From ae19c8ca2b69263aaa59b40da06b521fec3d3afb Mon Sep 17 00:00:00 2001 From: Aleix Lafita Date: Thu, 29 Jun 2017 16:03:42 -0700 Subject: [PATCH 01/10] Organize the MMTF tests --- .../io/mmtf/MmtfStructureReader.java | 2 + .../io/mmtf/MmtfStructureWriter.java | 5 +- .../structure/io/mmtf/TestBondFinding.java | 24 +- .../io/mmtf/TestMmtfPerformance.java | 19 +- .../structure/io/mmtf/TestMmtfRoundTrip.java | 21 +- .../io/mmtf/TestMmtfStructureReader.java | 65 + ...Mmtf.java => TestMmtfStructureWriter.java} | 55 +- .../nbio/structure/io/mmtf/TestMmtfUtils.java | 6 +- .../biojava/nbio/structure/io/mmtf/4CUP.cif | 3305 +++++++++++++++++ 9 files changed, 3449 insertions(+), 53 deletions(-) create mode 100644 biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java rename biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/{TestBasicMmtf.java => TestMmtfStructureWriter.java} (67%) create mode 100644 biojava-structure/src/test/resources/org/biojava/nbio/structure/io/mmtf/4CUP.cif diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java index 961a5a483f..7eb07e806a 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java @@ -47,6 +47,8 @@ * Should be ported to biojava code. * * @author Anthony Bradley + * @since 5.0 + * */ public class MmtfStructureReader implements StructureAdapterInterface, Serializable { diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureWriter.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureWriter.java index f8a2d13672..b47b2b1dcb 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureWriter.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureWriter.java @@ -19,14 +19,15 @@ import org.rcsb.mmtf.dataholders.MmtfStructure; /** - * Class to take Biojava structure data and covert to the DataApi for encoding. + * Class to take Biojava structure data and covert to the DataApi for encoding. * Must implement all the functions in {@link StructureAdapterInterface}. + * * @author Anthony Bradley + * @since 5.0 * */ public class MmtfStructureWriter { - private StructureAdapterInterface mmtfDecoderInterface; /** diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestBondFinding.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestBondFinding.java index 38ac99899b..e5580c4c94 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestBondFinding.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestBondFinding.java @@ -21,37 +21,46 @@ /** * Test bond finding in BioJava + * * @author Anthony Bradley * */ public class TestBondFinding { /** - * Test that the bonds we are finding is consistenty. + * Test that the bonds we are finding are consistent. + * * @throws IOException * @throws StructureException */ @Test public void testInterGroupBonds() throws IOException, StructureException { + // Normal assertEquals(2236, getInterBonds("1QMZ")); + // Disulphide assertEquals(956, getInterBonds("2QWO")); + // Covalent ligand assertEquals(2294, getInterBonds("4QDV")); + // DNA assertEquals(22, getInterBonds("4XSN")); } /** - * Find all of the inter group bonds in a structure + * Find all of the inter group bonds in a structure. + * * @param pdbId the pdb id of the structure to determine * @return the number of inter group bonds (double counted) in a structure * @throws IOException * @throws StructureException */ - public int getInterBonds(String pdbId) throws IOException, StructureException{ + public int getInterBonds(String pdbId) throws IOException, StructureException { + + // Download parameters AtomCache cache = new AtomCache(); cache.setUseMmCif(true); cache.setFetchBehavior(FetchBehavior.FETCH_FILES); @@ -64,10 +73,13 @@ public int getInterBonds(String pdbId) throws IOException, StructureException{ dcc.checkDoFirstInstall(); cache.setFileParsingParams(params); StructureIO.setAtomCache(cache); - int counter =0; - // Now get the structure + + // Get the structure Structure newStruc = StructureIO.getStructure(pdbId); - // Now loop through the atoms + + int counter =0; + + // Loop through the atoms and count the bonds for(Chain c: newStruc.getChains()){ for(Group g: c.getAtomGroups()){ List theseAtoms = g.getAtoms(); diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfPerformance.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfPerformance.java index 2f7b9cbe65..823ff20236 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfPerformance.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfPerformance.java @@ -1,31 +1,23 @@ package org.biojava.nbio.structure.io.mmtf; import org.biojava.nbio.structure.Structure; -import org.biojava.nbio.structure.StructureIO; -import org.biojava.nbio.structure.TestStructureCrossReferences; import org.biojava.nbio.structure.io.PDBFileParser; -import org.biojava.nbio.structure.io.mmcif.AllChemCompProvider; -import org.biojava.nbio.structure.io.mmcif.ChemCompGroupFactory; -import org.biojava.nbio.structure.io.mmcif.ChemCompProvider; import org.junit.Test; -import org.rcsb.mmtf.dataholders.MmtfStructure; -import org.rcsb.mmtf.decoder.ReaderUtils; import org.slf4j.Logger; import org.slf4j.LoggerFactory; import java.io.*; import java.net.URL; -import java.nio.file.Files; -import java.nio.file.Path; -import java.nio.file.Paths; import java.util.zip.GZIPInputStream; -import static org.junit.Assert.assertEquals; -import static org.junit.Assert.assertNotNull; import static org.junit.Assert.assertTrue; /** - * Created by andreas on 1/9/17. + * Test the performance of MMTF format in BioJava. + * + * @author Andreas Prlic + * on 1/9/17. + * */ public class TestMmtfPerformance { @@ -35,6 +27,7 @@ public class TestMmtfPerformance { // Returns the contents of the file in a byte array. public static byte[] getBytesFromFile(File file) throws IOException { + // Get the size of the file long length = file.length(); diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfRoundTrip.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfRoundTrip.java index e3ef070731..d22fae960d 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfRoundTrip.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfRoundTrip.java @@ -24,6 +24,7 @@ /** * Tests to see if roundtripping of MMTF can be done. + * * @author Anthony Bradley * */ @@ -31,22 +32,29 @@ public class TestMmtfRoundTrip { /** * Test that we can round trip a simple structure. + * * @throws IOException an error reading the file * @throws StructureException an error parsing the structure */ @Test public void testRoundTrip() throws IOException, StructureException { + + // Load a structure in MMCIF format AtomCache cache = new AtomCache(); cache.setUseMmCif(true); ChemCompGroupFactory.setChemCompProvider(new DownloadChemCompProvider()); - StructureIO.setAtomCache(cache); Structure structure = StructureIO.getStructure("4CUP"); + + // Write the structure to a MMTF encoding AdapterToStructureData writerToEncoder = new AdapterToStructureData(); new MmtfStructureWriter(structure, writerToEncoder); + + // Load back the structure from the MMTF encoding MmtfStructureReader mmtfStructureReader = new MmtfStructureReader(); new StructureDataToAdapter(writerToEncoder, mmtfStructureReader); + assertTrue(checkIfAtomsSame(structure,mmtfStructureReader.getStructure())); } @@ -58,18 +66,23 @@ public void testRoundTrip() throws IOException, StructureException { * @return */ private boolean checkIfAtomsSame(Structure structOne, Structure structTwo) { + + // Check the same number of models int numModels = structOne.nrModels(); if(numModels!=structTwo.nrModels()){ System.out.println("Error - diff number models: "+structOne.getPDBCode()); return false; } + for(int i=0;i chainsOne = structOne.getChains(i); List chainsTwo = structTwo.getChains(i); if(chainsOne.size()!=chainsTwo.size()){ System.out.println("Error - diff number chains: "+structOne.getPDBCode()); return false; } + // Now make sure they're sorted in the right order sortChains(chainsOne, chainsTwo); // Check that each one has the same number of poly, non-poly and water chains @@ -182,8 +195,9 @@ else if(atomOne.getBonds().size()!=atomTwo.getBonds().size()){ } return true; } + /** - * Check both structures have the same number of poly,non-poly and water chains + * Check both structures have the same number of poly, non-poly and water chains * @param structOne the first structure * @param structTwo the second structure * @param i the model index @@ -193,8 +207,10 @@ private void checkDiffChains(Structure structOne, Structure structTwo, int i) { assertEquals(structOne.getNonPolyChains(i).size(), structTwo.getNonPolyChains(i).size()); assertEquals(structOne.getWaterChains(i).size(), structTwo.getWaterChains(i).size()); } + /** * Sort the atom based on PDB serial id + * * @param atomsOne the first list * @param atomsTwo the second list */ @@ -227,6 +243,7 @@ public int compare(Atom o1, Atom o2) { /** * Sort the chains based on chain id. + * * @param chainsOne the first list of chains * @param chainsTwo the second list of chains */ diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java new file mode 100644 index 0000000000..0f797bc55a --- /dev/null +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java @@ -0,0 +1,65 @@ +package org.biojava.nbio.structure.io.mmtf; + +import static org.junit.Assert.assertEquals; + +import java.io.IOException; +import java.nio.file.Paths; +import org.biojava.nbio.structure.Structure; +import org.biojava.nbio.structure.StructureException; +import org.biojava.nbio.structure.StructureIO; +import org.junit.Test; + +/** + * Test the Biojava MMTF reader. + * + * @author Anthony Bradley + * @author Aleix Lafita + * + */ +public class TestMmtfStructureReader { + + /** + * Test reading an MMTF file into a BioJava structure. + */ + @Test + public void testRead() throws IOException { + + // Get the MMTF file from the resources folder + ClassLoader classLoader = getClass().getClassLoader(); + String resource = "org/biojava/nbio/structure/io/mmtf/4CUP.mmtf"; + + // Load the structure into memory + Structure structure = MmtfActions.readFromFile(( + Paths.get(classLoader.getResource(resource).getPath()))); + + // Check header properties of the structure + assertEquals(structure.getPDBCode(), "4CUP"); + assertEquals(MmtfUtils.dateToIsoString(structure.getPDBHeader().getDepDate()), + "2014-03-21"); + + assertEquals(structure.getChains().size(), 6); + } + + /** + * Compare structures loaded from MMCIF and MMTF files. + */ + @Test + public void compareMmcif() throws IOException, StructureException { + + // Get the MMTF and MMCIF files from the resources folder + ClassLoader classLoader = getClass().getClassLoader(); + String resource = "org/biojava/nbio/structure/io/mmtf/4CUP"; + + // Load the structures into memory + Structure mmtf = StructureIO.getStructure(classLoader.getResource(resource).getPath() + ".mmtf"); + Structure mmcif = StructureIO.getStructure(classLoader.getResource(resource).getPath() + ".mmcif"); + + // Compare the SEQRES + assertEquals(mmcif.getChain("A").getSeqResSequence(), + mmtf.getChain("A").getSeqResSequence()); + + + + } + +} diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestBasicMmtf.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureWriter.java similarity index 67% rename from biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestBasicMmtf.java rename to biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureWriter.java index 5e91ff195e..0f7178abc4 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestBasicMmtf.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureWriter.java @@ -1,10 +1,7 @@ package org.biojava.nbio.structure.io.mmtf; -import static org.junit.Assert.assertEquals; - import java.io.File; import java.io.IOException; -import java.nio.file.Paths; import java.util.ArrayList; import org.biojava.nbio.structure.AminoAcidImpl; @@ -25,63 +22,65 @@ import org.junit.rules.TemporaryFolder; /** - * Test that Biojava can read and write MMTF data. + * Test the Biojava MMTF writer. + * * @author Anthony Bradley + * @author Aleix Lafita * */ -public class TestBasicMmtf { +public class TestMmtfStructureWriter { - /** - * A test folder for testing writing files. - */ - @Rule - public TemporaryFolder testFolder = new TemporaryFolder(); - - - /** - * Test that Biojava can read a file from the file system. - * @throws IOException - */ - @Test - public void testRead() throws IOException { - ClassLoader classLoader = getClass().getClassLoader(); - Structure structure = MmtfActions.readFromFile((Paths.get(classLoader.getResource("org/biojava/nbio/structure/io/mmtf/4CUP.mmtf").getPath()))); - assertEquals(structure.getPDBCode(),"4CUP"); - assertEquals(structure.getChains().size(),6); - } + @Rule + public TemporaryFolder testFolder = new TemporaryFolder(); /** * Test the writing of Structure objects to a file. - * @throws IOException + * + * @throws IOException */ @Test public void testWrite() throws IOException { + + // Create a structure Structure structure = new StructureImpl(); + + // Add some header information PDBHeader pdbHeader = new PDBHeader(); pdbHeader.setExperimentalTechnique("X-RAY DIFFRACTION"); - structure.setEntityInfos(new ArrayList()); structure.setPDBHeader(pdbHeader); + + // Create one chain + structure.setEntityInfos(new ArrayList()); Chain chain = new ChainImpl(); chain.setId("A"); chain.setName("A"); - Group group = new AminoAcidImpl(); + + // Create one group + Group group = new AminoAcidImpl(); group.setPDBName("FKF"); ChemComp chemComp = new ChemComp(); chemComp.setType("TYPfdl"); chemComp.setOne_letter_code("A"); group.setChemComp(chemComp); + + // Create one Atom Atom atom = new AtomImpl(); atom.setName("A"); atom.setElement(Element.Ag); - atom.setCoords(new double[] {1.0,2.0,3.0}); + atom.setCoords(new double[] { 1.0, 2.0, 3.0 }); + + // Link together the objects chain.addGroup(group); group.addAtom(atom); + ResidueNumber residueNumber = new ResidueNumber(); residueNumber.setInsCode('A'); residueNumber.setSeqNum(100); group.setResidueNumber(residueNumber); + structure.addChain(chain); + File tempFile = testFolder.newFile("tmpfile"); - MmtfActions.writeToFile(structure, tempFile.toPath()); + MmtfActions.writeToFile(structure, tempFile.toPath()); } } diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfUtils.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfUtils.java index af0db75615..3e5e2021df 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfUtils.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfUtils.java @@ -1,6 +1,5 @@ package org.biojava.nbio.structure.io.mmtf; - import org.junit.Test; import static org.junit.Assert.*; @@ -38,8 +37,10 @@ import org.biojava.nbio.structure.xtal.BravaisLattice; import org.biojava.nbio.structure.xtal.CrystalCell; import org.biojava.nbio.structure.xtal.SpaceGroup; + /** - * Test the MMTF utils class + * Test the MMTF utils class. + * * @author Anthony Bradley * */ @@ -47,6 +48,7 @@ public class TestMmtfUtils { /** * Integration test to see that the microheterogenity is being dealt with correctly. + * * @throws IOException * @throws StructureException */ diff --git a/biojava-structure/src/test/resources/org/biojava/nbio/structure/io/mmtf/4CUP.cif b/biojava-structure/src/test/resources/org/biojava/nbio/structure/io/mmtf/4CUP.cif new file mode 100644 index 0000000000..3f88049aa2 --- /dev/null +++ b/biojava-structure/src/test/resources/org/biojava/nbio/structure/io/mmtf/4CUP.cif @@ -0,0 +1,3305 @@ +data_4CUP +# +_entry.id 4CUP +# +_audit_conform.dict_name mmcif_pdbx.dic +_audit_conform.dict_version 4.040 +_audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic +# +loop_ +_database_2.database_id +_database_2.database_code +PDB 4CUP +PDBE EBI-60082 +# +_database_PDB_rev.num 1 +_database_PDB_rev.date 2014-04-02 +_database_PDB_rev.date_original 2014-03-21 +_database_PDB_rev.status ? +_database_PDB_rev.replaces 4CUP +_database_PDB_rev.mod_type 0 +# +loop_ +_pdbx_database_related.db_name +_pdbx_database_related.db_id +_pdbx_database_related.content_type +_pdbx_database_related.details +PDB 4CUQ unspecified 'CRYSTAL STRUCTURE OF HUMAN BAZ2B IN COMPLEX WITH FRAGMENT-2 N09594' +PDB 4CUR unspecified 'CRYSTAL STRUCTURE OF HUMAN BAZ2B IN COMPLEX WITH FRAGMENT-3 N09555' +PDB 4CUS unspecified 'CRYSTAL STRUCTURE OF HUMAN BAZ2B IN COMPLEX WITH FRAGMENT-4 N09496' +PDB 4CUT unspecified 'CRYSTAL STRUCTURE OF HUMAN BAZ2B IN COMPLEX WITH FRAGMENT-5 N09428' +PDB 4CUU unspecified 'CRYSTAL STRUCTURE OF HUMAN BAZ2B IN COMPLEX WITH FRAGMENT-6 N09645' +# +_pdbx_database_status.status_code REL +_pdbx_database_status.entry_id 4CUP +_pdbx_database_status.deposit_site PDBE +_pdbx_database_status.process_site PDBE +_pdbx_database_status.SG_entry . +# +loop_ +_audit_author.name +_audit_author.pdbx_ordinal +'Bradley, A.R.' 1 +'Liu, Y.' 2 +'Krojer, T.' 3 +'Bountra, C.' 4 +'Arrowsmith, C.H.' 5 +'Edwards, A.' 6 +'Knapp, S.' 7 +'von Delft, F.' 8 +# +_citation.id primary +_citation.title 'Crystal Structure of Human Baz2B in Complex with Fragment-1 N09421' +_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 'R Bradley, A.' 1 +primary 'Liu, Y.' 2 +primary 'Krojer, T.' 3 +primary 'Bountra, C.' 4 +primary 'Arrowsmith, C.H.' 5 +primary 'Edwards, A.' 6 +primary 'Knapp, S.' 7 +primary 'Von Delft, F.' 8 +# +_cell.entry_id 4CUP +_cell.length_a 80.370 +_cell.length_b 96.120 +_cell.length_c 57.670 +_cell.angle_alpha 90.00 +_cell.angle_beta 90.00 +_cell.angle_gamma 90.00 +_cell.Z_PDB 8 +_cell.pdbx_unique_axis ? +# +_symmetry.entry_id 4CUP +_symmetry.space_group_name_H-M 'C 2 2 21' +_symmetry.pdbx_full_space_group_name_H-M ? +_symmetry.cell_setting ? +_symmetry.Int_Tables_number ? +# +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 'BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B' 13618.761 1 ? ? 'BROMODOMAIN, RESIDUES 1858-1972' ? +2 non-polymer syn 4-FLUOROBENZAMIDOXIME 154.144 1 ? ? ? ? +3 non-polymer syn METHANOL 32.042 3 ? ? ? ? +4 water nat water 18.015 146 ? ? ? ? +# +loop_ +_entity_keywords.entity_id +_entity_keywords.text +1 ? +2 ? +3 ? +4 ? +# +loop_ +_entity_name_com.entity_id +_entity_name_com.name +1 'HWALP4, BAZ2B' +2 ? +3 ? +4 ? +# +_entity_poly.entity_id 1 +_entity_poly.type 'polypeptide(L)' +_entity_poly.nstd_linkage no +_entity_poly.nstd_monomer no +_entity_poly.pdbx_seq_one_letter_code +;SMSVKKPKRDDSKDLALCSMILTEMETHEDAWPFLLPVNLKLVPGYKKVIKKPMDFSTIREKLSSGQYPNLETFALDVRL +VFDNCETFNEDDSDIGRAGHNMRKYFEKKWTDTFKVS +; +_entity_poly.pdbx_seq_one_letter_code_can +;SMSVKKPKRDDSKDLALCSMILTEMETHEDAWPFLLPVNLKLVPGYKKVIKKPMDFSTIREKLSSGQYPNLETFALDVRL +VFDNCETFNEDDSDIGRAGHNMRKYFEKKWTDTFKVS +; +_entity_poly.pdbx_strand_id A +# +loop_ +_entity_poly_seq.entity_id +_entity_poly_seq.num +_entity_poly_seq.mon_id +_entity_poly_seq.hetero +1 1 SER n +1 2 MET n +1 3 SER n +1 4 VAL n +1 5 LYS n +1 6 LYS n +1 7 PRO n +1 8 LYS n +1 9 ARG n +1 10 ASP n +1 11 ASP n +1 12 SER n +1 13 LYS n +1 14 ASP n +1 15 LEU n +1 16 ALA n +1 17 LEU n +1 18 CYS n +1 19 SER n +1 20 MET n +1 21 ILE n +1 22 LEU n +1 23 THR n +1 24 GLU n +1 25 MET n +1 26 GLU n +1 27 THR n +1 28 HIS n +1 29 GLU n +1 30 ASP n +1 31 ALA n +1 32 TRP n +1 33 PRO n +1 34 PHE n +1 35 LEU n +1 36 LEU n +1 37 PRO n +1 38 VAL n +1 39 ASN n +1 40 LEU n +1 41 LYS n +1 42 LEU n +1 43 VAL n +1 44 PRO n +1 45 GLY n +1 46 TYR n +1 47 LYS n +1 48 LYS n +1 49 VAL n +1 50 ILE n +1 51 LYS n +1 52 LYS n +1 53 PRO n +1 54 MET n +1 55 ASP n +1 56 PHE n +1 57 SER n +1 58 THR n +1 59 ILE n +1 60 ARG n +1 61 GLU n +1 62 LYS n +1 63 LEU n +1 64 SER n +1 65 SER n +1 66 GLY n +1 67 GLN n +1 68 TYR n +1 69 PRO n +1 70 ASN n +1 71 LEU n +1 72 GLU n +1 73 THR n +1 74 PHE n +1 75 ALA n +1 76 LEU n +1 77 ASP n +1 78 VAL n +1 79 ARG n +1 80 LEU n +1 81 VAL n +1 82 PHE n +1 83 ASP n +1 84 ASN n +1 85 CYS n +1 86 GLU n +1 87 THR n +1 88 PHE n +1 89 ASN n +1 90 GLU n +1 91 ASP n +1 92 ASP n +1 93 SER n +1 94 ASP n +1 95 ILE n +1 96 GLY n +1 97 ARG n +1 98 ALA n +1 99 GLY n +1 100 HIS n +1 101 ASN n +1 102 MET n +1 103 ARG n +1 104 LYS n +1 105 TYR n +1 106 PHE n +1 107 GLU n +1 108 LYS n +1 109 LYS n +1 110 TRP n +1 111 THR n +1 112 ASP n +1 113 THR n +1 114 PHE n +1 115 LYS n +1 116 VAL n +1 117 SER n +# +_entity_src_gen.entity_id 1 +_entity_src_gen.gene_src_common_name HUMAN +_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 'HOMO SAPIENS' +_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 +_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 'ESCHERICHIA COLI' +_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 469008 +_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 'BL21(DE3)' +_entity_src_gen.pdbx_host_org_variant R3 +_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 PLASMID +_entity_src_gen.pdbx_host_org_vector ? +_entity_src_gen.plasmid_name PNIC28-BSA4 +_entity_src_gen.plasmid_details ? +_entity_src_gen.pdbx_description ? +# +_struct_ref.id 1 +_struct_ref.db_name UNP +_struct_ref.db_code BAZ2B_HUMAN +_struct_ref.entity_id 1 +_struct_ref.pdbx_seq_one_letter_code ? +_struct_ref.pdbx_align_begin ? +_struct_ref.biol_id . +_struct_ref.pdbx_db_accession Q9UIF8 +# +_struct_ref_seq.align_id 1 +_struct_ref_seq.ref_id 1 +_struct_ref_seq.pdbx_PDB_id_code 4CUP +_struct_ref_seq.pdbx_strand_id A +_struct_ref_seq.seq_align_beg 3 +_struct_ref_seq.pdbx_seq_align_beg_ins_code ? +_struct_ref_seq.seq_align_end 117 +_struct_ref_seq.pdbx_seq_align_end_ins_code ? +_struct_ref_seq.pdbx_db_accession Q9UIF8 +_struct_ref_seq.db_align_beg 1858 +_struct_ref_seq.pdbx_db_align_beg_ins_code ? +_struct_ref_seq.db_align_end 1972 +_struct_ref_seq.pdbx_db_align_end_ins_code ? +_struct_ref_seq.pdbx_auth_seq_align_beg 1858 +_struct_ref_seq.pdbx_auth_seq_align_end 1972 +# +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 +1 4CUP SER A 1 ? UNP Q9UIF8 ? ? 'EXPRESSION TAG' 1856 1 +1 4CUP MET A 2 ? UNP Q9UIF8 ? ? 'EXPRESSION TAG' 1857 2 +# +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 +SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 +MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.207 +VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.147 +LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.197 +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 +ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.104 +LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.174 +ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.094 +CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.154 +ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.174 +THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.120 +GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.130 +HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.164 +TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.228 +PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.191 +ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.119 +GLY 'PEPTIDE LINKING' y GLYCINE ? 'C2 H5 N O2' 75.067 +TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.191 +GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.146 +ZYB NON-POLYMER . 4-FLUOROBENZAMIDOXIME ? 'C7 H7 F N2 O' 154.144 +MOH NON-POLYMER . METHANOL ? 'C H4 O' 32.042 +HOH NON-POLYMER . WATER ? 'H2 O' 18.015 +# +_exptl.entry_id 4CUP +_exptl.method 'X-RAY DIFFRACTION' +_exptl.crystals_number 1 +# +_exptl_crystal.id 1 +_exptl_crystal.density_meas ? +_exptl_crystal.density_Matthews 4.3 +_exptl_crystal.density_percent_sol 70 +_exptl_crystal.description NONE +# +_exptl_crystal_grow.crystal_id 1 +_exptl_crystal_grow.method ? +_exptl_crystal_grow.temp ? +_exptl_crystal_grow.temp_details ? +_exptl_crystal_grow.pH 6.4 +_exptl_crystal_grow.pdbx_pH_range ? +_exptl_crystal_grow.pdbx_details '34% PEG SMEAR LOW, 0.1M MES PH 6.4' +# +_diffrn.id 1 +_diffrn.ambient_temp 100 +_diffrn.ambient_temp_details ? +_diffrn.crystal_id 1 +# +_diffrn_detector.diffrn_id 1 +_diffrn_detector.detector 'PIXEL (PILATUS)' +_diffrn_detector.type DECTRIS +_diffrn_detector.pdbx_collection_date 2012-04-29 +_diffrn_detector.details ? +# +_diffrn_radiation.diffrn_id 1 +_diffrn_radiation.wavelength_id 1 +_diffrn_radiation.pdbx_monochromatic_or_laue_m_l M +_diffrn_radiation.monochromator ? +_diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' +_diffrn_radiation.pdbx_scattering_type x-ray +# +_diffrn_radiation_wavelength.id 1 +_diffrn_radiation_wavelength.wavelength 0.97 +_diffrn_radiation_wavelength.wt 1.0 +# +_diffrn_source.diffrn_id 1 +_diffrn_source.source SYNCHROTRON +_diffrn_source.type 'DIAMOND BEAMLINE I04' +_diffrn_source.pdbx_synchrotron_site DIAMOND +_diffrn_source.pdbx_synchrotron_beamline I04 +_diffrn_source.pdbx_wavelength 0.97 +_diffrn_source.pdbx_wavelength_list ? +# +_reflns.pdbx_diffrn_id 1 +_reflns.pdbx_ordinal 1 +_reflns.entry_id 4CUP +_reflns.observed_criterion_sigma_I -3.0 +_reflns.observed_criterion_sigma_F ? +_reflns.d_resolution_low 32.97 +_reflns.d_resolution_high 1.88 +_reflns.number_obs 18470 +_reflns.number_all ? +_reflns.percent_possible_obs 99.5 +_reflns.pdbx_Rmerge_I_obs 0.06 +_reflns.pdbx_Rsym_value ? +_reflns.pdbx_netI_over_sigmaI 16.20 +_reflns.B_iso_Wilson_estimate 26.58 +_reflns.pdbx_redundancy 5.4 +# +_reflns_shell.pdbx_diffrn_id 1 +_reflns_shell.pdbx_ordinal 1 +_reflns_shell.d_res_high 1.88 +_reflns_shell.d_res_low 1.93 +_reflns_shell.percent_possible_all 98.6 +_reflns_shell.Rmerge_I_obs 0.74 +_reflns_shell.pdbx_Rsym_value ? +_reflns_shell.meanI_over_sigI_obs 1.90 +_reflns_shell.pdbx_redundancy 4.8 +# +_computing.entry_id 4CUP +_computing.pdbx_data_reduction_ii XDS +_computing.pdbx_data_reduction_ds AIMLESS +_computing.data_collection ? +_computing.structure_solution ? +_computing.structure_refinement 'PHENIX (PHENIX.REFINE)' +_computing.pdbx_structure_refinement_method ? +# +_refine.pdbx_refine_id 'X-RAY DIFFRACTION' +_refine.entry_id 4CUP +_refine.pdbx_diffrn_id 1 +_refine.pdbx_TLS_residual_ADP_flag ? +_refine.ls_number_reflns_obs 18429 +_refine.ls_number_reflns_all ? +_refine.pdbx_ls_sigma_I ? +_refine.pdbx_ls_sigma_F 1.90 +_refine.pdbx_data_cutoff_high_absF ? +_refine.pdbx_data_cutoff_low_absF ? +_refine.pdbx_data_cutoff_high_rms_absF ? +_refine.ls_d_res_low 18.538 +_refine.ls_d_res_high 1.880 +_refine.ls_percent_reflns_obs 99.44 +_refine.ls_R_factor_obs 0.1779 +_refine.ls_R_factor_all ? +_refine.ls_R_factor_R_work 0.1763 +_refine.ls_R_factor_R_free 0.2078 +_refine.ls_R_factor_R_free_error ? +_refine.ls_R_factor_R_free_error_details ? +_refine.ls_percent_reflns_R_free 5.1 +_refine.ls_number_reflns_R_free 940 +_refine.ls_number_parameters ? +_refine.ls_number_restraints ? +_refine.occupancy_min ? +_refine.occupancy_max ? +_refine.correlation_coeff_Fo_to_Fc ? +_refine.correlation_coeff_Fo_to_Fc_free ? +_refine.B_iso_mean ? +_refine.aniso_B[1][1] ? +_refine.aniso_B[2][2] ? +_refine.aniso_B[3][3] ? +_refine.aniso_B[1][2] ? +_refine.aniso_B[1][3] ? +_refine.aniso_B[2][3] ? +_refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' +_refine.solvent_model_param_ksol ? +_refine.solvent_model_param_bsol ? +_refine.pdbx_solvent_vdw_probe_radii 1.11 +_refine.pdbx_solvent_ion_probe_radii ? +_refine.pdbx_solvent_shrinkage_radii 0.90 +_refine.pdbx_ls_cross_valid_method ? +_refine.details ? +_refine.pdbx_starting_model ? +_refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' +_refine.pdbx_isotropic_thermal_model ? +_refine.pdbx_stereochemistry_target_values ML +_refine.pdbx_stereochem_target_val_spec_case ? +_refine.pdbx_R_Free_selection_details ? +_refine.pdbx_overall_ESU_R ? +_refine.pdbx_overall_ESU_R_Free ? +_refine.overall_SU_ML 0.20 +_refine.pdbx_overall_phase_error 25.38 +_refine.overall_SU_B ? +_refine.overall_SU_R_Cruickshank_DPI ? +_refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? +_refine.pdbx_overall_SU_R_Blow_DPI ? +_refine.pdbx_overall_SU_R_free_Blow_DPI ? +# +_refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' +_refine_hist.cycle_id LAST +_refine_hist.pdbx_number_atoms_protein 924 +_refine_hist.pdbx_number_atoms_nucleic_acid 0 +_refine_hist.pdbx_number_atoms_ligand 17 +_refine_hist.number_atoms_solvent 146 +_refine_hist.number_atoms_total 1087 +_refine_hist.d_res_high 1.880 +_refine_hist.d_res_low 18.538 +# +loop_ +_refine_ls_restr.type +_refine_ls_restr.dev_ideal +_refine_ls_restr.dev_ideal_target +_refine_ls_restr.weight +_refine_ls_restr.number +_refine_ls_restr.pdbx_refine_id +_refine_ls_restr.pdbx_restraint_function +f_bond_d 0.006 ? ? 973 'X-RAY DIFFRACTION' ? +f_angle_d 0.898 ? ? 1309 'X-RAY DIFFRACTION' ? +f_dihedral_angle_d 12.740 ? ? 365 'X-RAY DIFFRACTION' ? +f_chiral_restr 0.034 ? ? 141 'X-RAY DIFFRACTION' ? +f_plane_restr 0.005 ? ? 168 'X-RAY DIFFRACTION' ? +# +loop_ +_refine_ls_shell.pdbx_refine_id +_refine_ls_shell.pdbx_total_number_of_bins_used +_refine_ls_shell.d_res_high +_refine_ls_shell.d_res_low +_refine_ls_shell.number_reflns_R_work +_refine_ls_shell.R_factor_R_work +_refine_ls_shell.percent_reflns_obs +_refine_ls_shell.R_factor_R_free +_refine_ls_shell.R_factor_R_free_error +_refine_ls_shell.percent_reflns_R_free +_refine_ls_shell.number_reflns_R_free +_refine_ls_shell.number_reflns_all +_refine_ls_shell.R_factor_all +'X-RAY DIFFRACTION' ? 1.8800 1.9790 2458 0.3152 99.00 0.3338 ? ? 133 ? ? +'X-RAY DIFFRACTION' ? 1.9790 2.1029 2430 0.2368 99.00 0.2971 ? ? 139 ? ? +'X-RAY DIFFRACTION' ? 2.1029 2.2650 2453 0.1915 99.00 0.2154 ? ? 138 ? ? +'X-RAY DIFFRACTION' ? 2.2650 2.4924 2496 0.1683 100.00 0.2131 ? ? 137 ? ? +'X-RAY DIFFRACTION' ? 2.4924 2.8519 2493 0.1662 100.00 0.2138 ? ? 138 ? ? +'X-RAY DIFFRACTION' ? 2.8519 3.5889 2505 0.1669 100.00 0.1748 ? ? 143 ? ? +'X-RAY DIFFRACTION' ? 3.5889 18.5386 2654 0.1558 100.00 0.1894 ? ? 112 ? ? +# +_struct.entry_id 4CUP +_struct.title 'Crystal structure of human BAZ2B in complex with fragment-1 N09421' +_struct.pdbx_descriptor 'BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B' +_struct.pdbx_model_details ? +_struct.pdbx_CASP_flag ? +_struct.pdbx_model_type_details ? +# +_struct_keywords.entry_id 4CUP +_struct_keywords.pdbx_keywords TRANSCRIPTION +_struct_keywords.text TRANSCRIPTION +# +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 3 ? +F N N 4 ? +# +_struct_biol.id 1 +# +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 LYS A 13 ? HIS A 28 ? LYS A 1868 HIS A 1883 1 ? 16 +HELX_P HELX_P2 2 ALA A 31 ? LEU A 35 ? ALA A 1886 LEU A 1890 5 ? 5 +HELX_P HELX_P3 3 GLY A 45 ? ILE A 50 ? GLY A 1900 ILE A 1905 1 ? 6 +HELX_P HELX_P4 4 ASP A 55 ? SER A 65 ? ASP A 1910 SER A 1920 1 ? 11 +HELX_P HELX_P5 5 ASN A 70 ? ASN A 89 ? ASN A 1925 ASN A 1944 1 ? 20 +HELX_P HELX_P6 6 SER A 93 ? LYS A 115 ? SER A 1948 LYS A 1970 1 ? 23 +# +_struct_conf_type.id HELX_P +_struct_conf_type.criteria ? +_struct_conf_type.reference ? +# +_struct_site.id AC1 +_struct_site.details 'BINDING SITE FOR RESIDUE ZYB A 2971' +_struct_site.pdbx_evidence_code 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 6 VAL A 43 ? VAL A 1898 . . 1_555 ? +2 AC1 6 PRO A 44 ? PRO A 1899 . . 4_566 ? +3 AC1 6 ASN A 89 ? ASN A 1944 . . 1_555 ? +4 AC1 6 ILE A 95 ? ILE A 1950 . . 1_555 ? +5 AC1 6 HOH F . ? HOH A 2072 . . 4_566 ? +6 AC1 6 HOH F . ? HOH A 2124 . . 1_555 ? +# +_database_PDB_matrix.entry_id 4CUP +_database_PDB_matrix.origx[1][1] 1.000000 +_database_PDB_matrix.origx[1][2] 0.000000 +_database_PDB_matrix.origx[1][3] 0.000000 +_database_PDB_matrix.origx[2][1] 0.000000 +_database_PDB_matrix.origx[2][2] 1.000000 +_database_PDB_matrix.origx[2][3] 0.000000 +_database_PDB_matrix.origx[3][1] 0.000000 +_database_PDB_matrix.origx[3][2] 0.000000 +_database_PDB_matrix.origx[3][3] 1.000000 +_database_PDB_matrix.origx_vector[1] 0.00000 +_database_PDB_matrix.origx_vector[2] 0.00000 +_database_PDB_matrix.origx_vector[3] 0.00000 +# +_atom_sites.entry_id 4CUP +_atom_sites.Cartn_transform_axes ? +_atom_sites.fract_transf_matrix[1][1] 0.012442 +_atom_sites.fract_transf_matrix[1][2] 0.000000 +_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] 0.010404 +_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] 0.017340 +_atom_sites.fract_transf_vector[1] 0.00000 +_atom_sites.fract_transf_vector[2] 0.00000 +_atom_sites.fract_transf_vector[3] 0.00000 +# +loop_ +_atom_type.symbol +C +F +H +N +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 . SER A 1 1 ? 