data_5882 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone chemical shift assignments for the C-terminal globular domain of EMILIN-1 ; _BMRB_accession_number 5882 _BMRB_flat_file_name bmr5882.str _Entry_type original _Submission_date 2003-07-25 _Accession_date 2003-07-25 _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 Verdone Giuliana . . 2 Colebrooke Simon A. . 3 Boyd Jonathan . . 4 Viglino Paolo . . 5 Corazza Alessandra . . 6 Esposito Gennaro . . 7 Campbell Iain D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 142 "13C chemical shifts" 438 "15N chemical shifts" 137 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-04-19 update BMRB 'add related PDB ID' 2007-01-12 update author 'update the residue sequence' 2004-04-07 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific backbone NMR assignments for the C-terminal globular domain of EMILIN-1. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15017143 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Verdone Giuliana . . 2 Colebrooke Simon A. . 3 Boyd Jonathan . . 4 Viglino Paolo . . 5 Corazza Alessandra . . 6 Doliana Roberto . . 7 Mungiguerra Gabriella . . 8 Colombatti Alfonso . . 9 Esposito Gennaro . . 10 Campbell Iain D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 29 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 91 _Page_last 92 _Year 2004 _Details . loop_ _Keyword 'C1q-like domain' 'elastic fibres' EMILIN TROSY 'partially deuterated proteins' stop_ save_ ################################## # Molecular system description # ################################## save_system_gC1q-like _Saveframe_category molecular_system _Mol_system_name 'C1q trimer' _Abbreviation_common gC1q-like _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'C1q subunit 1' $C1q_monomer 'C1q subunit 2' $C1q_monomer 'C1q subunit 3' $C1q_monomer stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state trimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'C1q subunit 1' 1 'C1q subunit 2' 1 'C1q subunit 3' stop_ loop_ _Biological_function 'trimerization of h-EMILIN-1' 'cell-adhesion promoting function' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_C1q_monomer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'C1q domain of h-EMILIN-1' _Abbreviation_common gC1q-like _Molecular_mass 16824 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 162 _Mol_residue_sequence ; MRGSHHHHHHGSPVPQVAFS AALSLPRSEPGTVPFDRVLL NDGGYYDPETGVFTAPLAGR YLLSAVLTGHRHEKVEAVLS RSNQGVARVDSGGYEPEGLE NKPVAESQPSPGTLGVFSLI LPLQAGDTVCVDLVMGQLAH SEEPLTIFSGALLYGDPELE HA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 GLY 4 SER 5 HIS 6 HIS 7 HIS 8 HIS 9 HIS 10 HIS 11 GLY 12 SER 13 PRO 14 VAL 15 PRO 16 GLN 17 VAL 18 ALA 19 PHE 20 SER 21 ALA 22 ALA 23 LEU 24 SER 25 LEU 26 PRO 27 ARG 28 SER 29 GLU 30 PRO 31 GLY 32 THR 33 VAL 34 PRO 35 PHE 36 ASP 37 ARG 38 VAL 39 LEU 40 LEU 41 ASN 42 ASP 43 GLY 44 GLY 45 TYR 46 TYR 47 ASP 48 PRO 49 GLU 50 THR 51 GLY 52 VAL 53 PHE 54 THR 55 ALA 56 PRO 57 LEU 58 ALA 59 GLY 60 ARG 61 TYR 62 LEU 63 LEU 64 SER 65 ALA 66 VAL 67 LEU 68 THR 69 GLY 70 HIS 71 ARG 72 HIS 73 GLU 74 LYS 75 VAL 76 GLU 77 ALA 78 VAL 79 LEU 80 SER 81 ARG 82 SER 83 ASN 84 GLN 85 GLY 86 VAL 87 ALA 88 ARG 89 VAL 90 ASP 91 SER 92 GLY 93 GLY 94 TYR 95 GLU 96 PRO 97 GLU 98 GLY 99 LEU 100 GLU 101 ASN 102 LYS 103 PRO 104 VAL 105 ALA 106 GLU 107 SER 108 GLN 109 PRO 110 SER 111 PRO 112 GLY 113 THR 114 LEU 115 GLY 116 VAL 117 PHE 118 SER 119 LEU 120 ILE 121 LEU 122 PRO 123 LEU 124 GLN 125 ALA 126 GLY 127 ASP 128 THR 129 VAL 130 CYS 131 VAL 132 ASP 133 LEU 134 VAL 135 MET 136 GLY 137 GLN 138 LEU 139 ALA 140 HIS 141 SER 142 GLU 143 GLU 144 PRO 145 LEU 146 THR 147 ILE 148 PHE 149 SER 150 GLY 151 ALA 152 LEU 153 LEU 154 TYR 155 GLY 156 ASP 157 PRO 158 GLU 159 LEU 160 GLU 161 HIS 162 ALA 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 PDB 2KA3 "Structure Of Emilin-1 C1q-Like