data_5350 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, and 13C resonance assignments of low molecular weight human cytoplasmic protein tyrosine phosphatase-A (HCPTP-A) ; _BMRB_accession_number 5350 _BMRB_flat_file_name bmr5350.str _Entry_type original _Submission_date 2002-04-22 _Accession_date 2002-04-22 _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 Rastogi Vinit K. . 2 Diven Conrad F. . 3 Seabrook Genevieve M. . 4 Genbauffe Frank S. . 5 Bechard Randy T. . 6 Fandl James P. . 7 Peters Kevin G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 237 "13C chemical shifts" 276 "15N chemical shifts" 134 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-06 original author . stop_ _Original_release_date 2003-01-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: 1H, 15N, and 13C Resonance Assignments of Low Molecular Weight Human Cytoplasmic Protein Tyrosine Phosphatase-A (HCPTP-A) ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22223355 _PubMed_ID 12238601 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rastogi Vinit K. . 2 Diven Conrad F. . 3 Seabrook Genevieve M. . 4 Genbauffe Frank S. . 5 Bechard Randy T. . 6 Fandl James P. . 7 Peters Kevin G. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 23 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 251 _Page_last 252 _Year 2002 _Details . loop_ _Keyword CSI 'Protein Tyrosine Phosphatase (PTP)' 'resonance assignment' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; Logan TM, Zhou MM, Nettesheim DG, Meadows RP, Van Etten RL, Fesik SW. Solution structure of a low molecular weight protein tyrosine phosphatase. Biochemistry. 1994 Sep 20;33(37):11087-96. ; _Citation_title 'Solution structure of a low molecular weight protein tyrosine phosphatase.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 7727361 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Logan 'T. M.' M. . 2 Zhou 'M. M.' M. . 3 Nettesheim 'D. G.' G. . 4 Meadows 'R. P.' P. . 5 'Van Etten' 'R. L.' L. . 6 Fesik 'S. W.' W. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 33 _Journal_issue 37 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 11087 _Page_last 11096 _Year 1994 _Details ; Protein tyrosine phosphatases (PTPs) are important enzymes involved in signal transduction, cell cycle regulation, and the control of differentiation. Despite the importance of this class of enzymes in the control of critical cell processes, very little structural information is available for this family of proteins. In this paper, we present the first solution structure of a protein tyrosine phosphatase. This protein is a low molecular weight cytosolic PTP that was initially isolated from bovine heart. The structure that was determined from 1747 NMR-derived restraints consists of a central four-stranded parallel beta-sheet surrounded by four alpha-helices and a short 3(10) helix. The phosphate binding site, identified by chemical shift changes upon the addition of the competitive inhibitors phosphate and vanadate, is in a loop region connecting the C-terminal end of the first beta-strand with the first alpha-helix. Residues in the second, fourth, and fifth alpha-helices and in some of the loop regions