data_5141 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-specific resonance assignments of the N-terminal, 105-residue KaiC-interacting domain of SasA, a protein necessary for a robust circadian rhythm in Synechococcus elongatus ; _BMRB_accession_number 5141 _BMRB_flat_file_name bmr5141.str _Entry_type original _Submission_date 2001-09-01 _Accession_date 2001-09-01 _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 Klewer Douglas A. . 2 Williams Stanly B. . 3 Golden Susan S. . 4 LiWang Andy C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 551 "13C chemical shifts" 343 "15N chemical shifts" 104 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-11-04 original author 'original release' 2003-03-12 update author 'update of chemical shifts' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Sequence-specific resonance assignments of the N-terminal, 105-residue KaiC-interacting domain of SasA, a protein necessary for a robust circadian rhythm in Synechococcus elongatus ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Klewer Douglas A. . 2 Williams Stanly B. . 3 Golden Susan S. . 4 LiWang Andy C. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 24 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 77 _Page_last 78 _Year 2002 _Details . loop_ _Keyword 'Circadian clock' NMR SasA 'Synechococcus elongatus' stop_ save_ ################################## # Molecular system description # ################################## save_system_SasA_N-terminus _Saveframe_category molecular_system _Mol_system_name 'SasA N-terminus' _Abbreviation_common 'SasA N-terminus' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'SasA N-terminus' $SasA_N-terminus stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'sensory domain' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_SasA_N-terminus _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common SasA _Name_variant N-terminus _Abbreviation_common 'SasA N-terminus' _Molecular_mass 11476.3 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; GSSLSPQALAQPLLLQLFVD TRPLSQHIVQRVKNILAAVE ATVPISLQVINVADQPQLVE YYRLVVTPALVKIGPGSRQV LSGIDLTDQLANQLPQWLVQ QEGIF ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 SER 4 LEU 5 SER 6 PRO 7 GLN 8 ALA 9 LEU 10 ALA 11 GLN 12 PRO 13 LEU 14 LEU 15 LEU 16 GLN 17 LEU 18 PHE 19 VAL 20 ASP 21 THR 22 ARG 23 PRO 24 LEU 25 SER 26 GLN 27 HIS 28 ILE 29 VAL 30 GLN 31 ARG 32 VAL 33 LYS 34 ASN 35 ILE 36 LEU 37 ALA 38 ALA 39 VAL 40 GLU 41 ALA 42 THR 43 VAL 44 PRO 45 ILE 46 SER 47 LEU 48 GLN 49 VAL 50 ILE 51 ASN 52 VAL 53 ALA 54 ASP 55 GLN 56 PRO 57 GLN 58 LEU 59 VAL 60 GLU 61 TYR 62 TYR 63 ARG 64 LEU 65 VAL 66 VAL 67 THR 68 PRO 69 ALA 70 LEU 71 VAL 72 LYS 73 ILE 74 GLY 75 PRO 76 GLY 77 SER 78 ARG 79 GLN 80 VAL 81 LEU 82 SER 83 GLY 84 ILE 85 ASP 86 LEU 87 THR 88 ASP 89 GLN 90 LEU 91 ALA 92 ASN 93 GLN 94 LEU 95 PRO 96 GLN 97 TRP 98 LEU 99 VAL 100 GLN 101 GLN 102 GLU 103 GLY 104 ILE 105 PHE 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 1T4Y "Solution Structure Of The N-Terminal Domain Of Synechococcus Elongatus Sasa (Average Minimized Structure)" 100.00 105 100.00 100.00 5.18e-65 PDB 1T4Z "Solution Structure Of The N-Terminal Domain Of Synechococcus Elongatus Sasa (25-Structures Ensemble)" 100.00 105 100.00 100.00 5.18e-65 DBJ BAA03145 "SarS [Synechococcus elongatus PCC 7942]" 100.00 387 97.14 97.14 4.17e-60 DBJ BAD80168 "two-component sensor histidine kinase [Synechococcus elongatus PCC 6301]" 100.00 399 97.14 97.14 6.80e-60 GB ABB58144 "histidine kinase [Synechococcus elongatus PCC 7942]" 100.00 387 97.14 97.14 4.40e-60 GB AJD57380 "ATPase [Synechococcus sp. UTEX 2973]" 100.00 387 97.14 97.14 4.40e-60 REF WP_011244288 "ATPase [Synechococcus elongatus]" 100.00 399 97.14 97.14 6.80e-60 REF WP_011378322 "ATPase [Synechococcus elongatus]" 100.00 387 97.14 97.14 4.40e-60 REF WP_039755926 "ATPase [Synechococcus sp. UTEX 2973]" 97.14 383 97.06 98.04 3.18e-58 REF YP_172688 "adaptive-response sensory kinase [Synechococcus elongatus PCC 6301]" 100.00 399 97.14 97.14 6.80e-60 REF YP_401131 "adaptive-response sensory kinase [Synechococcus elongatus PCC 7942]" 100.00 387 97.14 97.14 4.40e-60 SP Q06904 "RecName: Full=Adaptive-response sensory-kinase SasA; AltName: Full=Synechococcus adaptive sensor protein A [Synechococcus elong" 100.00 387 97.14 97.14 4.40e-60 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $SasA_N-terminus 'Synechoccus elongatus' . Eubacteria . Synechoccus elongatus 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 $SasA_N-terminus 'recombinant technology' Escherichia coli . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_SasA-105 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $SasA_N-terminus 0.6 mM '[U-99% 13C; U-99% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version '1.8 rev 2001.030.21.27' loop_ _Task 'NMR data processing' stop_ _Details ; Delaglio, F., S. Grzesiek, Vuister, G.W., Zhu, G., Pfeifer, J. and A. Bax. (1995) J. Biomol. NMR. 6, 277-293. ; save_ save_PIPP _Saveframe_category software _Name PIPP _Version 4.2.6 loop_ _Task 'Spectra visualization' stop_ _Details ; Garrett, D.S., Powers, R., Gronenborn, A.M. and Clore, G.M, (1991) J. Magn. Reson., 95, 214-220. ; save_ save_STAPP _Saveframe_category software _Name STAPP _Version 4.2.6 loop_ _Task 'partial sequence specific assignments' 'spin system creation' stop_ _Details ; Garrett, D.S., Powers, R., Gronenborn, A.M. and Clore, G.M, (1991) J. Magn. Reson., 95, 214-220. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_CBCA(CO)NH_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_CBCANH_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _Sample_label . save_ save_HBHA(CO)NH_4 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _Sample_label . save_ save_C(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _Sample_label . save_ save_H(CCO)NH_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _Sample_label . save_ save_H(C)CH-COSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(C)CH-COSY _Sample_label . save_ save_1H-15N_HSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNHA _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HBHA(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name C(CO)NH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name H(CCO)NH _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name H(C)CH-COSY _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 'Triple resonance, XYZ-PGF probe was used.' save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.22 0.02 M pH 7.0 0.05 na temperature 298 0.05 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.0 . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label CBCA(CO)NH CBCANH HNHA HBHA(CO)NH C(CO)NH H(CCO)NH H(C)CH-COSY '1H-15N HSQC' stop_ loop_ _Sample_label $sample_SasA-105 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'SasA N-terminus' _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 . 3 SER HA H 4.54 0.03 1 2 . 3 SER HB2 H 3.90 0.03 2 3 . 3 SER CA C 58.43 0.50 1 4 . 3 SER CB C 63.74 0.50 1 5 . 4 LEU H H 8.32 0.03 1 6 . 4 LEU HA H 4.71 0.03 1 7 . 4 LEU HB2 H 2.94 0.03 1 8 . 4 LEU HB3 H 2.94 0.03 1 9 . 4 LEU CA C 55.10 0.50 1 10 . 4 LEU CB C 42.02 0.50 1 11 . 4 LEU N N 123.92 0.50 1 12 . 5 SER H H 8.29 0.03 1 13 . 5 SER HB2 H 3.90 0.03 1 14 . 5 SER HB3 H 3.90 0.03 1 15 . 5 SER CA C 56.39 0.50 1 16 . 5 SER CB C 63.24 0.50 1 17 . 5 SER N N 118.08 0.50 1 18 . 6 PRO HA H 4.44 0.03 1 19 . 6 PRO HB2 H 2.33 0.03 2 20 . 6 PRO HB3 H 1.95 0.03 2 21 . 6 PRO HG2 H 2.05 0.03 1 22 . 6 PRO HG3 H 2.05 0.03 1 23 . 6 PRO HD2 H 3.40 0.03 2 24 . 6 PRO HD3 H 3.70 0.03 2 25 . 6 PRO CA C 63.67 0.50 1 26 . 6 PRO CB C 31.91 0.50 1 27 . 6 PRO CG C 27.41 0.50 1 28 . 6 PRO CD C 50.08 0.50 1 29 . 7 GLN H H 8.36 0.03 1 30 . 7 GLN CA C 56.14 0.50 1 31 . 7 GLN CB C 29.32 0.50 1 32 . 7 GLN N N 119.54 0.50 1 33 . 8 ALA H H 8.19 0.03 1 34 . 8 ALA HA H 4.00 0.03 1 35 . 8 ALA CA C 52.72 0.50 1 36 . 8 ALA CB C 19.29 0.50 1 37 . 8 ALA N N 124.86 0.50 1 38 . 9 LEU H H 8.05 0.03 1 39 . 9 LEU HA H 4.40 0.03 1 40 . 9 LEU HB2 H 1.65 0.03 1 41 . 9 LEU HB3 H 1.65 0.03 1 42 . 9 LEU HD1 H 0.96 0.03 2 43 . 9 LEU HG H 2.38 0.03 1 44 . 9 LEU CA C 55.03 0.50 1 45 . 9 LEU CB C 42.70 0.50 1 46 . 9 LEU N N 120.73 0.50 1 47 . 10 ALA H H 8.43 0.03 1 48 . 10 ALA CA C 52.25 0.50 1 49 . 10 ALA CB C 19.64 0.50 1 50 . 10 ALA N N 125.59 0.50 1 51 . 11 GLN H H 8.23 0.03 1 52 . 11 GLN HA H 4.60 0.03 1 53 . 11 GLN HB2 H 1.87 0.03 1 54 . 11 GLN HB3 H 2.13 0.03 1 55 . 11 GLN HG2 H 2.39 0.03 1 56 . 11 GLN HG3 H 2.39 0.03 1 57 . 11 GLN CA C 53.35 0.50 1 58 . 11 GLN CB C 29.70 0.50 1 59 . 11 GLN CG C 33.61 0.50 1 60 . 11 GLN N N 120.59 0.50 1 61 . 12 PRO HA H 4.42 0.03 1 62 . 12 PRO HB2 H 1.98 0.03 1 63 . 12 PRO HB3 H 1.60 0.03 1 64 . 12 PRO HG2 H 2.04 0.03 1 65 . 12 PRO HG3 H 2.04 0.03 1 66 . 12 PRO HD2 H 3.79 0.03 1 67 . 12 PRO HD3 H 3.79 0.03 1 68 . 12 PRO CA C 62.90 0.50 1 69 . 12 PRO CB C 32.42 0.50 1 70 . 12 PRO CG C 27.46 0.50 1 71 . 12 PRO CD C 50.36 0.50 1 72 . 13 LEU H H 8.15 0.03 1 73 . 13 LEU HA H 4.65 0.03 1 74 . 13 LEU HB2 H 1.42 0.03 1 75 . 13 LEU HB3 H 1.84 0.03 1 76 . 13 LEU HD1 H 0.97 0.03 1 77 . 13 LEU HD2 H 0.97 0.03 1 78 . 13 LEU CA C 54.89 0.50 1 79 . 13 LEU CB C 43.18 0.50 1 80 . 13 LEU CD1 C 26.83 0.50 1 81 . 13 LEU CD2 C 24.94 0.50 1 82 . 13 LEU N N 122.39 0.50 1 83 . 14 LEU H H 8.20 0.03 1 84 . 14 LEU HA H 4.78 0.03 1 85 . 14 LEU HB2 H 1.66 0.03 1 86 . 