50.346 19.287 17.288 1.00 32.02 ? ? ? ? ? ? 1856 SER A N 1 +ATOM 2 C CA . SER A 1 1 ? 50.745 19.964 16.058 1.00 34.08 ? ? ? ? ? ? 1856 SER A CA 1 +ATOM 3 C C . SER A 1 1 ? 50.691 18.998 14.887 1.00 35.85 ? ? ? ? ? ? 1856 SER A C 1 +ATOM 4 O O . SER A 1 1 ? 50.070 17.937 14.987 1.00 33.26 ? ? ? ? ? ? 1856 SER A O 1 +ATOM 5 C CB . SER A 1 1 ? 52.146 20.564 16.199 1.00 30.82 ? ? ? ? ? ? 1856 SER A CB 1 +ATOM 6 O OG . SER A 1 1 ? 53.116 19.545 16.371 1.00 32.50 ? ? ? ? ? ? 1856 SER A OG 1 +ATOM 7 N N . MET A 1 2 ? 51.330 19.363 13.776 1.00 35.47 ? ? ? ? ? ? 1857 MET A N 1 +ATOM 8 C CA . MET A 1 2 ? 51.310 18.508 12.593 1.00 36.62 ? ? ? ? ? ? 1857 MET A CA 1 +ATOM 9 C C . MET A 1 2 ? 51.837 17.105 12.904 1.00 32.24 ? ? ? ? ? ? 1857 MET A C 1 +ATOM 10 O O . MET A 1 2 ? 52.974 16.947 13.359 1.00 34.35 ? ? ? ? ? ? 1857 MET A O 1 +ATOM 11 C CB . MET A 1 2 ? 52.123 19.127 11.456 1.00 36.12 ? ? ? ? ? ? 1857 MET A CB 1 +ATOM 12 C CG . MET A 1 2 ? 51.875 18.454 10.119 1.00 37.34 ? ? ? ? ? ? 1857 MET A CG 1 +ATOM 13 S SD . MET A 1 2 ? 52.981 18.997 8.800 1.00 39.70 ? ? ? ? ? ? 1857 MET A SD 1 +ATOM 14 C CE . MET A 1 2 ? 52.932 20.770 8.993 1.00 36.58 ? ? ? ? ? ? 1857 MET A CE 1 +ATOM 15 N N . SER A 1 3 ? 50.992 16.104 12.654 1.00 35.27 ? ? ? ? ? ? 1858 SER A N 1 +ATOM 16 C CA . SER A 1 3 ? 51.276 14.687 12.929 1.00 35.35 ? ? ? ? ? ? 1858 SER A CA 1 +ATOM 17 C C . SER A 1 3 ? 51.511 14.388 14.413 1.00 36.48 ? ? ? ? ? ? 1858 SER A C 1 +ATOM 18 O O . SER A 1 3 ? 52.097 13.363 14.762 1.00 33.72 ? ? ? ? ? ? 1858 SER A O 1 +ATOM 19 C CB . SER A 1 3 ? 52.482 14.212 12.114 1.00 35.21 ? ? ? ? ? ? 1858 SER A CB 1 +ATOM 20 O OG . SER A 1 3 ? 52.279 14.436 10.727 1.00 35.86 ? ? ? ? ? ? 1858 SER A OG 1 +ATOM 21 N N . VAL A 1 4 ? 51.048 15.277 15.285 1.00 30.95 ? ? ? ? ? ? 1859 VAL A N 1 +ATOM 22 C CA . VAL A 1 4 ? 51.130 15.041 16.731 1.00 31.15 ? ? ? ? ? ? 1859 VAL A CA 1 +ATOM 23 C C . VAL A 1 4 ? 49.768 15.284 17.370 1.00 35.24 ? ? ? ? ? ? 1859 VAL A C 1 +ATOM 24 O O . VAL A 1 4 ? 49.410 16.424 17.672 1.00 36.46 ? ? ? ? ? ? 1859 VAL A O 1 +ATOM 25 C CB . VAL A 1 4 ? 52.177 15.945 17.413 1.00 31.83 ? ? ? ? ? ? 1859 VAL A CB 1 +ATOM 26 C CG1 . VAL A 1 4 ? 52.253 15.637 18.914 1.00 31.15 ? ? ? ? ? ? 1859 VAL A CG1 1 +ATOM 27 C CG2 . VAL A 1 4 ? 53.546 15.779 16.764 1.00 33.39 ? ? ? ? ? ? 1859 VAL A CG2 1 +ATOM 28 N N . LYS A 1 5 ? 49.005 14.214 17.571 1.00 42.36 ? ? ? ? ? ? 1860 LYS A N 1 +ATOM 29 C CA . LYS A 1 5 ? 47.636 14.345 18.058 1.00 45.72 ? ? ? ? ? ? 1860 LYS A CA 1 +ATOM 30 C C . LYS A 1 5 ? 47.418 13.675 19.410 1.00 44.41 ? ? ? ? ? ? 1860 LYS A C 1 +ATOM 31 O O . LYS A 1 5 ? 47.998 12.625 19.688 1.00 45.19 ? ? ? ? ? ? 1860 LYS A O 1 +ATOM 32 C CB . LYS A 1 5 ? 46.661 13.761 17.032 1.00 46.44 ? ? ? ? ? ? 1860 LYS A CB 1 +ATOM 33 C CG . LYS A 1 5 ? 46.603 14.552 15.731 1.00 61.31 ? ? ? ? ? ? 1860 LYS A CG 1 +ATOM 34 C CD . LYS A 1 5 ? 45.784 15.830 15.892 1.00 65.67 ? ? ? ? ? ? 1860 LYS A CD 1 +ATOM 35 C CE . LYS A 1 5 ? 46.118 16.850 14.820 1.00 68.56 ? ? ? ? ? ? 1860 LYS A CE 1 +ATOM 36 N NZ . LYS A 1 5 ? 47.383 17.565 15.134 1.00 71.00 ? ? ? ? ? ? 1860 LYS A NZ 1 +ATOM 37 N N . LYS A 1 6 ? 46.582 14.292 20.245 1.00 47.64 ? ? ? ? ? ? 1861 LYS A N 1 +ATOM 38 C CA . LYS A 1 6 ? 46.107 13.653 21.467 1.00 58.98 ? ? ? ? ? ? 1861 LYS A CA 1 +ATOM 39 C C . LYS A 1 6 ? 45.212 12.495 21.075 1.00 56.13 ? ? ? ? ? ? 1861 LYS A C 1 +ATOM 40 O O . LYS A 1 6 ? 44.629 12.513 19.990 1.00 58.78 ? ? ? ? ? ? 1861 LYS A O 1 +ATOM 41 C CB . LYS A 1 6 ? 45.323 14.628 22.354 1.00 69.74 ? ? ? ? ? ? 1861 LYS A CB 1 +ATOM 42 C CG . LYS A 1 6 ? 46.129 15.745 22.995 1.00 73.06 ? ? ? ? ? ? 1861 LYS A CG 1 +ATOM 43 C CD . LYS A 1 6 ? 45.315 16.398 24.110 1.00 76.41 ? ? ? ? ? ? 1861 LYS A CD 1 +ATOM 44 C CE . LYS A 1 6 ? 45.913 17.721 24.569 1.00 77.31 ? ? ? ? ? ? 1861 LYS A CE 1 +ATOM 45 N NZ . LYS A 1 6 ? 45.777 18.787 23.539 1.00 76.95 ? ? ? ? ? ? 1861 LYS A NZ 1 +ATOM 46 N N . PRO A 1 7 ? 45.102 11.484 21.949 1.00 56.20 ? ? ? ? ? ? 1862 PRO A N 1 +ATOM 47 C CA . PRO A 1 7 ? 44.136 10.405 21.727 1.00 60.79 ? ? ? ? ? ? 1862 PRO A CA 1 +ATOM 48 C C . PRO A 1 7 ? 42.751 10.956 21.409 1.00 65.14 ? ? ? ? ? ? 1862 PRO A C 1 +ATOM 49 O O . PRO A 1 7 ? 42.303 11.920 22.036 1.00 61.93 ? ? ? ? ? ? 1862 PRO A O 1 +ATOM 50 C CB . PRO A 1 7 ? 44.149 9.652 23.055 1.00 62.28 ? ? ? ? ? ? 1862 PRO A CB 1 +ATOM 51 C CG . PRO A 1 7 ? 45.547 9.829 23.540 1.00 62.61 ? ? ? ? ? ? 1862 PRO A CG 1 +ATOM 52 C CD . PRO A 1 7 ? 45.950 11.224 23.125 1.00 57.35 ? ? ? ? ? ? 1862 PRO A CD 1 +ATOM 53 N N . LYS A 1 8 ? 42.100 10.360 20.416 1.00 68.79 ? ? ? ? ? ? 1863 LYS A N 1 +ATOM 54 C CA . LYS A 1 8 ? 40.836 10.879 19.914 1.00 73.53 ? ? ? ? ? ? 1863 LYS A CA 1 +ATOM 55 C C . LYS A 1 8 ? 39.701 10.620 20.892 1.00 72.50 ? ? ? ? ? ? 1863 LYS A C 1 +ATOM 56 O O . LYS A 1 8 ? 39.396 9.473 21.215 1.00 73.78 ? ? ? ? ? ? 1863 LYS A O 1 +ATOM 57 C CB . LYS A 1 8 ? 40.507 10.266 18.550 1.00 73.63 ? ? ? ? ? ? 1863 LYS A CB 1 +ATOM 58 N N . ARG A 1 9 ? 39.091 11.698 21.369 1.00 70.21 ? ? ? ? ? ? 1864 ARG A N 1 +ATOM 59 C CA . ARG A 1 9 ? 37.895 11.604 22.190 1.00 69.66 ? ? ? ? ? ? 1864 ARG A CA 1 +ATOM 60 C C . ARG A 1 9 ? 36.694 11.259 21.314 1.00 70.65 ? ? ? ? ? ? 1864 ARG A C 1 +ATOM 61 O O . ARG A 1 9 ? 36.517 11.839 20.241 1.00 70.51 ? ? ? ? ? ? 1864 ARG A O 1 +ATOM 62 C CB . ARG A 1 9 ? 37.651 12.914 22.938 1.00 67.41 ? ? ? ? ? ? 1864 ARG A CB 1 +ATOM 63 C CG . ARG A 1 9 ? 36.356 12.937 23.721 1.00 64.44 ? ? ? ? ? ? 1864 ARG A CG 1 +ATOM 64 C CD . ARG A 1 9 ? 35.997 14.337 24.184 1.00 62.86 ? ? ? ? ? ? 1864 ARG A CD 1 +ATOM 65 N NE . ARG A 1 9 ? 34.678 14.349 24.805 1.00 62.84 ? ? ? ? ? ? 1864 ARG A NE 1 +ATOM 66 C CZ . ARG A 1 9 ? 33.550 14.599 24.151 1.00 65.98 ? ? ? ? ? ? 1864 ARG A CZ 1 +ATOM 67 N NH1 . ARG A 1 9 ? 33.579 14.880 22.855 1.00 71.46 ? ? ? ? ? ? 1864 ARG A NH1 1 +ATOM 68 N NH2 . ARG A 1 9 ? 32.392 14.578 24.795 1.00 67.66 ? ? ? ? ? ? 1864 ARG A NH2 1 +ATOM 69 N N . ASP A 1 10 ? 35.876 10.311 21.763 1.00 71.15 ? ? ? ? ? ? 1865 ASP A N 1 +ATOM 70 C CA . ASP A 1 10 ? 34.693 9.915 21.008 1.00 66.70 ? ? ? ? ? ? 1865 ASP A CA 1 +ATOM 71 C C . ASP A 1 10 ? 33.597 10.965 21.142 1.00 60.95 ? ? ? ? ? ? 1865 ASP A C 1 +ATOM 72 O O . ASP A 1 10 ? 32.969 11.089 22.191 1.00 62.37 ? ? ? ? ? ? 1865 ASP A O 1 +ATOM 73 C CB . ASP A 1 10 ? 34.183 8.548 21.472 1.00 71.14 ? ? ? ? ? ? 1865 ASP A CB 1 +ATOM 74 C CG . ASP A 1 10 ? 32.882 8.151 20.796 1.00 72.95 ? ? ? ? ? ? 1865 ASP A CG 1 +ATOM 75 O OD1 . ASP A 1 10 ? 32.567 8.705 19.717 1.00 65.36 ? ? ? ? ? ? 1865 ASP A OD1 1 +ATOM 76 O OD2 . ASP A 1 10 ? 32.173 7.280 21.343 1.00 74.36 ? ? ? ? ? ? 1865 ASP A OD2 1 +ATOM 77 N N . ASP A 1 11 ? 33.361 11.711 20.068 1.00 48.20 ? ? ? ? ? ? 1866 ASP A N 1 +ATOM 78 C CA . ASP A 1 11 ? 32.406 12.813 20.113 1.00 43.93 ? ? ? ? ? ? 1866 ASP A CA 1 +ATOM 79 C C . ASP A 1 11 ? 31.081 12.473 19.431 1.00 40.69 ? ? ? ? ? ? 1866 ASP A C 1 +ATOM 80 O O . ASP A 1 11 ? 30.235 13.348 19.233 1.00 41.33 ? ? ? ? ? ? 1866 ASP A O 1 +ATOM 81 C CB . ASP A 1 11 ? 33.020 14.063 19.472 1.00 47.30 ? ? ? ? ? ? 1866 ASP A CB 1 +ATOM 82 C CG . ASP A 1 11 ? 33.442 13.838 18.029 1.00 58.18 ? ? ? ? ? ? 1866 ASP A CG 1 +ATOM 83 O OD1 . ASP A 1 11 ? 33.545 12.666 17.610 1.00 64.93 ? ? ? ? ? ? 1866 ASP A OD1 1 +ATOM 84 O OD2 . ASP A 1 11 ? 33.681 14.834 17.313 1.00 64.43 ? ? ? ? ? ? 1866 ASP A OD2 1 +ATOM 85 N N . SER A 1 12 ? 30.896 11.200 19.096 1.00 44.14 ? ? ? ? ? ? 1867 SER A N 1 +ATOM 86 C CA . SER A 1 12 ? 29.765 10.775 18.275 1.00 43.67 ? ? ? ? ? ? 1867 SER A CA 1 +ATOM 87 C C . SER A 1 12 ? 28.422 10.980 18.960 1.00 42.67 ? ? ? ? ? ? 1867 SER A C 1 +ATOM 88 O O . SER A 1 12 ? 27.394 11.083 18.291 1.00 43.89 ? ? ? ? ? ? 1867 SER A O 1 +ATOM 89 C CB . SER A 1 12 ? 29.917 9.303 17.883 1.00 49.00 ? ? ? ? ? ? 1867 SER A CB 1 +ATOM 90 O OG . SER A 1 12 ? 29.813 8.468 19.024 1.00 54.91 ? ? ? ? ? ? 1867 SER A OG 1 +ATOM 91 N N . LYS A 1 13 ? 28.430 11.041 20.289 1.00 40.18 ? ? ? ? ? ? 1868 LYS A N 1 +ATOM 92 C CA . LYS A 1 13 ? 27.201 11.234 21.060 1.00 34.76 ? ? ? ? ? ? 1868 LYS A CA 1 +ATOM 93 C C . LYS A 1 13 ? 26.971 12.672 21.532 1.00 34.13 ? ? ? ? ? ? 1868 LYS A C 1 +ATOM 94 O O . LYS A 1 13 ? 25.970 12.949 22.194 1.00 35.15 ? ? ? ? ? ? 1868 LYS A O 1 +ATOM 95 C CB . LYS A 1 13 ? 27.201 10.318 22.285 1.00 36.58 ? ? ? ? ? ? 1868 LYS A CB 1 +ATOM 96 C CG . LYS A 1 13 ? 27.235 8.825 21.961 1.00 41.60 ? ? ? ? ? ? 1868 LYS A CG 1 +ATOM 97 C CD . LYS A 1 13 ? 27.236 8.002 23.238 1.00 58.66 ? ? ? ? ? ? 1868 LYS A CD 1 +ATOM 98 N N . ASP A 1 14 ? 27.893 13.577 21.220 1.00 36.26 ? ? ? ? ? ? 1869 ASP A N 1 +ATOM 99 C CA . ASP A 1 14 ? 27.801 14.944 21.749 1.00 33.90 ? ? ? ? ? ? 1869 ASP A CA 1 +ATOM 100 C C . ASP A 1 14 ? 26.513 15.639 21.331 1.00 36.45 ? ? ? ? ? ? 1869 ASP A C 1 +ATOM 101 O O . ASP A 1 14 ? 25.872 16.309 22.140 1.00 36.50 ? ? ? ? ? ? 1869 ASP A O 1 +ATOM 102 C CB . ASP A 1 14 ? 28.997 15.789 21.307 1.00 31.90 ? ? ? ? ? ? 1869 ASP A CB 1 +ATOM 103 C CG . ASP A 1 14 ? 30.280 15.382 21.990 1.00 43.01 ? ? ? ? ? ? 1869 ASP A CG 1 +ATOM 104 O OD1 . ASP A 1 14 ? 30.229 14.494 22.871 1.00 40.83 ? ? ? ? ? ? 1869 ASP A OD1 1 +ATOM 105 O OD2 . ASP A 1 14 ? 31.334 15.964 21.664 1.00 39.80 ? ? ? ? ? ? 1869 ASP A OD2 1 +ATOM 106 N N . LEU A 1 15 ? 26.130 15.476 20.069 1.00 32.79 ? ? ? ? ? ? 1870 LEU A N 1 +ATOM 107 C CA . LEU A 1 15 ? 24.940 16.138 19.558 1.00 32.80 ? ? ? ? ? ? 1870 LEU A CA 1 +ATOM 108 C C . LEU A 1 15 ? 23.701 15.689 20.336 1.00 35.75 ? ? ? ? ? ? 1870 LEU A C 1 +ATOM 109 O O . LEU A 1 15 ? 22.925 16.521 20.806 1.00 36.32 ? ? ? ? ? ? 1870 LEU A O 1 +ATOM 110 C CB . LEU A 1 15 ? 24.776 15.869 18.056 1.00 33.83 ? ? ? ? ? ? 1870 LEU A CB 1 +ATOM 111 C CG . LEU A 1 15 ? 23.582 16.530 17.365 1.00 31.69 ? ? ? ? ? ? 1870 LEU A CG 1 +ATOM 112 C CD1 . LEU A 1 15 ? 23.636 18.058 17.479 1.00 32.12 ? ? ? ? ? ? 1870 LEU A CD1 1 +ATOM 113 C CD2 . LEU A 1 15 ? 23.507 16.090 15.894 1.00 33.01 ? ? ? ? ? ? 1870 LEU A CD2 1 +ATOM 114 N N . ALA A 1 16 ? 23.540 14.380 20.504 1.00 34.82 ? ? ? ? ? ? 1871 ALA A N 1 +ATOM 115 C CA . ALA A 1 16 ? 22.419 13.834 21.269 1.00 36.97 ? ? ? ? ? ? 1871 ALA A CA 1 +ATOM 116 C C . ALA A 1 16 ? 22.444 14.286 22.729 1.00 37.20 ? ? ? ? ? ? 1871 ALA A C 1 +ATOM 117 O O . ALA A 1 16 ? 21.403 14.588 23.312 1.00 36.24 ? ? ? ? ? ? 1871 ALA A O 1 +ATOM 118 C CB . ALA A 1 16 ? 22.418 12.303 21.195 1.00 38.32 ? ? ? ? ? ? 1871 ALA A CB 1 +ATOM 119 N N . LEU A 1 17 ? 23.634 14.325 23.320 1.00 35.33 ? ? ? ? ? ? 1872 LEU A N 1 +ATOM 120 C CA . LEU A 1 17 ? 23.770 14.709 24.723 1.00 34.07 ? ? ? ? ? ? 1872 LEU A CA 1 +ATOM 121 C C . LEU A 1 17 ? 23.462 16.196 24.942 1.00 34.96 ? ? ? ? ? ? 1872 LEU A C 1 +ATOM 122 O O . LEU A 1 17 ? 22.828 16.574 25.930 1.00 37.32 ? ? ? ? ? ? 1872 LEU A O 1 +ATOM 123 C CB . LEU A 1 17 ? 25.175 14.377 25.229 1.00 35.88 ? ? ? ? ? ? 1872 LEU A CB 1 +ATOM 124 C CG . LEU A 1 17 ? 25.474 12.879 25.339 1.00 39.51 ? ? ? ? ? ? 1872 LEU A CG 1 +ATOM 125 C CD1 . LEU A 1 17 ? 26.935 12.631 25.680 1.00 39.12 ? ? ? ? ? ? 1872 LEU A CD1 1 +ATOM 126 C CD2 . LEU A 1 17 ? 24.560 12.228 26.367 1.00 44.69 ? ? ? ? ? ? 1872 LEU A CD2 1 +ATOM 127 N N . CYS A 1 18 ? 23.908 17.042 24.019 1.00 34.73 ? ? ? ? ? ? 1873 CYS A N 1 +ATOM 128 C CA . CYS A 1 18 ? 23.589 18.466 24.098 1.00 33.93 ? ? ? ? ? ? 1873 CYS A CA 1 +ATOM 129 C C . CYS A 1 18 ? 22.087 18.706 23.956 1.00 35.83 ? ? ? ? ? ? 1873 CYS A C 1 +ATOM 130 O O . CYS A 1 18 ? 21.515 19.559 24.648 1.00 32.57 ? ? ? ? ? ? 1873 CYS A O 1 +ATOM 131 C CB . CYS A 1 18 ? 24.360 19.249 23.033 1.00 32.12 ? ? ? ? ? ? 1873 CYS A CB 1 +ATOM 132 S SG . CYS A 1 18 ? 26.096 19.489 23.460 1.00 34.87 ? ? ? ? ? ? 1873 CYS A SG 1 +ATOM 133 N N . SER A 1 19 ? 21.456 17.945 23.063 1.00 31.48 ? ? ? ? ? ? 1874 SER A N 1 +ATOM 134 C CA . SER A 1 19 ? 20.009 18.011 22.874 1.00 29.68 ? ? ? ? ? ? 1874 SER A CA 1 +ATOM 135 C C . SER A 1 19 ? 19.281 17.609 24.153 1.00 31.01 ? ? ? ? ? ? 1874 SER A C 1 +ATOM 136 O O . SER A 1 19 ? 18.287 18.229 24.550 1.00 32.67 ? ? ? ? ? ? 1874 SER A O 1 +ATOM 137 C CB . SER A 1 19 ? 19.573 17.102 21.720 1.00 29.36 ? ? ? ? ? ? 1874 SER A CB 1 +ATOM 138 O OG . SER A 1 19 ? 18.157 17.090 21.603 1.00 37.19 ? ? ? ? ? ? 1874 SER A OG 1 +ATOM 139 N N . MET A 1 20 ? 19.779 16.554 24.786 1.00 32.48 ? ? ? ? ? ? 1875 MET A N 1 +ATOM 140 C CA . MET A 1 20 ? 19.235 16.095 26.056 1.00 34.40 ? ? ? ? ? ? 1875 MET A CA 1 +ATOM 141 C C . MET A 1 20 ? 19.314 17.198 27.110 1.00 34.75 ? ? ? ? ? ? 1875 MET A C 1 +ATOM 142 O O . MET A 1 20 ? 18.325 17.506 27.775 1.00 34.20 ? ? ? ? ? ? 1875 MET A O 1 +ATOM 143 C CB . MET A 1 20 ? 19.985 14.857 26.541 1.00 36.76 ? ? ? ? ? ? 1875 MET A CB 1 +ATOM 144 C CG . MET A 1 20 ? 19.603 14.413 27.948 1.00 46.65 ? ? ? ? ? ? 1875 MET A CG 1 +ATOM 145 S SD . MET A 1 20 ? 20.818 13.270 28.644 1.00 70.07 ? ? ? ? ? ? 1875 MET A SD 1 +ATOM 146 C CE . MET A 1 20 ? 22.116 14.422 29.100 1.00 61.11 ? ? ? ? ? ? 1875 MET A CE 1 +ATOM 147 N N . ILE A 1 21 ? 20.500 17.774 27.263 1.00 33.13 ? ? ? ? ? ? 1876 ILE A N 1 +ATOM 148 C CA . ILE A 1 21 ? 20.703 18.842 28.243 1.00 34.10 ? ? ? ? ? ? 1876 ILE A CA 1 +ATOM 149 C C . ILE A 1 21 ? 19.798 20.028 27.926 1.00 36.98 ? ? ? ? ? ? 1876 ILE A C 1 +ATOM 150 O O . ILE A 1 21 ? 19.167 20.590 28.820 1.00 31.38 ? ? ? ? ? ? 1876 ILE A O 1 +ATOM 151 C CB . ILE A 1 21 ? 22.178 19.300 28.292 1.00 32.28 ? ? ? ? ? ? 1876 ILE A CB 1 +ATOM 152 C CG1 . ILE A 1 21 ? 23.049 18.201 28.905 1.00 35.04 ? ? ? ? ? ? 1876 ILE A CG1 1 +ATOM 153 C CG2 . ILE A 1 21 ? 22.324 20.616 29.088 1.00 32.40 ? ? ? ? ? ? 1876 ILE A CG2 1 +ATOM 154 C CD1 . ILE A 1 21 ? 24.534 18.477 28.796 1.00 37.95 ? ? ? ? ? ? 1876 ILE A CD1 1 +ATOM 155 N N . LEU A 1 22 ? 19.709 20.387 26.647 1.00 34.79 ? ? ? ? ? ? 1877 LEU A N 1 +ATOM 156 C CA . LEU A 1 22 ? 18.880 21.519 26.252 1.00 31.03 ? ? ? ? ? ? 1877 LEU A CA 1 +ATOM 157 C C . LEU A 1 22 ? 17.412 21.245 26.591 1.00 28.71 ? ? ? ? ? ? 1877 LEU A C 1 +ATOM 158 O O . LEU A 1 22 ? 16.713 22.127 27.087 1.00 29.96 ? ? ? ? ? ? 1877 LEU A O 1 +ATOM 159 C CB . LEU A 1 22 ? 19.060 21.827 24.757 1.00 26.02 ? ? ? ? ? ? 1877 LEU A CB 1 +ATOM 160 C CG . LEU A 1 22 ? 18.305 23.039 24.209 1.00 30.76 ? ? ? ? ? ? 1877 LEU A CG 1 +ATOM 161 C CD1 . LEU A 1 22 ? 18.668 24.315 24.969 1.00 32.05 ? ? ? ? ? ? 1877 LEU A CD1 1 +ATOM 162 C CD2 . LEU A 1 22 ? 18.606 23.191 22.724 1.00 29.86 ? ? ? ? ? ? 1877 LEU A CD2 1 +ATOM 163 N N . THR A 1 23 ? 16.960 20.010 26.365 1.00 29.80 ? ? ? ? ? ? 1878 THR A N 1 +ATOM 164 C CA . THR A 1 23 ? 15.604 19.615 26.744 1.00 30.76 ? ? ? ? ? ? 1878 THR A CA 1 +ATOM 165 C C . THR A 1 23 ? 15.344 19.795 28.249 1.00 36.26 ? ? ? ? ? ? 1878 THR A C 1 +ATOM 166 O O . THR A 1 23 ? 14.270 20.242 28.658 1.00 34.92 ? ? ? ? ? ? 1878 THR A O 1 +ATOM 167 C CB . THR A 1 23 ? 15.326 18.162 26.348 1.00 40.24 ? ? ? ? ? ? 1878 THR A CB 1 +ATOM 168 O OG1 . THR A 1 23 ? 15.391 18.058 24.921 1.00 37.15 ? ? ? ? ? ? 1878 THR A OG1 1 +ATOM 169 C CG2 . THR A 1 23 ? 13.950 17.736 26.815 1.00 39.79 ? ? ? ? ? ? 1878 THR A CG2 1 +ATOM 170 N N . GLU A 1 24 ? 16.334 19.469 29.069 1.00 34.69 ? ? ? ? ? ? 1879 GLU A N 1 +ATOM 171 C CA . GLU A 1 24 ? 16.199 19.640 30.517 1.00 38.00 ? ? ? ? ? ? 1879 GLU A CA 1 +ATOM 172 C C . GLU A 1 24 ? 16.114 21.121 30.904 1.00 31.79 ? ? ? ? ? ? 1879 GLU A C 1 +ATOM 173 O O . GLU A 1 24 ? 15.377 21.491 31.814 1.00 31.13 ? ? ? ? ? ? 1879 GLU A O 1 +ATOM 174 C CB . GLU A 1 24 ? 17.362 18.971 31.239 1.00 34.00 ? ? ? ? ? ? 1879 GLU A CB 1 +ATOM 175 C CG . GLU A 1 24 ? 17.390 17.463 31.079 1.00 42.64 ? ? ? ? ? ? 1879 GLU A CG 1 +ATOM 176 C CD . GLU A 1 24 ? 18.576 16.834 31.775 1.00 57.52 ? ? ? ? ? ? 1879 GLU A CD 1 +ATOM 177 O OE1 . GLU A 1 24 ? 19.720 17.088 31.343 1.00 59.47 ? ? ? ? ? ? 1879 GLU A OE1 1 +ATOM 178 O OE2 . GLU A 1 24 ? 18.365 16.095 32.759 1.00 68.87 ? ? ? ? ? ? 1879 GLU A OE2 1 +ATOM 179 N N A MET A 1 25 ? 16.894 21.946 30.214 0.50 29.83 ? ? ? ? ? ? 1880 MET A N 1 +ATOM 180 N N B MET A 1 25 ? 16.861 21.973 30.215 0.50 30.08 ? ? ? ? ? ? 1880 MET A N 1 +ATOM 181 C CA A MET A 1 25 ? 16.841 23.392 30.395 0.50 32.58 ? ? ? ? ? ? 1880 MET A CA 1 +ATOM 182 C CA B MET A 1 25 ? 16.776 23.400 30.498 0.50 33.02 ? ? ? ? ? ? 1880 MET A CA 1 +ATOM 183 C C A MET A 1 25 ? 15.470 23.918 30.013 0.50 35.67 ? ? ? ? ? ? 1880 MET A C 1 +ATOM 184 C C B MET A 1 25 ? 15.465 23.980 29.993 0.50 35.47 ? ? ? ? ? ? 1880 MET A C 1 +ATOM 185 O O A MET A 1 25 ? 14.851 24.668 30.763 0.50 33.66 ? ? ? ? ? ? 1880 MET A O 1 +ATOM 186 O O B MET A 1 25 ? 14.881 24.839 30.646 0.50 33.82 ? ? ? ? ? ? 1880 MET A O 1 +ATOM 187 C CB A MET A 1 25 ? 17.914 24.079 29.553 0.50 27.06 ? ? ? ? ? ? 1880 MET A CB 1 +ATOM 188 C CB B MET A 1 25 ? 17.952 24.144 29.886 0.50 29.17 ? ? ? ? ? ? 1880 MET A CB 1 +ATOM 189 C CG A MET A 1 25 ? 19.311 23.593 29.839 0.50 35.88 ? ? ? ? ? ? 1880 MET A CG 1 +ATOM 190 C CG B MET A 1 25 ? 19.275 23.710 30.456 0.50 37.28 ? ? ? ? ? ? 1880 MET A CG 1 +ATOM 191 S SD A MET A 1 25 ? 19.882 24.127 31.457 0.50 28.14 ? ? ? ? ? ? 1880 MET A SD 1 +ATOM 192 S SD B MET A 1 25 ? 20.611 24.675 29.769 0.50 50.99 ? ? ? ? ? ? 1880 MET A SD 1 +ATOM 193 C CE A MET A 1 25 ? 20.137 25.867 31.121 0.50 39.07 ? ? ? ? ? ? 1880 MET A CE 1 +ATOM 194 C CE B MET A 1 25 ? 20.256 26.231 30.541 0.50 42.98 ? ? ? ? ? ? 1880 MET A CE 1 +ATOM 195 N N . GLU A 1 26 ? 15.004 23.503 28.839 1.00 31.13 ? ? ? ? ? ? 1881 GLU A N 1 +ATOM 196 C CA . GLU A 1 26 ? 13.712 23.922 28.308 1.00 29.36 ? ? ? ? ? ? 1881 GLU A CA 1 +ATOM 197 C C . GLU A 1 26 ? 12.547 23.576 29.227 1.00 34.55 ? ? ? ? ? ? 1881 GLU A C 1 +ATOM 198 O O . GLU A 1 26 ? 11.561 24.305 29.284 1.00 32.96 ? ? ? ? ? ? 1881 GLU A O 1 +ATOM 199 C CB . GLU A 1 26 ? 13.474 23.286 26.935 1.00 32.30 ? ? ? ? ? ? 1881 GLU A CB 1 +ATOM 200 C CG . GLU A 1 26 ? 14.297 23.903 25.821 1.00 33.09 ? ? ? ? ? ? 1881 GLU A CG 1 +ATOM 201 C CD . GLU A 1 26 ? 14.350 23.025 24.574 1.00 38.42 ? ? ? ? ? ? 1881 GLU A CD 1 +ATOM 202 O OE1 . GLU A 1 26 ? 13.998 21.829 24.664 1.00 39.73 ? ? ? ? ? ? 1881 GLU A OE1 1 +ATOM 203 O OE2 . GLU A 1 26 ? 14.760 23.530 23.510 1.00 45.56 ? ? ? ? ? ? 1881 GLU A OE2 1 +ATOM 204 N N . THR A 1 27 ? 12.651 22.460 29.945 1.00 25.47 ? ? ? ? ? ? 1882 THR A N 1 +ATOM 205 C CA . THR A 1 27 ? 11.531 22.002 30.761 1.00 30.27 ? ? ? ? ? ? 1882 THR A CA 1 +ATOM 206 C C . THR A 1 27 ? 11.632 22.451 32.232 1.00 31.67 ? ? ? ? ? ? 1882 THR A C 1 +ATOM 207 O O . THR A 1 27 ? 10.696 22.263 33.008 1.00 34.96 ? ? ? ? ? ? 1882 THR A O 1 +ATOM 208 C CB . THR A 1 27 ? 11.394 20.460 30.692 1.00 33.67 ? ? ? ? ? ? 1882 THR A CB 1 +ATOM 209 O OG1 . THR A 1 27 ? 12.640 19.855 31.035 1.00 38.66 ? ? ? ? ? ? 1882 THR A OG1 1 +ATOM 210 C CG2 . THR A 1 27 ? 11.036 20.041 29.285 1.00 37.00 ? ? ? ? ? ? 1882 THR A CG2 1 +ATOM 211 N N . HIS A 1 28 ? 12.760 23.047 32.605 1.00 29.70 ? ? ? ? ? ? 1883 HIS A N 1 +ATOM 212 C CA . HIS A 1 28 ? 12.923 23.639 33.936 1.00 32.25 ? ? ? ? ? ? 1883 HIS A CA 1 +ATOM 213 C C . HIS A 1 28 ? 11.846 24.700 34.183 1.00 36.99 ? ? ? ? ? ? 1883 HIS A C 1 +ATOM 214 O O . HIS A 1 28 ? 11.529 25.487 33.293 1.00 30.64 ? ? ? ? ? ? 1883 HIS A O 1 +ATOM 215 C CB . HIS A 1 28 ? 14.320 24.251 34.061 1.00 30.48 ? ? ? ? ? ? 1883 HIS A CB 1 +ATOM 216 C CG . HIS A 1 28 ? 14.718 24.603 35.462 1.00 33.35 ? ? ? ? ? ? 1883 HIS A CG 1 +ATOM 217 N ND1 . HIS A 1 28 ? 14.036 25.526 36.223 1.00 36.28 ? ? ? ? ? ? 1883 HIS A ND1 1 +ATOM 218 C CD2 . HIS A 1 28 ? 15.757 24.182 36.222 1.00 30.70 ? ? ? ? ? ? 1883 HIS A CD2 1 +ATOM 219 C CE1 . HIS A 1 28 ? 14.626 25.647 37.401 1.00 34.92 ? ? ? ? ? ? 1883 HIS A CE1 1 +ATOM 220 N NE2 . HIS A 1 28 ? 15.672 24.843 37.425 1.00 39.78 ? ? ? ? ? ? 1883 HIS A NE2 1 +ATOM 221 N N . GLU A 1 29 ? 11.278 24.738 35.385 1.00 34.00 ? ? ? ? ? ? 1884 GLU A N 1 +ATOM 222 C CA . GLU A 1 29 ? 10.160 25.645 35.622 1.00 35.82 ? ? ? ? ? ? 1884 GLU A CA 1 +ATOM 223 C C . GLU A 1 29 ? 10.586 27.122 35.551 1.00 34.04 ? ? ? ? ? ? 1884 GLU A C 1 +ATOM 224 O O . GLU A 1 29 ? 9.746 28.004 35.369 1.00 36.46 ? ? ? ? ? ? 1884 GLU A O 1 +ATOM 225 C CB . GLU A 1 29 ? 9.483 25.343 36.969 1.00 49.90 ? ? ? ? ? ? 1884 GLU A CB 1 +ATOM 226 C CG . GLU A 1 29 ? 10.188 25.869 38.208 1.00 53.04 ? ? ? ? ? ? 1884 GLU A CG 1 +ATOM 227 C CD . GLU A 1 29 ? 9.307 25.790 39.459 1.00 68.03 ? ? ? ? ? ? 1884 GLU A CD 1 +ATOM 228 O OE1 . GLU A 1 29 ? 8.420 26.658 39.624 1.00 64.96 ? ? ? ? ? ? 1884 GLU A OE1 1 +ATOM 229 O OE2 . GLU A 1 29 ? 9.501 24.864 40.281 1.00 72.50 ? ? ? ? ? ? 1884 GLU A OE2 1 +ATOM 230 N N . ASP A 1 30 ? 11.882 27.391 35.668 1.00 30.65 ? ? ? ? ? ? 1885 ASP A N 1 +ATOM 231 C CA . ASP A 1 30 ? 12.369 28.766 35.569 1.00 33.88 ? ? ? ? ? ? 1885 ASP A CA 1 +ATOM 232 C C . ASP A 1 30 ? 12.913 29.088 34.175 1.00 33.81 ? ? ? ? ? ? 1885 ASP A C 1 +ATOM 233 O O . ASP A 1 30 ? 13.650 30.056 34.003 1.00 27.56 ? ? ? ? ? ? 1885 ASP A O 1 +ATOM 234 C CB . ASP A 1 30 ? 13.463 29.036 36.605 1.00 28.96 ? ? ? ? ? ? 1885 ASP A CB 1 +ATOM 235 C CG . ASP A 1 30 ? 12.966 28.918 38.042 1.00 31.94 ? ? ? ? ? ? 1885 ASP A CG 1 +ATOM 236 O OD1 . ASP A 1 30 ? 11.742 28.962 38.296 1.00 35.25 ? ? ? ? ? ? 1885 ASP A OD1 1 +ATOM 237 O OD2 . ASP A 1 30 ? 13.827 28.805 38.927 1.00 32.07 ? ? ? ? ? ? 1885 ASP A OD2 1 +ATOM 238 N N . ALA A 1 31 ? 12.558 28.279 33.181 1.00 29.61 ? ? ? ? ? ? 1886 ALA A N 1 +ATOM 239 C CA . ALA A 1 31 ? 13.059 28.492 31.823 1.00 28.61 ? ? ? ? ? ? 1886 ALA A CA 1 +ATOM 240 C C . ALA A 1 31 ? 12.324 29.611 31.095 1.00 26.63 ? ? ? ? ? ? 1886 ALA A C 1 +ATOM 241 O O . ALA A 1 31 ? 12.806 30.122 30.092 1.00 31.44 ? ? ? ? ? ? 1886 ALA A O 1 +ATOM 242 C CB . ALA A 1 31 ? 12.955 27.206 31.015 1.00 29.69 ? ? ? ? ? ? 1886 ALA A CB 1 +ATOM 243 N N . TRP A 1 32 ? 11.158 29.990 31.607 1.00 29.05 ? ? ? ? ? ? 1887 TRP A N 1 +ATOM 244 C CA . TRP A 1 32 ? 10.261 30.870 30.869 1.00 32.31 ? ? ? ? ? ? 1887 TRP A CA 1 +ATOM 245 C C . TRP A 1 32 ? 10.870 32.201 30.396 1.00 33.67 ? ? ? ? ? ? 1887 TRP A C 1 +ATOM 246 O O . TRP A 1 32 ? 10.483 32.682 29.337 1.00 34.21 ? ? ? ? ? ? 1887 TRP A O 1 +ATOM 247 C CB . TRP A 1 32 ? 8.996 31.146 31.691 1.00 34.38 ? ? ? ? ? ? 1887 TRP A CB 1 +ATOM 248 C CG . TRP A 1 32 ? 9.226 31.762 33.047 1.00 33.00 ? ? ? ? ? ? 1887 TRP A CG 1 +ATOM 249 C CD1 . TRP A 1 32 ? 9.416 31.096 34.231 1.00 28.53 ? ? ? ? ? ? 1887 TRP A CD1 1 +ATOM 250 C CD2 . TRP A 1 32 ? 9.259 33.161 33.360 1.00 34.53 ? ? ? ? ? ? 1887 TRP A CD2 1 +ATOM 251 N NE1 . TRP A 1 32 ? 9.578 32.000 35.257 1.00 30.56 ? ? ? ? ? ? 1887 TRP A NE1 1 +ATOM 252 C CE2 . TRP A 1 32 ? 9.492 33.273 34.749 1.00 35.49 ? ? ? ? ? ? 1887 TRP A CE2 1 +ATOM 253 C CE3 . TRP A 1 32 ? 9.139 34.330 32.600 1.00 33.60 ? ? ? ? ? ? 1887 TRP A CE3 1 +ATOM 254 C CZ2 . TRP A 1 32 ? 9.594 34.509 35.394 1.00 35.74 ? ? ? ? ? ? 1887 TRP A CZ2 1 +ATOM 255 C CZ3 . TRP A 1 32 ? 9.239 35.559 33.242 1.00 34.23 ? ? ? ? ? ? 1887 TRP A CZ3 1 +ATOM 256 C CH2 . TRP A 1 32 ? 9.463 35.638 34.625 1.00 35.07 ? ? ? ? ? ? 1887 TRP A CH2 1 +ATOM 257 N N . PRO A 1 33 ? 11.829 32.792 31.146 1.00 28.38 ? ? ? ? ? ? 1888 PRO A N 1 +ATOM 258 C CA . PRO A 1 33 ? 12.350 34.041 30.578 1.00 27.50 ? ? ? ? ? ? 1888 PRO A CA 1 +ATOM 259 C C . PRO A 1 33 ? 13.239 33.826 29.347 1.00 26.54 ? ? ? ? ? ? 1888 PRO A C 1 +ATOM 260 O O . PRO A 1 33 ? 13.584 34.806 28.679 1.00 27.61 ? ? ? ? ? ? 1888 PRO A O 1 +ATOM 261 C CB . PRO A 1 33 ? 13.180 34.638 31.733 1.00 28.19 ? ? ? ? ? ? 1888 PRO A CB 1 +ATOM 262 C CG . PRO A 1 33 ? 12.712 33.929 32.972 1.00 28.71 ? ? ? ? ? ? 1888 PRO A CG 1 +ATOM 263 C CD . PRO A 1 33 ? 12.373 32.550 32.496 1.00 25.46 ? ? ? ? ? ? 1888 PRO A CD 1 +ATOM 264 N N . PHE A 1 34 ? 13.588 32.572 29.062 1.00 28.06 ? ? ? ? ? ? 1889 PHE A N 1 +ATOM 265 C CA . PHE A 1 34 ? 14.655 32.264 28.111 1.00 27.14 ? ? ? ? ? ? 1889 PHE A CA 1 +ATOM 266 C C . PHE A 1 34 ? 14.199 31.419 26.939 1.00 26.62 ? ? ? ? ? ? 1889 PHE A C 1 +ATOM 267 O O . PHE A 1 34 ? 15.010 31.052 26.090 1.00 27.89 ? ? ? ? ? ? 1889 PHE A O 1 +ATOM 268 C CB . PHE A 1 34 ? 15.799 31.547 28.835 1.00 30.41 ? ? ? ? ? ? 1889 PHE A CB 1 +ATOM 269 C CG . PHE A 1 34 ? 16.170 32.186 30.136 1.00 29.02 ? ? ? ? ? ? 1889 PHE A CG 1 +ATOM 270 C CD1 . PHE A 1 34 ? 16.737 33.452 30.154 1.00 28.32 ? ? ? ? ? ? 1889 PHE A CD1 1 +ATOM 271 C CD2 . PHE A 1 34 ? 15.933 31.541 31.339 1.00 26.75 ? ? ? ? ? ? 1889 PHE A CD2 1 +ATOM 272 C CE1 . PHE A 1 34 ? 17.069 34.073 31.359 1.00 27.87 ? ? ? ? ? ? 1889 PHE A CE1 1 +ATOM 273 C CE2 . PHE A 1 34 ? 16.267 32.147 32.548 1.00 28.96 ? ? ? ? ? ? 1889 PHE A CE2 1 +ATOM 274 C CZ . PHE A 1 34 ? 16.840 33.419 32.556 1.00 30.62 ? ? ? ? ? ? 1889 PHE A CZ 1 +ATOM 275 N N . LEU A 1 35 ? 12.913 31.083 26.901 1.00 27.89 ? ? ? ? ? ? 1890 LEU A N 1 +ATOM 276 C CA . LEU A 1 35 ? 12.435 30.097 25.937 1.00 31.41 ? ? ? ? ? ? 1890 LEU A CA 1 +ATOM 277 C C . LEU A 1 35 ? 12.409 30.654 24.523 1.00 36.61 ? ? ? ? ? ? 1890 LEU A C 1 +ATOM 278 O O . LEU A 1 35 ? 12.694 29.937 23.567 1.00 29.63 ? ? ? ? ? ? 1890 LEU A O 1 +ATOM 279 C CB . LEU A 1 35 ? 11.042 29.594 26.326 1.00 29.84 ? ? ? ? ? ? 1890 LEU A CB 1 +ATOM 280 C CG . LEU A 1 35 ? 11.004 28.701 27.566 1.00 32.90 ? ? ? ? ? ? 1890 LEU A CG 1 +ATOM 281 C CD1 . LEU A 1 35 ? 9.569 28.385 27.953 1.00 34.21 ? ? ? ? ? ? 1890 LEU A CD1 1 +ATOM 282 C CD2 . LEU A 1 35 ? 11.793 27.421 27.314 1.00 39.56 ? ? ? ? ? ? 1890 LEU A CD2 1 +ATOM 283 N N . LEU A 1 36 ? 12.075 31.934 24.407 1.00 28.94 ? ? ? ? ? ? 1891 LEU A N 1 +ATOM 284 C CA . LEU A 1 36 ? 11.895 32.575 23.112 1.00 30.89 ? ? ? ? ? ? 1891 LEU A CA 1 +ATOM 285 C C . LEU A 1 36 ? 12.724 33.845 23.030 1.00 33.60 ? ? ? ? ? ? 1891 LEU A C 1 +ATOM 286 O O . LEU A 1 36 ? 13.086 34.417 24.064 1.00 29.30 ? ? ? ? ? ? 1891 LEU A O 1 +ATOM 287 C CB . LEU A 1 36 ? 10.419 32.893 22.884 1.00 35.28 ? ? ? ? ? ? 1891 LEU A CB 1 +ATOM 288 C CG . LEU A 1 36 ? 9.467 31.700 22.830 1.00 35.57 ? ? ? ? ? ? 1891 LEU A CG 1 +ATOM 289 C CD1 . LEU A 1 36 ? 8.034 32.196 22.731 1.00 39.91 ? ? ? ? ? ? 1891 LEU A CD1 1 +ATOM 290 C CD2 . LEU A 1 36 ? 9.805 30.796 21.657 1.00 41.14 ? ? ? ? ? ? 1891 LEU A CD2 1 +ATOM 291 N N . PRO A 1 37 ? 13.034 34.296 21.801 1.00 29.55 ? ? ? ? ? ? 1892 PRO A N 1 +ATOM 292 C CA . PRO A 1 37 ? 13.814 35.533 21.691 1.00 27.16 ? ? ? ? ? ? 1892 PRO A CA 1 +ATOM 293 C C . PRO A 1 37 ? 13.045 36.734 22.242 1.00 25.28 ? ? ? ? ? ? 1892 PRO A C 1 +ATOM 294 O O . PRO A 1 37 ? 11.820 36.781 22.132 1.00 30.03 ? ? ? ? ? ? 1892 PRO A O 1 +ATOM 295 C CB . PRO A 1 37 ? 14.056 35.674 20.176 1.00 31.06 ? ? ? ? ? ? 1892 PRO A CB 1 +ATOM 296 C CG . PRO A 1 37 ? 13.058 34.797 19.530 1.00 30.15 ? ? ? ? ? ? 1892 PRO A CG 1 +ATOM 297 C CD . PRO A 1 37 ? 12.741 33.696 20.481 1.00 27.23 ? ? ? ? ? ? 1892 PRO A CD 1 +ATOM 298 N N . VAL A 1 38 ? 13.758 37.666 22.864 1.00 29.36 ? ? ? ? ? ? 1893 VAL A N 1 +ATOM 299 C CA . VAL A 1 38 ? 13.161 38.932 23.290 1.00 31.65 ? ? ? ? ? ? 1893 VAL A CA 1 +ATOM 300 C C . VAL A 1 38 ? 12.647 39.692 22.076 1.00 39.03 ? ? ? ? ? ? 1893 VAL A C 1 +ATOM 301 O O . VAL A 1 38 ? 13.336 39.764 21.056 1.00 37.18 ? ? ? ? ? ? 1893 VAL A O 1 +ATOM 302 C CB . VAL A 1 38 ? 14.175 39.803 24.058 1.00 35.58 ? ? ? ? ? ? 1893 VAL A CB 1 +ATOM 303 C CG1 . VAL A 1 38 ? 13.634 41.215 24.274 1.00 37.63 ? ? ? ? ? ? 1893 VAL A CG1 1 +ATOM 304 C CG2 . VAL A 1 38 ? 14.528 39.150 25.388 1.00 34.79 ? ? ? ? ? ? 1893 VAL A CG2 1 +ATOM 305 N N . ASN A 1 39 ? 11.425 40.216 22.168 1.00 39.34 ? ? ? ? ? ? 1894 ASN A N 1 +ATOM 306 C CA . ASN A 1 39 ? 10.860 41.038 21.102 1.00 47.30 ? ? ? ? ? ? 1894 ASN A CA 1 +ATOM 307 C C . ASN A 1 39 ? 11.486 42.426 21.145 1.00 43.68 ? ? ? ? ? ? 1894 ASN A C 1 +ATOM 308 O O . ASN A 1 39 ? 11.179 43.228 22.023 1.00 43.55 ? ? ? ? ? ? 1894 ASN A O 1 +ATOM 309 C CB . ASN A 1 39 ? 9.335 41.130 21.229 1.00 47.40 ? ? ? ? ? ? 1894 ASN A CB 1 +ATOM 310 C CG . ASN A 1 39 ? 8.686 41.844 20.053 1.00 50.62 ? ? ? ? ? ? 1894 ASN A CG 1 +ATOM 311 O OD1 . ASN A 1 39 ? 9.260 42.764 19.468 1.00 51.95 ? ? ? ? ? ? 1894 ASN A OD1 1 +ATOM 312 N ND2 . ASN A 1 39 ? 7.479 41.424 19.705 1.00 48.95 ? ? ? ? ? ? 1894 ASN A ND2 1 +ATOM 313 N N . LEU A 1 40 ? 12.356 42.701 20.179 1.00 42.52 ? ? ? ? ? ? 1895 LEU A N 1 +ATOM 314 C CA . LEU A 1 40 ? 13.168 43.910 20.186 1.00 40.45 ? ? ? ? ? ? 1895 LEU A CA 1 +ATOM 315 C C . LEU A 1 40 ? 12.364 45.167 19.869 1.00 41.59 ? ? ? ? ? ? 1895 LEU A C 1 +ATOM 316 O O . LEU A 1 40 ? 12.845 46.289 20.060 1.00 40.45 ? ? ? ? ? ? 1895 LEU A O 1 +ATOM 317 C CB . LEU A 1 40 ? 14.322 43.760 19.193 1.00 42.57 ? ? ? ? ? ? 1895 LEU A CB 1 +ATOM 318 C CG . LEU A 1 40 ? 15.246 42.566 19.440 1.00 44.45 ? ? ? ? ? ? 1895 LEU A CG 1 +ATOM 319 C CD1 . LEU A 1 40 ? 16.345 42.506 18.379 1.00 48.93 ? ? ? ? ? ? 1895 LEU A CD1 1 +ATOM 320 C CD2 . LEU A 1 40 ? 15.835 42.620 20.854 1.00 40.29 ? ? ? ? ? ? 1895 LEU A CD2 1 +ATOM 321 N N . LYS A 1 41 ? 11.138 44.982 19.391 1.00 49.11 ? ? ? ? ? ? 1896 LYS A N 1 +ATOM 322 C CA . LYS A 1 41 ? 10.271 46.113 19.099 1.00 57.85 ? ? ? ? ? ? 1896 LYS A CA 1 +ATOM 323 C C . LYS A 1 41 ? 9.396 46.467 20.298 1.00 58.57 ? ? ? ? ? ? 1896 LYS A C 1 +ATOM 324 O O . LYS A 1 41 ? 8.780 47.529 20.324 1.00 58.04 ? ? ? ? ? ? 1896 LYS A O 1 +ATOM 325 C CB . LYS A 1 41 ? 9.395 45.822 17.876 1.00 61.41 ? ? ? ? ? ? 1896 LYS A CB 1 +ATOM 326 C CG . LYS A 1 41 ? 10.183 45.455 16.627 1.00 66.66 ? ? ? ? ? ? 1896 LYS A CG 1 +ATOM 327 C CD . LYS A 1 41 ? 9.506 45.982 15.364 1.00 80.59 ? ? ? ? ? ? 1896 LYS A CD 1 +ATOM 328 C CE . LYS A 1 41 ? 8.207 45.248 15.057 1.00 89.11 ? ? ? ? ? ? 1896 LYS A CE 1 +ATOM 329 N NZ . LYS A 1 41 ? 8.440 43.883 14.504 1.00 90.85 ? ? ? ? ? ? 1896 LYS A NZ 1 +ATOM 330 N N . LEU A 1 42 ? 9.344 45.589 21.296 1.00 51.72 ? ? ? ? ? ? 1897 LEU A N 1 +ATOM 331 C CA . LEU A 1 42 ? 8.461 45.825 22.437 1.00 56.54 ? ? ? ? ? ? 1897 LEU A CA 1 +ATOM 332 C C . LEU A 1 42 ? 9.205 46.067 23.744 1.00 55.52 ? ? ? ? ? ? 1897 LEU A C 1 +ATOM 333 O O . LEU A 1 42 ? 8.626 46.570 24.704 1.00 60.78 ? ? ? ? ? ? 1897 LEU A O 1 +ATOM 334 C CB . LEU A 1 42 ? 7.495 44.656 22.615 1.00 52.50 ? ? ? ? ? ? 1897 LEU A CB 1 +ATOM 335 C CG . LEU A 1 42 ? 6.563 44.373 21.433 1.00 64.69 ? ? ? ? ? ? 1897 LEU A CG 1 +ATOM 336 C CD1 . LEU A 1 42 ? 5.508 43.344 21.818 1.00 69.25 ? ? ? ? ? ? 1897 LEU A CD1 1 +ATOM 337 C CD2 . LEU A 1 42 ? 5.915 45.651 20.923 1.00 68.57 ? ? ? ? ? ? 1897 LEU A CD2 1 +ATOM 338 N N . VAL A 1 43 ? 10.484 45.716 23.784 1.00 45.98 ? ? ? ? ? ? 1898 VAL A N 1 +ATOM 339 C CA . VAL A 1 43 ? 11.266 45.878 25.004 1.00 42.42 ? ? ? ? ? ? 1898 VAL A CA 1 +ATOM 340 C C . VAL A 1 43 ? 12.303 46.989 24.850 1.00 41.98 ? ? ? ? ? ? 1898 VAL A C 1 +ATOM 341 O O . VAL A 1 43 ? 13.318 46.808 24.174 1.00 39.52 ? ? ? ? ? ? 1898 VAL A O 1 +ATOM 342 C CB . VAL A 1 43 ? 11.976 44.571 25.396 1.00 42.66 ? ? ? ? ? ? 1898 VAL A CB 1 +ATOM 343 C CG1 . VAL A 1 43 ? 12.746 44.759 26.696 1.00 42.08 ? ? ? ? ? ? 1898 VAL A CG1 1 +ATOM 344 C CG2 . VAL A 1 43 ? 10.965 43.431 25.515 1.00 40.06 ? ? ? ? ? ? 1898 VAL A CG2 1 +ATOM 345 N N . PRO A 1 44 ? 12.045 48.151 25.476 1.00 40.07 ? ? ? ? ? ? 1899 PRO A N 1 +ATOM 346 C CA . PRO A 1 44 ? 12.974 49.281 25.405 1.00 40.44 ? ? ? ? ? ? 1899 PRO A CA 1 +ATOM 347 C C . PRO A 1 44 ? 14.377 48.914 25.877 1.00 41.94 ? ? ? ? ? ? 1899 PRO A C 1 +ATOM 348 O O . PRO A 1 44 ? 14.525 48.134 26.821 1.00 38.75 ? ? ? ? ? ? 1899 PRO A O 1 +ATOM 349 C CB . PRO A 1 44 ? 12.337 50.325 26.338 1.00 47.77 ? ? ? ? ? ? 1899 PRO A CB 1 +ATOM 350 C CG . PRO A 1 44 ? 10.892 49.974 26.362 1.00 50.19 ? ? ? ? ? ? 1899 PRO A CG 1 +ATOM 351 C CD . PRO A 1 44 ? 10.840 48.473 26.260 1.00 42.99 ? ? ? ? ? ? 1899 PRO A CD 1 +ATOM 352 N N . GLY A 1 45 ? 15.389 49.449 25.202 1.00 33.46 ? ? ? ? ? ? 1900 GLY A N 1 +ATOM 353 C CA . GLY A 1 45 ? 16.771 49.217 25.580 1.00 32.23 ? ? ? ? ? ? 1900 GLY A CA 1 +ATOM 354 C C . GLY A 1 45 ? 17.421 47.944 25.066 1.00 33.36 ? ? ? ? ? ? 1900 GLY A C 1 +ATOM 355 O O . GLY A 1 45 ? 18.625 47.926 24.815 1.00 35.28 ? ? ? ? ? ? 1900 GLY A O 1 +ATOM 356 N N . TYR A 1 46 ? 16.646 46.876 24.903 1.00 32.27 ? ? ? ? ? ? 1901 TYR A N 1 +ATOM 357 C CA . TYR A 1 46 ? 17.257 45.557 24.700 1.00 30.42 ? ? ? ? ? ? 1901 TYR A CA 1 +ATOM 358 C C . TYR A 1 46 ? 18.127 45.468 23.444 1.00 36.14 ? ? ? ? ? ? 1901 TYR A C 1 +ATOM 359 O O . TYR A 1 46 ? 19.244 44.943 23.500 1.00 30.38 ? ? ? ? ? ? 1901 TYR A O 1 +ATOM 360 C CB . TYR A 1 46 ? 16.198 44.459 24.660 1.00 34.29 ? ? ? ? ? ? 