data_4154 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 13C and Stereospecific 13C and 1H Resonance Assignments for Oxidized Putidaredoxin ; _BMRB_accession_number 4154 _BMRB_flat_file_name bmr4154.str _Entry_type update _Submission_date 1998-06-28 _Accession_date 1998-06-28 _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 Jain Nitin . . 2 Lyons Teresa . . 3 Pochapsky Thomas C. . 4 Kuti Miklos . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 507 "13C chemical shifts" 376 "15N chemical shifts" 96 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-09-28 update author 'chemical shift values updated' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Pochapsky, T. C., Jain, N. U., Kuti, M., Lyons, T. A., and Heymont, J., "A Refined Model for the Solution Structure of Oxidized Putidaredoxin", Biochemistry, 38, 4681-4690 (1999). ; _Citation_title 'A Refined Model for the Solution Structure of Oxidized Putidaredoxin' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99218076 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pochapsky Thomas C. . 2 Jain Nitin U. . 3 Lyons Teresa . . 4 Kuti Miklos . . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 38 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4681 _Page_last 4690 _Year 1999 _Details . loop_ _Keyword adrenodoxin 'cytochrome P450' ferredoxin stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Ye, X. M., Pochapsky, T. C. and Pochapsky, S. S., "1H NMR Sequential Assignments and Identification of Secondary Structural Elements in Oxidized Putidaredoxin, an Electron-transfer Protein from Pseudomonas," Biochemistry 31, 1961-1968 (1992) ; _Citation_title '1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 1536837 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ye 'X M' M. . 2 Pochapsky 'T C' C. . 3 Pochapsky 'S S' S. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 31 _Journal_issue 7 _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 1961 _Page_last 1968 _Year 1992 _Details ; Sequential 1H resonance assignments and secondary structural features of putidaredoxin (Pdx), a 106-residue globular protein consisting of a single polypeptide chain and a [2Fe-2S] cluster, are reported. No crystal structure has been obtained for Pdx or for any closely homologous protein. The sequentially assigned resonances represent ca. 83% of all the protons in Pdx and a large majority of those protons which are unaffected by the paramagnetism of the iron-sulfur cluster. A total of three alpha-helices, two beta-sheets, and two type I beta-turns have been identified from NOE (nuclear Overhauser effect) patterns. Besides the extensive beta-sheet described previously, a second sheet is identified, consisting of two short antiparallel strands (Ile 89-Thr 91 and Val 21-Leu 23), one of which ends in a tight type I turn (Thr 91-Pro 92-Glu 93-Leu 94). One short helix (Ala 26-Gly 31) and a second longer helical region (Glu 54-Cys 73) are present. This second helical region is discontinuous, breaking at Pro 61, resuming at Glu 65, and ending at Cys 73. The functionally important C-terminal tryptophan residue has been identified, and some structural constraints on this residue are described. Previously reported functional data concerning Pdx are discussed in light of present structural information. Finally, approaches to the determination of a high-resolution solution structure of the protein are discussed. ; save_ save_citation_two _Saveframe_category citation _Citation_full ; Lyons, T. A., Ratnaswamy, G. and Pochapsky, T. C., "Redox-dependent Dynamics of Putidaredoxin Characterized by Amide Proton Exchange," Protein Sci. 5, 627-639 (1996). ; _Citation_title 'Redox-dependent dynamics of putidaredoxin characterized by amide proton exchange.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8845752 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lyons 'T A' A. . 2 Ratnaswamy G . . 3 Pochapsky 'T C' C. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 5 _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 627 _Page_last 639 _Year 1996 _Details ; Multidimensional NMR methods were used to obtain 1H-15N correlations and 15N resonance assignments for amide and side-chain nitrogens of oxidized and reduced putidaredoxin (Pdx), the Fe2S2 ferredoxin, which acts as the physiological reductant of cytochrome P-450cam (CYP101). A model for the solution structure of oxidized Pdx has been determined recently using NMR methods (Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA, 1994, Biochemistry 33:6424-6432) and redox-dependent 1H NMR spectral features have been described (Pochapsky TC, Ratnaswamy G, Patera A, 1994, Biochemistry 33:6433-6441). 