data_5754 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N backbone resonance assignment of the VASP EVH1 domain ; _BMRB_accession_number 5754 _BMRB_flat_file_name bmr5754.str _Entry_type original _Submission_date 2003-03-24 _Accession_date 2003-03-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vogtherr Martin . . 2 Grimme Susanne . . 3 Pescatore Barbara . . 4 Schwalbe Harald . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 390 "13C chemical shifts" 332 "15N chemical shifts" 110 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-04-07 original author . stop_ _Original_release_date 2004-04-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 13C and 15N Backbone Resonance Assignment of the VASP EVH1 Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22794757 _PubMed_ID 12913419 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Vogtherr Martin . . 2 Grimme Susanne . . 3 Pescatore Barbara . . 4 Schwalbe Harald . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 27 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 189 _Page_last 190 _Year 2003 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Ch. Bartels, T.-H. Xia, M. Billeter, P. Guntert, K. Wuthrich (1995). J. Biomol. NMR 5, 1-10 ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ save_ref_2 _Saveframe_category citation _Citation_full ; G. Cornilescu, F. Delaglio, A. Bax (1999). J. Biomol. NMR 13, 289-302 ; _Citation_title 'Protein backbone angle restraints from searching a database for chemical shift and sequence homology.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10212987 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cornilescu G . . 2 Delaglio F . . 3 Bax A . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 13 _Journal_issue 3 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 289 _Page_last 302 _Year 1999 _Details ; Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Ball LJ, Kuhne R, Hoffmann B, Hafner A, Schmieder P, Volkmer-Engert R, Hof M, Wahl M, Schneider-Mergener J, Walter U, Oschkinat H, Jarchau T. EMBO J. 2000 Sep 15;19(18):4903-14. ; _Citation_title 'Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10990454 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ball 'L. J.' J. . 2 Koehne R. . . 3 Hoffmann B. . . 4 Hoefner A. . . 5 Schmieder P. . . 6 Volkmer-Engert R. . . 7 Hof M. . . 8 Wahl M. . . 9 Schneider-Mergener J. . . 10 Walter U. . . 11 Oschkinat H. . . 12 Jarchau T. . . stop_ _Journal_abbreviation 'EMBO J.' _Journal_name_full 'The EMBO journal' _Journal_volume 19 _Journal_issue 18 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 4903 _Page_last 4914 _Year 2000 _Details ; The Ena-VASP family of proteins act as molecular adaptors linking the cytoskeletal system to signal transduction pathways. Their N-terminal EVH1 domains use groups of exposed aromatic residues to specifically recognize 'FPPPP' motifs found in the mammalian zyxin and vinculin proteins, and ActA protein of the intracellular bacterium Listeria monocytogenes. Here, evidence is provided that the affinities of these EVH1-peptide interactions are strongly dependent on the recognition of residues flanking the core FPPPP motifs. Determination of the VASP EVH1 domain solution structure, together with peptide library screening, measurement of individual K(d)s by fluorescence titration, and NMR chemical shift mapping, revealed a second affinity-determining epitope present in all four ActA EVH1-binding motifs. The epitope was shown to interact with a complementary hydrophobic site on the EVH1 surface and to increase strongly the affinity of ActA for EVH1 domains. We propose that this epitope, which is absent in the sequences of the native EVH1-interaction partners zyxin and vinculin, may provide the pathogen with an advantage when competing for the recruitment of the host VASP and Mena proteins in the infected cell. ; save_ ################################## # Molecular system description # ################################## save_VASP_EVH1 _Saveframe_category molecular_system _Mol_system_name 'VASP EVH1 domain' _Abbreviation_common 'VASP EVH1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'VASP EVH1 domain' $EVH1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'polypproline binding module' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_EVH1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Human VASP Ena-Vasp homology domain 1' _Abbreviation_common