data_6221 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments of the Resuscitation Promoting Factor (Rpf) domain of M. tuberculosis ; _BMRB_accession_number 6221 _BMRB_flat_file_name bmr6221.str _Entry_type original _Submission_date 2004-05-27 _Accession_date 2004-05-28 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; Studies of starved Micrococcus luteus has led to the identification of a secreted protein which resuscitated dormant cells allowing them to enter the cell cycle. This factor was named resuscitation promoting factor (Rpf) and was classified as the first bacterial cytokine (Mukamolova, Kaprelyants et al. 1998). Homologues of the rpf genes are widely distributed among the high G+C cohort of Gram-positive bacteria including the Mycobacterial pathogens M. tuberculosis and M. leprae (Mukamolova, Turapov et al. 2002). M. tuberculosis can spend many years dormant in human tissue so the mechanism of revival of dormant M. tuberculosis is of major medical interest. Knockout of the unique rpf gene in M. luteus has showed to be lethal (Mukamolova, Turapov et al. 2002) while in M. tuberculosis, which has five rpf genes, none of these individual genes was found to be essential suggesting a functional redundancy (Tufariello, Jacobs et al. 2004). However, in a genome wide transposon study the rpfB knockout caused slowing of growth (Sassetti, Boyd et al. 2003) and all five rpf homologues are expressed in M. tuberculosis obtained from extended-stationary-phase cultures suggesting the possibility that Rpf may play a role in the reactivation of quiescent bacilli. Recently, using sequence analysis and homology modelling, we predicted that the structure of the common domain of the Rpf proteins (~100 amino-acid) possess a lysozyme-like domain (Cohen-Gonsaud, Keep et al. 2004). ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cohen-Gonsaud Martin . . 2 Barthe Philippe . . 3 Keep Nicholas H. . 4 Roumestand Christian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 555 "13C chemical shifts" 300 "15N chemical shifts" 124 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-12-16 original BMRB . stop_ _Original_release_date 2004-05-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 15N and 13C Chemical Shifts Assignments of the Resuscitation Promoting Factor domain of Rv1009 from Mycobacterium tuberculosis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15614636 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cohen-Gonsaud Martin . . 2 Barthe Philippe . . 3 Pommier Francoise . . 4 Harris Richard . . 5 Driscoll Paul C. . 6 Keep Nicholas H. . 7 Roumestand Christian . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 30 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 373 _Page_last 374 _Year 2004 _Details . loop_ _Keyword 'M. tuberculosis' 'NMR assignments' Resuscitation Rpf stop_ save_ ################################## # Molecular system description # ################################## save_system_RpfBc _Saveframe_category molecular_system _Mol_system_name RpfBc _Abbreviation_common RpfBc _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'RpfBc domain from M. tuberculosis' $RpfBc 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_RpfBc _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Rpf domain' _Name_variant 'Rpf domain' _Abbreviation_common 'Rpf domain' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 108 _Mol_residue_sequence ; NVVVTPAHEAVVRVGTKPGT EVPPVIDGSIWDAIAGCEAG GNWAINTGNGYYGGVQFDQG TWEANGGLRYAPRADLATRE EQIAVAEVTRLRQGWGAWPV CAARAGAR ; loop_ _Residue_seq_code _Residue_label 1 ASN 2 VAL 3 VAL 4 VAL 5 THR 6 PRO 7 ALA 8 HIS 9 GLU 10 ALA 11 VAL 12 VAL 13 ARG 14 VAL 15 GLY 16 THR 17 LYS 18 PRO 19 GLY 20 THR 21 GLU 22 VAL 23 PRO 24 PRO 25 VAL 26 ILE 27 ASP 28 GLY 29 SER 30 ILE 31 TRP 32 ASP 33 ALA 34 ILE 35 ALA 36 GLY 37 CYS 38 GLU 39 ALA 40 GLY 41 GLY 42 ASN 43 TRP 44 ALA 45 ILE 46 ASN 47 THR 48 GLY 49 ASN 50 GLY 51 TYR 52 TYR 53 GLY 54 GLY 55 VAL 56 GLN 57 PHE 58 ASP 59 GLN 60 GLY 61 THR 62 TRP 63 GLU 64 ALA 65 ASN 66 GLY 67 GLY 68 LEU 69 ARG 70 TYR 71 ALA 72 PRO 73 ARG 74 ALA 75 ASP 76 LEU 77 ALA 78 THR 79 ARG 80 GLU 81 GLU 82 GLN 83 ILE 84 ALA 85 VAL 86 ALA 87 GLU 88 VAL 89 THR 90 ARG 91 LEU 92 ARG 93 GLN 94 GLY 95 TRP 96 GLY 97 ALA 98 TRP 99 PRO 100 VAL 101 CYS 102 ALA 103 ALA 104 ARG 105 ALA 106 GLY 107 ALA 108 ARG stop_ _Sequence_homology_query_date 2010-09-18 _Sequence_homology_query_revised_last_date 2009-10-07 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 1XSF 'Solution Structure Of A Resuscitation Promoting Factor Domain From Mycobacterium Tuberculosis' 100.00 108 100.00 100.00 2.82e-54 PDB 3EO5 'Crystal Structure Of The Resuscitation Promoting Factor Rpfb' 100.00 171 100.00 100.00 4.85e-55 DBJ BAH25329 'putative resuscitation-promoting factor [Mycobacterium