data_5038 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Assignments for human ubiquitin-conjugating enzyme 2b (HsUbc2b) ; _BMRB_accession_number 5038 _BMRB_flat_file_name bmr5038.str _Entry_type original _Submission_date 2001-05-31 _Accession_date 2001-05-31 _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 Miura Takaaki . . 2 Klaus Werner . . 3 Ross Alfred . . 4 Guntert Peter . . 5 Senn Hans . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 888 "13C chemical shifts" 479 "15N chemical shifts" 150 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-06-11 update author 'correction of cs of 4 PRO CG' 2001-06-08 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The NMR Structure of the Class I Human Ubiquitin-conjugating Enzyme 2b' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21882792 _PubMed_ID 11885984 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miura Takaaki . . 2 Klaus Werner . . 3 Ross Alfred . . 4 Guntert Peter . . 5 Senn Hans . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 22 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 89 _Page_last 92 _Year 2002 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Miura T, Klaus W, Gsell B, Miyamoto C, Senn H. Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution. J Mol Biol. 1999 Jul 2;290(1):213-28. ; _Citation_title 'Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10388568 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miura T . . 2 Klaus W . . 3 Gsell B . . 4 Miyamoto C . . 5 Senn H . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 290 _Journal_issue 1 _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 213 _Page_last 228 _Year 1999 _Details ; Ubiquitin-conjugating enzymes (Ubc) are involved in ubiquitination of proteins in the protein degradation pathway of eukaryotic cells. Ubc transfers the ubiquitin (Ub) molecules to target proteins by forming a thioester bond between their active site cysteine residue and the C-terminal glycine residue of ubiquitin. Here, we report on the NMR assignment and secondary structure of class I human ubiquitin-conjugating enzyme 2b (HsUbc2b). Chemical shift perturbation studies allowed us to map the contact area and binding interface between ubiquitin and HsUbc2b by1H-15N HSQC NMR spectroscopy. The serine mutant of the active site Cys88 of HsUbc2b was employed to obtain a relatively stable covalent ubiquitin complex of HsUbc2b(C88S). Changes in chemical shifts of amide protons and nitrogen atoms induced by the formation of the covalent complex were measured by preparing two segmentally labeled complexes with either ubiquitin or HsUbc2b(C88S)15N-labeled. In ubiquitin, the interaction is primarily sensed by the C-terminal segment Val70 - Gly76, and residues Lys48 and Gln49. The surface area on ubiquitin, as defined by these residues, overlaps partially with the presumed binding site with ubiquitin-activating enzyme (E1). In HsUbc2b, most of the affected residues cluster in the vicinity of the active site, namely, around the active site Cys88 itself, the second alpha-helix, and the flexible loop which connects helices alpha2 and alpha3 and which is adjacent to the active site. An additional site on HsUbc2b for a weak interaction with ubiquitin could be detected in a titration study where the two proteins were not covalently linked. This site is located on the backside of HsUbc2b opposite to the active site and is part of the beta-sheet. The covalent and non-covalent interaction sites are clearly separated on the HsUbc2b surface, while no such clear-cut segregation of the interaction area was observed on ubiquitin. ; save_ ################################## # Molecular system description # ################################## save_system_Ubc2b _Saveframe_category molecular_system _Mol_system_name HsUbc2b _Abbreviation_common Ubc2b _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Ubc2b $Ubc2b stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Ubc2b _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ubiquitin-conjugating enzyme 2b' _Abbreviation_common Ubc2b _Molecular_mass 17312 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 152 _Mol_residue_sequence ; MSTPARRRLMRDFKRLQEDP PVGVSGAPSENNIMQWNAVI FGPEGTPFEDGTFKLVIEFS EEYPNKPPTVRFLSKMFHPN VYADGSICLDILQNRWSPTY DVSSILTSIQSLLDEPNPNS PANSQAAQLYQENKREYEKR VSAIVEQSWNDS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 THR 4 PRO 5 ALA 6 ARG 7 ARG 8 ARG 9 LEU 10 MET 11 ARG 12 ASP 13 PHE 14 LYS 15 ARG 16 LEU 17 GLN 18 GLU 19 ASP 20 PRO 21 PRO 22 VAL 23 GLY 24 VAL 25 SER 26 GLY 27 ALA 28 PRO 29 SER 30 GLU 31 ASN 32 ASN 33 ILE 34 MET 35 GLN 36 TRP 37 ASN 38 ALA 39 VAL 40 ILE 41 PHE 42 GLY 43 PRO 44 GLU 45 GLY 46 THR 47 PRO 48 PHE 49 GLU 50 ASP 51 GLY 52 THR 53 PHE 54 LYS 55 LEU 56 VAL 57 ILE 58 GLU 59 PHE 60 SER 61 GLU 62 GLU 63 TYR 64 PRO 65 ASN 66 LYS 67 PRO 68 PRO 69 THR 70 VAL 71 ARG 72 PHE 73 LEU 74 SER 75 LYS 76 MET 77 PHE 78 HIS 79 PRO 80 ASN 81 VAL 82 TYR 83 ALA 84 ASP 85 GLY 86 SER 87 ILE 88 CYS 89 LEU 90 ASP 91 ILE 92 LEU 93 GLN 94 ASN 95 ARG 96 TRP 97 SER 98 PRO 99 THR 100 TYR 101 ASP 102 VAL 103 SER 104 SER 105 ILE 106 LEU 107 THR 108 SER 109 ILE 110 GLN 111 SER 112 LEU 113 LEU 114 ASP 115 GLU 116 PRO 117 ASN 118 PRO 119 ASN 120 SER 121 PRO 122 ALA 123 ASN 124 SER 125 GLN 126 ALA 127 ALA 128 GLN 129 LEU 130 TYR 131 GLN 132 GLU 133 ASN 134 LYS 135 ARG 136 GLU 137 TYR 138 GLU 139 LYS 140 ARG 141 VAL 142 SER 143 ALA 144 ILE 145 VAL 146 GLU 147 GLN 148 SER 149 TRP 150 ASN 151 ASP 152 SER 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 17443 UBIQUITIN-CONJUGATING_ENZYME_E2_B 100.00 152 100.00 100.00 2.16e-107 PDB 1JAS Hsubc2b 100.00 152 100.00 100.00 2.16e-107 PDB 2Y4W "Solution Structure Of Human Ubiquitin Conjugating Enzyme Rad6b" 100.00 152 100.00 100.00 2.16e-107 PDB 2YB6 "Native Human Rad6" 100.00 152 100.00 100.00 2.16e-107 PDB 2YBF "Complex Of Rad18 (Rad6 Binding Domain) With Rad6b" 100.00 152 100.00 100.00 2.16e-107 DBJ BAB26934 "unnamed protein product [Mus musculus]" 100.00 152 100.00 100.00 2.16e-107 DBJ BAB27570 "unnamed protein product [Mus musculus]" 100.00 152 99.34 99.34 1.51e-106 DBJ BAE28135 "unnamed protein product [Mus musculus]" 100.00 152 100.00 100.00 2.16e-107 DBJ BAE40998 "unnamed protein product [Mus musculus]" 100.00 152 100.00 100.00 2.16e-107 DBJ BAE88681 "unnamed protein product [Macaca fascicularis]" 100.00 152 100.00 100.00 2.16e-107 EMBL CAA37339 "E2 protein [Homo sapiens]" 100.00 152 100.00 100.00 2.16e-107 EMBL CAA65602 "ubiquitin-conjugating enzym [Mus musculus]" 100.00 152 100.00 100.00 2.16e-107 EMBL CAG28562 "UBE2B [Homo sapiens]" 100.00 152 100.00 100.00 2.16e-107 EMBL CAJ83014 "ubiquitin-conjugating enzyme E2B (RAD6 homolog) [Xenopus (Silurana) tropicalis]" 94.08 143 98.60 99.30 1.08e-98 GB AAA21087 "ubiquitin conjugating-protein [Rattus norvegicus]" 100.00 152 100.00 100.00 2.16e-107 GB AAA31492 "ubiquitin conjugating-protein [Oryctolagus cuniculus]" 100.00 152 100.00 100.00 2.16e-107 GB AAA35982 "HHR6B (Human homologue of yeast RAD 6); putative [Homo sapiens]" 100.00 152 100.00 100.00 2.16e-107 GB