EVH1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 115 _Mol_residue_sequence ; MSETVICSSRATVMLYDDGN KRWLPAGTGPQAFSRVQIYH NPTANSFRVVGRKMQPDQQV VINCAIVRGVKYNQATPNFH QWRDARQVWGLNFGSKEDAA QFAAGMASALEALEG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 GLU 4 THR 5 VAL 6 ILE 7 CYS 8 SER 9 SER 10 ARG 11 ALA 12 THR 13 VAL 14 MET 15 LEU 16 TYR 17 ASP 18 ASP 19 GLY 20 ASN 21 LYS 22 ARG 23 TRP 24 LEU 25 PRO 26 ALA 27 GLY 28 THR 29 GLY 30 PRO 31 GLN 32 ALA 33 PHE 34 SER 35 ARG 36 VAL 37 GLN 38 ILE 39 TYR 40 HIS 41 ASN 42 PRO 43 THR 44 ALA 45 ASN 46 SER 47 PHE 48 ARG 49 VAL 50 VAL 51 GLY 52 ARG 53 LYS 54 MET 55 GLN 56 PRO 57 ASP 58 GLN 59 GLN 60 VAL 61 VAL 62 ILE 63 ASN 64 CYS 65 ALA 66 ILE 67 VAL 68 ARG 69 GLY 70 VAL 71 LYS 72 TYR 73 ASN 74 GLN 75 ALA 76 THR 77 PRO 78 ASN 79 PHE 80 HIS 81 GLN 82 TRP 83 ARG 84 ASP 85 ALA 86 ARG 87 GLN 88 VAL 89 TRP 90 GLY 91 LEU 92 ASN 93 PHE 94 GLY 95 SER 96 LYS 97 GLU 98 ASP 99 ALA 100 ALA 101 GLN 102 PHE 103 ALA 104 ALA 105 GLY 106 MET 107 ALA 108 SER 109 ALA 110 LEU 111 GLU 112 ALA 113 LEU 114 GLU 115 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18569 EVH1 100.00 115 100.00 100.00 5.47e-80 PDB 1EGX "Solution Structure Of The Ena-Vasp Homology 1 (Evh1) Domain Of Human Vasodilator-Stimulated Phosphoprotein (Vasp)" 100.00 115 100.00 100.00 5.47e-80 DBJ BAG37336 "unnamed protein product [Homo sapiens]" 100.00 380 100.00 100.00 4.03e-80 DBJ BAJ21098 "vasodilator-stimulated phosphoprotein [synthetic construct]" 100.00 380 100.00 100.00 4.03e-80 EMBL CAA67147 "vasodilator-stimulated phosphoprotein [Homo sapiens]" 98.26 378 100.00 100.00 1.29e-78 EMBL CAA86523 "vasodilator-stimulated phosphoprotein (VASP) [Homo sapiens]" 100.00 380 100.00 100.00 4.03e-80 GB AAH26019 "Vasodilator-stimulated phosphoprotein [Homo sapiens]" 99.13 380 100.00 100.00 2.88e-79 GB AAH38224 "Vasodilator-stimulated phosphoprotein [Homo sapiens]" 100.00 380 100.00 100.00 4.03e-80 GB AIC59345 "VASP, partial [synthetic construct]" 99.13 380 100.00 100.00 2.88e-79 GB EAW57362 "vasodilator-stimulated phosphoprotein, isoform CRA_a [Homo sapiens]" 100.00 380 100.00 100.00 4.03e-80 GB EAW57363 "vasodilator-stimulated phosphoprotein, isoform CRA_b [Homo sapiens]" 88.70 367 100.00 100.00 3.99e-70 REF NP_003361 "vasodilator-stimulated phosphoprotein [Homo sapiens]" 100.00 380 100.00 100.00 4.03e-80 REF XP_001106536 "PREDICTED: vasodilator-stimulated phosphoprotein-like [Macaca mulatta]" 98.26 420 99.12 100.00 1.46e-77 REF XP_002829453 "PREDICTED: vasodilator-stimulated phosphoprotein-like [Pongo abelii]" 100.00 147 100.00 100.00 1.70e-80 REF XP_003277690 "PREDICTED: uncharacterized protein LOC100597154 [Nomascus leucogenys]" 100.00 363 100.00 100.00 7.34e-80 REF XP_003817563 "PREDICTED: vasodilator-stimulated phosphoprotein isoform X1 [Pan paniscus]" 100.00 380 100.00 100.00 4.54e-80 SP P50552 "RecName: Full=Vasodilator-stimulated phosphoprotein; Short=VASP [Homo sapiens]" 100.00 380 100.00 100.00 4.03e-80 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $EVH1 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $EVH1 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EVH1 1.0 mM '[U-13C; U-15N]' DTT 10 mM . KCl 50 mM . KPi 20 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $EVH1 1.0 mM [U-15N] DTT 10 mM . KCl 50 mM . KPi 20 mM . stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Saveframe_category software _Name xwinnmr _Version 2.9 loop_ _Task acqusition processing stop_ _Details . save_ save_xeasy _Saveframe_category software _Name xeasy _Version 1.3.14 loop_ _Task 'peak assignment' stop_ _Details . _Citation_label $ref_1 save_ save_talos _Saveframe_category software _Name talos _Version 1999.019.15.47 loop_ _Task assignment 'structure validation' stop_ _Details . _Citation_label $ref_2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCO_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HCC(CO)NH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name HCC(CO)NH-TOCSY _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 n/a temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 . direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'VASP EVH1 domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 MET N N 121.003 0.032 1 2 . 1 MET H H 8.278 0.014 1 3 . 1 MET CA C 53.340 0.000 1 4 . 1 MET HA H 4.309 0.000 1 5 . 1 MET CB C 30.209 0.000 1 6 . 1 MET HB2 H 2.365 0.000 1 7 . 1 MET HG2 H 1.909 0.000 1 8 . 1 MET C C 173.625 0.000 1 9 . 2 SER N N 116.117 0.067 1 10 . 