data_5334 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N resonance assignments and secondary structure of the D54A mutant of HTLV-I capsid protein ; _BMRB_accession_number 5334 _BMRB_flat_file_name bmr5334.str _Entry_type original _Submission_date 2002-03-26 _Accession_date 2002-03-26 _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 Cornilescu Claudia C. . 2 Bouamr Fadila . . 3 Carter Carol . . 4 Tjandra Nico . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 410 "13C chemical shifts" 361 "15N chemical shifts" 115 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-06-10 original author . stop_ _Original_release_date 2003-06-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Backbone 1H, 13C, and 15N resonance assignments and secondary structure of the D54A mutant of HTLV-I capsid protein ; _Citation_status 'in preparation' _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cornilescu Claudia C. . 2 Bouamr Fadila . . 3 Carter Carol . . 4 Tjandra Nico . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword HTLV-I mutant retrovirus 'capsid protein' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Cornilescu, C. C., Bouamr, F., Yao, X., Carter, C. & Tjandra, N. (2001) J. Mol. Biol., 306, 783-797. ; _Citation_title 'Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11243788 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cornilescu 'C. C.' C. . 2 Bouamr F. . . 3 Yao X. . . 4 Carter C. . . 5 Tjandra N. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 306 _Journal_issue 4 _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 783 _Page_last 797 _Year 2001 _Details ; The N-terminal domain of the retroviral capsid (CA) protein is one of the least conserved regions encoded in the genome. Surprisingly, the three-dimensional structures of the CA from different genera exhibit alpha-helical structural features that are highly conserved. The N-terminal residues of the human immunodeficiency virus type 1 (HIV-1) and Rous sarcoma virus (RSV) capsid proteins form a beta-hairpin. To determine if this feature is conserved in the retroviral family, we cloned, expressed, purified, and solved the structure of a N-terminal 134 amino acid fragment (CA(134)) from the human T-cell leukemia virus type 1 (HTLV-I) using high resolution nuclear magnetic resonance (NMR) spectroscopy. The CA(134) fragment contains an N-terminal beta-hairpin and a central coiled-coil-like structure composed of six alpha-helices. The N-terminal Pro1 residue contacts Asp54 in the helical cluster through a salt bridge. Thus, the beta-hairpin is conserved and the helical cluster is structurally similar to other retroviral CA domains. However, although the same Asp residue defines the orientation of the hairpin in both the HTLV-1 and HIV-1 CA proteins, the HTLV-I hairpin is oriented away, rather than towards, the helical core. Significant differences were also detected in the spatial orientation and helical content of the long centrally located loop connecting the helices in the core. It has been proposed that the salt bridge allows the formation of a CA-CA interface that is important for the assembly of the conical cores that are characteristic of HIV-1. As HTLV-I forms spherical cores, the salt-bridge feature is apparently not conserved for this function although its role in determining the orientation of the beta-hairpin may be critical, along with the central loop. Comparison of three-dimensional structures is expected to elucidate the relationships between the retroviral capsid protein structure and its function. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. & Bax, A. (1995) J. Biomol. NMR, 6, 277-293. ; _Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8520220 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Delaglio F. . . 2 Grzesiek S. . . 3 Vuister 'G. W.' W. . 4 Zhu G. . . 5 Pfeifer J. . . 6 Bax A. . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _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 277 _Page_last 293 _Year 1995 _Details ; The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks. ; save_ save_ref_3 _Saveframe_category citation _Citation_full ; Cornilescu, G., Delaglio, F. & Bax, A. (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_4 _Saveframe_category citation _Citation_full ; Garrett, D. S., Powers, R., Gronenborn, A. M. & Clore, G. M. (1991) J. Magn. Reson, 95, 214-220. ; _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_ ################################## # Molecular system description # ################################## save_system_NTD_HTLV-I_CA _Saveframe_category molecular_system _Mol_system_name 'NTD HTLV-I capsid protein' _Abbreviation_common 'NTD HTLV-I CA' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HTLV-I $HTLV-I stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details 'Residue Asp 54 has been replaced by an Ala.' save_ ######################## # Monomeric polymers # ######################## save_HTLV-I _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Human T-cell Leukemia Virus type I' _Name_variant D54A _Abbreviation_common HTLV-I _Molecular_mass 14841.8 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 134 _Mol_residue_sequence ; PVMHPHGAPPNHRPWQMKDL QAIKQEVSQAAPGSPQFMQT IRLAVQQFDPTAKALQDLLQ YLCSSLVASLHHQQLDSLIS EAETRGITSYNPLAGPLRVQ ANNPQQQGLRREYQQLWLAA FAALPGSAKDPSWA ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 VAL 3 MET 4 HIS 5 PRO 6 HIS 7 GLY 8 ALA 9 PRO 10 PRO 11 ASN 12 HIS 13 ARG 14 PRO 15 TRP 16 GLN 17 MET 18 LYS 19 ASP 20 LEU 21 GLN 22 ALA 23 ILE 24 LYS 25 GLN 26 GLU 27 VAL 28 SER 29 GLN 30 ALA 31 ALA 32 PRO 33 GLY 34 SER 35 PRO 36 GLN 37 PHE 38 MET 39 GLN 40 THR 41 ILE 42 ARG 43 LEU 44 ALA 45 VAL 46 GLN 47 GLN 48 PHE 49 ASP 50 PRO 51 THR 52 ALA 53 LYS 54 ALA 55 LEU 56 GLN 57 ASP 58 LEU 59 LEU 60 GLN 61 TYR 62 LEU 63 CYS 64 SER 65 SER 66 LEU 67 VAL 68 ALA 69 SER 70 LEU 71 HIS 72 HIS 73 GLN 74 GLN 75 LEU 76 ASP 77 SER 78 LEU 79 ILE 80 SER 81 GLU 82 ALA 83 GLU 84 THR 85 ARG 86 GLY 87 ILE 88 THR 89 SER 90 TYR 91 ASN 92 PRO 93 LEU 94 ALA 95 GLY 96 PRO 97 LEU 98 ARG 99 VAL 100 GLN 101 ALA 102 ASN 103 ASN 104 PRO 105 GLN 106 GLN 107 GLN 108 GLY 109 LEU 110 ARG 111 ARG 112 GLU 113 TYR 114 GLN 115 GLN 116 LEU 117 TRP 118 LEU 119 ALA 120 ALA 121 PHE 122 ALA 123 ALA 124 LEU 125 PRO 126 GLY 127 SER 128 ALA 129 LYS 130 ASP 131 PRO 132 SER 133 TRP 134 ALA 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 4649 HTLV-I 100.00 134 99.25 99.25 5.21e-90 PDB 1G03 "Nmr Structure Of N-Terminal Domain Of Htlv-I Ca1-134" 99.25 134 99.25 99.25 2.77e-89 DBJ BAA02929 "gag polyprotein precursor [Human T-lymphotropic virus 1]" 100.00 429 98.51 98.51 3.47e-85 DBJ BAF31288 "gag protein [eukaryotic synthetic construct]" 100.00 429 97.76 99.25 1.57e-84 DBJ BAH85785 "Gag protein [Human T-lymphotropic virus 1]" 100.00 429 98.51 98.51 3.83e-85 DBJ BAP28584 "Gag protein [Human T-lymphotropic virus 1]" 100.00 429 98.51 98.51 3.70e-85 EMBL CAA34075 "unnamed protein product [Human T-lymphotropic virus 1]" 100.00 429 99.25 99.25 9.01e-86 EMBL CAA62992 "p24 protein [Human T-lymphotropic virus 1]" 99.25 213 98.50 98.50 5.30e-88 GB AAA85325 "gag protein [Human T-lymphotropic virus 1]" 100.00 429 98.51 98.51 3.83e-85 GB AAA85841 "gag [Human T-lymphotropic virus 1]" 100.00 429 98.51 98.51 3.83e-85 GB AAA96672 "gag [Human T-lymphotropic virus 1]" 100.00 429 98.51 98.51 2.86e-85 GB AAB20767 "Gag [Human T-lymphotropic virus 1]" 100.00 429 97.76 98.51 2.24e-84 GB AAC00185 "gag protein [Human T-lymphotropic virus 1]" 100.00 429 98.51 98.51 3.83e-85 REF NP_049558 "gag polyprotein [Simian T-lymphotropic virus 1]" 100.00 428 97.76 98.51 3.33e-84 REF NP_057860 "Pr gag-pro-pol [Human T-lymphotropic virus 1]" 100.00 1462 98.51 98.51 4.60e-80 REF NP_057861 "Pr gag-pro [Human T-lymphotropic virus 1]" 100.00 651 98.51 98.51 2.87e-83 REF NP_057862 "Pr55 [Human T-lymphotropic virus 1]" 100.00 429 98.51 98.51 3.47e-85 REF NP_955618 "p24 CA [Human T-lymphotropic virus 1]" 100.00 215 98.51 98.51 7.96e-89 SP P03345 "RecName: Full=Gag polyprotein; AltName: Full=Pr53Gag; Contains: RecName: Full=Matrix protein p19; Short=MA; Contains: RecName: " 100.00 429 98.51 98.51 2.86e-85 SP P03362 "RecName: Full=Gag-Pro-Pol polyprotein; AltName: Full=Pr160Gag-Pro-Pol; Contains: RecName: Full=Matrix protein p19; Short=MA; Co" 100.00 1462 98.51 98.51 4.16e-80 SP P10274 "RecName: Full=Gag-Pro polyprotein; AltName: Full=Pr76Gag-Pro; Contains: RecName: Full=Matrix protein p19; Short=MA; Contains: R" 100.00 651 98.51 98.51 2.50e-83 SP P14074 "RecName: Full=Gag-Pro polyprotein; AltName: Full=Pr76Gag-Pro; Contains: RecName: Full=Matrix protein p19; Short=MA; Contains: R" 100.00 651 98.51 98.51 2.87e-83 SP P14076 "RecName: Full=Gag polyprotein; AltName: Full=Pr53Gag; Contains: RecName: Full=Matrix protein p19; Short=MA; Contains: RecName: " 100.00 429 98.51 98.51 3.47e-85 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HTLV-I 'Human T-cell lymphotropic virus type 1' 11908 Viruses . Deltaretrovirus HTLV-I 