bovis BCG str. Tokyo 172]' 100.00 362 98.15 98.15 7.55e-56 EMBL CAB08136 'Probable resuscitation-promoting factor rpfB [Mycobacterium tuberculosis H37Rv]' 100.00 362 100.00 100.00 5.27e-57 EMBL CAD93897 'Probable resuscitation-promoting factor rpfB [Mycobacterium bovis AF2122/97]' 100.00 362 98.15 98.15 7.55e-56 EMBL CAL71053 'Probable resuscitation-promoting factor rpfB [Mycobacterium bovis BCG str. Pasteur 1173P2]' 100.00 362 98.15 98.15 7.55e-56 GB AAK45288 'conserved hypothetical protein [Mycobacterium tuberculosis CDC1551]' 100.00 362 100.00 100.00 5.27e-57 GB ABQ72752 'putative resuscitation-promoting factor RpfB [Mycobacterium tuberculosis H37Ra]' 100.00 362 100.00 100.00 5.27e-57 GB ABR05371 'resuscitation-promoting factor rpfB [Mycobacterium tuberculosis F11]' 100.00 362 100.00 100.00 5.27e-57 GB ACT26067 'resuscitation-promoting factor rpfB [Mycobacterium tuberculosis KZN 1435]' 100.00 362 100.00 100.00 5.27e-57 GB EAY59373 'resuscitation-promoting factor rpfB [Mycobacterium tuberculosis C]' 100.00 362 100.00 100.00 4.31e-57 REF NP_215525 'resuscitation-promoting factor rpfB [Mycobacterium tuberculosis H37Rv]' 100.00 362 100.00 100.00 5.27e-57 REF NP_335474 'hypothetical protein MT1038 [Mycobacterium tuberculosis CDC1551]' 100.00 362 100.00 100.00 5.27e-57 REF NP_854693 'resuscitation-promoting factor rpfB [Mycobacterium bovis AF2122/97]' 100.00 362 98.15 98.15 7.55e-56 REF YP_001282314 'putative resuscitation-promoting factor RpfB [Mycobacterium tuberculosis H37Ra]' 100.00 362 100.00 100.00 5.27e-57 REF YP_001286973 'resuscitation-promoting factor rpfB [Mycobacterium tuberculosis F11]' 100.00 362 100.00 100.00 5.27e-57 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $RpfBc 'Mycobacterium tuberculosis' 83332 Actinobacteria Actinomycetales Mycobacterium tuberculosis H37rv stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $RpfBc 'recombinant technology' 'E. coli' Escherichia coli BL21 Rosetta(DE3) 'modified pET15b (with TEV-site)' 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 $RpfBc 0.5 mM '[U-95% 15N]' Na-Acetate 25 mM . beta-mercaptoethanol 5 mM . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $RpfBc 0.5 mM '[U-95% 13C; U-95% 15N]' Na-Acetate 25 mM . beta-mercaptoethanol 5 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'A cryogenic probe equipped the 500 MHz spectrometer.' save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HN(CA)CO_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label . save_ save_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 25 1 mM pH 4.6 0.1 pH temperature 293 0.2 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 C 13 'methyl protons' ppm 0 internal indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCA HN(CO)CA HNCACB CBCA(CO)NH HNCO HN(CA)CO '1H-15N NOESY' '1H-15N TOCSY' stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'RpfBc domain from M. tuberculosis' _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 ASN H H 8.477 0.01 1 2 . 1 ASN N N 120.470 0.1 1 3 . 1 ASN CA C 53.180 0.1 1 4 . 1 ASN HA H 4.742 0.01 1 5 . 1 ASN C C 175.370 0.1 1 6 . 1 ASN CB C 38.730 0.1 1 7 . 1 ASN HB2 H 2.806 0.01 2 8 . 1 ASN HB3 H 2.772 0.01 2 9 . 1 ASN ND2 N 112.264 0.1 1 10 . 1 ASN HD21 H 7.582 0.01 2 11 . 1 ASN HD22 H 6.873 0.01 2 12 . 2 VAL H H 8.020 0.01 1 13 . 2 VAL N N 120.250 0.1 1 14 . 2 VAL CA C 62.230 0.1 1 15 . 2 VAL HA H 4.098 0.01 1 16 . 2 VAL C C 176.500 0.1 1 17 . 2 VAL CB C 32.950 0.1 1 18 . 2 VAL HB H 2.029 0.01 1 19 . 2 VAL HG1 H 0.891 0.01 2 20 . 2 VAL HG2 H 0.921 0.01 2 21 . 3 VAL H H 8.293 0.01 1 22 . 3 VAL N N 125.320 0.1 1 23 . 3 VAL CA C 62.230 0.1 1 24 . 3 VAL HA H 4.112 0.01 1 25 . 3 VAL C C 176.400 0.1 1 26 . 3 VAL CB C 32.790 0.1 1 27 . 3 VAL HB H 2.007 0.01 1 28 . 3 VAL HG1 H 0.890 0.01 2 29 . 3 VAL HG2 H 0.920 0.01 2 30 . 4 VAL H H 8.356 0.01 1 31 . 4 VAL N N 125.500 0.1 1 32 . 4 VAL CA C 62.110 0.1 1 33 . 4 VAL HA H 4.180 0.01 1 34 . 4 VAL C C 176.470 0.1 1 35 . 4 VAL CB C 32.920 0.1 1 36 . 4 VAL HB H 2.013 0.01 1 37 . 4 VAL HG1 H 0.892 0.01 2 38 . 4 VAL HG2 H 0.919 0.01 2 39 . 5 THR H H 8.343 0.01 1 40 . 5 THR N N 121.430 0.1 1 41 . 5 THR CA C 59.750 0.1 1 42 . 5 THR HA H 4.589 0.01 1 43 . 5 THR C C 173.160 0.1 1 44 . 5 THR CB C 69.680 0.1 1 45 . 5 THR HB H 4.116 0.01 1 46 . 5 THR HG2 H 1.233 0.01 1 47 . 6 PRO CA C 63.050 0.1 1 48 . 6 PRO HA H 4.369 0.01 1 49 . 6 PRO C C 177.150 0.1 1 50 . 6 PRO CB C 32.110 0.1 1 51 . 6 PRO HB2 H 2.294 0.01 2 52 . 6 PRO HB3 H 1.855 0.01 2 53 . 6 PRO HG2 H 2.020 0.01 2 54 . 6 PRO HG3 H 1.946 0.01 2 55 . 6 PRO HD2 H 3.884 0.01 2 56 . 6 PRO HD3 H 3.713 0.01 2 57 . 7 ALA H H 8.382 0.01 1 58 . 7 ALA N N 123.960 0.1 1 59 . 7 ALA CA C 52.440 0.1 1 60 . 7 ALA HA H 4.222 0.01 1 61 . 7 ALA C C 178.230 0.1 1 62 . 7 ALA CB C 19.340 0.1 1 63 . 7 ALA HB H 1.340 0.01 1 64 . 8 HIS H H 8.452 0.01 1 65 . 