2 SER H H 8.275 0.001 1 11 . 2 SER CA C 55.919 0.000 1 12 . 2 SER HA H 3.768 0.000 1 13 . 2 SER CB C 61.288 0.000 1 14 . 2 SER C C 171.292 0.000 1 15 . 3 GLU N N 119.075 0.077 1 16 . 3 GLU H H 7.860 0.000 1 17 . 3 GLU CA C 53.013 0.000 1 18 . 3 GLU HA H 4.777 0.000 1 19 . 3 GLU CB C 30.462 0.000 1 20 . 3 GLU HB2 H 1.857 0.000 1 21 . 3 GLU HG2 H 2.102 0.000 1 22 . 3 GLU C C 173.642 0.000 1 23 . 4 THR N N 116.283 0.074 1 24 . 4 THR H H 8.874 0.000 1 25 . 4 THR CA C 57.927 0.000 1 26 . 4 THR HA H 4.553 0.000 1 27 . 4 THR CB C 68.742 0.000 1 28 . 4 THR C C 170.996 0.000 1 29 . 5 VAL N N 125.428 0.366 1 30 . 5 VAL H H 8.576 0.002 1 31 . 5 VAL CA C 59.838 0.000 1 32 . 5 VAL HA H 4.013 0.000 1 33 . 5 VAL CB C 29.577 0.000 1 34 . 5 VAL HB H 1.778 0.000 1 35 . 5 VAL HG1 H 0.595 0.000 1 36 . 5 VAL HG2 H 0.454 0.000 1 37 . 5 VAL C C 174.562 0.000 1 38 . 6 ILE N N 123.571 0.007 1 39 . 6 ILE H H 8.864 0.013 1 40 . 6 ILE CA C 58.309 0.000 1 41 . 6 ILE HA H 4.258 0.000 1 42 . 6 ILE CB C 35.641 0.000 1 43 . 6 ILE HB H 1.873 0.000 1 44 . 6 ILE HG13 H 0.787 0.000 1 45 . 6 ILE HG12 H 1.120 0.000 1 46 . 6 ILE C C 173.56 0.000 1 47 . 7 CYS N N 114.316 0.227 1 48 . 7 CYS H H 7.174 0.000 1 49 . 7 CYS CA C 54.41 0.000 1 50 . 7 CYS HA H 4.573 0.000 1 51 . 7 CYS CB C 26.861 0.000 1 52 . 7 CYS HB2 H 2.790 0.000 1 53 . 7 CYS HB3 H 2.617 0.000 1 54 . 7 CYS C C 169.304 0.000 1 55 . 8 SER N N 117.450 0.097 1 56 . 8 SER H H 8.502 0.005 1 57 . 8 SER CA C 54.869 0.000 1 58 . 8 SER HA H 3.644 0.000 1 59 . 8 SER CB C 62.172 0.000 1 60 . 8 SER HB2 H 3.504 0.000 1 61 . 8 SER C C 170.848 0.000 1 62 . 9 SER N N 119.857 0.027 1 63 . 9 SER H H 9.168 0.000 1 64 . 9 SER CA C 55.175 0.000 1 65 . 9 SER HA H 3.881 0.000 1 66 . 9 SER CB C 64.573 0.000 1 67 . 9 SER HB2 H 3.750 0.000 1 68 . 9 SER C C 169.747 0.000 1 69 . 10 ARG N N 124.242 0.107 1 70 . 10 ARG H H 8.781 0.002 1 71 . 10 ARG CA C 52.27 0.000 1 72 . 10 ARG HA H 5.358 0.000 1 73 . 10 ARG CB C 29.451 0.000 1 74 . 10 ARG HB2 H 1.637 0.000 1 75 . 10 ARG HB3 H 1.532 0.000 1 76 . 10 ARG HG2 H 1.182 0.000 1 77 . 10 ARG C C 173.494 0.000 1 78 . 11 ALA N N 125.559 0.300 1 79 . 11 ALA H H 9.119 0.000 1 80 . 11 ALA CA C 49.159 0.000 1 81 . 11 ALA HA H 4.737 0.000 1 82 . 11 ALA HB H 0.425 0.000 1 83 . 11 ALA CB C 20.481 0.000 1 84 . 11 ALA C C 173.905 0.000 1 85 . 12 THR N N 118.974 0.161 1 86 . 12 THR H H 8.885 0.002 1 87 . 12 THR CA C 59.898 0.000 1 88 . 12 THR CB C 66.089 0.000 1 89 . 12 THR C C 171.637 0.000 1 90 . 13 VAL N N 127.690 0.232 1 91 . 13 VAL H H 8.227 0.005 1 92 . 13 VAL CA C 59.961 0.000 1 93 . 13 VAL HA H 4.145 0.000 1 94 . 13 VAL CB C 28.756 0.000 1 95 . 13 VAL HB H 1.830 0.000 1 96 . 13 VAL HG1 H 0.884 0.000 1 97 . 13 VAL HG2 H 0.595 0.000 1 98 . 13 VAL C C 172.886 0.000 1 99 . 14 MET N N 129.645 0.580 1 100 . 14 MET H H 9.877 0.010 1 101 . 14 MET CA C 50.802 0.000 1 102 . 14 MET HA H 5.409 0.000 1 103 . 14 MET CB C 33.873 0.000 1 104 . 14 MET HB2 H 2.251 0.000 1 105 . 14 MET HG2 H 1.725 0.000 1 106 . 14 MET C C 171.144 0.000 1 107 . 15 LEU N N 121.002 0.067 1 108 . 15 LEU H H 9.578 0.003 1 109 . 15 LEU CA C 50.97 0.000 1 110 . 15 LEU HA H 5.038 0.000 1 111 . 15 LEU CB C 43.98 0.000 1 112 . 15 LEU HB2 H 1.296 0.000 1 113 . 15 LEU C C 173.675 0.000 1 114 . 16 TYR N N 124.959 0.182 1 115 . 16 TYR H H 8.082 0.002 1 116 . 16 TYR CA C 55.476 0.000 1 117 . 16 TYR HA H 3.728 0.000 1 118 . 16 TYR CB C 35.705 0.000 1 119 . 16 TYR HB2 H 2.025 0.000 1 120 . 16 TYR HB3 H 0.904 0.000 1 121 . 16 TYR C C 171.818 0.000 1 122 . 17 ASP N N 128.127 0.354 1 123 . 17 ASP H H 8.047 0.001 1 124 . 17 ASP CA C 49.475 0.000 1 125 . 17 ASP HA H 3.583 0.000 1 126 . 17 ASP CB C 38.61 0.000 1 127 . 17 ASP HB2 H 2.617 0.000 1 128 . 17 ASP HB3 H 2.233 0.000 1 129 . 17 ASP C C 172.837 0.000 1 130 . 18 ASP N N 123.544 0.087 1 131 . 18 ASP H H 8.277 0.002 1 132 . 18 ASP CA C 53.799 0.000 1 133 . 18 ASP HA H 3.942 0.000 1 134 . 18 ASP CB C 38.989 0.000 1 135 . 18 ASP HB2 H 2.484 0.000 1 136 . 18 ASP C C 175.351 0.000 1 137 . 19 GLY N N 106.527 0.336 1 138 . 19 GLY H H 8.275 0.004 1 139 . 19 GLY CA C 44.09 0.000 1 140 . 19 GLY HA2 H 3.707 0.000 1 141 . 19 GLY C C 170.907 0.000 1 142 . 20 ASN N N 115.493 0.186 1 143 . 20 ASN H H 7.237 0.003 1 144 . 20 ASN CA C 50.206 0.000 1 145 . 20 ASN CB C 36.827 0.000 1 146 . 20 ASN HB2 H 2.504 0.000 1 147 . 20 ASN HB3 H 2.127 0.000 1 148 . 20 ASN C C 170.914 0.000 1 149 . 21 LYS N N 118.177 0.046 1 150 . 21 LYS H H 7.611 0.001 1 151 . 21 LYS CA C 53.897 0.000 1 152 . 