data_4089 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Peptide Deformylase Catalytic Core (Residues 1 - 147) ; _BMRB_accession_number 4089 _BMRB_flat_file_name bmr4089.str _Entry_type original _Submission_date 1997-12-31 _Accession_date 1997-12-31 _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 MEINNEL T. . . 2 DARDEL F. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 898 "13C chemical shifts" 487 "15N chemical shifts" 160 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 1999-06-09 original author . stop_ _Original_release_date 1999-06-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; DARDEL, F., RAGUSA, S., LAZENNEC, C., BLANQUET, S., and MEINNEL, T., "Solution Structure of Nickel-peptide Deformylase," J. Mol. Biol. 280, 501-513 (1998). ; _Citation_title 'Solution Structure of Nickel-peptide Deformylase' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 98332750 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 DARDEL F. . . 2 RAGUSA S. . . 3 LAZENNEC C. . . 4 BLANQUET S. . . 5 MEINNEL T. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 280 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 501 _Page_last 513 _Year 1998 _Details . loop_ _Keyword hydrolase metalloprotease stop_ save_ ################################## # Molecular system description # ################################## save_system_peptide_deformylase _Saveframe_category molecular_system _Mol_system_name 'peptide deformylase' _Abbreviation_common 'peptide deformylase' _Enzyme_commission_number 3.5.1.31 loop_ _Mol_system_component_name _Mol_label 'peptide deformylase' $peptide_deformylase Ni $NI stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic yes _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_peptide_deformylase _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'peptide deformylase' _Name_variant 'S 1 A' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 147 _Mol_residue_sequence ; AVLQVLHIPDERLRKVAKPV EEVNAEIQRIVDDMFETMYA EEGIGLAATQVDIHQRIIVI DVSENRDERLVLINPELLEK SGETGIEEGCLSIPEQRALV PRAEKVKIRALDRDGKPFEL EADGLLAICIQHEMDHLVGK LFMDYLS ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ALA 2 2 VAL 3 3 LEU 4 4 GLN 5 5 VAL 6 6 LEU 7 7 HIS 8 8 ILE 9 9 PRO 10 10 ASP 11 11 GLU 12 12 ARG 13 13 LEU 14 14 ARG 15 15 LYS 16 16 VAL 17 17 ALA 18 18 LYS 19 19 PRO 20 20 VAL 21 21 GLU 22 22 GLU 23 23 VAL 24 24 ASN 25 25 ALA 26 26 GLU 27 27 ILE 28 28 GLN 29 29 ARG 30 30 ILE 31 31 VAL 32 32 ASP 33 33 ASP 34 34 MET 35 35 PHE 36 36 GLU 37 37 THR 38 38 MET 39 39 TYR 40 40 ALA 41 41 GLU 42 42 GLU 43 43 GLY 44 44 ILE 45 45 GLY 46 46 LEU 47 47 ALA 48 48 ALA 49 49 THR 50 50 GLN 51 51 VAL 52 52 ASP 53 53 ILE 54 54 HIS 55 55 GLN 56 56 ARG 57 57 ILE 58 58 ILE 59 59 VAL 60 60 ILE 61 61 ASP 62 62 VAL 63 63 SER 64 64 GLU 65 65 ASN 66 66 ARG 67 67 ASP 68 68 GLU 69 69 ARG 70 70 LEU 71 71 VAL 72 72 LEU 73 73 ILE 74 74 ASN 75 75 PRO 76 76 GLU 77 77 LEU 78 78 LEU 79 79 GLU 80 80 LYS 81 81 SER 82 82 GLY 83 83 GLU 84 84 THR 85 85 GLY 86 86 ILE 87 87 GLU 88 88 GLU 89 89 GLY 90 90 CYS 91 91 LEU 92 92 SER 93 93 ILE 94 94 PRO 95 95 GLU 96 96 GLN 97 97 ARG 98 98 ALA 99 99 LEU 100 100 VAL 101 101 PRO 102 102 ARG 103 103 ALA 104 104 GLU 105 105 LYS 106 106 VAL 107 107 LYS 108 108 ILE 109 109 ARG 110 110 ALA 111 111 LEU 112 112 ASP 113 113 ARG 114 114 ASP 115 115 GLY 116 116 LYS 117 117 PRO 118 118 PHE 119 119 GLU 120 120 LEU 121 121 GLU 122 122 ALA 123 123 ASP 124 124 GLY 125 125 LEU 126 126 LEU 127 127 ALA 128 128 ILE 129 129 CYS 130 130 ILE 131 131 GLN 132 132 HIS 133 133 GLU 134 134 MET 135 135 ASP 136 136 HIS 137 137 LEU 138 138 VAL 139 139 GLY 140 140 LYS 141 141 LEU 142 142 PHE 143 143 MET 144 144 ASP 145 145 TYR 146 146 LEU 147 147 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1BS4 "Peptide Deformylase As Zn2+ Containing Form (Native) In Complex With Inhibitor Polyethylene Glycol" 100.00 168 99.32 100.00 1.69e-98 PDB 1BS5 "Peptide Deformylase As Zn2+ Containing Form" 100.00 168 99.32 100.00 1.69e-98 PDB 1BS6 "Peptide Deformylase As Ni2+ Containing Form In Complex With Tripeptide Met-Ala-Ser" 100.00 168 99.32 100.00 1.69e-98 PDB 1BS7 "Peptide Deformylase As Ni2+ Containing Form" 100.00 168 99.32 100.00 1.69e-98 PDB 1BS8 "Peptide Deformylase As Zn2+ Containing Form In Complex With Tripeptide Met-Ala-Ser" 100.00 168 99.32 100.00 1.69e-98 PDB 1BSJ "Cobalt Deformylase Inhibitor Complex From E.Coli" 100.00 168 99.32 100.00 1.69e-98 PDB 1BSK "Zinc Deformylase Inhibitor Complex From E.Coli" 100.00 168 99.32 100.00 1.69e-98 PDB 1BSZ "Peptide Deformylase As Fe2+ Containing Form (Native) In Complex With Inhibitor Polyethylene Glycol" 100.00 168 99.32 100.00 1.69e-98 PDB 1DEF "Peptide Deformylase Catalytic Core (Residues 1-147), Nmr, 9 Structures" 100.00 147 99.32 100.00 2.55e-98 PDB 1DFF "Peptide Deformylase" 100.00 164 99.32 100.00 1.82e-98 PDB 1G27 "Crystal Structure Of E.Coli Polypeptide Deformylase Complexed With The Inhibitor Bb-3497" 100.00 168 99.32 100.00 1.69e-98 PDB 1G2A "The Crystal Structure Of E.Coli Peptide Deformylase Complexed With Actinonin" 100.00 168 99.32 100.00 1.69e-98 PDB 1ICJ "Pdf Protein Is Crystallized As Ni2+ Containing Form, Cocrystallized With Inhibitor Polyethylene Glycol (Peg)" 100.00 168 99.32 100.00 1.69e-98 PDB 1LRU "Crystal Structure Of E.Coli Peptide Deformylase Complexed With Antibiotic Actinonin" 100.00 168 99.32 100.00 1.69e-98 PDB 1XEM "High Resolution Crystal Structure Of Escherichia Coli Zinc- Peptide Deformylase Bound To Formate" 100.00 168 99.32 100.00 1.69e-98 PDB 1XEN "High Resolution Crystal Structure Of Escherichia Coli Iron- Peptide Deformylase Bound To Formate" 100.00 168 99.32 100.00 1.69e-98 PDB 1XEO "High Resolution Crystals Structure Of Cobalt- Peptide Deformylase Bound To Formate" 100.00 168 99.32 100.00 1.69e-98 PDB 2AI8 "E.Coli Polypeptide Deformylase Complexed With Sb-485343" 100.00 168 99.32 100.00 1.69e-98 PDB 2DEF "Peptide Deformylase Catalytic Core (Residues 1-147), Nmr, 20 Structures" 100.00 147 100.00 100.00 1.02e-98 PDB 2KMN "Solution Structure Of Peptide Deformylase Complexed With Actinonin" 100.00 147 99.32 100.00 2.55e-98 PDB 2W3T "Chloro Complex Of The Ni-Form Of E.Coli Deformylase" 100.00 188 99.32 100.00 2.03e-98 PDB 2W3U "Formate Complex Of The Ni-Form Of E.Coli Deformylase" 100.00 188 99.32 100.00 2.03e-98 PDB 3K6L "The Structure Of E.Coli Peptide Deformylase (Pdf) In Complex With Peptidomimetic Ligand Bb2827" 100.00 169 99.32 100.00 1.50e-98 PDB 4AL2 "Peptide Deformylase (Ni-Form) With Hydrosulfide" 100.00 186 99.32 100.00 1.76e-98 PDB 4AL3 "Peptide Deformylase (Co-Form) With Mercaptoethanol" 100.00 186 98.64 99.32 4.70e-97 PDB 4AZ4 "E.Coli Deformylase With Co(Ii) And Hydrosulfide" 100.00 186 98.64 99.32 4.70e-97 DBJ BAB37575 "peptide deformylase [Escherichia coli O157:H7 str. Sakai]" 100.00 169 99.32 100.00 1.50e-98 DBJ BAE78005 "peptide deformylase [Escherichia coli str. K12 substr. W3110]" 100.00 169 99.32 100.00 1.50e-98 DBJ BAG79085 "polypeptide deformylase [Escherichia coli SE11]" 100.00 169 99.32 100.00 1.50e-98 DBJ BAH66202 "N-formylmethionylaminoacyl-tRNA deformylase [Klebsiella pneumoniae subsp. pneumoniae NTUH-K2044]" 100.00 169 97.96 99.32 1.26e-96 DBJ BAI27558 "peptide deformylase [Escherichia coli O26:H11 str. 11368]" 100.00 169 98.64 100.00 6.78e-98 EMBL CAA11508 "hypothetical protein [Escherichia coli]" 88.44 149 97.69 98.46 1.96e-80 EMBL CAA45206 "fms [Escherichia coli K-12]" 