Domain" 100.00 162 100.00 100.00 1.20e-110 PDB 2OII "Structure Of Emilin-1 C1q-Like Domain" 99.38 162 100.00 100.00 6.05e-110 EMBL CAB43287 "hypothetical protein [Homo sapiens]" 93.21 990 99.34 100.00 3.49e-93 GB AAD42161 "emilin precursor [Homo sapiens]" 93.21 1016 99.34 100.00 4.04e-93 GB AAF25006 "elastin microfibril interfase located protein [Homo sapiens]" 93.21 1016 99.34 100.00 4.04e-93 GB AAH07530 "EMILIN1 protein [Homo sapiens]" 93.21 347 99.34 100.00 7.48e-99 GB AAH09947 "EMILIN1 protein, partial [Homo sapiens]" 93.21 580 99.34 100.00 1.26e-96 GB AAI36280 "Elastin microfibril interfacer 1 [Homo sapiens]" 93.21 1016 99.34 100.00 4.04e-93 REF NP_001247837 "EMILIN-1 precursor [Macaca mulatta]" 93.21 1016 98.68 100.00 1.75e-92 REF NP_008977 "EMILIN-1 precursor [Homo sapiens]" 93.21 1016 99.34 100.00 4.04e-93 REF XP_002812243 "PREDICTED: EMILIN-1 [Pongo abelii]" 93.21 1016 98.68 100.00 1.86e-92 REF XP_003270673 "PREDICTED: EMILIN-1 [Nomascus leucogenys]" 93.21 1016 98.01 100.00 1.05e-91 REF XP_003827126 "PREDICTED: EMILIN-1 isoform X1 [Pan paniscus]" 93.21 1016 98.68 100.00 1.72e-92 SP Q9Y6C2 "RecName: Full=EMILIN-1; AltName: Full=Elastin microfibril interface-located protein 1; Short=Elastin microfibril interfacer 1; " 93.21 1016 99.34 100.00 4.26e-93 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Tissue _Fraction $C1q_monomer Human 9606 Eukaryota Metazoa Homo sapiens 'elastic tissue' 'extracellular matrix' 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 $C1q_monomer 'recombinant technology' 'E. coli' Escherichia coli . . 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 $C1q_monomer 1.8 mM '[U-100% 13C; U-100% 15N; 80% 2H]' 'phosphate buffer' 20 mM . 'sodium chloride' 100 mM . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2.3 loop_ _Task 'spectra processing' stop_ _Details . save_ save_XEasy _Saveframe_category software _Name XEasy _Version 1.3.13 loop_ _Task 'spectra assignment' stop_ _Details ; Bartels C, Xia TH, Billeter M, Guntert P, Wthrich K. (1995) J Biomol NMR 6:1-10. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer 'Oxford Instruments' _Model . _Field_strength 750 _Details ; Spectrometers are built in-house at the Oxford Centre for Molecular Sciences. They incorporate an Oxford Instruments magnet and a GE/Omega computer. ; save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer 'Oxford Instruments' _Model . _Field_strength 600 _Details . save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer 'Oxford Instruments' _Model . _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H,15N-HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H,15N-HSQC _Sample_label $sample_1 save_ save_3D_[15N,_1H]-TROSY-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HNCA' _Sample_label $sample_1 save_ save_3D_[15N,_1H]-TROSY-HN(CO)CA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HN(CO)CA' _Sample_label $sample_1 save_ save_3D_[15N,_1H]-TROSY-HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HNCACB' _Sample_label $sample_1 save_ save_3D_[15N,_1H]-TROSY-HN(CO)CACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HN(CO)CACB' _Sample_label $sample_1 save_ save_3D_[15N,_1H]-TROSY-HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HNCO' _Sample_label $sample_1 save_ save_3D_[15N,_1H]-TROSY-HN(CA)CO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HN(CA)CO' _Sample_label $sample_1 save_ save_3D_15N-NOESY-HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-NOESY-HSQC' _Sample_label $sample_1 save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name 1H,15N-HSQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HN(CO)CA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HN(CO)CACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HNCO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D [15N, 1H]-TROSY-HN(CA)CO' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-NOESY-HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.50 0.01 n/a temperature 310.0 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label dioxane H 1 'methylene protons' ppm 3.750 internal direct . . . 