1.00 30.62 ? ? ? ? ? ? 129 HOH A O 1 HETATM 2777 O O . HOH E 4 . ? 12.782 58.623 -49.336 1.00 9.72 ? ? ? ? ? ? 130 HOH A O 1 HETATM 2778 O O . HOH E 4 . ? 27.255 74.154 -12.084 1.00 2.00 ? ? ? ? ? ? 131 HOH A O 1 HETATM 2779 O O . HOH E 4 . ? 38.410 64.856 -21.218 1.00 25.09 ? ? ? ? ? ? 132 HOH A O 1 HETATM 2780 O O . HOH E 4 . ? 23.702 80.437 -33.309 1.00 30.94 ? ? ? ? ? ? 133 HOH A O 1 HETATM 2781 O O . HOH E 4 . ? 35.981 62.402 -21.737 1.00 37.89 ? ? ? ? ? ? 134 HOH A O 1 HETATM 2782 O O . HOH E 4 . ? 11.514 66.780 -20.572 1.00 2.04 ? ? ? ? ? ? 135 HOH A O 1 HETATM 2783 O O . HOH E 4 . ? 16.438 73.192 -26.757 1.00 17.46 ? ? ? ? ? ? 136 HOH A O 1 HETATM 2784 O O . HOH E 4 . ? 29.356 59.612 -50.313 1.00 7.09 ? ? ? ? ? ? 137 HOH A O 1 HETATM 2785 O O . HOH E 4 . ? 6.741 71.590 -24.367 1.00 28.21 ? ? ? ? ? ? 138 HOH A O 1 HETATM 2786 O O . HOH E 4 . ? 8.528 66.494 -26.463 1.00 9.50 ? ? ? ? ? ? 139 HOH A O 1 HETATM 2787 O O . HOH E 4 . ? 32.658 74.402 -10.804 1.00 3.27 ? ? ? ? ? ? 140 HOH A O 1 HETATM 2788 O O . HOH E 4 . ? 23.605 45.772 -32.154 1.00 14.30 ? ? ? ? ? ? 141 HOH A O 1 HETATM 2789 O O . HOH E 4 . ? 8.911 53.628 -21.582 1.00 19.47 ? ? ? ? ? ? 142 HOH A O 1 HETATM 2790 O O . HOH F 4 . ? 15.948 87.416 -57.354 1.00 15.43 ? ? ? ? ? ? 502 HOH B O 1 HETATM 2791 O O . HOH F 4 . ? 13.666 87.685 -47.900 1.00 6.93 ? ? ? ? ? ? 503 HOH B O 1 HETATM 2792 O O . HOH F 4 . ? 13.288 60.141 -65.353 1.00 2.00 ? ? ? ? ? ? 504 HOH B O 1 HETATM 2793 O O . HOH F 4 . ? -1.676 85.960 -65.112 1.00 10.43 ? ? ? ? ? ? 505 HOH B O 1 HETATM 2794 O O . HOH F 4 . ? 14.718 62.113 -72.938 1.00 14.13 ? ? ? ? ? ? 506 HOH B O 1 HETATM 2795 O O . HOH F 4 . ? -3.570 65.349 -66.746 1.00 8.81 ? ? ? ? ? ? 507 HOH B O 1 HETATM 2796 O O . HOH F 4 . ? 4.426 83.913 -68.067 1.00 14.05 ? ? ? ? ? ? 508 HOH B O 1 HETATM 2797 O O . HOH F 4 . ? -2.864 99.105 -43.629 1.00 11.21 ? ? ? ? ? ? 509 HOH B O 1 HETATM 2798 O O . HOH F 4 . ? 21.313 61.916 -61.230 1.00 21.60 ? ? ? ? ? ? 510 HOH B O 1 HETATM 2799 O O . HOH F 4 . ? 2.240 50.834 -54.403 1.00 7.32 ? ? ? ? ? ? 511 HOH B O 1 HETATM 2800 O O . HOH F 4 . ? -9.304 93.959 -50.286 1.00 12.13 ? ? ? ? ? ? 512 HOH B O 1 HETATM 2801 O O . HOH F 4 . ? 15.640 89.950 -71.754 1.00 15.30 ? ? ? ? ? ? 513 HOH B O 1 HETATM 2802 O O . HOH F 4 . ? 20.665 88.955 -40.919 1.00 25.14 ? ? ? ? ? ? 514 HOH B O 1 HETATM 2803 O O . HOH F 4 . ? 21.681 97.709 -60.959 1.00 32.97 ? ? ? ? ? ? 515 HOH B O 1 HETATM 2804 O O . HOH F 4 . ? -12.047 88.627 -42.940 1.00 11.95 ? ? ? ? ? ? 516 HOH B O 1 HETATM 2805 O O . HOH F 4 . ? 3.698 50.908 -62.479 1.00 7.90 ? ? ? ? ? ? 517 HOH B O 1 HETATM 2806 O O . HOH F 4 . ? 16.969 88.440 -44.944 1.00 19.77 ? ? ? ? ? ? 518 HOH B O 1 HETATM 2807 O O . HOH F 4 . ? -1.231 105.181 -50.928 1.00 5.66 ? ? ? ? ? ? 519 HOH B O 1 HETATM 2808 O O . HOH F 4 . ? -8.840 98.666 -62.849 1.00 15.61 ? ? ? ? ? ? 520 HOH B O 1 HETATM 2809 O O . HOH F 4 . ? 22.084 95.421 -56.123 1.00 21.12 ? ? ? ? ? ? 521 HOH B O 1 HETATM 2810 O O . HOH F 4 . ? -6.763 95.578 -47.449 1.00 13.50 ? ? ? ? ? ? 522 HOH B O 1 HETATM 2811 O O . HOH F 4 . ? -7.676 74.410 -38.966 1.00 8.74 ? ? ? ? ? ? 523 HOH B O 1 HETATM 2812 O O . HOH F 4 . ? 5.741 82.079 -74.711 1.00 6.71 ? ? ? ? ? ? 524 HOH B O 1 HETATM 2813 O O . HOH F 4 . ? 5.727 79.097 -75.274 1.00 20.18 ? ? ? ? ? ? 525 HOH B O 1 HETATM 2814 O O . HOH F 4 . ? -1.373 96.266 -48.791 1.00 9.16 ? ? ? ? ? ? 526 HOH B O 1 HETATM 2815 O O . HOH F 4 . ? 21.892 84.088 -47.516 1.00 13.11 ? ? ? ? ? ? 527 HOH B O 1 HETATM 2816 O O . HOH F 4 . ? 25.076 72.853 -64.831 1.00 17.21 ? ? ? ? ? ? 528 HOH B O 1 HETATM 2817 O O . HOH F 4 . ? -5.206 66.395 -44.356 1.00 25.02 ? ? ? ? ? ? 529 HOH B O 1 HETATM 2818 O O . HOH F 4 . ? 0.906 49.296 -63.066 1.00 14.09 ? ? ? ? ? ? 530 HOH B O 1 HETATM 2819 O O . HOH F 4 . ? -7.767 64.326 -43.482 1.00 8.13 ? ? ? ? ? ? 531 HOH B O 1 HETATM 2820 O O . HOH F 4 . ? 25.279 83.280 -69.454 1.00 18.15 ? ? ? ? ? ? 532 HOH B O 1 HETATM 2821 O O . HOH F 4 . ? -0.536 104.000 -48.471 1.00 27.48 ? ? ? ? ? ? 533 HOH B O 1 HETATM 2822 O O . HOH F 4 . ? 18.635 74.616 -70.571 1.00 11.66 ? ? ? ? ? ? 534 HOH B O 1 HETATM 2823 O O . HOH F 4 . ? -8.137 71.352 -43.664 1.00 23.54 ? ? ? ? ? ? 535 HOH B O 1 HETATM 2824 O O . HOH F 4 . ? -0.022 57.140 -64.467 1.00 20.91 ? ? ? ? ? ? 536 HOH B O 1 HETATM 2825 O O . HOH F 4 . ? 11.903 79.696 -77.926 1.00 24.79 ? ? ? ? ? ? 537 HOH B O 1 HETATM 2826 O O . HOH F 4 . ? 3.875 96.919 -66.349 1.00 23.34 ? ? ? ? ? ? 538 HOH B O 1 HETATM 2827 O O . HOH F 4 . ? -2.304 65.137 -27.581 1.00 12.23 ? ? ? ? ? ? 539 HOH B O 1 HETATM 2828 O O . HOH F 4 . ? 23.838 62.744 -60.728 1.00 20.76 ? ? ? ? ? ? 540 HOH B O 1 HETATM 2829 O O . HOH F 4 . ? 25.475 63.763 -52.306 1.00 121.53 ? ? ? ? ? ? 541 HOH B O 1 HETATM 2830 O O . HOH F 4 . ? 19.340 95.459 -52.256 1.00 15.56 ? ? ? ? ? ? 542 HOH B O 1 HETATM 2831 O O . HOH F 4 . ? 5.413 66.418 -75.339 1.00 22.66 ? ? ? ? ? ? 543 HOH B O 1 HETATM 2832 O O . HOH F 4 . ? 11.449 57.927 -65.290 1.00 16.66 ? ? ? ? ? ? 544 HOH B O 1 HETATM 2833 O O . HOH F 4 . ? -3.656 90.172 -37.863 1.00 5.02 ? ? ? ? ? ? 545 HOH B O 1 HETATM 2834 O O . HOH F 4 . ? 22.708 82.613 -62.073 1.00 29.31 ? ? ? ? ? ? 546 HOH B O 1 HETATM 2835 O O . HOH F 4 . ? 15.865 84.896 -51.020 1.00 14.07 ? ? ? ? ? ? 547 HOH B O 1 HETATM 2836 O O . HOH F 4 . ? -8.712 77.812 -29.905 1.00 19.01 ? ? ? ? ? ? 548 HOH B O 1 HETATM 2837 O O . HOH F 4 . ? 28.036 81.916 -68.836 1.00 46.06 ? ? ? ? ? ? 549 HOH B O 1 HETATM 2838 O O . HOH F 4 . ? -11.621 91.521 -42.425 1.00 16.22 ? ? ? ? ? ? 550 HOH B O 1 HETATM 2839 O O . HOH F 4 . ? -10.651 93.700 -64.906 1.00 23.83 ? ? ? ? ? ? 551 HOH B O 1 HETATM 2840 O O . HOH F 4 . ? -0.042 51.054 -58.193 1.00 14.07 ? ? ? ? ? ? 552 HOH B O 1 HETATM 2841 O O . HOH F 4 . ? 15.228 88.627 -51.416 1.00 5.73 ? ? ? ? ? ? 553 HOH B O 1 HETATM 2842 O O . HOH F 4 . ? 23.266 84.931 -50.360 1.00 21.74 ? ? ? ? ? ? 554 HOH B O 1 HETATM 2843 O O . HOH F 4 . ? -1.985 102.867 -54.348 1.00 53.93 ? ? ? ? ? ? 555 HOH B O 1 HETATM 2844 O O . HOH F 4 . ? 3.571 58.613 -32.101 1.00 5.05 ? ? ? ? ? ? 556 HOH B O 1 HETATM 2845 O O . HOH F 4 . ? -1.003 98.734 -65.736 1.00 11.36 ? ? ? ? ? ? 557 HOH B O 1 HETATM 2846 O O . HOH F 4 . ? -4.649 103.641 -64.052 1.00 13.19 ? ? ? ? ? ? 558 HOH B O 1 HETATM 2847 O O . HOH F 4 . ? -5.663 107.241 -64.985 1.00 28.57 ? ? ? ? ? ? 559 HOH B O 1 HETATM 2848 O O . HOH F 4 . ? -11.840 94.741 -46.578 1.00 15.36 ? ? ? ? ? ? 560 HOH B O 1 HETATM 2849 O O . HOH F 4 . ? 22.299 85.412 -68.489 1.00 39.76 ? ? ? ? ? ? 