data_4186 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure of Human Cellular Retinoic Acid Binding Protein-Type II ; _BMRB_accession_number 4186 _BMRB_flat_file_name bmr4186.str _Entry_type original _Submission_date 1998-08-13 _Accession_date 1998-08-13 _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 Wang L. . . 2 Li Yue . . 3 Abildgaard Frits . . 4 Markley John L. . 5 Yan Honggao . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 662 "13C chemical shifts" 331 "15N chemical shifts" 118 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-08 original author . stop_ _Original_release_date 2000-03-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Wang, L., Li, Y., Abildgaard, F., Markley, J.L., and Yan, H., "NMR Solution Structure of type II Human Cellular Retinoic Acid Binding Protein: Implications for Ligand Binding," Biochemistry 37, 12727-12736 (1998). ; _Citation_title ; NMR Solution Structure of type II Human Cellular Retinoic Acid Binding Protein: Implications for Ligand Binding ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98409425 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang L. . . 2 Li Yue . . 3 Abildgaard Frits . . 4 Markley John L. . 5 Yan Honggao . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 37 _Journal_issue 37 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 12727 _Page_last 12736 _Year 1998 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _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_ ################################## # Molecular system description # ################################## save_system_CRABPII _Saveframe_category molecular_system _Mol_system_name 'CRABPII system' _Abbreviation_common 'CRABPII system' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label CRABPII $CRABPII stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not reported' loop_ _Biological_function 'Binding all-trans-retinoic acid' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CRABPII _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Cellular Retinoic Acid Binding Protein-Type II' _Abbreviation_common CRABPII _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 137 _Mol_residue_sequence ; PNFSGNWKIIRSENFEELLK VLGVNVMLRKIAVAAASKPA VEIKQEGDTFYIKTSTTVRT TEINFKVGEEFEEQTVDGRP CKSLVKWESENKMVCEQKLL KGEGPKTSWTRELTNDGELI LTMTADDVVCTRVYVRE ; loop_ _Residue_seq_code _Residue_label 1 PRO 2 ASN 3 PHE 4 SER 5 GLY 6 ASN 7 TRP 8 LYS 9 ILE 10 ILE 11 ARG 12 SER 13 GLU 14 ASN 15 PHE 16 GLU 17 GLU 18 LEU 19 LEU 20 LYS 21 VAL 22 LEU 23 GLY 24 VAL 25 ASN 26 VAL 27 MET 28 LEU 29 ARG 30 LYS 31 ILE 32 ALA 33 VAL 34 ALA 35 ALA 36 ALA 37 SER 38 LYS 39 PRO 40 ALA 41 VAL 42 GLU 43 ILE 44 LYS 45 GLN 46 GLU 47 GLY 48 ASP 49 THR 50 PHE 51 TYR 52 ILE 53 LYS 54 THR 55 SER 56 THR 57 THR 58 VAL 59 ARG 60 THR 61 THR 62 GLU 63 ILE 64 ASN 65 PHE 66 LYS 67 VAL 68 GLY 69 GLU 70 GLU 71 PHE 72 GLU 73 GLU 74 GLN 75 THR 76 VAL 77 ASP 78 GLY 79 ARG 80 PRO 81 CYS 82 LYS 83 SER 84 LEU 85 VAL 86 LYS 87 TRP 88 GLU 89 SER 90 GLU 91 ASN 92 LYS 93 MET 94 VAL 95 CYS 96 GLU 97 GLN 98 LYS 99 LEU 100 LEU 101 LYS 102 GLY 103 GLU 104 GLY 105 PRO 106 LYS 107 THR 108 SER 109 TRP 110 THR 111 ARG 112 GLU 113 LEU 114 THR 115 ASN 116 ASP 117 GLY 118 GLU 119 LEU 120 ILE 121 LEU 122 THR 123 MET 124 THR 125 ALA 126 ASP 127 ASP 128 VAL 129 VAL 130 CYS 131 THR 132 ARG 133 VAL 134 TYR 135 VAL 136 ARG 137 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-02-25 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 PDB 1BLR "Nmr Solution Structure Of Human Cellular Retinoic Acid Binding Protein-Type Ii, 22 Structures" 100.00 137 100.00 100.00 1.45e-93 PDB 1BM5 "The Solution Structure Of A Site-Directed Mutant (R111m) Of Human Cellular Retionic Acid Binding Protein-Type Ii, Nmr, 31 Struc" 100.00 137 99.27 99.27 1.32e-92 PDB 1CBQ "Crystal Structure Of Cellular Retinoic-Acid-Binding Proteins I And Ii In Complex With All-Trans-Retinoic Acid And A Synthetic R" 100.00 137 100.00 100.00 1.45e-93 PDB 1CBS "Crystal Structure Of Cellular Retinoic-Acid-Binding Proteins I And Ii In Complex With All-Trans-Retinoic Acid And A Synthetic R" 100.00 137 100.00 100.00 1.45e-93 PDB 1XCA "Apo-Cellular Retinoic Acid Binding Protein Ii" 100.00 137 99.27 99.27 1.32e-92 PDB 2CBS "Cellular Retinoic Acid Binding Protein Ii In Complex With A Synthetic Retinoic Acid (Ro-13 6307)" 100.00 137 100.00 100.00 1.45e-93 PDB 2FR3 "Crystal Structure Of Cellular Retinoic Acid Binding Protein Type Ii In Complex With All-Trans-Retinoic Acid At 1.48 Angstroms R" 100.00 137 100.00 100.00 1.45e-93 PDB 2FRS "Crystal Structure Of The F15w Mutant Of Apo-Cellular Retinoic Acid Binding Protein Type Ii At 1.51 Angstroms Resolution" 100.00 137 99.27 100.00 1.75e-92 PDB 2FS6 "Crystal Structure Of Apo-Cellular Retinoic Acid Binding Protein Type Ii At 1.35 Angstroms Resolution" 100.00 137 100.00 100.00 1.45e-93 PDB 2FS7 "Crystal Structure Of Apo-Cellular Retinoic Acid Binding Protein Type Ii At 1.55 Angstroms Resolution" 100.00 137 100.00 100.00 1.45e-93 PDB 2G78 "Crystal Structure Of The R132k:y134f Mutant Of Cellular Retinoic Acid Binding Protein Type Ii In Complex With All- Trans-Retino" 100.00 137 98.54 100.00 2.43e-92 PDB 2G79 "Crystal Structure