data_5064 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N resonance assignments for a 14 kD protein, GABAA receptor associated protein (GABARAP) ; _BMRB_accession_number 5064 _BMRB_flat_file_name bmr5064.str _Entry_type original _Submission_date 2001-06-29 _Accession_date 2001-06-29 _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 Harris Richard . . 2 McAlister Mark S.B. . 3 Sankar Andrew . . 4 Moss Stephen J. . 5 Keep Nicholas H. . 6 Driscoll Paul C. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 345 "13C chemical shifts" 343 "15N chemical shifts" 91 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-11-06 original author . stop_ _Original_release_date 2001-11-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments for a 14 kD protein, GABAA receptor associated protein (GABARAP) ; _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 Harris Richard . . 2 McAlister Mark S.B. . 3 Sankar Andrew . . 4 Phelan John P. . 5 Moss Stephen J. . 6 Keep Nicholas H. . 7 Driscoll Paul C. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 21 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 185 _Page_last 186 _Year 2001 _Details . save_ ################################## # Molecular system description # ################################## save_system_GABARAP _Saveframe_category molecular_system _Mol_system_name 'GABAA receptor associated protein' _Abbreviation_common GABARAP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label GABARAP $GABARAP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details ; Expressed construct contains an N-terminal hexahistidine purification tag: MGSSHHHHHHSSGLVPRGS before the initiating Met of GABARAP. ; save_ ######################## # Monomeric polymers # ######################## save_GABARAP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'GABA(A) receptor associated protein' _Abbreviation_common GABARAP _Molecular_mass 15998 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 136 _Mol_residue_sequence ; MGSSHHHHHHSSGLVPRGSM KFVYKEEHPFEKRRSEGEKI RKKYPDRVPVIVEKAPKARI GDLDKKKYLVPSDLTVGQFY FLIRKRIHLRAEDALFFFVN NVIPPTSATMGQLYQEHHEE DFFLYIAYSDESVYGL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -18 MET 2 -17 GLY 3 -16 SER 4 -15 SER 5 -14 HIS 6 -13 HIS 7 -12 HIS 8 -11 HIS 9 -10 HIS 10 -9 HIS 11 -8 SER 12 -7 SER 13 -6 GLY 14 -5 LEU 15 -4 VAL 16 -3 PRO 17 -2 ARG 18 -1 GLY 19 0 SER 20 1 MET 21 2 LYS 22 3 PHE 23 4 VAL 24 5 TYR 25 6 LYS 26 7 GLU 27 8 GLU 28 9 HIS 29 10 PRO 30 11 PHE 31 12 GLU 32 13 LYS 33 14 ARG 34 15 ARG 35 16 SER 36 17 GLU 37 18 GLY 38 19 GLU 39 20 LYS 40 21 ILE 41 22 ARG 42 23 LYS 43 24 LYS 44 25 TYR 45 26 PRO 46 27 ASP 47 28 ARG 48 29 VAL 49 30 PRO 50 31 VAL 51 32 ILE 52 33 VAL 53 34 GLU 54 35 LYS 55 36 ALA 56 37 PRO 57 38 LYS 58 39 ALA 59 40 ARG 60 41 ILE 61 42 GLY 62 43 ASP 63 44 LEU 64 45 ASP 65 46 LYS 66 47 LYS 67 48 LYS 68 49 TYR 69 50 LEU 70 51 VAL 71 52 PRO 72 53 SER 73 54 ASP 74 55 LEU 75 56 THR 76 57 VAL 77 58 GLY 78 59 GLN 79 60 PHE 80 61 TYR 81 62 PHE 82 63 LEU 83 64 ILE 84 65 ARG 85 66 LYS 86 67 ARG 87 68 ILE 88 69 HIS 89 70 LEU 90 71 ARG 91 72 ALA 92 73 GLU 93 74 ASP 94 75 ALA 95 76 LEU 96 77 PHE 97 78 PHE 98 79 PHE 99 80 VAL 100 81 ASN 101 82 ASN 102 83 VAL 103 84 ILE 104 85 PRO 105 86 PRO 106 87 THR 107 88 SER 108 89 ALA 109 90 THR 110 91 MET 111 92 GLY 112 93 GLN 113 94 LEU 114 95 TYR 115 96 GLN 116 97 GLU 117 98 HIS 118 99 HIS 119 100 GLU 120 101 GLU 121 102 ASP 122 103 PHE 123 104 PHE 124 105 LEU 125 106 TYR 126 107 ILE 127 108 ALA 128 109 TYR 129 110 SER 130 111 ASP 131 112 GLU 132 113 SER 133 114 VAL 134 115 TYR 135 116 GLY 136 117 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 5058 GABARAP 87.50 119 100.00 100.00 7.20e-80 BMRB 5128 GABARAP 86.03 117 100.00 100.00 3.66e-78 PDB 1GNU "Gaba(a) Receptor Associated Protein Gabarap" 86.03 117 100.00 100.00 3.66e-78 PDB 1KJT "Crystal Structure Of The Gaba(A) Receptor Associated Protein, Gabarap" 87.50 119 99.16 99.16 4.08e-79 PDB 1KLV "Solution Structure And Backbone Dynamics Of Gabarap, Gabaa Receptor Associated Protein" 86.03 117 100.00 100.00 3.66e-78 PDB 1KM7 "Solution Structure And Backbone Dynamics Of Gabarap, Gabaa Receptor Associated Protein" 86.03 117 100.00 100.00 3.66e-78 PDB 1KOT "Solution Structure Of Human Gaba Receptor Associated Protein Gabarap" 87.50 119 100.00 100.00 7.20e-80 PDB 3D32 "Complex Of Gaba(a) Receptor-associated Protein (gabarap) With A Synthetic Peptide" 87.50 119 100.00 100.00 7.20e-80 PDB 3DOW "Complex Structure Of Gaba Type A Receptor Associated Protein And Its Binding Epitope On Calreticulin" 87.50 119 100.00 100.00 7.20e-80 PDB 3WIM "Gabarap-lir Peptide Complex" 86.03 117 100.00 100.00 3.66e-78 DBJ BAB21549 "MAP1 light chain 3 related protein [Homo sapiens]" 86.03 117 100.00 100.00 3.66e-78 DBJ BAB22426 "unnamed protein product [Mus musculus]" 86.03 117 99.15 100.00 1.46e-77 DBJ BAB27806 "unnamed protein product [Mus musculus]" 86.03 117 100.00 100.00 3.66e-78 DBJ BAG35138 "unnamed protein product [Homo sapiens]" 86.03 117 99.15 100.00 9.16e-78 EMBL CAG00707 "unnamed protein product, partial [Tetraodon nigroviridis]" 85.29 116 98.28 98.28 2.64e-75 EMBL CAG33324 "GABARAP [Homo sapiens]" 86.03 117 100.00 100.00 3.66e-78 EMBL CAG47031 "GABARAP [Homo sapiens]" 86.03 117 100.00 100.00 3.66e-78 EMBL CAP17839 "GABAA receptor-associated protein 1 [Carassius carassius]" 69.85 95 100.00 100.00 2.44e-61 EMBL CDQ58630 "unnamed protein product [Oncorhynchus mykiss]" 85.29 122 98.28 99.14 3.53e-76 GB AAD02337 "MM46 [Homo sapiens]" 86.03 117 100.00 100.00 3.66e-78 GB AAD32455 "ganglioside expression factor 2 homolog [Homo sapiens]" 86.03 117 100.00 100.00 3.66e-78 GB AAD47641 "GABA-A receptor-associated protein [Homo sapiens]" 86.03 117 100.00 100.00 3.66e-78 GB AAD47642 "GABA-A receptor-associated protein [Mus musculus]" 86.03 117 100.00 100.00 3.66e-78 GB AAD47643 "GABA-A receptor-associated protein [Rattus norvegicus]" 86.03 117 100.00 100.00 3.66e-78 REF NP_001011192 "GABA(A) receptor-associated protein like 1 [Xenopus (Silurana) tropicalis]" 86.03 117 100.00 100.00 3.66e-78 REF NP_001013278 "GABA(A) receptor-associated protein [Danio rerio]" 85.29 122 98.28 99.14 6.94e-76 REF NP_001029220 "gamma-aminobutyric acid receptor-associated protein [Bos taurus]" 86.03 117 100.00 100.00 3.66e-78 REF NP_001075611 "gamma-aminobutyric acid receptor-associated protein [Oryctolagus cuniculus]" 86.03 117 100.00 100.00 3.66e-78 REF NP_001084530 "uncharacterized protein LOC414477 [Xenopus laevis]" 86.03 117 98.29 99.15 4.76e-77 SP O95166 "RecName: Full=Gamma-aminobutyric acid receptor-associated protein; AltName: Full=GABA(A) receptor-associated protein; AltName: " 86.03 117 100.00 100.00 3.66e-78 SP P60517 "RecName: Full=Gamma-aminobutyric acid receptor-associated protein; AltName: Full=GABA(A) receptor-associated protein; Flags: Pr" 86.03 117 100.00 100.00 3.66e-78 SP Q8MK68 "RecName: Full=Gamma-aminobutyric acid receptor-associated protein; AltName: Full=GABA(A) receptor-associated protein; Flags: Pr" 86.03 117 100.00 100.00 3.66e-78 SP Q9DCD6 "RecName: Full=Gamma-aminobutyric acid receptor-associated protein; AltName: Full=GABA(A) receptor-associated protein; Flags: Pr" 86.03 117 100.00 100.00 3.66e-78 SP Q9GJW7 "RecName: Full=Gamma-aminobutyric acid receptor-associated protein; AltName: Full=GABA(A) receptor-associated protein; Flags: Pr" 86.03 117 100.00 100.00 3.66e-78 TPG DAA18837 "TPA: gamma-aminobutyric acid receptor-associated protein [Bos taurus]" 86.03 117 100.00 100.00 3.66e-78 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GABARAP Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_type _Vector_name $GABARAP 'recombinant technology' 'E. coli' Escherichia coli BL21 DE3 plasmid pET stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GABARAP . mM 0.5 1.0 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_nmrPIPE _Saveframe_category software _Name nmrPIPE _Version . loop_ _Task 'data processing' stop_ _Details ; Delaglio et al. Journal of Biomolecular NMR (1995) 6, 277-293. ; save_ save_ANSIG _Saveframe_category software _Name ANSIG _Version v3.3 loop_ _Task 'spectral analysis' stop_ _Details ; Kraulis et al. Biochemistry (1994) 33, 3315-3531. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_1H-13C_HCCH-TOCSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HCCH-TOCSY' _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCA_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCACB_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_9 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . 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 '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.2 n/a temperature 293 0.2 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 H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; Analysis of the triple resonance experiments allowed identification and sequential assignments for 91 out of the 110 GABARAP (117 less 7 prolines) backbone 15N and amide proton resonances (i.e. not including the hexahistidine tag). Definitive assignments have not been obtained for residues Met1-His9, Phe11-Arg15, Arg22, Lys47, Glu100, Phe103, and Phe104). Conformational slow exchange is observed as NH cross peak doubling for residues Glu17, Glu19, Lys20 and Leu105. Nine backbone NH cross-peaks in the HSQC spectrum, including two that display evidence of slow conformational exchange, remain unassigned to specific residues. The absence of an unambiguously identifiable NH crosspeak for 10 residues is tentatively attributed to exchange broadening. Examination of the spectrum under a variety of sample conditions (temperature, pH, peptide ligands, co-solvents) has failed to reveal these ?missing peaks?. Similar characteristics are obtained for a de-tagged variant of GABARAP and GABARAP expressed in the absence of a hexahistidine tag." ; loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name GABARAP _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 . 34 ARG CA C 58.265 0.05 1 2 . 34 ARG C C 178.7 0.05 1 3 . 34 ARG CB C 29.482 0.05 1 4 . 35 SER N N 112.389 0.05 1 5 . 35 SER H H 7.628 0.005 1 6 . 35 SER CA C 61.423 0.05 1 7 . 35 SER HA H 4.267 0.005 1 8 . 35 SER C C 177.758 0.05 1 9 . 35 SER CB C 62.864 0.05 1 10 . 35 SER HB2 H 4.017 0.005 2 11 . 36 GLU N N 121.794 0.05 1 12 . 36 GLU H H 7.77 0.005 1 13 . 36 GLU CA C 59.453 0.05 1 14 . 36 GLU HA H 4.108 0.005 1 15 . 36 GLU C C 179.514 0.05 1 16 . 36 GLU CB C 29.457 0.05 1 17 . 37 GLY N N 109.928 0.05 1 18 . 37 GLY H H 9.551 0.005 1 19 . 37 GLY CA C 47.365 0.05 1 20 . 37 GLY HA2 H 3.082 0.005 2 21 . 37 GLY HA3 H 4.087 0.005 2 22 . 37 GLY C C 176.044 0.05 1 23 . 38 GLU N N 120.555 0.05 1 24 . 38 GLU H H 8.722 0.005 1 25 . 38 GLU CA C 59.345 0.05 1 26 . 38 GLU HA H 3.16 0.005 1 27 . 38 GLU C C 179.74 0.05 1 28 . 38 GLU CB C 29.878 0.05 1 29 . 38 GLU CG C 36.805 0.05 1 30 . 38 GLU HG2 H 1.925 0.005 2 31 . 38 GLU HG3 H 2.033 0.005 2 32 . 38 GLU HB2 H 1.911 0.005 2 33 . 39 LYS N N 118.549 0.05 1 34 . 39 LYS H H 7.485 0.005 1 35 . 39 LYS CA C 59.546 0.05 1 36 . 39 LYS HA H 3.891 0.005 1 37 . 39 LYS C C 180.365 0.05 1 38 . 39 LYS CB C 32.576 0.05 1 39 . 39 LYS CG C 25.545 0.05 1 40 . 39 LYS HG2 H 1.377 0.005 2 41 . 39 LYS HG3 H 1.669 0.005 2 42 . 39 LYS CE C 41.768 0.05 1 43 . 39 LYS HB2 H 1.977 0.005 2 44 . 39 LYS HE2 H 2.965 0.005 2 45 . 40 ILE N N 121.326 0.05 1 46 . 40 ILE H H 8.327 0.005 1 47 . 40 ILE CA C 64.604 0.05 1 48 . 40 ILE HA H 3.8 0.005 1 49 . 40 ILE CB C 38.429 0.05 1 50 . 40 ILE HB H 1.824 0.005 1 51 . 40 ILE CG2 C 18.569 0.05 1 52 . 40 ILE HG2 H 0.86 0.005 1 53 . 40 ILE CD1 C 14.239 0.05 1 54 . 40 ILE HD1 H 0.869 0.005 1 55 . 40 ILE HG12 H 1.159 0.005 2 56 . 41 ARG CA C 56.303 0.05 1 57 . 41 ARG C C 178.995 0.05 1 58 . 41 ARG CB C 27.809 0.05 1 59 . 42 LYS N N 116.946 0.05 1 60 . 42 LYS H H 7.396 0.005 1 61 . 42 LYS CA C 57.935 0.05 1 62 . 42 LYS HA H 3.995 0.005 1 63 . 42 LYS C C 178.593 0.05 1 64 . 42 LYS CB C 32.896 0.05 1 65 . 42 LYS CG C 24.519 0.05 1 66 . 42 LYS HG2 H 1.353 0.005 2 67 . 42 LYS HG3 H 1.425 0.005 2 68 . 42 LYS CD C 29.684 0.05 1 69 . 42 LYS CE C 41.757 0.05 1 70 . 42 LYS HB2 H 1.763 0.005 2 71 . 42 LYS HD2 H 1.588 0.005 2 72 . 42 LYS HE2 H 2.878 0.005 2 73 . 43 LYS N N 118.977 0.05 1 74 . 43 LYS H H 7.735 0.005 1 75 . 43 LYS CA C 58.14 0.05 1 76 . 43 LYS HA H 3.802 0.005 1 77 . 43 LYS C C 176.959 0.05 1 78 . 43 LYS CB C 33.602 0.05 1 79 . 43 LYS HB2 H 1.499 0.005 2 80 . 43 LYS HB3 H 1.255 0.005 2 81 . 43 LYS CG C 24.962 0.05 1 82 . 43 LYS HG2 H 0.498 0.005 2 83 . 43 LYS HG3 H 0.934 0.005 2 84 . 43 LYS CD C 29.188 0.05 1 85 . 43 LYS CE C 41.758 0.05 1 86 . 43 LYS HD2 H 1.445 0.005 2 87 . 43 LYS HE2 H 2.791 0.005 2 88 . 44 TYR N N 115.229 0.05 1 89 . 44 TYR H H 8.07 0.005 1 90 . 44 TYR CA C 53.555 0.05 1 91 . 44 TYR HA H 5.091 0.005 1 92 . 44 TYR CB C 38.522 0.05 1 93 . 44 TYR HB2 H 2.679 0.005 2 94 . 44 TYR HB3 H 2.885 0.005 2 95 . 45 PRO CA C 64.515 0.05 1 96 . 45 PRO C C 177.614 0.05 1 97 . 45 PRO CB C 31.952 0.05 1 98 . 46 ASP N N 115.291 0.05 1 99 . 46 ASP H H 8.588 0.005 1 100 . 46 ASP CA C 53.038 0.05 1 101 . 46 ASP HA H 4.708 0.005 1 102 . 46 ASP C C 176.18 0.05 1 103 . 46 ASP CB C 40.533 0.05 1 104 . 