100.00 169 99.32 100.00 1.50e-98 EMBL CAA54367 "N-formylmethionylaminoacyl-tRNA deformylase [Escherichia coli K-12]" 100.00 169 99.32 100.00 1.50e-98 EMBL CAA54826 "deformylase [Escherichia coli]" 100.00 169 99.32 100.00 1.50e-98 EMBL CAD09179 "polypeptide deformylase [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 169 97.28 99.32 1.96e-96 GB AAA58084 "N-formylmethionylaminoacyl-tRNA deformylase [Escherichia coli str. K-12 substr. MG1655]" 100.00 169 99.32 100.00 1.50e-98 GB AAC76312 "peptide deformylase [Escherichia coli str. K-12 substr. MG1655]" 100.00 169 99.32 100.00 1.50e-98 GB AAF76758 "unknown [Escherichia coli]" 88.44 150 98.46 100.00 3.35e-83 GB AAG58408 "peptide deformylase [Escherichia coli O157:H7 str. EDL933]" 100.00 169 99.32 100.00 1.50e-98 GB AAL22269 "peptide deformylase [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 169 97.96 99.32 4.79e-97 PIR AB1010 "formylmethionine deformylase (EC 3.5.1.31) - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" 100.00 169 97.28 99.32 1.96e-96 REF NP_312179 "peptide deformylase [Escherichia coli O157:H7 str. Sakai]" 100.00 169 99.32 100.00 1.50e-98 REF NP_417745 "peptide deformylase [Escherichia coli str. K-12 substr. MG1655]" 100.00 169 99.32 100.00 1.50e-98 REF NP_458493 "polypeptide deformylase [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" 100.00 169 97.28 99.32 1.96e-96 REF NP_462310 "peptide deformylase [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" 100.00 169 97.96 99.32 4.79e-97 REF NP_709074 "peptide deformylase [Shigella flexneri 2a str. 301]" 100.00 169 98.64 100.00 6.78e-98 SP A1AGH8 "RecName: Full=Peptide deformylase; Short=PDF; AltName: Full=Polypeptide deformylase" 100.00 169 99.32 100.00 1.50e-98 SP A8A591 "RecName: Full=Peptide deformylase; Short=PDF; AltName: Full=Polypeptide deformylase" 100.00 169 99.32 100.00 1.50e-98 SP A8AQI1 "RecName: Full=Peptide deformylase; Short=PDF; AltName: Full=Polypeptide deformylase" 100.00 169 98.64 99.32 4.11e-97 SP A9MN80 "RecName: Full=Peptide deformylase; Short=PDF; AltName: Full=Polypeptide deformylase" 100.00 169 97.28 99.32 1.96e-96 SP A9N8B1 "RecName: Full=Peptide deformylase; Short=PDF; AltName: Full=Polypeptide deformylase" 100.00 169 97.96 99.32 4.79e-97 stop_ save_ ############# # Ligands # ############# save_NI _Saveframe_category ligand _Mol_type non-polymer _Name_common "NI (NICKEL (II) ION)" _BMRB_code . _PDB_code NI _Molecular_mass 58.693 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Wed Feb 15 15:20:30 2012 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons NI NI NI . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain _Plasmid _Gene_mnemonic _Details $peptide_deformylase . 562 Bacteria . ESCHERICHIA COLI PAL421TR PTDEF-DELTA 'FMS (CODONS 1-147)' ; PTDEF-DELTA WAS OBTAINED BY TRANSFER OF THE FMS GENE INTO PTRC99A. THIS HAS RESULTED IN THE MODIFICATION OF S-1 INTO A-1, WITHOUT ANY DETECTABLE EFFECTS ON THE CATALYTIC PROPERTIES ; 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 $peptide_deformylase 'recombinant technology' 'PUC18 (IPTG-INDUCIBLE LAC PROMOTURCE 5 EXPRESSION_SYSTEM_PLASMID: PDEF-EC1-147' 'PUC18 (IPTG-INDUCIBLE LAC PROMOTURCE 5 EXPRESSION_SYSTEM_PLASMID: PDEF-EC1-147' . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'dummy saveframe for use in entries where relevant information is missing' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'data not available' . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ save_NMR_spectrometer_two _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY _Sample_label $sample_1 save_ save_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label $sample_1 save_ save_CT-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name CT-HSQC _Sample_label $sample_1 save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label $sample_1 save_ save_NOESY-HMQC_5 _Saveframe_category NMR_applied_experiment _Experiment_name NOESY-HMQC _Sample_label $sample_1 save_ save_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_HMBC-HSQC,HNHB_7 _Saveframe_category NMR_applied_experiment _Experiment_name HMBC-HSQC,HNHB _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 20 . mM pH 7.2 . na pressure 1 . atm temperature 318 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_ref _Saveframe_category chemical_shift_reference _Details . 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_chem_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 $chem_shift_ref _Mol_system_component_name 'peptide deformylase' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 1 ALA HA H 3.92 0.01 1 2 . 1 ALA HB H 1.25 0.01 1 3 . 1 ALA CA C 51.3 0.3 1 4 . 1 ALA CB C 19.7 0.3 1 5 . 2 VAL H H 8.09 0.01 1 6 . 2 VAL HA H 4.02 0.01 1 7 . 2 VAL HB H 1.89 0.01 1 8 . 2 VAL HG1 H 0.93 0.01 2 9 . 2 VAL HG2 H 0.95 0.01 2 10 . 2 VAL CA C 62.3 0.3 1 11 . 2 VAL CB C 32.1 0.3 1 12 . 2 VAL CG1 C 21.9 0.3 2 13 . 2 VAL CG2 C 21.5 0.3 2 14 . 2 VAL N N 117.8 0.2 1 15 . 3 LEU H H 8.65 0.01 1 16 . 3 LEU HA H 4.42 0.01 1 17 . 3 LEU HB2 H 1.57 0.01 1 18 . 3 LEU HB3 H 1.50 0.01 1 19 . 3 LEU HG H 1.48 0.01 1 20 . 3 LEU HD1 H 0.78 0.01 1 21 . 3 LEU HD2 H 0.76 0.01 1 22 . 3 LEU CA C 53.1 0.3 1 23 . 3 LEU CB C 42.4 0.3 1 24 . 3 LEU CG C 26.8 0.3 1 25 . 3 LEU CD1 C 25.4 0.3 1 26 . 3 LEU CD2 C 21.5 0.3 1 27 . 3 LEU N N 127.1 0.2 1 28 . 4 GLN H H 8.05 0.01 1 29 . 4 GLN HA H 4.10 0.01 1 30 . 4 GLN HB2 H 1.90 0.01 1 31 . 4 GLN HB3 H 1.90 0.01 1 32 . 4 GLN HG2 H 2.16 0.01 2 33 . 4 GLN HG3 H 2.25 0.01 2 34 . 4 GLN HE21 H 6.74 0.01 2 35 . 4 GLN HE22 H 7.54 0.01 2 36 . 4 GLN CA C 55.9 0.3 1 37 . 4 GLN CB C 28.6 0.3 1 38 . 4 GLN CG C 33.9 0.3 1 39 . 4 GLN N N 116.2 0.2 1 40 . 4 GLN NE2 N 109.8 0.2 1 41 . 5 VAL H H 8.09 0.01 1 42 . 5 VAL HA H 4.11 0.01 1 43 . 5 VAL HB H 1.88 0.01 1 44 . 5 VAL HG1 H 0.75 0.01 1 45 . 5 VAL HG2 H 0.70 0.01 1 46 . 5 VAL CA C 61.6 0.3 1 47 . 5 VAL CB C 28.9 0.3 1 48 . 5 VAL CG1 C 21.9 0.3 1 49 . 5 VAL CG2 C 22.6 0.3 1 50 . 5 VAL N N 124.4 0.2 1 51 . 6 LEU H H 9.02 0.01 1 52 . 6 LEU HA H 4.21 0.01 1 53 . 6 LEU HB2 H 1.68 0.01 1 54 . 6 LEU HB3 H 1.11 0.01 1 55 . 6 LEU HG H 1.68 0.01 1 56 . 6 LEU HD1 H 0.71 0.01 1 57 . 6 LEU HD2 H 0.79 0.01 1 58 . 6 LEU CA C 54.5 0.3 1 59 . 6 LEU CB C 42.8 0.3 1 60 . 6 LEU CG C 44.2 0.3 1 61 . 6 LEU CD1 C 22.6 0.3 1 62 . 6 LEU CD2 C 26.5 0.3 1 63 . 6 LEU N N 124.3 0.2 1 64 . 7 HIS H H 8.75 0.01 1 65 . 7 HIS HA H 5.74 0.01 1 66 . 7 HIS HB2 H 3.04 0.01 1 67 . 7 HIS HB3 H 3.27 0.01 1 68 . 7 HIS HD2 H 7.23 0.01 1 69 . 7 HIS HE1 H 8.27 0.01 1 70 . 7 HIS CA C 52.4 0.2 1 71 . 7 HIS CB C 33.2 0.2 1 72 . 7 HIS N N 116.6 0.2 1 73 . 7 HIS ND1 N 197.0 1.0 1 74 . 7 HIS NE2 N 172.0 1.0 1 75 . 8 ILE H H 8.24 0.01 1 76 . 8 ILE HA H 4.26 0.01 1 77 . 8 ILE HB H 1.83 0.01 1 78 . 8 ILE HG12 H 1.34 0.01 2 79 . 8 ILE HG13 H 1.63 0.01 2 80 . 8 ILE HG2 H 1.02 0.01 1 81 . 8 ILE HD1 H 0.88 0.01 1 82 . 8 ILE CA C 60.5 0.3 1 83 . 8 ILE CB C 38.5 0.3 1 84 . 8 ILE CG1 C 25.8 0.3 1 85 . 8 ILE CG2 C 19.7 0.3 1 86 . 8 ILE CD1 C 14.8 0.3 1 87 . 8 ILE N N 114.8 0.3 1 88 . 9 PRO HA H 4.61 0.01 1 89 . 9 PRO HB2 H 2.00 0.01 1 90 . 9 PRO HB3 H 2.44 0.01 1 91 . 9 PRO HG2 H 1.82 0.01 2 92 . 9 PRO HG3 H 1.98 0.01 2 93 . 9 PRO HD2 H 3.57 0.01 2 94 . 9 PRO HD3 H 3.62 0.01 2 95 . 9 PRO CA C 63.0 0.3 1 96 . 9 PRO CB C 32.5 0.3 1 97 . 9 PRO CG C 24.0 0.3 1 98 . 9 PRO CD C 49.5 0.3 1 99 . 10 ASP HA H 4.36 0.01 1 100 . 10 ASP HB2 H 2.59 0.01 2 101 . 10 ASP HB3 H 2.98 0.01 2 102 . 