1901 TYR A CB 1 +ATOM 361 C CG . TYR A 1 46 ? 16.781 43.117 25.064 1.00 35.59 ? ? ? ? ? ? 1901 TYR A CG 1 +ATOM 362 C CD1 . TYR A 1 46 ? 17.358 42.268 24.123 1.00 30.79 ? ? ? ? ? ? 1901 TYR A CD1 1 +ATOM 363 C CD2 . TYR A 1 46 ? 16.801 42.728 26.401 1.00 30.40 ? ? ? ? ? ? 1901 TYR A CD2 1 +ATOM 364 C CE1 . TYR A 1 46 ? 17.915 41.043 24.505 1.00 31.12 ? ? ? ? ? ? 1901 TYR A CE1 1 +ATOM 365 C CE2 . TYR A 1 46 ? 17.353 41.512 26.791 1.00 34.55 ? ? ? ? ? ? 1901 TYR A CE2 1 +ATOM 366 C CZ . TYR A 1 46 ? 17.909 40.678 25.843 1.00 36.23 ? ? ? ? ? ? 1901 TYR A CZ 1 +ATOM 367 O OH . TYR A 1 46 ? 18.459 39.483 26.247 1.00 32.02 ? ? ? ? ? ? 1901 TYR A OH 1 +ATOM 368 N N . LYS A 1 47 ? 17.634 45.987 22.322 1.00 37.30 ? ? ? ? ? ? 1902 LYS A N 1 +ATOM 369 C CA . LYS A 1 47 ? 18.369 45.871 21.066 1.00 37.06 ? ? ? ? ? ? 1902 LYS A CA 1 +ATOM 370 C C . LYS A 1 47 ? 19.692 46.641 21.093 1.00 32.98 ? ? ? ? ? ? 1902 LYS A C 1 +ATOM 371 O O . LYS A 1 47 ? 20.710 46.152 20.601 1.00 38.46 ? ? ? ? ? ? 1902 LYS A O 1 +ATOM 372 C CB . LYS A 1 47 ? 17.509 46.348 19.890 1.00 37.99 ? ? ? ? ? ? 1902 LYS A CB 1 +ATOM 373 C CG . LYS A 1 47 ? 18.141 46.051 18.527 1.00 40.43 ? ? ? ? ? ? 1902 LYS A CG 1 +ATOM 374 C CD . LYS A 1 47 ? 17.258 46.494 17.371 1.00 42.73 ? ? ? ? ? ? 1902 LYS A CD 1 +ATOM 375 C CE . LYS A 1 47 ? 17.951 46.245 16.036 1.00 50.85 ? ? ? ? ? ? 1902 LYS A CE 1 +ATOM 376 N NZ . LYS A 1 47 ? 17.207 46.890 14.923 1.00 57.37 ? ? ? ? ? ? 1902 LYS A NZ 1 +ATOM 377 N N . LYS A 1 48 ? 19.683 47.838 21.673 1.00 32.27 ? ? ? ? ? ? 1903 LYS A N 1 +ATOM 378 C CA . LYS A 1 48 ? 20.895 48.649 21.746 1.00 32.40 ? ? ? ? ? ? 1903 LYS A CA 1 +ATOM 379 C C . LYS A 1 48 ? 21.882 48.107 22.787 1.00 35.38 ? ? ? ? ? ? 1903 LYS A C 1 +ATOM 380 O O . LYS A 1 48 ? 23.098 48.167 22.607 1.00 36.08 ? ? ? ? ? ? 1903 LYS A O 1 +ATOM 381 C CB . LYS A 1 48 ? 20.543 50.111 22.073 1.00 33.13 ? ? ? ? ? ? 1903 LYS A CB 1 +ATOM 382 C CG . LYS A 1 48 ? 21.739 51.039 22.110 1.00 34.50 ? ? ? ? ? ? 1903 LYS A CG 1 +ATOM 383 C CD . LYS A 1 48 ? 22.399 51.137 20.737 1.00 39.54 ? ? ? ? ? ? 1903 LYS A CD 1 +ATOM 384 C CE . LYS A 1 48 ? 23.422 52.266 20.683 1.00 37.79 ? ? ? ? ? ? 1903 LYS A CE 1 +ATOM 385 N NZ . LYS A 1 48 ? 22.789 53.615 20.601 1.00 37.62 ? ? ? ? ? ? 1903 LYS A NZ 1 +ATOM 386 N N . VAL A 1 49 ? 21.351 47.577 23.880 1.00 30.58 ? ? ? ? ? ? 1904 VAL A N 1 +ATOM 387 C CA . VAL A 1 49 ? 22.188 47.139 24.992 1.00 32.15 ? ? ? ? ? ? 1904 VAL A CA 1 +ATOM 388 C C . VAL A 1 49 ? 22.761 45.735 24.761 1.00 34.56 ? ? ? ? ? ? 1904 VAL A C 1 +ATOM 389 O O . VAL A 1 49 ? 23.956 45.509 24.950 1.00 33.83 ? ? ? ? ? ? 1904 VAL A O 1 +ATOM 390 C CB . VAL A 1 49 ? 21.398 47.184 26.317 1.00 30.41 ? ? ? ? ? ? 1904 VAL A CB 1 +ATOM 391 C CG1 . VAL A 1 49 ? 22.159 46.483 27.445 1.00 31.36 ? ? ? ? ? ? 1904 VAL A CG1 1 +ATOM 392 C CG2 . VAL A 1 49 ? 21.081 48.650 26.706 1.00 30.57 ? ? ? ? ? ? 1904 VAL A CG2 1 +ATOM 393 N N . ILE A 1 50 ? 21.920 44.799 24.336 1.00 30.97 ? ? ? ? ? ? 1905 ILE A N 1 +ATOM 394 C CA . ILE A 1 50 ? 22.343 43.402 24.225 1.00 32.63 ? ? ? ? ? ? 1905 ILE A CA 1 +ATOM 395 C C . ILE A 1 50 ? 22.824 43.113 22.811 1.00 36.52 ? ? ? ? ? ? 1905 ILE A C 1 +ATOM 396 O O . ILE A 1 50 ? 22.019 42.933 21.902 1.00 33.48 ? ? ? ? ? ? 1905 ILE A O 1 +ATOM 397 C CB . ILE A 1 50 ? 21.203 42.441 24.604 1.00 31.55 ? ? ? ? ? ? 1905 ILE A CB 1 +ATOM 398 C CG1 . ILE A 1 50 ? 20.724 42.736 26.029 1.00 35.63 ? ? ? ? ? ? 1905 ILE A CG1 1 +ATOM 399 C CG2 . ILE A 1 50 ? 21.638 40.961 24.450 1.00 25.75 ? ? ? ? ? ? 1905 ILE A CG2 1 +ATOM 400 C CD1 . ILE A 1 50 ? 21.817 42.611 27.087 1.00 30.40 ? ? ? ? ? ? 1905 ILE A CD1 1 +ATOM 401 N N . LYS A 1 51 ? 24.140 43.070 22.635 1.00 32.04 ? ? ? ? ? ? 1906 LYS A N 1 +ATOM 402 C CA . LYS A 1 51 ? 24.726 43.008 21.302 1.00 37.03 ? ? ? ? ? ? 1906 LYS A CA 1 +ATOM 403 C C . LYS A 1 51 ? 24.508 41.665 20.624 1.00 42.60 ? ? ? ? ? ? 1906 LYS A C 1 +ATOM 404 O O . LYS A 1 51 ? 24.452 41.591 19.401 1.00 36.95 ? ? ? ? ? ? 1906 LYS A O 1 +ATOM 405 C CB . LYS A 1 51 ? 26.222 43.317 21.366 1.00 43.52 ? ? ? ? ? ? 1906 LYS A CB 1 +ATOM 406 C CG . LYS A 1 51 ? 26.531 44.687 21.956 1.00 51.77 ? ? ? ? ? ? 1906 LYS A CG 1 +ATOM 407 C CD . LYS A 1 51 ? 25.713 45.780 21.283 1.00 56.04 ? ? ? ? ? ? 1906 LYS A CD 1 +ATOM 408 C CE . LYS A 1 51 ? 26.063 47.155 21.843 1.00 60.15 ? ? ? ? ? ? 1906 LYS A CE 1 +ATOM 409 N NZ . LYS A 1 51 ? 25.459 48.252 21.038 1.00 68.25 ? ? ? ? ? ? 1906 LYS A NZ 1 +ATOM 410 N N . LYS A 1 52 ? 24.400 40.606 21.421 1.00 32.40 ? ? ? ? ? ? 1907 LYS A N 1 +ATOM 411 C CA . LYS A 1 52 ? 24.177 39.271 20.878 1.00 38.26 ? ? ? ? ? ? 1907 LYS A CA 1 +ATOM 412 C C . LYS A 1 52 ? 23.059 38.573 21.636 1.00 32.50 ? ? ? ? ? ? 1907 LYS A C 1 +ATOM 413 O O . LYS A 1 52 ? 23.324 37.822 22.566 1.00 32.01 ? ? ? ? ? ? 1907 LYS A O 1 +ATOM 414 C CB . LYS A 1 52 ? 25.451 38.425 20.954 1.00 40.79 ? ? ? ? ? ? 1907 LYS A CB 1 +ATOM 415 C CG . LYS A 1 52 ? 26.658 38.995 20.226 1.00 52.88 ? ? ? ? ? ? 1907 LYS A CG 1 +ATOM 416 C CD . LYS A 1 52 ? 27.825 38.022 20.317 1.00 64.25 ? ? ? ? ? ? 1907 LYS A CD 1 +ATOM 417 C CE . LYS A 1 52 ? 29.103 38.594 19.730 1.00 70.75 ? ? ? ? ? ? 1907 LYS A CE 1 +ATOM 418 N NZ . LYS A 1 52 ? 30.235 37.639 19.894 1.00 74.50 ? ? ? ? ? ? 1907 LYS A NZ 1 +ATOM 419 N N . PRO A 1 53 ? 21.805 38.835 21.249 1.00 34.48 ? ? ? ? ? ? 1908 PRO A N 1 +ATOM 420 C CA . PRO A 1 53 ? 20.656 38.155 21.850 1.00 35.95 ? ? ? ? ? ? 1908 PRO A CA 1 +ATOM 421 C C . PRO A 1 53 ? 20.735 36.641 21.643 1.00 32.19 ? ? ? ? ? ? 1908 PRO A C 1 +ATOM 422 O O . PRO A 1 53 ? 21.178 36.187 20.593 1.00 29.35 ? ? ? ? ? ? 1908 PRO A O 1 +ATOM 423 C CB . PRO A 1 53 ? 19.462 38.744 21.090 1.00 32.29 ? ? ? ? ? ? 1908 PRO A CB 1 +ATOM 424 C CG . PRO A 1 53 ? 19.952 40.057 20.564 1.00 35.82 ? ? ? ? ? ? 1908 PRO A CG 1 +ATOM 425 C CD . PRO A 1 53 ? 21.391 39.810 20.226 1.00 40.19 ? ? ? ? ? ? 1908 PRO A CD 1 +ATOM 426 N N . MET A 1 54 ? 20.317 35.874 22.638 1.00 31.14 ? ? ? ? ? ? 1909 MET A N 1 +ATOM 427 C CA . MET A 1 54 ? 20.273 34.420 22.502 1.00 31.21 ? ? ? ? ? ? 1909 MET A CA 1 +ATOM 428 C C . MET A 1 54 ? 19.186 33.889 23.421 1.00 36.10 ? ? ? ? ? ? 1909 MET A C 1 +ATOM 429 O O . MET A 1 54 ? 18.899 34.476 24.464 1.00 32.24 ? ? ? ? ? ? 1909 MET A O 1 +ATOM 430 C CB . MET A 1 54 ? 21.632 33.786 22.821 1.00 27.46 ? ? ? ? ? ? 1909 MET A CB 1 +ATOM 431 C CG . MET A 1 54 ? 21.703 32.276 22.560 1.00 30.39 ? ? ? ? ? ? 1909 MET A CG 1 +ATOM 432 S SD . MET A 1 54 ? 21.231 31.849 20.860 1.00 31.61 ? ? ? ? ? ? 1909 MET A SD 1 +ATOM 433 C CE . MET A 1 54 ? 22.413 32.841 19.935 1.00 31.97 ? ? ? ? ? ? 1909 MET A CE 1 +ATOM 434 N N . ASP A 1 55 ? 18.559 32.797 23.006 1.00 28.10 ? ? ? ? ? ? 1910 ASP A N 1 +ATOM 435 C CA . ASP A 1 55 ? 17.488 32.167 23.764 1.00 26.44 ? ? ? ? ? ? 1910 ASP A CA 1 +ATOM 436 C C . ASP A 1 55 ? 17.478 30.676 23.438 1.00 27.11 ? ? ? ? ? ? 1910 ASP A C 1 +ATOM 437 O O . ASP A 1 55 ? 18.103 30.252 22.462 1.00 28.75 ? ? ? ? ? ? 1910 ASP A O 1 +ATOM 438 C CB . ASP A 1 55 ? 16.142 32.797 23.420 1.00 30.13 ? ? ? ? ? ? 1910 ASP A CB 1 +ATOM 439 C CG . ASP A 1 55 ? 15.704 32.466 22.000 1.00 36.62 ? ? ? ? ? ? 1910 ASP A CG 1 +ATOM 440 O OD1 . ASP A 1 55 ? 16.234 33.093 21.063 1.00 31.77 ? ? ? ? ? ? 1910 ASP A OD1 1 +ATOM 441 O OD2 . ASP A 1 55 ? 14.859 31.562 21.821 1.00 31.86 ? ? ? ? ? ? 1910 ASP A OD2 1 +ATOM 442 N N . PHE A 1 56 ? 16.754 29.888 24.235 1.00 24.97 ? ? ? ? ? ? 1911 PHE A N 1 +ATOM 443 C CA . PHE A 1 56 ? 16.744 28.437 24.077 1.00 27.50 ? ? ? ? ? ? 1911 PHE A CA 1 +ATOM 444 C C . PHE A 1 56 ? 16.227 27.982 22.709 1.00 26.99 ? ? ? ? ? ? 1911 PHE A C 1 +ATOM 445 O O . PHE A 1 56 ? 16.751 27.029 22.142 1.00 25.02 ? ? ? ? ? ? 1911 PHE A O 1 +ATOM 446 C CB . PHE A 1 56 ? 15.903 27.769 25.174 1.00 27.27 ? ? ? ? ? ? 1911 PHE A CB 1 +ATOM 447 C CG . PHE A 1 56 ? 16.472 27.918 26.573 1.00 31.18 ? ? ? ? ? ? 1911 PHE A CG 1 +ATOM 448 C CD1 . PHE A 1 56 ? 17.757 28.402 26.783 1.00 26.63 ? ? ? ? ? ? 1911 PHE A CD1 1 +ATOM 449 C CD2 . PHE A 1 56 ? 15.715 27.551 27.681 1.00 27.78 ? ? ? ? ? ? 1911 PHE A CD2 1 +ATOM 450 C CE1 . PHE A 1 56 ? 18.268 28.534 28.077 1.00 27.00 ? ? ? ? ? ? 1911 PHE A CE1 1 +ATOM 451 C CE2 . PHE A 1 56 ? 16.224 27.670 28.970 1.00 28.79 ? ? ? ? ? ? 1911 PHE A CE2 1 +ATOM 452 C CZ . PHE A 1 56 ? 17.500 28.165 29.165 1.00 30.35 ? ? ? ? ? ? 1911 PHE A CZ 1 +ATOM 453 N N . SER A 1 57 ? 15.190 28.633 22.191 1.00 26.47 ? ? ? ? ? ? 1912 SER A N 1 +ATOM 454 C CA . SER A 1 57 ? 14.603 28.194 20.930 1.00 33.83 ? ? ? ? ? ? 1912 SER A CA 1 +ATOM 455 C C . SER A 1 57 ? 15.586 28.418 19.779 1.00 34.95 ? ? ? ? ? ? 1912 SER A C 1 +ATOM 456 O O . SER A 1 57 ? 15.630 27.642 18.820 1.00 28.99 ? ? ? ? ? ? 1912 SER A O 1 +ATOM 457 C CB . SER A 1 57 ? 13.281 28.913 20.652 1.00 33.80 ? ? ? ? ? ? 1912 SER A CB 1 +ATOM 458 O OG . SER A 1 57 ? 13.496 30.242 20.197 1.00 38.46 ? ? ? ? ? ? 1912 SER A OG 1 +ATOM 459 N N . THR A 1 58 ? 16.388 29.471 19.885 1.00 31.25 ? ? ? ? ? ? 1913 THR A N 1 +ATOM 460 C CA . THR A 1 58 ? 17.395 29.745 18.866 1.00 31.67 ? ? ? ? ? ? 1913 THR A CA 1 +ATOM 461 C C . THR A 1 58 ? 18.520 28.719 18.986 1.00 29.55 ? ? ? ? ? ? 1913 THR A C 1 +ATOM 462 O O . THR A 1 58 ? 19.008 28.205 17.984 1.00 34.32 ? ? ? ? ? ? 1913 THR A O 1 +ATOM 463 C CB . THR A 1 58 ? 17.940 31.187 18.983 1.00 30.13 ? ? ? ? ? ? 1913 THR A CB 1 +ATOM 464 O OG1 . THR A 1 58 ? 16.860 32.105 18.780 1.00 29.32 ? ? ? ? ? ? 1913 THR A OG1 1 +ATOM 465 C CG2 . THR A 1 58 ? 19.016 31.461 17.927 1.00 31.08 ? ? ? ? ? ? 1913 THR A CG2 1 +ATOM 466 N N . ILE A 1 59 ? 18.918 28.414 20.218 1.00 25.28 ? ? ? ? ? ? 1914 ILE A N 1 +ATOM 467 C CA . ILE A 1 59 ? 19.932 27.393 20.446 1.00 26.38 ? ? ? ? ? ? 1914 ILE A CA 1 +ATOM 468 C C . ILE A 1 59 ? 19.460 26.062 19.866 1.00 30.29 ? ? ? ? ? ? 1914 ILE A C 1 +ATOM 469 O O . ILE A 1 59 ? 20.231 25.338 19.228 1.00 30.05 ? ? ? ? ? ? 1914 ILE A O 1 +ATOM 470 C CB . ILE A 1 59 ? 20.247 27.240 21.947 1.00 26.58 ? ? ? ? ? ? 1914 ILE A CB 1 +ATOM 471 C CG1 . ILE A 1 59 ? 20.925 28.510 22.466 1.00 26.62 ? ? ? ? ? ? 1914 ILE A CG1 1 +ATOM 472 C CG2 . ILE A 1 59 ? 21.136 26.013 22.205 1.00 21.45 ? ? ? ? ? ? 1914 ILE A CG2 1 +ATOM 473 C CD1 . ILE A 1 59 ? 21.130 28.533 23.994 1.00 24.52 ? ? ? ? ? ? 1914 ILE A CD1 1 +ATOM 474 N N . ARG A 1 60 ? 18.183 25.757 20.077 1.00 29.81 ? ? ? ? ? ? 1915 ARG A N 1 +ATOM 475 C CA . ARG A 1 60 ? 17.607 24.512 19.602 1.00 30.33 ? ? ? ? ? ? 1915 ARG A CA 1 +ATOM 476 C C . ARG A 1 60 ? 17.611 24.470 18.072 1.00 35.06 ? ? ? ? ? ? 1915 ARG A C 1 +ATOM 477 O O . ARG A 1 60 ? 17.918 23.437 17.476 1.00 31.40 ? ? ? ? ? ? 1915 ARG A O 1 +ATOM 478 C CB . ARG A 1 60 ? 16.188 24.338 20.151 1.00 28.64 ? ? ? ? ? ? 1915 ARG A CB 1 +ATOM 479 C CG . ARG A 1 60 ? 15.384 23.225 19.497 1.00 29.90 ? ? ? ? ? ? 1915 ARG A CG 1 +ATOM 480 C CD . ARG A 1 60 ? 15.922 21.873 19.869 1.00 33.14 ? ? ? ? ? ? 1915 ARG A CD 1 +ATOM 481 N NE . ARG A 1 60 ? 15.700 21.544 21.276 1.00 35.58 ? ? ? ? ? ? 1915 ARG A NE 1 +ATOM 482 C CZ . ARG A 1 60 ? 16.197 20.459 21.861 1.00 40.70 ? ? ? ? ? ? 1915 ARG A CZ 1 +ATOM 483 N NH1 . ARG A 1 60 ? 16.937 19.615 21.157 1.00 35.66 ? ? ? ? ? ? 1915 ARG A NH1 1 +ATOM 484 N NH2 . ARG A 1 60 ? 15.958 20.219 23.141 1.00 37.90 ? ? ? ? ? ? 1915 ARG A NH2 1 +ATOM 485 N N . GLU A 1 61 ? 17.295 25.596 17.435 1.00 29.84 ? ? ? ? ? ? 1916 GLU A N 1 +ATOM 486 C CA . GLU A 1 61 ? 17.260 25.633 15.973 1.00 30.91 ? ? ? ? ? ? 1916 GLU A CA 1 +ATOM 487 C C . GLU A 1 61 ? 18.666 25.472 15.398 1.00 29.06 ? ? ? ? ? ? 1916 GLU A C 1 +ATOM 488 O O . GLU A 1 61 ? 18.861 24.764 14.401 1.00 31.85 ? ? ? ? ? ? 1916 GLU A O 1 +ATOM 489 C CB . GLU A 1 61 ? 16.612 26.929 15.467 1.00 28.90 ? ? ? ? ? ? 1916 GLU A CB 1 +ATOM 490 C CG . GLU A 1 61 ? 16.574 27.044 13.930 1.00 37.82 ? ? ? ? ? ? 1916 GLU A CG 1 +ATOM 491 C CD . GLU A 1 61 ? 15.696 25.986 13.251 1.00 49.56 ? ? ? ? ? ? 1916 GLU A CD 1 +ATOM 492 O OE1 . GLU A 1 61 ? 14.669 25.588 13.839 1.00 50.88 ? ? ? ? ? ? 1916 GLU A OE1 1 +ATOM 493 O OE2 . GLU A 1 61 ? 16.030 25.555 12.118 1.00 51.91 ? ? ? ? ? ? 1916 GLU A OE2 1 +ATOM 494 N N . LYS A 1 62 ? 19.642 26.112 16.042 1.00 29.56 ? ? ? ? ? ? 1917 LYS A N 1 +ATOM 495 C CA . LYS A 1 62 ? 21.041 25.972 15.641 1.00 29.59 ? ? ? ? ? ? 1917 LYS A CA 1 +ATOM 496 C C . LYS A 1 62 ? 21.544 24.535 15.813 1.00 30.33 ? ? ? ? ? ? 1917 LYS A C 1 +ATOM 497 O O . LYS A 1 62 ? 22.188 23.971 14.913 1.00 30.89 ? ? ? ? ? ? 1917 LYS A O 1 +ATOM 498 C CB . LYS A 1 62 ? 21.919 26.939 16.441 1.00 25.57 ? ? ? ? ? ? 1917 LYS A CB 1 +ATOM 499 C CG . LYS A 1 62 ? 21.718 28.409 16.027 1.00 30.26 ? ? ? ? ? ? 1917 LYS A CG 1 +ATOM 500 C CD . LYS A 1 62 ? 22.485 29.397 16.918 1.00 35.48 ? ? ? ? ? ? 1917 LYS A CD 1 +ATOM 501 C CE . LYS A 1 62 ? 23.988 29.313 16.704 1.00 33.84 ? ? ? ? ? ? 1917 LYS A CE 1 +ATOM 502 N NZ . LYS A 1 62 ? 24.696 30.465 17.350 1.00 36.79 ? ? ? ? ? ? 1917 LYS A NZ 1 +ATOM 503 N N . LEU A 1 63 ? 21.248 23.952 16.968 1.00 29.86 ? ? ? ? ? ? 1918 LEU A N 1 +ATOM 504 C CA . LEU A 1 63 ? 21.651 22.587 17.267 1.00 34.49 ? ? ? ? ? ? 1918 LEU A CA 1 +ATOM 505 C C . LEU A 1 63 ? 21.065 21.617 16.240 1.00 31.75 ? ? ? ? ? ? 1918 LEU A C 1 +ATOM 506 O O . LEU A 1 63 ? 21.771 20.739 15.735 1.00 38.05 ? ? ? ? ? ? 1918 LEU A O 1 +ATOM 507 C CB . LEU A 1 63 ? 21.216 22.199 18.685 1.00 35.71 ? ? ? ? ? ? 1918 LEU A CB 1 +ATOM 508 C CG . LEU A 1 63 ? 21.814 20.910 19.261 1.00 32.32 ? ? ? ? ? ? 1918 LEU A CG 1 +ATOM 509 C CD1 . LEU A 1 63 ? 23.322 21.051 19.401 1.00 33.35 ? ? ? ? ? ? 1918 LEU A CD1 1 +ATOM 510 C CD2 . LEU A 1 63 ? 21.179 20.541 20.603 1.00 30.86 ? ? ? ? ? ? 1918 LEU A CD2 1 +ATOM 511 N N . SER A 1 64 ? 19.782 21.797 15.925 1.00 31.49 ? ? ? ? ? ? 1919 SER A N 1 +ATOM 512 C CA . SER A 1 64 ? 19.055 20.898 15.026 1.00 35.20 ? ? ? ? ? ? 1919 SER A CA 1 +ATOM 513 C C . SER A 1 64 ? 19.457 21.063 13.567 1.00 34.05 ? ? ? ? ? ? 1919 SER A C 1 +ATOM 514 O O . SER A 1 64 ? 19.078 20.255 12.728 1.00 38.36 ? ? ? ? ? ? 1919 SER A O 1 +ATOM 515 C CB . SER A 1 64 ? 17.540 21.109 15.152 1.00 40.18 ? ? ? ? ? ? 1919 SER A CB 1 +ATOM 516 O OG . SER A 1 64 ? 17.080 20.795 16.459 1.00 47.92 ? ? ? ? ? ? 1919 SER A OG 1 +ATOM 517 N N . SER A 1 65 ? 20.219 22.102 13.260 1.00 33.75 ? ? ? ? ? ? 1920 SER A N 1 +ATOM 518 C CA . SER A 1 65 ? 20.567 22.378 11.861 1.00 36.24 ? ? ? ? ? ? 1920 SER A CA 1 +ATOM 519 C C . SER A 1 65 ? 22.078 22.408 11.653 1.00 34.46 ? ? ? ? ? ? 1920 SER A C 1 +ATOM 520 O O . SER A 1 65 ? 22.570 23.001 10.691 1.00 36.07 ? ? ? ? ? ? 1920 SER A O 1 +ATOM 521 C CB . SER A 1 65 ? 19.938 23.697 11.403 1.00 34.42 ? ? ? ? ? ? 1920 SER A CB 1 +ATOM 522 O OG . SER A 1 65 ? 20.338 24.791 12.220 1.00 34.45 ? ? ? ? ? ? 1920 SER A OG 1 +ATOM 523 N N . GLY A 1 66 ? 22.803 21.767 12.573 1.00 33.82 ? ? ? ? ? ? 1921 GLY A N 1 +ATOM 524 C CA . GLY A 1 66 ? 24.244 21.625 12.461 1.00 34.38 ? ? ? ? ? ? 1921 GLY A CA 1 +ATOM 525 C C . GLY A 1 66 ? 25.022 22.927 12.495 1.00 34.51 ? ? ? ? ? ? 1921 GLY A C 1 +ATOM 526 O O . GLY A 1 66 ? 26.042 23.067 11.830 1.00 36.20 ? ? ? ? ? ? 1921 GLY A O 1 +ATOM 527 N N . GLN A 1 67 ? 24.560 23.889 13.281 1.00 33.26 ? ? ? ? ? ? 1922 GLN A N 1 +ATOM 528 C CA . GLN A 1 67 ? 25.256 25.167 13.328 1.00 35.41 ? ? ? ? ? ? 1922 GLN A CA 1 +ATOM 529 C C . GLN A 1 67 ? 26.207 25.285 14.528 1.00 35.45 ? ? ? ? ? ? 1922 GLN A C 1 +ATOM 530 O O . GLN A 1 67 ? 26.852 26.311 14.701 1.00 34.29 ? ? ? ? ? ? 1922 GLN A O 1 +ATOM 531 C CB . GLN A 1 67 ? 24.244 26.316 13.318 1.00 34.27 ? ? ? ? ? ? 1922 GLN A CB 1 +ATOM 532 C CG . GLN A 1 67 ? 23.422 26.361 12.032 1.00 37.66 ? ? ? ? ? ? 1922 GLN A CG 1 +ATOM 533 C CD . GLN A 1 67 ? 22.535 27.579 11.947 1.00 43.12 ? ? ? ? ? ? 1922 GLN A CD 1 +ATOM 534 O OE1 . GLN A 1 67 ? 22.998 28.706 12.094 1.00 51.92 ? ? ? ? ? ? 1922 GLN A OE1 1 +ATOM 535 N NE2 . GLN A 1 67 ? 21.250 27.359 11.707 1.00 46.61 ? ? ? ? ? ? 1922 GLN A NE2 1 +ATOM 536 N N . TYR A 1 68 ? 26.305 24.235 15.345 1.00 31.80 ? ? ? ? ? ? 1923 TYR A N 1 +ATOM 537 C CA . TYR A 1 68 ? 27.362 24.153 16.358 1.00 31.75 ? ? ? ? ? ? 1923 TYR A CA 1 +ATOM 538 C C . TYR A 1 68 ? 28.434 23.185 15.879 1.00 40.06 ? ? ? ? ? ? 1923 TYR A C 1 +ATOM 539 O O . TYR A 1 68 ? 28.165 21.999 15.682 1.00 36.46 ? ? ? ? ? ? 1923 TYR A O 1 +ATOM 540 C CB . TYR A 1 68 ? 26.816 23.710 17.730 1.00 31.01 ? ? ? ? ? ? 1923 TYR A CB 1 +ATOM 541 C CG . TYR A 1 68 ? 25.900 24.749 18.330 1.00 32.47 ? ? ? ? ? ? 1923 TYR A CG 1 +ATOM 542 C CD1 . TYR A 1 68 ? 26.367 26.024 18.612 1.00 30.54 ? ? ? ? ? ? 1923 TYR A CD1 1 +ATOM 543 C CD2 . TYR A 1 68 ? 24.566 24.466 18.585 1.00 30.01 ? ? ? ? ? ? 1923 TYR A CD2 1 +ATOM 544 C CE1 . TYR A 1 68 ? 25.529 26.993 19.136 1.00 30.27 ? ? ? ? ? ? 1923 TYR A CE1 1 +ATOM 545 C CE2 . TYR A 1 68 ? 23.718 25.429 19.107 1.00 31.24 ? ? ? ? ? ? 1923 TYR A CE2 1 +ATOM 546 C CZ . TYR A 1 68 ? 24.209 26.686 19.383 1.00 30.03 ? ? ? ? ? ? 1923 TYR A CZ 1 +ATOM 547 O OH . TYR A 1 68 ? 23.366 27.644 19.882 1.00 30.30 ? ? ? ? ? ? 1923 TYR A OH 1 +ATOM 548 N N . PRO A 1 69 ? 29.652 23.694 15.669 1.00 33.86 ? ? ? ? ? ? 1924 PRO A N 1 +ATOM 549 C CA . PRO A 1 69 ? 30.730 22.832 15.181 1.00 35.51 ? ? ? ? ? ? 1924 PRO A CA 1 +ATOM 550 C C . PRO A 1 69 ? 31.306 21.926 16.269 1.00 43.48 ? ? ? ? ? ? 1924 PRO A C 1 +ATOM 551 O O . PRO A 1 69 ? 31.987 20.958 15.941 1.00 40.53 ? ? ? ? ? ? 1924 PRO A O 1 +ATOM 552 C CB . PRO A 1 69 ? 31.780 23.828 14.676 1.00 40.57 ? ? ? ? ? ? 1924 PRO A CB 1 +ATOM 553 C CG . PRO A 1 69 ? 31.490 25.101 15.394 1.00 43.85 ? ? ? ? ? ? 1924 PRO A CG 1 +ATOM 554 C CD . PRO A 1 69 ? 30.013 25.123 15.648 1.00 42.71 ? ? ? ? ? ? 1924 PRO A CD 1 +ATOM 555 N N . ASN A 1 70 ? 31.026 22.226 17.535 1.00 35.69 ? ? ? ? ? ? 1925 ASN A N 1 +ATOM 556 C CA . ASN A 1 70 ? 31.537 21.419 18.646 1.00 38.09 ? ? ? ? ? ? 1925 ASN A CA 1 +ATOM 557 C C . ASN A 1 70 ? 30.831 21.743 19.965 1.00 38.90 ? ? ? ? ? ? 1925 ASN A C 1 +ATOM 558 O O . ASN A 1 70 ? 30.026 22.675 20.019 1.00 34.01 ? ? ? ? ? ? 1925 ASN A O 1 +ATOM 559 C CB . ASN A 1 70 ? 33.051 21.620 18.797 1.00 38.20 ? ? ? ? ? ? 1925 ASN A CB 1 +ATOM 560 C CG . ASN A 1 70 ? 33.436 23.076 19.015 1.00 43.89 ? ? ? ? ? ? 1925 ASN A CG 1 +ATOM 561 O OD1 . ASN A 1 70 ? 32.795 23.801 19.779 1.00 43.39 ? ? ? ? ? ? 1925 ASN A OD1 1 +ATOM 562 N ND2 . ASN A 1 70 ? 34.491 23.511 18.340 1.00 44.29 ? ? ? ? ? ? 1925 ASN A ND2 1 +ATOM 563 N N . LEU A 1 71 ? 31.143 20.972 21.013 1.00 34.25 ? ? ? ? ? ? 1926 LEU A N 1 +ATOM 564 C CA . LEU A 1 71 ? 30.608 21.194 22.363 1.00 35.00 ? ? ? ? ? ? 1926 LEU A CA 1 +ATOM 565 C C . LEU A 1 71 ? 30.763 22.617 22.868 1.00 35.07 ? ? ? ? ? ? 1926 LEU A C 1 +ATOM 566 O O . LEU A 1 71 ? 29.817 23.223 23.386 1.00 37.04 ? ? ? ? ? ? 1926 LEU A O 1 +ATOM 567 C CB . LEU A 1 71 ? 31.307 20.275 23.368 1.00 44.18 ? ? ? ? ? ? 1926 LEU A CB 1 +ATOM 568 C CG . LEU A 1 71 ? 30.919 18.812 23.382 1.00 49.79 ? ? ? ? ? ? 1926 LEU A CG 1 +ATOM 569 C CD1 . LEU A 1 71 ? 31.581 18.126 24.560 1.00 55.29 ? ? ? ? ? ? 1926 LEU A CD1 1 +ATOM 570 C CD2 . LEU A 1 71 ? 29.425 18.712 23.477 1.00 55.89 ? ? ? ? ? ? 1926 LEU A CD2 1 +ATOM 571 N N . GLU A 1 72 ? 31.987 23.118 22.749 1.00 39.82 ? ? ? ? ? ? 1927 GLU A N 1 +ATOM 572 C CA . GLU A 1 72 ? 32.363 24.426 23.263 1.00 40.34 ? ? ? ? ? ? 1927 GLU A CA 1 +ATOM 573 C C . GLU A 1 72 ? 31.459 25.539 22.733 1.00 39.22 ? ? ? ? ? ? 1927 GLU A C 1 +ATOM 574 O O . GLU A 1 72 ? 31.051 26.423 23.486 1.00 35.73 ? ? ? ? ? ? 1927 GLU A O 1 +ATOM 575 C CB . GLU A 1 72 ? 33.826 24.715 22.911 1.00 46.91 ? ? ? ? ? ? 1927 GLU A CB 1 +ATOM 576 C CG . GLU A 1 72 ? 34.325 26.079 23.362 1.00 63.97 ? ? ? ? ? ? 1927 GLU A CG 1 +ATOM 577 N N . THR A 1 73 ? 31.130 25.494 21.443 1.00 38.59 ? ? ? ? ? ? 1928 THR A N 1 +ATOM 578 C CA . THR A 1 73 ? 30.324 26.561 20.860 1.00 33.76 ? ? ? ? ? ? 1928 THR A CA 1 +ATOM 579 C C . THR A 1 73 ? 28.870 26.490 21.323 1.00 33.70 ? ? ? ? ? ? 1928 THR A C 1 +ATOM 580 O O . THR A 1 73 ? 28.206 27.518 21.432 1.00 32.64 ? ? ? ? ? ? 1928 THR A O 1 +ATOM 581 C CB . THR A 1 73 ? 30.384 26.548 19.317 1.00 30.44 ? ? ? ? ? ? 1928 THR A CB 1 +ATOM 582 O OG1 . THR A 1 73 ? 29.892 25.298 18.816 1.00 37.12 ? ? ? ? ? ? 1928 THR A OG1 1 +ATOM 583 C CG2 . THR A 1 73 ? 31.808 26.752 18.857 1.00 31.73 ? ? ? ? ? ? 1928 THR A CG2 1 +ATOM 584 N N . PHE A 1 74 ? 28.378 25.285 21.603 1.00 30.48 ? ? ? ? ? ? 1929 PHE A N 1 +ATOM 585 C CA . PHE A 1 74 ? 27.052 25.116 22.203 1.00 29.85 ? ? ? ? ? ? 1929 PHE A CA 1 +ATOM 586 C C . PHE A 1 74 ? 26.994 25.742 23.606 1.00 35.95 ? ? ? ? ? ? 1929 PHE A C 1 +ATOM 587 O O . PHE A 1 74 ? 26.075 26.511 23.937 1.00 30.77 ? ? ? ? ? ? 1929 PHE A O 1 +ATOM 588 C CB . PHE A 1 74 ? 26.688 23.621 22.265 1.00 32.02 ? ? ? ? ? ? 1929 PHE A CB 1 +ATOM 589 C CG . PHE A 1 74 ? 25.453 23.323 23.078 1.00 28.04 ? ? ? ? ? ? 1929 PHE A CG 1 +ATOM 590 C CD1 . PHE A 1 74 ? 24.185 23.520 22.541 1.00 28.81 ? ? ? ? ? ? 1929 PHE A CD1 1 +ATOM 591 C CD2 . PHE A 1 74 ? 25.557 22.827 24.376 1.00 24.98 ? ? ? ? ? ? 1929 PHE A CD2 1 +ATOM 592 C CE1 . PHE A 1 74 ? 23.043 23.240 23.284 1.00 26.80 ? ? ? ? ? ? 1929 PHE A CE1 1 +ATOM 593 C CE2 . PHE A 1 74 ? 24.417 22.552 25.128 1.00 28.74 ? ? ? ? ? ? 1929 PHE A CE2 1 +ATOM 594 C CZ . PHE A 1 74 ? 23.161 22.754 24.580 1.00 30.78 ? ? ? ? ? ? 1929 PHE A CZ 1 +ATOM 595 N N . ALA A 1 75 ? 27.985 25.416 24.432 1.00 31.73 ? ? ? ? ? ? 1930 ALA A N 1 +ATOM 596 C CA . ALA A 1 75 ? 28.056 25.955 25.784 1.00 31.43 ? ? ? ? ? ? 1930 ALA A CA 1 +ATOM 597 C C . ALA A 1 75 ? 28.166 27.482 25.772 1.00 30.25 ? ? ? ? ? ? 1930 ALA A C 1 +ATOM 598 O O . ALA A 1 75 ? 27.612 28.159 26.642 1.00 31.91 ? ? ? ? ? ? 1930 ALA A O 1 +ATOM 599 C CB . ALA A 1 75 ? 29.230 25.350 26.533 1.00 31.56 ? ? ? ? ? ? 1930 ALA A CB 1 +ATOM 600 N N . LEU A 1 76 ? 28.887 28.019 24.796 1.00 34.82 ? ? ? ? ? ? 1931 LEU A N 1 +ATOM 601 C CA . LEU A 1 76 ? 29.039 29.467 24.685 1.00 35.94 ? ? ? ? ? ? 1931 LEU A CA 1 +ATOM 602 C C . LEU A 1 76 ? 27.695 30.170 24.500 1.00 35.82 ? ? ? ? ? ? 1931 LEU A C 1 +ATOM 603 O O . LEU A 1 76 ? 27.444 31.208 25.118 1.00 32.68 ? ? ? ? ? ? 1931 LEU A O 1 +ATOM 604 C CB . LEU A 1 76 ? 29.978 29.824 23.535 1.00 41.45 ? ? ? ? ? ? 1931 LEU A CB 1 +ATOM 605 C CG . LEU A 1 76 ? 31.462 29.590 23.818 1.00 53.37 ? ? ? ? ? ? 1931 LEU A CG 1 +ATOM 606 C CD1 . LEU A 1 76 ? 32.308 29.881 22.586 1.00 57.14 ? ? ? ? ? ? 1931 LEU A CD1 1 +ATOM 607 C CD2 . LEU A 1 76 ? 31.915 30.436 24.997 1.00 60.29 ? ? ? ? ? ? 1931 LEU A CD2 1 +ATOM 608 N N . ASP A 1 77 ? 26.839 29.614 23.647 1.00 31.25 ? ? ? ? ? ? 1932 ASP A N 1 +ATOM 609 C CA . ASP A 1 77 ? 25.517 30.203 23.423 1.00 32.01 ? ? ? ? ? ? 1932 ASP A CA 1 +ATOM 610 C C . ASP A 1 77 ? 24.640 30.072 24.670 1.00 28.29 ? ? ? ? ? ? 1932 ASP A C 1 +ATOM 611 O O . ASP A 1 77 ? 23.914 31.002 25.032 1.00 27.78 ? ? ? ? ? ? 1932 ASP A O 1 +ATOM 612 C CB . ASP A 1 77 ? 24.827 29.556 22.215 1.00 30.42 ? ? ? ? ? ? 1932 ASP A CB 1 +ATOM 613 C CG . ASP A 1 77 ? 25.064 30.328 20.924 1.00 32.46 ? ? ? ? ? ? 1932 ASP A CG 1 +ATOM 614 O OD1 . ASP A 1 77 ? 25.721 31.397 20.973 1.00 38.41 ? ? ? ? ? ? 1932 ASP A OD1 1 +ATOM 615 O OD2 . ASP A 1 77 ? 24.573 29.882 19.862 1.00 32.64 ? ? ? ? ? ? 1932 ASP A OD2 1 +ATOM 616 N N . VAL A 1 78 ? 24.706 28.921 25.333 1.00 26.03 ? ? ? ? ? ? 1933 VAL A N 1 +ATOM 617 C CA . VAL A 1 78 ? 23.919 28.735 26.541 1.00 25.19 ? ? ? ? ? ? 1933 VAL A CA 1 +ATOM 618 C C . VAL A 1 78 ? 24.327 29.778 27.596 1.00 28.73 ? ? ? ? ? ? 1933 VAL A C 1 +ATOM 619 O O . VAL A 1 78 ? 23.479 30.393 28.248 1.00 29.59 ? ? ? ? ? ? 1933 VAL A O 1 +ATOM 620 C CB . VAL A 1 78 ? 24.076 27.309 27.118 1.00 25.85 ? ? ? ? ? ? 1933 VAL A CB 1 +ATOM 621 C CG1 . VAL A 1 78 ? 23.425 27.208 28.497 1.00 28.07 ? ? ? ? ? ? 1933 VAL A CG1 1 +ATOM 622 C CG2 . VAL A 1 78 ? 23.477 26.268 26.154 1.00 25.40 ? ? ? ? ? ? 1933 VAL A CG2 1 +ATOM 623 N N . ARG A 1 79 ? 25.629 29.982 27.754 1.00 28.03 ? ? ? ? ? ? 1934 ARG A N 1 +ATOM 624 C CA . ARG A 1 79 ? 26.113 30.895 28.785 1.00 27.43 ? ? ? ? ? ? 1934 ARG A CA 1 +ATOM 625 C C . ARG A 1 79 ? 25.792 32.332 28.400 1.00 30.65 ? ? ? ? ? ? 1934 ARG A C 1 +ATOM 626 O O . ARG A 1 79 ? 25.539 33.181 29.265 1.00 30.65 ? ? ? ? ? ? 1934 ARG A O 1 +ATOM 627 C CB . ARG A 1 79 ? 27.614 30.708 29.006 1.00 27.29 ? ? ? ? ? ? 1934 ARG A CB 1 +ATOM 628 C CG . ARG A 1 79 ? 27.941 29.384 29.669 1.00 33.20 ? ? ? ? ? ? 1934 ARG A CG 1 +ATOM 629 C CD . ARG A 1 79 ? 29.412 29.028 29.597 1.00 34.94 ? ? ? ? ? ? 1934 ARG A CD 1 +ATOM 630 N NE . ARG A 1 79 ? 29.644 27.736 30.235 1.00 38.04 ? ? ? ? ? ? 1934 ARG A NE 1 +ATOM 631 C CZ . ARG A 1 79 ? 30.617 26.893 29.905 1.00 42.83 ? ? ? ? ? ? 1934 ARG A CZ 1 +ATOM 632 N NH1 . ARG A 1 79 ? 31.468 27.197 28.933 1.00 38.09 ? ? ? ? ? ? 1934 ARG A NH1 1 +ATOM 633 N NH2 . ARG A 1 79 ? 30.735 25.740 30.552 1.00 42.69 ? ? ? ? ? ? 1934 ARG A NH2 1 +ATOM 634 N N . LEU A 1 80 ? 25.786 32.588 27.096 1.00 26.99 ? ? ? ? ? ? 1935 LEU A N 1 +ATOM 635 C CA . LEU A 1 80 ? 25.410 33.889 26.561 1.00 29.07 ? ? ? ? ? ? 1935 LEU A CA 1 +ATOM 636 C C . LEU A 1 80 ? 23.992 34.253 26.989 1.00 32.51 ? ? ? ? ? ? 1935 LEU A C 1 +ATOM 637 O O . LEU A 1 80 ? 23.719 35.411 27.317 1.00 27.66 ? ? ? ? ? ? 1935 LEU A O 1 +ATOM 638 C CB . LEU A 1 80 ? 25.530 33.892 25.028 1.00 28.32 ? ? ? ? ? ? 1935 LEU A CB 1 +ATOM 639 C CG . LEU A 1 80 ? 25.028 35.120 24.273 1.00 27.58 ? ? ? ? ? ? 1935 LEU A CG 1 +ATOM 640 C CD1 . LEU A 1 80 ? 25.833 36.375 24.639 1.00 30.42 ? ? ? ? ? ? 1935 LEU A CD1 1 +ATOM 641 C CD2 . LEU A 1 80 ? 25.068 34.867 22.757 1.00 27.70 ? ? ? ? ? ? 1935 LEU A CD2 1 +ATOM 642 N N . VAL A 1 81 ? 23.095 33.266 27.008 1.00 26.26 ? ? ? ? ? ? 1936 VAL A N 1 +ATOM 643 C CA . VAL A 1 81 ? 21.736 33.512 27.486 1.00 27.50 ? ? ? ? ? ? 1936 VAL A CA 1 +ATOM 644 C C . VAL A 1 81 ? 21.759 34.102 28.905 1.00 32.28 ? ? ? ? ? ? 1936 VAL A C 1 +ATOM 645 O O . VAL A 1 81 ? 21.052 35.067 29.211 1.00 27.70 ? ? ? ? ? ? 1936 VAL A O 1 +ATOM 646 C CB . VAL A 1 81 ? 20.885 32.224 27.497 1.00 28.63 ? ? ? ? ? ? 1936 VAL A CB 1 +ATOM 647 C CG1 . VAL A 1 81 ? 19.557 32.467 28.211 1.00 24.40 ? ? ? ? ? ? 1936 VAL A CG1 1 +ATOM 648 C CG2 . VAL A 1 81 ? 20.660 31.681 26.065 1.00 24.09 ? ? ? ? ? ? 1936 VAL A CG2 1 +ATOM 649 N N . PHE A 1 82 ? 22.587 33.533 29.774 1.00 27.41 ? ? ? ? ? ? 1937 PHE A N 1 +ATOM 650 C CA . PHE A 1 82 ? 22.579 33.975 31.170 1.00 26.33 ? ? ? ? ? ? 1937 PHE A CA 1 +ATOM 651 C C . PHE A 1 82 ? 23.418 35.227 31.406 1.00 29.45 ? ? ? ? ? ? 1937 PHE A C 1 +ATOM 652 O O . PHE A 1 82 ? 23.106 36.028 32.290 1.00 29.67 ? ? ? ? ? ? 1937 PHE A O 1 +ATOM 653 C CB . PHE A 1 82 ? 23.025 32.819 32.060 1.00 25.80 ? ? ? ? ? ? 1937 PHE A CB 1 +ATOM 654 C CG . PHE A 1 82 ? 22.212 31.597 31.840 1.00 30.27 ? ? ? ? ? ? 1937 PHE A CG 1 +ATOM 655 C CD1 . PHE A 1 82 ? 20.830 31.686 31.834 1.00 28.31 ? ? ? ? ? ? 1937 PHE A CD1 1 +ATOM 656 C CD2 . PHE A 1 82 ? 22.806 30.386 31.555 1.00 30.22 ? ? ? ? ? ? 1937 PHE A CD2 1 +ATOM 657 C CE1 . PHE A 1 82 ? 20.059 30.577 31.586 1.00 31.20 ? ? ? ? ? ? 1937 PHE A CE1 1 +ATOM 658 C CE2 . PHE A 1 82 ? 22.031 29.260 31.311 1.00 35.06 ? ? ? ? ? ? 1937 PHE A CE2 1 +ATOM 659 C CZ . PHE A 1 82 ? 20.657 29.367 31.319 1.00 32.47 ? ? ? ? ? ? 1937 PHE A CZ 1 +ATOM 660 N N . ASP A 1 83 ? 24.467 35.402 30.611 1.00 29.08 ? ? ? ? ? ? 1938 ASP A N 1 +ATOM 661 C CA . ASP A 1 83 ? 25.234 36.642 30.618 1.00 32.04 ? ? ? ? ? ? 1938 ASP A CA 1 +ATOM 662 C C . ASP A 1 83 ? 24.380 37.831 30.187 1.00 34.86 ? ? ? ? ? ? 1938 ASP A C 1 +ATOM 663 O O . ASP A 1 83 ? 24.466 38.909 30.780 1.00 29.17 ? ? ? ? ? ? 1938 ASP A O 1 +ATOM 664 C CB . ASP A 1 83 ? 26.452 36.528 29.706 1.00 32.61 ? ? ? ? ? ? 1938 ASP A CB 1 +ATOM 665 C CG . ASP A 1 83 ? 27.500 35.589 30.256 1.00 38.89 ? ? ? ? ? ? 1938 ASP A CG 1 +ATOM 666 O OD1 . ASP A 1 83 ? 27.415 35.232 31.456 1.00 32.48 ? ? ? ? ? ? 1938 ASP A OD1 1 +ATOM 667 O OD2 . ASP A 1 83 ? 28.418 35.218 29.494 1.00 35.36 ? ? ? ? ? ? 1938 ASP A OD2 1 +ATOM 668 N N . ASN A 1 84 ? 23.574 37.640 29.145 1.00 30.48 ? ? ? ? ? ? 1939 ASN A N 1 +ATOM 669 C CA . ASN A 1 84 ? 22.634 38.674 28.723 1.00 33.26 ? ? ? ? ? ? 1939 ASN A CA 1 +ATOM 670 C C . ASN A 1 84 ? 21.654 38.984 29.840 1.00 32.30 ? ? ? ? ? ? 1939 ASN A C 1 +ATOM 671 O O . ASN A 1 84 ? 21.332 40.146 30.095 1.00 30.36 ? ? ? ? ? ? 1939 ASN A O 1 +ATOM 672 C CB . ASN A 1 84 ? 21.857 38.255 27.472 1.00 25.18 ? ? ? ? ? ? 1939 ASN A CB 1 +ATOM 673 C CG . ASN A 1 84 ? 22.709 38.251 26.215 1.00 29.97 ? ? ? ? ? ? 1939 ASN A CG 1 +ATOM 674 O OD1 . ASN A 1 84 ? 23.794 38.836 26.176 1.00 28.27 ? ? ? ? ? ? 1939 ASN A OD1 1 +ATOM 675 N ND2 . ASN A 1 84 ? 22.198 37.612 25.159 1.00 26.96 ? ? ? ? ? ? 1939 ASN A ND2 1 +ATOM 676 N N . CYS A 1 85 ? 21.179 37.932 30.501 1.00 31.32 ? ? ? ? ? ? 1940 CYS A N 1 +ATOM 677 C CA . CYS A 1 85 ? 20.194 38.085 31.560 1.00 29.13 ? ? ? ? ? ? 1940 CYS A CA 1 +ATOM 678 C C . CYS A 1 85 ? 20.763 38.940 32.694 1.00 31.24 ? ? ? ? ? ? 1940 CYS A C 1 +ATOM 679 O O . CYS A 1 85 ? 20.077 39.811 33.227 1.00 31.83 ? ? ? ? ? ? 1940 CYS A O 1 +ATOM 680 C CB . CYS A 1 85 ? 19.749 36.707 32.085 1.00 28.82 ? ? ? ? ? ? 1940 CYS A CB 1 +ATOM 681 S SG . CYS A 1 85 ? 18.470 36.758 33.375 1.00 29.95 ? ? ? ? ? ? 1940 CYS A SG 1 +ATOM 682 N N . GLU A 1 86 ? 22.023 38.697 33.051 1.00 28.43 ? ? ? ? ? ? 1941 GLU A N 1 +ATOM 683 C CA . GLU A 1 86 ? 22.669 39.493 34.090 1.00 31.75 ? ? ? ? ? ? 1941 GLU A CA 1 +ATOM 684 C C . GLU A 1 86 ? 22.862 40.940 33.655 1.00 34.58 ? ? ? ? ? ? 1941 GLU A C 1 +ATOM 685 O O . GLU A 1 86 ? 22.776 41.856 34.470 1.00 31.05 ? ? ? ? ? ? 1941 GLU A O 1 +ATOM 686 C CB . GLU A 1 86 ? 24.024 38.904 34.476 1.00 36.13 ? ? ? ? ? ? 1941 GLU A CB 1 +ATOM 687 C CG . GLU A 1 86 ? 23.948 37.594 35.232 1.00 35.39 ? ? ? ? ? ? 1941 GLU A CG 1 +ATOM 688 C CD . GLU A 1 86 ? 25.213 37.326 36.023 1.00 38.45 ? ? ? ? ? ? 1941 GLU A CD 1 +ATOM 689 O OE1 . GLU A 1 86 ? 25.676 38.250 36.725 1.00 39.90 ? ? ? ? ? ? 1941 GLU A OE1 1 +ATOM 690 O OE2 . GLU A 1 86 ? 25.743 36.198 35.947 1.00 43.60 ? ? ? ? ? ? 1941 GLU A OE2 1 +ATOM 691 N N . THR A 1 87 ? 23.148 41.144 32.376 1.00 31.32 ? ? ? ? ? ? 1942 THR A N 1 +ATOM 692 C CA . THR A 1 87 ? 23.340 42.498 31.854 1.00 28.96 ? ? ? ? ? ? 1942 THR A CA 1 +ATOM 693 C C . THR A 1 87 ? 22.060 43.335 31.958 1.00 32.76 ? ? ? ? ? ? 1942 THR A C 1 +ATOM 694 O O . THR A 1 87 ? 22.109 44.534 32.235 1.00 30.32 ? ? ? ? ? ? 1942 THR A O 1 +ATOM 695 C CB . THR A 1 87 ? 23.816 42.460 30.385 1.00 28.57 ? ? ? ? ? ? 1942 THR A CB 1 +ATOM 696 O OG1 . THR A 1 87 ? 25.111 41.849 30.326 1.00 32.82 ? ? ? ? ? ? 1942 THR A OG1 1 +ATOM 697 C CG2 . THR A 1 87 ? 23.904 43.872 29.800 1.00 30.17 ? ? ? ? ? ? 1942 THR A CG2 1 +ATOM 698 N N . PHE A 1 88 ? 20.914 42.692 31.755 1.00 29.35 ? ? ? ? ? ? 1943 PHE A N 1 +ATOM 699 C CA . PHE A 1 88 ? 19.650 43.410 31.635 1.00 34.04 ? ? ? ? ? ? 1943 PHE A CA 1 +ATOM 700 C C . PHE A 1 88 ? 18.744 43.304 32.858 1.00 34.49 ? ? ? ? ? ? 1943 PHE A C 1 +ATOM 701 O O . PHE A 1 88 ? 17.689 43.949 32.896 1.00 35.90 ? ? ? ? ? ? 1943 PHE A O 1 +ATOM 702 C CB . PHE A 1 88 ? 18.888 42.912 30.401 1.00 29.33 ? ? ? ? ? ? 1943 PHE A CB 1 +ATOM 703 C CG . PHE A 1 88 ? 17.982 43.944 29.782 1.00 32.47 ? ? ? ? ? ? 1943 PHE A CG 1 +ATOM 704 C CD1 . PHE A 1 88 ? 18.507 44.976 29.017 1.00 31.42 ? ? ? ? ? ? 1943 PHE A CD1 1 +ATOM 705 C CD2 . PHE A 1 88 ? 16.609 43.874 29.952 1.00 29.77 ? ? ? ? ? ? 1943 PHE A CD2 1 +ATOM 706 C CE1 . PHE A 1 88 ? 17.679 45.928 28.434 1.00 36.08 ? ? ? ? ? ? 1943 PHE A CE1 1 +ATOM 707 C CE2 . PHE A 1 88 ? 15.778 44.822 29.377 1.00 31.01 ? ? ? ? ? ? 1943 PHE A CE2 1 +ATOM 708 C CZ . PHE A 1 88 ? 16.314 45.852 28.617 1.00 37.00 ? ? ? ? ? ? 1943 PHE A CZ 1 +ATOM 709 N N . ASN A 1 89 ? 19.137 42.505 33.854 1.00 28.83 ? ? ? ? ? ? 1944 ASN A N 1 +ATOM 710 C CA . ASN A 1 89 ? 18.284 42.300 35.022 1.00 30.73 ? ? ? ? ? ? 1944 ASN A CA 1 +ATOM 711 C C . ASN A 1 89 ? 19.016 42.414 36.354 1.00 32.65 ? ? ? ? ? ? 1944 ASN A C 1 +ATOM 712 O O . ASN A 1 89 ? 20.125 41.898 36.507 1.00 31.45 ? ? ? ? ? ? 1944 ASN A O 1 +ATOM 713 C CB . ASN A 1 89 ? 17.611 40.927 34.943 1.00 34.61 ? ? ? ? ? ? 1944 ASN A CB 1 +ATOM 714 C CG . ASN A 1 89 ? 16.723 40.785 33.727 1.00 32.63 ? ? ? ? ? ? 1944 ASN A CG 1 +ATOM 715 O OD1 . ASN A 1 89 ? 15.546 41.142 33.760 1.00 35.63 ? ? ? ? ? ? 1944 ASN A OD1 1 +ATOM 716 N ND2 . ASN A 1 89 ? 17.280 40.252 32.646 1.00 27.99 ? ? ? ? ? ? 1944 ASN A ND2 1 +ATOM 717 N N . GLU A 1 90 ? 