21 LYS HA H 3.493 0.000 1 153 . 21 LYS CB C 26.125 0.000 1 154 . 21 LYS HB2 H 1.971 0.000 1 155 . 21 LYS HB3 H 1.620 0.000 1 156 . 21 LYS HG2 H 1.291 0.109 1 157 . 21 LYS C C 172.261 0.000 1 158 . 22 ARG N N 113.687 0.168 1 159 . 22 ARG H H 6.921 0.001 1 160 . 22 ARG CA C 51.276 0.000 1 161 . 22 ARG HA H 4.604 0.000 1 162 . 22 ARG CB C 30.841 0.000 1 163 . 22 ARG HB2 H 1.585 0.000 1 164 . 22 ARG HG2 H 1.191 0.000 1 165 . 22 ARG C C 170.848 0.000 1 166 . 23 TRP N N 121.494 0.202 1 167 . 23 TRP H H 8.659 0.001 1 168 . 23 TRP CA C 54.181 0.000 1 169 . 23 TRP HA H 4.808 0.000 1 170 . 23 TRP CB C 28.377 0.000 1 171 . 23 TRP HB2 H 2.908 0.000 1 172 . 23 TRP C C 173.445 0.000 1 173 . 24 LEU N N 122.971 0.120 1 174 . 24 LEU H H 9.029 0.002 1 175 . 24 LEU CA C 49.441 0.000 1 176 . 24 LEU CB C 41.642 0.000 1 177 . 24 LEU C C 171.525 0.000 1 178 . 25 PRO CA C 60.467 0.000 1 179 . 25 PRO HA H 4.900 0.000 1 180 . 25 PRO CB C 29.072 0.000 1 181 . 25 PRO HB2 H 2.101 0.000 1 182 . 25 PRO HB3 H 1.864 0.000 1 183 . 25 PRO C C 174.578 0.000 1 184 . 26 ALA N N 125.732 0.243 1 185 . 26 ALA H H 8.359 0.006 1 186 . 26 ALA CA C 49.948 0.000 1 187 . 26 ALA HA H 2.905 1.495 1 188 . 26 ALA CB C 17.828 0.000 1 189 . 27 GLY N N 110.626 0.245 1 190 . 27 GLY H H 8.856 0.004 1 191 . 27 GLY CA C 41.644 0.000 1 192 . 27 GLY HA2 H 4.309 0.000 1 193 . 27 GLY HA3 H 3.860 0.000 1 194 . 27 GLY C C 172.754 0.000 1 195 . 28 THR N N 111.410 0.233 1 196 . 28 THR H H 8.625 0.003 1 197 . 28 THR CA C 58.003 0.000 1 198 . 28 THR HA H 4.594 0.000 1 199 . 28 THR CB C 68.868 0.000 1 200 . 28 THR C C 172.771 0.000 1 201 . 29 GLY N N 109.181 0.279 1 202 . 29 GLY H H 8.471 0.003 1 203 . 29 GLY CA C 42.021 0.000 1 204 . 30 PRO CA C 52.255 0.000 1 205 . 30 PRO HA H 4.482 0.000 1 206 . 30 PRO CB C 27.682 0.000 1 207 . 30 PRO HB2 H 2.109 0.000 1 208 . 30 PRO HB3 H 1.855 0.000 1 209 . 30 PRO HG2 H 2.434 0.000 1 210 . 30 PRO C C 172.837 0.000 1 211 . 31 GLN N N 120.161 0.189 1 212 . 31 GLN H H 8.231 0.002 1 213 . 31 GLN CA C 53.455 0.000 1 214 . 31 GLN HA H 4.115 0.000 1 215 . 31 GLN CB C 26.229 0.000 1 216 . 31 GLN HB2 H 1.917 0.000 1 217 . 31 GLN HB3 H 1.830 0.000 1 218 . 31 GLN HG2 H 2.137 0.000 1 219 . 31 GLN C C 173.132 0.000 1 220 . 32 ALA N N 126.957 0.500 1 221 . 32 ALA H H 8.822 0.006 1 222 . 32 ALA CA C 49.033 0.000 1 223 . 32 ALA HA H 4.482 0.000 1 224 . 32 ALA HB H 1.241 0.000 1 225 . 32 ALA CB C 20.039 0.000 1 226 . 32 ALA C C 174.299 0.000 1 227 . 33 PHE N N 118.001 0.035 1 228 . 33 PHE H H 8.521 0.006 1 229 . 33 PHE CA C 56.933 0.000 1 230 . 33 PHE HA H 5.450 0.000 1 231 . 33 PHE CB C 38.421 0.000 1 232 . 33 PHE HB2 H 3.119 0.000 1 233 . 33 PHE HB3 H 2.759 0.000 1 234 . 33 PHE C C 172.738 0.000 1 235 . 34 SER N N 115.141 0.079 1 236 . 34 SER H H 8.756 0.002 1 237 . 34 SER CA C 56.613 0.000 1 238 . 34 SER CB C 63.688 0.000 1 239 . 34 SER C C 170.832 0.000 1 240 . 35 ARG N N 121.930 0.030 1 241 . 35 ARG H H 8.494 0.005 1 242 . 35 ARG CA C 52.697 0.000 1 243 . 35 ARG HA H 4.757 0.000 1 244 . 35 ARG CB C 27.429 0.000 1 245 . 35 ARG HB2 H 1.725 0.000 1 246 . 35 ARG HB3 H 1.883 0.000 1 247 . 35 ARG HG2 H 1.480 0.000 1 248 . 35 ARG C C 173.576 0.000 1 249 . 36 VAL N N 129.231 0.495 1 250 . 36 VAL H H 9.362 0.008 1 251 . 36 VAL CA C 58.538 0.000 1 252 . 36 VAL HA H 4.757 0.000 1 253 . 36 VAL CB C 30.019 0.000 1 254 . 36 VAL HB H 1.618 0.000 1 255 . 36 VAL HG1 H 0.497 0.000 1 256 . 36 VAL C C 172.015 0.000 1 257 . 37 GLN N N 123.710 0.385 1 258 . 37 GLN H H 9.095 0.004 1 259 . 37 GLN CA C 51.199 0.000 1 260 . 37 GLN HA H 5.450 0.000 1 261 . 37 GLN CB C 31.725 0.000 1 262 . 37 GLN HB2 H 1.964 0.000 1 263 . 37 GLN C C 172.327 0.000 1 264 . 38 ILE N N 117.834 0.218 1 265 . 38 ILE H H 7.513 0.003 1 266 . 38 ILE CA C 58.129 0.000 1 267 . 38 ILE HA H 5.002 0.000 1 268 . 38 ILE CB C 36.905 0.000 1 269 . 38 ILE HB H 1.393 0.000 1 270 . 38 ILE HG2 H 0.621 0.000 1 271 . 38 ILE C C 172.771 0.000 1 272 . 39 TYR N N 126.470 0.326 1 273 . 39 TYR H H 9.401 0.011 1 274 . 39 TYR CA C 53.875 0.000 1 275 . 39 TYR HA H 5.175 0.000 1 276 . 39 TYR CB C 39.431 0.000 1 277 . 39 TYR HB2 H 2.708 0.000 1 278 . 39 TYR C C 173.346 0.000 1 279 . 40 HIS N N 121.613 0.001 1 280 . 40 HIS H H 9.476 0.008 1 281 . 40 HIS CA C 49.9 0.000 1 282 . 40 HIS HA H 4.523 0.000 1 283 . 40 HIS CB C 32.42 0.000 1 284 . 40 HIS HB2 H 2.496 0.000 1 285 . 40 HIS C C 171.045 0.000 1 286 . 41 ASN N N 125.606 0.337 1 287 . 41 ASN H H 8.434 0.008 1 288 . 