14 LEU HB3 H 1.30 0.03 1 87 . 14 LEU HG H 1.52 0.03 1 88 . 14 LEU HD1 H 0.76 0.03 1 89 . 14 LEU CA C 54.36 0.50 1 90 . 14 LEU CB C 43.66 0.50 1 91 . 14 LEU CG C 25.68 0.50 1 92 . 14 LEU CD1 C 23.92 0.50 1 93 . 14 LEU N N 128.00 0.50 1 94 . 15 LEU H H 8.69 0.03 1 95 . 15 LEU HA H 5.47 0.03 1 96 . 15 LEU HB2 H 2.01 0.03 1 97 . 15 LEU HB3 H 1.20 0.03 1 98 . 15 LEU HD1 H 0.95 0.03 1 99 . 15 LEU CA C 52.77 0.50 1 100 . 15 LEU CB C 46.02 0.50 1 101 . 15 LEU CG C 27.29 0.50 1 102 . 15 LEU CD1 C 24.14 0.50 1 103 . 15 LEU N N 122.33 0.50 1 104 . 16 GLN H H 9.34 0.03 1 105 . 16 GLN HA H 5.08 0.03 1 106 . 16 GLN HB2 H 2.16 0.03 1 107 . 16 GLN HB3 H 1.46 0.03 1 108 . 16 GLN CA C 54.36 0.50 1 109 . 16 GLN CB C 32.25 0.50 1 110 . 16 GLN CG C 34.52 0.50 1 111 . 16 GLN N N 122.08 0.50 1 112 . 17 LEU H H 9.06 0.03 1 113 . 17 LEU HA H 5.24 0.03 1 114 . 17 LEU HB2 H 1.19 0.03 1 115 . 17 LEU HB3 H 1.94 0.03 1 116 . 17 LEU HD1 H 0.90 0.03 1 117 . 17 LEU CA C 53.27 0.50 1 118 . 17 LEU CB C 44.94 0.50 1 119 . 17 LEU CG C 28.24 0.50 1 120 . 17 LEU CD1 C 23.26 0.50 1 121 . 17 LEU N N 126.62 0.50 1 122 . 18 PHE H H 9.78 0.03 1 123 . 18 PHE HA H 5.41 0.03 1 124 . 18 PHE HB2 H 3.06 0.03 1 125 . 18 PHE HB3 H 2.70 0.03 1 126 . 18 PHE HD1 H 7.03 0.03 1 127 . 18 PHE HD2 H 7.03 0.03 1 128 . 18 PHE HE1 H 7.18 0.03 1 129 . 18 PHE HE2 H 7.18 0.03 1 130 . 18 PHE CA C 57.37 0.50 1 131 . 18 PHE CB C 40.49 0.50 1 132 . 18 PHE CD1 C 131.90 0.50 1 133 . 18 PHE CD2 C 131.90 0.50 1 134 . 18 PHE CE1 C 132.07 0.50 1 135 . 18 PHE CE2 C 132.07 0.50 1 136 . 18 PHE N N 127.30 0.50 1 137 . 19 VAL H H 8.70 0.03 1 138 . 19 VAL HA H 4.84 0.03 1 139 . 19 VAL HB H 2.44 0.03 1 140 . 19 VAL HG1 H 0.87 0.03 1 141 . 19 VAL HG2 H 0.72 0.03 1 142 . 19 VAL CA C 59.00 0.50 1 143 . 19 VAL CB C 36.01 0.50 1 144 . 19 VAL CG1 C 21.95 0.50 1 145 . 19 VAL CG2 C 17.69 0.50 1 146 . 19 VAL N N 113.62 0.50 1 147 . 20 ASP H H 7.86 0.03 1 148 . 20 ASP HA H 5.13 0.03 1 149 . 20 ASP HB2 H 2.60 0.03 1 150 . 20 ASP HB3 H 3.38 0.03 1 151 . 20 ASP CA C 52.38 0.50 1 152 . 20 ASP CB C 42.36 0.50 1 153 . 20 ASP N N 119.74 0.50 1 154 . 21 THR H H 7.75 0.03 1 155 . 21 THR HA H 4.37 0.03 1 156 . 21 THR HB H 4.61 0.03 1 157 . 21 THR HG2 H 1.27 0.03 1 158 . 21 THR CA C 61.89 0.50 1 159 . 21 THR CB C 69.11 0.50 1 160 . 21 THR CG2 C 22.14 0.50 1 161 . 21 THR N N 106.05 0.50 1 162 . 22 ARG H H 8.42 0.03 1 163 . 22 ARG HA H 4.52 0.03 1 164 . 22 ARG HB2 H 2.06 0.03 1 165 . 22 ARG HB3 H 2.06 0.03 1 166 . 22 ARG HG2 H 1.83 0.03 1 167 . 22 ARG HG3 H 1.83 0.03 1 168 . 22 ARG HD2 H 3.24 0.03 1 169 . 22 ARG HD3 H 3.35 0.03 1 170 . 22 ARG CA C 56.27 0.50 1 171 . 22 ARG CB C 29.36 0.50 1 172 . 22 ARG CG C 27.34 0.50 1 173 . 22 ARG CD C 43.57 0.50 1 174 . 22 ARG N N 123.98 0.50 1 175 . 23 PRO HA H 4.30 0.03 1 176 . 23 PRO HB2 H 2.44 0.03 1 177 . 23 PRO HB3 H 2.01 0.03 1 178 . 23 PRO HG2 H 2.27 0.03 1 179 . 23 PRO HG3 H 2.12 0.03 1 180 . 23 PRO HD2 H 3.91 0.03 2 181 . 23 PRO HD3 H 4.01 0.03 2 182 . 23 PRO CA C 66.05 0.50 1 183 . 23 PRO CB C 31.87 0.50 1 184 . 23 PRO CG C 27.91 0.50 1 185 . 23 PRO CD C 50.39 0.50 1 186 . 23 PRO N N 137.15 0.50 1 187 . 24 LEU H H 8.19 0.03 1 188 . 24 LEU HA H 4.28 0.03 1 189 . 24 LEU HB2 H 1.85 0.03 1 190 . 24 LEU HB3 H 1.67 0.03 1 191 . 24 LEU HG H 1.70 0.03 1 192 . 24 LEU HD1 H 1.01 0.03 1 193 . 24 LEU HD2 H 0.99 0.03 1 194 . 24 LEU CA C 57.86 0.50 1 195 . 24 LEU CB C 41.72 0.50 1 196 . 24 LEU CG C 27.39 0.50 1 197 . 24 LEU CD1 C 24.12 0.50 1 198 . 24 LEU CD2 C 25.50 0.50 1 199 . 24 LEU N N 116.34 0.50 1 200 . 25 SER H H 7.80 0.03 1 201 . 25 SER HA H 4.12 0.03 1 202 . 25 SER HB2 H 3.82 0.03 1 203 . 25 SER HB3 H 4.28 0.03 1 204 . 25 SER CA C 62.87 0.50 1 205 . 25 SER CB C 62.87 0.50 1 206 . 25 SER N N 115.48 0.50 1 207 . 26 GLN H H 7.74 0.03 1 208 . 26 GLN HA H 4.01 0.03 1 209 . 26 GLN HB2 H 2.11 0.03 1 210 . 26 GLN HB3 H 2.11 0.03 1 211 . 26 GLN HG2 H 2.37 0.03 1 212 . 26 GLN HG3 H 2.37 0.03 1 213 . 26 GLN HE21 H 7.46 0.03 2 214 . 26 GLN CA C 58.69 0.50 1 215 . 26 GLN CB C 27.95 0.50 1 216 . 26 GLN CG C 33.66 0.50 1 217 . 26 GLN N N 119.26 0.50 1 218 . 26 GLN NE2 N 112.32 0.50 1 219 . 27 HIS H H 7.86 0.03 1 220 . 27 HIS HA H 4.54 0.03 1 221 . 27 HIS HB2 H 3.29 0.03 1 222 . 27 HIS HB3 H 3.29 0.03 1 223 . 27 HIS HD2 H 6.99 0.03 1 224 . 27 HIS HE1 H 7.73 0.03 1 225 . 27 HIS CA C 58.51 0.50 1 226 . 27 HIS CB C 30.45 0.50 1 227 . 27 HIS CD2 C 119.82 0.50 1 228 . 27 HIS CE1 C 138.77 0.50 1 229 . 27 HIS N N 118.97 0.50 1 230 . 28 ILE H H 7.91 0.03 1 231 . 28 ILE HA H 3.75 0.03 1 232 . 28 ILE HB H 2.20 0.03 1 233 . 28 ILE HG12 H 1.73 0.03 2 234 . 28 ILE HG13 H 1.51 0.03 2 235 . 28 ILE HG2 H 0.94 0.03 1 236 . 28 ILE HD1 H 0.98 0.03 1 237 . 28 ILE CA C 64.16 0.50 1 238 . 28 ILE CB C 37.35 0.50 1 239 . 