8 HIS N N 117.130 0.1 1 66 . 8 HIS CA C 55.370 0.1 1 67 . 8 HIS HA H 4.652 0.01 1 68 . 8 HIS C C 174.850 0.1 1 69 . 8 HIS CB C 29.310 0.1 1 70 . 8 HIS HB2 H 3.246 0.01 2 71 . 8 HIS HB3 H 3.190 0.01 2 72 . 9 GLU H H 8.452 0.01 1 73 . 9 GLU N N 121.850 0.1 1 74 . 9 GLU CA C 56.290 0.1 1 75 . 9 GLU HA H 4.270 0.01 1 76 . 9 GLU C C 176.420 0.1 1 77 . 9 GLU CB C 30.350 0.1 1 78 . 9 GLU HB2 H 2.029 0.01 2 79 . 9 GLU HB3 H 1.913 0.01 2 80 . 9 GLU HG2 H 2.254 0.01 2 81 . 10 ALA H H 8.413 0.01 1 82 . 10 ALA N N 125.302 0.1 1 83 . 10 ALA CA C 52.500 0.1 1 84 . 10 ALA HA H 4.331 0.01 1 85 . 10 ALA C C 178.050 0.1 1 86 . 10 ALA CB C 19.230 0.1 1 87 . 10 ALA HB H 1.374 0.01 1 88 . 11 VAL H H 8.102 0.01 1 89 . 11 VAL N N 119.740 0.1 1 90 . 11 VAL CA C 62.100 0.1 1 91 . 11 VAL HA H 4.082 0.01 1 92 . 11 VAL C C 176.640 0.1 1 93 . 11 VAL CB C 32.920 0.1 1 94 . 11 VAL HB H 2.019 0.01 1 95 . 11 VAL HG1 H 0.900 0.01 2 96 . 11 VAL HG2 H 0.940 0.01 2 97 . 12 VAL H H 8.261 0.01 1 98 . 12 VAL N N 124.780 0.1 1 99 . 12 VAL CA C 61.940 0.1 1 100 . 12 VAL HA H 4.082 0.01 1 101 . 12 VAL C C 176.380 0.1 1 102 . 12 VAL CB C 32.990 0.1 1 103 . 12 VAL HB H 2.005 0.01 1 104 . 12 VAL HG1 H 0.890 0.01 2 105 . 12 VAL HG2 H 0.920 0.01 2 106 . 13 ARG H H 8.471 0.01 1 107 . 13 ARG N N 125.740 0.1 1 108 . 13 ARG CA C 52.540 0.1 1 109 . 13 ARG HA H 4.410 0.01 1 110 . 13 ARG C C 176.590 0.1 1 111 . 13 ARG CB C 31.100 0.1 1 112 . 13 ARG HB2 H 1.803 0.01 4 113 . 13 ARG HB3 H 1.803 0.01 4 114 . 13 ARG HG2 H 1.620 0.01 4 115 . 13 ARG HG3 H 1.582 0.01 4 116 . 13 ARG HD2 H 3.175 0.01 1 117 . 13 ARG HD3 H 3.175 0.01 1 118 . 13 ARG NE N 84.363 0.1 1 119 . 13 ARG HE H 7.235 0.01 1 120 . 14 VAL H H 8.288 0.01 1 121 . 14 VAL N N 122.240 0.1 1 122 . 14 VAL CA C 62.500 0.1 1 123 . 14 VAL HA H 4.120 0.01 1 124 . 14 VAL C C 177.040 0.1 1 125 . 14 VAL CB C 32.900 0.1 1 126 . 14 VAL HB H 2.066 0.01 1 127 . 14 VAL HG1 H 0.937 0.01 2 128 . 14 VAL HG2 H 0.968 0.01 2 129 . 15 GLY H H 8.560 0.01 1 130 . 15 GLY N N 112.565 0.1 1 131 . 15 GLY CA C 45.150 0.1 1 132 . 15 GLY HA2 H 3.983 0.01 2 133 . 15 GLY HA3 H 4.034 0.01 2 134 . 15 GLY C C 174.640 0.1 1 135 . 16 THR H H 8.057 0.01 1 136 . 16 THR N N 113.710 0.1 1 137 . 16 THR CA C 61.440 0.1 1 138 . 16 THR HA H 4.314 0.01 1 139 . 16 THR C C 174.990 0.1 1 140 . 16 THR CB C 70.070 0.1 1 141 . 16 THR HB H 4.161 0.01 1 142 . 16 THR HG2 H 1.180 0.01 1 143 . 17 LYS H H 8.441 0.01 1 144 . 17 LYS N N 124.950 0.1 1 145 . 17 LYS CA C 54.150 0.1 1 146 . 17 LYS HA H 4.638 0.01 1 147 . 17 LYS C C 178.020 0.1 1 148 . 17 LYS CB C 32.790 0.1 1 149 . 17 LYS HB2 H 1.828 0.01 4 150 . 17 LYS HB3 H 1.700 0.01 4 151 . 17 LYS HG2 H 1.476 0.01 4 152 . 17 LYS HD2 H 1.739 0.01 4 153 . 17 LYS HE2 H 2.950 0.01 2 154 . 17 LYS HE3 H 3.060 0.01 2 155 . 18 PRO CA C 63.390 0.1 1 156 . 18 PRO HA H 4.449 0.01 1 157 . 18 PRO C C 177.980 0.1 1 158 . 18 PRO CB C 31.820 0.1 1 159 . 18 PRO HB2 H 2.324 0.01 2 160 . 18 PRO HB3 H 1.961 0.01 2 161 . 18 PRO HG2 H 2.076 0.01 2 162 . 18 PRO HG3 H 2.041 0.01 2 163 . 18 PRO HD2 H 3.865 0.01 2 164 . 18 PRO HD3 H 3.667 0.01 2 165 . 19 GLY H H 8.649 0.01 1 166 . 19 GLY N N 109.710 0.1 1 167 . 19 GLY CA C 45.330 0.1 1 168 . 19 GLY HA2 H 3.994 0.01 2 169 . 19 GLY HA3 H 4.065 0.01 2 170 . 19 GLY C C 175.020 0.1 1 171 . 20 THR H H 7.981 0.01 1 172 . 20 THR N N 112.980 0.1 1 173 . 20 THR CA C 61.870 0.1 1 174 . 20 THR HA H 4.357 0.01 1 175 . 20 THR C C 174.990 0.1 1 176 . 20 THR CB C 69.800 0.1 1 177 . 20 THR HB H 4.240 0.01 1 178 . 20 THR HG2 H 1.194 0.01 1 179 . 21 GLU H H 8.610 0.01 1 180 . 21 GLU N N 123.600 0.1 1 181 . 21 GLU CA C 56.480 0.1 1 182 . 21 GLU HA H 4.350 0.01 1 183 . 21 GLU C C 176.570 0.1 1 184 . 21 GLU CB C 29.970 0.1 1 185 . 21 GLU HB2 H 2.031 0.01 2 186 . 21 GLU HB3 H 1.950 0.01 2 187 . 21 GLU HG2 H 2.266 0.01 2 188 . 22 VAL H H 8.299 0.01 1 189 . 22 VAL N N 123.460 0.1 1 190 . 22 VAL CA C 59.550 0.1 1 191 . 22 VAL HA H 4.425 0.01 1 192 . 22 VAL C C 174.430 0.1 1 193 . 22 VAL CB C 32.830 0.1 1 194 . 22 VAL HB H 2.031 0.01 1 195 . 22 VAL HG1 H 0.870 0.01 2 196 . 22 VAL HG2 H 0.920 0.01 2 197 . 23 PRO HA H 4.690 0.01 1 198 . 23 PRO HB2 H 2.270 0.01 2 199 . 23 PRO HB3 H 1.946 0.01 2 200 . 23 PRO HG2 H 2.056 0.01 2 201 . 23 PRO HG3 H 2.024 0.01 2 202 . 23 PRO HD2 H 3.891 0.01 2 203 . 23 PRO HD3 H 3.631 0.01 2 204 . 24 PRO CA C 62.800 0.1 1 205 . 24 PRO HA H 4.428 0.01 1 206 . 24 PRO C C 178.000 0.1 1 207 . 24 PRO CB C 31.820 0.1 1 208 . 24 PRO HB2 H 2.284 0.01 2 209 . 24 PRO HB3 H 1.850 0.01 2 210 . 24 PRO HG2 H 2.053 0.01 2 211 . 24 PRO HG3 H 2.010 0.01 2 212 . 24 PRO HD2 H 3.666 0.01 2 213 . 24 PRO HD3 H 3.900 0.01 2 214 . 25 VAL H H 8.242 0.01 1 215 . 25 VAL N N 120.570 0.1 1 216 . 25 VAL CA C 62.290 0.1 1 217 . 25 VAL HA H 4.076 0.01 1 218 . 25 VAL C C 176.590 0.1 1 219 . 25 VAL CB C 32.860 0.1 1 220 . 25 VAL HB H 2.017 0.01 1 221 . 