561 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ALA 1 2 2 ALA ALA A . n A 1 2 ALA 2 3 3 ALA ALA A . n A 1 3 VAL 3 4 4 VAL VAL A . n A 1 4 THR 4 5 5 THR THR A . n A 1 5 GLN 5 6 6 GLN GLN A . n A 1 6 SER 6 7 7 SER SER A . n A 1 7 PRO 7 8 8 PRO PRO A . n A 1 8 ARG 8 9 9 ARG ARG A . n A 1 9 ASN 9 10 10 ASN ASN A . n A 1 10 LYS 10 11 11 LYS LYS A . n A 1 11 VAL 11 12 12 VAL VAL A . n A 1 12 ALA 12 13 13 ALA ALA A . n A 1 13 VAL 13 14 14 VAL VAL A . n A 1 14 THR 14 15 15 THR THR A . n A 1 15 GLY 15 16 16 GLY GLY A . n A 1 16 GLU 16 17 17 GLU GLU A . n A 1 17 LYS 17 18 18 LYS LYS A . n A 1 18 VAL 18 19 19 VAL VAL A . n A 1 19 THR 19 20 20 THR THR A . n A 1 20 LEU 20 21 21 LEU LEU A . n A 1 21 SER 21 22 22 SER SER A . n A 1 22 CYS 22 23 23 CYS CYS A . n A 1 23 GLN 23 24 24 GLN GLN A . n A 1 24 GLN 24 25 25 GLN GLN A . n A 1 25 THR 25 26 26 THR THR A . n A 1 26 ASN 26 27 27 ASN ASN A . n A 1 27 ASN 27 28 28 ASN ASN A . n A 1 28 HIS 28 29 29 HIS HIS A . n A 1 29 ASN 29 30 30 ASN ASN A . n A 1 30 ASN 30 31 31 ASN ASN A . n A 1 31 MET 31 32 32 MET MET A . n A 1 32 TYR 32 33 33 TYR TYR A . n A 1 33 TRP 33 34 34 TRP TRP A . n A 1 34 TYR 34 35 35 TYR TYR A . n A 1 35 ARG 35 36 36 ARG ARG A . n A 1 36 GLN 36 37 37 GLN GLN A . n A 1 37 ASP 37 38 38 ASP ASP A . n A 1 38 THR 38 39 39 THR THR A . n A 1 39 GLY 39 40 40 GLY GLY A . n A 1 40 HIS 40 41 41 HIS HIS A . n A 1 41 GLY 41 42 42 GLY GLY A . n A 1 42 LEU 42 43 43 LEU LEU A . n A 1 43 ARG 43 44 44 ARG ARG A . n A 1 44 LEU 44 45 45 LEU LEU A . n A 1 45 ILE 45 46 46 ILE ILE A . n A 1 46 HIS 46 47 47 HIS HIS A . n A 1 47 TYR 47 48 48 TYR TYR A . n A 1 48 SER 48 49 49 SER SER A . n A 1 49 TYR 49 50 50 TYR TYR A . n A 1 50 GLY 50 51 51 GLY GLY A . n A 1 51 ALA 51 52 52 ALA ALA A . n A 1 52 GLY 52 53 53 GLY GLY A . n A 1 53 SER 53 54 54 SER SER A . n A 1 54 THR 54 55 55 THR THR A . n A 1 55 GLU 55 56 56 GLU GLU A . n A 1 56 LYS 56 57 57 LYS LYS A . n A 1 57 GLY 57 58 58 GLY GLY A . n A 1 58 ASP 58 59 59 ASP ASP A . n A 1 59 ILE 59 60 60 ILE ILE A . n A 1 60 PRO 60 61 61 PRO PRO A . n A 1 61 ASP 61 62 62 ASP ASP A . n A 1 62 GLY 62 63 63 GLY GLY A . n A 1 63 TYR 63 65 65 TYR TYR A . n A 1 64 LYS 64 66 66 LYS LYS A . n A 1 65 ALA 65 67 67 ALA ALA A . n A 1 66 SER 66 68 68 SER SER A . n A 1 67 ARG 67 69 69 ARG ARG A . n A 1 68 PRO 68 70 70 PRO PRO A . n A 1 69 SER 69 71 71 SER SER A . n A 1 70 GLN 70 72 72 GLN GLN A . n A 1 71 GLU 71 73 73 GLU GLU A . n A 1 72 GLN 72 74 74 GLN GLN A . n A 1 73 PHE 73 75 75 PHE PHE A . n A 1 74 SER 74 76 76 SER SER A . n A 1 75 LEU 75 77 77 LEU LEU A . n A 1 76 ILE 76 78 78 ILE ILE A . n A 1 77 LEU 77 79 79 LEU LEU A . n A 1 78 GLU 78 80 80 GLU GLU A . n A 1 79 SER 79 81 81 SER SER A . n A 1 80 ALA 80 82 82 ALA ALA A . n A 1 81 THR 81 83 83 THR THR A . n A 1 82 PRO 82 84 84 PRO PRO A . n A 1 83 SER 83 85 85 SER SER A . n A 1 84 GLN 84 86 86 GLN GLN A . n A 1 85 THR 85 87 87 THR THR A . n A 1 86 SER 86 88 88 SER SER A . n A 1 87 VAL 87 89 89 VAL VAL A . n A 1 88 TYR 88 90 90 TYR TYR A . n A 1 89 PHE 89 91 91 PHE PHE A . n A 1 90 CYS 90 92 92 CYS CYS A . n A 1 91 ALA 91 93 93 ALA ALA A . n A 1 92 SER 92 94 94 SER SER A . n A 1 93 GLY 93 95 95 GLY GLY A . n A 1 94 GLY 94 96 96 GLY GLY A . n A 1 95 GLY 95 97 97 GLY GLY A . n A 1 96 GLY 96 98 98 GLY GLY A . n A 1 97 THR 97 99 99 THR THR A . n A 1 98 LEU 98 100 100 LEU LEU A . n A 1 99 TYR 99 101 101 TYR TYR A . n A 1 100 PHE 100 108 108 PHE PHE A . n A 1 101 GLY 101 109 109 GLY GLY A . n A 1 102 ALA 102 110 110 ALA ALA A . n A 1 103 GLY 103 111 111 GLY GLY A . n A 1 104 THR 104 112 112 THR THR A . n A 1 105 ARG 105 113 113 ARG ARG A . n A 1 106 LEU 106 114 114 LEU LEU A . n A 1 107 SER 107 115 115 SER SER A . n A 1 108 VAL 108 116 116 VAL VAL A . n A 1 109 LEU 109 117 117 LEU LEU A . n B 2 1 GLU 1 1 ? ? ? B . n B 2 2 SER 2 2 2 SER SER B . n B 2 3 GLN 3 3 3 GLN GLN B . n B 2 4 PRO 4 4 4 PRO PRO B . n B 2 5 ASP 5 5 5 ASP ASP B . n B 2 6 PRO 6 6 6 PRO PRO B . n B 2 7 MET 7 7 7 MET MET B . n B 2 8 PRO 8 8 8 PRO PRO B . n B 2 9 ASP 9 9 9 ASP ASP B . n B 2 10 ASP 10 10 10 ASP ASP B . n B 2 11 LEU 11 11 11 LEU LEU B . n B 2 12 HIS 12 12 12 HIS HIS B . n B 2 13 LYS 13 13 13 LYS LYS B . n B 2 14 SER 14 14 14 SER SER B . n B 2 15 SER 15 15 15 SER SER B . n B 2 16 GLU 16 16 16 GLU GLU B . n B 2 17 PHE 17 17 17 PHE PHE B . n B 2 18 THR 18 18 18 THR THR B . n B 2 19 GLY 19 19 19 GLY GLY B . n B 2 20 THR 20 20 20 THR THR B . n B 2 21 MET 21 21 21 MET MET B . n B 2 22 GLY 22 22 22 GLY GLY B . n B 2 23 ASN 23 23 23 ASN ASN B . n B 2 24 MET 24 24 24 MET MET B . n B 2 25 LYS 25 25 25 LYS LYS B . n B 2 26 TYR 26 26 26 TYR TYR B . n B 2 27 LEU 27 27 27 LEU LEU B . n B 2 28 TYR 28 28 28 TYR TYR B . n B 2 29 ASP 29 29 29 ASP ASP B . n B 2 30 ASP 30 30 30 ASP ASP B . n B 2 31 HIS 31 31 31 HIS HIS B . n B 2 32 TYR 32 32 32 TYR TYR B . n B 2 33 VAL 33 33 33 VAL VAL B . n B 2 34 SER 34 34 34 SER SER B . n B 2 35 ALA 35 35 35 ALA ALA B . n B 2 36 THR 36 36 36 THR THR B . n B 2 37 LYS 37 37 37 LYS LYS B . n B 2 38 VAL 38 38 38 VAL VAL B . n B 2 39 LYS 39 39 39 LYS LYS B . n B 2 40 SER 40 40 40 SER SER B . n B 2 41 VAL 41 41 41 VAL VAL B . n B 2 42 ASP 42 42 42 ASP ASP B . n B 2 43 LYS 43 43 43 LYS LYS B . n B 2 44 PHE 44 44 44 PHE PHE B . n B 2 45 LEU 45 45 45 LEU LEU B . n B 2 46 ALA 46 46 46 ALA ALA B . n B 2 47 HIS 47 47 47 HIS HIS B . n B 2 48 ASP 48 48 48 ASP ASP B . n B 2 49 LEU 49 49 49 LEU LEU B . n B 2 50 ILE 50 50 50 ILE ILE B . n B 2 51 TYR 51 51 51 TYR TYR B . n B 2 52 ASN 52 52 52 ASN ASN B . n B 2 53 ILE 53 53 53 ILE ILE B . n B 2 54 SER 54 54 54 SER SER B . n B 2 55 ASP 55 55 55 ASP ASP B . n B 2 56 LYS 56 56 56 LYS LYS B . n B 2 57 LYS 57 57 57 LYS LYS B . n B 2 58 LEU 58 58 58 LEU LEU B . n B 2 59 LYS 59 59 59 LYS LYS B . n B 2 60 ASN 60 60 60 ASN ASN B . n B 2 61 TYR 61 61 61 TYR TYR B . n B 2 62 ASP 62 62 62 ASP ASP B . n B 2 63 LYS 63 63 63 LYS LYS B . n B 2 64 VAL 64 64 64 VAL VAL B . n B 2 65 LYS 65 65 65 LYS LYS B . n B 2 66 THR 66 66 66 THR THR B . n B 2 67 GLU 67 67 67 GLU GLU B . n B 2 68 LEU 68 68 68 LEU LEU B . n B 2 69 LEU 69 69 69 LEU LEU B . n B 2 70 ASN 70 70 70 ASN ASN B . n B 2 71 GLU 71 71 71 GLU GLU B . n B 2 72 ASP 72 72 72 ASP ASP B . n B 2 73 LEU 73 73 73 LEU LEU B . n B 2 74 ALA 74 74 74 ALA ALA B . n B 2 75 LYS 75 75 75 LYS LYS B . n B 2 76 LYS 76 76 76 LYS LYS B . n B 2 77 TYR 77 77 77 TYR TYR B . n B 2 78 LYS 78 78 78 LYS LYS B . n B 2 79 ASP 79 79 79 ASP ASP B . n B 2 80 GLU 80 80 80 GLU GLU B . n B 2 81 VAL 81 81 81 VAL VAL B . n B 2 82 VAL 82 82 82 VAL VAL B . n B 2 83 ASP 83 83 83 ASP ASP B . n B 2 84 VAL 84 84 84 VAL VAL B . n B 2 85 TYR 85 85 85 TYR TYR B . n B 2 86 GLY 86 86 86 GLY GLY B . n B 2 87 SER 87 87 87 SER SER B . n B 2 88 ASN 88 88 88 ASN ASN B . n B 2 89 TYR 89 89 89 TYR TYR B . n B 2 90 TYR 90 90 90 TYR TYR B . n B 2 91 VAL 91 91 91 VAL VAL B . n B 2 92 ASN 92 92 92 ASN ASN B . n B 2 93 CYS 93 93 93 CYS CYS B . n B 2 94 TYR 94 94 94 TYR TYR B . n B 2 95 PHE 95 95 95 PHE PHE B . n B 2 96 SER 96 96 96 SER SER B . n B 2 97 SER 97 97 97 SER SER B . n B 2 98 LYS 98 98 98 LYS LYS B . n B 2 99 ASP 99 99 99 ASP ASP B . n B 2 100 ASN 100 100 100 ASN ASN B . n B 2 101 VAL 101 101 101 VAL VAL B . n B 2 102 TRP 102 102 102 TRP TRP B . n B 2 103 TRP 103 103 103 TRP TRP B . n B 2 104 HIS 104 104 104 HIS HIS B . n B 2 105 GLY 105 105 105 GLY GLY B . n B 2 106 LYS 106 106 106 LYS LYS B . n B 2 107 THR 107 107 107 THR THR B . n B 2 108 CYS 108 108 108 CYS CYS B . n B 2 109 MET 109 109 109 MET MET B . n B 2 110 TYR 110 110 110 TYR TYR B . n B 2 111 GLY 111 111 111 GLY GLY B . n B 2 112 GLY 112 112 112 GLY GLY B . n B 2 113 ILE 113 113 113 ILE ILE B . n B 2 114 THR 114 114 114 THR THR B . n B 2 115 LYS 115 115 115 LYS LYS B . n B 2 116 HIS 116 116 116 HIS HIS B . n B 2 117 GLU 117 117 117 GLU GLU B . n B 2 118 GLY 118 118 118 GLY GLY B . n B 2 119 ASN 119 119 119 ASN ASN B . n B 2 120 HIS 120 120 120 HIS HIS B . n B 2 121 PHE 121 121 121 PHE PHE B . n B 2 122 ASP 122 122 122 ASP ASP