data_6392 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Refined solution structure of the human TSG-6 Link module ; _BMRB_accession_number 6392 _BMRB_flat_file_name bmr6392.str _Entry_type original _Submission_date 2004-11-17 _Accession_date 2004-11-17 _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 Blundell C. D. . 2 Teriete P. . . 3 Kahmann J. D. . 4 Pickford A. R. . 5 Campbell I. D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 581 "13C chemical shifts" 412 "15N chemical shifts" 111 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-11-14 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6393 'Complex form with HA octasaccharide' 7221 'Link_TSG6 and hyaluronan octasaccharide complex, additional set of chemical shifts' 7222 'Link_TSG6 free form, additional set of chemical shifts' stop_ _Original_release_date 2005-11-14 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Towards a Structure for a TSG-6{middle dot}Hyaluronan Complex by Modeling and NMR Spectroscopy: INSIGHTS INTO OTHER MEMBERS OF THE LINK MODULE SUPERFAMILY. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15718240 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Blundell C. D. . 2 Almond A. . . 3 Mahoney D. J. . 4 Deangelis P. L. . 5 Campbell I. D. . 6 Day A. J. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 280 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 18189 _Page_last 18201 _Year 2005 _Details . loop_ _Keyword 'hyaluronan-binding domain' 'carbohydrate-binding domain' 'Link module' stop_ save_ ################################## # Molecular system description # ################################## save_system_Link_TSG6 _Saveframe_category molecular_system _Mol_system_name 'human TSG-6' _Abbreviation_common 'Link TSG6' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Link TSG6' $Link_TSG6 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Link_TSG6 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human TSG-6' _Abbreviation_common 'Link TSG6' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 98 _Mol_residue_sequence ; GVYHREARSGKYKLTYAEAK AVCEFEGGHLATYKQLEAAR KIGFHVCAAGWMAKGRVGYP IVKPGPNCGFGKTGIIDYGI RLNRSERWDAYCYNPHAK ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 VAL 3 TYR 4 HIS 5 ARG 6 GLU 7 ALA 8 ARG 9 SER 10 GLY 11 LYS 12 TYR 13 LYS 14 LEU 15 THR 16 TYR 17 ALA 18 GLU 19 ALA 20 LYS 21 ALA 22 VAL 23 CYS 24 GLU 25 PHE 26 GLU 27 GLY 28 GLY 29 HIS 30 LEU 31 ALA 32 THR 33 TYR 34 LYS 35 GLN 36 LEU 37 GLU 38 ALA 39 ALA 40 ARG 41 LYS 42 ILE 43 GLY 44 PHE 45 HIS 46 VAL 47 CYS 48 ALA 49 ALA 50 GLY 51 TRP 52 MET 53 ALA 54 LYS 55 GLY 56 ARG 57 VAL 58 GLY 59 TYR 60 PRO 61 ILE 62 VAL 63 LYS 64 PRO 65 GLY 66 PRO 67 ASN 68 CYS 69 GLY 70 PHE 71 GLY 72 LYS 73 THR 74 GLY 75 ILE 76 ILE 77 ASP 78 TYR 79 GLY 80 ILE 81 ARG 82 LEU 83 ASN 84 ARG 85 SER 86 GLU 87 ARG 88 TRP 89 ASP 90 ALA 91 TYR 92 CYS 93 TYR 94 ASN 95 PRO 96 HIS 97 ALA 98 LYS 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 6393 "human TSG-6" 100.00 98 100.00 100.00 7.62e-65 BMRB 7221 Link_TSG6 100.00 98 100.00 100.00 7.62e-65 BMRB 7222 Link_TSG6 100.00 98 100.00 100.00 7.62e-65 PDB 1O7B "Refined Solution Structure Of The Human Tsg-6 Link Module" 100.00 98 100.00 100.00 7.62e-65 PDB 1O7C "Solution Structure Of The Human Tsg-6 Link Module In The Presence Of A Hyaluronan Octasaccharide" 100.00 98 100.00 100.00 7.62e-65 PDB 2PF5 "Crystal Structure Of The Human Tsg-6 Link Module" 100.00 98 100.00 100.00 7.62e-65 DBJ BAE24204 "unnamed protein product [Mus musculus]" 100.00 275 96.94 98.98 2.36e-61 DBJ BAJ20799 "tumor necrosis factor, alpha-induced protein 6 [synthetic construct]" 100.00 277 100.00 100.00 8.65e-64 EMBL CAD12353 "TSG-6 protein [Homo sapiens]" 100.00 277 100.00 100.00 8.65e-64 EMBL CAD13434 "TSG-6 protein [Homo sapiens]" 100.00 277 100.00 100.00 9.33e-64 EMBL CAH74219 "tumor necrosis factor-stimulated protein TSG-6 precursor [Bos taurus]" 100.00 280 98.98 100.00 3.97e-63 GB AAA03342 "secreted hyaluronate binding protein [Oryctolagus cuniculus]" 100.00 276 97.96 97.96 1.96e-61 GB AAB00792 "adhesion receptor CD44 [Homo sapiens]" 100.00 277 97.96 97.96 1.81e-61 GB AAC53527 "TNF-stimulated gene 6 protein [Mus musculus]" 100.00 275 96.94 98.98 2.36e-61 GB AAH21155 "Tnfaip6 protein [Mus musculus]" 100.00 275 96.94 98.98 2.36e-61 GB AAH30205 "Tumor necrosis factor, alpha-induced protein 6 [Homo sapiens]" 100.00 277 100.00 100.00 8.65e-64 REF NP_001007814 "tumor necrosis factor-inducible gene 6 protein precursor [Bos taurus]" 100.00 280 98.98 100.00 3.97e-63 REF NP_001075375 "tumor necrosis factor alpha-induced protein 6 precursor [Equus caballus]" 100.00 277 98.98 100.00 4.20e-63 REF NP_001075780 "tumor necrosis factor-inducible gene 6 protein precursor [Oryctolagus cuniculus]" 100.00 276 97.96 97.96 1.96e-61 REF NP_001252869 "tumor necrosis factor-inducible gene 6 protein precursor [Macaca mulatta]" 100.00 277 97.96 100.00 3.38e-63 REF NP_009046 "tumor necrosis factor-inducible gene 6 protein precursor [Homo sapiens]" 100.00 277 100.00 100.00 8.65e-64 SP O08859 "RecName: Full=Tumor necrosis factor-inducible gene 6 protein; AltName: Full=TNF-stimulated gene 6 protein; Short=TSG-6; AltName" 100.00 275 96.94 98.98 2.36e-61 SP P98065 "RecName: Full=Tumor necrosis factor-inducible gene 6 protein; AltName: Full=Hyaluronate-binding protein PS4; AltName: Full=TNF-" 100.00 276 97.96 97.96 1.96e-61 SP P98066 "RecName: Full=Tumor necrosis factor-inducible gene 6 protein; AltName: Full=Hyaluronate-binding protein; AltName: Full=TNF-stim" 100.00 277 100.00 100.00 8.65e-64 TPG DAA32671 "TPA: tumor necrosis factor, alpha-induced protein 6 [Bos taurus]" 100.00 280 98.98 100.00 3.97e-63 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Details $Link_TSG6 Human 9606 Eukaryota Metazoa Homo sapiens 'Extracellular, inflammation-associated.' 