connecting the elements of regular secondary structure also contribute to the binding site. The structure determined here is consistent with previous mutagenesis and chemical modification studies conducted on this protein. ; save_ ################################## # Molecular system description # ################################## save_system_HCPTP-A _Saveframe_category molecular_system _Mol_system_name 'human cytoplasmic tyrosine phosphatase A' _Abbreviation_common HCPTP-A _Enzyme_commission_number 3.1.3.2 loop_ _Mol_system_component_name _Mol_label HCPTP-A $HCPTP-A stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'protein tyrosine phosphatase' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HCPTP-A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'human cytoplasmic protein tyrosine phosphatase-A' _Abbreviation_common HCPTP-A _Molecular_mass 18890 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 157 _Mol_residue_sequence ; AEQATKSVLFVCLGNICRSP IAEAVFRKLVTDQNISENWR VDSAATSGYEIGNPPDYRGQ SCMKRHGIPMSHVARQITKE DFATFDYILCMDESNLRDLN RKSNQVKTCKAKIELLGSYD PQKQLIIEDPYYGNDSDFET VYQQCVRCCRAFLEKAH ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 GLU 3 GLN 4 ALA 5 THR 6 LYS 7 SER 8 VAL 9 LEU 10 PHE 11 VAL 12 CYS 13 LEU 14 GLY 15 ASN 16 ILE 17 CYS 18 ARG 19 SER 20 PRO 21 ILE 22 ALA 23 GLU 24 ALA 25 VAL 26 PHE 27 ARG 28 LYS 29 LEU 30 VAL 31 THR 32 ASP 33 GLN 34 ASN 35 ILE 36 SER 37 GLU 38 ASN 39 TRP 40 ARG 41 VAL 42 ASP 43 SER 44 ALA 45 ALA 46 THR 47 SER 48 GLY 49 TYR 50 GLU 51 ILE 52 GLY 53 ASN 54 PRO 55 PRO 56 ASP 57 TYR 58 ARG 59 GLY 60 GLN 61 SER 62 CYS 63 MET 64 LYS 65 ARG 66 HIS 67 GLY 68 ILE 69 PRO 70 MET 71 SER 72 HIS 73 VAL 74 ALA 75 ARG 76 GLN 77 ILE 78 THR 79 LYS 80 GLU 81 ASP 82 PHE 83 ALA 84 THR 85 PHE 86 ASP 87 TYR 88 ILE 89 LEU 90 CYS 91 MET 92 ASP 93 GLU 94 SER 95 ASN 96 LEU 97 ARG 98 ASP 99 LEU 100 ASN 101 ARG 102 LYS 103 SER 104 ASN 105 GLN 106 VAL 107 LYS 108 THR 109 CYS 110 LYS 111 ALA 112 LYS 113 ILE 114 GLU 115 LEU 116 LEU 117 GLY 118 SER 119 TYR 120 ASP 121 PRO 122 GLN 123 LYS 124 GLN 125 LEU 126 ILE 127 ILE 128 GLU 129 ASP 130 PRO 131 TYR 132 TYR 133 GLY 134 ASN 135 ASP 136 SER 137 ASP 138 PHE 139 GLU 140 THR 141 VAL 142 TYR 143 GLN 144 GLN 145 CYS 146 VAL 147 ARG 148 CYS 149 CYS 150 ARG 151 ALA 152 PHE 153 LEU 154 GLU 155 LYS 156 ALA 157 HIS 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 3N8I "Crystal Structure Of The A Isoform Of Human Cytoplasmic Protein Tyrosine Phosphatase (Hcptp-A) In Complex With 1-Naphtylacetic " 100.00 157 100.00 100.00 1.10e-113 PDB 5PNT "Crystal Structure Of A Human Low Molecular Weight Phosphotyrosyl Phosphatase. Implications For Substrate Specificity" 100.00 157 100.00 100.00 1.10e-113 DBJ BAD93075 "acid phosphatase 1 isoform c variant [Homo sapiens]" 100.00 165 99.36 100.00 2.84e-113 DBJ BAF84550 "unnamed protein product [Homo sapiens]" 100.00 158 100.00 100.00 7.50e-114 DBJ BAG11407 "acid phosphatase 1 [synthetic construct]" 100.00 158 99.36 100.00 4.60e-113 EMBL CAH89780 "hypothetical protein [Pongo abelii]" 100.00 158 98.73 100.00 5.79e-113 GB AAB20259 "acid phosphatase isozyme Bf, ACP1 isozyme Bf {EC 3.1.3.2} [human, red cells, Peptide, 157 aa]" 100.00 157 100.00 