10 ASP CA C 56.3 0.3 1 103 . 10 ASP CB C 43.1 0.3 1 104 . 11 GLU HA H 4.06 0.01 1 105 . 11 GLU HB2 H 2.09 0.01 1 106 . 11 GLU HB3 H 2.09 0.01 1 107 . 11 GLU HG2 H 2.34 0.01 1 108 . 11 GLU HG3 H 2.34 0.01 1 109 . 11 GLU CA C 59.1 0.3 1 110 . 11 GLU CB C 29.3 0.3 1 111 . 11 GLU CG C 36.0 0.3 1 112 . 12 ARG H H 9.51 0.01 1 113 . 12 ARG HA H 3.83 0.01 1 114 . 12 ARG HB2 H 1.82 0.01 1 115 . 12 ARG HB3 H 1.92 0.01 1 116 . 12 ARG HG2 H 1.82 0.01 2 117 . 12 ARG HG3 H 1.75 0.01 2 118 . 12 ARG HD2 H 3.31 0.01 2 119 . 12 ARG HD3 H 3.56 0.01 2 120 . 12 ARG HE H 6.07 0.01 1 121 . 12 ARG HH11 H 8.10 0.01 4 122 . 12 ARG HH12 H 8.10 0.01 4 123 . 12 ARG HH21 H 8.65 0.01 4 124 . 12 ARG HH22 H 8.65 0.01 4 125 . 12 ARG CA C 59.4 0.3 1 126 . 12 ARG CB C 30.4 0.3 1 127 . 12 ARG CG C 27.5 0.3 1 128 . 12 ARG CD C 43.1 0.3 1 129 . 12 ARG N N 120.2 0.2 1 130 . 13 LEU H H 7.36 0.01 1 131 . 13 LEU HA H 4.08 0.01 1 132 . 13 LEU HB2 H 2.01 0.01 1 133 . 13 LEU HB3 H 1.49 0.01 1 134 . 13 LEU HG H 1.54 0.01 1 135 . 13 LEU HD1 H 0.90 0.01 1 136 . 13 LEU HD2 H 0.88 0.01 1 137 . 13 LEU CA C 55.9 0.3 1 138 . 13 LEU CB C 42.8 0.3 1 139 . 13 LEU CG C 27.9 0.3 1 140 . 13 LEU CD1 C 24.7 0.3 1 141 . 13 LEU CD2 C 26.5 0.3 1 142 . 13 LEU N N 110.7 0.2 1 143 . 14 ARG H H 7.46 0.01 1 144 . 14 ARG HA H 4.55 0.01 1 145 . 14 ARG HB2 H 1.94 0.01 1 146 . 14 ARG HB3 H 2.16 0.01 1 147 . 14 ARG HG2 H 1.53 0.01 2 148 . 14 ARG HG3 H 1.79 0.01 2 149 . 14 ARG HD2 H 3.00 0.01 2 150 . 14 ARG HD3 H 3.05 0.01 2 151 . 14 ARG CA C 53.8 0.3 1 152 . 14 ARG CB C 30.4 0.3 1 153 . 14 ARG CG C 26.1 0.3 1 154 . 14 ARG CD C 43.5 0.3 1 155 . 14 ARG N N 112.1 0.2 1 156 . 15 LYS H H 6.81 0.01 1 157 . 15 LYS HA H 3.96 0.01 1 158 . 15 LYS HB2 H 1.32 0.01 1 159 . 15 LYS HB3 H 1.44 0.01 1 160 . 15 LYS HG2 H 1.11 0.01 2 161 . 15 LYS HG3 H 1.32 0.01 2 162 . 15 LYS HD2 H 1.00 0.01 2 163 . 15 LYS HD3 H 1.20 0.01 2 164 . 15 LYS HE2 H 2.57 0.01 1 165 . 15 LYS HE3 H 2.57 0.01 1 166 . 15 LYS CA C 57.0 0.3 1 167 . 15 LYS CB C 32.8 0.3 1 168 . 15 LYS CG C 25.8 0.3 1 169 . 15 LYS CD C 28.6 0.3 1 170 . 15 LYS CE C 41.7 0.3 1 171 . 15 LYS N N 118.4 0.2 1 172 . 16 VAL H H 7.85 0.01 1 173 . 16 VAL HA H 3.93 0.01 1 174 . 16 VAL HB H 1.91 0.01 1 175 . 16 VAL HG1 H 0.88 0.01 1 176 . 16 VAL HG2 H 1.04 0.01 1 177 . 16 VAL CA C 62.3 0.3 1 178 . 16 VAL CB C 32.1 0.3 1 179 . 16 VAL CG1 C 21.5 0.3 1 180 . 16 VAL CG2 C 21.9 0.3 1 181 . 16 VAL N N 118.4 0.2 1 182 . 17 ALA H H 8.37 0.01 1 183 . 17 ALA HA H 4.07 0.01 1 184 . 17 ALA HB H 1.34 0.01 1 185 . 17 ALA CA C 52.4 0.3 1 186 . 17 ALA CB C 20.4 0.3 1 187 . 17 ALA N N 128.5 0.2 1 188 . 18 LYS H H 8.11 0.01 1 189 . 18 LYS HA H 4.82 0.01 1 190 . 18 LYS HB2 H 1.99 0.01 1 191 . 18 LYS HB3 H 1.90 0.01 1 192 . 18 LYS HG2 H 1.72 0.01 4 193 . 18 LYS HG3 H 1.72 0.01 4 194 . 18 LYS HD2 H 1.63 0.01 4 195 . 18 LYS HD3 H 1.63 0.01 4 196 . 18 LYS CA C 54.1 0.3 1 197 . 18 LYS CB C 32.5 0.3 1 198 . 18 LYS CG C 24.3 0.3 4 199 . 18 LYS N N 120.6 0.2 1 200 . 19 PRO HA H 4.32 0.01 1 201 . 19 PRO HB2 H 1.78 0.01 1 202 . 19 PRO HB3 H 2.18 0.01 1 203 . 19 PRO HG2 H 1.90 0.01 2 204 . 19 PRO HG3 H 2.12 0.01 2 205 . 19 PRO HD2 H 3.87 0.01 1 206 . 19 PRO HD3 H 3.66 0.01 1 207 . 19 PRO CA C 63.0 0.3 1 208 . 19 PRO CB C 31.4 0.3 1 209 . 19 PRO CG C 27.9 0.3 1 210 . 19 PRO CD C 50.6 0.3 1 211 . 20 VAL H H 10.12 0.01 1 212 . 20 VAL HA H 3.98 0.01 1 213 . 20 VAL HB H 1.78 0.01 1 214 . 20 VAL HG1 H 1.00 0.01 1 215 . 20 VAL HG2 H 0.74 0.01 1 216 . 20 VAL CA C 62.6 0.3 1 217 . 20 VAL CB C 31.8 0.3 1 218 . 20 VAL CG1 C 23.3 0.3 1 219 . 20 VAL CG2 C 22.6 0.3 1 220 . 20 VAL N N 123.5 0.2 1 221 . 21 GLU H H 8.84 0.01 1 222 . 21 GLU HA H 4.12 0.01 1 223 . 21 GLU HB2 H 2.11 0.01 1 224 . 21 GLU HB3 H 2.11 0.01 1 225 . 21 GLU HG2 H 1.87 0.01 1 226 . 21 GLU HG3 H 1.87 0.01 1 227 . 21 GLU CA C 55.5 0.3 1 228 . 21 GLU CB C 29.3 0.3 1 229 . 21 GLU N N 127.0 0.2 1 230 . 22 GLU H H 7.18 0.01 1 231 . 22 GLU HA H 4.39 0.01 1 232 . 22 GLU HB2 H 1.92 0.01 1 233 . 22 GLU HB3 H 1.92 0.01 1 234 . 22 GLU HG2 H 2.15 0.01 2 235 . 22 GLU HG3 H 1.99 0.01 2 236 . 22 GLU CA C 54.8 0.3 1 237 . 22 GLU CB C 32.8 0.3 1 238 . 22 GLU CG C 36.0 0.3 1 239 . 22 GLU N N 113.3 0.2 1 240 . 23 VAL H H 8.73 0.01 1 241 . 23 VAL HA H 3.61 0.01 1 242 . 23 VAL HB H 1.97 0.01 1 243 . 23 VAL HG1 H 0.82 0.01 1 244 . 23 VAL HG2 H 0.91 0.01 1 245 . 23 VAL CA C 64.1 0.3 1 246 . 23 VAL CB C 29.7 0.3 1 247 . 23 VAL CG1 C 21.9 0.3 1 248 . 23 VAL CG2 C 22.6 0.3 1 249 . 23 VAL N N 124.2 0.2 1 250 . 24 ASN H H 6.83 0.01 1 251 . 24 ASN HA H 4.88 0.01 1 252 . 24 ASN HB2 H 3.39 0.01 1 253 . 24 ASN HB3 H 2.81 0.01 1 254 . 24 ASN HD21 H 6.83 0.01 2 255 . 24 ASN HD22 H 7.71 0.01 2 256 . 24 ASN CA C 50.6 0.3 1 257 . 24 ASN CB C 39.9 0.3 1 258 . 24 ASN N N 123.0 0.2 1 259 . 24 ASN ND2 N 108.5 0.2 1 260 . 25 ALA H H 7.72 0.01 1 261 . 25 ALA HA H 4.22 0.01 1 262 . 25 ALA HB H 1.53 0.01 1 263 . 25 ALA CA C 55.5 0.3 1 264 . 25 ALA CB C 18.3 0.3 1 265 . 25 ALA N N 116.3 0.2 1 266 . 26 GLU H H 7.86 0.01 1 267 . 26 GLU HA H 4.15 0.01 1 268 . 26 GLU HB2 H 2.11 0.01 1 269 . 26 GLU HB3 H 2.11 0.01 1 270 . 26 GLU HG2 H 2.27 0.01 1 271 . 26 GLU HG3 H 2.27 0.01 1 272 . 26 GLU CA C 58.7 0.3 1 273 . 26 GLU CB C 29.7 0.3 1 274 . 26 GLU CG C 36.0 0.3 1 275 . 26 GLU N N 116.7 0.2 1 276 . 27 ILE H H 7.71 0.01 1 277 . 27 ILE HA H 3.88 0.01 1 278 . 27 ILE HB H 2.37 0.01 1 279 . 27 ILE HG12 H 2.03 0.01 2 280 . 27 ILE HG13 H 1.73 0.01 2 281 . 27 ILE HG2 H 0.90 0.01 1 282 . 27 ILE HD1 H 0.80 0.01 1 283 . 27 ILE CA C 61.2 0.3 1 284 . 27 ILE CB C 35.3 0.3 1 285 . 27 ILE CG1 C 32.1 0.3 1 286 . 27 ILE CG2 C 18.3 0.3 1 287 . 27 ILE CD1 C 8.7 0.3 1 288 . 27 ILE N N 116.5 0.2 1 289 . 28 GLN H H 8.19 0.01 1 290 . 28 GLN HA H 3.72 0.01 1 291 . 28 GLN HB2 H 1.91 0.01 1 292 . 28 GLN HB3 H 2.22 0.01 1 293 . 28 GLN HG2 H 2.56 0.01 2 294 . 28 GLN HG3 H 2.41 0.01 2 295 . 28 GLN HE21 H 6.76 0.01 2 296 . 28 GLN HE22 H 7.68 0.01 2 297 . 28 GLN CA C 60.2 0.3 1 298 . 28 GLN CB C 26.8 0.3 1 299 . 28 GLN CG C 33.9 0.3 1 300 . 28 GLN N N 115.6 0.2 1 301 . 28 GLN NE2 N 108.9 0.2 1 302 . 29 ARG H H 7.76 0.01 1 303 . 29 ARG HA H 4.15 0.01 1 304 . 29 ARG HB2 H 2.07 0.01 1 305 . 29 ARG HB3 H 1.96 0.01 1 306 . 29 ARG HG2 H 1.78 0.01 1 307 . 29 ARG HG3 H 1.78 0.01 1 308 . 29 ARG HD2 H 3.24 0.01 1 309 . 29 ARG HD3 H 3.24 0.01 1 310 . 29 ARG CA C 59.4 0.3 1 311 . 29 ARG CB C 29.7 0.3 1 312 . 29 ARG CG C 26.8 0.3 1 313 . 29 ARG CD C 43.5 0.3 1 314 . 29 ARG N N 116.7 0.2 1 315 . 30 ILE H H 7.71 0.01 1 316 . 30 ILE HA H 3.62 0.01 1 317 . 30 ILE HB H 2.02 0.01 1 318 . 30 ILE HG12 H 1.88 0.01 2 319 . 30 ILE HG13 H 0.97 0.01 2 320 . 30 ILE HG2 H 0.77 0.01 1 321 . 30 ILE HD1 H 0.81 0.01 1 322 . 30 ILE CA C 65.8 0.3 1 323 . 30 ILE CB C 38.2 0.3 1 324 . 30 ILE CG1 C 29.3 0.3 1 325 . 30 ILE CG2 C 18.0 0.3 1 326 . 30 ILE CD1 C 13.7 0.3 1 327 . 30 ILE N N 118.1 0.2 1 328 . 31 VAL H H 8.25 0.01 1 329 . 31 VAL HA H 3.33 0.01 1 330 . 31 VAL HB H 2.41 0.01 1 331 . 31 VAL HG1 H 1.08 0.01 1 332 . 31 VAL HG2 H 0.96 0.01 1 333 . 31 VAL CA C 66.9 0.3 1 334 . 31 VAL CB C 31.4 0.3 1 335 . 31 VAL CG1 C 22.9 0.3 1 336 . 31 VAL CG2 C 24.0 0.3 1 337 . 31 VAL N N 117.2 0.2 1 338 . 32 ASP H H 8.12 0.01 1 339 . 32 ASP HA H 4.66 0.01 1 340 . 32 ASP HB2 H 2.83 0.01 1 341 . 32 ASP HB3 H 2.95 0.01 1 342 . 32 ASP CA C 58.4 0.3 1 343 . 32 ASP CB C 39.6 0.3 1 344 . 32 ASP N N 118.1 0.2 1 345 . 33 ASP H H 8.85 0.01 1 346 . 33 ASP HA H 4.68 0.01 1 347 . 33 ASP HB2 H 2.67 0.01 1 348 . 