1.0 $entry_citation $entry_citation dioxane C 13 'methylene protons' ppm . external indirect . . . 0.251449530 $entry_citation $entry_citation dioxane N 15 'methylene protons' ppm . external indirect . . . 0.101329118 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'C1q subunit 1' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 846 13 PRO CA C 62.9 0.2 1 2 846 13 PRO C C 176.4 0.2 1 3 846 13 PRO CB C 30.7 0.2 1 4 847 14 VAL H H 7.98 0.01 1 5 847 14 VAL N N 119.91 0.03 1 6 847 14 VAL CA C 58.9 0.2 1 7 847 14 VAL C C 174.2 0.2 1 8 847 14 VAL CB C 31.6 0.2 1 9 848 15 PRO CA C 62.4 0.2 1 10 848 15 PRO C C 175.2 0.2 1 11 848 15 PRO CB C 30.6 0.2 1 12 849 16 GLN H H 7.68 0.01 1 13 849 16 GLN N N 119.90 0.03 1 14 849 16 GLN CA C 54.7 0.2 1 15 849 16 GLN C C 174.4 0.2 1 16 849 16 GLN CB C 26.1 0.2 1 17 850 17 VAL H H 7.98 0.01 1 18 850 17 VAL N N 122.91 0.03 1 19 850 17 VAL CA C 61.2 0.2 1 20 850 17 VAL C C 173.7 0.2 1 21 850 17 VAL CB C 34.2 0.2 1 22 851 18 ALA H H 7.59 0.01 1 23 851 18 ALA N N 124.83 0.03 1 24 851 18 ALA CA C 52.0 0.2 1 25 851 18 ALA C C 174.7 0.2 1 26 851 18 ALA CB C 21.3 0.2 1 27 852 19 PHE H H 9.00 0.01 1 28 852 19 PHE N N 116.05 0.03 1 29 852 19 PHE CA C 55.0 0.2 1 30 852 19 PHE C C 172.2 0.2 1 31 852 19 PHE CB C 42.4 0.2 1 32 853 20 SER H H 8.70 0.01 1 33 853 20 SER N N 114.66 0.03 1 34 853 20 SER CA C 58.5 0.2 1 35 853 20 SER C C 173.5 0.2 1 36 853 20 SER CB C 65.9 0.2 1 37 854 21 ALA H H 9.90 0.01 1 38 854 21 ALA N N 131.92 0.03 1 39 854 21 ALA CA C 51.0 0.2 1 40 854 21 ALA C C 173.4 0.2 1 41 854 21 ALA CB C 22.8 0.2 1 42 855 22 ALA H H 9.79 0.01 1 43 855 22 ALA N N 123.31 0.03 1 44 855 22 ALA CA C 49.1 0.2 1 45 855 22 ALA C C 175.8 0.2 1 46 855 22 ALA CB C 23.4 0.2 1 47 856 23 LEU H H 8.31 0.01 1 48 856 23 LEU N N 120.92 0.03 1 49 856 23 LEU CA C 54.2 0.2 1 50 856 23 LEU C C 176.8 0.2 1 51 856 23 LEU CB C 43.4 0.2 1 52 857 24 SER H H 10.92 0.01 1 53 857 24 SER N N 128.32 0.03 1 54 857 24 SER CA C 58.8 0.2 1 55 857 24 SER C C 172.3 0.2 1 56 857 24 SER CB C 64.7 0.2 1 57 858 25 LEU H H 7.23 0.01 1 58 858 25 LEU N N 125.70 0.03 1 59 858 25 LEU CA C 51.5 0.2 1 60 858 25 LEU C C 172.8 0.2 1 61 858 25 LEU CB C 42.2 0.2 1 62 859 26 PRO CA C 62.7 0.2 1 63 859 26 PRO C C 177.7 0.2 1 64 859 26 PRO CB C 31.1 0.2 1 65 860 27 ARG H H 8.41 0.01 1 66 860 27 ARG N N 120.50 0.03 1 67 860 27 ARG CA C 56.5 0.2 1 68 860 27 ARG C C 176.4 0.2 1 69 860 27 ARG CB C 29.0 0.2 1 70 861 28 SER H H 8.03 0.01 1 71 861 28 SER N N 115.37 0.03 1 72 861 28 SER CA C 57.7 0.2 1 73 861 28 SER C C 174.0 0.2 1 74 861 28 SER CB C 63.1 0.2 1 75 862 29 GLU H H 8.30 0.01 1 76 862 29 GLU N N 122.44 0.03 1 77 862 29 GLU CA C 53.2 0.2 1 78 862 29 GLU C C 175.0 0.2 1 79 862 29 GLU CB C 28.0 0.2 1 80 863 30 PRO CA C 62.5 0.2 1 81 863 30 PRO C C 176.2 0.2 1 82 863 30 PRO CB C 31.7 0.2 1 83 864 31 GLY H H 8.75 0.01 1 84 864 31 GLY N N 108.28 0.03 1 85 864 31 GLY CA C 42.6 0.2 1 86 864 31 GLY C C 174.6 0.2 1 87 865 32 THR H H 8.40 0.01 1 88 865 32 THR N N 121.13 0.03 1 89 865 32 THR CA C 64.1 0.2 1 90 865 32 THR C C 174.9 0.2 1 91 865 32 THR CB C 68.4 0.2 1 92 866 33 VAL H H 9.07 0.01 1 93 866 33 VAL N N 128.92 0.03 1 94 866 33 VAL CA C 60.3 0.2 1 95 866 33 VAL C C 173.2 0.2 1 96 866 33 VAL CB C 32.6 0.2 1 97 867 34 PRO CA C 60.0 0.2 1 98 867 34 PRO C C 174.9 0.2 1 99 867 34 PRO CB C 28.1 0.2 1 100 868 35 PHE H H 6.98 0.01 1 101 868 35 PHE N N 123.47 0.03 1 102 868 35 PHE CA C 58.9 0.2 1 103 868 35 PHE C C 176.3 0.2 1 104 868 35 PHE CB C 36.2 0.2 1 105 869 36 ASP H H 8.61 0.01 1 106 869 36 ASP N N 124.75 0.03 1 107 869 36 ASP CA C 55.9 0.2 1 108 869 36 ASP C C 174.8 0.2 1 109 869 36 ASP CB C 42.1 0.2 1 110 870 37 ARG H