100.00 1.10e-113 GB AAB22514 "acid phosphatase isoenzyme Af [human, erythrocytes, Peptide, 157 aa]" 100.00 157 99.36 100.00 5.02e-113 GB AAB22515 "acid phosphatase isoenzyme Cf [human, erythrocytes, Peptide, 157 aa]" 100.00 157 100.00 100.00 1.10e-113 GB AAB27085 "adipocyte acid phosphatase alpha, partial [Homo sapiens]" 87.90 146 99.28 100.00 2.03e-98 GB AAB59354 "cytoplasmic phosphotyrosyl protein phosphatase [Homo sapiens]" 100.00 158 100.00 100.00 7.50e-114 REF NP_001124815 "low molecular weight phosphotyrosine protein phosphatase [Pongo abelii]" 100.00 158 98.73 100.00 5.79e-113 REF NP_004291 "low molecular weight phosphotyrosine protein phosphatase isoform c [Homo sapiens]" 100.00 158 100.00 100.00 7.50e-114 REF XP_003278849 "PREDICTED: low molecular weight phosphotyrosine protein phosphatase isoform 1 [Nomascus leucogenys]" 100.00 158 99.36 100.00 1.43e-113 REF XP_003807854 "PREDICTED: low molecular weight phosphotyrosine protein phosphatase isoform X1 [Pan paniscus]" 100.00 158 100.00 100.00 7.50e-114 REF XP_003908262 "PREDICTED: low molecular weight phosphotyrosine protein phosphatase isoform X1 [Papio anubis]" 99.36 158 98.72 99.36 5.46e-111 SP P24666 "RecName: Full=Low molecular weight phosphotyrosine protein phosphatase; Short=LMW-PTP; Short=LMW-PTPase; AltName: Full=Adipocyt" 100.00 158 100.00 100.00 7.50e-114 SP Q5REM7 "RecName: Full=Low molecular weight phosphotyrosine protein phosphatase; Short=LMW-PTP; Short=LMW-PTPase; AltName: Full=Low mole" 100.00 158 98.73 100.00 5.79e-113 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HCPTP-A 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_name $HCPTP-A 'recombinant technology' 'E. Coli' Escherichia coli BL21 DE3 . 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 $HCPTP-A 1.0 mM '[U-13C; U-15N]' stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_Pulsed_field_gradients_for_coherence_selection_and_artifact_suppression_and_1 _Saveframe_category NMR_applied_experiment _Experiment_name 'Pulsed field gradients for coherence selection and artifact suppression and' _Sample_label $sample_1 save_ save_gradient_sensitivity_enhancement_schemes_were_applied_where_appropriate._2 _Saveframe_category NMR_applied_experiment _Experiment_name 'gradient sensitivity enhancement schemes were applied where appropriate.' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 5.1 0.2 n/a temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000 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 . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name HCPTP-A _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 ALA CA C 51.850 0.200 1 2 . 1 ALA C C 173.670 0.200 1 3 . 2 GLU N N 120.660 0.050 1 4 . 2 GLU H H 8.740 0.010 1 5 . 2 GLU HA H 4.770 0.010 1 6 . 2 GLU CA C 56.490 0.200 1 7 . 2 GLU C C 176.070 0.200 1 8 . 3 GLN N N 121.790 0.050 1 9 . 3 GLN H H 8.510 0.010 1 10 . 3 GLN HA H 4.330 0.010 1 11 . 3 GLN CA C 55.580 0.200 1 12 . 3 GLN C C 175.270 0.200 1 13 . 4 ALA N N 125.980 0.050 1 14 . 4 ALA H H 8.390 0.010 1 15 . 4 ALA HA H 4.380 0.010 1 16 . 4 ALA CA C 52.510 0.200 1 17 . 4 ALA C C 177.500 0.200 1 18 . 5 THR N N 114.730 0.050 1 19 . 5 THR H H 8.010 0.010 1 20 . 5 THR HA H 4.230 0.010 1 21 . 