Of The R132k:y134f Mutant Of Cellular Retinoic Acid Binding Protein Type Ii In Complex With All- Trans-Retina" 100.00 137 98.54 100.00 2.43e-92 PDB 2G7B "Crystal Structure Of The R132k:r111l:l121e Mutant Of Cellular Retinoic Acid Binding Protein Type Ii In Complex With All-trans-r" 100.00 137 97.81 98.54 1.09e-90 PDB 3CBS "Cellular Retinoic Acid Binding Protein Ii In Complex With A Synthetic Retinoic Acid (Ro-12 7310)" 100.00 137 100.00 100.00 1.45e-93 PDB 3CR6 "Crystal Structure Of The R132k:r111l:a32e Mutant Of Cellular Retinoic Acid Binding Protein Type Ii Complexed With C15-Aldehyde " 100.00 137 97.81 98.54 6.80e-91 PDB 3D96 "Crystal Structure Of The R132k:y134f Mutant Of Apo-Cellular Retinoic Acid Binding Protein Type Ii At 1.71 Angstroms Resolution" 100.00 137 98.54 100.00 2.43e-92 PDB 3D97 "Crystal Structure Of The R132k:r111l:l121e Mutant Of Apo- Cellular Retinoic Acid Binding Protein Type Ii At 1.50 Angstroms Reso" 100.00 137 97.81 98.54 1.09e-90 PDB 3F8A "Crystal Structure Of The R132k:r111l:l121e:r59w Mutant Of Cellular Retinoic Acid-Binding Protein Type Ii Complexed With C15-Ald" 100.00 137 97.08 97.81 3.47e-89 PDB 3F9D "Crystal Structure Of The R132k:r111l:t54e Mutant Of Cellular Retinoic Acid-Binding Protein Ii Complexed With C15- Aldehyde (A R" 100.00 137 97.81 98.54 5.71e-91 PDB 3FA7 "Crystal Structure Of The Apo R132k:r111l:l121e:r59e Mutant Of Cellular Retinoic Acid-binding Protein Ii At 1.90 Angstrom Resolu" 100.00 137 97.08 97.81 8.66e-90 PDB 3FA8 "Crystal Structure Of The Apo R132k:y134f:r111l:l121e Mutant Of Cellular Retinoic Acid-Binding Protein Ii At 1.78 Anstrom Resolu" 100.00 137 97.08 98.54 5.13e-90 PDB 3FA9 "Crystal Structure Of The Apo R132k:y134f:r111l:l121d Mutant Of Cellular Retinoic Acid-binding Protein Ii At 1.94 Angstrom Resol" 100.00 137 97.08 98.54 5.60e-90 PDB 3FEL "Crystal Structure Of The R132k:r111l:t54e Mutant Of Cellular Retinoic Acid-Binding Protein Ii At 1.85 Anstrom Resolution" 100.00 137 97.81 98.54 5.71e-91 PDB 3FEN "Crystal Structure Of The R132k:r111l:a32e Mutant Of Cellular Retinoic Acid-Binding Protein Ii At 1.56 Anstrom Resolution" 100.00 137 97.81 98.54 6.80e-91 PDB 3FEP "Crystal Sturcture Of The R132k:r111l:l121e:r59w-crabpii Mutant Complexed With A Synthetic Ligand (merocyanin) At 2.60 Anstrom R" 100.00 137 97.08 97.81 3.47e-89 PDB 3I17 "Crystal Structure Of The Apo R132k:l121e Mutant Of Cellular Retinoic Acid-Binding Protein Ii At 1.68 Anstrom Resolution" 100.00 137 98.54 99.27 8.45e-92 PDB 4QGV "Crystal Sturcture Of The R132k:r111l Mutant Of Cellular Retinoic Acid Binding Proteinii Complexed With A Synthetic Ligand (mero" 100.00 137 98.54 99.27 6.43e-92 PDB 4QGW "Crystal Sturcture Of The R132k:r111l:l121d Mutant Of Cellular Retinoic Acid Binding Proteinii Complexed With A Synthetic Ligand" 100.00 137 97.81 98.54 1.30e-90 PDB 4QGX "Crystal Sturcture Of The R132k:r111l:l121e Mutant Of Cellular Retinoic Acid Binding Proteinii Complexed With A Synthetic Ligand" 100.00 137 97.81 98.54 1.09e-90 DBJ BAG34945 "unnamed protein product [Homo sapiens]" 100.00 138 100.00 100.00 1.39e-93 DBJ BAJ83972 "cellular retinoic acid binding protein 2 [Homo sapiens]" 100.00 138 100.00 100.00 1.39e-93 EMBL CAG29353 "CRABP2 [Homo sapiens]" 100.00 138 100.00 100.00 1.39e-93 GB AAA52068 "retinoic acid binding protein II [Homo sapiens]" 100.00 138 100.00 100.00 1.39e-93 GB AAA58430 "retinoic acid-binding protein II [Homo sapiens]" 100.00 138 100.00 100.00 1.39e-93 GB AAH01109 "Cellular retinoic acid binding protein 2 [Homo sapiens]" 100.00 138 100.00 100.00 1.39e-93 GB AAV38629 "cellular retinoic acid binding protein 2 [synthetic construct]" 100.00 139 100.00 100.00 1.27e-93 GB AAV38630 "cellular retinoic acid binding protein 2 [Homo sapiens]" 100.00 138 100.00 100.00 1.39e-93 REF NP_001008670 "cellular retinoic acid-binding protein 2 [Bos taurus]" 100.00 138 97.08 100.00 2.06e-92 REF NP_001186652 "cellular retinoic acid-binding protein 2 [Homo sapiens]" 100.00 138 100.00 100.00 1.39e-93 REF NP_001253818 "cellular retinoic acid-binding protein 2 [Macaca mulatta]" 100.00 138 99.27 100.00 4.28e-93 REF NP_001869 "cellular retinoic acid-binding protein 2 [Homo sapiens]" 100.00 138 100.00 100.00 1.39e-93 REF XP_001166367 "PREDICTED: cellular retinoic acid-binding protein 2 [Pan troglodytes]" 100.00 138 100.00 100.00 1.39e-93 SP P29373 "RecName: Full=Cellular retinoic acid-binding protein 2; AltName: Full=Cellular retinoic acid-binding protein II; Short=CRABP-II" 100.00 138 100.00 100.00 1.39e-93 SP Q5PXY7 "RecName: Full=Cellular retinoic acid-binding protein 2; AltName: Full=Cellular retinoic acid-binding protein II; Short=CRABP-II" 100.00 138 97.08 100.00 2.06e-92 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CRABPII human 9606 Eucaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $CRABPII 'recombinant technology' . . . . pET-17b 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $CRABPII . mM 1.5 2.0 . stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name FELIX _Version 95 loop_ _Task 'Data processing and peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer VARIAN _Model UNITY _Field_strength 500 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer BRUKER _Model DMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_one save_ save_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name TOCSY _Sample_label $sample_one save_ save_triple_resonance_experiments_3 _Saveframe_category NMR_applied_experiment _Experiment_name 'triple resonance experiments' _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.3 0.1 n/a temperature 298 0.5 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_one DSS H 1 'methyl protons' ppm 0.00 . direct . . . . $citation_one DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_one 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 CRABPII _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 PRO HA H 4.32 . 