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 $HTLV-I 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_N15_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $HTLV-I . mM 0.8 1.0 [U-15N] stop_ save_ save_C13-N15_sample _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $HTLV-I . mM 0.8 1.0 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Task 'processed data' stop_ _Details . _Citation_label $ref_2 save_ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Task 'predicted torsion angles' stop_ _Details . _Citation_label $ref_3 save_ save_PIPP_STAPP _Saveframe_category software _Name PIPP_STAPP _Version . loop_ _Task 'peak assignments' stop_ _Details . _Citation_label $ref_4 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_CBCACONH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HBHACONH_4 _Saveframe_category NMR_applied_experiment _Experiment_name HBHACONH _Sample_label . save_ save_3D_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label . save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label . save_ save_1H-13C_CT-HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C CT-HSQC' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.05 n/a temperature 300 0.2 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 internal direct . . . 1.000000000 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_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $N15_sample $C13-N15_sample stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name HTLV-I _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 . 2 VAL HA H 3.952 . 1 2 . 2 VAL HB H 1.882 . 1 3 . 2 VAL C C 175.661 . 1 4 . 2 VAL CA C 62.744 . 1 5 . 2 VAL CB C 32.603 . 1 6 . 3 MET H H 8.427 . 1 7 . 3 MET HA H 4.337 . 1 8 . 3 MET HB2 H 1.828 . 1 9 . 3 MET HB3 H 1.828 . 1 10 . 3 MET C C 175.457 . 1 11 . 3 MET CA C 55.123 . 1 12 . 3 MET CB C 33.082 . 1 13 . 3 MET N N 124.513 . 1 14 . 4 HIS H H 8.385 . 1 15 . 4 HIS CA C 53.867 . 1 16 . 4 HIS CB C 29.913 . 1 17 . 4 HIS N N 121.194 . 1 18 . 5 PRO HA H 4.652 . 1 19 . 5 PRO HB2 H 1.430 . 2 20 . 5 PRO HB3 H 1.953 . 2 21 . 5 PRO C C 176.537 . 1 22 . 5 PRO CA C 64.121 . 1 23 . 5 PRO CB C 32.179 . 1 24 . 6 HIS H H 8.408 . 1 25 . 6 HIS HA H 4.579 . 1 26 . 6 HIS HB2 H 3.088 . 1 27 . 6 HIS HB3 H 3.088 . 1 28 . 6 HIS C C 175.387 . 1 29 . 6 HIS CA C 55.782 . 1 30 . 6 HIS CB C 29.931 . 1 31 . 6 HIS N N 115.135 . 1 32 . 7 GLY H H 8.249 . 1 33 . 7 GLY HA2 H 3.825 . 1 34 . 7 GLY HA3 H 3.825 . 1 35 . 7 GLY C C 173.171 . 1 36 . 7 GLY CA C 45.046 . 1 37 . 7 GLY N N 109.859 . 1 38 . 8 ALA H H 8.107 . 1 39 . 8 ALA CA C 50.498 . 1 40 . 8 ALA CB C 18.481 . 1 41 . 8 ALA N N 124.625 . 1 42 . 10 PRO HA H 4.256 . 1 43 . 10 PRO HB2 H 1.652 . 2 44 . 10 PRO HB3 H 2.093 . 2 45 . 10 PRO C C 176.522 . 1 46 . 10 PRO CA C 63.105 . 1 47 . 10 PRO CB C 32.111 . 1 48 . 11 ASN H H 8.287 . 1 49 . 11 ASN HB2 H 2.191 . 1 50 . 11 ASN HB3 H 2.191 . 1 51 . 11 ASN C C 174.758 . 1 52 . 11 ASN CA C 53.107 . 1 53 . 11 ASN CB C 39.096 . 1 54 . 11 ASN N N 117.976 . 1 55 . 12 HIS H H 8.273 . 1 56 . 12 HIS HA H 4.487 . 1 57 . 12 HIS HB2 H 2.962 . 1 58 . 12 HIS HB3 H 2.962 . 1 59 . 12 HIS CA C 55.950 . 1 60 . 12 HIS CB C 29.984 . 1 61 . 12 HIS N N 118.996 . 1 62 . 13 ARG H H 8.113 . 1 63 . 13 ARG CA C 54.023 . 1 64 . 13 ARG CB C 30.244 . 1 65 . 13 ARG N N 122.952 . 1 66 . 14 PRO HA H 4.331 . 1 67 . 14 PRO HB2 H 1.711 . 2 68 . 14 PRO HB3 H 2.026 . 2 69 . 14 PRO C C 176.804 . 1 70 . 14 PRO CA C 62.499 . 1 71 . 14 PRO CB C 32.248 . 1 72 . 15 TRP H H 7.276 . 1 73 . 15 TRP HA H 4.249 . 1 74 . 15 TRP HB2 H 2.070 . 2 75 . 15 TRP HB3 H 2.605 . 2 76 . 15 TRP C C 177.530 . 1 77 . 15 TRP CA C 55.009 . 1 78 . 15 TRP CB C 28.092 . 1 79 . 15 TRP N N 117.022 . 1 80 . 16 GLN H H 9.328 . 1 81 . 16 GLN HA H 4.586 . 1 82 . 16 GLN HB2 H 1.855 . 2 83 . 16 GLN HB3 H 2.328 . 2 84 . 16 GLN C C 177.662 . 1 85 . 16 GLN CA C 53.828 . 1 86 . 16 GLN CB C 31.232 . 1 87 . 16 GLN N N 118.636 . 1 88 . 17 MET H H 8.915 . 1 89 . 17 MET HA H 3.998 . 1 90 . 17 MET HB2 H 1.948 . 1 91 . 17 MET HB3 H 1.948 . 1 92 . 17 MET CA C 58.736 . 1 93 . 17 MET CB C 30.743 . 1 94 . 17 MET N N 123.118 . 1 95 . 18 LYS H H 8.571 . 1 96 . 18 LYS HA H 4.013 . 1 97 . 18 LYS HB2 H 1.702 . 1 98 . 18 LYS HB3 H 1.702 . 1 99 . 18 LYS C C 178.989 . 1 100 . 18 LYS CA C 59.221 . 1 101 . 18 LYS CB C 31.852 . 1 102 . 18 LYS N N 115.584 . 1 103 . 19 ASP H H 7.159 . 1 104 . 19 ASP HA H 4.414 . 1 105 . 19 ASP HB2 H 2.508 . 2 106 . 19 ASP HB3 H 2.741 . 2 107 . 19 ASP C C 178.064 . 1 108 . 19 ASP CA C 57.105 . 1 109 . 