5 THR CA C 61.970 0.200 1 22 . 5 THR C C 174.230 0.200 1 23 . 6 LYS N N 125.290 0.050 1 24 . 6 LYS H H 7.850 0.010 1 25 . 6 LYS HA H 4.570 0.010 1 26 . 6 LYS CA C 54.950 0.200 1 27 . 6 LYS C C 175.160 0.200 1 28 . 7 SER N N 114.620 0.050 1 29 . 7 SER H H 9.030 0.010 1 30 . 7 SER HA H 6.100 0.010 1 31 . 7 SER CA C 56.720 0.200 1 32 . 7 SER C C 173.460 0.200 1 33 . 8 VAL N N 121.880 0.050 1 34 . 8 VAL H H 9.250 0.010 1 35 . 8 VAL HA H 5.160 0.010 1 36 . 8 VAL CA C 59.310 0.200 1 37 . 8 VAL C C 169.320 0.200 1 38 . 9 LEU N N 128.450 0.050 1 39 . 9 LEU H H 7.980 0.010 1 40 . 9 LEU CA C 51.120 0.200 1 41 . 10 PHE N N 125.300 0.050 1 42 . 10 PHE H H 8.200 0.010 1 43 . 10 PHE HA H 5.160 0.010 1 44 . 10 PHE CA C 56.930 0.200 1 45 . 12 CYS CA C 57.480 0.200 1 46 . 12 CYS C C 175.060 0.200 1 47 . 13 LEU N N 118.810 0.050 1 48 . 13 LEU H H 7.100 0.010 1 49 . 13 LEU CA C 57.680 0.200 1 50 . 13 LEU C C 178.060 0.200 1 51 . 14 GLY N N 103.110 0.050 1 52 . 14 GLY H H 8.560 0.010 1 53 . 14 GLY HA2 H 4.250 0.010 2 54 . 14 GLY CA C 45.670 0.200 1 55 . 14 GLY C C 174.650 0.200 1 56 . 15 ASN N N 118.750 0.050 1 57 . 15 ASN H H 9.130 0.010 1 58 . 15 ASN CA C 54.880 0.200 1 59 . 15 ASN C C 172.000 0.200 1 60 . 16 ILE N N 103.100 0.050 1 61 . 16 ILE H H 7.550 0.010 1 62 . 16 ILE HA H 5.030 0.010 1 63 . 16 ILE CA C 63.000 0.200 1 64 . 16 ILE C C 177.780 0.200 1 65 . 17 CYS N N 122.220 0.050 1 66 . 17 CYS H H 9.580 0.010 1 67 . 17 CYS HA H 4.770 0.010 1 68 . 17 CYS CA C 59.690 0.200 1 69 . 17 CYS C C 175.280 0.200 1 70 . 18 ARG N N 118.740 0.050 1 71 . 18 ARG H H 9.860 0.010 1 72 . 18 ARG CA C 60.260 0.200 1 73 . 18 ARG C C 176.870 0.200 1 74 . 19 SER N N 117.360 0.050 1 75 . 19 SER H H 10.050 0.010 1 76 . 19 SER CA C 64.290 0.200 1 77 . 20 PRO CA C 65.740 0.200 1 78 . 20 PRO C C 179.360 0.200 1 79 . 21 ILE N N 118.450 0.050 1 80 . 21 ILE H H 6.510 0.010 1 81 . 21 ILE HA H 3.860 0.010 1 82 . 21 ILE CA C 65.600 0.200 1 83 . 21 ILE C C 176.300 0.200 1 84 . 22 ALA N N 122.680 0.050 1 85 . 22 ALA H H 7.830 0.010 1 86 . 22 ALA HA H 5.150 0.010 1 87 . 22 ALA CA C 57.000 0.200 1 88 . 22 ALA C C 176.810 0.200 1 89 . 23 GLU N N 115.000 0.050 1 90 . 23 GLU H H 7.850 0.010 1 91 . 23 GLU HA H 3.800 0.010 1 92 . 23 GLU CA C 58.860 0.200 1 93 . 23 GLU C C 176.880 0.200 1 94 . 24 ALA N N 121.320 0.050 1 95 . 24 ALA H H 7.620 0.010 1 96 . 24 ALA HA H 3.990 0.010 1 97 . 24 ALA CA C 55.090 0.200 1 98 . 24 ALA C C 181.230 0.200 1 99 . 25 VAL N N 120.460 0.050 1 100 . 25 VAL H H 8.900 0.010 1 101 . 25 VAL HA H 4.640 0.010 1 102 . 25 VAL CA C 66.830 0.200 1 103 . 25 VAL C C 177.210 0.200 1 104 . 26 PHE N N 121.680 0.050 1 105 . 26 PHE H H 8.700 0.010 1 106 . 26 PHE CA C 63.410 0.200 1 107 . 26 PHE C C 176.880 0.200 1 108 . 27 ARG N N 116.630 0.050 1 109 . 27 ARG H H 8.870 0.010 1 110 . 27 ARG CA C 59.980 0.200 1 111 . 27 ARG C C 179.240 0.200 1 112 . 28 LYS N N 119.100 0.050 1 113 . 28 LYS H H 8.520 0.010 1 114 . 28 LYS HA H 4.900 0.010 1 115 . 28 LYS CA C 60.010 0.200 1 116 . 28 LYS C C 179.570 0.200 1 117 . 29 LEU N N 121.560 0.050 1 118 . 29 LEU H H 7.900 0.010 1 119 . 29 LEU HA H 4.640 0.010 1 120 . 29 LEU CA C 58.460 0.200 1 121 . 29 LEU C C 180.000 0.200 1 122 . 