41 ASN CA C 46.57 0.000 1 289 . 41 ASN CB C 36.21 0.000 1 290 . 41 ASN HB2 H 1.969 0.000 1 291 . 41 ASN C C 171.87 0.000 1 292 . 42 PRO CA C 61.288 0.000 1 293 . 42 PRO HA H 3.677 0.000 1 294 . 42 PRO CB C 29.388 0.000 1 295 . 42 PRO HB3 H 1.803 0.000 1 296 . 42 PRO C C 175.548 0.000 1 297 . 43 THR N N 113.893 0.074 1 298 . 43 THR H H 7.657 0.001 1 299 . 43 THR CA C 62.743 0.000 1 300 . 43 THR HA H 4.064 0.000 1 301 . 43 THR CB C 65.583 0.000 1 302 . 43 THR HG2 H 1.118 0.000 1 303 . 43 THR C C 172.738 0.000 1 304 . 44 ALA N N 121.481 0.110 1 305 . 44 ALA H H 6.874 0.006 1 306 . 44 ALA CA C 48.906 0.000 1 307 . 44 ALA HA H 4.223 0.000 1 308 . 44 ALA HB H 1.128 0.000 1 309 . 44 ALA CB C 16.754 0.000 1 310 . 44 ALA C C 174.644 0.000 1 311 . 45 ASN N N 116.712 0.136 1 312 . 45 ASN H H 7.841 0.002 1 313 . 45 ASN CA C 51.123 0.000 1 314 . 45 ASN HA H 4.135 0.000 1 315 . 45 ASN CB C 34.631 0.000 1 316 . 45 ASN HB2 H 3.304 0.000 1 317 . 45 ASN HB3 H 2.417 0.000 1 318 . 45 ASN C C 169.912 0.000 1 319 . 46 SER N N 109.097 0.297 1 320 . 46 SER H H 7.492 0.003 1 321 . 46 SER CA C 53.493 0.000 1 322 . 46 SER HA H 4.074 0.000 1 323 . 46 SER CB C 64.194 0.000 1 324 . 46 SER HB2 H 3.495 0.000 1 325 . 46 SER C C 171.21 0.000 1 326 . 47 PHE N N 119.533 0.079 1 327 . 47 PHE H H 9.320 0.000 1 328 . 47 PHE CA C 53.951 0.000 1 329 . 47 PHE HA H 5.797 0.000 1 330 . 47 PHE CB C 42.337 0.000 1 331 . 47 PHE HB2 H 2.663 0.000 1 332 . 47 PHE C C 173.067 0.000 1 333 . 48 ARG N N 118.531 0.079 1 334 . 48 ARG H H 8.842 0.004 1 335 . 48 ARG CA C 52.27 0.000 1 336 . 48 ARG HA H 5.185 0.000 1 337 . 48 ARG CB C 31.409 0.000 1 338 . 48 ARG HB2 H 1.743 0.000 1 339 . 48 ARG HG2 H 1.524 0.000 1 340 . 48 ARG C C 171.029 0.000 1 341 . 49 VAL N N 122.356 0.040 1 342 . 49 VAL H H 9.143 0.001 1 343 . 49 VAL CA C 58.066 0.000 1 344 . 49 VAL HA H 5.002 0.000 1 345 . 49 VAL CB C 31.156 0.000 1 346 . 49 VAL HB H 1.944 0.000 1 347 . 49 VAL HG1 H 0.812 0.000 1 348 . 49 VAL C C 172.196 0.000 1 349 . 50 VAL N N 124.720 0.326 1 350 . 50 VAL H H 8.808 0.001 1 351 . 50 VAL CA C 57.94 0.000 1 352 . 50 VAL HA H 5.002 0.000 1 353 . 50 VAL CB C 32.925 0.000 1 354 . 50 VAL HB H 1.954 0.000 1 355 . 50 VAL HG1 H 0.925 0.000 1 356 . 50 VAL HG2 H 0.762 0.000 1 357 . 50 VAL C C 172.944 0.000 1 358 . 51 GLY N N 115.618 0.157 1 359 . 51 GLY H H 8.971 0.003 1 360 . 51 GLY CA C 42.332 0.000 1 361 . 51 GLY HA2 H 5.685 0.000 1 362 . 51 GLY HA3 H 3.057 0.000 1 363 . 51 GLY C C 173.355 0.000 1 364 . 52 ARG N N 123.065 0.071 1 365 . 52 ARG H H 8.051 0.001 1 366 . 52 ARG CA C 51.352 0.000 1 367 . 52 ARG HA H 5.277 0.000 1 368 . 52 ARG CB C 31.283 0.000 1 369 . 52 ARG HB2 H 1.550 0.000 1 370 . 52 ARG C C 173.346 0.000 1 371 . 53 LYS N N 124.940 0.198 1 372 . 53 LYS H H 9.116 0.002 1 373 . 53 LYS CA C 55.54 0.000 1 374 . 53 LYS HA H 4.472 0.000 1 375 . 53 LYS CB C 32.483 0.000 1 376 . 53 LYS HB2 H 1.637 0.000 1 377 . 53 LYS HG2 H 1.383 0.000 1 378 . 53 LYS C C 175.318 0.000 1 379 . 54 MET N N 121.877 0.107 1 380 . 54 MET H H 8.867 0.006 1 381 . 54 MET CA C 52.76 0.000 1 382 . 54 MET HA H 4.521 0.000 1 383 . 54 MET CB C 27.493 0.000 1 384 . 54 MET C C 172.246 0.000 1 385 . 55 GLN N N 120.457 0.033 1 386 . 55 GLN H H 8.557 0.038 1 387 . 55 GLN CA C 52.823 0.000 1 388 . 55 GLN CB C 27.556 0.000 1 389 . 56 PRO CA C 64.194 0.000 1 390 . 56 PRO HA H 4.166 0.000 1 391 . 56 PRO CB C 29.324 0.000 1 392 . 56 PRO HB2 H 2.311 0.000 1 393 . 56 PRO HB3 H 1.890 0.000 1 394 . 56 PRO C C 174.192 0.000 1 395 . 57 ASP N N 112.857 0.146 1 396 . 57 ASP H H 8.211 0.007 1 397 . 57 ASP CA C 51.658 0.000 1 398 . 57 ASP HA H 4.298 0.000 1 399 . 57 ASP CB C 37.157 0.000 1 400 . 57 ASP HB2 H 2.899 0.000 1 401 . 57 ASP HB3 H 2.575 0.000 1 402 . 57 ASP C C 173.79 0.000 1 403 . 58 GLN N N 115.909 0.029 1 404 . 58 GLN H H 8.316 0.004 1 405 . 58 GLN CA C 53.455 0.000 1 406 . 58 GLN HA H 4.468 0.000 1 407 . 58 GLN CB C 25.408 0.000 1 408 . 58 GLN HB2 H 2.084 0.000 1 409 . 58 GLN HG2 H 2.330 0.000 1 410 . 58 GLN C C 173.797 0.000 1 411 . 59 GLN N N 115.852 0.099 1 412 . 59 GLN H H 7.421 0.000 1 413 . 59 GLN CA C 54.869 0.000 1 414 . 59 GLN HA H 3.789 0.000 1 415 . 59 GLN CB C 28.693 0.000 1 416 . 59 GLN HB2 H 1.673 0.000 1 417 . 59 GLN HG2 H 2.067 0.000 1 418 . 59 GLN C C 173.757 0.000 1 419 . 60 VAL N N 126.866 0.270 1 420 . 60 VAL H H 8.731 0.002 1 421 . 60 VAL CA C 60.373 0.000 1 422 . 60 VAL HA H 4.380 0.000 1 423 . 60 VAL CB C 28.819 0.000 1 424 . 60 VAL HB H 2.025 0.000 1 425 . 