AAB60669 "14 kDa ubiquitin conjugating enzyme [Rattus norvegicus]" 100.00 152 100.00 100.00 2.16e-107 GB AAC52884 "E214K [Mus musculus]" 100.00 152 100.00 100.00 2.16e-107 PRF 2016220A "ubiquitin-conjugating enzyme:ISOTYPE=E2-14k" 100.00 152 100.00 100.00 2.16e-107 REF NP_001005124 "ubiquitin-conjugating enzyme E2 B [Xenopus (Silurana) tropicalis]" 100.00 152 98.68 99.34 8.14e-106 REF NP_001032536 "ubiquitin-conjugating enzyme E2 B [Bos taurus]" 100.00 152 100.00 100.00 2.16e-107 REF NP_001075765 "ubiquitin-conjugating enzyme E2 B [Oryctolagus cuniculus]" 100.00 152 100.00 100.00 2.16e-107 REF NP_001085320 "ubiquitin-conjugating enzyme E2B [Xenopus laevis]" 100.00 152 98.68 99.34 8.14e-106 REF NP_001181362 "ubiquitin-conjugating enzyme E2 B [Macaca mulatta]" 100.00 152 100.00 100.00 2.16e-107 SP P63146 "RecName: Full=Ubiquitin-conjugating enzyme E2 B; AltName: Full=RAD6 homolog B; Short=HR6B; Short=hHR6B; AltName: Full=Ubiquitin" 100.00 152 100.00 100.00 2.16e-107 SP P63147 "RecName: Full=Ubiquitin-conjugating enzyme E2 B; AltName: Full=E214K; AltName: Full=RAD6 homolog B; Short=HR6B; Short=mHR6B; Al" 100.00 152 100.00 100.00 2.16e-107 SP P63148 "RecName: Full=Ubiquitin-conjugating enzyme E2 B; AltName: Full=RAD6 homolog B; Short=HR6B; AltName: Full=Ubiquitin carrier prot" 100.00 152 100.00 100.00 2.16e-107 SP P63149 "RecName: Full=Ubiquitin-conjugating enzyme E2 B; AltName: Full=RAD6 homolog B; Short=HR6B; AltName: Full=Ubiquitin carrier prot" 100.00 152 100.00 100.00 2.16e-107 SP Q32P99 "RecName: Full=Ubiquitin-conjugating enzyme E2 B; AltName: Full=Ubiquitin carrier protein B; AltName: Full=Ubiquitin-protein lig" 100.00 152 100.00 100.00 2.16e-107 TPG DAA27462 "TPA: ubiquitin-conjugating enzyme E2 B [Bos taurus]" 100.00 152 100.00 100.00 2.16e-107 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Ubc2b 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 $Ubc2b 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Ubc2b 1.0 mM '[U-13C; U-15N]' 'ammonium acetate' 75 mM [U-2H] 'ammonium sulfate' 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_nmrPipe _Saveframe_category software _Name nmrPipe _Version 1.7 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ####################### # Sample conditions # ####################### save_cond_set_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.7 0.05 n/a temperature 308 0.01 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond_set_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Ubc2b _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 SER CA C 59.0 0.20 1 2 . 2 SER HA H 4.42 0.05 1 3 . 2 SER CB C 63.7 0.20 1 4 . 2 SER HB2 H 3.90 0.05 1 5 . 2 SER HB3 H 3.90 0.05 1 6 . 3 THR N N 111.9 0.15 1 7 . 3 THR H H 7.32 0.05 1 8 . 3 THR CA C 59.0 0.20 1 9 . 3 THR HA H 4.95 0.05 1 10 . 3 THR CB C 69.1 0.20 1 11 . 3 THR HB H 4.69 0.05 1 12 . 3 THR HG2 H 1.28 0.05 1 13 . 3 THR CG2 C 22.4 0.20 1 14 . 4 PRO CD C 50.8 0.20 1 15 . 4 PRO CA C 66.3 0.20 1 16 . 4 PRO HA H 4.24 0.05 1 17 . 4 PRO CB C 31.7 0.20 1 18 . 4 PRO HB2 H 2.24 0.05 1 19 . 4 PRO HB3 H 2.46 0.05 1 20 . 4 PRO CG C 27.9 0.20 1 21 . 4 PRO HG2 H 1.99 0.05 2 22 . 4 PRO HG3 H 1.84 0.05 2 23 . 4 PRO HD2 H 4.09 0.05 1 24 . 4 PRO HD3 H 3.94 0.05 1 25 . 5 ALA N N 120.6 0.15 1 26 . 5 ALA H H 8.90 0.05 1 27 . 5 ALA CA C 56.2 0.20 1 28 . 5 ALA HA H 4.22 0.05 1 29 . 5 ALA HB H 1.72 0.05 1 30 . 5 ALA CB C 20.7 0.20 1 31 . 6 ARG N N 116.3 0.15 1 32 . 6 ARG H H 7.46 0.05 1 33 . 6 ARG CA C 60.1 0.20 1 34 . 6 ARG HA H 3.88 0.05 1 35 . 6 ARG CB C 30.3 0.20 1 36 . 6 ARG HB2 H 0.60 0.05 2 37 . 6 ARG HB3 H 1.42 0.05 2 38 . 6 ARG HD2 H 3.30 0.05 1 39 . 6 ARG HD3 H 3.30 0.05 1 40 . 7 ARG N N 117.5 0.15 1 41 . 7 ARG H H 8.27 0.05 1 42 . 7 ARG CA C 60.0 0.20 1 43 . 7 ARG HA H 4.12 0.05 1 44 . 7 ARG CB C 30.6 0.20 1 45 . 7 ARG HB2 H 1.92 0.05 1 46 . 7 ARG HB3 H 1.92 0.05 1 47 . 7 ARG CG C 29.2 0.20 1 48 . 7 ARG HG2 H 1.86 0.05 1 49 . 7 ARG HG3 H 1.60 0.05 1 50 . 7 ARG CD C 43.7 0.20 1 51 . 7 ARG HD2 H 3.29 0.05 2 52 . 7 ARG HD3 H 3.16 0.05 2 53 . 8 ARG N N 120.9 0.15 1 54 . 8 ARG H H 8.07 0.05 1 55 . 8 ARG CA C 57.9 0.20 1 56 . 8 ARG HA H 4.22 0.05 1 57 . 8 ARG CB C 29.2 0.20 1 58 . 8 ARG HB2 H 2.10 0.05 1 59 . 8 ARG HB3 H 2.10 0.05 1 60 . 8 ARG CD C 41.5 0.20 1 61 . 8 ARG HD2 H 3.27 0.05 2 62 . 8 ARG HD3 H 3.54 0.05 2 63 . 9 LEU N N 120.7 0.15 1 64 . 9 LEU H H 8.66 0.05 1 65 . 9 LEU CA C 58.5 0.20 1 66 . 9 LEU HA H 4.13 0.05 1 67 . 9 LEU CB C 42.5 0.20 1 68 . 9 LEU HB2 H 2.04 0.05 1 69 . 9 LEU HB3 H 1.31 0.05 1 70 . 9 LEU CG C 27.7 0.20 1 71 . 9 LEU HG H 1.42 0.05 1 72 . 9 LEU HD1 H 0.44 0.05 1 73 . 9 LEU HD2 H -0.75 0.05 1 74 . 9 LEU CD1 C 26.0 0.20 1 75 . 9 LEU CD2 C 21.4 0.20 1 76 . 10 MET N N 117.8 0.15 1 77 . 10 MET H H 8.07 0.05 1 78 . 10 MET CA C 58.0 0.20 1 79 . 10 MET HA H 4.64 0.05 1 80 . 10 MET CB C 31.6 0.20 1 81 . 10 MET HB2 H 2.34 0.05 1 82 . 10 MET HB3 H 2.29 0.05 1 83 . 10 MET CG C 32.9 0.20 1 84 . 10 MET HG2 H 2.81 0.05 2 85 . 10 MET HG3 H 2.74 0.05 2 86 . 10 MET HE H 2.13 0.05 1 87 . 10 MET CE C 16.9 0.20 1 88 . 11 ARG N N 122.7 0.15 1 89 . 11 ARG H H 7.80 0.05 1 90 . 11 ARG CA C 60.0 0.20 1 91 . 11 ARG HA H 4.23 0.05 1 92 . 11 ARG CB C 29.6 0.20 1 93 . 11 ARG HB2 H 2.24 0.05 1 94 . 11 ARG HB3 H 2.24 0.05 1 95 . 11 ARG CG C 27.7 0.20 1 96 . 11 ARG HG2 H 2.03 0.05 2 97 . 11 ARG HG3 H 1.73 0.05 2 98 . 11 ARG CD C 43.9 0.20 1 99 . 11 ARG HD2 H 3.29 0.05 1 100 . 11 ARG HD3 H 3.29 0.05 1 101 . 12 ASP N N 122.3 0.15 1 102 . 12 ASP H H 9.38 0.05 1 103 . 12 ASP CA C 57.9 0.20 1 104 . 12 ASP HA H 4.49 0.05 1 105 . 12 ASP CB C 40.9 0.20 1 106 . 12 ASP HB2 H 3.31 0.05 2 107 . 12 ASP HB3 H 2.71 0.05 2 108 . 13 PHE N N 120.5 0.15 1 109 . 13 PHE H H 8.94 0.05 1 110 . 13 PHE CA C 59.3 0.20 1 111 . 13 PHE HA H 4.85 0.05 1 112 . 13 PHE CB C 38.5 0.20 1 113 . 13 PHE HB2 H 3.63 0.05 1 114 . 13 PHE HB3 H 3.42 0.05 1 115 . 13 PHE HD1 H 7.25 0.05 1 116 . 13 PHE HD2 H 7.25 0.05 1 117 . 13 PHE HE1 H 7.36 0.05 1 118 . 13 PHE HE2 H 7.36 0.05 1 119 . 13 PHE HZ H 7.23 0.05 1 120 . 14 LYS N N 120.3 0.15 1 121 . 14 LYS H H 8.11 0.05 1 122 . 14 LYS CA C 59.7 0.20 1 123 . 14 LYS HA H 3.84 0.05 1 124 . 14 LYS CB C 32.1 0.20 1 125 . 14 LYS HB2 H 2.03 0.05 1 126 . 14 LYS HB3 H 2.03 0.05 1 127 . 14 LYS CG C 24.9 0.20 1 128 . 14 LYS HG2 H 1.56 0.05 2 129 . 14 LYS HG3 H 1.43 0.05 2 130 . 14 LYS CD C 29.2 0.20 1 131 . 14 LYS HD2 H 1.75 0.05 1 132 . 14 LYS HD3 H 1.75 0.05 1 133 . 14 LYS CE C 42.0 0.20 1 134 . 14 LYS HE2 H 3.01 0.05 1 135 . 14 LYS HE3 H 3.01 0.05 1 136 . 15 ARG N N 117.2 0.15 1 137 . 15 ARG H H 8.05 0.05 1 138 . 15 ARG CA C 59.4 0.20 1 139 . 15 ARG HA H 4.14 0.05 1 140 . 15 ARG CB C 30.0 0.20 1 141 . 15 ARG HB2 H 2.01 0.05 1 142 . 15 ARG HB3 H 2.01 0.05 1 143 . 15 ARG CG C 27.9 0.20 1 144 . 15 ARG HG2 H 1.88 0.05 1 145 . 15 ARG HG3 H 1.88 0.05 1 146 . 15 ARG CD C 43.2 0.20 1 147 . 15 ARG HD2 H 3.35 0.05 1 148 . 15 ARG HD3 H 3.35 0.05 1 149 . 16 LEU N N 119.5 0.15 1 150 . 16 LEU H H 7.65 0.05 1 151 . 16 LEU CA C 57.6 0.20 1 152 . 16 LEU HA H 4.06 0.05 1 153 . 16 LEU CB C 42.6 0.20 1 154 . 16 LEU HB2 H 1.87 0.05 1 155 . 16 LEU HB3 H 2.12 0.05 1 156 . 