1 2 . 1 PRO HB2 H 2.37 . 2 3 . 1 PRO HB3 H 1.91 . 2 4 . 1 PRO HG2 H 2.10 . 2 5 . 1 PRO HG3 H 2.08 . 2 6 . 1 PRO HD2 H 3.32 . 2 7 . 1 PRO HD3 H 3.25 . 2 8 . 1 PRO CA C 63.0 . 1 9 . 1 PRO CB C 33.2 . 1 10 . 2 ASN HA H 5.03 . 1 11 . 2 ASN HB2 H 2.95 . 2 12 . 2 ASN HB3 H 2.89 . 2 13 . 2 ASN C C 171.9 . 1 14 . 2 ASN CA C 52.7 . 1 15 . 2 ASN CB C 39.3 . 1 16 . 3 PHE H H 9.82 . 1 17 . 3 PHE HA H 4.32 . 1 18 . 3 PHE HB2 H 3.28 . 2 19 . 3 PHE HB3 H 2.70 . 2 20 . 3 PHE C C 173.5 . 1 21 . 3 PHE CA C 60.4 . 1 22 . 3 PHE CB C 32.3 . 1 23 . 3 PHE N N 121.9 . 1 24 . 4 SER H H 8.49 . 1 25 . 4 SER HA H 4.30 . 1 26 . 4 SER HB2 H 3.99 . 1 27 . 4 SER HB3 H 3.99 . 1 28 . 4 SER C C 171.8 . 1 29 . 4 SER CA C 60.7 . 1 30 . 4 SER CB C 64.5 . 1 31 . 4 SER N N 112.5 . 1 32 . 5 GLY H H 9.22 . 1 33 . 5 GLY HA2 H 3.96 . 2 34 . 5 GLY HA3 H 3.76 . 2 35 . 5 GLY C C 167.9 . 1 36 . 5 GLY CA C 44.9 . 1 37 . 5 GLY N N 110.6 . 1 38 . 6 ASN H H 8.15 . 1 39 . 6 ASN HA H 5.52 . 1 40 . 6 ASN HB2 H 2.69 . 2 41 . 6 ASN HB3 H 2.52 . 2 42 . 6 ASN C C 171.5 . 1 43 . 6 ASN CA C 53.0 . 1 44 . 6 ASN CB C 40.2 . 1 45 . 6 ASN N N 118.6 . 1 46 . 7 TRP H H 9.35 . 1 47 . 7 TRP HA H 5.14 . 1 48 . 7 TRP HB2 H 3.06 . 2 49 . 7 TRP HB3 H 2.66 . 2 50 . 7 TRP C C 172.5 . 1 51 . 7 TRP CA C 56.7 . 1 52 . 7 TRP CB C 32.2 . 1 53 . 7 TRP N N 123.3 . 1 54 . 8 LYS H H 10.17 . 1 55 . 8 LYS HA H 5.28 . 1 56 . 8 LYS HB2 H 1.90 . 2 57 . 8 LYS HB3 H 1.85 . 2 58 . 8 LYS HG2 H 1.63 . 2 59 . 8 LYS HG3 H 1.52 . 2 60 . 8 LYS HD2 H 1.37 . 2 61 . 8 LYS HD3 H 1.33 . 2 62 . 8 LYS HE2 H 2.85 . 1 63 . 8 LYS HE3 H 2.85 . 1 64 . 8 LYS C C 172.4 . 1 65 . 8 LYS CA C 54.1 . 1 66 . 8 LYS CB C 36.1 . 1 67 . 8 LYS N N 123.2 . 1 68 . 9 ILE H H 9.05 . 1 69 . 9 ILE HA H 3.92 . 1 70 . 9 ILE HB H 1.76 . 1 71 . 9 ILE HG12 H 1.65 . 2 72 . 9 ILE HG13 H 1.56 . 2 73 . 9 ILE HG2 H 1.39 . 1 74 . 9 ILE HD1 H 0.48 . 1 75 . 9 ILE C C 173.3 . 1 76 . 9 ILE CA C 55.5 . 1 77 . 9 ILE CB C 33.6 . 1 78 . 9 ILE N N 125.6 . 1 79 . 10 ILE H H 9.24 . 1 80 . 10 ILE HA H 4.61 . 1 81 . 10 ILE HB H 1.83 . 1 82 . 10 ILE HG2 H 0.87 . 1 83 . 10 ILE C C 173.3 . 1 84 . 10 ILE CA C 61.3 . 1 85 . 10 ILE CB C 41.8 . 1 86 . 10 ILE N N 118.8 . 1 87 . 12 SER H H 8.33 . 1 88 . 12 SER HA H 5.12 . 1 89 . 12 SER HB2 H 3.61 . 2 90 . 12 SER HB3 H 3.43 . 2 91 . 12 SER C C 171.0 . 1 92 . 12 SER CA C 62.8 . 1 93 . 12 SER N N 115.8 . 1 94 . 13 GLU H H 8.71 . 1 95 . 13 GLU HA H 4.80 . 1 96 . 13 GLU HB2 H 2.19 . 2 97 . 13 GLU HB3 H 2.08 . 2 98 . 13 GLU HG2 H 1.93 . 1 99 . 13 GLU HG3 H 1.93 . 1 100 . 13 GLU CA C 61.7 . 1 101 . 13 GLU CB C 40.1 . 1 102 . 13 GLU N N 124.0 . 1 103 . 14 ASN H H 9.25 . 1 104 . 14 ASN HA H 4.95 . 1 105 . 14 ASN HB2 H 3.31 . 2 106 . 14 ASN HB3 H 3.22 . 2 107 . 14 ASN CA C 55.7 . 1 108 . 14 ASN CB C 41.4 . 1 109 . 14 ASN N N 117.8 . 1 110 . 15 PHE H H 8.72 . 1 111 . 15 PHE HA H 4.59 . 1 112 . 15 PHE HB2 H 2.98 . 2 113 . 15 PHE HB3 H 2.85 . 2 114 . 15 PHE CA C 55.3 . 1 115 . 15 PHE CB C 33.7 . 1 116 . 15 PHE N N 119.3 . 1 117 . 16 GLU H H 8.36 . 1 118 . 16 GLU HA H 3.30 . 1 119 . 16 GLU HB2 H 1.96 . 1 120 . 16 GLU HB3 H 1.96 . 1 121 . 16 GLU HG2 H 2.16 . 1 122 . 16 GLU HG3 H 2.16 . 1 123 . 16 GLU C C 172.1 . 1 124 . 16 GLU CA C 63.2 . 1 125 . 16 GLU CB C 32.6 . 1 126 . 16 GLU N N 117.4 . 1 127 . 17 GLU H H 8.36 . 1 128 . 17 GLU HA H 3.68 . 1 129 . 17 GLU HB2 H 1.84 . 2 130 . 17 GLU HB3 H 1.73 . 2 131 . 17 GLU HG2 H 2.38 . 2 132 . 17 GLU HG3 H 2.19 . 2 133 . 17 GLU C C 175.9 . 1 134 . 17 GLU CA C 59.6 . 1 135 . 17 GLU CB C 28.1 . 1 136 . 17 GLU N N 118.5 . 1 137 . 18 LEU H H 7.59 . 1 138 . 18 LEU HA H 3.73 . 1 139 . 18 LEU HB2 H 2.17 . 2 140 . 18 LEU HB3 H 1.34 . 2 141 . 18 LEU HG H 0.81 . 1 142 . 18 LEU HD1 H 0.74 . 2 143 . 18 LEU HD2 H 0.70 . 2 144 . 18 LEU C C 174.9 . 1 145 . 18 LEU CA C 58.5 . 1 146 . 18 LEU CB C 42.4 . 1 147 . 18 LEU N N 121.4 . 1 148 . 19 LEU H H 7.36 . 1 149 . 19 LEU HA H 3.62 . 1 150 . 19 LEU HB2 H 1.62 . 2 151 . 19 LEU HB3 H 1.56 . 2 152 . 19 LEU HG H 1.12 . 1 153 . 19 LEU HD1 H 0.36 . 2 154 . 19 LEU HD2 H 0.32 . 2 155 . 19 LEU C C 176.0 . 1 156 . 19 LEU CA C 57.6 . 1 157 . 19 LEU CB C 41.1 . 1 158 . 19 LEU N N 114.5 . 1 159 . 20 LYS H H 8.18 . 1 160 . 20 LYS HA H 3.83 . 1 161 . 20 LYS HB2 H 1.93 . 2 162 . 20 LYS HB3 H 1.61 . 2 163 . 20 LYS HG2 H 1.35 . 2 164 . 20 LYS HG3 H 1.14 . 2 165 . 20 LYS HE2 H 2.91 . 1 166 . 20 LYS HE3 H 2.91 . 1 167 . 20 LYS C C 178.3 . 1 168 . 20 LYS CA C 60.5 . 1 169 . 20 LYS CB C 32.6 . 1 170 . 20 LYS N N 118.9 . 1 171 . 21 VAL H H 7.83 . 1 172 . 21 VAL HA H 3.78 . 1 173 . 