18.386 43.090 37.313 1.00 32.24 ? ? ? ? ? ? 1945 GLU A N 1 +ATOM 718 C CA . GLU A 1 90 ? 18.886 43.108 38.677 1.00 33.29 ? ? ? ? ? ? 1945 GLU A CA 1 +ATOM 719 C C . GLU A 1 90 ? 18.905 41.679 39.231 1.00 32.47 ? ? ? ? ? ? 1945 GLU A C 1 +ATOM 720 O O . GLU A 1 90 ? 17.983 40.909 38.976 1.00 31.39 ? ? ? ? ? ? 1945 GLU A O 1 +ATOM 721 C CB A GLU A 1 90 ? 18.011 43.988 39.579 0.38 35.34 ? ? ? ? ? ? 1945 GLU A CB 1 +ATOM 722 C CB B GLU A 1 90 ? 18.042 44.036 39.556 0.62 35.37 ? ? ? ? ? ? 1945 GLU A CB 1 +ATOM 723 C CG A GLU A 1 90 ? 17.770 45.411 39.096 0.38 42.01 ? ? ? ? ? ? 1945 GLU A CG 1 +ATOM 724 C CG B GLU A 1 90 ? 18.309 45.531 39.315 0.62 37.27 ? ? ? ? ? ? 1945 GLU A CG 1 +ATOM 725 C CD A GLU A 1 90 ? 16.688 46.118 39.901 0.38 54.23 ? ? ? ? ? ? 1945 GLU A CD 1 +ATOM 726 C CD B GLU A 1 90 ? 19.695 45.965 39.774 0.62 40.34 ? ? ? ? ? ? 1945 GLU A CD 1 +ATOM 727 O OE1 A GLU A 1 90 ? 16.878 46.321 41.121 0.38 56.59 ? ? ? ? ? ? 1945 GLU A OE1 1 +ATOM 728 O OE1 B GLU A 1 90 ? 20.288 45.277 40.633 0.62 46.18 ? ? ? ? ? ? 1945 GLU A OE1 1 +ATOM 729 O OE2 A GLU A 1 90 ? 15.643 46.466 39.312 0.38 62.75 ? ? ? ? ? ? 1945 GLU A OE2 1 +ATOM 730 O OE2 B GLU A 1 90 ? 20.196 46.993 39.282 0.62 44.10 ? ? ? ? ? ? 1945 GLU A OE2 1 +ATOM 731 N N . ASP A 1 91 ? 19.954 41.340 39.975 1.00 35.86 ? ? ? ? ? ? 1946 ASP A N 1 +ATOM 732 C CA . ASP A 1 91 ? 20.018 40.057 40.675 1.00 36.39 ? ? ? ? ? ? 1946 ASP A CA 1 +ATOM 733 C C . ASP A 1 91 ? 18.778 39.863 41.539 1.00 42.48 ? ? ? ? ? ? 1946 ASP A C 1 +ATOM 734 O O . ASP A 1 91 ? 18.210 38.773 41.594 1.00 40.19 ? ? ? ? ? ? 1946 ASP A O 1 +ATOM 735 C CB . ASP A 1 91 ? 21.269 39.965 41.550 1.00 36.05 ? ? ? ? ? ? 1946 ASP A CB 1 +ATOM 736 C CG . ASP A 1 91 ? 22.543 39.886 40.746 1.00 42.27 ? ? ? ? ? ? 1946 ASP A CG 1 +ATOM 737 O OD1 . ASP A 1 91 ? 22.476 39.556 39.545 1.00 37.88 ? ? ? ? ? ? 1946 ASP A OD1 1 +ATOM 738 O OD2 . ASP A 1 91 ? 23.617 40.146 41.324 1.00 46.40 ? ? ? ? ? ? 1946 ASP A OD2 1 +ATOM 739 N N . ASP A 1 92 ? 18.365 40.934 42.211 1.00 38.15 ? ? ? ? ? ? 1947 ASP A N 1 +ATOM 740 C CA . ASP A 1 92 ? 17.180 40.900 43.061 1.00 43.91 ? ? ? ? ? ? 1947 ASP A CA 1 +ATOM 741 C C . ASP A 1 92 ? 15.919 41.183 42.245 1.00 39.14 ? ? ? ? ? ? 1947 ASP A C 1 +ATOM 742 O O . ASP A 1 92 ? 15.275 42.227 42.401 1.00 40.30 ? ? ? ? ? ? 1947 ASP A O 1 +ATOM 743 C CB . ASP A 1 92 ? 17.310 41.904 44.215 1.00 43.31 ? ? ? ? ? ? 1947 ASP A CB 1 +ATOM 744 C CG . ASP A 1 92 ? 16.215 41.745 45.255 1.00 52.31 ? ? ? ? ? ? 1947 ASP A CG 1 +ATOM 745 O OD1 . ASP A 1 92 ? 15.443 40.763 45.171 1.00 47.68 ? ? ? ? ? ? 1947 ASP A OD1 1 +ATOM 746 O OD2 . ASP A 1 92 ? 16.137 42.597 46.168 1.00 56.72 ? ? ? ? ? ? 1947 ASP A OD2 1 +ATOM 747 N N . SER A 1 93 ? 15.588 40.239 41.371 1.00 38.75 ? ? ? ? ? ? 1948 SER A N 1 +ATOM 748 C CA . SER A 1 93 ? 14.357 40.264 40.593 1.00 39.48 ? ? ? ? ? ? 1948 SER A CA 1 +ATOM 749 C C . SER A 1 93 ? 14.030 38.826 40.217 1.00 33.30 ? ? ? ? ? ? 1948 SER A C 1 +ATOM 750 O O . SER A 1 93 ? 14.900 37.955 40.303 1.00 35.25 ? ? ? ? ? ? 1948 SER A O 1 +ATOM 751 C CB . SER A 1 93 ? 14.493 41.151 39.343 1.00 38.54 ? ? ? ? ? ? 1948 SER A CB 1 +ATOM 752 O OG . SER A 1 93 ? 15.382 40.592 38.385 1.00 32.01 ? ? ? ? ? ? 1948 SER A OG 1 +ATOM 753 N N . ASP A 1 94 ? 12.791 38.561 39.811 1.00 35.44 ? ? ? ? ? ? 1949 ASP A N 1 +ATOM 754 C CA . ASP A 1 94 ? 12.407 37.194 39.422 1.00 33.10 ? ? ? ? ? ? 1949 ASP A CA 1 +ATOM 755 C C . ASP A 1 94 ? 13.248 36.653 38.260 1.00 33.47 ? ? ? ? ? ? 1949 ASP A C 1 +ATOM 756 O O . ASP A 1 94 ? 13.710 35.506 38.288 1.00 32.07 ? ? ? ? ? ? 1949 ASP A O 1 +ATOM 757 C CB . ASP A 1 94 ? 10.920 37.138 39.050 1.00 37.99 ? ? ? ? ? ? 1949 ASP A CB 1 +ATOM 758 C CG . ASP A 1 94 ? 10.005 37.337 40.253 1.00 48.36 ? ? ? ? ? ? 1949 ASP A CG 1 +ATOM 759 O OD1 . ASP A 1 94 ? 9.739 36.355 40.978 1.00 41.29 ? ? ? ? ? ? 1949 ASP A OD1 1 +ATOM 760 O OD2 . ASP A 1 94 ? 9.538 38.475 40.467 1.00 56.01 ? ? ? ? ? ? 1949 ASP A OD2 1 +ATOM 761 N N . ILE A 1 95 ? 13.445 37.481 37.241 1.00 30.24 ? ? ? ? ? ? 1950 ILE A N 1 +ATOM 762 C CA . ILE A 1 95 ? 14.180 37.055 36.048 1.00 30.04 ? ? ? ? ? ? 1950 ILE A CA 1 +ATOM 763 C C . ILE A 1 95 ? 15.668 36.953 36.371 1.00 32.86 ? ? ? ? ? ? 1950 ILE A C 1 +ATOM 764 O O . ILE A 1 95 ? 16.347 36.033 35.916 1.00 30.59 ? ? ? ? ? ? 1950 ILE A O 1 +ATOM 765 C CB . ILE A 1 95 ? 13.927 38.029 34.871 1.00 33.92 ? ? ? ? ? ? 1950 ILE A CB 1 +ATOM 766 C CG1 . ILE A 1 95 ? 12.476 37.904 34.411 1.00 33.14 ? ? ? ? ? ? 1950 ILE A CG1 1 +ATOM 767 C CG2 . ILE A 1 95 ? 14.886 37.780 33.705 1.00 35.56 ? ? ? ? ? ? 1950 ILE A CG2 1 +ATOM 768 C CD1 . ILE A 1 95 ? 12.095 38.915 33.365 1.00 36.92 ? ? ? ? ? ? 1950 ILE A CD1 1 +ATOM 769 N N . GLY A 1 96 ? 16.165 37.891 37.176 1.00 32.60 ? ? ? ? ? ? 1951 GLY A N 1 +ATOM 770 C CA . GLY A 1 96 ? 17.537 37.839 37.656 1.00 30.59 ? ? ? ? ? ? 1951 GLY A CA 1 +ATOM 771 C C . GLY A 1 96 ? 17.839 36.536 38.387 1.00 36.77 ? ? ? ? ? ? 1951 GLY A C 1 +ATOM 772 O O . GLY A 1 96 ? 18.833 35.861 38.109 1.00 33.48 ? ? ? ? ? ? 1951 GLY A O 1 +ATOM 773 N N . ARG A 1 97 ? 16.970 36.171 39.320 1.00 32.93 ? ? ? ? ? ? 1952 ARG A N 1 +ATOM 774 C CA . ARG A 1 97 ? 17.131 34.922 40.052 1.00 34.35 ? ? ? ? ? ? 1952 ARG A CA 1 +ATOM 775 C C . ARG A 1 97 ? 17.006 33.712 39.120 1.00 31.54 ? ? ? ? ? ? 1952 ARG A C 1 +ATOM 776 O O . ARG A 1 97 ? 17.763 32.749 39.248 1.00 33.69 ? ? ? ? ? ? 1952 ARG A O 1 +ATOM 777 C CB . ARG A 1 97 ? 16.112 34.837 41.185 1.00 33.09 ? ? ? ? ? ? 1952 ARG A CB 1 +ATOM 778 C CG . ARG A 1 97 ? 16.488 35.691 42.396 1.00 41.69 ? ? ? ? ? ? 1952 ARG A CG 1 +ATOM 779 C CD . ARG A 1 97 ? 15.514 35.495 43.543 1.00 42.50 ? ? ? ? ? ? 1952 ARG A CD 1 +ATOM 780 N NE . ARG A 1 97 ? 14.232 36.143 43.284 1.00 40.68 ? ? ? ? ? ? 1952 ARG A NE 1 +ATOM 781 C CZ . ARG A 1 97 ? 13.961 37.411 43.575 1.00 44.47 ? ? ? ? ? ? 1952 ARG A CZ 1 +ATOM 782 N NH1 . ARG A 1 97 ? 14.885 38.184 44.134 1.00 45.51 ? ? ? ? ? ? 1952 ARG A NH1 1 +ATOM 783 N NH2 . ARG A 1 97 ? 12.762 37.903 43.307 1.00 51.23 ? ? ? ? ? ? 1952 ARG A NH2 1 +ATOM 784 N N . ALA A 1 98 ? 16.050 33.766 38.198 1.00 29.50 ? ? ? ? ? ? 1953 ALA A N 1 +ATOM 785 C CA . ALA A 1 98 ? 15.882 32.690 37.213 1.00 32.25 ? ? ? ? ? ? 1953 ALA A CA 1 +ATOM 786 C C . ALA A 1 98 ? 17.183 32.411 36.472 1.00 29.92 ? ? ? ? ? ? 1953 ALA A C 1 +ATOM 787 O O . ALA A 1 98 ? 17.586 31.248 36.300 1.00 29.24 ? ? ? ? ? ? 1953 ALA A O 1 +ATOM 788 C CB . ALA A 1 98 ? 14.781 33.040 36.220 1.00 29.72 ? ? ? ? ? ? 1953 ALA A CB 1 +ATOM 789 N N . GLY A 1 99 ? 17.839 33.482 36.029 1.00 30.97 ? ? ? ? ? ? 1954 GLY A N 1 +ATOM 790 C CA . GLY A 1 99 ? 19.076 33.351 35.278 1.00 28.98 ? ? ? ? ? ? 1954 GLY A CA 1 +ATOM 791 C C . GLY A 1 99 ? 20.159 32.670 36.087 1.00 30.72 ? ? ? ? ? ? 1954 GLY A C 1 +ATOM 792 O O . GLY A 1 99 ? 20.821 31.744 35.612 1.00 29.33 ? ? ? ? ? ? 1954 GLY A O 1 +ATOM 793 N N . HIS A 1 100 ? 20.339 33.125 37.321 1.00 31.19 ? ? ? ? ? ? 1955 HIS A N 1 +ATOM 794 C CA . HIS A 1 100 ? 21.316 32.505 38.198 1.00 31.81 ? ? ? ? ? ? 1955 HIS A CA 1 +ATOM 795 C C . HIS A 1 100 ? 20.991 31.031 38.433 1.00 33.17 ? ? ? ? ? ? 1955 HIS A C 1 +ATOM 796 O O . HIS A 1 100 ? 21.888 30.188 38.375 1.00 35.31 ? ? ? ? ? ? 1955 HIS A O 1 +ATOM 797 C CB . HIS A 1 100 ? 21.399 33.264 39.529 1.00 35.90 ? ? ? ? ? ? 1955 HIS A CB 1 +ATOM 798 C CG . HIS A 1 100 ? 22.066 34.600 39.410 1.00 40.36 ? ? ? ? ? ? 1955 HIS A CG 1 +ATOM 799 N ND1 . HIS A 1 100 ? 23.424 34.739 39.225 1.00 40.84 ? ? ? ? ? ? 1955 HIS A ND1 1 +ATOM 800 C CD2 . HIS A 1 100 ? 21.559 35.856 39.439 1.00 38.62 ? ? ? ? ? ? 1955 HIS A CD2 1 +ATOM 801 C CE1 . HIS A 1 100 ? 23.726 36.025 39.146 1.00 39.21 ? ? ? ? ? ? 1955 HIS A CE1 1 +ATOM 802 N NE2 . HIS A 1 100 ? 22.613 36.722 39.273 1.00 36.18 ? ? ? ? ? ? 1955 HIS A NE2 1 +ATOM 803 N N . ASN A 1 101 ? 19.722 30.719 38.694 1.00 32.99 ? ? ? ? ? ? 1956 ASN A N 1 +ATOM 804 C CA . ASN A 1 101 ? 19.299 29.326 38.903 1.00 34.70 ? ? ? ? ? ? 1956 ASN A CA 1 +ATOM 805 C C . ASN A 1 101 ? 19.578 28.459 37.676 1.00 34.43 ? ? ? ? ? ? 1956 ASN A C 1 +ATOM 806 O O . ASN A 1 101 ? 20.085 27.343 37.789 1.00 36.59 ? ? ? ? ? ? 1956 ASN A O 1 +ATOM 807 C CB . ASN A 1 101 ? 17.807 29.250 39.229 1.00 34.70 ? ? ? ? ? ? 1956 ASN A CB 1 +ATOM 808 C CG . ASN A 1 101 ? 17.483 29.711 40.637 1.00 40.79 ? ? ? ? ? ? 1956 ASN A CG 1 +ATOM 809 O OD1 . ASN A 1 101 ? 18.375 30.019 41.430 1.00 43.96 ? ? ? ? ? ? 1956 ASN A OD1 1 +ATOM 810 N ND2 . ASN A 1 101 ? 16.191 29.769 40.951 1.00 38.39 ? ? ? ? ? ? 1956 ASN A ND2 1 +ATOM 811 N N . MET A 1 102 ? 19.234 28.985 36.500 1.00 28.43 ? ? ? ? ? ? 1957 MET A N 1 +ATOM 812 C CA . MET A 1 102 ? 19.356 28.207 35.265 1.00 28.51 ? ? ? ? ? ? 1957 MET A CA 1 +ATOM 813 C C . MET A 1 102 ? 20.816 28.021 34.891 1.00 32.93 ? ? ? ? ? ? 1957 MET A C 1 +ATOM 814 O O . MET A 1 102 ? 21.192 26.987 34.350 1.00 30.25 ? ? ? ? ? ? 1957 MET A O 1 +ATOM 815 C CB . MET A 1 102 ? 18.604 28.871 34.114 1.00 27.47 ? ? ? ? ? ? 1957 MET A CB 1 +ATOM 816 C CG . MET A 1 102 ? 17.097 28.897 34.268 1.00 39.52 ? ? ? ? ? ? 1957 MET A CG 1 +ATOM 817 S SD . MET A 1 102 ? 16.345 27.268 34.380 1.00 49.64 ? ? ? ? ? ? 1957 MET A SD 1 +ATOM 818 C CE . MET A 1 102 ? 16.875 26.538 32.833 1.00 45.28 ? ? ? ? ? ? 1957 MET A CE 1 +ATOM 819 N N . ARG A 1 103 ? 21.646 29.016 35.189 1.00 29.70 ? ? ? ? ? ? 1958 ARG A N 1 +ATOM 820 C CA . ARG A 1 103 ? 23.072 28.885 34.919 1.00 32.76 ? ? ? ? ? ? 1958 ARG A CA 1 +ATOM 821 C C . ARG A 1 103 ? 23.687 27.764 35.757 1.00 32.90 ? ? ? ? ? ? 1958 ARG A C 1 +ATOM 822 O O . ARG A 1 103 ? 24.428 26.919 35.246 1.00 33.36 ? ? ? ? ? ? 1958 ARG A O 1 +ATOM 823 C CB . ARG A 1 103 ? 23.808 30.197 35.193 1.00 31.20 ? ? ? ? ? ? 1958 ARG A CB 1 +ATOM 824 C CG . ARG A 1 103 ? 25.253 30.163 34.725 1.00 32.68 ? ? ? ? ? ? 1958 ARG A CG 1 +ATOM 825 C CD . ARG A 1 103 ? 26.096 31.232 35.384 1.00 31.57 ? ? ? ? ? ? 1958 ARG A CD 1 +ATOM 826 N NE . ARG A 1 103 ? 25.736 32.575 34.924 1.00 31.75 ? ? ? ? ? ? 1958 ARG A NE 1 +ATOM 827 C CZ . ARG A 1 103 ? 26.204 33.146 33.817 1.00 35.48 ? ? ? ? ? ? 1958 ARG A CZ 1 +ATOM 828 N NH1 . ARG A 1 103 ? 27.050 32.489 33.024 1.00 32.53 ? ? ? ? ? ? 1958 ARG A NH1 1 +ATOM 829 N NH2 . ARG A 1 103 ? 25.819 34.378 33.499 1.00 30.07 ? ? ? ? ? ? 1958 ARG A NH2 1 +ATOM 830 N N . LYS A 1 104 ? 23.374 27.766 37.048 1.00 32.49 ? ? ? ? ? ? 1959 LYS A N 1 +ATOM 831 C CA . LYS A 1 104 ? 23.852 26.728 37.954 1.00 32.19 ? ? ? ? ? ? 1959 LYS A CA 1 +ATOM 832 C C . LYS A 1 104 ? 23.352 25.369 37.481 1.00 35.33 ? ? ? ? ? ? 1959 LYS A C 1 +ATOM 833 O O . LYS A 1 104 ? 24.099 24.389 37.459 1.00 36.31 ? ? ? ? ? ? 1959 LYS A O 1 +ATOM 834 C CB . LYS A 1 104 ? 23.385 27.010 39.384 1.00 33.87 ? ? ? ? ? ? 1959 LYS A CB 1 +ATOM 835 C CG . LYS A 1 104 ? 23.866 25.994 40.405 1.00 43.97 ? ? ? ? ? ? 1959 LYS A CG 1 +ATOM 836 C CD . LYS A 1 104 ? 25.302 26.262 40.817 1.00 51.40 ? ? ? ? ? ? 1959 LYS A CD 1 +ATOM 837 N N . TYR A 1 105 ? 22.082 25.329 37.093 1.00 32.80 ? ? ? ? ? ? 1960 TYR A N 1 +ATOM 838 C CA . TYR A 1 105 ? 21.460 24.112 36.601 1.00 36.37 ? ? ? ? ? ? 1960 TYR A CA 1 +ATOM 839 C C . TYR A 1 105 ? 22.227 23.581 35.389 1.00 37.71 ? ? ? ? ? ? 1960 TYR A C 1 +ATOM 840 O O . TYR A 1 105 ? 22.574 22.398 35.340 1.00 33.30 ? ? ? ? ? ? 1960 TYR A O 1 +ATOM 841 C CB . TYR A 1 105 ? 19.992 24.369 36.251 1.00 30.23 ? ? ? ? ? ? 1960 TYR A CB 1 +ATOM 842 C CG . TYR A 1 105 ? 19.191 23.115 35.960 1.00 40.26 ? ? ? ? ? ? 1960 TYR A CG 1 +ATOM 843 C CD1 . TYR A 1 105 ? 18.833 22.234 36.984 1.00 41.13 ? ? ? ? ? ? 1960 TYR A CD1 1 +ATOM 844 C CD2 . TYR A 1 105 ? 18.783 22.816 34.664 1.00 33.74 ? ? ? ? ? ? 1960 TYR A CD2 1 +ATOM 845 C CE1 . TYR A 1 105 ? 18.095 21.083 36.716 1.00 41.13 ? ? ? ? ? ? 1960 TYR A CE1 1 +ATOM 846 C CE2 . TYR A 1 105 ? 18.042 21.678 34.393 1.00 33.48 ? ? ? ? ? ? 1960 TYR A CE2 1 +ATOM 847 C CZ . TYR A 1 105 ? 17.705 20.817 35.416 1.00 36.28 ? ? ? ? ? ? 1960 TYR A CZ 1 +ATOM 848 O OH . TYR A 1 105 ? 16.972 19.687 35.128 1.00 45.03 ? ? ? ? ? ? 1960 TYR A OH 1 +ATOM 849 N N . PHE A 1 106 ? 22.513 24.465 34.437 1.00 31.27 ? ? ? ? ? ? 1961 PHE A N 1 +ATOM 850 C CA . PHE A 1 106 ? 23.262 24.083 33.235 1.00 31.21 ? ? ? ? ? ? 1961 PHE A CA 1 +ATOM 851 C C . PHE A 1 106 ? 24.652 23.563 33.541 1.00 32.40 ? ? ? ? ? ? 1961 PHE A C 1 +ATOM 852 O O . PHE A 1 106 ? 25.042 22.504 33.063 1.00 32.91 ? ? ? ? ? ? 1961 PHE A O 1 +ATOM 853 C CB . PHE A 1 106 ? 23.419 25.254 32.274 1.00 28.14 ? ? ? ? ? ? 1961 PHE A CB 1 +ATOM 854 C CG . PHE A 1 106 ? 24.362 24.954 31.127 1.00 30.53 ? ? ? ? ? ? 1961 PHE A CG 1 +ATOM 855 C CD1 . PHE A 1 106 ? 23.998 24.060 30.134 1.00 30.88 ? ? ? ? ? ? 1961 PHE A CD1 1 +ATOM 856 C CD2 . PHE A 1 106 ? 25.617 25.546 31.060 1.00 32.26 ? ? ? ? ? ? 1961 PHE A CD2 1 +ATOM 857 C CE1 . PHE A 1 106 ? 24.857 23.772 29.081 1.00 29.70 ? ? ? ? ? ? 1961 PHE A CE1 1 +ATOM 858 C CE2 . PHE A 1 106 ? 26.484 25.258 30.005 1.00 32.55 ? ? ? ? ? ? 1961 PHE A CE2 1 +ATOM 859 C CZ . PHE A 1 106 ? 26.105 24.372 29.023 1.00 28.34 ? ? ? ? ? ? 1961 PHE A CZ 1 +ATOM 860 N N . GLU A 1 107 ? 25.406 24.328 34.324 1.00 33.72 ? ? ? ? ? ? 1962 GLU A N 1 +ATOM 861 C CA . GLU A 1 107 ? 26.809 24.010 34.550 1.00 37.64 ? ? ? ? ? ? 1962 GLU A CA 1 +ATOM 862 C C . GLU A 1 107 ? 26.988 22.655 35.226 1.00 39.50 ? ? ? ? ? ? 1962 GLU A C 1 +ATOM 863 O O . GLU A 1 107 ? 27.959 21.952 34.954 1.00 36.63 ? ? ? ? ? ? 1962 GLU A O 1 +ATOM 864 C CB . GLU A 1 107 ? 27.486 25.111 35.371 1.00 39.16 ? ? ? ? ? ? 1962 GLU A CB 1 +ATOM 865 C CG . GLU A 1 107 ? 27.549 26.475 34.649 1.00 39.91 ? ? ? ? ? ? 1962 GLU A CG 1 +ATOM 866 C CD . GLU A 1 107 ? 28.307 26.437 33.316 1.00 47.97 ? ? ? ? ? ? 1962 GLU A CD 1 +ATOM 867 O OE1 . GLU A 1 107 ? 29.002 25.435 33.020 1.00 42.54 ? ? ? ? ? ? 1962 GLU A OE1 1 +ATOM 868 O OE2 . GLU A 1 107 ? 28.208 27.428 32.558 1.00 37.48 ? ? ? ? ? ? 1962 GLU A OE2 1 +ATOM 869 N N . LYS A 1 108 ? 26.050 22.276 36.088 1.00 37.04 ? ? ? ? ? ? 1963 LYS A N 1 +ATOM 870 C CA . LYS A 1 108 ? 26.137 20.954 36.716 1.00 41.72 ? ? ? ? ? ? 1963 LYS A CA 1 +ATOM 871 C C . LYS A 1 108 ? 25.835 19.846 35.711 1.00 40.43 ? ? ? ? ? ? 1963 LYS A C 1 +ATOM 872 O O . LYS A 1 108 ? 26.542 18.836 35.675 1.00 42.16 ? ? ? ? ? ? 1963 LYS A O 1 +ATOM 873 C CB . LYS A 1 108 ? 25.191 20.833 37.909 1.00 40.30 ? ? ? ? ? ? 1963 LYS A CB 1 +ATOM 874 C CG . LYS A 1 108 ? 25.520 19.621 38.793 1.00 50.69 ? ? ? ? ? ? 1963 LYS A CG 1 +ATOM 875 C CD . LYS A 1 108 ? 24.282 19.018 39.423 1.00 58.23 ? ? ? ? ? ? 1963 LYS A CD 1 +ATOM 876 C CE . LYS A 1 108 ? 24.642 18.038 40.538 1.00 62.27 ? ? ? ? ? ? 1963 LYS A CE 1 +ATOM 877 N NZ . LYS A 1 108 ? 25.690 17.053 40.151 1.00 55.24 ? ? ? ? ? ? 1963 LYS A NZ 1 +ATOM 878 N N . LYS A 1 109 ? 24.778 20.027 34.918 1.00 36.41 ? ? ? ? ? ? 1964 LYS A N 1 +ATOM 879 C CA . LYS A 1 109 ? 24.452 19.070 33.856 1.00 38.89 ? ? ? ? ? ? 1964 LYS A CA 1 +ATOM 880 C C . LYS A 1 109 ? 25.639 18.936 32.918 1.00 36.92 ? ? ? ? ? ? 1964 LYS A C 1 +ATOM 881 O O . LYS A 1 109 ? 25.984 17.839 32.483 1.00 39.37 ? ? ? ? ? ? 1964 LYS A O 1 +ATOM 882 C CB . LYS A 1 109 ? 23.215 19.508 33.061 1.00 38.49 ? ? ? ? ? ? 1964 LYS A CB 1 +ATOM 883 C CG . LYS A 1 109 ? 21.915 19.561 33.850 1.00 47.19 ? ? ? ? ? ? 1964 LYS A CG 1 +ATOM 884 C CD . LYS A 1 109 ? 21.390 18.172 34.161 1.00 56.84 ? ? ? ? ? ? 1964 LYS A CD 1 +ATOM 885 C CE . LYS A 1 109 ? 20.048 18.232 34.877 1.00 57.29 ? ? ? ? ? ? 1964 LYS A CE 1 +ATOM 886 N N . TRP A 1 110 ? 26.267 20.068 32.617 1.00 35.24 ? ? ? ? ? ? 1965 TRP A N 1 +ATOM 887 C CA . TRP A 1 110 ? 27.410 20.094 31.715 1.00 36.43 ? ? ? ? ? ? 1965 TRP A CA 1 +ATOM 888 C C . TRP A 1 110 ? 28.555 19.268 32.286 1.00 41.14 ? ? ? ? ? ? 1965 TRP A C 1 +ATOM 889 O O . TRP A 1 110 ? 29.107 18.407 31.610 1.00 39.79 ? ? ? ? ? ? 1965 TRP A O 1 +ATOM 890 C CB . TRP A 1 110 ? 27.853 21.538 31.459 1.00 34.92 ? ? ? ? ? ? 1965 TRP A CB 1 +ATOM 891 C CG . TRP A 1 110 ? 28.814 21.688 30.316 1.00 34.06 ? ? ? ? ? ? 1965 TRP A CG 1 +ATOM 892 C CD1 . TRP A 1 110 ? 30.143 21.986 30.396 1.00 39.20 ? ? ? ? ? ? 1965 TRP A CD1 1 +ATOM 893 C CD2 . TRP A 1 110 ? 28.524 21.526 28.921 1.00 29.86 ? ? ? ? ? ? 1965 TRP A CD2 1 +ATOM 894 N NE1 . TRP A 1 110 ? 30.694 22.033 29.140 1.00 39.13 ? ? ? ? ? ? 1965 TRP A NE1 1 +ATOM 895 C CE2 . TRP A 1 110 ? 29.722 21.749 28.217 1.00 29.67 ? ? ? ? ? ? 1965 TRP A CE2 1 +ATOM 896 C CE3 . TRP A 1 110 ? 27.366 21.222 28.200 1.00 24.15 ? ? ? ? ? ? 1965 TRP A CE3 1 +ATOM 897 C CZ2 . TRP A 1 110 ? 29.797 21.679 26.824 1.00 27.82 ? ? ? ? ? ? 1965 TRP A CZ2 1 +ATOM 898 C CZ3 . TRP A 1 110 ? 27.443 21.156 26.814 1.00 28.78 ? ? ? ? ? ? 1965 TRP A CZ3 1 +ATOM 899 C CH2 . TRP A 1 110 ? 28.649 21.385 26.146 1.00 26.52 ? ? ? ? ? ? 1965 TRP A CH2 1 +ATOM 900 N N . THR A 1 111 ? 28.891 19.519 33.546 1.00 36.20 ? ? ? ? ? ? 1966 THR A N 1 +ATOM 901 C CA . THR A 1 111 ? 29.960 18.784 34.204 1.00 48.09 ? ? ? ? ? ? 1966 THR A CA 1 +ATOM 902 C C . THR A 1 111 ? 29.626 17.299 34.329 1.00 47.68 ? ? ? ? ? ? 1966 THR A C 1 +ATOM 903 O O . THR A 1 111 ? 30.461 16.443 34.032 1.00 52.24 ? ? ? ? ? ? 1966 THR A O 1 +ATOM 904 C CB . THR A 1 111 ? 30.254 19.363 35.599 1.00 51.62 ? ? ? ? ? ? 1966 THR A CB 1 +ATOM 905 O OG1 . THR A 1 111 ? 30.772 20.692 35.456 1.00 59.18 ? ? ? ? ? ? 1966 THR A OG1 1 +ATOM 906 C CG2 . THR A 1 111 ? 31.273 18.511 36.327 1.00 60.31 ? ? ? ? ? ? 1966 THR A CG2 1 +ATOM 907 N N . ASP A 1 112 ? 28.404 16.993 34.760 1.00 48.06 ? ? ? ? ? ? 1967 ASP A N 1 +ATOM 908 C CA . ASP A 1 112 ? 27.997 15.601 34.957 1.00 49.92 ? ? ? ? ? ? 1967 ASP A CA 1 +ATOM 909 C C . ASP A 1 112 ? 27.962 14.815 33.654 1.00 48.00 ? ? ? ? ? ? 1967 ASP A C 1 +ATOM 910 O O . ASP A 1 112 ? 28.092 13.594 33.655 1.00 50.67 ? ? ? ? ? ? 1967 ASP A O 1 +ATOM 911 C CB . ASP A 1 112 ? 26.623 15.528 35.618 1.00 50.79 ? ? ? ? ? ? 1967 ASP A CB 1 +ATOM 912 C CG . ASP A 1 112 ? 26.642 16.003 37.056 1.00 58.55 ? ? ? ? ? ? 1967 ASP A CG 1 +ATOM 913 O OD1 . ASP A 1 112 ? 27.745 16.187 37.615 1.00 55.68 ? ? ? ? ? ? 1967 ASP A OD1 1 +ATOM 914 O OD2 . ASP A 1 112 ? 25.548 16.185 37.626 1.00 54.57 ? ? ? ? ? ? 1967 ASP A OD2 1 +ATOM 915 N N . THR A 1 113 ? 27.772 15.514 32.541 1.00 44.16 ? ? ? ? ? ? 1968 THR A N 1 +ATOM 916 C CA . THR A 1 113 ? 27.627 14.831 31.264 1.00 42.40 ? ? ? ? ? ? 1968 THR A CA 1 +ATOM 917 C C . THR A 1 113 ? 28.976 14.606 30.593 1.00 43.79 ? ? ? ? ? ? 1968 THR A C 1 +ATOM 918 O O . THR A 1 113 ? 29.202 13.558 30.000 1.00 53.58 ? ? ? ? ? ? 1968 THR A O 1 +ATOM 919 C CB . THR A 1 113 ? 26.695 15.613 30.321 1.00 43.22 ? ? ? ? ? ? 1968 THR A CB 1 +ATOM 920 O OG1 . THR A 1 113 ? 25.412 15.759 30.945 1.00 39.24 ? ? ? ? ? ? 1968 THR A OG1 1 +ATOM 921 C CG2 . THR A 1 113 ? 26.532 14.884 28.984 1.00 39.18 ? ? ? ? ? ? 1968 THR A CG2 1 +ATOM 922 N N . PHE A 1 114 ? 29.887 15.566 30.708 1.00 54.37 ? ? ? ? ? ? 1969 PHE A N 1 +ATOM 923 C CA . PHE A 1 114 ? 31.148 15.467 29.980 1.00 58.67 ? ? ? ? ? ? 1969 PHE A CA 1 +ATOM 924 C C . PHE A 1 114 ? 32.385 15.400 30.880 1.00 71.55 ? ? ? ? ? ? 1969 PHE A C 1 +ATOM 925 O O . PHE A 1 114 ? 33.348 14.706 30.558 1.00 82.08 ? ? ? ? ? ? 1969 PHE A O 1 +ATOM 926 C CB . PHE A 1 114 ? 31.266 16.638 29.001 1.00 54.23 ? ? ? ? ? ? 1969 PHE A CB 1 +ATOM 927 C CG . PHE A 1 114 ? 30.148 16.694 27.995 1.00 45.53 ? ? ? ? ? ? 1969 PHE A CG 1 +ATOM 928 C CD1 . PHE A 1 114 ? 30.067 15.757 26.973 1.00 49.90 ? ? ? ? ? ? 1969 PHE A CD1 1 +ATOM 929 C CD2 . PHE A 1 114 ? 29.175 17.676 28.077 1.00 41.75 ? ? ? ? ? ? 1969 PHE A CD2 1 +ATOM 930 C CE1 . PHE A 1 114 ? 29.033 15.804 26.049 1.00 45.03 ? ? ? ? ? ? 1969 PHE A CE1 1 +ATOM 931 C CE2 . PHE A 1 114 ? 28.143 17.733 27.160 1.00 39.17 ? ? ? ? ? ? 1969 PHE A CE2 1 +ATOM 932 C CZ . PHE A 1 114 ? 28.068 16.800 26.145 1.00 40.53 ? ? ? ? ? ? 1969 PHE A CZ 1 +ATOM 933 N N . LYS A 1 115 ? 32.363 16.107 32.004 1.00 77.87 ? ? ? ? ? ? 1970 LYS A N 1 +ATOM 934 C CA . LYS A 1 115 ? 33.495 16.083 32.929 1.00 84.68 ? ? ? ? ? ? 1970 LYS A CA 1 +ATOM 935 C C . LYS A 1 115 ? 33.430 14.872 33.857 1.00 86.35 ? ? ? ? ? ? 1970 LYS A C 1 +ATOM 936 O O . LYS A 1 115 ? 33.662 13.738 33.432 1.00 87.69 ? ? ? ? ? ? 1970 LYS A O 1 +ATOM 937 C CB . LYS A 1 115 ? 33.549 17.374 33.750 1.00 80.81 ? ? ? ? ? ? 1970 LYS A CB 1 +HETATM 938 F F . ZYB B 2 . ? 13.101 41.429 28.043 1.00 57.66 ? ? ? ? ? ? 2971 ZYB A F 1 +HETATM 939 C C2 . ZYB B 2 . ? 12.706 41.725 29.252 1.00 56.97 ? ? ? ? ? ? 2971 ZYB A C2 1 +HETATM 940 C C1 . ZYB B 2 . ? 13.585 41.632 30.293 1.00 55.75 ? ? ? ? ? ? 2971 ZYB A C1 1 +HETATM 941 C C3 . ZYB B 2 . ? 11.420 42.125 29.483 1.00 52.80 ? ? ? ? ? ? 2971 ZYB A C3 1 +HETATM 942 C C4 . ZYB B 2 . ? 11.019 42.445 30.749 1.00 44.44 ? ? ? ? ? ? 2971 ZYB A C4 1 +HETATM 943 C C5 . ZYB B 2 . ? 11.884 42.352 31.805 1.00 44.59 ? ? ? ? ? ? 2971 ZYB A C5 1 +HETATM 944 C C . ZYB B 2 . ? 13.173 41.955 31.565 1.00 45.42 ? ? ? ? ? ? 2971 ZYB A C 1 +HETATM 945 C C6 . ZYB B 2 . ? 11.464 42.703 33.214 1.00 53.45 ? ? ? ? ? ? 2971 ZYB A C6 1 +HETATM 946 N N . ZYB B 2 . ? 12.323 43.272 34.165 1.00 56.95 ? ? ? ? ? ? 2971 ZYB A N 1 +HETATM 947 N N1 . ZYB B 2 . ? 10.288 42.524 33.655 1.00 62.80 ? ? ? ? ? ? 2971 ZYB A N1 1 +HETATM 948 O O . ZYB B 2 . ? 9.346 41.983 32.897 1.00 74.37 ? ? ? ? ? ? 2971 ZYB A O 1 +HETATM 949 H H1 . ZYB B 2 . ? 14.499 41.347 30.130 1.00 66.90 ? ? ? ? ? ? 2971 ZYB A H1 1 +HETATM 950 H H3 . ZYB B 2 . ? 10.792 42.194 28.744 1.00 63.37 ? ? ? ? ? ? 2971 ZYB A H3 1 +HETATM 951 H H . ZYB B 2 . ? 13.802 41.889 32.302 1.00 54.51 ? ? ? ? ? ? 2971 ZYB A H 1 +HETATM 952 H H4 . ZYB B 2 . ? 10.105 42.732 30.881 1.00 53.33 ? ? ? ? ? ? 2971 ZYB A H4 1 +HETATM 953 H HN1 . ZYB B 2 . ? 12.007 43.463 34.999 1.00 68.34 ? ? ? ? ? ? 2971 ZYB A HN1 1 +HETATM 954 H HN2 . ZYB B 2 . ? 13.192 43.451 33.952 1.00 68.34 ? ? ? ? ? ? 2971 ZYB A HN2 1 +HETATM 955 H HB . ZYB B 2 . ? 9.117 42.563 32.266 1.00 89.25 ? ? ? ? ? ? 2971 ZYB A HB 1 +HETATM 956 C C . MOH C 3 . ? 14.843 38.427 29.938 1.00 20.02 ? ? ? ? ? ? 2972 MOH A C 1 +HETATM 957 O O . MOH C 3 . ? 15.883 39.362 30.110 1.00 23.93 ? ? ? ? ? ? 2972 MOH A O 1 +HETATM 958 C C . MOH D 3 . ? 19.997 17.491 15.480 1.00 47.26 ? ? ? ? ? ? 2973 MOH A C 1 +HETATM 959 O O . MOH D 3 . ? 19.916 17.750 16.873 1.00 51.18 ? ? ? ? ? ? 2973 MOH A O 1 +HETATM 960 C C . MOH E 3 . ? 20.262 13.641 17.581 1.00 65.59 ? ? ? ? ? ? 2974 MOH A C 1 +HETATM 961 O O . MOH E 3 . ? 19.727 14.187 18.770 1.00 65.24 ? ? ? ? ? ? 2974 MOH A O 1 +HETATM 962 O O . HOH F 4 . ? 10.022 21.482 25.696 1.00 72.06 ? ? ? ? ? ? 2001 HOH A O 1 +HETATM 963 O O . HOH F 4 . ? 9.855 23.456 23.774 1.00 66.16 ? ? ? ? ? ? 2002 HOH A O 1 +HETATM 964 O O . HOH F 4 . ? 49.309 8.719 21.892 1.00 45.11 ? ? ? ? ? ? 2003 HOH A O 1 +HETATM 965 O O . HOH F 4 . ? 13.719 20.834 37.413 1.00 62.79 ? ? ? ? ? ? 2004 HOH A O 1 +HETATM 966 O O . HOH F 4 . ? 4.983 33.736 30.894 1.00 67.99 ? ? ? ? ? ? 2005 HOH A O 1 +HETATM 967 O O . HOH F 4 . ? 6.459 35.205 30.033 1.00 61.90 ? ? ? ? ? ? 2006 HOH A O 1 +HETATM 968 O O . HOH F 4 . ? 7.918 32.035 26.603 1.00 61.36 ? ? ? ? ? ? 2007 HOH A O 1 +HETATM 969 O O . HOH F 4 . ? 10.497 38.082 29.860 1.00 67.61 ? ? ? ? ? ? 2008 HOH A O 1 +HETATM 970 O O . HOH F 4 . ? 9.999 27.064 20.875 1.00 70.16 ? ? ? ? ? ? 2009 HOH A O 1 +HETATM 971 O O . HOH F 4 . ? 16.743 38.611 18.320 1.00 33.23 ? ? ? ? ? ? 2010 HOH A O 1 +HETATM 972 O O . HOH F 4 . ? 14.593 38.990 16.988 1.00 75.27 ? ? ? ? ? ? 2011 HOH A O 1 +HETATM 973 O O . HOH F 4 . ? 12.283 49.752 21.320 1.00 55.93 ? ? ? ? ? ? 2012 HOH A O 1 +HETATM 974 O O . HOH F 4 . ? 20.363 42.495 17.546 1.00 39.08 ? ? ? ? ? ? 2013 HOH A O 1 +HETATM 975 O O . HOH F 4 . ? 13.381 45.493 15.888 1.00 49.69 ? ? ? ? ? ? 2014 HOH A O 1 +HETATM 976 O O . HOH F 4 . ? 27.826 39.234 23.817 1.00 37.96 ? ? ? ? ? ? 2015 HOH A O 1 +HETATM 977 O O . HOH F 4 . ? 21.090 38.507 16.588 1.00 45.63 ? ? ? ? ? ? 2016 HOH A O 1 +HETATM 978 O O . HOH F 4 . ? 29.397 34.268 22.742 1.00 55.62 ? ? ? ? ? ? 2017 HOH A O 1 +HETATM 979 O O . HOH F 4 . ? 31.710 37.827 23.339 1.00 72.95 ? ? ? ? ? ? 2018 HOH A O 1 +HETATM 980 O O . HOH F 4 . ? 17.743 36.110 18.353 1.00 30.04 ? ? ? ? ? ? 2019 HOH A O 1 +HETATM 981 O O . HOH F 4 . ? 12.010 25.049 19.917 1.00 41.58 ? ? ? ? ? ? 2020 HOH A O 1 +HETATM 982 O O . HOH F 4 . ? 15.066 30.157 15.335 1.00 56.83 ? ? ? ? ? ? 2021 HOH A O 1 +HETATM 983 O O . HOH F 4 . ? 28.488 34.280 19.639 1.00 77.03 ? ? ? ? ? ? 2022 HOH A O 1 +HETATM 984 O O . HOH F 4 . ? 13.795 19.144 14.680 1.00 66.35 ? ? ? ? ? ? 2023 HOH A O 1 +HETATM 985 O O . HOH F 4 . ? 20.388 31.994 14.337 1.00 52.47 ? ? ? ? ? ? 2024 HOH A O 1 +HETATM 986 O O . HOH F 4 . ? 17.099 30.537 14.683 1.00 46.13 ? ? ? ? ? ? 2025 HOH A O 1 +HETATM 987 O O . HOH F 4 . ? 19.150 30.128 14.146 1.00 55.85 ? ? ? ? ? ? 2026 HOH A O 1 +HETATM 988 O O . HOH F 4 . ? 30.873 32.142 27.922 1.00 43.66 ? ? ? ? ? ? 2027 HOH A O 1 +HETATM 989 O O . HOH F 4 . ? 28.359 38.272 26.378 1.00 36.65 ? ? ? ? ? ? 2028 HOH A O 1 +HETATM 990 O O . HOH F 4 . ? 26.162 44.602 34.444 1.00 76.95 ? ? ? ? ? ? 2029 HOH A O 1 +HETATM 991 O O . HOH F 4 . ? 20.950 34.480 42.959 1.00 54.47 ? ? ? ? ? ? 2030 HOH A O 1 +HETATM 992 O O . HOH F 4 . ? 23.798 36.496 43.163 1.00 55.30 ? ? ? ? ? ? 2031 HOH A O 1 +HETATM 993 O O . HOH F 4 . ? 28.782 29.253 36.276 1.00 58.23 ? ? ? ? ? ? 2032 HOH A O 1 +HETATM 994 O O . HOH F 4 . ? 32.622 23.373 33.061 1.00 57.54 ? ? ? ? ? ? 2033 HOH A O 1 +HETATM 995 O O . HOH F 4 . ? 7.889 28.220 23.936 1.00 66.20 ? ? ? ? ? ? 2034 HOH A O 1 +HETATM 996 O O . HOH F 4 . ? 18.062 36.986 14.008 1.00 64.39 ? ? ? ? ? ? 2035 HOH A O 1 +HETATM 997 O O . HOH F 4 . ? 6.759 29.564 25.379 1.00 61.49 ? ? ? ? ? ? 2036 HOH A O 1 +HETATM 998 O O . HOH F 4 . ? 18.877 40.002 17.035 1.00 41.58 ? ? ? ? ? ? 2037 HOH A O 1 +HETATM 999 O O . HOH F 4 . ? 17.947 40.034 14.360 1.00 71.33 ? ? ? ? ? ? 2038 HOH A O 1 +HETATM 1000 O O . HOH F 4 . ? 49.700 17.754 20.028 1.00 33.75 ? ? ? ? ? ? 2039 HOH A O 1 +HETATM 1001 O O . HOH F 4 . ? 54.699 18.951 14.314 1.00 36.13 ? ? ? ? ? ? 2040 HOH A O 1 +HETATM 1002 O O . HOH F 4 . ? 48.417 16.913 11.414 1.00 44.68 ? ? ? ? ? ? 2041 HOH A O 1 +HETATM 1003 O O . HOH F 4 . ? 47.833 9.932 20.324 1.00 44.46 ? ? ? ? ? ? 2042 HOH A O 1 +HETATM 1004 O O . HOH F 4 . ? 47.016 20.600 15.420 1.00 56.49 ? ? ? ? ? ? 2043 HOH A O 1 +HETATM 1005 O O . HOH F 4 . ? 36.084 8.857 24.173 1.00 64.01 ? ? ? ? ? ? 2044 HOH A O 1 +HETATM 1006 O O . HOH F 4 . ? 30.306 11.616 22.382 1.00 41.64 ? ? ? ? ? ? 2045 HOH A O 1 +HETATM 1007 O O . HOH F 4 . ? 24.872 12.423 18.724 1.00 31.83 ? ? ? ? ? ? 2046 HOH A O 1 +HETATM 1008 O O . HOH F 4 . ? 32.113 18.160 20.044 1.00 43.06 ? ? ? ? ? ? 2047 HOH A O 1 +HETATM 1009 O O . HOH F 4 . ? 18.823 13.311 22.917 1.00 51.53 ? ? ? ? ? ? 2048 HOH A O 1 +HETATM 1010 O O . HOH F 4 . ? 16.161 15.671 23.834 1.00 53.90 ? ? ? ? ? ? 2049 HOH A O 1 +HETATM 1011 O O . HOH F 4 . ? 16.474 15.356 28.505 1.00 49.39 ? ? ? ? ? ? 2050 HOH A O 1 +HETATM 1012 O O . HOH F 4 . ? 19.716 11.870 25.898 1.00 55.67 ? ? ? ? ? ? 2051 HOH A O 1 +HETATM 1013 O O . HOH F 4 . ? 14.190 20.080 33.755 1.00 40.86 ? ? ? ? ? ? 2052 HOH A O 1 +HETATM 1014 O O . HOH F 4 . ? 16.006 16.626 33.801 1.00 63.70 ? ? ? ? ? ? 2053 HOH A O 1 +HETATM 1015 O O . HOH F 4 . ? 9.820 25.253 31.112 1.00 38.19 ? ? ? ? ? ? 2054 HOH A O 1 +HETATM 1016 O O . HOH F 4 . ? 9.286 23.840 26.837 1.00 71.54 ? ? ? ? ? ? 2055 HOH A O 1 +HETATM 1017 O O . HOH F 4 . ? 11.813 22.481 37.237 1.00 40.67 ? ? ? ? ? ? 2056 HOH A O 1 +HETATM 1018 O O . HOH F 4 . ? 8.637 27.688 31.635 1.00 50.11 ? ? ? ? ? ? 2057 HOH A O 1 +HETATM 1019 O O . HOH F 4 . ? 7.209 33.128 28.724 1.00 71.36 ? ? ? ? ? ? 2058 HOH A O 1 +HETATM 1020 O O . HOH F 4 . ? 10.592 33.431 26.632 1.00 31.26 ? ? ? ? ? ? 2059 HOH A O 1 +HETATM 1021 O O . HOH F 4 . ? 11.235 37.314 27.829 1.00 50.09 ? ? ? ? ? ? 2060 HOH A O 1 +HETATM 1022 O O . HOH F 4 . ? 14.805 35.285 26.097 1.00 28.85 ? ? ? ? ? ? 2061 HOH A O 1 +HETATM 1023 O O . HOH F 4 . ? 12.020 27.287 23.727 1.00 39.16 ? ? ? ? ? ? 2062 HOH A O 1 +HETATM 1024 O O . HOH F 4 . ? 10.652 36.085 25.723 1.00 45.42 ? ? ? ? ? ? 2063 HOH A O 1 +HETATM 1025 O O . HOH F 4 . ? 9.631 36.738 20.608 1.00 68.57 ? ? ? ? ? ? 2064 HOH A O 1 +HETATM 1026 O O . HOH F 4 . ? 15.877 39.137 20.800 1.00 31.10 ? ? ? ? ? ? 2065 HOH A O 1 +HETATM 1027 O O . HOH F 4 . ? 16.548 37.288 22.780 1.00 27.50 ? ? ? ? ? ? 2066 HOH A O 1 +HETATM 1028 O O . HOH F 4 . ? 9.739 39.897 24.415 1.00 38.01 ? ? ? ? ? ? 2067 HOH A O 1 +HETATM 1029 O O . HOH F 4 . ? 12.396 41.088 17.671 1.00 54.61 ? ? ? ? ? ? 2068 HOH A O 1 +HETATM 1030 O O . HOH F 4 . ? 14.917 46.883 22.021 1.00 34.11 ? ? ? ? ? ? 2069 HOH A O 1 +HETATM 1031 O O . HOH F 4 . ? 10.354 49.867 22.445 1.00 54.04 ? ? ? ? ? ? 2070 HOH A O 1 +HETATM 1032 O O . HOH F 4 . ? 17.013 49.205 22.232 1.00 35.94 ? ? ? ? ? ? 2071 HOH A O 1 +HETATM 1033 O O . HOH F 4 . ? 15.002 51.840 23.760 1.00 38.50 ? ? ? ? ? ? 2072 HOH A O 1 +HETATM 1034 O O . HOH F 4 . ? 18.929 37.372 24.878 1.00 26.24 ? ? ? ? ? ? 2073 HOH A O 1 +HETATM 1035 O O . HOH F 4 . ? 18.365 38.934 28.770 1.00 27.93 ? ? ? ? ? ? 2074 HOH A O 1 +HETATM 1036 O O . HOH F 4 . ? 20.711 43.703 19.713 1.00 38.04 ? ? ? ? ? ? 2075 HOH A O 1 +HETATM 1037 O O . HOH F 4 . ? 15.285 43.920 14.949 1.00 62.80 ? ? ? ? ? ? 2076 HOH A O 1 +HETATM 1038 O O . HOH F 4 . ? 24.523 55.530 19.752 1.00 41.19 ? ? ? ? ? ? 2077 HOH A O 1 +HETATM 1039 O O . HOH F 4 . ? 25.819 42.790 24.965 1.00 41.83 ? ? ? ? ? ? 2078 HOH A O 1 +HETATM 1040 O O . HOH F 4 . ? 25.262 40.180 24.148 1.00 32.73 ? ? ? ? ? ? 2079 HOH A O 1 +HETATM 1041 O O . HOH F 4 . ? 23.236 40.295 16.935 1.00 65.81 ? ? ? ? ? ? 2080 HOH A O 1 +HETATM 1042 O O . HOH F 4 . ? 23.693 44.108 18.054 1.00 51.91 ? ? ? ? ? ? 2081 HOH A O 1 +HETATM 1043 O O . HOH F 4 . ? 24.530 49.151 18.245 1.00 68.10 ? ? ? ? ? ? 2082 HOH A O 1 +HETATM 1044 O O . HOH F 4 . ? 29.757 36.549 22.673 1.00 59.13 ? ? ? ? ? ? 2083 HOH A O 1 +HETATM 1045 O O . HOH F 4 . ? 17.620 35.461 21.013 1.00 26.30 ? ? ? ? ? ? 2084 HOH A O 1 +HETATM 1046 O O . HOH F 4 . ? 20.282 36.066 18.152 1.00 47.27 ? ? ? ? ? ? 2085 HOH A O 1 +HETATM 1047 O O . HOH F 4 . ? 17.191 35.183 26.434 1.00 31.45 ? ? ? ? ? ? 2086 HOH A O 1 +HETATM 1048 O O . HOH F 4 . ? 13.631 26.057 18.018 1.00 31.32 ? ? ? ? ? ? 2087 HOH A O 1 +HETATM 1049 O O . HOH F 4 . ? 13.876 31.159 17.942 1.00 48.99 ? ? ? ? ? ? 2088 HOH A O 1 +HETATM 1050 O O . HOH F 4 . ? 16.769 34.148 16.880 1.00 37.84 ? ? ? ? ? ? 2089 HOH A O 1 +HETATM 1051 O O . HOH F 4 . ? 18.148 19.502 18.580 1.00 41.24 ? ? ? ? ? ? 2090 HOH A O 1 +HETATM 1052 O O . HOH F 4 . ? 13.480 17.462 21.017 1.00 63.97 ? ? ? ? ? ? 2091 HOH A O 1 +HETATM 1053 O O . HOH F 4 . ? 14.246 24.172 16.064 1.00 40.37 ? ? ? ? ? ? 2092 HOH A O 1 +HETATM 1054 O O . HOH F 4 . ? 13.807 24.254 10.402 1.00 53.41 ? ? ? ? ? ? 2093 HOH A O 1 +HETATM 1055 O O . HOH F 4 . ? 18.290 26.528 10.971 1.00 37.65 ? ? ? ? ? ? 2094 HOH A O 1 +HETATM 1056 O O . HOH F 4 . ? 23.456 32.819 16.199 1.00 41.64 ? ? ? ? ? ? 2095 HOH A O 1 +HETATM 1057 O O . HOH F 4 . ? 27.413 30.028 17.492 1.00 49.77 ? ? ? ? ? ? 2096 HOH A O 1 +HETATM 1058 O O . HOH F 4 . ? 26.076 32.886 18.780 1.00 39.46 ? ? ? ? ? ? 2097 HOH A O 1 +HETATM 1059 O O . HOH F 4 . ? 24.839 21.430 15.660 1.00 26.90 ? ? ? ? ? ? 2098 HOH A O 1 +HETATM 1060 O O . HOH F 4 . ? 17.451 17.851 12.901 1.00 47.85 ? ? ? ? ? ? 2099 HOH A O 1 +HETATM 1061 O O . HOH F 4 . ? 14.075 21.548 16.258 1.00 52.21 ? ? ? ? ? ? 2100 HOH A O 1 +HETATM 1062 O O . HOH F 4 . ? 28.093 28.077 16.234 1.00 53.38 ? ? ? ? ? ? 2101 HOH A O 1 +HETATM 1063 O O . HOH F 4 . ? 22.331 30.655 10.032 1.00 57.12 ? ? ? ? ? ? 2102 HOH A O 1 +HETATM 1064 O O . HOH F 4 . ? 22.795 31.536 13.460 1.00 58.79 ? ? ? ? ? ? 2103 HOH A O 1 +HETATM 1065 O O . HOH F 4 . ? 25.878 30.199 13.548 1.00 62.49 ? ? ? ? ? ? 2104 HOH A O 1 +HETATM 1066 O O . HOH F 4 . ? 18.842 29.119 12.218 1.00 43.86 ? ? ? ? ? ? 2105 HOH A O 1 +HETATM 1067 O O . HOH F 4 . ? 36.270 22.341 16.173 1.00 63.22 ? ? ? ? ? ? 2106 HOH A O 1 +HETATM 1068 O O . HOH F 4 . ? 35.040 21.758 21.898 1.00 58.36 ? ? ? ? ? ? 2107 HOH A O 1 +HETATM 1069 O O . HOH F 4 . ? 28.536 29.888 20.202 1.00 41.22 ? ? ? ? ? ? 2108 HOH A O 1 +HETATM 1070 O O . HOH F 4 . ? 29.358 32.925 25.925 1.00 31.19 ? ? ? ? ? ? 2109 HOH A O 1 +HETATM 1071 O O . HOH F 4 . ? 32.517 29.815 28.520 1.00 49.95 ? ? ? ? ? ? 