15N assignments were made with NOESY-(1H/15N) HMQC and TOCSY-(1H/15N) HSQC spectra obtained using samples of Pdx uniformly labeled with 15N. Local dynamics in both oxidation states of Pdx were then characterized by comparison of residue-specific amide proton exchange rates, which were measured by a combination of saturation transfer and H2O/D2O exchange methods at pH 6.4 and 7.4 (uncorrected for isotope effects). In general, where exchange rates for a given site exhibit significant oxidation-state dependence, the oxidized protein exchanges more rapidly than the reduced protein. The largest dependence of exchange rate upon oxidation state is found for residues near the metal center and in a region of compact structure that includes the loop-turn Val 74-Ser 82 and the C-terminal residues (Pro 102-Trp 106). The significance of these findings is discussed in light of the considerable dependence of the binding interaction between Pdx and CYP101 upon the oxidation state of Pdx. ; save_ save_citation_three _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _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 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ save_citation_four _Saveframe_category citation _Citation_full ; "Recommendations for Presentations of NMR Structures of Proteins and Nucleic Acids," IUPAC/IUB Draft version. ; _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_Pdxo _Saveframe_category molecular_system _Mol_system_name 'oxidized putidaredoxin' _Abbreviation_common Pdxo _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Pdxo $Pdxo 2Fe2S $FES stop_ _System_molecular_weight 12600 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state . loop_ _Biological_function 'Electron transfer to cytochrome P450cam' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Pdxo _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common putidaredoxin _Abbreviation_common Pdxo _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 106 _Mol_residue_sequence ; SKVVYVSHDGTRRELDVADG VSLMQAAVSNGIYDIVGDCG GSASCATCHVYVNEAFTDKV PAANEREIGMLECVTAELKP NSRLCCQIIMTPELDGIVVD VPDRQW ; loop_ _Residue_seq_code _Residue_label 1 SER 2 LYS 3 VAL 4 VAL 5 TYR 6 VAL 7 SER 8 HIS 9 ASP 10 GLY 11 THR 12 ARG 13 ARG 14 GLU 15 LEU 16 ASP 17 VAL 18 ALA 19 ASP 20 GLY 21 VAL 22 SER 23 LEU 24 MET 25 GLN 26 ALA 27 ALA 28 VAL 29 SER 30 ASN 31 GLY 32 ILE 33 TYR 34 ASP 35 ILE 36 VAL 37 GLY 38 ASP 39 CYS 40 GLY 41 GLY 42 SER 43 ALA 44 SER 45 CYS 46 ALA 47 THR 48 CYS 49 HIS 50 VAL 51 TYR 52 VAL 53 ASN 54 GLU 55 ALA 56 PHE 57 THR 58 ASP 59 LYS 60 VAL 61 PRO 62 ALA 63 ALA 64 ASN 65 GLU 66 ARG 67 GLU 68 ILE 69 GLY 70 MET 71 LEU 72 GLU 73 CYS 74 VAL 75 THR 76 ALA 77 GLU 78 LEU 79 LYS 80 PRO 81 ASN 82 SER 83 ARG 84 LEU 85 CYS 86 CYS 87 GLN 88 ILE 89 ILE 90 MET 91 THR 92 PRO 93 GLU 94 LEU 95 ASP 96 GLY 97 ILE 98 VAL 99 VAL 100 ASP 101 VAL 102 PRO 103 ASP 104 ARG 105 GLN 106 TRP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-13 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 1551 "P450 reductase" 100.00 106 99.06 100.00 2.13e-70 BMRB 2278 putidaredoxin 100.00 106 99.06 100.00 2.13e-70 BMRB 4149 putidaredoxin 100.00 106 99.06 99.06 7.48e-70 PDB 1GPX "C85s Gapdx, Nmr, 20 Structures" 100.00 106 99.06 99.06 7.48e-70 PDB 1OQQ "Crystal Structure Of C73sC85S MUTANT OF PUTIDAREDOXIN, A [2FE-2s] Ferredoxin From Pseudomonas Putida, At 1.47a Resolution" 100.00 106 98.11 98.11 7.80e-69 PDB 1OQR "Crystal Structure Of C73s Mutant Of Putidaredoxin, A [2fe- 2s] Ferredoxin From Pseudomonas Putida, At 1.65a Resolution" 100.00 106 99.06 99.06 7.48e-70 PDB 1PDX Putidaredoxin 100.00 106 100.00 100.00 8.07e-71 PDB 1PUT "An Nmr-Derived Model For The Solution Structure Of Oxidized Putidaredoxin, A 2fe, 2-S Ferredoxin From Pseudomonas" 100.00 106 99.06 100.00 2.13e-70 PDB 1R7S "Putidaredoxin (Fe2s2 Ferredoxin), C73g Mutant" 100.00 106 99.06 99.06 2.18e-69 PDB 1XLN "Crystal Structure Of Oxidized C73sC85S PUTIDAREDOXIN, A [2fe-2s] Ferredoxin From Pseudomonas Putida" 100.00 106 98.11 98.11 7.80e-69 PDB 1XLO "Structure Of Reduced C73s/c85s Putidaredoxin, A [2fe-2s] Ferredoxin From Pseudomonas Putida" 100.00 106 98.11 98.11 7.80e-69 PDB 1XLP "Structure Of Oxidized C73s Putidaredoxin From Pseudomonas Putida" 100.00 106 99.06 99.06 7.48e-70 PDB 1XLQ "Crystal Structure Of Reduced C73s Putidaredoxin From Pseudomonas Putida" 100.00 106 99.06 99.06 7.48e-70 PDB 1YJI "Rdc-Refined Solution Nmr Structure Of Reduced Putidaredoxin" 100.00 106 100.00 100.00 8.07e-71 PDB 1YJJ "Rdc-Refined Solution Nmr Structure Of Oxidized Putidaredoxin" 100.00 106 100.00 100.00 8.07e-71 PDB 2M56 "The Structure Of The Complex Of Cytochrome P450cam And Its Electron Donor Putidaredoxin Determined By Paramagnetic Nmr Spectros" 100.00 106 99.06 99.06 7.48e-70 PDB 3LB8 "Crystal Structure Of The Covalent Putidaredoxin Reductase- Putidaredoxin Complex" 100.00 106 98.11 98.11 7.80e-69 PDB 3W9C "Crystal Structure Of The Electron Transfer Complex Of Cytochrome P450cam With Putidaredoxin" 100.00 108 99.06 99.06 1.00e-69 PDB 4JWS "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" 100.00 112 100.00 100.00 7.91e-71 PDB 4JWU "Crystal Structure Of Cytochrome P450cam-putidaredoxin Complex" 100.00 113 98.11 98.11 3.22e-68 PDB 4JX1 "Crystal Structure Of Reduced Cytochrome P450cam-putidaredoxin Complex Bound To Camphor And 5-exo-hydroxycamphor" 100.00 113 98.11 98.11 3.22e-68 DBJ BAA00414 "putidaredoxin [Pseudomonas putida]" 100.00 107 100.00 100.00 8.06e-71 DBJ BAN13288 "putidaredoxin [Pseudomonas putida]" 100.00 107 100.00 100.00 8.06e-71 GB AAA25759 "putidaredoxin [Pseudomonas putida]" 100.00 107 100.00 100.00 8.06e-71 REF WP_032492635 "putidaredoxin [Pseudomonas putida]" 100.00 107 100.00 100.00 8.06e-71 REF YP_009083114 "putidaredoxin [Pseudomonas putida]" 100.00 107 100.00 100.00 8.06e-71 SP P00259 "RecName: Full=Putidaredoxin; Short=PDX" 100.00 107 100.00 100.00 8.06e-71 stop_ save_ ############# # Ligands # ############# save_FES _Saveframe_category ligand _Mol_type non-polymer _Name_common "FES (FE2/S2 (INORGANIC) CLUSTER)" _BMRB_code . _PDB_code FES _Molecular_mass 175.820 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 14 11:26:54 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons FE1 FE1 FE . 