46 ASP HB2 H 2.709 0.005 2 105 . 46 ASP HB3 H 2.831 0.005 2 106 . 47 ARG N N 119.391 0.05 1 107 . 47 ARG H H 7.842 0.005 1 108 . 47 ARG CA C 53.706 0.05 1 109 . 47 ARG HA H 4.913 0.005 1 110 . 47 ARG C C 175.023 0.05 1 111 . 47 ARG CB C 34.251 0.05 1 112 . 48 VAL N N 116.427 0.05 1 113 . 48 VAL H H 9.156 0.005 1 114 . 48 VAL CA C 57.168 0.05 1 115 . 48 VAL HA H 4.174 0.005 1 116 . 48 VAL CB C 34.057 0.05 1 117 . 48 VAL HB H 1.394 0.005 1 118 . 48 VAL CG1 C 18.792 0.05 2 119 . 48 VAL HG1 H 0.421 0.005 2 120 . 48 VAL CG2 C 21.866 0.05 2 121 . 48 VAL HG2 H 0.381 0.005 2 122 . 49 PRO CA C 60.963 0.05 1 123 . 49 PRO C C 175.561 0.05 1 124 . 49 PRO CB C 31.586 0.05 1 125 . 50 VAL N N 123.626 0.05 1 126 . 50 VAL H H 8.897 0.005 1 127 . 50 VAL CA C 59.297 0.05 1 128 . 50 VAL HA H 5.123 0.005 1 129 . 50 VAL C C 174.629 0.05 1 130 . 50 VAL CB C 36.274 0.05 1 131 . 50 VAL HB H 1.758 0.005 1 132 . 50 VAL CG1 C 22.485 0.05 2 133 . 50 VAL HG1 H 0.62 0.005 1 134 . 51 ILE N N 128.315 0.05 1 135 . 51 ILE H H 8.819 0.005 1 136 . 51 ILE CA C 56.83 0.05 1 137 . 51 ILE HA H 4.957 0.005 1 138 . 51 ILE C C 175.439 0.05 1 139 . 51 ILE CB C 36.478 0.05 1 140 . 51 ILE HB H 1.293 0.005 1 141 . 51 ILE CG2 C 17.428 0.05 1 142 . 51 ILE HG2 H 0.662 0.005 1 143 . 51 ILE CD1 C 8.659 0.05 1 144 . 51 ILE HD1 H -0.556 0.005 1 145 . 52 VAL N N 126.726 0.05 1 146 . 52 VAL H H 9.13 0.005 1 147 . 52 VAL CA C 59.847 0.05 1 148 . 52 VAL HA H 5.746 0.005 1 149 . 52 VAL C C 176.383 0.05 1 150 . 52 VAL CB C 34.028 0.05 1 151 . 52 VAL HB H 2.064 0.005 1 152 . 52 VAL HG2 H 0.865 0.005 2 153 . 52 VAL CG1 C 22.388 0.05 2 154 . 52 VAL HG1 H 0.857 0.005 1 155 . 53 GLU N N 121.509 0.05 1 156 . 53 GLU H H 8.717 0.005 1 157 . 53 GLU CA C 54.567 0.05 1 158 . 53 GLU HA H 4.977 0.005 1 159 . 53 GLU C C 175.042 0.05 1 160 . 53 GLU CB C 36.4 0.05 1 161 . 53 GLU HB2 H 1.911 0.005 2 162 . 53 GLU HB3 H 2.304 0.005 2 163 . 53 GLU HG2 H 2.61 0.005 2 164 . 54 LYS N N 123.43 0.05 1 165 . 54 LYS H H 8.9 0.005 1 166 . 54 LYS CA C 56.056 0.05 1 167 . 54 LYS HA H 3.07 0.005 1 168 . 54 LYS C C 177.675 0.05 1 169 . 54 LYS CB C 32.867 0.05 1 170 . 55 ALA N N 130.41 0.05 1 171 . 55 ALA H H 8.943 0.005 1 172 . 55 ALA CA C 50.612 0.05 1 173 . 55 ALA HA H 4.424 0.005 1 174 . 55 ALA CB C 18.01 0.05 1 175 . 55 ALA HB H 1.205 0.005 1 176 . 56 PRO CA C 64.861 0.05 1 177 . 56 PRO C C 178.293 0.05 1 178 . 56 PRO CB C 32.099 0.05 1 179 . 57 LYS N N 114.561 0.05 1 180 . 57 LYS H H 8.465 0.005 1 181 . 57 LYS CA C 56.562 0.05 1 182 . 57 LYS HA H 4.057 0.005 1 183 . 57 LYS C C 176.985 0.05 1 184 . 57 LYS CB C 31.184 0.05 1 185 . 58 ALA N N 122.159 0.05 1 186 . 58 ALA H H 7.478 0.005 1 187 . 58 ALA CA C 52.816 0.05 1 188 . 58 ALA HA H 4.475 0.005 1 189 . 58 ALA C C 179.134 0.05 1 190 . 58 ALA CB C 20.932 0.05 1 191 . 58 ALA HB H 1.61 0.005 1 192 . 59 ARG N N 125.002 0.05 1 193 . 59 ARG H H 9.172 0.005 1 194 . 59 ARG CA C 55.748 0.05 1 195 . 59 ARG HA H 4.478 0.005 1 196 . 59 ARG C C 176.313 0.05 1 197 . 59 ARG CB C 29.431 0.05 1 198 . 60 ILE N N 115.5 0.05 1 199 . 60 ILE H H 6.961 0.005 1 200 . 60 ILE CA C 60.13 0.05 1 201 . 60 ILE HA H 4.488 0.005 1 202 . 60 ILE C C 174.415 0.05 1 203 . 60 ILE CB C 40.621 0.05 1 204 . 60 ILE HB H 2.076 0.005 1 205 . 60 ILE HG12 H 1.466 0.005 2 206 . 60 ILE HG13 H 1.785 0.005 2 207 . 60 ILE CG2 C 18.34 0.05 1 208 . 60 ILE HG2 H 1.107 0.005 1 209 . 60 ILE CD1 C 15.697 0.05 1 210 . 60 ILE HD1 H 1.142 0.005 1 211 . 61 GLY N N 108.02 0.05 1 212 . 61 GLY H H 8.337 0.005 1 213 . 61 GLY CA C 45.352 0.05 1 214 . 61 GLY HA2 H 3.895 0.005 2 215 . 61 GLY HA3 H 4.098 0.005 2 216 . 61 GLY C C 173.392 0.05 1 217 . 62 ASP N N 118.877 0.05 1 218 . 62 ASP H H 8.366 0.005 1 219 . 62 ASP CA C 54.044 0.05 1 220 . 62 ASP HA H 4.773 0.005 1 221 . 62 ASP C C 176.308 0.05 1 222 . 62 ASP CB C 43.06 0.05 1 223 . 62 ASP HB2 H 2.535 0.005 2 224 . 62 ASP HB3 H 2.733 0.005 2 225 . 63 LEU N N 123.497 0.05 1 226 . 63 LEU H H 8.151 0.005 1 227 . 63 LEU CA C 54.044 0.05 1 228 . 63 LEU HA H 4.423 0.005 1 229 . 63 LEU C C 177.406 0.05 1 230 . 63 LEU CB C 44.74 0.05 1 231 . 63 LEU HB3 H 1.84 0.005 2 232 . 63 LEU CD1 C 26.212 0.05 2 233 . 63 LEU HD1 H 0.957 0.005 2 234 . 64 ASP N N 122.569 0.05 1 235 . 64 ASP H H 8.726 0.005 1 236 . 64 ASP CA C 55.329 0.05 1 237 . 64 ASP HA H 4.41 0.005 1 238 . 64 ASP C C 176.14 0.05 1 239 . 64 ASP CB C 40.107 0.05 1 240 . 64 ASP HB2 H 2.791 0.005 2 241 . 