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 $Link_TSG6 'recombinant technology' 'Escherichia coli' Escherichia coli BL21(DE3) pET 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 $Link_TSG6 1.0 mM . 'Na ions' 2 mM . D2O 100 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Link_TSG6 2.0 mM [U-15N] 'Na ions' 2 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Link_TSG6 2.3 mM '[U-15N; U-13C]' 'Na ions' 2 mM . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2.3 loop_ _Task 'spectrum processing' stop_ _Details . save_ save_XEasy _Saveframe_category software _Name XEasy _Version . loop_ _Task 'spectrum analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer n/a _Model n/a _Field_strength 750 _Details 'Homebuilt Spectrometer incorporating Oxford Instruments Magnet, 600MHz.' save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer n/a _Model n/a _Field_strength 750 _Details 'Homebuilt Spectrometer incorporating Oxford Instruments Magnet, 750MHz.' save_ ############################# # NMR applied experiments # ############################# save_15N-NOESY-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY-HSQC _Sample_label . save_ save_15N-HSQC-NOESY-HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC-NOESY-HSQC _Sample_label . save_ save_13C-NOESY-HSQC_3 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-NOESY-HSQC _Sample_label . save_ save_2D-NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details 'Full details given in the publication.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HSQC-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details 'Full details given in the publication.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name 13C-NOESY-HSQC _BMRB_pulse_sequence_accession_number . _Details 'Full details given in the publication.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-NOESY _BMRB_pulse_sequence_accession_number . _Details 'Full details given in the publication.' save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details ; The sample was equilibrated for 20 minutes under these conditions before the spectra were collected. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.2 pH temperature 298 0.5 K 'ionic strength' 2 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio 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_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 $sample_2 $sample_3 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'Link TSG6' _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 GLY CA C 43.60 0.05 1 2 . 1 GLY HA2 H 3.83 0.02 1 3 . 1 GLY HA3 H 3.52 0.02 1 4 . 1 GLY C C 169.82 0.05 1 5 . 2 VAL N N 123.05 0.05 1 6 . 2 VAL H H 8.45 0.02 1 7 . 2 VAL CA C 60.75 0.05 1 8 . 2 VAL HA H 5.24 0.02 1 9 . 2 VAL CB C 33.41 0.05 1 10 . 2 VAL HB H 1.30 0.02 1 11 . 2 VAL CG1 C 23.67 0.05 1 12 . 2 VAL HG1 H 0.85 0.02 1 13 . 2 VAL CG2 C 23.03 0.05 1 14 . 2 VAL HG2 H 0.74 0.02 1 15 . 2 VAL C C 174.81 0.05 1 16 . 3 TYR N N 120.47 0.05 1 17 . 3 TYR H H 8.78 0.02 1 18 . 3 TYR CA C 56.17 0.05 1 19 . 3 TYR HA H 5.02 0.02 1 20 . 3 TYR CB C 40.43 0.05 1 21 . 3 TYR HB2 H 3.09 0.02 1 22 . 3 TYR HB3 H 2.97 0.02 1 23 . 3 TYR CD1 C 133.95 0.05 1 24 . 3 TYR HD1 H 6.79 0.02 1 25 . 3 TYR CD2 C 133.95 0.05 1 26 . 3 TYR HD2 H 6.79 0.02 1 27 . 3 TYR CE1 C 117.95 0.05 1 28 . 3 TYR HE1 H 6.59 0.02 1 29 . 3 TYR CE2 C 117.95 0.05 1 30 . 3 TYR HE2 H 6.59 0.02 1 31 . 3 TYR C C 172.74 0.05 1 32 . 4 HIS N N 121.64 0.05 1 33 . 4 HIS H H 9.31 0.02 1 34 . 4 HIS CA C 54.71 0.05 1 35 . 4 HIS HA H 4.91 0.02 1 36 . 4 HIS NE2 N 175.93 0.05 1 37 . 4 HIS CD2 C 117.22 0.05 1 38 . 4 HIS HD2 H 6.34 0.02 1 39 . 4 HIS CE1 C 137.91 0.05 1 40 . 4 HIS HE1 H 8.13 0.02 1 41 . 4 HIS CB C 32.64 0.05 1 42 . 4 HIS HB2 H 3.36 0.02 1 43 . 4 HIS HB3 H 3.27 0.02 1 44 . 4 HIS C C 173.35 0.05 1 45 . 5 ARG N N 128.76 0.05 1 46 . 5 ARG H H 8.79 0.02 1 47 . 5 ARG CA C 53.31 0.05 1 48 . 5 ARG HA H 4.60 0.02 1 49 . 5 ARG CB C 33.99 0.05 1 50 . 5 ARG HB2 H 1.48 0.02 1 51 . 5 ARG HB3 H 1.48 0.02 1 52 . 5 ARG CG C 27.97 0.05 1 53 . 5 ARG HG2 H 1.48 0.02 1 54 . 5 ARG HG3 H 1.48 0.02 1 55 . 5 ARG CD C 41.91 0.05 1 56 . 5 ARG HD2 H 3.49 0.02 1 57 . 5 ARG HD3 H 3.27 0.02 1 58 . 5 ARG NE N 87.05 0.05 1 59 . 5 ARG HE H 8.79 0.02 1 60 . 5 ARG C C 173.05 0.05 1 61 . 6 GLU N N 121.14 0.05 1 62 . 6 GLU H H 8.19 0.02 1 63 . 6 GLU CA C 53.36 0.05 1 64 . 6 GLU HA H 4.48 0.02 1 65 . 6 GLU CB C 33.32 0.05 1 66 . 6 GLU HB2 H 1.91 0.02 1 67 . 6 GLU HB3 H 1.74 0.02 1 68 . 6 GLU CG C 35.66 0.05 1 69 . 6 GLU HG2 H 2.27 0.02 1 70 . 6 GLU HG3 H 2.00 0.02 1 71 . 6 GLU C C 176.75 0.05 1 72 . 7 ALA N N 123.68 0.05 1 73 . 7 ALA H H 8.86 0.02 1 74 . 7 ALA CA C 52.33 0.05 1 75 . 7 ALA HA H 4.22 0.02 1 76 . 7 ALA CB C 20.18 0.05 1 77 . 7 ALA HB H 1.50 0.02 1 78 . 