25 VAL HG1 H 0.931 0.01 2 222 . 25 VAL HG2 H 0.966 0.01 2 223 . 26 ILE H H 8.610 0.01 1 224 . 26 ILE N N 126.719 0.1 1 225 . 26 ILE CA C 60.270 0.1 1 226 . 26 ILE HA H 4.265 0.01 1 227 . 26 ILE C C 175.980 0.1 1 228 . 26 ILE CB C 38.460 0.1 1 229 . 26 ILE HB H 1.953 0.01 1 230 . 26 ILE HG12 H 1.447 0.01 4 231 . 26 ILE HD1 H 0.835 0.01 4 232 . 27 ASP H H 8.426 0.01 1 233 . 27 ASP N N 122.790 0.1 1 234 . 27 ASP CA C 54.430 0.1 1 235 . 27 ASP HA H 4.646 0.01 1 236 . 27 ASP C C 177.390 0.1 1 237 . 27 ASP CB C 41.140 0.1 1 238 . 27 ASP HB2 H 2.844 0.01 2 239 . 27 ASP HB3 H 2.783 0.01 2 240 . 28 GLY H H 8.676 0.01 1 241 . 28 GLY N N 109.131 0.1 1 242 . 28 GLY CA C 47.020 0.1 1 243 . 28 GLY HA2 H 3.902 0.01 2 244 . 28 GLY HA3 H 3.941 0.01 2 245 . 28 GLY C C 175.090 0.1 1 246 . 29 SER H H 8.502 0.01 1 247 . 29 SER N N 114.960 0.1 1 248 . 29 SER CA C 60.140 0.1 1 249 . 29 SER HA H 4.421 0.01 1 250 . 29 SER C C 178.070 0.1 1 251 . 29 SER CB C 63.460 0.1 1 252 . 29 SER HB2 H 3.977 0.01 2 253 . 29 SER HB3 H 4.008 0.01 2 254 . 30 ILE H H 8.032 0.01 1 255 . 30 ILE N N 124.920 0.1 1 256 . 30 ILE CA C 63.110 0.1 1 257 . 30 ILE HA H 3.876 0.01 1 258 . 30 ILE C C 177.670 0.1 1 259 . 30 ILE CB C 36.950 0.1 1 260 . 30 ILE HB H 1.647 0.01 1 261 . 30 ILE HG2 H 0.092 0.01 1 262 . 30 ILE HG12 H 1.151 0.01 2 263 . 30 ILE HG13 H 0.848 0.01 2 264 . 30 ILE HD1 H 0.509 0.01 1 265 . 31 TRP H H 7.206 0.01 1 266 . 31 TRP N N 120.660 0.1 1 267 . 31 TRP CA C 59.420 0.1 1 268 . 31 TRP HA H 4.429 0.01 1 269 . 31 TRP C C 179.200 0.1 1 270 . 31 TRP CB C 29.900 0.1 1 271 . 31 TRP HB2 H 3.125 0.01 2 272 . 31 TRP HB3 H 3.391 0.01 2 273 . 31 TRP HD1 H 7.210 0.01 1 274 . 31 TRP NE1 N 128.967 0.1 1 275 . 31 TRP HE1 H 10.465 0.01 1 276 . 31 TRP HE3 H 6.572 0.01 1 277 . 31 TRP HZ2 H 7.117 0.01 1 278 . 31 TRP HZ3 H 7.127 0.01 1 279 . 31 TRP HH2 H 5.543 0.01 1 280 . 32 ASP H H 8.413 0.01 1 281 . 32 ASP N N 117.842 0.1 1 282 . 32 ASP CA C 57.960 0.1 1 283 . 32 ASP HA H 4.838 0.01 1 284 . 32 ASP C C 180.040 0.1 1 285 . 32 ASP CB C 40.420 0.1 1 286 . 32 ASP HB2 H 2.815 0.01 2 287 . 32 ASP HB3 H 2.765 0.01 2 288 . 33 ALA H H 7.657 0.01 1 289 . 33 ALA N N 124.890 0.1 1 290 . 33 ALA CA C 54.980 0.1 1 291 . 33 ALA HA H 4.251 0.01 1 292 . 33 ALA C C 182.210 0.1 1 293 . 33 ALA CB C 18.050 0.1 1 294 . 33 ALA HB H 1.522 0.01 1 295 . 34 ILE H H 8.529 0.01 1 296 . 34 ILE N N 122.150 0.1 1 297 . 34 ILE CA C 66.680 0.1 1 298 . 34 ILE HA H 3.399 0.01 1 299 . 34 ILE C C 178.260 0.1 1 300 . 34 ILE CB C 37.060 0.1 1 301 . 35 ALA H H 8.801 0.01 1 302 . 35 ALA N N 122.840 0.1 1 303 . 35 ALA CA C 54.300 0.1 1 304 . 35 ALA HA H 4.315 0.01 1 305 . 35 ALA C C 183.240 0.1 1 306 . 35 ALA CB C 18.690 0.1 1 307 . 35 ALA HB H 0.482 0.01 1 308 . 36 GLY H H 8.286 0.01 1 309 . 36 GLY N N 109.530 0.1 1 310 . 36 GLY CA C 47.390 0.1 1 311 . 36 GLY HA2 H 3.837 0.01 2 312 . 36 GLY HA3 H 3.513 0.01 2 313 . 36 GLY C C 174.860 0.1 1 314 . 37 CYS H H 7.276 0.01 1 315 . 37 CYS N N 121.100 0.1 1 316 . 37 CYS CA C 58.020 0.1 1 317 . 37 CYS HA H 4.315 0.01 1 318 . 37 CYS C C 176.430 0.1 1 319 . 37 CYS CB C 38.330 0.1 1 320 . 37 CYS HB2 H 3.211 0.01 2 321 . 37 CYS HB3 H 3.134 0.01 2 322 . 38 GLU H H 9.252 0.01 1 323 . 38 GLU N N 118.750 0.1 1 324 . 38 GLU CA C 57.650 0.1 1 325 . 38 GLU HA H 4.098 0.01 1 326 . 38 GLU C C 178.690 0.1 1 327 . 38 GLU CB C 29.290 0.1 1 328 . 38 GLU HB2 H 2.074 0.01 2 329 . 38 GLU HB3 H 1.761 0.01 2 330 . 38 GLU HG2 H 2.533 0.01 2 331 . 38 GLU HG3 H 2.220 0.01 2 332 . 39 ALA H H 7.790 0.01 1 333 . 39 ALA N N 117.940 0.1 1 334 . 39 ALA CA C 51.660 0.1 1 335 . 39 ALA HA H 4.586 0.01 1 336 . 39 ALA C C 179.190 0.1 1 337 . 39 ALA CB C 22.350 0.1 1 338 . 39 ALA HB H 1.354 0.01 1 339 . 40 GLY H H 7.708 0.01 1 340 . 40 GLY N N 111.610 0.1 1 341 . 40 GLY CA C 47.310 0.1 1 342 . 40 GLY HA2 H 3.898 0.01 2 343 . 40 GLY HA3 H 4.140 0.01 2 344 . 40 GLY C C 175.800 0.1 1 345 . 41 GLY H H 7.892 0.01 1 346 . 41 GLY N N 104.580 0.1 1 347 . 41 GLY CA C 44.750 0.1 1 348 . 41 GLY HA2 H 3.121 0.01 1 349 . 41 GLY HA3 H 4.126 0.01 1 350 . 41 GLY C C 172.450 0.1 1 351 . 42 ASN H H 7.090 0.01 1 352 . 42 ASN N N 116.400 0.1 1 353 . 42 ASN CA C 51.190 0.1 1 354 . 42 ASN HA H 4.878 0.01 1 355 . 42 ASN C C 176.030 0.1 1 356 . 42 ASN CB C 37.520 0.1 1 357 . 42 ASN HB2 H 3.218 0.01 2 358 . 42 ASN HB3 H 2.744 0.01 2 359 . 42 ASN ND2 N 109.485 0.1 1 360 . 42 ASN HD21 H 7.742 0.01 2 361 . 42 ASN HD22 H 7.063 0.01 2 362 . 43 TRP H H 8.580 0.01 1 363 . 43 TRP N N 123.914 0.1 1 364 . 43 TRP CA C 60.830 0.1 1 365 . 43 TRP HA H 3.850 0.01 1 366 . 43 TRP C C 175.810 0.1 1 367 . 43 TRP CB C 27.570 0.1 1 368 . 43 TRP HB2 H 3.524 0.01 2 369 . 43 TRP HB3 H 3.111 0.01 2 370 . 43 TRP HD1 H 7.511 0.01 1 371 . 43 TRP NE1 N 129.377 0.1 1 372 . 43 TRP HE1 H 10.490 0.01 1 373 . 43 TRP HE3 H 7.758 0.01 1 374 . 