data_4915 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure and Function of the C-terminal PABC Domain of Human Poly(A)-binding Protein ; _BMRB_accession_number 4915 _BMRB_flat_file_name bmr4915.str _Entry_type original _Submission_date 2000-12-09 _Accession_date 2000-12-12 _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 Kozlov G. . . 2 Trempe J.-F. . . 3 Khaleghpour K. . . 4 Kahvejian A. . . 5 Ekiel I. . . 6 Gehring K. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 655 "13C chemical shifts" 504 "15N chemical shifts" 126 "coupling constants" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-03-07 original author . stop_ _Original_release_date 2001-03-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure and Function of the C-terminal PABC Domain of Human Poly(A)-binding Protein ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21192642 _PubMed_ID 11287632 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kozlov G. . . 2 Trempe J.-F. . . 3 Khaleghpour K. . . 4 Kahvejian A. . . 5 Ekiel I. . . 6 Gehring K. . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 98 _Journal_issue 8 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4409 _Page_last 4413 _Year 2001 _Details . loop_ _Keyword 'all-helical domain' 'peptide-binding domain' stop_ save_ ################################## # Molecular system description # ################################## save_system_PABP _Saveframe_category molecular_system _Mol_system_name 'Polyadenylate-binding protein 1' _Abbreviation_common PABP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Polyadenylate-binding protein 1' $PABC stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PABC _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'C-terminal domain of PABP' _Abbreviation_common PABC _Molecular_mass 15271 _Mol_thiol_state 'not present' _Details 'The first five residues GPLGS are cloning artifacts.' ############################## # Polymer residue sequence # ############################## _Residue_count 144 _Mol_residue_sequence ; GPLGSAAAATPAVRTVPQYK YAAGVRNPQQHLNAQPQVTM QQPAVHVQGQEPLTASMLAS APPQEQKQMLGERLFPLIQA MHPTLAGKITGMLLEIDNSE LLHMLESPESLRSKVDEAVA VLQAHQAKEAAQKAVNSATG VPTV ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PRO 3 LEU 4 GLY 5 SER 6 ALA 7 ALA 8 ALA 9 ALA 10 THR 11 PRO 12 ALA 13 VAL 14 ARG 15 THR 16 VAL 17 PRO 18 GLN 19 TYR 20 LYS 21 TYR 22 ALA 23 ALA 24 GLY 25 VAL 26 ARG 27 ASN 28 PRO 29 GLN 30 GLN 31 HIS 32 LEU 33 ASN 34 ALA 35 GLN 36 PRO 37 GLN 38 VAL 39 THR 40 MET 41 GLN 42 GLN 43 PRO 44 ALA 45 VAL 46 HIS 47 VAL 48 GLN 49 GLY 50 GLN 51 GLU 52 PRO 53 LEU 54 THR 55 ALA 56 SER 57 MET 58 LEU 59 ALA 60 SER 61 ALA 62 PRO 63 PRO 64 GLN 65 GLU 66 GLN 67 LYS 68 GLN 69 MET 70 LEU 71 GLY 72 GLU 73 ARG 74 LEU 75 PHE 76 PRO 77 LEU 78 ILE 79 GLN 80 ALA 81 MET 82 HIS 83 PRO 84 THR 85 LEU 86 ALA 87 GLY 88 LYS 89 ILE 90 THR 91 GLY 92 MET 93 LEU 94 LEU 95 GLU 96 ILE 97 ASP 98 ASN 99 SER 100 GLU 101 LEU 102 LEU 103 HIS 104 MET 105 LEU 106 GLU 107 SER 108 PRO 109 GLU 110 SER 111 LEU 112 ARG 113 SER 114 LYS 115 VAL 116 ASP 117 GLU 118 ALA 119 VAL 120 ALA 121 VAL 122 LEU 123 GLN 124 ALA 125 HIS 126 GLN 127 ALA 128 LYS 129 GLU 130 ALA 131 ALA 132 GLN 133 LYS 134 ALA 135 VAL 136 ASN 137 SER 138 ALA 139 THR 140 GLY 141 VAL 142 PRO 143 THR 144 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 10019 polyA-binding_protein 57.64 83 100.00 100.00 2.48e-49 BMRB 7033 "PABC domain" 57.64 83 100.00 100.00 2.48e-49 PDB 1G9L "Solution Structure Of The Pabc Domain Of Human Poly(A) Binding Protein" 100.00 144 100.00 100.00 8.08e-96 PDB 1JGN "Solution Structure Of The C-Terminal Pabc Domain Of Human Poly(A)-Binding Protein In Complex With The Peptide From Paip2" 64.58 98 100.00 100.00 1.49e-56 PDB 1JH4 "Solution Structure Of The C-Terminal Pabc Domain Of Human Poly(A)-Binding Protein In Complex With The Peptide From Paip1" 64.58 98 100.00 100.00 1.49e-56 PDB 2RQG "Structure Of Gspt1ERF3A-Pabc" 57.64 83 100.00 100.00 2.48e-49 PDB 2RQH "Structure Of Gspt1ERF3A-Pabc" 57.64 83 100.00 100.00 2.48e-49 PDB 2X04 "Crystal Structure Of The Pabc-Tnrc6c Complex" 52.08 80 100.00 100.00 3.88e-43 PDB 3KTP "Structural Basis Of Gw182 Recognition By Poly(a)-binding Protein" 57.64 88 100.00 100.00 1.07e-48 PDB 3KTR "Structural Basis Of Ataxin-2 Recognition By Poly(A)-Binding" 57.64 88 100.00 100.00 1.07e-48 PDB 3KUI "Crystal Structure Of C-Terminal Domain Of Pabpc1 In Complex Binding Region Of Erf3a" 57.64 88 100.00 100.00 1.07e-48 PDB 3KUJ "Crystal Structure Of C-Terminal Domain Of Pabpc1 In Complex With Binding Region Of Erf3a" 57.64 88 100.00 100.00 1.07e-48 PDB 3KUR "Crystal Structure Of The Mlle Domain Of Poly(A)-Binding Protein" 51.39 79 100.00 100.00 1.20e-42 PDB 3KUS "Crystal Structure Of The Mlle Domain Of Poly(A)-Binding Protein In Complex With The Binding Region Of Paip2" 57.64 88 100.00 100.00 1.07e-48 PDB 3KUT "Crystal Structure Of The Mlle Domain Of Poly(a)-binding Protein In Complex With The Binding Region Of Paip2" 57.64 88 100.00 100.00 1.07e-48 PDB 3PKN "Crystal Structure Of Mlle Domain Of Poly(A) Binding Protein In Complex With Pam2 Motif Of La-Related Protein 4 (Larp4)" 57.64 88 100.00 100.00 1.07e-48 PDB 3PTH "The Pabc1 Mlle Domain Bound To The Variant Pam2 Motif Of Larp4b" 54.86 82 100.00 100.00 1.81e-46 DBJ BAC32110 "unnamed protein product [Mus musculus]" 99.31 636 97.20 98.60 3.41e-87 DBJ BAC40951 "unnamed protein product [Mus musculus]" 99.31 636 97.20 98.60 3.10e-87 DBJ BAC56450 "similar to poly(A)-binding protein 1 [Bos taurus]" 77.08 138 99.10 99.10 2.22e-70 DBJ BAE21553 "unnamed protein product [Mus musculus]" 99.31 636 97.20 98.60 3.41e-87 DBJ BAE30919 "unnamed protein product [Mus musculus]" 99.31 636 97.20 98.60 3.72e-87 EMBL CAA46522 "poly(A) binding protein [Mus musculus]" 99.31 636 97.20 98.60 3.27e-87 EMBL CAA68428 "unnamed protein product [Homo sapiens]" 99.31 633 97.90 98.60 8.18e-88 EMBL CAB96752 "polyadenylate-binding protein 1 [Bos taurus]" 99.31 636 97.90 98.60 1.03e-87 EMBL CAH91893 "hypothetical protein [Pongo abelii]" 99.31 636 97.90 98.60 1.01e-87 EMBL CAH91953 "hypothetical protein [Pongo abelii]" 99.31 636 97.90 98.60 1.14e-87 GB AAD08718 "poly(A)-binding protein [Homo sapiens]" 99.31 636 97.90 98.60 1.03e-87 GB AAH03870 "Poly(A) binding protein, cytoplasmic 1 [Mus musculus]" 99.31 636 97.20 98.60 3.41e-87 GB AAH11207 "Poly(A) binding protein, cytoplasmic 1 [Mus musculus]" 99.31 636 97.20 98.60 3.41e-87 GB AAH15958 "PABPC1 protein [Homo sapiens]" 99.31 636 97.90 98.60 1.03e-87 GB AAH23145 "Poly(A) binding protein, cytoplasmic 1 [Mus musculus]" 99.31 636 97.20 98.60 3.41e-87 REF NP_001126097 "polyadenylate-binding protein 1 [Pongo abelii]" 99.31 636 97.90 98.60 1.01e-87 REF NP_001128842 "polyadenylate-binding protein 1 [Pongo abelii]" 99.31 636 97.90 98.60 1.14e-87 REF NP_001244826 "polyadenylate-binding protein 1 [Macaca mulatta]" 99.31 636 97.90 98.60 1.03e-87 REF NP_002559 "polyadenylate-binding protein 1 [Homo sapiens]" 99.31 636 97.90 98.60 1.03e-87 REF NP_032800 "polyadenylate-binding protein 1 [Mus musculus]" 99.31 636 97.20 98.60 3.41e-87 SP P11940 "RecName: Full=Polyadenylate-binding protein 1; Short=PABP-1; Short=Poly(A)-binding protein 1 [Homo sapiens]" 99.31 636 97.90 98.60 1.03e-87 SP P29341 "RecName: Full=Polyadenylate-binding protein 1; Short=PABP-1; Short=Poly(A)-binding protein 1 [Mus musculus]" 99.31 636 97.20 98.60 3.41e-87 SP P61286 "RecName: Full=Polyadenylate-binding protein 1; Short=PABP-1; Short=Poly(A)-binding protein 1 [Bos taurus]" 99.31 636 97.90 98.60 1.03e-87 SP Q5R8F7 "RecName: Full=Polyadenylate-binding protein 1; Short=PABP-1; Short=Poly(A)-binding protein 1 [Pongo abelii]" 99.31 636 97.90 98.60 1.14e-87 TPG DAA22579 "TPA: polyadenylate-binding protein 1 [Bos taurus]" 99.31 636 97.90 98.60 1.03e-87 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PABC human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $PABC 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $PABC . mM 2.5 3.0 [U-15N] 'phosphate buffer' 50 mM . . . NaCl 0.1 M . . . NaN3 1 mM . . . H2O 90 % . . . D2O 10 % . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PABC 3.0 mM '[U-15N; U-13C]' 'phosphate buffer' 50 mM . NaCl 0.1 M . NaN3 1 mM . D2O 100 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $PABC 3.0 mM . 'phosphate buffer' 50 mM . NaCl 0.1 M . NaN3 1 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.1 loop_ _Task 'data collection' stop_ _Details 'Bruker Spectrospin' save_ save_GIFA _Saveframe_category software _Name GIFA _Version 4.31 loop_ _Task 'data processing' stop_ _Details Delsuc save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.3.13 loop_ _Task 'data analysis' stop_ _Details Wuthrich save_ save_CNS _Saveframe_category software _Name CNS _Version 0.9 loop_ _Task 'structure solution' stop_ _Details Brunger save_ save_ARIA _Saveframe_category software _Name ARIA _Version 0.9 loop_ _Task 'structure solution' stop_ _Details Nilges save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_3D_13C-separated_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.3 0.1 n/a temperature 303 0.1 K 'ionic strength' 0.2 . M pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 . indirect . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Polyadenylate-binding protein 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 PRO CA C 62.5 0.20 1 2 . 2 PRO CB C 31.7 0.20 1 3 . 2 PRO C C 176.7 0.20 1 4 . 3 LEU N N 122.1 0.25 1 5 . 3 LEU H H 8.59 0.03 1 6 . 3 LEU CA C 54.9 0.20 1 7 . 3 LEU HA H 4.44 0.03 1 8 . 3 LEU CB C 41.7 0.20 1 9 . 3 LEU HB2 H 1.75 0.03 2 10 . 3 LEU HB3 H 1.69 0.03 2 11 . 3 LEU HD1 H 0.99 0.03 1 12 . 3 LEU HD2 H 0.99 0.03 1 13 . 3 LEU C C 177.6 0.20 1 14 . 4 GLY N N 109.7 0.25 1 15 . 4 GLY H H 8.49 0.03 1 16 . 4 GLY CA C 44.7 0.20 1 17 . 4 GLY HA2 H 4.06 0.03 1 18 . 4 GLY HA3 H 4.06 0.03 1 19 . 4 GLY C C 174.0 0.20 1 20 . 5 SER N N 115.5 0.25 1 21 . 5 SER H H 8.28 0.03 1 22 . 5 SER CA C 59.2 0.20 1 23 . 5 SER HA H 3.96 0.03 1 24 . 5 SER HB2 H 4.52 0.03 1 25 . 5 SER HB3 H 4.52 0.03 1 26 . 5 SER C C 174.2 0.20 1 27 . 8 ALA CA C 51.6 0.20 1 28 . 8 ALA CB C 18.8 0.20 1 29 . 8 ALA C C 177.2 0.20 1 30 . 9 ALA N N 123.0 0.25 1 31 . 9 ALA H H 8.26 0.03 1 32 . 9 ALA CA C 51.6 0.20 1 33 . 9 ALA HA H 4.43 0.03 1 34 . 9 ALA CB C 18.9 0.20 1 35 . 9 ALA HB H 1.46 0.03 1 36 . 9 ALA C C 177.1 0.20 1 37 . 10 THR N N 115.9 0.25 1 38 . 10 THR H H 8.18 0.03 1 39 . 10 THR CA C 59.2 0.20 1 40 . 11 PRO CD C 49.6 0.20 1 41 . 11 PRO CA C 62.5 0.20 1 42 . 11 PRO CB C 31.6 0.20 1 43 . 11 PRO CG C 26.3 0.20 1 44 . 11 PRO C C 176.1 0.20 1 45 . 12 ALA N N 124.3 0.25 1 46 . 12 ALA H H 8.42 0.03 1 47 . 12 ALA CA C 51.8 0.20 1 48 . 12 ALA HA H 4.38 0.03 1 49 . 12 ALA CB C 18.6 0.20 1 50 . 12 ALA HB H 1.45 0.03 1 51 . 12 ALA C C 177.4 0.20 1 52 . 13 VAL N N 119.2 0.25 1 53 . 13 VAL H H 8.14 0.03 1 54 . 13 VAL CA C 61.6 0.20 1 55 . 13 VAL HA H 4.17 0.03 1 56 . 13 VAL CB C 32.3 0.20 1 57 . 13 VAL HB H 2.12 0.03 1 58 . 13 VAL CG1 C 20.2 0.20 1 59 . 13 VAL HG1 H 1.01 0.03 1 60 . 13 VAL CG2 C 20.2 0.20 1 61 . 13 VAL HG2 H 1.01 0.03 1 62 . 13 VAL C C 175.6 0.20 1 63 . 14 ARG N N 124.7 0.25 1 64 . 14 ARG H H 8.49 0.03 1 65 . 14 ARG CA C 55.4 0.20 1 66 . 14 ARG HA H 4.50 0.03 1 67 . 14 ARG CB C 30.2 0.20 1 68 . 14 ARG HB2 H 1.92 0.03 2 69 . 14 ARG HB3 H 1.83 0.03 2 70 . 14 ARG HG2 H 1.69 0.03 1 71 . 14 ARG HG3 H 1.69 0.03 1 72 . 14 ARG HD2 H 3.27 0.03 1 73 . 14 ARG HD3 H 3.27 0.03 1 74 . 14 ARG C C 175.8 0.20 1 75 . 15 THR N N 116.3 0.25 1 76 . 15 THR H H 8.30 0.03 1 77 . 15 THR CA C 61.2 0.20 1 78 . 15 THR HA H 4.42 0.03 1 79 . 15 THR CB C 69.3 0.20 1 80 . 15 THR HB H 4.21 0.03 1 81 . 15 THR HG2 H 1.24 0.03 1 82 . 15 THR C C 173.8 0.20 1 83 . 16 VAL N N 123.6 0.25 1 84 . 16 VAL H H 8.25 0.03 1 85 . 16 VAL CA C 59.2 0.20 1 86 . 16 VAL HA H 4.51 0.03 1 87 . 16 VAL HB H 2.14 0.03 1 88 . 16 VAL HG1 H 1.02 0.03 1 89 . 16 VAL HG2 H 1.02 0.03 1 90 . 16 VAL C C 173.9 0.20 1 91 . 17 PRO CA C 62.5 0.20 1 92 . 17 PRO HA H 4.39 0.03 1 93 . 17 PRO CB C 31.6 0.20 1 94 . 17 PRO C C 175.3 0.20 1 95 . 18 GLN N N 120.1 0.25 1 96 . 18 GLN H H 8.43 0.03 1 97 . 18 GLN CA C 55.5 0.20 1 98 . 18 GLN HA H 4.28 0.03 1 99 . 18 GLN CB C 28.7 0.20 1 100 . 18 GLN HB2 H 2.01 0.03 2 101 . 18 GLN HB3 H 1.98 0.03 2 102 . 18 GLN CG C 33.5 0.20 1 103 . 18 GLN HG2 H 2.36 0.03 1 104 . 18 GLN HG3 H 2.36 0.03 1 105 . 18 GLN C C 176.2 0.20 1 106 . 19 TYR N N 120.9 0.25 1 107 . 19 TYR H H 8.16 0.03 1 108 . 19 TYR CA C 57.0 0.20 1 109 . 19 TYR HA H 4.57 0.03 1 110 . 19 TYR CB C 38.4 0.20 1 111 . 19 TYR HB2 H 2.98 0.03 2 112 . 19 TYR HB3 H 2.93 0.03 2 113 . 19 TYR HD1 H 7.10 0.03 3 114 . 19 TYR HE1 H 6.84 0.03 3 115 . 19 TYR C C 175.1 0.20 1 116 . 20 LYS N N 123.0 0.25 1 117 . 20 LYS H H 8.12 0.03 1 118 . 20 LYS CA C 55.6 0.20 1 119 . 20 LYS HA H 4.26 0.03 1 120 . 20 LYS CB C 32.7 0.20 1 121 . 20 LYS HB2 H 1.66 0.03 1 122 . 20 LYS HB3 H 1.66 0.03 1 123 . 20 LYS CG C 28.4 0.20 1 124 . 20 LYS HG2 H 1.28 0.03 1 125 . 20 LYS HG3 H 1.28 0.03 1 126 . 20 LYS HE2 H 3.00 0.03 1 127 . 20 LYS HE3 H 3.00 0.03 1 128 . 20 LYS C C 175.3 0.20 1 129 . 21 TYR N N 120.9 0.25 1 130 . 21 TYR H H 8.04 0.03 1 131 . 21 TYR CA C 57.0 0.20 1 132 . 21 TYR HA H 4.56 0.03 1 133 . 21 TYR CB C 38.2 0.20 1 134 . 21 TYR HB2 H 3.08 0.03 2 135 . 21 TYR HB3 H 2.93 0.03 2 136 . 21 TYR HD1 H 7.18 0.03 3 137 . 21 TYR HE1 H 6.87 0.03 3 138 . 21 TYR C C 175.1 0.20 1 139 . 22 ALA N N 125.7 0.25 1 140 . 22 ALA H H 8.16 0.03 1 141 . 