7 ALA C C 178.69 0.05 1 79 . 8 ARG N N 122.55 0.05 1 80 . 8 ARG H H 8.97 0.02 1 81 . 8 ARG CA C 58.78 0.05 1 82 . 8 ARG HA H 4.00 0.02 1 83 . 8 ARG CB C 29.45 0.05 1 84 . 8 ARG HB2 H 1.82 0.02 1 85 . 8 ARG HB3 H 1.82 0.02 1 86 . 8 ARG CG C 27.15 0.05 1 87 . 8 ARG HG2 H 1.70 0.02 1 88 . 8 ARG HG3 H 1.70 0.02 1 89 . 8 ARG CD C 43.27 0.05 1 90 . 8 ARG HD2 H 3.18 0.02 1 91 . 8 ARG HD3 H 3.18 0.02 1 92 . 8 ARG NE N 84.47 0.05 1 93 . 8 ARG HE H 7.18 0.02 1 94 . 8 ARG C C 177.64 0.05 1 95 . 9 SER N N 107.37 0.05 1 96 . 9 SER H H 7.50 0.02 1 97 . 9 SER CA C 58.19 0.05 1 98 . 9 SER HA H 4.28 0.02 1 99 . 9 SER CB C 63.07 0.05 1 100 . 9 SER HB2 H 3.91 0.02 1 101 . 9 SER HB3 H 3.75 0.02 1 102 . 9 SER C C 174.71 0.05 1 103 . 10 GLY N N 109.70 0.05 1 104 . 10 GLY H H 7.44 0.02 1 105 . 10 GLY CA C 44.17 0.05 1 106 . 10 GLY HA2 H 4.53 0.02 1 107 . 10 GLY HA3 H 3.66 0.02 1 108 . 10 GLY C C 171.74 0.05 1 109 . 11 LYS N N 121.06 0.05 1 110 . 11 LYS H H 8.01 0.02 1 111 . 11 LYS CA C 57.35 0.05 1 112 . 11 LYS HA H 4.02 0.02 1 113 . 11 LYS CB C 33.80 0.05 1 114 . 11 LYS HB2 H 1.59 0.02 1 115 . 11 LYS HB3 H 1.35 0.02 1 116 . 11 LYS CG C 24.54 0.05 1 117 . 11 LYS HG2 H 1.12 0.02 1 118 . 11 LYS HG3 H 0.42 0.02 1 119 . 11 LYS CD C 29.70 0.05 1 120 . 11 LYS HD2 H 1.32 0.02 1 121 . 11 LYS HD3 H 1.20 0.02 1 122 . 11 LYS CE C 41.84 0.05 1 123 . 11 LYS HE2 H 2.36 0.02 1 124 . 11 LYS HE3 H 2.26 0.02 1 125 . 11 LYS C C 176.19 0.05 1 126 . 12 TYR N N 122.94 0.05 1 127 . 12 TYR H H 9.93 0.02 1 128 . 12 TYR CA C 54.58 0.05 1 129 . 12 TYR HA H 3.96 0.02 1 130 . 12 TYR CB C 32.54 0.05 1 131 . 12 TYR HB2 H 3.25 0.02 1 132 . 12 TYR HB3 H 3.08 0.02 1 133 . 12 TYR HD1 H 7.24 0.02 1 134 . 12 TYR HD2 H 7.24 0.02 1 135 . 12 TYR CE1 C 119.40 0.05 1 136 . 12 TYR HE1 H 7.36 0.02 1 137 . 12 TYR CE2 C 119.40 0.05 1 138 . 12 TYR HE2 H 7.36 0.02 1 139 . 12 TYR C C 174.20 0.05 1 140 . 13 LYS N N 114.49 0.05 1 141 . 13 LYS H H 8.54 0.02 1 142 . 13 LYS CA C 54.98 0.05 1 143 . 13 LYS HA H 4.58 0.02 1 144 . 13 LYS CB C 35.06 0.05 1 145 . 13 LYS HB2 H 1.89 0.02 1 146 . 13 LYS HB3 H 1.48 0.02 1 147 . 13 LYS CG C 23.98 0.05 1 148 . 13 LYS HG2 H 1.04 0.02 1 149 . 13 LYS HG3 H 1.04 0.02 1 150 . 13 LYS CD C 28.33 0.05 1 151 . 13 LYS HD2 H 1.49 0.02 1 152 . 13 LYS HD3 H 1.30 0.02 1 153 . 13 LYS CE C 42.55 0.05 1 154 . 13 LYS HE2 H 2.84 0.02 1 155 . 13 LYS HE3 H 2.84 0.02 1 156 . 13 LYS C C 177.24 0.05 1 157 . 14 LEU N N 123.03 0.05 1 158 . 14 LEU H H 9.39 0.02 1 159 . 14 LEU CA C 54.95 0.05 1 160 . 14 LEU HA H 5.14 0.02 1 161 . 14 LEU CB C 43.65 0.05 1 162 . 14 LEU HB2 H 2.60 0.02 1 163 . 14 LEU HB3 H 1.40 0.02 1 164 . 14 LEU CG C 26.17 0.05 1 165 . 14 LEU HG H 1.98 0.02 1 166 . 14 LEU CD1 C 24.55 0.05 1 167 . 14 LEU HD1 H 0.79 0.02 1 168 . 14 LEU CD2 C 27.13 0.05 1 169 . 14 LEU HD2 H 0.81 0.02 1 170 . 14 LEU C C 178.60 0.05 1 171 . 15 THR N N 116.42 0.05 1 172 . 15 THR H H 8.87 0.02 1 173 . 15 THR CA C 61.87 0.05 1 174 . 15 THR HA H 5.49 0.02 1 175 . 15 THR CB C 71.06 0.05 1 176 . 15 THR HB H 4.84 0.02 1 177 . 15 THR CG2 C 22.06 0.05 1 178 . 15 THR HG2 H 1.36 0.02 1 179 . 15 THR C C 174.95 0.05 1 180 . 16 TYR N N 120.62 0.05 1 181 . 16 TYR H H 7.50 0.02 1 182 . 16 TYR CA C 61.63 0.05 1 183 . 16 TYR HA H 2.39 0.02 1 184 . 16 TYR CB C 36.99 0.05 1 185 . 16 TYR HB2 H 2.23 0.02 1 186 . 16 TYR HB3 H 0.89 0.02 1 187 . 16 TYR CD1 C 132.62 0.05 1 188 . 16 TYR HD1 H 6.75 0.02 1 189 . 16 TYR CD2 C 132.62 0.05 1 190 . 16 TYR HD2 H 6.75 0.02 1 191 . 16 TYR CE1 C 117.98 0.05 1 192 . 16 TYR HE1 H 6.79 0.02 1 193 . 16 TYR CE2 C 117.98 0.05 1 194 . 16 TYR HE2 H 6.79 0.02 1 195 . 16 TYR C C 176.16 0.05 1 196 . 17 ALA N N 118.15 0.05 1 197 . 17 ALA H H 8.57 0.02 1 198 . 17 ALA CA C 54.81 0.05 1 199 . 17 ALA HA H 3.52 0.02 1 200 . 17 ALA CB C 18.24 0.05 1 201 . 17 ALA HB H 1.28 0.02 1 202 . 17 ALA C C 181.78 0.05 1 203 . 18 GLU N N 117.77 0.05 1 204 . 18 GLU H H 7.36 0.02 1 205 . 18 GLU CA C 58.52 0.05 1 206 . 18 GLU HA H 3.88 0.02 1 207 . 18 GLU CB C 31.09 0.05 1 208 . 18 GLU HB2 H 2.17 0.02 1 209 . 18 GLU HB3 H 1.97 0.02 1 210 . 18 GLU CG C 37.34 0.05 1 211 . 18 GLU HG2 H 2.26 0.02 1 212 . 18 GLU HG3 H 2.18 0.02 1 213 . 18 GLU C C 178.79 0.05 1 214 . 19 ALA N N 124.54 0.05 1 215 . 19 ALA H H 8.74 0.02 1 216 . 19 ALA CA C 54.98 0.05 1 217 . 19 ALA HA H 3.87 0.02 1 218 . 19 ALA CB C 19.79 0.05 1 219 . 19 ALA HB H 1.52 0.02 1 220 . 19 ALA C C 177.50 0.05 1 221 . 20 LYS N N 117.83 0.05 1 222 . 20 LYS H H 8.20 0.02 1 223 . 20 LYS CA C 60.09 0.05 1 224 . 20 LYS HA H 3.44 0.02 1 225 . 20 LYS CB C 33.51 0.05 1 226 . 20 LYS HB2 H 1.46 0.02 1 227 . 20 LYS HB3 H 1.09 0.02 1 228 . 20 LYS CG C 24.59 0.05 1 229 . 20 LYS HG2 H 1.28 0.02 1 230 . 20 LYS HG3 H 1.14 0.02 1 231 . 20 LYS CD C 30.06 0.05 1 232 . 20 LYS HD2 H 1.47 0.02 1 233 . 20 LYS HD3 H 1.47 0.02 1 234 . 20 LYS CE C 42.28 0.05 1 235 . 20 LYS HE2 H 3.03 0.02 1 236 . 20 LYS HE3 H 2.90 0.02 1 237 . 20 LYS C C 178.20 0.05 1 238 . 21 ALA N N 117.63 0.05 1 239 . 21 ALA H H 7.42 0.02 1 240 . 21 ALA CA C 55.00 0.05 1 241 . 21 ALA HA H 4.05 0.02 1 242 . 21 ALA CB C 18.34 0.05 1 243 . 21 ALA HB H 1.38 0.02 1 244 . 21 ALA C C 180.82 0.05 1 245 . 22 VAL N N 120.41 0.05 1 246 . 22 VAL H H 8.28 0.02 1 247 . 22 VAL CA C 66.31 0.05 1 248 . 22 VAL HA H 3.89 0.02 1 249 . 22 VAL CB C 31.09 0.05 1 250 . 22 VAL HB H 2.11 0.02 1 251 . 22 VAL CG1 C 23.49 0.05 1 252 . 