19 ASP CB C 42.034 . 1 110 . 19 ASP N N 118.465 . 1 111 . 20 LEU H H 7.261 . 1 112 . 20 LEU HA H 3.313 . 1 113 . 20 LEU HB2 H 1.216 . 1 114 . 20 LEU HB3 H 1.216 . 1 115 . 20 LEU C C 178.679 . 1 116 . 20 LEU CA C 57.953 . 1 117 . 20 LEU CB C 39.943 . 1 118 . 20 LEU N N 119.466 . 1 119 . 21 GLN H H 8.332 . 1 120 . 21 GLN HA H 4.019 . 1 121 . 21 GLN HB2 H 1.989 . 1 122 . 21 GLN HB3 H 1.989 . 1 123 . 21 GLN C C 178.654 . 1 124 . 21 GLN CA C 58.973 . 1 125 . 21 GLN CB C 28.324 . 1 126 . 21 GLN N N 117.214 . 1 127 . 22 ALA H H 7.409 . 1 128 . 22 ALA HA H 4.085 . 1 129 . 22 ALA HB H 1.510 . 1 130 . 22 ALA C C 180.507 . 1 131 . 22 ALA CA C 55.369 . 1 132 . 22 ALA CB C 18.139 . 1 133 . 22 ALA N N 121.958 . 1 134 . 23 ILE H H 7.735 . 1 135 . 23 ILE HA H 3.484 . 1 136 . 23 ILE HB H 1.579 . 1 137 . 23 ILE C C 177.359 . 1 138 . 23 ILE CA C 65.473 . 1 139 . 23 ILE CB C 38.545 . 1 140 . 23 ILE N N 120.026 . 1 141 . 24 LYS H H 8.209 . 1 142 . 24 LYS HA H 3.643 . 1 143 . 24 LYS HB2 H 1.666 . 2 144 . 24 LYS HB3 H 2.012 . 2 145 . 24 LYS C C 178.982 . 1 146 . 24 LYS CA C 59.950 . 1 147 . 24 LYS CB C 32.965 . 1 148 . 24 LYS N N 118.622 . 1 149 . 25 GLN H H 8.131 . 1 150 . 25 GLN HA H 3.954 . 1 151 . 25 GLN HB2 H 2.108 . 1 152 . 25 GLN HB3 H 2.108 . 1 153 . 25 GLN C C 178.910 . 1 154 . 25 GLN CA C 58.861 . 1 155 . 25 GLN CB C 28.471 . 1 156 . 25 GLN N N 117.586 . 1 157 . 26 GLU H H 7.835 . 1 158 . 26 GLU HA H 4.022 . 1 159 . 26 GLU HB2 H 2.067 . 1 160 . 26 GLU HB3 H 2.067 . 1 161 . 26 GLU C C 179.111 . 1 162 . 26 GLU CA C 59.222 . 1 163 . 26 GLU CB C 30.130 . 1 164 . 26 GLU N N 119.623 . 1 165 . 27 VAL H H 7.897 . 1 166 . 27 VAL HA H 4.098 . 1 167 . 27 VAL HB H 2.414 . 1 168 . 27 VAL C C 176.935 . 1 169 . 27 VAL CA C 62.905 . 1 170 . 27 VAL CB C 31.755 . 1 171 . 27 VAL N N 112.113 . 1 172 . 28 SER H H 7.586 . 1 173 . 28 SER HA H 4.037 . 1 174 . 28 SER HB2 H 3.836 . 1 175 . 28 SER HB3 H 3.836 . 1 176 . 28 SER C C 175.591 . 1 177 . 28 SER CA C 60.740 . 1 178 . 28 SER CB C 62.682 . 1 179 . 28 SER N N 115.068 . 1 180 . 29 GLN H H 8.367 . 1 181 . 29 GLN HA H 4.332 . 1 182 . 29 GLN HB2 H 1.855 . 2 183 . 29 GLN HB3 H 2.291 . 2 184 . 29 GLN C C 174.870 . 1 185 . 29 GLN CA C 55.313 . 1 186 . 29 GLN CB C 28.694 . 1 187 . 29 GLN N N 118.063 . 1 188 . 30 ALA H H 7.856 . 1 189 . 30 ALA HA H 4.406 . 1 190 . 30 ALA HB H 1.328 . 1 191 . 30 ALA C C 175.953 . 1 192 . 30 ALA CA C 51.352 . 1 193 . 30 ALA CB C 20.630 . 1 194 . 30 ALA N N 124.199 . 1 195 . 31 ALA H H 8.617 . 1 196 . 31 ALA CA C 50.505 . 1 197 . 31 ALA CB C 17.915 . 1 198 . 31 ALA N N 124.587 . 1 199 . 32 PRO HB2 H 1.519 . 2 200 . 32 PRO C C 176.199 . 1 201 . 32 PRO CA C 63.027 . 1 202 . 32 PRO CB C 31.620 . 1 203 . 33 GLY H H 5.460 . 1 204 . 33 GLY HA2 H 3.463 . 2 205 . 33 GLY HA3 H 4.231 . 2 206 . 33 GLY C C 172.772 . 1 207 . 33 GLY CA C 45.427 . 1 208 . 33 GLY N N 107.707 . 1 209 . 34 SER H H 7.978 . 1 210 . 34 SER CA C 58.243 . 1 211 . 34 SER CB C 62.799 . 1 212 . 34 SER N N 117.124 . 1 213 . 35 PRO HA H 4.176 . 1 214 . 35 PRO HB2 H 1.884 . 2 215 . 35 PRO HB3 H 2.323 . 2 216 . 35 PRO C C 179.513 . 1 217 . 35 PRO CA C 66.905 . 1 218 . 35 PRO CB C 31.986 . 1 219 . 36 GLN H H 8.920 . 1 220 . 36 GLN HA H 3.974 . 1 221 . 36 GLN HB2 H 1.830 . 2 222 . 36 GLN HB3 H 2.059 . 2 223 . 36 GLN C C 178.289 . 1 224 . 36 GLN CA C 59.314 . 1 225 . 36 GLN CB C 28.317 . 1 226 . 36 GLN N N 116.642 . 1 227 . 37 PHE H H 7.155 . 1 228 . 37 PHE HA H 3.791 . 1 229 . 37 PHE HB2 H 2.579 . 2 230 . 37 PHE HB3 H 3.194 . 2 231 . 37 PHE C C 176.695 . 1 232 . 37 PHE CA C 61.063 . 1 233 . 37 PHE CB C 40.643 . 1 234 . 37 PHE N N 120.421 . 1 235 . 38 MET H H 8.762 . 1 236 . 38 MET HA H 4.253 . 1 237 . 38 MET HB2 H 1.895 . 2 238 . 38 MET HB3 H 2.079 . 2 239 . 38 MET C C 178.846 . 1 240 . 38 MET CA C 55.397 . 1 241 . 38 MET CB C 28.955 . 1 242 . 38 MET N N 113.948 . 1 243 . 39 GLN H H 8.280 . 1 244 . 39 GLN HA H 3.974 . 1 245 . 39 GLN HB2 H 2.071 . 1 246 . 39 GLN HB3 H 2.071 . 1 247 . 39 GLN C C 178.420 . 1 248 . 39 GLN CA C 59.415 . 1 249 . 39 GLN CB C 28.469 . 1 250 . 39 GLN N N 119.316 . 1 251 . 40 THR H H 7.293 . 1 252 . 40 THR HA H 3.768 . 4 253 . 40 THR HB H 3.768 . 4 254 . 40 THR CA C 67.113 . 1 255 . 40 THR CB C 68.745 . 1 256 . 40 THR N N 115.054 . 1 257 . 41 ILE H H 8.008 . 1 258 . 41 ILE HA H 3.766 . 1 259 . 41 ILE HB H 1.580 . 1 260 . 41 ILE C C 177.668 . 1 261 . 41 ILE CA C 64.067 . 1 262 . 41 ILE CB C 36.831 . 1 263 . 41 ILE N N 118.994 . 1 264 . 42 ARG H H 8.904 . 1 265 . 42 ARG HB2 H 1.805 . 1 266 . 42 ARG HB3 H 1.805 . 1 267 . 