H 9.29 0.01 1 111 870 37 ARG N N 122.72 0.03 1 112 870 37 ARG CA C 54.1 0.2 1 113 870 37 ARG C C 175.3 0.2 1 114 870 37 ARG CB C 28.5 0.2 1 115 871 38 VAL H H 9.01 0.01 1 116 871 38 VAL N N 128.08 0.03 1 117 871 38 VAL CA C 64.3 0.2 1 118 871 38 VAL C C 176.1 0.2 1 119 871 38 VAL CB C 31.2 0.2 1 120 872 39 LEU H H 9.03 0.01 1 121 872 39 LEU N N 130.22 0.03 1 122 872 39 LEU CA C 55.8 0.2 1 123 872 39 LEU C C 176.0 0.2 1 124 872 39 LEU CB C 40.9 0.2 1 125 873 40 LEU H H 8.12 0.01 1 126 873 40 LEU N N 119.75 0.03 1 127 873 40 LEU CA C 54.7 0.2 1 128 873 40 LEU C C 174.9 0.2 1 129 873 40 LEU CB C 44.3 0.2 1 130 874 41 ASN CA C 52.1 0.2 1 131 874 41 ASN C C 175.7 0.2 1 132 874 41 ASN CB C 35.8 0.2 1 133 875 42 ASP H H 8.84 0.01 1 134 875 42 ASP N N 126.80 0.03 1 135 875 42 ASP CA C 56.4 0.2 1 136 875 42 ASP C C 176.6 0.2 1 137 875 42 ASP CB C 38.4 0.2 1 138 876 43 GLY H H 8.93 0.01 1 139 876 43 GLY N N 116.22 0.03 1 140 876 43 GLY CA C 44.5 0.2 1 141 876 43 GLY C C 173.9 0.2 1 142 877 44 GLY H H 7.54 0.01 1 143 877 44 GLY N N 105.28 0.03 1 144 877 44 GLY CA C 45.9 0.2 1 145 877 44 GLY C C 174.6 0.2 1 146 878 45 TYR H H 8.03 0.01 1 147 878 45 TYR N N 118.12 0.03 1 148 878 45 TYR CA C 59.3 0.2 1 149 878 45 TYR C C 175.4 0.2 1 150 878 45 TYR CB C 36.6 0.2 1 151 879 46 TYR H H 8.04 0.01 1 152 879 46 TYR N N 119.06 0.03 1 153 879 46 TYR CA C 57.1 0.2 1 154 879 46 TYR C C 173.3 0.2 1 155 879 46 TYR CB C 38.1 0.2 1 156 880 47 ASP H H 6.99 0.01 1 157 880 47 ASP N N 127.88 0.03 1 158 880 47 ASP CA C 49.1 0.2 1 159 880 47 ASP C C 173.3 0.2 1 160 880 47 ASP CB C 41.9 0.2 1 161 881 48 PRO CA C 63.2 0.2 1 162 881 48 PRO C C 176.8 0.2 1 163 881 48 PRO CB C 31.1 0.2 1 164 882 49 GLU H H 7.97 0.01 1 165 882 49 GLU N N 115.26 0.03 1 166 882 49 GLU CA C 57.8 0.2 1 167 882 49 GLU C C 178.2 0.2 1 168 882 49 GLU CB C 28.6 0.2 1 169 883 50 THR H H 6.90 0.01 1 170 883 50 THR N N 103.96 0.03 1 171 883 50 THR CA C 60.4 0.2 1 172 883 50 THR C C 175.9 0.2 1 173 883 50 THR CB C 70.5 0.2 1 174 884 51 GLY H H 8.59 0.01 1 175 884 51 GLY N N 108.40 0.03 1 176 884 51 GLY CA C 45.1 0.2 1 177 884 51 GLY C C 173.6 0.2 1 178 885 52 VAL H H 7.30 0.01 1 179 885 52 VAL N N 118.10 0.03 1 180 885 52 VAL CA C 61.6 0.2 1 181 885 52 VAL C C 177.1 0.2 1 182 885 52 VAL CB C 33.0 0.2 1 183 886 53 PHE H H 9.19 0.01 1 184 886 53 PHE N N 130.16 0.03 1 185 886 53 PHE CA C 55.1 0.2 1 186 886 53 PHE C C 173.6 0.2 1 187 886 53 PHE CB C 40.1 0.2 1 188 887 54 THR H H 7.35 0.01 1 189 887 54 THR N N 124.84 0.03 1 190 887 54 THR CA C 60.4 0.2 1 191 887 54 THR C C 172.4 0.2 1 192 887 54 THR CB C 68.1 0.2 1 193 888 55 ALA H H 8.29 0.01 1 194 888 55 ALA N N 127.64 0.03 1 195 888 55 ALA CA C 49.1 0.2 1 196 888 55 ALA C C 177.6 0.2 1 197 888 55 ALA CB C 16.9 0.2 1 198 889 56 PRO CA C 62.4 0.2 1 199 889 56 PRO C C 175.4 0.2 1 200 889 56 PRO CB C 29.9 0.2 1 201 890 57 LEU H H 6.47 0.01 1 202 890 57 LEU N N 114.77 0.03 1 203 890 57 LEU CA C 52.6 0.2 1 204 890 57 LEU C C 175.3 0.2 1 205 890 57 LEU CB C 44.5 0.2 1 206 891 58 ALA H H 8.99 0.01 1 207 891 58 ALA N N 127.29 0.03 1 208 891 58 ALA CA C 51.4 0.2 1 209 891 58 ALA C C 177.4 0.2 1 210 891 58 ALA CB C 17.7 0.2 1 211 892 59 GLY H H 8.78 0.01 1 212 892 59 GLY N N 111.26 0.03 1 213 892 59 GLY CA C 45.7 0.2 1 214 892 59 GLY C C 170.1 0.2 1 215 893 60 ARG H H 8.39 0.01 1 216 893 60 ARG N N 122.06 0.03 1 217 893 60 ARG CA C 55.3 0.2 1 218 893 60 ARG C C 174.3 0.2 1 219 893 60 ARG CB C 29.0 0.2 1 220 894 61 TYR H H 8.79 0.01 1 221 894 61 TYR N N 121.57 0.03 1 222 894 61 TYR CA C 55.5 0.2 1 223 894 61 TYR C C 174.2 0.2 1 224 894 61 TYR CB C 39.0 0.2 1 225 895 62 LEU H H 8.73 0.01 1 226 895 62 LEU N N 125.08 0.03 1 227 895 62 LEU CA C 53.9 0.2 1 228 895 62 LEU C C 174.9 0.2 1 229 895 62 LEU CB C 42.7 0.2 1 230 896 63 LEU H H 8.66 0.01 1 231 896 63 LEU N N 126.27 0.03 1 232 896 63 LEU CA C 53.0 0.2 1 233 896 63 LEU C C 174.8 0.2 1 234 896 63 