43 TRP HZ2 H 7.587 0.01 1 375 . 43 TRP HZ3 H 6.875 0.01 1 376 . 43 TRP HH2 H 6.817 0.01 1 377 . 44 ALA H H 7.990 0.01 1 378 . 44 ALA N N 119.840 0.1 1 379 . 44 ALA CA C 50.360 0.1 1 380 . 44 ALA HA H 5.113 0.01 1 381 . 44 ALA C C 178.320 0.1 1 382 . 44 ALA CB C 19.450 0.1 1 383 . 44 ALA HB H 1.514 0.01 1 384 . 45 ILE H H 6.818 0.01 1 385 . 45 ILE N N 121.440 0.1 1 386 . 45 ILE CA C 63.900 0.1 1 387 . 45 ILE HA H 3.784 0.01 1 388 . 45 ILE C C 173.600 0.1 1 389 . 45 ILE CB C 38.880 0.1 1 390 . 45 ILE HB H 1.832 0.01 1 391 . 45 ILE HG2 H 0.767 0.01 1 392 . 45 ILE HG12 H 1.369 0.01 2 393 . 45 ILE HG13 H 1.329 0.01 2 394 . 45 ILE HD1 H 0.902 0.01 1 395 . 46 ASN H H 8.438 0.01 1 396 . 46 ASN N N 121.700 0.1 1 397 . 46 ASN CA C 52.680 0.1 1 398 . 46 ASN HA H 4.767 0.01 1 399 . 46 ASN C C 176.300 0.1 1 400 . 46 ASN CB C 37.790 0.1 1 401 . 46 ASN HB2 H 3.089 0.01 2 402 . 46 ASN HB3 H 2.936 0.01 2 403 . 46 ASN ND2 N 108.846 0.1 1 404 . 46 ASN HD21 H 7.270 0.01 2 405 . 46 ASN HD22 H 7.210 0.01 2 406 . 47 THR H H 9.043 0.01 1 407 . 47 THR N N 113.710 0.1 1 408 . 47 THR CA C 61.640 0.1 1 409 . 47 THR HA H 4.386 0.01 1 410 . 47 THR C C 176.830 0.1 1 411 . 47 THR CB C 69.490 0.1 1 412 . 47 THR HB H 4.523 0.01 1 413 . 47 THR HG2 H 1.253 0.01 1 414 . 48 GLY H H 8.591 0.01 1 415 . 48 GLY N N 110.810 0.1 1 416 . 48 GLY CA C 45.840 0.1 1 417 . 48 GLY HA2 H 4.240 0.01 2 418 . 48 GLY HA3 H 3.937 0.01 2 419 . 48 GLY C C 175.080 0.1 1 420 . 49 ASN H H 7.889 0.01 1 421 . 49 ASN N N 117.800 0.1 1 422 . 49 ASN CA C 52.190 0.1 1 423 . 49 ASN HA H 4.625 0.01 1 424 . 49 ASN C C 176.030 0.1 1 425 . 49 ASN CB C 38.250 0.1 1 426 . 49 ASN HB2 H 3.310 0.01 2 427 . 49 ASN HB3 H 2.708 0.01 2 428 . 49 ASN ND2 N 108.521 0.1 1 429 . 49 ASN HD21 H 7.502 0.01 2 430 . 49 ASN HD22 H 6.998 0.01 2 431 . 50 GLY H H 8.210 0.01 1 432 . 50 GLY N N 107.450 0.1 1 433 . 50 GLY CA C 44.650 0.1 1 434 . 50 GLY HA2 H 3.302 0.01 2 435 . 50 GLY HA3 H 3.946 0.01 2 436 . 50 GLY C C 172.710 0.1 1 437 . 51 TYR H H 7.543 0.01 1 438 . 51 TYR N N 117.410 0.1 1 439 . 51 TYR CA C 55.950 0.1 1 440 . 51 TYR HA H 4.867 0.01 1 441 . 51 TYR C C 177.010 0.1 1 442 . 51 TYR CB C 41.140 0.1 1 443 . 51 TYR HB2 H 2.476 0.01 2 444 . 51 TYR HB3 H 2.124 0.01 2 445 . 51 TYR HD1 H 6.919 0.01 3 446 . 51 TYR HE1 H 6.861 0.01 3 447 . 52 TYR H H 9.240 0.01 1 448 . 52 TYR N N 117.230 0.1 1 449 . 52 TYR CA C 58.260 0.1 1 450 . 52 TYR HA H 4.927 0.01 1 451 . 52 TYR C C 177.360 0.1 1 452 . 52 TYR CB C 42.870 0.1 1 453 . 52 TYR HB2 H 2.736 0.01 2 454 . 52 TYR HB3 H 3.290 0.01 2 455 . 52 TYR HD1 H 7.104 0.01 3 456 . 52 TYR HE1 H 6.744 0.01 3 457 . 53 GLY H H 9.174 0.01 1 458 . 53 GLY N N 110.000 0.1 1 459 . 53 GLY CA C 45.200 0.1 1 460 . 53 GLY HA2 H 4.014 0.01 2 461 . 53 GLY HA3 H 4.102 0.01 2 462 . 53 GLY C C 175.940 0.1 1 463 . 54 GLY H H 8.510 0.01 1 464 . 54 GLY N N 106.500 0.1 1 465 . 54 GLY CA C 47.000 0.1 1 466 . 54 GLY C C 172.160 0.1 1 467 . 55 VAL H H 8.590 0.01 1 468 . 55 VAL N N 104.690 0.1 1 469 . 55 VAL CA C 59.040 0.1 1 470 . 55 VAL HA H 4.283 0.01 1 471 . 55 VAL C C 175.440 0.1 1 472 . 55 VAL CB C 30.170 0.1 1 473 . 55 VAL HB H 2.213 0.01 1 474 . 55 VAL HG1 H 0.617 0.01 2 475 . 55 VAL HG2 H 0.663 0.01 2 476 . 56 GLN H H 7.733 0.01 1 477 . 56 GLN N N 112.970 0.1 1 478 . 56 GLN CA C 55.510 0.1 1 479 . 56 GLN HA H 3.474 0.01 1 480 . 56 GLN C C 175.940 0.1 1 481 . 56 GLN CB C 26.400 0.1 1 482 . 56 GLN NE2 N 111.895 0.1 1 483 . 56 GLN HE21 H 7.496 0.01 2 484 . 56 GLN HE22 H 6.814 0.01 2 485 . 57 PHE H H 7.568 0.01 1 486 . 57 PHE N N 116.710 0.1 1 487 . 57 PHE CA C 59.670 0.1 1 488 . 57 PHE HA H 4.945 0.01 1 489 . 57 PHE C C 180.330 0.1 1 490 . 57 PHE CB C 41.850 0.1 1 491 . 57 PHE HB2 H 3.791 0.01 2 492 . 57 PHE HB3 H 2.797 0.01 2 493 . 57 PHE HD1 H 7.793 0.01 3 494 . 57 PHE HE1 H 7.677 0.01 3 495 . 57 PHE HZ H 7.166 0.01 1 496 . 58 ASP H H 9.017 0.01 1 497 . 58 ASP N N 120.220 0.1 1 498 . 58 ASP CA C 52.470 0.1 1 499 . 58 ASP HA H 5.387 0.01 1 500 . 58 ASP C C 176.980 0.1 1 501 . 58 ASP CB C 41.260 0.1 1 502 . 58 ASP HB2 H 3.171 0.01 2 503 . 58 ASP HB3 H 2.833 0.01 2 504 . 59 GLN H H 9.430 0.01 1 505 . 59 GLN N N 121.600 0.1 1 506 . 59 GLN CA C 58.800 0.1 1 507 . 59 GLN HA H 4.133 0.01 1 508 . 59 GLN C C 179.240 0.1 1 509 . 59 GLN CB C 27.550 0.1 1 510 . 59 GLN HB2 H 2.306 0.01 2 511 . 59 GLN HB3 H 1.964 0.01 2 512 . 59 GLN HG2 H 2.478 0.01 2 513 . 59 GLN HG3 H 2.444 0.01 2 514 . 59 GLN NE2 N 112.363 0.1 1 515 . 59 GLN HE21 H 8.854 0.01 2 516 . 59 GLN HE22 H 7.486 0.01 2 517 . 60 GLY H H 8.776 0.01 1 518 . 60 GLY N N 106.100 0.1 1 519 . 60 GLY CA C 47.320 0.1 1 520 . 60 GLY HA2 H 3.880 0.01 2 521 . 60 GLY HA3 H 3.976 0.01 2 522 . 60 GLY C C 177.940 0.1 1 523 . 61 THR H H 8.653 0.01 1 524 . 61 THR N N 120.878 0.1 1 525 . 61 THR CA C 67.140 0.1 1 526 . 61 THR HA H 3.994 0.01 1 527 . 61 THR C C 177.160 0.1 1 528 . 