22 ALA CA C 51.7 0.20 1 142 . 22 ALA HA H 4.31 0.03 1 143 . 22 ALA CB C 18.6 0.20 1 144 . 22 ALA HB H 1.40 0.03 1 145 . 22 ALA C C 176.5 0.20 1 146 . 23 ALA N N 122.8 0.25 1 147 . 23 ALA H H 8.19 0.03 1 148 . 23 ALA CA C 52.0 0.20 1 149 . 23 ALA HA H 4.34 0.03 1 150 . 23 ALA CB C 18.5 0.20 1 151 . 23 ALA HB H 1.46 0.03 1 152 . 23 ALA C C 177.9 0.20 1 153 . 24 GLY N N 107.6 0.25 1 154 . 24 GLY H H 8.36 0.03 1 155 . 24 GLY CA C 44.7 0.20 1 156 . 24 GLY HA2 H 4.01 0.03 1 157 . 24 GLY HA3 H 4.01 0.03 1 158 . 24 GLY C C 173.7 0.20 1 159 . 25 VAL N N 119.0 0.25 1 160 . 25 VAL H H 7.92 0.03 1 161 . 25 VAL CA C 61.8 0.20 1 162 . 25 VAL HA H 4.17 0.03 1 163 . 25 VAL CB C 32.0 0.20 1 164 . 25 VAL HB H 2.14 0.03 1 165 . 25 VAL HG1 H 0.97 0.03 1 166 . 25 VAL HG2 H 0.97 0.03 1 167 . 25 VAL C C 175.7 0.20 1 168 . 26 ARG N N 124.4 0.25 1 169 . 26 ARG H H 8.47 0.03 1 170 . 26 ARG CA C 55.4 0.20 1 171 . 26 ARG HA H 4.38 0.03 1 172 . 26 ARG CB C 30.2 0.20 1 173 . 26 ARG HB2 H 1.82 0.03 2 174 . 26 ARG HB3 H 1.66 0.03 2 175 . 26 ARG HG2 H 1.46 0.03 1 176 . 26 ARG HG3 H 1.46 0.03 1 177 . 26 ARG HD2 H 3.22 0.03 1 178 . 26 ARG HD3 H 3.22 0.03 1 179 . 26 ARG C C 175.3 0.20 1 180 . 27 ASN N N 120.5 0.25 1 181 . 27 ASN H H 8.54 0.03 1 182 . 27 ASN CA C 50.7 0.20 1 183 . 27 ASN HA H 5.00 0.03 1 184 . 27 ASN HB2 H 2.90 0.03 2 185 . 27 ASN HB3 H 2.77 0.03 2 186 . 27 ASN C C 173.2 0.20 1 187 . 28 PRO CA C 63.1 0.20 1 188 . 28 PRO HA H 4.43 0.03 1 189 . 28 PRO CB C 31.6 0.20 1 190 . 28 PRO C C 176.7 0.20 1 191 . 29 GLN N N 118.6 0.25 1 192 . 29 GLN H H 8.40 0.03 1 193 . 29 GLN CA C 55.4 0.20 1 194 . 29 GLN HA H 4.34 0.03 1 195 . 29 GLN CB C 28.6 0.20 1 196 . 29 GLN HB2 H 2.16 0.03 2 197 . 29 GLN HB3 H 2.04 0.03 2 198 . 29 GLN HG2 H 2.44 0.03 1 199 . 29 GLN HG3 H 2.44 0.03 1 200 . 29 GLN C C 175.8 0.20 1 201 . 30 GLN N N 120.3 0.25 1 202 . 30 GLN H H 8.21 0.03 1 203 . 30 GLN CA C 55.4 0.20 1 204 . 30 GLN HA H 4.31 0.03 1 205 . 30 GLN HB2 H 2.04 0.03 1 206 . 30 GLN HB3 H 2.04 0.03 1 207 . 30 GLN HG2 H 2.36 0.03 1 208 . 30 GLN HG3 H 2.36 0.03 1 209 . 30 GLN C C 175.3 0.20 1 210 . 31 HIS CA C 55.1 0.20 1 211 . 31 HIS CB C 28.9 0.20 1 212 . 32 LEU N N 122.7 0.25 1 213 . 32 LEU H H 8.49 0.03 1 214 . 32 LEU CA C 54.6 0.20 1 215 . 32 LEU CB C 41.6 0.20 1 216 . 32 LEU C C 176.7 0.20 1 217 . 33 ASN N N 119.0 0.25 1 218 . 33 ASN H H 8.52 0.03 1 219 . 33 ASN CA C 52.5 0.20 1 220 . 33 ASN HA H 4.75 0.03 1 221 . 33 ASN CB C 38.2 0.20 1 222 . 33 ASN HB2 H 2.92 0.03 2 223 . 33 ASN HB3 H 2.82 0.03 2 224 . 33 ASN C C 174.3 0.20 1 225 . 34 ALA N N 123.6 0.25 1 226 . 34 ALA H H 8.22 0.03 1 227 . 34 ALA CA C 51.8 0.20 1 228 . 34 ALA HA H 4.39 0.03 1 229 . 34 ALA CB C 18.8 0.20 1 230 . 34 ALA HB H 1.45 0.03 1 231 . 34 ALA C C 176.9 0.20 1 232 . 35 GLN N N 120.3 0.25 1 233 . 35 GLN H H 8.36 0.03 1 234 . 35 GLN CA C 53.1 0.20 1 235 . 35 GLN HA H 4.68 0.03 1 236 . 35 GLN HB2 H 2.17 0.03 2 237 . 35 GLN HB3 H 2.01 0.03 2 238 . 35 GLN HG2 H 2.46 0.03 1 239 . 35 GLN HG3 H 2.46 0.03 1 240 . 35 GLN C C 173.7 0.20 1 241 . 36 PRO CA C 62.7 0.20 1 242 . 36 PRO HA H 4.47 0.03 1 243 . 36 PRO CB C 31.6 0.20 1 244 . 36 PRO CG C 26.3 0.20 1 245 . 36 PRO C C 176.5 0.20 1 246 . 37 GLN N N 120.5 0.25 1 247 . 37 GLN H H 8.58 0.03 1 248 . 37 GLN CA C 55.3 0.20 1 249 . 37 GLN HA H 4.42 0.03 1 250 . 37 GLN CB C 28.9 0.20 1 251 . 37 GLN HB2 H 2.15 0.03 2 252 . 37 GLN HB3 H 2.06 0.03 2 253 . 37 GLN CG C 33.6 0.20 1 254 . 37 GLN HG2 H 2.46 0.03 1 255 . 37 GLN HG3 H 2.46 0.03 1 256 . 37 GLN C C 175.7 0.20 1 257 . 38 VAL N N 121.1 0.25 1 258 . 38 VAL H H 8.28 0.03 1 259 . 38 VAL CA C 61.7 0.20 1 260 . 38 VAL HA H 4.26 0.03 1 261 . 38 VAL CB C 32.3 0.20 1 262 . 38 VAL HB H 2.17 0.03 1 263 . 38 VAL CG1 C 20.2 0.20 1 264 . 38 VAL HG1 H 1.01 0.03 1 265 . 38 VAL CG2 C 20.2 0.20 1 266 . 38 VAL HG2 H 1.01 0.03 1 267 . 38 VAL C C 175.8 0.20 1 268 . 39 THR N N 117.6 0.25 1 269 . 39 THR H H 8.29 0.03 1 270 . 39 THR CA C 61.2 0.20 1 271 . 39 THR HA H 4.42 0.03 1 272 . 39 THR CB C 69.2 0.20 1 273 . 39 THR HB H 4.26 0.03 1 274 . 39 THR CG2 C 21.2 0.20 1 275 . 39 THR HG2 H 1.27 0.03 1 276 . 39 THR C C 174.0 0.20 1 277 . 40 MET N N 122.6 0.25 1 278 . 40 MET H H 8.44 0.03 1 279 . 40 MET CA C 55.0 0.20 1 280 . 40 MET HA H 4.55 0.03 1 281 . 40 MET CB C 32.2 0.20 1 282 . 40 MET HB2 H 2.14 0.03 2 283 . 40 MET HB3 H 2.07 0.03 2 284 . 40 MET HG2 H 2.64 0.03 2 285 . 40 MET HG3 H 2.60 0.03 2 286 . 40 MET CE C 16.5 0.20 1 287 . 40 MET HE H 2.16 0.03 1 288 . 40 MET C C 175.5 0.20 1 289 . 41 GLN N N 121.7 0.25 1 290 . 41 GLN H H 8.45 0.03 1 291 . 41 GLN CA C 55.1 0.20 1 292 . 41 GLN HA H 4.39 0.03 1 293 . 41 GLN HB2 H 2.15 0.03 2 294 . 41 GLN HB3 H 2.04 0.03 2 295 . 41 GLN HG2 H 2.43 0.03 1 296 . 41 GLN HG3 H 2.43 0.03 1 297 . 41 GLN C C 175.2 0.20 1 298 . 42 GLN N N 120.3 0.25 1 299 . 42 GLN H H 8.42 0.03 1 300 . 42 GLN HA H 4.28 0.03 1 301 . 42 GLN HB2 H 1.99 0.03 1 302 . 42 GLN HB3 H 1.99 0.03 1 303 . 42 GLN HG2 H 2.36 0.03 1 304 . 42 GLN HG3 H 2.36 0.03 1 305 . 42 GLN C C 176.2 0.20 1 306 . 43 PRO CD C 49.1 0.20 1 307 . 43 PRO CA C 62.5 0.20 1 308 . 43 PRO HA H 4.47 0.03 1 309 . 43 PRO CB C 31.6 0.20 1 310 . 43 PRO CG C 26.4 0.20 1 311 . 43 PRO C C 176.1 0.20 1 312 . 44 ALA N N 124.0 0.25 1 313 . 44 ALA H H 8.43 0.03 1 314 . 44 ALA CA C 51.7 0.20 1 315 . 44 ALA HA H 4.38 0.03 1 316 . 44 ALA CB C 18.7 0.20 1 317 . 44 ALA HB H 1.43 0.03 1 318 . 44 ALA C C 177.2 0.20 1 319 . 45 VAL N N 118.8 0.25 1 320 . 45 VAL H H 8.10 0.03 1 321 . 45 VAL CA C 61.3 0.20 1 322 . 45 VAL HA H 4.14 0.03 1 323 . 45 VAL CB C 32.2 0.20 1 324 . 45 VAL HB H 2.07 0.03 1 325 . 45 VAL CG1 C 20.1 0.20 1 326 . 45 VAL HG1 H 0.96 0.03 1 327 . 45 VAL CG2 C 20.1 0.20 1 328 . 45 VAL HG2 H 0.96 0.03 1 329 . 45 VAL C C 175.4 0.20 1 330 . 46 HIS N N 123.0 0.25 1 331 . 46 HIS H H 8.56 0.03 1 332 . 46 HIS CA C 54.9 0.20 1 333 . 46 HIS HA H 4.82 0.03 1 334 . 46 HIS CB C 29.4 0.20 1 335 . 46 HIS HB2 H 3.23 0.03 2 336 . 46 HIS HB3 H 3.17 0.03 2 337 . 46 HIS C C 174.2 0.20 1 338 . 47 VAL N N 122.4 0.25 1 339 . 47 VAL H H 8.27 0.03 1 340 . 47 VAL CA C 61.8 0.20 1 341 . 47 VAL HA H 4.16 0.03 1 342 . 47 VAL CB C 32.1 0.20 1 343 . 47 VAL HB H 2.09 0.03 1 344 . 47 VAL CG1 C 20.2 0.20 1 345 . 47 VAL HG1 H 0.98 0.03 1 346 . 47 VAL CG2 C 20.2 0.20 1 347 . 47 VAL HG2 H 0.98 0.03 1 348 . 47 VAL C C 175.5 0.20 1 349 . 48 GLN N N 124.4 0.25 1 350 . 48 GLN H H 8.62 0.03 1 351 . 48 GLN CA C 55.6 0.20 1 352 . 48 GLN HA H 4.38 0.03 1 353 . 48 GLN CB C 28.8 0.20 1 354 . 48 GLN HB2 H 2.17 0.03 2 355 . 48 GLN HB3 H 2.10 0.03 2 356 . 48 GLN CG C 32.9 0.20 1 357 . 48 GLN HG2 H 2.47 0.03 1 358 . 48 GLN HG3 H 2.47 0.03 1 359 . 48 GLN C C 176.0 0.20 1 360 . 49 GLY N N 110.7 0.25 1 361 . 49 GLY H H 8.62 0.03 1 362 . 49 GLY CA C 44.6 0.20 1 363 . 