22 VAL HG1 H 1.01 0.02 1 253 . 22 VAL CG2 C 21.05 0.05 1 254 . 22 VAL HG2 H 0.86 0.02 1 255 . 22 VAL C C 178.15 0.05 1 256 . 23 CYS N N 116.48 0.05 1 257 . 23 CYS H H 7.82 0.02 1 258 . 23 CYS CA C 55.39 0.05 1 259 . 23 CYS HA H 4.35 0.02 1 260 . 23 CYS CB C 33.70 0.05 1 261 . 23 CYS HB2 H 2.59 0.02 1 262 . 23 CYS HB3 H 2.37 0.02 1 263 . 23 CYS C C 178.95 0.05 1 264 . 24 GLU N N 120.33 0.05 1 265 . 24 GLU H H 8.17 0.02 1 266 . 24 GLU CA C 58.53 0.05 1 267 . 24 GLU HA H 4.30 0.02 1 268 . 24 GLU CB C 28.97 0.05 1 269 . 24 GLU HB2 H 2.02 0.02 1 270 . 24 GLU HB3 H 1.94 0.02 1 271 . 24 GLU CG C 37.16 0.05 1 272 . 24 GLU HG2 H 2.60 0.02 1 273 . 24 GLU HG3 H 2.42 0.02 1 274 . 24 GLU C C 180.85 0.05 1 275 . 25 PHE N N 125.02 0.05 1 276 . 25 PHE H H 9.01 0.02 1 277 . 25 PHE CA C 60.90 0.05 1 278 . 25 PHE HA H 4.29 0.02 1 279 . 25 PHE CB C 39.02 0.05 1 280 . 25 PHE HB2 H 3.44 0.02 1 281 . 25 PHE HB3 H 3.22 0.02 1 282 . 25 PHE HD1 H 7.29 0.02 1 283 . 25 PHE HD2 H 7.29 0.02 1 284 . 25 PHE HE1 H 7.35 0.02 1 285 . 25 PHE HE2 H 7.35 0.02 1 286 . 25 PHE C C 177.80 0.05 1 287 . 26 GLU N N 114.59 0.05 1 288 . 26 GLU H H 7.40 0.02 1 289 . 26 GLU CA C 56.40 0.05 1 290 . 26 GLU HA H 4.11 0.02 1 291 . 26 GLU CB C 29.55 0.05 1 292 . 26 GLU HB2 H 2.35 0.02 1 293 . 26 GLU HB3 H 1.85 0.02 1 294 . 26 GLU CG C 37.23 0.05 1 295 . 26 GLU HG2 H 2.84 0.02 1 296 . 26 GLU HG3 H 2.28 0.02 1 297 . 26 GLU C C 175.86 0.05 1 298 . 27 GLY N N 106.50 0.05 1 299 . 27 GLY H H 7.74 0.02 1 300 . 27 GLY CA C 45.53 0.05 1 301 . 27 GLY HA2 H 4.24 0.02 1 302 . 27 GLY HA3 H 3.71 0.02 1 303 . 27 GLY C C 174.27 0.05 1 304 . 28 GLY N N 109.70 0.05 1 305 . 28 GLY H H 7.79 0.02 1 306 . 28 GLY CA C 43.89 0.05 1 307 . 28 GLY HA2 H 4.49 0.02 1 308 . 28 GLY HA3 H 3.95 0.02 1 309 . 28 GLY C C 172.07 0.05 1 310 . 29 HIS N N 116.56 0.05 1 311 . 29 HIS H H 8.42 0.02 1 312 . 29 HIS CA C 54.47 0.05 1 313 . 29 HIS HA H 4.88 0.02 1 314 . 29 HIS NE2 N 182.35 0.05 1 315 . 29 HIS CD2 C 121.37 0.05 1 316 . 29 HIS HD2 H 7.25 0.02 1 317 . 29 HIS ND1 N 189.33 0.05 1 318 . 29 HIS CE1 C 137.42 0.05 1 319 . 29 HIS HE1 H 8.28 0.02 1 320 . 29 HIS CB C 33.80 0.05 1 321 . 29 HIS HB2 H 3.58 0.02 1 322 . 29 HIS HB3 H 2.95 0.02 1 323 . 29 HIS C C 174.59 0.05 1 324 . 30 LEU N N 123.90 0.05 1 325 . 30 LEU H H 9.34 0.02 1 326 . 30 LEU CA C 56.84 0.05 1 327 . 30 LEU HA H 4.90 0.02 1 328 . 30 LEU CB C 42.78 0.05 1 329 . 30 LEU HB2 H 1.70 0.02 1 330 . 30 LEU HB3 H 1.42 0.02 1 331 . 30 LEU CG C 28.06 0.05 1 332 . 30 LEU HG H 1.50 0.02 1 333 . 30 LEU CD1 C 27.36 0.05 1 334 . 30 LEU HD1 H 0.79 0.02 1 335 . 30 LEU CD2 C 24.18 0.05 1 336 . 30 LEU HD2 H 0.87 0.02 1 337 . 30 LEU C C 178.32 0.05 1 338 . 31 ALA N N 126.73 0.05 1 339 . 31 ALA H H 9.35 0.02 1 340 . 31 ALA CA C 52.01 0.05 1 341 . 31 ALA HA H 4.40 0.02 1 342 . 31 ALA CB C 19.69 0.05 1 343 . 31 ALA HB H 1.23 0.02 1 344 . 31 ALA C C 177.24 0.05 1 345 . 32 THR N N 111.23 0.05 1 346 . 32 THR H H 8.58 0.02 1 347 . 32 THR CA C 59.98 0.05 1 348 . 32 THR HA H 4.54 0.02 1 349 . 32 THR CB C 71.29 0.05 1 350 . 32 THR HB H 4.71 0.02 1 351 . 32 THR HG1 H 5.48 0.02 1 352 . 32 THR CG2 C 22.06 0.05 1 353 . 32 THR HG2 H 1.14 0.02 1 354 . 32 THR C C 175.20 0.05 1 355 . 33 TYR N N 122.01 0.05 1 356 . 33 TYR H H 8.70 0.02 1 357 . 33 TYR CA C 62.44 0.05 1 358 . 33 TYR HA H 3.86 0.02 1 359 . 33 TYR CB C 38.82 0.05 1 360 . 33 TYR HB2 H 3.02 0.02 1 361 . 33 TYR HB3 H 2.75 0.02 1 362 . 33 TYR CD1 C 132.50 0.05 1 363 . 33 TYR HD1 H 6.72 0.02 1 364 . 33 TYR CD2 C 132.50 0.05 1 365 . 33 TYR HD2 H 6.72 0.02 1 366 . 33 TYR CE1 C 118.11 0.05 1 367 . 33 TYR HE1 H 6.58 0.02 1 368 . 33 TYR CE2 C 118.11 0.05 1 369 . 33 TYR HE2 H 6.58 0.02 1 370 . 33 TYR C C 176.61 0.05 1 371 . 34 LYS N N 116.40 0.05 1 372 . 34 LYS H H 8.26 0.02 1 373 . 34 LYS CA C 59.93 0.05 1 374 . 34 LYS HA H 3.91 0.02 1 375 . 34 LYS CB C 32.82 0.05 1 376 . 34 LYS HB2 H 1.75 0.02 1 377 . 34 LYS HB3 H 1.67 0.02 1 378 . 34 LYS CG C 25.90 0.05 1 379 . 34 LYS HG2 H 1.59 0.02 1 380 . 34 LYS HG3 H 1.41 0.02 1 381 . 34 LYS CD C 29.46 0.05 1 382 . 34 LYS HD2 H 1.67 0.02 1 383 . 34 LYS HD3 H 1.67 0.02 1 384 . 34 LYS CE C 42.11 0.05 1 385 . 34 LYS HE2 H 2.95 0.02 1 386 . 34 LYS HE3 H 2.95 0.02 1 387 . 34 LYS C C 180.36 0.05 1 388 . 35 GLN N N 119.28 0.05 1 389 . 35 GLN H H 7.77 0.02 1 390 . 35 GLN CA C 58.53 0.05 1 391 . 35 GLN HA H 3.84 0.02 1 392 . 35 GLN CB C 26.95 0.05 1 393 . 35 GLN HB2 H 2.21 0.02 1 394 . 35 GLN HB3 H 1.42 0.02 1 395 . 35 GLN CG C 33.65 0.05 1 396 . 35 GLN HG2 H 2.02 0.02 1 397 . 35 GLN HG3 H 1.89 0.02 1 398 . 35 GLN CD C 178.45 0.05 1 399 . 35 GLN NE2 N 107.03 0.05 1 400 . 35 GLN HE21 H 6.70 0.02 1 401 . 35 GLN HE22 H 5.24 0.02 1 402 . 35 GLN C C 179.18 0.05 1 403 . 36 LEU N N 122.98 0.05 1 404 . 36 LEU H H 8.49 0.02 1 405 . 36 LEU CA C 58.29 0.05 1 406 . 36 LEU HA H 3.86 0.02 1 407 . 36 LEU CB C 41.91 0.05 1 408 . 36 LEU HB2 H 1.69 0.02 1 409 . 36 LEU HB3 H 1.14 0.02 1 410 . 36 LEU CG C 27.22 0.05 1 411 . 36 LEU HG H 1.20 0.02 1 412 . 36 LEU CD1 C 25.79 0.05 1 413 . 36 LEU HD1 H 0.29 0.02 1 414 . 36 LEU CD2 C 25.04 0.05 1 415 . 36 LEU HD2 H 0.57 0.02 1 416 . 36 LEU C C 178.04 0.05 1 417 . 37 GLU N N 120.53 0.05 1 418 . 37 GLU H H 8.53 0.02 1 419 . 37 GLU CA C 58.07 0.05 1 420 . 37 GLU HA H 4.24 0.02 1 421 . 37 GLU CB C 28.29 0.05 1 422 . 37 GLU HB2 H 1.80 0.02 1 423 . 