42 ARG C C 179.580 . 1 268 . 42 ARG CA C 61.025 . 1 269 . 42 ARG CB C 30.100 . 1 270 . 42 ARG N N 121.799 . 1 271 . 43 LEU H H 7.401 . 1 272 . 43 LEU HA H 4.082 . 1 273 . 43 LEU HB2 H 1.692 . 1 274 . 43 LEU HB3 H 1.692 . 1 275 . 43 LEU C C 178.949 . 1 276 . 43 LEU CA C 58.092 . 1 277 . 43 LEU CB C 41.306 . 1 278 . 43 LEU N N 119.594 . 1 279 . 44 ALA H H 7.767 . 1 280 . 44 ALA HA H 4.403 . 1 281 . 44 ALA HB H 1.526 . 1 282 . 44 ALA C C 180.130 . 1 283 . 44 ALA CA C 55.424 . 1 284 . 44 ALA CB C 17.727 . 1 285 . 44 ALA N N 121.685 . 1 286 . 45 VAL H H 8.464 . 1 287 . 45 VAL HA H 3.372 . 1 288 . 45 VAL HB H 2.272 . 1 289 . 45 VAL C C 178.681 . 1 290 . 45 VAL CA C 66.981 . 1 291 . 45 VAL CB C 31.614 . 1 292 . 45 VAL N N 117.886 . 1 293 . 46 GLN H H 8.013 . 1 294 . 46 GLN HA H 3.913 . 1 295 . 46 GLN HB2 H 2.137 . 1 296 . 46 GLN HB3 H 2.137 . 1 297 . 46 GLN C C 177.873 . 1 298 . 46 GLN CA C 59.059 . 1 299 . 46 GLN CB C 29.000 . 1 300 . 46 GLN N N 120.242 . 1 301 . 47 GLN H H 8.385 . 1 302 . 47 GLN HA H 3.776 . 1 303 . 47 GLN HB2 H 1.443 . 2 304 . 47 GLN HB3 H 1.902 . 2 305 . 47 GLN C C 177.943 . 1 306 . 47 GLN CA C 58.719 . 1 307 . 47 GLN CB C 29.154 . 1 308 . 47 GLN N N 116.576 . 1 309 . 48 PHE H H 8.135 . 1 310 . 48 PHE HA H 4.350 . 1 311 . 48 PHE HB2 H 2.643 . 2 312 . 48 PHE HB3 H 2.822 . 2 313 . 48 PHE C C 174.801 . 1 314 . 48 PHE CA C 59.381 . 1 315 . 48 PHE CB C 40.327 . 1 316 . 48 PHE N N 112.747 . 1 317 . 49 ASP H H 7.813 . 1 318 . 49 ASP CA C 54.264 . 1 319 . 49 ASP CB C 40.380 . 1 320 . 49 ASP N N 117.704 . 1 321 . 50 PRO HA H 4.195 . 1 322 . 50 PRO HB2 H 1.273 . 2 323 . 50 PRO HB3 H 1.813 . 2 324 . 50 PRO C C 177.984 . 1 325 . 50 PRO CA C 61.794 . 1 326 . 50 PRO CB C 33.562 . 1 327 . 51 THR H H 7.466 . 1 328 . 51 THR HA H 5.160 . 1 329 . 51 THR HB H 3.793 . 1 330 . 51 THR C C 174.057 . 1 331 . 51 THR CA C 60.870 . 1 332 . 51 THR CB C 70.366 . 1 333 . 51 THR N N 108.023 . 1 334 . 52 ALA H H 6.285 . 1 335 . 52 ALA HA H 3.757 . 1 336 . 52 ALA HB H 0.583 . 1 337 . 52 ALA C C 180.995 . 1 338 . 52 ALA CA C 56.159 . 1 339 . 52 ALA CB C 18.441 . 1 340 . 52 ALA N N 120.282 . 1 341 . 53 LYS H H 8.952 . 1 342 . 53 LYS HA H 3.902 . 1 343 . 53 LYS HB2 H 1.512 . 2 344 . 53 LYS HB3 H 1.726 . 2 345 . 53 LYS C C 178.372 . 1 346 . 53 LYS CA C 59.526 . 1 347 . 53 LYS CB C 32.280 . 1 348 . 53 LYS N N 122.038 . 1 349 . 54 ALA H H 7.366 . 1 350 . 54 ALA C C 180.922 . 1 351 . 54 ALA CA C 55.172 . 1 352 . 54 ALA CB C 18.454 . 1 353 . 54 ALA N N 122.120 . 1 354 . 55 LEU H H 8.252 . 1 355 . 55 LEU N N 119.202 . 1 356 . 57 ASP HA H 4.333 . 1 357 . 57 ASP HB2 H 2.563 . 2 358 . 57 ASP HB3 H 3.153 . 2 359 . 57 ASP C C 179.548 . 1 360 . 57 ASP CA C 57.539 . 1 361 . 57 ASP CB C 39.966 . 1 362 . 58 LEU H H 8.194 . 1 363 . 58 LEU HA H 3.730 . 1 364 . 58 LEU HB2 H 1.327 . 2 365 . 58 LEU HB3 H 2.042 . 2 366 . 58 LEU C C 177.852 . 1 367 . 58 LEU CA C 58.262 . 1 368 . 58 LEU CB C 41.45 . 1 369 . 58 LEU N N 120.767 . 1 370 . 59 LEU H H 8.608 . 1 371 . 59 LEU HA H 3.970 . 1 372 . 59 LEU HB2 H 1.862 . 2 373 . 59 LEU HB3 H 2.265 . 2 374 . 59 LEU C C 178.215 . 1 375 . 59 LEU CA C 59.167 . 1 376 . 59 LEU CB C 43.288 . 1 377 . 59 LEU N N 119.777 . 1 378 . 60 GLN H H 8.131 . 1 379 . 60 GLN HA H 4.073 . 1 380 . 60 GLN HB2 H 2.099 . 1 381 . 60 GLN HB3 H 2.099 . 1 382 . 60 GLN C C 176.944 . 1 383 . 60 GLN CA C 57.835 . 1 384 . 60 GLN CB C 28.913 . 1 385 . 60 GLN N N 113.194 . 1 386 . 61 TYR H H 7.753 . 1 387 . 61 TYR HA H 4.192 . 1 388 . 61 TYR HB2 H 2.784 . 2 389 . 61 TYR HB3 H 3.083 . 2 390 . 61 TYR C C 177.112 . 1 391 . 61 TYR CA C 60.463 . 1 392 . 61 TYR CB C 39.912 . 1 393 . 61 TYR N N 118.467 . 1 394 . 62 LEU H H 8.018 . 1 395 . 62 LEU HA H 4.036 . 1 396 . 62 LEU HB2 H 1.640 . 2 397 . 62 LEU HB3 H 1.983 . 2 398 . 62 LEU C C 178.408 . 1 399 . 62 LEU CA C 56.558 . 1 400 . 62 LEU CB C 46.096 . 1 401 . 62 LEU N N 113.915 . 1 402 . 63 CYS H H 8.054 . 1 403 . 63 CYS HA H 4.729 . 1 404 . 63 CYS HB2 H 2.749 . 2 405 . 63 CYS HB3 H 2.988 . 2 406 . 63 CYS C C 173.697 . 1 407 . 63 CYS CA C 58.300 . 1 408 . 63 CYS CB C 31.953 . 1 409 . 63 CYS N N 114.666 . 1 410 . 64 SER H H 8.848 . 1 411 . 64 SER HA H 3.970 . 1 412 . 64 SER HB2 H 4.329 . 1 413 . 64 SER HB3 H 4.329 . 1 414 . 64 SER C C 174.454 . 1 415 . 64 SER CA C 57.251 . 1 416 . 64 SER CB C 64.957 . 1 417 . 64 SER N N 117.713 . 1 418 . 65 SER H H 8.954 . 1 419 . 65 SER HA H 4.082 . 1 420 . 65 SER HB2 H 3.866 . 1 421 . 65 SER HB3 H 3.866 . 1 422 . 65 SER C C 177.392 . 1 423 . 65 SER CB C 62.452 . 1 424 . 65 SER N N 116.271 . 