49 GLY HA2 H 4.04 0.03 1 364 . 49 GLY HA3 H 4.04 0.03 1 365 . 49 GLY C C 173.5 0.20 1 366 . 50 GLN N N 119.2 0.25 1 367 . 50 GLN H H 8.25 0.03 1 368 . 50 GLN CA C 54.9 0.20 1 369 . 50 GLN HA H 4.46 0.03 1 370 . 50 GLN CB C 29.3 0.20 1 371 . 50 GLN HB2 H 2.17 0.03 2 372 . 50 GLN HB3 H 2.00 0.03 2 373 . 50 GLN CG C 33.6 0.20 1 374 . 50 GLN HG2 H 2.38 0.03 1 375 . 50 GLN HG3 H 2.38 0.03 1 376 . 50 GLN C C 175.5 0.20 1 377 . 51 GLU N N 124.2 0.25 1 378 . 51 GLU H H 8.73 0.03 1 379 . 51 GLU CA C 54.3 0.20 1 380 . 51 GLU HA H 4.59 0.03 1 381 . 51 GLU HB2 H 2.12 0.03 2 382 . 51 GLU HB3 H 1.99 0.03 2 383 . 51 GLU HG2 H 2.38 0.03 1 384 . 51 GLU HG3 H 2.38 0.03 1 385 . 51 GLU C C 174.0 0.20 1 386 . 52 PRO CA C 62.5 0.20 1 387 . 52 PRO HA H 4.41 0.03 1 388 . 52 PRO CB C 31.8 0.20 1 389 . 52 PRO CG C 26.6 0.20 1 390 . 52 PRO C C 175.3 0.20 1 391 . 53 LEU N N 122.4 0.25 1 392 . 53 LEU H H 8.49 0.03 1 393 . 53 LEU CA C 54.3 0.20 1 394 . 53 LEU HA H 4.66 0.03 1 395 . 53 LEU CB C 42.5 0.20 1 396 . 53 LEU HB2 H 1.61 0.03 2 397 . 53 LEU HB3 H 1.45 0.03 2 398 . 53 LEU CD1 C 26.2 0.20 2 399 . 53 LEU HD1 H 0.98 0.03 2 400 . 53 LEU CD2 C 24.2 0.20 2 401 . 53 LEU HD2 H 0.88 0.03 2 402 . 53 LEU C C 175.8 0.20 1 403 . 54 THR N N 113.1 0.25 1 404 . 54 THR H H 7.43 0.03 1 405 . 54 THR CA C 58.7 0.20 1 406 . 54 THR HA H 4.76 0.03 1 407 . 54 THR CB C 71.5 0.20 1 408 . 54 THR HB H 4.71 0.03 1 409 . 54 THR CG2 C 21.1 0.20 1 410 . 54 THR HG2 H 1.31 0.03 1 411 . 54 THR C C 174.7 0.20 1 412 . 55 ALA N N 123.2 0.25 1 413 . 55 ALA H H 9.15 0.03 1 414 . 55 ALA CA C 54.6 0.20 1 415 . 55 ALA HA H 4.07 0.03 1 416 . 55 ALA CB C 17.2 0.20 1 417 . 55 ALA HB H 1.54 0.03 1 418 . 55 ALA C C 180.4 0.20 1 419 . 56 SER N N 112.8 0.25 1 420 . 56 SER H H 8.44 0.03 1 421 . 56 SER CA C 61.9 0.20 1 422 . 56 SER HA H 4.29 0.03 1 423 . 56 SER CB C 60.6 0.20 1 424 . 56 SER HB2 H 3.96 0.03 2 425 . 56 SER HB3 H 3.94 0.03 2 426 . 56 SER C C 176.5 0.20 1 427 . 57 MET N N 122.1 0.25 1 428 . 57 MET H H 7.72 0.03 1 429 . 57 MET CA C 57.8 0.20 1 430 . 57 MET HA H 4.21 0.03 1 431 . 57 MET CB C 33.2 0.20 1 432 . 57 MET HB2 H 2.21 0.03 2 433 . 57 MET HB3 H 2.27 0.03 2 434 . 57 MET CG C 30.7 0.20 1 435 . 57 MET HG2 H 2.69 0.03 2 436 . 57 MET HG3 H 2.61 0.03 2 437 . 57 MET CE C 16.5 0.20 1 438 . 57 MET HE H 2.19 0.03 1 439 . 57 MET C C 178.5 0.20 1 440 . 58 LEU N N 118.5 0.25 1 441 . 58 LEU H H 7.83 0.03 1 442 . 58 LEU CA C 57.0 0.20 1 443 . 58 LEU HA H 4.12 0.03 1 444 . 58 LEU CB C 41.5 0.20 1 445 . 58 LEU HB2 H 1.79 0.03 2 446 . 58 LEU HB3 H 1.72 0.03 2 447 . 58 LEU CD1 C 26.1 0.20 2 448 . 58 LEU HD1 H 0.98 0.03 1 449 . 58 LEU CD2 C 24.3 0.20 2 450 . 58 LEU HD2 H 0.98 0.03 1 451 . 58 LEU C C 177.6 0.20 1 452 . 59 ALA N N 116.8 0.25 1 453 . 59 ALA H H 7.86 0.03 1 454 . 59 ALA CA C 53.5 0.20 1 455 . 59 ALA HA H 4.16 0.03 1 456 . 59 ALA CB C 18.0 0.20 1 457 . 59 ALA HB H 1.57 0.03 1 458 . 59 ALA C C 178.3 0.20 1 459 . 60 SER N N 110.3 0.25 1 460 . 60 SER H H 7.49 0.03 1 461 . 60 SER CA C 58.1 0.20 1 462 . 60 SER HA H 4.50 0.03 1 463 . 60 SER CB C 63.3 0.20 1 464 . 60 SER HB2 H 4.02 0.03 2 465 . 60 SER HB3 H 4.07 0.03 2 466 . 60 SER C C 172.9 0.20 1 467 . 61 ALA N N 126.5 0.25 1 468 . 61 ALA H H 7.72 0.03 1 469 . 61 ALA CA C 49.1 0.20 1 470 . 61 ALA HA H 4.95 0.03 1 471 . 61 ALA HB H 1.50 0.03 1 472 . 61 ALA C C 174.4 0.20 1 473 . 63 PRO CA C 65.8 0.20 1 474 . 63 PRO CB C 31.7 0.20 1 475 . 63 PRO CG C 27.3 0.20 1 476 . 63 PRO C C 178.7 0.20 1 477 . 64 GLN N N 116.3 0.25 1 478 . 64 GLN H H 9.27 0.03 1 479 . 64 GLN CA C 58.3 0.20 1 480 . 64 GLN HA H 4.27 0.03 1 481 . 64 GLN CB C 27.1 0.20 1 482 . 64 GLN HB2 H 2.21 0.03 2 483 . 64 GLN HB3 H 2.12 0.03 2 484 . 64 GLN CG C 32.8 0.20 1 485 . 64 GLN HG2 H 2.62 0.03 2 486 . 64 GLN HG3 H 2.52 0.03 2 487 . 64 GLN C C 178.1 0.20 1 488 . 65 GLU N N 120.2 0.25 1 489 . 65 GLU H H 7.68 0.03 1 490 . 65 GLU CA C 57.6 0.20 1 491 . 65 GLU HA H 4.35 0.03 1 492 . 65 GLU CB C 29.2 0.20 1 493 . 65 GLU HB2 H 2.26 0.03 2 494 . 65 GLU HB3 H 2.17 0.03 2 495 . 65 GLU HG2 H 2.42 0.03 1 496 . 65 GLU HG3 H 2.42 0.03 1 497 . 65 GLU C C 178.1 0.20 1 498 . 66 GLN N N 118.8 0.25 1 499 . 66 GLN H H 8.12 0.03 1 500 . 66 GLN CA C 59.2 0.20 1 501 . 66 GLN HA H 4.25 0.03 1 502 . 66 GLN CB C 28.1 0.20 1 503 . 66 GLN HB2 H 2.52 0.03 2 504 . 66 GLN HB3 H 2.41 0.03 2 505 . 66 GLN CG C 33.6 0.20 1 506 . 66 GLN HG2 H 2.70 0.03 2 507 . 66 GLN HG3 H 2.60 0.03 2 508 . 66 GLN HE21 H 6.78 0.03 2 509 . 66 GLN HE22 H 7.68 0.03 2 510 . 66 GLN C C 177.1 0.20 1 511 . 67 LYS N N 113.4 0.25 1 512 . 67 LYS H H 7.62 0.03 1 513 . 67 LYS CA C 57.0 0.20 1 514 . 67 LYS HA H 4.13 0.03 1 515 . 67 LYS CB C 31.2 0.20 1 516 . 67 LYS HB2 H 2.20 0.03 2 517 . 67 LYS HB3 H 1.91 0.03 2 518 . 67 LYS CG C 23.3 0.20 1 519 . 67 LYS HG2 H 1.77 0.03 1 520 . 67 LYS HG3 H 1.77 0.03 1 521 . 67 LYS CD C 27.4 0.20 1 522 . 67 LYS C C 178.3 0.20 1 523 . 68 GLN N N 118.9 0.25 1 524 . 68 GLN H H 7.71 0.03 1 525 . 68 GLN CA C 58.6 0.20 1 526 . 68 GLN HA H 4.13 0.03 1 527 . 68 GLN CB C 27.6 0.20 1 528 . 68 GLN HB2 H 2.30 0.03 1 529 . 68 GLN HB3 H 2.30 0.03 1 530 . 68 GLN CG C 32.6 0.20 1 531 . 68 GLN HG2 H 2.53 0.03 1 532 . 68 GLN HG3 H 2.53 0.03 1 533 . 68 GLN C C 178.3 0.20 1 534 . 69 MET N N 118.6 0.25 1 535 . 69 MET H H 8.48 0.03 1 536 . 69 MET CA C 58.7 0.20 1 537 . 69 MET HA H 4.16 0.03 1 538 . 69 MET CB C 33.3 0.20 1 539 . 69 MET HB2 H 2.31 0.03 2 540 . 69 MET HB3 H 2.13 0.03 2 541 . 69 MET CG C 31.6 0.20 1 542 . 69 MET HG2 H 2.86 0.03 2 543 . 69 MET HG3 H 2.69 0.03 2 544 . 69 MET CE C 16.5 0.20 1 545 . 69 MET HE H 2.08 0.03 1 546 . 69 MET C C 179.2 0.20 1 547 . 70 LEU N N 118.8 0.25 1 548 . 70 LEU H H 7.94 0.03 1 549 . 70 LEU CA C 57.6 0.20 1 550 . 70 LEU HA H 4.01 0.03 1 551 . 70 LEU CB C 41.5 0.20 1 552 . 70 LEU HB2 H 2.05 0.03 2 553 . 70 LEU HB3 H 1.23 0.03 2 554 . 70 LEU HG H 1.79 0.03 1 555 . 70 LEU CD1 C 25.3 0.20 2 556 . 70 LEU HD1 H 1.01 0.03 2 557 . 70 LEU CD2 C 23.3 0.20 2 558 . 70 LEU HD2 H 0.91 0.03 2 559 . 70 LEU C C 179.0 0.20 1 560 . 71 GLY N N 108.4 0.25 1 561 . 71 GLY H H 9.11 0.03 1 562 . 71 GLY CA C 47.8 0.20 1 563 . 71 GLY HA2 H 4.14 0.03 2 564 . 71 GLY HA3 H 3.67 0.03 2 565 . 71 GLY C C 175.0 0.20 1 566 . 72 GLU N N 118.9 0.25 1 567 . 72 GLU H H 8.25 0.03 1 568 . 72 GLU CA C 58.1 0.20 1 569 . 72 GLU HA H 4.24 0.03 1 570 . 72 GLU CB C 29.1 0.20 1 571 . 72 GLU HB2 H 2.23 0.03 1 572 . 72 GLU HB3 H 2.23 0.03 1 573 . 72 GLU CG C 35.6 0.20 1 574 . 72 GLU HG2 H 2.58 0.03 2 575 . 72 GLU HG3 H 2.52 0.03 2 576 . 72 GLU C C 178.1 0.20 1 577 . 73 ARG N N 115.3 0.25 1 578 . 73 ARG H H 7.25 0.03 1 579 . 73 ARG CA C 56.0 0.20 1 580 . 73 ARG HA H 4.47 0.03 1 581 . 73 ARG CB C 30.3 0.20 1 582 . 73 ARG HB2 H 2.07 0.03 2 583 . 73 ARG HB3 H 1.97 0.03 2 584 . 73 ARG CG C 27.3 0.20 1 585 . 