0 . ? FE2 FE2 FE . 0 . ? S1 S1 S . 0 . ? S2 S2 S . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING FE1 S1 ? ? SING FE1 S2 ? ? SING FE2 S1 ? ? SING FE2 S2 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Pdxo 'Pseudomonas putida' 303 Eubacteria . Pseudomonas putida 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 $Pdxo . . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Pdxo 1 mM '[U-13C, U-15N]' deutero-trisbuffer . mM . stop_ save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_one save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_one save_ save_HCCH-TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_one save_ save_1H-13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _Sample_label $sample_one save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 na temperature 290 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 _Indirect_shift_ratio_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $citation_three DSS H 1 'methyl protons' ppm 0.00 . direct . . . 1.0 $citation_three DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_four 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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name Pdxo _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 SER HA H 3.88 0.02 1 2 . 1 SER HB2 H 3.57 0.02 1 3 . 1 SER HB3 H 3.40 0.02 1 4 . 1 SER C C 169.3 0.1 1 5 . 1 SER CA C 58.3 0.1 1 6 . 1 SER CB C 63.7 0.1 1 7 . 2 LYS H H 9.15 0.02 1 8 . 2 LYS HA H 4.58 0.02 1 9 . 2 LYS HB2 H 1.56 0.02 1 10 . 2 LYS HB3 H 1.25 0.02 1 11 . 2 LYS HG2 H 1.12 0.02 2 12 . 2 LYS HG3 H 1.00 0.02 2 13 . 2 LYS HD2 H 1.25 0.02 2 14 . 2 LYS HD3 H 1.35 0.02 2 15 . 2 LYS HE2 H 2.65 0.02 2 16 . 2 LYS HE3 H 2.63 0.02 2 17 . 2 LYS C C 175.0 0.1 1 18 . 2 LYS CA C 56.8 0.1 1 19 . 2 LYS CB C 33.0 0.1 1 20 . 2 LYS CG C 24.3 0.1 1 21 . 2 LYS CD C 28.3 0.1 1 22 . 2 LYS CE C 41.2 0.1 1 23 . 2 LYS N N 128.4 0.1 1 24 . 3 VAL H H 8.48 0.02 1 25 . 3 VAL HA H 4.18 0.02 1 26 . 3 VAL HB H 1.38 0.02 1 27 . 3 VAL HG1 H 0.05 0.02 1 28 . 3 VAL HG2 H 0.45 0.02 1 29 . 3 VAL C C 173.5 0.1 1 30 . 3 VAL CA C 60.0 0.1 1 31 . 3 VAL CB C 34.9 0.1 1 32 . 3 VAL CG1 C 20.4 0.1 1 33 . 3 VAL CG2 C 22.5 0.1 1 34 . 3 VAL N N 124.3 0.1 1 35 . 4 VAL H H 8.50 0.02 1 36 . 4 VAL HA H 4.40 0.02 1 37 . 4 VAL HB H 1.78 0.02 1 38 . 4 VAL HG1 H 0.53 0.02 1 39 . 4 VAL HG2 H 0.50 0.02 1 40 . 4 VAL C C 173.6 0.1 1 41 . 4 VAL CA C 60.5 0.1 1 42 . 4 VAL CB C 32.8 0.1 1 43 . 4 VAL CG1 C 21.0 0.1 1 44 . 4 VAL CG2 C 20.0 0.1 1 45 . 4 VAL N N 126.8 0.1 1 46 . 5 TYR H H 8.84 0.02 1 47 . 5 TYR HA H 4.72 0.02 1 48 . 5 TYR HB2 H 2.23 0.02 1 49 . 5 TYR HB3 H 2.72 0.02 1 50 . 5 TYR HD1 H 6.48 0.02 1 51 . 5 TYR HD2 H 6.48 0.02 1 52 . 5 TYR HE1 H 6.05 0.02 1 53 . 5 TYR HE2 H 6.05 0.02 1 54 . 5 TYR HH H 8.02 0.02 1 55 . 5 TYR C C 176.4 0.1 1 56 . 5 TYR CA C 55.2 0.1 1 57 . 5 TYR CB C 39.2 0.1 1 58 . 5 TYR CD1 C 133.1 0.1 1 59 . 5 TYR CD2 C 133.1 0.1 1 60 . 5 TYR CE1 C 117.7 0.1 1 61 . 5 TYR CE2 C 117.7 0.1 1 62 . 5 TYR N N 125.3 0.1 1 63 . 6 VAL H H 9.50 0.02 1 64 . 6 VAL HA H 4.68 0.02 1 65 . 6 VAL HB H 2.18 0.02 1 66 . 6 VAL HG1 H 0.72 0.02 1 67 . 6 VAL HG2 H 0.56 0.02 1 68 . 6 VAL C C 176.6 0.1 1 69 . 6 VAL CA C 61.7 0.1 1 70 . 6 VAL CB C 31.2 0.1 1 71 . 6 VAL CG1 C 20.8 0.1 1 72 . 6 VAL CG2 C 21.5 0.1 1 73 . 6 VAL N N 130.2 0.1 1 74 . 7 SER H H 8.95 0.02 1 75 . 7 SER HA H 4.31 0.02 1 76 . 7 SER HB2 H 3.78 0.02 2 77 . 7 SER HB3 H 3.68 0.02 2 78 . 7 SER C C 175.3 0.1 1 79 . 7 SER CA C 59.2 0.1 1 80 . 7 SER CB C 64.2 0.1 1 81 . 7 SER N N 124.2 0.1 1 82 . 8 HIS HA H 4.23 0.02 1 83 . 8 HIS HB2 H 3.10 0.02 2 84 . 8 HIS HB3 H 2.90 0.02 2 85 . 8 HIS HD1 H 9.45 0.02 1 86 . 8 HIS HD2 H 7.15 0.02 1 87 . 8 HIS HE1 H 7.92 0.02 1 88 . 8 HIS C C 175.1 0.1 1 89 . 8 HIS CA C 58.8 0.1 1 90 . 8 HIS CB C 29.6 0.1 1 91 . 8 HIS CD2 C 125.9 0.1 1 92 . 8 HIS CE1 C 138.0 0.1 1 93 . 8 HIS ND1 N 126.0 0.1 1 94 . 8 HIS NE2 N 187.0 0.1 1 95 . 9 ASP H H 7.41 0.02 1 96 . 9 ASP HA H 4.18 0.02 1 97 . 9 ASP HB2 H 2.09 0.02 1 98 . 9 ASP HB3 H 2.75 0.02 1 99 . 9 ASP C C 176.6 0.1 1 100 . 9 ASP CA C 52.5 0.1 1 101 . 9 ASP CB C 39.4 0.1 1 102 . 9 ASP N N 116.7 0.1 1 103 . 10 GLY H H 7.99 0.02 1 104 . 10 GLY HA2 H 4.05 0.02 2 105 . 10 GLY HA3 H 3.27 0.02 2 106 . 10 GLY C C 173.7 0.1 1 107 . 10 GLY CA C 44.6 0.1 1 108 . 10 GLY N N 109.7 0.1 1 109 . 11 THR H H 7.81 0.02 1 110 . 11 THR HA H 3.78 0.02 1 111 . 11 THR HB H 3.94 0.02 1 112 . 11 THR HG2 H 0.95 0.02 1 113 . 11 THR C C 173.1 0.1 1 114 . 11 THR CA C 64.2 0.1 1 115 . 11 THR CB C 68.2 0.1 1 116 . 11 THR CG2 C 21.3 0.1 1 117 . 11 THR N N 119.6 0.1 1 118 . 12 ARG H H 8.72 0.02 1 119 . 