37 GLU HB3 H 1.64 0.02 1 424 . 37 GLU CG C 34.81 0.05 1 425 . 37 GLU HG2 H 2.29 0.02 1 426 . 37 GLU HG3 H 2.00 0.02 1 427 . 37 GLU C C 178.25 0.05 1 428 . 38 ALA N N 121.26 0.05 1 429 . 38 ALA H H 7.83 0.02 1 430 . 38 ALA CA C 54.98 0.05 1 431 . 38 ALA HA H 4.01 0.02 1 432 . 38 ALA CB C 18.05 0.05 1 433 . 38 ALA HB H 1.41 0.02 1 434 . 38 ALA C C 180.68 0.05 1 435 . 39 ALA N N 120.15 0.05 1 436 . 39 ALA H H 7.60 0.02 1 437 . 39 ALA CA C 54.15 0.05 1 438 . 39 ALA HA H 4.15 0.02 1 439 . 39 ALA CB C 18.05 0.05 1 440 . 39 ALA HB H 1.31 0.02 1 441 . 39 ALA C C 180.40 0.05 1 442 . 40 ARG N N 124.53 0.05 1 443 . 40 ARG H H 8.87 0.02 1 444 . 40 ARG CA C 58.72 0.05 1 445 . 40 ARG HA H 4.60 0.02 1 446 . 40 ARG CB C 30.80 0.05 1 447 . 40 ARG HB2 H 2.09 0.02 1 448 . 40 ARG HB3 H 1.69 0.02 1 449 . 40 ARG CG C 26.78 0.05 1 450 . 40 ARG HG2 H 1.68 0.02 1 451 . 40 ARG HG3 H 1.42 0.02 1 452 . 40 ARG CD C 42.46 0.05 1 453 . 40 ARG HD2 H 3.44 0.02 1 454 . 40 ARG HD3 H 2.43 0.02 1 455 . 40 ARG NE N 83.16 0.05 1 456 . 40 ARG HE H 9.33 0.02 1 457 . 40 ARG C C 180.71 0.05 1 458 . 41 LYS N N 117.66 0.05 1 459 . 41 LYS H H 8.25 0.02 1 460 . 41 LYS CA C 59.49 0.05 1 461 . 41 LYS HA H 3.94 0.02 1 462 . 41 LYS CB C 32.83 0.05 1 463 . 41 LYS HB2 H 1.95 0.02 1 464 . 41 LYS HB3 H 1.88 0.02 1 465 . 41 LYS CG C 25.96 0.05 1 466 . 41 LYS HG2 H 1.73 0.02 1 467 . 41 LYS HG3 H 1.40 0.02 1 468 . 41 LYS CD C 29.37 0.05 1 469 . 41 LYS HD2 H 1.68 0.02 1 470 . 41 LYS HD3 H 1.68 0.02 1 471 . 41 LYS CE C 42.18 0.05 1 472 . 41 LYS HE2 H 2.99 0.02 1 473 . 41 LYS HE3 H 2.99 0.02 1 474 . 41 LYS C C 178.32 0.05 1 475 . 42 ILE N N 110.90 0.05 1 476 . 42 ILE H H 7.32 0.02 1 477 . 42 ILE CA C 60.84 0.05 1 478 . 42 ILE HA H 4.59 0.02 1 479 . 42 ILE CB C 37.95 0.05 1 480 . 42 ILE HB H 2.29 0.02 1 481 . 42 ILE CG2 C 18.67 0.05 1 482 . 42 ILE HG2 H 0.97 0.02 1 483 . 42 ILE CG1 C 27.29 0.05 1 484 . 42 ILE HG12 H 1.58 0.02 1 485 . 42 ILE HG13 H 1.41 0.02 1 486 . 42 ILE CD1 C 14.42 0.05 1 487 . 42 ILE HD1 H 0.94 0.02 1 488 . 42 ILE C C 176.73 0.05 1 489 . 43 GLY N N 108.28 0.05 1 490 . 43 GLY H H 7.84 0.02 1 491 . 43 GLY CA C 45.73 0.05 1 492 . 43 GLY HA2 H 4.59 0.02 1 493 . 43 GLY HA3 H 3.54 0.02 1 494 . 43 GLY C C 174.10 0.05 1 495 . 44 PHE N N 125.83 0.05 1 496 . 44 PHE H H 8.08 0.02 1 497 . 44 PHE CA C 59.33 0.05 1 498 . 44 PHE HA H 4.49 0.02 1 499 . 44 PHE CB C 40.18 0.05 1 500 . 44 PHE HB2 H 2.97 0.02 1 501 . 44 PHE HB3 H 2.41 0.02 1 502 . 44 PHE CD1 C 131.62 0.05 1 503 . 44 PHE HD1 H 7.12 0.02 1 504 . 44 PHE CD2 C 131.62 0.05 1 505 . 44 PHE HD2 H 7.12 0.02 1 506 . 44 PHE HE1 H 7.39 0.02 1 507 . 44 PHE HE2 H 7.39 0.02 1 508 . 44 PHE HZ H 7.23 0.02 1 509 . 44 PHE C C 171.20 0.05 1 510 . 45 HIS N N 127.03 0.05 1 511 . 45 HIS H H 7.28 0.02 1 512 . 45 HIS CA C 55.35 0.05 1 513 . 45 HIS HA H 4.65 0.02 1 514 . 45 HIS NE2 N 167.14 0.05 1 515 . 45 HIS HD2 H 6.79 0.02 1 516 . 45 HIS ND1 N 246.94 0.05 1 517 . 45 HIS CE1 C 139.16 0.05 1 518 . 45 HIS HE1 H 8.18 0.02 1 519 . 45 HIS CB C 34.67 0.05 1 520 . 45 HIS HB2 H 2.96 0.02 1 521 . 45 HIS HB3 H 2.68 0.02 1 522 . 45 HIS C C 175.85 0.05 1 523 . 46 VAL N N 126.35 0.05 1 524 . 46 VAL H H 8.06 0.02 1 525 . 46 VAL CA C 61.65 0.05 1 526 . 46 VAL HA H 3.69 0.02 1 527 . 46 VAL CB C 35.34 0.05 1 528 . 46 VAL HB H 2.21 0.02 1 529 . 46 VAL CG1 C 22.32 0.05 1 530 . 46 VAL HG1 H 0.29 0.02 1 531 . 46 VAL CG2 C 21.80 0.05 1 532 . 46 VAL HG2 H 0.27 0.02 1 533 . 46 VAL C C 174.20 0.05 1 534 . 47 CYS N N 124.40 0.05 1 535 . 47 CYS H H 8.41 0.02 1 536 . 47 CYS CA C 54.54 0.05 1 537 . 47 CYS HA H 4.29 0.02 1 538 . 47 CYS CB C 42.11 0.05 1 539 . 47 CYS HB2 H 3.29 0.02 1 540 . 47 CYS HB3 H 2.57 0.02 1 541 . 47 CYS C C 173.52 0.05 1 542 . 48 ALA N N 121.88 0.05 1 543 . 48 ALA H H 6.54 0.02 1 544 . 48 ALA CA C 51.65 0.05 1 545 . 48 ALA HA H 4.31 0.02 1 546 . 48 ALA CB C 20.18 0.05 1 547 . 48 ALA HB H 1.11 0.02 1 548 . 48 ALA C C 174.27 0.05 1 549 . 49 ALA N N 130.21 0.05 1 550 . 49 ALA H H 8.50 0.02 1 551 . 49 ALA CA C 52.92 0.05 1 552 . 49 ALA HA H 4.04 0.02 1 553 . 49 ALA CB C 18.82 0.05 1 554 . 49 ALA HB H 0.67 0.02 1 555 . 49 ALA C C 176.02 0.05 1 556 . 50 GLY N N 106.70 0.05 1 557 . 50 GLY H H 8.73 0.02 1 558 . 50 GLY CA C 43.81 0.05 1 559 . 50 GLY HA2 H 4.49 0.02 1 560 . 50 GLY HA3 H 3.37 0.02 1 561 . 50 GLY C C 171.11 0.05 1 562 . 51 TRP N N 121.17 0.05 1 563 . 51 TRP H H 8.64 0.02 1 564 . 51 TRP CA C 58.82 0.05 1 565 . 51 TRP HA H 4.95 0.02 1 566 . 51 TRP CB C 32.25 0.05 1 567 . 51 TRP HB2 H 3.51 0.02 1 568 . 51 TRP HB3 H 3.04 0.02 1 569 . 51 TRP CD1 C 129.73 0.05 1 570 . 51 TRP HD1 H 7.38 0.02 1 571 . 51 TRP NE1 N 131.19 0.05 1 572 . 51 TRP HE1 H 10.34 0.02 1 573 . 51 TRP CE3 C 122.93 0.05 1 574 . 51 TRP HE3 H 7.68 0.02 1 575 . 51 TRP CZ2 C 116.32 0.05 1 576 . 51 TRP HZ2 H 8.17 0.02 1 577 . 51 TRP CZ3 C 121.67 0.05 1 578 . 51 TRP HZ3 H 7.30 0.02 1 579 . 51 TRP HH2 H 7.47 0.02 1 580 . 51 TRP C C 174.34 0.05 1 581 . 52 MET N N 118.52 0.05 1 582 . 52 MET H H 9.14 0.02 1 583 . 52 MET CA C 54.46 0.05 1 584 . 52 MET HA H 4.97 0.02 1 585 . 52 MET CB C 39.40 0.05 1 586 . 52 MET HB2 H 2.65 0.02 1 587 . 52 MET HB3 H 2.01 0.02 1 588 . 52 MET CG C 32.66 0.05 1 589 . 52 MET HG2 H 2.65 0.02 1 590 . 52 MET HG3 H 2.42 0.02 1 591 . 52 MET CE C 17.23 0.05 1 592 . 52 MET HE H 1.63 0.02 1 593 . 52 MET C C 174.97 0.05 1 594 . 53 ALA N N 120.39 0.05 1 595 . 