73 ARG HG2 H 1.89 0.03 2 586 . 73 ARG CD C 41.9 0.20 1 587 . 73 ARG HD2 H 3.24 0.03 2 588 . 73 ARG HD3 H 3.30 0.03 2 589 . 73 ARG C C 177.6 0.20 1 590 . 74 LEU N N 118.8 0.25 1 591 . 74 LEU H H 8.59 0.03 1 592 . 74 LEU CA C 57.0 0.20 1 593 . 74 LEU HA H 4.16 0.03 1 594 . 74 LEU CB C 43.5 0.20 1 595 . 74 LEU HB2 H 1.91 0.03 2 596 . 74 LEU HB3 H 1.57 0.03 2 597 . 74 LEU HG H 1.82 0.03 1 598 . 74 LEU CD1 C 26.0 0.20 2 599 . 74 LEU HD1 H 0.91 0.03 1 600 . 74 LEU CD2 C 23.4 0.20 2 601 . 74 LEU HD2 H 0.91 0.03 1 602 . 74 LEU C C 177.8 0.20 1 603 . 75 PHE N N 117.2 0.25 1 604 . 75 PHE H H 8.54 0.03 1 605 . 75 PHE CA C 63.2 0.20 1 606 . 75 PHE HA H 4.41 0.03 1 607 . 75 PHE HB2 H 3.36 0.03 2 608 . 75 PHE HB3 H 3.24 0.03 2 609 . 75 PHE HD1 H 7.20 0.03 3 610 . 75 PHE HE1 H 7.35 0.03 3 611 . 75 PHE C C 173.1 0.20 1 612 . 76 PRO CA C 65.3 0.20 1 613 . 76 PRO HA H 4.27 0.03 1 614 . 76 PRO CB C 30.2 0.20 1 615 . 76 PRO CG C 27.3 0.20 1 616 . 76 PRO C C 179.1 0.20 1 617 . 77 LEU N N 116.3 0.25 1 618 . 77 LEU H H 6.91 0.03 1 619 . 77 LEU CA C 56.5 0.20 1 620 . 77 LEU HA H 4.16 0.03 1 621 . 77 LEU CB C 41.0 0.20 1 622 . 77 LEU HB2 H 2.13 0.03 2 623 . 77 LEU HB3 H 1.51 0.03 2 624 . 77 LEU HG H 1.29 0.03 1 625 . 77 LEU CD1 C 25.3 0.20 2 626 . 77 LEU HD1 H 1.05 0.03 2 627 . 77 LEU CD2 C 21.1 0.20 2 628 . 77 LEU HD2 H 0.96 0.03 2 629 . 77 LEU C C 179.2 0.20 1 630 . 78 ILE N N 119.5 0.25 1 631 . 78 ILE H H 7.96 0.03 1 632 . 78 ILE CA C 63.8 0.20 1 633 . 78 ILE HA H 3.74 0.03 1 634 . 78 ILE CB C 36.8 0.20 1 635 . 78 ILE HB H 1.82 0.03 1 636 . 78 ILE CG2 C 18.1 0.20 2 637 . 78 ILE HG2 H 0.98 0.03 1 638 . 78 ILE CG1 C 28.4 0.20 2 639 . 78 ILE HG12 H 1.85 0.03 2 640 . 78 ILE HG13 H 1.28 0.03 2 641 . 78 ILE CD1 C 13.9 0.20 1 642 . 78 ILE HD1 H 0.91 0.03 1 643 . 78 ILE C C 178.1 0.20 1 644 . 79 GLN N N 122.3 0.25 1 645 . 79 GLN H H 9.01 0.03 1 646 . 79 GLN CA C 58.3 0.20 1 647 . 79 GLN HA H 3.58 0.03 1 648 . 79 GLN CB C 27.7 0.20 1 649 . 79 GLN HB2 H 1.84 0.03 1 650 . 79 GLN HB3 H 1.84 0.03 1 651 . 79 GLN CG C 33.5 0.20 1 652 . 79 GLN HG2 H 2.16 0.03 1 653 . 79 GLN HG3 H 2.16 0.03 1 654 . 79 GLN C C 175.6 0.20 1 655 . 80 ALA N N 115.7 0.25 1 656 . 80 ALA H H 6.88 0.03 1 657 . 80 ALA CA C 53.1 0.20 1 658 . 80 ALA HA H 4.16 0.03 1 659 . 80 ALA CB C 17.8 0.20 1 660 . 80 ALA HB H 1.51 0.03 1 661 . 80 ALA C C 178.1 0.20 1 662 . 81 MET N N 114.6 0.25 1 663 . 81 MET H H 7.29 0.03 1 664 . 81 MET CA C 57.0 0.20 1 665 . 81 MET HA H 4.27 0.03 1 666 . 81 MET CB C 35.1 0.20 1 667 . 81 MET HB2 H 2.18 0.03 2 668 . 81 MET HB3 H 1.96 0.03 2 669 . 81 MET CG C 31.5 0.20 1 670 . 81 MET HG2 H 2.72 0.03 2 671 . 81 MET HG3 H 2.58 0.03 2 672 . 81 MET CE C 17.2 0.20 1 673 . 81 MET HE H 2.12 0.03 1 674 . 81 MET C C 175.9 0.20 1 675 . 82 HIS N N 115.8 0.25 1 676 . 82 HIS H H 8.18 0.03 1 677 . 82 HIS CA C 53.7 0.20 1 678 . 82 HIS HA H 4.96 0.03 1 679 . 82 HIS HB2 H 3.04 0.03 2 680 . 82 HIS HB3 H 2.58 0.03 2 681 . 82 HIS HD2 H 6.72 0.03 1 682 . 82 HIS HE1 H 8.03 0.03 1 683 . 82 HIS C C 177.2 0.20 1 684 . 83 PRO CA C 65.3 0.20 1 685 . 83 PRO CB C 31.3 0.20 1 686 . 83 PRO CG C 26.3 0.20 1 687 . 83 PRO C C 179.2 0.20 1 688 . 84 THR N N 108.4 0.25 1 689 . 84 THR H H 8.35 0.03 1 690 . 84 THR CA C 63.4 0.20 1 691 . 84 THR HA H 4.48 0.03 1 692 . 84 THR CB C 68.4 0.20 1 693 . 84 THR CG2 C 21.3 0.20 1 694 . 84 THR HG2 H 1.39 0.03 1 695 . 84 THR C C 175.8 0.20 1 696 . 85 LEU N N 119.6 0.25 1 697 . 85 LEU H H 7.76 0.03 1 698 . 85 LEU CA C 53.5 0.20 1 699 . 85 LEU HA H 4.15 0.03 1 700 . 85 LEU CB C 43.0 0.20 1 701 . 85 LEU HB2 H 2.27 0.03 2 702 . 85 LEU HB3 H 1.69 0.03 2 703 . 85 LEU CD1 C 25.2 0.20 2 704 . 85 LEU HD1 H 0.95 0.03 2 705 . 85 LEU CD2 C 22.2 0.20 2 706 . 85 LEU C C 176.9 0.20 1 707 . 86 ALA N N 121.2 0.25 1 708 . 86 ALA H H 7.51 0.03 1 709 . 86 ALA CA C 56.0 0.20 1 710 . 86 ALA HA H 3.91 0.03 1 711 . 86 ALA CB C 17.8 0.20 1 712 . 86 ALA HB H 1.29 0.03 1 713 . 86 ALA C C 179.7 0.20 1 714 . 87 GLY N N 109.5 0.25 1 715 . 87 GLY H H 9.34 0.03 1 716 . 87 GLY CA C 47.2 0.20 1 717 . 87 GLY C C 175.8 0.20 1 718 . 88 LYS N N 123.7 0.25 1 719 . 88 LYS H H 7.99 0.03 1 720 . 88 LYS CA C 58.1 0.20 1 721 . 88 LYS HA H 4.27 0.03 1 722 . 88 LYS CB C 32.4 0.20 1 723 . 88 LYS HB2 H 1.96 0.03 2 724 . 88 LYS HB3 H 1.67 0.03 2 725 . 88 LYS CG C 24.4 0.20 1 726 . 88 LYS HG2 H 1.80 0.03 1 727 . 88 LYS HG3 H 1.80 0.03 1 728 . 88 LYS CD C 28.5 0.20 1 729 . 88 LYS HE2 H 2.99 0.03 2 730 . 88 LYS HE3 H 3.06 0.03 2 731 . 88 LYS C C 179.4 0.20 1 732 . 89 ILE N N 118.4 0.25 1 733 . 89 ILE H H 8.74 0.03 1 734 . 89 ILE CA C 64.5 0.20 1 735 . 89 ILE HA H 3.75 0.03 1 736 . 89 ILE CB C 38.1 0.20 1 737 . 89 ILE HB H 1.76 0.03 1 738 . 89 ILE CG2 C 18.1 0.20 2 739 . 89 ILE HG2 H 1.02 0.03 1 740 . 89 ILE CG1 C 28.4 0.20 2 741 . 89 ILE HG12 H 1.67 0.03 2 742 . 89 ILE HG13 H 1.18 0.03 2 743 . 89 ILE CD1 C 14.9 0.20 1 744 . 89 ILE HD1 H 0.66 0.03 1 745 . 89 ILE C C 177.4 0.20 1 746 . 90 THR N N 116.3 0.25 1 747 . 90 THR H H 8.51 0.03 1 748 . 90 THR CA C 67.6 0.20 1 749 . 90 THR HA H 4.46 0.03 1 750 . 90 THR CB C 68.3 0.20 1 751 . 90 THR HB H 3.67 0.03 1 752 . 90 THR CG2 C 21.2 0.20 1 753 . 90 THR HG2 H 1.30 0.03 1 754 . 90 THR C C 175.3 0.20 1 755 . 91 GLY N N 104.3 0.25 1 756 . 91 GLY H H 7.74 0.03 1 757 . 91 GLY CA C 46.9 0.20 1 758 . 91 GLY HA2 H 4.03 0.03 2 759 . 91 GLY HA3 H 3.82 0.03 2 760 . 91 GLY C C 175.8 0.20 1 761 . 92 MET N N 119.3 0.25 1 762 . 92 MET H H 7.67 0.03 1 763 . 92 MET CA C 58.4 0.20 1 764 . 92 MET HA H 4.24 0.03 1 765 . 92 MET CB C 33.3 0.20 1 766 . 92 MET HB2 H 2.32 0.03 1 767 . 92 MET HB3 H 2.32 0.03 1 768 . 92 MET CG C 30.5 0.20 1 769 . 92 MET HG2 H 2.79 0.03 2 770 . 92 MET HG3 H 2.64 0.03 2 771 . 92 MET CE C 16.0 0.20 1 772 . 92 MET HE H 2.20 0.03 1 773 . 92 MET C C 179.2 0.20 1 774 . 93 LEU N N 120.4 0.25 1 775 . 93 LEU H H 8.45 0.03 1 776 . 93 LEU CA C 56.8 0.20 1 777 . 93 LEU HA H 4.23 0.03 1 778 . 93 LEU CB C 40.1 0.20 1 779 . 93 LEU HB2 H 2.05 0.03 2 780 . 93 LEU HB3 H 1.88 0.03 2 781 . 93 LEU CG C 27.4 0.20 1 782 . 93 LEU HG H 1.47 0.03 1 783 . 93 LEU CD1 C 25.3 0.20 2 784 . 93 LEU HD1 H 0.92 0.03 2 785 . 93 LEU CD2 C 23.3 0.20 2 786 . 93 LEU HD2 H 0.84 0.03 2 787 . 93 LEU C C 177.6 0.20 1 788 . 94 LEU N N 114.9 0.25 1 789 . 94 LEU H H 7.93 0.03 1 790 . 94 LEU CA C 56.1 0.20 1 791 . 94 LEU HA H 4.23 0.03 1 792 . 94 LEU CB C 41.0 0.20 1 793 . 94 LEU HB2 H 1.99 0.03 2 794 . 94 LEU HB3 H 1.66 0.03 2 795 . 94 LEU HG H 1.88 0.03 1 796 . 94 LEU CD1 C 25.2 0.20 2 797 . 94 LEU HD1 H 0.99 0.03 1 798 . 94 LEU CD2 C 22.3 0.20 2 799 . 94 LEU HD2 H 0.99 0.03 1 800 . 94 LEU C C 177.2 0.20 1 801 . 95 GLU N N 116.3 0.25 1 802 . 95 GLU H H 7.25 0.03 1 803 . 95 GLU CA C 56.8 0.20 1 804 . 95 GLU HA H 4.28 0.03 1 805 . 95 GLU CB C 29.6 0.20 1 806 . 