12 ARG HA H 4.58 0.02 1 120 . 12 ARG HB2 H 1.46 0.02 1 121 . 12 ARG HB3 H 1.53 0.02 1 122 . 12 ARG HG2 H 1.17 0.02 2 123 . 12 ARG HG3 H 1.50 0.02 2 124 . 12 ARG HD2 H 2.89 0.02 2 125 . 12 ARG HD3 H 3.12 0.02 2 126 . 12 ARG HE H 7.29 0.02 1 127 . 12 ARG C C 175.4 0.1 1 128 . 12 ARG CA C 55.5 0.1 1 129 . 12 ARG CB C 32.1 0.1 1 130 . 12 ARG CG C 28.2 0.1 1 131 . 12 ARG CD C 43.2 0.1 1 132 . 12 ARG N N 128.0 0.1 1 133 . 12 ARG NE N 86.1 0.1 1 134 . 13 ARG H H 8.49 0.02 1 135 . 13 ARG HA H 4.45 0.02 1 136 . 13 ARG HB2 H 1.66 0.02 1 137 . 13 ARG HB3 H 1.66 0.02 1 138 . 13 ARG HG2 H 1.30 0.02 2 139 . 13 ARG HG3 H 1.51 0.02 2 140 . 13 ARG HD2 H 2.97 0.02 2 141 . 13 ARG HD3 H 3.02 0.02 2 142 . 13 ARG HE H 6.74 0.02 1 143 . 13 ARG HH11 H 6.23 0.02 1 144 . 13 ARG HH12 H 6.23 0.02 1 145 . 13 ARG HH21 H 7.20 0.02 1 146 . 13 ARG HH22 H 7.20 0.02 1 147 . 13 ARG C C 173.4 0.1 1 148 . 13 ARG CA C 54.6 0.1 1 149 . 13 ARG CB C 32.4 0.1 1 150 . 13 ARG CG C 26.6 0.1 1 151 . 13 ARG CD C 43.2 0.1 1 152 . 13 ARG N N 123.2 0.1 1 153 . 13 ARG NE N 86.4 0.1 1 154 . 14 GLU H H 8.55 0.02 1 155 . 14 GLU HA H 5.10 0.02 1 156 . 14 GLU HB2 H 1.65 0.02 1 157 . 14 GLU HB3 H 1.68 0.02 1 158 . 14 GLU HG2 H 1.82 0.02 2 159 . 14 GLU HG3 H 1.97 0.02 2 160 . 14 GLU C C 175.3 0.1 1 161 . 14 GLU CA C 54.5 0.1 1 162 . 14 GLU CB C 31.8 0.1 1 163 . 14 GLU CG C 36.6 0.1 1 164 . 14 GLU N N 125.0 0.1 1 165 . 15 LEU H H 9.19 0.02 1 166 . 15 LEU HA H 4.54 0.02 1 167 . 15 LEU HB2 H 1.31 0.02 1 168 . 15 LEU HB3 H 1.23 0.02 1 169 . 15 LEU HG H 1.31 0.02 1 170 . 15 LEU HD1 H 0.52 0.02 1 171 . 15 LEU HD2 H 0.61 0.02 1 172 . 15 LEU C C 174.4 0.1 1 173 . 15 LEU CA C 53.0 0.1 1 174 . 15 LEU CB C 46.1 0.1 1 175 . 15 LEU CG C 26.5 0.1 1 176 . 15 LEU CD1 C 26.0 0.1 1 177 . 15 LEU CD2 C 23.5 0.1 1 178 . 15 LEU N N 126.8 0.1 1 179 . 16 ASP H H 8.19 0.02 1 180 . 16 ASP HA H 4.71 0.02 1 181 . 16 ASP HB2 H 2.42 0.02 2 182 . 16 ASP HB3 H 2.14 0.02 2 183 . 16 ASP C C 174.9 0.1 1 184 . 16 ASP CA C 53.3 0.1 1 185 . 16 ASP CB C 41.6 0.1 1 186 . 16 ASP N N 121.8 0.1 1 187 . 17 VAL H H 8.99 0.02 1 188 . 17 VAL HA H 3.81 0.02 1 189 . 17 VAL HB H 1.58 0.02 1 190 . 17 VAL HG1 H 0.66 0.02 1 191 . 17 VAL HG2 H 0.58 0.02 1 192 . 17 VAL C C 174.5 0.1 1 193 . 17 VAL CA C 61.5 0.1 1 194 . 17 VAL CB C 34.2 0.1 1 195 . 17 VAL CG1 C 21.4 0.1 1 196 . 17 VAL CG2 C 22.5 0.1 1 197 . 17 VAL N N 127.8 0.1 1 198 . 18 ALA H H 8.40 0.02 1 199 . 18 ALA HA H 3.92 0.02 1 200 . 18 ALA HB H 1.10 0.02 1 201 . 18 ALA C C 175.5 0.1 1 202 . 18 ALA CA C 51.7 0.1 1 203 . 18 ALA CB C 18.7 0.1 1 204 . 18 ALA N N 132.7 0.1 1 205 . 19 ASP H H 7.77 0.02 1 206 . 19 ASP HA H 3.88 0.02 1 207 . 19 ASP HB2 H 2.19 0.02 1 208 . 19 ASP HB3 H 2.42 0.02 1 209 . 19 ASP C C 178.1 0.1 1 210 . 19 ASP CA C 55.0 0.1 1 211 . 19 ASP CB C 39.8 0.1 1 212 . 19 ASP N N 119.4 0.1 1 213 . 20 GLY H H 8.80 0.02 1 214 . 20 GLY HA2 H 3.23 0.02 1 215 . 20 GLY HA3 H 4.08 0.02 1 216 . 20 GLY C C 173.2 0.1 1 217 . 20 GLY CA C 44.9 0.1 1 218 . 20 GLY N N 110.9 0.1 1 219 . 21 VAL H H 7.34 0.02 1 220 . 21 VAL HA H 3.87 0.02 1 221 . 21 VAL HB H 1.93 0.02 1 222 . 21 VAL HG1 H 0.89 0.02 1 223 . 21 VAL HG2 H 0.62 0.02 1 224 . 21 VAL C C 175.2 0.1 1 225 . 21 VAL CA C 61.4 0.1 1 226 . 21 VAL CB C 32.3 0.1 1 227 . 21 VAL CG1 C 20.8 0.1 1 228 . 21 VAL CG2 C 22.1 0.1 1 229 . 21 VAL N N 124.3 0.1 1 230 . 22 SER H H 8.75 0.02 1 231 . 22 SER HA H 5.18 0.02 1 232 . 22 SER HB2 H 3.69 0.02 1 233 . 22 SER HB3 H 4.08 0.02 1 234 . 22 SER C C 174.8 0.1 1 235 . 22 SER CA C 57.0 0.1 1 236 . 22 SER CB C 65.8 0.1 1 237 . 22 SER N N 122.8 0.1 1 238 . 23 LEU H H 8.38 0.02 1 239 . 23 LEU HA H 3.90 0.02 1 240 . 23 LEU HB2 H 1.65 0.02 1 241 . 23 LEU HB3 H 1.36 0.02 1 242 . 23 LEU HG H 1.65 0.02 1 243 . 23 LEU HD1 H 0.57 0.02 1 244 . 23 LEU HD2 H 0.52 0.02 1 245 . 23 LEU C C 180.5 0.1 1 246 . 23 LEU CA C 57.8 0.1 1 247 . 23 LEU CB C 41.4 0.1 1 248 . 23 LEU CG C 29.5 0.1 1 249 . 23 LEU CD1 C 23.5 0.1 1 250 . 23 LEU CD2 C 24.2 0.1 1 251 . 23 LEU N N 120.1 0.1 1 252 . 24 MET H H 7.98 0.02 1 253 . 24 MET HA H 4.18 0.02 1 254 . 24 MET HB2 H 1.83 0.02 1 255 . 24 MET HB3 H 2.05 0.02 1 256 . 24 MET HG2 H 0.69 0.02 1 257 . 24 MET HG3 H 0.69 0.02 1 258 . 24 MET C C 175.6 0.1 1 259 . 25 GLN HA H 3.63 0.02 1 260 . 25 GLN HB2 H 2.16 0.02 1 261 . 25 GLN HB3 H 1.80 0.02 1 262 . 25 GLN HG2 H 2.32 0.02 1 263 . 25 GLN HG3 H 2.32 0.02 1 264 . 25 GLN HE21 H 7.60 0.02 2 265 . 25 GLN HE22 H 6.34 0.02 2 266 . 25 GLN C C 179.2 0.1 1 267 . 25 GLN CA C 57.9 0.1 1 268 . 25 GLN CB C 32.3 0.1 1 269 . 25 GLN CG C 31.7 0.1 1 270 . 25 GLN CD C 175.5 0.1 1 271 . 25 GLN N N 115.3 0.1 1 272 . 25 GLN NE2 N 103.5 0.1 1 273 . 26 ALA H H 7.87 0.02 1 274 . 26 ALA HA H 3.82 0.02 1 275 . 26 ALA HB H 1.23 0.02 1 276 . 26 ALA C C 178.7 0.1 1 277 . 26 ALA CA C 54.3 0.1 1 278 . 26 ALA CB C 18.6 0.1 1 279 . 26 ALA N N 121.4 0.1 1 280 . 27 ALA H H 6.81 0.02 1 281 . 27 ALA HA H 3.23 0.02 1 282 . 27 ALA HB H 1.04 0.02 1 283 . 27 ALA C C 179.5 0.1 1 284 . 27 ALA CA C 54.6 0.1 1 285 . 27 ALA CB C 18.4 0.1 1 286 . 27 ALA N N 120.5 0.1 1 287 . 28 VAL H H 8.18 0.02 1 288 . 28 VAL HA H 3.71 0.02 1 289 . 28 VAL HB H 1.90 0.02 1 290 . 28 VAL HG1 H 0.68 0.02 1 291 . 28 VAL HG2 H 0.75 0.02 1 292 . 