61 THR HB H 4.457 0.01 1 529 . 61 THR HG2 H 1.415 0.01 1 530 . 62 TRP H H 8.130 0.01 1 531 . 62 TRP N N 122.310 0.1 1 532 . 62 TRP CA C 60.460 0.1 1 533 . 62 TRP HA H 3.841 0.01 1 534 . 62 TRP C C 177.860 0.1 1 535 . 62 TRP CB C 30.460 0.1 1 536 . 62 TRP HB2 H 3.477 0.01 2 537 . 62 TRP HB3 H 3.086 0.01 2 538 . 62 TRP HD1 H 6.752 0.01 1 539 . 62 TRP NE1 N 127.031 0.1 1 540 . 62 TRP HE1 H 9.409 0.01 1 541 . 62 TRP HE3 H 6.185 0.01 1 542 . 62 TRP HZ2 H 7.190 0.01 1 543 . 62 TRP HZ3 H 7.917 0.01 1 544 . 62 TRP HH2 H 7.676 0.01 1 545 . 63 GLU H H 8.397 0.01 1 546 . 63 GLU N N 114.105 0.1 1 547 . 63 GLU CA C 59.270 0.1 1 548 . 63 GLU HA H 3.699 0.01 1 549 . 63 GLU C C 181.210 0.1 1 550 . 63 GLU CB C 29.270 0.1 1 551 . 64 ALA H H 8.586 0.01 1 552 . 64 ALA N N 121.345 0.1 1 553 . 64 ALA CA C 54.610 0.1 1 554 . 64 ALA HA H 4.133 0.01 1 555 . 64 ALA C C 179.110 0.1 1 556 . 64 ALA CB C 18.780 0.1 1 557 . 64 ALA HB H 1.490 0.01 1 558 . 65 ASN H H 7.117 0.01 1 559 . 65 ASN N N 112.410 0.1 1 560 . 65 ASN CA C 52.770 0.1 1 561 . 65 ASN HA H 4.790 0.01 1 562 . 65 ASN C C 174.310 0.1 1 563 . 65 ASN CB C 39.870 0.1 1 564 . 65 ASN HB2 H 2.926 0.01 2 565 . 65 ASN HB3 H 2.284 0.01 2 566 . 65 ASN ND2 N 115.387 0.1 1 567 . 65 ASN HD21 H 7.684 0.01 2 568 . 65 ASN HD22 H 7.293 0.01 2 569 . 66 GLY H H 7.019 0.01 1 570 . 66 GLY N N 103.680 0.1 1 571 . 66 GLY CA C 45.780 0.1 1 572 . 66 GLY HA2 H 4.010 0.01 2 573 . 66 GLY HA3 H 3.666 0.01 2 574 . 66 GLY C C 176.770 0.1 1 575 . 67 GLY H H 8.108 0.01 1 576 . 67 GLY N N 107.180 0.1 1 577 . 67 GLY CA C 45.920 0.1 1 578 . 67 GLY C C 175.620 0.1 1 579 . 68 LEU H H 8.405 0.01 1 580 . 68 LEU N N 115.720 0.1 1 581 . 68 LEU CA C 56.200 0.1 1 582 . 68 LEU HA H 4.314 0.01 1 583 . 68 LEU C C 179.750 0.1 1 584 . 68 LEU CB C 39.960 0.1 1 585 . 68 LEU HB2 H 1.654 0.01 2 586 . 68 LEU HB3 H 1.540 0.01 2 587 . 68 LEU HD1 H 0.998 0.01 2 588 . 68 LEU HD2 H 0.845 0.01 2 589 . 68 LEU HG H 1.315 0.01 1 590 . 69 ARG H H 7.099 0.01 1 591 . 69 ARG N N 116.690 0.1 1 592 . 69 ARG CA C 57.680 0.1 1 593 . 69 ARG HA H 3.784 0.01 1 594 . 69 ARG C C 176.950 0.1 1 595 . 69 ARG CB C 29.830 0.1 1 596 . 69 ARG HB2 H 1.312 0.01 2 597 . 69 ARG HB3 H 1.322 0.01 2 598 . 69 ARG HG2 H 1.055 0.01 2 599 . 69 ARG HG3 H 1.021 0.01 2 600 . 69 ARG HD2 H 2.815 0.01 2 601 . 69 ARG HD3 H 2.783 0.01 2 602 . 69 ARG NE N 84.102 0.1 1 603 . 69 ARG HE H 6.932 0.01 1 604 . 70 TYR H H 7.768 0.01 1 605 . 70 TYR N N 116.560 0.1 1 606 . 70 TYR CA C 58.080 0.1 1 607 . 70 TYR HA H 4.756 0.01 1 608 . 70 TYR C C 176.510 0.1 1 609 . 70 TYR CB C 39.730 0.1 1 610 . 70 TYR HB2 H 2.936 0.01 2 611 . 70 TYR HB3 H 3.294 0.01 2 612 . 70 TYR HD1 H 6.924 0.01 3 613 . 70 TYR HE1 H 6.656 0.01 3 614 . 71 ALA H H 8.625 0.01 1 615 . 71 ALA N N 118.280 0.1 1 616 . 71 ALA CA C 51.710 0.1 1 617 . 71 ALA HA H 4.831 0.01 1 618 . 71 ALA C C 176.880 0.1 1 619 . 71 ALA CB C 21.190 0.1 1 620 . 71 ALA HB H 1.518 0.01 1 621 . 72 PRO CA C 64.580 0.1 1 622 . 72 PRO HA H 4.330 0.01 1 623 . 72 PRO C C 176.160 0.1 1 624 . 72 PRO CB C 32.620 0.1 1 625 . 72 PRO HB2 H 2.448 0.01 2 626 . 72 PRO HB3 H 1.696 0.01 2 627 . 72 PRO HG2 H 2.044 0.01 2 628 . 72 PRO HG3 H 1.994 0.01 2 629 . 72 PRO HD2 H 3.912 0.01 2 630 . 72 PRO HD3 H 3.556 0.01 2 631 . 73 ARG H H 6.731 0.01 1 632 . 73 ARG N N 108.850 0.1 1 633 . 73 ARG CA C 53.420 0.1 1 634 . 73 ARG HA H 3.960 0.01 1 635 . 73 ARG C C 177.030 0.1 1 636 . 73 ARG CB C 38.810 0.1 1 637 . 73 ARG HB2 H 1.376 0.01 4 638 . 73 ARG HB3 H 1.260 0.01 4 639 . 73 ARG HG2 H 0.803 0.01 4 640 . 73 ARG HG3 H 1.116 0.01 4 641 . 73 ARG HD2 H 2.902 0.01 2 642 . 73 ARG HD3 H 2.939 0.01 2 643 . 73 ARG NE N 84.478 0.1 1 644 . 73 ARG HE H 9.188 0.01 1 645 . 74 ALA H H 7.504 0.01 1 646 . 74 ALA N N 121.230 0.1 1 647 . 74 ALA CA C 54.570 0.1 1 648 . 74 ALA HA H 3.960 0.01 1 649 . 74 ALA C C 177.910 0.1 1 650 . 74 ALA CB C 21.200 0.1 1 651 . 74 ALA HB H 0.826 0.01 1 652 . 75 ASP H H 8.706 0.01 1 653 . 75 ASP N N 105.510 0.1 1 654 . 75 ASP CA C 55.760 0.1 1 655 . 75 ASP HA H 4.358 0.01 1 656 . 75 ASP C C 176.080 0.1 1 657 . 75 ASP CB C 38.750 0.1 1 658 . 75 ASP HB2 H 2.525 0.01 2 659 . 75 ASP HB3 H 2.625 0.01 2 660 . 76 LEU H H 6.709 0.01 1 661 . 76 LEU N N 115.890 0.1 1 662 . 76 LEU CA C 53.940 0.1 1 663 . 76 LEU HA H 4.357 0.01 1 664 . 76 LEU C C 176.350 0.1 1 665 . 76 LEU CB C 42.860 0.1 1 666 . 76 LEU HB2 H 1.798 0.01 2 667 . 76 LEU HB3 H 1.747 0.01 2 668 . 76 LEU HD1 H 1.117 0.01 2 669 . 76 LEU HD2 H 0.806 0.01 2 670 . 76 LEU HG H 1.386 0.01 1 671 . 77 ALA H H 7.302 0.01 1 672 . 77 ALA N N 123.720 0.1 1 673 . 77 ALA CA C 49.930 0.1 1 674 . 77 ALA HA H 4.826 0.01 1 675 . 77 ALA C C 178.500 0.1 1 676 . 77 ALA CB C 21.500 0.1 1 677 . 77 ALA HB H 1.808 0.01 1 678 . 78 THR H H 8.779 0.01 1 679 . 78 THR N N 113.090 0.1 1 680 . 78 THR CA C 61.500 0.1 1 681 . 78 THR HA H 4.214 0.01 1 682 . 