65 LYS N N 120.57 0.05 1 242 . 65 LYS H H 7.455 0.005 1 243 . 65 LYS CA C 55.324 0.05 1 244 . 65 LYS HA H 4.502 0.005 1 245 . 65 LYS CB C 34.611 0.05 1 246 . 66 LYS CA C 56.634 0.05 1 247 . 66 LYS C C 174.707 0.05 1 248 . 67 LYS N N 119.361 0.05 1 249 . 67 LYS H H 6.968 0.005 1 250 . 67 LYS CA C 54.995 0.05 1 251 . 67 LYS HA H 5.088 0.005 1 252 . 67 LYS C C 175.466 0.05 1 253 . 67 LYS CB C 34.502 0.05 1 254 . 67 LYS HB2 H 1.577 0.005 2 255 . 67 LYS HG2 H 1.214 0.005 2 256 . 68 TYR N N 125.283 0.05 1 257 . 68 TYR H H 9.541 0.005 1 258 . 68 TYR CA C 57.059 0.05 1 259 . 68 TYR C C 174.539 0.05 1 260 . 68 TYR CB C 42.585 0.05 1 261 . 69 LEU N N 125.016 0.05 1 262 . 69 LEU H H 8.659 0.005 1 263 . 69 LEU CA C 53.689 0.05 1 264 . 69 LEU HA H 4.911 0.005 1 265 . 69 LEU C C 177.156 0.05 1 266 . 69 LEU CB C 42.592 0.05 1 267 . 69 LEU CG C 27.384 0.05 1 268 . 69 LEU HG H 1.059 0.005 1 269 . 69 LEU CD1 C 25.003 0.05 2 270 . 69 LEU HD1 H 0.406 0.005 2 271 . 69 LEU CD2 C 24.12 0.05 2 272 . 69 LEU HD2 H 0.458 0.005 2 273 . 69 LEU HB3 H 1.307 0.005 2 274 . 70 VAL N N 121.702 0.05 1 275 . 70 VAL H H 8.455 0.005 1 276 . 70 VAL CA C 58.314 0.05 1 277 . 70 VAL HA H 4.832 0.005 1 278 . 70 VAL CB C 33.35 0.05 1 279 . 70 VAL HB H 1.982 0.005 1 280 . 70 VAL CG1 C 20.479 0.05 2 281 . 70 VAL HG1 H 0.567 0.005 2 282 . 70 VAL CG2 C 22.345 0.05 2 283 . 70 VAL HG2 H 0.877 0.005 2 284 . 71 PRO CA C 63.561 0.05 1 285 . 71 PRO HA H 4.125 0.005 1 286 . 71 PRO C C 178.048 0.05 1 287 . 71 PRO CB C 32.601 0.05 1 288 . 71 PRO CG C 31.683 0.05 1 289 . 71 PRO CD C 48.684 0.05 1 290 . 71 PRO HD2 H 3.338 0.005 2 291 . 71 PRO HD3 H 3.412 0.005 2 292 . 71 PRO HB2 H 2.353 0.005 2 293 . 71 PRO HG2 H 2.064 0.005 2 294 . 72 SER N N 118.386 0.05 1 295 . 72 SER H H 8.38 0.005 1 296 . 72 SER CA C 60.895 0.05 1 297 . 72 SER C C 175.295 0.05 1 298 . 72 SER CB C 62.682 0.05 1 299 . 73 ASP N N 115.373 0.05 1 300 . 73 ASP H H 8.284 0.005 1 301 . 73 ASP CA C 53.355 0.05 1 302 . 73 ASP HA H 4.545 0.005 1 303 . 73 ASP C C 176.879 0.05 1 304 . 73 ASP CB C 40.32 0.05 1 305 . 73 ASP HB2 H 2.709 0.005 2 306 . 73 ASP HB3 H 2.791 0.005 2 307 . 74 LEU N N 123.864 0.05 1 308 . 74 LEU H H 7.405 0.005 1 309 . 74 LEU CA C 55.562 0.05 1 310 . 74 LEU HA H 4.276 0.005 1 311 . 74 LEU C C 177.715 0.05 1 312 . 74 LEU CB C 43.752 0.05 1 313 . 74 LEU HB2 H 1.474 0.005 2 314 . 74 LEU HB3 H 1.724 0.005 2 315 . 74 LEU HD1 H 0.878 0.005 2 316 . 74 LEU CD2 C 25.364 0.05 2 317 . 74 LEU HD2 H 1.001 0.005 2 318 . 75 THR N N 116.727 0.05 1 319 . 75 THR H H 8.775 0.005 1 320 . 75 THR CA C 60.918 0.05 1 321 . 75 THR HA H 4.997 0.005 1 322 . 75 THR C C 176.967 0.05 1 323 . 75 THR CB C 71.342 0.05 1 324 . 75 THR HB H 4.829 0.005 1 325 . 75 THR CG2 C 22.207 0.05 1 326 . 75 THR HG2 H 1.269 0.005 1 327 . 76 VAL N N 123.12 0.05 1 328 . 76 VAL H H 9.145 0.005 1 329 . 76 VAL CA C 66.546 0.05 1 330 . 76 VAL HA H 3.694 0.005 1 331 . 76 VAL C C 179.462 0.05 1 332 . 76 VAL CB C 31.801 0.05 1 333 . 76 VAL HB H 2.401 0.005 1 334 . 76 VAL HG1 H 0.872 0.005 2 335 . 76 VAL HG2 H 0.973 0.005 2 336 . 76 VAL CG1 C 22.699 0.05 2 337 . 77 GLY N N 105.524 0.05 1 338 . 77 GLY H H 8.943 0.005 1 339 . 77 GLY CA C 47.64 0.05 1 340 . 77 GLY HA2 H 3.933 0.005 2 341 . 77 GLY HA3 H 4.106 0.005 2 342 . 77 GLY C C 177.056 0.05 1 343 . 78 GLN N N 121.739 0.05 1 344 . 78 GLN H H 8.148 0.005 1 345 . 78 GLN CA C 58.726 0.05 1 346 . 78 GLN HA H 4.268 0.005 1 347 . 78 GLN C C 180.023 0.05 1 348 . 78 GLN CB C 28.963 0.05 1 349 . 78 GLN CG C 35.217 0.05 1 350 . 78 GLN HB2 H 2.101 0.005 2 351 . 78 GLN HG2 H 2.491 0.005 2 352 . 79 PHE N N 125.694 0.05 1 353 . 79 PHE H H 8.885 0.005 1 354 . 79 PHE CA C 61.266 0.05 1 355 . 79 PHE HA H 4.471 0.005 1 356 . 79 PHE C C 178.173 0.05 1 357 . 79 PHE CB C 39.559 0.05 1 358 . 79 PHE HB2 H 3.157 0.005 2 359 . 79 PHE HB3 H 3.282 0.005 2 360 . 80 TYR N N 118.811 0.05 1 361 . 80 TYR H H 9.156 0.005 1 362 . 80 TYR CA C 61.388 0.05 1 363 . 80 TYR HA H 3.954 0.005 1 364 . 80 TYR C C 178.751 0.05 1 365 . 80 TYR CB C 38.216 0.05 1 366 . 80 TYR HB2 H 2.771 0.005 2 367 . 80 TYR HB3 H 3.021 0.005 2 368 . 81 PHE N N 117.084 0.05 1 369 . 81 PHE H H 7.402 0.005 1 370 . 81 PHE CA C 61.652 0.05 1 371 . 81 PHE HA H 4.048 0.005 1 372 . 81 PHE C C 178.121 0.05 1 373 . 81 PHE CB C 38.623 0.05 1 374 . 81 PHE HB2 H 3.184 0.005 2 375 . 81 PHE HB3 H 3.288 0.005 2 376 . 82 LEU N N 120.433 0.05 1 377 . 