28 ILE CG1 C 29.72 0.50 1 240 . 28 ILE CG2 C 17.95 0.50 1 241 . 28 ILE CD1 C 13.36 0.50 1 242 . 28 ILE N N 120.11 0.50 1 243 . 29 VAL H H 8.08 0.03 1 244 . 29 VAL HA H 3.28 0.03 1 245 . 29 VAL HB H 2.19 0.03 1 246 . 29 VAL HG2 H 1.12 0.03 1 247 . 29 VAL HG1 H 0.90 0.03 1 248 . 29 VAL CA C 67.53 0.50 1 249 . 29 VAL CB C 31.69 0.50 1 250 . 29 VAL CG2 C 23.65 0.50 1 251 . 29 VAL CG1 C 21.65 0.50 1 252 . 29 VAL N N 119.72 0.50 1 253 . 30 GLN H H 7.57 0.03 1 254 . 30 GLN HA H 3.90 0.03 1 255 . 30 GLN HB2 H 2.19 0.03 1 256 . 30 GLN HB3 H 2.19 0.03 1 257 . 30 GLN HG2 H 2.45 0.03 1 258 . 30 GLN HG3 H 2.45 0.03 1 259 . 30 GLN HE21 H 7.04 0.03 1 260 . 30 GLN HE22 H 7.44 0.03 1 261 . 30 GLN CA C 58.67 0.50 1 262 . 30 GLN CB C 28.46 0.50 1 263 . 30 GLN CG C 33.95 0.50 1 264 . 30 GLN N N 116.65 0.50 1 265 . 30 GLN NE2 N 113.81 0.50 1 266 . 31 ARG H H 8.05 0.03 1 267 . 31 ARG HA H 4.07 0.03 1 268 . 31 ARG HB2 H 1.91 0.03 1 269 . 31 ARG HB3 H 1.91 0.03 1 270 . 31 ARG HG2 H 1.65 0.03 2 271 . 31 ARG HG3 H 1.77 0.03 2 272 . 31 ARG HD2 H 3.22 0.03 1 273 . 31 ARG HD3 H 3.22 0.03 1 274 . 31 ARG CA C 59.18 0.50 1 275 . 31 ARG CB C 30.42 0.50 1 276 . 31 ARG CG C 27.49 0.50 1 277 . 31 ARG CD C 43.23 0.50 1 278 . 31 ARG N N 118.49 0.50 1 279 . 32 VAL H H 8.67 0.03 1 280 . 32 VAL HA H 3.42 0.03 1 281 . 32 VAL HB H 2.20 0.03 1 282 . 32 VAL HG1 H 0.96 0.03 1 283 . 32 VAL HG2 H 0.81 0.03 1 284 . 32 VAL CA C 67.50 0.50 1 285 . 32 VAL CB C 30.90 0.50 1 286 . 32 VAL CG1 C 24.35 0.50 1 287 . 32 VAL CG2 C 21.70 0.50 1 288 . 32 VAL N N 119.53 0.50 1 289 . 33 LYS H H 8.35 0.03 1 290 . 33 LYS HA H 3.77 0.03 1 291 . 33 LYS HB2 H 1.86 0.03 1 292 . 33 LYS HB3 H 1.86 0.03 1 293 . 33 LYS HG2 H 1.63 0.03 2 294 . 33 LYS HG3 H 1.26 0.03 2 295 . 33 LYS HD2 H 1.59 0.03 1 296 . 33 LYS HD3 H 1.59 0.03 1 297 . 33 LYS HE2 H 3.01 0.03 1 298 . 33 LYS HE3 H 2.86 0.03 1 299 . 33 LYS CA C 61.13 0.50 1 300 . 33 LYS CB C 32.08 0.50 1 301 . 33 LYS CG C 26.91 0.50 1 302 . 33 LYS CD C 29.88 0.50 1 303 . 33 LYS CE C 41.89 0.50 1 304 . 33 LYS N N 118.27 0.50 1 305 . 34 ASN H H 8.22 0.03 1 306 . 34 ASN HA H 4.47 0.03 1 307 . 34 ASN HB2 H 3.01 0.03 1 308 . 34 ASN HB3 H 2.85 0.03 1 309 . 34 ASN CA C 56.09 0.50 1 310 . 34 ASN CB C 38.08 0.50 1 311 . 34 ASN N N 118.40 0.50 1 312 . 35 ILE H H 8.06 0.03 1 313 . 35 ILE HA H 3.72 0.03 1 314 . 35 ILE HB H 1.94 0.03 1 315 . 35 ILE HG12 H 1.83 0.03 1 316 . 35 ILE HG13 H 1.13 0.03 1 317 . 35 ILE HG2 H 0.78 0.03 1 318 . 35 ILE HD1 H 0.86 0.03 1 319 . 35 ILE CA C 65.20 0.50 1 320 . 35 ILE CB C 38.40 0.50 1 321 . 35 ILE CG2 C 17.02 0.50 1 322 . 35 ILE CG1 C 29.75 0.50 1 323 . 35 ILE CD1 C 14.11 0.50 1 324 . 35 ILE N N 122.89 0.50 1 325 . 36 LEU H H 8.11 0.03 1 326 . 36 LEU HA H 4.00 0.03 1 327 . 36 LEU HB2 H 1.89 0.03 1 328 . 36 LEU HB3 H 1.50 0.03 1 329 . 36 LEU HD1 H 0.85 0.03 1 330 . 36 LEU CA C 57.34 0.50 1 331 . 36 LEU CB C 40.92 0.50 1 332 . 36 LEU CG C 27.07 0.50 1 333 . 36 LEU CD1 C 22.98 0.50 1 334 . 36 LEU N N 117.74 0.50 1 335 . 37 ALA H H 7.98 0.03 1 336 . 37 ALA HA H 4.25 0.03 1 337 . 37 ALA HB H 1.54 0.03 1 338 . 37 ALA CA C 53.90 0.50 1 339 . 37 ALA CB C 18.41 0.50 1 340 . 37 ALA N N 119.52 0.50 1 341 . 38 ALA H H 7.23 0.03 1 342 . 38 ALA HA H 4.35 0.03 1 343 . 38 ALA HB H 1.52 0.03 1 344 . 38 ALA CA C 52.83 0.50 1 345 . 38 ALA CB C 19.14 0.50 1 346 . 38 ALA N N 117.96 0.50 1 347 . 39 VAL H H 7.20 0.03 1 348 . 39 VAL HA H 4.18 0.03 1 349 . 39 VAL HB H 2.24 0.03 1 350 . 39 VAL HG1 H 1.02 0.03 1 351 . 39 VAL CA C 62.04 0.50 1 352 . 39 VAL CB C 32.77 0.50 1 353 . 39 VAL CG1 C 21.66 0.50 1 354 . 39 VAL N N 115.42 0.50 1 355 . 40 GLU H H 8.22 0.03 1 356 . 40 GLU HA H 4.36 0.03 1 357 . 40 GLU HB2 H 2.05 0.03 1 358 . 40 GLU HB3 H 2.05 0.03 1 359 . 40 GLU HG2 H 2.31 0.03 1 360 . 40 GLU HG3 H 2.31 0.03 1 361 . 40 GLU CA C 56.85 0.50 1 362 . 40 GLU CB C 29.48 0.50 1 363 . 40 GLU CG C 36.38 0.50 1 364 . 40 GLU N N 124.77 0.50 1 365 . 41 ALA H H 8.29 0.03 1 366 . 41 ALA HA H 4.47 0.03 1 367 . 41 ALA HB H 1.50 0.03 1 368 . 41 ALA CA C 52.67 0.50 1 369 . 41 ALA CB C 20.21 0.50 1 370 . 41 ALA N N 124.26 0.50 1 371 . 42 THR H H 8.32 0.03 1 372 . 42 THR HA H 4.28 0.03 1 373 . 42 THR HB H 4.39 0.03 1 374 . 42 THR HG2 H 1.27 0.03 1 375 . 42 THR CA C 62.67 0.50 1 376 . 42 THR CB C 69.11 0.50 1 377 . 42 THR CG2 C 22.20 0.50 1 378 . 42 THR N N 111.12 0.50 1 379 . 43 VAL H H 7.37 0.03 1 380 . 43 VAL HA H 4.48 0.03 1 381 . 43 VAL HB H 2.02 0.03 1 382 . 43 VAL HG1 H 0.90 0.03 1 383 . 43 VAL CA C 58.77 0.50 1 384 . 43 VAL CB C 33.79 0.50 1 385 . 43 VAL CG1 C 19.68 0.50 2 386 . 43 VAL N N 120.70 0.50 1 387 . 44 PRO HA H 4.39 0.03 1 388 . 44 PRO HB2 H 1.61 0.03 1 389 . 44 PRO HB3 H 2.12 0.03 1 390 . 44 PRO HG2 H 1.92 0.03 1 391 . 