LEU CB C 44.5 0.2 1 235 897 64 SER H H 8.86 0.01 1 236 897 64 SER N N 114.17 0.03 1 237 897 64 SER CA C 55.0 0.2 1 238 897 64 SER C C 172.8 0.2 1 239 897 64 SER CB C 65.8 0.2 1 240 898 65 ALA H H 9.20 0.01 1 241 898 65 ALA N N 124.41 0.03 1 242 898 65 ALA CA C 51.5 0.2 1 243 898 65 ALA C C 175.3 0.2 1 244 898 65 ALA CB C 22.0 0.2 1 245 899 66 VAL H H 9.06 0.01 1 246 899 66 VAL N N 121.85 0.03 1 247 899 66 VAL CA C 62.2 0.2 1 248 899 66 VAL C C 174.0 0.2 1 249 899 66 VAL CB C 33.4 0.2 1 250 900 67 LEU H H 9.35 0.01 1 251 900 67 LEU N N 125.15 0.03 1 252 900 67 LEU CA C 52.9 0.2 1 253 900 67 LEU C C 174.2 0.2 1 254 900 67 LEU CB C 41.4 0.2 1 255 901 68 THR H H 7.58 0.01 1 256 901 68 THR N N 118.82 0.03 1 257 901 68 THR CA C 61.9 0.2 1 258 901 68 THR C C 174.3 0.2 1 259 901 68 THR CB C 68.4 0.2 1 260 902 69 GLY H H 9.21 0.01 1 261 902 69 GLY N N 114.66 0.03 1 262 902 69 GLY CA C 43.5 0.2 1 263 902 69 GLY C C 174.4 0.2 1 264 903 70 HIS H H 8.31 0.01 1 265 903 70 HIS N N 118.13 0.03 1 266 903 70 HIS CA C 55.3 0.2 1 267 903 70 HIS C C 175.9 0.2 1 268 903 70 HIS CB C 31.0 0.2 1 269 904 71 ARG H H 8.44 0.01 1 270 904 71 ARG N N 119.97 0.03 1 271 904 71 ARG CA C 57.8 0.2 1 272 904 71 ARG C C 175.9 0.2 1 273 904 71 ARG CB C 29.1 0.2 1 274 905 72 HIS H H 8.50 0.01 1 275 905 72 HIS N N 114.71 0.03 1 276 905 72 HIS CA C 57.6 0.2 1 277 905 72 HIS C C 174.2 0.2 1 278 905 72 HIS CB C 28.6 0.2 1 279 906 73 GLU H H 7.70 0.01 1 280 906 73 GLU N N 119.62 0.03 1 281 906 73 GLU CA C 54.7 0.2 1 282 906 73 GLU C C 174.3 0.2 1 283 906 73 GLU CB C 31.4 0.2 1 284 907 74 LYS H H 8.10 0.01 1 285 907 74 LYS N N 120.29 0.03 1 286 907 74 LYS CA C 55.3 0.2 1 287 907 74 LYS C C 174.3 0.2 1 288 907 74 LYS CB C 31.8 0.2 1 289 908 75 VAL H H 8.45 0.01 1 290 908 75 VAL N N 118.34 0.03 1 291 908 75 VAL CA C 60.3 0.2 1 292 908 75 VAL C C 174.5 0.2 1 293 908 75 VAL CB C 33.6 0.2 1 294 909 76 GLU H H 8.39 0.01 1 295 909 76 GLU N N 125.67 0.03 1 296 909 76 GLU CA C 54.0 0.2 1 297 909 76 GLU C C 175.2 0.2 1 298 909 76 GLU CB C 32.9 0.2 1 299 910 77 ALA H H 8.71 0.01 1 300 910 77 ALA N N 126.57 0.03 1 301 910 77 ALA CA C 50.7 0.2 1 302 910 77 ALA C C 173.7 0.2 1 303 910 77 ALA CB C 22.5 0.2 1 304 911 78 VAL H H 9.37 0.01 1 305 911 78 VAL N N 120.37 0.03 1 306 911 78 VAL CA C 60.3 0.2 1 307 911 78 VAL C C 173.7 0.2 1 308 911 78 VAL CB C 35.8 0.2 1 309 912 79 LEU H H 8.21 0.01 1 310 912 79 LEU N N 128.75 0.03 1 311 912 79 LEU CA C 53.1 0.2 1 312 912 79 LEU C C 174.6 0.2 1 313 912 79 LEU CB C 40.2 0.2 1 314 913 80 SER H H 8.87 0.01 1 315 913 80 SER N N 124.54 0.03 1 316 913 80 SER CA C 56.4 0.2 1 317 913 80 SER C C 173.3 0.2 1 318 913 80 SER CB C 64.3 0.2 1 319 914 81 ARG H H 8.93 0.01 1 320 914 81 ARG N N 126.10 0.03 1 321 914 81 ARG CA C 52.9 0.2 1 322 914 81 ARG C C 176.3 0.2 1 323 914 81 ARG CB C 30.9 0.2 1 324 915 82 SER H H 10.19 0.01 1 325 915 82 SER N N 127.33 0.03 1 326 915 82 SER CA C 58.2 0.2 1 327 915 82 SER C C 174.4 0.2 1 328 915 82 SER CB C 61.6 0.2 1 329 916 83 ASN H H 8.28 0.01 1 330 916 83 ASN N N 108.53 0.03 1 331 916 83 ASN CA C 54.8 0.2 1 332 916 83 ASN C C 173.5 0.2 1 333 916 83 ASN CB C 36.8 0.2 1 334 916 83 ASN CG C 178.7 0.2 1 335 916 83 ASN ND2 N 112.60 0.03 1 336 916 83 ASN HD21 H 7.38 0.01 2 337 916 83 ASN HD22 H 6.75 0.01 2 338 917 84 GLN H H 7.81 0.01 1 339 917 84 GLN N N 118.81 0.03 1 340 917 84 GLN CA C 53.9 0.2 1 341 917 84 GLN C C 175.5 0.2 1 342 917 84 GLN CB C 30.1 0.2 1 343 917 84 GLN CG C 32.5 0.2 1 344 917 84 GLN CD C 180.6 0.2 1 345 917 84 GLN NE2 N 112.02 0.03 1 346 917 84 GLN HE21 H 7.46 0.01 2 347 917 84 GLN HE22 H 6.79 0.01 2 348 918 85 GLY H H 8.78 0.01 1 349 918 85 GLY N N 113.22 0.03 1 350 918 85 GLY CA C 46.3 0.2 1 351 918 85 GLY C C 174.7 0.2 1 352 919 86 VAL H H 9.19 0.01 1 353 919 86 VAL N N 121.23 0.03 1 354 919 86 VAL CA C 61.4 0.2 1 355 919 86 VAL C C 174.1 0.2 1 356 919 86 VAL CB C 32.6 0.2 1 357 920 87 