60 VAL HG1 H 1.037 0.000 1 426 . 60 VAL HG2 H 0.925 0.000 1 427 . 60 VAL C C 175.104 0.000 1 428 . 61 VAL N N 119.962 0.071 1 429 . 61 VAL H H 8.356 0.002 1 430 . 61 VAL CA C 58.508 0.000 1 431 . 61 VAL HA H 4.461 0.000 1 432 . 61 VAL CB C 30.525 0.000 1 433 . 61 VAL HB H 2.046 0.000 1 434 . 61 VAL HG1 H 0.863 0.000 1 435 . 61 VAL HG2 H 0.700 0.000 1 436 . 61 VAL C C 171.867 0.000 1 437 . 62 ILE N N 116.389 0.163 1 438 . 62 ILE H H 7.183 0.005 1 439 . 62 ILE CA C 58.003 0.000 1 440 . 62 ILE HA H 4.054 0.000 1 441 . 62 ILE CB C 36.652 0.000 1 442 . 62 ILE HB H 1.366 0.000 1 443 . 62 ILE HG2 H 0.533 0.000 1 444 . 62 ILE C C 170.24 0.000 1 445 . 63 ASN N N 125.023 0.210 1 446 . 63 ASN H H 8.121 0.003 1 447 . 63 ASN CA C 50.053 0.000 1 448 . 63 ASN HA H 5.348 0.000 1 449 . 63 ASN CB C 35.136 0.000 1 450 . 63 ASN HB2 H 2.780 0.000 1 451 . 63 ASN HB3 H 2.566 0.000 1 452 . 63 ASN C C 171.867 0.000 1 453 . 64 CYS N N 119.774 0.019 1 454 . 64 CYS H H 8.835 0.003 1 455 . 64 CYS CA C 53.187 0.000 1 456 . 64 CYS HA H 5.012 0.000 1 457 . 64 CYS CB C 28.44 0.000 1 458 . 64 CYS HB2 H 2.812 0.000 1 459 . 64 CYS C C 170.536 0.000 1 460 . 65 ALA N N 126.960 0.400 1 461 . 65 ALA H H 8.844 0.003 1 462 . 65 ALA CA C 49.981 0.000 1 463 . 65 ALA HA H 4.533 0.000 1 464 . 65 ALA HB H 1.427 0.000 1 465 . 65 ALA CB C 16.88 0.000 1 466 . 65 ALA C C 175.17 0.000 1 467 . 66 ILE N N 123.013 0.126 1 468 . 66 ILE H H 8.146 0.003 1 469 . 66 ILE CA C 58.256 0.000 1 470 . 66 ILE HA H 4.033 0.000 1 471 . 66 ILE CB C 35.073 0.000 1 472 . 66 ILE HB H 1.506 0.000 1 473 . 66 ILE HG2 H 0.454 0.000 1 474 . 66 ILE C C 171.522 0.000 1 475 . 67 VAL N N 117.971 0.089 1 476 . 67 VAL H H 6.796 0.010 1 477 . 67 VAL CA C 56.245 0.000 1 478 . 67 VAL HA H 4.645 0.000 1 479 . 67 VAL CB C 32.672 0.000 1 480 . 67 VAL HB H 2.242 0.000 1 481 . 67 VAL HG1 H 1.015 0.000 1 482 . 67 VAL HG2 H 0.884 0.000 1 483 . 67 VAL C C 171.916 0.000 1 484 . 68 ARG N N 119.554 0.010 1 485 . 68 ARG H H 8.429 0.003 1 486 . 68 ARG CA C 55.71 0.000 1 487 . 68 ARG HA H 3.840 0.000 1 488 . 68 ARG CB C 27.619 0.000 1 489 . 68 ARG HB2 H 1.708 0.000 1 490 . 68 ARG HG2 H 1.559 0.000 1 491 . 68 ARG C C 175.061 0.000 1 492 . 69 GLY N N 113.357 0.217 1 493 . 69 GLY H H 8.973 0.003 1 494 . 69 GLY CA C 42.527 0.000 1 495 . 69 GLY HA2 H 4.278 0.000 1 496 . 69 GLY HA3 H 3.574 0.000 1 497 . 69 GLY C C 172.392 0.000 1 498 . 70 VAL N N 121.252 0.139 1 499 . 70 VAL H H 7.463 0.004 1 500 . 70 VAL CA C 61.288 0.000 1 501 . 70 VAL HA H 4.064 0.000 1 502 . 70 VAL CB C 29.64 0.000 1 503 . 70 VAL HB H 2.087 0.000 1 504 . 70 VAL HG1 H 1.251 0.000 1 505 . 70 VAL HG2 H 0.833 0.000 1 506 . 70 VAL C C 172.297 0.000 1 507 . 71 LYS N N 126.220 0.409 1 508 . 71 LYS H H 8.439 0.004 1 509 . 71 LYS CA C 51.813 0.000 1 510 . 71 LYS HA H 4.533 0.000 1 511 . 71 LYS CB C 30.082 0.000 1 512 . 71 LYS HB2 H 1.760 0.000 1 513 . 71 LYS HG2 H 1.410 0.000 1 514 . 71 LYS C C 172.076 0.000 1 515 . 72 TYR N N 127.700 0.434 1 516 . 72 TYR H H 8.690 0.001 1 517 . 72 TYR CA C 55.098 0.000 1 518 . 72 TYR HA H 4.971 0.000 1 519 . 72 TYR CB C 37.979 0.000 1 520 . 72 TYR HB2 H 2.829 0.000 1 521 . 72 TYR HB3 H 2.465 0.109 1 522 . 72 TYR C C 171.999 0.000 1 523 . 73 ASN N N 126.666 0.416 1 524 . 73 ASN H H 9.082 0.001 1 525 . 73 ASN CA C 49.791 0.000 1 526 . 73 ASN CB C 38.8 0.000 1 527 . 73 ASN HB2 H 2.688 0.000 1 528 . 73 ASN C C 172.048 0.000 1 529 . 74 GLN N N 125.366 0.316 1 530 . 74 GLN H H 8.722 0.005 1 531 . 74 GLN CA C 51.964 0.000 1 532 . 74 GLN HA H 4.125 0.000 1 533 . 74 GLN CB C 23.702 0.000 1 534 . 74 GLN HB2 H 1.436 0.000 1 535 . 74 GLN HG2 H 1.646 0.000 1 536 . 74 GLN C C 172.327 0.000 1 537 . 75 ALA N N 129.438 0.525 1 538 . 75 ALA H H 7.682 0.003 1 539 . 75 ALA CA C 52.958 0.000 1 540 . 75 ALA HA H 3.972 0.000 1 541 . 75 ALA HB H 1.480 0.000 1 542 . 75 ALA CB C 16.375 0.000 1 543 . 75 ALA C C 176.337 0.000 1 544 . 76 THR N N 109.493 0.348 1 545 . 76 THR H H 8.732 0.003 1 546 . 76 THR CA C 56.398 0.000 1 547 . 76 THR CB C 67.036 0.000 1 548 . 76 THR C C 170.752 0.000 1 549 . 77 PRO CA C 62.381 0.000 1 550 . 77 PRO HA H 4.459 0.000 1 551 . 77 PRO CB C 29.451 0.000 1 552 . 77 PRO HB2 H 1.917 0.000 1 553 . 77 PRO HB3 H 1.785 0.000 1 554 . 77 PRO C C 174.417 0.000 1 555 . 78 ASN N N 109.109 0.301 1 556 . 78 ASN H H 7.772 0.007 1 557 . 78 ASN CA C 50.681 0.000 1 558 . 78 ASN CB C 37.93 0.000 1 559 . 78 ASN HB2 H 2.759 0.000 1 560 . 78 ASN HB3 H 2.645 0.000 1 561 . 78 ASN C C 170.224 0.000 1 562 . 79 PHE N N 122.806 0.098 1 563 . 