1 425 . 66 LEU H H 8.029 . 1 426 . 66 LEU HA H 4.099 . 1 427 . 66 LEU HB2 H 1.575 . 1 428 . 66 LEU HB3 H 1.575 . 1 429 . 66 LEU C C 179.066 . 1 430 . 66 LEU CA C 58.348 . 1 431 . 66 LEU CB C 42.205 . 1 432 . 66 LEU N N 122.685 . 1 433 . 67 VAL H H 7.476 . 1 434 . 67 VAL HA H 3.376 . 1 435 . 67 VAL HB H 2.030 . 1 436 . 67 VAL C C 177.664 . 1 437 . 67 VAL CA C 67.108 . 1 438 . 67 VAL CB C 31.794 . 1 439 . 67 VAL N N 120.315 . 1 440 . 68 ALA H H 8.760 . 1 441 . 68 ALA HA H 3.852 . 1 442 . 68 ALA HB H 1.322 . 1 443 . 68 ALA C C 179.905 . 1 444 . 68 ALA CA C 55.730 . 1 445 . 68 ALA CB C 17.712 . 1 446 . 68 ALA N N 120.716 . 1 447 . 69 SER H H 7.977 . 1 448 . 69 SER HA H 4.215 . 1 449 . 69 SER HB2 H 3.983 . 1 450 . 69 SER HB3 H 3.983 . 1 451 . 69 SER C C 177.230 . 1 452 . 69 SER CA C 61.851 . 1 453 . 69 SER CB C 62.865 . 1 454 . 69 SER N N 113.968 . 1 455 . 70 LEU H H 7.940 . 1 456 . 70 LEU HA H 4.011 . 1 457 . 70 LEU HB2 H 1.308 . 2 458 . 70 LEU HB3 H 1.818 . 2 459 . 70 LEU C C 179.836 . 1 460 . 70 LEU CA C 57.954 . 1 461 . 70 LEU CB C 42.178 . 1 462 . 70 LEU N N 123.623 . 1 463 . 71 HIS H H 8.782 . 1 464 . 71 HIS HA H 3.326 . 1 465 . 71 HIS HB2 H 2.306 . 2 466 . 71 HIS HB3 H 2.940 . 2 467 . 71 HIS C C 176.562 . 1 468 . 71 HIS CA C 62.212 . 1 469 . 71 HIS CB C 31.298 . 1 470 . 71 HIS N N 120.990 . 1 471 . 72 HIS H H 8.281 . 1 472 . 72 HIS HA H 4.085 . 1 473 . 72 HIS HB2 H 3.341 . 2 474 . 72 HIS HB3 H 3.434 . 2 475 . 72 HIS C C 176.970 . 1 476 . 72 HIS CA C 59.340 . 1 477 . 72 HIS CB C 29.011 . 1 478 . 72 HIS N N 116.404 . 1 479 . 73 GLN H H 7.694 . 1 480 . 73 GLN HA H 3.955 . 1 481 . 73 GLN HB2 H 2.081 . 2 482 . 73 GLN C C 178.906 . 1 483 . 73 GLN CA C 58.926 . 1 484 . 73 GLN CB C 29.012 . 1 485 . 73 GLN N N 116.707 . 1 486 . 74 GLN H H 7.742 . 1 487 . 74 GLN HA H 4.014 . 1 488 . 74 GLN HB2 H 1.705 . 2 489 . 74 GLN C C 178.213 . 1 490 . 74 GLN CA C 57.69 . 1 491 . 74 GLN CB C 27.585 . 1 492 . 74 GLN N N 118.888 . 1 493 . 75 LEU H H 8.970 . 1 494 . 75 LEU C C 177.836 . 1 495 . 75 LEU CA C 57.918 . 1 496 . 75 LEU CB C 40.678 . 1 497 . 75 LEU N N 121.828 . 1 498 . 76 ASP H H 8.229 . 1 499 . 76 ASP HA H 4.275 . 1 500 . 76 ASP HB2 H 2.533 . 1 501 . 76 ASP HB3 H 2.533 . 1 502 . 76 ASP C C 179.837 . 1 503 . 76 ASP CA C 57.940 . 1 504 . 76 ASP CB C 39.644 . 1 505 . 76 ASP N N 118.717 . 1 506 . 77 SER H H 7.299 . 1 507 . 77 SER HA H 4.192 . 1 508 . 77 SER HB2 H 3.881 . 1 509 . 77 SER HB3 H 3.881 . 1 510 . 77 SER C C 176.880 . 1 511 . 77 SER CA C 61.838 . 1 512 . 77 SER CB C 62.772 . 1 513 . 77 SER N N 115.448 . 1 514 . 78 LEU H H 8.215 . 1 515 . 78 LEU HA H 3.967 . 1 516 . 78 LEU HB2 H 1.319 . 2 517 . 78 LEU HB3 H 1.860 . 2 518 . 78 LEU C C 180.820 . 1 519 . 78 LEU CA C 57.962 . 1 520 . 78 LEU CB C 42.427 . 1 521 . 78 LEU N N 122.517 . 1 522 . 79 ILE H H 8.980 . 1 523 . 79 ILE HA H 3.451 . 1 524 . 79 ILE HB H 1.836 . 1 525 . 79 ILE C C 177.316 . 1 526 . 79 ILE CA C 66.310 . 1 527 . 79 ILE CB C 38.156 . 1 528 . 79 ILE N N 121.026 . 1 529 . 80 SER H H 7.853 . 1 530 . 80 SER CA C 61.797 . 1 531 . 80 SER N N 114.555 . 1 532 . 81 GLU H H 7.852 . 1 533 . 81 GLU HA H 3.964 . 1 534 . 81 GLU HB2 H 1.990 . 1 535 . 81 GLU HB3 H 1.990 . 1 536 . 81 GLU C C 178.681 . 1 537 . 81 GLU CA C 59.597 . 1 538 . 81 GLU CB C 29.738 . 1 539 . 81 GLU N N 120.611 . 1 540 . 82 ALA H H 8.146 . 1 541 . 82 ALA HA H 3.948 . 1 542 . 82 ALA HB H 1.362 . 1 543 . 82 ALA C C 180.040 . 1 544 . 82 ALA CA C 55.348 . 1 545 . 82 ALA CB C 18.212 . 1 546 . 82 ALA N N 123.179 . 1 547 . 83 GLU H H 8.755 . 1 548 . 83 GLU HA H 3.786 . 1 549 . 83 GLU HB2 H 2.019 . 2 550 . 83 GLU HB3 H 2.239 . 2 551 . 83 GLU C C 179.664 . 1 552 . 83 GLU CA C 59.608 . 1 553 . 83 GLU CB C 30.030 . 1 554 . 83 GLU N N 116.698 . 1 555 . 84 THR H H 7.776 . 1 556 . 84 THR HA H 3.959 . 1 557 . 84 THR HB H 4.214 . 1 558 . 84 THR C C 175.857 . 1 559 . 84 THR CA C 65.862 . 1 560 . 84 THR CB C 69.057 . 1 561 . 84 THR N N 114.322 . 1 562 . 85 ARG H H 7.694 . 1 563 . 85 ARG HA H 4.121 . 1 564 . 85 ARG HB2 H 1.838 . 1 565 . 85 ARG HB3 H 1.838 . 1 566 . 85 ARG C C 177.142 . 1 567 . 85 ARG CA C 58.325 . 1 568 . 85 ARG CB C 30.874 . 1 569 . 85 ARG N N 120.449 . 1 570 . 86 GLY H H 7.897 . 1 571 . 86 GLY HA2 H 3.625 . 2 572 . 86 GLY HA3 H 4.271 . 2 573 . 86 GLY C C 173.269 . 1 574 . 86 GLY CA C 45.258 . 1 575 . 86 GLY N N 108.881 . 1 576 . 87 ILE H H 8.610 . 1 577 . 87 ILE HA H 4.169 . 1 578 . 87 ILE HB H 1.565 . 1 579 . 87 ILE C C 176.360 . 1 580 . 87 ILE CA C 60.556 . 1 581 . 87 ILE CB C 40.165 . 1 582 . 87 ILE N N 124.963 . 