30 VAL N N 109.960 0.050 1 123 . 30 VAL H H 7.920 0.010 1 124 . 30 VAL HA H 3.630 0.010 1 125 . 30 VAL CA C 64.980 0.200 1 126 . 30 VAL C C 178.200 0.200 1 127 . 31 THR N N 119.750 0.050 1 128 . 31 THR H H 7.920 0.010 1 129 . 31 THR HA H 4.120 0.010 1 130 . 31 THR CA C 67.120 0.200 1 131 . 31 THR C C 178.230 0.200 1 132 . 32 ASP N N 125.340 0.050 1 133 . 32 ASP H H 8.950 0.010 1 134 . 32 ASP HA H 6.100 0.010 1 135 . 32 ASP CA C 57.300 0.200 1 136 . 32 ASP C C 178.020 0.200 1 137 . 33 GLN N N 115.100 0.050 1 138 . 33 GLN H H 7.480 0.010 1 139 . 33 GLN HA H 4.330 0.010 1 140 . 33 GLN CA C 55.830 0.200 1 141 . 33 GLN C C 174.660 0.200 1 142 . 34 ASN N N 115.620 0.050 1 143 . 34 ASN H H 8.060 0.010 1 144 . 34 ASN HA H 4.770 0.010 1 145 . 34 ASN CA C 54.790 0.200 1 146 . 34 ASN C C 175.420 0.200 1 147 . 35 ILE N N 110.060 0.050 1 148 . 35 ILE H H 8.250 0.010 1 149 . 35 ILE HA H 4.910 0.010 1 150 . 35 ILE CA C 61.000 0.200 1 151 . 35 ILE C C 177.330 0.200 1 152 . 36 SER N N 118.940 0.050 1 153 . 36 SER H H 8.060 0.010 1 154 . 36 SER HA H 3.990 0.010 1 155 . 36 SER CA C 59.400 0.200 1 156 . 36 SER C C 176.010 0.200 1 157 . 37 GLU N N 116.590 0.050 1 158 . 37 GLU H H 8.240 0.010 1 159 . 37 GLU CA C 58.000 0.200 1 160 . 37 GLU C C 176.680 0.200 1 161 . 38 ASN N N 116.070 0.050 1 162 . 38 ASN H H 7.960 0.010 1 163 . 38 ASN HA H 4.800 0.010 1 164 . 38 ASN CA C 53.640 0.200 1 165 . 38 ASN C C 173.810 0.200 1 166 . 39 TRP N N 119.430 0.050 1 167 . 39 TRP H H 7.830 0.010 1 168 . 39 TRP HA H 5.540 0.010 1 169 . 39 TRP CA C 56.760 0.200 1 170 . 39 TRP C C 175.370 0.200 1 171 . 40 ARG N N 125.010 0.050 1 172 . 40 ARG H H 9.190 0.010 1 173 . 40 ARG HA H 4.900 0.010 1 174 . 40 ARG CA C 55.400 0.200 1 175 . 40 ARG C C 174.690 0.200 1 176 . 41 VAL N N 125.440 0.050 1 177 . 41 VAL H H 8.820 0.010 1 178 . 41 VAL HA H 5.580 0.010 1 179 . 41 VAL CA C 60.050 0.200 1 180 . 41 VAL C C 173.990 0.200 1 181 . 42 ASP N N 124.520 0.050 1 182 . 42 ASP H H 8.480 0.010 1 183 . 42 ASP HA H 5.220 0.010 1 184 . 42 ASP CA C 52.550 0.200 1 185 . 42 ASP C C 174.260 0.200 1 186 . 43 SER N N 114.600 0.050 1 187 . 43 SER H H 8.990 0.010 1 188 . 43 SER HA H 5.440 0.010 1 189 . 43 SER CA C 58.130 0.200 1 190 . 43 SER C C 176.530 0.200 1 191 . 44 ALA N N 118.090 0.050 1 192 . 44 ALA H H 8.530 0.010 1 193 . 44 ALA HA H 4.760 0.010 1 194 . 44 ALA CA C 51.070 0.200 1 195 . 44 ALA C C 174.070 0.200 1 196 . 45 ALA N N 119.040 0.050 1 197 . 45 ALA H H 9.060 0.010 1 198 . 45 ALA HA H 4.380 0.010 1 199 . 45 ALA CA C 49.230 0.200 1 200 . 45 ALA C C 179.430 0.200 1 201 . 46 THR N N 108.890 0.050 1 202 . 46 THR H H 8.730 0.010 1 203 . 46 THR HA H 4.230 0.010 1 204 . 46 THR CA C 64.480 0.200 1 205 . 46 THR C C 175.970 0.200 1 206 . 47 SER N N 118.480 0.050 1 207 . 47 SER H H 8.150 0.010 1 208 . 47 SER HA H 4.070 0.010 1 209 . 47 SER CA C 57.560 0.200 1 210 . 47 SER C C 174.620 0.200 1 211 . 48 GLY N N 108.660 0.050 1 212 . 48 GLY H H 8.470 0.010 1 213 . 48 GLY CA C 44.870 0.200 1 214 . 48 GLY C C 176.270 0.200 1 215 . 49 TYR N N 118.680 0.050 1 216 . 49 TYR H H 7.580 0.010 1 217 . 49 TYR CA C 60.420 0.200 1 218 . 49 TYR C C 176.970 0.200 1 219 . 50 GLU N N 115.210 0.050 1 220 . 50 GLU H H 8.550 0.010 1 221 . 