ALA H H 7.45 0.01 1 358 920 87 ALA N N 116.39 0.03 1 359 920 87 ALA CA C 51.1 0.2 1 360 920 87 ALA C C 174.4 0.2 1 361 920 87 ALA CB C 21.2 0.2 1 362 921 88 ARG H H 8.84 0.01 1 363 921 88 ARG N N 121.76 0.03 1 364 921 88 ARG CA C 54.5 0.2 1 365 921 88 ARG C C 173.7 0.2 1 366 921 88 ARG CB C 34.2 0.2 1 367 922 89 VAL H H 8.77 0.01 1 368 922 89 VAL N N 117.91 0.03 1 369 922 89 VAL CA C 59.2 0.2 1 370 922 89 VAL C C 174.9 0.2 1 371 922 89 VAL CB C 34.0 0.2 1 372 923 90 ASP H H 8.38 0.01 1 373 923 90 ASP N N 122.36 0.03 1 374 923 90 ASP CA C 53.3 0.2 1 375 923 90 ASP C C 177.7 0.2 1 376 923 90 ASP CB C 41.3 0.2 1 377 924 91 SER H H 9.27 0.01 1 378 924 91 SER N N 121.43 0.03 1 379 924 91 SER CA C 60.5 0.2 1 380 924 91 SER C C 175.0 0.2 1 381 924 91 SER CB C 62.4 0.2 1 382 925 92 GLY H H 8.88 0.01 1 383 925 92 GLY N N 109.79 0.03 1 384 925 92 GLY CA C 45.0 0.2 1 385 925 92 GLY C C 174.8 0.2 1 386 926 93 GLY H H 7.39 0.01 1 387 926 93 GLY N N 107.18 0.03 1 388 926 93 GLY CA C 43.7 0.2 1 389 926 93 GLY C C 172.1 0.2 1 390 927 94 TYR H H 8.16 0.01 1 391 927 94 TYR N N 119.72 0.03 1 392 927 94 TYR CA C 57.7 0.2 1 393 927 94 TYR C C 174.6 0.2 1 394 927 94 TYR CB C 39.9 0.2 1 395 928 95 GLU H H 7.80 0.01 1 396 928 95 GLU N N 127.70 0.03 1 397 928 95 GLU CA C 52.3 0.2 1 398 928 95 GLU C C 172.8 0.2 1 399 928 95 GLU CB C 30.3 0.2 1 400 929 96 PRO CA C 62.2 0.2 1 401 929 96 PRO C C 176.5 0.2 1 402 929 96 PRO CB C 30.9 0.2 1 403 930 97 GLU H H 8.37 0.01 1 404 930 97 GLU N N 120.66 0.03 1 405 930 97 GLU CA C 56.4 0.2 1 406 930 97 GLU C C 177.3 0.2 1 407 930 97 GLU CB C 29.1 0.2 1 408 931 98 GLY H H 8.39 0.01 1 409 931 98 GLY N N 109.70 0.03 1 410 931 98 GLY CA C 45.0 0.2 1 411 931 98 GLY C C 174.5 0.2 1 412 932 99 LEU H H 7.95 0.01 1 413 932 99 LEU N N 121.31 0.03 1 414 932 99 LEU CA C 55.1 0.2 1 415 932 99 LEU C C 177.6 0.2 1 416 932 99 LEU CB C 41.1 0.2 1 417 933 100 GLU H H 8.46 0.01 1 418 933 100 GLU N N 120.40 0.03 1 419 933 100 GLU CA C 56.5 0.2 1 420 933 100 GLU C C 176.2 0.2 1 421 933 100 GLU CB C 29.0 0.2 1 422 934 101 ASN CA C 52.9 0.2 1 423 934 101 ASN CB C 37.8 0.2 1 424 934 101 ASN CG C 177.2 0.2 1 425 934 101 ASN ND2 N 112.76 0.03 1 426 934 101 ASN HD21 H 7.50 0.01 2 427 934 101 ASN HD22 H 6.83 0.01 2 428 935 102 LYS H H 7.95 0.01 1 429 935 102 LYS N N 121.98 0.03 1 430 935 102 LYS CA C 53.9 0.2 1 431 935 102 LYS C C 174.4 0.2 1 432 935 102 LYS CB C 31.5 0.2 1 433 936 103 PRO CA C 62.8 0.2 1 434 936 103 PRO C C 177.0 0.2 1 435 936 103 PRO CB C 31.0 0.2 1 436 937 104 VAL H H 8.04 0.01 1 437 937 104 VAL N N 119.65 0.03 1 438 937 104 VAL CA C 61.9 0.2 1 439 937 104 VAL C C 176.1 0.2 1 440 937 104 VAL CB C 31.7 0.2 1 441 938 105 ALA H H 8.19 0.01 1 442 938 105 ALA N N 126.34 0.03 1 443 938 105 ALA CA C 52.1 0.2 1 444 938 105 ALA C C 177.6 0.2 1 445 938 105 ALA CB C 19.6 0.2 1 446 939 106 GLU H H 8.24 0.01 1 447 939 106 GLU N N 119.03 0.03 1 448 939 106 GLU CA C 56.4 0.2 1 449 939 106 GLU C C 177.6 0.2 1 450 939 106 GLU CB C 28.9 0.2 1 451 940 107 SER CA C 57.5 0.2 1 452 940 107 SER C C 173.4 0.2 1 453 940 107 SER CB C 64.2 0.2 1 454 941 108 GLN H H 7.64 0.01 1 455 941 108 GLN N N 122.93 0.03 1 456 941 108 GLN CA C 53.4 0.2 1 457 941 108 GLN C C 173.4 0.2 1 458 941 108 GLN CB C 29.3 0.2 1 459 941 108 GLN CG C 33.0 0.2 1 460 941 108 GLN NE2 N 114.27 0.03 1 461 941 108 GLN HE21 H 7.69 0.01 2 462 941 108 GLN HE22 H 6.95 0.01 2 463 942 109 PRO CA C 62.5 0.2 1 464 942 109 PRO C C 176.6 0.2 1 465 942 109 PRO CB C 30.7 0.2 1 466 943 110 SER H H 8.45 0.01 1 467 943 110 SER N N 117.49 0.03 1 468 943 110 SER CA C 56.2 0.2 1 469 943 110 SER CB C 63.4 0.2 1 470 944 111 PRO CA C 62.4 0.2 1 471 944 111 PRO C C 177.0 0.2 1 472 944 111 PRO CB C 31.2 0.2 1 473 945 112 GLY H H 7.99 0.01 1 474 945 112 GLY N N 106.44 0.03 1 475 945 112 GLY CA C 45.0 0.2 1 476 945 112 GLY C C 175.6 0.2 1 477 946 113 THR H H 8.50 0.01 1 478 946 113 THR N N 111.27 