2110 HOH A O 1 +HETATM 1072 O O . HOH F 4 . ? 18.672 36.149 28.506 1.00 26.69 ? ? ? ? ? ? 2111 HOH A O 1 +HETATM 1073 O O . HOH F 4 . ? 21.697 35.070 34.500 1.00 23.79 ? ? ? ? ? ? 2112 HOH A O 1 +HETATM 1074 O O . HOH F 4 . ? 27.482 39.559 32.373 1.00 56.82 ? ? ? ? ? ? 2113 HOH A O 1 +HETATM 1075 O O . HOH F 4 . ? 29.646 35.212 33.130 1.00 50.55 ? ? ? ? ? ? 2114 HOH A O 1 +HETATM 1076 O O . HOH F 4 . ? 28.416 35.532 26.914 1.00 38.68 ? ? ? ? ? ? 2115 HOH A O 1 +HETATM 1077 O O . HOH F 4 . ? 30.252 33.192 30.122 1.00 38.14 ? ? ? ? ? ? 2116 HOH A O 1 +HETATM 1078 O O . HOH F 4 . ? 26.307 39.198 27.582 1.00 37.97 ? ? ? ? ? ? 2117 HOH A O 1 +HETATM 1079 O O . HOH F 4 . ? 20.619 36.858 36.208 1.00 26.65 ? ? ? ? ? ? 2118 HOH A O 1 +HETATM 1080 O O . HOH F 4 . ? 23.667 34.037 36.165 1.00 31.26 ? ? ? ? ? ? 2119 HOH A O 1 +HETATM 1081 O O . HOH F 4 . ? 27.237 34.635 37.381 1.00 53.65 ? ? ? ? ? ? 2120 HOH A O 1 +HETATM 1082 O O . HOH F 4 . ? 26.758 41.946 35.152 1.00 68.46 ? ? ? ? ? ? 2121 HOH A O 1 +HETATM 1083 O O . HOH F 4 . ? 24.279 45.804 32.838 1.00 31.87 ? ? ? ? ? ? 2122 HOH A O 1 +HETATM 1084 O O . HOH F 4 . ? 21.112 39.380 37.230 1.00 27.53 ? ? ? ? ? ? 2123 HOH A O 1 +HETATM 1085 O O . HOH F 4 . ? 14.000 41.650 36.058 1.00 40.53 ? ? ? ? ? ? 2124 HOH A O 1 +HETATM 1086 O O . HOH F 4 . ? 16.010 44.370 36.642 1.00 31.64 ? ? ? ? ? ? 2125 HOH A O 1 +HETATM 1087 O O . HOH F 4 . ? 22.159 43.235 40.031 1.00 35.31 ? ? ? ? ? ? 2126 HOH A O 1 +HETATM 1088 O O . HOH F 4 . ? 19.831 43.489 42.462 1.00 29.68 ? ? ? ? ? ? 2127 HOH A O 1 +HETATM 1089 O O . HOH F 4 . ? 22.549 48.439 39.132 1.00 55.22 ? ? ? ? ? ? 2128 HOH A O 1 +HETATM 1090 O O . HOH F 4 . ? 13.893 48.371 41.323 1.00 71.57 ? ? ? ? ? ? 2129 HOH A O 1 +HETATM 1091 O O . HOH F 4 . ? 18.115 38.151 45.161 1.00 56.51 ? ? ? ? ? ? 2130 HOH A O 1 +HETATM 1092 O O . HOH F 4 . ? 19.704 36.599 42.356 1.00 48.79 ? ? ? ? ? ? 2131 HOH A O 1 +HETATM 1093 O O . HOH F 4 . ? 12.235 40.880 43.778 1.00 50.38 ? ? ? ? ? ? 2132 HOH A O 1 +HETATM 1094 O O . HOH F 4 . ? 14.322 39.623 47.341 1.00 56.25 ? ? ? ? ? ? 2133 HOH A O 1 +HETATM 1095 O O . HOH F 4 . ? 11.799 40.005 36.902 1.00 32.82 ? ? ? ? ? ? 2134 HOH A O 1 +HETATM 1096 O O . HOH F 4 . ? 10.801 40.634 39.586 1.00 45.53 ? ? ? ? ? ? 2135 HOH A O 1 +HETATM 1097 O O . HOH F 4 . ? 18.804 32.671 41.946 1.00 50.79 ? ? ? ? ? ? 2136 HOH A O 1 +HETATM 1098 O O . HOH F 4 . ? 23.623 34.350 42.820 1.00 62.35 ? ? ? ? ? ? 2137 HOH A O 1 +HETATM 1099 O O . HOH F 4 . ? 25.654 32.960 38.818 1.00 38.93 ? ? ? ? ? ? 2138 HOH A O 1 +HETATM 1100 O O . HOH F 4 . ? 24.552 30.490 39.019 1.00 37.91 ? ? ? ? ? ? 2139 HOH A O 1 +HETATM 1101 O O . HOH F 4 . ? 28.619 30.000 33.367 1.00 34.88 ? ? ? ? ? ? 2140 HOH A O 1 +HETATM 1102 O O . HOH F 4 . ? 30.386 31.617 32.147 1.00 45.65 ? ? ? ? ? ? 2141 HOH A O 1 +HETATM 1103 O O . HOH F 4 . ? 26.947 28.741 37.897 1.00 44.53 ? ? ? ? ? ? 2142 HOH A O 1 +HETATM 1104 O O . HOH F 4 . ? 21.982 20.442 37.227 1.00 34.13 ? ? ? ? ? ? 2143 HOH A O 1 +HETATM 1105 O O . HOH F 4 . ? 30.213 23.289 34.002 1.00 38.74 ? ? ? ? ? ? 2144 HOH A O 1 +HETATM 1106 O O . HOH F 4 . ? 32.249 27.856 33.935 1.00 59.39 ? ? ? ? ? ? 2145 HOH A O 1 +HETATM 1107 O O . HOH F 4 . ? 6.377 28.531 21.462 1.00 71.01 ? ? ? ? ? ? 2146 HOH A O 1 +# +loop_ +_atom_site_anisotrop.id +_atom_site_anisotrop.type_symbol +_atom_site_anisotrop.pdbx_label_atom_id +_atom_site_anisotrop.pdbx_label_alt_id +_atom_site_anisotrop.pdbx_label_comp_id +_atom_site_anisotrop.pdbx_label_asym_id +_atom_site_anisotrop.pdbx_label_seq_id +_atom_site_anisotrop.U[1][1] +_atom_site_anisotrop.U[2][2] +_atom_site_anisotrop.U[3][3] +_atom_site_anisotrop.U[1][2] +_atom_site_anisotrop.U[1][3] +_atom_site_anisotrop.U[2][3] +_atom_site_anisotrop.U[1][1]_esd +_atom_site_anisotrop.U[2][2]_esd +_atom_site_anisotrop.U[3][3]_esd +_atom_site_anisotrop.U[1][2]_esd +_atom_site_anisotrop.U[1][3]_esd +_atom_site_anisotrop.U[2][3]_esd +_atom_site_anisotrop.pdbx_auth_seq_id +_atom_site_anisotrop.pdbx_auth_comp_id +_atom_site_anisotrop.pdbx_auth_asym_id +_atom_site_anisotrop.pdbx_auth_atom_id +1 N N . SER A 1 0.4738 0.4524 0.2904 -0.0309 -0.0231 0.0036 ? ? ? ? ? ? 1856 SER A N +2 C CA . SER A 1 0.5262 0.4447 0.3239 -0.0195 -0.0197 0.0010 ? ? ? ? ? ? 1856 SER A CA +3 C C . SER A 1 0.5639 0.4532 0.3452 -0.0370 -0.0113 0.0088 ? ? ? ? ? ? 1856 SER A C +4 O O . SER A 1 0.5214 0.4379 0.3045 -0.0533 -0.0125 0.0141 ? ? ? ? ? ? 1856 SER A O +5 C CB . SER A 1 0.4971 0.3714 0.3023 -0.0165 -0.0119 0.0024 ? ? ? ? ? ? 1856 SER A CB +6 O OG . SER A 1 0.5159 0.3779 0.3411 -0.0339 0.0002 0.0133 ? ? ? ? ? ? 1856 SER A OG +7 N N . MET A 2 0.5837 0.4186 0.3455 -0.0378 -0.0030 0.0086 ? ? ? ? ? ? 1857 MET A N +8 C CA . MET A 2 0.6137 0.4220 0.3555 -0.0563 0.0075 0.0102 ? ? ? ? ? ? 1857 MET A CA +9 C C . MET A 2 0.5509 0.3572 0.3169 -0.0727 0.0190 0.0130 ? ? ? ? ? ? 1857 MET A C +10 O O . MET A 2 0.5733 0.3648 0.3670 -0.0718 0.0282 0.0138 ? ? ? ? ? ? 1857 MET A O +11 C CB . MET A 2 0.6333 0.3897 0.3494 -0.0611 0.0183 0.0080 ? ? ? ? ? ? 1857 MET A CB +12 C CG . MET A 2 0.6662 0.4019 0.3504 -0.0816 0.0276 0.0051 ? ? ? ? ? ? 1857 MET A CG +13 S SD . MET A 2 0.7242 0.4097 0.3748 -0.0992 0.0465 0.0007 ? ? ? ? ? ? 1857 MET A SD +14 C CE . MET A 2 0.6967 0.3644 0.3288 -0.0833 0.0238 0.0119 ? ? ? ? ? ? 1857 MET A CE +15 N N . SER A 3 0.5878 0.4076 0.3446 -0.0878 0.0151 0.0151 ? ? ? ? ? ? 1858 SER A N +16 C CA . SER A 3 0.5857 0.3954 0.3621 -0.1048 0.0183 0.0192 ? ? ? ? ? ? 1858 SER A CA +17 C C . SER A 3 0.5798 0.4172 0.3892 -0.1053 0.0073 0.0323 ? ? ? ? ? ? 1858 SER A C +18 O O . SER A 3 0.5438 0.3604 0.3770 -0.1155 0.0058 0.0394 ? ? ? ? ? ? 1858 SER A O +19 C CB . SER A 3 0.5979 0.3558 0.3839 -0.1078 0.0384 0.0078 ? ? ? ? ? ? 1858 SER A CB +20 O OG . SER A 3 0.6262 0.3621 0.3742 -0.1152 0.0497 -0.0044 ? ? ? ? ? ? 1858 SER A OG +21 N N . VAL A 4 0.4939 0.3776 0.3045 -0.0949 -0.0024 0.0344 ? ? ? ? ? ? 1859 VAL A N +22 C CA . VAL A 4 0.4767 0.3977 0.3092 -0.1020 -0.0135 0.0465 ? ? ? ? ? ? 1859 VAL A CA +23 C C . VAL A 4 0.5088 0.5015 0.3286 -0.1077 -0.0251 0.0451 ? ? ? ? ? ? 1859 VAL A C +24 O O . VAL A 4 0.5134 0.5399 0.3319 -0.0881 -0.0267 0.0318 ? ? ? ? ? ? 1859 VAL A O +25 C CB . VAL A 4 0.4800 0.3967 0.3327 -0.0859 -0.0107 0.0446 ? ? ? ? ? ? 1859 VAL A CB +26 C CG1 . VAL A 4 0.4519 0.4100 0.3216 -0.0993 -0.0239 0.0587 ? ? ? ? ? ? 1859 VAL A CG1 +27 C CG2 . VAL A 4 0.5126 0.3724 0.3835 -0.0805 0.0028 0.0427 ? ? ? ? ? ? 1859 VAL A CG2 +28 N N . LYS A 5 0.4184 0.6083 0.5828 -0.0988 -0.1528 0.2685 ? ? ? ? ? ? 1860 LYS A N +29 C CA . LYS A 5 0.4552 0.6496 0.6325 -0.0654 -0.1521 0.2879 ? ? ? ? ? ? 1860 LYS A CA +30 C C . LYS A 5 0.4328 0.6577 0.5968 -0.0092 -0.1309 0.2755 ? ? ? ? ? ? 1860 LYS A C +31 O O . LYS A 5 0.4454 0.6901 0.5816 0.0006 -0.1073 0.2704 ? ? ? ? ? ? 1860 LYS A O +32 C CB . LYS A 5 0.4611 0.6595 0.6439 -0.0955 -0.1461 0.3268 ? ? ? ? ? ? 1860 LYS A CB +33 C CG . LYS A 5 0.6581 0.8246 0.8468 -0.1371 -0.1692 0.3453 ? ? ? ? ? ? 1860 LYS A CG +34 C CD . LYS A 5 0.7149 0.8580 0.9223 -0.1116 -0.1903 0.3526 ? ? ? ? ? ? 1860 LYS A CD +35 C CE . LYS A 5 0.7720 0.8624 0.9706 -0.1413 -0.2066 0.3626 ? ? ? ? ? ? 1860 LYS A CE +36 N NZ . LYS A 5 0.8178 0.8686 1.0113 -0.1511 -0.2051 0.3295 ? ? ? ? ? ? 1860 LYS A NZ +37 N N . LYS A 6 0.4692 0.6928 0.6480 0.0313 -0.1362 0.2725 ? ? ? ? ? ? 1861 LYS A N +38 C CA . LYS A 6 0.6114 0.8554 0.7743 0.0867 -0.1112 0.2684 ? ? ? ? ? ? 1861 LYS A CA +39 C C . LYS A 6 0.5733 0.8254 0.7342 0.0749 -0.0786 0.2996 ? ? ? ? ? ? 1861 LYS A C +40 O O . LYS A 6 0.5994 0.8503 0.7837 0.0317 -0.0861 0.3218 ? ? ? ? ? ? 1861 LYS A O +41 C CB . LYS A 6 0.7434 0.9802 0.9261 0.1278 -0.1232 0.2597 ? ? ? ? ? ? 1861 LYS A CB +42 C CG . LYS A 6 0.7862 1.0176 0.9719 0.1455 -0.1467 0.2195 ? ? ? ? ? ? 1861 LYS A CG +43 C CD . LYS A 6 0.8266 1.0544 1.0221 0.1964 -0.1476 0.2103 ? ? ? ? ? ? 1861 LYS A CD +44 C CE . LYS A 6 0.8375 1.0530 1.0469 0.2029 -0.1703 0.1696 ? ? ? ? ? ? 1861 LYS A CE +45 N NZ . LYS A 6 0.8385 1.0090 1.0763 0.1584 -0.1875 0.1810 ? ? ? ? ? ? 1861 LYS A NZ +46 N N . PRO A 7 0.5816 0.8418 0.7121 0.1142 -0.0387 0.2989 ? ? ? ? ? ? 1862 PRO A N +47 C CA . PRO A 7 0.6381 0.9005 0.7711 0.1039 0.0042 0.3218 ? ? ? ? ? ? 1862 PRO A CA +48 C C . PRO A 7 0.6730 0.9453 0.8566 0.0916 -0.0078 0.3341 ? ? ? ? ? ? 1862 PRO A C +49 O O . PRO A 7 0.6273 0.8969 0.8289 0.1239 -0.0295 0.3269 ? ? ? ? ? ? 1862 PRO A O +50 C CB . PRO A 7 0.6742 0.9288 0.7631 0.1672 0.0488 0.3153 ? ? ? ? ? ? 1862 PRO A CB +51 C CG . PRO A 7 0.6893 0.9500 0.7394 0.1956 0.0316 0.2926 ? ? ? ? ? ? 1862 PRO A CG +52 C CD . PRO A 7 0.6081 0.8758 0.6951 0.1702 -0.0265 0.2749 ? ? ? ? ? ? 1862 PRO A CD +53 N N . LYS A 8 0.7059 0.9950 0.9129 0.0455 0.0055 0.3496 ? ? ? ? ? ? 1863 LYS A N +54 C CA . LYS A 8 0.7398 1.0556 0.9985 0.0313 -0.0125 0.3585 ? ? ? ? ? ? 1863 LYS A CA +55 C C . LYS A 8 0.7165 1.0435 0.9948 0.0696 0.0212 0.3536 ? ? ? ? ? ? 1863 LYS A C +56 O O . LYS A 8 0.7360 1.0631 1.0042 0.0701 0.0769 0.3512 ? ? ? ? ? ? 1863 LYS A O +57 C CB . LYS A 8 0.7246 1.0699 1.0032 -0.0290 -0.0092 0.3690 ? ? ? ? ? ? 1863 LYS A CB +58 N N . ARG A 9 0.6778 1.0076 0.9823 0.1019 -0.0072 0.3517 ? ? ? ? ? ? 1864 ARG A N +59 C CA . ARG A 9 0.6566 1.0008 0.9892 0.1352 0.0201 0.3470 ? ? ? ? ? ? 1864 ARG A CA +60 C C . ARG A 9 0.6321 1.0311 1.0213 0.0983 0.0267 0.3499 ? ? ? ? ? ? 1864 ARG A C +61 O O . ARG A 9 0.6122 1.0401 1.0269 0.0699 -0.0162 0.3588 ? ? ? ? ? ? 1864 ARG A O +62 C CB . ARG A 9 0.6292 0.9594 0.9727 0.1807 -0.0134 0.3432 ? ? ? ? ? ? 1864 ARG A CB +63 C CG . ARG A 9 0.5745 0.9213 0.9527 0.2143 0.0111 0.3389 ? ? ? ? ? ? 1864 ARG A CG +64 C CD . ARG A 9 0.5640 0.8839 0.9405 0.2369 -0.0241 0.3215 ? ? ? ? ? ? 1864 ARG A CD +65 N NE . ARG A 9 0.5445 0.8849 0.9583 0.2629 -0.0026 0.3175 ? ? ? ? ? ? 1864 ARG A NE +66 C CZ . ARG A 9 0.5468 0.9388 1.0212 0.2529 -0.0155 0.3255 ? ? ? ? ? ? 1864 ARG A CZ +67 N NH1 . ARG A 9 0.5996 1.0224 1.0932 0.2187 -0.0514 0.3384 ? ? ? ? ? ? 1864 ARG A NH1 +68 N NH2 . ARG A 9 0.5486 0.9622 1.0598 0.2776 0.0076 0.3169 ? ? ? ? ? ? 1864 ARG A NH2 +69 N N . ASP A 10 0.7256 0.8417 1.1362 0.2683 0.2421 0.2356 ? ? ? ? ? ? 1865 ASP A N +70 C CA . ASP A 10 0.7403 0.7329 1.0610 0.2483 0.2581 0.1826 ? ? ? ? ? ? 1865 ASP A CA +71 C C . ASP A 10 0.7015 0.6912 0.9233 0.1950 0.2095 0.1579 ? ? ? ? ? ? 1865 ASP A C +72 O O . ASP A 10 0.7150 0.7259 0.9290 0.1788 0.1645 0.1822 ? ? ? ? ? ? 1865 ASP A O +73 C CB . ASP A 10 0.8165 0.7280 1.1585 0.2739 0.2703 0.1987 ? ? ? ? ? ? 1865 ASP A CB +74 C CG . ASP A 10 0.9099 0.7057 1.1560 0.2439 0.2842 0.1412 ? ? ? ? ? ? 1865 ASP A CG +75 O OD1 . ASP A 10 0.8455 0.6158 1.0222 0.2174 0.2979 0.0871 ? ? ? ? ? ? 1865 ASP A OD1 +76 O OD2 . ASP A 10 0.9524 0.6845 1.1886 0.2439 0.2813 0.1501 ? ? ? ? ? ? 1865 ASP A OD2 +77 N N . ASP A 11 0.5749 0.5367 0.7198 0.1683 0.2192 0.1089 ? ? ? ? ? ? 1866 ASP A N +78 C CA . ASP A 11 0.5516 0.5121 0.6054 0.1256 0.1724 0.0859 ? ? ? ? ? ? 1866 ASP A CA +79 C C . ASP A 11 0.5709 0.4370 0.5379 0.1077 0.1738 0.0332 ? ? ? ? ? ? 1866 ASP A C +80 O O . ASP A 11 0.6087 0.4659 0.4959 0.0785 0.1386 0.0055 ? ? ? ? ? ? 1866 ASP A O +81 C CB . ASP A 11 0.5950 0.5917 0.6105 0.1051 0.1720 0.0736 ? ? ? ? ? ? 1866 ASP A CB +82 C CG . ASP A 11 0.7604 0.7038 0.7461 0.1085 0.2261 0.0337 ? ? ? ? ? ? 1866 ASP A CG +83 O OD1 . ASP A 11 0.8501 0.7459 0.8712 0.1342 0.2704 0.0215 ? ? ? ? ? ? 1866 ASP A OD1 +84 O OD2 . ASP A 11 0.8603 0.8046 0.7830 0.0829 0.2267 0.0138 ? ? ? ? ? ? 1866 ASP A OD2 +85 N N . SER A 12 0.6320 0.4296 0.6157 0.1257 0.2142 0.0188 ? ? ? ? ? ? 1867 SER A N +86 C CA . SER A 12 0.6814 0.3936 0.5843 0.1053 0.2269 -0.0379 ? ? ? ? ? ? 1867 SER A CA +87 C C . SER A 12 0.6849 0.3969 0.5396 0.0775 0.1768 -0.0499 ? ? ? ? ? ? 1867 SER A C +88 O O . SER A 12 0.7401 0.4117 0.5161 0.0534 0.1698 -0.1005 ? ? ? ? ? ? 1867 SER A O +89 C CB . SER A 12 0.7634 0.3993 0.6992 0.1274 0.2868 -0.0499 ? ? ? ? ? ? 1867 SER A CB +90 O OG . SER A 12 0.8212 0.4518 0.8132 0.1438 0.2792 -0.0100 ? ? ? ? ? ? 1867 SER A OG +91 N N . LYS A 13 0.6196 0.3847 0.5225 0.0791 0.1420 -0.0056 ? ? ? ? ? ? 1868 LYS A N +92 C CA . LYS A 13 0.5594 0.3358 0.4255 0.0498 0.0964 -0.0178 ? ? ? ? ? ? 1868 LYS A CA +93 C C . LYS A 13 0.5357 0.3838 0.3774 0.0305 0.0412 -0.0137 ? ? ? ? ? ? 1868 LYS A C +94 O O . LYS A 13 0.5501 0.4187 0.3667 0.0066 0.0025 -0.0278 ? ? ? ? ? ? 1868 LYS A O +95 C CB . LYS A 13 0.5625 0.3427 0.4848 0.0549 0.0937 0.0244 ? ? ? ? ? ? 1868 LYS A CB +96 C CG . LYS A 13 0.6511 0.3411 0.5886 0.0718 0.1468 0.0197 ? ? ? ? ? ? 1868 LYS A CG +97 C CD . LYS A 13 0.8535 0.5396 0.8356 0.0757 0.1386 0.0691 ? ? ? ? ? ? 1868 LYS A CD +98 N N . ASP A 14 0.5792 0.3303 0.4684 0.0423 -0.0386 -0.0023 ? ? ? ? ? ? 1869 ASP A N +99 C CA . ASP A 14 0.5678 0.3073 0.4127 0.0349 -0.0492 0.0045 ? ? ? ? ? ? 1869 ASP A CA +100 C C . ASP A 14 0.6101 0.3378 0.4371 0.0335 -0.0449 -0.0058 ? ? ? ? ? ? 1869 ASP A C +101 O O . ASP A 14 0.6273 0.3336 0.4261 0.0321 -0.0465 -0.0005 ? ? ? ? ? ? 1869 ASP A O +102 C CB . ASP A 14 0.5388 0.2972 0.3760 0.0245 -0.0586 0.0021 ? ? ? ? ? ? 1869 ASP A CB +103 C CG . ASP A 14 0.6681 0.4483 0.5179 0.0278 -0.0681 0.0065 ? ? ? ? ? ? 1869 ASP A CG +104 O OD1 . ASP A 14 0.6410 0.4160 0.4944 0.0440 -0.0684 0.0185 ? ? ? ? ? ? 1869 ASP A OD1 +105 O OD2 . ASP A 14 0.6181 0.4211 0.4730 0.0164 -0.0729 -0.0030 ? ? ? ? ? ? 1869 ASP A OD2 +106 N N . LEU A 15 0.5514 0.2997 0.3946 0.0377 -0.0407 -0.0232 ? ? ? ? ? ? 1870 LEU A N +107 C CA . LEU A 15 0.5578 0.3070 0.3816 0.0456 -0.0398 -0.0364 ? ? ? ? ? ? 1870 LEU A CA +108 C C . LEU A 15 0.5951 0.3328 0.4304 0.0472 -0.0318 -0.0464 ? ? ? ? ? ? 1870 LEU A C +109 O O . LEU A 15 0.6180 0.3389 0.4232 0.0491 -0.0348 -0.0454 ? ? ? ? ? ? 1870 LEU A O +110 C CB . LEU A 15 0.5520 0.3412 0.3925 0.0574 -0.0381 -0.0580 ? ? ? ? ? ? 1870 LEU A CB +111 C CG . LEU A 15 0.5274 0.3326 0.3440 0.0770 -0.0402 -0.0750 ? ? ? ? ? ? 1870 LEU A CG +112 C CD1 . LEU A 15 0.5653 0.3347 0.3204 0.0821 -0.0437 -0.0515 ? ? ? ? ? ? 1870 LEU A CD1 +113 C CD2 . LEU A 15 0.5195 0.3802 0.3546 0.0945 -0.0401 -0.1006 ? ? ? ? ? ? 1870 LEU A CD2 +114 N N . ALA A 16 0.5666 0.3090 0.4473 0.0454 -0.0173 -0.0565 ? ? ? ? ? ? 1871 ALA A N +115 C CA . ALA A 16 0.5937 0.3192 0.4919 0.0431 0.0005 -0.0671 ? ? ? ? ? ? 1871 ALA A CA +116 C C . ALA A 16 0.6230 0.3085 0.4819 0.0398 -0.0006 -0.0384 ? ? ? ? ? ? 1871 ALA A C +117 O O . ALA A 16 0.6187 0.2914 0.4668 0.0380 0.0061 -0.0458 ? ? ? ? ? ? 1871 ALA A O +118 C CB . ALA A 16 0.5909 0.3165 0.5484 0.0402 0.0262 -0.0798 ? ? ? ? ? ? 1871 ALA A CB +119 N N . LEU A 17 0.6095 0.2840 0.4489 0.0408 -0.0096 -0.0104 ? ? ? ? ? ? 1872 LEU A N +120 C CA . LEU A 17 0.6141 0.2645 0.4157 0.0425 -0.0130 0.0129 ? ? ? ? ? ? 1872 LEU A CA +121 C C . LEU A 17 0.6387 0.2879 0.4016 0.0364 -0.0290 0.0099 ? ? ? ? ? ? 1872 LEU A C +122 O O . LEU A 17 0.6820 0.3146 0.4212 0.0357 -0.0266 0.0142 ? ? ? ? ? ? 1872 LEU A O +123 C CB . LEU A 17 0.6376 0.2941 0.4317 0.0510 -0.0222 0.0350 ? ? ? ? ? ? 1872 LEU A CB +124 C CG . LEU A 17 0.6777 0.3222 0.5014 0.0641 -0.0023 0.0464 ? ? ? ? ? ? 1872 LEU A CG +125 C CD1 . LEU A 17 0.6695 0.3318 0.4852 0.0791 -0.0171 0.0641 ? ? ? ? ? ? 1872 LEU A CD1 +126 C CD2 . LEU A 17 0.7596 0.3640 0.5745 0.0715 0.0256 0.0601 ? ? ? ? ? ? 1872 LEU A CD2 +127 N N . CYS A 18 0.6335 0.2966 0.3896 0.0327 -0.0413 0.0031 ? ? ? ? ? ? 1873 CYS A N +128 C CA . CYS A 18 0.6385 0.2901 0.3607 0.0287 -0.0491 0.0007 ? ? ? ? ? ? 1873 CYS A CA +129 C C . CYS A 18 0.6661 0.3114 0.3836 0.0353 -0.0438 -0.0149 ? ? ? ? ? ? 1873 CYS A C +130 O O . CYS A 18 0.6390 0.2677 0.3309 0.0337 -0.0463 -0.0152 ? ? ? ? ? ? 1873 CYS A O +131 C CB . CYS A 18 0.6163 0.2733 0.3310 0.0261 -0.0529 0.0002 ? ? ? ? ? ? 1873 CYS A CB +132 S SG . CYS A 18 0.6459 0.3141 0.3649 0.0123 -0.0590 0.0080 ? ? ? ? ? ? 1873 CYS A SG +133 N N . SER A 19 0.4692 0.2749 0.4520 0.0232 -0.0131 -0.0129 ? ? ? ? ? ? 1874 SER A N +134 C CA . SER A 19 0.4433 0.2640 0.4204 0.0160 0.0026 -0.0235 ? ? ? ? ? ? 1874 SER A CA +135 C C . SER A 19 0.4728 0.2763 0.4291 0.0073 0.0096 -0.0021 ? ? ? ? ? ? 1874 SER A C +136 O O . SER A 19 0.4994 0.3140 0.4279 0.0031 0.0179 -0.0038 ? ? ? ? ? ? 1874 SER A O +137 C CB . SER A 19 0.4195 0.2523 0.4438 0.0114 0.0132 -0.0454 ? ? ? ? ? ? 1874 SER A CB +138 O OG . SER A 19 0.5132 0.3642 0.5358 0.0042 0.0279 -0.0576 ? ? ? ? ? ? 1874 SER A OG +139 N N . MET A 20 0.4965 0.2714 0.4660 0.0050 0.0070 0.0177 ? ? ? ? ? ? 1875 MET A N +140 C CA . MET A 20 0.5371 0.2878 0.4822 -0.0030 0.0140 0.0415 ? ? ? ? ? ? 1875 MET A CA +141 C C . MET A 20 0.5594 0.3103 0.4507 -0.0003 0.0056 0.0568 ? ? ? ? ? ? 1875 MET A C +142 O O . MET A 20 0.5613 0.3137 0.4244 -0.0089 0.0169 0.0608 ? ? ? ? ? ? 1875 MET A O +143 C CB . MET A 20 0.5730 0.2878 0.5358 -0.0011 0.0095 0.0633 ? ? ? ? ? ? 1875 MET A CB +144 C CG . MET A 20 0.7207 0.4031 0.6487 -0.0073 0.0151 0.0928 ? ? ? ? ? ? 1875 MET A CG +145 S SD . MET A 20 1.0298 0.6680 0.9644 0.0036 0.0012 0.1240 ? ? ? ? ? ? 1875 MET A SD +146 C CE . MET A 20 0.9212 0.5748 0.8259 0.0201 -0.0290 0.1319 ? ? ? ? ? ? 1875 MET A CE +147 N N . ILE A 21 0.5427 0.2937 0.4223 0.0106 -0.0132 0.0630 ? ? ? ? ? ? 1876 ILE A N +148 C CA . ILE A 21 0.5705 0.3237 0.4014 0.0129 -0.0217 0.0749 ? ? ? ? ? ? 1876 ILE A CA +149 C C . ILE A 21 0.6057 0.3842 0.4153 0.0099 -0.0116 0.0570 ? ? ? ? ? ? 1876 ILE A C +150 O O . ILE A 21 0.5472 0.3256 0.3194 0.0044 -0.0063 0.0655 ? ? ? ? ? ? 1876 ILE A O +151 C CB . ILE A 21 0.5472 0.3026 0.3767 0.0245 -0.0426 0.0774 ? ? ? ? ? ? 1876 ILE A CB +152 C CG1 . ILE A 21 0.5864 0.3165 0.4286 0.0304 -0.0556 0.0995 ? ? ? ? ? ? 1876 ILE A CG1 +153 C CG2 . ILE A 21 0.5611 0.3267 0.3433 0.0253 -0.0485 0.0811 ? ? ? ? ? ? 1876 ILE A CG2 +154 C CD1 . ILE A 21 0.6169 0.3542 0.4709 0.0427 -0.0766 0.0967 ? ? ? ? ? ? 1876 ILE A CD1 +155 N N . LEU A 22 0.5634 0.3626 0.3959 0.0142 -0.0085 0.0322 ? ? ? ? ? ? 1877 LEU A N +156 C CA . LEU A 22 0.5152 0.3367 0.3271 0.0153 -0.0002 0.0153 ? ? ? ? ? ? 1877 LEU A CA +157 C C . LEU A 22 0.4851 0.3129 0.2929 0.0055 0.0161 0.0133 ? ? ? ? ? ? 1877 LEU A C +158 O O . LEU A 22 0.5084 0.3455 0.2844 0.0040 0.0218 0.0122 ? ? ? ? ? ? 1877 LEU A O +159 C CB . LEU A 22 0.4378 0.2772 0.2735 0.0233 0.0001 -0.0096 ? ? ? ? ? ? 1877 LEU A CB +160 C CG . LEU A 22 0.4987 0.3588 0.3113 0.0293 0.0069 -0.0269 ? ? ? ? ? ? 1877 LEU A CG +161 C CD1 . LEU A 22 0.5316 0.3867 0.2995 0.0326 0.0031 -0.0185 ? ? ? ? ? ? 1877 LEU A CD1 +162 C CD2 . LEU A 22 0.4763 0.3487 0.3097 0.0379 0.0063 -0.0487 ? ? ? ? ? ? 1877 LEU A CD2 +163 N N . THR A 23 0.4987 0.2395 0.3943 -0.0643 0.0641 -0.0004 ? ? ? ? ? ? 1878 THR A N +164 C CA . THR A 23 0.5130 0.2464 0.4093 -0.0903 0.0735 -0.0121 ? ? ? ? ? ? 1878 THR A CA +165 C C . THR A 23 0.5878 0.3106 0.4792 -0.0858 0.0744 0.0106 ? ? ? ? ? ? 1878 THR A C +166 O O . THR A 23 0.5609 0.3074 0.4583 -0.1021 0.0705 0.0066 ? ? ? ? ? ? 1878 THR A O +167 C CB . THR A 23 0.6509 0.3353 0.5429 -0.1052 0.0979 -0.0297 ? ? ? ? ? ? 1878 THR A CB +168 O OG1 . THR A 23 0.6050 0.3057 0.5009 -0.1095 0.0946 -0.0550 ? ? ? ? ? ? 1878 THR A OG1 +169 C CG2 . THR A 23 0.6457 0.3212 0.5451 -0.1335 0.1108 -0.0417 ? ? ? ? ? ? 1878 THR A CG2 +170 N N . GLU A 24 0.5832 0.2725 0.4624 -0.0610 0.0787 0.0336 ? ? ? ? ? ? 1879 GLU A N +171 C CA . GLU A 24 0.6323 0.3103 0.5013 -0.0498 0.0787 0.0562 ? ? ? ? ? ? 1879 GLU A CA +172 C C . GLU A 24 0.5307 0.2659 0.4114 -0.0414 0.0512 0.0642 ? ? ? ? ? ? 1879 GLU A C +173 O O . GLU A 24 0.5199 0.2654 0.3975 -0.0452 0.0485 0.0721 ? ? ? ? ? ? 1879 GLU A O +174 C CB . GLU A 24 0.6036 0.2341 0.4541 -0.0195 0.0867 0.0765 ? ? ? ? ? ? 1879 GLU A CB +175 C CG . GLU A 24 0.7399 0.3054 0.5748 -0.0257 0.1156 0.0721 ? ? ? ? ? ? 1879 GLU A CG +176 C CD . GLU A 24 0.9405 0.4824 0.7625 0.0080 0.1157 0.0874 ? ? ? ? ? ? 1879 GLU A CD +177 O OE1 . GLU A 24 0.9598 0.5124 0.7875 0.0285 0.1035 0.0880 ? ? ? ? ? ? 1879 GLU A OE1 +178 O OE2 . GLU A 24 1.0959 0.6160 0.9048 0.0138 0.1270 0.0965 ? ? ? ? ? ? 1879 GLU A OE2 +179 N N A MET A 25 0.4896 0.2596 0.3842 -0.0295 0.0326 0.0624 ? ? ? ? ? ? 1880 MET A N +180 N N B MET A 25 0.4922 0.2635 0.3871 -0.0300 0.0322 0.0622 ? ? ? ? ? ? 1880 MET A N +181 C CA A MET A 25 0.5014 0.3253 0.4112 -0.0233 0.0067 0.0674 ? ? ? ? ? ? 1880 MET A CA +182 C CA B MET A 25 0.5072 0.3309 0.4163 -0.0235 0.0066 0.0682 ? ? ? ? ? ? 1880 MET A CA +183 C C A MET A 25 0.5271 0.3859 0.4424 -0.0500 0.0013 0.0514 ? ? ? ? ? ? 1880 MET A C +184 C C B MET A 25 0.5234 0.3847 0.4395 -0.0499 0.0002 0.0512 ? ? ? ? ? ? 1880 MET A C +185 O O A MET A 25 0.4920 0.3769 0.4102 -0.0510 -0.0112 0.0572 ? ? ? ? ? ? 1880 MET A O +186 O O B MET A 25 0.4908 0.3827 0.4114 -0.0507 -0.0144 0.0563 ? ? ? ? ? ? 1880 MET A O +187 C CB A MET A 25 0.4174 0.2671 0.3436 -0.0091 -0.0063 0.0669 ? ? ? ? ? ? 1880 MET A CB +188 C CB B MET A 25 0.4446 0.2934 0.3704 -0.0051 -0.0083 0.0712 ? ? ? ? ? ? 1880 MET A CB +189 C CG A MET A 25 0.5384 0.3600 0.4647 0.0177 -0.0023 0.0787 ? ? ? ? ? ? 1880 MET A CG +190 C CG B MET A 25 0.5571 0.3777 0.4816 0.0238 -0.0061 0.0856 ? ? ? ? ? ? 1880 MET A CG +191 S SD A MET A 25 0.4384 0.2633 0.3676 0.0476 -0.0187 0.1000 ? ? ? ? ? ? 1880 MET A SD +192 S SD B MET A 25 0.7091 0.5653 0.6630 0.0426 -0.0219 0.0873 ? ? ? ? ? ? 1880 MET A SD +193 C CE A MET A 25 0.5438 0.4337 0.5069 0.0512 -0.0466 0.0994 ? ? ? ? ? ? 1880 MET A CE +194 C CE B MET A 25 0.5847 0.4907 0.5578 0.0472 -0.0494 0.0952 ? ? ? ? ? ? 1880 MET A CE +195 N N . GLU A 26 0.4688 0.3289 0.3853 -0.0694 0.0098 0.0293 ? ? ? ? ? ? 1881 GLU A N +196 C CA . GLU A 26 0.4328 0.3275 0.3552 -0.0933 0.0039 0.0084 ? ? ? ? ? ? 1881 GLU A CA +197 C C . GLU A 26 0.5013 0.3887 0.4226 -0.1109 0.0135 0.0064 ? ? ? ? ? ? 1881 GLU A C +198 O O . GLU A 26 0.4657 0.3921 0.3945 -0.1232 0.0015 -0.0031 ? ? ? ? ? ? 1881 GLU A O +199 C CB . GLU A 26 0.4718 0.3617 0.3937 -0.1077 0.0134 -0.0180 ? ? ? ? ? ? 1881 GLU A CB +200 C CG . GLU A 26 0.4743 0.3864 0.3965 -0.0935 0.0023 -0.0201 ? ? ? ? ? ? 1881 GLU A CG +201 C CD . GLU A 26 0.5494 0.4448 0.4654 -0.1002 0.0150 -0.0430 ? ? ? ? ? ? 1881 GLU A CD +202 O OE1 . GLU A 26 0.5788 0.4376 0.4930 -0.1134 0.0333 -0.0546 ? ? ? ? ? ? 1881 GLU A OE1 +203 O OE2 . GLU A 26 0.6336 0.5510 0.5463 -0.0910 0.0076 -0.0490 ? ? ? ? ? ? 1881 GLU A OE2 +204 N N . THR A 27 0.2402 0.3235 0.4042 -0.0194 -0.0022 -0.0112 ? ? ? ? ? ? 1882 THR A N +205 C CA . THR A 27 0.3182 0.3588 0.4732 -0.0398 0.0500 -0.0119 ? ? ? ? ? ? 1882 THR A CA +206 C C . THR A 27 0.3855 0.3624 0.4554 -0.0377 0.0727 0.0009 ? ? ? ? ? ? 1882 THR A C +207 O O . THR A 27 0.4394 0.3924 0.4964 -0.0600 0.1185 -0.0031 ? ? ? ? ? ? 1882 THR A O +208 C CB . THR A 27 0.3803 0.3746 0.5246 -0.0550 0.0624 -0.0094 ? ? ? ? ? ? 1882 THR A CB +209 O OG1 . THR A 27 0.4878 0.4203 0.5607 -0.0382 0.0311 0.0041 ? ? ? ? ? ? 1882 THR A OG1 +210 C CG2 . THR A 27 0.3676 0.4327 0.6056 -0.0613 0.0499 -0.0273 ? ? ? ? ? ? 1882 THR A CG2 +211 N N . HIS A 28 0.3870 0.3427 0.3988 -0.0141 0.0416 0.0139 ? ? ? ? ? ? 1883 HIS A N +212 C CA . HIS A 28 0.4622 0.3668 0.3965 -0.0103 0.0588 0.0246 ? ? ? ? ? ? 1883 HIS A CA +213 C C . HIS A 28 0.4888 0.4423 0.4743 -0.0171 0.0865 0.0043 ? ? ? ? ? ? 1883 HIS A C +214 O O . HIS A 28 0.3572 0.3818 0.4250 -0.0094 0.0654 -0.0107 ? ? ? ? ? ? 1883 HIS A O +215 C CB . HIS A 28 0.4623 0.3528 0.3430 0.0190 0.0143 0.0388 ? ? ? ? ? ? 1883 HIS A CB +216 C CG . HIS A 28 0.5530 0.3756 0.3384 0.0239 0.0274 0.0542 ? ? ? ? ? ? 1883 HIS A CG +217 N ND1 . HIS A 28 0.5869 0.4207 0.3710 0.0187 0.0566 0.0450 ? ? ? ? ? ? 1883 HIS A ND1 +218 C CD2 . HIS A 28 0.5765 0.3224 0.2674 0.0340 0.0117 0.0754 ? ? ? ? ? ? 1883 HIS A CD2 +219 C CE1 . HIS A 28 0.6232 0.3919 0.3118 0.0226 0.0623 0.0614 ? ? ? ? ? ? 1883 HIS A CE1 +220 N NE2 . HIS A 28 0.7239 0.4349 0.3526 0.0314 0.0344 0.0824 ? ? ? ? ? ? 1883 HIS A NE2 +221 N N . GLU A 29 0.4781 0.3963 0.4174 -0.0336 0.1303 0.0009 ? ? ? ? ? ? 1884 GLU A N +222 C CA . GLU A 29 0.4619 0.4358 0.4632 -0.0404 0.1589 -0.0302 ? ? ? ? ? ? 1884 GLU A CA +223 C C . GLU A 29 0.4199 0.4289 0.4447 -0.0098 0.1221 -0.0376 ? ? ? ? ? ? 1884 GLU A C +224 O O . GLU A 29 0.4045 0.4713 0.5094 -0.0067 0.1245 -0.0677 ? ? ? ? ? ? 1884 GLU A O +225 C CB . GLU A 29 0.6711 0.6107 0.6143 -0.0708 0.2167 -0.0383 ? ? ? ? ? ? 1884 GLU A CB +226 C CG . GLU A 29 0.7593 0.6500 0.6061 -0.0636 0.2190 -0.0261 ? ? ? ? ? ? 1884 GLU A CG +227 C CD . GLU A 29 0.9640 0.8494 0.7713 -0.1009 0.2798 -0.0453 ? ? ? ? ? ? 1884 GLU A CD +228 O OE1 . GLU A 29 0.8792 0.8338 0.7551 -0.1012 0.3025 -0.0873 ? ? ? ? ? ? 1884 GLU A OE1 +229 O OE2 . GLU A 29 1.0775 0.8914 0.7858 -0.1326 0.3019 -0.0207 ? ? ? ? ? ? 1884 GLU A OE2 +230 N N . ASP A 30 0.4104 0.3844 0.3698 0.0125 0.0836 -0.0120 ? ? ? ? ? ? 1885 ASP A N +231 C CA . ASP A 30 0.4370 0.4388 0.4115 0.0387 0.0429 -0.0143 ? ? ? ? ? ? 1885 ASP A CA +232 C C . ASP A 30 0.4027 0.4518 0.4300 0.0494 -0.0144 -0.0062 ? ? ? ? ? ? 1885 ASP A C +233 O O . ASP A 30 0.3230 0.3838 0.3405 0.0670 -0.0590 0.0028 ? ? ? ? ? ? 1885 ASP A O +234 C CB . ASP A 30 0.4306 0.3711 0.2986 0.0543 0.0346 0.0074 ? ? ? ? ? ? 1885 ASP A CB +235 C CG . ASP A 30 0.5016 0.4015 0.3106 0.0388 0.0876 -0.0010 ? ? ? ? ? ? 1885 ASP A CG +236 O OD1 . ASP A 30 0.5150 0.4494 0.3749 0.0192 0.1290 -0.0315 ? ? ? ? ? ? 1885 ASP A OD1 +237 O OD2 . ASP A 30 0.5570 0.3944 0.2672 0.0440 0.0866 0.0212 ? ? ? ? ? ? 1885 ASP A OD2 +238 N N . ALA A 31 0.5429 0.3202 0.2619 0.0479 0.0596 0.0166 ? ? ? ? ? ? 1886 ALA A N +239 C CA . ALA A 31 0.5369 0.2954 0.2548 0.0415 0.0479 0.0104 ? ? ? ? ? ? 1886 ALA A CA +240 C C . ALA A 31 0.5010 0.2677 0.2430 0.0312 0.0353 0.0001 ? ? ? ? ? ? 1886 ALA A C +241 O O . ALA A 31 0.5622 0.3256 0.3069 0.0279 0.0240 -0.0042 ? ? ? ? ? ? 1886 ALA A O +242 C CB . ALA A 31 0.5662 0.2889 0.2730 0.0342 0.0536 0.0170 ? ? ? ? ? ? 1886 ALA A CB +243 N N . TRP A 32 0.5200 0.3015 0.2822 0.0284 0.0393 0.0001 ? ? ? ? ? ? 1887 TRP A N +244 C CA . TRP A 32 0.5482 0.3397 0.3399 0.0195 0.0311 -0.0021 ? ? ? ? ? ? 1887 TRP A CA +245 C C . TRP A 32 0.5598 0.3574 0.3622 0.0233 0.0199 -0.0117 ? ? ? ? ? ? 1887 TRP A C +246 O O . TRP A 32 0.5578 0.3604 0.3818 0.0146 0.0105 -0.0084 ? ? ? ? ? ? 1887 TRP A O +247 C CB . TRP A 32 0.5603 0.3720 0.3738 0.0225 0.0417 0.0033 ? ? ? ? ? ? 1887 TRP A CB +248 C CG . TRP A 32 0.5422 0.3659 0.3460 0.0399 0.0524 -0.0059 ? ? ? ? ? ? 1887 TRP A CG +249 C CD1 . TRP A 32 0.4903 0.3211 0.2727 0.0488 0.0644 -0.0026 ? ? ? ? ? ? 1887 TRP A CD1 +250 C CD2 . TRP A 32 0.5567 0.3858 0.3695 0.0493 0.0526 -0.0205 ? ? ? ? ? ? 1887 TRP A CD2 +251 N NE1 . TRP A 32 0.5152 0.3586 0.2874 0.0620 0.0707 -0.0167 ? ? ? ? ? ? 1887 TRP A NE1 +252 C CE2 . TRP A 32 0.5742 0.4112 0.3632 0.0621 0.0640 -0.0300 ? ? ? ? ? ? 1887 TRP A CE2 +253 C CE3 . TRP A 32 0.5374 0.3638 0.3755 0.0480 0.0448 -0.0259 ? ? ? ? ? ? 1887 TRP A CE3 +254 C CZ2 . TRP A 32 0.5794 0.4147 0.3637 0.0717 0.0679 -0.0500 ? ? ? ? ? ? 1887 TRP A CZ2 +255 C CZ3 . TRP A 32 0.5462 0.3684 0.3861 0.0592 0.0501 -0.0425 ? ? ? ? ? ? 1887 TRP A CZ3 +256 C CH2 . TRP A 32 0.5663 0.3894 0.3766 0.0701 0.0614 -0.0571 ? ? ? ? ? ? 1887 TRP A CH2 +257 N N . PRO A 33 0.4964 0.2964 0.2854 0.0340 0.0197 -0.0215 ? ? ? ? ? ? 1888 PRO A N +258 C CA . PRO A 33 0.4793 0.2814 0.2840 0.0334 0.0076 -0.0282 ? ? ? ? ? ? 1888 PRO A CA +259 C C . PRO A 33 0.4698 0.2681 0.2705 0.0281 -0.0046 -0.0213 ? ? ? ? ? ? 1888 PRO A C +260 O O . PRO A 33 0.4749 0.2791 0.2950 0.0260 -0.0154 -0.0212 ? ? ? ? ? ? 1888 PRO A O +261 C CB . PRO A 33 0.4932 0.2978 0.2801 0.0408 0.0082 -0.0412 ? ? ? ? ? ? 1888 PRO A CB +262 C CG . PRO A 33 0.5042 0.3148 0.2718 0.0477 0.0233 -0.0419 ? ? ? ? ? ? 1888 PRO A CG +263 C CD . PRO A 33 0.4659 0.2716 0.2299 0.0441 0.0282 -0.0257 ? ? ? ? ? ? 1888 PRO A CD +264 N N . PHE A 34 0.5008 0.2881 0.2774 0.0275 -0.0008 -0.0145 ? ? ? ? ? ? 1889 PHE A N +265 C CA . PHE A 34 0.4953 0.2777 0.2581 0.0288 -0.0071 -0.0086 ? ? ? ? ? ? 1889 PHE A CA +266 C C . PHE A 34 0.4966 0.2639 0.2509 0.0196 -0.0070 -0.0054 ? ? ? ? ? ? 1889 PHE A C +267 O O . PHE A 34 0.5209 0.2808 0.2579 0.0227 -0.0087 -0.0018 ? ? ? ? ? ? 1889 PHE A O +268 C CB . PHE A 34 0.5467 0.3266 0.2821 0.0406 0.0004 -0.0031 ? ? ? ? ? ? 1889 PHE A CB +269 C CG . PHE A 34 0.5233 0.3207 0.2584 0.0453 -0.0002 -0.0077 ? ? ? ? ? ? 1889 PHE A CG +270 C CD1 . PHE A 34 0.5053 0.3167 0.2541 0.0424 -0.0134 -0.0131 ? ? ? ? ? ? 1889 PHE A CD1 +271 C CD2 . PHE A 34 0.4986 0.2987 0.2189 0.0506 0.0120 -0.0067 ? ? ? ? ? ? 1889 PHE A CD2 +272 C CE1 . PHE A 34 0.4978 0.3212 0.2398 0.0423 -0.0155 -0.0222 ? ? ? ? ? ? 1889 PHE A CE1 +273 C CE2 . PHE A 34 0.5225 0.3422 0.2357 0.0531 0.0107 -0.0133 ? ? ? ? ? ? 1889 PHE A CE2 +274 C CZ . PHE A 34 0.5377 0.3668 0.2589 0.0477 -0.0037 -0.0234 ? ? ? ? ? ? 1889 PHE A CZ +275 N N . LEU A 35 0.5106 0.2744 0.2746 0.0076 -0.0047 -0.0061 ? ? ? ? ? ? 1890 LEU A N +276 C CA . LEU A 35 0.5668 0.3116 0.3150 -0.0067 -0.0053 -0.0059 ? ? ? ? ? ? 1890 LEU A CA +277 C C . LEU A 35 0.6253 0.3845 0.3814 -0.0165 -0.0192 -0.0045 ? ? ? ? ? ? 1890 LEU A C +278 O O . LEU A 35 0.5520 0.2934 0.2803 -0.0226 -0.0203 -0.0080 ? ? ? ? ? ? 1890 LEU A O +279 C CB . LEU A 35 0.5433 0.2871 0.3036 -0.0213 -0.0015 -0.0030 ? ? ? ? ? ? 1890 LEU A CB +280 C CG . LEU A 35 0.5914 0.3192 0.3395 -0.0139 0.0140 -0.0005 ? ? ? ? ? ? 1890 LEU A CG +281 C CD1 . LEU A 35 0.5980 0.3350 0.3669 -0.0283 0.0165 0.0073 ? ? ? ? ? ? 1890 LEU A CD1 +282 C CD2 . LEU A 35 0.7012 0.3891 0.4128 -0.0109 0.0232 -0.0021 ? ? ? ? ? ? 1890 LEU A CD2 +283 N N . LEU A 36 0.5053 0.2959 0.2984 -0.0166 -0.0283 0.0009 ? ? ? ? ? ? 1891 LEU A N +284 C CA . LEU A 36 0.5160 0.3313 0.3262 -0.0259 -0.0416 0.0085 ? ? ? ? ? ? 1891 LEU A CA +285 C C . LEU A 36 0.5357 0.3707 0.3704 -0.0133 -0.0477 0.0144 ? ? ? ? ? ? 1891 LEU A C +286 O O . LEU A 36 0.4790 0.3102 0.3240 -0.0021 -0.0433 0.0104 ? ? ? ? ? ? 1891 LEU A O +287 C CB . LEU A 36 0.5523 0.3927 0.3955 -0.0419 -0.0467 0.0180 ? ? ? ? ? ? 1891 LEU A CB +288 C CG . LEU A 36 0.5662 0.3936 0.3917 -0.0618 -0.0452 0.0161 ? ? ? ? ? ? 1891 LEU A CG +289 C CD1 . LEU A 36 0.5943 0.4596 0.4625 -0.0756 -0.0505 0.0328 ? ? ? ? ? ? 1891 LEU A CD1 +290 C CD2 . LEU A 36 0.6564 0.4658 0.4411 -0.0766 -0.0517 0.0082 ? ? ? ? ? ? 1891 LEU A CD2 +291 N N . PRO A 37 0.4743 0.3312 0.3174 -0.0168 -0.0584 0.0242 ? ? ? ? ? ? 1892 PRO A N +292 C CA . PRO A 37 0.4277 0.3040 0.3004 -0.0069 -0.0650 0.0338 ? ? ? ? ? ? 1892 PRO A CA +293 C C . PRO A 37 0.3838 0.2721 0.3049 -0.0062 -0.0651 0.0384 ? ? ? ? ? ? 1892 PRO A C +294 O O . PRO A 37 0.4330 0.3337 0.3745 -0.0141 -0.0637 0.0441 ? ? ? ? ? ? 1892 PRO A O +295 C CB . PRO A 37 0.4672 0.3713 0.3415 -0.0121 -0.0753 0.0476 ? ? ? ? ? ? 1892 PRO A CB +296 C CG . PRO A 37 0.4622 0.3670 0.3164 -0.0290 -0.0766 0.0441 ? ? ? ? ? ? 1892 PRO A CG +297 C CD . PRO A 37 0.4485 0.3141 0.2719 -0.0309 -0.0652 0.0271 ? ? ? ? ? ? 1892 PRO A CD +298 N N . VAL A 38 0.4942 0.2174 0.4040 -0.0429 -0.0705 -0.0274 ? ? ? ? ? ? 1893 VAL A N +299 C CA . VAL A 38 0.5101 0.2401 0.4522 -0.0415 -0.0589 -0.0233 ? ? ? ? ? ? 1893 VAL A CA +300 C C . VAL A 38 0.6208 0.3203 0.5418 -0.0191 -0.0972 -0.0229 ? ? ? ? ? ? 1893 VAL A C +301 O O . VAL A 38 0.6349 0.3025 0.4751 -0.0082 -0.1142 -0.0213 ? ? ? ? ? ? 1893 VAL A O +302 C CB . VAL A 38 0.5722 0.3104 0.4694 -0.0539 -0.0107 -0.0162 ? ? ? ? ? ? 1893 VAL A CB +303 C CG1 . VAL A 38 0.5924 0.3232 0.5140 -0.0520 0.0058 -0.0148 ? ? ? ? ? ? 1893 VAL A CG1 +304 C CG2 . VAL A 38 0.5375 0.3218 0.4626 -0.0733 0.0259 -0.0133 ? ? ? ? ? ? 1893 VAL A CG2 +305 N N . ASN A 39 0.5962 0.3081 0.5906 -0.0103 -0.1108 -0.0228 ? ? ? ? ? ? 1894 ASN A N +306 C CA . ASN A 39 0.7082 0.4000 0.6889 0.0171 -0.1454 -0.0153 ? ? ? ? ? ? 1894 ASN A CA +307 C C . ASN A 39 0.6909 0.3501 0.6187 0.0239 -0.1094 0.0009 ? ? ? ? ? ? 1894 ASN A C +308 O O . ASN A 39 0.6708 0.3376 0.6462 0.0168 -0.0721 0.0048 ? ? ? ? ? ? 1894 ASN A O +309 C CB . ASN A 39 0.6637 0.3873 0.7499 0.0268 -0.1699 -0.0190 ? ? ? ? ? ? 1894 ASN A CB +310 C CG . ASN A 39 0.7107 0.4265 0.7861 0.0614 -0.2133 -0.0075 ? ? ? ? ? ? 1894 ASN A CG +311 O OD1 . ASN A 39 0.7650 0.4428 0.7660 0.0796 -0.2058 0.0114 ? ? ? ? ? ? 1894 ASN A OD1 +312 N ND2 . ASN A 39 0.6513 0.4064 0.8020 0.0715 -0.2574 -0.0182 ? ? ? ? ? ? 1894 ASN A ND2 +313 N N . LEU A 40 0.7217 0.3417 0.5522 0.0360 -0.1167 0.0078 ? ? ? ? ? ? 