50 GLU HA H 4.480 0.010 1 222 . 50 GLU CA C 54.100 0.200 1 223 . 50 GLU C C 175.140 0.200 1 224 . 51 ILE N N 115.540 0.050 1 225 . 51 ILE H H 6.660 0.010 1 226 . 51 ILE CA C 63.670 0.200 1 227 . 51 ILE C C 176.870 0.200 1 228 . 52 GLY N N 112.140 0.050 1 229 . 52 GLY H H 8.780 0.010 1 230 . 52 GLY HA2 H 4.640 0.010 2 231 . 52 GLY CA C 44.860 0.200 1 232 . 52 GLY C C 174.120 0.200 1 233 . 53 ASN N N 120.410 0.050 1 234 . 53 ASN H H 8.110 0.010 1 235 . 53 ASN HA H 5.230 0.010 1 236 . 53 ASN CA C 51.640 0.200 1 237 . 55 PRO CA C 62.790 0.200 1 238 . 55 PRO C C 176.150 0.200 1 239 . 56 ASP N N 122.330 0.050 1 240 . 56 ASP H H 8.380 0.010 1 241 . 56 ASP HA H 4.250 0.010 1 242 . 56 ASP CA C 54.850 0.200 1 243 . 56 ASP C C 178.530 0.200 1 244 . 57 TYR N N 128.670 0.050 1 245 . 57 TYR H H 9.180 0.010 1 246 . 57 TYR CA C 61.450 0.200 1 247 . 57 TYR C C 176.410 0.200 1 248 . 58 ARG N N 119.290 0.050 1 249 . 58 ARG H H 9.060 0.010 1 250 . 58 ARG CA C 58.110 0.200 1 251 . 58 ARG C C 180.460 0.200 1 252 . 59 GLY N N 110.150 0.050 1 253 . 59 GLY H H 7.190 0.010 1 254 . 59 GLY HA2 H 4.250 0.010 2 255 . 59 GLY CA C 47.340 0.200 1 256 . 60 GLN CA C 59.630 0.200 1 257 . 60 GLN C C 179.150 0.200 1 258 . 61 SER N N 115.220 0.050 1 259 . 61 SER H H 8.300 0.010 1 260 . 61 SER HA H 3.990 0.010 1 261 . 61 SER CA C 61.510 0.200 1 262 . 65 ARG CA C 54.500 0.200 1 263 . 65 ARG C C 175.710 0.200 1 264 . 66 HIS N N 115.990 0.050 1 265 . 66 HIS H H 7.620 0.010 1 266 . 66 HIS CA C 55.800 0.200 1 267 . 66 HIS C C 173.700 0.200 1 268 . 67 GLY N N 110.330 0.050 1 269 . 67 GLY H H 7.900 0.010 1 270 . 67 GLY HA2 H 3.990 0.010 2 271 . 67 GLY CA C 46.810 0.200 1 272 . 67 GLY C C 174.300 0.200 1 273 . 68 ILE N N 121.280 0.050 1 274 . 68 ILE H H 8.130 0.010 1 275 . 68 ILE HA H 4.520 0.010 1 276 . 68 ILE CA C 57.660 0.200 1 277 . 69 PRO CA C 65.140 0.200 1 278 . 69 PRO C C 178.120 0.200 1 279 . 70 MET N N 114.120 0.050 1 280 . 70 MET H H 8.210 0.010 1 281 . 70 MET HA H 4.250 0.010 1 282 . 70 MET CA C 55.640 0.200 1 283 . 70 MET C C 174.200 0.200 1 284 . 71 SER N N 122.470 0.050 1 285 . 71 SER H H 8.790 0.010 1 286 . 71 SER HA H 4.770 0.010 1 287 . 71 SER CA C 57.300 0.200 1 288 . 71 SER C C 172.680 0.200 1 289 . 72 HIS N N 123.760 0.050 1 290 . 72 HIS H H 8.210 0.010 1 291 . 72 HIS HA H 4.770 0.010 1 292 . 72 HIS CA C 56.270 0.200 1 293 . 72 HIS C C 171.520 0.200 1 294 . 73 VAL N N 124.070 0.050 1 295 . 73 VAL H H 7.090 0.010 1 296 . 73 VAL HA H 3.960 0.010 1 297 . 73 VAL CA C 61.210 0.200 1 298 . 73 VAL C C 174.600 0.200 1 299 . 74 ALA N N 127.940 0.050 1 300 . 74 ALA H H 8.720 0.010 1 301 . 74 ALA HA H 4.640 0.010 1 302 . 74 ALA CA C 53.040 0.200 1 303 . 74 ALA C C 178.920 0.200 1 304 . 75 ARG N N 120.230 0.050 1 305 . 75 ARG H H 8.970 0.010 1 306 . 75 ARG HA H 4.770 0.010 1 307 . 75 ARG CA C 53.880 0.200 1 308 . 75 ARG C C 172.460 0.200 1 309 . 76 GLN N N 123.140 0.050 1 310 . 76 GLN H H 8.880 0.010 1 311 . 76 GLN HA H 4.090 0.010 1 312 . 76 GLN CA C 54.620 0.200 1 313 . 76 GLN C C 175.390 0.200 1 314 . 77 ILE N N 126.680 0.050 1 315 . 77 ILE H H 9.000 0.010 1 316 . 77 ILE CA C 61.780 0.200 1 317 . 77 ILE C C 173.310 0.200 1 318 . 78 THR N N 119.510 0.050 1 319 . 