21 VAL HB H 2.15 . 1 174 . 21 VAL HG1 H 1.10 . 2 175 . 21 VAL HG2 H 0.95 . 2 176 . 21 VAL C C 174.9 . 1 177 . 21 VAL CA C 66.0 . 1 178 . 21 VAL CB C 31.7 . 1 179 . 21 VAL N N 121.3 . 1 180 . 22 LEU H H 7.24 . 1 181 . 22 LEU HA H 3.91 . 1 182 . 22 LEU HB2 H 1.39 . 1 183 . 22 LEU HB3 H 1.39 . 1 184 . 22 LEU HD1 H 0.49 . 1 185 . 22 LEU HD2 H 0.49 . 1 186 . 22 LEU C C 173.6 . 1 187 . 22 LEU CA C 55.4 . 1 188 . 22 LEU CB C 41.5 . 1 189 . 22 LEU N N 117.5 . 1 190 . 23 GLY H H 7.69 . 1 191 . 23 GLY HA2 H 3.96 . 2 192 . 23 GLY HA3 H 3.58 . 2 193 . 23 GLY C C 172.0 . 1 194 . 23 GLY CA C 45.9 . 1 195 . 23 GLY N N 106.5 . 1 196 . 24 VAL H H 7.62 . 1 197 . 24 VAL HA H 3.72 . 1 198 . 24 VAL HB H 1.45 . 1 199 . 24 VAL HG1 H 0.83 . 1 200 . 24 VAL HG2 H 0.83 . 1 201 . 24 VAL C C 173.6 . 1 202 . 24 VAL CA C 63.3 . 1 203 . 24 VAL CB C 31.7 . 1 204 . 24 VAL N N 121.4 . 1 205 . 25 ASN H H 8.68 . 1 206 . 25 ASN HA H 4.38 . 1 207 . 25 ASN HB2 H 3.09 . 2 208 . 25 ASN HB3 H 2.74 . 2 209 . 25 ASN C C 172.8 . 1 210 . 25 ASN CA C 54.2 . 1 211 . 25 ASN CB C 39.3 . 1 212 . 25 ASN N N 127.9 . 1 213 . 26 VAL H H 8.47 . 1 214 . 26 VAL HA H 3.46 . 1 215 . 26 VAL HB H 2.03 . 1 216 . 26 VAL HG1 H 0.96 . 2 217 . 26 VAL HG2 H 0.91 . 2 218 . 26 VAL C C 173.4 . 1 219 . 26 VAL CA C 66.7 . 1 220 . 26 VAL CB C 32.1 . 1 221 . 26 VAL N N 120.3 . 1 222 . 27 MET H H 7.95 . 1 223 . 27 MET HA H 4.14 . 1 224 . 27 MET HB2 H 2.07 . 2 225 . 27 MET HB3 H 2.01 . 2 226 . 27 MET HG2 H 2.59 . 2 227 . 27 MET HG3 H 2.46 . 2 228 . 27 MET CA C 58.5 . 1 229 . 27 MET CB C 32.0 . 1 230 . 27 MET N N 119.7 . 1 231 . 28 LEU H H 7.82 . 1 232 . 28 LEU HA H 4.08 . 1 233 . 28 LEU HB2 H 1.63 . 2 234 . 28 LEU HB3 H 1.32 . 2 235 . 28 LEU HG H 1.09 . 1 236 . 28 LEU HD1 H 0.82 . 2 237 . 28 LEU HD2 H 0.76 . 2 238 . 28 LEU N N 118.6 . 1 239 . 29 ARG HA H 4.32 . 1 240 . 29 ARG HB2 H 2.20 . 2 241 . 29 ARG HB3 H 1.97 . 2 242 . 29 ARG HG2 H 1.74 . 1 243 . 29 ARG HG3 H 1.74 . 1 244 . 29 ARG HD2 H 2.70 . 1 245 . 29 ARG HD3 H 2.70 . 1 246 . 30 LYS H H 7.66 . 1 247 . 30 LYS HA H 3.87 . 1 248 . 30 LYS HB2 H 1.89 . 2 249 . 30 LYS HB3 H 1.81 . 2 250 . 30 LYS HG2 H 1.68 . 2 251 . 30 LYS HG3 H 1.59 . 2 252 . 30 LYS C C 177.7 . 1 253 . 30 LYS CA C 59.6 . 1 254 . 30 LYS CB C 32.2 . 1 255 . 30 LYS N N 116.5 . 1 256 . 31 ILE H H 7.16 . 1 257 . 31 ILE HA H 3.72 . 1 258 . 31 ILE HB H 1.80 . 1 259 . 31 ILE HG2 H 0.88 . 1 260 . 31 ILE HD1 H 0.80 . 1 261 . 31 ILE CA C 64.3 . 1 262 . 31 ILE CB C 39.2 . 1 263 . 31 ILE N N 119.2 . 1 264 . 33 VAL H H 8.66 . 1 265 . 33 VAL HA H 3.62 . 1 266 . 33 VAL HB H 2.07 . 1 267 . 33 VAL HG1 H 0.94 . 1 268 . 33 VAL HG2 H 0.94 . 1 269 . 33 VAL CA C 66.6 . 1 270 . 33 VAL N N 116.7 . 1 271 . 34 ALA HA H 4.08 . 1 272 . 34 ALA HB H 1.38 . 1 273 . 35 ALA HA H 4.21 . 1 274 . 35 ALA HB H 1.38 . 1 275 . 36 ALA C C 174.8 . 1 276 . 36 ALA CA C 52.2 . 1 277 . 36 ALA CB C 19.1 . 1 278 . 37 SER H H 7.43 . 1 279 . 37 SER HA H 4.70 . 1 280 . 37 SER HB2 H 4.23 . 2 281 . 37 SER HB3 H 4.02 . 2 282 . 37 SER CA C 60.4 . 1 283 . 37 SER N N 113.9 . 1 284 . 40 ALA H H 8.71 . 1 285 . 40 ALA HA H 4.96 . 1 286 . 40 ALA HB H 1.45 . 1 287 . 40 ALA C C 174.4 . 1 288 . 40 ALA CA C 51.9 . 1 289 . 40 ALA CB C 20.9 . 1 290 . 40 ALA N N 123.9 . 1 291 . 41 VAL H H 7.93 . 1 292 . 41 VAL HA H 5.13 . 1 293 . 41 VAL HB H 1.73 . 1 294 . 41 VAL HG1 H 0.63 . 2 295 . 41 VAL HG2 H 0.46 . 2 296 . 41 VAL C C 171.5 . 1 297 . 41 VAL CA C 61.2 . 1 298 . 41 VAL CB C 35.3 . 1 299 . 41 VAL N N 125.2 . 1 300 . 42 GLU H H 9.30 . 1 301 . 42 GLU HA H 5.36 . 1 302 . 42 GLU HB2 H 2.06 . 2 303 . 42 GLU HB3 H 1.99 . 2 304 . 42 GLU HG2 H 2.25 . 1 305 . 42 GLU HG3 H 2.25 . 1 306 . 42 GLU C C 172.1 . 1 307 . 42 GLU CA C 54.6 . 1 308 . 42 GLU CB C 33.4 . 1 309 . 42 GLU N N 130.0 . 1 310 . 43 ILE H H 9.30 . 1 311 . 43 ILE HA H 5.34 . 1 312 . 43 ILE HB H 2.27 . 1 313 . 43 ILE HG12 H 1.66 . 1 314 . 43 ILE HG13 H 1.66 . 1 315 . 43 ILE HG2 H 0.85 . 1 316 . 43 ILE HD1 H 0.51 . 1 317 . 43 ILE C C 173.9 . 1 318 . 43 ILE CA C 60.0 . 1 319 . 43 ILE CB C 40.8 . 1 320 . 43 ILE N N 123.1 . 1 321 . 44 LYS H H 9.56 . 1 322 . 44 LYS HA H 4.60 . 1 323 . 44 LYS HB2 H 1.87 . 2 324 . 44 LYS HB3 H 1.76 . 2 325 . 44 LYS HG2 H 1.54 . 2 326 . 44 LYS HG3 H 1.41 . 2 327 . 44 LYS HD2 H 1.33 . 2 328 . 44 LYS HD3 H 1.24 . 2 329 . 44 LYS C C 170.8 . 1 330 . 44 LYS CA C 56.4 . 1 331 . 44 LYS CB C 35.3 . 1 332 . 44 LYS N N 128.9 . 1 333 . 45 GLN H H 8.58 . 1 334 . 45 GLN HA H 4.45 . 1 335 . 45 GLN HB2 H 1.82 . 2 336 . 45 GLN HB3 H 1.71 . 2 337 . 45 GLN HG2 H 2.03 . 1 338 . 45 GLN HG3 H 2.03 . 1 339 . 45 GLN C C 172.2 . 1 340 . 45 GLN CA C 53.9 . 1 341 . 45 GLN CB C 30.6 . 1 342 . 45 GLN N N 128.0 . 1 343 . 46 GLU H H 8.53 . 1 344 . 46 GLU HA H 4.37 . 1 345 . 46 GLU HB2 H 1.62 . 2 346 . 46 GLU HB3 H 1.26 . 2 347 . 46 GLU HG2 H 2.02 . 1 348 . 46 GLU HG3 H 2.02 . 1 349 . 46 GLU C C 173.5 . 1 350 . 46 GLU CA C 55.1 . 1 351 . 46 GLU CB C 31.0 . 1 352 . 46 GLU N N 128.9 . 1 353 . 47 GLY H H 9.10 . 1 354 . 47 GLY HA2 H 3.94 . 2 355 . 47 GLY HA3 H 3.58 . 2 356 . 47 GLY C C 170.6 . 1 357 . 47 GLY CA C 48.0 . 1 358 . 47 GLY N N 117.9 . 1 359 . 48 ASP H H 8.54 . 1 360 . 48 ASP HA H 5.18 . 1 361 . 48 ASP HB2 H 3.15 . 2 362 . 48 ASP HB3 H 2.68 . 2 363 . 48 ASP C C 172.5 . 1 364 . 