28 VAL C C 180.0 0.1 1 293 . 28 VAL CA C 64.7 0.1 1 294 . 28 VAL CB C 32.1 0.1 1 295 . 28 VAL CG1 C 20.1 0.1 1 296 . 28 VAL CG2 C 23.6 0.1 1 297 . 28 VAL N N 116.3 0.1 1 298 . 29 SER H H 7.71 0.02 1 299 . 29 SER HA H 4.18 0.02 1 300 . 29 SER HB2 H 3.71 0.02 2 301 . 29 SER HB3 H 3.65 0.02 2 302 . 29 SER C C 174.1 0.1 1 303 . 29 SER CA C 60.0 0.1 1 304 . 29 SER CB C 63.4 0.1 1 305 . 29 SER N N 115.3 0.1 1 306 . 30 ASN H H 7.04 0.02 1 307 . 30 ASN HA H 4.69 0.02 1 308 . 30 ASN HB2 H 2.60 0.02 1 309 . 30 ASN HB3 H 2.28 0.02 1 310 . 30 ASN HD21 H 7.05 0.02 2 311 . 30 ASN HD22 H 8.41 0.02 2 312 . 30 ASN C C 174.0 0.1 1 313 . 30 ASN CA C 53.1 0.1 1 314 . 30 ASN CB C 40.8 0.1 1 315 . 30 ASN CG C 178.2 0.1 1 316 . 30 ASN N N 118.2 0.1 1 317 . 30 ASN ND2 N 119.1 0.1 1 318 . 31 GLY H H 7.39 0.02 1 319 . 31 GLY HA2 H 3.55 0.02 1 320 . 31 GLY HA3 H 3.33 0.02 1 321 . 31 GLY C C 174.1 0.1 1 322 . 31 GLY CA C 46.7 0.1 1 323 . 31 GLY N N 107.2 0.1 1 324 . 32 ILE H H 7.52 0.02 1 325 . 32 ILE HA H 3.68 0.02 1 326 . 32 ILE HB H 1.37 0.02 1 327 . 32 ILE HG12 H 0.39 0.02 2 328 . 32 ILE HG13 H 0.65 0.02 2 329 . 32 ILE HG2 H 0.23 0.02 1 330 . 32 ILE HD1 H -0.02 0.02 1 331 . 32 ILE C C 175.1 0.1 1 332 . 32 ILE CA C 58.5 0.1 1 333 . 32 ILE CB C 32.8 0.1 1 334 . 32 ILE CG1 C 27.5 0.1 1 335 . 32 ILE CG2 C 15.8 0.1 1 336 . 32 ILE CD1 C 10.7 0.1 1 337 . 32 ILE N N 122.7 0.1 1 338 . 33 TYR H H 6.96 0.02 1 339 . 33 TYR HA H 4.25 0.02 1 340 . 33 TYR HB2 H 2.71 0.02 1 341 . 33 TYR HB3 H 2.88 0.02 1 342 . 33 TYR HD1 H 6.93 0.02 1 343 . 33 TYR HD2 H 6.93 0.02 1 344 . 33 TYR HE1 H 6.67 0.02 1 345 . 33 TYR HE2 H 6.67 0.02 1 346 . 33 TYR C C 175.3 0.1 1 347 . 33 TYR CA C 58.6 0.1 1 348 . 33 TYR CB C 38.0 0.1 1 349 . 33 TYR CD1 C 132.7 0.1 1 350 . 33 TYR CD2 C 132.7 0.1 1 351 . 33 TYR CE1 C 118.2 0.1 1 352 . 33 TYR CE2 C 118.2 0.1 1 353 . 33 TYR N N 122.2 0.1 1 354 . 34 ASP H H 9.47 0.02 1 355 . 34 ASP HA H 4.09 0.02 1 356 . 34 ASP HB2 H 2.50 0.02 1 357 . 34 ASP HB3 H 2.43 0.02 1 358 . 34 ASP C C 175.1 0.1 1 359 . 34 ASP CA C 52.2 0.1 1 360 . 34 ASP CB C 38.6 0.1 1 361 . 34 ASP N N 116.1 0.1 1 362 . 35 ILE H H 7.41 0.02 1 363 . 35 ILE HA H 3.50 0.02 1 364 . 35 ILE HB H 1.39 0.02 1 365 . 35 ILE HG12 H 0.40 0.02 2 366 . 35 ILE HG13 H 1.12 0.02 2 367 . 35 ILE CA C 61.4 0.1 1 368 . 35 ILE CB C 38.6 0.1 1 369 . 35 ILE CG1 C 27.9 0.1 1 370 . 35 ILE N N 121.5 0.1 1 371 . 49 HIS HB2 H 3.07 0.02 1 372 . 49 HIS HB3 H 3.18 0.02 1 373 . 49 HIS HD1 H 12.01 0.02 1 374 . 49 HIS HD2 H 6.68 0.02 1 375 . 49 HIS HE1 H 7.23 0.02 1 376 . 49 HIS C C 174.0 0.1 1 377 . 49 HIS CB C 37.1 0.1 1 378 . 49 HIS CD2 C 122.8 0.1 1 379 . 49 HIS CE1 C 136.3 0.1 1 380 . 49 HIS ND1 N 167.8 0.1 1 381 . 49 HIS NE2 N 246.8 0.1 1 382 . 50 VAL H H 8.92 0.02 1 383 . 50 VAL HA H 4.12 0.02 1 384 . 50 VAL HB H 1.78 0.02 1 385 . 50 VAL HG1 H 0.38 0.02 1 386 . 50 VAL HG2 H 0.71 0.02 1 387 . 50 VAL C C 171.7 0.1 1 388 . 50 VAL CA C 58.4 0.1 1 389 . 50 VAL CB C 36.8 0.1 1 390 . 50 VAL CG1 C 18.7 0.1 1 391 . 50 VAL CG2 C 23.8 0.1 1 392 . 50 VAL N N 118.0 0.1 1 393 . 51 TYR H H 8.95 0.02 1 394 . 51 TYR HA H 4.96 0.02 1 395 . 51 TYR HB2 H 2.69 0.02 1 396 . 51 TYR HB3 H 2.62 0.02 1 397 . 51 TYR HD1 H 6.63 0.02 1 398 . 51 TYR HD2 H 6.63 0.02 1 399 . 51 TYR HE1 H 6.65 0.02 1 400 . 51 TYR HE2 H 6.65 0.02 1 401 . 51 TYR C C 177.2 0.1 1 402 . 51 TYR CA C 53.9 0.1 1 403 . 51 TYR CB C 38.5 0.1 1 404 . 51 TYR CD1 C 132.5 0.1 1 405 . 51 TYR CD2 C 132.5 0.1 1 406 . 51 TYR CE1 C 117.8 0.1 1 407 . 51 TYR CE2 C 117.8 0.1 1 408 . 51 TYR N N 118.3 0.1 1 409 . 52 VAL H H 8.61 0.02 1 410 . 52 VAL HA H 3.63 0.02 1 411 . 52 VAL HB H 1.89 0.02 1 412 . 52 VAL HG1 H 0.82 0.02 1 413 . 52 VAL HG2 H 0.65 0.02 1 414 . 52 VAL C C 174.9 0.1 1 415 . 52 VAL CA C 64.5 0.1 1 416 . 52 VAL CB C 31.9 0.1 1 417 . 52 VAL CG1 C 21.1 0.1 1 418 . 52 VAL CG2 C 22.5 0.1 1 419 . 52 VAL N N 128.2 0.1 1 420 . 53 ASN H H 8.26 0.02 1 421 . 53 ASN HA H 4.28 0.02 1 422 . 53 ASN HB2 H 2.57 0.02 1 423 . 53 ASN HB3 H 2.79 0.02 1 424 . 53 ASN HD21 H 7.08 0.02 1 425 . 53 ASN HD22 H 8.04 0.02 1 426 . 53 ASN C C 176.5 0.1 1 427 . 53 ASN CA C 56.0 0.1 1 428 . 53 ASN CB C 38.6 0.1 1 429 . 53 ASN CG C 176.4 0.1 1 430 . 53 ASN N N 128.8 0.1 1 431 . 53 ASN ND2 N 116.9 0.1 1 432 . 54 GLU H H 9.09 0.02 1 433 . 54 GLU HA H 4.04 0.02 1 434 . 54 GLU HB2 H 1.80 0.02 1 435 . 54 GLU HB3 H 1.90 0.02 1 436 . 54 GLU HG2 H 2.14 0.02 1 437 . 54 GLU HG3 H 2.14 0.02 1 438 . 54 GLU C C 176.3 0.1 1 439 . 54 GLU CA C 59.3 0.1 1 440 . 54 GLU CB C 28.4 0.1 1 441 . 54 GLU CG C 35.9 0.1 1 442 . 54 GLU N N 125.5 0.1 1 443 . 55 ALA H H 8.30 0.02 1 444 . 55 ALA HA H 4.00 0.02 1 445 . 55 ALA HB H 1.00 0.02 1 446 . 55 ALA C C 177.7 0.1 1 447 . 55 ALA CA C 53.4 0.1 1 448 . 55 ALA CB C 17.6 0.1 1 449 . 55 ALA N N 122.2 0.1 1 450 . 56 PHE H H 8.66 0.02 1 451 . 56 PHE HA H 4.26 0.02 1 452 . 56 PHE HB2 H 2.98 0.02 1 453 . 56 PHE HB3 H 2.57 0.02 1 454 . 56 PHE HD1 H 6.96 0.02 1 455 . 56 PHE HD2 H 6.96 0.02 1 456 . 56 PHE HE1 H 7.10 0.02 1 457 . 56 PHE HE2 H 7.10 0.02 1 458 . 56 PHE HZ H 7.00 0.02 1 459 . 56 PHE C C 176.4 0.1 1 460 . 56 PHE CA C 58.1 0.1 1 461 . 56 PHE CB C 42.3 0.1 1 462 . 56 PHE CD1 C 133.1 0.1 1 463 . 56 PHE CD2 C 133.1 0.1 1 464 . 