44 PRO HG3 H 1.92 0.03 1 392 . 44 PRO HD2 H 3.83 0.03 1 393 . 44 PRO HD3 H 3.79 0.03 1 394 . 44 PRO CA C 62.64 0.50 1 395 . 44 PRO CB C 31.72 0.50 1 396 . 44 PRO CG C 27.58 0.50 1 397 . 44 PRO CD C 50.68 0.50 1 398 . 44 PRO N N 136.83 0.50 1 399 . 45 ILE H H 8.21 0.03 1 400 . 45 ILE HA H 4.62 0.03 1 401 . 45 ILE HB H 1.76 0.03 1 402 . 45 ILE HG12 H 1.05 0.03 2 403 . 45 ILE HG13 H 1.84 0.03 2 404 . 45 ILE HG2 H 0.85 0.03 1 405 . 45 ILE HD1 H 0.94 0.03 1 406 . 45 ILE CA C 60.60 0.50 1 407 . 45 ILE CB C 40.74 0.50 1 408 . 45 ILE CG1 C 27.26 0.50 1 409 . 45 ILE CG2 C 18.03 0.50 1 410 . 45 ILE CD1 C 14.40 0.50 1 411 . 45 ILE N N 121.94 0.50 1 412 . 46 SER H H 9.01 0.03 1 413 . 46 SER HA H 4.72 0.03 1 414 . 46 SER HB2 H 3.93 0.03 2 415 . 46 SER HB3 H 3.61 0.03 2 416 . 46 SER CA C 56.36 0.50 1 417 . 46 SER CB C 64.12 0.50 1 418 . 46 SER N N 123.49 0.50 1 419 . 47 LEU H H 8.58 0.03 1 420 . 47 LEU HA H 5.03 0.03 1 421 . 47 LEU HB2 H 1.04 0.03 2 422 . 47 LEU HB3 H 1.85 0.03 2 423 . 47 LEU HD1 H 0.73 0.03 1 424 . 47 LEU HD2 H 0.73 0.03 1 425 . 47 LEU CA C 53.46 0.50 1 426 . 47 LEU CB C 44.18 0.50 1 427 . 47 LEU CG C 27.90 0.50 1 428 . 47 LEU CD1 C 26.23 0.50 1 429 . 47 LEU CD2 C 24.27 0.50 1 430 . 47 LEU N N 128.26 0.50 1 431 . 48 GLN H H 8.35 0.03 1 432 . 48 GLN HA H 4.65 0.03 1 433 . 48 GLN HB2 H 1.96 0.03 1 434 . 48 GLN HB3 H 1.88 0.03 1 435 . 48 GLN HG2 H 2.39 0.03 2 436 . 48 GLN HG3 H 2.16 0.03 2 437 . 48 GLN CA C 54.12 0.50 1 438 . 48 GLN CB C 31.10 0.50 1 439 . 48 GLN CG C 33.58 0.50 1 440 . 48 GLN N N 127.97 0.50 1 441 . 49 VAL H H 8.83 0.03 1 442 . 49 VAL HA H 4.54 0.03 1 443 . 49 VAL HB H 1.99 0.03 1 444 . 49 VAL HG1 H 0.86 0.03 1 445 . 49 VAL CA C 62.51 0.50 1 446 . 49 VAL CB C 31.91 0.50 1 447 . 49 VAL CG1 C 21.71 0.50 1 448 . 49 VAL N N 127.55 0.50 1 449 . 50 ILE H H 9.34 0.03 1 450 . 50 ILE HA H 4.06 0.03 1 451 . 50 ILE HB H 0.87 0.03 1 452 . 50 ILE HG2 H 0.74 0.03 1 453 . 50 ILE HG12 H 0.94 0.03 1 454 . 50 ILE HG13 H 0.62 0.03 1 455 . 50 ILE HD1 H 0.32 0.03 1 456 . 50 ILE CA C 60.22 0.50 1 457 . 50 ILE CB C 41.23 0.50 1 458 . 50 ILE CG1 C 27.48 0.50 1 459 . 50 ILE CG2 C 18.30 0.50 1 460 . 50 ILE CD1 C 13.66 0.50 1 461 . 50 ILE N N 131.37 0.50 1 462 . 51 ASN H H 8.94 0.03 1 463 . 51 ASN HA H 5.14 0.03 1 464 . 51 ASN HB2 H 2.67 0.03 1 465 . 51 ASN HB3 H 2.96 0.03 1 466 . 51 ASN CA C 52.23 0.50 1 467 . 51 ASN CB C 38.31 0.50 1 468 . 51 ASN N N 126.34 0.50 1 469 . 52 VAL H H 8.94 0.03 1 470 . 52 VAL HA H 3.83 0.03 1 471 . 52 VAL HB H 2.28 0.03 1 472 . 52 VAL HG1 H 1.17 0.03 1 473 . 52 VAL HG2 H 1.09 0.03 1 474 . 52 VAL CA C 65.42 0.50 1 475 . 52 VAL CB C 31.61 0.50 1 476 . 52 VAL CG1 C 22.79 0.50 1 477 . 52 VAL CG2 C 19.30 0.50 1 478 . 52 VAL N N 123.36 0.50 1 479 . 53 ALA H H 8.43 0.03 1 480 . 53 ALA HA H 4.20 0.03 1 481 . 53 ALA HB H 1.43 0.03 1 482 . 53 ALA CA C 53.74 0.50 1 483 . 53 ALA CB C 18.87 0.50 1 484 . 53 ALA N N 121.01 0.50 1 485 . 54 ASP H H 7.87 0.03 1 486 . 54 ASP HA H 4.70 0.03 1 487 . 54 ASP HB2 H 2.93 0.03 1 488 . 54 ASP HB3 H 2.93 0.03 1 489 . 54 ASP CA C 55.48 0.50 1 490 . 54 ASP CB C 41.89 0.50 1 491 . 54 ASP N N 115.47 0.50 1 492 . 55 GLN H H 6.96 0.03 1 493 . 55 GLN HA H 5.13 0.03 1 494 . 55 GLN HB2 H 2.41 0.03 1 495 . 55 GLN HB3 H 1.76 0.03 1 496 . 55 GLN HG2 H 2.33 0.03 1 497 . 55 GLN HG3 H 2.33 0.03 1 498 . 55 GLN CA C 53.42 0.50 1 499 . 55 GLN CB C 29.67 0.50 1 500 . 55 GLN CG C 33.23 0.50 1 501 . 55 GLN N N 114.97 0.50 1 502 . 56 PRO HA H 4.36 0.03 1 503 . 56 PRO HB2 H 2.06 0.03 1 504 . 56 PRO HB3 H 2.33 0.03 1 505 . 56 PRO HG2 H 2.06 0.03 1 506 . 56 PRO HG3 H 2.06 0.03 1 507 . 56 PRO HD2 H 3.38 0.03 1 508 . 56 PRO HD3 H 3.77 0.03 1 509 . 56 PRO CA C 65.15 0.50 1 510 . 56 PRO CB C 31.30 0.50 1 511 . 56 PRO CG C 27.51 0.50 1 512 . 56 PRO CD C 50.33 0.50 1 513 . 56 PRO N N 138.01 0.50 1 514 . 57 GLN H H 8.88 0.03 1 515 . 57 GLN HA H 4.24 0.03 1 516 . 57 GLN HB2 H 2.08 0.03 1 517 . 57 GLN HB3 H 2.08 0.03 1 518 . 57 GLN HG2 H 2.52 0.03 2 519 . 57 GLN HG3 H 2.38 0.03 2 520 . 57 GLN CA C 58.73 0.50 1 521 . 57 GLN CB C 27.27 0.50 1 522 . 57 GLN CG C 34.13 0.50 1 523 . 57 GLN N N 118.58 0.50 1 524 . 58 LEU H H 7.62 0.03 1 525 . 58 LEU HA H 4.13 0.03 1 526 . 58 LEU HB2 H 1.91 0.03 1 527 . 58 LEU HB3 H 1.79 0.03 1 528 . 58 LEU HG H 1.66 0.03 1 529 . 58 LEU HD1 H 0.90 0.03 2 530 . 58 LEU HD2 H 0.89 0.03 2 531 . 58 LEU CA C 57.18 0.50 1 532 . 58 LEU CB C 42.34 0.50 1 533 . 58 LEU CG C 27.03 0.50 1 534 . 58 LEU CD1 C 24.51 0.50 1 535 . 58 LEU CD2 C 23.74 0.50 1 536 . 58 LEU N N 121.95 0.50 1 537 . 59 VAL H H 7.23 0.03 1 538 . 59 VAL HA H 3.17 0.03 1 539 . 59 VAL HB H 2.24 0.03 1 540 . 59 VAL HG2 H 1.08 0.03 1 541 . 59 VAL HG1 H 0.88 0.03 1 542 . 59 VAL CA C 66.67 0.50 1 543 . 59 VAL CB C 31.93 0.50 1 544 . 