48 ASP CA C 54.5 . 1 365 . 48 ASP CB C 42.1 . 1 366 . 48 ASP N N 126.6 . 1 367 . 49 THR H H 8.08 . 1 368 . 49 THR HA H 4.70 . 1 369 . 49 THR HB H 4.14 . 1 370 . 49 THR HG2 H 0.99 . 1 371 . 49 THR C C 170.1 . 1 372 . 49 THR CA C 63.0 . 1 373 . 49 THR CB C 69.6 . 1 374 . 49 THR N N 116.7 . 1 375 . 50 PHE H H 9.08 . 1 376 . 50 PHE HA H 4.56 . 1 377 . 50 PHE HB2 H 1.65 . 1 378 . 50 PHE HB3 H 1.65 . 1 379 . 50 PHE C C 173.1 . 1 380 . 50 PHE CA C 57.6 . 1 381 . 50 PHE CB C 44.6 . 1 382 . 50 PHE N N 124.2 . 1 383 . 51 TYR H H 8.35 . 1 384 . 51 TYR HA H 5.24 . 1 385 . 51 TYR HB2 H 3.01 . 2 386 . 51 TYR HB3 H 2.70 . 2 387 . 51 TYR C C 172.8 . 1 388 . 51 TYR CA C 56.3 . 1 389 . 51 TYR CB C 41.0 . 1 390 . 51 TYR N N 122.5 . 1 391 . 52 ILE H H 8.41 . 1 392 . 52 ILE HA H 4.60 . 1 393 . 52 ILE HB H 1.84 . 1 394 . 52 ILE HG12 H 1.26 . 1 395 . 52 ILE HG13 H 1.26 . 1 396 . 52 ILE HG2 H 0.80 . 1 397 . 52 ILE HD1 H 0.31 . 1 398 . 52 ILE C C 171.6 . 1 399 . 52 ILE CA C 61.0 . 1 400 . 52 ILE CB C 40.4 . 1 401 . 52 ILE N N 123.3 . 1 402 . 53 LYS H H 9.30 . 1 403 . 53 LYS HA H 5.08 . 1 404 . 53 LYS HB2 H 1.76 . 2 405 . 53 LYS HB3 H 1.58 . 2 406 . 53 LYS HG2 H 1.17 . 1 407 . 53 LYS HG3 H 1.17 . 1 408 . 53 LYS HD2 H 0.44 . 2 409 . 53 LYS HD3 H 0.29 . 2 410 . 53 LYS HE2 H 2.84 . 1 411 . 53 LYS HE3 H 2.84 . 1 412 . 53 LYS C C 172.0 . 1 413 . 53 LYS CA C 54.5 . 1 414 . 53 LYS CB C 34.9 . 1 415 . 53 LYS N N 133.1 . 1 416 . 54 THR H H 8.85 . 1 417 . 54 THR HA H 4.88 . 1 418 . 54 THR HB H 3.86 . 1 419 . 54 THR HG2 H 0.94 . 1 420 . 54 THR CA C 62.1 . 1 421 . 54 THR CB C 70.0 . 1 422 . 54 THR N N 124.4 . 1 423 . 55 SER H H 9.43 . 1 424 . 55 SER HA H 5.30 . 1 425 . 55 SER HB2 H 3.83 . 2 426 . 55 SER HB3 H 3.74 . 2 427 . 55 SER CA C 58.0 . 1 428 . 55 SER CB C 65.0 . 1 429 . 55 SER N N 122.7 . 1 430 . 56 THR H H 8.71 . 1 431 . 56 THR HA H 4.85 . 1 432 . 56 THR HB H 4.61 . 1 433 . 56 THR HG2 H 1.07 . 1 434 . 56 THR N N 124.0 . 1 435 . 57 THR HA H 4.00 . 1 436 . 57 THR HB H 4.23 . 1 437 . 57 THR HG2 H 1.27 . 1 438 . 57 THR C C 173.5 . 1 439 . 57 THR CA C 64.9 . 1 440 . 57 THR CB C 66.7 . 1 441 . 58 VAL HA H 4.16 . 1 442 . 58 VAL HB H 1.96 . 1 443 . 58 VAL HG1 H 0.79 . 2 444 . 58 VAL HG2 H 0.74 . 2 445 . 58 VAL CA C 62.2 . 1 446 . 60 THR H H 8.58 . 1 447 . 60 THR HA H 5.20 . 1 448 . 60 THR HB H 3.90 . 1 449 . 60 THR HG2 H 1.06 . 1 450 . 60 THR CA C 60.3 . 1 451 . 60 THR CB C 71.7 . 1 452 . 60 THR N N 123.5 . 1 453 . 61 THR HA H 4.61 . 1 454 . 61 THR HB H 3.97 . 1 455 . 61 THR HG2 H 1.06 . 1 456 . 61 THR CA C 60.1 . 1 457 . 61 THR CB C 71.7 . 1 458 . 62 GLU H H 8.73 . 1 459 . 62 GLU HA H 4.98 . 1 460 . 62 GLU HB2 H 2.02 . 2 461 . 62 GLU HB3 H 1.91 . 2 462 . 62 GLU N N 122.9 . 1 463 . 63 ILE HA H 4.88 . 1 464 . 63 ILE HB H 1.85 . 1 465 . 63 ILE HG12 H 1.16 . 2 466 . 63 ILE HG13 H 1.01 . 2 467 . 63 ILE HG2 H 1.09 . 1 468 . 63 ILE HD1 H 0.80 . 1 469 . 63 ILE C C 170.5 . 1 470 . 63 ILE CA C 59.5 . 1 471 . 63 ILE CB C 42.2 . 1 472 . 64 ASN H H 8.10 . 1 473 . 64 ASN HA H 5.56 . 1 474 . 64 ASN HB2 H 2.54 . 2 475 . 64 ASN HB3 H 2.50 . 2 476 . 64 ASN C C 169.7 . 1 477 . 64 ASN CA C 52.3 . 1 478 . 64 ASN CB C 42.8 . 1 479 . 64 ASN N N 120.4 . 1 480 . 65 PHE H H 8.34 . 1 481 . 65 PHE HA H 4.65 . 1 482 . 65 PHE HB2 H 2.15 . 1 483 . 65 PHE HB3 H 2.15 . 1 484 . 65 PHE C C 169.1 . 1 485 . 65 PHE CA C 55.9 . 1 486 . 65 PHE CB C 39.8 . 1 487 . 65 PHE N N 117.2 . 1 488 . 66 LYS H H 9.32 . 1 489 . 66 LYS HA H 4.65 . 1 490 . 66 LYS HB2 H 1.63 . 2 491 . 66 LYS HB3 H 1.49 . 2 492 . 66 LYS HG2 H 1.45 . 2 493 . 66 LYS HG3 H 1.28 . 2 494 . 66 LYS HE2 H 2.92 . 1 495 . 66 LYS HE3 H 2.92 . 1 496 . 66 LYS C C 175.2 . 1 497 . 66 LYS CA C 53.9 . 1 498 . 66 LYS CB C 35.4 . 1 499 . 66 LYS N N 120.8 . 1 500 . 67 VAL H H 9.01 . 1 501 . 67 VAL HA H 3.23 . 1 502 . 67 VAL HB H 1.85 . 1 503 . 67 VAL HG1 H 0.64 . 2 504 . 67 VAL HG2 H 0.43 . 2 505 . 67 VAL C C 174.1 . 1 506 . 67 VAL CA C 67.1 . 1 507 . 67 VAL CB C 31.9 . 1 508 . 67 VAL N N 127.5 . 1 509 . 68 GLY H H 8.91 . 1 510 . 68 GLY HA2 H 4.38 . 2 511 . 68 GLY HA3 H 3.61 . 2 512 . 68 GLY C C 170.7 . 1 513 . 68 GLY CA C 45.7 . 1 514 . 68 GLY N N 114.9 . 1 515 . 69 GLU H H 7.94 . 1 516 . 69 GLU HA H 4.77 . 1 517 . 69 GLU HB2 H 2.16 . 2 518 . 69 GLU HB3 H 1.96 . 2 519 . 69 GLU HG2 H 2.19 . 1 520 . 69 GLU HG3 H 2.19 . 1 521 . 69 GLU C C 171.5 . 1 522 . 69 GLU CA C 54.9 . 1 523 . 69 GLU CB C 35.3 . 1 524 . 69 GLU N N 120.2 . 1 525 . 70 GLU H H 9.21 . 1 526 . 70 GLU HA H 4.88 . 1 527 . 70 GLU HB2 H 1.99 . 2 528 . 70 GLU HB3 H 1.91 . 2 529 . 70 GLU HG2 H 2.20 . 2 530 . 70 GLU HG3 H 2.13 . 2 531 . 70 GLU C C 172.6 . 1 532 . 70 GLU CA C 57.6 . 1 533 . 70 GLU CB C 31.4 . 1 534 . 70 GLU N N 130.3 . 1 535 . 71 PHE H H 9.06 . 1 536 . 71 PHE HA H 5.11 . 1 537 . 71 PHE HB2 H 3.53 . 2 538 . 71 PHE HB3 H 3.20 . 2 539 . 71 PHE C C 169.5 . 1 540 . 71 PHE CA C 55.8 . 1 541 . 71 PHE CB C 41.4 . 1 542 . 71 PHE N N 121.4 . 1 543 . 72 GLU H H 8.67 . 1 544 . 72 GLU HA H 5.05 . 1 545 . 72 GLU HB2 H 2.02 . 2 546 . 72 GLU HB3 H 1.91 . 2 547 . 72 GLU HG2 H 2.30 . 2 548 . 72 GLU HG3 H 2.13 . 2 549 . 72 GLU C C 173.1 . 1 550 . 72 GLU CA C 55.3 . 1 551 . 72 GLU CB C 31.9 . 1 552 . 72 GLU N N 119.6 . 1 553 . 73 GLU H H 8.44 . 1 554 . 73 GLU HA H 4.73 . 1 555 . 