0.03 1 479 946 113 THR CA C 60.7 0.2 1 480 946 113 THR C C 172.6 0.2 1 481 946 113 THR CB C 69.3 0.2 1 482 947 114 LEU H H 7.63 0.01 1 483 947 114 LEU N N 123.50 0.03 1 484 947 114 LEU CA C 53.4 0.2 1 485 947 114 LEU C C 175.3 0.2 1 486 947 114 LEU CB C 45.1 0.2 1 487 948 115 GLY H H 9.13 0.01 1 488 948 115 GLY N N 111.15 0.03 1 489 948 115 GLY CA C 43.6 0.2 1 490 948 115 GLY C C 170.1 0.2 1 491 949 116 VAL H H 8.24 0.01 1 492 949 116 VAL N N 122.60 0.03 1 493 949 116 VAL CA C 60.1 0.2 1 494 949 116 VAL C C 174.2 0.2 1 495 949 116 VAL CB C 35.6 0.2 1 496 950 117 PHE H H 8.93 0.01 1 497 950 117 PHE N N 119.63 0.03 1 498 950 117 PHE CA C 55.9 0.2 1 499 950 117 PHE C C 176.5 0.2 1 500 950 117 PHE CB C 40.3 0.2 1 501 951 118 SER H H 9.04 0.01 1 502 951 118 SER N N 116.77 0.03 1 503 951 118 SER CA C 58.2 0.2 1 504 951 118 SER C C 172.5 0.2 1 505 951 118 SER CB C 61.9 0.2 1 506 952 119 LEU H H 8.74 0.01 1 507 952 119 LEU N N 126.19 0.03 1 508 952 119 LEU CA C 55.0 0.2 1 509 952 119 LEU C C 172.7 0.2 1 510 952 119 LEU CB C 40.8 0.2 1 511 953 120 ILE H H 6.61 0.01 1 512 953 120 ILE N N 117.66 0.03 1 513 953 120 ILE CA C 59.1 0.2 1 514 953 120 ILE C C 174.1 0.2 1 515 953 120 ILE CB C 38.7 0.2 1 516 954 121 LEU H H 8.67 0.01 1 517 954 121 LEU N N 121.43 0.03 1 518 954 121 LEU CA C 49.9 0.2 1 519 954 121 LEU CB C 45.3 0.2 1 520 955 122 PRO CA C 61.3 0.2 1 521 955 122 PRO C C 175.5 0.2 1 522 955 122 PRO CB C 30.1 0.2 1 523 956 123 LEU H H 9.14 0.01 1 524 956 123 LEU N N 123.19 0.03 1 525 956 123 LEU CA C 52.8 0.2 1 526 956 123 LEU C C 177.1 0.2 1 527 956 123 LEU CB C 42.1 0.2 1 528 957 124 GLN H H 9.23 0.01 1 529 957 124 GLN N N 121.82 0.03 1 530 957 124 GLN CA C 53.3 0.2 1 531 957 124 GLN C C 176.1 0.2 1 532 957 124 GLN CB C 28.9 0.2 1 533 957 124 GLN CG C 33.3 0.2 1 534 957 124 GLN CD C 180.8 0.2 1 535 957 124 GLN NE2 N 113.28 0.03 1 536 957 124 GLN HE21 H 7.59 0.01 2 537 957 124 GLN HE22 H 6.84 0.01 2 538 958 125 ALA H H 8.20 0.01 1 539 958 125 ALA N N 122.12 0.03 1 540 958 125 ALA CA C 53.2 0.2 1 541 958 125 ALA C C 178.9 0.2 1 542 958 125 ALA CB C 17.3 0.2 1 543 959 126 GLY H H 8.99 0.01 1 544 959 126 GLY N N 112.43 0.03 1 545 959 126 GLY CA C 44.3 0.2 1 546 959 126 GLY C C 174.8 0.2 1 547 960 127 ASP H H 7.92 0.01 1 548 960 127 ASP N N 120.66 0.03 1 549 960 127 ASP CA C 55.0 0.2 1 550 960 127 ASP C C 175.2 0.2 1 551 960 127 ASP CB C 41.1 0.2 1 552 961 128 THR H H 7.51 0.01 1 553 961 128 THR N N 107.93 0.03 1 554 961 128 THR CA C 57.5 0.2 1 555 961 128 THR C C 175.6 0.2 1 556 961 128 THR CB C 70.6 0.2 1 557 962 129 VAL H H 9.45 0.01 1 558 962 129 VAL N N 120.48 0.03 1 559 962 129 VAL CA C 60.1 0.2 1 560 962 129 VAL C C 174.2 0.2 1 561 962 129 VAL CB C 34.7 0.2 1 562 963 130 CYS H H 8.58 0.01 1 563 963 130 CYS N N 119.83 0.03 1 564 963 130 CYS CA C 55.3 0.2 1 565 963 130 CYS C C 170.4 0.2 1 566 963 130 CYS CB C 31.2 0.2 1 567 964 131 VAL H H 9.85 0.01 1 568 964 131 VAL N N 121.19 0.03 1 569 964 131 VAL CA C 61.3 0.2 1 570 964 131 VAL C C 173.3 0.2 1 571 964 131 VAL CB C 31.9 0.2 1 572 965 132 ASP H H 9.32 0.01 1 573 965 132 ASP N N 127.10 0.03 1 574 965 132 ASP CA C 52.1 0.2 1 575 965 132 ASP C C 175.4 0.2 1 576 965 132 ASP CB C 40.5 0.2 1 577 966 133 LEU H H 8.64 0.01 1 578 966 133 LEU N N 126.77 0.03 1 579 966 133 LEU CA C 54.9 0.2 1 580 966 133 LEU C C 176.1 0.2 1 581 966 133 LEU CB C 42.9 0.2 1 582 967 134 VAL H H 8.98 0.01 1 583 967 134 VAL N N 128.46 0.03 1 584 967 134 VAL CA C 63.9 0.2 1 585 967 134 VAL C C 175.2 0.2 1 586 967 134 VAL CB C 32.3 0.2 1 587 968 135 MET H H 7.98 0.01 1 588 968 135 MET N N 116.05 0.03 1 589 968 135 MET CA C 55.0 0.2 1 590 968 135 MET C C 173.5 0.2 1 591 968 135 MET CB C 35.1 0.2 1 592 969 136 GLY H H 8.05 0.01 1 593 969 136 GLY N N 108.68 0.03 1 594 969 136 GLY CA C 43.6 0.2 1 595 969 136 GLY C C 172.2 0.2 1 596 970 137 GLN H H 7.95 0.01 1 597 970 137 GLN N N 114.94 0.03 1 598 970 137 