82 LEU H H 7.602 0.005 1 378 . 82 LEU CA C 58.356 0.05 1 379 . 82 LEU HA H 3.949 0.005 1 380 . 82 LEU C C 180.138 0.05 1 381 . 82 LEU CB C 42.188 0.05 1 382 . 83 ILE N N 119.929 0.05 1 383 . 83 ILE H H 7.852 0.005 1 384 . 83 ILE CA C 61.337 0.05 1 385 . 83 ILE HA H 3.441 0.005 1 386 . 83 ILE C C 178.371 0.05 1 387 . 83 ILE CB C 34.781 0.05 1 388 . 83 ILE HB H 1.811 0.005 1 389 . 83 ILE CG1 C 26.686 0.05 1 390 . 83 ILE HG12 H 0.459 0.005 2 391 . 83 ILE HG13 H 0.694 0.005 2 392 . 83 ILE CG2 C 17.552 0.05 1 393 . 83 ILE HG2 H 0.373 0.005 1 394 . 83 ILE CD1 C 7.815 0.05 1 395 . 83 ILE HD1 H -0.115 0.005 1 396 . 84 ARG N N 118.83 0.05 1 397 . 84 ARG H H 8.546 0.005 1 398 . 84 ARG CA C 60.473 0.05 1 399 . 84 ARG HA H 3.397 0.005 1 400 . 84 ARG C C 179.143 0.05 1 401 . 84 ARG CB C 30.497 0.05 1 402 . 84 ARG CG C 29.683 0.05 1 403 . 84 ARG CD C 43.128 0.05 1 404 . 84 ARG HB2 H 1.639 0.005 2 405 . 84 ARG HG2 H 1.177 0.005 2 406 . 84 ARG HD2 H 2.827 0.005 2 407 . 85 LYS N N 115.547 0.05 1 408 . 85 LYS H H 7.353 0.005 1 409 . 85 LYS CA C 58.374 0.05 1 410 . 85 LYS HA H 4 0.005 1 411 . 85 LYS C C 180.062 0.05 1 412 . 85 LYS CB C 32.257 0.05 1 413 . 86 ARG N N 118.98 0.05 1 414 . 86 ARG H H 7.552 0.005 1 415 . 86 ARG CA C 58.336 0.05 1 416 . 86 ARG HA H 4.019 0.005 1 417 . 86 ARG C C 176.003 0.05 1 418 . 86 ARG CB C 30.664 0.05 1 419 . 87 ILE N N 112.804 0.05 1 420 . 87 ILE H H 7.501 0.005 1 421 . 87 ILE CA C 61.264 0.05 1 422 . 87 ILE HA H 4.157 0.005 1 423 . 87 ILE C C 175.605 0.05 1 424 . 87 ILE CB C 38.478 0.05 1 425 . 87 ILE HB H 1.734 0.005 1 426 . 87 ILE CG1 C 27.681 0.05 1 427 . 87 ILE HG12 H 0.939 0.005 2 428 . 87 ILE HG13 H 1.346 0.005 2 429 . 87 ILE CG2 C 18.261 0.05 1 430 . 87 ILE HG2 H 0.744 0.005 1 431 . 87 ILE CD1 C 15.217 0.05 1 432 . 87 ILE HD1 H 0.445 0.005 1 433 . 88 HIS N N 116.043 0.05 1 434 . 88 HIS H H 7.514 0.005 1 435 . 88 HIS CA C 56.34 0.05 1 436 . 88 HIS HA H 4.225 0.005 1 437 . 88 HIS C C 175.4 0.05 1 438 . 88 HIS CB C 26.322 0.05 1 439 . 88 HIS HB2 H 3.299 0.005 2 440 . 88 HIS HB3 H 3.513 0.005 2 441 . 89 LEU N N 119.524 0.05 1 442 . 89 LEU H H 7.803 0.005 1 443 . 89 LEU CA C 54.575 0.05 1 444 . 89 LEU HA H 4.479 0.005 1 445 . 89 LEU C C 178.786 0.05 1 446 . 89 LEU CB C 43.279 0.05 1 447 . 89 LEU HB2 H 1.394 0.005 2 448 . 89 LEU HB3 H 1.71 0.005 2 449 . 89 LEU CD1 C 26.635 0.05 2 450 . 89 LEU HD1 H 0.85 0.005 2 451 . 90 ARG N N 123.67 0.05 1 452 . 90 ARG H H 9.144 0.005 1 453 . 90 ARG CA C 55.288 0.05 1 454 . 90 ARG HA H 4.357 0.005 1 455 . 90 ARG C C 178.759 0.05 1 456 . 90 ARG CB C 30.964 0.05 1 457 . 91 ALA N N 125.002 0.05 1 458 . 91 ALA H H 8.816 0.005 1 459 . 91 ALA CA C 55.374 0.05 1 460 . 91 ALA HA H 4.709 0.005 1 461 . 91 ALA C C 179.598 0.05 1 462 . 91 ALA CB C 18.191 0.05 1 463 . 92 GLU N N 112.177 0.05 1 464 . 92 GLU H H 8.888 0.005 1 465 . 92 GLU CA C 57.224 0.05 1 466 . 92 GLU HA H 4.094 0.005 1 467 . 92 GLU C C 177.281 0.05 1 468 . 92 GLU CB C 29.093 0.05 1 469 . 93 ASP N N 121.613 0.05 1 470 . 93 ASP H H 7.493 0.005 1 471 . 93 ASP CA C 54.634 0.05 1 472 . 93 ASP HA H 4.631 0.005 1 473 . 93 ASP CB C 42.358 0.05 1 474 . 94 ALA N N 127.085 0.05 1 475 . 94 ALA H H 8.53 0.005 1 476 . 94 ALA CA C 52.065 0.05 1 477 . 94 ALA HA H 4.048 0.005 1 478 . 94 ALA C C 175.834 0.05 1 479 . 94 ALA CB C 20.944 0.05 1 480 . 94 ALA HB H 1.435 0.005 1 481 . 95 LEU N N 117.128 0.05 1 482 . 95 LEU H H 7.046 0.005 1 483 . 95 LEU CA C 54.843 0.05 1 484 . 95 LEU HA H 4.574 0.005 1 485 . 95 LEU C C 174.001 0.05 1 486 . 95 LEU CB C 44.792 0.05 1 487 . 95 LEU CD1 C 27.477 0.05 2 488 . 95 LEU HD1 H 0.458 0.005 2 489 . 95 LEU CD2 C 24.818 0.05 2 490 . 95 LEU HD2 H 0.831 0.005 2 491 . 95 LEU HB3 H 1.123 0.005 2 492 . 96 PHE N N 124.206 0.05 1 493 . 96 PHE H H 9.212 0.005 1 494 . 96 PHE CA C 57.067 0.05 1 495 . 96 PHE C C 174.869 0.05 1 496 . 96 PHE CB C 43.12 0.05 1 497 . 97 PHE N N 119.924 0.05 1 498 . 97 PHE CA C 52.108 0.05 1 499 . 97 PHE HA H 6.037 0.005 1 500 . 97 PHE C C 174.394 0.05 1 501 . 97 PHE CB C 41.853 0.05 1 502 . 97 PHE HB2 H 2.837 0.005 2 503 . 97 PHE HB3 H 2.912 0.005 2 504 . 98 PHE N N 112.38 0.05 1 505 . 98 PHE H H 9.107 0.005 1 506 . 98 PHE CA C 56.204 0.05 1 507 . 98 PHE HA H 5.104 0.005 1 508 . 98 PHE C C 176.226 0.05 1 509 . 98 PHE CB C 43.759 0.05 1 510 . 98 PHE HB2 H 2.662 0.005 2 511 . 98 PHE HB3 H 2.808 0.005 2 512 . 99 VAL N N 121.911 0.05 1 513 . 99 VAL H H 9.358 0.005 1 514 . 