73 GLU HB2 H 2.02 . 2 556 . 73 GLU HB3 H 1.90 . 2 557 . 73 GLU HG2 H 2.14 . 1 558 . 73 GLU HG3 H 2.14 . 1 559 . 73 GLU C C 171.6 . 1 560 . 73 GLU CA C 55.3 . 1 561 . 73 GLU CB C 29.7 . 1 562 . 73 GLU N N 122.4 . 1 563 . 74 GLN H H 7.59 . 1 564 . 74 GLN HA H 5.30 . 1 565 . 74 GLN HB2 H 1.73 . 2 566 . 74 GLN HB3 H 1.70 . 2 567 . 74 GLN HG2 H 2.17 . 2 568 . 74 GLN HG3 H 1.99 . 2 569 . 74 GLN C C 174.3 . 1 570 . 74 GLN CA C 54.2 . 1 571 . 74 GLN CB C 33.1 . 1 572 . 74 GLN N N 117.9 . 1 573 . 75 THR H H 9.18 . 1 574 . 75 THR HA H 4.55 . 1 575 . 75 THR HB H 4.16 . 1 576 . 75 THR HG2 H 1.03 . 1 577 . 75 THR C C 175.4 . 1 578 . 75 THR CA C 62.4 . 1 579 . 75 THR CB C 71.2 . 1 580 . 75 THR N N 111.8 . 1 581 . 76 VAL H H 9.18 . 1 582 . 76 VAL HA H 3.82 . 1 583 . 76 VAL HB H 2.00 . 1 584 . 76 VAL HG1 H 1.01 . 2 585 . 76 VAL HG2 H 0.81 . 2 586 . 76 VAL CA C 65.6 . 1 587 . 76 VAL CB C 32.1 . 1 588 . 76 VAL N N 122.4 . 1 589 . 78 GLY H H 7.93 . 1 590 . 78 GLY HA2 H 4.10 . 2 591 . 78 GLY HA3 H 3.55 . 2 592 . 78 GLY CA C 45.9 . 1 593 . 78 GLY N N 107.2 . 1 594 . 79 ARG H H 7.86 . 1 595 . 79 ARG C C 171.4 . 1 596 . 79 ARG CA C 54.0 . 1 597 . 79 ARG CB C 29.8 . 1 598 . 79 ARG N N 121.0 . 1 599 . 80 PRO HA H 4.66 . 1 600 . 80 PRO HB2 H 2.38 . 2 601 . 80 PRO HB3 H 1.86 . 2 602 . 80 PRO HG2 H 2.15 . 2 603 . 80 PRO HG3 H 1.99 . 2 604 . 80 PRO C C 173.6 . 1 605 . 80 PRO CA C 63.8 . 1 606 . 80 PRO CB C 33.0 . 1 607 . 81 CYS H H 8.87 . 1 608 . 81 CYS HA H 5.05 . 1 609 . 81 CYS HB2 H 2.58 . 1 610 . 81 CYS HB3 H 2.58 . 1 611 . 81 CYS C C 168.5 . 1 612 . 81 CYS CA C 55.9 . 1 613 . 81 CYS CB C 31.6 . 1 614 . 81 CYS N N 118.8 . 1 615 . 82 LYS H H 8.87 . 1 616 . 82 LYS HA H 4.73 . 1 617 . 82 LYS HB2 H 1.54 . 2 618 . 82 LYS HB3 H 1.47 . 2 619 . 82 LYS HG2 H 1.26 . 2 620 . 82 LYS HG3 H 1.22 . 2 621 . 82 LYS HD2 H 1.03 . 1 622 . 82 LYS HD3 H 1.03 . 1 623 . 82 LYS C C 173.0 . 1 624 . 82 LYS CA C 54.5 . 1 625 . 82 LYS CB C 34.3 . 1 626 . 82 LYS N N 120.0 . 1 627 . 83 SER H H 9.06 . 1 628 . 83 SER HA H 4.86 . 1 629 . 83 SER HB2 H 2.78 . 2 630 . 83 SER HB3 H 1.54 . 2 631 . 83 SER C C 168.7 . 1 632 . 83 SER CA C 58.7 . 1 633 . 83 SER CB C 68.0 . 1 634 . 83 SER N N 124.9 . 1 635 . 84 LEU H H 7.36 . 1 636 . 84 LEU HA H 4.23 . 1 637 . 84 LEU HB2 H 2.00 . 2 638 . 84 LEU HB3 H 1.58 . 2 639 . 84 LEU HG H 1.17 . 1 640 . 84 LEU HD1 H 0.68 . 2 641 . 84 LEU HD2 H 0.51 . 2 642 . 84 LEU C C 173.7 . 1 643 . 84 LEU CA C 54.9 . 1 644 . 84 LEU CB C 45.2 . 1 645 . 84 LEU N N 120.7 . 1 646 . 85 VAL H H 9.20 . 1 647 . 85 VAL HA H 4.35 . 1 648 . 85 VAL HB H 1.35 . 1 649 . 85 VAL HG1 H 0.23 . 2 650 . 85 VAL HG2 H 0.02 . 2 651 . 85 VAL C C 171.5 . 1 652 . 85 VAL CA C 60.6 . 1 653 . 85 VAL CB C 32.6 . 1 654 . 85 VAL N N 130.1 . 1 655 . 86 LYS H H 8.47 . 1 656 . 86 LYS HA H 4.48 . 1 657 . 86 LYS HB2 H 1.61 . 2 658 . 86 LYS HB3 H 1.43 . 2 659 . 86 LYS HG2 H 1.26 . 2 660 . 86 LYS HG3 H 1.12 . 2 661 . 86 LYS C C 173.3 . 1 662 . 86 LYS CA C 54.2 . 1 663 . 86 LYS CB C 36.9 . 1 664 . 86 LYS N N 123.8 . 1 665 . 87 TRP H H 8.65 . 1 666 . 87 TRP HA H 5.11 . 1 667 . 87 TRP HB2 H 3.22 . 2 668 . 87 TRP HB3 H 2.99 . 2 669 . 87 TRP C C 174.9 . 1 670 . 87 TRP CA C 57.0 . 1 671 . 87 TRP CB C 29.5 . 1 672 . 87 TRP N N 120.2 . 1 673 . 88 GLU H H 9.21 . 1 674 . 88 GLU HA H 4.35 . 1 675 . 88 GLU HB2 H 1.80 . 2 676 . 88 GLU HB3 H 1.66 . 2 677 . 88 GLU HG2 H 1.99 . 1 678 . 88 GLU HG3 H 1.99 . 1 679 . 88 GLU C C 173.3 . 1 680 . 88 GLU CA C 58.0 . 1 681 . 88 GLU CB C 32.3 . 1 682 . 88 GLU N N 127.7 . 1 683 . 89 SER H H 8.59 . 1 684 . 89 SER HA H 4.55 . 1 685 . 89 SER HB2 H 4.11 . 2 686 . 89 SER HB3 H 3.98 . 2 687 . 89 SER C C 171.2 . 1 688 . 89 SER CA C 57.0 . 1 689 . 89 SER CB C 65.0 . 1 690 . 89 SER N N 112.5 . 1 691 . 90 GLU H H 8.71 . 1 692 . 90 GLU HA H 3.66 . 1 693 . 90 GLU HB2 H 1.84 . 2 694 . 90 GLU HB3 H 1.78 . 2 695 . 90 GLU HG2 H 2.08 . 1 696 . 90 GLU HG3 H 2.08 . 1 697 . 90 GLU C C 173.1 . 1 698 . 90 GLU CA C 59.1 . 1 699 . 90 GLU CB C 29.5 . 1 700 . 90 GLU N N 116.7 . 1 701 . 91 ASN H H 8.05 . 1 702 . 91 ASN HA H 4.96 . 1 703 . 91 ASN HB2 H 3.15 . 2 704 . 91 ASN HB3 H 2.85 . 2 705 . 91 ASN C C 171.3 . 1 706 . 91 ASN CA C 52.9 . 1 707 . 91 ASN CB C 40.4 . 1 708 . 91 ASN N N 111.2 . 1 709 . 92 LYS H H 7.84 . 1 710 . 92 LYS HA H 5.46 . 1 711 . 92 LYS HB2 H 1.98 . 2 712 . 92 LYS HB3 H 1.47 . 2 713 . 92 LYS HG2 H 1.22 . 1 714 . 92 LYS HG3 H 1.22 . 1 715 . 92 LYS HD2 H 1.10 . 1 716 . 92 LYS HD3 H 1.10 . 1 717 . 92 LYS HE2 H 2.68 . 1 718 . 92 LYS HE3 H 2.68 . 1 719 . 92 LYS C C 171.0 . 1 720 . 92 LYS CA C 56.7 . 1 721 . 92 LYS CB C 37.2 . 1 722 . 92 LYS N N 120.1 . 1 723 . 93 MET H H 9.35 . 1 724 . 93 MET HA H 5.18 . 1 725 . 93 MET HB2 H 1.99 . 1 726 . 93 MET HB3 H 1.99 . 1 727 . 93 MET HG2 H 2.19 . 2 728 . 93 MET HG3 H 2.08 . 2 729 . 93 MET HE H 0.41 . 1 730 . 93 MET C C 171.0 . 1 731 . 93 MET CA C 53.4 . 1 732 . 93 MET CB C 35.1 . 1 733 . 93 MET N N 127.0 . 1 734 . 94 VAL H H 8.86 . 1 735 . 94 VAL HA H 4.30 . 1 736 . 94 VAL HB H 1.77 . 1 737 . 94 VAL HG1 H 0.73 . 2 738 . 94 VAL HG2 H 0.70 . 2 739 . 94 VAL C C 170.0 . 1 740 . 94 VAL CA C 60.3 . 1 741 . 94 VAL CB C 34.9 . 1 742 . 94 VAL N N 119.3 . 1 743 . 95 CYS H H 8.85 . 1 744 . 95 CYS HA H 4.48 . 1 745 . 95 CYS HB2 H 0.36 . 2 746 . 