GLN CA C 53.8 0.2 1 599 970 137 GLN C C 175.1 0.2 1 600 970 137 GLN CB C 30.1 0.2 1 601 971 138 LEU H H 7.90 0.01 1 602 971 138 LEU N N 118.52 0.03 1 603 971 138 LEU CA C 52.8 0.2 1 604 971 138 LEU C C 176.7 0.2 1 605 971 138 LEU CB C 42.7 0.2 1 606 972 139 ALA H H 9.26 0.01 1 607 972 139 ALA N N 123.33 0.03 1 608 972 139 ALA CA C 52.2 0.2 1 609 972 139 ALA C C 176.0 0.2 1 610 972 139 ALA CB C 20.2 0.2 1 611 973 140 HIS H H 7.66 0.01 1 612 973 140 HIS N N 123.02 0.03 1 613 973 140 HIS CA C 53.9 0.2 1 614 973 140 HIS C C 172.4 0.2 1 615 973 140 HIS CB C 32.5 0.2 1 616 974 141 SER H H 7.30 0.01 1 617 974 141 SER N N 112.05 0.03 1 618 974 141 SER CA C 57.2 0.2 1 619 974 141 SER C C 173.6 0.2 1 620 974 141 SER CB C 62.9 0.2 1 621 975 142 GLU H H 8.44 0.01 1 622 975 142 GLU N N 123.56 0.03 1 623 975 142 GLU CA C 58.5 0.2 1 624 975 142 GLU C C 177.1 0.2 1 625 975 142 GLU CB C 28.3 0.2 1 626 976 143 GLU H H 7.64 0.01 1 627 976 143 GLU N N 119.35 0.03 1 628 976 143 GLU CA C 53.0 0.2 1 629 976 143 GLU C C 174.0 0.2 1 630 976 143 GLU CB C 28.5 0.2 1 631 977 144 PRO CA C 62.2 0.2 1 632 977 144 PRO C C 177.3 0.2 1 633 977 144 PRO CB C 30.9 0.2 1 634 978 145 LEU H H 8.19 0.01 1 635 978 145 LEU N N 120.53 0.03 1 636 978 145 LEU CA C 54.5 0.2 1 637 978 145 LEU C C 173.6 0.2 1 638 978 145 LEU CB C 44.1 0.2 1 639 979 146 THR H H 8.28 0.01 1 640 979 146 THR N N 120.74 0.03 1 641 979 146 THR CA C 61.5 0.2 1 642 979 146 THR C C 174.3 0.2 1 643 979 146 THR CB C 71.5 0.2 1 644 980 147 ILE H H 9.34 0.01 1 645 980 147 ILE N N 127.59 0.03 1 646 980 147 ILE CA C 60.6 0.2 1 647 980 147 ILE C C 171.9 0.2 1 648 980 147 ILE CB C 43.1 0.2 1 649 981 148 PHE H H 8.85 0.01 1 650 981 148 PHE N N 129.39 0.03 1 651 981 148 PHE CA C 52.8 0.2 1 652 981 148 PHE C C 173.1 0.2 1 653 981 148 PHE CB C 40.5 0.2 1 654 982 149 SER H H 9.21 0.01 1 655 982 149 SER N N 120.72 0.03 1 656 982 149 SER CA C 56.2 0.2 1 657 982 149 SER C C 170.4 0.2 1 658 982 149 SER CB C 66.2 0.2 1 659 983 150 GLY H H 6.79 0.01 1 660 983 150 GLY N N 106.09 0.03 1 661 983 150 GLY CA C 44.6 0.2 1 662 983 150 GLY C C 171.2 0.2 1 663 984 151 ALA H H 8.66 0.01 1 664 984 151 ALA N N 116.86 0.03 1 665 984 151 ALA CA C 51.0 0.2 1 666 984 151 ALA C C 175.7 0.2 1 667 984 151 ALA CB C 22.2 0.2 1 668 985 152 LEU H H 8.27 0.01 1 669 985 152 LEU N N 122.84 0.03 1 670 985 152 LEU CA C 54.4 0.2 1 671 985 152 LEU C C 175.0 0.2 1 672 985 152 LEU CB C 41.4 0.2 1 673 986 153 LEU H H 8.70 0.01 1 674 986 153 LEU N N 127.98 0.03 1 675 986 153 LEU CA C 55.9 0.2 1 676 986 153 LEU C C 176.7 0.2 1 677 986 153 LEU CB C 41.0 0.2 1 678 987 154 TYR H H 6.58 0.01 1 679 987 154 TYR N N 108.79 0.03 1 680 987 154 TYR CA C 55.8 0.2 1 681 987 154 TYR C C 174.0 0.2 1 682 987 154 TYR CB C 37.7 0.2 1 683 988 155 GLY H H 8.85 0.01 1 684 988 155 GLY N N 107.24 0.03 1 685 988 155 GLY CA C 43.5 0.2 1 686 988 155 GLY C C 172.7 0.2 1 687 989 156 ASP H H 7.78 0.01 1 688 989 156 ASP N N 122.21 0.03 1 689 989 156 ASP CA C 52.3 0.2 1 690 989 156 ASP C C 175.8 0.2 1 691 989 156 ASP CB C 39.9 0.2 1 692 990 157 PRO CA C 63.2 0.2 1 693 990 157 PRO C C 177.3 0.2 1 694 990 157 PRO CB C 31.2 0.2 1 695 991 158 GLU H H 8.50 0.01 1 696 991 158 GLU N N 119.44 0.03 1 697 991 158 GLU CA C 56.3 0.2 1 698 991 158 GLU C C 176.7 0.2 1 699 991 158 GLU CB C 28.9 0.2 1 700 992 159 LEU H H 7.84 0.01 1 701 992 159 LEU N N 121.37 0.03 1 702 992 159 LEU CA C 54.8 0.2 1 703 992 159 LEU C C 177.3 0.2 1 704 992 159 LEU CB C 41.4 0.2 1 705 993 160 GLU H H 8.08 0.01 1 706 993 160 GLU N N 120.60 0.03 1 707 993 160 GLU CA C 56.2 0.2 1 708 993 160 GLU C C 176.0 0.2 1 709 993 160 GLU CB C 29.2 0.2 1 710 994 161 HIS CA C 55.3 0.2 1 711 994 161 HIS C C 173.9 0.2 1 712 994 161 HIS CB C 29.7 0.2 1 713 995 162 ALA H H 7.87 0.01 1 714 995 162 ALA N N 130.54 0.03 1 715 995 162 ALA CA C 53.3 0.2 1 716 995 162 ALA C C 170.2 0.2 1 717 995 162 ALA CB C 20.1 0.2 1 stop_ save_