56 PHE CE1 C 132.1 0.1 1 465 . 56 PHE CE2 C 131.7 0.1 1 466 . 56 PHE CZ C 126.8 0.1 1 467 . 56 PHE N N 114.6 0.1 1 468 . 57 THR H H 7.33 0.02 1 469 . 57 THR HA H 3.58 0.02 1 470 . 57 THR HB H 4.03 0.02 1 471 . 57 THR HG2 H 1.11 0.02 1 472 . 57 THR C C 175.5 0.1 1 473 . 57 THR CA C 65.6 0.1 1 474 . 57 THR CB C 68.1 0.1 1 475 . 57 THR CG2 C 23.0 0.1 1 476 . 57 THR N N 114.6 0.1 1 477 . 58 ASP H H 8.52 0.02 1 478 . 58 ASP HA H 4.45 0.02 1 479 . 58 ASP HB2 H 2.45 0.02 2 480 . 58 ASP HB3 H 2.46 0.02 2 481 . 58 ASP C C 176.2 0.1 1 482 . 58 ASP CA C 54.4 0.1 1 483 . 58 ASP CB C 39.8 0.1 1 484 . 58 ASP CG C 178.9 0.1 1 485 . 58 ASP N N 118.4 0.1 1 486 . 59 LYS H H 7.32 0.02 1 487 . 59 LYS HA H 4.12 0.02 1 488 . 59 LYS HB2 H 1.73 0.02 1 489 . 59 LYS HB3 H 1.56 0.02 1 490 . 59 LYS HG2 H 1.25 0.02 2 491 . 59 LYS HG3 H 1.20 0.02 2 492 . 59 LYS HD2 H 1.49 0.02 2 493 . 59 LYS HD3 H 1.32 0.02 2 494 . 59 LYS HE2 H 2.74 0.02 2 495 . 59 LYS HE3 H 2.72 0.02 2 496 . 59 LYS C C 175.9 0.1 1 497 . 59 LYS CA C 56.1 0.1 1 498 . 59 LYS CB C 34.1 0.1 1 499 . 59 LYS CG C 24.9 0.1 1 500 . 59 LYS CD C 29.1 0.1 1 501 . 59 LYS CE C 41.7 0.1 1 502 . 59 LYS N N 118.3 0.1 1 503 . 60 VAL H H 6.88 0.02 1 504 . 60 VAL HA H 4.11 0.02 1 505 . 60 VAL HB H 1.86 0.02 1 506 . 60 VAL HG1 H 0.87 0.02 1 507 . 60 VAL HG2 H 0.79 0.02 1 508 . 60 VAL CA C 59.1 0.1 1 509 . 60 VAL CB C 32.5 0.1 1 510 . 60 VAL CG1 C 23.2 0.1 1 511 . 60 VAL CG2 C 21.4 0.1 1 512 . 60 VAL N N 118.4 0.1 1 513 . 61 PRO HA H 4.13 0.02 1 514 . 61 PRO HB2 H 2.18 0.02 2 515 . 61 PRO HB3 H 1.71 0.02 2 516 . 61 PRO HG2 H 1.84 0.02 2 517 . 61 PRO HG3 H 1.97 0.02 2 518 . 61 PRO HD2 H 3.84 0.02 1 519 . 61 PRO HD3 H 3.44 0.02 1 520 . 61 PRO C C 176.0 0.1 1 521 . 61 PRO CA C 63.2 0.1 1 522 . 61 PRO CB C 31.4 0.1 1 523 . 61 PRO CG C 27.8 0.1 1 524 . 61 PRO CD C 50.7 0.1 1 525 . 62 ALA H H 8.36 0.02 1 526 . 62 ALA HA H 3.88 0.02 1 527 . 62 ALA HB H 1.21 0.02 1 528 . 62 ALA C C 177.6 0.1 1 529 . 62 ALA CA C 52.1 0.1 1 530 . 62 ALA CB C 18.9 0.1 1 531 . 62 ALA N N 127.2 0.1 1 532 . 63 ALA H H 8.53 0.02 1 533 . 63 ALA HA H 3.89 0.02 1 534 . 63 ALA HB H 1.01 0.02 1 535 . 63 ALA C C 177.2 0.1 1 536 . 63 ALA CA C 53.0 0.1 1 537 . 63 ALA CB C 19.2 0.1 1 538 . 63 ALA N N 126.0 0.1 1 539 . 64 ASN H H 8.45 0.02 1 540 . 64 ASN HA H 4.57 0.02 1 541 . 64 ASN HB2 H 2.75 0.02 1 542 . 64 ASN HB3 H 3.15 0.02 1 543 . 64 ASN HD21 H 6.47 0.02 2 544 . 64 ASN HD22 H 7.48 0.02 2 545 . 64 ASN C C 174.3 0.1 1 546 . 64 ASN CA C 50.6 0.1 1 547 . 64 ASN CB C 38.6 0.1 1 548 . 64 ASN CG C 175.8 0.1 1 549 . 64 ASN N N 121.4 0.1 1 550 . 64 ASN ND2 N 111.9 0.1 1 551 . 65 GLU H H 8.48 0.02 1 552 . 65 GLU HA H 3.71 0.02 1 553 . 65 GLU HB2 H 1.88 0.02 1 554 . 65 GLU HB3 H 1.83 0.02 1 555 . 65 GLU HG2 H 2.09 0.02 2 556 . 65 GLU HG3 H 1.83 0.02 2 557 . 65 GLU C C 178.7 0.1 1 558 . 65 GLU CA C 59.7 0.1 1 559 . 65 GLU CB C 29.4 0.1 1 560 . 65 GLU CG C 35.5 0.1 1 561 . 65 GLU N N 117.3 0.1 1 562 . 66 ARG H H 7.88 0.02 1 563 . 66 ARG HA H 3.90 0.02 1 564 . 66 ARG HB2 H 1.70 0.02 1 565 . 66 ARG HB3 H 1.63 0.02 1 566 . 66 ARG HG2 H 1.52 0.02 1 567 . 66 ARG HG3 H 1.52 0.02 1 568 . 66 ARG HD2 H 2.99 0.02 2 569 . 66 ARG HD3 H 3.01 0.02 2 570 . 66 ARG HE H 6.74 0.02 1 571 . 66 ARG C C 178.7 0.1 1 572 . 66 ARG CA C 58.7 0.1 1 573 . 66 ARG CB C 28.9 0.1 1 574 . 66 ARG CG C 27.2 0.1 1 575 . 66 ARG CD C 43.0 0.1 1 576 . 66 ARG N N 122.3 0.1 1 577 . 67 GLU H H 8.09 0.02 1 578 . 67 GLU HA H 4.04 0.02 1 579 . 67 GLU HB2 H 1.61 0.02 1 580 . 67 GLU HB3 H 1.61 0.02 1 581 . 67 GLU HG2 H 2.00 0.02 1 582 . 67 GLU HG3 H 2.00 0.02 1 583 . 67 GLU C C 177.3 0.1 1 584 . 67 GLU CA C 59.0 0.1 1 585 . 67 GLU CB C 29.1 0.1 1 586 . 67 GLU CG C 33.5 0.1 1 587 . 67 GLU N N 122.2 0.1 1 588 . 68 ILE H H 8.29 0.02 1 589 . 68 ILE HA H 3.40 0.02 1 590 . 68 ILE HB H 1.61 0.02 1 591 . 68 ILE HG12 H 0.92 0.02 2 592 . 68 ILE HG13 H 1.36 0.02 2 593 . 68 ILE HG2 H 0.72 0.02 1 594 . 68 ILE HD1 H 0.52 0.02 1 595 . 68 ILE C C 178.3 0.1 1 596 . 68 ILE CA C 64.9 0.1 1 597 . 68 ILE CB C 37.4 0.1 1 598 . 68 ILE CG1 C 28.7 0.1 1 599 . 68 ILE CG2 C 16.8 0.1 1 600 . 68 ILE CD1 C 12.1 0.1 1 601 . 68 ILE N N 119.2 0.1 1 602 . 69 GLY H H 7.62 0.02 1 603 . 69 GLY HA2 H 3.62 0.02 1 604 . 69 GLY HA3 H 3.71 0.02 1 605 . 69 GLY C C 176.3 0.1 1 606 . 69 GLY CA C 46.7 0.1 1 607 . 69 GLY N N 105.3 0.1 1 608 . 70 MET H H 7.42 0.02 1 609 . 70 MET HA H 4.37 0.02 1 610 . 70 MET HE H 1.86 0.02 1 611 . 70 MET C C 179.3 0.1 1 612 . 70 MET CE C 16.6 0.1 1 613 . 70 MET N N 121.7 0.1 1 614 . 71 LEU H H 8.38 0.02 1 615 . 71 LEU HD1 H 0.71 0.02 1 616 . 71 LEU HD2 H 0.41 0.02 1 617 . 71 LEU C C 177.3 0.1 1 618 . 71 LEU CD1 C 25.6 0.1 1 619 . 71 LEU CD2 C 23.0 0.1 1 620 . 71 LEU N N 122.7 0.1 1 621 . 72 GLU H H 6.77 0.02 1 622 . 72 GLU HA H 3.83 0.02 1 623 . 72 GLU HB2 H 1.90 0.02 1 624 . 72 GLU HB3 H 1.90 0.02 1 625 . 72 GLU HG2 H 2.13 0.02 2 626 . 72 GLU HG3 H 2.36 0.02 2 627 . 72 GLU C C 177.8 0.1 1 628 . 72 GLU CA C 57.8 0.1 1 629 . 72 GLU CB C 28.9 0.1 1 630 . 72 GLU CG C 36.3 0.1 1 631 . 72 GLU N N 113.8 0.1 1 632 . 73 CYS H H 7.80 0.02 1 633 . 73 CYS HA H 4.49 0.02 1 634 . 73 CYS HB2 H 3.15 0.02 1 635 . 73 CYS HB3 H 2.89 0.02 1 636 . 73 CYS C C 175.3 0.1 1 637 . 73 CYS CA C 54.0 0.1 1 638 . 