95 GLU HB2 H 2.07 0.03 1 807 . 95 GLU HB3 H 2.07 0.03 1 808 . 95 GLU CG C 35.6 0.20 1 809 . 95 GLU HG2 H 2.60 0.03 2 810 . 95 GLU HG3 H 2.38 0.03 2 811 . 95 GLU C C 177.3 0.20 1 812 . 96 ILE N N 121.3 0.25 1 813 . 96 ILE H H 7.89 0.03 1 814 . 96 ILE CA C 61.2 0.20 1 815 . 96 ILE HA H 4.05 0.03 1 816 . 96 ILE CB C 36.9 0.20 1 817 . 96 ILE HB H 2.22 0.03 1 818 . 96 ILE CG2 C 16.1 0.20 2 819 . 96 ILE HG2 H 1.20 0.03 1 820 . 96 ILE CG1 C 27.3 0.20 2 821 . 96 ILE HG12 H 1.79 0.03 2 822 . 96 ILE HG13 H 1.45 0.03 2 823 . 96 ILE CD1 C 13.9 0.20 1 824 . 96 ILE HD1 H 0.99 0.03 1 825 . 96 ILE C C 172.6 0.20 1 826 . 97 ASP N N 119.3 0.25 1 827 . 97 ASP H H 7.87 0.03 1 828 . 97 ASP CA C 54.9 0.20 1 829 . 97 ASP HA H 4.39 0.03 1 830 . 97 ASP CB C 42.7 0.20 1 831 . 97 ASP HB2 H 2.85 0.03 2 832 . 97 ASP HB3 H 2.73 0.03 2 833 . 97 ASP C C 177.3 0.20 1 834 . 98 ASN N N 122.6 0.25 1 835 . 98 ASN H H 8.76 0.03 1 836 . 98 ASN CA C 55.6 0.20 1 837 . 98 ASN HA H 4.38 0.03 1 838 . 98 ASN CB C 37.0 0.20 1 839 . 98 ASN HB2 H 2.99 0.03 2 840 . 98 ASN HB3 H 2.64 0.03 2 841 . 98 ASN HD21 H 7.40 0.03 2 842 . 98 ASN HD22 H 6.59 0.03 2 843 . 98 ASN C C 176.9 0.20 1 844 . 99 SER N N 114.3 0.25 1 845 . 99 SER H H 8.70 0.03 1 846 . 99 SER CA C 61.3 0.20 1 847 . 99 SER HA H 4.21 0.03 1 848 . 99 SER CB C 61.8 0.20 1 849 . 99 SER HB2 H 4.03 0.03 1 850 . 99 SER HB3 H 4.03 0.03 1 851 . 99 SER C C 177.0 0.20 1 852 . 100 GLU N N 123.6 0.25 1 853 . 100 GLU H H 7.49 0.03 1 854 . 100 GLU CA C 58.1 0.20 1 855 . 100 GLU HA H 4.40 0.03 1 856 . 100 GLU CB C 28.7 0.20 1 857 . 100 GLU HB2 H 2.24 0.03 2 858 . 100 GLU HB3 H 2.19 0.03 2 859 . 100 GLU HG2 H 2.45 0.03 2 860 . 100 GLU HG3 H 2.39 0.03 2 861 . 100 GLU C C 179.0 0.20 1 862 . 101 LEU N N 120.9 0.25 1 863 . 101 LEU H H 8.04 0.03 1 864 . 101 LEU CA C 57.6 0.20 1 865 . 101 LEU HA H 4.33 0.03 1 866 . 101 LEU CB C 42.6 0.20 1 867 . 101 LEU HB2 H 1.67 0.03 2 868 . 101 LEU HB3 H 1.20 0.03 2 869 . 101 LEU HG H 1.41 0.03 1 870 . 101 LEU CD1 C 26.2 0.20 2 871 . 101 LEU HD1 H 0.96 0.03 1 872 . 101 LEU CD2 C 22.2 0.20 2 873 . 101 LEU HD2 H 0.96 0.03 1 874 . 101 LEU C C 178.5 0.20 1 875 . 102 LEU N N 117.6 0.25 1 876 . 102 LEU H H 8.38 0.03 1 877 . 102 LEU CA C 57.5 0.20 1 878 . 102 LEU HA H 4.02 0.03 1 879 . 102 LEU CB C 40.9 0.20 1 880 . 102 LEU HB2 H 1.83 0.03 2 881 . 102 LEU HB3 H 1.71 0.03 2 882 . 102 LEU HG H 1.75 0.03 1 883 . 102 LEU CD1 C 26.2 0.20 2 884 . 102 LEU HD1 H 0.89 0.03 2 885 . 102 LEU CD2 C 23.8 0.20 2 886 . 102 LEU HD2 H 0.86 0.03 2 887 . 102 LEU C C 179.5 0.20 1 888 . 103 HIS N N 116.5 0.25 1 889 . 103 HIS H H 7.52 0.03 1 890 . 103 HIS CA C 57.7 0.20 1 891 . 103 HIS HA H 4.63 0.03 1 892 . 103 HIS CB C 27.6 0.20 1 893 . 103 HIS HB2 H 3.60 0.03 2 894 . 103 HIS HB3 H 3.43 0.03 2 895 . 103 HIS HD2 H 7.44 0.03 1 896 . 103 HIS C C 177.0 0.20 1 897 . 104 MET N N 119.2 0.25 1 898 . 104 MET H H 8.34 0.03 1 899 . 104 MET CA C 58.8 0.20 1 900 . 104 MET HA H 3.94 0.03 1 901 . 104 MET CB C 32.8 0.20 1 902 . 104 MET HB2 H 2.50 0.03 2 903 . 104 MET HB3 H 2.45 0.03 2 904 . 104 MET CG C 31.6 0.20 1 905 . 104 MET HG2 H 2.83 0.03 1 906 . 104 MET HG3 H 2.83 0.03 1 907 . 104 MET CE C 17.6 0.20 1 908 . 104 MET HE H 2.47 0.03 1 909 . 104 MET C C 176.3 0.20 1 910 . 105 LEU N N 115.5 0.25 1 911 . 105 LEU H H 7.65 0.03 1 912 . 105 LEU CA C 56.2 0.20 1 913 . 105 LEU HA H 4.04 0.03 1 914 . 105 LEU CB C 41.0 0.20 1 915 . 105 LEU HB2 H 2.09 0.03 2 916 . 105 LEU HB3 H 1.62 0.03 2 917 . 105 LEU HG H 1.92 0.03 1 918 . 105 LEU CD1 C 25.5 0.20 2 919 . 105 LEU HD1 H 1.00 0.03 2 920 . 105 LEU CD2 C 23.2 0.20 2 921 . 105 LEU HD2 H 0.86 0.03 2 922 . 105 LEU C C 178.0 0.20 1 923 . 106 GLU N N 115.9 0.25 1 924 . 106 GLU H H 7.37 0.03 1 925 . 106 GLU CA C 55.5 0.20 1 926 . 106 GLU HA H 4.52 0.03 1 927 . 106 GLU CB C 30.2 0.20 1 928 . 106 GLU HB2 H 2.21 0.03 1 929 . 106 GLU HB3 H 2.21 0.03 1 930 . 106 GLU CG C 35.4 0.20 1 931 . 106 GLU HG2 H 2.48 0.03 1 932 . 106 GLU HG3 H 2.48 0.03 1 933 . 106 GLU C C 175.6 0.20 1 934 . 107 SER N N 113.6 0.25 1 935 . 107 SER H H 7.43 0.03 1 936 . 107 SER CA C 53.2 0.20 1 937 . 107 SER HA H 5.14 0.03 1 938 . 107 SER HB2 H 3.67 0.03 2 939 . 107 SER HB3 H 3.55 0.03 2 940 . 107 SER C C 171.4 0.20 1 941 . 108 PRO CA C 64.7 0.20 1 942 . 108 PRO CB C 31.6 0.20 1 943 . 108 PRO CG C 26.3 0.20 1 944 . 108 PRO C C 178.9 0.20 1 945 . 109 GLU N N 117.3 0.25 1 946 . 109 GLU H H 9.07 0.03 1 947 . 109 GLU CA C 59.2 0.20 1 948 . 109 GLU HA H 4.20 0.03 1 949 . 109 GLU CB C 28.3 0.20 1 950 . 109 GLU HB2 H 2.11 0.03 1 951 . 109 GLU HB3 H 2.11 0.03 1 952 . 109 GLU CG C 35.6 0.20 1 953 . 109 GLU HG2 H 2.45 0.03 2 954 . 109 GLU HG3 H 2.42 0.03 2 955 . 109 GLU C C 179.0 0.20 1 956 . 110 SER N N 117.0 0.25 1 957 . 110 SER H H 7.91 0.03 1 958 . 110 SER CA C 60.9 0.20 1 959 . 110 SER HA H 4.45 0.03 1 960 . 110 SER CB C 62.3 0.20 1 961 . 110 SER HB2 H 4.06 0.03 1 962 . 110 SER HB3 H 4.06 0.03 1 963 . 110 SER C C 176.2 0.20 1 964 . 111 LEU N N 121.7 0.25 1 965 . 111 LEU H H 8.01 0.03 1 966 . 111 LEU CA C 57.6 0.20 1 967 . 111 LEU HA H 4.24 0.03 1 968 . 111 LEU CB C 39.9 0.20 1 969 . 111 LEU HB2 H 2.02 0.03 2 970 . 111 LEU HB3 H 1.88 0.03 2 971 . 111 LEU CD1 C 26.3 0.20 1 972 . 111 LEU HD1 H 0.86 0.03 1 973 . 111 LEU CD2 C 26.3 0.20 1 974 . 111 LEU HD2 H 0.86 0.03 1 975 . 111 LEU C C 177.6 0.20 1 976 . 112 ARG N N 117.4 0.25 1 977 . 112 ARG H H 8.45 0.03 1 978 . 112 ARG CA C 59.2 0.20 1 979 . 112 ARG HA H 3.88 0.03 1 980 . 112 ARG CB C 29.1 0.20 1 981 . 112 ARG HB2 H 2.05 0.03 1 982 . 112 ARG HB3 H 2.05 0.03 1 983 . 112 ARG CG C 26.2 0.20 1 984 . 112 ARG HG2 H 1.81 0.03 1 985 . 112 ARG HG3 H 1.81 0.03 1 986 . 112 ARG CD C 42.9 0.20 1 987 . 112 ARG HD2 H 3.35 0.03 1 988 . 112 ARG HD3 H 3.35 0.03 1 989 . 112 ARG C C 177.4 0.20 1 990 . 113 SER N N 111.7 0.25 1 991 . 113 SER H H 7.82 0.03 1 992 . 113 SER CA C 62.3 0.20 1 993 . 113 SER HA H 4.40 0.03 1 994 . 113 SER CB C 61.8 0.20 1 995 . 113 SER HB2 H 4.12 0.03 1 996 . 113 SER HB3 H 4.12 0.03 1 997 . 113 SER C C 177.1 0.20 1 998 . 114 LYS N N 120.9 0.25 1 999 . 114 LYS H H 7.66 0.03 1 1000 . 114 LYS CA C 56.7 0.20 1 1001 . 114 LYS HA H 4.23 0.03 1 1002 . 114 LYS CB C 31.4 0.20 1 1003 . 114 LYS HB2 H 2.18 0.03 2 1004 . 114 LYS HB3 H 1.92 0.03 2 1005 . 114 LYS CG C 24.2 0.20 1 1006 . 114 LYS HG2 H 1.68 0.03 1 1007 . 114 LYS HG3 H 1.68 0.03 1 1008 . 114 LYS CD C 27.4 0.20 1 1009 . 114 LYS C C 179.3 0.20 1 1010 . 115 VAL N N 121.8 0.25 1 1011 . 115 VAL H H 8.82 0.03 1 1012 . 115 VAL CA C 66.8 0.20 1 1013 . 115 VAL HA H 3.60 0.03 1 1014 . 115 VAL CB C 31.0 0.20 1 1015 . 115 VAL HB H 2.39 0.03 1 1016 . 115 VAL CG1 C 24.2 0.20 1 1017 . 115 VAL HG1 H 1.12 0.03 2 1018 . 115 VAL CG2 C 21.3 0.20 1 1019 . 115 VAL HG2 H 1.20 0.03 2 1020 . 115 VAL C C 176.7 0.20 1 1021 . 