33 ASP HB3 H 2.84 0.01 1 349 . 33 ASP CA C 57.3 0.3 1 350 . 33 ASP CB C 40.3 0.3 1 351 . 33 ASP N N 121.5 0.2 1 352 . 34 MET H H 9.33 0.01 1 353 . 34 MET HA H 3.53 0.01 1 354 . 34 MET HB2 H 2.18 0.01 1 355 . 34 MET HB3 H 1.85 0.01 1 356 . 34 MET HG2 H 1.92 0.01 1 357 . 34 MET HG3 H 2.70 0.01 1 358 . 34 MET HE H 1.68 0.01 1 359 . 34 MET CA C 60.9 0.3 1 360 . 34 MET CB C 32.8 0.3 1 361 . 34 MET CG C 32.8 0.3 1 362 . 34 MET CE C 16.5 0.3 1 363 . 34 MET N N 122.9 0.2 1 364 . 35 PHE H H 8.61 0.01 1 365 . 35 PHE HA H 3.90 0.01 1 366 . 35 PHE HB2 H 3.15 0.01 1 367 . 35 PHE HB3 H 3.15 0.01 1 368 . 35 PHE HD1 H 7.17 0.01 1 369 . 35 PHE HD2 H 7.17 0.01 1 370 . 35 PHE HE1 H 7.13 0.01 1 371 . 35 PHE HE2 H 7.13 0.01 1 372 . 35 PHE HZ H 7.09 0.01 1 373 . 35 PHE CA C 64.1 0.3 1 374 . 35 PHE CB C 38.9 0.3 1 375 . 35 PHE N N 116.2 0.2 1 376 . 36 GLU H H 8.15 0.01 1 377 . 36 GLU HA H 4.05 0.01 1 378 . 36 GLU HB2 H 2.21 0.01 1 379 . 36 GLU HB3 H 2.15 0.01 1 380 . 36 GLU HG2 H 2.52 0.01 1 381 . 36 GLU HG3 H 2.52 0.01 1 382 . 36 GLU CA C 60.5 0.3 1 383 . 36 GLU CB C 29.3 0.3 1 384 . 36 GLU CG C 36.7 0.3 1 385 . 36 GLU N N 115.5 0.2 1 386 . 37 THR H H 8.30 0.01 1 387 . 37 THR HA H 3.85 0.01 1 388 . 37 THR HB H 4.18 0.01 1 389 . 37 THR HG1 H 5.57 0.01 1 390 . 37 THR HG2 H 1.08 0.01 1 391 . 37 THR CA C 67.6 0.3 1 392 . 37 THR CB C 69.0 0.3 1 393 . 37 THR CG2 C 21.1 0.3 1 394 . 37 THR N N 113.7 0.2 1 395 . 38 MET H H 8.50 0.01 1 396 . 38 MET HA H 3.41 0.01 1 397 . 38 MET HB2 H 1.67 0.01 1 398 . 38 MET HB3 H 1.88 0.01 1 399 . 38 MET HG2 H 1.85 0.01 1 400 . 38 MET HG3 H 1.68 0.01 1 401 . 38 MET HE H 1.49 0.01 1 402 . 38 MET CA C 60.2 0.3 1 403 . 38 MET CB C 33.6 0.3 1 404 . 38 MET CG C 30.4 0.3 1 405 . 38 MET CE C 17.6 0.3 1 406 . 38 MET N N 119.3 0.2 1 407 . 39 TYR H H 8.81 0.01 1 408 . 39 TYR HA H 4.61 0.01 1 409 . 39 TYR HB2 H 2.93 0.01 1 410 . 39 TYR HB3 H 3.19 0.01 1 411 . 39 TYR HD1 H 7.19 0.01 1 412 . 39 TYR HD2 H 7.19 0.01 1 413 . 39 TYR HE1 H 6.59 0.01 1 414 . 39 TYR HE2 H 6.59 0.01 1 415 . 39 TYR CA C 60.2 0.3 1 416 . 39 TYR CB C 37.5 0.3 1 417 . 39 TYR N N 113.4 0.2 1 418 . 40 ALA H H 8.20 0.01 1 419 . 40 ALA HA H 4.24 0.01 1 420 . 40 ALA HB H 1.68 0.01 1 421 . 40 ALA CA C 55.5 0.3 1 422 . 40 ALA CB C 18.3 0.3 1 423 . 40 ALA N N 121.1 0.2 1 424 . 41 GLU H H 7.60 0.01 1 425 . 41 GLU HA H 4.50 0.01 1 426 . 41 GLU HB2 H 1.69 0.01 1 427 . 41 GLU HB3 H 2.57 0.01 1 428 . 41 GLU HG2 H 2.36 0.01 2 429 . 41 GLU HG3 H 2.29 0.01 2 430 . 41 GLU CA C 55.5 0.3 1 431 . 41 GLU CB C 30.7 0.3 1 432 . 41 GLU CG C 35.7 0.3 1 433 . 41 GLU N N 111.9 0.2 1 434 . 42 GLU H H 7.85 0.01 1 435 . 42 GLU HA H 4.01 0.01 1 436 . 42 GLU HB2 H 2.19 0.01 2 437 . 42 GLU HB3 H 2.25 0.01 2 438 . 42 GLU HG2 H 2.24 0.01 1 439 . 42 GLU HG3 H 2.24 0.01 1 440 . 42 GLU CA C 58.4 0.3 1 441 . 42 GLU CB C 28.6 0.3 1 442 . 42 GLU CG C 36.7 0.3 1 443 . 42 GLU N N 111.3 0.2 1 444 . 43 GLY H H 8.54 0.01 1 445 . 43 GLY HA2 H 4.59 0.01 2 446 . 43 GLY HA3 H 3.41 0.01 2 447 . 43 GLY CA C 44.2 0.3 1 448 . 43 GLY N N 102.6 0.2 1 449 . 44 ILE H H 8.06 0.01 1 450 . 44 ILE HA H 4.72 0.01 1 451 . 44 ILE HB H 2.15 0.01 1 452 . 44 ILE HG12 H 1.34 0.01 2 453 . 44 ILE HG13 H 1.36 0.01 2 454 . 44 ILE HG2 H 0.98 0.01 1 455 . 44 ILE HD1 H 0.83 0.01 1 456 . 44 ILE CA C 61.6 0.3 1 457 . 44 ILE CB C 39.6 0.3 1 458 . 44 ILE CG1 C 25.4 0.3 1 459 . 44 ILE CG2 C 17.6 0.3 1 460 . 44 ILE CD1 C 14.4 0.3 1 461 . 44 ILE N N 107.1 0.2 1 462 . 45 GLY H H 7.11 0.01 1 463 . 45 GLY HA2 H 3.37 0.01 2 464 . 45 GLY HA3 H 4.74 0.01 2 465 . 45 GLY CA C 45.3 0.3 1 466 . 45 GLY N N 104.7 0.2 1 467 . 46 LEU H H 8.58 0.01 1 468 . 46 LEU HA H 4.34 0.01 1 469 . 46 LEU HB2 H 1.00 0.01 1 470 . 46 LEU HB3 H 1.00 0.01 1 471 . 46 LEU HG H 1.35 0.01 1 472 . 46 LEU HD1 H 0.60 0.01 1 473 . 46 LEU HD2 H 0.78 0.01 1 474 . 46 LEU CA C 55.5 0.3 1 475 . 46 LEU CB C 46.0 0.3 1 476 . 46 LEU CG C 26.5 0.3 1 477 . 46 LEU CD1 C 27.2 0.3 1 478 . 46 LEU CD2 C 24.7 0.3 1 479 . 46 LEU N N 117.1 0.2 1 480 . 47 ALA H H 8.35 0.01 1 481 . 47 ALA HA H 5.12 0.01 1 482 . 47 ALA HB H 1.73 0.01 1 483 . 47 ALA CA C 49.9 0.3 1 484 . 47 ALA CB C 21.5 0.3 1 485 . 47 ALA N N 126.2 0.2 1 486 . 48 ALA H H 8.81 0.01 1 487 . 48 ALA HA H 3.92 0.01 1 488 . 48 ALA HB H 1.70 0.01 1 489 . 48 ALA CA C 55.9 0.3 1 490 . 48 ALA CB C 18.3 0.3 1 491 . 48 ALA N N 124.6 0.2 1 492 . 49 THR H H 7.12 0.01 1 493 . 49 THR HA H 3.32 0.01 1 494 . 49 THR HB H 3.26 0.01 1 495 . 49 THR HG1 H 6.53 0.01 1 496 . 49 THR HG2 H 1.63 0.01 1 497 . 49 THR CA C 66.9 0.3 1 498 . 49 THR CB C 72.2 0.3 1 499 . 49 THR CG2 C 21.5 0.3 1 500 . 49 THR N N 110.5 0.2 1 501 . 50 GLN H H 7.61 0.01 1 502 . 50 GLN HA H 3.77 0.01 1 503 . 50 GLN HB2 H 2.39 0.01 1 504 . 50 GLN HB3 H 2.03 0.01 1 505 . 50 GLN HG2 H 1.86 0.01 1 506 . 50 GLN HG3 H 1.33 0.01 1 507 . 50 GLN HE21 H 6.08 0.01 1 508 . 50 GLN HE22 H 8.12 0.01 1 509 . 50 GLN CA C 58.4 0.3 1 510 . 50 GLN CB C 32.1 0.3 1 511 . 50 GLN CG C 36.0 0.3 1 512 . 50 GLN N N 108.5 0.2 1 513 . 50 GLN NE2 N 104.6 0.2 1 514 . 51 VAL H H 7.86 0.01 1 515 . 51 VAL HA H 4.92 0.01 1 516 . 51 VAL HB H 2.47 0.01 1 517 . 51 VAL HG1 H 0.77 0.01 1 518 . 51 VAL HG2 H 0.67 0.01 1 519 . 51 VAL CA C 59.1 0.3 1 520 . 51 VAL CB C 30.0 0.3 1 521 . 51 VAL CG1 C 20.1 0.3 1 522 . 51 VAL CG2 C 23.3 0.3 1 523 . 51 VAL N N 106.3 0.2 1 524 . 52 ASP H H 7.79 0.01 1 525 . 52 ASP HA H 4.05 0.01 1 526 . 52 ASP HB2 H 2.04 0.01 1 527 . 52 ASP HB3 H 3.33 0.01 1 528 . 52 ASP CA C 54.5 0.3 1 529 . 52 ASP CB C 41.4 0.3 1 530 . 52 ASP N N 115.9 0.2 1 531 . 53 ILE H H 7.22 0.01 1 532 . 53 ILE HA H 3.91 0.01 1 533 . 53 ILE HB H 1.53 0.01 1 534 . 53 ILE HG12 H 0.84 0.01 2 535 . 53 ILE HG13 H 1.43 0.01 2 536 . 53 ILE HG2 H 0.75 0.01 1 537 . 53 ILE HD1 H 0.74 0.01 1 538 . 53 ILE CA C 60.5 0.3 1 539 . 53 ILE CB C 38.9 0.3 1 540 . 53 ILE CG1 C 26.5 0.3 1 541 . 53 ILE CG2 C 16.2 0.3 1 542 . 53 ILE CD1 C 13.7 0.3 1 543 . 53 ILE N N 116.8 0.2 1 544 . 54 HIS H H 8.11 0.01 1 545 . 54 HIS HA H 4.59 0.01 1 546 . 54 HIS HB2 H 2.84 0.01 1 547 . 54 HIS HB3 H 2.94 0.01 1 548 . 54 HIS HD2 H 6.86 0.01 1 549 . 54 HIS HE1 H 7.98 0.01 1 550 . 54 HIS CA C 55.9 0.3 1 551 . 54 HIS CB C 28.9 0.3 1 552 . 54 HIS N N 125.2 0.2 1 553 . 54 HIS ND1 N 247.5 0.2 1 554 . 54 HIS NE2 N 161.5 0.2 1 555 . 55 GLN H H 8.09 0.01 1 556 . 55 GLN HA H 5.77 0.01 1 557 . 55 GLN HB2 H 2.10 0.01 1 558 . 55 GLN HB3 H 1.34 0.01 1 559 . 55 GLN HG2 H 2.09 0.01 1 560 . 55 GLN HG3 H 2.09 0.01 1 561 . 55 GLN HE21 H 6.44 0.01 2 562 . 55 GLN HE22 H 6.81 0.01 2 563 . 55 GLN CA C 53.8 0.3 1 564 . 55 GLN CB C 34.6 0.3 1 565 . 55 GLN CG C 35.0 0.3 1 566 . 55 GLN N N 116.3 0.2 1 567 . 55 GLN NE2 N 105.8 0.2 1 568 . 56 ARG H H 7.74 0.01 1 569 . 56 ARG HA H 4.33 0.01 1 570 . 56 ARG HB2 H 2.47 0.01 1 571 . 56 ARG HB3 H 1.85 0.01 1 572 . 56 ARG HG2 H 1.53 0.01 2 573 . 56 ARG HG3 H 1.40 0.01 2 574 . 56 ARG HD2 H 3.34 0.01 2 575 . 56 ARG HD3 H 2.85 0.01 2 576 . 56 ARG CA C 57.7 0.3 1 577 . 56 ARG CB C 28.6 0.3 1 578 . 56 ARG CG C 27.9 0.3 1 579 . 56 ARG CD C 42.8 0.3 1 580 . 56 ARG N N 116.1 0.2 1 581 . 57 ILE H H 8.07 0.01 1 582 . 57 ILE HA H 4.59 0.01 1 583 . 57 ILE HB H 1.47 0.01 1 584 . 57 ILE HG12 H 1.24 0.01 1 585 . 57 ILE HG13 H 1.24 0.01 1 586 . 57 ILE HG2 H 0.70 0.01 1 587 . 57 ILE HD1 H 0.72 0.01 1 588 . 57 ILE CA C 61.2 0.3 1 589 . 57 ILE CB C 42.8 0.3 1 590 . 57 ILE CG1 C 27.5 0.3 1 591 . 57 ILE CG2 C 18.0 0.3 1 592 . 57 ILE CD1 C 14.4 0.3 1 593 . 57 ILE N N 123.8 0.2 1 594 . 58 ILE H H 8.72 0.01 1 595 . 