B . n B 2 123 ASN 123 123 123 ASN ASN B . n B 2 124 GLY 124 124 124 GLY GLY B . n B 2 125 ASN 125 125 125 ASN ASN B . n B 2 126 LEU 126 126 126 LEU LEU B . n B 2 127 GLN 127 127 127 GLN GLN B . n B 2 128 ASN 128 128 128 ASN ASN B . n B 2 129 VAL 129 129 129 VAL VAL B . n B 2 130 LEU 130 130 130 LEU LEU B . n B 2 131 VAL 131 131 131 VAL VAL B . n B 2 132 ARG 132 132 132 ARG ARG B . n B 2 133 VAL 133 133 133 VAL VAL B . n B 2 134 TYR 134 134 134 TYR TYR B . n B 2 135 GLU 135 135 135 GLU GLU B . n B 2 136 ASN 136 136 136 ASN ASN B . n B 2 137 LYS 137 137 137 LYS LYS B . n B 2 138 ARG 138 138 138 ARG ARG B . n B 2 139 ASN 139 139 139 ASN ASN B . n B 2 140 THR 140 140 140 THR THR B . n B 2 141 ILE 141 141 141 ILE ILE B . n B 2 142 SER 142 142 142 SER SER B . n B 2 143 PHE 143 143 143 PHE PHE B . n B 2 144 GLU 144 144 144 GLU GLU B . n B 2 145 VAL 145 145 145 VAL VAL B . n B 2 146 GLN 146 146 146 GLN GLN B . n B 2 147 THR 147 147 147 THR THR B . n B 2 148 ASP 148 148 148 ASP ASP B . n B 2 149 LYS 149 149 149 LYS LYS B . n B 2 150 LYS 150 150 150 LYS LYS B . n B 2 151 SER 151 151 151 SER SER B . n B 2 152 VAL 152 152 152 VAL VAL B . n B 2 153 THR 153 153 153 THR THR B . n B 2 154 ALA 154 154 154 ALA ALA B . n B 2 155 GLN 155 155 155 GLN GLN B . n B 2 156 GLU 156 156 156 GLU GLU B . n B 2 157 LEU 157 157 157 LEU LEU B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 ILE 159 159 159 ILE ILE B . n B 2 160 LYS 160 160 160 LYS LYS B . n B 2 161 ALA 161 161 161 ALA ALA B . n B 2 162 ARG 162 162 162 ARG ARG B . n B 2 163 ASN 163 163 163 ASN ASN B . n B 2 164 PHE 164 164 164 PHE PHE B . n B 2 165 LEU 165 165 165 LEU LEU B . n B 2 166 ILE 166 166 166 ILE ILE B . n B 2 167 ASN 167 167 167 ASN ASN B . n B 2 168 LYS 168 168 168 LYS LYS B . n B 2 169 LYS 169 169 169 LYS LYS B . n B 2 170 ASN 170 170 170 ASN ASN B . n B 2 171 LEU 171 171 171 LEU LEU B . n B 2 172 TYR 172 172 172 TYR TYR B . n B 2 173 GLU 173 173 173 GLU GLU B . n B 2 174 PHE 174 174 174 PHE PHE B . n B 2 175 ASN 175 175 175 ASN ASN B . n B 2 176 SER 176 176 176 SER SER B . n B 2 177 SER 177 177 177 SER SER B . n B 2 178 PRO 178 178 178 PRO PRO B . n B 2 179 TYR 179 179 179 TYR TYR B . n B 2 180 GLU 180 180 180 GLU GLU B . n B 2 181 THR 181 181 181 THR THR B . n B 2 182 GLY 182 182 182 GLY GLY B . n B 2 183 TYR 183 183 183 TYR TYR B . n B 2 184 ILE 184 184 184 ILE ILE B . n B 2 185 LYS 185 185 185 LYS LYS B . n B 2 186 PHE 186 186 186 PHE PHE B . n B 2 187 ILE 187 187 187 ILE ILE B . n B 2 188 GLU 188 188 188 GLU GLU B . n B 2 189 ASN 189 189 189 ASN ASN B . n B 2 190 ASN 190 190 190 ASN ASN B . n B 2 191 GLY 191 191 191 GLY GLY B . n B 2 192 ASN 192 192 192 ASN ASN B . n B 2 193 THR 193 193 193 THR THR B . n B 2 194 PHE 194 194 194 PHE PHE B . n B 2 195 TRP 195 195 195 TRP TRP B . n B 2 196 TYR 196 196 196 TYR TYR B . n B 2 197 ASP 197 197 197 ASP ASP B . n B 2 198 MET 198 198 198 MET MET B . n B 2 199 MET 199 199 199 MET MET B . n B 2 200 PRO 200 200 200 PRO PRO B . n B 2 201 ALA 201 201 201 ALA ALA B . n B 2 202 PRO 202 202 202 PRO PRO B . n B 2 203 GLY 203 203 203 GLY GLY B . n B 2 204 ASP 204 204 204 ASP ASP B . n B 2 205 LYS 205 205 205 LYS LYS B . n B 2 206 PHE 206 206 206 PHE PHE B . n B 2 207 ASP 207 207 207 ASP ASP B . n B 2 208 GLN 208 208 208 GLN GLN B . n B 2 209 SER 209 209 209 SER SER B . n B 2 210 LYS 210 210 210 LYS LYS B . n B 2 211 TYR 211 211 211 TYR TYR B . n B 2 212 LEU 212 212 212 LEU LEU B . n B 2 213 MET 213 213 213 MET MET B . n B 2 214 MET 214 214 214 MET MET B . n B 2 215 TYR 215 215 215 TYR TYR B . n B 2 216 ASN 216 216 216 ASN ASN B . n B 2 217 ASP 217 217 217 ASP ASP B . n B 2 218 ASN 218 218 218 ASN ASN B . n B 2 219 LYS 219 219 219 LYS LYS B . n B 2 220 THR 220 220 220 THR THR B . n B 2 221 VAL 221 221 221 VAL VAL B . n B 2 222 ASP 222 222 222 ASP ASP B . n B 2 223 SER 223 223 223 SER SER B . n B 2 224 LYS 224 224 224 LYS LYS B . n B 2 225 SER 225 225 225 SER SER B . n B 2 226 VAL 226 226 226 VAL VAL B . n B 2 227 LYS 227 227 227 LYS LYS B . n B 2 228 ILE 228 228 228 ILE ILE B . n B 2 229 GLU 229 229 229 GLU GLU B . n B 2 230 VAL 230 230 230 VAL VAL B . n B 2 231 HIS 231 231 231 HIS HIS B . n B 2 232 LEU 232 232 232 LEU LEU B . n B 2 233 THR 233 233 233 THR THR B . n B 2 234 THR 234 234 234 THR THR B . n B 2 235 LYS 235 235 235 LYS LYS B . n B 2 236 ASN 236 236 ? ? ? B . n B 2 237 GLY 237 237 ? ? ? B . n # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,E,B,C,D,F # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # _pdbx_entry_details.entry_id 3BZD _pdbx_entry_details.sequence_details 'RESIDUES 129-133 (GKVTG) OF UNP ENTRY P0A0L5 WERE REPLACED WITH RESIDUES 102-104 (WWH) IN THE CRYSTALLIZED SEQUENCE.' # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code 1 Y 1 1 B GLU 1 ? 2 Y 1 1 B ASN 236 ? 3 Y 1 1 B GLY 237 ? # loop_ _pdbx_version.entry_id _pdbx_version.revision_date _pdbx_version.major_version _pdbx_version.minor_version _pdbx_version.revision_type _pdbx_version.details 3BZD 2008-01-31 3 2 'Version format compliance' 'compliance with PDB format V.3.20' 3BZD 2011-07-13 4 0000 'Version format compliance' 'compliance with PDB Exchange Dictionary V4' # loop_ _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id _software.pdbx_ordinal REFMAC5 5.2.0019 ? program 'Murshudov, G.N.' ccp4@dl.ac.uk refinement http://www.ccp4.ac.uk/main.html Fortran_77 ? 1 pdb_extract 3.004 'September 10, 2007' package PDB sw-help@rcsb.rutgers.edu 'data extraction' http://pdb.rutgers.edu/software/ C++ ? 2 # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 SO4 1 500 500 SO4 SO4 B . D 3 SO4 1 501 501 SO4 SO4 B . E 4 HOH 1 118 1 HOH HOH A . E 4 HOH 2 119 6 HOH HOH A . E 4 HOH 3 120 11 HOH HOH A . E 4 HOH 4 121 14 HOH HOH A . E 4 HOH 5 122 16 HOH HOH A . E 4 HOH 6 123 17 HOH HOH A . E 4 HOH 7 124 19 HOH HOH A . E 4 HOH 8 125 23 HOH HOH A . E 4 HOH 9 126 28 HOH HOH A . E 4 HOH 10 127 31 HOH HOH A . E 4 HOH 11 128 37 HOH HOH A . E 4 HOH 12 129 38 HOH HOH A . E 4 HOH 13 130 41 HOH HOH A . E 4 HOH 14 131 43 HOH HOH A . E 4 HOH 15 132 44 HOH HOH A . E 4 HOH 16 133 45 HOH HOH A . E 4 HOH 17 134 47 HOH HOH A . E 4 HOH 18 135 52 HOH HOH A . E 4 HOH 19 136 55 HOH HOH A . E 4 HOH 20 137 60 HOH HOH A . E 4 HOH 21 138 62 HOH HOH A . E 4 HOH 22 139 65 HOH HOH A . E 4 HOH 23 140 71 HOH HOH A . E 4 HOH 24 141 75 HOH HOH A . E 4 HOH 25 142 80 HOH HOH A . F 4 HOH 1 502 2 HOH HOH B . F 4 HOH 2 503 3 HOH HOH B . F 4 HOH 3 504 4 HOH HOH B . F 4 HOH 4 505 5 HOH HOH B . F 4 HOH 5 506 7 HOH HOH B . F 4 HOH 6 507 8 HOH HOH B . F 4 HOH 7 508 9 HOH HOH B . F 4 HOH 8 509 10 HOH HOH B . F 4 HOH 9 510 12 HOH HOH B . F 4 HOH 10 511 13 HOH HOH B . F 4 HOH 11 512 15 HOH HOH B . F 4 HOH 12 513 18 HOH HOH B . F 4 HOH 13 514 20 HOH HOH B . F 4 HOH 14 515 21 HOH HOH B . F 4 HOH 15 516 22 HOH HOH B . F 4 HOH 16 517 24 HOH HOH B . F 4 HOH 17 518 25 HOH HOH B . F 4 HOH 18 519 26 HOH HOH B . F 4 HOH 19 520 27 HOH HOH B . F 4 HOH 20 521 29 HOH HOH B . F 4 HOH 21 522 30 HOH HOH B . F 4 HOH 22 523 32 HOH HOH B . F 4 HOH 23 524 33 HOH HOH B . F 4 HOH 24 525 34 HOH HOH B . F 4 HOH 25 526 35 HOH HOH B . F 4 HOH 26 527 36 HOH HOH B . F 4 HOH 27 528 39 HOH HOH B . F 4 HOH 28 529 40 HOH HOH B . F 4 HOH 29 530 42 HOH HOH B . F 4 HOH 30 531 46 HOH HOH B . F 4 HOH 31 532 