1895 LEU A N +314 C CA . LEU A 40 0.7282 0.3101 0.4985 0.0379 -0.0740 0.0191 ? ? ? ? ? ? 1895 LEU A CA +315 C C . LEU A 40 0.7414 0.3010 0.5376 0.0647 -0.0710 0.0382 ? ? ? ? ? ? 1895 LEU A C +316 O O . LEU A 40 0.7475 0.2734 0.5160 0.0642 -0.0234 0.0464 ? ? ? ? ? ? 1895 LEU A O +317 C CB . LEU A 40 0.8050 0.3479 0.4644 0.0432 -0.0811 0.0203 ? ? ? ? ? ? 1895 LEU A CB +318 C CG . LEU A 40 0.8330 0.3932 0.4627 0.0206 -0.0785 0.0049 ? ? ? ? ? ? 1895 LEU A CG +319 C CD1 . LEU A 40 0.9397 0.4571 0.4622 0.0274 -0.0839 0.0056 ? ? ? ? ? ? 1895 LEU A CD1 +320 C CD2 . LEU A 40 0.7600 0.3540 0.4168 -0.0086 -0.0259 -0.0022 ? ? ? ? ? ? 1895 LEU A CD2 +321 N N . LYS A 41 0.8106 0.3912 0.6642 0.0883 -0.1186 0.0446 ? ? ? ? ? ? 1896 LYS A N +322 C CA . LYS A 41 0.9136 0.4811 0.8033 0.1201 -0.1185 0.0679 ? ? ? ? ? ? 1896 LYS A CA +323 C C . LYS A 41 0.8753 0.4727 0.8774 0.1078 -0.0881 0.0635 ? ? ? ? ? ? 1896 LYS A C +324 O O . LYS A 41 0.8602 0.4429 0.9022 0.1295 -0.0693 0.0825 ? ? ? ? ? ? 1896 LYS A O +325 C CB . LYS A 41 0.9521 0.5374 0.8438 0.1567 -0.1889 0.0790 ? ? ? ? ? ? 1896 LYS A CB +326 C CG . LYS A 41 1.0659 0.6232 0.8438 0.1684 -0.2207 0.0816 ? ? ? ? ? ? 1896 LYS A CG +327 C CD . LYS A 41 1.2516 0.8070 1.0034 0.2164 -0.2675 0.1087 ? ? ? ? ? ? 1896 LYS A CD +328 C CE . LYS A 41 1.3088 0.9363 1.1407 0.2276 -0.3328 0.0968 ? ? ? ? ? ? 1896 LYS A CE +329 N NZ . LYS A 41 1.3332 0.9864 1.1324 0.2074 -0.3768 0.0645 ? ? ? ? ? ? 1896 LYS A NZ +330 N N . LEU A 42 0.7870 0.4509 0.7273 0.0312 -0.1080 -0.0253 ? ? ? ? ? ? 1897 LEU A N +331 C CA . LEU A 42 0.8228 0.4968 0.8288 0.0409 -0.0926 -0.0355 ? ? ? ? ? ? 1897 LEU A CA +332 C C . LEU A 42 0.8150 0.4832 0.8113 0.0431 -0.0578 -0.0448 ? ? ? ? ? ? 1897 LEU A C +333 O O . LEU A 42 0.8639 0.5385 0.9069 0.0475 -0.0412 -0.0552 ? ? ? ? ? ? 1897 LEU A O +334 C CB . LEU A 42 0.7542 0.4467 0.7937 0.0369 -0.0892 -0.0497 ? ? ? ? ? ? 1897 LEU A CB +335 C CG . LEU A 42 0.8972 0.6045 0.9562 0.0315 -0.1249 -0.0450 ? ? ? ? ? ? 1897 LEU A CG +336 C CD1 . LEU A 42 0.9322 0.6597 1.0393 0.0270 -0.1166 -0.0629 ? ? ? ? ? ? 1897 LEU A CD1 +337 C CD2 . LEU A 42 0.9307 0.6422 1.0324 0.0407 -0.1561 -0.0264 ? ? ? ? ? ? 1897 LEU A CD2 +338 N N . VAL A 43 0.7164 0.3760 0.6545 0.0378 -0.0464 -0.0427 ? ? ? ? ? ? 1898 VAL A N +339 C CA . VAL A 43 0.6759 0.3364 0.5996 0.0366 -0.0184 -0.0490 ? ? ? ? ? ? 1898 VAL A CA +340 C C . VAL A 43 0.6844 0.3320 0.5787 0.0359 -0.0189 -0.0422 ? ? ? ? ? ? 1898 VAL A C +341 O O . VAL A 43 0.6706 0.3116 0.5195 0.0317 -0.0242 -0.0346 ? ? ? ? ? ? 1898 VAL A O +342 C CB . VAL A 43 0.6877 0.3532 0.5800 0.0319 -0.0038 -0.0500 ? ? ? ? ? ? 1898 VAL A CB +343 C CG1 . VAL A 43 0.6832 0.3562 0.5596 0.0283 0.0191 -0.0516 ? ? ? ? ? ? 1898 VAL A CG1 +344 C CG2 . VAL A 43 0.6423 0.3156 0.5644 0.0302 -0.0012 -0.0562 ? ? ? ? ? ? 1898 VAL A CG2 +345 N N . PRO A 44 0.6511 0.2951 0.5762 0.0382 -0.0101 -0.0481 ? ? ? ? ? ? 1899 PRO A N +346 C CA . PRO A 44 0.6676 0.2970 0.5720 0.0353 -0.0076 -0.0441 ? ? ? ? ? ? 1899 PRO A CA +347 C C . PRO A 44 0.7014 0.3382 0.5539 0.0266 0.0075 -0.0463 ? ? ? ? ? ? 1899 PRO A C +348 O O . PRO A 44 0.6574 0.3121 0.5029 0.0230 0.0232 -0.0539 ? ? ? ? ? ? 1899 PRO A O +349 C CB . PRO A 44 0.7434 0.3713 0.7005 0.0371 0.0094 -0.0600 ? ? ? ? ? ? 1899 PRO A CB +350 C CG . PRO A 44 0.7513 0.3891 0.7666 0.0450 0.0042 -0.0651 ? ? ? ? ? ? 1899 PRO A CG +351 C CD . PRO A 44 0.6642 0.3172 0.6518 0.0420 0.0012 -0.0625 ? ? ? ? ? ? 1899 PRO A CD +352 N N . GLY A 45 0.6092 0.2342 0.4281 0.0223 0.0015 -0.0373 ? ? ? ? ? ? 1900 GLY A N +353 C CA . GLY A 45 0.6028 0.2388 0.3828 0.0144 0.0140 -0.0395 ? ? ? ? ? ? 1900 GLY A CA +354 C C . GLY A 45 0.6235 0.2690 0.3750 0.0147 0.0107 -0.0339 ? ? ? ? ? ? 1900 GLY A C +355 O O . GLY A 45 0.6555 0.3054 0.3797 0.0093 0.0149 -0.0321 ? ? ? ? ? ? 1900 GLY A O +356 N N . TYR A 46 0.6042 0.2531 0.3687 0.0201 0.0058 -0.0337 ? ? ? ? ? ? 1901 TYR A N +357 C CA . TYR A 46 0.5828 0.2402 0.3329 0.0208 0.0096 -0.0327 ? ? ? ? ? ? 1901 TYR A CA +358 C C . TYR A 46 0.6679 0.3178 0.3875 0.0156 0.0049 -0.0316 ? ? ? ? ? ? 1901 TYR A C +359 O O . TYR A 46 0.5951 0.2549 0.3044 0.0146 0.0153 -0.0333 ? ? ? ? ? ? 1901 TYR A O +360 C CB . TYR A 46 0.6239 0.2817 0.3972 0.0249 0.0068 -0.0352 ? ? ? ? ? ? 1901 TYR A CB +361 C CG . TYR A 46 0.6372 0.3033 0.4118 0.0271 0.0180 -0.0335 ? ? ? ? ? ? 1901 TYR A CG +362 C CD1 . TYR A 46 0.5813 0.2418 0.3469 0.0266 0.0184 -0.0373 ? ? ? ? ? ? 1901 TYR A CD1 +363 C CD2 . TYR A 46 0.5632 0.2425 0.3495 0.0280 0.0293 -0.0275 ? ? ? ? ? ? 1901 TYR A CD2 +364 C CE1 . TYR A 46 0.5788 0.2437 0.3597 0.0312 0.0298 -0.0347 ? ? ? ? ? ? 1901 TYR A CE1 +365 C CE2 . TYR A 46 0.6115 0.2962 0.4050 0.0312 0.0364 -0.0186 ? ? ? ? ? ? 1901 TYR A CE2 +366 C CZ . TYR A 46 0.6346 0.3105 0.4313 0.0350 0.0366 -0.0218 ? ? ? ? ? ? 1901 TYR A CZ +367 O OH . TYR A 46 0.5736 0.2519 0.3909 0.0407 0.0444 -0.0117 ? ? ? ? ? ? 1901 TYR A OH +368 N N . LYS A 47 0.6918 0.3268 0.3987 0.0107 -0.0107 -0.0280 ? ? ? ? ? ? 1902 LYS A N +369 C CA . LYS A 47 0.7033 0.3323 0.3724 -0.0004 -0.0130 -0.0287 ? ? ? ? ? ? 1902 LYS A CA +370 C C . LYS A 47 0.6587 0.2887 0.3056 -0.0071 -0.0017 -0.0271 ? ? ? ? ? ? 1902 LYS A C +371 O O . LYS A 47 0.7321 0.3688 0.3603 -0.0139 0.0101 -0.0346 ? ? ? ? ? ? 1902 LYS A O +372 C CB . LYS A 47 0.7250 0.3406 0.3780 -0.0085 -0.0366 -0.0195 ? ? ? ? ? ? 1902 LYS A CB +373 C CG . LYS A 47 0.7732 0.3857 0.3771 -0.0266 -0.0375 -0.0231 ? ? ? ? ? ? 1902 LYS A CG +374 C CD . LYS A 47 0.8132 0.4170 0.3935 -0.0389 -0.0662 -0.0090 ? ? ? ? ? ? 1902 LYS A CD +375 C CE . LYS A 47 0.9365 0.5396 0.4558 -0.0639 -0.0637 -0.0146 ? ? ? ? ? ? 1902 LYS A CE +376 N NZ . LYS A 47 1.0326 0.6289 0.5181 -0.0802 -0.0963 0.0076 ? ? ? ? ? ? 1902 LYS A NZ +377 N N . LYS A 48 0.6491 0.2731 0.3038 -0.0066 -0.0025 -0.0205 ? ? ? ? ? ? 1903 LYS A N +378 C CA . LYS A 48 0.6562 0.2814 0.2935 -0.0157 0.0087 -0.0206 ? ? ? ? ? ? 1903 LYS A CA +379 C C . LYS A 48 0.6806 0.3332 0.3304 -0.0124 0.0250 -0.0299 ? ? ? ? ? ? 1903 LYS A C +380 O O . LYS A 48 0.6895 0.3536 0.3276 -0.0198 0.0355 -0.0338 ? ? ? ? ? ? 1903 LYS A O +381 C CB . LYS A 48 0.6675 0.2751 0.3163 -0.0176 0.0047 -0.0136 ? ? ? ? ? ? 1903 LYS A CB +382 C CG . LYS A 48 0.6908 0.2965 0.3235 -0.0304 0.0169 -0.0149 ? ? ? ? ? ? 1903 LYS A CG +383 C CD . LYS A 48 0.7722 0.3665 0.3637 -0.0450 0.0154 -0.0066 ? ? ? ? ? ? 1903 LYS A CD +384 C CE . LYS A 48 0.7570 0.3431 0.3358 -0.0604 0.0273 -0.0053 ? ? ? ? ? ? 1903 LYS A CE +385 N NZ . LYS A 48 0.7623 0.3145 0.3525 -0.0627 0.0181 0.0098 ? ? ? ? ? ? 1903 LYS A NZ +386 N N . VAL A 49 0.6071 0.2725 0.2823 -0.0027 0.0263 -0.0316 ? ? ? ? ? ? 1904 VAL A N +387 C CA . VAL A 49 0.6139 0.3080 0.2997 -0.0013 0.0358 -0.0334 ? ? ? ? ? ? 1904 VAL A CA +388 C C . VAL A 49 0.6367 0.3441 0.3324 0.0058 0.0394 -0.0319 ? ? ? ? ? ? 1904 VAL A C +389 O O . VAL A 49 0.6181 0.3471 0.3202 0.0048 0.0458 -0.0319 ? ? ? ? ? ? 1904 VAL A O +390 C CB . VAL A 49 0.5833 0.2866 0.2856 0.0009 0.0371 -0.0337 ? ? ? ? ? ? 1904 VAL A CB +391 C CG1 . VAL A 49 0.5827 0.3186 0.2901 0.0005 0.0414 -0.0284 ? ? ? ? ? ? 1904 VAL A CG1 +392 C CG2 . VAL A 49 0.5884 0.2817 0.2912 -0.0077 0.0405 -0.0419 ? ? ? ? ? ? 1904 VAL A CG2 +393 N N . ILE A 50 0.4941 0.2495 0.4330 -0.0620 0.0377 -0.0105 ? ? ? ? ? ? 1905 ILE A N +394 C CA . ILE A 50 0.5233 0.2878 0.4288 -0.0397 0.0202 -0.0219 ? ? ? ? ? ? 1905 ILE A CA +395 C C . ILE A 50 0.6079 0.3288 0.4510 -0.0237 0.0572 -0.0068 ? ? ? ? ? ? 1905 ILE A C +396 O O . ILE A 50 0.6180 0.2819 0.3724 -0.0104 0.0506 0.0152 ? ? ? ? ? ? 1905 ILE A O +397 C CB . ILE A 50 0.5374 0.2784 0.3829 -0.0299 -0.0330 -0.0197 ? ? ? ? ? ? 1905 ILE A CB +398 C CG1 . ILE A 50 0.5576 0.3358 0.4604 -0.0433 -0.0664 -0.0325 ? ? ? ? ? ? 1905 ILE A CG1 +399 C CG2 . ILE A 50 0.4791 0.2158 0.2834 -0.0058 -0.0413 -0.0304 ? ? ? ? ? ? 1905 ILE A CG2 +400 C CD1 . ILE A 50 0.4390 0.2914 0.4247 -0.0372 -0.0651 -0.0614 ? ? ? ? ? ? 1905 ILE A CD1 +401 N N . LYS A 51 0.5238 0.2778 0.4156 -0.0226 0.0954 -0.0232 ? ? ? ? ? ? 1906 LYS A N +402 C CA . LYS A 51 0.6171 0.3291 0.4608 -0.0105 0.1416 -0.0086 ? ? ? ? ? ? 1906 LYS A CA +403 C C . LYS A 51 0.7278 0.4092 0.4817 0.0168 0.1177 -0.0013 ? ? ? ? ? ? 1906 LYS A C +404 O O . LYS A 51 0.6980 0.3273 0.3786 0.0325 0.1413 0.0192 ? ? ? ? ? ? 1906 LYS A O +405 C CB . LYS A 51 0.6524 0.4157 0.5855 -0.0205 0.1915 -0.0364 ? ? ? ? ? ? 1906 LYS A CB +406 C CG . LYS A 51 0.7122 0.5083 0.7466 -0.0522 0.2272 -0.0529 ? ? ? ? ? ? 1906 LYS A CG +407 C CD . LYS A 51 0.8099 0.5256 0.7937 -0.0600 0.2585 -0.0147 ? ? ? ? ? ? 1906 LYS A CD +408 C CE . LYS A 51 0.8195 0.5591 0.9067 -0.0943 0.3051 -0.0324 ? ? ? ? ? ? 1906 LYS A CE +409 N NZ . LYS A 51 0.9728 0.6195 1.0008 -0.0948 0.3537 0.0080 ? ? ? ? ? ? 1906 LYS A NZ +410 N N . LYS A 52 0.5879 0.2982 0.3450 0.0253 0.0754 -0.0191 ? ? ? ? ? ? 1907 LYS A N +411 C CA . LYS A 52 0.6989 0.3774 0.3772 0.0480 0.0573 -0.0172 ? ? ? ? ? ? 1907 LYS A CA +412 C C . LYS A 52 0.6391 0.3058 0.2900 0.0484 0.0091 -0.0231 ? ? ? ? ? ? 1907 LYS A C +413 O O . LYS A 52 0.6176 0.3087 0.2900 0.0571 -0.0078 -0.0395 ? ? ? ? ? ? 1907 LYS A O +414 C CB . LYS A 52 0.7118 0.4252 0.4130 0.0647 0.0722 -0.0359 ? ? ? ? ? ? 1907 LYS A CB +415 C CG . LYS A 52 0.8474 0.5770 0.5846 0.0623 0.1248 -0.0384 ? ? ? ? ? ? 1907 LYS A CG +416 C CD . LYS A 52 0.9725 0.7418 0.7268 0.0833 0.1319 -0.0612 ? ? ? ? ? ? 1907 LYS A CD +417 C CE . LYS A 52 1.0273 0.8250 0.8360 0.0769 0.1867 -0.0737 ? ? ? ? ? ? 1907 LYS A CE +418 N NZ . LYS A 52 1.0514 0.8989 0.8805 0.1009 0.1886 -0.1013 ? ? ? ? ? ? 1907 LYS A NZ +419 N N . PRO A 53 0.6932 0.3217 0.2950 0.0424 -0.0097 -0.0120 ? ? ? ? ? ? 1908 PRO A N +420 C CA . PRO A 53 0.7254 0.3382 0.3023 0.0385 -0.0490 -0.0236 ? ? ? ? ? ? 1908 PRO A CA +421 C C . PRO A 53 0.6770 0.2942 0.2517 0.0520 -0.0476 -0.0281 ? ? ? ? ? ? 1908 PRO A C +422 O O . PRO A 53 0.6607 0.2598 0.1947 0.0657 -0.0305 -0.0268 ? ? ? ? ? ? 1908 PRO A O +423 C CB . PRO A 53 0.6863 0.2893 0.2512 0.0342 -0.0567 -0.0117 ? ? ? ? ? ? 1908 PRO A CB +424 C CG . PRO A 53 0.7441 0.3295 0.2874 0.0351 -0.0296 0.0079 ? ? ? ? ? ? 1908 PRO A CG +425 C CD . PRO A 53 0.7881 0.3860 0.3528 0.0432 0.0085 0.0092 ? ? ? ? ? ? 1908 PRO A CD +426 N N . MET A 54 0.6788 0.1783 0.3262 -0.0349 0.0269 0.0263 ? ? ? ? ? ? 1909 MET A N +427 C CA . MET A 54 0.6402 0.2193 0.3265 -0.0283 0.0067 0.0252 ? ? ? ? ? ? 1909 MET A CA +428 C C . MET A 54 0.6941 0.2935 0.3841 -0.0051 -0.0057 0.0194 ? ? ? ? ? ? 1909 MET A C +429 O O . MET A 54 0.6652 0.2273 0.3323 -0.0035 -0.0021 0.0097 ? ? ? ? ? ? 1909 MET A O +430 C CB . MET A 54 0.5640 0.1894 0.2901 -0.0623 -0.0022 0.0126 ? ? ? ? ? ? 1909 MET A CB +431 C CG . MET A 54 0.5663 0.2609 0.3274 -0.0513 -0.0153 0.0136 ? ? ? ? ? ? 1909 MET A CG +432 S SD . MET A 54 0.5831 0.2862 0.3319 -0.0286 -0.0069 0.0294 ? ? ? ? ? ? 1909 MET A SD +433 C CE . MET A 54 0.6009 0.2745 0.3392 -0.0503 0.0200 0.0413 ? ? ? ? ? ? 1909 MET A CE +434 N N . ASP A 55 0.5662 0.2199 0.2815 0.0114 -0.0168 0.0244 ? ? ? ? ? ? 1910 ASP A N +435 C CA . ASP A 55 0.5309 0.2124 0.2611 0.0291 -0.0233 0.0222 ? ? ? ? ? ? 1910 ASP A CA +436 C C . ASP A 55 0.5085 0.2463 0.2753 0.0239 -0.0353 0.0193 ? ? ? ? ? ? 1910 ASP A C +437 O O . ASP A 55 0.5231 0.2743 0.2951 0.0155 -0.0381 0.0194 ? ? ? ? ? ? 1910 ASP A O +438 C CB . ASP A 55 0.5837 0.2584 0.3028 0.0628 -0.0171 0.0355 ? ? ? ? ? ? 1910 ASP A CB +439 C CG . ASP A 55 0.6507 0.3621 0.3787 0.0756 -0.0271 0.0464 ? ? ? ? ? ? 1910 ASP A CG +440 O OD1 . ASP A 55 0.6092 0.2904 0.3076 0.0765 -0.0212 0.0558 ? ? ? ? ? ? 1910 ASP A OD1 +441 O OD2 . ASP A 55 0.5599 0.3291 0.3216 0.0817 -0.0404 0.0444 ? ? ? ? ? ? 1910 ASP A OD2 +442 N N . PHE A 56 0.4664 0.2287 0.2538 0.0294 -0.0371 0.0170 ? ? ? ? ? ? 1911 PHE A N +443 C CA . PHE A 56 0.4768 0.2738 0.2943 0.0209 -0.0427 0.0130 ? ? ? ? ? ? 1911 PHE A CA +444 C C . PHE A 56 0.4579 0.2806 0.2870 0.0218 -0.0513 0.0112 ? ? ? ? ? ? 1911 PHE A C +445 O O . PHE A 56 0.4288 0.2582 0.2639 0.0108 -0.0542 0.0034 ? ? ? ? ? ? 1911 PHE A O +446 C CB . PHE A 56 0.4637 0.2736 0.2991 0.0253 -0.0355 0.0149 ? ? ? ? ? ? 1911 PHE A CB +447 C CG . PHE A 56 0.5287 0.3153 0.3407 0.0264 -0.0295 0.0151 ? ? ? ? ? ? 1911 PHE A CG +448 C CD1 . PHE A 56 0.4840 0.2535 0.2741 0.0168 -0.0373 0.0093 ? ? ? ? ? ? 1911 PHE A CD1 +449 C CD2 . PHE A 56 0.4854 0.2729 0.2974 0.0359 -0.0163 0.0209 ? ? ? ? ? ? 1911 PHE A CD2 +450 C CE1 . PHE A 56 0.5018 0.2587 0.2656 0.0169 -0.0395 0.0057 ? ? ? ? ? ? 1911 PHE A CE1 +451 C CE2 . PHE A 56 0.5176 0.2826 0.2935 0.0407 -0.0129 0.0207 ? ? ? ? ? ? 1911 PHE A CE2 +452 C CZ . PHE A 56 0.5508 0.3021 0.3003 0.0313 -0.0284 0.0113 ? ? ? ? ? ? 1911 PHE A CZ +453 N N . SER A 57 0.4467 0.2843 0.2749 0.0380 -0.0561 0.0175 ? ? ? ? ? ? 1912 SER A N +454 C CA . SER A 57 0.5260 0.3987 0.3608 0.0393 -0.0719 0.0131 ? ? ? ? ? ? 1912 SER A CA +455 C C . SER A 57 0.5609 0.4103 0.3569 0.0381 -0.0730 0.0130 ? ? ? ? ? ? 1912 SER A C +456 O O . SER A 57 0.4827 0.3472 0.2718 0.0311 -0.0831 0.0014 ? ? ? ? ? ? 1912 SER A O +457 C CB . SER A 57 0.5103 0.4187 0.3554 0.0643 -0.0804 0.0240 ? ? ? ? ? ? 1912 SER A CB +458 O OG . SER A 57 0.5952 0.4688 0.3972 0.0892 -0.0748 0.0406 ? ? ? ? ? ? 1912 SER A OG +459 N N . THR A 58 0.5369 0.3454 0.3051 0.0425 -0.0594 0.0243 ? ? ? ? ? ? 1913 THR A N +460 C CA . THR A 58 0.5605 0.3464 0.2963 0.0393 -0.0513 0.0285 ? ? ? ? ? ? 1913 THR A CA +461 C C . THR A 58 0.5263 0.3176 0.2791 0.0193 -0.0453 0.0164 ? ? ? ? ? ? 1913 THR A C +462 O O . THR A 58 0.5915 0.3852 0.3275 0.0189 -0.0419 0.0122 ? ? ? ? ? ? 1913 THR A O +463 C CB . THR A 58 0.5669 0.3029 0.2749 0.0423 -0.0330 0.0443 ? ? ? ? ? ? 1913 THR A CB +464 O OG1 . THR A 58 0.5684 0.2917 0.2538 0.0712 -0.0345 0.0593 ? ? ? ? ? ? 1913 THR A OG1 +465 C CG2 . THR A 58 0.5953 0.3099 0.2755 0.0353 -0.0167 0.0525 ? ? ? ? ? ? 1913 THR A CG2 +466 N N . ILE A 59 0.4623 0.2553 0.2430 0.0084 -0.0430 0.0122 ? ? ? ? ? ? 1914 ILE A N +467 C CA . ILE A 59 0.4660 0.2702 0.2661 -0.0010 -0.0380 0.0054 ? ? ? ? ? ? 1914 ILE A CA +468 C C . ILE A 59 0.5118 0.3249 0.3142 0.0011 -0.0420 -0.0067 ? ? ? ? ? ? 1914 ILE A C +469 O O . ILE A 59 0.5119 0.3217 0.3080 0.0018 -0.0328 -0.0122 ? ? ? ? ? ? 1914 ILE A O +470 C CB . ILE A 59 0.4598 0.2687 0.2813 -0.0060 -0.0399 0.0055 ? ? ? ? ? ? 1914 ILE A CB +471 C CG1 . ILE A 59 0.4667 0.2629 0.2816 -0.0165 -0.0378 0.0090 ? ? ? ? ? ? 1914 ILE A CG1 +472 C CG2 . ILE A 59 0.3829 0.2078 0.2243 -0.0046 -0.0359 0.0035 ? ? ? ? ? ? 1914 ILE A CG2 +473 C CD1 . ILE A 59 0.4373 0.2369 0.2574 -0.0205 -0.0456 0.0052 ? ? ? ? ? ? 1914 ILE A CD1 +474 N N . ARG A 60 0.4991 0.3222 0.3113 0.0007 -0.0533 -0.0122 ? ? ? ? ? ? 1915 ARG A N +475 C CA . ARG A 60 0.5024 0.3297 0.3203 -0.0075 -0.0583 -0.0290 ? ? ? ? ? ? 1915 ARG A CA +476 C C . ARG A 60 0.5748 0.4014 0.3559 -0.0050 -0.0656 -0.0400 ? ? ? ? ? ? 1915 ARG A C +477 O O . ARG A 60 0.5393 0.3486 0.3053 -0.0110 -0.0611 -0.0573 ? ? ? ? ? ? 1915 ARG A O +478 C CB . ARG A 60 0.4626 0.3145 0.3111 -0.0143 -0.0680 -0.0316 ? ? ? ? ? ? 1915 ARG A CB +479 C CG . ARG A 60 0.4714 0.3342 0.3307 -0.0331 -0.0779 -0.0537 ? ? ? ? ? ? 1915 ARG A CG +480 C CD . ARG A 60 0.5246 0.3473 0.3874 -0.0457 -0.0601 -0.0633 ? ? ? ? ? ? 1915 ARG A CD +481 N NE . ARG A 60 0.5476 0.3633 0.4408 -0.0478 -0.0445 -0.0494 ? ? ? ? ? ? 1915 ARG A NE +482 C CZ . ARG A 60 0.6266 0.4007 0.5192 -0.0500 -0.0241 -0.0476 ? ? ? ? ? ? 1915 ARG A CZ +483 N NH1 . ARG A 60 0.5839 0.3193 0.4518 -0.0495 -0.0158 -0.0607 ? ? ? ? ? ? 1915 ARG A NH1 +484 N NH2 . ARG A 60 0.5880 0.3542 0.4977 -0.0475 -0.0086 -0.0306 ? ? ? ? ? ? 1915 ARG A NH2 +485 N N . GLU A 61 0.5132 0.3504 0.2703 0.0075 -0.0742 -0.0293 ? ? ? ? ? ? 1916 GLU A N +486 C CA . GLU A 61 0.5432 0.3798 0.2513 0.0156 -0.0820 -0.0362 ? ? ? ? ? ? 1916 GLU A CA +487 C C . GLU A 61 0.5402 0.3460 0.2179 0.0191 -0.0573 -0.0345 ? ? ? ? ? ? 1916 GLU A C +488 O O . GLU A 61 0.5927 0.3860 0.2315 0.0207 -0.0556 -0.0512 ? ? ? ? ? ? 1916 GLU A O +489 C CB . GLU A 61 0.5218 0.3720 0.2045 0.0369 -0.0933 -0.0171 ? ? ? ? ? ? 1916 GLU A CB +490 C CG . GLU A 61 0.6569 0.5061 0.2740 0.0520 -0.1024 -0.0193 ? ? ? ? ? ? 1916 GLU A CG +491 C CD . GLU A 61 0.7974 0.6794 0.4062 0.0410 -0.1329 -0.0506 ? ? ? ? ? ? 1916 GLU A CD +492 O OE1 . GLU A 61 0.7831 0.7062 0.4440 0.0271 -0.1533 -0.0618 ? ? ? ? ? ? 1916 GLU A OE1 +493 O OE2 . GLU A 61 0.8505 0.7186 0.4033 0.0434 -0.1338 -0.0651 ? ? ? ? ? ? 1916 GLU A OE2 +494 N N . LYS A 62 0.5433 0.3400 0.2401 0.0192 -0.0375 -0.0163 ? ? ? ? ? ? 1917 LYS A N +495 C CA . LYS A 62 0.5498 0.3354 0.2389 0.0211 -0.0107 -0.0115 ? ? ? ? ? ? 1917 LYS A CA +496 C C . LYS A 62 0.5556 0.3371 0.2598 0.0205 -0.0018 -0.0280 ? ? ? ? ? ? 1917 LYS A C +497 O O . LYS A 62 0.5774 0.3446 0.2515 0.0301 0.0165 -0.0353 ? ? ? ? ? ? 1917 LYS A O +498 C CB . LYS A 62 0.4864 0.2769 0.2081 0.0129 0.0030 0.0075 ? ? ? ? ? ? 1917 LYS A CB +499 C CG . LYS A 62 0.5621 0.3325 0.2550 0.0149 0.0082 0.0261 ? ? ? ? ? ? 1917 LYS A CG +500 C CD . LYS A 62 0.6198 0.3843 0.3440 -0.0033 0.0199 0.0374 ? ? ? ? ? ? 1917 LYS A CD +501 C CE . LYS A 62 0.5837 0.3673 0.3347 -0.0164 0.0452 0.0426 ? ? ? ? ? ? 1917 LYS A CE +502 N NZ . LYS A 62 0.6141 0.3918 0.3921 -0.0432 0.0554 0.0509 ? ? ? ? ? ? 1917 LYS A NZ +503 N N . LEU A 63 0.5349 0.3214 0.2784 0.0134 -0.0100 -0.0318 ? ? ? ? ? ? 1918 LEU A N +504 C CA . LEU A 63 0.5952 0.3654 0.3499 0.0174 0.0017 -0.0423 ? ? ? ? ? ? 1918 LEU A CA +505 C C . LEU A 63 0.5855 0.3229 0.2981 0.0147 0.0003 -0.0692 ? ? ? ? ? ? 1918 LEU A C +506 O O . LEU A 63 0.6824 0.3902 0.3730 0.0263 0.0218 -0.0793 ? ? ? ? ? ? 1918 LEU A O +507 C CB . LEU A 63 0.5970 0.3703 0.3895 0.0116 -0.0059 -0.0375 ? ? ? ? ? ? 1918 LEU A CB +508 C CG . LEU A 63 0.5575 0.3084 0.3620 0.0234 0.0114 -0.0370 ? ? ? ? ? ? 1918 LEU A CG +509 C CD1 . LEU A 63 0.5559 0.3328 0.3783 0.0433 0.0270 -0.0205 ? ? ? ? ? ? 1918 LEU A CD1 +510 C CD2 . LEU A 63 0.5330 0.2787 0.3608 0.0185 0.0062 -0.0292 ? ? ? ? ? ? 1918 LEU A CD2 +511 N N . SER A 64 0.6048 0.2953 0.2965 -0.0049 -0.0686 -0.0288 ? ? ? ? ? ? 1919 SER A N +512 C CA . SER A 64 0.6727 0.3168 0.3479 -0.0024 -0.0860 -0.0300 ? ? ? ? ? ? 1919 SER A CA +513 C C . SER A 64 0.6920 0.2863 0.3155 0.0038 -0.0916 -0.0344 ? ? ? ? ? ? 1919 SER A C +514 O O . SER A 64 0.7697 0.3206 0.3674 0.0072 -0.1051 -0.0379 ? ? ? ? ? ? 1919 SER A O +515 C CB . SER A 64 0.7247 0.3685 0.4334 -0.0112 -0.1066 -0.0350 ? ? ? ? ? ? 1919 SER A CB +516 O OG . SER A 64 0.7923 0.4832 0.5450 -0.0180 -0.0986 -0.0304 ? ? ? ? ? ? 1919 SER A OG +517 N N . SER A 65 0.6918 0.2921 0.2983 0.0041 -0.0819 -0.0341 ? ? ? ? ? ? 1920 SER A N +518 C CA . SER A 65 0.7556 0.3128 0.3086 0.0068 -0.0858 -0.0354 ? ? ? ? ? ? 1920 SER A CA +519 C C . SER A 65 0.7375 0.3060 0.2659 0.0143 -0.0581 -0.0301 ? ? ? ? ? ? 1920 SER A C +520 O O . SER A 65 0.7771 0.3266 0.2667 0.0135 -0.0540 -0.0277 ? ? ? ? ? ? 1920 SER A O +521 C CB . SER A 65 0.7356 0.2817 0.2904 -0.0028 -0.1050 -0.0357 ? ? ? ? ? ? 1920 SER A CB +522 O OG . SER A 65 0.7107 0.2974 0.3008 -0.0073 -0.0956 -0.0335 ? ? ? ? ? ? 1920 SER A OG +523 N N . GLY A 66 0.7095 0.3116 0.2639 0.0204 -0.0396 -0.0259 ? ? ? ? ? ? 1921 GLY A N +524 C CA . GLY A 66 0.7151 0.3324 0.2590 0.0291 -0.0134 -0.0203 ? ? ? ? ? ? 1921 GLY A CA +525 C C . GLY A 66 0.7065 0.3495 0.2552 0.0227 -0.0028 -0.0128 ? ? ? ? ? ? 1921 GLY A C +526 O O . GLY A 66 0.7360 0.3778 0.2617 0.0273 0.0159 -0.0080 ? ? ? ? ? ? 1921 GLY A O +527 N N . GLN A 67 0.6714 0.3391 0.2531 0.0118 -0.0138 -0.0124 ? ? ? ? ? ? 1922 GLN A N +528 C CA . GLN A 67 0.6889 0.3767 0.2801 0.0043 -0.0083 -0.0059 ? ? ? ? ? ? 1922 GLN A CA +529 C C . GLN A 67 0.6599 0.3978 0.2894 0.0036 0.0056 -0.0003 ? ? ? ? ? ? 1922 GLN A C +530 O O . GLN A 67 0.6337 0.3912 0.2781 -0.0034 0.0085 0.0049 ? ? ? ? ? ? 1922 GLN A O +531 C CB . GLN A 67 0.6730 0.3512 0.2779 -0.0067 -0.0316 -0.0115 ? ? ? ? ? ? 1922 GLN A CB +532 C CG . GLN A 67 0.7456 0.3732 0.3120 -0.0084 -0.0498 -0.0126 ? ? ? ? ? ? 1922 GLN A CG +533 C CD . GLN A 67 0.8112 0.4286 0.3987 -0.0186 -0.0750 -0.0150 ? ? ? ? ? ? 1922 GLN A CD +534 O OE1 . GLN A 67 0.9121 0.5429 0.5178 -0.0256 -0.0755 -0.0099 ? ? ? ? ? ? 1922 GLN A OE1 +535 N NE2 . GLN A 67 0.8624 0.4550 0.4537 -0.0196 -0.0981 -0.0226 ? ? ? ? ? ? 1922 GLN A NE2 +536 N N . TYR A 68 0.6017 0.3588 0.2477 0.0094 0.0111 0.0006 ? ? ? ? ? ? 1923 TYR A N +537 C CA . TYR A 68 0.5763 0.3777 0.2522 0.0094 0.0228 0.0097 ? ? ? ? ? ? 1923 TYR A CA +538 C C . TYR A 68 0.6847 0.4835 0.3540 0.0227 0.0415 0.0188 ? ? ? ? ? ? 1923 TYR A C +539 O O . TYR A 68 0.6485 0.4277 0.3092 0.0326 0.0420 0.0169 ? ? ? ? ? ? 1923 TYR A O +540 C CB . TYR A 68 0.5486 0.3791 0.2506 0.0044 0.0148 0.0084 ? ? ? ? ? ? 1923 TYR A CB +541 C CG . TYR A 68 0.5586 0.4012 0.2739 -0.0073 0.0018 -0.0043 ? ? ? ? ? ? 1923 TYR A CG +542 C CD1 . TYR A 68 0.5235 0.3843 0.2524 -0.0149 0.0002 -0.0082 ? ? ? ? ? ? 1923 TYR A CD1 +543 C CD2 . TYR A 68 0.5285 0.3640 0.2479 -0.0101 -0.0090 -0.0135 ? ? ? ? ? ? 1923 TYR A CD2 +544 C CE1 . TYR A 68 0.5120 0.3811 0.2571 -0.0232 -0.0117 -0.0244 ? ? ? ? ? ? 1923 TYR A CE1 +545 C CE2 . TYR A 68 0.5335 0.3823 0.2713 -0.0183 -0.0181 -0.0284 ? ? ? ? ? ? 1923 TYR A CE2 +546 C CZ . TYR A 68 0.5088 0.3732 0.2589 -0.0238 -0.0192 -0.0355 ? ? ? ? ? ? 1923 TYR A CZ +547 O OH . TYR A 68 0.5013 0.3762 0.2737 -0.0296 -0.0284 -0.0544 ? ? ? ? ? ? 1923 TYR A OH +548 N N . PRO A 69 0.5966 0.4150 0.2749 0.0234 0.0567 0.0281 ? ? ? ? ? ? 1924 PRO A N +549 C CA . PRO A 69 0.6162 0.4369 0.2961 0.0381 0.0781 0.0349 ? ? ? ? ? ? 1924 PRO A CA +550 C C . PRO A 69 0.6932 0.5453 0.4134 0.0438 0.0789 0.0442 ? ? ? ? ? ? 1924 PRO A C +551 O O . PRO A 69 0.6541 0.5031 0.3828 0.0591 0.0928 0.0472 ? ? ? ? ? ? 1924 PRO A O +552 C CB . PRO A 69 0.6727 0.5111 0.3575 0.0336 0.0934 0.0445 ? ? ? ? ? ? 1924 PRO A CB +553 C CG . PRO A 69 0.7023 0.5588 0.4051 0.0160 0.0761 0.0457 ? ? ? ? ? ? 1924 PRO A CG +554 C CD . PRO A 69 0.7009 0.5339 0.3881 0.0111 0.0546 0.0317 ? ? ? ? ? ? 1924 PRO A CD +555 N N . ASN A 70 0.4315 0.4773 0.4474 -0.0358 0.0433 -0.0702 ? ? ? ? ? ? 1925 ASN A N +556 C CA . ASN A 70 0.4714 0.4996 0.4763 0.0139 0.0064 -0.0819 ? ? ? ? ? ? 1925 ASN A CA +557 C C . ASN A 70 0.5267 0.4946 0.4568 0.0472 -0.0018 -0.0448 ? ? ? ? ? ? 1925 ASN A C +558 O O . ASN A 70 0.4838 0.4307 0.3776 0.0312 0.0198 -0.0159 ? ? ? ? ? ? 1925 ASN A O +559 C CB . ASN A 70 0.4381 0.5189 0.4946 0.0198 -0.0205 -0.1458 ? ? ? ? ? ? 1925 ASN A CB +560 C CG . ASN A 70 0.5050 0.6016 0.5610 -0.0002 -0.0158 -0.1643 ? ? ? ? ? ? 1925 ASN A CG +561 O OD1 . ASN A 70 0.5318 0.5851 0.5317 0.0105 -0.0139 -0.1350 ? ? ? ? ? ? 1925 ASN A OD1 +562 N ND2 . ASN A 70 0.4676 0.6274 0.5879 -0.0300 -0.0136 -0.2145 ? ? ? ? ? ? 1925 ASN A ND2 +563 N N . LEU A 71 0.4852 0.4256 0.3905 0.0947 -0.0338 -0.0468 ? ? ? ? ? ? 1926 LEU A N +564 C CA . LEU A 71 0.5380 0.4234 0.3683 0.1321 -0.0447 -0.0156 ? ? ? ? ? ? 1926 LEU A CA +565 C C . LEU A 71 0.5436 0.4346 0.3544 0.1281 -0.0453 -0.0276 ? ? ? ? ? ? 1926 LEU A C +566 O O . LEU A 71 0.5993 0.4542 0.3537 0.1323 -0.0308 0.0098 ? ? ? ? ? ? 1926 LEU A O +567 C CB . LEU A 71 0.6675 0.5310 0.4802 0.1844 -0.0862 -0.0315 ? ? ? ? ? ? 1926 LEU A CB +568 C CG . LEU A 71 0.7550 0.5819 0.5549 0.2042 -0.0922 -0.0045 ? ? ? ? ? ? 1926 LEU A CG +569 C CD1 . LEU A 71 0.8475 0.6409 0.6123 0.2603 -0.1361 -0.0174 ? ? ? ? ? ? 1926 LEU A CD1 +570 C CD2 . LEU A 71 0.8658 0.6447 0.6129 0.1951 -0.0593 0.0605 ? ? ? ? ? ? 1926 LEU A CD2 +571 N N . GLU A 72 0.5715 0.5093 0.4320 0.1217 -0.0641 -0.0830 ? ? ? ? ? ? 1927 GLU A N +572 C CA . GLU A 72 0.5779 0.5240 0.4307 0.1197 -0.0720 -0.1047 ? ? ? ? ? ? 1927 GLU A CA +573 C C . GLU A 72 0.5730 0.5093 0.4077 0.0802 -0.0371 -0.0756 ? ? ? ? ? ? 1927 GLU A C +574 O O . GLU A 72 0.5537 0.4621 0.3419 0.0926 -0.0399 -0.0625 ? ? ? ? ? ? 1927 GLU A O +575 C CB . GLU A 72 0.6153 0.6239 0.5431 0.1064 -0.0911 -0.1718 ? ? ? ? ? ? 1927 GLU A CB +576 C CG . GLU A 72 0.8258 0.8469 0.7580 0.0993 -0.1005 -0.2004 ? ? ? ? ? ? 1927 GLU A CG +577 N N . THR A 73 0.5470 0.5041 0.4151 0.0354 -0.0062 -0.0664 ? ? ? ? ? ? 1928 THR A N +578 C CA . THR A 73 0.4955 0.4412 0.3461 -0.0018 0.0240 -0.0418 ? ? ? ? ? ? 1928 THR A CA +579 C C . THR A 73 0.5349 0.4277 0.3179 0.0150 0.0389 0.0147 ? ? ? ? ? ? 1928 THR A C +580 O O . THR A 73 0.5398 0.4114 0.2889 0.0049 0.0508 0.0327 ? ? ? ? ? ? 1928 THR A O +581 C CB . THR A 73 0.4250 0.4065 0.3250 -0.0531 0.0524 -0.0485 ? ? ? ? ? ? 1928 THR A CB +582 O OG1 . THR A 73 0.5080 0.4871 0.4154 -0.0486 0.0618 -0.0272 ? ? ? ? ? ? 1928 THR A OG1 +583 C CG2 . THR A 73 0.3993 0.4391 0.3670 -0.0741 0.0425 -0.1057 ? ? ? ? ? ? 1928 THR A CG2 +584 N N . PHE A 74 0.5646 0.3316 0.2618 -0.0301 0.0485 -0.0061 ? ? ? ? ? ? 1929 PHE A N +585 C CA . PHE A 74 0.5491 0.3251 0.2601 -0.0229 0.0348 -0.0180 ? ? ? ? ? ? 1929 PHE A CA +586 C C . PHE A 74 0.6157 0.4065 0.3437 -0.0182 0.0268 -0.0127 ? ? ? ? ? ? 1929 PHE A C +587 O O . PHE A 74 0.5543 0.3386 0.2761 -0.0130 0.0104 -0.0174 ? ? ? ? ? ? 1929 PHE A O +588 C CB . PHE A 74 0.5645 0.3486 0.3036 -0.0227 0.0548 -0.0283 ? ? ? ? ? ? 1929 PHE A CB +589 C CG . PHE A 74 0.4998 0.2935 0.2719 -0.0189 0.0558 -0.0403 ? ? ? ? ? ? 1929 PHE A CG +590 C CD1 . PHE A 74 0.5029 0.3076 0.2841 -0.0216 0.0370 -0.0672 ? ? ? ? ? ? 1929 PHE A CD1 +591 C CD2 . PHE A 74 0.4529 0.2497 0.2464 -0.0064 0.0787 -0.0252 ? ? ? ? ? ? 1929 PHE A CD2 +592 C CE1 . PHE A 74 0.4579 0.2769 0.2836 -0.0213 0.0436 -0.0812 ? ? ? ? ? ? 1929 PHE A CE1 +593 C CE2 . PHE A 74 0.4903 0.2868 0.3147 -0.0010 0.0906 -0.0325 ? ? ? ? ? ? 1929 PHE A CE2 +594 C CZ . PHE A 74 0.5045 0.3123 0.3525 -0.0132 0.0747 -0.0618 ? ? ? ? ? ? 1929 PHE A CZ +595 N N . ALA A 75 0.5479 0.3644 0.2934 -0.0140 0.0373 -0.0050 ? ? ? ? ? ? 1930 ALA A N +596 C CA . ALA A 75 0.5326 0.3743 0.2874 -0.0025 0.0267 -0.0066 ? ? ? ? ? ? 1930 ALA A CA +597 C C . ALA A 75 0.5248 0.3534 0.2712 -0.0180 0.0099 -0.0174 ? ? ? ? ? ? 1930 ALA A C +598 O O . ALA A 75 0.5468 0.3755 0.2903 -0.0108 -0.0030 -0.0243 ? ? ? ? ? ? 1930 ALA A O +599 C CB . ALA A 75 0.5136 0.4026 0.2828 0.0147 0.0364 -0.0018 ? ? ? ? ? ? 1930 ALA A CB +600 N N . LEU A 76 0.5911 0.3997 0.3323 -0.0377 0.0184 -0.0181 ? ? ? ? ? ? 1931 LEU A N +601 C CA . LEU A 76 0.6182 0.3946 0.3528 -0.0541 0.0200 -0.0270 ? ? ? ? ? ? 1931 LEU A CA +602 C C . LEU A 76 0.6446 0.3746 0.3419 -0.0414 0.0111 -0.0210 ? ? ? ? ? ? 1931 LEU A C +603 O O . LEU A 76 0.6124 0.3233 0.3062 -0.0438 0.0082 -0.0297 ? ? ? ? ? ? 1931 LEU A O +604 C CB . LEU A 76 0.6987 0.4455 0.4305 -0.0728 0.0463 -0.0220 ? ? ? ? ? ? 1931 LEU A CB +605 C CG . LEU A 76 0.8144 0.6146 0.5990 -0.0911 0.0578 -0.0364 ? ? ? ? ? ? 1931 LEU A CG +606 C CD1 . LEU A 76 0.8747 0.6378 0.6587 -0.1087 0.0935 -0.0274 ? ? ? ? ? ? 1931 LEU A CD1 +607 C CD2 . LEU A 76 0.8739 0.7145 0.7025 -0.1062 0.0478 -0.0702 ? ? ? ? ? ? 1931 LEU A CD2 +608 N N . ASP A 77 0.5992 0.3174 0.2707 -0.0258 0.0065 -0.0110 ? ? ? ? ? ? 1932 ASP A N +609 C CA . ASP A 77 0.6270 0.3221 0.2671 -0.0051 -0.0063 -0.0086 ? ? ? ? ? ? 1932 ASP A CA +610 C C . ASP A 77 0.5628 0.2847 0.2273 0.0035 -0.0213 -0.0160 ? ? ? ? ? ? 1932 ASP A C +611 O O . ASP A 77 0.5691 0.2700 0.2162 0.0157 -0.0277 -0.0151 ? ? ? ? ? ? 1932 ASP A O +612 C CB . ASP A 77 0.6125 0.3143 0.2290 0.0122 -0.0140 -0.0097 ? ? ? ? ? ? 1932 ASP A CB +613 C CG . ASP A 77 0.6747 0.3288 0.2298 0.0290 -0.0012 0.0045 ? ? ? ? ? ? 1932 ASP A CG +614 O OD1 . ASP A 77 0.7730 0.3761 0.3102 0.0225 0.0230 0.0180 ? ? ? ? ? ? 1932 ASP A OD1 +615 O OD2 . ASP A 77 0.6836 0.3495 0.2072 0.0517 -0.0112 -0.0005 ? ? ? ? ? ? 1932 ASP A OD2 +616 N N . VAL A 78 0.4379 0.3036 0.2476 0.0313 -0.0191 0.0152 ? ? ? ? ? ? 1933 VAL A N +617 C CA . VAL A 78 0.4338 0.2859 0.2373 0.0247 -0.0186 0.0129 ? ? ? ? ? ? 1933 VAL A CA +618 C C . VAL A 78 0.4840 0.3284 0.2793 0.0198 -0.0215 0.0172 ? ? ? ? ? ? 1933 VAL A C +619 O O . VAL A 78 0.5009 0.3348 0.2884 0.0149 -0.0170 0.0160 ? ? ? ? ? ? 1933 VAL A O +620 C CB . VAL A 78 0.4509 0.2860 0.2452 0.0258 -0.0167 0.0125 ? ? ? ? ? ? 1933 VAL A CB +621 C CG1 . VAL A 78 0.4988 0.2992 0.2683 0.0210 -0.0062 0.0136 ? ? ? ? ? ? 1933 VAL A CG1 +622 C CG2 . VAL A 78 0.4373 0.2800 0.2479 0.0279 -0.0118 0.0030 ? ? ? ? ? ? 1933 VAL A CG2 +623 N N . ARG A 79 0.4693 0.3215 0.2741 0.0217 -0.0294 0.0172 ? ? ? ? ? ? 1934 ARG A N +624 C CA . ARG A 79 0.4629 0.3113 0.2681 0.0196 -0.0377 0.0133 ? ? ? ? ? ? 1934 ARG A CA +625 C C . ARG A 79 0.4983 0.3517 0.3146 0.0114 -0.0269 0.0147 ? ? ? ? ? ? 1934 ARG A C +626 O O . ARG A 79 0.5035 0.3481 0.3130 0.0075 -0.0297 0.0123 ? ? ? ? ? ? 1934 ARG A O +627 C CB . ARG A 79 0.4473 0.3108 0.2786 0.0259 -0.0529 0.0017 ? ? ? ? ? ? 1934 ARG A CB +628 C CG . ARG A 79 0.5368 0.3831 0.3417 0.0417 -0.0697 -0.0004 ? ? ? ? ? ? 1934 ARG A CG +629 C CD . ARG A 79 0.5386 0.4082 0.3808 0.0528 -0.0886 -0.0175 ? ? ? ? ? ? 1934 ARG A CD +630 N NE . ARG A 79 0.6002 0.4425 0.4026 0.0746 -0.1070 -0.0180 ? ? ? ? ? ? 1934 ARG A NE +631 C CZ . ARG A 79 0.6484 0.5052 0.4737 0.0878 -0.1203 -0.0287 ? ? ? ? ? ? 1934 ARG A CZ +632 N NH1 . ARG A 79 0.5504 0.4519 0.4452 0.0782 -0.1132 -0.0412 ? ? ? ? ? ? 1934 ARG A NH1 +633 N NH2 . ARG A 79 0.6762 0.4951 0.4505 0.1119 -0.1365 -0.0270 ? ? ? ? ? ? 1934 ARG A NH2 +634 N N . LEU A 80 0.4479 0.3065 0.2710 0.0121 -0.0136 0.0189 ? ? ? ? ? ? 1935 LEU A N +635 C CA . LEU A 80 0.4804 0.3277 0.2965 0.0107 0.0002 0.0230 ? ? ? ? ? ? 1935 LEU A CA +636 C C . LEU A 80 0.5333 0.3719 0.3301 0.0129 -0.0049 0.0233 ? ? ? ? ? ? 1935 LEU A C +637 O O . LEU A 80 0.4765 0.3051 0.2692 0.0096 -0.0004 0.0240 ? ? ? ? ? ? 1935 LEU A O +638 C CB . LEU A 80 0.4799 0.3155 0.2807 0.0208 0.0158 0.0290 ? ? ? ? ? ? 1935 LEU A CB +639 C CG . LEU A 80 0.4921 0.2961 0.2597 0.0299 0.0312 0.0360 ? ? ? ? ? ? 1935 LEU A CG +640 C CD1 . LEU A 80 0.5264 0.3171 0.3122 0.0159 0.0528 0.0363 ? ? ? ? ? ? 1935 LEU A CD1 +641 C CD2 . LEU A 80 0.5157 0.2933 0.2436 0.0496 0.0433 0.0418 ? ? ? ? ? ? 1935 LEU A CD2 +642 N N . VAL A 81 0.4541 0.2968 0.2469 0.0170 -0.0113 0.0191 ? ? ? ? ? ? 1936 VAL A N +643 C CA . VAL A 81 0.4711 0.3103 0.2635 0.0165 -0.0117 0.0117 ? ? ? ? ? ? 1936 VAL A CA +644 C C . VAL A 81 0.5379 0.3649 0.3239 0.0062 -0.0090 0.0131 ? ? ? ? ? ? 1936 VAL A C +645 O O . VAL A 81 0.4820 0.3036 0.2667 0.0050 -0.0061 0.0103 ? ? ? ? ? ? 1936 VAL A O +646 C CB . VAL A 81 0.4790 0.3237 0.2852 0.0166 -0.0106 0.0003 ? ? ? ? ? ? 1936 VAL A CB +647 C CG1 . VAL A 81 0.4216 0.2627 0.2428 0.0110 -0.0022 -0.0131 ? ? ? ? ? ? 1936 VAL A CG1 +648 C CG2 . VAL A 81 0.4144 0.2728 0.2280 0.0310 -0.0190 -0.0082 ? ? ? ? ? ? 1936 VAL A CG2 +649 N N . PHE A 82 0.4821 0.3009 0.2584 0.0033 -0.0131 0.0155 ? ? ? ? ? ? 1937 PHE A N +650 C CA . PHE A 82 0.4827 0.2802 0.2376 0.0007 -0.0145 0.0142 ? ? ? ? ? ? 1937 PHE A CA +651 C C . PHE A 82 0.5163 0.3206 0.2818 -0.0016 -0.0229 0.0113 ? ? ? ? ? ? 1937 PHE A C +652 O O . PHE A 82 0.5282 0.3185 0.2808 -0.0039 -0.0231 0.0080 ? ? ? ? ? ? 1937 PHE A O +653 C CB . PHE A 82 0.4952 0.2670 0.2182 0.0080 -0.0189 0.0151 ? ? ? ? ? ? 1937 PHE A CB +654 C CG . PHE A 82 0.5580 0.3163 0.2756 0.0067 -0.0019 0.0162 ? ? ? ? ? ? 1937 PHE A CG +655 C CD1 . PHE A 82 0.5301 0.2841 0.2612 -0.0021 0.0192 0.0098 ? ? ? ? ? ? 1937 PHE A CD1 +656 C CD2 . PHE A 82 0.5609 0.3150 0.2723 0.0136 -0.0058 0.0186 ? ? ? ? ? ? 1937 PHE A CD2 +657 C CE1 . PHE A 82 0.5648 0.3109 0.3099 -0.0064 0.0386 0.0026 ? ? ? ? ? ? 1937 PHE A CE1 +658 C CE2 . PHE A 82 0.6261 0.3662 0.3400 0.0100 0.0140 0.0164 ? ? ? ? ? ? 1937 PHE A CE2 +659 C CZ . PHE A 82 0.5869 0.3244 0.3222 -0.0014 0.0373 0.0067 ? ? ? ? ? ? 1937 PHE A CZ +660 N N . ASP A 83 0.4960 0.3194 0.2894 -0.0024 -0.0253 0.0098 ? ? ? ? ? ? 1938 ASP A N +661 C CA . ASP A 83 0.5226 0.3523 0.3427 -0.0091 -0.0228 0.0024 ? ? ? ? ? ? 1938 ASP A CA +662 C C . ASP A 83 0.5649 0.3822 0.3775 -0.0129 -0.0067 0.0090 ? ? ? ? ? ? 1938 ASP A C +663 O O . ASP A 83 0.4929 0.3032 0.3121 -0.0188 -0.0051 0.0030 ? ? ? ? ? ? 1938 ASP A O +664 C CB . ASP A 83 0.5111 0.3582 0.3697 -0.0119 -0.0154 -0.0028 ? ? ? ? ? ? 1938 ASP A CB +665 C CG . ASP A 83 0.5785 0.4424 0.4568 -0.0053 -0.0371 -0.0172 ? ? ? ? ? ? 1938 ASP A CG +666 O OD1 . ASP A 83 0.5093 0.3629 0.3618 0.0047 -0.0602 -0.0236 ? ? ? ? ? ? 1938 ASP A OD1 +667 O OD2 . ASP A 83 0.5160 0.3973 0.4301 -0.0065 -0.0304 -0.0234 ? ? ? ? ? ? 