78 THR C C 175.830 0.1 1 683 . 78 THR CB C 70.920 0.1 1 684 . 78 THR HB H 4.609 0.01 1 685 . 78 THR HG2 H 1.317 0.01 1 686 . 79 ARG H H 8.908 0.01 1 687 . 79 ARG N N 121.450 0.1 1 688 . 79 ARG CA C 59.210 0.1 1 689 . 79 ARG HA H 3.255 0.01 1 690 . 79 ARG C C 176.810 0.1 1 691 . 79 ARG CB C 29.240 0.1 1 692 . 79 ARG HB2 H 0.565 0.01 4 693 . 79 ARG HB3 H 0.303 0.01 4 694 . 79 ARG HG2 H 1.266 0.01 4 695 . 79 ARG HG3 H 0.960 0.01 4 696 . 79 ARG HD2 H 2.637 0.01 2 697 . 79 ARG HD3 H 2.259 0.01 2 698 . 79 ARG NE N 85.475 0.1 1 699 . 79 ARG HE H 8.355 0.01 1 700 . 80 GLU H H 8.171 0.01 1 701 . 80 GLU N N 113.960 0.1 1 702 . 80 GLU CA C 61.020 0.1 1 703 . 80 GLU HA H 3.464 0.01 1 704 . 80 GLU C C 179.870 0.1 1 705 . 80 GLU CB C 28.520 0.1 1 706 . 80 GLU HB2 H 1.937 0.01 2 707 . 80 GLU HB3 H 1.745 0.01 2 708 . 80 GLU HG2 H 2.425 0.01 2 709 . 80 GLU HG3 H 2.397 0.01 2 710 . 81 GLU H H 7.560 0.01 1 711 . 81 GLU N N 121.160 0.1 1 712 . 81 GLU CA C 58.680 0.1 1 713 . 81 GLU HA H 3.281 0.01 1 714 . 81 GLU C C 178.070 0.1 1 715 . 81 GLU CB C 29.990 0.1 1 716 . 81 GLU HB2 H 1.931 0.01 2 717 . 81 GLU HB3 H 1.801 0.01 2 718 . 81 GLU HG2 H 2.386 0.01 2 719 . 81 GLU HG3 H 2.127 0.01 2 720 . 82 GLN H H 8.628 0.01 1 721 . 82 GLN N N 117.682 0.1 1 722 . 82 GLN CA C 61.110 0.1 1 723 . 82 GLN HA H 4.308 0.01 1 724 . 82 GLN C C 179.650 0.1 1 725 . 82 GLN CB C 30.100 0.1 1 726 . 82 GLN HB2 H 1.931 0.01 2 727 . 82 GLN HB3 H 2.292 0.01 2 728 . 82 GLN HG2 H 2.749 0.01 2 729 . 82 GLN HG3 H 2.515 0.01 2 730 . 82 GLN NE2 N 116.030 0.1 1 731 . 82 GLN HE21 H 8.255 0.01 2 732 . 82 GLN HE22 H 6.985 0.01 2 733 . 83 ILE H H 8.375 0.01 1 734 . 83 ILE N N 118.524 0.1 1 735 . 83 ILE CA C 65.750 0.1 1 736 . 83 ILE HA H 2.910 0.01 1 737 . 83 ILE C C 177.030 0.1 1 738 . 83 ILE CB C 37.730 0.1 1 739 . 83 ILE HB H 1.588 0.01 4 740 . 83 ILE HG2 H 0.418 0.01 4 741 . 83 ILE HG12 H 1.403 0.01 4 742 . 83 ILE HG13 H 0.562 0.01 4 743 . 83 ILE HD1 H 0.314 0.01 4 744 . 84 ALA H H 7.562 0.01 1 745 . 84 ALA N N 122.060 0.1 1 746 . 84 ALA CA C 55.630 0.1 1 747 . 84 ALA HA H 3.950 0.01 1 748 . 84 ALA C C 181.950 0.1 1 749 . 84 ALA CB C 17.160 0.1 1 750 . 84 ALA HB H 1.469 0.01 1 751 . 85 VAL H H 7.701 0.01 1 752 . 85 VAL N N 118.020 0.1 1 753 . 85 VAL CA C 65.710 0.1 1 754 . 85 VAL HA H 3.643 0.01 1 755 . 85 VAL C C 180.190 0.1 1 756 . 85 VAL CB C 31.510 0.1 1 757 . 85 VAL HB H 2.069 0.01 1 758 . 85 VAL HG1 H 0.425 0.01 1 759 . 85 VAL HG2 H 0.525 0.01 1 760 . 86 ALA H H 9.189 0.01 1 761 . 86 ALA N N 129.610 0.1 1 762 . 86 ALA CA C 56.370 0.1 1 763 . 86 ALA HA H 4.280 0.01 1 764 . 86 ALA C C 179.440 0.1 1 765 . 86 ALA CB C 16.450 0.1 1 766 . 86 ALA HB H 0.762 0.01 1 767 . 87 GLU H H 8.807 0.01 1 768 . 87 GLU N N 118.610 0.1 1 769 . 87 GLU CA C 59.230 0.1 1 770 . 87 GLU HA H 4.457 0.01 1 771 . 87 GLU C C 180.030 0.1 1 772 . 87 GLU CB C 29.370 0.1 1 773 . 87 GLU HB2 H 2.206 0.01 2 774 . 87 GLU HB3 H 2.147 0.01 2 775 . 87 GLU HG2 H 2.484 0.01 2 776 . 87 GLU HG3 H 2.440 0.01 2 777 . 88 VAL H H 7.360 0.01 1 778 . 88 VAL N N 119.760 0.1 1 779 . 88 VAL CA C 66.990 0.1 1 780 . 88 VAL HA H 3.669 0.01 1 781 . 88 VAL C C 179.100 0.1 1 782 . 88 VAL CB C 31.860 0.1 1 783 . 88 VAL HB H 2.399 0.01 1 784 . 88 VAL HG1 H 1.184 0.01 2 785 . 88 VAL HG2 H 1.025 0.01 2 786 . 89 THR H H 8.389 0.01 1 787 . 89 THR N N 117.392 0.1 1 788 . 89 THR CA C 67.190 0.1 1 789 . 89 THR HA H 3.876 0.01 1 790 . 89 THR C C 177.100 0.1 1 791 . 89 THR CB C 68.140 0.1 1 792 . 89 THR HB H 4.836 0.01 1 793 . 89 THR HG2 H 1.111 0.01 1 794 . 90 ARG H H 9.180 0.01 1 795 . 90 ARG N N 123.060 0.1 1 796 . 90 ARG CA C 58.610 0.1 1 797 . 90 ARG HA H 4.242 0.01 1 798 . 90 ARG C C 180.430 0.1 1 799 . 90 ARG CB C 29.740 0.1 1 800 . 90 ARG HB2 H 2.047 0.01 4 801 . 90 ARG HB3 H 1.976 0.01 4 802 . 90 ARG HG2 H 1.810 0.01 4 803 . 90 ARG HG3 H 1.655 0.01 4 804 . 90 ARG HD2 H 2.473 0.01 2 805 . 90 ARG HD3 H 2.324 0.01 2 806 . 90 ARG NE N 82.881 0.1 1 807 . 90 ARG HE H 7.310 0.01 1 808 . 91 LEU H H 8.165 0.01 1 809 . 91 LEU N N 121.150 0.1 1 810 . 91 LEU CA C 57.650 0.1 1 811 . 91 LEU HA H 4.024 0.01 1 812 . 91 LEU C C 179.200 0.1 1 813 . 91 LEU CB C 41.750 0.1 1 814 . 91 LEU HB2 H 2.010 0.01 2 815 . 91 LEU HB3 H 1.966 0.01 2 816 . 91 LEU HD1 H 0.940 0.01 2 817 . 91 LEU HD2 H 0.910 0.01 2 818 . 91 LEU HG H 1.643 0.01 1 819 . 92 ARG H H 7.803 0.01 1 820 . 92 ARG N N 116.750 0.1 1 821 . 92 ARG CA C 58.540 0.1 1 822 . 92 ARG HA H 4.280 0.01 1 823 . 92 ARG C C 178.650 0.1 1 824 . 92 ARG CB C 31.720 0.1 1 825 . 92 ARG HB2 H 2.014 0.01 4 826 . 92 ARG HB3 H 1.984 0.01 4 827 . 92 ARG HG2 H 1.910 0.01 4 828 . 92 ARG HG3 H 1.884 0.01 4 829 . 92 ARG HD2 H 3.232 0.01 2 830 . 92 ARG HD3 H 3.210 0.01 2 831 . 92 ARG NE N 84.719 0.1 1 832 . 92 ARG HE H 7.227 0.01 1 833 . 93 GLN H H 8.830 0.01 1 834 . 93 GLN N N 114.390 0.1 1 835 . 93 GLN CA C 55.500 0.1 1 836 . 