116 ASP N N 119.7 0.25 1 1022 . 116 ASP H H 8.74 0.03 1 1023 . 116 ASP CA C 57.0 0.20 1 1024 . 116 ASP HA H 4.46 0.03 1 1025 . 116 ASP CB C 39.0 0.20 1 1026 . 116 ASP HB2 H 2.96 0.03 2 1027 . 116 ASP HB3 H 2.72 0.03 2 1028 . 116 ASP C C 179.5 0.20 1 1029 . 117 GLU N N 120.3 0.25 1 1030 . 117 GLU H H 7.74 0.03 1 1031 . 117 GLU CA C 58.7 0.20 1 1032 . 117 GLU HA H 4.17 0.03 1 1033 . 117 GLU CB C 29.4 0.20 1 1034 . 117 GLU HB2 H 2.30 0.03 2 1035 . 117 GLU HB3 H 2.27 0.03 2 1036 . 117 GLU CG C 35.6 0.20 1 1037 . 117 GLU HG2 H 2.58 0.03 1 1038 . 117 GLU HG3 H 2.58 0.03 1 1039 . 117 GLU C C 177.9 0.20 1 1040 . 118 ALA N N 122.8 0.25 1 1041 . 118 ALA H H 8.03 0.03 1 1042 . 118 ALA CA C 54.5 0.20 1 1043 . 118 ALA HA H 4.20 0.03 1 1044 . 118 ALA HB H 1.67 0.03 1 1045 . 118 ALA CB C 17.8 0.20 1 1046 . 118 ALA C C 179.2 0.20 1 1047 . 119 VAL N N 117.9 0.25 1 1048 . 119 VAL H H 8.80 0.03 1 1049 . 119 VAL CA C 66.6 0.20 1 1050 . 119 VAL HA H 3.38 0.03 1 1051 . 119 VAL CB C 31.0 0.20 1 1052 . 119 VAL HB H 2.10 0.03 1 1053 . 119 VAL CG1 C 23.3 0.20 1 1054 . 119 VAL HG1 H 0.63 0.03 2 1055 . 119 VAL CG2 C 20.1 0.20 1 1056 . 119 VAL HG2 H 0.81 0.03 2 1057 . 119 VAL C C 177.2 0.20 1 1058 . 120 ALA N N 120.6 0.25 1 1059 . 120 ALA H H 7.66 0.03 1 1060 . 120 ALA CA C 54.6 0.20 1 1061 . 120 ALA HA H 4.23 0.03 1 1062 . 120 ALA CB C 17.1 0.20 1 1063 . 120 ALA HB H 1.62 0.03 1 1064 . 120 ALA C C 180.9 0.20 1 1065 . 121 VAL N N 119.8 0.25 1 1066 . 121 VAL H H 7.84 0.03 1 1067 . 121 VAL CA C 65.7 0.20 1 1068 . 121 VAL HA H 3.81 0.03 1 1069 . 121 VAL CB C 31.3 0.20 1 1070 . 121 VAL HB H 2.33 0.03 1 1071 . 121 VAL CG1 C 21.9 0.20 1 1072 . 121 VAL HG1 H 1.18 0.03 2 1073 . 121 VAL CG2 C 20.6 0.20 1 1074 . 121 VAL HG2 H 0.98 0.03 2 1075 . 121 VAL C C 178.5 0.20 1 1076 . 122 LEU N N 121.0 0.25 1 1077 . 122 LEU H H 8.39 0.03 1 1078 . 122 LEU CA C 57.4 0.20 1 1079 . 122 LEU HA H 4.14 0.03 1 1080 . 122 LEU CB C 41.1 0.20 1 1081 . 122 LEU HB2 H 1.98 0.03 2 1082 . 122 LEU HB3 H 1.61 0.03 2 1083 . 122 LEU HG H 1.88 0.03 1 1084 . 122 LEU CD1 C 26.2 0.20 2 1085 . 122 LEU HD1 H 0.89 0.03 2 1086 . 122 LEU CD2 C 23.3 0.20 2 1087 . 122 LEU HD2 H 0.96 0.03 2 1088 . 122 LEU C C 179.7 0.20 1 1089 . 123 GLN N N 117.8 0.25 1 1090 . 123 GLN H H 8.70 0.03 1 1091 . 123 GLN CA C 57.5 0.20 1 1092 . 123 GLN HA H 4.24 0.03 1 1093 . 123 GLN CB C 27.7 0.20 1 1094 . 123 GLN HB2 H 2.24 0.03 2 1095 . 123 GLN HB3 H 2.17 0.03 2 1096 . 123 GLN CG C 33.6 0.20 1 1097 . 123 GLN HG2 H 2.63 0.03 2 1098 . 123 GLN HG3 H 2.44 0.03 2 1099 . 123 GLN HE21 H 7.34 0.03 1 1100 . 123 GLN HE22 H 6.86 0.03 1 1101 . 123 GLN C C 177.8 0.20 1 1102 . 124 ALA N N 122.5 0.25 1 1103 . 124 ALA H H 7.88 0.03 1 1104 . 124 ALA CA C 53.8 0.20 1 1105 . 124 ALA HA H 4.34 0.03 1 1106 . 124 ALA CB C 17.6 0.20 1 1107 . 124 ALA HB H 1.59 0.03 1 1108 . 125 HIS N N 117.4 0.25 1 1109 . 125 HIS H H 8.24 0.03 1 1110 . 125 HIS CA C 57.0 0.20 1 1111 . 125 HIS HA H 4.57 0.03 1 1112 . 125 HIS CB C 28.9 0.20 1 1113 . 125 HIS HB2 H 3.38 0.03 2 1114 . 125 HIS HB3 H 3.31 0.03 2 1115 . 125 HIS HD2 H 7.26 0.03 1 1116 . 125 HIS C C 176.0 0.20 1 1117 . 126 GLN N N 119.6 0.25 1 1118 . 126 GLN H H 8.24 0.03 1 1119 . 126 GLN CA C 55.1 0.20 1 1120 . 126 GLN HA H 4.26 0.03 1 1121 . 126 GLN CB C 29.2 0.20 1 1122 . 126 GLN HB2 H 2.38 0.03 2 1123 . 126 GLN HB3 H 2.21 0.03 2 1124 . 126 GLN HG2 H 2.58 0.03 2 1125 . 126 GLN HG3 H 2.50 0.03 2 1126 . 126 GLN C C 176.9 0.20 1 1127 . 127 ALA N N 123.0 0.25 1 1128 . 127 ALA H H 8.27 0.03 1 1129 . 127 ALA CA C 53.0 0.20 1 1130 . 127 ALA HA H 4.31 0.03 1 1131 . 127 ALA CB C 17.8 0.20 1 1132 . 127 ALA HB H 1.53 0.03 1 1133 . 127 ALA C C 178.8 0.20 1 1134 . 128 LYS N N 119.8 0.25 1 1135 . 128 LYS H H 8.07 0.03 1 1136 . 128 LYS CA C 57.1 0.20 1 1137 . 128 LYS HA H 4.27 0.03 1 1138 . 128 LYS CB C 32.1 0.20 1 1139 . 128 LYS HB2 H 1.96 0.03 1 1140 . 128 LYS HB3 H 1.96 0.03 1 1141 . 128 LYS CG C 24.3 0.20 1 1142 . 128 LYS HG2 H 1.76 0.03 2 1143 . 128 LYS HG3 H 1.60 0.03 2 1144 . 128 LYS CD C 28.4 0.20 1 1145 . 128 LYS HD2 H 1.51 0.03 1 1146 . 128 LYS HD3 H 1.51 0.03 1 1147 . 128 LYS HE2 H 3.05 0.03 1 1148 . 128 LYS HE3 H 3.05 0.03 1 1149 . 128 LYS C C 177.6 0.20 1 1150 . 129 GLU N N 120.1 0.25 1 1151 . 129 GLU H H 8.25 0.03 1 1152 . 129 GLU CA C 57.0 0.20 1 1153 . 129 GLU HA H 4.21 0.03 1 1154 . 129 GLU CB C 29.1 0.20 1 1155 . 129 GLU HB2 H 2.08 0.03 1 1156 . 129 GLU HB3 H 2.08 0.03 1 1157 . 129 GLU CG C 35.5 0.20 1 1158 . 129 GLU HG2 H 2.37 0.03 2 1159 . 129 GLU HG3 H 2.30 0.03 2 1160 . 129 GLU C C 177.2 0.20 1 1161 . 130 ALA N N 122.8 0.25 1 1162 . 130 ALA H H 8.20 0.03 1 1163 . 130 ALA CA C 52.9 0.20 1 1164 . 130 ALA HA H 4.32 0.03 1 1165 . 130 ALA CB C 18.2 0.20 1 1166 . 130 ALA HB H 1.51 0.03 1 1167 . 130 ALA C C 178.1 0.20 1 1168 . 131 ALA N N 121.5 0.25 1 1169 . 131 ALA H H 8.05 0.03 1 1170 . 131 ALA CA C 52.7 0.20 1 1171 . 131 ALA HA H 4.33 0.03 1 1172 . 131 ALA CB C 18.2 0.20 1 1173 . 131 ALA HB H 1.53 0.03 1 1174 . 131 ALA C C 178.3 0.20 1 1175 . 132 GLN N N 118.0 0.25 1 1176 . 132 GLN H H 8.12 0.03 1 1177 . 132 GLN CA C 55.5 0.20 1 1178 . 132 GLN HA H 4.32 0.03 1 1179 . 132 GLN CB C 28.8 0.20 1 1180 . 132 GLN HB2 H 2.15 0.03 2 1181 . 132 GLN HB3 H 2.22 0.03 2 1182 . 132 GLN HG2 H 2.50 0.03 1 1183 . 132 GLN HG3 H 2.50 0.03 1 1184 . 132 GLN C C 176.2 0.20 1 1185 . 133 LYS N N 120.9 0.25 1 1186 . 133 LYS H H 8.15 0.03 1 1187 . 133 LYS CA C 56.1 0.20 1 1188 . 133 LYS HA H 4.33 0.03 1 1189 . 133 LYS CB C 32.2 0.20 1 1190 . 133 LYS HB2 H 1.93 0.03 2 1191 . 133 LYS HB3 H 1.88 0.03 2 1192 . 133 LYS CG C 24.3 0.20 1 1193 . 133 LYS HG2 H 1.56 0.03 2 1194 . 133 LYS HG3 H 1.51 0.03 2 1195 . 133 LYS CD C 28.4 0.20 1 1196 . 133 LYS HD2 H 1.77 0.03 1 1197 . 133 LYS HD3 H 1.77 0.03 1 1198 . 133 LYS HE2 H 3.07 0.03 1 1199 . 133 LYS HE3 H 3.07 0.03 1 1200 . 133 LYS C C 176.2 0.20 1 1201 . 134 ALA N N 124.0 0.25 1 1202 . 134 ALA H H 8.17 0.03 1 1203 . 134 ALA CA C 52.0 0.20 1 1204 . 134 ALA HA H 4.40 0.03 1 1205 . 134 ALA CB C 18.5 0.20 1 1206 . 134 ALA HB H 1.49 0.03 1 1207 . 134 ALA C C 177.6 0.20 1 1208 . 135 VAL N N 118.6 0.25 1 1209 . 135 VAL H H 8.07 0.03 1 1210 . 135 VAL CA C 62.0 0.20 1 1211 . 135 VAL HA H 4.14 0.03 1 1212 . 135 VAL CB C 32.1 0.20 1 1213 . 135 VAL HB H 2.16 0.03 1 1214 . 135 VAL CG1 C 20.1 0.20 1 1215 . 135 VAL HG1 H 1.02 0.03 1 1216 . 135 VAL CG2 C 20.1 0.20 1 1217 . 135 VAL HG2 H 1.02 0.03 1 1218 . 135 VAL C C 175.8 0.20 1 1219 . 136 ASN N N 121.7 0.25 1 1220 . 136 ASN H H 8.48 0.03 1 1221 . 136 ASN CA C 52.7 0.20 1 1222 . 136 ASN HA H 4.82 0.03 1 1223 . 136 ASN CB C 38.4 0.20 1 1224 . 136 ASN HB2 H 2.96 0.03 2 1225 . 136 ASN HB3 H 2.87 0.03 2 1226 . 136 ASN C C 175.0 0.20 1 1227 . 137 SER N N 116.3 0.25 1 1228 . 137 SER H H 8.35 0.03 1 1229 . 