59 VAL CG2 C 23.22 0.50 1 545 . 59 VAL CG1 C 21.25 0.50 1 546 . 59 VAL N N 118.78 0.50 1 547 . 60 GLU H H 7.48 0.03 1 548 . 60 GLU HA H 4.11 0.03 1 549 . 60 GLU HB2 H 2.05 0.03 1 550 . 60 GLU HB3 H 2.05 0.03 1 551 . 60 GLU HG2 H 2.27 0.03 1 552 . 60 GLU HG3 H 2.27 0.03 1 553 . 60 GLU CA C 58.73 0.50 1 554 . 60 GLU CB C 29.68 0.50 1 555 . 60 GLU CG C 36.17 0.50 1 556 . 60 GLU N N 117.07 0.50 1 557 . 61 TYR H H 8.05 0.03 1 558 . 61 TYR HA H 4.14 0.03 1 559 . 61 TYR HB2 H 3.18 0.03 1 560 . 61 TYR HB3 H 2.75 0.03 1 561 . 61 TYR HD1 H 6.62 0.03 1 562 . 61 TYR HD2 H 6.62 0.03 1 563 . 61 TYR HE1 H 6.71 0.03 1 564 . 61 TYR HE2 H 6.71 0.03 1 565 . 61 TYR CA C 61.16 0.50 1 566 . 61 TYR CB C 38.63 0.50 1 567 . 61 TYR CD1 C 133.16 0.50 1 568 . 61 TYR CD2 C 133.16 0.50 1 569 . 61 TYR CE1 C 118.09 0.50 1 570 . 61 TYR CE2 C 118.09 0.50 1 571 . 61 TYR N N 121.94 0.50 1 572 . 62 TYR H H 7.84 0.03 1 573 . 62 TYR HA H 4.32 0.03 1 574 . 62 TYR HB2 H 2.55 0.03 1 575 . 62 TYR HB3 H 3.07 0.03 1 576 . 62 TYR HD1 H 6.81 0.03 1 577 . 62 TYR HD2 H 6.81 0.03 1 578 . 62 TYR HE1 H 7.02 0.03 1 579 . 62 TYR HE2 H 7.02 0.03 1 580 . 62 TYR CA C 56.87 0.50 1 581 . 62 TYR CB C 37.82 0.50 1 582 . 62 TYR CD1 C 131.63 0.50 1 583 . 62 TYR CD2 C 131.63 0.50 1 584 . 62 TYR CE1 C 118.05 0.50 1 585 . 62 TYR CE2 C 118.05 0.50 1 586 . 62 TYR N N 114.46 0.50 1 587 . 63 ARG H H 7.78 0.03 1 588 . 63 ARG HA H 3.86 0.03 1 589 . 63 ARG HB2 H 2.01 0.03 1 590 . 63 ARG HB3 H 1.85 0.03 1 591 . 63 ARG HG2 H 1.55 0.03 1 592 . 63 ARG HG3 H 1.55 0.03 1 593 . 63 ARG HD2 H 3.19 0.03 1 594 . 63 ARG HD3 H 3.19 0.03 1 595 . 63 ARG CA C 56.52 0.50 1 596 . 63 ARG CB C 26.57 0.50 1 597 . 63 ARG CG C 27.01 0.50 1 598 . 63 ARG CD C 43.51 0.50 1 599 . 63 ARG N N 117.25 0.50 1 600 . 64 LEU H H 7.57 0.03 1 601 . 64 LEU HA H 4.24 0.03 1 602 . 64 LEU HB2 H 1.06 0.03 1 603 . 64 LEU HB3 H 1.61 0.03 1 604 . 64 LEU HG H 1.46 0.03 1 605 . 64 LEU HD1 H 0.14 0.03 2 606 . 64 LEU HD2 H 0.51 0.03 2 607 . 64 LEU CA C 54.63 0.50 1 608 . 64 LEU CB C 40.97 0.50 1 609 . 64 LEU CG C 25.08 0.50 1 610 . 64 LEU CD1 C 24.82 0.50 2 611 . 64 LEU CD2 C 22.71 0.50 2 612 . 64 LEU N N 116.66 0.50 1 613 . 65 VAL H H 8.34 0.03 1 614 . 65 VAL HA H 4.10 0.03 1 615 . 65 VAL HB H 2.18 0.03 1 616 . 65 VAL HG2 H 0.92 0.03 1 617 . 65 VAL HG1 H 0.92 0.03 1 618 . 65 VAL CA C 62.93 0.50 1 619 . 65 VAL CB C 32.92 0.50 1 620 . 65 VAL CG2 C 21.50 0.50 1 621 . 65 VAL CG1 C 20.10 0.50 1 622 . 65 VAL N N 119.87 0.50 1 623 . 66 VAL H H 7.64 0.03 1 624 . 66 VAL HA H 4.39 0.03 1 625 . 66 VAL HB H 1.98 0.03 1 626 . 66 VAL HG1 H 0.94 0.03 1 627 . 66 VAL CA C 61.31 0.50 1 628 . 66 VAL CB C 35.02 0.50 1 629 . 66 VAL CG1 C 21.20 0.50 1 630 . 66 VAL N N 119.65 0.50 1 631 . 67 THR H H 7.82 0.03 1 632 . 67 THR HA H 4.38 0.03 1 633 . 67 THR HB H 4.03 0.03 1 634 . 67 THR HG2 H 1.03 0.03 1 635 . 67 THR CA C 58.67 0.50 1 636 . 67 THR CB C 69.61 0.50 1 637 . 67 THR CG2 C 22.39 0.50 1 638 . 67 THR N N 113.75 0.50 1 639 . 68 PRO HA H 5.11 0.03 1 640 . 68 PRO HB2 H 1.96 0.03 1 641 . 68 PRO HB3 H 2.61 0.03 1 642 . 68 PRO HG2 H 1.93 0.03 1 643 . 68 PRO HG3 H 1.93 0.03 1 644 . 68 PRO HD2 H 3.54 0.03 1 645 . 68 PRO HD3 H 3.54 0.03 1 646 . 68 PRO CA C 62.14 0.50 1 647 . 68 PRO CB C 35.67 0.50 1 648 . 68 PRO CG C 25.14 0.50 1 649 . 68 PRO CD C 50.69 0.50 1 650 . 68 PRO N N 132.89 0.50 1 651 . 69 ALA H H 8.73 0.03 1 652 . 69 ALA HA H 5.14 0.03 1 653 . 69 ALA HB H 1.49 0.03 1 654 . 69 ALA CA C 51.71 0.50 1 655 . 69 ALA CB C 23.45 0.50 1 656 . 69 ALA N N 121.45 0.50 1 657 . 70 LEU H H 9.71 0.03 1 658 . 70 LEU HA H 5.47 0.03 1 659 . 70 LEU HB2 H 1.56 0.03 1 660 . 70 LEU HB3 H 2.06 0.03 1 661 . 70 LEU HG H 1.69 0.03 1 662 . 70 LEU HD1 H 1.11 0.03 1 663 . 70 LEU HD2 H 1.11 0.03 1 664 . 70 LEU CA C 53.42 0.50 1 665 . 70 LEU CB C 46.26 0.50 1 666 . 70 LEU CG C 27.60 0.50 1 667 . 70 LEU CD1 C 26.38 0.50 1 668 . 70 LEU CD2 C 26.38 0.50 1 669 . 70 LEU N N 125.54 0.50 1 670 . 71 VAL H H 9.94 0.03 1 671 . 71 VAL HA H 4.77 0.03 1 672 . 71 VAL HB H 2.12 0.03 1 673 . 71 VAL HG1 H 0.84 0.03 1 674 . 71 VAL HG2 H 0.38 0.03 1 675 . 71 VAL CA C 60.91 0.50 1 676 . 71 VAL CB C 34.22 0.50 1 677 . 71 VAL CG1 C 21.66 0.50 1 678 . 71 VAL CG2 C 20.90 0.50 1 679 . 71 VAL N N 127.50 0.50 1 680 . 72 LYS H H 9.12 0.03 1 681 . 72 LYS HA H 4.60 0.03 1 682 . 72 LYS HB2 H 1.08 0.03 2 683 . 72 LYS HB3 H 0.61 0.03 2 684 . 72 LYS CA C 55.52 0.50 1 685 . 72 LYS CB C 31.48 0.50 1 686 . 72 LYS N N 130.27 0.50 1 687 . 73 ILE H H 8.52 0.03 1 688 . 73 ILE HA H 4.00 0.03 1 689 . 73 ILE HB H 1.89 0.03 1 690 . 73 ILE HG12 H 1.33 0.03 2 691 . 73 ILE HG13 H 1.05 0.03 2 692 . 73 ILE HD1 H 0.81 0.03 1 693 . 73 ILE HG2 H 0.87 0.03 1 694 . 73 ILE CA C 61.96 0.50 1 695 . 73 ILE CB C 38.68 0.50 1 696 . 