99 VAL CA C 59.714 0.05 1 515 . 99 VAL HA H 4.565 0.005 1 516 . 99 VAL C C 175.905 0.05 1 517 . 99 VAL CB C 34.156 0.05 1 518 . 99 VAL HB H 1.71 0.005 1 519 . 99 VAL CG1 C 20.838 0.05 2 520 . 99 VAL HG1 H 0.635 0.005 2 521 . 99 VAL CG2 C 21.767 0.05 2 522 . 99 VAL HG2 H 0.831 0.005 2 523 . 100 ASN N N 126.129 0.05 1 524 . 100 ASN H H 9.964 0.005 1 525 . 100 ASN CA C 55.297 0.05 1 526 . 100 ASN HA H 4.317 0.005 1 527 . 100 ASN C C 175.331 0.05 1 528 . 100 ASN CB C 37.54 0.05 1 529 . 100 ASN HB2 H 2.724 0.005 2 530 . 100 ASN HB3 H 2.979 0.005 2 531 . 101 ASN N N 106.947 0.05 1 532 . 101 ASN H H 8.139 0.005 1 533 . 101 ASN CA C 55.532 0.05 1 534 . 101 ASN HA H 4.068 0.005 1 535 . 101 ASN C C 174.44 0.05 1 536 . 101 ASN CB C 38.284 0.05 1 537 . 102 VAL N N 118.743 0.05 1 538 . 102 VAL H H 8.237 0.005 1 539 . 102 VAL CA C 60.57 0.05 1 540 . 102 VAL HA H 4.703 0.005 1 541 . 102 VAL CB C 35.185 0.05 1 542 . 102 VAL HB H 2.217 0.005 1 543 . 102 VAL CG2 C 20.088 0.05 2 544 . 102 VAL HG2 H 0.98 0.005 2 545 . 103 ILE N N 126.972 0.05 1 546 . 103 ILE H H 8.53 0.005 1 547 . 103 ILE CA C 58.31 0.05 1 548 . 103 ILE HA H 5.209 0.005 1 549 . 103 ILE CB C 39.008 0.05 1 550 . 103 ILE HB H 1.765 0.005 1 551 . 103 ILE CG2 C 16.833 0.05 1 552 . 103 ILE HG2 H 1.166 0.005 1 553 . 103 ILE CD1 C 13.776 0.05 1 554 . 103 ILE HD1 H 0.832 0.005 1 555 . 103 ILE HG12 H 1.543 0.005 2 556 . 105 PRO CA C 62.067 0.05 1 557 . 105 PRO C C 178.979 0.05 1 558 . 105 PRO CB C 32.091 0.05 1 559 . 106 THR N N 113.672 0.05 1 560 . 106 THR H H 8.629 0.005 1 561 . 106 THR CA C 64.781 0.05 1 562 . 106 THR HA H 3.862 0.005 1 563 . 106 THR C C 176.17 0.05 1 564 . 106 THR CB C 68.718 0.05 1 565 . 106 THR HB H 4.241 0.005 1 566 . 106 THR CG2 C 23.003 0.05 1 567 . 106 THR HG2 H 1.368 0.005 1 568 . 107 SER N N 111.165 0.05 1 569 . 107 SER H H 7.816 0.005 1 570 . 107 SER CA C 57.876 0.05 1 571 . 107 SER HA H 4.444 0.005 1 572 . 107 SER C C 175.904 0.05 1 573 . 107 SER CB C 63.655 0.05 1 574 . 107 SER HB2 H 3.912 0.005 2 575 . 107 SER HB3 H 4.113 0.005 2 576 . 108 ALA N N 124.985 0.05 1 577 . 108 ALA H H 7.285 0.005 1 578 . 108 ALA CA C 52.264 0.05 1 579 . 108 ALA HA H 4.511 0.005 1 580 . 108 ALA C C 177.592 0.05 1 581 . 108 ALA CB C 19.146 0.05 1 582 . 108 ALA HB H 1.523 0.005 1 583 . 109 THR N N 108.767 0.05 1 584 . 109 THR H H 8.231 0.005 1 585 . 109 THR CA C 59.904 0.05 1 586 . 109 THR HA H 4.928 0.005 1 587 . 109 THR C C 176.906 0.05 1 588 . 109 THR CB C 70.714 0.05 1 589 . 109 THR HB H 4.903 0.005 1 590 . 109 THR CG2 C 21.993 0.05 1 591 . 109 THR HG2 H 1.223 0.005 1 592 . 110 MET N N 120.021 0.05 1 593 . 110 MET H H 9.391 0.005 1 594 . 110 MET CA C 55.815 0.05 1 595 . 110 MET HA H 4.883 0.005 1 596 . 110 MET C C 180.245 0.05 1 597 . 110 MET CB C 28.557 0.05 1 598 . 111 GLY N N 108.097 0.05 1 599 . 111 GLY H H 9.506 0.005 1 600 . 111 GLY CA C 47.065 0.05 1 601 . 111 GLY HA2 H 3.72 0.005 2 602 . 111 GLY HA3 H 4.04 0.005 2 603 . 111 GLY C C 177.116 0.05 1 604 . 112 GLN N N 124.43 0.05 1 605 . 112 GLN H H 8.024 0.005 1 606 . 112 GLN CA C 58.815 0.05 1 607 . 112 GLN HA H 4.137 0.005 1 608 . 112 GLN C C 180.108 0.05 1 609 . 112 GLN CB C 28.173 0.05 1 610 . 112 GLN HB2 H 2.131 0.005 2 611 . 112 GLN HB3 H 2.398 0.005 2 612 . 112 GLN HG2 H 2.453 0.005 2 613 . 113 LEU N N 120.805 0.05 1 614 . 113 LEU H H 8.478 0.005 1 615 . 113 LEU CA C 57.754 0.05 1 616 . 113 LEU HA H 4.269 0.005 1 617 . 113 LEU C C 179.574 0.05 1 618 . 113 LEU CB C 42.723 0.05 1 619 . 113 LEU HB2 H 1.644 0.005 2 620 . 113 LEU HB3 H 1.815 0.005 2 621 . 113 LEU CD1 C 24.322 0.05 2 622 . 113 LEU HD1 H 0.9 0.005 2 623 . 114 TYR N N 118.67 0.05 1 624 . 114 TYR H H 9.04 0.005 1 625 . 114 TYR CA C 63.094 0.05 1 626 . 114 TYR HA H 3.862 0.005 1 627 . 114 TYR C C 178.63 0.05 1 628 . 114 TYR CB C 39.622 0.05 1 629 . 114 TYR HB2 H 3.066 0.005 2 630 . 114 TYR HB3 H 3.327 0.005 2 631 . 115 GLN N N 119.182 0.05 1 632 . 115 GLN H H 8.387 0.005 1 633 . 115 GLN CA C 59.172 0.05 1 634 . 115 GLN C C 177.846 0.05 1 635 . 115 GLN CB C 28.506 0.05 1 636 . 116 GLU N N 114.95 0.05 1 637 . 116 GLU H H 7.419 0.005 1 638 . 116 GLU CA C 58.069 0.05 1 639 . 116 GLU HA H 3.98 0.005 1 640 . 116 GLU C C 178.737 0.05 1 641 . 116 GLU CB C 31.384 0.05 1 642 . 116 GLU HB2 H 1.518 0.005 2 643 . 116 GLU HB3 H 1.836 0.005 2 644 . 116 GLU HG3 H 2.055 0.005 2 645 . 117 HIS N N 112.267 0.05 1 646 . 117 HIS H H 8.136 0.005 1 647 . 