93 GLN HA H 4.668 0.01 1 837 . 93 GLN C C 177.140 0.1 1 838 . 93 GLN CB C 30.950 0.1 1 839 . 93 GLN HB2 H 2.195 0.01 2 840 . 93 GLN HB3 H 1.656 0.01 2 841 . 93 GLN HG2 H 2.447 0.01 2 842 . 93 GLN HG3 H 2.417 0.01 2 843 . 93 GLN NE2 N 110.832 0.1 1 844 . 93 GLN HE21 H 7.308 0.01 2 845 . 93 GLN HE22 H 7.021 0.01 2 846 . 94 GLY H H 8.324 0.01 1 847 . 94 GLY N N 111.603 0.1 1 848 . 94 GLY CA C 45.120 0.1 1 849 . 94 GLY HA2 H 4.291 0.01 2 850 . 94 GLY HA3 H 3.817 0.01 2 851 . 94 GLY C C 174.730 0.1 1 852 . 95 TRP H H 8.623 0.01 1 853 . 95 TRP N N 119.200 0.1 1 854 . 95 TRP CA C 57.530 0.1 1 855 . 95 TRP HA H 5.005 0.01 1 856 . 95 TRP C C 178.390 0.1 1 857 . 95 TRP CB C 29.940 0.1 1 858 . 95 TRP HB2 H 3.546 0.01 2 859 . 95 TRP HB3 H 2.951 0.01 2 860 . 95 TRP HD1 H 7.182 0.01 1 861 . 95 TRP NE1 N 127.660 0.1 1 862 . 95 TRP HE1 H 9.858 0.01 1 863 . 95 TRP HE3 H 7.656 0.01 1 864 . 95 TRP HZ2 H 7.250 0.01 1 865 . 95 TRP HZ3 H 6.055 0.01 1 866 . 95 TRP HH2 H 6.229 0.01 1 867 . 96 GLY H H 8.439 0.01 1 868 . 96 GLY N N 107.127 0.1 1 869 . 96 GLY CA C 46.860 0.1 1 870 . 96 GLY HA2 H 3.817 0.01 2 871 . 96 GLY HA3 H 3.895 0.01 2 872 . 96 GLY C C 174.510 0.1 1 873 . 97 ALA H H 7.628 0.01 1 874 . 97 ALA N N 120.710 0.1 1 875 . 97 ALA CA C 52.800 0.1 1 876 . 97 ALA HA H 3.921 0.01 1 877 . 97 ALA C C 177.240 0.1 1 878 . 97 ALA CB C 16.380 0.1 1 879 . 97 ALA HB H 0.170 0.01 1 880 . 98 TRP H H 7.879 0.01 1 881 . 98 TRP N N 116.980 0.1 1 882 . 98 TRP CA C 56.330 0.1 1 883 . 98 TRP HA H 4.991 0.01 1 884 . 98 TRP CB C 28.360 0.1 1 885 . 98 TRP HB2 H 3.136 0.01 2 886 . 98 TRP HB3 H 3.413 0.01 2 887 . 98 TRP HD1 H 7.106 0.01 1 888 . 98 TRP NE1 N 129.940 0.1 1 889 . 98 TRP HE1 H 9.902 0.01 1 890 . 98 TRP HE3 H 7.920 0.01 1 891 . 98 TRP HZ2 H 6.933 0.01 1 892 . 98 TRP HZ3 H 7.061 0.01 1 893 . 98 TRP HH2 H 7.279 0.01 1 894 . 99 PRO HA H 4.361 0.01 1 895 . 99 PRO C C 179.430 0.1 1 896 . 99 PRO HB2 H 2.330 0.01 2 897 . 99 PRO HB3 H 2.000 0.01 2 898 . 99 PRO HG2 H 2.030 0.01 2 899 . 99 PRO HG3 H 2.050 0.01 2 900 . 99 PRO HD2 H 3.580 0.01 2 901 . 99 PRO HD3 H 3.532 0.01 2 902 . 100 VAL H H 7.992 0.01 1 903 . 100 VAL N N 118.200 0.1 1 904 . 100 VAL CA C 65.120 0.1 1 905 . 100 VAL HA H 3.867 0.01 1 906 . 100 VAL C C 179.290 0.1 1 907 . 100 VAL HB H 2.151 0.01 1 908 . 100 VAL HG1 H 0.822 0.01 2 909 . 100 VAL HG2 H 0.962 0.01 2 910 . 101 CYS H H 8.718 0.01 1 911 . 101 CYS N N 117.830 0.1 1 912 . 101 CYS CA C 55.430 0.1 1 913 . 101 CYS HA H 4.550 0.01 1 914 . 101 CYS C C 177.030 0.1 1 915 . 101 CYS CB C 38.160 0.1 1 916 . 101 CYS HB2 H 3.135 0.01 2 917 . 101 CYS HB3 H 3.017 0.01 2 918 . 102 ALA H H 8.757 0.01 1 919 . 102 ALA N N 122.330 0.1 1 920 . 102 ALA CA C 55.540 0.1 1 921 . 102 ALA HA H 3.806 0.01 1 922 . 102 ALA C C 178.960 0.1 1 923 . 102 ALA CB C 18.340 0.1 1 924 . 102 ALA HB H 1.466 0.01 1 925 . 103 ALA H H 7.606 0.01 1 926 . 103 ALA N N 119.750 0.1 1 927 . 103 ALA CA C 54.310 0.1 1 928 . 103 ALA HA H 4.076 0.01 1 929 . 103 ALA C C 181.690 0.1 1 930 . 103 ALA CB C 18.090 0.1 1 931 . 103 ALA HB H 1.418 0.01 1 932 . 104 ARG H H 7.835 0.01 1 933 . 104 ARG N N 118.260 0.1 1 934 . 104 ARG CA C 58.060 0.1 1 935 . 104 ARG HA H 4.013 0.01 1 936 . 104 ARG C C 177.730 0.1 1 937 . 104 ARG CB C 30.090 0.1 1 938 . 104 ARG HB2 H 1.866 0.01 4 939 . 104 ARG HB3 H 1.836 0.01 4 940 . 104 ARG HG2 H 1.743 0.01 4 941 . 104 ARG HG3 H 1.666 0.01 4 942 . 104 ARG HD2 H 3.117 0.01 2 943 . 104 ARG HD3 H 3.084 0.01 2 944 . 104 ARG NE N 83.809 0.1 1 945 . 104 ARG HE H 7.175 0.01 1 946 . 105 ALA H H 7.524 0.01 1 947 . 105 ALA N N 119.254 0.1 1 948 . 105 ALA CA C 52.260 0.1 1 949 . 105 ALA HA H 4.120 0.01 1 950 . 105 ALA C C 177.330 0.1 1 951 . 105 ALA CB C 19.970 0.1 1 952 . 105 ALA HB H 1.196 0.01 1 953 . 106 GLY H H 7.587 0.01 1 954 . 106 GLY N N 105.100 0.1 1 955 . 106 GLY CA C 45.150 0.1 1 956 . 106 GLY HA2 H 3.624 0.01 2 957 . 106 GLY HA3 H 3.924 0.01 2 958 . 106 GLY C C 174.420 0.1 1 959 . 107 ALA H H 7.562 0.01 1 960 . 107 ALA N N 122.980 0.1 1 961 . 107 ALA CA C 52.270 0.1 1 962 . 107 ALA HA H 3.790 0.01 1 963 . 107 ALA C C 176.310 0.1 1 964 . 107 ALA CB C 17.910 0.1 1 965 . 107 ALA HB H 0.088 0.01 1 966 . 108 ARG H H 7.530 0.01 1 967 . 108 ARG N N 124.260 0.1 1 968 . 108 ARG CA C 56.970 0.1 1 969 . 108 ARG HA H 4.109 0.01 1 970 . 108 ARG C C 181.190 0.1 1 971 . 108 ARG CB C 32.210 0.1 1 972 . 108 ARG HB2 H 1.754 0.01 4 973 . 108 ARG HB3 H 1.654 0.01 4 974 . 108 ARG HG2 H 1.480 0.01 4 975 . 108 ARG HG3 H 1.450 0.01 4 976 . 108 ARG HD2 H 3.140 0.01 2 977 . 108 ARG HD3 H 3.117 0.01 2 978 . 108 ARG NE N 84.748 0.1 1 979 . 108 ARG HE H 7.162 0.01 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 112,113,114,115 149,150,151,152 230,231,231,231 637,638,639,640 692,693,694,695 739,740,740,740,741,742,743 800,801,802,803 825,826,827,828 938,939,940,941 972,973,974,975 stop_ save_