95 CYS HB3 H -0.28 . 2 747 . 95 CYS C C 171.4 . 1 748 . 95 CYS CA C 55.6 . 1 749 . 95 CYS CB C 27.9 . 1 750 . 95 CYS N N 127.3 . 1 751 . 96 GLU H H 7.70 . 1 752 . 96 GLU HA H 4.31 . 1 753 . 96 GLU HB2 H 1.81 . 2 754 . 96 GLU HB3 H 1.73 . 2 755 . 96 GLU HG2 H 2.14 . 2 756 . 96 GLU HG3 H 1.95 . 2 757 . 96 GLU C C 172.6 . 1 758 . 96 GLU CA C 55.2 . 1 759 . 96 GLU CB C 31.6 . 1 760 . 96 GLU N N 127.7 . 1 761 . 97 GLN H H 7.43 . 1 762 . 97 GLN HA H 4.91 . 1 763 . 97 GLN HB2 H 1.75 . 1 764 . 97 GLN HB3 H 1.75 . 1 765 . 97 GLN HG2 H 2.43 . 2 766 . 97 GLN HG3 H 2.02 . 2 767 . 97 GLN C C 173.1 . 1 768 . 97 GLN CA C 54.7 . 1 769 . 97 GLN CB C 30.8 . 1 770 . 97 GLN N N 121.0 . 1 771 . 98 LYS H H 8.94 . 1 772 . 98 LYS HA H 4.60 . 1 773 . 98 LYS HB2 H 2.10 . 1 774 . 98 LYS HB3 H 2.10 . 1 775 . 98 LYS HG2 H 1.96 . 2 776 . 98 LYS HG3 H 1.78 . 2 777 . 98 LYS HD2 H 1.24 . 1 778 . 98 LYS HD3 H 1.24 . 1 779 . 98 LYS HE2 H 3.16 . 2 780 . 98 LYS HE3 H 2.84 . 2 781 . 98 LYS C C 172.9 . 1 782 . 98 LYS CA C 54.7 . 1 783 . 98 LYS CB C 35.0 . 1 784 . 98 LYS N N 123.1 . 1 785 . 99 LEU H H 8.78 . 1 786 . 99 LEU HA H 4.00 . 1 787 . 99 LEU HB2 H 1.98 . 2 788 . 99 LEU HB3 H 1.63 . 2 789 . 99 LEU HG H 1.36 . 1 790 . 99 LEU HD1 H 0.86 . 2 791 . 99 LEU HD2 H 0.65 . 2 792 . 99 LEU C C 175.4 . 1 793 . 99 LEU CA C 56.0 . 1 794 . 99 LEU CB C 42.0 . 1 795 . 99 LEU N N 126.1 . 1 796 . 100 LEU H H 7.77 . 1 797 . 100 LEU HA H 4.07 . 1 798 . 100 LEU HB2 H 1.64 . 2 799 . 100 LEU HB3 H 1.47 . 2 800 . 100 LEU HG H 1.35 . 1 801 . 100 LEU HD1 H 0.80 . 2 802 . 100 LEU HD2 H 0.76 . 2 803 . 100 LEU C C 174.8 . 1 804 . 100 LEU CA C 57.0 . 1 805 . 100 LEU CB C 42.5 . 1 806 . 100 LEU N N 121.9 . 1 807 . 101 LYS H H 8.05 . 1 808 . 101 LYS HA H 4.37 . 1 809 . 101 LYS HB2 H 1.72 . 2 810 . 101 LYS HB3 H 1.61 . 2 811 . 101 LYS HG2 H 1.37 . 2 812 . 101 LYS HG3 H 1.27 . 2 813 . 101 LYS C C 172.7 . 1 814 . 101 LYS CA C 55.4 . 1 815 . 101 LYS CB C 34.9 . 1 816 . 101 LYS N N 117.4 . 1 817 . 102 GLY H H 8.18 . 1 818 . 102 GLY HA2 H 4.02 . 2 819 . 102 GLY HA3 H 3.71 . 2 820 . 102 GLY C C 169.7 . 1 821 . 102 GLY CA C 45.1 . 1 822 . 102 GLY N N 108.6 . 1 823 . 103 GLU H H 8.10 . 1 824 . 103 GLU C C 173.1 . 1 825 . 103 GLU N N 117.2 . 1 826 . 104 GLY H H 8.14 . 1 827 . 104 GLY HA2 H 4.10 . 2 828 . 104 GLY HA3 H 3.90 . 2 829 . 104 GLY CA C 45.5 . 1 830 . 104 GLY N N 109.1 . 1 831 . 105 PRO HA H 4.48 . 1 832 . 105 PRO HB2 H 2.03 . 2 833 . 105 PRO HB3 H 1.33 . 2 834 . 105 PRO HG2 H 1.84 . 2 835 . 105 PRO HG3 H 1.76 . 2 836 . 105 PRO HD2 H 3.60 . 2 837 . 105 PRO HD3 H 3.29 . 2 838 . 105 PRO C C 172.8 . 1 839 . 105 PRO CA C 62.7 . 1 840 . 105 PRO CB C 32.7 . 1 841 . 106 LYS H H 8.58 . 1 842 . 106 LYS HA H 4.38 . 1 843 . 106 LYS HB2 H 1.81 . 2 844 . 106 LYS HB3 H 1.51 . 2 845 . 106 LYS HG2 H 1.35 . 2 846 . 106 LYS HG3 H 1.30 . 2 847 . 106 LYS C C 175.1 . 1 848 . 106 LYS CA C 56.6 . 1 849 . 106 LYS CB C 32.6 . 1 850 . 106 LYS N N 123.5 . 1 851 . 107 THR H H 8.79 . 1 852 . 107 THR HA H 5.36 . 1 853 . 107 THR HB H 4.46 . 1 854 . 107 THR HG2 H 1.13 . 1 855 . 107 THR C C 170.8 . 1 856 . 107 THR CA C 60.1 . 1 857 . 107 THR CB C 72.5 . 1 858 . 107 THR N N 118.7 . 1 859 . 108 SER H H 7.80 . 1 860 . 108 SER HA H 4.63 . 1 861 . 108 SER HB2 H 3.86 . 2 862 . 108 SER HB3 H 3.78 . 2 863 . 108 SER C C 171.2 . 1 864 . 108 SER CA C 57.3 . 1 865 . 108 SER CB C 66.8 . 1 866 . 108 SER N N 112.3 . 1 867 . 109 TRP H H 8.21 . 1 868 . 109 TRP HA H 5.76 . 1 869 . 109 TRP HB2 H 3.48 . 2 870 . 109 TRP HB3 H 3.29 . 2 871 . 109 TRP C C 171.8 . 1 872 . 109 TRP CA C 56.1 . 1 873 . 109 TRP CB C 33.1 . 1 874 . 109 TRP N N 116.3 . 1 875 . 110 THR H H 9.56 . 1 876 . 110 THR HA H 5.24 . 1 877 . 110 THR HB H 4.16 . 1 878 . 110 THR HG2 H 1.09 . 1 879 . 110 THR C C 171.7 . 1 880 . 110 THR CA C 61.0 . 1 881 . 110 THR CB C 72.2 . 1 882 . 110 THR N N 111.2 . 1 883 . 111 ARG H H 8.79 . 1 884 . 111 ARG HA H 5.57 . 1 885 . 111 ARG HB2 H 1.85 . 2 886 . 111 ARG HB3 H 1.50 . 2 887 . 111 ARG HG2 H 1.35 . 2 888 . 111 ARG HG3 H 1.23 . 2 889 . 111 ARG HD2 H 3.00 . 1 890 . 111 ARG HD3 H 3.00 . 1 891 . 111 ARG C C 170.9 . 1 892 . 111 ARG CA C 56.1 . 1 893 . 111 ARG CB C 33.1 . 1 894 . 111 ARG N N 120.1 . 1 895 . 112 GLU H H 8.87 . 1 896 . 112 GLU HA H 5.78 . 1 897 . 112 GLU HB2 H 1.94 . 1 898 . 112 GLU HB3 H 1.94 . 1 899 . 112 GLU HG2 H 2.03 . 1 900 . 112 GLU HG3 H 2.03 . 1 901 . 112 GLU C C 170.5 . 1 902 . 112 GLU CA C 53.9 . 1 903 . 112 GLU CB C 34.9 . 1 904 . 112 GLU N N 123.3 . 1 905 . 113 LEU H H 8.25 . 1 906 . 113 LEU HA H 5.28 . 1 907 . 113 LEU HB2 H 1.25 . 1 908 . 113 LEU HB3 H 1.25 . 1 909 . 113 LEU HG H 0.94 . 1 910 . 113 LEU HD1 H 0.51 . 2 911 . 113 LEU HD2 H 0.44 . 2 912 . 113 LEU C C 175.1 . 1 913 . 113 LEU CA C 52.8 . 1 914 . 113 LEU CB C 43.9 . 1 915 . 113 LEU N N 126.4 . 1 916 . 114 THR H H 9.35 . 1 917 . 114 THR HA H 4.76 . 1 918 . 114 THR HB H 4.70 . 1 919 . 114 THR HG2 H 1.25 . 1 920 . 114 THR N N 116.9 . 1 921 . 115 ASN HA H 4.44 . 1 922 . 115 ASN HB2 H 2.79 . 2 923 . 115 ASN HB3 H 2.76 . 2 924 . 115 ASN C C 173.1 . 1 925 . 115 ASN CA C 55.5 . 1 926 . 115 ASN CB C 38.1 . 1 927 . 116 ASP H H 7.75 . 1 928 . 116 ASP HA H 4.74 . 1 929 . 116 ASP HB2 H 2.79 . 2 930 . 116 ASP HB3 H 2.39 . 2 931 . 116 ASP C C 173.5 . 