16 LEU CG C 27.6 0.20 1 157 . 16 LEU HG H 1.88 0.05 1 158 . 16 LEU HD1 H 1.07 0.05 1 159 . 16 LEU HD2 H 1.07 0.05 1 160 . 16 LEU CD1 C 25.0 0.20 1 161 . 16 LEU CD2 C 26.4 0.20 1 162 . 17 GLN N N 114.5 0.15 1 163 . 17 GLN H H 7.93 0.05 1 164 . 17 GLN CA C 57.9 0.20 1 165 . 17 GLN HA H 4.04 0.05 1 166 . 17 GLN CB C 29.6 0.20 1 167 . 17 GLN HB2 H 1.98 0.05 1 168 . 17 GLN HB3 H 1.98 0.05 1 169 . 17 GLN CG C 34.5 0.20 1 170 . 17 GLN HG2 H 1.98 0.05 1 171 . 17 GLN HG3 H 1.98 0.05 1 172 . 18 GLU N N 116.8 0.15 1 173 . 18 GLU H H 7.98 0.05 1 174 . 18 GLU CA C 58.1 0.20 1 175 . 18 GLU HA H 4.12 0.05 1 176 . 18 GLU CB C 30.4 0.20 1 177 . 18 GLU HB2 H 2.01 0.05 1 178 . 18 GLU HB3 H 2.01 0.05 1 179 . 18 GLU CG C 36.7 0.20 1 180 . 18 GLU HG2 H 2.46 0.05 2 181 . 18 GLU HG3 H 2.28 0.05 2 182 . 19 ASP N N 117.0 0.15 1 183 . 19 ASP H H 7.84 0.05 1 184 . 19 ASP CA C 52.1 0.20 1 185 . 19 ASP HA H 5.02 0.05 1 186 . 19 ASP CB C 41.2 0.20 1 187 . 19 ASP HB2 H 2.80 0.05 2 188 . 19 ASP HB3 H 2.43 0.05 2 189 . 20 PRO CD C 50.0 0.20 1 190 . 20 PRO CA C 61.8 0.20 1 191 . 20 PRO HA H 4.85 0.05 1 192 . 20 PRO HB2 H 2.12 0.05 1 193 . 20 PRO HB3 H 2.12 0.05 1 194 . 20 PRO CG C 27.7 0.20 1 195 . 20 PRO HG2 H 2.12 0.05 1 196 . 20 PRO HG3 H 2.12 0.05 1 197 . 20 PRO HD2 H 3.60 0.05 1 198 . 20 PRO HD3 H 3.44 0.05 1 199 . 21 PRO CD C 50.8 0.20 1 200 . 21 PRO CA C 61.8 0.20 1 201 . 21 PRO HA H 4.59 0.05 1 202 . 21 PRO CB C 31.8 0.20 1 203 . 21 PRO HB2 H 1.73 0.05 1 204 . 21 PRO HB3 H 2.38 0.05 1 205 . 21 PRO CG C 27.9 0.20 1 206 . 21 PRO HG2 H 2.02 0.05 1 207 . 21 PRO HG3 H 1.85 0.05 1 208 . 21 PRO HD2 H 3.44 0.05 1 209 . 21 PRO HD3 H 4.11 0.05 1 210 . 22 VAL N N 121.0 0.15 1 211 . 22 VAL H H 8.31 0.05 1 212 . 22 VAL CA C 64.1 0.20 1 213 . 22 VAL HA H 3.87 0.05 1 214 . 22 VAL CB C 32.0 0.20 1 215 . 22 VAL HB H 1.99 0.05 1 216 . 22 VAL HG1 H 0.98 0.05 1 217 . 22 VAL HG2 H 1.10 0.05 1 218 . 22 VAL CG1 C 20.8 0.20 1 219 . 22 VAL CG2 C 21.9 0.20 1 220 . 23 GLY N N 113.2 0.15 1 221 . 23 GLY H H 8.65 0.05 1 222 . 23 GLY CA C 46.3 0.20 1 223 . 23 GLY HA2 H 4.17 0.05 2 224 . 23 GLY HA3 H 3.61 0.05 2 225 . 24 VAL N N 112.0 0.15 1 226 . 24 VAL H H 7.31 0.05 1 227 . 24 VAL CA C 59.3 0.20 1 228 . 24 VAL HA H 5.22 0.05 1 229 . 24 VAL CB C 35.5 0.20 1 230 . 24 VAL HB H 2.04 0.05 1 231 . 24 VAL HG1 H 0.85 0.05 1 232 . 24 VAL HG2 H 0.78 0.05 1 233 . 24 VAL CG1 C 22.7 0.20 1 234 . 24 VAL CG2 C 20.5 0.20 1 235 . 25 SER N N 114.9 0.15 1 236 . 25 SER H H 8.60 0.05 1 237 . 25 SER CA C 57.5 0.20 1 238 . 25 SER HA H 4.72 0.05 1 239 . 25 SER CB C 65.5 0.20 1 240 . 25 SER HB2 H 3.92 0.05 2 241 . 25 SER HB3 H 3.82 0.05 2 242 . 26 GLY N N 107.0 0.15 1 243 . 26 GLY H H 7.96 0.05 1 244 . 26 GLY CA C 46.3 0.20 1 245 . 26 GLY HA2 H 4.03 0.05 1 246 . 26 GLY HA3 H 4.87 0.05 1 247 . 27 ALA N N 118.8 0.15 1 248 . 27 ALA H H 8.54 0.05 1 249 . 27 ALA CA C 50.8 0.20 1 250 . 27 ALA HA H 4.03 0.05 1 251 . 27 ALA HB H 1.22 0.05 1 252 . 27 ALA CB C 20.8 0.20 1 253 . 28 PRO CD C 48.8 0.20 1 254 . 28 PRO CA C 61.8 0.20 1 255 . 28 PRO HA H 3.77 0.05 1 256 . 28 PRO CB C 32.0 0.20 1 257 . 28 PRO HB2 H 1.35 0.05 1 258 . 28 PRO HB3 H 1.35 0.05 1 259 . 28 PRO HG2 H 1.20 0.05 1 260 . 28 PRO HG3 H 1.20 0.05 1 261 . 28 PRO HD2 H 0.88 0.05 1 262 . 28 PRO HD3 H 1.92 0.05 1 263 . 29 SER N N 118.2 0.15 1 264 . 29 SER H H 8.80 0.05 1 265 . 29 SER CA C 58.7 0.20 1 266 . 29 SER HA H 4.26 0.05 1 267 . 29 SER CB C 64.1 0.20 1 268 . 29 SER HB2 H 4.06 0.05 1 269 . 29 SER HB3 H 4.06 0.05 1 270 . 30 GLU N N 122.2 0.15 1 271 . 30 GLU H H 8.76 0.05 1 272 . 30 GLU CA C 59.1 0.20 1 273 . 30 GLU HA H 3.85 0.05 1 274 . 30 GLU CB C 29.4 0.20 1 275 . 30 GLU HB2 H 1.92 0.05 1 276 . 30 GLU HB3 H 1.92 0.05 1 277 . 30 GLU HG2 H 2.24 0.05 1 278 . 30 GLU HG3 H 2.24 0.05 1 279 . 31 ASN N N 111.9 0.15 1 280 . 31 ASN H H 8.17 0.05 1 281 . 31 ASN CA C 53.0 0.20 1 282 . 31 ASN HA H 4.76 0.05 1 283 . 31 ASN CB C 39.4 0.20 1 284 . 31 ASN HB2 H 2.86 0.05 1 285 . 31 ASN HB3 H 2.77 0.05 1 286 . 31 ASN ND2 N 111.3 0.15 1 287 . 31 ASN HD21 H 7.13 0.05 1 288 . 31 ASN HD22 H 7.59 0.05 1 289 . 32 ASN N N 115.7 0.15 1 290 . 32 ASN H H 7.26 0.05 1 291 . 32 ASN CA C 52.6 0.20 1 292 . 32 ASN HA H 4.82 0.05 1 293 . 32 ASN CB C 38.8 0.20 1 294 . 32 ASN HB2 H 2.80 0.05 1 295 . 32 ASN HB3 H 2.80 0.05 1 296 . 32 ASN ND2 N 112.7 0.15 1 297 . 32 ASN HD21 H 6.88 0.05 1 298 . 32 ASN HD22 H 7.53 0.05 1 299 . 33 ILE N N 126.4 0.15 1 300 . 33 ILE H H 8.74 0.05 1 301 . 33 ILE CA C 62.3 0.20 1 302 . 33 ILE HA H 4.03 0.05 1 303 . 33 ILE CB C 38.9 0.20 1 304 . 33 ILE HB H 1.84 0.05 1 305 . 33 ILE HG2 H 0.95 0.05 1 306 . 33 ILE CG2 C 17.4 0.20 1 307 . 33 ILE CG1 C 29.8 0.20 1 308 . 33 ILE HG12 H 1.53 0.05 2 309 . 33 ILE HG13 H 1.49 0.05 2 310 . 33 ILE HD1 H 0.88 0.05 1 311 . 33 ILE CD1 C 14.6 0.20 1 312 . 34 MET N N 112.7 0.15 1 313 . 34 MET H H 7.54 0.05 1 314 . 34 MET CA C 54.7 0.20 1 315 . 34 MET HA H 4.65 0.05 1 316 . 34 MET CB C 31.0 0.20 1 317 . 34 MET HB2 H 2.36 0.05 2 318 . 34 MET HB3 H 2.16 0.05 2 319 . 34 MET CG C 33.2 0.20 1 320 . 34 MET HG2 H 2.74 0.05 1 321 . 34 MET HG3 H 2.35 0.05 1 322 . 34 MET HE H 1.71 0.05 1 323 . 34 MET CE C 17.7 0.20 1 324 . 35 GLN N N 119.5 0.15 1 325 . 35 GLN H H 7.85 0.05 1 326 . 35 GLN CA C 55.2 0.20 1 327 . 35 GLN HA H 5.42 0.05 1 328 . 35 GLN CB C 32.0 0.20 1 329 . 35 GLN HB2 H 2.11 0.05 2 330 . 35 GLN HB3 H 1.99 0.05 2 331 . 35 GLN CG C 34.9 0.20 1 332 . 35 GLN HG2 H 2.28 0.05 2 333 . 35 GLN HG3 H 2.04 0.05 2 334 . 36 TRP N N 125.9 0.15 1 335 . 36 TRP H H 9.92 0.05 1 336 . 36 TRP CA C 55.4 0.20 1 337 . 36 TRP HA H 5.42 0.05 1 338 . 36 TRP CB C 31.4 0.20 1 339 . 36 TRP HB2 H 2.99 0.05 1 340 . 36 TRP HB3 H 3.08 0.05 1 341 . 36 TRP CD1 C 125.7 0.20 1 342 . 36 TRP CE3 C 118.8 0.20 1 343 . 36 TRP HD1 H 7.13 0.05 1 344 . 36 TRP HE3 H 7.07 0.05 1 345 . 36 TRP CZ3 C 121.5 0.20 1 346 . 36 TRP CZ2 C 114.8 0.20 1 347 . 36 TRP HZ3 H 6.99 0.05 1 348 . 36 TRP CH2 C 123.6 0.20 1 349 . 36 TRP HZ2 H 7.32 0.05 1 350 . 36 TRP HH2 H 6.99 0.05 1 351 . 37 ASN N N 117.7 0.15 1 352 . 37 ASN H H 8.34 0.05 1 353 . 37 ASN CA C 52.6 0.20 1 354 . 37 ASN HA H 5.47 0.05 1 355 . 37 ASN CB C 41.4 0.20 1 356 . 37 ASN HB2 H 2.88 0.05 2 357 . 37 ASN HB3 H 2.74 0.05 2 358 . 37 ASN ND2 N 112.5 0.15 1 359 . 37 ASN HD21 H 6.98 0.05 1 360 . 37 ASN HD22 H 7.64 0.05 1 361 . 38 ALA N N 122.6 0.15 1 362 . 38 ALA H H 8.66 0.05 1 363 . 38 ALA CA C 50.9 0.20 1 364 . 38 ALA HA H 5.44 0.05 1 365 . 38 ALA HB H 1.41 0.05 1 366 . 38 ALA CB C 24.5 0.20 1 367 . 39 VAL N N 120.9 0.15 1 368 . 39 VAL H H 8.84 0.05 1 369 . 39 VAL CA C 61.0 0.20 1 370 . 39 VAL HA H 5.09 0.05 1 371 . 39 VAL CB C 35.4 0.20 1 372 . 39 VAL HB H 1.78 0.05 1 373 . 39 VAL HG1 H 0.61 0.05 1 374 . 39 VAL HG2 H 0.83 0.05 1 375 . 39 VAL CG1 C 21.2 0.20 1 376 . 39 VAL CG2 C 21.8 0.20 1 377 . 40 ILE N N 122.0 0.15 1 378 . 40 ILE H H 8.92 0.05 1 379 . 40 ILE CA C 59.2 0.20 1 380 . 40 ILE HA H 4.93 0.05 1 381 . 40 ILE CB C 42.0 0.20 1 382 . 40 ILE HB H 1.84 0.05 1 383 . 40 ILE HG2 H 0.95 0.05 1 384 . 40 ILE CG2 C 17.9 0.20 1 385 . 40 ILE CG1 C 27.1 0.20 1 386 . 40 ILE HG12 H 1.21 0.05 1 387 . 40 ILE HG13 H 1.66 0.05 1 388 . 40 ILE HD1 H 0.82 0.05 1 389 . 