48 HOH HOH B . F 4 HOH 32 533 49 HOH HOH B . F 4 HOH 33 534 50 HOH HOH B . F 4 HOH 34 535 51 HOH HOH B . F 4 HOH 35 536 53 HOH HOH B . F 4 HOH 36 537 54 HOH HOH B . F 4 HOH 37 538 56 HOH HOH B . F 4 HOH 38 539 57 HOH HOH B . F 4 HOH 39 540 58 HOH HOH B . F 4 HOH 40 541 59 HOH HOH B . F 4 HOH 41 542 61 HOH HOH B . F 4 HOH 42 543 63 HOH HOH B . F 4 HOH 43 544 64 HOH HOH B . F 4 HOH 44 545 66 HOH HOH B . F 4 HOH 45 546 67 HOH HOH B . F 4 HOH 46 547 68 HOH HOH B . F 4 HOH 47 548 69 HOH HOH B . F 4 HOH 48 549 70 HOH HOH B . F 4 HOH 49 550 72 HOH HOH B . F 4 HOH 50 551 73 HOH HOH B . F 4 HOH 51 552 74 HOH HOH B . F 4 HOH 52 553 76 HOH HOH B . F 4 HOH 53 554 77 HOH HOH B . F 4 HOH 54 555 78 HOH HOH B . F 4 HOH 55 556 79 HOH HOH B . F 4 HOH 56 557 81 HOH HOH B . F 4 HOH 57 558 82 HOH HOH B . F 4 HOH 58 559 83 HOH HOH B . F 4 HOH 59 560 84 HOH HOH B . F 4 HOH 60 561 85 HOH HOH B . # loop_ _pdbx_prerelease_seq.entity_id _pdbx_prerelease_seq.seq_one_letter_code 1 ;AAVTQSPRNKVAVTGEKVTLSCQQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIPDGYKASRPSQEQFSLILESA TPSQTSVYFCASGGGGTLYFGAGTRLSVL ; 2 ;ESQPDPMPDDLHKSSEFTGTMGNMKYLYDDHYVSATKVKSVDKFLAHDLIYNISDKKLKNYDKVKTELLNEDLAKKYKDE VVDVYGSNYYVNCYFSSKDNVWWHGKTCMYGGITKHEGNHFDNGNLQNVLVRVYENKRNTISFEVQTDKKSVTAQELDIK ARNFLINKKNLYEFNSSPYETGYIKFIENNGNTFWYDMMPAPGDKFDQSKYLMMYNDNKTVDSKSVKIEVHLTTKNG ; # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 O B SER 223 ? ? N B SER 225 ? ? 2.10 2 1 O B LEU 171 ? ? OG B SER 177 ? ? 2.19 # loop_ _pdbx_validate_rmsd_bond.id _pdbx_validate_rmsd_bond.PDB_model_num _pdbx_validate_rmsd_bond.auth_atom_id_1 _pdbx_validate_rmsd_bond.auth_asym_id_1 _pdbx_validate_rmsd_bond.auth_comp_id_1 _pdbx_validate_rmsd_bond.auth_seq_id_1 _pdbx_validate_rmsd_bond.PDB_ins_code_1 _pdbx_validate_rmsd_bond.label_alt_id_1 _pdbx_validate_rmsd_bond.auth_atom_id_2 _pdbx_validate_rmsd_bond.auth_asym_id_2 _pdbx_validate_rmsd_bond.auth_comp_id_2 _pdbx_validate_rmsd_bond.auth_seq_id_2 _pdbx_validate_rmsd_bond.PDB_ins_code_2 _pdbx_validate_rmsd_bond.label_alt_id_2 _pdbx_validate_rmsd_bond.bond_deviation 1 1 C A GLY 63 ? ? N A TYR 65 ? ? 0.261 2 1 CB B VAL 38 ? ? CG2 B VAL 38 ? ? 0.159 3 1 CD1 B TYR 90 ? ? CE1 B TYR 90 ? ? 0.154 4 1 CB B CYS 108 ? ? SG B CYS 108 ? ? 0.105 5 1 CG B TYR 179 ? ? CD2 B TYR 179 ? ? 0.082 6 1 CB B TYR 211 ? ? CG B TYR 211 ? ? 0.106 7 1 CD B LYS 219 ? ? CE B LYS 219 ? ? 0.173 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_deviation 1 1 CD B LYS 160 ? ? CE B LYS 160 ? ? NZ B LYS 160 ? ? 14.1 2 1 NE B ARG 162 ? ? CZ B ARG 162 ? ? NH2 B ARG 162 ? ? 3.1 3 1 C B SER 177 ? ? N B PRO 178 ? ? CA B PRO 178 ? ? 9.2 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ALA A 3 ? -17.76 -87.97 2 1 GLU A 17 ? -46.35 156.83 3 1 THR A 26 ? -140.73 -11.39 4 1 ASN A 28 ? 38.73 70.91 5 1 THR A 39 ? -35.57 95.42 6 1 HIS A 41 ? -130.08 -131.21 7 1 ILE A 60 ? -101.30 55.40 8 1 ASP A 62 ? -31.69 132.25 9 1 SER A 71 ? -176.45 122.12 10 1 GLN A 72 ? -10.18 -45.37 11 1 GLU A 80 ? -76.30 -73.08 12 1 GLN A 86 ? -63.55 11.10 13 1 SER A 88 ? -172.08 -153.45 14 1 LEU A 100 ? -164.44 117.59 15 1 PRO B 8 ? -29.10 -72.62 16 1 MET B 21 ? -55.03 6.75 17 1 LYS B 37 ? 58.33 79.06 18 1 SER B 40 ? -42.98 153.02 19 1 ASP B 42 ? 179.36 -160.55 20 1 LYS B 43 ? 176.07 144.25 21 1 PHE B 44 ? -102.92 -89.31 22 1 ALA B 46 ? -56.77 16.78 23 1 HIS B 47 ? -162.73 32.09 24 1 ASN B 52 ? -115.19 75.45 25 1 LEU B 58 ? -112.12 -112.91 26 1 LYS B 59 ? -168.17 22.92 27 1 LYS B 76 ? -32.17 -32.28 28 1 TYR B 85 ? -161.74 101.83 29 1 TYR B 90 ? -133.65 -59.32 30 1 VAL B 91 ? -47.17 109.63 31 1 ASN B 92 ? 79.24 36.09 32 1 PHE B 95 ? -145.61 21.94 33 1 SER B 96 ? -156.32 -142.10 34 1 TRP B 103 ? -139.40 -81.24 35 1 HIS B 104 ? 112.76 156.86 36 1 MET B 109 ? -169.30 -160.19 37 1 ASN B 119 ? -140.95 -16.61 38 1 ASP B 122 ? -27.07 -79.71 39 1 LYS B 137 ? 74.52 30.58 40 1 ILE B 166 ? -59.11 -70.69 41 1 ASN B 167 ? -50.50 -6.64 42 1 LYS B 168 ? -142.62 -17.93 43 1 ASN B 170 ? 36.28 52.90 44 1 SER B 176 ? -179.19 -154.69 45 1 ASN B 189 ? -30.53 -39.03 46 1 PRO B 200 ? -44.78 172.58 47 1 SER B 209 ? -34.48 -87.49 48 1 LYS B 210 ? -34.81 -21.19 49 1 ASN B 218 ? 31.13 36.46 50 1 SER B 223 ? -38.65 -84.58 51 1 LYS B 224 ? -25.16 -12.45 52 1 SER B 225 ? -131.81 -56.18 53 1 VAL B 226 ? -31.89 145.22 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 'SULFATE ION' SO4 4 water HOH # prodigy-2.2.2/pyproject.toml000066400000000000000000000021561461273102600161140ustar00rootroot00000000000000[tool.poetry] name = "prodigy-prot" license = "Apache-2.0" version = "2.2.2" description = "PROtein binDIng enerGY prediction" authors = [ "Computational Structural Biology Group at Utrecht University ", ] readme = "README.md" classifiers = [ "Development Status :: 5 - Production/Stable", "License :: OSI Approved :: Apache Software License", "Programming Language :: Python :: 3.8", "Programming Language :: Python :: 3.9", "Programming Language :: Python :: 3.10", "Topic :: Scientific/Engineering :: Chemistry", "Topic :: Scientific/Engineering :: Bio-Informatics", ] [tool.poetry.dependencies] python = "^3.9" biopython = "1.80" freesasa = "2.2.1" numpy = "^1.22.0" [tool.poetry.group.test.dependencies] pytest = "^8.1.1" coverage = "^7.4.4" pytest-cov = "^5.0.0" hypothesis = "^6.100.1" [tool.poetry.scripts] prodigy = "prodigy_prot.predict_IC:main" [tool.black] line-length = 79 [tool.setuptools] include-package-data = true packages = ["src"] [tool.pytest.ini_options] pythonpath = ["src"] [build-system] requires = ["poetry-core"] build-backend = "poetry.core.masonry.api" prodigy-2.2.2/src/000077500000000000000000000000001461273102600137635ustar00rootroot00000000000000prodigy-2.2.2/src/prodigy_prot/000077500000000000000000000000001461273102600165045ustar00rootroot00000000000000prodigy-2.2.2/src/prodigy_prot/__init__.py000066400000000000000000000000001461273102600206030ustar00rootroot00000000000000prodigy-2.2.2/src/prodigy_prot/modules/000077500000000000000000000000001461273102600201545ustar00rootroot00000000000000prodigy-2.2.2/src/prodigy_prot/modules/__init__.py000066400000000000000000000004441461273102600222670ustar00rootroot00000000000000#!/usr/bin/env python # # This code is part of the binding affinity prediction tools distribution # and governed by its license. Please see the LICENSE file that should # have been included as part of this package. # """ Binding affinity prediction methods developed by the Bonvin Lab. """ prodigy-2.2.2/src/prodigy_prot/modules/aa_properties.py000066400000000000000000000050411461273102600233630ustar00rootroot00000000000000#!