1938 ASP A OD2 +668 N N . ASN A 84 0.5161 0.3285 0.3133 -0.0057 0.0018 0.0183 ? ? ? ? ? ? 1939 ASN A N +669 C CA . ASN A 84 0.5625 0.3581 0.3431 0.0000 0.0100 0.0220 ? ? ? ? ? ? 1939 ASN A CA +670 C C . ASN A 84 0.5528 0.3461 0.3285 -0.0030 0.0039 0.0162 ? ? ? ? ? ? 1939 ASN A C +671 O O . ASN A 84 0.5340 0.3143 0.3054 -0.0040 0.0089 0.0154 ? ? ? ? ? ? 1939 ASN A O +672 C CB . ASN A 84 0.4680 0.2594 0.2293 0.0178 0.0087 0.0249 ? ? ? ? ? ? 1939 ASN A CB +673 C CG . ASN A 84 0.5388 0.3144 0.2857 0.0256 0.0224 0.0333 ? ? ? ? ? ? 1939 ASN A CG +674 O OD1 . ASN A 84 0.5172 0.2816 0.2753 0.0149 0.0415 0.0365 ? ? ? ? ? ? 1939 ASN A OD1 +675 N ND2 . ASN A 84 0.5097 0.2812 0.2335 0.0452 0.0154 0.0330 ? ? ? ? ? ? 1939 ASN A ND2 +676 N N . CYS A 85 0.5390 0.3383 0.3127 -0.0044 -0.0016 0.0121 ? ? ? ? ? ? 1940 CYS A N +677 C CA . CYS A 85 0.5175 0.3059 0.2835 -0.0079 0.0027 0.0058 ? ? ? ? ? ? 1940 CYS A CA +678 C C . CYS A 85 0.5534 0.3270 0.3065 -0.0135 -0.0001 0.0044 ? ? ? ? ? ? 1940 CYS A C +679 O O . CYS A 85 0.5661 0.3289 0.3143 -0.0154 0.0055 0.0006 ? ? ? ? ? ? 1940 CYS A O +680 C CB . CYS A 85 0.5181 0.2995 0.2774 -0.0097 0.0093 0.0025 ? ? ? ? ? ? 1940 CYS A CB +681 S SG . CYS A 85 0.5454 0.2995 0.2930 -0.0160 0.0312 -0.0066 ? ? ? ? ? ? 1940 CYS A SG +682 N N . GLU A 86 0.5174 0.2928 0.2700 -0.0138 -0.0118 0.0027 ? ? ? ? ? ? 1941 GLU A N +683 C CA . GLU A 86 0.5642 0.3302 0.3120 -0.0150 -0.0224 -0.0074 ? ? ? ? ? ? 1941 GLU A CA +684 C C . GLU A 86 0.5890 0.3603 0.3647 -0.0230 -0.0145 -0.0106 ? ? ? ? ? ? 1941 GLU A C +685 O O . GLU A 86 0.5495 0.3093 0.3208 -0.0255 -0.0168 -0.0190 ? ? ? ? ? ? 1941 GLU A O +686 C CB . GLU A 86 0.6149 0.3886 0.3693 -0.0082 -0.0440 -0.0184 ? ? ? ? ? ? 1941 GLU A CB +687 C CG . GLU A 86 0.6297 0.3788 0.3361 0.0060 -0.0536 -0.0160 ? ? ? ? ? ? 1941 GLU A CG +688 C CD . GLU A 86 0.6721 0.4182 0.3706 0.0230 -0.0860 -0.0345 ? ? ? ? ? ? 1941 GLU A CD +689 O OE1 . GLU A 86 0.6873 0.4342 0.3944 0.0264 -0.1028 -0.0532 ? ? ? ? ? ? 1941 GLU A OE1 +690 O OE2 . GLU A 86 0.7424 0.4857 0.4286 0.0357 -0.0977 -0.0343 ? ? ? ? ? ? 1941 GLU A OE2 +691 N N . THR A 87 0.5378 0.3175 0.3348 -0.0252 -0.0020 -0.0038 ? ? ? ? ? ? 1942 THR A N +692 C CA . THR A 87 0.5072 0.2743 0.3188 -0.0310 0.0155 -0.0037 ? ? ? ? ? ? 1942 THR A CA +693 C C . THR A 87 0.5701 0.3178 0.3566 -0.0258 0.0214 0.0017 ? ? ? ? ? ? 1942 THR A C +694 O O . THR A 87 0.5430 0.2747 0.3343 -0.0308 0.0302 -0.0025 ? ? ? ? ? ? 1942 THR A O +695 C CB . THR A 87 0.5028 0.2629 0.3198 -0.0289 0.0356 0.0061 ? ? ? ? ? ? 1942 THR A CB +696 O OG1 . THR A 87 0.5373 0.3181 0.3918 -0.0363 0.0342 -0.0041 ? ? ? ? ? ? 1942 THR A OG1 +697 C CG2 . THR A 87 0.5361 0.2612 0.3491 -0.0314 0.0639 0.0102 ? ? ? ? ? ? 1942 THR A CG2 +698 N N . PHE A 88 0.5319 0.2831 0.3002 -0.0156 0.0168 0.0065 ? ? ? ? ? ? 1943 PHE A N +699 C CA . PHE A 88 0.5991 0.3386 0.3556 -0.0061 0.0199 0.0056 ? ? ? ? ? ? 1943 PHE A CA +700 C C . PHE A 88 0.6044 0.3460 0.3602 -0.0102 0.0179 -0.0040 ? ? ? ? ? ? 1943 PHE A C +701 O O . PHE A 88 0.6236 0.3597 0.3806 -0.0035 0.0210 -0.0100 ? ? ? ? ? ? 1943 PHE A O +702 C CB . PHE A 88 0.5408 0.2840 0.2897 0.0127 0.0155 0.0074 ? ? ? ? ? ? 1943 PHE A CB +703 C CG . PHE A 88 0.5934 0.3157 0.3247 0.0330 0.0145 0.0053 ? ? ? ? ? ? 1943 PHE A CG +704 C CD1 . PHE A 88 0.6036 0.2865 0.3035 0.0426 0.0272 0.0172 ? ? ? ? ? ? 1943 PHE A CD1 +705 C CD2 . PHE A 88 0.5494 0.2859 0.2958 0.0447 0.0035 -0.0113 ? ? ? ? ? ? 1943 PHE A CD2 +706 C CE1 . PHE A 88 0.6842 0.3348 0.3517 0.0689 0.0245 0.0164 ? ? ? ? ? ? 1943 PHE A CE1 +707 C CE2 . PHE A 88 0.5767 0.2944 0.3069 0.0702 -0.0045 -0.0179 ? ? ? ? ? ? 1943 PHE A CE2 +708 C CZ . PHE A 88 0.6842 0.3551 0.3667 0.0851 0.0036 -0.0021 ? ? ? ? ? ? 1943 PHE A CZ +709 N N . ASN A 89 0.5350 0.2771 0.2832 -0.0179 0.0148 -0.0067 ? ? ? ? ? ? 1944 ASN A N +710 C CA . ASN A 89 0.5694 0.2966 0.3016 -0.0202 0.0230 -0.0138 ? ? ? ? ? ? 1944 ASN A CA +711 C C . ASN A 89 0.6123 0.3161 0.3121 -0.0220 0.0167 -0.0173 ? ? ? ? ? ? 1944 ASN A C +712 O O . ASN A 89 0.5993 0.3047 0.2910 -0.0194 0.0015 -0.0175 ? ? ? ? ? ? 1944 ASN A O +713 C CB . ASN A 89 0.6164 0.3469 0.3517 -0.0198 0.0329 -0.0158 ? ? ? ? ? ? 1944 ASN A CB +714 C CG . ASN A 89 0.5703 0.3266 0.3427 -0.0130 0.0326 -0.0227 ? ? ? ? ? ? 1944 ASN A CG +715 O OD1 . ASN A 89 0.5987 0.3603 0.3947 -0.0103 0.0404 -0.0371 ? ? ? ? ? ? 1944 ASN A OD1 +716 N ND2 . ASN A 89 0.5041 0.2763 0.2830 -0.0071 0.0213 -0.0166 ? ? ? ? ? ? 1944 ASN A ND2 +717 N N . GLU A 90 0.6617 0.2709 0.2922 -0.0009 -0.0431 -0.0189 ? ? ? ? ? ? 1945 GLU A N +718 C CA . GLU A 90 0.6969 0.2833 0.2846 -0.0021 -0.0453 -0.0373 ? ? ? ? ? ? 1945 GLU A CA +719 C C . GLU A 90 0.6842 0.2900 0.2597 0.0095 -0.0515 -0.0338 ? ? ? ? ? ? 1945 GLU A C +720 O O . GLU A 90 0.6618 0.2758 0.2550 0.0213 -0.0391 -0.0205 ? ? ? ? ? ? 1945 GLU A O +721 C CB A GLU A 90 0.7491 0.2830 0.3105 0.0061 -0.0212 -0.0437 ? ? ? ? ? ? 1945 GLU A CB +722 C CB B GLU A 90 0.7496 0.2831 0.3113 0.0053 -0.0215 -0.0440 ? ? ? ? ? ? 1945 GLU A CB +723 C CG A GLU A 90 0.8407 0.3404 0.4150 0.0013 -0.0078 -0.0433 ? ? ? ? ? ? 1945 GLU A CG +724 C CG B GLU A 90 0.7861 0.2833 0.3468 -0.0078 -0.0140 -0.0528 ? ? ? ? ? ? 1945 GLU A CG +725 C CD A GLU A 90 1.0169 0.4661 0.5775 0.0165 0.0229 -0.0479 ? ? ? ? ? ? 1945 GLU A CD +726 C CD B GLU A 90 0.8351 0.3297 0.3681 -0.0336 -0.0307 -0.0781 ? ? ? ? ? ? 1945 GLU A CD +727 O OE1 A GLU A 90 1.0741 0.4898 0.5862 0.0113 0.0317 -0.0701 ? ? ? ? ? ? 1945 GLU A OE1 +728 O OE1 B GLU A 90 0.9127 0.4252 0.4165 -0.0358 -0.0473 -0.0906 ? ? ? ? ? ? 1945 GLU A OE1 +729 O OE2 A GLU A 90 1.1134 0.5589 0.7121 0.0342 0.0383 -0.0298 ? ? ? ? ? ? 1945 GLU A OE2 +730 O OE2 B GLU A 90 0.8864 0.3619 0.4274 -0.0522 -0.0275 -0.0848 ? ? ? ? ? ? 1945 GLU A OE2 +731 N N . ASP A 91 0.7341 0.3474 0.2809 0.0059 -0.0707 -0.0454 ? ? ? ? ? ? 1946 ASP A N +732 C CA . ASP A 91 0.7468 0.3653 0.2707 0.0211 -0.0762 -0.0384 ? ? ? ? ? ? 1946 ASP A CA +733 C C . ASP A 91 0.8490 0.4263 0.3389 0.0340 -0.0490 -0.0321 ? ? ? ? ? ? 1946 ASP A C +734 O O . ASP A 91 0.8195 0.3961 0.3115 0.0457 -0.0373 -0.0186 ? ? ? ? ? ? 1946 ASP A O +735 C CB . ASP A 91 0.7500 0.3796 0.2401 0.0189 -0.1045 -0.0505 ? ? ? ? ? ? 1946 ASP A CB +736 C CG . ASP A 91 0.7965 0.4780 0.3315 0.0084 -0.1292 -0.0571 ? ? ? ? ? ? 1946 ASP A CG +737 O OD1 . ASP A 91 0.7169 0.4222 0.3003 0.0060 -0.1226 -0.0493 ? ? ? ? ? ? 1946 ASP A OD1 +738 O OD2 . ASP A 91 0.8463 0.5483 0.3685 0.0011 -0.1548 -0.0722 ? ? ? ? ? ? 1946 ASP A OD2 +739 N N . ASP A 92 0.8167 0.3564 0.2763 0.0298 -0.0345 -0.0444 ? ? ? ? ? ? 1947 ASP A N +740 C CA . ASP A 92 0.9132 0.4127 0.3425 0.0403 -0.0021 -0.0427 ? ? ? ? ? ? 1947 ASP A CA +741 C C . ASP A 92 0.8321 0.3366 0.3186 0.0465 0.0237 -0.0331 ? ? ? ? ? ? 1947 ASP A C +742 O O . ASP A 92 0.8541 0.3316 0.3453 0.0484 0.0445 -0.0403 ? ? ? ? ? ? 1947 ASP A O +743 C CB . ASP A 92 0.9411 0.3954 0.3089 0.0328 0.0058 -0.0644 ? ? ? ? ? ? 1947 ASP A CB +744 C CG . ASP A 92 1.0843 0.4946 0.4086 0.0425 0.0428 -0.0653 ? ? ? ? ? ? 1947 ASP A CG +745 O OD1 . ASP A 92 1.0182 0.4348 0.3585 0.0540 0.0603 -0.0481 ? ? ? ? ? ? 1947 ASP A OD1 +746 O OD2 . ASP A 92 1.1634 0.5412 0.4503 0.0350 0.0566 -0.0822 ? ? ? ? ? ? 1947 ASP A OD2 +747 N N . SER A 93 0.7999 0.3407 0.3316 0.0502 0.0215 -0.0178 ? ? ? ? ? ? 1948 SER A N +748 C CA . SER A 93 0.7836 0.3439 0.3725 0.0559 0.0399 -0.0079 ? ? ? ? ? ? 1948 SER A CA +749 C C . SER A 93 0.6889 0.2767 0.2998 0.0558 0.0427 0.0019 ? ? ? ? ? ? 1948 SER A C +750 O O . SER A 93 0.7197 0.3107 0.3088 0.0533 0.0277 0.0033 ? ? ? ? ? ? 1948 SER A O +751 C CB . SER A 93 0.7489 0.3332 0.3822 0.0514 0.0248 -0.0029 ? ? ? ? ? ? 1948 SER A CB +752 O OG . SER A 93 0.6493 0.2695 0.2976 0.0404 -0.0007 0.0011 ? ? ? ? ? ? 1948 SER A OG +753 N N . ASP A 94 0.6936 0.3018 0.3511 0.0586 0.0627 0.0073 ? ? ? ? ? ? 1949 ASP A N +754 C CA . ASP A 94 0.6483 0.2801 0.3294 0.0526 0.0697 0.0119 ? ? ? ? ? ? 1949 ASP A CA +755 C C . ASP A 94 0.6349 0.3011 0.3356 0.0423 0.0423 0.0138 ? ? ? ? ? ? 1949 ASP A C +756 O O . ASP A 94 0.6226 0.2847 0.3112 0.0388 0.0422 0.0141 ? ? ? ? ? ? 1949 ASP A O +757 C CB . ASP A 94 0.6801 0.3424 0.4208 0.0527 0.0921 0.0131 ? ? ? ? ? ? 1949 ASP A CB +758 C CG . ASP A 94 0.8270 0.4565 0.5538 0.0611 0.1303 0.0087 ? ? ? ? ? ? 1949 ASP A CG +759 O OD1 . ASP A 94 0.7538 0.3596 0.4553 0.0565 0.1554 0.0079 ? ? ? ? ? ? 1949 ASP A OD1 +760 O OD2 . ASP A 94 0.9217 0.5447 0.6619 0.0722 0.1393 0.0060 ? ? ? ? ? ? 1949 ASP A OD2 +761 N N . ILE A 95 0.5754 0.2699 0.3035 0.0382 0.0226 0.0157 ? ? ? ? ? ? 1950 ILE A N +762 C CA . ILE A 95 0.5564 0.2841 0.3011 0.0256 0.0014 0.0155 ? ? ? ? ? ? 1950 ILE A CA +763 C C . ILE A 95 0.6088 0.3209 0.3189 0.0247 -0.0143 0.0103 ? ? ? ? ? ? 1950 ILE A C +764 O O . ILE A 95 0.5735 0.3000 0.2888 0.0191 -0.0207 0.0072 ? ? ? ? ? ? 1950 ILE A O +765 C CB . ILE A 95 0.5855 0.3434 0.3599 0.0211 -0.0133 0.0226 ? ? ? ? ? ? 1950 ILE A CB +766 C CG1 . ILE A 95 0.5492 0.3409 0.3691 0.0230 -0.0048 0.0281 ? ? ? ? ? ? 1950 ILE A CG1 +767 C CG2 . ILE A 95 0.5971 0.3807 0.3732 0.0053 -0.0325 0.0207 ? ? ? ? ? ? 1950 ILE A CG2 +768 C CD1 . ILE A 95 0.5795 0.3987 0.4246 0.0255 -0.0219 0.0414 ? ? ? ? ? ? 1950 ILE A CD1 +769 N N . GLY A 96 0.6252 0.3097 0.3037 0.0299 -0.0193 0.0071 ? ? ? ? ? ? 1951 GLY A N +770 C CA . GLY A 96 0.6116 0.2894 0.2611 0.0290 -0.0371 -0.0001 ? ? ? ? ? ? 1951 GLY A CA +771 C C . GLY A 96 0.7012 0.3677 0.3282 0.0394 -0.0348 0.0026 ? ? ? ? ? ? 1951 GLY A C +772 O O . GLY A 96 0.6510 0.3354 0.2856 0.0403 -0.0491 0.0011 ? ? ? ? ? ? 1951 GLY A O +773 N N . ARG A 97 0.6723 0.3063 0.2726 0.0486 -0.0137 0.0077 ? ? ? ? ? ? 1952 ARG A N +774 C CA . ARG A 97 0.7080 0.3186 0.2785 0.0598 -0.0067 0.0157 ? ? ? ? ? ? 1952 ARG A CA +775 C C . ARG A 97 0.6532 0.2819 0.2632 0.0559 0.0016 0.0190 ? ? ? ? ? ? 1952 ARG A C +776 O O . ARG A 97 0.6859 0.3071 0.2872 0.0654 -0.0040 0.0240 ? ? ? ? ? ? 1952 ARG A O +777 C CB . ARG A 97 0.7201 0.2869 0.2501 0.0660 0.0221 0.0206 ? ? ? ? ? ? 1952 ARG A CB +778 C CG . ARG A 97 0.8602 0.3962 0.3279 0.0712 0.0148 0.0155 ? ? ? ? ? ? 1952 ARG A CG +779 C CD . ARG A 97 0.9027 0.3907 0.3213 0.0760 0.0489 0.0196 ? ? ? ? ? ? 1952 ARG A CD +780 N NE . ARG A 97 0.8657 0.3574 0.3226 0.0700 0.0787 0.0127 ? ? ? ? ? ? 1952 ARG A NE +781 C CZ . ARG A 97 0.9191 0.4007 0.3699 0.0686 0.0845 0.0005 ? ? ? ? ? ? 1952 ARG A CZ +782 N NH1 . ARG A 97 0.9534 0.4189 0.3569 0.0669 0.0633 -0.0099 ? ? ? ? ? ? 1952 ARG A NH1 +783 N NH2 . ARG A 97 0.9872 0.4760 0.4833 0.0689 0.1122 -0.0028 ? ? ? ? ? ? 1952 ARG A NH2 +784 N N . ALA A 98 0.6050 0.2574 0.2584 0.0426 0.0147 0.0153 ? ? ? ? ? ? 1953 ALA A N +785 C CA . ALA A 98 0.6213 0.2933 0.3109 0.0320 0.0231 0.0120 ? ? ? ? ? ? 1953 ALA A CA +786 C C . ALA A 98 0.5805 0.2741 0.2824 0.0309 0.0029 0.0067 ? ? ? ? ? ? 1953 ALA A C +787 O O . ALA A 98 0.5731 0.2573 0.2806 0.0340 0.0110 0.0057 ? ? ? ? ? ? 1953 ALA A O +788 C CB . ALA A 98 0.5618 0.2712 0.2961 0.0154 0.0291 0.0066 ? ? ? ? ? ? 1953 ALA A CB +789 N N . GLY A 99 0.5830 0.3023 0.2914 0.0262 -0.0190 0.0024 ? ? ? ? ? ? 1954 GLY A N +790 C CA . GLY A 99 0.5429 0.2889 0.2692 0.0219 -0.0342 -0.0053 ? ? ? ? ? ? 1954 GLY A CA +791 C C . GLY A 99 0.5743 0.3068 0.2859 0.0415 -0.0428 -0.0026 ? ? ? ? ? ? 1954 GLY A C +792 O O . GLY A 99 0.5464 0.2882 0.2800 0.0454 -0.0400 -0.0067 ? ? ? ? ? ? 1954 GLY A O +793 N N . HIS A 100 0.6004 0.3108 0.2738 0.0550 -0.0536 0.0042 ? ? ? ? ? ? 1955 HIS A N +794 C CA . HIS A 100 0.6181 0.3190 0.2715 0.0772 -0.0682 0.0110 ? ? ? ? ? ? 1955 HIS A CA +795 C C . HIS A 100 0.6493 0.3154 0.2956 0.0930 -0.0475 0.0236 ? ? ? ? ? ? 1955 HIS A C +796 O O . HIS A 100 0.6697 0.3404 0.3316 0.1100 -0.0540 0.0273 ? ? ? ? ? ? 1955 HIS A O +797 C CB . HIS A 100 0.6945 0.3748 0.2946 0.0853 -0.0832 0.0149 ? ? ? ? ? ? 1955 HIS A CB +798 C CG . HIS A 100 0.7385 0.4490 0.3460 0.0705 -0.1052 -0.0004 ? ? ? ? ? ? 1955 HIS A CG +799 N ND1 . HIS A 100 0.7218 0.4744 0.3556 0.0704 -0.1313 -0.0099 ? ? ? ? ? ? 1955 HIS A ND1 +800 C CD2 . HIS A 100 0.7230 0.4251 0.3191 0.0544 -0.1013 -0.0088 ? ? ? ? ? ? 1955 HIS A CD2 +801 C CE1 . HIS A 100 0.6958 0.4631 0.3311 0.0505 -0.1417 -0.0249 ? ? ? ? ? ? 1955 HIS A CE1 +802 N NE2 . HIS A 100 0.6775 0.4098 0.2875 0.0418 -0.1234 -0.0235 ? ? ? ? ? ? 1955 HIS A NE2 +803 N N . ASN A 101 0.6652 0.2957 0.2925 0.0876 -0.0200 0.0298 ? ? ? ? ? ? 1956 ASN A N +804 C CA . ASN A 101 0.7039 0.2917 0.3228 0.0966 0.0072 0.0406 ? ? ? ? ? ? 1956 ASN A CA +805 C C . ASN A 101 0.6778 0.2829 0.3474 0.0883 0.0186 0.0290 ? ? ? ? ? ? 1956 ASN A C +806 O O . ASN A 101 0.7138 0.2916 0.3849 0.1057 0.0279 0.0365 ? ? ? ? ? ? 1956 ASN A O +807 C CB . ASN A 101 0.7194 0.2767 0.3225 0.0834 0.0394 0.0430 ? ? ? ? ? ? 1956 ASN A CB +808 C CG . ASN A 101 0.8299 0.3496 0.3703 0.0948 0.0414 0.0560 ? ? ? ? ? ? 1956 ASN A CG +809 O OD1 . ASN A 101 0.8855 0.3989 0.3860 0.1126 0.0157 0.0641 ? ? ? ? ? ? 1956 ASN A OD1 +810 N ND2 . ASN A 101 0.8093 0.3078 0.3418 0.0827 0.0727 0.0555 ? ? ? ? ? ? 1956 ASN A ND2 +811 N N . MET A 102 0.5470 0.2688 0.2644 0.0023 0.0138 0.0050 ? ? ? ? ? ? 1957 MET A N +812 C CA . MET A 102 0.5273 0.2765 0.2795 0.0003 0.0000 0.0099 ? ? ? ? ? ? 1957 MET A CA +813 C C . MET A 102 0.5890 0.3390 0.3233 0.0050 -0.0262 0.0155 ? ? ? ? ? ? 1957 MET A C +814 O O . MET A 102 0.5523 0.3040 0.2933 0.0031 -0.0288 0.0191 ? ? ? ? ? ? 1957 MET A O +815 C CB . MET A 102 0.4798 0.2734 0.2908 0.0000 -0.0063 0.0075 ? ? ? ? ? ? 1957 MET A CB +816 C CG . MET A 102 0.6127 0.4222 0.4668 -0.0037 0.0165 0.0017 ? ? ? ? ? ? 1957 MET A CG +817 S SD . MET A 102 0.7378 0.5435 0.6050 -0.0199 0.0399 -0.0088 ? ? ? ? ? ? 1957 MET A SD +818 C CE . MET A 102 0.6630 0.5093 0.5480 -0.0285 0.0121 -0.0150 ? ? ? ? ? ? 1957 MET A CE +819 N N . ARG A 103 0.5532 0.3017 0.2736 0.0092 -0.0411 0.0124 ? ? ? ? ? ? 1958 ARG A N +820 C CA . ARG A 103 0.5915 0.3459 0.3073 0.0129 -0.0644 0.0150 ? ? ? ? ? ? 1958 ARG A CA +821 C C . ARG A 103 0.6116 0.3478 0.2906 0.0199 -0.0693 0.0265 ? ? ? ? ? ? 1958 ARG A C +822 O O . ARG A 103 0.6111 0.3510 0.3056 0.0247 -0.0768 0.0352 ? ? ? ? ? ? 1958 ARG A O +823 C CB . ARG A 103 0.5698 0.3285 0.2873 0.0118 -0.0755 0.0030 ? ? ? ? ? ? 1958 ARG A CB +824 C CG . ARG A 103 0.5778 0.3516 0.3121 0.0134 -0.0970 0.0022 ? ? ? ? ? ? 1958 ARG A CG +825 C CD . ARG A 103 0.5623 0.3408 0.2962 0.0079 -0.1080 -0.0171 ? ? ? ? ? ? 1958 ARG A CD +826 N NE . ARG A 103 0.5556 0.3292 0.3215 0.0018 -0.0900 -0.0273 ? ? ? ? ? ? 1958 ARG A NE +827 C CZ . ARG A 103 0.5862 0.3670 0.3949 0.0016 -0.0853 -0.0233 ? ? ? ? ? ? 1958 ARG A CZ +828 N NH1 . ARG A 103 0.5390 0.3340 0.3631 0.0039 -0.0963 -0.0151 ? ? ? ? ? ? 1958 ARG A NH1 +829 N NH2 . ARG A 103 0.5120 0.2812 0.3494 0.0003 -0.0635 -0.0254 ? ? ? ? ? ? 1958 ARG A NH2 +830 N N . LYS A 104 0.6302 0.3448 0.2594 0.0220 -0.0618 0.0287 ? ? ? ? ? ? 1959 LYS A N +831 C CA . LYS A 104 0.6481 0.3436 0.2313 0.0341 -0.0652 0.0496 ? ? ? ? ? ? 1959 LYS A CA +832 C C . LYS A 104 0.6873 0.3628 0.2922 0.0364 -0.0403 0.0657 ? ? ? ? ? ? 1959 LYS A C +833 O O . LYS A 104 0.7014 0.3684 0.3097 0.0491 -0.0444 0.0856 ? ? ? ? ? ? 1959 LYS A O +834 C CB . LYS A 104 0.7007 0.3735 0.2126 0.0337 -0.0543 0.0494 ? ? ? ? ? ? 1959 LYS A CB +835 C CG . LYS A 104 0.8488 0.5102 0.3116 0.0497 -0.0575 0.0780 ? ? ? ? ? ? 1959 LYS A CG +836 C CD . LYS A 104 0.9248 0.6347 0.3935 0.0573 -0.0990 0.0775 ? ? ? ? ? ? 1959 LYS A CD +837 N N . TYR A 105 0.6488 0.3193 0.2783 0.0236 -0.0122 0.0545 ? ? ? ? ? ? 1960 TYR A N +838 C CA . TYR A 105 0.6885 0.3442 0.3491 0.0176 0.0165 0.0576 ? ? ? ? ? ? 1960 TYR A CA +839 C C . TYR A 105 0.6848 0.3589 0.3893 0.0160 0.0049 0.0531 ? ? ? ? ? ? 1960 TYR A C +840 O O . TYR A 105 0.6336 0.2832 0.3486 0.0206 0.0217 0.0647 ? ? ? ? ? ? 1960 TYR A O +841 C CB . TYR A 105 0.5946 0.2630 0.2911 0.0007 0.0400 0.0378 ? ? ? ? ? ? 1960 TYR A CB +842 C CG . TYR A 105 0.7147 0.3684 0.4467 -0.0118 0.0761 0.0324 ? ? ? ? ? ? 1960 TYR A CG +843 C CD1 . TYR A 105 0.7521 0.3543 0.4563 -0.0085 0.1148 0.0494 ? ? ? ? ? ? 1960 TYR A CD1 +844 C CD2 . TYR A 105 0.5998 0.2911 0.3913 -0.0290 0.0745 0.0084 ? ? ? ? ? ? 1960 TYR A CD2 +845 C CE1 . TYR A 105 0.7438 0.3271 0.4918 -0.0235 0.1565 0.0405 ? ? ? ? ? ? 1960 TYR A CE1 +846 C CE2 . TYR A 105 0.5860 0.2680 0.4182 -0.0469 0.1098 -0.0069 ? ? ? ? ? ? 1960 TYR A CE2 +847 C CZ . TYR A 105 0.6454 0.2710 0.4622 -0.0449 0.1533 0.0080 ? ? ? ? ? ? 1960 TYR A CZ +848 O OH . TYR A 105 0.7435 0.3555 0.6120 -0.0661 0.1962 -0.0113 ? ? ? ? ? ? 1960 TYR A OH +849 N N . PHE A 106 0.5825 0.2940 0.3116 0.0102 -0.0181 0.0378 ? ? ? ? ? ? 1961 PHE A N +850 C CA . PHE A 106 0.5650 0.2935 0.3274 0.0062 -0.0252 0.0303 ? ? ? ? ? ? 1961 PHE A CA +851 C C . PHE A 106 0.5854 0.2997 0.3458 0.0224 -0.0348 0.0469 ? ? ? ? ? ? 1961 PHE A C +852 O O . PHE A 106 0.5875 0.2884 0.3746 0.0225 -0.0181 0.0481 ? ? ? ? ? ? 1961 PHE A O +853 C CB . PHE A 106 0.5090 0.2744 0.2855 0.0010 -0.0455 0.0188 ? ? ? ? ? ? 1961 PHE A CB +854 C CG . PHE A 106 0.5280 0.3059 0.3262 -0.0026 -0.0492 0.0122 ? ? ? ? ? ? 1961 PHE A CG +855 C CD1 . PHE A 106 0.5238 0.3091 0.3405 -0.0181 -0.0322 -0.0043 ? ? ? ? ? ? 1961 PHE A CD1 +856 C CD2 . PHE A 106 0.5468 0.3292 0.3498 0.0061 -0.0654 0.0173 ? ? ? ? ? ? 1961 PHE A CD2 +857 C CE1 . PHE A 106 0.5019 0.2942 0.3322 -0.0241 -0.0284 -0.0146 ? ? ? ? ? ? 1961 PHE A CE1 +858 C CE2 . PHE A 106 0.5402 0.3303 0.3663 0.0018 -0.0606 0.0100 ? ? ? ? ? ? 1961 PHE A CE2 +859 C CZ . PHE A 106 0.4832 0.2755 0.3182 -0.0128 -0.0408 -0.0052 ? ? ? ? ? ? 1961 PHE A CZ +860 N N . GLU A 107 0.6308 0.3621 0.2885 0.0459 0.0259 0.0233 ? ? ? ? ? ? 1962 GLU A N +861 C CA . GLU A 107 0.6750 0.4314 0.3239 0.0624 -0.0334 0.0085 ? ? ? ? ? ? 1962 GLU A CA +862 C C . GLU A 107 0.7379 0.4337 0.3291 0.0886 -0.0551 0.0185 ? ? ? ? ? ? 1962 GLU A C +863 O O . GLU A 107 0.6771 0.4122 0.3023 0.1097 -0.0960 0.0118 ? ? ? ? ? ? 1962 GLU A O +864 C CB . GLU A 107 0.7188 0.4540 0.3153 0.0495 -0.0596 -0.0018 ? ? ? ? ? ? 1962 GLU A CB +865 C CG . GLU A 107 0.6809 0.4838 0.3519 0.0234 -0.0513 -0.0105 ? ? ? ? ? ? 1962 GLU A CG +866 C CD . GLU A 107 0.6981 0.6326 0.4920 0.0238 -0.0736 -0.0132 ? ? ? ? ? ? 1962 GLU A CD +867 O OE1 . GLU A 107 0.6091 0.5814 0.4258 0.0483 -0.1007 -0.0151 ? ? ? ? ? ? 1962 GLU A OE1 +868 O OE2 . GLU A 107 0.5176 0.5195 0.3870 0.0009 -0.0619 -0.0120 ? ? ? ? ? ? 1962 GLU A OE2 +869 N N . LYS A 108 0.7637 0.3681 0.2755 0.0890 -0.0262 0.0387 ? ? ? ? ? ? 1963 LYS A N +870 C CA . LYS A 108 0.8576 0.4050 0.3225 0.1110 -0.0475 0.0562 ? ? ? ? ? ? 1963 LYS A CA +871 C C . LYS A 108 0.8072 0.3802 0.3489 0.1231 -0.0448 0.0589 ? ? ? ? ? ? 1963 LYS A C +872 O O . LYS A 108 0.8247 0.3966 0.3806 0.1477 -0.0827 0.0566 ? ? ? ? ? ? 1963 LYS A O +873 C CB . LYS A 108 0.8793 0.3647 0.2872 0.1003 -0.0129 0.0707 ? ? ? ? ? ? 1963 LYS A CB +874 C CG . LYS A 108 1.0339 0.4843 0.4077 0.1140 -0.0424 0.0856 ? ? ? ? ? ? 1963 LYS A CG +875 C CD . LYS A 108 1.1386 0.5653 0.5087 0.1061 -0.0046 0.1074 ? ? ? ? ? ? 1963 LYS A CD +876 C CE . LYS A 108 1.2177 0.6085 0.5398 0.1146 -0.0333 0.1280 ? ? ? ? ? ? 1963 LYS A CE +877 N NZ . LYS A 108 1.1147 0.5149 0.4693 0.1335 -0.0849 0.1300 ? ? ? ? ? ? 1963 LYS A NZ +878 N N . LYS A 109 0.7345 0.3249 0.3241 0.1054 -0.0020 0.0649 ? ? ? ? ? ? 1964 LYS A N +879 C CA . LYS A 109 0.7366 0.3481 0.3932 0.1098 -0.0029 0.0626 ? ? ? ? ? ? 1964 LYS A CA +880 C C . LYS A 109 0.6631 0.3560 0.3838 0.1276 -0.0372 0.0276 ? ? ? ? ? ? 1964 LYS A C +881 O O . LYS A 109 0.6881 0.3753 0.4324 0.1508 -0.0595 0.0165 ? ? ? ? ? ? 1964 LYS A O +882 C CB . LYS A 109 0.7077 0.3419 0.4127 0.0798 0.0426 0.0765 ? ? ? ? ? ? 1964 LYS A CB +883 C CG . LYS A 109 0.8109 0.4535 0.5288 0.0552 0.0724 0.0930 ? ? ? ? ? ? 1964 LYS A CG +884 C CD . LYS A 109 0.9384 0.5568 0.6646 0.0563 0.0582 0.1092 ? ? ? ? ? ? 1964 LYS A CD +885 C CE . LYS A 109 0.9305 0.5681 0.6782 0.0378 0.0791 0.1298 ? ? ? ? ? ? 1964 LYS A CE +886 N N . TRP A 110 0.6067 0.3747 0.3576 0.1180 -0.0401 0.0118 ? ? ? ? ? ? 1965 TRP A N +887 C CA . TRP A 110 0.5672 0.4306 0.3863 0.1342 -0.0668 -0.0144 ? ? ? ? ? ? 1965 TRP A CA +888 C C . TRP A 110 0.6376 0.4849 0.4406 0.1710 -0.1118 -0.0185 ? ? ? ? ? ? 1965 TRP A C +889 O O . TRP A 110 0.5958 0.4730 0.4432 0.2002 -0.1264 -0.0350 ? ? ? ? ? ? 1965 TRP A O +890 C CB . TRP A 110 0.5090 0.4529 0.3647 0.1124 -0.0655 -0.0193 ? ? ? ? ? ? 1965 TRP A CB +891 C CG . TRP A 110 0.4299 0.4932 0.3713 0.1227 -0.0812 -0.0377 ? ? ? ? ? ? 1965 TRP A CG +892 C CD1 . TRP A 110 0.4626 0.5917 0.4352 0.1381 -0.1179 -0.0416 ? ? ? ? ? ? 1965 TRP A CD1 +893 C CD2 . TRP A 110 0.3311 0.4671 0.3365 0.1183 -0.0603 -0.0504 ? ? ? ? ? ? 1965 TRP A CD2 +894 N NE1 . TRP A 110 0.3967 0.6381 0.4519 0.1457 -0.1142 -0.0540 ? ? ? ? ? ? 1965 TRP A NE1 +895 C CE2 . TRP A 110 0.2699 0.5174 0.3399 0.1351 -0.0800 -0.0630 ? ? ? ? ? ? 1965 TRP A CE2 +896 C CE3 . TRP A 110 0.2616 0.3817 0.2745 0.0992 -0.0287 -0.0488 ? ? ? ? ? ? 1965 TRP A CE3 +897 C CZ2 . TRP A 110 0.2137 0.5192 0.3242 0.1221 -0.0570 -0.0726 ? ? ? ? ? ? 1965 TRP A CZ2 +898 C CZ3 . TRP A 110 0.2713 0.4802 0.3421 0.0956 -0.0201 -0.0650 ? ? ? ? ? ? 1965 TRP A CZ3 +899 C CH2 . TRP A 110 0.1983 0.4980 0.3112 0.1087 -0.0338 -0.0781 ? ? ? ? ? ? 1965 TRP A CH2 +900 N N . THR A 111 0.6141 0.4106 0.3506 0.1700 -0.1335 -0.0024 ? ? ? ? ? ? 1966 THR A N +901 C CA . THR A 111 0.7745 0.5557 0.4969 0.2002 -0.1809 0.0040 ? ? ? ? ? ? 1966 THR A CA +902 C C . THR A 111 0.7963 0.5077 0.5076 0.2262 -0.1854 0.0125 ? ? ? ? ? ? 1966 THR A C +903 O O . THR A 111 0.8314 0.5646 0.5891 0.2604 -0.2120 0.0047 ? ? ? ? ? ? 1966 THR A O +904 C CB . THR A 111 0.8654 0.5951 0.5009 0.1857 -0.2059 0.0229 ? ? ? ? ? ? 1966 THR A CB +905 O OG1 . THR A 111 0.9338 0.7260 0.5887 0.1634 -0.2144 0.0128 ? ? ? ? ? ? 1966 THR A OG1 +906 C CG2 . THR A 111 0.9783 0.6988 0.6144 0.2047 -0.2481 0.0362 ? ? ? ? ? ? 1966 THR A CG2 +907 N N . ASP A 112 0.8599 0.5261 0.4400 0.2514 0.0300 -0.0040 ? ? ? ? ? ? 1967 ASP A N +908 C CA . ASP A 112 0.9086 0.5111 0.4771 0.2866 0.0345 0.0318 ? ? ? ? ? ? 1967 ASP A CA +909 C C . ASP A 112 0.8628 0.4610 0.5001 0.2906 0.0369 0.0277 ? ? ? ? ? ? 1967 ASP A C +910 O O . ASP A 112 0.9063 0.4738 0.5450 0.3262 0.0298 0.0473 ? ? ? ? ? ? 1967 ASP A O +911 C CB . ASP A 112 0.9629 0.4778 0.4889 0.2765 0.0715 0.0643 ? ? ? ? ? ? 1967 ASP A CB +912 C CG . ASP A 112 1.0945 0.5950 0.5351 0.2767 0.0733 0.0728 ? ? ? ? ? ? 1967 ASP A CG +913 O OD1 . ASP A 112 1.0520 0.6041 0.4594 0.2898 0.0390 0.0611 ? ? ? ? ? ? 1967 ASP A OD1 +914 O OD2 . ASP A 112 1.0768 0.5131 0.4834 0.2611 0.1101 0.0912 ? ? ? ? ? ? 1967 ASP A OD2 +915 N N . THR A 113 0.7881 0.4116 0.4783 0.2510 0.0470 0.0026 ? ? ? ? ? ? 1968 THR A N +916 C CA . THR A 113 0.7523 0.3614 0.4972 0.2435 0.0533 -0.0016 ? ? ? ? ? ? 1968 THR A CA +917 C C . THR A 113 0.7321 0.4150 0.5166 0.2569 0.0290 -0.0364 ? ? ? ? ? ? 1968 THR A C +918 O O . THR A 113 0.8527 0.5188 0.6642 0.2772 0.0298 -0.0353 ? ? ? ? ? ? 1968 THR A O +919 C CB . THR A 113 0.7564 0.3480 0.5379 0.1882 0.0740 -0.0069 ? ? ? ? ? ? 1968 THR A CB +920 O OG1 . THR A 113 0.7213 0.2767 0.4928 0.1671 0.0942 0.0252 ? ? ? ? ? ? 1968 THR A OG1 +921 C CG2 . THR A 113 0.6879 0.2779 0.5231 0.1644 0.0753 -0.0096 ? ? ? ? ? ? 1968 THR A CG2 +922 N N . PHE A 114 0.8377 0.6014 0.6268 0.2459 0.0096 -0.0682 ? ? ? ? ? ? 1969 PHE A N +923 C CA . PHE A 114 0.8504 0.6915 0.6875 0.2521 -0.0093 -0.1052 ? ? ? ? ? ? 1969 PHE A CA +924 C C . PHE A 114 0.9949 0.9019 0.8218 0.2921 -0.0423 -0.1117 ? ? ? ? ? ? 1969 PHE A C +925 O O . PHE A 114 1.0997 1.0486 0.9703 0.3222 -0.0567 -0.1259 ? ? ? ? ? ? 1969 PHE A O +926 C CB . PHE A 114 0.7676 0.6575 0.6352 0.1956 -0.0062 -0.1422 ? ? ? ? ? ? 1969 PHE A CB +927 C CG . PHE A 114 0.6713 0.5018 0.5569 0.1514 0.0187 -0.1346 ? ? ? ? ? ? 1969 PHE A CG +928 C CD1 . PHE A 114 0.7263 0.5269 0.6430 0.1485 0.0302 -0.1373 ? ? ? ? ? ? 1969 PHE A CD1 +929 C CD2 . PHE A 114 0.6371 0.4390 0.5103 0.1115 0.0299 -0.1237 ? ? ? ? ? ? 1969 PHE A CD2 +930 C CE1 . PHE A 114 0.6797 0.4232 0.6082 0.1024 0.0483 -0.1265 ? ? ? ? ? ? 1969 PHE A CE1 +931 C CE2 . PHE A 114 0.6139 0.3633 0.5112 0.0694 0.0469 -0.1117 ? ? ? ? ? ? 1969 PHE A CE2 +932 C CZ . PHE A 114 0.6327 0.3528 0.5544 0.0627 0.0540 -0.1117 ? ? ? ? ? ? 1969 PHE A CZ +933 N N . LYS A 115 1.0908 1.0054 0.8625 0.2910 -0.0540 -0.1009 ? ? ? ? ? ? 1970 LYS A N +934 C CA . LYS A 115 1.1633 1.1367 0.9175 0.3230 -0.0907 -0.1015 ? ? ? ? ? ? 1970 LYS A CA +935 C C . LYS A 115 1.2127 1.1336 0.9346 0.3736 -0.1031 -0.0597 ? ? ? ? ? ? 1970 LYS A C +936 O O . LYS A 115 1.2202 1.1268 0.9847 0.4077 -0.1050 -0.0523 ? ? ? ? ? ? 1970 LYS A O +937 C CB . LYS A 115 1.1242 1.1240 0.8221 0.2942 -0.0995 -0.1088 ? ? ? ? ? ? 1970 LYS A CB +# +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 SER 1 1856 1856 SER SER A . n +A 1 2 MET 2 1857 1857 MET MET A . n +A 1 3 SER 3 1858 1858 SER SER A . n +A 1 4 VAL 4 1859 1859 VAL VAL A . n +A 1 5 LYS 5 1860 1860 LYS LYS A . n +A 1 6 LYS 6 1861 1861 LYS LYS A . n +A 1 7 PRO 7 1862 1862 PRO PRO A . n +A 1 8 LYS 8 1863 1863 LYS LYS A . n +A 1 9 ARG 9 1864 1864 ARG ARG A . n +A 1 10 ASP 10 1865 1865 ASP ASP A . n +A 1 11 ASP 11 1866 1866 ASP ASP A . n +A 1 12 SER 12 1867 1867 SER SER A . n +A 1 13 LYS 13 1868 1868 LYS LYS A . n +A 1 14 ASP 14 1869 1869 ASP ASP A . n +A 1 15 LEU 15 1870 1870 LEU LEU A . n +A 1 16 ALA 16 1871 1871 ALA ALA A . n +A 1 17 LEU 17 1872 1872 LEU LEU A . n +A 1 18 CYS 18 1873 1873 CYS CYS A . n +A 1 19 SER 19 1874 1874 SER SER A . n +A 1 20 MET 20 1875 1875 MET MET A . n +A 1 21 ILE 21 1876 1876 ILE ILE A . n +A 1 22 LEU 22 1877 1877 LEU LEU A . n +A 1 23 THR 23 1878 1878 THR THR A . n +A 1 24 GLU 24 1879 1879 GLU GLU A . n +A 1 25 MET 25 1880 1880 MET MET A . n +A 1 26 GLU 26 1881 1881 GLU GLU A . n +A 1 27 THR 27 1882 1882 THR THR A . n +A 1 28 HIS 28 1883 1883 HIS HIS A . n +A 1 29 GLU 29 1884 1884 GLU GLU A . n +A 1 30 ASP 30 1885 1885 ASP ASP A . n +A 1 31 ALA 31 1886 1886 ALA ALA A . n +A 1 32 TRP 32 1887 1887 TRP TRP A . n +A 1 33 PRO 33 1888 1888 PRO PRO A . n +A 1 34 PHE 34 1889 1889 PHE PHE A . n +A 1 35 LEU 35 1890 1890 LEU LEU A . n +A 1 36 LEU 36 1891 1891 LEU LEU A . n +A 1 37 PRO 37 1892 1892 PRO PRO A . n +A 1 38 VAL 38 1893 1893 VAL VAL A . n +A 1 39 ASN 39 1894 1894 ASN ASN A . n +A 1 40 LEU 40 1895 1895 LEU LEU A . n +A 1 41 LYS 41 1896 1896 LYS LYS A . n +A 1 42 LEU 42 1897 1897 LEU LEU A . n +A 1 43 VAL 43 1898 1898 VAL VAL A . n +A 1 44 PRO 44 1899 1899 PRO PRO A . n +A 1 45 GLY 45 1900 1900 GLY GLY A . n +A 1 46 TYR 46 1901 1901 TYR TYR A . n +A 1 47 LYS 47 1902 1902 LYS LYS A . n +A 1 48 LYS 48 1903 1903 LYS LYS A . n +A 1 49 VAL 49 1904 1904 VAL VAL A . n +A 1 50 ILE 50 1905 1905 ILE ILE A . n +A 1 51 LYS 51 1906 1906 LYS LYS A . n +A 1 52 LYS 52 1907 1907 LYS LYS A . n +A 1 53 PRO 53 1908 1908 PRO PRO A . n +A 1 54 MET 54 1909 1909 MET MET A . n +A 1 55 ASP 55 1910 1910 ASP ASP A . n +A 1 56 PHE 56 1911 1911 PHE PHE A . n +A 1 57 SER 57 1912 1912 SER SER A . n +A 1 58 THR 58 1913 1913 THR THR A . n +A 1 59 ILE 59 1914 1914 ILE ILE A . n +A 1 60 ARG 60 1915 1915 ARG ARG A . n +A 1 61 GLU 61 1916 1916 GLU GLU A . n +A 1 62 LYS 62 1917 1917 LYS LYS A . n +A 1 63 LEU 63 1918 1918 LEU LEU A . n +A 1 64 SER 64 1919 1919 SER SER A . n +A 1 65 SER 65 1920 1920 SER SER A . n +A 1 66 GLY 66 1921 1921 GLY GLY A . n +A 1 67 GLN 67 1922 1922 GLN GLN A . n +A 1 68 TYR 68 1923 1923 TYR TYR A . n +A 1 69 PRO 69 1924 1924 PRO PRO A . n +A 1 70 ASN 70 1925 1925 ASN ASN A . n +A 1 71 LEU 71 1926 1926 LEU LEU A . n +A 1 72 GLU 72 1927 1927 GLU GLU A . n +A 1 73 THR 73 1928 1928 THR THR A . n +A 1 74 PHE 74 1929 1929 PHE PHE A . n +A 1 75 ALA 75 1930 1930 ALA ALA A . n +A 1 76 LEU 76 1931 1931 LEU LEU A . n +A 1 77 ASP 77 1932 1932 ASP ASP A . n +A 1 78 VAL 78 1933 1933 VAL VAL A . n +A 1 79 ARG 79 1934 1934 ARG ARG A . n +A 1 80 LEU 80 1935 1935 LEU LEU A . n +A 1 81 VAL 81 1936 1936 VAL VAL A . n +A 1 82 PHE 82 1937 1937 PHE PHE A . n +A 1 83 ASP 83 1938 1938 ASP ASP A . n +A 1 84 ASN 84 1939 1939 ASN ASN A . n +A 1 85 CYS 85 1940 1940 CYS CYS A . n +A 1 86 GLU 86 1941 1941 GLU GLU A . n +A 1 87 THR 87 1942 1942 THR THR A . n +A 1 88 PHE 88 1943 1943 PHE PHE A . n +A 1 89 ASN 89 1944 1944 ASN ASN A . n +A 1 90 GLU 90 1945 1945 GLU GLU A . n +A 1 91 ASP 91 1946 1946 ASP ASP A . n +A 1 92 ASP 92 1947 1947 ASP ASP A . n +A 1 93 SER 93 1948 1948 SER SER A . n +A 1 94 ASP 94 1949 1949 ASP ASP A . n +A 1 95 ILE 95 1950 1950 ILE ILE A . n +A 1 96 GLY 96 1951 1951 GLY GLY A . n +A 1 97 ARG 97 1952 1952 ARG ARG A . n +A 1 98 ALA 98 1953 1953 ALA ALA A . n +A 1 99 GLY 99 1954 1954 GLY GLY A . n +A 1 100 HIS 100 1955 1955 HIS HIS A . n +A 1 101 ASN 101 1956 1956 ASN ASN A . n +A 1 102 MET 102 1957 1957 MET MET A . n +A 1 103 ARG 103 1958 1958 ARG ARG A . n +A 1 104 LYS 104 1959 1959 LYS LYS A . n +A 1 105 TYR 105 1960 1960 TYR TYR A . n +A 1 106 PHE 106 1961 1961 PHE PHE A . n +A 1 107 GLU 107 1962 1962 GLU GLU A . n +A 1 108 LYS 108 1963 1963 LYS LYS A . n +A 1 109 LYS 109 1964 1964 LYS LYS A . n +A 1 110 TRP 110 1965 1965 TRP TRP A . n +A 1 111 THR 111 1966 1966 THR THR A . n +A 1 112 ASP 112 1967 1967 ASP ASP A . n +A 1 113 THR 113 1968 1968 THR THR A . n +A 1 114 PHE 114 1969 1969 PHE PHE A . n +A 1 115 LYS 115 1970 1970 LYS LYS A . n +A 1 116 VAL 116 1971 ? ? ? A . n +A 1 117 SER 117 1972 ? ? ? A . n +# +loop_ +_pdbx_refine_tls.pdbx_refine_id +_pdbx_refine_tls.id +_pdbx_refine_tls.details +_pdbx_refine_tls.method +_pdbx_refine_tls.origin_x +_pdbx_refine_tls.origin_y +_pdbx_refine_tls.origin_z +_pdbx_refine_tls.T[1][1] +_pdbx_refine_tls.T[2][2] +_pdbx_refine_tls.T[3][3] +_pdbx_refine_tls.T[1][2] +_pdbx_refine_tls.T[1][3] +_pdbx_refine_tls.T[2][3] +_pdbx_refine_tls.L[1][1] +_pdbx_refine_tls.L[2][2] +_pdbx_refine_tls.L[3][3] +_pdbx_refine_tls.L[1][2] +_pdbx_refine_tls.L[1][3] +_pdbx_refine_tls.L[2][3] +_pdbx_refine_tls.S[1][1] +_pdbx_refine_tls.S[1][2] +_pdbx_refine_tls.S[1][3] +_pdbx_refine_tls.S[2][1] +_pdbx_refine_tls.S[2][2] +_pdbx_refine_tls.S[2][3] +_pdbx_refine_tls.S[3][1] +_pdbx_refine_tls.S[3][2] +_pdbx_refine_tls.S[3][3] +'X-RAY DIFFRACTION' 1 ? refined 51.7028 17.1821 14.0205 0.5031 0.3420 0.2895 -0.0671 0.0101 0.0176 5.7992 3.5258 6.0477 3.2401 +2.5199 1.0981 -0.1168 -0.2207 -0.2330 -0.5495 0.0610 -0.3682 0.0226 -0.7649 0.0478 +'X-RAY DIFFRACTION' 2 ? refined 42.4520 13.1926 21.0656 0.4230 0.6859 0.6532 0.0898 -0.0825 0.3308 4.0626 3.8144 6.1364 -2.3137 +-4.9969 3.1409 -1.3114 -0.2286 0.6970 0.3171 0.9615 0.6816 -0.3104 -0.3295 0.3944 +'X-RAY DIFFRACTION' 3 ? refined 30.9297 10.9717 20.1215 0.6035 0.4343 0.6338 0.1338 0.1929 0.0564 4.8720 3.6220 8.1344 3.1681 +-1.7368 2.2974 -0.5739 -0.1423 -2.0455 -1.0255 -0.4365 -1.5901 1.2374 1.0387 1.0343 +'X-RAY DIFFRACTION' 4 ? refined 24.9736 15.8473 22.3096 0.5504 0.2498 0.3584 0.0361 -0.0383 -0.0065 7.0249 3.3900 5.0728 -2.8125 +-3.8763 4.1012 -0.1369 0.1165 -0.6617 0.3502 -0.1947 0.0007 -0.1270 0.1826 0.2831 +'X-RAY DIFFRACTION' 5 ? refined 19.8248 18.4657 26.3083 0.5076 0.2863 0.3932 0.0095 -0.0044 0.0375 2.1489 2.1690 2.2850 -0.0077 +-1.3098 1.8074 -0.0188 -0.3145 -1.0586 0.7185 -0.1463 -0.1241 0.3930 -0.1897 0.1294 +'X-RAY DIFFRACTION' 6 ? refined 16.5283 22.0022 29.2251 0.4324 0.2186 0.3336 -0.0452 0.0328 0.0454 2.4656 2.5873 2.0098 -2.1360 +-0.4599 1.4935 -0.4931 0.1661 -0.8137 0.1552 -0.0212 -0.0001 1.0938 -0.2369 0.5633 +'X-RAY DIFFRACTION' 7 ? refined 12.0584 25.3550 35.2106 0.4467 0.3712 0.3756 -0.0106 0.0959 0.0082 4.7862 2.5992 3.6907 3.4538 +4.1960 2.9932 -0.1064 -0.4934 -0.2901 1.7150 -0.4447 1.3036 0.9397 -0.7725 0.5716 +'X-RAY DIFFRACTION' 8 ? refined 12.2558 32.3038 28.3473 0.4360 0.2224 0.2301 0.0152 -0.0008 -0.0103 5.3004 2.4000 4.3745 0.1590 +-1.0980 -3.1474 -0.2325 -0.1494 0.1781 0.1259 0.1722 0.4258 0.3504 -0.1263 0.1180 +'X-RAY DIFFRACTION' 9 ? refined 11.5957 42.8738 20.2128 0.6552 0.2868 0.5332 0.0442 -0.1285 0.0101 6.0673 3.4729 3.8865 0.1395 +-4.5955 1.0862 0.7227 0.6985 0.2798 -1.2197 -0.3470 1.8211 -0.5498 -0.5622 -0.3211 +'X-RAY DIFFRACTION' 10 ? refined 16.3571 46.5450 23.5539 0.6036 0.2413 0.3569 0.0195 -0.0108 -0.0286 6.9735 5.2432 2.7354 3.1230 +-1.1141 0.6592 -0.1130 0.1813 0.2376 -0.4285 0.0510 0.6625 -0.2049 0.0641 0.0605 +'X-RAY DIFFRACTION' 11 ? refined 23.6802 