40 ILE CD1 C 14.7 0.20 1 390 . 41 PHE N N 125.7 0.15 1 391 . 41 PHE H H 8.99 0.05 1 392 . 41 PHE CA C 55.0 0.20 1 393 . 41 PHE HA H 5.47 0.05 1 394 . 41 PHE CB C 38.4 0.20 1 395 . 41 PHE HB2 H 3.27 0.05 2 396 . 41 PHE HB3 H 3.18 0.05 2 397 . 43 PRO CD C 51.9 0.20 1 398 . 43 PRO CA C 63.1 0.20 1 399 . 43 PRO HA H 4.54 0.05 1 400 . 43 PRO CB C 31.6 0.20 1 401 . 43 PRO HB2 H 2.08 0.05 1 402 . 43 PRO HB3 H 2.40 0.05 1 403 . 43 PRO CG C 27.8 0.20 1 404 . 43 PRO HG2 H 2.28 0.05 1 405 . 43 PRO HG3 H 2.08 0.05 1 406 . 43 PRO HD2 H 3.55 0.05 1 407 . 43 PRO HD3 H 4.00 0.05 1 408 . 44 GLU N N 124.7 0.15 1 409 . 44 GLU H H 8.87 0.05 1 410 . 44 GLU CA C 57.7 0.20 1 411 . 44 GLU HA H 4.06 0.05 1 412 . 44 GLU CB C 30.0 0.20 1 413 . 44 GLU HB2 H 2.08 0.05 1 414 . 44 GLU HB3 H 2.08 0.05 1 415 . 44 GLU CG C 36.4 0.20 1 416 . 44 GLU HG2 H 2.41 0.05 1 417 . 44 GLU HG3 H 2.41 0.05 1 418 . 45 GLY N N 111.6 0.15 1 419 . 45 GLY H H 9.47 0.05 1 420 . 45 GLY CA C 45.8 0.20 1 421 . 45 GLY HA2 H 4.22 0.05 2 422 . 45 GLY HA3 H 3.87 0.05 2 423 . 46 THR N N 108.6 0.15 1 424 . 46 THR H H 7.48 0.05 1 425 . 46 THR CA C 59.7 0.20 1 426 . 46 THR HA H 5.29 0.05 1 427 . 46 THR CB C 71.3 0.20 1 428 . 46 THR HB H 4.87 0.05 1 429 . 46 THR HG2 H 1.35 0.05 1 430 . 46 THR CG2 C 22.3 0.20 1 431 . 47 PRO CD C 51.4 0.20 1 432 . 47 PRO CA C 64.5 0.20 1 433 . 47 PRO HA H 4.55 0.05 1 434 . 47 PRO CB C 31.4 0.20 1 435 . 47 PRO HB2 H 2.29 0.05 1 436 . 47 PRO HB3 H 1.59 0.05 1 437 . 47 PRO CG C 28.1 0.20 1 438 . 47 PRO HG2 H 2.20 0.05 1 439 . 47 PRO HG3 H 2.20 0.05 1 440 . 47 PRO HD2 H 4.28 0.05 2 441 . 47 PRO HD3 H 4.20 0.05 2 442 . 48 PHE N N 112.2 0.15 1 443 . 48 PHE H H 7.38 0.05 1 444 . 48 PHE CA C 58.8 0.20 1 445 . 48 PHE HA H 4.14 0.05 1 446 . 48 PHE CB C 40.2 0.20 1 447 . 48 PHE HB2 H 2.73 0.05 1 448 . 48 PHE HB3 H 3.50 0.05 1 449 . 48 PHE HD1 H 7.15 0.05 1 450 . 48 PHE HD2 H 7.15 0.05 1 451 . 48 PHE HE1 H 7.54 0.05 1 452 . 48 PHE HE2 H 7.54 0.05 1 453 . 48 PHE CE1 C 132.9 0.20 1 454 . 48 PHE CZ C 132.6 0.20 1 455 . 48 PHE HZ H 7.85 0.05 1 456 . 49 GLU N N 123.0 0.15 1 457 . 49 GLU H H 7.56 0.05 1 458 . 49 GLU CA C 58.7 0.20 1 459 . 49 GLU HA H 3.63 0.05 1 460 . 49 GLU CB C 30.4 0.20 1 461 . 49 GLU HB2 H 2.50 0.05 1 462 . 49 GLU HB3 H 2.08 0.05 1 463 . 49 GLU CG C 35.9 0.20 1 464 . 49 GLU HG2 H 2.37 0.05 2 465 . 49 GLU HG3 H 2.56 0.05 2 466 . 50 ASP N N 116.8 0.15 1 467 . 50 ASP H H 8.75 0.05 1 468 . 50 ASP CA C 57.8 0.20 1 469 . 50 ASP HA H 4.46 0.05 1 470 . 50 ASP CB C 39.7 0.20 1 471 . 50 ASP HB2 H 3.45 0.05 1 472 . 50 ASP HB3 H 3.05 0.05 1 473 . 51 GLY N N 108.6 0.15 1 474 . 51 GLY H H 8.81 0.05 1 475 . 51 GLY CA C 46.4 0.20 1 476 . 51 GLY HA2 H 3.90 0.05 1 477 . 51 GLY HA3 H 3.45 0.05 1 478 . 52 THR N N 116.9 0.15 1 479 . 52 THR H H 7.92 0.05 1 480 . 52 THR CA C 58.5 0.20 1 481 . 52 THR HA H 4.24 0.05 1 482 . 52 THR CB C 69.9 0.20 1 483 . 52 THR HB H 3.84 0.05 1 484 . 52 THR HG2 H 0.81 0.05 1 485 . 52 THR CG2 C 21.1 0.20 1 486 . 53 PHE N N 122.8 0.15 1 487 . 53 PHE H H 8.51 0.05 1 488 . 53 PHE CA C 56.7 0.20 1 489 . 53 PHE HA H 5.03 0.05 1 490 . 53 PHE CB C 40.9 0.20 1 491 . 53 PHE HB2 H 3.17 0.05 1 492 . 53 PHE HB3 H 3.17 0.05 1 493 . 53 PHE HD1 H 7.25 0.05 1 494 . 53 PHE HD2 H 7.25 0.05 1 495 . 53 PHE HE1 H 7.42 0.05 1 496 . 53 PHE HE2 H 7.42 0.05 1 497 . 53 PHE HZ H 7.14 0.05 1 498 . 54 LYS N N 122.3 0.15 1 499 . 54 LYS H H 9.32 0.05 1 500 . 54 LYS CA C 56.0 0.20 1 501 . 54 LYS HA H 5.18 0.05 1 502 . 54 LYS CB C 34.6 0.20 1 503 . 54 LYS HB2 H 1.91 0.05 1 504 . 54 LYS HB3 H 2.08 0.05 1 505 . 54 LYS CG C 26.1 0.20 1 506 . 54 LYS HG2 H 1.64 0.05 2 507 . 54 LYS HG3 H 1.53 0.05 2 508 . 54 LYS CD C 29.5 0.20 1 509 . 54 LYS HD2 H 1.75 0.05 1 510 . 54 LYS HD3 H 1.75 0.05 1 511 . 54 LYS CE C 42.0 0.20 1 512 . 54 LYS HE2 H 2.97 0.05 1 513 . 54 LYS HE3 H 2.97 0.05 1 514 . 55 LEU N N 122.6 0.15 1 515 . 55 LEU H H 9.17 0.05 1 516 . 55 LEU CA C 55.2 0.20 1 517 . 55 LEU HA H 5.24 0.05 1 518 . 55 LEU CB C 46.5 0.20 1 519 . 55 LEU HB2 H 1.29 0.05 2 520 . 55 LEU HB3 H 1.12 0.05 2 521 . 55 LEU CG C 27.4 0.20 1 522 . 55 LEU HG H 1.24 0.05 1 523 . 55 LEU HD1 H 0.47 0.05 1 524 . 55 LEU HD2 H -0.03 0.05 1 525 . 55 LEU CD1 C 27.1 0.20 1 526 . 55 LEU CD2 C 26.6 0.20 1 527 . 56 VAL N N 119.2 0.15 1 528 . 56 VAL H H 8.85 0.05 1 529 . 56 VAL CA C 60.0 0.20 1 530 . 56 VAL HA H 5.20 0.05 1 531 . 56 VAL CB C 35.3 0.20 1 532 . 56 VAL HB H 1.95 0.05 1 533 . 56 VAL HG1 H 0.95 0.05 1 534 . 56 VAL HG2 H 0.98 0.05 1 535 . 56 VAL CG1 C 20.8 0.20 1 536 . 56 VAL CG2 C 21.3 0.20 1 537 . 57 ILE N N 124.7 0.15 1 538 . 57 ILE H H 8.48 0.05 1 539 . 57 ILE CA C 60.0 0.20 1 540 . 57 ILE HA H 4.56 0.05 1 541 . 57 ILE CB C 40.6 0.20 1 542 . 57 ILE HB H 1.34 0.05 1 543 . 57 ILE HG2 H -0.15 0.05 1 544 . 57 ILE CG2 C 19.8 0.20 1 545 . 57 ILE CG1 C 26.8 0.20 1 546 . 57 ILE HG12 H 0.60 0.05 1 547 . 57 ILE HG13 H 1.29 0.05 1 548 . 57 ILE HD1 H 0.52 0.05 1 549 . 57 ILE CD1 C 14.1 0.20 1 550 . 58 GLU N N 125.4 0.15 1 551 . 58 GLU H H 8.55 0.05 1 552 . 58 GLU CA C 55.0 0.20 1 553 . 58 GLU HA H 5.09 0.05 1 554 . 58 GLU CB C 31.7 0.20 1 555 . 58 GLU HB2 H 1.82 0.05 1 556 . 58 GLU HB3 H 1.93 0.05 1 557 . 58 GLU CG C 36.7 0.20 1 558 . 58 GLU HG2 H 2.08 0.05 1 559 . 58 GLU HG3 H 2.08 0.05 1 560 . 59 PHE N N 123.6 0.15 1 561 . 59 PHE H H 9.06 0.05 1 562 . 59 PHE CA C 57.4 0.20 1 563 . 59 PHE HA H 4.32 0.05 1 564 . 59 PHE CB C 42.2 0.20 1 565 . 59 PHE HB2 H 2.85 0.05 1 566 . 59 PHE HB3 H 2.74 0.05 1 567 . 59 PHE HD1 H 6.29 0.05 1 568 . 59 PHE HD2 H 6.29 0.05 1 569 . 59 PHE HE1 H 5.71 0.05 1 570 . 59 PHE HE2 H 5.71 0.05 1 571 . 59 PHE CD1 C 132.0 0.20 1 572 . 59 PHE CE1 C 129.8 0.20 1 573 . 59 PHE CZ C 129.2 0.20 1 574 . 59 PHE HZ H 5.86 0.05 1 575 . 60 SER N N 114.0 0.15 1 576 . 60 SER H H 7.64 0.05 1 577 . 60 SER CA C 56.3 0.20 1 578 . 60 SER HA H 4.94 0.05 1 579 . 60 SER CB C 67.5 0.20 1 580 . 60 SER HB2 H 4.28 0.05 2 581 . 60 SER HB3 H 3.88 0.05 2 582 . 61 GLU CA C 57.4 0.20 1 583 . 61 GLU N N 116.9 0.15 1 584 . 61 GLU H H 8.78 0.05 1 585 . 61 GLU HA H 4.33 0.05 1 586 . 61 GLU CB C 28.6 0.20 1 587 . 61 GLU HB2 H 2.39 0.05 2 588 . 61 GLU HB3 H 1.86 0.05 2 589 . 61 GLU CG C 35.0 0.20 1 590 . 61 GLU HG2 H 2.54 0.05 2 591 . 61 GLU HG3 H 2.44 0.05 2 592 . 62 GLU N N 115.2 0.15 1 593 . 62 GLU H H 7.97 0.05 1 594 . 62 GLU CA C 56.5 0.20 1 595 . 62 GLU HA H 4.47 0.05 1 596 . 62 GLU CB C 31.0 0.20 1 597 . 62 GLU HB2 H 2.32 0.05 2 598 . 62 GLU HB3 H 1.70 0.05 2 599 . 62 GLU CG C 37.7 0.20 1 600 . 62 GLU HG2 H 2.24 0.05 1 601 . 62 GLU HG3 H 2.24 0.05 1 602 . 63 TYR N N 125.5 0.15 1 603 . 63 TYR H H 7.88 0.05 1 604 . 63 TYR CA C 57.9 0.20 1 605 . 63 TYR HA H 4.80 0.05 1 606 . 63 TYR CB C 39.3 0.20 1 607 . 63 TYR HB2 H 3.71 0.05 1 608 . 63 TYR HB3 H 3.00 0.05 1 609 . 64 PRO CA C 64.0 0.20 1 610 . 64 PRO HA H 4.15 0.05 1 611 . 64 PRO CB C 32.7 0.20 1 612 . 64 PRO HB2 H 0.81 0.05 2 613 . 64 PRO HB3 H 2.42 0.05 2 614 . 65 ASN N N 123.8 0.15 1 615 . 65 ASN H H 8.92 0.05 1 616 . 65 ASN CA C 56.2 0.20 1 617 . 65 ASN HA H 4.70 0.05 1 618 . 65 ASN CB C 38.8 0.20 1 619 . 65 ASN HB2 H 3.05 0.05 2 620 . 65 ASN HB3 H 2.92 0.05 2 621 . 65 ASN ND2 N 113.9 0.15 1 622 . 