58 ILE HA H 4.79 0.01 1 596 . 58 ILE HB H 1.73 0.01 1 597 . 58 ILE HG12 H 1.80 0.01 2 598 . 58 ILE HG13 H 1.13 0.01 2 599 . 58 ILE HG2 H 0.70 0.01 1 600 . 58 ILE HD1 H 0.85 0.01 1 601 . 58 ILE CA C 59.8 0.3 1 602 . 58 ILE CB C 44.6 0.3 1 603 . 58 ILE CG1 C 27.9 0.3 1 604 . 58 ILE CG2 C 18.0 0.3 1 605 . 58 ILE CD1 C 16.2 0.3 1 606 . 58 ILE N N 125.9 0.2 1 607 . 59 VAL H H 8.56 0.01 1 608 . 59 VAL HA H 5.04 0.01 1 609 . 59 VAL HB H 0.89 0.01 1 610 . 59 VAL HG1 H 0.32 0.01 1 611 . 59 VAL HG2 H 0.35 0.01 1 612 . 59 VAL CA C 58.7 0.3 1 613 . 59 VAL CB C 33.2 0.3 1 614 . 59 VAL CG1 C 19.4 0.3 1 615 . 59 VAL CG2 C 22.6 0.3 1 616 . 59 VAL N N 116.2 0.2 1 617 . 60 ILE H H 8.71 0.01 1 618 . 60 ILE HA H 4.66 0.01 1 619 . 60 ILE HB H 1.50 0.01 1 620 . 60 ILE HG12 H 1.15 0.01 2 621 . 60 ILE HG13 H 1.61 0.01 2 622 . 60 ILE HG2 H 1.09 0.01 1 623 . 60 ILE HD1 H 0.66 0.01 1 624 . 60 ILE CA C 60.5 0.3 1 625 . 60 ILE CG1 C 28.9 0.3 1 626 . 60 ILE CG2 C 18.3 0.3 1 627 . 60 ILE CD1 C 15.8 0.3 1 628 . 60 ILE N N 119.6 0.2 1 629 . 61 ASP H H 8.33 0.01 1 630 . 61 ASP HA H 4.92 0.01 1 631 . 61 ASP HB2 H 2.98 0.01 1 632 . 61 ASP HB3 H 2.85 0.01 1 633 . 61 ASP CA C 55.5 0.3 1 634 . 61 ASP CB C 42.4 0.3 1 635 . 61 ASP N N 119.0 0.2 1 636 . 62 VAL H H 9.04 0.01 1 637 . 62 VAL HA H 4.61 0.01 1 638 . 62 VAL HB H 2.62 0.01 1 639 . 62 VAL HG1 H 0.89 0.01 1 640 . 62 VAL HG2 H 1.00 0.01 1 641 . 62 VAL CA C 60.5 0.3 1 642 . 62 VAL CB C 31.4 0.3 1 643 . 62 VAL CG1 C 19.0 0.3 1 644 . 62 VAL CG2 C 23.3 0.3 1 645 . 62 VAL N N 115.4 0.2 1 646 . 63 SER H H 9.30 0.01 1 647 . 63 SER HA H 4.42 0.01 1 648 . 63 SER HB2 H 4.30 0.01 1 649 . 63 SER HB3 H 4.14 0.01 1 650 . 63 SER CA C 59.1 0.3 1 651 . 63 SER CB C 65.1 0.3 1 652 . 63 SER N N 120.2 0.2 1 653 . 64 GLU H H 8.85 0.01 1 654 . 64 GLU HA H 4.15 0.01 1 655 . 64 GLU HB2 H 2.00 0.01 1 656 . 64 GLU HB3 H 2.00 0.01 1 657 . 64 GLU HG2 H 2.29 0.01 1 658 . 64 GLU HG3 H 2.29 0.01 1 659 . 64 GLU CA C 58.4 0.3 1 660 . 64 GLU CB C 30.0 0.3 1 661 . 64 GLU CG C 35.7 0.3 1 662 . 64 GLU N N 120.0 0.2 1 663 . 65 ASN H H 8.45 0.01 1 664 . 65 ASN HA H 4.72 0.01 1 665 . 65 ASN HB2 H 2.79 0.01 1 666 . 65 ASN HB3 H 2.68 0.01 1 667 . 65 ASN HD21 H 6.80 0.01 2 668 . 65 ASN HD22 H 7.64 0.01 2 669 . 65 ASN CA C 52.7 0.3 1 670 . 65 ASN CB C 38.2 0.3 1 671 . 65 ASN N N 111.6 0.2 1 672 . 65 ASN ND2 N 110.4 0.2 1 673 . 66 ARG H H 7.86 0.01 1 674 . 66 ARG HA H 4.17 0.01 1 675 . 66 ARG HB2 H 1.87 0.01 1 676 . 66 ARG HB3 H 1.59 0.01 1 677 . 66 ARG HG2 H 1.48 0.01 1 678 . 66 ARG HG3 H 1.48 0.01 1 679 . 66 ARG HD2 H 2.99 0.01 2 680 . 66 ARG HD3 H 3.03 0.01 2 681 . 66 ARG CA C 55.9 0.3 1 682 . 66 ARG CB C 25.4 0.3 1 683 . 66 ARG CG C 26.5 0.3 1 684 . 66 ARG CD C 43.1 0.3 1 685 . 66 ARG N N 114.1 0.2 1 686 . 67 ASP H H 8.12 0.01 1 687 . 67 ASP HA H 4.63 0.01 1 688 . 67 ASP HB2 H 2.71 0.01 1 689 . 67 ASP HB3 H 2.26 0.01 1 690 . 67 ASP CA C 52.7 0.3 1 691 . 67 ASP CB C 41.4 0.3 1 692 . 67 ASP N N 114.2 0.2 1 693 . 68 GLU H H 8.18 0.01 1 694 . 68 GLU HA H 4.56 0.01 1 695 . 68 GLU HB2 H 1.83 0.01 1 696 . 68 GLU HB3 H 2.10 0.01 1 697 . 68 GLU HG2 H 2.28 0.01 1 698 . 68 GLU HG3 H 2.28 0.01 1 699 . 68 GLU CA C 54.8 0.3 1 700 . 68 GLU CB C 30.7 0.3 1 701 . 68 GLU CG C 36.4 0.3 1 702 . 68 GLU N N 122.0 0.2 1 703 . 69 ARG H H 7.67 0.01 1 704 . 69 ARG HA H 4.29 0.01 1 705 . 69 ARG HB2 H 1.56 0.01 1 706 . 69 ARG HB3 H 1.37 0.01 1 707 . 69 ARG HG2 H 1.19 0.01 2 708 . 69 ARG HG3 H 1.27 0.01 2 709 . 69 ARG HD2 H 2.34 0.01 2 710 . 69 ARG HD3 H 2.04 0.01 2 711 . 69 ARG HE H 7.77 0.01 1 712 . 69 ARG CA C 57.0 0.3 1 713 . 69 ARG CB C 31.1 0.3 1 714 . 69 ARG CG C 27.2 0.3 1 715 . 69 ARG CD C 39.6 0.3 1 716 . 69 ARG N N 118.1 0.2 1 717 . 69 ARG NE N 81.0 0.5 1 718 . 70 LEU H H 9.35 0.01 1 719 . 70 LEU HA H 4.68 0.01 1 720 . 70 LEU HB2 H 1.73 0.01 1 721 . 70 LEU HB3 H 1.53 0.01 1 722 . 70 LEU HG H 1.46 0.01 1 723 . 70 LEU HD1 H 0.96 0.01 1 724 . 70 LEU HD2 H 0.87 0.01 1 725 . 70 LEU CA C 54.8 0.3 1 726 . 70 LEU CB C 44.9 0.3 1 727 . 70 LEU CG C 26.8 0.3 1 728 . 70 LEU CD1 C 24.3 0.3 1 729 . 70 LEU CD2 C 25.8 0.3 1 730 . 70 LEU N N 124.6 0.2 1 731 . 71 VAL H H 8.08 0.01 1 732 . 71 VAL HA H 4.66 0.01 1 733 . 71 VAL HB H 2.11 0.01 1 734 . 71 VAL HG1 H 0.94 0.01 1 735 . 71 VAL HG2 H 1.27 0.01 1 736 . 71 VAL CA C 60.9 0.3 1 737 . 71 VAL CB C 34.3 0.3 1 738 . 71 VAL CG1 C 21.5 0.3 1 739 . 71 VAL CG2 C 24.0 0.3 1 740 . 71 VAL N N 121.6 0.2 1 741 . 72 LEU H H 8.94 0.01 1 742 . 72 LEU HA H 4.84 0.01 1 743 . 72 LEU HB2 H 1.00 0.01 1 744 . 72 LEU HB3 H 1.92 0.01 1 745 . 72 LEU HG H 1.73 0.01 1 746 . 72 LEU HD1 H 0.83 0.01 1 747 . 72 LEU HD2 H 0.83 0.01 1 748 . 72 LEU CA C 53.4 0.3 1 749 . 72 LEU CB C 44.2 0.3 1 750 . 72 LEU CG C 21.1 0.3 1 751 . 72 LEU CD1 C 26.1 0.3 1 752 . 72 LEU CD2 C 26.1 0.3 1 753 . 72 LEU N N 121.4 0.2 1 754 . 73 ILE H H 9.04 0.01 1 755 . 73 ILE HA H 4.83 0.01 1 756 . 73 ILE HB H 1.79 0.01 1 757 . 73 ILE HG12 H 0.83 0.01 2 758 . 73 ILE HG13 H 1.54 0.01 2 759 . 73 ILE HG2 H 0.73 0.01 1 760 . 73 ILE HD1 H 0.68 0.01 1 761 . 73 ILE CA C 60.2 0.3 1 762 . 73 ILE CB C 38.2 0.3 1 763 . 73 ILE CG1 C 29.7 0.3 1 764 . 73 ILE CG2 C 17.2 0.3 1 765 . 73 ILE CD1 C 13.7 0.3 1 766 . 73 ILE N N 122.2 0.2 1 767 . 74 ASN H H 9.30 0.01 1 768 . 74 ASN HA H 4.32 0.01 1 769 . 74 ASN HB2 H 3.05 0.01 1 770 . 74 ASN HB3 H 3.10 0.01 1 771 . 74 ASN HD21 H 7.05 0.01 2 772 . 74 ASN HD22 H 7.77 0.01 2 773 . 74 ASN CA C 54.1 0.3 1 774 . 74 ASN CB C 36.7 0.3 1 775 . 74 ASN N N 119.3 0.2 1 776 . 74 ASN ND2 N 106.1 0.2 1 777 . 75 PRO HA H 5.12 0.01 1 778 . 75 PRO HB2 H 1.79 0.01 1 779 . 75 PRO HB3 H 2.00 0.01 1 780 . 75 PRO HG2 H 1.75 0.01 1 781 . 75 PRO HG3 H 1.75 0.01 1 782 . 75 PRO HD2 H 3.40 0.01 1 783 . 75 PRO HD3 H 3.27 0.01 1 784 . 75 PRO CA C 62.6 0.3 1 785 . 75 PRO CB C 32.1 0.3 1 786 . 75 PRO CG C 27.9 0.3 1 787 . 75 PRO CD C 50.2 0.3 1 788 . 76 GLU H H 9.35 0.01 1 789 . 76 GLU HA H 4.54 0.01 1 790 . 76 GLU HB2 H 1.90 0.01 1 791 . 76 GLU HB3 H 1.80 0.01 1 792 . 76 GLU HG2 H 2.17 0.01 2 793 . 76 GLU HG3 H 2.06 0.01 2 794 . 76 GLU CA C 54.8 0.3 1 795 . 76 GLU CB C 33.6 0.3 1 796 . 76 GLU CG C 36.4 0.3 1 797 . 76 GLU N N 118.5 0.01 1 798 . 77 LEU H H 8.82 0.01 1 799 . 77 LEU HA H 4.45 0.01 1 800 . 77 LEU HB2 H 1.27 0.01 1 801 . 77 LEU HB3 H 1.86 0.01 1 802 . 77 LEU HG H 1.40 0.01 1 803 . 77 LEU HD1 H 0.89 0.01 1 804 . 77 LEU HD2 H 0.83 0.01 1 805 . 77 LEU CA C 55.2 0.3 1 806 . 77 LEU CB C 42.8 0.3 1 807 . 77 LEU CG C 27.5 0.3 1 808 . 77 LEU CD1 C 24.7 0.3 1 809 . 77 LEU CD2 C 25.4 0.3 1 810 . 77 LEU N N 123.4 0.2 1 811 . 78 LEU H H 9.14 0.01 1 812 . 78 LEU HA H 4.45 0.01 1 813 . 78 LEU HB2 H 1.46 0.01 2 814 . 78 LEU HB3 H 1.59 0.01 2 815 . 78 LEU HG H 1.42 0.01 1 816 . 78 LEU HD1 H 0.73 0.01 1 817 . 78 LEU HD2 H 0.73 0.01 1 818 . 78 LEU CA C 55.9 0.3 1 819 . 78 LEU CB C 42.8 0.3 1 820 . 78 LEU CG C 28.9 0.3 1 821 . 78 LEU CD1 C 25.4 0.3 2 822 . 78 LEU CD2 C 21.9 0.3 2 823 . 78 LEU N N 125.4 0.2 1 824 . 79 GLU H H 7.66 0.01 1 825 . 79 GLU HA H 4.60 0.01 1 826 . 79 GLU HB2 H 2.02 0.01 1 827 . 79 GLU HB3 H 1.87 0.01 1 828 . 79 GLU HG2 H 2.15 0.01 1 829 . 79 GLU HG3 H 2.15 0.01 1 830 . 79 GLU CA C 55.5 0.3 1 831 . 79 GLU CB C 34.3 0.3 1 832 . 79 GLU CG C 39.6 0.3 1 833 . 79 GLU N N 112.9 0.2 1 834 . 80 LYS H H 8.37 0.01 1 835 . 80 LYS HA H 5.33 0.01 1 836 . 80 LYS HB2 H 1.74 0.01 1 837 . 80 LYS HB3 H 1.80 0.01 1 838 . 80 LYS HG2 H 1.22 0.01 1 839 . 80 LYS HG3 H 1.22 0.01 1 840 . 80 LYS HD2 H 1.34 0.01 2 841 . 