41.1211 21.8391 0.5657 0.2720 0.3311 0.0137 0.0586 -0.0140 4.1251 4.0476 5.3170 -4.0621 +-4.6203 4.6329 0.5135 0.3499 0.8601 -1.4383 0.0666 -1.1686 0.0655 0.8293 -0.6056 +'X-RAY DIFFRACTION' 12 ? refined 18.4353 27.5606 20.0883 0.3986 0.2077 0.1894 0.0090 -0.0497 0.0046 6.0865 7.5463 9.7191 -1.8657 +-3.0431 -0.7044 0.1115 0.5094 -0.0441 -0.4900 -0.0858 0.0693 -0.3356 -0.2682 -0.0162 +'X-RAY DIFFRACTION' 13 ? refined 24.4900 23.9184 14.6960 0.6220 0.3324 0.2481 0.0078 -0.0132 -0.0121 5.1692 4.8504 2.0828 0.9603 +1.6702 -0.5802 -0.0147 -0.0525 -0.0270 -0.8332 -0.1793 0.0751 0.1942 0.3749 0.1700 +'X-RAY DIFFRACTION' 14 ? refined 31.2758 23.4917 21.2425 0.4733 0.4321 0.3634 0.0615 -0.0186 -0.0631 2.8833 3.2327 3.2546 -1.1102 +1.3483 2.1959 -0.4924 -0.2820 -0.2985 1.0556 1.4267 -1.0819 0.1691 0.9400 -0.9175 +'X-RAY DIFFRACTION' 15 ? refined 26.8945 27.5460 23.7543 0.4822 0.2508 0.1870 -0.0216 0.0094 -0.0124 8.0179 7.1898 8.3202 -5.8089 +-6.6000 3.1255 -0.1503 0.0185 0.1006 -0.5472 -0.0187 -0.1842 -0.5116 0.1461 0.1819 +'X-RAY DIFFRACTION' 16 ? refined 22.7495 36.5039 30.4054 0.4434 0.2548 0.2240 -0.0050 -0.0107 0.0143 2.6955 9.8561 3.7702 -3.5102 +-2.0328 4.8267 0.1136 -0.0208 0.1876 0.2430 -0.0417 -0.2487 -0.0826 0.1457 -0.0535 +'X-RAY DIFFRACTION' 17 ? refined 17.2344 37.4881 39.5019 0.6457 0.2743 0.2348 0.0444 -0.0230 -0.0001 5.3185 6.4588 5.7668 1.0649 +-2.5329 1.0621 -0.1798 -0.3139 0.0723 1.0978 0.2017 0.2587 -0.1173 0.2469 -0.1121 +'X-RAY DIFFRACTION' 18 ? refined 22.2045 26.2103 34.8182 0.5133 0.2435 0.2278 0.0105 -0.0345 0.0298 9.3593 8.2893 4.5231 0.5053 +-4.8951 1.0187 -0.2980 -0.3294 -0.3719 0.9189 0.0026 0.2408 0.3713 0.0019 0.3063 +'X-RAY DIFFRACTION' 19 ? refined 27.2243 20.7729 33.5863 0.5648 0.3303 0.2710 0.1217 -0.0692 0.0099 7.3775 6.7995 4.6886 0.9350 +1.6224 -4.7865 0.1544 -0.1645 -0.6502 1.8910 0.2371 -0.4276 0.7722 1.0419 -0.1655 +'X-RAY DIFFRACTION' 20 ? refined 29.3472 15.6284 31.7260 0.7479 0.4722 0.4878 0.2564 0.0149 -0.0419 2.6405 5.7804 2.6468 3.8115 +0.0362 -0.6806 -0.3472 -0.9397 -0.9159 1.2543 0.7286 -0.3107 0.8458 1.6357 -0.4624 +# +loop_ +_pdbx_refine_tls_group.pdbx_refine_id +_pdbx_refine_tls_group.id +_pdbx_refine_tls_group.refine_tls_id +_pdbx_refine_tls_group.beg_auth_asym_id +_pdbx_refine_tls_group.beg_auth_seq_id +_pdbx_refine_tls_group.beg_label_asym_id +_pdbx_refine_tls_group.beg_label_seq_id +_pdbx_refine_tls_group.end_auth_asym_id +_pdbx_refine_tls_group.end_auth_seq_id +_pdbx_refine_tls_group.end_label_asym_id +_pdbx_refine_tls_group.end_label_seq_id +_pdbx_refine_tls_group.selection +_pdbx_refine_tls_group.selection_details +'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1856:1859)' +'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1860:1864)' +'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1865:1868)' +'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1869:1873)' +'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1874:1877)' +'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1878:1881)' +'X-RAY DIFFRACTION' 7 7 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1882:1885)' +'X-RAY DIFFRACTION' 8 8 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1886:1892)' +'X-RAY DIFFRACTION' 9 9 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1893:1896)' +'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1897:1904)' +'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1905:1908)' +'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1909:1918)' +'X-RAY DIFFRACTION' 13 13 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1919:1924)' +'X-RAY DIFFRACTION' 14 14 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1925:1928)' +'X-RAY DIFFRACTION' 15 15 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1929:1932)' +'X-RAY DIFFRACTION' 16 16 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1933:1944)' +'X-RAY DIFFRACTION' 17 17 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1945:1956)' +'X-RAY DIFFRACTION' 18 18 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1957:1961)' +'X-RAY DIFFRACTION' 19 19 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1962:1966)' +'X-RAY DIFFRACTION' 20 20 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESID 1967:1970)' +# +_software.name PHENIX +_software.classification refinement +_software.version '(PHENIX.REFINE)' +_software.citation_id ? +_software.pdbx_ordinal 1 +# +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 A VAL 1971 ? +2 Y 1 1 A SER 1972 ? +# +loop_ +_pdbx_unobs_or_zero_occ_atoms.id +_pdbx_unobs_or_zero_occ_atoms.polymer_flag +_pdbx_unobs_or_zero_occ_atoms.occupancy_flag +_pdbx_unobs_or_zero_occ_atoms.PDB_model_num +_pdbx_unobs_or_zero_occ_atoms.auth_asym_id +_pdbx_unobs_or_zero_occ_atoms.auth_comp_id +_pdbx_unobs_or_zero_occ_atoms.auth_seq_id +_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code +_pdbx_unobs_or_zero_occ_atoms.auth_atom_id +_pdbx_unobs_or_zero_occ_atoms.label_alt_id +1 Y 1 1 A LYS 1863 ? CG ? +2 Y 1 1 A LYS 1863 ? CD ? +3 Y 1 1 A LYS 1863 ? CE ? +4 Y 1 1 A LYS 1863 ? NZ ? +5 Y 1 1 A LYS 1868 ? CE ? +6 Y 1 1 A LYS 1868 ? NZ ? +7 Y 1 1 A GLU 1927 ? CD ? +8 Y 1 1 A GLU 1927 ? OE1 ? +9 Y 1 1 A GLU 1927 ? OE2 ? +10 Y 1 1 A LYS 1959 ? CE ? +11 Y 1 1 A LYS 1959 ? NZ ? +12 Y 1 1 A LYS 1964 ? NZ ? +13 Y 1 1 A LYS 1970 ? CG ? +14 Y 1 1 A LYS 1970 ? CD ? +15 Y 1 1 A LYS 1970 ? CE ? +16 Y 1 1 A LYS 1970 ? NZ ? +# +_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 1,2 +_pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F +# +loop_ +_pdbx_struct_assembly_prop.biol_id +_pdbx_struct_assembly_prop.type +_pdbx_struct_assembly_prop.value +_pdbx_struct_assembly_prop.details +1 'ABSA (A^2)' 2050 ? +1 'SSA (A^2)' 14260 ? +1 MORE -16.8 ? +# +loop_ +_pdbx_struct_oper_list.id +_pdbx_struct_oper_list.type +_pdbx_struct_oper_list.name +_pdbx_struct_oper_list.symmetry_operation +_pdbx_struct_oper_list.matrix[1][1] +_pdbx_struct_oper_list.matrix[1][2] +_pdbx_struct_oper_list.matrix[1][3] +_pdbx_struct_oper_list.vector[1] +_pdbx_struct_oper_list.matrix[2][1] +_pdbx_struct_oper_list.matrix[2][2] +_pdbx_struct_oper_list.matrix[2][3] +_pdbx_struct_oper_list.vector[2] +_pdbx_struct_oper_list.matrix[3][1] +_pdbx_struct_oper_list.matrix[3][2] +_pdbx_struct_oper_list.matrix[3][3] +_pdbx_struct_oper_list.vector[3] +1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 +0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 +2 'crystal symmetry operation' 3_655 -x+1,y,-z+1/2 -1.0000000000 0.0000000000 0.0000000000 80.3700000000 0.0000000000 1.0000000000 +0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 28.8350000000 +# +_pdbx_version.entry_id 4CUP +_pdbx_version.revision_date 2014-04-02 +_pdbx_version.major_version 4 +_pdbx_version.minor_version 0000 +_pdbx_version.revision_type 'Initial release' +_pdbx_version.details 'Entry released' +# +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 +B 2 ZYB 1 2971 2971 ZYB ZYB A . +C 3 MOH 1 2972 2972 MOH MOH A . +D 3 MOH 1 2973 2973 MOH MOH A . +E 3 MOH 1 2974 2974 MOH MOH A . +F 4 HOH 1 2001 2001 HOH HOH A . +F 4 HOH 2 2002 2002 HOH HOH A . +F 4 HOH 3 2003 2003 HOH HOH A . +F 4 HOH 4 2004 2004 HOH HOH A . +F 4 HOH 5 2005 2005 HOH HOH A . +F 4 HOH 6 2006 2006 HOH HOH A . +F 4 HOH 7 2007 2007 HOH HOH A . +F 4 HOH 8 2008 2008 HOH HOH A . +F 4 HOH 9 2009 2009 HOH HOH A . +F 4 HOH 10 2010 2010 HOH HOH A . +F 4 HOH 11 2011 2011 HOH HOH A . +F 4 HOH 12 2012 2012 HOH HOH A . +F 4 HOH 13 2013 2013 HOH HOH A . +F 4 HOH 14 2014 2014 HOH HOH A . +F 4 HOH 15 2015 2015 HOH HOH A . +F 4 HOH 16 2016 2016 HOH HOH A . +F 4 HOH 17 2017 2017 HOH HOH A . +F 4 HOH 18 2018 2018 HOH HOH A . +F 4 HOH 19 2019 2019 HOH HOH A . +F 4 HOH 20 2020 2020 HOH HOH A . +F 4 HOH 21 2021 2021 HOH HOH A . +F 4 HOH 22 2022 2022 HOH HOH A . +F 4 HOH 23 2023 2023 HOH HOH A . +F 4 HOH 24 2024 2024 HOH HOH A . +F 4 HOH 25 2025 2025 HOH HOH A . +F 4 HOH 26 2026 2026 HOH HOH A . +F 4 HOH 27 2027 2027 HOH HOH A . +F 4 HOH 28 2028 2028 HOH HOH A . +F 4 HOH 29 2029 2029 HOH HOH A . +F 4 HOH 30 2030 2030 HOH HOH A . +F 4 HOH 31 2031 2031 HOH HOH A . +F 4 HOH 32 2032 2032 HOH HOH A . +F 4 HOH 33 2033 2033 HOH HOH A . +F 4 HOH 34 2034 2034 HOH HOH A . +F 4 HOH 35 2035 2035 HOH HOH A . +F 4 HOH 36 2036 2036 HOH HOH A . +F 4 HOH 37 2037 2037 HOH HOH A . +F 4 HOH 38 2038 2038 HOH HOH A . +F 4 HOH 39 2039 2039 HOH HOH A . +F 4 HOH 40 2040 2040 HOH HOH A . +F 4 HOH 41 2041 2041 HOH HOH A . +F 4 HOH 42 2042 2042 HOH HOH A . +F 4 HOH 43 2043 2043 HOH HOH A . +F 4 HOH 44 2044 2044 HOH HOH A . +F 4 HOH 45 2045 2045 HOH HOH A . +F 4 HOH 46 2046 2046 HOH HOH A . +F 4 HOH 47 2047 2047 HOH HOH A . +F 4 HOH 48 2048 2048 HOH HOH A . +F 4 HOH 49 2049 2049 HOH HOH A . +F 4 HOH 50 2050 2050 HOH HOH A . +F 4 HOH 51 2051 2051 HOH HOH A . +F 4 HOH 52 2052 2052 HOH HOH A . +F 4 HOH 53 2053 2053 HOH HOH A . +F 4 HOH 54 2054 2054 HOH HOH A . +F 4 HOH 55 2055 2055 HOH HOH A . +F 4 HOH 56 2056 2056 HOH HOH A . +F 4 HOH 57 2057 2057 HOH HOH A . +F 4 HOH 58 2058 2058 HOH HOH A . +F 4 HOH 59 2059 2059 HOH HOH A . +F 4 HOH 60 2060 2060 HOH HOH A . +F 4 HOH 61 2061 2061 HOH HOH A . +F 4 HOH 62 2062 2062 HOH HOH A . +F 4 HOH 63 2063 2063 HOH HOH A . +F 4 HOH 64 2064 2064 HOH HOH A . +F 4 HOH 65 2065 2065 HOH HOH A . +F 4 HOH 66 2066 2066 HOH HOH A . +F 4 HOH 67 2067 2067 HOH HOH A . +F 4 HOH 68 2068 2068 HOH HOH A . +F 4 HOH 69 2069 2069 HOH HOH A . +F 4 HOH 70 2070 2070 HOH HOH A . +F 4 HOH 71 2071 2071 HOH HOH A . +F 4 HOH 72 2072 2072 HOH HOH A . +F 4 HOH 73 2073 2073 HOH HOH A . +F 4 HOH 74 2074 2074 HOH HOH A . +F 4 HOH 75 2075 2075 HOH HOH A . +F 4 HOH 76 2076 2076 HOH HOH A . +F 4 HOH 77 2077 2077 HOH HOH A . +F 4 HOH 78 2078 2078 HOH HOH A . +F 4 HOH 79 2079 2079 HOH HOH A . +F 4 HOH 80 2080 2080 HOH HOH A . +F 4 HOH 81 2081 2081 HOH HOH A . +F 4 HOH 82 2082 2082 HOH HOH A . +F 4 HOH 83 2083 2083 HOH HOH A . +F 4 HOH 84 2084 2084 HOH HOH A . +F 4 HOH 85 2085 2085 HOH HOH A . +F 4 HOH 86 2086 2086 HOH HOH A . +F 4 HOH 87 2087 2087 HOH HOH A . +F 4 HOH 88 2088 2088 HOH HOH A . +F 4 HOH 89 2089 2089 HOH HOH A . +F 4 HOH 90 2090 2090 HOH HOH A . +F 4 HOH 91 2091 2091 HOH HOH A . +F 4 HOH 92 2092 2092 HOH HOH A . +F 4 HOH 93 2093 2093 HOH HOH A . +F 4 HOH 94 2094 2094 HOH HOH A . +F 4 HOH 95 2095 2095 HOH HOH A . +F 4 HOH 96 2096 2096 HOH HOH A . +F 4 HOH 97 2097 2097 HOH HOH A . +F 4 HOH 98 2098 2098 HOH HOH A . +F 4 HOH 99 2099 2099 HOH HOH A . +F 4 HOH 100 2100 2100 HOH HOH A . +F 4 HOH 101 2101 2101 HOH HOH A . +F 4 HOH 102 2102 2102 HOH HOH A . +F 4 HOH 103 2103 2103 HOH HOH A . +F 4 HOH 104 2104 2104 HOH HOH A . +F 4 HOH 105 2105 2105 HOH HOH A . +F 4 HOH 106 2106 2106 HOH HOH A . +F 4 HOH 107 2107 2107 HOH HOH A . +F 4 HOH 108 2108 2108 HOH HOH A . +F 4 HOH 109 2109 2109 HOH HOH A . +F 4 HOH 110 2110 2110 HOH HOH A . +F 4 HOH 111 2111 2111 HOH HOH A . +F 4 HOH 112 2112 2112 HOH HOH A . +F 4 HOH 113 2113 2113 HOH HOH A . +F 4 HOH 114 2114 2114 HOH HOH A . +F 4 HOH 115 2115 2115 HOH HOH A . +F 4 HOH 116 2116 2116 HOH HOH A . +F 4 HOH 117 2117 2117 HOH HOH A . +F 4 HOH 118 2118 2118 HOH HOH A . +F 4 HOH 119 2119 2119 HOH HOH A . +F 4 HOH 120 2120 2120 HOH HOH A . +F 4 HOH 121 2121 2121 HOH HOH A . +F 4 HOH 122 2122 2122 HOH HOH A . +F 4 HOH 123 2123 2123 HOH HOH A . +F 4 HOH 124 2124 2124 HOH HOH A . +F 4 HOH 125 2125 2125 HOH HOH A . +F 4 HOH 126 2126 2126 HOH HOH A . +F 4 HOH 127 2127 2127 HOH HOH A . +F 4 HOH 128 2128 2128 HOH HOH A . +F 4 HOH 129 2129 2129 HOH HOH A . +F 4 HOH 130 2130 2130 HOH HOH A . +F 4 HOH 131 2131 2131 HOH HOH A . +F 4 HOH 132 2132 2132 HOH HOH A . +F 4 HOH 133 2133 2133 HOH HOH A . +F 4 HOH 134 2134 2134 HOH HOH A . +F 4 HOH 135 2135 2135 HOH HOH A . +F 4 HOH 136 2136 2136 HOH HOH A . +F 4 HOH 137 2137 2137 HOH HOH A . +F 4 HOH 138 2138 2138 HOH HOH A . +F 4 HOH 139 2139 2139 HOH HOH A . +F 4 HOH 140 2140 2140 HOH HOH A . +F 4 HOH 141 2141 2141 HOH HOH A . +F 4 HOH 142 2142 2142 HOH HOH A . +F 4 HOH 143 2143 2143 HOH HOH A . +F 4 HOH 144 2144 2144 HOH HOH A . +F 4 HOH 145 2145 2145 HOH HOH A . +F 4 HOH 146 2146 2146 HOH HOH A . +# +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 A HOH 2025 ? ? O A HOH 2026 ? ? 2.16 +2 1 O A HOH 2021 ? ? O A HOH 2025 ? ? 2.17 +3 1 O A HOH 2031 ? ? O A HOH 2137 ? ? 2.18 +# +loop_ +_pdbx_entity_nonpoly.entity_id +_pdbx_entity_nonpoly.name +_pdbx_entity_nonpoly.comp_id +2 4-FLUOROBENZAMIDOXIME ZYB +3 METHANOL MOH +4 water HOH +# From d3fcbc1e66d0dda0363196e5072066c2b400ec14 Mon Sep 17 00:00:00 2001 From: Aleix Lafita Date: Fri, 30 Jun 2017 12:02:28 -0700 Subject: [PATCH 02/10] Remove the warnings in MMTF reader --- .../io/mmtf/MmtfStructureReader.java | 23 ++++++++++--------- 1 file changed, 12 insertions(+), 11 deletions(-) diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java index 7eb07e806a..8b74ea3993 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java @@ -304,14 +304,15 @@ public void setAtomInfo(String atomName, * face#setGroupBonds(int, int, int) */ @Override - public void setGroupBond(int indOne, - int indTwo, int bondOrder) { - // Get the atom + public void setGroupBond(int indOne, int indTwo, int bondOrder) { + + // Get the atoms Atom atomOne = atomsInGroup.get(indOne); Atom atomTwo = atomsInGroup.get(indTwo); + // set the new bond - @SuppressWarnings("unused") - BondImpl bond = new BondImpl(atomOne, atomTwo, bondOrder); + new BondImpl(atomOne, atomTwo, bondOrder); + } /* (non-Javadoc) @@ -319,14 +320,14 @@ public void setGroupBond(int indOne, * Interface#setInterGroupBonds(int, int, int) */ @Override - public void setInterGroupBond(int indOne, - int indTwo, int bondOrder) { - // Get the atom + public void setInterGroupBond(int indOne, int indTwo, int bondOrder) { + + // Get the atoms Atom atomOne = allAtoms[indOne]; Atom atomTwo = allAtoms[indTwo]; - // set the new bond - @SuppressWarnings("unused") - BondImpl bond = new BondImpl(atomOne, atomTwo, bondOrder); + + // set the new bond (this + new BondImpl(atomOne, atomTwo, bondOrder); } From c6dddfd9b3c228ea7b8c4f8dfd36b0b09a48384c Mon Sep 17 00:00:00 2001 From: Aleix Lafita Date: Thu, 6 Jul 2017 15:09:13 +0100 Subject: [PATCH 03/10] Fix path bug in mmtf test --- .../nbio/structure/io/mmtf/MmtfUtils.java | 4 ++++ .../io/mmtf/TestMmtfStructureReader.java | 22 ++++++++++++++----- 2 files changed, 21 insertions(+), 5 deletions(-) diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java index 929a5db4b8..8e14f7d1db 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java @@ -479,9 +479,12 @@ public static void insertSeqResGroup(Chain chain, Group group, int sequenceIndex * @param sequence the sequence of the construct */ public static void addSeqRes(Chain modelChain, String sequence) { + List seqResGroups = modelChain.getSeqResGroups(); GroupType chainType = getChainType(modelChain.getAtomGroups()); + for(int i=0; i Date: Mon, 2 Sep 2019 15:10:53 -0700 Subject: [PATCH 04/10] Cosmetics --- .../nbio/structure/io/mmtf/MmtfStructureReader.java | 4 ++-- .../org/biojava/nbio/structure/io/mmtf/MmtfUtils.java | 11 +++-------- .../structure/io/mmtf/TestMmtfStructureReader.java | 2 -- 3 files changed, 5 insertions(+), 12 deletions(-) diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java index 69744a3f19..7c7c24e9ec 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfStructureReader.java @@ -229,7 +229,7 @@ public void setGroupInfo(String groupName, int groupNumber, group = new HetatomImpl(); break; } - atomsInGroup = new ArrayList(); + atomsInGroup = new ArrayList<>(); ChemComp chemComp = new ChemComp(); chemComp.setOne_letter_code(String.valueOf(singleLetterCode)); chemComp.setType(chemCompType.toUpperCase()); @@ -243,7 +243,7 @@ public void setGroupInfo(String groupName, int groupNumber, group.setResidueNumber(chain.getName().trim(), groupNumber, insertionCode); } - group.setAtoms(new ArrayList(atomCount)); + group.setAtoms(new ArrayList<>(atomCount)); if (polymerType==1 || polymerType==2) { MmtfUtils.insertSeqResGroup(chain, group, sequenceIndexId); } diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java index 3b61957009..7085944462 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java @@ -371,7 +371,7 @@ public static int getSecStructType(Group group) { /** * Get the secondary structure as defined by DSSP. * @param group the input group to be calculated - * @param the integer index of the group type. + * @param dsspIndex integer index of the group type. */ public static void setSecStructType(Group group, int dsspIndex) { SecStrucType secStrucType = getSecStructTypeFromDsspIndex(dsspIndex); @@ -508,9 +508,7 @@ public static void addSeqRes(Chain modelChain, String sequence) { char singleLetterCode = sequence.charAt(i); Group group = null; - if(seqResGroups.size()<=i){ - } - else{ + if (seqResGroups.size() > i) { group=seqResGroups.get(i); } if(group!=null){ @@ -525,10 +523,7 @@ public static void addSeqRes(Chain modelChain, String sequence) { private static GroupType getChainType(List groups) { for(Group group : groups) { - if(group==null){ - continue; - } - else if(group.getType()!=GroupType.HETATM){ + if(group!=null && group.getType()!=GroupType.HETATM){ return group.getType(); } } diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java index 3611a56c30..b591b02672 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java @@ -64,8 +64,6 @@ public void compareMmcif() throws IOException, StructureException { assertEquals(mmcif.getPDBHeader().getExperimentalTechniques(), mmtf.getPDBHeader().getExperimentalTechniques()); - - // Compare the SEQRES assertEquals(mmcif.getChainByIndex(0).getSeqResSequence(), mmtf.getChainByIndex(0).getSeqResSequence()); From 18f2b6e6625fae157cb427e603878930013899f9 Mon Sep 17 00:00:00 2001 From: Jose Manuel Duarte Date: Mon, 2 Sep 2019 15:17:39 -0700 Subject: [PATCH 05/10] More cosmetics --- .../main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java | 2 -- 1 file changed, 2 deletions(-) diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java index 7085944462..fbe880d4e8 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java @@ -379,8 +379,6 @@ public static void setSecStructType(Group group, int dsspIndex) { if(secStrucType!=null){ group.setProperty("secstruc", secStrucState); } - else{ - } } From dc5639c4e057db63ab8b79820d4909c1a6ff0557 Mon Sep 17 00:00:00 2001 From: Jose Manuel Duarte Date: Mon, 2 Sep 2019 15:42:22 -0700 Subject: [PATCH 06/10] Fixing potential bug --- .../java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java | 2 +- .../nbio/structure/io/mmtf/TestMmtfStructureReader.java | 4 +--- 2 files changed, 2 insertions(+), 4 deletions(-) diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java index fbe880d4e8..afbb7bb40e 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java @@ -392,7 +392,7 @@ public static SecStrucType getSecStructTypeFromDsspIndex(int dsspIndex) { String dsspType = DsspType.dsspTypeFromInt(dsspIndex).getDsspType(); for(SecStrucType secStrucType : SecStrucType.values()) { - if(dsspType==secStrucType.name) + if(dsspType.equals(secStrucType.name)) { return secStrucType; } diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java index b591b02672..43f20c801c 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java @@ -64,12 +64,10 @@ public void compareMmcif() throws IOException, StructureException { assertEquals(mmcif.getPDBHeader().getExperimentalTechniques(), mmtf.getPDBHeader().getExperimentalTechniques()); - // Compare the SEQRES + // Compare the SEQRES, see issue https://github.com/biojava/biojava/issues/671 assertEquals(mmcif.getChainByIndex(0).getSeqResSequence(), mmtf.getChainByIndex(0).getSeqResSequence()); - - } } From 93832066d86bff68fe1cebb4324aa693011f88b4 Mon Sep 17 00:00:00 2001 From: Jose Manuel Duarte Date: Mon, 2 Sep 2019 16:30:01 -0700 Subject: [PATCH 07/10] Fixing #671 --- .../biojava/nbio/structure/io/mmtf/MmtfUtils.java | 12 ++++++++++-- .../nbio/structure/io/mmtf/TestMmtfRoundTrip.java | 1 - .../structure/io/mmtf/TestMmtfStructureReader.java | 2 +- 3 files changed, 11 insertions(+), 4 deletions(-) diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java index afbb7bb40e..93e7ab0f46 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java @@ -50,6 +50,7 @@ import org.biojava.nbio.structure.io.FileParsingParameters; import org.biojava.nbio.structure.io.mmcif.ChemCompGroupFactory; import org.biojava.nbio.structure.io.mmcif.DownloadChemCompProvider; +import org.biojava.nbio.structure.io.mmcif.chem.PolymerType; import org.biojava.nbio.structure.io.mmcif.model.ChemComp; import org.biojava.nbio.structure.quaternary.BioAssemblyInfo; import org.biojava.nbio.structure.quaternary.BiologicalAssemblyTransformation; @@ -513,7 +514,7 @@ public static void addSeqRes(Chain modelChain, String sequence) { continue; } - group = getSeqResGroup(modelChain, singleLetterCode, chainType); + group = getSeqResGroup(singleLetterCode, chainType); addGroupAtId(seqResGroups, group, i); seqResGroups.set(i, group); } @@ -537,7 +538,7 @@ private static void addGroupAtId(List seqResGroups, T group, int sequence } } - private static Group getSeqResGroup(Chain modelChain, char singleLetterCode, GroupType type) { + private static Group getSeqResGroup(char singleLetterCode, GroupType type) { if(type==GroupType.AMINOACID){ AminoAcidImpl a = new AminoAcidImpl(); a.setRecordType(AminoAcid.SEQRESRECORD); @@ -545,6 +546,7 @@ private static Group getSeqResGroup(Chain modelChain, char singleLetterCode, Gro ChemComp chemComp = new ChemComp(); chemComp.setOne_letter_code(""+singleLetterCode); a.setChemComp(chemComp); + chemComp.setPolymerType(PolymerType.peptide); return a; } else if (type==GroupType.NUCLEOTIDE) { @@ -552,6 +554,12 @@ private static Group getSeqResGroup(Chain modelChain, char singleLetterCode, Gro ChemComp chemComp = new ChemComp(); chemComp.setOne_letter_code(""+singleLetterCode); n.setChemComp(chemComp); + // TODO this could be either dna or rna, how to distinguish properly? + if (singleLetterCode == 'U') { + chemComp.setPolymerType(PolymerType.rna); + } else { + chemComp.setPolymerType(PolymerType.dna); + } return n; } else{ diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfRoundTrip.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfRoundTrip.java index c2124c983b..d9bdb05bc0 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfRoundTrip.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfRoundTrip.java @@ -94,7 +94,6 @@ public void testRoundTrip() throws IOException, StructureException { * Broad test of atom similarity * @param structOne the first input structure * @param structTwo the second input structure - * @param mmtfParams * @return */ private boolean checkIfAtomsSame(Structure structOne, Structure structTwo) { diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java index 43f20c801c..b0928b3836 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java @@ -44,7 +44,7 @@ public void testRead() throws IOException { /** * Compare structures loaded from MMCIF and MMTF files. */ - @Test @Ignore + @Test public void compareMmcif() throws IOException, StructureException { // Get the MMTF and MMCIF files from the resources folder From ee6a478bbf36bdd1e82015a0500b8eb2d83658d1 Mon Sep 17 00:00:00 2001 From: Jose Manuel Duarte Date: Mon, 2 Sep 2019 16:54:56 -0700 Subject: [PATCH 08/10] New test for #792 --- .../io/mmtf/TestMmtfStructureReader.java | 35 +++++++++++++++++++ 1 file changed, 35 insertions(+) diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java index b0928b3836..ac2d81e8d5 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfStructureReader.java @@ -4,11 +4,19 @@ import java.io.IOException; import java.nio.file.Paths; +import java.util.List; + +import org.biojava.nbio.structure.Group; import org.biojava.nbio.structure.Structure; import org.biojava.nbio.structure.StructureException; import org.biojava.nbio.structure.StructureIO; +import org.biojava.nbio.structure.align.util.AtomCache; +import org.biojava.nbio.structure.io.FileParsingParameters; +import org.biojava.nbio.structure.io.mmcif.ChemCompGroupFactory; +import org.biojava.nbio.structure.io.mmcif.DownloadChemCompProvider; import org.junit.Ignore; import org.junit.Test; +import static org.junit.Assert.*; /** * Test the Biojava MMTF reader. @@ -70,4 +78,31 @@ public void compareMmcif() throws IOException, StructureException { } + /** + * Test for issue https://github.com/biojava/biojava/issues/792 + */ + @Test + @Ignore("Issue not fixed yet") + public void checkNonStandardAminoSeqresGroupsPopulated() throws StructureException, IOException { + // 2X3T, see issue https://github.com/biojava/biojava/issues/792 + // Load a structure in mmtf format + AtomCache cache = new AtomCache(); + FileParsingParameters params = new FileParsingParameters(); + cache.setFileParsingParams(params); + cache.setUseMmCif(false); + cache.setUseMmtf(true); + + StructureIO.setAtomCache(cache); + + ChemCompGroupFactory.setChemCompProvider(new DownloadChemCompProvider()); + + Structure structure1 = StructureIO.getStructure("2X3T"); + // chain E is a glycopeptide with unobserved non-standard aminoacids. Because of mmtf limitations (representing seqres sequences as 1-letter strings) the non-standard unobserved residues are read as null + List seqresGroups = structure1.getChain("E").getSeqResGroups(); + for (Group g : seqresGroups) { + assertNotNull("SeqRes group should not be null", g); + } + + } + } From 3d0274b0891ea7c80445f87fb4abcf3936106a15 Mon Sep 17 00:00:00 2001 From: Jose Duarte Date: Mon, 2 Sep 2019 21:33:38 -0700 Subject: [PATCH 09/10] Better solution --- .../nbio/structure/io/mmtf/MmtfUtils.java | 24 +++++++++---------- 1 file changed, 12 insertions(+), 12 deletions(-) diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java index 93e7ab0f46..2a25a270fc 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java @@ -50,7 +50,7 @@ import org.biojava.nbio.structure.io.FileParsingParameters; import org.biojava.nbio.structure.io.mmcif.ChemCompGroupFactory; import org.biojava.nbio.structure.io.mmcif.DownloadChemCompProvider; -import org.biojava.nbio.structure.io.mmcif.chem.PolymerType; +import org.biojava.nbio.structure.io.mmcif.chem.ChemCompTools; import org.biojava.nbio.structure.io.mmcif.model.ChemComp; import org.biojava.nbio.structure.quaternary.BioAssemblyInfo; import org.biojava.nbio.structure.quaternary.BiologicalAssemblyTransformation; @@ -539,27 +539,27 @@ private static void addGroupAtId(List seqResGroups, T group, int sequence } private static Group getSeqResGroup(char singleLetterCode, GroupType type) { + if(type==GroupType.AMINOACID){ + String threeLetter = ChemCompTools.getAminoThreeLetter(singleLetterCode); + if (threeLetter == null) return null; + ChemComp chemComp = ChemCompGroupFactory.getChemComp(threeLetter); + AminoAcidImpl a = new AminoAcidImpl(); a.setRecordType(AminoAcid.SEQRESRECORD); a.setAminoType(singleLetterCode); - ChemComp chemComp = new ChemComp(); - chemComp.setOne_letter_code(""+singleLetterCode); + a.setPDBName(threeLetter); a.setChemComp(chemComp); - chemComp.setPolymerType(PolymerType.peptide); return a; } else if (type==GroupType.NUCLEOTIDE) { + String twoLetter = ChemCompTools.getDNATwoLetter(singleLetterCode); + if (twoLetter == null) return null; + ChemComp chemComp = ChemCompGroupFactory.getChemComp(twoLetter); + NucleotideImpl n = new NucleotideImpl(); - ChemComp chemComp = new ChemComp(); - chemComp.setOne_letter_code(""+singleLetterCode); + n.setPDBName(twoLetter); n.setChemComp(chemComp); - // TODO this could be either dna or rna, how to distinguish properly? - if (singleLetterCode == 'U') { - chemComp.setPolymerType(PolymerType.rna); - } else { - chemComp.setPolymerType(PolymerType.dna); - } return n; } else{ From 9afde8fc5e19807fb4e787ed57f5865ff8925e58 Mon Sep 17 00:00:00 2001 From: Jose Manuel Duarte Date: Tue, 3 Sep 2019 10:19:46 -0700 Subject: [PATCH 10/10] Fixing test and clean up --- .../nbio/structure/io/mmtf/MmtfUtils.java | 1 - .../io/mmtf/TestMmtfPerformance.java | 58 +++---------------- 2 files changed, 8 insertions(+), 51 deletions(-) diff --git a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java index 2a25a270fc..bbd34c9610 100644 --- a/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java +++ b/biojava-structure/src/main/java/org/biojava/nbio/structure/io/mmtf/MmtfUtils.java @@ -516,7 +516,6 @@ public static void addSeqRes(Chain modelChain, String sequence) { group = getSeqResGroup(singleLetterCode, chainType); addGroupAtId(seqResGroups, group, i); - seqResGroups.set(i, group); } } diff --git a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfPerformance.java b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfPerformance.java index d18f856cd8..e0b576d79a 100644 --- a/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfPerformance.java +++ b/biojava-structure/src/test/java/org/biojava/nbio/structure/io/mmtf/TestMmtfPerformance.java @@ -44,54 +44,14 @@ public class TestMmtfPerformance { private static final int NUMBER_OF_REPEATS = 10; - // Returns the contents of the file in a byte array. - public static byte[] getBytesFromFile(File file) throws IOException { - // Get the size of the file - long length = file.length(); - - // You cannot create an array using a long type. - // It needs to be an int type. - // Before converting to an int type, check - // to ensure that file is not larger than Integer.MAX_VALUE. - if (length > Integer.MAX_VALUE) { - // File is too large - throw new IOException("File is too large!"); - } - - // Create the byte array to hold the data - byte[] bytes = new byte[(int)length]; - - // Read in the bytes - int offset = 0; - int numRead = 0; - - InputStream is = new FileInputStream(file); - try { - while (offset < bytes.length - && (numRead=is.read(bytes, offset, bytes.length-offset)) >= 0) { - offset += numRead; - } - } finally { - is.close(); - } - - // Ensure all the bytes have been read in - if (offset < bytes.length) { - throw new IOException("Could not completely read file "+file.getName()); - } - return bytes; - } - - static String convertStreamToString(java.io.InputStream is) { + private static String convertStreamToString(java.io.InputStream is) { try ( java.util.Scanner s = new java.util.Scanner(is)){ return s.useDelimiter("\\A").hasNext() ? s.next() : ""; } - } - - public byte[] getByteArrayFromInputStream(InputStream is) throws IOException { + private byte[] getByteArrayFromInputStream(InputStream is) throws IOException { ByteArrayOutputStream buffer = new ByteArrayOutputStream(); int nRead; @@ -104,7 +64,6 @@ public byte[] getByteArrayFromInputStream(InputStream is) throws IOException { buffer.flush(); return buffer.toByteArray(); - } @Test @@ -128,31 +87,30 @@ public void test3HBX() throws Exception{ byte[] mmtfdata = getByteArrayFromInputStream(new GZIPInputStream((mmtfURL.openStream()))); + // first make sure chemcomp cache is warmed up (chemcomp files are parsed). Like that we count the parsing time without the influence of chemcomp parsing + MmtfActions.readFromInputStream(new ByteArrayInputStream(mmtfdata)); + parser.parsePDBFile(new ByteArrayInputStream(pdbBytes)); + for ( int i =0 ; i< NUMBER_OF_REPEATS ; i++) { long mmtfStart = System.nanoTime(); MmtfActions.readFromInputStream(new ByteArrayInputStream(mmtfdata)); long mmtfEnd = System.nanoTime(); - - long pdbStart = System.nanoTime(); parser.parsePDBFile(new ByteArrayInputStream(pdbBytes)); long pdbEnd = System.nanoTime(); totalTimePDB += (pdbEnd - pdbStart); - totalTimeMMTF += (mmtfEnd-mmtfStart); } - long timePDB = (totalTimePDB/NUMBER_OF_REPEATS); long timeMMTF = (totalTimeMMTF/NUMBER_OF_REPEATS); - - logger.warn("average time to parse mmtf: " + timeMMTF/(1000*1000) + " ms."); - logger.warn("average time to parse PDB : " + timePDB/(1000*1000) + " ms. "); + logger.info("average time to parse mmtf: " + timeMMTF/(1000*1000) + " ms."); + logger.info("average time to parse PDB : " + timePDB/(1000*1000) + " ms. "); assertTrue( "It should not be the case, but it is faster to parse a PDB file ("+timePDB+" ns.) than MMTF ("+( timeMMTF)+" ns.)!",( timePDB) > ( timeMMTF));