53 ALA H H 8.62 0.02 1 596 . 53 ALA CA C 53.87 0.05 1 597 . 53 ALA HA H 4.18 0.02 1 598 . 53 ALA CB C 19.60 0.05 1 599 . 53 ALA HB H 1.32 0.02 1 600 . 53 ALA C C 178.39 0.05 1 601 . 54 LYS N N 112.32 0.05 1 602 . 54 LYS H H 8.83 0.02 1 603 . 54 LYS CA C 57.72 0.05 1 604 . 54 LYS HA H 3.80 0.02 1 605 . 54 LYS CB C 29.93 0.05 1 606 . 54 LYS HB2 H 2.29 0.02 1 607 . 54 LYS HB3 H 2.00 0.02 1 608 . 54 LYS CG C 25.72 0.05 1 609 . 54 LYS HG2 H 1.46 0.02 1 610 . 54 LYS HG3 H 1.40 0.02 1 611 . 54 LYS CD C 29.12 0.05 1 612 . 54 LYS HD2 H 1.69 0.02 1 613 . 54 LYS HD3 H 1.69 0.02 1 614 . 54 LYS CE C 42.37 0.05 1 615 . 54 LYS HE2 H 3.00 0.02 1 616 . 54 LYS HE3 H 3.00 0.02 1 617 . 54 LYS C C 175.93 0.05 1 618 . 55 GLY N N 104.19 0.05 1 619 . 55 GLY H H 8.28 0.02 1 620 . 55 GLY CA C 45.99 0.05 1 621 . 55 GLY HA2 H 3.96 0.02 1 622 . 55 GLY HA3 H 3.72 0.02 1 623 . 55 GLY C C 173.85 0.05 1 624 . 56 ARG N N 122.17 0.05 1 625 . 56 ARG H H 6.85 0.02 1 626 . 56 ARG CA C 55.02 0.05 1 627 . 56 ARG HA H 4.84 0.02 1 628 . 56 ARG CB C 32.24 0.05 1 629 . 56 ARG HB2 H 1.74 0.02 1 630 . 56 ARG HB3 H 1.63 0.02 1 631 . 56 ARG CG C 28.21 0.05 1 632 . 56 ARG HG2 H 1.56 0.02 1 633 . 56 ARG HG3 H 1.46 0.02 1 634 . 56 ARG CD C 43.68 0.05 1 635 . 56 ARG HD2 H 3.20 0.02 1 636 . 56 ARG HD3 H 3.05 0.02 1 637 . 56 ARG NE N 82.59 0.05 1 638 . 56 ARG HE H 7.85 0.02 1 639 . 56 ARG C C 174.03 0.05 1 640 . 57 VAL N N 122.43 0.05 1 641 . 57 VAL H H 7.15 0.02 1 642 . 57 VAL CA C 60.05 0.05 1 643 . 57 VAL HA H 4.72 0.02 1 644 . 57 VAL CB C 35.54 0.05 1 645 . 57 VAL HB H 0.78 0.02 1 646 . 57 VAL CG1 C 24.03 0.05 1 647 . 57 VAL HG1 H -0.40 0.02 1 648 . 57 VAL CG2 C 20.84 0.05 1 649 . 57 VAL HG2 H -0.97 0.02 1 650 . 57 VAL C C 174.38 0.05 1 651 . 58 GLY N N 112.58 0.05 1 652 . 58 GLY H H 8.08 0.02 1 653 . 58 GLY CA C 46.22 0.05 1 654 . 58 GLY HA2 H 4.00 0.02 1 655 . 58 GLY HA3 H 3.92 0.02 1 656 . 58 GLY C C 171.60 0.05 1 657 . 59 TYR N N 111.82 0.05 1 658 . 59 TYR H H 7.88 0.02 1 659 . 59 TYR CA C 55.37 0.05 1 660 . 59 TYR HA H 4.69 0.02 1 661 . 59 TYR CB C 36.34 0.05 1 662 . 59 TYR HB2 H 3.46 0.02 1 663 . 59 TYR HB3 H 3.13 0.02 1 664 . 59 TYR CD1 C 133.78 0.05 1 665 . 59 TYR HD1 H 6.54 0.02 1 666 . 59 TYR CD2 C 133.78 0.05 1 667 . 59 TYR HD2 H 6.54 0.02 1 668 . 59 TYR CE1 C 117.65 0.05 1 669 . 59 TYR HE1 H 6.45 0.02 1 670 . 59 TYR CE2 C 117.65 0.05 1 671 . 59 TYR HE2 H 6.45 0.02 1 672 . 60 PRO CA C 61.85 0.05 1 673 . 60 PRO HA H 4.46 0.02 1 674 . 60 PRO CB C 33.46 0.05 1 675 . 60 PRO HB2 H 1.94 0.02 1 676 . 60 PRO HB3 H 1.78 0.02 1 677 . 61 ILE CA C 61.15 0.05 1 678 . 61 ILE HA H 4.20 0.02 1 679 . 61 ILE CB C 39.58 0.05 1 680 . 61 ILE HB H 2.04 0.02 1 681 . 61 ILE CG2 C 18.67 0.05 1 682 . 61 ILE HG2 H 0.86 0.02 1 683 . 61 ILE CG1 C 27.31 0.05 1 684 . 61 ILE HG12 H 1.30 0.02 1 685 . 61 ILE HG13 H 1.20 0.02 1 686 . 61 ILE CD1 C 12.54 0.05 1 687 . 61 ILE HD1 H 0.62 0.02 1 688 . 62 VAL H H 11.34 0.02 1 689 . 62 VAL CA C 64.60 0.05 1 690 . 62 VAL HA H 4.01 0.02 1 691 . 62 VAL CB C 33.91 0.05 1 692 . 62 VAL HB H 2.06 0.02 1 693 . 62 VAL CG1 C 22.97 0.05 1 694 . 62 VAL HG1 H 0.95 0.02 1 695 . 62 VAL CG2 C 21.44 0.05 1 696 . 62 VAL HG2 H 0.93 0.02 1 697 . 63 LYS N N 120.54 0.05 1 698 . 63 LYS H H 7.27 0.02 1 699 . 63 LYS CA C 52.75 0.05 1 700 . 63 LYS HA H 4.77 0.02 1 701 . 63 LYS CB C 33.90 0.05 1 702 . 63 LYS HB2 H 1.57 0.02 1 703 . 63 LYS HB3 H 1.43 0.02 1 704 . 63 LYS CG C 24.65 0.05 1 705 . 63 LYS HG2 H 1.20 0.02 1 706 . 63 LYS HG3 H 1.20 0.02 1 707 . 63 LYS HD2 H 1.46 0.02 1 708 . 63 LYS HD3 H 1.46 0.02 1 709 . 63 LYS HE2 H 2.94 0.02 1 710 . 63 LYS HE3 H 2.67 0.02 1 711 . 64 PRO CA C 62.39 0.05 1 712 . 64 PRO HA H 4.52 0.02 1 713 . 64 PRO CD C 50.67 0.05 1 714 . 64 PRO HD2 H 3.68 0.02 1 715 . 64 PRO HD3 H 3.65 0.02 1 716 . 64 PRO CB C 32.74 0.05 1 717 . 64 PRO HB2 H 2.01 0.02 1 718 . 64 PRO HB3 H 1.76 0.02 1 719 . 64 PRO CG C 26.92 0.05 1 720 . 64 PRO HG2 H 2.01 0.02 1 721 . 64 PRO HG3 H 1.95 0.02 1 722 . 65 GLY N N 107.86 0.05 1 723 . 65 GLY H H 8.37 0.02 1 724 . 65 GLY CA C 45.64 0.05 1 725 . 65 GLY HA2 H 4.07 0.02 1 726 . 65 GLY HA3 H 3.50 0.02 1 727 . 66 PRO CA C 64.50 0.05 1 728 . 66 PRO HA H 4.16 0.02 1 729 . 66 PRO CD C 49.80 0.05 1 730 . 66 PRO HD2 H 3.61 0.02 1 731 . 66 PRO HD3 H 3.55 0.02 1 732 . 66 PRO CB C 32.16 0.05 1 733 . 66 PRO HB2 H 2.26 0.02 1 734 . 66 PRO HB3 H 1.88 0.02 1 735 . 66 PRO CG C 27.30 0.05 1 736 . 66 PRO HG2 H 2.00 0.02 1 737 . 66 PRO HG3 H 2.00 0.02 1 738 . 66 PRO C C 177.92 0.05 1 739 . 67 ASN N N 115.08 0.05 1 740 . 67 ASN H H 8.56 0.02 1 741 . 67 ASN CA C 54.05 0.05 1 742 . 67 ASN HA H 4.60 0.02 1 743 . 67 ASN CB C 38.53 0.05 1 744 . 67 ASN HB2 H 2.89 0.02 1 745 . 67 ASN HB3 H 2.80 0.02 1 746 . 67 ASN CG C 175.68 0.05 1 747 . 67 ASN ND2 N 113.42 0.05 1 748 . 67 ASN HD21 H 7.39 0.02 1 749 . 67 ASN HD22 H 6.92 0.02 1 750 . 67 ASN C C 174.85 0.05 1 751 . 68 CYS N N 118.81 0.05 1 752 . 68 CYS H H 7.60 0.02 1 753 . 68 CYS CA C 56.29 0.05 1 754 . 68 CYS HA H 4.77 0.02 1 755 . 68 CYS CB C 45.08 0.05 1 756 . 68 CYS HB2 H 3.29 0.02 1 757 . 68 CYS HB3 H 2.90 0.02 1 758 . 68 CYS C C 175.83 0.05 1 759 . 69 GLY N N 111.63 0.05 1 760 . 69 GLY H H 8.53 0.02 1 761 . 69 GLY CA C 46.07 0.05 1 762 . 69 GLY HA2 H 4.07 0.02 1 763 . 69 GLY HA3 H 3.55 0.02 1 764 . 69 GLY C C 174.03 0.05 1 765 . 70 PHE N N 116.99 0.05 1 766 . 