80 LYS HD3 H 1.38 0.01 2 842 . 80 LYS HE2 H 2.94 0.01 1 843 . 80 LYS HE3 H 2.94 0.01 1 844 . 80 LYS CA C 55.2 0.3 1 845 . 80 LYS CB C 36.0 0.3 1 846 . 80 LYS CG C 18.7 0.3 1 847 . 80 LYS CD C 23.3 0.3 1 848 . 80 LYS CE C 42.1 0.3 1 849 . 80 LYS N N 116.2 0.2 1 850 . 81 SER H H 8.78 0.01 1 851 . 81 SER HA H 4.78 0.01 1 852 . 81 SER HB2 H 3.84 0.01 1 853 . 81 SER HB3 H 3.79 0.01 1 854 . 81 SER CA C 58.0 0.3 1 855 . 81 SER CB C 65.8 0.3 1 856 . 81 SER N N 111.2 0.2 1 857 . 82 GLY H H 8.52 0.01 1 858 . 82 GLY HA2 H 4.32 0.01 2 859 . 82 GLY HA3 H 3.97 0.01 2 860 . 82 GLY CA C 44.9 0.3 1 861 . 82 GLY N N 106.3 0.2 1 862 . 83 GLU H H 8.48 0.01 1 863 . 83 GLU HA H 5.09 0.01 1 864 . 83 GLU HB2 H 1.89 0.01 1 865 . 83 GLU HB3 H 1.93 0.01 1 866 . 83 GLU HG2 H 2.11 0.01 1 867 . 83 GLU HG3 H 2.11 0.01 1 868 . 83 GLU CA C 55.9 0.3 1 869 . 83 GLU CB C 33.2 0.3 1 870 . 83 GLU CG C 36.7 0.3 1 871 . 83 GLU N N 115.9 0.2 1 872 . 84 THR H H 8.86 0.01 1 873 . 84 THR HA H 4.62 0.01 1 874 . 84 THR HB H 4.01 0.01 1 875 . 84 THR HG2 H 0.86 0.01 1 876 . 84 THR CA C 59.4 0.3 1 877 . 84 THR CB C 69.0 0.3 1 878 . 84 THR CG2 C 19.0 0.3 1 879 . 84 THR N N 117.0 0.2 1 880 . 85 GLY H H 7.75 0.01 1 881 . 85 GLY HA2 H 4.35 0.01 2 882 . 85 GLY HA3 H 3.80 0.01 2 883 . 85 GLY CA C 46.7 0.3 1 884 . 85 GLY N N 107.1 0.2 1 885 . 86 ILE H H 10.06 0.01 1 886 . 86 ILE HA H 4.49 0.01 1 887 . 86 ILE HB H 1.84 0.01 1 888 . 86 ILE HG12 H 1.17 0.01 2 889 . 86 ILE HG13 H 1.11 0.01 2 890 . 86 ILE HG2 H 0.82 0.01 1 891 . 86 ILE HD1 H 0.64 0.01 1 892 . 86 ILE CA C 59.8 0.3 1 893 . 86 ILE CB C 42.1 0.3 1 894 . 86 ILE CG1 C 26.1 0.3 1 895 . 86 ILE CG2 C 17.2 0.3 1 896 . 86 ILE CD1 C 15.5 0.3 1 897 . 86 ILE N N 121.6 0.2 1 898 . 87 GLU H H 7.96 0.01 1 899 . 87 GLU HA H 3.95 0.01 1 900 . 87 GLU HB2 H 1.67 0.01 1 901 . 87 GLU HB3 H 1.89 0.01 1 902 . 87 GLU HG2 H 1.90 0.01 1 903 . 87 GLU HG3 H 2.05 0.01 1 904 . 87 GLU CA C 57.0 0.3 1 905 . 87 GLU CB C 28.9 0.3 1 906 . 87 GLU CG C 37.8 0.3 1 907 . 87 GLU N N 116.4 0.2 1 908 . 88 GLU H H 8.37 0.01 1 909 . 88 GLU HA H 4.18 0.01 1 910 . 88 GLU HB2 H 1.53 0.01 1 911 . 88 GLU HB3 H 1.84 0.01 1 912 . 88 GLU HG2 H 1.97 0.01 1 913 . 88 GLU HG3 H 2.44 0.01 1 914 . 88 GLU CA C 56.6 0.3 1 915 . 88 GLU CB C 32.8 0.3 1 916 . 88 GLU CG C 36.7 0.3 1 917 . 88 GLU N N 127.4 0.2 1 918 . 89 GLY H H 7.67 0.01 1 919 . 89 GLY HA2 H 4.69 0.01 2 920 . 89 GLY HA3 H 3.65 0.01 2 921 . 89 GLY CA C 43.1 0.3 1 922 . 89 GLY N N 100.6 0.2 1 923 . 90 CYS H H 9.65 0.01 1 924 . 90 CYS HA H 4.50 0.01 1 925 . 90 CYS HB2 H 3.41 0.01 1 926 . 90 CYS HB3 H 2.83 0.01 1 927 . 90 CYS CA C 61.6 0.3 1 928 . 90 CYS CB C 32.5 0.3 1 929 . 90 CYS N N 117.7 0.2 1 930 . 91 LEU H H 9.49 0.01 1 931 . 91 LEU HA H 4.36 0.01 1 932 . 91 LEU HB2 H 1.74 0.01 1 933 . 91 LEU HB3 H 1.67 0.01 1 934 . 91 LEU HG H 2.06 0.01 1 935 . 91 LEU HD1 H 1.04 0.01 1 936 . 91 LEU HD2 H 0.97 0.01 1 937 . 91 LEU CA C 58.0 0.3 1 938 . 91 LEU CB C 42.8 0.3 1 939 . 91 LEU CG C 27.5 0.3 1 940 . 91 LEU CD1 C 23.3 0.3 1 941 . 91 LEU CD2 C 25.4 0.3 1 942 . 91 LEU N N 128.4 0.2 1 943 . 92 SER H H 8.66 0.01 1 944 . 92 SER HA H 5.04 0.01 1 945 . 92 SER HB2 H 4.05 0.01 1 946 . 92 SER HB3 H 4.42 0.01 1 947 . 92 SER HG H 5.58 0.01 1 948 . 92 SER CA C 60.9 0.3 1 949 . 92 SER CB C 64.8 0.3 1 950 . 92 SER N N 109.1 0.2 1 951 . 93 ILE H H 7.72 0.01 1 952 . 93 ILE HA H 4.55 0.01 1 953 . 93 ILE HB H 2.08 0.01 1 954 . 93 ILE HG12 H 1.52 0.01 1 955 . 93 ILE HG13 H 1.52 0.01 1 956 . 93 ILE HG2 H 0.90 0.01 1 957 . 93 ILE HD1 H 0.54 0.01 1 958 . 93 ILE CA C 58.7 0.3 1 959 . 93 ILE CB C 38.5 0.3 1 960 . 93 ILE CG1 C 26.5 0.3 1 961 . 93 ILE CG2 C 19.0 0.3 1 962 . 93 ILE CD1 C 14.0 0.3 1 963 . 93 ILE N N 117.4 0.2 1 964 . 94 PRO HA H 4.37 0.01 1 965 . 94 PRO HB2 H 1.92 0.01 1 966 . 94 PRO HB3 H 2.30 0.01 1 967 . 94 PRO HG2 H 1.59 0.01 2 968 . 94 PRO HG3 H 1.83 0.01 2 969 . 94 PRO HD2 H 3.31 0.01 1 970 . 94 PRO HD3 H 3.60 0.01 1 971 . 94 PRO CA C 64.4 0.3 1 972 . 94 PRO CB C 32.1 0.3 1 973 . 94 PRO CG C 27.5 0.3 1 974 . 94 PRO CD C 50.2 0.3 1 975 . 95 GLU H H 8.85 0.01 1 976 . 95 GLU HA H 4.02 0.01 1 977 . 95 GLU HB2 H 2.22 0.01 1 978 . 95 GLU HB3 H 2.22 0.01 1 979 . 95 GLU HG2 H 2.27 0.01 2 980 . 95 GLU HG3 H 2.32 0.01 2 981 . 95 GLU CA C 58.0 0.3 1 982 . 95 GLU CB C 36.7 0.3 1 983 . 95 GLU CG C 26.5 0.3 1 984 . 95 GLU N N 112.4 0.2 1 985 . 96 GLN H H 7.49 0.01 1 986 . 96 GLN HA H 4.75 0.01 1 987 . 96 GLN HB2 H 2.12 0.01 1 988 . 96 GLN HB3 H 1.93 0.01 1 989 . 96 GLN HG2 H 2.30 0.01 1 990 . 96 GLN HG3 H 2.30 0.01 1 991 . 96 GLN HE21 H 6.63 0.01 2 992 . 96 GLN HE22 H 7.35 0.01 2 993 . 96 GLN CA C 55.5 0.3 1 994 . 96 GLN CB C 31.8 0.3 1 995 . 96 GLN CG C 33.6 0.3 1 996 . 96 GLN N N 115.0 0.2 1 997 . 96 GLN NE2 N 108.0 0.2 1 998 . 97 ARG H H 8.28 0.01 1 999 . 97 ARG HA H 5.34 0.01 1 1000 . 97 ARG HB2 H 1.51 0.01 1 1001 . 97 ARG HB3 H 1.51 0.01 1 1002 . 97 ARG HG2 H 1.51 0.01 2 1003 . 97 ARG HG3 H 1.56 0.01 2 1004 . 97 ARG HD2 H 3.02 0.01 2 1005 . 97 ARG HD3 H 3.05 0.01 2 1006 . 97 ARG CA C 54.5 0.3 1 1007 . 97 ARG CB C 34.3 0.3 1 1008 . 97 ARG CG C 27.5 0.3 1 1009 . 97 ARG CD C 43.1 0.3 1 1010 . 97 ARG N N 119.5 0.2 1 1011 . 98 ALA H H 8.04 0.01 1 1012 . 98 ALA HA H 4.58 0.01 1 1013 . 98 ALA HB H 1.23 0.01 1 1014 . 98 ALA CA C 51.6 0.3 1 1015 . 98 ALA CB C 23.3 0.3 1 1016 . 98 ALA N N 119.0 0.2 1 1017 . 99 LEU H H 8.18 0.01 1 1018 . 99 LEU HA H 4.73 0.01 1 1019 . 99 LEU HB2 H 1.32 0.01 1 1020 . 99 LEU HB3 H 1.56 0.01 1 1021 . 99 LEU HG H 1.25 0.01 1 1022 . 99 LEU HD1 H 0.66 0.01 1 1023 . 99 LEU HD2 H 0.66 0.01 1 1024 . 99 LEU CA C 55.2 0.3 1 1025 . 99 LEU CB C 42.8 0.3 1 1026 . 99 LEU CG C 27.9 0.3 1 1027 . 99 LEU CD1 C 24.7 0.3 1 1028 . 99 LEU CD2 C 24.7 0.3 1 1029 . 99 LEU N N 121.5 0.2 1 1030 . 100 VAL H H 7.45 0.01 1 1031 . 100 VAL HA H 4.54 0.01 1 1032 . 100 VAL HB H 1.94 0.01 1 1033 . 100 VAL HG1 H 0.80 0.01 1 1034 . 100 VAL HG2 H 0.55 0.01 1 1035 . 100 VAL CA C 58.4 0.3 1 1036 . 100 VAL CB C 35.0 0.3 1 1037 . 100 VAL CG1 C 21.1 0.3 1 1038 . 100 VAL CG2 C 20.4 0.3 1 1039 . 100 VAL N N 122.4 0.2 1 1040 . 101 PRO HA H 4.64 0.01 1 1041 . 101 PRO HB2 H 1.87 0.01 1 1042 . 101 PRO HB3 H 2.15 0.01 1 1043 . 101 PRO HG2 H 2.14 0.01 2 1044 . 101 PRO HG3 H 1.92 0.01 2 1045 . 101 PRO HD2 H 3.39 0.01 1 1046 . 101 PRO HD3 H 3.72 0.01 1 1047 . 101 PRO CA C 63.0 0.3 1 1048 . 101 PRO CB C 31.4 0.3 1 1049 . 101 PRO CG C 27.9 0.3 1 1050 . 101 PRO CD C 50.6 0.3 1 1051 . 102 ARG H H 8.32 0.01 1 1052 . 102 ARG HA H 4.48 0.01 1 1053 . 102 ARG HB2 H 1.65 0.01 1 1054 . 102 ARG HB3 H 1.45 0.01 1 1055 . 102 ARG HG2 H 1.66 0.01 1 1056 . 102 ARG HG3 H 1.75 0.01 1 1057 . 102 ARG HD2 H 2.62 0.01 1 1058 . 102 ARG HD3 H 3.16 0.01 1 1059 . 102 ARG HE H 6.28 0.01 1 1060 . 102 ARG HH11 H 10.30 0.01 1 1061 . 102 ARG HH12 H 10.30 0.01 1 1062 . 102 ARG HH21 H 7.73 0.01 1 1063 . 102 ARG HH22 H 9.43 0.01 1 1064 . 102 ARG CA C 53.1 0.3 1 1065 . 102 ARG CB C 35.3 0.3 1 1066 . 102 ARG CG C 26.5 0.3 1 1067 . 102 ARG CD C 43.5 0.3 1 1068 . 102 ARG N N 120.8 0.2 1 1069 . 102 ARG NE N 66.0 0.5 1 1070 . 102 ARG NH1 N 85.0 0.5 1 1071 . 102 ARG NH2 N 70.0 0.5 1 1072 . 103 ALA H H 8.64 0.01 1 1073 . 103 ALA HA H 4.65 0.01 1 1074 . 103 ALA HB H 1.23 0.01 1 1075 . 103 ALA CA C 51.6 0.3 1 1076 . 103 ALA CB C 18.7 0.3 1 1077 . 103 ALA N N 120.5 0.2 1 1078 . 104 GLU H H 7.07 0.01 1 1079 . 104 GLU HA H 4.03 0.01 1 1080 . 104 GLU HB2 H 1.79 0.01 1 1081 . 104 GLU HB3 H 2.08 0.01 1 1082 . 104 GLU HG2 H 2.20 0.01 2 1083 . 104 GLU HG3 H 2.32 0.01 2 1084 . 