65 ASN HD21 H 6.97 0.05 1 623 . 65 ASN HD22 H 7.64 0.05 1 624 . 66 LYS N N 117.5 0.15 1 625 . 66 LYS H H 7.12 0.05 1 626 . 66 LYS CA C 52.0 0.20 1 627 . 66 LYS HA H 4.57 0.05 1 628 . 66 LYS CB C 35.2 0.20 1 629 . 66 LYS HB2 H 1.59 0.05 2 630 . 66 LYS HB3 H 1.29 0.05 2 631 . 66 LYS CG C 25.0 0.20 1 632 . 66 LYS HG2 H 1.39 0.05 1 633 . 66 LYS HG3 H 1.39 0.05 1 634 . 66 LYS HD2 H 1.68 0.05 1 635 . 66 LYS HD3 H 1.68 0.05 1 636 . 66 LYS CE C 42.1 0.20 1 637 . 66 LYS HE2 H 2.93 0.05 1 638 . 66 LYS HE3 H 2.93 0.05 1 639 . 67 PRO CD C 50.3 0.20 1 640 . 67 PRO HD2 H 3.04 0.05 1 641 . 67 PRO HD3 H 3.40 0.05 1 642 . 68 PRO CA C 61.4 0.20 1 643 . 68 PRO HA H 4.49 0.05 1 644 . 68 PRO CB C 32.6 0.20 1 645 . 68 PRO HB2 H 0.92 0.05 1 646 . 68 PRO HB3 H 0.92 0.05 1 647 . 69 THR N N 111.0 0.15 1 648 . 69 THR H H 7.95 0.05 1 649 . 69 THR CA C 61.5 0.20 1 650 . 69 THR HA H 4.35 0.05 1 651 . 69 THR CB C 70.0 0.20 1 652 . 69 THR HB H 4.00 0.05 1 653 . 69 THR HG2 H 1.10 0.05 1 654 . 69 THR CG2 C 21.6 0.20 1 655 . 70 VAL N N 123.3 0.15 1 656 . 70 VAL H H 8.29 0.05 1 657 . 70 VAL CA C 60.6 0.20 1 658 . 70 VAL HA H 4.68 0.05 1 659 . 70 VAL CB C 34.3 0.20 1 660 . 70 VAL HB H 1.60 0.05 1 661 . 70 VAL HG1 H 0.50 0.05 1 662 . 70 VAL HG2 H 0.55 0.05 1 663 . 70 VAL CG1 C 22.6 0.20 1 664 . 70 VAL CG2 C 21.8 0.20 1 665 . 71 ARG N N 123.1 0.15 1 666 . 71 ARG H H 8.30 0.05 1 667 . 71 ARG CA C 54.3 0.20 1 668 . 71 ARG HA H 4.84 0.05 1 669 . 71 ARG CB C 34.3 0.20 1 670 . 71 ARG HB2 H 1.57 0.05 2 671 . 71 ARG HB3 H 1.44 0.05 2 672 . 71 ARG CG C 27.4 0.20 1 673 . 71 ARG HG2 H 1.42 0.05 2 674 . 71 ARG HG3 H 1.30 0.05 2 675 . 71 ARG CD C 43.5 0.20 1 676 . 71 ARG HD2 H 3.07 0.05 2 677 . 71 ARG HD3 H 3.04 0.05 2 678 . 72 PHE N N 121.1 0.15 1 679 . 72 PHE H H 9.23 0.05 1 680 . 72 PHE CA C 60.3 0.20 1 681 . 72 PHE HA H 4.61 0.05 1 682 . 72 PHE CB C 39.3 0.20 1 683 . 72 PHE HB2 H 2.97 0.05 1 684 . 72 PHE HB3 H 3.46 0.05 1 685 . 72 PHE HD1 H 7.26 0.05 1 686 . 72 PHE HD2 H 7.26 0.05 1 687 . 72 PHE HE1 H 6.75 0.05 1 688 . 72 PHE HE2 H 6.75 0.05 1 689 . 72 PHE CE1 C 130.6 0.20 1 690 . 72 PHE CZ C 128.3 0.20 1 691 . 72 PHE HZ H 6.56 0.05 1 692 . 73 LEU N N 124.1 0.15 1 693 . 73 LEU H H 9.36 0.05 1 694 . 73 LEU CA C 55.4 0.20 1 695 . 73 LEU HA H 4.47 0.05 1 696 . 73 LEU CB C 43.0 0.20 1 697 . 73 LEU HB2 H 1.65 0.05 1 698 . 73 LEU HB3 H 1.52 0.05 1 699 . 73 LEU CG C 27.5 0.20 1 700 . 73 LEU HG H 1.55 0.05 1 701 . 73 LEU HD1 H 0.90 0.05 1 702 . 73 LEU HD2 H 0.85 0.05 1 703 . 73 LEU CD1 C 25.7 0.20 1 704 . 73 LEU CD2 C 22.8 0.20 1 705 . 74 SER N N 114.9 0.15 1 706 . 74 SER H H 7.38 0.05 1 707 . 74 SER CA C 59.7 0.20 1 708 . 74 SER HA H 4.61 0.05 1 709 . 74 SER CB C 64.8 0.20 1 710 . 74 SER HB2 H 3.68 0.05 1 711 . 74 SER HB3 H 3.68 0.05 1 712 . 75 LYS N N 124.9 0.15 1 713 . 75 LYS H H 8.74 0.05 1 714 . 75 LYS CA C 57.5 0.20 1 715 . 75 LYS HA H 4.07 0.05 1 716 . 75 LYS CB C 32.0 0.20 1 717 . 75 LYS HB2 H 1.82 0.05 2 718 . 75 LYS HB3 H 1.73 0.05 2 719 . 75 LYS CG C 25.1 0.20 1 720 . 75 LYS HG2 H 1.60 0.05 2 721 . 75 LYS HG3 H 1.52 0.05 2 722 . 75 LYS CD C 28.8 0.20 1 723 . 75 LYS HD2 H 1.73 0.05 1 724 . 75 LYS HD3 H 1.73 0.05 1 725 . 75 LYS CE C 42.1 0.20 1 726 . 75 LYS HE2 H 3.03 0.05 1 727 . 75 LYS HE3 H 3.03 0.05 1 728 . 76 MET N N 120.3 0.15 1 729 . 76 MET H H 8.45 0.05 1 730 . 76 MET CA C 52.1 0.20 1 731 . 76 MET HA H 4.81 0.05 1 732 . 76 MET CB C 33.2 0.20 1 733 . 76 MET HB2 H 1.39 0.05 1 734 . 76 MET HB3 H 1.56 0.05 1 735 . 76 MET CG C 31.3 0.20 1 736 . 76 MET HG2 H 1.58 0.05 2 737 . 76 MET HG3 H 1.81 0.05 2 738 . 76 MET HE H 0.36 0.05 1 739 . 76 MET CE C 13.2 0.20 1 740 . 77 PHE N N 124.2 0.15 1 741 . 77 PHE H H 6.82 0.05 1 742 . 77 PHE CA C 58.2 0.20 1 743 . 77 PHE HA H 4.43 0.05 1 744 . 77 PHE CB C 40.4 0.20 1 745 . 77 PHE HB2 H 2.90 0.05 1 746 . 77 PHE HB3 H 2.70 0.05 1 747 . 77 PHE HD1 H 7.21 0.05 1 748 . 77 PHE HD2 H 7.21 0.05 1 749 . 77 PHE HE1 H 7.32 0.05 1 750 . 77 PHE HE2 H 7.32 0.05 1 751 . 77 PHE CZ C 128.5 0.20 1 752 . 77 PHE HZ H 6.98 0.05 1 753 . 78 HIS N N 122.5 0.15 1 754 . 78 HIS H H 8.44 0.05 1 755 . 78 HIS CA C 55.1 0.20 1 756 . 78 HIS HA H 4.84 0.05 1 757 . 78 HIS CB C 34.4 0.20 1 758 . 78 HIS HB2 H 3.16 0.05 1 759 . 78 HIS HB3 H 2.23 0.05 1 760 . 78 HIS CD2 C 117.5 0.20 1 761 . 78 HIS CE1 C 139.3 0.20 1 762 . 78 HIS HD2 H 6.94 0.05 1 763 . 78 HIS HE1 H 8.17 0.05 1 764 . 79 PRO CD C 49.0 0.20 1 765 . 79 PRO CA C 65.7 0.20 1 766 . 79 PRO HA H 4.10 0.05 1 767 . 79 PRO CB C 33.5 0.20 1 768 . 79 PRO HB2 H 1.90 0.05 1 769 . 79 PRO HB3 H 1.35 0.05 1 770 . 79 PRO HG2 H 1.41 0.05 1 771 . 79 PRO HG3 H 1.85 0.05 1 772 . 79 PRO HD2 H 3.38 0.05 1 773 . 79 PRO HD3 H 3.14 0.05 1 774 . 80 ASN N N 114.6 0.15 1 775 . 80 ASN H H 11.28 0.05 1 776 . 80 ASN CA C 53.5 0.20 1 777 . 80 ASN HA H 4.80 0.05 1 778 . 80 ASN CB C 41.4 0.20 1 779 . 80 ASN HB2 H 3.72 0.05 2 780 . 80 ASN HB3 H 2.49 0.05 2 781 . 80 ASN ND2 N 108.0 0.15 1 782 . 80 ASN HD21 H 7.31 0.05 1 783 . 80 ASN HD22 H 7.96 0.05 1 784 . 81 VAL N N 120.3 0.15 1 785 . 81 VAL H H 7.41 0.05 1 786 . 81 VAL CA C 61.3 0.20 1 787 . 81 VAL HA H 4.63 0.05 1 788 . 81 VAL CB C 33.7 0.20 1 789 . 81 VAL HB H 1.80 0.05 1 790 . 81 VAL HG1 H 1.08 0.05 1 791 . 81 VAL HG2 H 0.59 0.05 1 792 . 81 VAL CG1 C 21.0 0.20 1 793 . 81 VAL CG2 C 21.5 0.20 1 794 . 82 TYR N N 124.8 0.15 1 795 . 82 TYR H H 8.82 0.05 1 796 . 82 TYR CA C 59.3 0.20 1 797 . 82 TYR HA H 4.33 0.05 1 798 . 82 TYR HB2 H 3.10 0.05 1 799 . 82 TYR HB3 H 3.38 0.05 1 800 . 82 TYR HD1 H 7.23 0.05 1 801 . 82 TYR HD2 H 7.23 0.05 1 802 . 82 TYR HE1 H 6.78 0.05 1 803 . 82 TYR HE2 H 6.78 0.05 1 804 . 82 TYR CD1 C 134.4 0.20 1 805 . 82 TYR CE1 C 118.3 0.20 1 806 . 83 ALA CA C 55.2 0.20 1 807 . 83 ALA HA H 4.29 0.05 1 808 . 83 ALA HB H 1.58 0.05 1 809 . 83 ALA CB C 18.5 0.20 1 810 . 84 ASP N N 113.7 0.15 1 811 . 84 ASP H H 7.88 0.05 1 812 . 84 ASP CA C 53.6 0.20 1 813 . 84 ASP HA H 4.58 0.05 1 814 . 84 ASP CB C 40.0 0.20 1 815 . 84 ASP HB2 H 3.11 0.05 2 816 . 84 ASP HB3 H 2.63 0.05 2 817 . 85 GLY N N 107.9 0.15 1 818 . 85 GLY H H 8.35 0.05 1 819 . 85 GLY CA C 45.6 0.20 1 820 . 85 GLY HA2 H 4.88 0.05 1 821 . 85 GLY HA3 H 3.64 0.05 1 822 . 86 SER N N 118.0 0.15 1 823 . 86 SER H H 8.52 0.05 1 824 . 86 SER CA C 60.3 0.20 1 825 . 86 SER HA H 4.65 0.05 1 826 . 86 SER CB C 63.3 0.20 1 827 . 86 SER HB2 H 4.15 0.05 2 828 . 86 SER HB3 H 3.93 0.05 2 829 . 87 ILE N N 119.9 0.15 1 830 . 87 ILE H H 8.34 0.05 1 831 . 87 ILE CA C 61.2 0.20 1 832 . 87 ILE HA H 4.57 0.05 1 833 . 87 ILE CB C 41.3 0.20 1 834 . 87 ILE HB H 1.52 0.05 1 835 . 87 ILE HG2 H 0.69 0.05 1 836 . 87 ILE CG2 C 18.5 0.20 1 837 . 87 ILE CG1 C 28.6 0.20 1 838 . 87 ILE HG12 H 1.75 0.05 2 839 . 87 ILE HG13 H 0.88 0.05 2 840 . 87 ILE HD1 H 0.39 0.05 1 841 . 87 ILE CD1 C 15.7 0.20 1 842 . 88 CYS N N 127.5 0.15 1 843 . 88 CYS H H 8.61 0.05 1 844 . 88 CYS CA C 58.3 0.20 1 845 . 88 CYS HA H 4.62 0.05 1 846 . 88 CYS CB C 26.5 0.20 1 847 . 88 CYS HB2 H 2.88 0.05 1 848 . 88 CYS HB3 H 2.64 0.05 1 849 . 89 LEU N N 127.1 0.15 1 850 . 89 LEU H H 7.74 0.05 1 851 . 89 LEU CA C 53.9 0.20 1 852 . 89 LEU HA H 4.61 0.05 1 853 . 89 LEU CB C 45.5 0.20 1 854 . 89 LEU HB2 H 1.57 0.05 1 855 . 