70 PHE H H 8.02 0.02 1 767 . 70 PHE CA C 58.48 0.05 1 768 . 70 PHE HA H 4.40 0.02 1 769 . 70 PHE CB C 37.95 0.05 1 770 . 70 PHE HB2 H 3.29 0.02 1 771 . 70 PHE HB3 H 3.00 0.02 1 772 . 70 PHE CD1 C 131.94 0.05 1 773 . 70 PHE HD1 H 7.24 0.02 1 774 . 70 PHE CD2 C 131.94 0.05 1 775 . 70 PHE HD2 H 7.24 0.02 1 776 . 70 PHE C C 175.91 0.05 1 777 . 71 GLY N N 107.97 0.05 1 778 . 71 GLY H H 8.23 0.02 1 779 . 71 GLY CA C 45.63 0.05 1 780 . 71 GLY HA2 H 4.12 0.02 1 781 . 71 GLY HA3 H 3.53 0.02 1 782 . 71 GLY C C 173.96 0.05 1 783 . 72 LYS N N 120.25 0.05 1 784 . 72 LYS H H 7.59 0.02 1 785 . 72 LYS CA C 55.41 0.05 1 786 . 72 LYS HA H 4.45 0.02 1 787 . 72 LYS CB C 34.19 0.05 1 788 . 72 LYS HB2 H 1.76 0.02 1 789 . 72 LYS HB3 H 1.76 0.02 1 790 . 72 LYS CG C 25.02 0.05 1 791 . 72 LYS HG2 H 1.41 0.02 1 792 . 72 LYS HG3 H 1.37 0.02 1 793 . 72 LYS CD C 28.95 0.05 1 794 . 72 LYS HD2 H 1.66 0.02 1 795 . 72 LYS HD3 H 1.66 0.02 1 796 . 72 LYS CE C 42.46 0.05 1 797 . 72 LYS HE2 H 2.97 0.02 1 798 . 72 LYS HE3 H 2.97 0.02 1 799 . 72 LYS C C 175.79 0.05 1 800 . 73 THR N N 110.26 0.05 1 801 . 73 THR H H 7.94 0.02 1 802 . 73 THR CA C 60.92 0.05 1 803 . 73 THR HA H 4.16 0.02 1 804 . 73 THR CB C 70.84 0.05 1 805 . 73 THR HB H 4.04 0.02 1 806 . 73 THR CG2 C 22.20 0.05 1 807 . 73 THR HG2 H 1.05 0.02 1 808 . 73 THR C C 173.66 0.05 1 809 . 74 GLY N N 108.81 0.05 1 810 . 74 GLY H H 8.00 0.02 1 811 . 74 GLY CA C 43.74 0.05 1 812 . 74 GLY HA2 H 4.42 0.02 1 813 . 74 GLY HA3 H 3.42 0.02 1 814 . 74 GLY C C 173.00 0.05 1 815 . 75 ILE N N 119.83 0.05 1 816 . 75 ILE H H 8.30 0.02 1 817 . 75 ILE CA C 60.16 0.05 1 818 . 75 ILE HA H 4.23 0.02 1 819 . 75 ILE CB C 36.89 0.05 1 820 . 75 ILE HB H 1.60 0.02 1 821 . 75 ILE CG2 C 16.74 0.05 1 822 . 75 ILE HG2 H 0.27 0.02 1 823 . 75 ILE CG1 C 28.13 0.05 1 824 . 75 ILE HG12 H 1.20 0.02 1 825 . 75 ILE HG13 H 0.65 0.02 1 826 . 75 ILE CD1 C 12.42 0.05 1 827 . 75 ILE HD1 H 0.13 0.02 1 828 . 75 ILE C C 176.51 0.05 1 829 . 76 ILE N N 133.32 0.05 1 830 . 76 ILE H H 8.67 0.02 1 831 . 76 ILE CA C 59.25 0.05 1 832 . 76 ILE HA H 3.69 0.02 1 833 . 76 ILE CB C 33.61 0.05 1 834 . 76 ILE HB H 0.50 0.02 1 835 . 76 ILE CG2 C 17.51 0.05 1 836 . 76 ILE HG2 H 0.54 0.02 1 837 . 76 ILE CG1 C 27.15 0.05 1 838 . 76 ILE HG12 H 0.96 0.02 1 839 . 76 ILE HG13 H 0.72 0.02 1 840 . 76 ILE CD1 C 9.38 0.05 1 841 . 76 ILE HD1 H 0.36 0.02 1 842 . 76 ILE C C 173.89 0.05 1 843 . 77 ASP N N 126.74 0.05 1 844 . 77 ASP H H 8.11 0.02 1 845 . 77 ASP CA C 53.16 0.05 1 846 . 77 ASP HA H 4.80 0.02 1 847 . 77 ASP CB C 44.04 0.05 1 848 . 77 ASP HB2 H 2.87 0.02 1 849 . 77 ASP HB3 H 2.48 0.02 1 850 . 77 ASP C C 176.80 0.05 1 851 . 78 TYR N N 126.57 0.05 1 852 . 78 TYR H H 9.41 0.02 1 853 . 78 TYR CA C 55.33 0.05 1 854 . 78 TYR HA H 4.68 0.02 1 855 . 78 TYR CB C 36.60 0.05 1 856 . 78 TYR HB2 H 3.00 0.02 1 857 . 78 TYR HB3 H 2.59 0.02 1 858 . 78 TYR HD1 H 6.94 0.02 1 859 . 78 TYR HD2 H 6.94 0.02 1 860 . 78 TYR HE1 H 6.61 0.02 1 861 . 78 TYR HE2 H 6.61 0.02 1 862 . 78 TYR C C 176.75 0.05 1 863 . 79 GLY N N 111.06 0.05 1 864 . 79 GLY H H 8.93 0.02 1 865 . 79 GLY CA C 44.53 0.05 1 866 . 79 GLY HA2 H 4.06 0.02 1 867 . 79 GLY HA3 H 3.71 0.02 1 868 . 79 GLY C C 172.42 0.05 1 869 . 80 ILE N N 117.59 0.05 1 870 . 80 ILE H H 8.21 0.02 1 871 . 80 ILE CA C 61.35 0.05 1 872 . 80 ILE HA H 3.93 0.02 1 873 . 80 ILE CB C 36.60 0.05 1 874 . 80 ILE HB H 1.77 0.02 1 875 . 80 ILE CG2 C 17.53 0.05 1 876 . 80 ILE HG2 H 0.82 0.02 1 877 . 80 ILE CG1 C 27.60 0.05 1 878 . 80 ILE HG12 H 1.51 0.02 1 879 . 80 ILE HG13 H 1.15 0.02 1 880 . 80 ILE CD1 C 11.80 0.05 1 881 . 80 ILE HD1 H 0.78 0.02 1 882 . 80 ILE C C 177.69 0.05 1 883 . 81 ARG N N 128.47 0.05 1 884 . 81 ARG H H 8.43 0.02 1 885 . 81 ARG CA C 52.92 0.05 1 886 . 81 ARG HA H 4.37 0.02 1 887 . 81 ARG CB C 30.10 0.05 1 888 . 81 ARG HB2 H 2.13 0.02 1 889 . 81 ARG HB3 H 2.13 0.02 1 890 . 81 ARG HG2 H 1.86 0.02 1 891 . 81 ARG HG3 H 1.51 0.02 1 892 . 81 ARG CD C 40.61 0.05 1 893 . 81 ARG HD2 H 2.72 0.02 1 894 . 81 ARG HD3 H 2.72 0.02 1 895 . 81 ARG NE N 84.42 0.05 1 896 . 81 ARG HE H 9.92 0.02 1 897 . 81 ARG C C 176.51 0.05 1 898 . 82 LEU N N 124.62 0.05 1 899 . 82 LEU H H 8.20 0.02 1 900 . 82 LEU CA C 56.90 0.05 1 901 . 82 LEU HA H 4.16 0.02 1 902 . 82 LEU CB C 42.30 0.05 1 903 . 82 LEU HB2 H 1.66 0.02 1 904 . 82 LEU HB3 H 1.57 0.02 1 905 . 82 LEU CG C 27.39 0.05 1 906 . 82 LEU HG H 1.69 0.02 1 907 . 82 LEU CD1 C 24.74 0.05 1 908 . 82 LEU HD1 H 0.91 0.02 1 909 . 82 LEU CD2 C 23.57 0.05 1 910 . 82 LEU HD2 H 0.82 0.02 1 911 . 82 LEU C C 177.69 0.05 1 912 . 83 ASN N N 115.82 0.05 1 913 . 83 ASN H H 8.65 0.02 1 914 . 83 ASN CA C 51.77 0.05 1 915 . 83 ASN HA H 4.90 0.02 1 916 . 83 ASN CB C 37.66 0.05 1 917 . 83 ASN HB2 H 3.27 0.02 1 918 . 83 ASN HB3 H 2.82 0.02 1 919 . 83 ASN CG C 178.15 0.05 1 920 . 83 ASN ND2 N 111.89 0.05 1 921 . 83 ASN HD21 H 7.93 0.02 1 922 . 83 ASN HD22 H 7.06 0.02 1 923 . 83 ASN C C 175.91 0.05 1 924 . 84 ARG N N 121.46 0.05 1 925 . 84 ARG H H 8.63 0.02 1 926 . 84 ARG CA C 56.72 0.05 1 927 . 84 ARG HA H 4.63 0.02 1 928 . 84 ARG CB C 29.45 0.05 1 929 . 84 ARG HB2 H 2.01 0.02 1 930 . 84 ARG HB3 H 1.85 0.02 1 931 . 84 ARG CG C 27.98 0.05 1 932 . 84 ARG HG2 H 1.82 0.02 1 933 . 84 ARG HG3 H 1.46 0.02 1 934 . 84 ARG CD C 43.00 0.05 1 935 . 84 ARG HD2 H 2.89 0.02 1 936 . 84 ARG HD3 H 2.68 0.02 1 937 . 84 ARG NE N 85.05 0.05 1 938 . 