1 583 . 88 THR HA H 3.910 . 4 584 . 88 THR HB H 3.910 . 4 585 . 88 THR C C 175.115 . 1 586 . 88 THR CA C 64.779 . 1 587 . 88 THR CB C 69.256 . 1 588 . 89 SER H H 8.877 . 1 589 . 89 SER HB2 H 4.037 . 1 590 . 89 SER HB3 H 4.037 . 1 591 . 89 SER C C 173.349 . 1 592 . 89 SER CA C 60.157 . 1 593 . 89 SER CB C 63.161 . 1 594 . 89 SER N N 117.528 . 1 595 . 90 TYR H H 7.851 . 1 596 . 90 TYR HA H 4.543 . 1 597 . 90 TYR HB2 H 2.589 . 2 598 . 90 TYR HB3 H 3.055 . 2 599 . 90 TYR C C 173.329 . 1 600 . 90 TYR CA C 56.561 . 1 601 . 90 TYR CB C 39.308 . 1 602 . 90 TYR N N 120.920 . 1 603 . 91 ASN H H 8.948 . 1 604 . 91 ASN CA C 48.734 . 1 605 . 91 ASN CB C 39.382 . 1 606 . 91 ASN N N 127.153 . 1 607 . 92 PRO HA H 3.871 . 1 608 . 92 PRO HB2 H 1.821 . 2 609 . 92 PRO HB3 H 2.196 . 2 610 . 92 PRO C C 178.533 . 1 611 . 92 PRO CA C 63.605 . 1 612 . 92 PRO CB C 32.132 . 1 613 . 93 LEU H H 7.585 . 1 614 . 93 LEU HA H 4.003 . 1 615 . 93 LEU HB2 H 1.388 . 2 616 . 93 LEU HB3 H 1.572 . 2 617 . 93 LEU C C 178.373 . 1 618 . 93 LEU CA C 56.627 . 1 619 . 93 LEU CB C 40.861 . 1 620 . 93 LEU N N 117.668 . 1 621 . 94 ALA H H 7.406 . 1 622 . 94 ALA HA H 4.331 . 1 623 . 94 ALA HB H 1.282 . 1 624 . 94 ALA C C 176.451 . 1 625 . 94 ALA CA C 51.937 . 1 626 . 94 ALA CB C 18.111 . 1 627 . 94 ALA N N 119.448 . 1 628 . 95 GLY H H 7.215 . 1 629 . 95 GLY CA C 43.991 . 1 630 . 95 GLY N N 106.935 . 1 631 . 96 PRO HA H 4.715 . 1 632 . 96 PRO HB2 H 1.844 . 2 633 . 96 PRO HB3 H 2.572 . 2 634 . 96 PRO C C 177.917 . 1 635 . 96 PRO CA C 63.141 . 1 636 . 96 PRO CB C 32.950 . 1 637 . 97 LEU H H 8.838 . 1 638 . 97 LEU HA H 3.697 . 1 639 . 97 LEU HB2 H 1.079 . 2 640 . 97 LEU HB3 H 1.646 . 2 641 . 97 LEU C C 177.422 . 1 642 . 97 LEU CA C 59.618 . 1 643 . 97 LEU CB C 40.922 . 1 644 . 97 LEU N N 126.874 . 1 645 . 98 ARG H H 9.000 . 1 646 . 98 ARG HA H 3.263 . 1 647 . 98 ARG HB2 H 1.592 . 1 648 . 98 ARG HB3 H 1.592 . 1 649 . 98 ARG C C 175.662 . 1 650 . 98 ARG CA C 59.208 . 1 651 . 98 ARG CB C 30.285 . 1 652 . 98 ARG N N 113.359 . 1 653 . 99 VAL H H 6.789 . 1 654 . 99 VAL HA H 3.747 . 1 655 . 99 VAL HB H 1.967 . 1 656 . 99 VAL C C 180.022 . 1 657 . 99 VAL CA C 64.845 . 1 658 . 99 VAL CB C 32.741 . 1 659 . 99 VAL N N 115.252 . 1 660 . 100 GLN H H 8.156 . 1 661 . 100 GLN HA H 4.011 . 1 662 . 100 GLN HB2 H 1.637 . 2 663 . 100 GLN HB3 H 2.273 . 2 664 . 100 GLN C C 177.790 . 1 665 . 100 GLN CA C 60.943 . 1 666 . 100 GLN CB C 29.714 . 1 667 . 100 GLN N N 121.205 . 1 668 . 101 ALA H H 8.232 . 1 669 . 101 ALA HA H 3.764 . 1 670 . 101 ALA HB H 0.980 . 1 671 . 101 ALA C C 177.720 . 1 672 . 101 ALA CA C 53.740 . 1 673 . 101 ALA CB C 18.776 . 1 674 . 101 ALA N N 116.368 . 1 675 . 102 ASN H H 7.415 . 1 676 . 102 ASN CA C 53.075 . 1 677 . 102 ASN CB C 39.235 . 1 678 . 102 ASN N N 115.653 . 1 679 . 104 PRO HA H 4.099 . 1 680 . 104 PRO HB2 H 1.895 . 2 681 . 104 PRO HB3 H 2.259 . 2 682 . 104 PRO C C 177.334 . 1 683 . 104 PRO CA C 64.902 . 1 684 . 104 PRO CB C 32.480 . 1 685 . 105 GLN H H 8.135 . 1 686 . 105 GLN HA H 4.284 . 1 687 . 105 GLN HB2 H 1.890 . 2 688 . 105 GLN HB3 H 2.203 . 2 689 . 105 GLN C C 177.133 . 1 690 . 105 GLN CA C 56.592 . 1 691 . 105 GLN CB C 29.079 . 1 692 . 105 GLN N N 113.896 . 1 693 . 106 GLN H H 7.637 . 1 694 . 106 GLN HA H 4.700 . 1 695 . 106 GLN HB2 H 2.086 . 1 696 . 106 GLN HB3 H 2.086 . 1 697 . 106 GLN C C 175.230 . 1 698 . 106 GLN CA C 53.493 . 1 699 . 106 GLN CB C 26.707 . 1 700 . 106 GLN N N 119.742 . 1 701 . 107 GLN H H 7.756 . 1 702 . 107 GLN HA H 3.686 . 1 703 . 107 GLN HB2 H 1.891 . 2 704 . 107 GLN HB3 H 2.123 . 2 705 . 107 GLN C C 177.501 . 1 706 . 107 GLN CA C 60.016 . 1 707 . 107 GLN CB C 29.496 . 1 708 . 107 GLN N N 120.794 . 1 709 . 108 GLY H H 8.481 . 1 710 . 108 GLY HA2 H 3.689 . 1 711 . 108 GLY HA3 H 3.689 . 1 712 . 108 GLY C C 177.200 . 1 713 . 108 GLY CA C 47.378 . 1 714 . 108 GLY N N 105.892 . 1 715 . 109 LEU H H 7.873 . 1 716 . 109 LEU HA H 4.015 . 1 717 . 109 LEU HB2 H 1.152 . 2 718 . 109 LEU HB3 H 1.675 . 2 719 . 109 LEU C C 178.904 . 1 720 . 109 LEU CA C 49.031 . 1 721 . 109 LEU CB C 40.510 . 1 722 . 109 LEU N N 120.688 . 1 723 . 110 ARG H H 8.255 . 1 724 . 110 ARG HA H 3.899 . 1 725 . 110 ARG HB2 H 2.001 . 1 726 . 110 ARG HB3 H 2.001 . 1 727 . 110 ARG C C 178.994 . 1 728 . 110 ARG CA C 60.770 . 1 729 . 110 ARG CB C 29.211 . 1 730 . 110 ARG N N 120.343 . 1 731 . 111 ARG H H 8.157 . 1 732 . 111 ARG HA H 3.951 . 1 733 . 111 ARG HB2 H 1.851 . 2 734 . 111 ARG HB3 H 1.931 . 2 735 . 111 ARG C C 179.221 . 1 736 . 111 ARG CA C 58.421 . 1 737 . 