89 LEU HB3 H 1.35 0.05 1 856 . 89 LEU CG C 27.5 0.20 1 857 . 89 LEU HG H 1.58 0.05 1 858 . 89 LEU HD1 H 0.97 0.05 1 859 . 89 LEU HD2 H 0.77 0.05 1 860 . 89 LEU CD1 C 24.4 0.20 1 861 . 89 LEU CD2 C 26.0 0.20 1 862 . 90 ASP N N 128.4 0.15 1 863 . 90 ASP H H 9.07 0.05 1 864 . 90 ASP CA C 58.3 0.20 1 865 . 90 ASP HA H 4.35 0.05 1 866 . 90 ASP CB C 39.6 0.20 1 867 . 90 ASP HB2 H 2.78 0.05 1 868 . 90 ASP HB3 H 2.78 0.05 1 869 . 91 ILE N N 116.7 0.15 1 870 . 91 ILE H H 8.11 0.05 1 871 . 91 ILE CA C 64.1 0.20 1 872 . 91 ILE HA H 3.83 0.05 1 873 . 91 ILE CB C 38.4 0.20 1 874 . 91 ILE HB H 1.92 0.05 1 875 . 91 ILE HG2 H 0.89 0.05 1 876 . 91 ILE CG2 C 18.4 0.20 1 877 . 91 ILE CG1 C 27.7 0.20 1 878 . 91 ILE HG12 H 1.31 0.05 2 879 . 91 ILE HG13 H 1.14 0.05 2 880 . 91 ILE HD1 H 0.60 0.05 1 881 . 91 ILE CD1 C 14.2 0.20 1 882 . 92 LEU N N 113.8 0.15 1 883 . 92 LEU H H 7.29 0.05 1 884 . 92 LEU CA C 54.4 0.20 1 885 . 92 LEU HA H 4.59 0.05 1 886 . 92 LEU CB C 41.6 0.20 1 887 . 92 LEU HB2 H 1.75 0.05 1 888 . 92 LEU HB3 H 1.94 0.05 1 889 . 92 LEU CG C 27.7 0.20 1 890 . 92 LEU HG H 1.57 0.05 1 891 . 92 LEU HD1 H 0.86 0.05 1 892 . 92 LEU HD2 H 0.80 0.05 1 893 . 92 LEU CD1 C 26.2 0.20 1 894 . 92 LEU CD2 C 22.4 0.20 1 895 . 93 GLN N N 118.8 0.15 1 896 . 93 GLN H H 7.82 0.05 1 897 . 93 GLN CA C 56.4 0.20 1 898 . 93 GLN HA H 4.46 0.05 1 899 . 93 GLN CB C 29.5 0.20 1 900 . 93 GLN HB2 H 2.18 0.05 1 901 . 93 GLN HB3 H 2.18 0.05 1 902 . 93 GLN CG C 34.1 0.20 1 903 . 93 GLN HG2 H 2.43 0.05 1 904 . 93 GLN HG3 H 2.43 0.05 1 905 . 93 GLN NE2 N 110.8 0.15 1 906 . 93 GLN HE21 H 6.74 0.05 1 907 . 93 GLN HE22 H 7.44 0.05 1 908 . 94 ASN N N 117.1 0.15 1 909 . 94 ASN H H 8.49 0.05 1 910 . 94 ASN CA C 55.0 0.20 1 911 . 94 ASN HA H 4.83 0.05 1 912 . 94 ASN CB C 38.7 0.20 1 913 . 94 ASN HB2 H 2.88 0.05 1 914 . 94 ASN HB3 H 2.97 0.05 1 915 . 94 ASN ND2 N 112.9 0.15 1 916 . 94 ASN HD21 H 6.95 0.05 1 917 . 94 ASN HD22 H 7.71 0.05 1 918 . 95 ARG N N 117.3 0.15 1 919 . 95 ARG H H 7.88 0.05 1 920 . 95 ARG CA C 54.6 0.20 1 921 . 95 ARG HA H 4.76 0.05 1 922 . 95 ARG CB C 30.0 0.20 1 923 . 95 ARG HB2 H 2.10 0.05 2 924 . 95 ARG HB3 H 1.32 0.05 2 925 . 95 ARG CG C 27.6 0.20 1 926 . 95 ARG HG2 H 1.65 0.05 2 927 . 95 ARG HG3 H 1.57 0.05 2 928 . 95 ARG CD C 43.2 0.20 1 929 . 95 ARG HD2 H 3.21 0.05 1 930 . 95 ARG HD3 H 3.21 0.05 1 931 . 96 TRP N N 121.1 0.15 1 932 . 96 TRP H H 7.54 0.05 1 933 . 96 TRP CA C 59.3 0.20 1 934 . 96 TRP HA H 4.77 0.05 1 935 . 96 TRP CB C 29.9 0.20 1 936 . 96 TRP HB2 H 2.96 0.05 2 937 . 96 TRP HB3 H 3.59 0.05 2 938 . 96 TRP CD1 C 126.1 0.20 1 939 . 96 TRP CE3 C 122.5 0.20 1 940 . 96 TRP NE1 N 129.8 0.15 1 941 . 96 TRP HD1 H 6.92 0.05 1 942 . 96 TRP HE1 H 9.93 0.05 1 943 . 96 TRP HE3 H 8.41 0.05 1 944 . 96 TRP CZ3 C 121.5 0.20 1 945 . 96 TRP CZ2 C 116.0 0.20 1 946 . 96 TRP HZ3 H 6.85 0.05 1 947 . 96 TRP CH2 C 124.8 0.20 1 948 . 96 TRP HZ2 H 7.38 0.05 1 949 . 96 TRP HH2 H 7.22 0.05 1 950 . 97 SER CA C 53.2 0.20 1 951 . 97 SER HA H 4.56 0.05 1 952 . 97 SER CB C 64.7 0.20 1 953 . 97 SER HB2 H 3.34 0.05 2 954 . 97 SER HB3 H 2.25 0.05 2 955 . 98 PRO CD C 51.2 0.20 1 956 . 98 PRO CA C 63.6 0.20 1 957 . 98 PRO HA H 4.52 0.05 1 958 . 98 PRO CB C 32.0 0.20 1 959 . 98 PRO HB2 H 1.85 0.05 1 960 . 98 PRO HB3 H 2.08 0.05 1 961 . 98 PRO CG C 27.4 0.20 1 962 . 98 PRO HG2 H 2.00 0.05 1 963 . 98 PRO HG3 H 1.86 0.05 1 964 . 98 PRO HD2 H 3.62 0.05 1 965 . 98 PRO HD3 H 3.62 0.05 1 966 . 99 THR N N 107.3 0.15 1 967 . 99 THR H H 6.96 0.05 1 968 . 99 THR CA C 62.5 0.20 1 969 . 99 THR HA H 3.96 0.05 1 970 . 99 THR CB C 68.8 0.20 1 971 . 99 THR HB H 4.00 0.05 1 972 . 99 THR HG2 H 0.97 0.05 1 973 . 99 THR CG2 C 11.7 0.20 1 974 . 100 TYR N N 122.8 0.15 1 975 . 100 TYR H H 7.11 0.05 1 976 . 100 TYR CA C 56.4 0.20 1 977 . 100 TYR HA H 4.49 0.05 1 978 . 100 TYR CB C 37.7 0.20 1 979 . 100 TYR HB2 H 2.76 0.05 1 980 . 100 TYR HB3 H 2.38 0.05 1 981 . 100 TYR HD1 H 6.78 0.05 1 982 . 100 TYR HD2 H 6.78 0.05 1 983 . 100 TYR HE1 H 6.82 0.05 1 984 . 100 TYR HE2 H 6.82 0.05 1 985 . 100 TYR CD1 C 131.6 0.20 1 986 . 100 TYR CE1 C 118.3 0.20 1 987 . 101 ASP N N 115.7 0.15 1 988 . 101 ASP H H 7.80 0.05 1 989 . 101 ASP CA C 51.5 0.20 1 990 . 101 ASP HA H 5.07 0.05 1 991 . 101 ASP CB C 43.6 0.20 1 992 . 101 ASP HB2 H 2.75 0.05 2 993 . 101 ASP HB3 H 3.15 0.05 2 994 . 102 VAL N N 117.0 0.15 1 995 . 102 VAL H H 7.51 0.05 1 996 . 102 VAL CA C 68.0 0.20 1 997 . 102 VAL HA H 3.48 0.05 1 998 . 102 VAL CB C 31.4 0.20 1 999 . 102 VAL HB H 1.78 0.05 1 1000 . 102 VAL HG1 H 0.77 0.05 1 1001 . 102 VAL HG2 H 0.53 0.05 1 1002 . 102 VAL CG1 C 21.8 0.20 1 1003 . 102 VAL CG2 C 23.2 0.20 1 1004 . 103 SER N N 114.5 0.15 1 1005 . 103 SER H H 8.03 0.05 1 1006 . 103 SER CA C 63.7 0.20 1 1007 . 103 SER HA H 3.94 0.05 1 1008 . 103 SER CB C 62.8 0.20 1 1009 . 103 SER HB2 H 4.05 0.05 1 1010 . 103 SER HB3 H 4.05 0.05 1 1011 . 104 SER N N 116.7 0.15 1 1012 . 104 SER H H 8.31 0.05 1 1013 . 104 SER CA C 61.6 0.20 1 1014 . 104 SER HA H 4.34 0.05 1 1015 . 104 SER CB C 62.1 0.20 1 1016 . 104 SER HB2 H 4.06 0.05 2 1017 . 104 SER HB3 H 3.89 0.05 2 1018 . 105 ILE N N 123.5 0.15 1 1019 . 105 ILE H H 8.30 0.05 1 1020 . 105 ILE CA C 66.0 0.20 1 1021 . 105 ILE HA H 3.50 0.05 1 1022 . 105 ILE CB C 38.5 0.20 1 1023 . 105 ILE HB H 2.07 0.05 1 1024 . 105 ILE HG2 H 0.70 0.05 1 1025 . 105 ILE CG2 C 17.0 0.20 1 1026 . 105 ILE CG1 C 28.6 0.20 1 1027 . 105 ILE HG12 H 0.94 0.05 2 1028 . 105 ILE HG13 H 2.17 0.05 2 1029 . 105 ILE HD1 H 0.90 0.05 1 1030 . 105 ILE CD1 C 14.3 0.20 1 1031 . 106 LEU N N 117.1 0.15 1 1032 . 106 LEU H H 8.28 0.05 1 1033 . 106 LEU CA C 58.5 0.20 1 1034 . 106 LEU HA H 3.88 0.05 1 1035 . 106 LEU CB C 41.4 0.20 1 1036 . 106 LEU HB2 H 2.02 0.05 1 1037 . 106 LEU HB3 H 1.27 0.05 1 1038 . 106 LEU CG C 26.6 0.20 1 1039 . 106 LEU HG H 1.92 0.05 1 1040 . 106 LEU HD1 H 0.75 0.05 1 1041 . 106 LEU HD2 H 0.63 0.05 1 1042 . 106 LEU CD1 C 26.2 0.20 1 1043 . 106 LEU CD2 C 22.5 0.20 1 1044 . 107 THR N N 111.5 0.15 1 1045 . 107 THR H H 8.57 0.05 1 1046 . 107 THR CA C 66.0 0.20 1 1047 . 107 THR HA H 4.13 0.05 1 1048 . 107 THR CB C 68.4 0.20 1 1049 . 107 THR HB H 4.31 0.05 1 1050 . 107 THR HG2 H 1.38 0.05 1 1051 . 107 THR CG2 C 22.5 0.20 1 1052 . 108 SER N N 120.0 0.15 1 1053 . 108 SER H H 7.95 0.05 1 1054 . 108 SER CA C 63.1 0.20 1 1055 . 108 SER HA H 4.27 0.05 1 1056 . 108 SER CB C 62.8 0.20 1 1057 . 108 SER HB2 H 4.12 0.05 1 1058 . 108 SER HB3 H 3.82 0.05 1 1059 . 109 ILE N N 122.6 0.15 1 1060 . 109 ILE H H 7.94 0.05 1 1061 . 109 ILE CA C 65.4 0.20 1 1062 . 109 ILE HA H 3.48 0.05 1 1063 . 109 ILE CB C 37.6 0.20 1 1064 . 109 ILE HB H 1.74 0.05 1 1065 . 109 ILE HG2 H 0.61 0.05 1 1066 . 109 ILE CG2 C 18.6 0.20 1 1067 . 109 ILE CG1 C 29.9 0.20 1 1068 . 109 ILE HG12 H 1.89 0.05 1 1069 . 109 ILE HG13 H 0.62 0.05 1 1070 . 109 ILE HD1 H 0.50 0.05 1 1071 . 109 ILE CD1 C 15.4 0.20 1 1072 . 110 GLN N N 119.1 0.15 1 1073 . 110 GLN H H 8.05 0.05 1 1074 . 110 GLN CA C 60.4 0.20 1 1075 . 110 GLN HA H 3.68 0.05 1 1076 . 110 GLN CB C 29.8 0.20 1 1077 . 110 GLN HB2 H 2.01 0.05 2 1078 . 110 GLN HB3 H 2.42 0.05 2 1079 . 110 GLN CG C 34.4 0.20 1 1080 . 110 GLN HG2 H 2.42 0.05 2 1081 . 110 GLN HG3 H 2.26 0.05 2 1082 . 