137 SER CA C 57.9 0.20 1 1230 . 137 SER HA H 4.50 0.03 1 1231 . 137 SER CB C 63.3 0.20 1 1232 . 137 SER HB2 H 4.00 0.03 2 1233 . 137 SER HB3 H 3.96 0.03 2 1234 . 137 SER C C 174.1 0.20 1 1235 . 138 ALA N N 125.5 0.25 1 1236 . 138 ALA H H 8.43 0.03 1 1237 . 138 ALA CA C 52.2 0.20 1 1238 . 138 ALA HA H 4.49 0.03 1 1239 . 138 ALA CB C 18.6 0.20 1 1240 . 138 ALA HB H 1.51 0.03 1 1241 . 138 ALA C C 177.7 0.20 1 1242 . 139 THR N N 111.5 0.25 1 1243 . 139 THR H H 8.11 0.03 1 1244 . 139 THR CA C 61.3 0.20 1 1245 . 139 THR HA H 4.43 0.03 1 1246 . 139 THR CB C 69.1 0.20 1 1247 . 139 THR HB H 4.37 0.03 1 1248 . 139 THR CG2 C 21.2 0.20 1 1249 . 139 THR HG2 H 1.30 0.03 1 1250 . 139 THR C C 174.9 0.20 1 1251 . 140 GLY N N 110.8 0.25 1 1252 . 140 GLY H H 8.37 0.03 1 1253 . 140 GLY CA C 44.6 0.20 1 1254 . 140 GLY HA2 H 4.07 0.03 2 1255 . 140 GLY HA3 H 4.03 0.03 2 1256 . 140 GLY C C 173.4 0.20 1 1257 . 141 VAL N N 120.3 0.25 1 1258 . 141 VAL H H 8.00 0.03 1 1259 . 141 VAL CA C 57.9 0.20 1 1260 . 141 VAL HA H 4.53 0.03 1 1261 . 141 VAL HB H 2.16 0.03 1 1262 . 141 VAL HG1 H 1.07 0.03 2 1263 . 141 VAL HG2 H 0.99 0.03 2 1264 . 141 VAL C C 174.2 0.20 1 1265 . 142 PRO CD C 50.1 0.20 1 1266 . 142 PRO CA C 62.6 0.20 1 1267 . 142 PRO CB C 31.6 0.20 1 1268 . 142 PRO CG C 26.4 0.20 1 1269 . 142 PRO C C 176.6 0.20 1 1270 . 143 THR N N 115.3 0.25 1 1271 . 143 THR H H 8.38 0.03 1 1272 . 143 THR CA C 61.2 0.20 1 1273 . 143 THR HA H 4.42 0.03 1 1274 . 143 THR CB C 69.3 0.20 1 1275 . 143 THR HB H 4.30 0.03 1 1276 . 143 THR CG2 C 21.2 0.20 1 1277 . 143 THR HG2 H 1.32 0.03 1 1278 . 143 THR C C 173.5 0.20 1 1279 . 144 VAL N N 125.9 0.25 1 1280 . 144 VAL H H 7.79 0.03 1 1281 . 144 VAL HA H 4.14 0.03 1 1282 . 144 VAL HB H 2.15 0.03 1 1283 . 144 VAL HG1 H 0.97 0.03 1 1284 . 144 VAL HG2 H 0.97 0.03 1 1285 . 144 VAL C C 180.5 0.20 1 stop_ save_ ######################## # Coupling constants # ######################## save_J_values _Saveframe_category coupling_constants _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H . _Mol_system_component_name 'Polyadenylate-binding protein 1' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 3 LEU HA 3 LEU H 7.1 7.05 7.1 . 2 3JHNHA 4 GLY HA 4 GLY H 7.8 7.8 7.86 . 3 3JHNHA 5 SER HA 5 SER H 7.9 7.86 7.91 . 4 3JHNHA 12 ALA HA 12 ALA H 7.1 6.88 7.39 . 5 3JHNHA 13 VAL HA 13 VAL H 7.9 7.9 7.99 . 6 3JHNHA 14 ARG HA 14 ARG H 7.1 7.04 7.08 . 7 3JHNHA 15 THR HA 15 THR H 8.3 8.33 8.37 . 8 3JHNHA 16 VAL HA 16 VAL H 8.7 8.69 8.79 . 9 3JHNHA 18 GLN HA 18 GLN H 7.2 7.25 7.18 . 10 3JHNHA 19 TYR HA 19 TYR H 4.4 4.42 4.41 . 11 3JHNHA 20 LYS HA 20 LYS H 7.4 7.5 7.28 . 12 3JHNHA 21 TYR HA 21 TYR H 6.3 6.29 6.3 . 13 3JHNHA 22 ALA HA 22 ALA H 6.7 6.67 6.71 . 14 3JHNHA 23 ALA HA 23 ALA H 5.8 5.56 5.98 . 15 3JHNHA 24 GLY HA 24 GLY H 7.8 7.79 7.91 . 16 3JHNHA 25 VAL HA 25 VAL H 8.3 8.24 8.3 . 17 3JHNHA 26 ARG HA 26 ARG H 6.9 6.91 6.89 . 18 3JHNHA 27 ASN HA 27 ASN H 7.1 7.12 7.13 . 19 3JHNHA 29 GLN HA 29 GLN H 7.1 7.06 7.05 . 20 3JHNHA 30 GLN HA 30 GLN H 7.1 7 7.19 . 21 3JHNHA 32 LEU HA 32 LEU H 7.0 6.98 7.1 . 22 3JHNHA 33 ASN HA 33 ASN H 7.9 7.93 7.94 . 23 3JHNHA 34 ALA HA 34 ALA H 6.4 6.38 6.46 . 24 3JHNHA 35 GLN HA 35 GLN H 7.8 7.76 7.79 . 25 3JHNHA 37 GLN HA 37 GLN H 7.3 7.25 7.3 . 26 3JHNHA 38 VAL HA 38 VAL H 7.7 7.75 7.57 . 27 3JHNHA 39 THR HA 39 THR H 8.2 8.16 8.19 . 28 3JHNHA 40 MET HA 40 MET H 7.5 7.42 7.56 . 29 3JHNHA 44 ALA HA 44 ALA H 5.9 5.86 5.87 . 30 3JHNHA 45 VAL HA 45 VAL H 7.8 7.72 7.79 . 31 3JHNHA 46 HIS HA 46 HIS H 8.2 8.18 8.19 . 32 3JHNHA 47 VAL HA 47 VAL H 8.4 8.37 8.36 . 33 3JHNHA 48 GLN HA 48 GLN H 6.9 6.87 6.89 . 34 3JHNHA 49 GLY HA 49 GLY H 7.4 7.31 7.51 . 35 3JHNHA 50 GLN HA 50 GLN H 8.6 8.55 8.65 . 36 3JHNHA 51 GLU HA 51 GLU H 6.0 5.91 6.02 . 37 3JHNHA 53 LEU HA 53 LEU H 7.0 6.98 7.1 . 38 3JHNHA 55 ALA HA 55 ALA H 2.8 2.75 2.78 . 39 3JHNHA 56 SER HA 56 SER H 4.3 4.5 4.16 . 40 3JHNHA 57 MET HA 57 MET H 5.6 5.61 5.68 . 41 3JHNHA 58 LEU HA 58 LEU H 5.3 5.23 5.44 . 42 3JHNHA 59 ALA HA 59 ALA H 3.5 3.47 3.59 . 43 3JHNHA 60 SER HA 60 SER H 6.8 6.5 7.18 . 44 3JHNHA 61 ALA HA 61 ALA H 7.8 7.71 7.89 . 45 3JHNHA 65 GLU HA 65 GLU H 7.8 7.94 7.75 . 46 3JHNHA 69 MET HA 69 MET H 4.0 3.73 4.34 . 47 3JHNHA 70 LEU HA 70 LEU H 5.7 5.86 5.5 . 48 3JHNHA 73 ARG HA 73 ARG H 8.4 8.27 8.52 . 49 3JHNHA 74 LEU HA 74 LEU H 4.3 4.5 4.16 . 50 3JHNHA 77 LEU HA 77 LEU H 6.9 7 6.81 . 51 3JHNHA 78 ILE HA 78 ILE H 5.9 5.85 5.88 . 52 3JHNHA 79 GLN HA 79 GLN H 3.0 2.77 3.31 . 53 3JHNHA 80 ALA HA 80 ALA H 5.1 5 5.19 . 54 3JHNHA 88 LYS HA 88 LYS H 5.0 4.9 5.07 . 55 3JHNHA 89 ILE HA 89 ILE H 4.5 4.52 4.48 . 56 3JHNHA 90 THR HA 90 THR H 3.3 3.06 3.56 . 57 3JHNHA 91 GLY HA 91 GLY H 3.7 3.24 4.12 . 58 3JHNHA 92 MET HA 92 MET H 5.5 5.38 5.69 . 59 3JHNHA 94 LEU HA 94 LEU H 3.8 3.63 3.89 . 60 3JHNHA 95 GLU HA 95 GLU H 6.2 6.1 6.28 . 61 3JHNHA 96 ILE HA 96 ILE H 6.4 6.39 6.45 . 62 3JHNHA 97 ASP HA 97 ASP H 2.4 2.34 2.53 . 63 3JHNHA 99 SER HA 99 SER H 4.6 4.51 4.62 . 64 3JHNHA 100 GLU HA 100 GLU H 6.9 6.86 6.98 . 65 3JHNHA 101 LEU HA 101 LEU H 3.9 3.87 3.99 . 66 3JHNHA 103 HIS HA 103 HIS H 4.9 4.79 5.04 . 67 3JHNHA 104 MET HA 104 MET H 4.5 4.59 4.52 . 68 3JHNHA 105 LEU HA 105 LEU H 5.4 5.32 5.52 . 69 3JHNHA 106 GLU HA 106 GLU H 8.4 8.35 8.36 . 70 3JHNHA 107 SER HA 107 SER H 8.8 8.63 8.89 . 71 3JHNHA 110 SER HA 110 SER H 6.4 6.36 6.43 . 72 3JHNHA 111 LEU HA 111 LEU H 4.3 4.08 4.65 . 73 3JHNHA 113 SER HA 113 SER H 3.7 3.59 3.81 . 74 3JHNHA 114 LYS HA 114 LYS H 4.4 4.36 4.38 . 75 3JHNHA 115 VAL HA 115 VAL H 4.7 4.68 4.79 . 76 3JHNHA 116 ASP HA 116 ASP H 3.4 3.35 3.45 . 77 3JHNHA 117 GLU HA 117 GLU H 4.6 4.38 4.75 . 78 3JHNHA 118 ALA HA 118 ALA H 4.8 4.74 4.84 . 79 3JHNHA 119 VAL HA 119 VAL H 3.5 3.3 3.64 . 80 3JHNHA 120 ALA HA 120 ALA H 4.9 4.54 5.26 . 81 3JHNHA 121 VAL HA 121 VAL H 5.4 5.38 5.46 . 82 3JHNHA 122 LEU HA 122 LEU H 4.1 4.15 4.14 . 83 3JHNHA 123 GLN HA 123 GLN H 5.4 5.37 5.33 . 84 3JHNHA 124 ALA HA 124 ALA H 5.6 5.61 5.68 . 85 3JHNHA 126 GLN HA 126 GLN H 5.5 4.95 6.05 . 86 3JHNHA 127 ALA HA 127 ALA H 6.5 6.48 6.51 . 87 3JHNHA 128 LYS HA 128 LYS H 6.6 6.57 6.62 . 88 3JHNHA 129 GLU HA 129 GLU H 5.5 5.32 5.61 . 89 3JHNHA 130 ALA HA 130 ALA H 5.6 5.03 6.31 . 90 3JHNHA 131 ALA HA 131 ALA H 6.0 6 6.08 . 91 3JHNHA 132 GLN HA 132 GLN H 6.9 6.97 6.87 . 92 3JHNHA 133 LYS HA 133 LYS H 5.8 5.85 5.75 . 93 3JHNHA 134 ALA HA 134 ALA H 6.4 6.39 6.41 . 94 3JHNHA 135 VAL HA 135 VAL H 7.6 7.56 7.59 . 95 3JHNHA 136 ASN HA 136 ASN H 6.2 6.21 6.26 . 96 3JHNHA 137 SER HA 137 SER H 7.5 7.34 7.67 . 97 3JHNHA 138 ALA HA 138 ALA H 5.9 5.62 6.15 . 98 3JHNHA 139 THR HA 139 THR H 8.8 8.79 8.77 . 99 3JHNHA 140 GLY HA 140 GLY H 7.9 7.88 7.87 . 100 3JHNHA 141 VAL HA 141 VAL H 7.3 7.54 7.07 . 101 3JHNHA 143 THR HA 143 THR H 7.9 7.85 7.86 . stop_ save_