/usr/bin/env python # # This code is part of the binding affinity prediction tools distribution # and governed by its license. Please see the LICENSE file that should # have been included as part of this package. # """ Generic properties of amino acids required for the binding affinity prediction methods. """ __author__ = ["Anna Vangone", "Joao Rodrigues"] aa_character_ic = { "ALA": "A", "CYS": "A", # ? "GLU": "C", "ASP": "C", "GLY": "A", "PHE": "A", "ILE": "A", "HIS": "C", "LYS": "C", "MET": "A", "LEU": "A", "ASN": "P", "GLN": "P", "PRO": "A", "SER": "P", "ARG": "C", "THR": "P", "TRP": "A", "VAL": "A", "TYR": "A", } aa_character_protorp = { "ALA": "A", "CYS": "P", "GLU": "C", "ASP": "C", "GLY": "A", "PHE": "A", "ILE": "A", "HIS": "P", "LYS": "C", "MET": "A", "LEU": "A", "ASN": "P", "GLN": "P", "PRO": "A", "SER": "P", "ARG": "C", "THR": "P", "TRP": "P", "VAL": "A", "TYR": "P", } # Scaling factors for relative ASA # Calculated using extended ALA-X-ALA peptides # Taken from NACCESS rel_asa = { "total": { "ALA": 107.95, "CYS": 134.28, "ASP": 140.39, "GLU": 172.25, "PHE": 199.48, "GLY": 80.10, "HIS": 182.88, "ILE": 175.12, "LYS": 200.81, "LEU": 178.63, "MET": 194.15, "ASN": 143.94, "PRO": 136.13, "GLN": 178.50, "ARG": 238.76, "SER": 116.50, "THR": 139.27, "VAL": 151.44, "TRP": 249.36, "TYR": 212.76, }, "bb": { "ALA": 38.54, "CYS": 37.53, "ASP": 37.70, "GLU": 37.51, "PHE": 35.37, "GLY": 47.77, "HIS": 35.80, "ILE": 37.16, "LYS": 37.51, "LEU": 37.51, "MET": 37.51, "ASN": 37.70, "PRO": 16.23, "GLN": 37.51, "ARG": 37.51, "SER": 38.40, "THR": 37.57, "VAL": 37.16, "TRP": 38.10, "TYR": 35.38, }, "sc": { "ALA": 69.41, "CYS": 96.75, "ASP": 102.69, "GLU": 134.74, "PHE": 164.11, "GLY": 32.33, "HIS": 147.08, "ILE": 137.96, "LYS": 163.30, "LEU": 141.12, "MET": 156.64, "ASN": 106.24, "PRO": 119.90, "GLN": 140.99, "ARG": 201.25, "SER": 78.11, "THR": 101.70, "VAL": 114.28, "TRP": 211.26, "TYR": 177.38, }, } prodigy-2.2.2/src/prodigy_prot/modules/freesasa_tools.py000066400000000000000000000157051461273102600235470ustar00rootroot00000000000000#!/usr/bin/env python # # This code is part of the binding affinity prediction tools distribution # and governed by its license. Please see the LICENSE file that should # have been included as part of this package. # """ Functions to execute freesasa and parse its output. """ from __future__ import division, print_function import os import subprocess # nosec import sys import tempfile import pkg_resources try: from Bio.PDB import PDBIO, PDBParser, Select except ImportError as e: print( "[!] The binding affinity prediction tools require Biopython", file=sys.stderr, ) raise ImportError(e) import contextlib from .aa_properties import rel_asa @contextlib.contextmanager def stdchannel_redirected(stdchannel, dest_filename): """ A context manager to temporarily redirect stdout or stderr https://stackoverflow.com/questions/977840/redirecting-fortran-called-via-f2py-output-in-python/978264#978264 e.g.: with stdchannel_redirected(sys.stderr, os.devnull): if compiler.has_function('clock_gettime', libraries=['rt']): libraries.append('rt') """ oldstdchannel, dest_file = None, None try: oldstdchannel = os.dup(stdchannel.fileno()) dest_file = open(dest_filename, "w") os.dup2(dest_file.fileno(), stdchannel.fileno()) yield finally: if oldstdchannel is not None: os.dup2(oldstdchannel, stdchannel.fileno()) if dest_file is not None: dest_file.close() def execute_freesasa(structure, selection=None): """ Runs the freesasa executable on a PDB file. You can get the executable from: https://github.com/mittinatten/freesasa The binding affinity models are calibrated with the parameter set for vdW radii used in NACCESS: http://www.ncbi.nlm.nih.gov/pubmed/994183 """ io = PDBIO() # try to get freesasa paths from environment if not use the # ones defined in config file try: freesasa, param_f = [ os.environ[key] for key in ["FREESASA_BIN", "FREESASA_PAR"] ] except KeyError as err: message = ( "{} not found. In order to use PRODIGY, set the FREESASA_BIN and " "FREESASA_PAR environment variables to point to the freesasa " "executable and the naccess.config file respectively." ) raise KeyError(message.format(err)) if not os.path.isfile(freesasa): raise IOError( "[!] freesasa binary not found at `{0}`".format(freesasa) ) if not os.path.isfile(param_f): raise IOError( "[!] Atomic radii file not found at `{0}`".format(param_f) ) # Rewrite PDB using Biopython to have a proper format # freesasa is very picky with line width (80 characters or fails!) # Select chains if necessary class ChainSelector(Select): def accept_chain(self, chain): if selection and chain.id in selection: return 1 elif not selection: return 1 else: return 0 _pdbf = tempfile.NamedTemporaryFile() io.set_structure(structure) io.save(_pdbf.name, ChainSelector()) # Run freesasa # Save atomic asa output to another temp file _outf = tempfile.NamedTemporaryFile() cmd = "{0} -o {1} --format=pdb -c {2} {3}".format( freesasa, _outf.name, param_f, _pdbf.name ) p = subprocess.Popen( # nosec cmd, shell=False, stdout=subprocess.PIPE, stderr=subprocess.PIPE, ) stdout, stderr = p.communicate() if p.returncode: print("[!] freesasa did not run successfully", file=sys.stderr) print(cmd, file=sys.stderr) raise Exception(stderr) # Rewind & Parse results file # Save _outf.seek(0) asa, rsa = parse_freesasa_output(_outf) _pdbf.close() _outf.close() return asa, rsa def parse_freesasa_output(fpath): """ Returns per-residue relative accessibility of side-chain and main-chain atoms as calculated by freesasa. """ asa_data, rsa_data = {}, {} _rsa = rel_asa # _bb = {'CA', 'C', 'N', 'O'} p = PDBParser(QUIET=1) s = p.get_structure("bogus", fpath.name) for res in s.get_residues(): res_id = (res.parent.id, res.resname, res.id[1]) _, _, total_asa = 0, 0, 0 for atom in res: aname = atom.name at_id = (res.parent.id, res.resname, res.id[1], aname) asa = atom.bfactor # if atom.name in _bb: # asa_mc += asa # else: # asa_sc += asa total_asa += asa asa_data[at_id] = asa rsa_data[res_id] = total_asa / _rsa["total"][res.resname] return asa_data, rsa_data def execute_freesasa_api(structure): """ Calls freesasa using its Python API and returns per-residue accessibilities. """ try: from freesasa import Classifier, calc, structureFromBioPDB except ImportError as err: print( ( "[!] The binding affinity prediction tools require the " "'freesasa' Python API" ), file=sys.stderr, ) raise ImportError(err) asa_data, rsa_data = {}, {} _rsa = rel_asa["total"] config_path = os.environ.get( "FREESASA_PAR", pkg_resources.resource_filename("prodigy_prot", "naccess.config"), ) classifier = Classifier(config_path) pkg_resources.cleanup_resources() # classifier = freesasa.Classifier( os.environ["FREESASA_PAR"]) # Disable with stdchannel_redirected(sys.stderr, os.devnull): try: struct = structureFromBioPDB( structure, classifier, ) result = calc(struct) except AssertionError as e: error_message = "" + os.linesep() error_message += "[!] Error when running freesasa:" + os.linesep() error_message += f"[!] {e}" + os.linesep() error_message += ( "[!] Make sure the atom names in your PDB file match" " the canonical naming and belong " "to default residues" + os.linesep() ) print(error_message) raise Exception(error_message) # iterate over all atoms to get SASA and residue name for idx in range(struct.nAtoms()): atname = struct.atomName(idx) resname = struct.residueName(idx) resid = struct.residueNumber(idx) chain = struct.chainLabel(idx) at_uid = (chain, resname, resid, atname) res_uid = (chain, resname, resid) asa = result.atomArea(idx) asa_data[at_uid] = asa # add asa to residue rsa_data[res_uid] = rsa_data.get(res_uid, 0) + asa # convert total asa ro relative asa rsa_data.update( (res_uid, asa / _rsa[res_uid[1]]) for res_uid, asa in rsa_data.items() ) return asa_data, rsa_data prodigy-2.2.2/src/prodigy_prot/modules/models.py000066400000000000000000000016631461273102600220170ustar00rootroot00000000000000#!