84 ARG HE H 7.40 0.02 1 939 . 84 ARG C C 177.38 0.05 1 940 . 85 SER N N 116.59 0.05 1 941 . 85 SER H H 8.61 0.02 1 942 . 85 SER CA C 58.94 0.05 1 943 . 85 SER HA H 4.64 0.02 1 944 . 85 SER CB C 63.17 0.05 1 945 . 85 SER HB2 H 4.07 0.02 1 946 . 85 SER HB3 H 4.07 0.02 1 947 . 85 SER C C 175.34 0.05 1 948 . 86 GLU N N 121.10 0.05 1 949 . 86 GLU H H 7.28 0.02 1 950 . 86 GLU CA C 57.44 0.05 1 951 . 86 GLU HA H 3.86 0.02 1 952 . 86 GLU CB C 31.48 0.05 1 953 . 86 GLU HB2 H 2.27 0.02 1 954 . 86 GLU HB3 H 1.75 0.02 1 955 . 86 GLU CG C 36.95 0.05 1 956 . 86 GLU HG2 H 2.80 0.02 1 957 . 86 GLU HG3 H 2.29 0.02 1 958 . 86 GLU C C 174.66 0.05 1 959 . 87 ARG N N 118.11 0.05 1 960 . 87 ARG H H 7.35 0.02 1 961 . 87 ARG CA C 54.54 0.05 1 962 . 87 ARG HA H 4.75 0.02 1 963 . 87 ARG CB C 31.77 0.05 1 964 . 87 ARG HB2 H 1.29 0.02 1 965 . 87 ARG HB3 H 1.15 0.02 1 966 . 87 ARG CG C 28.60 0.05 1 967 . 87 ARG CD C 43.74 0.05 1 968 . 87 ARG HD2 H 3.07 0.02 1 969 . 87 ARG HD3 H 3.00 0.02 1 970 . 87 ARG NE N 85.68 0.05 1 971 . 87 ARG HE H 7.21 0.02 1 972 . 87 ARG C C 173.85 0.05 1 973 . 88 TRP N N 121.77 0.05 1 974 . 88 TRP H H 8.84 0.02 1 975 . 88 TRP CA C 54.70 0.05 1 976 . 88 TRP HA H 4.78 0.02 1 977 . 88 TRP CB C 33.51 0.05 1 978 . 88 TRP HB2 H 2.95 0.02 1 979 . 88 TRP HB3 H 2.26 0.02 1 980 . 88 TRP CD1 C 127.70 0.05 1 981 . 88 TRP HD1 H 5.65 0.02 1 982 . 88 TRP NE1 N 129.02 0.05 1 983 . 88 TRP HE1 H 10.30 0.02 1 984 . 88 TRP CE3 C 121.64 0.05 1 985 . 88 TRP HE3 H 6.23 0.02 1 986 . 88 TRP CZ2 C 112.73 0.05 1 987 . 88 TRP HZ2 H 7.02 0.02 1 988 . 88 TRP CZ3 C 120.74 0.05 1 989 . 88 TRP HZ3 H 6.55 0.02 1 990 . 88 TRP HH2 H 6.91 0.02 1 991 . 88 TRP C C 175.44 0.05 1 992 . 89 ASP N N 119.47 0.05 1 993 . 89 ASP H H 8.29 0.02 1 994 . 89 ASP CA C 54.79 0.05 1 995 . 89 ASP HA H 5.60 0.02 1 996 . 89 ASP CB C 40.66 0.05 1 997 . 89 ASP HB2 H 3.13 0.02 1 998 . 89 ASP HB3 H 2.84 0.02 1 999 . 89 ASP C C 173.87 0.05 1 1000 . 90 ALA N N 121.12 0.05 1 1001 . 90 ALA H H 8.47 0.02 1 1002 . 90 ALA CA C 52.17 0.05 1 1003 . 90 ALA HA H 5.09 0.02 1 1004 . 90 ALA CB C 23.27 0.05 1 1005 . 90 ALA HB H 1.19 0.02 1 1006 . 90 ALA C C 175.04 0.05 1 1007 . 91 TYR N N 117.87 0.05 1 1008 . 91 TYR H H 8.44 0.02 1 1009 . 91 TYR CA C 58.73 0.05 1 1010 . 91 TYR HA H 5.11 0.02 1 1011 . 91 TYR CB C 40.66 0.05 1 1012 . 91 TYR HB2 H 2.83 0.02 1 1013 . 91 TYR HB3 H 2.58 0.02 1 1014 . 91 TYR CD1 C 132.42 0.05 1 1015 . 91 TYR HD1 H 6.96 0.02 1 1016 . 91 TYR CD2 C 132.42 0.05 1 1017 . 91 TYR HD2 H 6.96 0.02 1 1018 . 91 TYR CE1 C 117.92 0.05 1 1019 . 91 TYR HE1 H 7.15 0.02 1 1020 . 91 TYR CE2 C 117.92 0.05 1 1021 . 91 TYR HE2 H 7.15 0.02 1 1022 . 91 TYR C C 174.97 0.05 1 1023 . 92 CYS N N 119.90 0.05 1 1024 . 92 CYS H H 8.51 0.02 1 1025 . 92 CYS CA C 50.62 0.05 1 1026 . 92 CYS HA H 5.27 0.02 1 1027 . 92 CYS CB C 37.86 0.05 1 1028 . 92 CYS HB2 H 2.88 0.02 1 1029 . 92 CYS HB3 H 0.94 0.02 1 1030 . 92 CYS C C 173.85 0.05 1 1031 . 93 TYR N N 120.66 0.05 1 1032 . 93 TYR H H 9.45 0.02 1 1033 . 93 TYR CA C 57.20 0.05 1 1034 . 93 TYR HA H 4.89 0.02 1 1035 . 93 TYR CB C 41.82 0.05 1 1036 . 93 TYR HB2 H 2.75 0.02 1 1037 . 93 TYR HB3 H 2.57 0.02 1 1038 . 93 TYR CD1 C 132.91 0.05 1 1039 . 93 TYR HD1 H 6.84 0.02 1 1040 . 93 TYR CD2 C 132.91 0.05 1 1041 . 93 TYR HD2 H 6.84 0.02 1 1042 . 93 TYR CE1 C 117.66 0.05 1 1043 . 93 TYR HE1 H 6.75 0.02 1 1044 . 93 TYR CE2 C 117.66 0.05 1 1045 . 93 TYR HE2 H 6.75 0.02 1 1046 . 93 TYR C C 174.08 0.05 1 1047 . 94 ASN N N 124.43 0.05 1 1048 . 94 ASN H H 7.80 0.02 1 1049 . 94 ASN CA C 49.65 0.05 1 1050 . 94 ASN HA H 4.79 0.02 1 1051 . 94 ASN HB2 H 2.79 0.02 1 1052 . 94 ASN HB3 H 2.79 0.02 1 1053 . 94 ASN ND2 N 113.43 0.05 1 1054 . 94 ASN HD21 H 7.57 0.02 1 1055 . 94 ASN HD22 H 6.98 0.02 1 1056 . 95 PRO CA C 64.03 0.05 1 1057 . 95 PRO HA H 4.13 0.02 1 1058 . 95 PRO CD C 51.25 0.05 1 1059 . 95 PRO HD2 H 3.78 0.02 1 1060 . 95 PRO HD3 H 3.46 0.02 1 1061 . 95 PRO CB C 32.16 0.05 1 1062 . 95 PRO HB2 H 2.25 0.02 1 1063 . 95 PRO HB3 H 1.71 0.02 1 1064 . 95 PRO CG C 26.54 0.05 1 1065 . 95 PRO HG2 H 2.04 0.02 1 1066 . 95 PRO HG3 H 1.55 0.02 1 1067 . 95 PRO C C 177.03 0.05 1 1068 . 96 HIS N N 116.31 0.05 1 1069 . 96 HIS H H 8.33 0.02 1 1070 . 96 HIS CA C 55.33 0.05 1 1071 . 96 HIS HA H 4.63 0.02 1 1072 . 96 HIS NE2 N 177.04 0.05 1 1073 . 96 HIS CD2 C 120.10 0.05 1 1074 . 96 HIS HD2 H 7.22 0.02 1 1075 . 96 HIS ND1 N 193.85 0.05 1 1076 . 96 HIS CE1 C 137.50 0.05 1 1077 . 96 HIS HE1 H 8.20 0.02 1 1078 . 96 HIS CB C 29.45 0.05 1 1079 . 96 HIS HB2 H 3.25 0.02 1 1080 . 96 HIS HB3 H 3.00 0.02 1 1081 . 96 HIS C C 174.45 0.05 1 1082 . 97 ALA N N 123.76 0.05 1 1083 . 97 ALA H H 7.40 0.02 1 1084 . 97 ALA CA C 51.97 0.05 1 1085 . 97 ALA HA H 4.28 0.02 1 1086 . 97 ALA CB C 19.69 0.05 1 1087 . 97 ALA HB H 1.24 0.02 1 1088 . 97 ALA C C 176.47 0.05 1 1089 . 98 LYS N N 127.52 0.05 1 1090 . 98 LYS H H 8.04 0.02 1 1091 . 98 LYS CA C 58.04 0.05 1 1092 . 98 LYS HA H 4.02 0.02 1 1093 . 98 LYS CB C 33.47 0.05 1 1094 . 98 LYS HB2 H 1.76 0.02 1 1095 . 98 LYS HB3 H 1.63 0.02 1 1096 . 98 LYS CG C 24.82 0.05 1 1097 . 98 LYS HG2 H 1.36 0.02 1 1098 . 98 LYS HG3 H 1.36 0.02 1 1099 . 98 LYS CD C 29.07 0.05 1 1100 . 98 LYS HD2 H 1.64 0.02 1 1101 . 98 LYS HD3 H 1.64 0.02 1 1102 . 98 LYS CE C 42.10 0.05 1 1103 . 98 LYS HE2 H 2.99 0.02 1 1104 . 98 LYS HE3 H 2.99 0.02 1 stop_ save_