73 ILE CG1 C 28.02 0.50 1 697 . 73 ILE CG2 C 18.16 0.50 1 698 . 73 ILE CD1 C 13.22 0.50 1 699 . 73 ILE N N 124.99 0.50 1 700 . 74 GLY H H 7.40 0.03 1 701 . 74 GLY HA2 H 3.53 0.03 2 702 . 74 GLY HA3 H 4.01 0.03 2 703 . 74 GLY CA C 44.70 0.50 1 704 . 74 GLY N N 106.80 0.50 1 705 . 75 PRO HA H 4.54 0.03 1 706 . 75 PRO HB2 H 2.06 0.03 1 707 . 75 PRO HB3 H 2.29 0.03 1 708 . 75 PRO HG2 H 1.77 0.03 2 709 . 75 PRO HG3 H 1.79 0.03 2 710 . 75 PRO HD2 H 3.42 0.03 1 711 . 75 PRO HD3 H 3.82 0.03 1 712 . 75 PRO CA C 61.87 0.50 1 713 . 75 PRO CB C 34.67 0.50 1 714 . 75 PRO CG C 24.82 0.50 1 715 . 75 PRO CD C 49.92 0.50 1 716 . 76 GLY H H 8.63 0.03 1 717 . 76 GLY HA2 H 3.70 0.03 2 718 . 76 GLY HA3 H 4.08 0.03 2 719 . 76 GLY CA C 45.16 0.50 1 720 . 76 GLY N N 108.07 0.50 1 721 . 77 SER H H 8.43 0.03 1 722 . 77 SER HA H 4.24 0.03 1 723 . 77 SER HB2 H 3.89 0.03 2 724 . 77 SER HB3 H 3.79 0.03 2 725 . 77 SER CA C 58.60 0.50 1 726 . 77 SER CB C 64.06 0.50 1 727 . 77 SER N N 116.61 0.50 1 728 . 78 ARG H H 8.46 0.03 1 729 . 78 ARG HA H 4.73 0.03 1 730 . 78 ARG HB2 H 1.90 0.03 2 731 . 78 ARG HB3 H 1.66 0.03 2 732 . 78 ARG HG2 H 1.37 0.03 2 733 . 78 ARG HG3 H 1.64 0.03 2 734 . 78 ARG HD2 H 2.98 0.03 2 735 . 78 ARG HD3 H 3.13 0.03 2 736 . 78 ARG CA C 56.15 0.50 1 737 . 78 ARG CB C 30.96 0.50 1 738 . 78 ARG CD C 44.08 0.50 1 739 . 78 ARG CG C 27.22 0.50 1 740 . 78 ARG N N 124.09 0.50 1 741 . 79 GLN H H 8.19 0.03 1 742 . 79 GLN HA H 4.73 0.03 1 743 . 79 GLN HB2 H 2.06 0.03 2 744 . 79 GLN HB3 H 1.76 0.03 2 745 . 79 GLN HG2 H 2.37 0.03 1 746 . 79 GLN HG3 H 2.37 0.03 1 747 . 79 GLN CA C 54.96 0.50 1 748 . 79 GLN CB C 33.48 0.50 1 749 . 79 GLN CG C 34.05 0.50 1 750 . 79 GLN N N 124.81 0.50 1 751 . 80 VAL H H 8.76 0.03 1 752 . 80 VAL HA H 4.84 0.03 1 753 . 80 VAL HB H 1.99 0.03 1 754 . 80 VAL HG1 H 0.85 0.03 1 755 . 80 VAL CA C 61.76 0.50 1 756 . 80 VAL CB C 33.76 0.50 1 757 . 80 VAL CG1 C 21.21 0.50 1 758 . 80 VAL N N 123.52 0.50 1 759 . 81 LEU H H 9.68 0.03 1 760 . 81 LEU HA H 5.01 0.03 1 761 . 81 LEU HB2 H 1.94 0.03 1 762 . 81 LEU HB3 H 1.54 0.03 1 763 . 81 LEU HG H 1.94 0.03 1 764 . 81 LEU HD1 H 0.93 0.03 2 765 . 81 LEU HD2 H 0.99 0.03 2 766 . 81 LEU CA C 53.65 0.50 1 767 . 81 LEU CB C 43.54 0.50 1 768 . 81 LEU CG C 27.89 0.50 1 769 . 81 LEU CD1 C 25.44 0.50 1 770 . 81 LEU CD2 C 23.99 0.50 1 771 . 81 LEU N N 129.73 0.50 1 772 . 82 SER H H 8.96 0.03 1 773 . 82 SER HA H 5.05 0.03 1 774 . 82 SER HB2 H 3.88 0.03 2 775 . 82 SER HB3 H 3.79 0.03 2 776 . 82 SER CA C 58.22 0.50 1 777 . 82 SER CB C 66.29 0.50 1 778 . 82 SER N N 116.43 0.50 1 779 . 83 GLY H H 8.47 0.03 1 780 . 83 GLY HA2 H 3.69 0.03 1 781 . 83 GLY HA3 H 4.67 0.03 1 782 . 83 GLY CA C 44.00 0.50 1 783 . 83 GLY N N 107.24 0.50 1 784 . 84 ILE H H 8.47 0.03 1 785 . 84 ILE HA H 3.98 0.03 1 786 . 84 ILE HB H 2.01 0.03 1 787 . 84 ILE HG2 H 1.03 0.03 1 788 . 84 ILE HG12 H 1.37 0.03 2 789 . 84 ILE HG13 H 1.53 0.03 2 790 . 84 ILE HD1 H 0.99 0.03 1 791 . 84 ILE CA C 63.73 0.50 1 792 . 84 ILE CB C 38.37 0.50 1 793 . 84 ILE CG1 C 27.73 0.50 1 794 . 84 ILE CG2 C 18.00 0.50 1 795 . 84 ILE CD1 C 13.23 0.50 1 796 . 84 ILE N N 116.57 0.50 1 797 . 85 ASP H H 8.37 0.03 1 798 . 85 ASP HA H 4.95 0.03 1 799 . 85 ASP HB2 H 3.06 0.03 1 800 . 85 ASP HB3 H 2.65 0.03 1 801 . 85 ASP CA C 53.05 0.50 1 802 . 85 ASP CB C 39.83 0.50 1 803 . 85 ASP N N 119.57 0.50 1 804 . 86 LEU H H 7.54 0.03 1 805 . 86 LEU HA H 3.81 0.03 1 806 . 86 LEU HB2 H 1.70 0.03 1 807 . 86 LEU HB3 H 1.89 0.03 1 808 . 86 LEU HG H 1.60 0.03 1 809 . 86 LEU HD1 H 0.78 0.03 2 810 . 86 LEU CA C 59.75 0.50 1 811 . 86 LEU CB C 41.95 0.50 1 812 . 86 LEU CG C 27.46 0.50 1 813 . 86 LEU CD1 C 26.00 0.50 2 814 . 86 LEU N N 121.11 0.50 1 815 . 87 THR H H 8.55 0.03 1 816 . 87 THR HA H 3.67 0.03 1 817 . 87 THR HB H 4.18 0.03 1 818 . 87 THR HG2 H 1.21 0.03 1 819 . 87 THR CA C 66.09 0.50 1 820 . 87 THR CB C 66.73 0.50 1 821 . 87 THR CG2 C 23.66 0.50 1 822 . 87 THR N N 109.48 0.50 1 823 . 88 ASP H H 7.44 0.03 1 824 . 88 ASP HA H 4.42 0.03 1 825 . 88 ASP HB2 H 2.71 0.03 2 826 . 88 ASP HB3 H 2.81 0.03 2 827 . 88 ASP CA C 57.24 0.50 1 828 . 88 ASP CB C 40.62 0.50 1 829 . 88 ASP N N 123.98 0.50 1 830 . 89 GLN H H 7.84 0.03 1 831 . 89 GLN HA H 4.13 0.03 1 832 . 89 GLN HB2 H 2.20 0.03 2 833 . 89 GLN HB3 H 2.08 0.03 2 834 . 89 GLN HG2 H 2.35 0.03 1 835 . 89 GLN HG3 H 2.35 0.03 1 836 . 89 GLN CA C 58.76 0.50 1 837 . 89 GLN CB C 30.02 0.50 1 838 . 89 GLN CG C 34.42 0.50 1 839 . 89 GLN N N 118.32 0.50 1 840 . 90 LEU H H 8.54 0.03 1 841 . 90 LEU HA H 3.55 0.03 1 842 . 90 LEU HB2 H 1.31 0.03 1 843 . 90 LEU HB3 H 2.02 0.03 1 844 . 90 LEU HD1 H 0.91 0.03 1 845 . 90 LEU CA C 57.98 0.50 1 846 . 90 LEU CB C 41.55 0.50 1 847 . 90 LEU CG C 27.53 0.50 1 848 . 90 LEU CD1 C 24.19 0.50 1 849 . 