/usr/bin/env python # # This code is part of the binding affinity prediction tools distribution # and governed by its license. Please see the LICENSE file that should # have been included as part of this package. # """ Models to predict binding affinity based on molecular properties. """ def IC_NIS(ic_cc, ic_ca, ic_pp, ic_pa, p_nis_a, p_nis_c): """ Calculates the predicted binding affinity value based on the IC-NIS model. """ return ( -0.09459 * ic_cc + -0.10007 * ic_ca + 0.19577 * ic_pp + -0.22671 * ic_pa + 0.18681 * p_nis_a + 0.13810 * p_nis_c + -15.9433 ) def NIS(p_nis_c, p_nis_p, n_int_atoms): """ Calculates the predicted binding affinity value based on the NIS model. """ return ( 0.0856851248873 * p_nis_p + -0.0685254498746 * p_nis_c + 0.0261591389985 * n_int_atoms + 3.0124939659498 ) prodigy-2.2.2/src/prodigy_prot/modules/nis_utils.py000066400000000000000000000000001461273102600225250ustar00rootroot00000000000000prodigy-2.2.2/src/prodigy_prot/modules/parsers.py000066400000000000000000000112741461273102600222120ustar00rootroot00000000000000#!/usr/bin/env python # # This code is part of the binding affinity prediction tools distribution # and governed by its license. Please see the LICENSE file that should # have been included as part of this package. # """ Functions to read PDB/mmCIF files """ from __future__ import division, print_function import logging import os import sys try: from Bio.PDB import MMCIFParser, PDBParser from Bio.PDB.Polypeptide import PPBuilder, is_aa except ImportError as e: print( "[!] The binding affinity prediction tools require Biopython", file=sys.stderr, ) raise ImportError(e) def validate_structure(s, selection=None, clean=True): # setup logging logger = logging.getLogger("Prodigy") # Keep first model only if len(s) > 1: logger.warning( ( "[!] Structure contains more than one model." " Only the first one will be kept" ) ) model_one = s[0].id for m in s.child_list[:]: if m.id != model_one: s.detach_child(m.id) # process selected chains chains = list(s.get_chains()) chain_ids = set([c.id for c in chains]) if selection: sel_chains = [] # Match selected chain with structure for sel in selection: for c in sel.split(","): sel_chains.append(c) if c not in chain_ids: raise ValueError( "Selected chain not present" f" in provided structure: {c}" ) # Remove unselected chains def _ignore(x): return x.id not in sel_chains for c in chains: if _ignore(c): c.parent.detach_child(c.id) # Double occupancy check for atom in list(s.get_atoms()): if atom.is_disordered(): residue = atom.parent sel_at = atom.selected_child sel_at.altloc = " " sel_at.disordered_flag = 0 residue.detach_child(atom.id) residue.add(sel_at) # Insertion code check for c in chains: for residue in c.get_residues(): if residue.get_id()[2] != " ": c.detach_child(residue.id) if clean: # Remove HETATMs and solvent res_list = list(s.get_residues()) def _ignore(r): return r.id[0][0] == "W" or r.id[0][0] == "H" for res in res_list: if _ignore(res): chain = res.parent chain.detach_child(res.id) elif not is_aa(res, standard=True): raise ValueError( "Unsupported non-standard amino acid found: {0}".format( res.resname ) ) # Remove Hydrogens atom_list = list(s.get_atoms()) def _ignore(x): return x.element == "H" for atom in atom_list: if _ignore(atom): residue = atom.parent residue.detach_child(atom.name) # Detect gaps and compare with no. of chains pep_builder = PPBuilder() peptides = pep_builder.build_peptides(s) n_peptides = len(peptides) if n_peptides != len(chain_ids): message = "[!] Structure contains gaps:\n" for i_pp, pp in enumerate(peptides): message += ( "\t{1.parent.id} {1.resname}{1.id[1]} < Fragment {0} > " "{2.parent.id} {2.resname}{2.id[1]}\n".format( i_pp, pp[0], pp[-1] ) ) logger.warning(message) # raise Exception(message) return s def parse_structure(path): """ Parses a structure using Biopython's PDB/mmCIF Parser Verifies the integrity of the structure (gaps) and its suitability for the calculation (is it a complex?). """ # setup logging logger = logging.getLogger("Prodigy") logger.info("[+] Reading structure file: {0}".format(path)) fname = os.path.basename(path) sname = ".".join(fname.split(".")[:-1]) s_ext = fname.split(".")[-1] _ext = {"pdb", "ent", "cif"} if s_ext not in _ext: raise IOError( f"[!] Structure format '{s_ext}' is " "not supported. Use '.pdb' or '.cif'." ) sparser = PDBParser(QUIET=1) if s_ext in {"pdb", "ent"} else MMCIFParser() try: s = sparser.get_structure(sname, path) except Exception as exeption: logger.error("[!] Structure '{0}' could not be parsed".format(sname)) raise Exception(exeption) return ( validate_structure(s), len(set([c.id for c in s.get_chains()])), len(list(s.get_residues())), ) prodigy-2.2.2/src/prodigy_prot/modules/utils.py000066400000000000000000000013101461273102600216610ustar00rootroot00000000000000#!/usr/bin/env python # # This code is part of the binding affinity prediction tools distribution # and governed by its license. Please see the LICENSE file that should # have been included as part of this package. # """ Assorted utility functions. """ import math import os def check_path(path): """ Checks if a file is readable. """ full_path = os.path.abspath(path) if not os.path.isfile(full_path): raise IOError("Could not read file: {0}".format(path)) return full_path def dg_to_kd(dg, temperature=25.0): """Coversion of DG into the dissociation constant kd""" temp_in_k = temperature + 273.15 rt = 0.0019858775 * temp_in_k return math.exp(dg / rt) prodigy-2.2.2/src/prodigy_prot/naccess.config000066400000000000000000000053241461273102600213160ustar00rootroot00000000000000# Contributed by João Rodrigues name: NACCESS types: C_ALI 1.87 apolar C_CAR 1.76 apolar C_NUC 1.80 apolar N_AMN 1.50 polar N_AMD 1.65 polar N_NUC 1.60 polar O 1.40 polar S 1.85 apolar SE 1.80 apolar P 1.90 apolar atoms: ANY C C_CAR ANY O O ANY CA C_ALI ANY N N_AMD ANY CB C_ALI ANY OXT O # nucleic acid ANY P P ANY OP1 O ANY OP2 O ANY OP3 O ANY O5' O ANY O4' O ANY O3' O ANY O2' O ANY C5' C_NUC ANY C4' C_NUC ANY C3' C_NUC ANY C2' C_NUC ANY C1' C_NUC ALA CB C_ALI # included so that RSA values will be generated ARG CG C_ALI ARG CD C_ALI ARG NE N_AMD ARG CZ C_CAR ARG NH1 N_AMD ARG NH2 N_AMD ASN CG C_CAR ASN OD1 O ASN ND2 N_AMD ASP CG C_CAR ASP OD1 O ASP OD2 O CYS SG S GLN CG C_ALI GLN CD C_CAR GLN OE1 O GLN NE2 N_AMD GLU CG C_ALI GLU CD C_CAR GLU OE1 O GLU OE2 O GLY CA C_ALI # included so that RSA values will be generated HIS CG C_CAR HIS ND1 N_AMD HIS CD2 C_CAR HIS NE2 N_AMD HIS CE1 C_CAR ILE CG1 C_ALI ILE CG2 C_ALI ILE CD1 C_ALI LEU CG C_ALI LEU CD1 C_ALI LEU CD2 C_ALI LYS CG C_ALI LYS CD C_ALI LYS CE C_ALI LYS NZ N_AMN MET CG C_ALI MET SD S MET CE C_ALI PHE CG C_CAR PHE CD1 C_CAR PHE CD2 C_CAR PHE CE1 C_CAR PHE CE2 C_CAR PHE CZ C_CAR PRO CG C_ALI PRO CD C_ALI SEC SE SE SER OG O THR OG1 O THR CG2 C_ALI TRP CG C_CAR TRP CD1 C_CAR TRP CD2 C_CAR TRP NE1 N_AMD TRP CE2 C_CAR TRP CE3 C_CAR TRP CZ2 C_CAR TRP CZ3 C_CAR TRP CH2 C_CAR TYR CG C_CAR TYR CD1 C_CAR TYR CD2 C_CAR TYR CE1 C_CAR TYR CE2 C_CAR TYR CZ C_CAR TYR OH O VAL CG1 C_ALI VAL CG2 C_ALI A N9 N_NUC A C8 C_NUC A N7 N_NUC A C5 C_NUC A C6 C_NUC A N6 N_NUC A N1 N_NUC A C2 C_NUC A N3 N_NUC A C4 C_NUC C N1 N_NUC C C2 C_NUC C