78 THR H H 9.500 0.010 1 320 . 78 THR HA H 4.790 0.010 1 321 . 78 THR CA C 59.610 0.200 1 322 . 78 THR C C 175.720 0.200 1 323 . 79 LYS N N 118.670 0.050 1 324 . 79 LYS H H 8.770 0.010 1 325 . 79 LYS HA H 4.190 0.010 1 326 . 79 LYS CA C 59.620 0.200 1 327 . 79 LYS C C 180.900 0.200 1 328 . 80 GLU N N 120.370 0.050 1 329 . 80 GLU H H 7.950 0.010 1 330 . 80 GLU HA H 3.990 0.010 1 331 . 80 GLU CA C 59.440 0.200 1 332 . 80 GLU C C 177.470 0.200 1 333 . 81 ASP N N 119.840 0.050 1 334 . 81 ASP H H 8.030 0.010 1 335 . 81 ASP HA H 3.990 0.010 1 336 . 81 ASP CA C 58.460 0.200 1 337 . 81 ASP C C 178.190 0.200 1 338 . 82 PHE N N 118.960 0.050 1 339 . 82 PHE H H 8.120 0.010 1 340 . 82 PHE HA H 4.130 0.010 1 341 . 82 PHE CA C 59.830 0.200 1 342 . 82 PHE C C 175.920 0.200 1 343 . 83 ALA N N 119.840 0.050 1 344 . 83 ALA H H 7.470 0.010 1 345 . 83 ALA HA H 4.510 0.010 1 346 . 83 ALA CA C 53.150 0.200 1 347 . 83 ALA C C 177.860 0.200 1 348 . 84 THR N N 108.160 0.050 1 349 . 84 THR H H 7.600 0.010 1 350 . 84 THR HA H 4.220 0.010 1 351 . 84 THR CA C 63.100 0.200 1 352 . 84 THR C C 174.650 0.200 1 353 . 85 PHE N N 121.490 0.050 1 354 . 85 PHE H H 7.410 0.010 1 355 . 85 PHE HA H 4.730 0.010 1 356 . 85 PHE CA C 58.990 0.200 1 357 . 85 PHE C C 174.440 0.200 1 358 . 86 ASP N N 118.100 0.050 1 359 . 86 ASP H H 8.230 0.010 1 360 . 86 ASP HA H 4.250 0.010 1 361 . 86 ASP CA C 57.000 0.200 1 362 . 86 ASP C C 177.190 0.200 1 363 . 87 TYR N N 115.940 0.050 1 364 . 87 TYR H H 7.860 0.010 1 365 . 87 TYR HA H 5.170 0.010 1 366 . 87 TYR CA C 57.010 0.200 1 367 . 87 TYR C C 174.110 0.200 1 368 . 88 ILE N N 123.540 0.050 1 369 . 88 ILE H H 9.020 0.010 1 370 . 88 ILE HA H 4.510 0.010 1 371 . 88 ILE CA C 60.720 0.200 1 372 . 88 ILE C C 173.540 0.200 1 373 . 89 LEU N N 125.440 0.050 1 374 . 89 LEU H H 8.330 0.010 1 375 . 89 LEU HA H 5.560 0.010 1 376 . 89 LEU CA C 51.800 0.200 1 377 . 89 LEU C C 176.130 0.200 1 378 . 90 CYS N N 118.810 0.050 1 379 . 90 CYS H H 9.270 0.010 1 380 . 90 CYS HA H 6.280 0.010 1 381 . 90 CYS CA C 54.710 0.200 1 382 . 91 MET N N 128.100 0.050 1 383 . 91 MET H H 10.100 0.010 1 384 . 91 MET CA C 56.900 0.200 1 385 . 91 MET C C 176.590 0.200 1 386 . 92 ASP N N 117.720 0.050 1 387 . 92 ASP H H 7.990 0.010 1 388 . 92 ASP HA H 4.930 0.010 1 389 . 92 ASP CA C 52.520 0.200 1 390 . 93 GLU CA C 59.690 0.200 1 391 . 93 GLU C C 178.910 0.200 1 392 . 94 SER N N 118.680 0.050 1 393 . 94 SER H H 8.380 0.010 1 394 . 94 SER HA H 4.270 0.010 1 395 . 94 SER CA C 61.670 0.200 1 396 . 94 SER C C 176.910 0.200 1 397 . 95 ASN N N 120.580 0.050 1 398 . 95 ASN H H 8.680 0.010 1 399 . 95 ASN CA C 56.180 0.200 1 400 . 95 ASN C C 177.030 0.200 1 401 . 96 LEU N N 117.700 0.050 1 402 . 96 LEU H H 7.940 0.010 1 403 . 96 LEU HA H 4.120 0.010 1 404 . 98 ASP C C 179.210 0.200 1 405 . 99 LEU N N 119.950 0.050 1 406 . 99 LEU H H 8.790 0.010 1 407 . 99 LEU CA C 57.880 0.200 1 408 . 99 LEU C C 178.990 0.200 1 409 . 100 ASN N N 119.560 0.050 1 410 . 100 ASN H H 8.830 0.010 1 411 . 100 ASN HA H 4.510 0.010 1 412 . 100 ASN CA C 56.270 0.200 1 413 . 101 ARG CA C 59.450 0.200 1 414 . 101 ARG C C 179.330 0.200 1 415 . 102 LYS N N 119.610 0.050 1 416 . 102 LYS H H 8.050 0.010 1 417 . 102 LYS HA H 3.860 0.010 1 418 . 