104 GLU CA C 57.3 0.3 1 1085 . 104 GLU CB C 31.8 0.3 1 1086 . 104 GLU CG C 36.7 0.3 1 1087 . 104 GLU N N 118.2 0.2 1 1088 . 105 LYS H H 8.09 0.01 1 1089 . 105 LYS HA H 5.20 0.01 1 1090 . 105 LYS HB2 H 1.60 0.01 1 1091 . 105 LYS HB3 H 1.72 0.01 1 1092 . 105 LYS HG2 H 1.21 0.01 1 1093 . 105 LYS HG3 H 1.21 0.01 1 1094 . 105 LYS HD2 H 1.28 0.01 2 1095 . 105 LYS HD3 H 1.32 0.01 2 1096 . 105 LYS HE2 H 2.86 0.01 1 1097 . 105 LYS HE3 H 2.86 0.01 1 1098 . 105 LYS CA C 54.5 0.3 1 1099 . 105 LYS CB C 35.7 0.3 1 1100 . 105 LYS CG C 18.0 0.3 1 1101 . 105 LYS CD C 25.0 0.3 1 1102 . 105 LYS CE C 41.7 0.3 1 1103 . 105 LYS N N 112.7 0.2 1 1104 . 106 VAL H H 8.48 0.01 1 1105 . 106 VAL HA H 5.20 0.01 1 1106 . 106 VAL HB H 2.02 0.01 1 1107 . 106 VAL HG1 H 0.72 0.01 1 1108 . 106 VAL HG2 H 0.81 0.01 1 1109 . 106 VAL CA C 58.4 0.3 1 1110 . 106 VAL CB C 36.0 0.3 1 1111 . 106 VAL CG1 C 19.0 0.3 1 1112 . 106 VAL CG2 C 22.6 0.3 1 1113 . 106 VAL N N 109.6 0.2 1 1114 . 107 LYS H H 8.55 0.01 1 1115 . 107 LYS HA H 5.48 0.01 1 1116 . 107 LYS HB2 H 1.70 0.01 1 1117 . 107 LYS HB3 H 1.77 0.01 1 1118 . 107 LYS HG2 H 1.30 0.01 2 1119 . 107 LYS HG3 H 1.20 0.01 2 1120 . 107 LYS HD2 H 1.60 0.01 1 1121 . 107 LYS HD3 H 1.60 0.01 1 1122 . 107 LYS HE2 H 2.78 0.01 1 1123 . 107 LYS HE3 H 2.78 0.01 1 1124 . 107 LYS CA C 55.2 0.3 1 1125 . 107 LYS CB C 36.0 0.3 1 1126 . 107 LYS CG C 25.8 0.3 1 1127 . 107 LYS CE C 42.1 0.3 1 1128 . 107 LYS N N 120.2 0.2 1 1129 . 108 ILE H H 9.09 0.01 1 1130 . 108 ILE HA H 5.39 0.01 1 1131 . 108 ILE HB H 1.82 0.01 1 1132 . 108 ILE HG12 H 1.57 0.01 2 1133 . 108 ILE HG13 H 1.40 0.01 2 1134 . 108 ILE HG2 H 0.82 0.01 1 1135 . 108 ILE HD1 H 0.70 0.01 1 1136 . 108 ILE CA C 57.7 0.3 1 1137 . 108 ILE CB C 42.4 0.3 1 1138 . 108 ILE CG1 C 26.8 0.3 1 1139 . 108 ILE CG2 C 19.0 0.3 1 1140 . 108 ILE CD1 C 15.5 0.3 1 1141 . 108 ILE N N 118.7 0.2 1 1142 . 109 ARG H H 8.54 0.01 1 1143 . 109 ARG HA H 5.20 0.01 1 1144 . 109 ARG HB2 H 1.68 0.01 1 1145 . 109 ARG HB3 H 1.75 0.01 1 1146 . 109 ARG HG2 H 1.53 0.01 2 1147 . 109 ARG HG3 H 1.59 0.01 2 1148 . 109 ARG HD2 H 3.18 0.01 1 1149 . 109 ARG HD3 H 3.18 0.01 1 1150 . 109 ARG HE H 8.35 0.01 1 1151 . 109 ARG CA C 54.1 0.3 1 1152 . 109 ARG CB C 33.9 0.3 1 1153 . 109 ARG CG C 27.2 0.3 1 1154 . 109 ARG CD C 43.5 0.3 1 1155 . 109 ARG N N 118.1 0.2 1 1156 . 109 ARG NE N 83.0 0.5 1 1157 . 110 ALA H H 8.35 0.01 1 1158 . 110 ALA HA H 4.43 0.01 1 1159 . 110 ALA HB H 1.02 0.01 1 1160 . 110 ALA CA C 50.9 0.3 1 1161 . 110 ALA CB C 22.6 0.3 1 1162 . 110 ALA N N 122.4 0.2 1 1163 . 111 LEU H H 9.09 0.01 1 1164 . 111 LEU HA H 5.14 0.01 1 1165 . 111 LEU HB2 H 1.70 0.01 1 1166 . 111 LEU HB3 H 1.12 0.01 1 1167 . 111 LEU HG H 1.60 0.01 1 1168 . 111 LEU HD1 H 0.69 0.01 1 1169 . 111 LEU HD2 H 0.81 0.01 1 1170 . 111 LEU CA C 53.4 0.3 1 1171 . 111 LEU CB C 43.8 0.3 1 1172 . 111 LEU CG C 29.3 0.3 1 1173 . 111 LEU CD1 C 22.2 0.3 1 1174 . 111 LEU CD2 C 25.0 0.3 1 1175 . 111 LEU N N 114.2 0.2 1 1176 . 112 ASP H H 8.48 0.01 1 1177 . 112 ASP HA H 4.83 0.01 1 1178 . 112 ASP HB2 H 3.40 0.01 1 1179 . 112 ASP HB3 H 2.76 0.01 1 1180 . 112 ASP CA C 52.0 0.3 1 1181 . 112 ASP CB C 41.4 0.3 1 1182 . 112 ASP N N 117.1 0.2 1 1183 . 113 ARG H H 8.05 0.01 1 1184 . 113 ARG HA H 3.84 0.01 1 1185 . 113 ARG HB2 H 1.78 0.01 1 1186 . 113 ARG HB3 H 1.92 0.01 1 1187 . 113 ARG HG2 H 1.42 0.01 2 1188 . 113 ARG HG3 H 1.94 0.01 2 1189 . 113 ARG HD2 H 3.09 0.01 2 1190 . 113 ARG HD3 H 3.24 0.01 2 1191 . 113 ARG CA C 58.7 0.3 1 1192 . 113 ARG CB C 30.4 0.3 1 1193 . 113 ARG CG C 27.9 0.3 1 1194 . 113 ARG CD C 43.5 0.3 1 1195 . 113 ARG N N 112.1 0.2 1 1196 . 114 ASP H H 8.07 0.01 1 1197 . 114 ASP HA H 4.70 0.01 1 1198 . 114 ASP HB2 H 2.70 0.01 1 1199 . 114 ASP HB3 H 2.85 0.01 1 1200 . 114 ASP CA C 54.1 0.3 1 1201 . 114 ASP CB C 42.4 0.3 1 1202 . 114 ASP N N 111.7 0.2 1 1203 . 115 GLY H H 8.68 0.01 1 1204 . 115 GLY HA2 H 3.51 0.01 1 1205 . 115 GLY HA3 H 4.22 0.01 1 1206 . 115 GLY CA C 45.6 0.3 1 1207 . 115 GLY N N 107.2 0.2 1 1208 . 116 LYS H H 8.66 0.01 1 1209 . 116 LYS HA H 4.83 0.01 1 1210 . 116 LYS HB2 H 2.09 0.01 1 1211 . 116 LYS HB3 H 1.93 0.01 1 1212 . 116 LYS HG2 H 1.46 0.01 2 1213 . 116 LYS HG3 H 1.50 0.01 2 1214 . 116 LYS HD2 H 1.78 0.01 1 1215 . 116 LYS HD3 H 1.78 0.01 1 1216 . 116 LYS HE2 H 3.05 0.01 1 1217 . 116 LYS HE3 H 3.05 0.01 1 1218 . 116 LYS CA C 53.1 0.3 1 1219 . 116 LYS CB C 32.1 0.3 1 1220 . 116 LYS CG C 24.7 0.3 1 1221 . 116 LYS CD C 28.9 0.3 1 1222 . 116 LYS CE C 42.1 0.3 1 1223 . 116 LYS N N 120.9 0.2 1 1224 . 117 PRO HA H 5.37 0.01 1 1225 . 117 PRO HB2 H 2.12 0.01 1 1226 . 117 PRO HB3 H 1.92 0.01 1 1227 . 117 PRO HG2 H 2.00 0.01 2 1228 . 117 PRO HG3 H 2.16 0.01 2 1229 . 117 PRO HD2 H 3.80 0.01 1 1230 . 117 PRO HD3 H 3.98 0.01 1 1231 . 117 PRO CA C 62.3 0.3 1 1232 . 117 PRO CB C 32.5 0.3 1 1233 . 117 PRO CG C 27.5 0.3 1 1234 . 117 PRO CD C 50.9 0.3 1 1235 . 118 PHE H H 9.24 0.01 1 1236 . 118 PHE HA H 4.97 0.01 1 1237 . 118 PHE HB2 H 3.09 0.01 1 1238 . 118 PHE HB3 H 3.31 0.01 1 1239 . 118 PHE HD1 H 7.20 0.01 1 1240 . 118 PHE HD2 H 7.20 0.01 1 1241 . 118 PHE HE1 H 7.10 0.01 1 1242 . 118 PHE HE2 H 7.10 0.01 1 1243 . 118 PHE HZ H 7.37 0.01 1 1244 . 118 PHE CA C 56.3 0.3 1 1245 . 118 PHE CB C 41.4 0.3 1 1246 . 118 PHE N N 116.8 0.2 1 1247 . 119 GLU H H 8.30 0.01 1 1248 . 119 GLU HA H 5.23 0.01 1 1249 . 119 GLU HB2 H 1.84 0.01 2 1250 . 119 GLU HB3 H 1.88 0.01 2 1251 . 119 GLU HG2 H 2.09 0.01 2 1252 . 119 GLU HG3 H 2.25 0.01 2 1253 . 119 GLU CA C 54.1 0.3 1 1254 . 119 GLU CB C 33.2 0.3 1 1255 . 119 GLU CG C 36.7 0.3 1 1256 . 119 GLU N N 115.5 0.2 1 1257 . 120 LEU H H 8.79 0.01 1 1258 . 120 LEU HA H 4.82 0.01 1 1259 . 120 LEU HB2 H 1.58 0.01 1 1260 . 120 LEU HB3 H 1.63 0.01 1 1261 . 120 LEU HG H 1.46 0.01 1 1262 . 120 LEU HD1 H 0.89 0.01 1 1263 . 120 LEU HD2 H 1.02 0.01 1 1264 . 120 LEU CA C 54.5 0.3 1 1265 . 120 LEU CB C 47.0 0.3 1 1266 . 120 LEU CG C 27.2 0.3 1 1267 . 120 LEU CD1 C 27.2 0.3 1 1268 . 120 LEU CD2 C 22.6 0.3 1 1269 . 120 LEU N N 121.8 0.2 1 1270 . 121 GLU H H 8.62 0.01 1 1271 . 121 GLU HA H 5.14 0.01 1 1272 . 121 GLU HB2 H 2.05 0.01 1 1273 . 121 GLU HB3 H 1.89 0.01 1 1274 . 121 GLU HG2 H 2.18 0.01 2 1275 . 121 GLU HG3 H 2.05 0.01 2 1276 . 121 GLU CA C 55.2 0.3 1 1277 . 121 GLU CB C 31.4 0.3 1 1278 . 121 GLU CG C 37.1 0.3 1 1279 . 121 GLU N N 124.5 0.2 1 1280 . 122 ALA H H 9.04 0.01 1 1281 . 122 ALA HA H 4.92 0.01 1 1282 . 122 ALA HB H 1.14 0.01 1 1283 . 122 ALA CA C 50.2 0.3 1 1284 . 122 ALA CB C 23.3 0.3 1 1285 . 122 ALA N N 123.9 0.2 1 1286 . 123 ASP H H 8.28 0.01 1 1287 . 123 ASP HA H 5.42 0.01 1 1288 . 123 ASP HB2 H 2.98 0.01 1 1289 . 123 ASP HB3 H 2.63 0.01 1 1290 . 123 ASP CA C 52.0 0.3 1 1291 . 123 ASP CB C 43.8 0.3 1 1292 . 123 ASP N N 118.2 0.2 1 1293 . 124 GLY H H 8.28 0.01 1 1294 . 124 GLY HA2 H 3.85 0.01 1 1295 . 124 GLY HA3 H 4.02 0.01 1 1296 . 124 GLY CA C 46.7 0.3 1 1297 . 124 GLY N N 104.4 0.2 1 1298 . 125 LEU H H 8.65 0.01 1 1299 . 125 LEU HA H 4.05 0.01 1 1300 . 125 LEU HB2 H 1.79 0.01 1 1301 . 125 LEU HB3 H 1.68 0.01 1 1302 . 125 LEU HG H 1.56 0.01 1 1303 . 125 LEU HD1 H 0.93 0.01 1 1304 . 125 LEU HD2 H 0.93 0.01 1 1305 . 125 LEU CA C 57.7 0.3 1 1306 . 125 LEU CB C 42.1 0.3 1 1307 . 125 LEU CG C 27.2 0.3 1 1308 . 125 LEU CD1 C 22.6 0.3 1 1309 . 125 LEU CD2 C 22.6 0.3 1 1310 . 125 LEU N N 123.4 0.2 1 1311 . 126 LEU H H 8.70 0.01 1 1312 . 126 LEU HA H 4.06 0.01 1 1313 . 126 LEU HB2 H 2.08 0.01 1 1314 . 126 LEU HB3 H 1.67 0.01 1 1315 . 