110 GLN NE2 N 113.3 0.15 1 1083 . 110 GLN HE21 H 6.86 0.05 1 1084 . 110 GLN HE22 H 7.73 0.05 1 1085 . 111 SER N N 112.6 0.15 1 1086 . 111 SER H H 8.11 0.05 1 1087 . 111 SER CA C 61.7 0.20 1 1088 . 111 SER HA H 4.31 0.05 1 1089 . 111 SER CB C 63.0 0.20 1 1090 . 111 SER HB2 H 4.04 0.05 1 1091 . 111 SER HB3 H 4.04 0.05 1 1092 . 112 LEU N N 122.3 0.15 1 1093 . 112 LEU H H 7.51 0.05 1 1094 . 112 LEU CA C 56.3 0.20 1 1095 . 112 LEU HA H 4.14 0.05 1 1096 . 112 LEU CB C 42.5 0.20 1 1097 . 112 LEU HB2 H 1.79 0.05 2 1098 . 112 LEU HB3 H 1.63 0.05 2 1099 . 112 LEU CG C 26.7 0.20 1 1100 . 112 LEU HG H 1.66 0.05 1 1101 . 112 LEU HD1 H 0.98 0.05 1 1102 . 112 LEU HD2 H 0.72 0.05 1 1103 . 112 LEU CD1 C 24.4 0.20 1 1104 . 112 LEU CD2 C 25.2 0.20 1 1105 . 113 LEU N N 116.3 0.15 1 1106 . 113 LEU H H 7.34 0.05 1 1107 . 113 LEU CA C 57.8 0.20 1 1108 . 113 LEU HA H 3.48 0.05 1 1109 . 113 LEU CB C 39.6 0.20 1 1110 . 113 LEU HB2 H 1.77 0.05 1 1111 . 113 LEU HB3 H 0.55 0.05 1 1112 . 113 LEU CG C 26.2 0.20 1 1113 . 113 LEU HG H 1.55 0.05 1 1114 . 113 LEU HD1 H 0.53 0.05 1 1115 . 113 LEU HD2 H -0.30 0.05 1 1116 . 113 LEU CD1 C 25.7 0.20 1 1117 . 113 LEU CD2 C 21.0 0.20 1 1118 . 114 ASP N N 114.7 0.15 1 1119 . 114 ASP H H 7.31 0.05 1 1120 . 114 ASP CA C 55.3 0.20 1 1121 . 114 ASP HA H 4.84 0.05 1 1122 . 114 ASP CB C 43.5 0.20 1 1123 . 114 ASP HB2 H 2.98 0.05 1 1124 . 114 ASP HB3 H 2.59 0.05 1 1125 . 115 GLU N N 117.5 0.15 1 1126 . 115 GLU H H 7.71 0.05 1 1127 . 115 GLU CA C 53.2 0.20 1 1128 . 115 GLU HA H 4.77 0.05 1 1129 . 115 GLU CB C 31.3 0.20 1 1130 . 115 GLU HB2 H 2.03 0.05 1 1131 . 115 GLU HB3 H 1.84 0.05 1 1132 . 115 GLU CG C 36.4 0.20 1 1133 . 115 GLU HG2 H 2.21 0.05 1 1134 . 115 GLU HG3 H 2.21 0.05 1 1135 . 116 PRO CD C 50.5 0.20 1 1136 . 116 PRO CA C 62.3 0.20 1 1137 . 116 PRO HA H 4.47 0.05 1 1138 . 116 PRO CB C 32.5 0.20 1 1139 . 116 PRO HB2 H 1.38 0.05 2 1140 . 116 PRO HB3 H 0.90 0.05 2 1141 . 116 PRO HG3 H 1.44 0.05 1 1142 . 116 PRO HD2 H 3.49 0.05 2 1143 . 116 PRO HD3 H 3.40 0.05 2 1144 . 117 ASN N N 119.3 0.15 1 1145 . 117 ASN H H 9.45 0.05 1 1146 . 117 ASN CA C 49.8 0.20 1 1147 . 117 ASN HA H 5.19 0.05 1 1148 . 117 ASN CB C 39.3 0.20 1 1149 . 117 ASN HB2 H 3.01 0.05 1 1150 . 117 ASN HB3 H 2.78 0.05 1 1151 . 117 ASN ND2 N 112.1 0.15 1 1152 . 117 ASN HD21 H 7.04 0.05 1 1153 . 117 ASN HD22 H 7.52 0.05 1 1154 . 118 PRO CD C 51.3 0.20 1 1155 . 118 PRO CA C 64.0 0.20 1 1156 . 118 PRO HA H 4.11 0.05 1 1157 . 118 PRO CB C 32.3 0.20 1 1158 . 118 PRO HB2 H 2.05 0.05 1 1159 . 118 PRO HB3 H 2.14 0.05 1 1160 . 118 PRO CG C 26.9 0.20 1 1161 . 118 PRO HG2 H 2.01 0.05 1 1162 . 118 PRO HG3 H 2.01 0.05 1 1163 . 118 PRO HD2 H 3.95 0.05 1 1164 . 118 PRO HD3 H 3.83 0.05 1 1165 . 119 ASN N N 114.8 0.15 1 1166 . 119 ASN H H 7.98 0.05 1 1167 . 119 ASN CA C 54.0 0.20 1 1168 . 119 ASN HA H 4.63 0.05 1 1169 . 119 ASN CB C 38.8 0.20 1 1170 . 119 ASN HB2 H 2.87 0.05 1 1171 . 119 ASN HB3 H 2.78 0.05 1 1172 . 119 ASN ND2 N 114.0 0.15 1 1173 . 119 ASN HD21 H 6.98 0.05 1 1174 . 119 ASN HD22 H 7.63 0.05 1 1175 . 120 SER N N 113.0 0.15 1 1176 . 120 SER H H 7.00 0.05 1 1177 . 120 SER CA C 55.2 0.20 1 1178 . 120 SER HA H 4.75 0.05 1 1179 . 120 SER CB C 63.9 0.20 1 1180 . 120 SER HB2 H 3.92 0.05 2 1181 . 120 SER HB3 H 3.58 0.05 2 1182 . 121 PRO CD C 49.9 0.20 1 1183 . 121 PRO CA C 62.7 0.20 1 1184 . 121 PRO HA H 4.16 0.05 1 1185 . 121 PRO CB C 30.7 0.20 1 1186 . 121 PRO HB2 H 1.73 0.05 1 1187 . 121 PRO HB3 H 1.84 0.05 1 1188 . 121 PRO CG C 27.3 0.20 1 1189 . 121 PRO HG2 H 2.02 0.05 1 1190 . 121 PRO HG3 H 2.02 0.05 1 1191 . 121 PRO HD2 H 3.30 0.05 1 1192 . 121 PRO HD3 H 3.50 0.05 1 1193 . 122 ALA N N 128.4 0.15 1 1194 . 122 ALA H H 8.51 0.05 1 1195 . 122 ALA CA C 53.5 0.20 1 1196 . 122 ALA HA H 3.81 0.05 1 1197 . 122 ALA HB H 0.14 0.05 1 1198 . 122 ALA CB C 18.3 0.20 1 1199 . 123 ASN N N 114.7 0.15 1 1200 . 123 ASN H H 7.24 0.05 1 1201 . 123 ASN CA C 51.3 0.20 1 1202 . 123 ASN HA H 4.80 0.05 1 1203 . 123 ASN CB C 38.4 0.20 1 1204 . 123 ASN HB2 H 3.01 0.05 1 1205 . 123 ASN HB3 H 3.01 0.05 1 1206 . 123 ASN ND2 N 112.2 0.15 1 1207 . 123 ASN HD21 H 6.32 0.05 1 1208 . 123 ASN HD22 H 8.39 0.05 1 1209 . 124 SER CA C 61.9 0.20 1 1210 . 124 SER HA H 3.94 0.05 1 1211 . 124 SER CB C 62.7 0.20 1 1212 . 124 SER HB2 H 3.94 0.05 1 1213 . 124 SER HB3 H 3.94 0.05 1 1214 . 125 GLN N N 122.4 0.15 1 1215 . 125 GLN H H 8.21 0.05 1 1216 . 125 GLN CA C 59.2 0.20 1 1217 . 125 GLN HA H 4.26 0.05 1 1218 . 125 GLN CB C 28.7 0.20 1 1219 . 125 GLN HB2 H 2.30 0.05 1 1220 . 125 GLN HB3 H 2.30 0.05 1 1221 . 125 GLN CG C 34.6 0.20 1 1222 . 125 GLN HG2 H 2.62 0.05 2 1223 . 125 GLN HG3 H 2.44 0.05 2 1224 . 125 GLN NE2 N 111.3 0.15 1 1225 . 125 GLN HE21 H 6.92 0.05 1 1226 . 125 GLN HE22 H 7.60 0.05 1 1227 . 126 ALA N N 120.2 0.15 1 1228 . 126 ALA H H 7.22 0.05 1 1229 . 126 ALA CA C 54.9 0.20 1 1230 . 126 ALA HA H 3.82 0.05 1 1231 . 126 ALA HB H 0.12 0.05 1 1232 . 126 ALA CB C 16.6 0.20 1 1233 . 127 ALA N N 118.5 0.15 1 1234 . 127 ALA H H 8.22 0.05 1 1235 . 127 ALA CA C 55.6 0.20 1 1236 . 127 ALA HA H 3.69 0.05 1 1237 . 127 ALA HB H 1.46 0.05 1 1238 . 127 ALA CB C 18.7 0.20 1 1239 . 128 GLN N N 117.4 0.15 1 1240 . 128 GLN H H 8.03 0.05 1 1241 . 128 GLN CA C 59.2 0.20 1 1242 . 128 GLN HA H 4.08 0.05 1 1243 . 128 GLN CB C 27.9 0.20 1 1244 . 128 GLN HB2 H 2.21 0.05 1 1245 . 128 GLN HB3 H 2.21 0.05 1 1246 . 128 GLN CG C 33.5 0.20 1 1247 . 128 GLN HG2 H 2.48 0.05 2 1248 . 128 GLN HG3 H 2.29 0.05 2 1249 . 128 GLN NE2 N 111.0 0.15 1 1250 . 128 GLN HE21 H 6.67 0.05 1 1251 . 128 GLN HE22 H 7.62 0.05 1 1252 . 129 LEU N N 118.5 0.15 1 1253 . 129 LEU H H 8.11 0.05 1 1254 . 129 LEU CA C 57.9 0.20 1 1255 . 129 LEU HA H 4.06 0.05 1 1256 . 129 LEU CB C 43.0 0.20 1 1257 . 129 LEU HB2 H 2.07 0.05 1 1258 . 129 LEU HB3 H 1.68 0.05 1 1259 . 129 LEU CG C 27.0 0.20 1 1260 . 129 LEU HG H 2.12 0.05 1 1261 . 129 LEU HD1 H 1.07 0.05 1 1262 . 129 LEU HD2 H 1.04 0.05 1 1263 . 129 LEU CD1 C 25.9 0.20 1 1264 . 129 LEU CD2 C 24.0 0.20 1 1265 . 130 TYR N N 117.1 0.15 1 1266 . 130 TYR H H 8.28 0.05 1 1267 . 130 TYR CA C 62.0 0.20 1 1268 . 130 TYR HA H 3.17 0.05 1 1269 . 130 TYR CB C 38.2 0.20 1 1270 . 130 TYR HB2 H 2.62 0.05 2 1271 . 130 TYR HB3 H 2.34 0.05 2 1272 . 130 TYR HD1 H 6.24 0.05 1 1273 . 130 TYR HD2 H 6.24 0.05 1 1274 . 130 TYR HE1 H 6.71 0.05 1 1275 . 130 TYR HE2 H 6.71 0.05 1 1276 . 130 TYR CD1 C 132.7 0.20 1 1277 . 130 TYR CE1 C 117.9 0.20 1 1278 . 131 GLN N N 111.2 0.15 1 1279 . 131 GLN H H 7.14 0.05 1 1280 . 131 GLN CA C 57.8 0.20 1 1281 . 131 GLN HA H 3.98 0.05 1 1282 . 131 GLN CB C 30.6 0.20 1 1283 . 131 GLN HB2 H 2.15 0.05 1 1284 . 131 GLN HB3 H 2.15 0.05 1 1285 . 131 GLN CG C 34.6 0.20 1 1286 . 131 GLN HG2 H 2.54 0.05 2 1287 . 131 GLN HG3 H 2.37 0.05 2 1288 . 131 GLN NE2 N 110.9 0.15 1 1289 . 131 GLN HE21 H 6.81 0.05 1 1290 . 131 GLN HE22 H 7.36 0.05 1 1291 . 132 GLU N N 115.4 0.15 1 1292 . 132 GLU H H 8.26 0.05 1 1293 . 132 GLU CA C 57.4 0.20 1 1294 . 132 GLU HA H 4.40 0.05 1 1295 . 132 GLU CB C 32.3 0.20 1 1296 . 132 GLU HB2 H 2.00 0.05 1 1297 . 132 GLU HB3 H 2.07 0.05 1 1298 . 132 GLU CG C 36.4 0.20 1 1299 . 132 GLU HG2 H 2.40 0.05 2 1300 . 