117 HIS CA C 56.696 0.05 1 648 . 117 HIS HA H 4.735 0.005 1 649 . 117 HIS C C 177.859 0.05 1 650 . 117 HIS CB C 33.831 0.05 1 651 . 117 HIS HB2 H 2.811 0.005 2 652 . 117 HIS HB3 H 3.073 0.005 2 653 . 118 HIS N N 119.606 0.05 1 654 . 118 HIS H H 8.485 0.005 1 655 . 118 HIS CA C 57.255 0.05 1 656 . 118 HIS CB C 26.812 0.05 1 657 . 119 GLU CA C 55.903 0.05 1 658 . 119 GLU C C 175.572 0.05 1 659 . 120 GLU N N 120.776 0.05 1 660 . 120 GLU H H 8.212 0.005 1 661 . 120 GLU CA C 55.225 0.05 1 662 . 120 GLU HA H 4.227 0.005 1 663 . 120 GLU C C 175.611 0.05 1 664 . 120 GLU CB C 33.861 0.05 1 665 . 121 ASP N N 123.955 0.05 1 666 . 121 ASP H H 8.641 0.005 1 667 . 121 ASP CA C 57.381 0.05 1 668 . 121 ASP HA H 4.755 0.005 1 669 . 121 ASP C C 177.662 0.05 1 670 . 121 ASP CB C 40.71 0.05 1 671 . 123 PHE CA C 59.333 0.05 1 672 . 123 PHE C C 175.172 0.05 1 673 . 124 LEU N N 121.769 0.05 1 674 . 124 LEU H H 7.858 0.005 1 675 . 124 LEU CA C 53.155 0.05 1 676 . 124 LEU HA H 4.733 0.005 1 677 . 124 LEU C C 173.47 0.05 1 678 . 124 LEU CB C 46.053 0.05 1 679 . 124 LEU HB2 H 1.38 0.005 2 680 . 124 LEU HB3 H 2.065 0.005 2 681 . 124 LEU HG H 1.695 0.005 1 682 . 124 LEU CD1 C 26.83 0.05 2 683 . 124 LEU HD1 H 0.771 0.005 2 684 . 124 LEU CD2 C 24.79 0.05 2 685 . 124 LEU HD2 H 0.9 0.005 2 686 . 125 TYR N N 127.017 0.05 1 687 . 125 TYR H H 8.931 0.005 1 688 . 125 TYR CA C 57.781 0.05 1 689 . 125 TYR HA H 4.668 0.005 1 690 . 125 TYR C C 175.65 0.05 1 691 . 125 TYR CB C 38.751 0.05 1 692 . 126 ILE N N 123.577 0.05 1 693 . 126 ILE H H 9.381 0.005 1 694 . 126 ILE CA C 59.76 0.05 1 695 . 126 ILE HA H 4.858 0.005 1 696 . 126 ILE C C 175.188 0.05 1 697 . 126 ILE CB C 41.547 0.05 1 698 . 126 ILE HB H 1.539 0.005 1 699 . 126 ILE CG1 C 27.96 0.05 1 700 . 126 ILE HG12 H 0.832 0.005 2 701 . 126 ILE HG13 H 1.315 0.005 2 702 . 126 ILE CG2 C 16.909 0.05 1 703 . 126 ILE HG2 H 0.461 0.005 1 704 . 126 ILE CD1 C 13.296 0.05 1 705 . 126 ILE HD1 H 0.31 0.005 1 706 . 127 ALA N N 127.935 0.05 1 707 . 127 ALA H H 9.076 0.005 1 708 . 127 ALA CA C 48.861 0.05 1 709 . 127 ALA HA H 6.514 0.005 1 710 . 127 ALA C C 178.287 0.05 1 711 . 127 ALA CB C 23.381 0.05 1 712 . 127 ALA HB H 1.564 0.005 1 713 . 128 TYR N N 115.771 0.05 1 714 . 128 TYR H H 8.528 0.005 1 715 . 128 TYR CA C 55.027 0.05 1 716 . 128 TYR HA H 6.73 0.005 1 717 . 128 TYR C C 174.387 0.05 1 718 . 128 TYR CB C 42.918 0.05 1 719 . 128 TYR HB2 H 2.853 0.005 2 720 . 128 TYR HB3 H 3.274 0.005 2 721 . 129 SER N N 112.368 0.05 1 722 . 129 SER CA C 55.966 0.05 1 723 . 129 SER C C 173.059 0.05 1 724 . 129 SER HA H 4.652 0.005 1 725 . 129 SER CB C 65.162 0.05 1 726 . 129 SER HB2 H 4.268 0.005 2 727 . 130 ASP N N 120.193 0.05 1 728 . 130 ASP H H 9.466 0.005 1 729 . 130 ASP CA C 53.994 0.05 1 730 . 130 ASP HA H 4.835 0.005 1 731 . 130 ASP C C 175.635 0.05 1 732 . 130 ASP CB C 40.891 0.05 1 733 . 130 ASP HB2 H 3.074 0.005 2 734 . 131 GLU N N 119.224 0.05 1 735 . 131 GLU H H 8.569 0.005 1 736 . 131 GLU CA C 55.035 0.05 1 737 . 131 GLU HA H 4.629 0.005 1 738 . 131 GLU C C 175.698 0.05 1 739 . 131 GLU CB C 33.322 0.05 1 740 . 132 SER N N 112.192 0.05 1 741 . 132 SER H H 7.995 0.005 1 742 . 132 SER CA C 58.31 0.05 1 743 . 132 SER HA H 3.376 0.005 1 744 . 132 SER C C 174.04 0.05 1 745 . 132 SER CB C 62.729 0.05 1 746 . 132 SER HB2 H 2.461 0.005 2 747 . 132 SER HB3 H 3.494 0.005 2 748 . 133 VAL N N 118.985 0.05 1 749 . 133 VAL H H 6.988 0.005 1 750 . 133 VAL CA C 61.069 0.05 1 751 . 133 VAL HA H 4.16 0.005 1 752 . 133 VAL C C 175.297 0.05 1 753 . 133 VAL CB C 34.24 0.05 1 754 . 133 VAL HB H 1.818 0.005 1 755 . 133 VAL CG1 C 20.484 0.05 2 756 . 133 VAL HG1 H 0.753 0.005 2 757 . 133 VAL CG2 C 21 0.05 2 758 . 133 VAL HG2 H 0.756 0.005 2 759 . 134 TYR N N 127.374 0.05 1 760 . 134 TYR H H 8.279 0.005 1 761 . 134 TYR CA C 58.798 0.05 1 762 . 134 TYR HA H 3.684 0.005 1 763 . 134 TYR C C 178.544 0.05 1 764 . 134 TYR CB C 38.042 0.05 1 765 . 135 GLY N N 112.645 0.05 1 766 . 135 GLY H H 7.492 0.005 1 767 . 135 GLY CA C 45.127 0.05 1 768 . 135 GLY HA2 H 3.589 0.005 2 769 . 135 GLY HA3 H 3.688 0.005 2 770 . 135 GLY C C 172.661 0.05 1 771 . 136 LEU N N 126.912 0.05 1 772 . 136 LEU H H 7.467 0.005 1 773 . 136 LEU CA C 56.24 0.05 1 774 . 136 LEU HA H 4.078 0.005 1 775 . 136 LEU C C 174.286 0.05 1 776 . 136 LEU CB C 43.56 0.05 1 777 . 136 LEU HB3 H 1.492 0.005 2 778 . 136 LEU CD1 C 25.189 0.05 2 779 . 136 LEU HD1 H 0.823 0.005 2 stop_ save_