O2 O C N3 N_NUC C C4 C_NUC C N4 N_NUC C C5 C_NUC C C6 C_NUC G N9 N_NUC G C8 C_NUC G N7 N_NUC G C5 C_NUC G C6 C_NUC G O6 O G N1 N_NUC G C2 C_NUC G N2 N_NUC G N3 N_NUC G C4 C_NUC I N9 N_NUC I C8 C_NUC I N7 N_NUC I C5 C_NUC I C6 C_NUC I O6 O I N1 N_NUC I C2 C_NUC I N3 N_NUC I C4 C_NUC T N1 N_NUC T C2 C_NUC T O2 O T N3 N_NUC T C4 C_NUC T O4 O T C5 C_NUC T C7 C_NUC T C6 C_NUC U N1 N_NUC U C2 C_NUC U O2 O U N3 N_NUC U C4 C_NUC U O4 O U C5 C_NUC U C6 C_NUC DA N9 N_NUC DA C8 C_NUC DA N7 N_NUC DA C5 C_NUC DA C6 C_NUC DA N6 N_NUC DA N1 N_NUC DA C2 C_NUC DA N3 N_NUC DA C4 C_NUC DC N1 N_NUC DC C2 C_NUC DC O2 O DC N3 N_NUC DC C4 C_NUC DC N4 N_NUC DC C5 C_NUC DC C6 C_NUC DG N9 N_NUC DG C8 C_NUC DG N7 N_NUC DG C5 C_NUC DG C6 C_NUC DG O6 O DG N1 N_NUC DG C2 C_NUC DG N2 N_NUC DG N3 N_NUC DG C4 C_NUC DI N9 N_NUC DI C8 C_NUC DI N7 N_NUC DI C5 C_NUC DI C6 C_NUC DI O6 O DI N1 N_NUC DI C2 C_NUC DI N3 N_NUC DI C4 C_NUC DT N1 N_NUC DT C2 C_NUC DT O2 O DT N3 N_NUC DT C4 C_NUC DT O4 O DT C5 C_NUC DT C7 C_NUC DT C6 C_NUC DU N1 N_NUC DU C2 C_NUC DU O2 O DU N3 N_NUC DU C4 C_NUC DU O4 O DU C5 C_NUC DU C6 C_NUC prodigy-2.2.2/src/prodigy_prot/predict_IC.py000066400000000000000000000317501461273102600210710ustar00rootroot00000000000000# coding: utf-8 # !/usr/bin/env python # # This code is part of the binding affinity prediction tools distribution # and governed by its license. Please see the LICENSE file that should # have been included as part of this package. # """ Binding affinity predictor based on Intermolecular Contacts (ICs). Anna Vangone and Alexandre M.J.J. Bonvin, Contacts-based prediction of binding affinity in protein-protein complexes. eLife (2015) """ from __future__ import division, print_function __author__ = ["Anna Vangone", "Joao Rodrigues", "Joerg Schaarschmidt"] import logging import sys try: from Bio.PDB import NeighborSearch except ImportError as e: print( "[!] The binding affinity prediction tools require Biopython", file=sys.stderr, ) raise ImportError(e) from prodigy_prot.modules import aa_properties from prodigy_prot.modules.freesasa_tools import execute_freesasa_api from prodigy_prot.modules.models import IC_NIS from prodigy_prot.modules.parsers import parse_structure from prodigy_prot.modules.utils import check_path, dg_to_kd def calculate_ic(struct, d_cutoff=5.5, selection=None): """ Calculates intermolecular contacts in a parsed struct object. """ atom_list = list(struct.get_atoms()) ns = NeighborSearch(atom_list) all_list = ns.search_all(radius=d_cutoff, level="R") if selection: _sd = selection def _chain(x): return x.parent.id ic_list = [ c for c in all_list if (_chain(c[0]) in _sd and _chain(c[1]) in _sd) and (_sd[_chain(c[0])] != _sd[_chain(c[1])]) ] else: ic_list = [c for c in all_list if c[0].parent.id != c[1].parent.id] if not ic_list: raise ValueError("No contacts found for selection") return ic_list def analyse_contacts(contact_list): """ Enumerates and classifies contacts based on the chemical characteristics of the participating amino acids. """ bins = { "AA": 0, "PP": 0, "CC": 0, "AP": 0, "CP": 0, "AC": 0, } _data = aa_properties.aa_character_ic for res_i, res_j in contact_list: contact_type = (_data.get(res_i.resname), _data.get(res_j.resname)) contact_type = "".join(sorted(contact_type)) bins[contact_type] += 1 return bins def analyse_nis(sasa_dict, acc_threshold=0.05): """ Returns the percentages of apolar, polar, and charged residues at the interface, according to an accessibility criterion. """ _data = aa_properties.aa_character_protorp def _char_to_index(x): return {"A": 0, "C": 1, "P": 2}.get(x) count = [0, 0, 0] for res, rsa in sasa_dict.items(): chain, resn, resi = res if rsa >= acc_threshold: aa_character = _data[resn] aa_index = _char_to_index(aa_character) count[aa_index] += 1 percentages = [100 * x / sum(count) for x in count] # print('[+] No. of buried interface residues: {0}'.format(sum(count))) return percentages class Prodigy: # init parameters def __init__(self, struct_obj, selection=None, temp=25.0): self.temp = float(temp) if selection is None: self.selection = [chain.id for chain in struct_obj.get_chains()] else: self.selection = selection self.structure = struct_obj self.ic_network = {} self.bins = {} self.nis_a = 0 self.nis_c = 0 self.ba_val = 0 self.kd_val = 0 def predict(self, temp=None, distance_cutoff=5.5, acc_threshold=0.05): if temp is not None: self.temp = temp # Make selection dict from user option or PDB chains selection_dict = {} for igroup, group in enumerate(self.selection): chains = group.split(",") for chain in chains: if chain in selection_dict: errmsg = ( "Selections must be disjoint sets: " f"{chain} is repeated" ) raise ValueError(errmsg) selection_dict[chain] = igroup # Contacts self.ic_network = calculate_ic( self.structure, d_cutoff=distance_cutoff, selection=selection_dict ) self.bins = analyse_contacts(self.ic_network) # SASA _, cmplx_sasa = execute_freesasa_api(self.structure) self.nis_a, self.nis_c, _ = analyse_nis( cmplx_sasa, acc_threshold=acc_threshold ) # Affinity Calculation self.ba_val = IC_NIS( self.bins["CC"], self.bins["AC"], self.bins["PP"], self.bins["AP"], self.nis_a, self.nis_c, ) self.kd_val = dg_to_kd(self.ba_val, self.temp) def as_dict(self): return_dict = { "structure": self.structure.id, "selection": self.selection, "temp": self.temp, "ICs": len(self.ic_network), "nis_a": self.nis_a, "nis_c": self.nis_c, "ba_val": self.ba_val, "kd_val": self.kd_val, } return_dict.update(self.bins) return return_dict def print_prediction(self, outfile="", quiet=False): if outfile: handle = open(outfile, "w") else: handle = sys.stdout if quiet: handle.write( "{0}\t{1:8.3f}\n".format(self.structure.id, self.ba_val) ) else: handle.write( "[+] No. of intermolecular contacts: {0}\n".format( len(self.ic_network) ) ) handle.write( "[+] No. of charged-charged contacts: {0}\n".format( self.bins["CC"] ) ) handle.write( "[+] No. of charged-polar contacts: {0}\n".format( self.bins["CP"] ) ) handle.write( "[+] No. of charged-apolar contacts: {0}\n".format( self.bins["AC"] ) ) handle.write( "[+] No. of polar-polar contacts: {0}\n".format( self.bins["PP"] ) ) handle.write( "[+] No. of apolar-polar contacts: {0}\n".format( self.bins["AP"] ) ) handle.write( "[+] No. of apolar-apolar contacts: {0}\n".format( self.bins["AA"] ) ) handle.write( "[+] Percentage of apolar NIS residues: {0:3.2f}\n".format( self.nis_a ) ) handle.write( "[+] Percentage of charged NIS residues: {0:3.2f}\n".format( self.nis_c ) ) handle.write( "[++] Predicted binding " "affinity (kcal.mol-1): {0:8.1f}\n".format(self.ba_val) ) handle.write( "[++] Predicted dissociation constant (M) at {:.1f}˚C:" " {:8.1e}\n".format(self.temp, self.kd_val) ) if handle is not sys.stdout: handle.close() def print_contacts(self, outfile=""): if outfile: handle = open(outfile, "w") else: handle = sys.stdout for res1, res2 in self.ic_network: _fmt_str = ( "{0.resname:>5s} {0.id[1]:5} {0.parent.id:>3s} {1.resname:>5s}" " {1.id[1]:5} {1.parent.id:>3s}\n" ) if res1.parent.id not in self.selection[0]: res1, res2 = res2, res1 handle.write(_fmt_str.format(res1, res2)) if handle is not sys.stdout: handle.close() def print_pymol_script(self, outfile=""): # Writing output PYMOL: pml script # initialize array with