79 PHE H H 7.841 0.000 1 564 . 79 PHE CA C 54.104 0.000 1 565 . 79 PHE HA H 5.695 0.000 1 566 . 79 PHE CB C 38.294 0.000 1 567 . 79 PHE HB2 H 3.106 0.000 1 568 . 79 PHE HB3 H 2.525 0.000 1 569 . 79 PHE C C 171.276 0.000 1 570 . 80 HIS N N 125.802 0.473 1 571 . 80 HIS H H 8.006 0.008 1 572 . 80 HIS CA C 49.059 0.000 1 573 . 80 HIS HA H 5.450 0.000 1 574 . 80 HIS CB C 32.609 0.000 1 575 . 80 HIS HB2 H 2.996 0.000 1 576 . 80 HIS HB3 H 2.750 0.000 1 577 . 80 HIS C C 170.917 0.000 1 578 . 81 GLN N N 115.074 0.074 1 579 . 81 GLN H H 8.758 0.002 1 580 . 81 GLN CA C 51.623 0.000 1 581 . 81 GLN HA H 5.623 0.000 1 582 . 81 GLN CB C 31.599 0.000 1 583 . 81 GLN HB2 H 2.093 0.000 1 584 . 81 GLN HG2 H 1.900 0.000 1 585 . 81 GLN C C 171.489 0.000 1 586 . 82 TRP N N 119.178 0.093 1 587 . 82 TRP H H 9.026 0.004 1 588 . 82 TRP CA C 55.287 0.000 1 589 . 82 TRP HA H 5.256 0.000 1 590 . 82 TRP CB C 30.525 0.000 1 591 . 82 TRP HB2 H 3.565 0.000 1 592 . 82 TRP HB3 H 3.127 0.000 1 593 . 82 TRP C C 169.632 0.000 1 594 . 83 ARG N N 119.565 0.202 1 595 . 83 ARG H H 8.409 0.000 1 596 . 83 ARG CA C 52.318 0.000 1 597 . 83 ARG HA H 5.124 0.000 1 598 . 83 ARG CB C 30.588 0.000 1 599 . 83 ARG HB2 H 1.830 0.000 1 600 . 83 ARG HG2 H 1.594 0.000 1 601 . 83 ARG C C 173.707 0.000 1 602 . 84 ASP N N 126.177 0.391 1 603 . 84 ASP H H 8.898 0.004 1 604 . 84 ASP CA C 50.129 0.000 1 605 . 84 ASP HA H 4.512 0.000 1 606 . 84 ASP CB C 40.379 0.000 1 607 . 84 ASP HB2 H 2.978 0.000 1 608 . 84 ASP C C 172.952 0.000 1 609 . 85 ALA N N 120.951 0.046 1 610 . 85 ALA H H 8.483 0.002 1 611 . 85 ALA CA C 52.27 0.000 1 612 . 85 ALA HA H 4.012 0.000 1 613 . 85 ALA HB H 1.475 0.000 1 614 . 85 ALA CB C 15.68 0.000 1 615 . 85 ALA C C 175.548 0.000 1 616 . 86 ARG N N 116.586 0.116 1 617 . 86 ARG H H 8.569 0.003 1 618 . 86 ARG CA C 54.104 0.000 1 619 . 86 ARG HA H 4.398 0.000 1 620 . 86 ARG CB C 29.703 0.000 1 621 . 86 ARG HB2 H 1.857 0.000 1 622 . 86 ARG HG2 H 1.585 0.000 1 623 . 86 ARG C C 173.395 0.000 1 624 . 87 GLN N N 119.361 0.045 1 625 . 87 GLN H H 8.540 0.002 1 626 . 87 GLN CA C 52.652 0.000 1 627 . 87 GLN HA H 4.410 0.000 1 628 . 87 GLN CB C 29.072 0.000 1 629 . 87 GLN HB2 H 1.366 0.000 1 630 . 87 GLN HG2 H 1.637 0.000 1 631 . 87 GLN C C 170.553 0.000 1 632 . 88 VAL N N 121.106 0.004 1 633 . 88 VAL H H 8.142 0.000 1 634 . 88 VAL CA C 59.203 0.000 1 635 . 88 VAL HA H 4.360 0.000 1 636 . 88 VAL CB C 29.64 0.000 1 637 . 88 VAL HB H 1.690 0.000 1 638 . 88 VAL HG1 H 0.709 0.000 1 639 . 88 VAL C C 171.851 0.000 1 640 . 89 TRP N N 126.988 0.366 1 641 . 89 TRP H H 8.370 0.005 1 642 . 89 TRP CA C 52.958 0.000 1 643 . 89 TRP HA H 4.933 0.000 1 644 . 89 TRP CB C 28.945 0.000 1 645 . 89 TRP HB2 H 2.209 0.000 1 646 . 89 TRP HB3 H 1.199 0.000 1 647 . 89 TRP C C 173.118 0.000 1 648 . 90 GLY N N 106.082 0.410 1 649 . 90 GLY H H 8.859 0.003 1 650 . 90 GLY CA C 41.644 0.000 1 651 . 90 GLY HA2 H 4.686 0.000 1 652 . 90 GLY HA3 H 2.777 0.000 1 653 . 90 GLY C C 170.197 0.000 1 654 . 91 LEU N N 121.346 0.029 1 655 . 91 LEU H H 8.416 0.000 1 656 . 91 LEU CA C 49.9 0.000 1 657 . 91 LEU HA H 3.732 0.000 1 658 . 91 LEU CB C 42.021 0.000 1 659 . 91 LEU HB2 H 1.049 0.000 1 660 . 91 LEU HD1 H -0.362 0.000 1 661 . 91 LEU C C 170.175 0.000 1 662 . 92 ASN N N 119.373 0.150 1 663 . 92 ASN H H 8.005 0.003 1 664 . 92 ASN CA C 48.465 0.000 1 665 . 92 ASN HA H 5.336 0.000 1 666 . 92 ASN CB C 37.157 0.000 1 667 . 92 ASN HB2 H 2.780 0.000 1 668 . 92 ASN HB3 H 2.137 0.000 1 669 . 92 ASN C C 173.28 0.000 1 670 . 93 PHE N N 123.968 0.283 1 671 . 93 PHE H H 8.957 0.003 1 672 . 93 PHE CA C 57.056 0.000 1 673 . 93 PHE HA H 4.451 0.000 1 674 . 93 PHE CB C 39.179 0.000 1 675 . 93 PHE HB2 H 3.208 0.000 1 676 . 93 PHE HB3 H 2.759 0.000 1 677 . 93 PHE C C 174.492 0.000 1 678 . 94 GLY N N 106.859 0.291 1 679 . 94 GLY H H 9.110 0.000 1 680 . 94 GLY CA C 43.727 0.000 1 681 . 94 GLY HA2 H 4.003 0.000 1 682 . 94 GLY HA3 H 3.493 0.000 1 683 . 94 GLY C C 172.123 0.000 1 684 . 95 SER N N 109.973 0.241 1 685 . 95 SER H H 7.559 0.000 1 686 . 95 SER CA C 54.563 0.000 1 687 . 95 SER HA H 4.195 0.000 1 688 . 95 SER CB C 63.878 0.000 1 689 . 95 SER HB2 H 4.054 0.000 1 690 . 95 SER C C 172.146 0.000 1 691 . 96 LYS N N 122.524 0.098 1 692 . 96 LYS H H 9.063 0.000 1 693 . 96 LYS CA C 56.424 0.000 1 694 . 96 LYS HA H 4.083 0.000 1 695 . 96 LYS CB C 29.64 0.000 1 696 . 96 LYS HB2 H 1.786 0.000 1 697 . 96 LYS C C 176.592 0.000 1 698 . 97 GLU N N 121.695 0.098 1 699 . 