132 GLU HG3 H 2.28 0.05 2 1301 . 133 ASN N N 119.8 0.15 1 1302 . 133 ASN H H 9.11 0.05 1 1303 . 133 ASN CA C 52.0 0.20 1 1304 . 133 ASN HA H 4.80 0.05 1 1305 . 133 ASN CB C 37.9 0.20 1 1306 . 133 ASN HB2 H 3.10 0.05 2 1307 . 133 ASN HB3 H 2.65 0.05 2 1308 . 134 LYS N N 124.9 0.15 1 1309 . 134 LYS H H 8.70 0.05 1 1310 . 134 LYS CA C 59.6 0.20 1 1311 . 134 LYS HA H 3.94 0.05 1 1312 . 134 LYS CB C 32.5 0.20 1 1313 . 134 LYS HB2 H 1.83 0.05 1 1314 . 134 LYS HB3 H 1.83 0.05 1 1315 . 134 LYS CG C 25.6 0.20 1 1316 . 134 LYS HG2 H 1.43 0.05 1 1317 . 134 LYS HG3 H 1.43 0.05 1 1318 . 134 LYS CD C 28.7 0.20 1 1319 . 134 LYS HD2 H 1.57 0.05 1 1320 . 134 LYS HD3 H 1.57 0.05 1 1321 . 134 LYS CE C 42.0 0.20 1 1322 . 134 LYS HE2 H 2.82 0.05 1 1323 . 134 LYS HE3 H 2.82 0.05 1 1324 . 135 ARG N N 117.3 0.15 1 1325 . 135 ARG H H 8.41 0.05 1 1326 . 135 ARG CA C 59.2 0.20 1 1327 . 135 ARG HA H 4.22 0.05 1 1328 . 135 ARG CB C 29.7 0.20 1 1329 . 135 ARG HB2 H 1.91 0.05 1 1330 . 135 ARG HB3 H 1.91 0.05 1 1331 . 135 ARG CG C 27.3 0.20 1 1332 . 135 ARG HG2 H 1.73 0.05 1 1333 . 135 ARG HG3 H 1.73 0.05 1 1334 . 135 ARG CD C 43.1 0.20 1 1335 . 135 ARG HD2 H 3.30 0.05 1 1336 . 135 ARG HD3 H 3.30 0.05 1 1337 . 136 GLU N N 120.0 0.15 1 1338 . 136 GLU H H 7.38 0.05 1 1339 . 136 GLU CA C 58.3 0.20 1 1340 . 136 GLU HA H 4.14 0.05 1 1341 . 136 GLU CB C 29.6 0.20 1 1342 . 136 GLU HB2 H 1.97 0.05 1 1343 . 136 GLU HB3 H 1.97 0.05 1 1344 . 136 GLU CG C 35.9 0.20 1 1345 . 136 GLU HG2 H 2.33 0.05 2 1346 . 136 GLU HG3 H 2.27 0.05 2 1347 . 137 TYR N N 120.4 0.15 1 1348 . 137 TYR H H 8.39 0.05 1 1349 . 137 TYR CA C 62.8 0.20 1 1350 . 137 TYR HA H 4.05 0.05 1 1351 . 137 TYR CB C 38.0 0.20 1 1352 . 137 TYR HB2 H 2.89 0.05 1 1353 . 137 TYR HB3 H 3.44 0.05 1 1354 . 137 TYR HD1 H 7.21 0.05 1 1355 . 137 TYR HD2 H 7.21 0.05 1 1356 . 137 TYR HE1 H 6.73 0.05 1 1357 . 137 TYR HE2 H 6.73 0.05 1 1358 . 137 TYR CD1 C 132.9 0.20 1 1359 . 137 TYR CE1 C 118.6 0.20 1 1360 . 138 GLU N N 116.7 0.15 1 1361 . 138 GLU H H 8.67 0.05 1 1362 . 138 GLU CA C 60.3 0.20 1 1363 . 138 GLU HA H 3.56 0.05 1 1364 . 138 GLU CB C 29.1 0.20 1 1365 . 138 GLU HB2 H 2.29 0.05 1 1366 . 138 GLU HB3 H 2.08 0.05 1 1367 . 138 GLU CG C 37.9 0.20 1 1368 . 138 GLU HG2 H 2.86 0.05 2 1369 . 138 GLU HG3 H 2.20 0.05 2 1370 . 139 LYS N N 120.5 0.15 1 1371 . 139 LYS H H 7.75 0.05 1 1372 . 139 LYS CA C 59.7 0.20 1 1373 . 139 LYS HA H 4.00 0.05 1 1374 . 139 LYS CB C 32.5 0.20 1 1375 . 139 LYS HB2 H 1.92 0.05 1 1376 . 139 LYS HB3 H 1.92 0.05 1 1377 . 139 LYS CG C 25.0 0.20 1 1378 . 139 LYS HG2 H 1.57 0.05 2 1379 . 139 LYS HG3 H 1.37 0.05 2 1380 . 139 LYS CD C 29.4 0.20 1 1381 . 139 LYS HD2 H 1.67 0.05 1 1382 . 139 LYS HD3 H 1.67 0.05 1 1383 . 139 LYS CE C 41.8 0.20 1 1384 . 139 LYS HE2 H 2.90 0.05 1 1385 . 139 LYS HE3 H 2.90 0.05 1 1386 . 140 ARG N N 119.9 0.15 1 1387 . 140 ARG H H 7.88 0.05 1 1388 . 140 ARG CA C 57.9 0.20 1 1389 . 140 ARG HA H 3.77 0.05 1 1390 . 140 ARG CB C 28.8 0.20 1 1391 . 140 ARG HB2 H 0.64 0.05 1 1392 . 140 ARG HB3 H 1.49 0.05 1 1393 . 140 ARG CG C 26.9 0.20 1 1394 . 140 ARG HG2 H 1.29 0.05 1 1395 . 140 ARG HG3 H 1.29 0.05 1 1396 . 140 ARG CD C 41.8 0.20 1 1397 . 140 ARG HD2 H 2.62 0.05 2 1398 . 140 ARG HD3 H 2.70 0.05 2 1399 . 141 VAL N N 120.1 0.15 1 1400 . 141 VAL H H 8.16 0.05 1 1401 . 141 VAL CA C 66.8 0.20 1 1402 . 141 VAL HA H 3.33 0.05 1 1403 . 141 VAL CB C 31.4 0.20 1 1404 . 141 VAL HB H 1.53 0.05 1 1405 . 141 VAL HG1 H -0.22 0.05 1 1406 . 141 VAL HG2 H 0.51 0.05 1 1407 . 141 VAL CG1 C 21.1 0.20 1 1408 . 141 VAL CG2 C 23.2 0.20 1 1409 . 142 SER N N 115.9 0.15 1 1410 . 142 SER H H 8.35 0.05 1 1411 . 142 SER CA C 62.5 0.20 1 1412 . 142 SER HA H 3.99 0.05 1 1413 . 142 SER CB C 62.5 0.20 1 1414 . 142 SER HB2 H 3.99 0.05 1 1415 . 142 SER HB3 H 3.99 0.05 1 1416 . 143 ALA N N 121.4 0.15 1 1417 . 143 ALA H H 7.09 0.05 1 1418 . 143 ALA CA C 54.9 0.20 1 1419 . 143 ALA HA H 4.18 0.05 1 1420 . 143 ALA HB H 1.40 0.05 1 1421 . 143 ALA CB C 18.1 0.20 1 1422 . 144 ILE N N 116.4 0.15 1 1423 . 144 ILE H H 7.26 0.05 1 1424 . 144 ILE CA C 62.1 0.20 1 1425 . 144 ILE HA H 4.05 0.05 1 1426 . 144 ILE CB C 37.5 0.20 1 1427 . 144 ILE HB H 2.37 0.05 1 1428 . 144 ILE HG2 H 1.02 0.05 1 1429 . 144 ILE CG2 C 20.8 0.20 1 1430 . 144 ILE CG1 C 28.7 0.20 1 1431 . 144 ILE HG12 H 1.72 0.05 2 1432 . 144 ILE HG13 H 1.43 0.05 2 1433 . 144 ILE HD1 H 0.92 0.05 1 1434 . 144 ILE CD1 C 13.2 0.20 1 1435 . 145 VAL N N 125.3 0.15 1 1436 . 145 VAL H H 8.52 0.05 1 1437 . 145 VAL CA C 67.4 0.20 1 1438 . 145 VAL HA H 3.41 0.05 1 1439 . 145 VAL CB C 31.4 0.20 1 1440 . 145 VAL HB H 2.27 0.05 1 1441 . 145 VAL HG1 H 0.69 0.05 1 1442 . 145 VAL HG2 H 1.19 0.05 1 1443 . 145 VAL CG1 C 20.5 0.20 1 1444 . 145 VAL CG2 C 24.2 0.20 1 1445 . 146 GLU N N 119.4 0.15 1 1446 . 146 GLU H H 7.51 0.05 1 1447 . 146 GLU CA C 58.1 0.20 1 1448 . 146 GLU HA H 2.44 0.05 1 1449 . 146 GLU CB C 28.9 0.20 1 1450 . 146 GLU HB2 H 2.40 0.05 2 1451 . 146 GLU HB3 H 1.80 0.05 2 1452 . 146 GLU CG C 36.2 0.20 1 1453 . 146 GLU HG2 H 2.23 0.05 2 1454 . 146 GLU HG3 H 1.96 0.05 2 1455 . 147 GLN N N 116.4 0.15 1 1456 . 147 GLN H H 7.60 0.05 1 1457 . 147 GLN CA C 58.2 0.20 1 1458 . 147 GLN HA H 4.03 0.05 1 1459 . 147 GLN CB C 28.6 0.20 1 1460 . 147 GLN HB2 H 2.20 0.05 1 1461 . 147 GLN HB3 H 2.07 0.05 1 1462 . 147 GLN CG C 34.6 0.20 1 1463 . 147 GLN HG2 H 2.54 0.05 1 1464 . 147 GLN HG3 H 2.54 0.05 1 1465 . 147 GLN NE2 N 110.4 0.15 1 1466 . 147 GLN HE21 H 6.68 0.05 1 1467 . 147 GLN HE22 H 7.27 0.05 1 1468 . 148 SER N N 116.5 0.15 1 1469 . 148 SER H H 7.60 0.05 1 1470 . 148 SER CA C 61.1 0.20 1 1471 . 148 SER HA H 4.38 0.05 1 1472 . 148 SER CB C 62.7 0.20 1 1473 . 148 SER HB2 H 4.09 0.05 1 1474 . 148 SER HB3 H 4.09 0.05 1 1475 . 149 TRP N N 121.5 0.15 1 1476 . 149 TRP H H 7.02 0.05 1 1477 . 149 TRP CA C 56.3 0.20 1 1478 . 149 TRP HA H 4.84 0.05 1 1479 . 149 TRP CB C 28.8 0.20 1 1480 . 149 TRP HB2 H 3.42 0.05 1 1481 . 149 TRP HB3 H 3.28 0.05 1 1482 . 149 TRP CD1 C 125.6 0.20 1 1483 . 149 TRP CE3 C 121.2 0.20 1 1484 . 149 TRP HD1 H 7.26 0.05 1 1485 . 149 TRP NE1 N 128.3 0.15 1 1486 . 149 TRP HE1 H 9.91 0.05 1 1487 . 149 TRP HE3 H 7.65 0.05 1 1488 . 149 TRP CZ3 C 121.6 0.20 1 1489 . 149 TRP CZ2 C 114.4 0.20 1 1490 . 149 TRP HZ3 H 7.13 0.05 1 1491 . 149 TRP CH2 C 124.3 0.20 1 1492 . 149 TRP HZ2 H 7.24 0.05 1 1493 . 149 TRP HH2 H 7.21 0.05 1 1494 . 150 ASN N N 116.7 0.15 1 1495 . 150 ASN H H 7.81 0.05 1 1496 . 150 ASN CA C 53.3 0.20 1 1497 . 150 ASN HA H 4.85 0.05 1 1498 . 150 ASN CB C 39.7 0.20 1 1499 . 150 ASN HB2 H 2.75 0.05 2 1500 . 150 ASN HB3 H 2.93 0.05 2 1501 . 150 ASN ND2 N 112.9 0.15 1 1502 . 150 ASN HD21 H 6.99 0.05 1 1503 . 150 ASN HD22 H 7.58 0.05 1 1504 . 151 ASP N N 121.2 0.15 1 1505 . 151 ASP H H 8.06 0.05 1 1506 . 151 ASP CA C 54.5 0.20 1 1507 . 151 ASP HA H 4.74 0.05 1 1508 . 151 ASP CB C 41.3 0.20 1 1509 . 151 ASP HB2 H 2.80 0.05 1 1510 . 151 ASP HB3 H 2.80 0.05 1 1511 . 152 SER N N 120.7 0.15 1 1512 . 152 SER H H 7.84 0.05 1 1513 . 152 SER CA C 60.2 0.20 1 1514 . 152 SER HA H 4.27 0.05 1 1515 . 152 SER CB C 65.0 0.20 1 1516 . 152 SER HB2 H 3.88 0.05 1 1517 . 152 SER HB3 H 3.88 0.05 1 stop_ save_