126 LEU HG H 1.41 0.01 1 1316 . 126 LEU HD1 H 1.02 0.01 1 1317 . 126 LEU HD2 H 0.89 0.01 1 1318 . 126 LEU CA C 58.4 0.3 1 1319 . 126 LEU CB C 40.7 0.3 1 1320 . 126 LEU CG C 27.2 0.3 1 1321 . 126 LEU CD1 C 25.8 0.3 1 1322 . 126 LEU CD2 C 20.8 0.3 1 1323 . 126 LEU N N 116.2 0.2 1 1324 . 127 ALA H H 7.13 0.01 1 1325 . 127 ALA HA H 3.68 0.01 1 1326 . 127 ALA HB H 1.20 0.01 1 1327 . 127 ALA CA C 55.2 0.3 1 1328 . 127 ALA CB C 18.0 0.3 1 1329 . 127 ALA N N 116.2 0.2 1 1330 . 128 ILE H H 7.79 0.01 1 1331 . 128 ILE HA H 3.42 0.01 1 1332 . 128 ILE HB H 2.02 0.01 1 1333 . 128 ILE HG12 H 1.63 0.01 1 1334 . 128 ILE HG13 H 1.00 0.01 1 1335 . 128 ILE HG2 H 0.92 0.01 1 1336 . 128 ILE HD1 H 0.79 0.01 1 1337 . 128 ILE CA C 65.8 0.3 1 1338 . 128 ILE CB C 38.2 0.3 1 1339 . 128 ILE CG1 C 28.9 0.3 1 1340 . 128 ILE CG2 C 16.9 0.3 1 1341 . 128 ILE CD1 C 13.3 0.3 1 1342 . 128 ILE N N 119.7 0.2 1 1343 . 129 CYS H H 8.75 0.01 1 1344 . 129 CYS HA H 4.10 0.01 1 1345 . 129 CYS HB2 H 2.88 0.01 2 1346 . 129 CYS HB3 H 2.93 0.01 2 1347 . 129 CYS CA C 63.0 0.3 1 1348 . 129 CYS CB C 26.8 0.3 1 1349 . 129 CYS N N 117.1 0.2 1 1350 . 130 ILE H H 8.66 0.01 1 1351 . 130 ILE HA H 3.33 0.01 1 1352 . 130 ILE HB H 1.74 0.01 1 1353 . 130 ILE HG12 H 0.62 0.01 2 1354 . 130 ILE HG13 H 1.93 0.01 2 1355 . 130 ILE HG2 H 0.59 0.01 1 1356 . 130 ILE HD1 H 0.63 0.01 1 1357 . 130 ILE CA C 66.9 0.3 1 1358 . 130 ILE CB C 38.2 0.3 1 1359 . 130 ILE CG1 C 30.4 0.3 1 1360 . 130 ILE CG2 C 14.8 0.3 1 1361 . 130 ILE N N 115.7 0.2 1 1362 . 131 GLN H H 7.49 0.01 1 1363 . 131 GLN HA H 3.88 0.01 1 1364 . 131 GLN HB2 H 2.11 0.01 1 1365 . 131 GLN HB3 H 2.41 0.01 1 1366 . 131 GLN HG2 H 2.13 0.01 1 1367 . 131 GLN HG3 H 2.41 0.01 1 1368 . 131 GLN HE21 H 6.59 0.01 2 1369 . 131 GLN HE22 H 8.31 0.01 2 1370 . 131 GLN CA C 59.8 0.3 1 1371 . 131 GLN CB C 31.4 0.3 1 1372 . 131 GLN CG C 36.7 0.3 1 1373 . 131 GLN N N 115.2 0.2 1 1374 . 131 GLN NE2 N 110.3 0.2 1 1375 . 132 HIS H H 8.69 0.01 1 1376 . 132 HIS HA H 4.04 0.01 1 1377 . 132 HIS HB2 H 3.25 0.01 1 1378 . 132 HIS HB3 H 3.53 0.01 1 1379 . 132 HIS HD1 H 13.86 0.01 1 1380 . 132 HIS HD2 H 6.82 0.01 1 1381 . 132 HIS HE1 H 8.05 0.01 1 1382 . 132 HIS CA C 59.4 0.3 1 1383 . 132 HIS CB C 28.6 0.3 1 1384 . 132 HIS N N 117.1 0.2 1 1385 . 132 HIS ND1 N 172.9 0.5 1 1386 . 132 HIS NE2 N 205.1 0.5 1 1387 . 133 GLU H H 9.19 0.01 1 1388 . 133 GLU HA H 4.83 0.01 1 1389 . 133 GLU HB2 H 1.87 0.01 1 1390 . 133 GLU HB3 H 2.33 0.01 1 1391 . 133 GLU HG2 H 2.03 0.01 1 1392 . 133 GLU HG3 H 2.92 0.01 1 1393 . 133 GLU CA C 58.7 0.3 1 1394 . 133 GLU CB C 29.7 0.3 1 1395 . 133 GLU CG C 32.8 0.3 1 1396 . 133 GLU N N 116.5 0.2 1 1397 . 134 MET H H 8.99 0.01 1 1398 . 134 MET HA H 3.88 0.01 1 1399 . 134 MET HB2 H 2.09 0.01 1 1400 . 134 MET HB3 H 2.28 0.01 1 1401 . 134 MET HG2 H 2.84 0.01 1 1402 . 134 MET HG3 H 2.06 0.01 1 1403 . 134 MET HE H 1.92 0.01 1 1404 . 134 MET CA C 61.2 0.3 1 1405 . 134 MET CB C 32.1 0.3 1 1406 . 134 MET CG C 34.6 0.3 1 1407 . 134 MET CE C 16.9 0.3 1 1408 . 134 MET N N 116.5 0.2 1 1409 . 135 ASP H H 8.03 0.01 1 1410 . 135 ASP HA H 4.47 0.01 1 1411 . 135 ASP HB2 H 2.36 0.01 1 1412 . 135 ASP HB3 H 3.05 0.01 1 1413 . 135 ASP CA C 56.6 0.3 1 1414 . 135 ASP CB C 38.9 0.3 1 1415 . 135 ASP N N 118.6 0.2 1 1416 . 136 HIS H H 7.39 0.01 1 1417 . 136 HIS HA H 4.65 0.01 1 1418 . 136 HIS HB2 H 3.90 0.01 1 1419 . 136 HIS HB3 H 2.78 0.01 1 1420 . 136 HIS HD1 H 12.80 0.01 1 1421 . 136 HIS HD2 H 7.91 0.01 1 1422 . 136 HIS HE1 H 7.62 0.01 1 1423 . 136 HIS CA C 59.8 0.3 1 1424 . 136 HIS CB C 29.3 0.3 1 1425 . 136 HIS N N 113.8 0.2 1 1426 . 136 HIS ND1 N 165.8 0.5 1 1427 . 136 HIS NE2 N 215.3 0.5 1 1428 . 137 LEU H H 7.29 0.01 1 1429 . 137 LEU HA H 4.59 0.01 1 1430 . 137 LEU HB2 H 2.26 0.01 1 1431 . 137 LEU HB3 H 1.64 0.01 1 1432 . 137 LEU HG H 2.30 0.01 1 1433 . 137 LEU HD1 H 1.26 0.01 1 1434 . 137 LEU HD2 H 0.91 0.01 1 1435 . 137 LEU CA C 55.9 0.3 1 1436 . 137 LEU CB C 42.4 0.3 1 1437 . 137 LEU CG C 26.1 0.3 1 1438 . 137 LEU CD1 C 22.2 0.3 1 1439 . 137 LEU CD2 C 25.4 0.3 1 1440 . 137 LEU N N 109.0 0.2 1 1441 . 138 VAL H H 7.61 0.01 1 1442 . 138 VAL HA H 4.75 0.01 1 1443 . 138 VAL HB H 2.67 0.01 1 1444 . 138 VAL HG1 H 1.00 0.01 1 1445 . 138 VAL HG2 H 1.04 0.01 1 1446 . 138 VAL CA C 60.2 0.3 1 1447 . 138 VAL CB C 30.4 0.3 1 1448 . 138 VAL CG1 C 21.9 0.3 1 1449 . 138 VAL CG2 C 18.7 0.3 1 1450 . 138 VAL N N 109.3 0.2 1 1451 . 139 GLY H H 8.03 0.01 1 1452 . 139 GLY HA2 H 4.10 0.01 2 1453 . 139 GLY HA3 H 3.74 0.01 2 1454 . 139 GLY CA C 46.3 0.3 1 1455 . 139 GLY N N 107.9 0.2 1 1456 . 140 LYS H H 7.97 0.01 1 1457 . 140 LYS HA H 4.34 0.01 1 1458 . 140 LYS HB2 H 1.51 0.01 1 1459 . 140 LYS HB3 H 1.38 0.01 1 1460 . 140 LYS HG2 H 1.15 0.01 2 1461 . 140 LYS HG3 H 1.35 0.01 2 1462 . 140 LYS HD2 H 1.00 0.01 1 1463 . 140 LYS HD3 H 1.00 0.01 1 1464 . 140 LYS HE2 H 2.55 0.01 2 1465 . 140 LYS HE3 H 2.59 0.01 2 1466 . 140 LYS CA C 55.2 0.3 1 1467 . 140 LYS CB C 34.6 0.3 1 1468 . 140 LYS CG C 24.3 0.3 1 1469 . 140 LYS CE C 41.4 0.3 1 1470 . 140 LYS N N 117.3 0.2 1 1471 . 141 LEU H H 8.07 0.01 1 1472 . 141 LEU HA H 4.41 0.01 1 1473 . 141 LEU HB2 H 1.49 0.01 1 1474 . 141 LEU HB3 H 1.27 0.01 1 1475 . 141 LEU HG H 1.59 0.01 1 1476 . 141 LEU HD1 H 0.95 0.01 1 1477 . 141 LEU HD2 H 0.80 0.01 1 1478 . 141 LEU CA C 52.0 0.3 1 1479 . 141 LEU CB C 44.9 0.3 1 1480 . 141 LEU CG C 27.5 0.3 1 1481 . 141 LEU CD1 C 24.3 0.3 1 1482 . 141 LEU CD2 C 24.3 0.3 1 1483 . 141 LEU N N 121.5 0.01 1 1484 . 142 PHE H H 8.66 0.01 1 1485 . 142 PHE HA H 4.57 0.01 1 1486 . 142 PHE HB2 H 3.36 0.01 1 1487 . 142 PHE HB3 H 2.58 0.01 1 1488 . 142 PHE HD1 H 7.08 0.01 1 1489 . 142 PHE HD2 H 7.08 0.01 1 1490 . 142 PHE HE1 H 7.23 0.01 1 1491 . 142 PHE HE2 H 7.23 0.01 1 1492 . 142 PHE HZ H 7.37 0.01 1 1493 . 142 PHE CA C 60.5 0.3 1 1494 . 142 PHE CB C 37.5 0.3 1 1495 . 142 PHE N N 117.2 0.2 1 1496 . 143 MET H H 5.82 0.01 1 1497 . 143 MET HA H 4.14 0.01 1 1498 . 143 MET HB2 H 1.64 0.01 1 1499 . 143 MET HB3 H 1.92 0.01 1 1500 . 143 MET HG2 H 2.20 0.01 1 1501 . 143 MET HG3 H 1.74 0.01 1 1502 . 143 MET HE H 2.03 0.01 1 1503 . 143 MET CA C 55.5 0.3 1 1504 . 143 MET CB C 31.4 0.3 1 1505 . 143 MET CG C 31.4 0.3 1 1506 . 143 MET CE C 17.2 0.3 1 1507 . 143 MET N N 112.5 0.2 1 1508 . 144 ASP H H 8.06 0.01 1 1509 . 144 ASP HA H 4.24 0.01 1 1510 . 144 ASP HB2 H 2.47 0.01 1 1511 . 144 ASP HB3 H 2.56 0.01 1 1512 . 144 ASP CA C 56.3 0.3 1 1513 . 144 ASP CB C 39.9 0.3 1 1514 . 144 ASP N N 117.9 0.2 1 1515 . 145 TYR H H 7.26 0.01 1 1516 . 145 TYR HA H 4.36 0.01 1 1517 . 145 TYR HB2 H 3.29 0.01 1 1518 . 145 TYR HB3 H 2.91 0.01 1 1519 . 145 TYR HD1 H 7.40 0.01 1 1520 . 145 TYR HD2 H 7.40 0.01 1 1521 . 145 TYR HE1 H 6.78 0.01 1 1522 . 145 TYR HE2 H 6.78 0.01 1 1523 . 145 TYR CA C 59.4 0.3 1 1524 . 145 TYR CB C 38.5 0.3 1 1525 . 145 TYR N N 112.6 0.2 1 1526 . 146 LEU H H 7.37 0.01 1 1527 . 146 LEU HA H 4.55 0.01 1 1528 . 146 LEU HB2 H 1.78 0.01 1 1529 . 146 LEU HB3 H 1.78 0.01 1 1530 . 146 LEU HG H 1.76 0.01 1 1531 . 146 LEU HD1 H 0.93 0.01 1 1532 . 146 LEU HD2 H 0.93 0.01 1 1533 . 146 LEU CA C 54.8 0.3 1 1534 . 146 LEU CB C 42.1 0.3 1 1535 . 146 LEU CG C 27.5 0.3 1 1536 . 146 LEU CD1 C 22.6 0.3 1 1537 . 146 LEU CD2 C 22.6 0.3 1 1538 . 146 LEU N N 117.6 0.2 1 1539 . 147 SER H H 7.60 0.01 1 1540 . 147 SER HA H 4.28 0.01 1 1541 . 147 SER HB2 H 3.85 0.01 1 1542 . 147 SER HB3 H 3.85 0.01 1 1543 . 147 SER CA C 60.2 0.3 1 1544 . 147 SER CB C 65.1 0.3 1 1545 . 147 SER N N 118.5 0.2 1 stop_ save_