111 ARG CB C 28.969 . 1 738 . 111 ARG N N 118.576 . 1 739 . 112 GLU H H 8.062 . 1 740 . 112 GLU HA H 4.265 . 1 741 . 112 GLU HB2 H 1.712 . 2 742 . 112 GLU HB3 H 2.126 . 2 743 . 112 GLU C C 179.182 . 1 744 . 112 GLU CA C 59.252 . 1 745 . 112 GLU CB C 28.880 . 1 746 . 112 GLU N N 120.105 . 1 747 . 113 TYR H H 8.596 . 1 748 . 113 TYR CB C 38.723 . 1 749 . 113 TYR N N 119.166 . 1 750 . 114 GLN HA H 3.716 . 1 751 . 114 GLN HB2 H 1.738 . 2 752 . 114 GLN HB3 H 2.702 . 2 753 . 114 GLN C C 178.308 . 1 754 . 114 GLN CA C 59.243 . 1 755 . 114 GLN CB C 28.144 . 1 756 . 115 GLN H H 7.680 . 1 757 . 115 GLN C C 175.129 . 1 758 . 115 GLN CA C 59.115 . 1 759 . 115 GLN CB C 28.295 . 1 760 . 115 GLN N N 114.472 . 1 761 . 116 LEU H H 7.777 . 1 762 . 116 LEU HA H 3.927 . 1 763 . 116 LEU HB2 H 0.953 . 2 764 . 116 LEU HB3 H 1.554 . 2 765 . 116 LEU C C 176.990 . 1 766 . 116 LEU CA C 58.264 . 1 767 . 116 LEU CB C 41.790 . 1 768 . 116 LEU N N 121.771 . 1 769 . 117 TRP H H 8.875 . 1 770 . 117 TRP HA H 3.728 . 1 771 . 117 TRP HB2 H 2.702 . 2 772 . 117 TRP HB3 H 3.518 . 2 773 . 117 TRP C C 179.401 . 1 774 . 117 TRP CA C 62.662 . 1 775 . 117 TRP CB C 29.605 . 1 776 . 117 TRP N N 120.988 . 1 777 . 118 LEU H H 8.606 . 1 778 . 118 LEU HA H 4.263 . 1 779 . 118 LEU HB2 H 1.417 . 2 780 . 118 LEU HB3 H 2.157 . 2 781 . 118 LEU C C 179.397 . 1 782 . 118 LEU CA C 58.366 . 1 783 . 118 LEU CB C 43.035 . 1 784 . 118 LEU N N 118.621 . 1 785 . 119 ALA H H 8.054 . 1 786 . 119 ALA HA H 4.044 . 1 787 . 119 ALA HB H 1.437 . 1 788 . 119 ALA C C 180.680 . 1 789 . 119 ALA CA C 54.800 . 1 790 . 119 ALA CB C 18.160 . 1 791 . 119 ALA N N 122.392 . 1 792 . 120 ALA H H 7.917 . 1 793 . 120 ALA HA H 3.589 . 1 794 . 120 ALA HB H 0.452 . 1 795 . 120 ALA C C 177.752 . 1 796 . 120 ALA CA C 54.413 . 1 797 . 120 ALA CB C 16.727 . 1 798 . 120 ALA N N 120.335 . 1 799 . 121 PHE H H 7.136 . 1 800 . 121 PHE HA H 3.904 . 1 801 . 121 PHE HB2 H 3.013 . 1 802 . 121 PHE HB3 H 3.013 . 1 803 . 121 PHE C C 177.147 . 1 804 . 121 PHE CA C 62.263 . 1 805 . 121 PHE CB C 40.299 . 1 806 . 121 PHE N N 111.355 . 1 807 . 122 ALA H H 7.576 . 1 808 . 122 ALA HA H 4.198 . 1 809 . 122 ALA HB H 1.395 . 1 810 . 122 ALA C C 177.711 . 1 811 . 122 ALA CA C 54.075 . 1 812 . 122 ALA CB C 18.531 . 1 813 . 122 ALA N N 119.705 . 1 814 . 123 ALA H H 7.198 . 1 815 . 123 ALA HA H 4.237 . 1 816 . 123 ALA HB H 1.189 . 1 817 . 123 ALA C C 177.491 . 1 818 . 123 ALA CA C 51.790 . 1 819 . 123 ALA CB C 19.239 . 1 820 . 123 ALA N N 117.577 . 1 821 . 124 LEU H H 7.332 . 1 822 . 124 LEU CA C 54.568 . 1 823 . 124 LEU CB C 40.174 . 1 824 . 124 LEU N N 119.394 . 1 825 . 125 PRO HA H 4.274 . 1 826 . 125 PRO HB2 H 1.774 . 2 827 . 125 PRO HB3 H 2.166 . 2 828 . 125 PRO C C 177.695 . 1 829 . 125 PRO CA C 64.119 . 1 830 . 125 PRO CB C 31.696 . 1 831 . 126 GLY H H 8.409 . 1 832 . 126 GLY HA2 H 3.766 . 1 833 . 126 GLY HA3 H 3.766 . 1 834 . 126 GLY C C 174.500 . 1 835 . 126 GLY CA C 45.683 . 1 836 . 126 GLY N N 107.943 . 1 837 . 127 SER H H 7.820 . 1 838 . 127 SER HA H 3.970 . 1 839 . 127 SER C C 174.369 . 1 840 . 127 SER CA C 58.710 . 1 841 . 127 SER CB C 64.034 . 1 842 . 127 SER N N 114.623 . 1 843 . 128 ALA H H 8.013 . 1 844 . 128 ALA HA H 4.229 . 1 845 . 128 ALA HB H 1.182 . 1 846 . 128 ALA C C 177.197 . 1 847 . 128 ALA CA C 52.585 . 1 848 . 128 ALA CB C 19.531 . 1 849 . 128 ALA N N 124.520 . 1 850 . 129 LYS H H 8.059 . 1 851 . 129 LYS HA H 4.099 . 1 852 . 129 LYS HB2 H 1.626 . 1 853 . 129 LYS HB3 H 1.626 . 1 854 . 129 LYS C C 175.873 . 1 855 . 129 LYS CA C 56.152 . 1 856 . 129 LYS CB C 33.263 . 1 857 . 129 LYS N N 119.320 . 1 858 . 130 ASP H H 7.773 . 1 859 . 130 ASP CA C 52.332 . 1 860 . 130 ASP CB C 41.697 . 1 861 . 130 ASP N N 122.443 . 1 862 . 131 PRO HA H 4.269 . 1 863 . 131 PRO HB2 H 1.689 . 2 864 . 131 PRO HB3 H 2.079 . 2 865 . 131 PRO C C 177.083 . 1 866 . 131 PRO CA C 63.754 . 1 867 . 131 PRO CB C 32.134 . 1 868 . 132 SER H H 8.419 . 1 869 . 132 SER HA H 4.220 . 1 870 . 132 SER HB2 H 3.705 . 2 871 . 132 SER C C 174.372 . 1 872 . 132 SER CA C 59.203 . 1 873 . 132 SER CB C 63.695 . 1 874 . 132 SER N N 114.659 . 1 875 . 133 TRP H H 7.790 . 1 876 . 133 TRP HA H 4.585 . 1 877 . 133 TRP HB2 H 3.167 . 1 878 . 133 TRP HB3 H 3.167 . 1 879 . 133 TRP C C 174.773 . 1 880 . 133 TRP CA C 56.975 . 1 881 . 133 TRP CB C 29.692 . 1 882 . 133 TRP N N 122.387 . 1 883 . 134 ALA H H 7.543 . 1 884 . 134 ALA CA C 54.031 . 1 885 . 134 ALA CB C 20.575 . 1 886 . 134 ALA N N 130.152 . 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 253 252 '584,583' stop_ save_