1 932 . 116 ASP CA C 54.3 . 1 933 . 116 ASP CB C 41.2 . 1 934 . 116 ASP N N 115.7 . 1 935 . 117 GLY H H 7.96 . 1 936 . 117 GLY HA2 H 4.17 . 2 937 . 117 GLY HA3 H 3.69 . 2 938 . 117 GLY C C 171.7 . 1 939 . 117 GLY CA C 46.1 . 1 940 . 117 GLY N N 107.6 . 1 941 . 118 GLU H H 7.43 . 1 942 . 118 GLU HA H 4.98 . 1 943 . 118 GLU HB2 H 2.02 . 2 944 . 118 GLU HB3 H 1.98 . 2 945 . 118 GLU C C 172.0 . 1 946 . 118 GLU N N 117.5 . 1 947 . 119 LEU H H 8.73 . 1 948 . 119 LEU HA H 5.08 . 1 949 . 119 LEU HB2 H 0.89 . 1 950 . 119 LEU HB3 H 0.89 . 1 951 . 119 LEU HG H 0.44 . 1 952 . 119 LEU HD1 H 0.18 . 2 953 . 119 LEU HD2 H -0.36 . 2 954 . 119 LEU C C 172.6 . 1 955 . 119 LEU CA C 53.4 . 1 956 . 119 LEU CB C 43.3 . 1 957 . 119 LEU N N 124.6 . 1 958 . 120 ILE H H 9.47 . 1 959 . 120 ILE HA H 4.83 . 1 960 . 120 ILE HB H 1.77 . 1 961 . 120 ILE HG12 H 1.35 . 1 962 . 120 ILE HG13 H 1.35 . 1 963 . 120 ILE HG2 H 0.75 . 1 964 . 120 ILE HD1 H 0.99 . 1 965 . 120 ILE CA C 60.8 . 1 966 . 120 ILE CB C 39.4 . 1 967 . 120 ILE N N 125.2 . 1 968 . 121 LEU H H 9.88 . 1 969 . 121 LEU HA H 5.56 . 1 970 . 121 LEU HB2 H 2.15 . 1 971 . 121 LEU HB3 H 2.15 . 1 972 . 121 LEU HG H 1.22 . 1 973 . 121 LEU HD1 H 0.85 . 2 974 . 121 LEU HD2 H 0.74 . 2 975 . 121 LEU C C 172.8 . 1 976 . 121 LEU CA C 53.3 . 1 977 . 121 LEU CB C 45.3 . 1 978 . 121 LEU N N 135.5 . 1 979 . 122 THR H H 9.13 . 1 980 . 122 THR HA H 5.76 . 1 981 . 122 THR HB H 4.03 . 1 982 . 122 THR HG2 H 1.06 . 1 983 . 122 THR C C 171.4 . 1 984 . 122 THR CA C 60.4 . 1 985 . 122 THR CB C 71.0 . 1 986 . 122 THR N N 120.1 . 1 987 . 123 MET H H 9.29 . 1 988 . 123 MET HA H 5.14 . 1 989 . 123 MET HB2 H 1.84 . 2 990 . 123 MET HB3 H 1.81 . 2 991 . 123 MET HG2 H 2.55 . 2 992 . 123 MET HG3 H 2.28 . 2 993 . 123 MET C C 171.5 . 1 994 . 123 MET CA C 55.1 . 1 995 . 123 MET CB C 38.3 . 1 996 . 123 MET N N 121.7 . 1 997 . 124 THR H H 8.26 . 1 998 . 124 THR HA H 5.46 . 1 999 . 124 THR HB H 3.93 . 1 1000 . 124 THR HG2 H 0.96 . 1 1001 . 124 THR C C 172.1 . 1 1002 . 124 THR CA C 60.7 . 1 1003 . 124 THR CB C 71.2 . 1 1004 . 124 THR N N 115.2 . 1 1005 . 125 ALA H H 8.39 . 1 1006 . 125 ALA HA H 4.84 . 1 1007 . 125 ALA HB H 1.03 . 1 1008 . 125 ALA C C 172.7 . 1 1009 . 125 ALA CA C 51.6 . 1 1010 . 125 ALA CB C 21.3 . 1 1011 . 125 ALA N N 125.3 . 1 1012 . 126 ASP H H 9.28 . 1 1013 . 126 ASP HA H 4.14 . 1 1014 . 126 ASP HB2 H 2.72 . 1 1015 . 126 ASP HB3 H 2.72 . 1 1016 . 126 ASP C C 172.7 . 1 1017 . 126 ASP CA C 57.3 . 1 1018 . 126 ASP CB C 39.6 . 1 1019 . 126 ASP N N 122.4 . 1 1020 . 127 ASP H H 8.48 . 1 1021 . 127 ASP HA H 4.50 . 1 1022 . 127 ASP HB2 H 2.66 . 1 1023 . 127 ASP HB3 H 2.66 . 1 1024 . 127 ASP C C 172.8 . 1 1025 . 127 ASP CA C 54.7 . 1 1026 . 127 ASP CB C 41.4 . 1 1027 . 127 ASP N N 121.1 . 1 1028 . 128 VAL H H 8.41 . 1 1029 . 128 VAL HA H 3.95 . 1 1030 . 128 VAL HB H 2.14 . 1 1031 . 128 VAL HG1 H 0.92 . 2 1032 . 128 VAL HG2 H 0.69 . 2 1033 . 128 VAL C C 171.2 . 1 1034 . 128 VAL CA C 63.6 . 1 1035 . 128 VAL CB C 32.9 . 1 1036 . 128 VAL N N 123.4 . 1 1037 . 129 VAL H H 8.38 . 1 1038 . 129 VAL HA H 4.50 . 1 1039 . 129 VAL HB H 1.83 . 1 1040 . 129 VAL HG1 H 0.77 . 2 1041 . 129 VAL HG2 H 0.69 . 2 1042 . 129 VAL C C 172.9 . 1 1043 . 129 VAL CA C 61.4 . 1 1044 . 129 VAL CB C 34.4 . 1 1045 . 129 VAL N N 125.7 . 1 1046 . 130 CYS H H 9.56 . 1 1047 . 130 CYS HA H 5.16 . 1 1048 . 130 CYS HB2 H 3.00 . 2 1049 . 130 CYS HB3 H 2.66 . 2 1050 . 130 CYS CA C 56.4 . 1 1051 . 130 CYS CB C 35.4 . 1 1052 . 130 CYS N N 129.4 . 1 1053 . 131 THR H H 8.11 . 1 1054 . 131 THR HA H 5.13 . 1 1055 . 131 THR HB H 3.74 . 1 1056 . 131 THR HG2 H 0.98 . 1 1057 . 131 THR N N 124.6 . 1 1058 . 132 ARG H H 9.77 . 1 1059 . 132 ARG HA H 5.01 . 1 1060 . 132 ARG HB2 H 1.78 . 2 1061 . 132 ARG HB3 H 1.67 . 2 1062 . 132 ARG HG2 H 1.50 . 1 1063 . 132 ARG HG3 H 1.50 . 1 1064 . 132 ARG N N 128.3 . 1 1065 . 133 VAL H H 8.62 . 1 1066 . 133 VAL HA H 4.90 . 1 1067 . 133 VAL HB H 1.66 . 1 1068 . 133 VAL HG1 H 0.85 . 2 1069 . 133 VAL HG2 H 0.80 . 2 1070 . 133 VAL C C 171.2 . 1 1071 . 133 VAL CA C 62.2 . 1 1072 . 133 VAL N N 122.8 . 1 1073 . 134 TYR H H 9.79 . 1 1074 . 134 TYR HA H 5.59 . 1 1075 . 134 TYR HB2 H 3.23 . 2 1076 . 134 TYR HB3 H 3.01 . 2 1077 . 134 TYR C C 172.5 . 1 1078 . 134 TYR CA C 56.5 . 1 1079 . 134 TYR CB C 43.6 . 1 1080 . 134 TYR N N 127.2 . 1 1081 . 135 VAL H H 9.55 . 1 1082 . 135 VAL HA H 5.33 . 1 1083 . 135 VAL HB H 2.36 . 1 1084 . 135 VAL HG1 H 1.04 . 2 1085 . 135 VAL HG2 H 0.85 . 2 1086 . 135 VAL C C 172.8 . 1 1087 . 135 VAL CA C 59.7 . 1 1088 . 135 VAL CB C 36.2 . 1 1089 . 135 VAL N N 112.1 . 1 1090 . 136 ARG H H 8.55 . 1 1091 . 136 ARG HA H 3.89 . 1 1092 . 136 ARG HB2 H 1.29 . 2 1093 . 136 ARG HB3 H 1.11 . 2 1094 . 136 ARG HG2 H 0.59 . 2 1095 . 136 ARG HG3 H 0.06 . 2 1096 . 136 ARG HD2 H 2.70 . 2 1097 . 136 ARG HD3 H 2.79 . 2 1098 . 136 ARG C C 174.5 . 1 1099 . 136 ARG CA C 57.3 . 1 1100 . 136 ARG CB C 30.3 . 1 1101 . 136 ARG N N 123.2 . 1 1102 . 137 GLU H H 8.08 . 1 1103 . 137 GLU HA H 3.86 . 1 1104 . 137 GLU HB2 H 1.80 . 2 1105 . 137 GLU HB3 H 1.68 . 2 1106 . 137 GLU HG2 H 2.05 . 2 1107 . 137 GLU HG3 H 1.90 . 2 1108 . 137 GLU C C 178.7 . 1 1109 . 137 GLU CA C 58.9 . 1 1110 . 137 GLU CB C 31.6 . 1 1111 . 137 GLU N N 125.6 . 1 stop_ save_