73 CYS CB C 29.9 0.1 1 639 . 73 CYS N N 115.9 0.1 1 640 . 74 VAL H H 7.11 0.02 1 641 . 74 VAL HA H 4.09 0.02 1 642 . 74 VAL HB H 1.68 0.02 1 643 . 74 VAL HG1 H 0.39 0.02 1 644 . 74 VAL HG2 H 0.68 0.02 1 645 . 74 VAL C C 176.6 0.1 1 646 . 74 VAL CA C 61.5 0.1 1 647 . 74 VAL CB C 32.9 0.1 1 648 . 74 VAL CG1 C 21.1 0.1 1 649 . 74 VAL CG2 C 17.7 0.1 1 650 . 74 VAL N N 115.8 0.1 1 651 . 75 THR H H 8.16 0.02 1 652 . 75 THR HA H 4.02 0.02 1 653 . 75 THR HB H 3.80 0.02 1 654 . 75 THR HG2 H 0.97 0.02 1 655 . 75 THR C C 176.6 0.1 1 656 . 75 THR CA C 61.9 0.1 1 657 . 75 THR CB C 68.5 0.1 1 658 . 75 THR CG2 C 22.7 0.1 1 659 . 75 THR N N 112.6 0.1 1 660 . 76 ALA H H 7.62 0.02 1 661 . 76 ALA HA H 4.38 0.02 1 662 . 76 ALA HB H 1.41 0.02 1 663 . 76 ALA C C 175.0 0.1 1 664 . 76 ALA CA C 50.6 0.1 1 665 . 76 ALA CB C 21.0 0.1 1 666 . 76 ALA N N 125.7 0.1 1 667 . 77 GLU H H 7.91 0.02 1 668 . 77 GLU HA H 3.71 0.02 1 669 . 77 GLU HB2 H 1.81 0.02 1 670 . 77 GLU HB3 H 1.58 0.02 1 671 . 77 GLU HG2 H 2.09 0.02 1 672 . 77 GLU HG3 H 2.09 0.02 1 673 . 77 GLU C C 176.5 0.1 1 674 . 77 GLU CA C 57.3 0.1 1 675 . 77 GLU CB C 30.2 0.1 1 676 . 77 GLU CG C 36.1 0.1 1 677 . 77 GLU N N 117.7 0.1 1 678 . 78 LEU H H 8.49 0.02 1 679 . 78 LEU HA H 4.41 0.02 1 680 . 78 LEU HB2 H 1.58 0.02 2 681 . 78 LEU HB3 H 1.18 0.02 2 682 . 78 LEU HG H 1.17 0.02 1 683 . 78 LEU HD1 H 0.82 0.02 1 684 . 78 LEU HD2 H 0.67 0.02 1 685 . 78 LEU C C 176.0 0.1 1 686 . 78 LEU CA C 54.8 0.1 1 687 . 78 LEU CB C 41.4 0.1 1 688 . 78 LEU CG C 26.1 0.1 1 689 . 78 LEU CD1 C 22.8 0.1 1 690 . 78 LEU CD2 C 25.4 0.1 1 691 . 78 LEU N N 131.1 0.1 1 692 . 79 LYS H H 9.71 0.02 1 693 . 79 LYS HA H 4.80 0.02 1 694 . 79 LYS HB2 H 1.73 0.02 1 695 . 79 LYS HB3 H 1.58 0.02 1 696 . 79 LYS HG2 H 0.93 0.02 2 697 . 79 LYS HG3 H 2.14 0.02 2 698 . 79 LYS HD2 H 1.07 0.02 2 699 . 79 LYS HD3 H 0.43 0.02 2 700 . 79 LYS HE2 H 2.57 0.02 2 701 . 79 LYS HE3 H 2.51 0.02 2 702 . 79 LYS CA C 54.3 0.1 1 703 . 79 LYS CB C 34.1 0.1 1 704 . 79 LYS CD C 28.4 0.1 1 705 . 79 LYS CE C 41.5 0.1 1 706 . 79 LYS N N 130.5 0.1 1 707 . 80 PRO HA H 4.24 0.02 1 708 . 80 PRO HB2 H 2.28 0.02 2 709 . 80 PRO HB3 H 1.76 0.02 2 710 . 80 PRO HG2 H 1.93 0.02 2 711 . 80 PRO HG3 H 2.14 0.02 2 712 . 80 PRO HD2 H 3.70 0.02 1 713 . 80 PRO HD3 H 3.52 0.02 1 714 . 80 PRO C C 176.7 0.1 1 715 . 80 PRO CA C 64.8 0.1 1 716 . 80 PRO CB C 31.5 0.1 1 717 . 80 PRO CG C 28.0 0.1 1 718 . 80 PRO CD C 50.4 0.1 1 719 . 81 ASN H H 8.62 0.02 1 720 . 81 ASN HA H 4.68 0.02 1 721 . 81 ASN HB2 H 2.58 0.02 1 722 . 81 ASN HB3 H 3.51 0.02 1 723 . 81 ASN HD21 H 7.45 0.02 1 724 . 81 ASN HD22 H 6.54 0.02 1 725 . 81 ASN C C 175.0 0.1 1 726 . 81 ASN CA C 51.3 0.1 1 727 . 81 ASN CB C 34.9 0.1 1 728 . 81 ASN CG C 178.6 0.1 1 729 . 81 ASN N N 110.9 0.1 1 730 . 81 ASN ND2 N 112.9 0.1 1 731 . 82 SER H H 7.98 0.02 1 732 . 82 SER HA H 5.03 0.02 1 733 . 82 SER HB2 H 3.98 0.02 1 734 . 82 SER HB3 H 3.90 0.02 1 735 . 82 SER HG H 10.10 0.02 1 736 . 82 SER C C 174.2 0.1 1 737 . 82 SER CA C 61.9 0.1 1 738 . 82 SER CB C 64.0 0.1 1 739 . 82 SER N N 122.0 0.1 1 740 . 83 ARG H H 9.37 0.02 1 741 . 83 ARG HA H 4.65 0.02 1 742 . 83 ARG HB2 H 1.57 0.02 1 743 . 83 ARG HB3 H 1.05 0.02 1 744 . 83 ARG HG2 H 1.56 0.02 2 745 . 83 ARG HG3 H 1.22 0.02 2 746 . 83 ARG HD2 H 3.39 0.02 2 747 . 83 ARG HD3 H 3.08 0.02 2 748 . 83 ARG HE H 10.29 0.02 1 749 . 83 ARG HH11 H 8.37 0.02 1 750 . 83 ARG HH12 H 8.37 0.02 1 751 . 83 ARG HH21 H 5.50 0.02 1 752 . 83 ARG HH22 H 5.50 0.02 1 753 . 83 ARG CA C 51.5 0.1 1 754 . 83 ARG CB C 34.2 0.1 1 755 . 83 ARG CD C 38.8 0.1 1 756 . 83 ARG N N 121.4 0.1 1 757 . 83 ARG NE N 85.6 0.1 1 758 . 87 GLN C C 180.6 0.1 1 759 . 88 ILE H H 6.84 0.02 1 760 . 88 ILE HA H 3.88 0.02 1 761 . 88 ILE HB H 1.56 0.02 1 762 . 88 ILE HG12 H 0.64 0.02 2 763 . 88 ILE HG13 H 1.34 0.02 2 764 . 88 ILE HG2 H 0.47 0.02 1 765 . 88 ILE HD1 H 0.35 0.02 1 766 . 88 ILE C C 172.4 0.1 1 767 . 88 ILE CA C 60.6 0.1 1 768 . 88 ILE CB C 38.1 0.1 1 769 . 88 ILE CG2 C 17.1 0.1 1 770 . 88 ILE CD1 C 13.8 0.1 1 771 . 88 ILE N N 120.2 0.1 1 772 . 89 ILE H H 8.37 0.02 1 773 . 89 ILE HA H 3.63 0.02 1 774 . 89 ILE HB H 1.60 0.02 1 775 . 89 ILE HG12 H 1.08 0.02 2 776 . 89 ILE HG13 H 1.12 0.02 2 777 . 89 ILE HG2 H 0.49 0.02 1 778 . 89 ILE HD1 H 0.33 0.02 1 779 . 89 ILE C C 175.1 0.1 1 780 . 89 ILE CA C 58.0 0.1 1 781 . 89 ILE CB C 36.2 0.1 1 782 . 89 ILE CG2 C 17.4 0.1 1 783 . 89 ILE CD1 C 9.3 0.1 1 784 . 89 ILE N N 129.1 0.1 1 785 . 90 MET H H 8.12 0.02 1 786 . 90 MET HA H 4.26 0.02 1 787 . 90 MET HB2 H 2.12 0.02 1 788 . 90 MET HB3 H 1.58 0.02 1 789 . 90 MET HG2 H 2.20 0.02 1 790 . 90 MET HG3 H 2.20 0.02 1 791 . 90 MET HE H 1.54 0.02 1 792 . 90 MET C C 175.3 0.1 1 793 . 90 MET CA C 56.2 0.1 1 794 . 90 MET CB C 30.8 0.1 1 795 . 90 MET CG C 32.4 0.1 1 796 . 90 MET CE C 18.1 0.1 1 797 . 90 MET N N 126.6 0.1 1 798 . 91 THR H H 7.10 0.02 1 799 . 91 THR HA H 4.53 0.02 1 800 . 91 THR HB H 4.40 0.02 1 801 . 91 THR HG2 H 1.04 0.02 1 802 . 91 THR CA C 58.3 0.1 1 803 . 91 THR CB C 69.7 0.1 1 804 . 91 THR CG2 C 21.2 0.1 1 805 . 91 THR N N 116.7 0.1 1 806 . 92 PRO HA H 4.28 0.02 1 807 . 92 PRO HB2 H 1.67 0.02 2 808 . 92 PRO HB3 H 2.24 0.02 2 809 . 92 PRO HG2 H 1.90 0.02 1 810 . 