90 LEU N N 120.19 0.50 1 850 . 91 ALA H H 7.86 0.03 1 851 . 91 ALA HA H 3.84 0.03 1 852 . 91 ALA HB H 1.48 0.03 1 853 . 91 ALA CA C 55.13 0.50 1 854 . 91 ALA CB C 17.84 0.50 1 855 . 91 ALA N N 119.04 0.50 1 856 . 92 ASN H H 7.34 0.03 1 857 . 92 ASN HA H 4.50 0.03 1 858 . 92 ASN HB2 H 2.85 0.03 1 859 . 92 ASN HB3 H 2.76 0.03 1 860 . 92 ASN CA C 55.18 0.50 1 861 . 92 ASN CB C 39.61 0.50 1 862 . 92 ASN N N 112.56 0.50 1 863 . 93 GLN H H 7.90 0.03 1 864 . 93 GLN HA H 3.92 0.03 1 865 . 93 GLN HB2 H 1.16 0.03 1 866 . 93 GLN HB3 H 1.09 0.03 1 867 . 93 GLN HG2 H 1.95 0.03 2 868 . 93 GLN HG3 H 2.20 0.03 2 869 . 93 GLN HE21 H 6.88 0.03 2 870 . 93 GLN CA C 56.83 0.50 1 871 . 93 GLN CB C 29.28 0.50 1 872 . 93 GLN CG C 34.18 0.50 1 873 . 93 GLN N N 117.66 0.50 1 874 . 93 GLN NE2 N 112.47 0.50 1 875 . 94 LEU H H 8.06 0.03 1 876 . 94 LEU HA H 3.72 0.03 1 877 . 94 LEU HB2 H 1.44 0.03 1 878 . 94 LEU HB3 H 1.67 0.03 1 879 . 94 LEU HG H 1.55 0.03 1 880 . 94 LEU CA C 59.68 0.50 1 881 . 94 LEU CB C 39.72 0.50 1 882 . 94 LEU N N 119.56 0.50 1 883 . 95 PRO HA H 4.19 0.03 1 884 . 95 PRO HB2 H 1.76 0.03 1 885 . 95 PRO HB3 H 2.32 0.03 1 886 . 95 PRO HG2 H 2.06 0.03 1 887 . 95 PRO HG3 H 1.88 0.03 1 888 . 95 PRO HD2 H 3.29 0.03 1 889 . 95 PRO HD3 H 3.50 0.03 1 890 . 95 PRO CA C 66.28 0.50 1 891 . 95 PRO CB C 30.93 0.50 1 892 . 95 PRO CG C 28.70 0.50 1 893 . 95 PRO CD C 50.22 0.50 1 894 . 95 PRO N N 132.56 0.50 1 895 . 96 GLN H H 7.16 0.03 1 896 . 96 GLN HA H 4.23 0.03 1 897 . 96 GLN HB2 H 2.20 0.03 1 898 . 96 GLN HB3 H 2.20 0.03 1 899 . 96 GLN HG2 H 2.41 0.03 1 900 . 96 GLN HG3 H 2.41 0.03 1 901 . 96 GLN HE21 H 7.39 0.03 2 902 . 96 GLN CA C 57.97 0.50 1 903 . 96 GLN CB C 28.27 0.50 1 904 . 96 GLN CG C 34.38 0.50 1 905 . 96 GLN N N 114.08 0.50 1 906 . 96 GLN NE2 N 111.75 0.50 1 907 . 97 TRP H H 8.11 0.03 1 908 . 97 TRP HA H 4.80 0.03 1 909 . 97 TRP HB2 H 3.14 0.03 1 910 . 97 TRP HB3 H 3.60 0.03 1 911 . 97 TRP HD1 H 7.15 0.03 1 912 . 97 TRP HE1 H 10.20 0.03 1 913 . 97 TRP HH2 H 6.81 0.03 1 914 . 97 TRP HZ2 H 7.13 0.03 1 915 . 97 TRP CA C 57.00 0.50 1 916 . 97 TRP CB C 29.26 0.50 1 917 . 97 TRP CD1 C 124.50 0.50 1 918 . 97 TRP CH2 C 123.50 0.50 1 919 . 97 TRP CZ2 C 113.87 0.50 1 920 . 97 TRP N N 120.74 0.50 1 921 . 97 TRP NE1 N 128.91 0.50 1 922 . 98 LEU H H 7.80 0.03 1 923 . 98 LEU HA H 4.27 0.03 1 924 . 98 LEU HB2 H 1.89 0.03 1 925 . 98 LEU HB3 H 1.66 0.03 1 926 . 98 LEU HD1 H 0.91 0.03 1 927 . 98 LEU CA C 56.45 0.50 1 928 . 98 LEU CB C 41.93 0.50 1 929 . 98 LEU CG C 26.26 0.50 1 930 . 98 LEU CD1 C 23.23 0.50 1 931 . 98 LEU N N 116.27 0.50 1 932 . 99 VAL H H 7.37 0.03 1 933 . 99 VAL HA H 4.19 0.03 1 934 . 99 VAL HB H 2.27 0.03 1 935 . 99 VAL HG1 H 1.04 0.03 1 936 . 99 VAL CA C 63.09 0.50 1 937 . 99 VAL CB C 32.40 0.50 1 938 . 99 VAL CG1 C 21.29 0.50 1 939 . 99 VAL N N 117.16 0.50 1 940 . 100 GLN H H 8.10 0.03 1 941 . 100 GLN HA H 4.32 0.03 1 942 . 100 GLN HB2 H 2.05 0.03 1 943 . 100 GLN HB3 H 2.21 0.03 1 944 . 100 GLN HG2 H 2.54 0.03 1 945 . 100 GLN HG3 H 2.54 0.03 1 946 . 100 GLN CA C 56.71 0.50 1 947 . 100 GLN CB C 28.88 0.50 1 948 . 100 GLN CG C 34.10 0.50 1 949 . 100 GLN N N 122.39 0.50 1 950 . 101 GLN H H 8.27 0.03 1 951 . 101 GLN HA H 4.34 0.03 1 952 . 101 GLN HB2 H 2.02 0.03 2 953 . 101 GLN HB3 H 2.19 0.03 2 954 . 101 GLN HG2 H 2.41 0.03 1 955 . 101 GLN HG3 H 2.41 0.03 1 956 . 101 GLN CA C 56.05 0.50 1 957 . 101 GLN CB C 29.82 0.50 1 958 . 101 GLN CG C 34.00 0.50 1 959 . 101 GLN N N 120.57 0.50 1 960 . 102 GLU H H 8.36 0.03 1 961 . 102 GLU HA H 4.31 0.03 1 962 . 102 GLU HB2 H 2.07 0.03 1 963 . 102 GLU HB3 H 2.07 0.03 1 964 . 102 GLU HG2 H 2.33 0.03 1 965 . 102 GLU HG3 H 2.33 0.03 1 966 . 102 GLU CA C 56.88 0.50 1 967 . 102 GLU CB C 30.33 0.50 1 968 . 102 GLU CG C 36.48 0.50 1 969 . 102 GLU N N 121.35 0.50 1 970 . 103 GLY H H 8.37 0.03 1 971 . 103 GLY HA2 H 3.95 0.03 1 972 . 103 GLY HA3 H 3.95 0.03 1 973 . 103 GLY CA C 45.44 0.50 1 974 . 103 GLY N N 109.43 0.50 1 975 . 104 ILE H H 7.72 0.03 1 976 . 104 ILE HA H 4.14 0.03 1 977 . 104 ILE HB H 1.80 0.03 1 978 . 104 ILE HG12 H 1.32 0.03 2 979 . 104 ILE HG13 H 1.08 0.03 2 980 . 104 ILE HG2 H 0.82 0.03 1 981 . 104 ILE HD1 H 0.81 0.03 1 982 . 104 ILE CA C 61.02 0.50 1 983 . 104 ILE CB C 38.59 0.50 1 984 . 104 ILE CG1 C 26.91 0.50 1 985 . 104 ILE CG2 C 17.51 0.50 1 986 . 104 ILE CD1 C 13.16 0.50 1 987 . 104 ILE N N 119.75 0.50 1 988 . 105 PHE H H 7.77 0.03 1 989 . 105 PHE HA H 4.51 0.03 1 990 . 105 PHE HB2 H 2.95 0.03 1 991 . 105 PHE HB3 H 3.20 0.03 1 992 . 105 PHE HD1 H 7.23 0.03 1 993 . 105 PHE HD2 H 7.24 0.03 1 994 . 105 PHE CA C 58.96 0.50 1 995 . 105 PHE CB C 40.60 0.50 1 996 . 105 PHE CD1 C 132.13 0.50 1 997 . 105 PHE CD2 C 132.01 0.50 1 998 . 105 PHE N N 128.83 0.50 1 stop_ save_