97 GLU H H 8.794 0.003 1 700 . 97 GLU CA C 57.927 0.000 1 701 . 97 GLU HA H 4.023 0.000 1 702 . 97 GLU CB C 25.85 0.000 1 703 . 97 GLU HB2 H 1.900 0.000 1 704 . 97 GLU HG2 H 2.067 0.000 1 705 . 97 GLU C C 176.583 0.000 1 706 . 98 ASP N N 120.377 0.191 1 707 . 98 ASP H H 7.814 0.003 1 708 . 98 ASP CA C 54.945 0.000 1 709 . 98 ASP HA H 4.349 0.000 1 710 . 98 ASP CB C 39.495 0.000 1 711 . 98 ASP HB2 H 2.917 0.000 1 712 . 98 ASP C C 175.762 0.000 1 713 . 99 ALA N N 122.249 0.226 1 714 . 99 ALA H H 7.122 0.000 1 715 . 99 ALA CA C 51.199 0.000 1 716 . 99 ALA HA H 4.125 0.000 1 717 . 99 ALA HB H 0.945 0.000 1 718 . 99 ALA CB C 17.259 0.000 1 719 . 99 ALA C C 176.041 0.000 1 720 . 100 ALA N N 119.182 0.074 1 721 . 100 ALA H H 7.938 0.007 1 722 . 100 ALA CA C 52.255 0.000 1 723 . 100 ALA HA H 4.039 0.000 1 724 . 100 ALA HB H 1.404 0.000 1 725 . 100 ALA CB C 15.554 0.000 1 726 . 100 ALA C C 179.245 0.000 1 727 . 101 GLN N N 117.146 0.074 1 728 . 101 GLN H H 7.940 0.001 1 729 . 101 GLN CA C 55.71 0.000 1 730 . 101 GLN HA H 3.972 0.000 1 731 . 101 GLN CB C 25.85 0.000 1 732 . 101 GLN HB2 H 2.111 0.000 1 733 . 101 GLN HG2 H 2.453 0.000 1 734 . 101 GLN C C 176.254 0.000 1 735 . 102 PHE N N 122.346 0.196 1 736 . 102 PHE H H 7.717 0.003 1 737 . 102 PHE CA C 59.303 0.000 1 738 . 102 PHE HA H 4.105 0.000 1 739 . 102 PHE CB C 37.663 0.000 1 740 . 102 PHE HB2 H 3.048 0.000 1 741 . 102 PHE HB3 H 2.899 0.000 1 742 . 102 PHE C C 174.792 0.000 1 743 . 103 ALA N N 119.806 0.155 1 744 . 103 ALA H H 8.589 0.003 1 745 . 103 ALA CA C 52.575 0.000 1 746 . 103 ALA HA H 3.748 0.000 1 747 . 103 ALA HB H 1.506 0.000 1 748 . 103 ALA CB C 15.617 0.000 1 749 . 103 ALA C C 178.095 0.000 1 750 . 104 ALA N N 119.638 0.009 1 751 . 104 ALA H H 7.666 0.001 1 752 . 104 ALA CA C 52.117 0.000 1 753 . 104 ALA HA H 4.004 0.000 1 754 . 104 ALA HB H 1.322 0.000 1 755 . 104 ALA CB C 15.111 0.000 1 756 . 104 ALA C C 178.266 0.000 1 757 . 105 GLY N N 108.488 0.226 1 758 . 105 GLY H H 7.563 0.001 1 759 . 105 GLY CA C 44.396 0.000 1 760 . 105 GLY HA2 H 3.494 0.000 1 761 . 105 GLY HA3 H 3.363 0.000 1 762 . 105 GLY C C 175.155 0.000 1 763 . 106 MET N N 121.535 0.097 1 764 . 106 MET H H 8.064 0.001 1 765 . 106 MET CA C 53.897 0.000 1 766 . 106 MET HA H 3.544 0.000 1 767 . 106 MET CB C 27.24 0.000 1 768 . 106 MET HB2 H 1.243 0.000 1 769 . 106 MET HG2 H 0.928 0.000 1 770 . 106 MET C C 175.17 0.000 1 771 . 107 ALA N N 119.688 0.106 1 772 . 107 ALA H H 7.885 0.002 1 773 . 107 ALA CA C 52.551 0.000 1 774 . 107 ALA HA H 3.758 0.000 1 775 . 107 ALA HB H 1.261 0.000 1 776 . 107 ALA CB C 14.796 0.000 1 777 . 107 ALA C C 178.276 0.000 1 778 . 108 SER N N 113.882 0.105 1 779 . 108 SER H H 7.570 0.000 1 780 . 108 SER CA C 58.508 0.000 1 781 . 108 SER HA H 3.723 0.000 1 782 . 108 SER CB C 59.961 0.000 1 783 . 108 SER C C 175.424 0.000 1 784 . 109 ALA N N 125.865 0.467 1 785 . 109 ALA H H 7.525 0.002 1 786 . 109 ALA CA C 51.582 0.000 1 787 . 109 ALA HA H 2.593 0.000 1 788 . 109 ALA HB H 0.323 0.000 1 789 . 109 ALA CB C 14.922 0.000 1 790 . 109 ALA C C 175.433 0.000 1 791 . 110 LEU N N 115.022 0.116 1 792 . 110 LEU H H 7.961 0.003 1 793 . 110 LEU CA C 55.098 0.000 1 794 . 110 LEU HA H 3.575 0.000 1 795 . 110 LEU CB C 38.042 0.000 1 796 . 110 LEU HB2 H 1.576 0.000 1 797 . 110 LEU HB3 H 1.252 0.000 1 798 . 110 LEU C C 177.848 0.000 1 799 . 111 GLU N N 118.327 0.074 1 800 . 111 GLU H H 7.811 0.000 1 801 . 111 GLU CA C 56.398 0.000 1 802 . 111 GLU HA H 3.881 0.000 1 803 . 111 GLU CB C 27.05 0.000 1 804 . 111 GLU HB2 H 1.927 0.000 1 805 . 111 GLU HG2 H 2.172 0.000 1 806 . 111 GLU C C 176.912 0.000 1 807 . 112 ALA N N 121.885 0.214 1 808 . 112 ALA H H 7.466 0.007 1 809 . 112 ALA CA C 52.002 0.000 1 810 . 112 ALA HA H 4.074 0.000 1 811 . 112 ALA HB H 1.515 0.000 1 812 . 112 ALA CB C 16.059 0.000 1 813 . 112 ALA C C 178.111 0.000 1 814 . 113 LEU N N 117.049 0.074 1 815 . 113 LEU H H 7.732 0.006 1 816 . 113 LEU CA C 53.722 0.000 1 817 . 113 LEU HA H 4.156 0.000 1 818 . 113 LEU CB C 40.632 0.000 1 819 . 113 LEU HB2 H 1.751 0.000 1 820 . 113 LEU HB3 H 1.322 0.000 1 821 . 113 LEU C C 175.646 0.000 1 822 . 114 GLU N N 118.131 0.026 1 823 . 114 GLU H H 7.544 0.003 1 824 . 114 GLU CA C 54.402 0.000 1 825 . 114 GLU HA H 4.115 0.000 1 826 . 114 GLU CB C 27.493 0.000 1 827 . 114 GLU HB2 H 2.058 0.000 1 828 . 114 GLU HG2 H 2.321 0.000 1 829 . 114 GLU C C 174.034 0.000 1 830 . 115 GLY N N 113.010 0.123 1 831 . 115 GLY H H 7.545 0.000 1 832 . 115 GLY CA C 43.727 0.000 1 stop_ save_