92 PRO HG3 H 1.90 0.02 1 811 . 92 PRO HD2 H 3.64 0.02 2 812 . 92 PRO HD3 H 3.61 0.02 2 813 . 92 PRO C C 179.4 0.1 1 814 . 92 PRO CA C 64.8 0.1 1 815 . 92 PRO CB C 31.4 0.1 1 816 . 92 PRO CG C 27.8 0.1 1 817 . 92 PRO CD C 50.4 0.1 1 818 . 93 GLU H H 8.13 0.02 1 819 . 93 GLU HA H 3.92 0.02 1 820 . 93 GLU HB2 H 1.81 0.02 2 821 . 93 GLU HB3 H 1.82 0.02 2 822 . 93 GLU HG2 H 2.14 0.02 2 823 . 93 GLU HG3 H 2.26 0.02 2 824 . 93 GLU C C 177.5 0.1 1 825 . 93 GLU CA C 58.8 0.1 1 826 . 93 GLU CB C 28.9 0.1 1 827 . 93 GLU CG C 37.1 0.1 1 828 . 93 GLU N N 117.0 0.1 1 829 . 94 LEU H H 7.56 0.02 1 830 . 94 LEU HA H 4.23 0.02 1 831 . 94 LEU HB2 H 1.39 0.02 1 832 . 94 LEU HB3 H 1.88 0.02 1 833 . 94 LEU HG H 1.57 0.02 1 834 . 94 LEU HD1 H 0.78 0.02 1 835 . 94 LEU HD2 H 0.61 0.02 1 836 . 94 LEU C C 174.3 0.1 1 837 . 94 LEU CA C 53.2 0.1 1 838 . 94 LEU CB C 41.9 0.1 1 839 . 94 LEU CG C 26.4 0.1 1 840 . 94 LEU CD1 C 25.8 0.1 1 841 . 94 LEU CD2 C 23.5 0.1 1 842 . 94 LEU N N 118.6 0.1 1 843 . 95 ASP H H 6.96 0.02 1 844 . 95 ASP HA H 3.89 0.02 1 845 . 95 ASP HB2 H 2.48 0.02 1 846 . 95 ASP HB3 H 2.74 0.02 1 847 . 95 ASP C C 176.3 0.1 1 848 . 95 ASP CA C 61.1 0.1 1 849 . 95 ASP CB C 42.3 0.1 1 850 . 95 ASP N N 118.1 0.1 1 851 . 96 GLY H H 9.64 0.02 1 852 . 96 GLY HA2 H 4.02 0.02 1 853 . 96 GLY HA3 H 2.82 0.02 1 854 . 96 GLY C C 171.8 0.1 1 855 . 96 GLY CA C 44.2 0.1 1 856 . 96 GLY N N 118.6 0.1 1 857 . 97 ILE H H 7.77 0.02 1 858 . 97 ILE HA H 1.03 0.02 1 859 . 97 ILE HB H 1.33 0.02 1 860 . 97 ILE HG12 H 0.53 0.02 2 861 . 97 ILE HG13 H 0.31 0.02 2 862 . 97 ILE HG2 H 0.64 0.02 1 863 . 97 ILE HD1 H 0.47 0.02 1 864 . 97 ILE C C 169.5 0.1 1 865 . 97 ILE CA C 61.1 0.1 1 866 . 97 ILE CB C 37.0 0.1 1 867 . 97 ILE CG1 C 28.9 0.1 1 868 . 97 ILE CG2 C 16.2 0.1 1 869 . 97 ILE CD1 C 14.1 0.1 1 870 . 97 ILE N N 121.6 0.1 1 871 . 98 VAL H H 4.88 0.02 1 872 . 98 VAL HA H 4.48 0.02 1 873 . 98 VAL HB H 1.39 0.02 1 874 . 98 VAL HG1 H 0.60 0.02 1 875 . 98 VAL HG2 H 0.74 0.02 1 876 . 98 VAL C C 175.1 0.1 1 877 . 98 VAL CA C 59.0 0.1 1 878 . 98 VAL CB C 34.5 0.1 1 879 . 98 VAL CG1 C 21.3 0.1 1 880 . 98 VAL CG2 C 20.2 0.1 1 881 . 98 VAL N N 126.2 0.1 1 882 . 99 VAL H H 8.59 0.02 1 883 . 99 VAL HA H 4.75 0.02 1 884 . 99 VAL HB H 1.48 0.02 1 885 . 99 VAL HG1 H 0.36 0.02 1 886 . 99 VAL HG2 H 0.30 0.02 1 887 . 99 VAL C C 172.5 0.1 1 888 . 99 VAL CA C 57.3 0.1 1 889 . 99 VAL CB C 33.7 0.1 1 890 . 99 VAL CG1 C 22.2 0.1 1 891 . 99 VAL CG2 C 19.5 0.1 1 892 . 99 VAL N N 118.5 0.1 1 893 . 100 ASP H H 8.82 0.02 1 894 . 100 ASP HA H 5.28 0.02 1 895 . 100 ASP HB2 H 2.50 0.02 1 896 . 100 ASP HB3 H 2.50 0.02 1 897 . 100 ASP C C 174.6 0.1 1 898 . 100 ASP CA C 52.4 0.1 1 899 . 100 ASP CB C 42.8 0.1 1 900 . 100 ASP N N 125.0 0.1 1 901 . 101 VAL H H 8.96 0.02 1 902 . 101 VAL HA H 4.23 0.02 1 903 . 101 VAL HB H 1.88 0.02 1 904 . 101 VAL HG1 H 0.73 0.02 1 905 . 101 VAL HG2 H 0.58 0.02 1 906 . 101 VAL CA C 59.0 0.1 1 907 . 101 VAL CB C 32.9 0.1 1 908 . 101 VAL CG1 C 22.9 0.1 1 909 . 101 VAL CG2 C 20.8 0.1 1 910 . 101 VAL N N 125.0 0.1 1 911 . 102 PRO HA H 4.50 0.02 1 912 . 102 PRO HB2 H 2.02 0.02 1 913 . 102 PRO HB3 H 1.72 0.02 1 914 . 102 PRO HG2 H 0.70 0.02 2 915 . 102 PRO HG3 H 1.20 0.02 2 916 . 102 PRO HD2 H 3.54 0.02 2 917 . 102 PRO HD3 H 2.73 0.02 2 918 . 102 PRO C C 176.1 0.1 1 919 . 102 PRO CA C 61.7 0.1 1 920 . 102 PRO CB C 31.5 0.1 1 921 . 102 PRO CG C 25.7 0.1 1 922 . 102 PRO CD C 51.7 0.1 1 923 . 103 ASP H H 8.64 0.02 1 924 . 103 ASP HA H 3.76 0.02 1 925 . 103 ASP HB2 H 2.60 0.02 1 926 . 103 ASP HB3 H 2.18 0.02 1 927 . 103 ASP C C 175.9 0.1 1 928 . 103 ASP CA C 54.4 0.1 1 929 . 103 ASP CB C 41.4 0.1 1 930 . 103 ASP N N 119.4 0.1 1 931 . 104 ARG H H 6.82 0.02 1 932 . 104 ARG HA H 4.37 0.02 1 933 . 104 ARG HB2 H 1.59 0.02 2 934 . 104 ARG HB3 H 1.66 0.02 2 935 . 104 ARG HG2 H 1.31 0.02 1 936 . 104 ARG HG3 H 1.31 0.02 1 937 . 104 ARG HD2 H 2.78 0.02 2 938 . 104 ARG HD3 H 2.83 0.02 2 939 . 104 ARG HE H 7.13 0.02 1 940 . 104 ARG C C 173.5 0.1 1 941 . 104 ARG CA C 55.0 0.1 1 942 . 104 ARG CB C 30.5 0.1 1 943 . 104 ARG CG C 24.0 0.1 1 944 . 104 ARG CD C 43.5 0.1 1 945 . 104 ARG N N 115.1 0.1 1 946 . 104 ARG NE N 70.0 0.1 1 947 . 105 GLN H H 8.43 0.02 1 948 . 105 GLN HA H 4.34 0.02 1 949 . 105 GLN HB2 H 0.97 0.02 1 950 . 105 GLN HB3 H 0.97 0.02 1 951 . 105 GLN HG2 H 2.33 0.02 2 952 . 105 GLN HG3 H 1.44 0.02 2 953 . 105 GLN HE21 H 7.31 0.02 2 954 . 105 GLN HE22 H 6.77 0.02 2 955 . 105 GLN C C 176.8 0.1 1 956 . 105 GLN CA C 55.0 0.1 1 957 . 105 GLN CB C 27.0 0.1 1 958 . 105 GLN CD C 179.6 0.1 1 959 . 105 GLN N N 118.5 0.1 1 960 . 105 GLN NE2 N 113.6 0.1 1 961 . 106 TRP H H 7.84 0.02 1 962 . 106 TRP HA H 4.46 0.02 1 963 . 106 TRP HB2 H 3.32 0.02 1 964 . 106 TRP HB3 H 2.82 0.02 1 965 . 106 TRP HD1 H 7.06 0.02 1 966 . 106 TRP HE1 H 10.04 0.02 1 967 . 106 TRP HE3 H 7.56 0.02 1 968 . 106 TRP HZ2 H 7.20 0.02 1 969 . 106 TRP HZ3 H 6.90 0.02 1 970 . 106 TRP HH2 H 6.92 0.02 1 971 . 106 TRP CA C 57.8 0.1 1 972 . 106 TRP CB C 30.2 0.1 1 973 . 106 TRP CD1 C 126.5 0.1 1 974 . 106 TRP CE3 C 138.5 0.1 1 975 . 106 TRP CZ2 C 114.1 0.1 1 976 . 106 TRP CZ3 C 132.7 0.1 1 977 . 106 TRP CH2 C 133.1 0.1 1 978 . 106 TRP N N 127.0 0.1 1 979 . 106 TRP NE1 N 126.9 0.1 1 stop_ save_