chains and save chain selection string selection_strings = [] chains = {} for s in self.selection: selection_strings.append(s.replace(",", "+")) for c in s.split(","): chains[c] = set() # loop over pairs and add interface residues to respective chains for pair in self.ic_network: for r in pair: chains[r.parent.id].add(str(r.id[1])) # set output stream handle = open(outfile, "w") if outfile else sys.stdout # write default setup strings handle.writelines( [ "color silver\n", "as cartoon\n", "bg_color white\n", "center\n", "color lightblue, chain {}\n".format(selection_strings[0]), "color lightpink, chain {}\n".format(selection_strings[1]), ] ) # loop over interfaces construct selection strings # and write interface related commands for color, iface in [("blue", 1), ("hotpink", 2)]: p_sel_string = " or ".join( [ "chain {} and resi {}".format(c, "+".join(chains[c])) for c in selection_strings[iface - 1].split("+") ] ) handle.write("select iface{}, {}\n".format(iface, p_sel_string)) handle.write("color {}, iface{}\n".format(color, iface)) handle.write("show sticks, iface{}\n".format(iface)) # close file handle if applicable if handle is not sys.stdout: handle.close() def main(): try: import argparse from argparse import RawTextHelpFormatter except ImportError as err: print( "[!] The binding affinity prediction tools require Python 2.7+", file=sys.stderr, ) raise ImportError(err) ap = argparse.ArgumentParser( description=__doc__, formatter_class=RawTextHelpFormatter ) ap.add_argument( "structf", help="Structure to analyse in PDB or mmCIF format" ) ap.add_argument( "--distance-cutoff", type=float, default=5.5, help="Distance cutoff to calculate ICs", ) ap.add_argument( "--acc-threshold", type=float, default=0.05, help="Accessibility threshold for BSA analysis", ) ap.add_argument( "--temperature", type=float, default=25.0, help="Temperature (C) for Kd prediction", ) ap.add_argument( "--contact_list", action="store_true", help="Output a list of contacts" ) ap.add_argument( "--pymol_selection", action="store_true", help="Output a script to highlight the interface (pymol)", ) ap.add_argument( "-q", "--quiet", action="store_true", help="Outputs only the predicted affinity value", ) _co_help = """ By default, all intermolecular contacts are taken into consideration, a molecule being defined as an isolated group of amino acids sharing a common chain identifier. In specific cases, for example antibody-antigen complexes, some chains should be considered as a single molecule. Use the --selection option to provide collections of chains that should be considered for the calculation. Separate by a space the chains that are to be considered _different_ molecules. Use commas to include multiple chains as part of a single group: --selection A B => Contacts calculated (only) between chains A and B. --selection A,B C => Contacts calculated (only) between \ chains A and C; and B and C. --selection A B C => Contacts calculated (only) between \ chains A and B; B and C; and A and C. """ sel_opt = ap.add_argument_group("Selection Options", description=_co_help) sel_opt.add_argument("--selection", nargs="+", metavar=("A B", "A,B C")) cmd = ap.parse_args() # setup logging log_level = logging.ERROR if cmd.quiet else logging.INFO logging.basicConfig( level=log_level, stream=sys.stdout, format="%(message)s" ) logger = logging.getLogger("Prodigy") struct_path = check_path(cmd.structf) # Parse structure structure, n_chains, n_res = parse_structure(struct_path) logger.info( "[+] Parsed structure file {0} ({1} chains, {2} residues)".format( structure.id, n_chains, n_res ) ) prodigy = Prodigy(structure, cmd.selection, cmd.temperature) prodigy.predict( distance_cutoff=cmd.distance_cutoff, acc_threshold=cmd.acc_threshold ) prodigy.print_prediction(quiet=cmd.quiet) # Print out interaction network if cmd.contact_list: fname = struct_path[:-4] + ".ic" prodigy.print_contacts(fname) # Print out interaction network if cmd.pymol_selection: fname = struct_path[:-4] + ".pml" prodigy.print_pymol_script(fname) if __name__ == "__main__": main() prodigy-2.2.2/tests/000077500000000000000000000000001461273102600143365ustar00rootroot00000000000000prodigy-2.2.2/tests/__init__.py000066400000000000000000000000001461273102600164350ustar00rootroot00000000000000prodigy-2.2.2/tests/test_prodigy.py000066400000000000000000000066051461273102600174330ustar00rootroot00000000000000# !/usr/bin/env python """ Run the prodigy tests. """ from __future__ import division, print_function import json import tarfile import unittest from io import BufferedReader, TextIOWrapper from os import devnull from os.path import basename, dirname, join, splitext from sys import stderr, version_info import numpy as np from Bio.PDB import PDBParser, Structure from prodigy_prot.modules.freesasa_tools import stdchannel_redirected from prodigy_prot.modules.parsers import validate_structure from prodigy_prot.predict_IC import Prodigy def get_data_path(path): """ Get the path of a file in data for file input Args: path: path within data folder Returns: The path to the data file in unix notation """ try: return join(dirname(__file__), "..", "data", *path.split("/")) except NameError: # return join("data", *path.split("/")) class ProdigyOutputTest(unittest.TestCase): def test_dataset(self): """ Test method to compare prediction for 80 dataset cases with expected values. """ # load expected data from json with open(get_data_path("dataset.json")) as fh: expected_data = json.load(fh) # load dataset PDBs dataset = tarfile.open(get_data_path("dataset.tgz")) parser = PDBParser(QUIET=True) keys_equal = ["AA", "PP", "CC", "AP", "CP", "AC"] diffs = {"ba_val": [], "nis_a": [], "nis_c": []} # run prodigy for each dataset in the PDB for entry in dataset: s_name, s_ext = splitext(basename(entry.name)) # skip system files in archive if not s_name.isalnum() or s_ext != ".pdb": continue # chains = expected_data[s_name]["Interacting_chains"] handle = dataset.extractfile(entry) # Wrap filehandle to ensure string file handle in Python 3 if version_info[0] >= 3: handle = TextIOWrapper(BufferedReader(handle)) # type: ignore # Suppress gap warnings when parsing structure with stdchannel_redirected(stderr, devnull): s = validate_structure( parser.get_structure(s_name, handle), selection=["A", "B"] ) # Test for structure object self.assertIsInstance(s, Structure.Structure) # instantiate Prdigy object, # run prediction and retrieve result dict prod = Prodigy(s, selection=["A", "B"]) prod.predict() results = prod.as_dict() # check for equality of prdicted interface residues for k in keys_equal: self.assertEqual(results[k], expected_data[s_name][k]) # check that NIS and binding afinity values are within 2% of # expected values and add diffs for summary for k in diffs.keys(): delta = abs(results[k] / expected_data[s_name][k] - 1) # assume a difference of less then 2% self.assertAlmostEqual(delta, 0, delta=0.02) diffs[k].append(delta) # summarize and print calculated delta values print("Deltas:") for k in diffs.keys(): print(" {} max: {:.2%}".format(k, max(diffs[k]))) print(" {} mean: {:.2%}".format(k, np.mean(diffs[k]))) if __name__ == "__main__": unittest.main()

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