102 LYS CA C 59.080 0.200 1 419 . 102 LYS C C 179.200 0.200 1 420 . 103 SER N N 115.220 0.050 1 421 . 103 SER H H 8.420 0.010 1 422 . 103 SER CA C 61.020 0.200 1 423 . 103 SER C C 175.020 0.200 1 424 . 104 ASN N N 118.400 0.050 1 425 . 104 ASN H H 7.170 0.010 1 426 . 104 ASN HA H 4.630 0.010 1 427 . 104 ASN CA C 54.630 0.200 1 428 . 104 ASN C C 175.800 0.200 1 429 . 105 GLN N N 115.990 0.050 1 430 . 105 GLN H H 7.620 0.010 1 431 . 105 GLN HA H 4.300 0.010 1 432 . 105 GLN CA C 55.840 0.200 1 433 . 105 GLN C C 175.930 0.200 1 434 . 106 VAL N N 114.650 0.050 1 435 . 106 VAL H H 7.150 0.010 1 436 . 106 VAL HA H 4.370 0.010 1 437 . 106 VAL CA C 60.440 0.200 1 438 . 106 VAL C C 175.690 0.200 1 439 . 107 LYS N N 123.300 0.050 1 440 . 107 LYS H H 8.610 0.010 1 441 . 107 LYS HA H 4.770 0.010 1 442 . 107 LYS CA C 58.840 0.200 1 443 . 107 LYS C C 177.390 0.200 1 444 . 108 THR N N 111.240 0.050 1 445 . 108 THR H H 7.530 0.010 1 446 . 108 THR HA H 4.380 0.010 1 447 . 108 THR CA C 60.950 0.200 1 448 . 108 THR C C 172.830 0.200 1 449 . 109 CYS N N 126.280 0.050 1 450 . 109 CYS H H 8.670 0.010 1 451 . 109 CYS HA H 4.380 0.010 1 452 . 109 CYS CA C 58.230 0.200 1 453 . 109 CYS C C 173.650 0.200 1 454 . 110 LYS N N 129.080 0.050 1 455 . 110 LYS H H 8.590 0.010 1 456 . 110 LYS HA H 4.360 0.010 1 457 . 110 LYS CA C 56.950 0.200 1 458 . 110 LYS C C 176.370 0.200 1 459 . 111 ALA N N 122.750 0.050 1 460 . 111 ALA H H 7.500 0.010 1 461 . 111 ALA HA H 4.120 0.010 1 462 . 111 ALA CA C 53.230 0.200 1 463 . 111 ALA C C 177.560 0.200 1 464 . 112 LYS N N 122.160 0.050 1 465 . 112 LYS H H 7.680 0.010 1 466 . 112 LYS HA H 4.380 0.010 1 467 . 112 LYS CA C 56.010 0.200 1 468 . 112 LYS C C 175.320 0.200 1 469 . 113 ILE N N 127.170 0.050 1 470 . 113 ILE H H 8.530 0.010 1 471 . 113 ILE HA H 5.050 0.010 1 472 . 113 ILE CA C 60.990 0.200 1 473 . 113 ILE C C 178.340 0.200 1 474 . 114 GLU N N 124.800 0.050 1 475 . 114 GLU H H 8.920 0.010 1 476 . 114 GLU HA H 4.790 0.010 1 477 . 114 GLU CA C 53.820 0.200 1 478 . 114 GLU C C 175.510 0.200 1 479 . 115 LEU N N 121.210 0.050 1 480 . 115 LEU H H 8.950 0.010 1 481 . 115 LEU HA H 4.640 0.010 1 482 . 115 LEU CA C 53.880 0.200 1 483 . 116 LEU N N 131.180 0.050 1 484 . 116 LEU H H 10.040 0.010 1 485 . 116 LEU HA H 5.820 0.010 1 486 . 116 LEU CA C 58.400 0.200 1 487 . 116 LEU C C 178.120 0.200 1 488 . 117 GLY N N 105.000 0.050 1 489 . 117 GLY H H 10.050 0.010 1 490 . 117 GLY CA C 46.400 0.200 1 491 . 117 GLY C C 176.950 0.200 1 492 . 118 SER N N 117.550 0.050 1 493 . 118 SER H H 7.930 0.010 1 494 . 118 SER HA H 4.050 0.010 1 495 . 118 SER CA C 61.650 0.200 1 496 . 123 LYS CA C 57.020 0.200 1 497 . 123 LYS C C 174.940 0.200 1 498 . 124 GLN N N 120.670 0.050 1 499 . 124 GLN H H 8.200 0.010 1 500 . 124 GLN HA H 4.030 0.010 1 501 . 124 GLN CA C 54.600 0.200 1 502 . 124 GLN C C 174.100 0.200 1 503 . 125 LEU N N 122.310 0.050 1 504 . 125 LEU H H 7.290 0.010 1 505 . 125 LEU HA H 3.730 0.010 1 506 . 125 LEU CA C 58.160 0.200 1 507 . 125 LEU C C 178.190 0.200 1 508 . 126 ILE N N 118.620 0.050 1 509 . 126 ILE H H 8.130 0.010 1 510 . 126 ILE HA H 4.070 0.010 1 511 . 126 ILE CA C 58.610 0.200 1 512 . 126 ILE C C 175.800 0.200 1 513 . 127 ILE N N 129.270 0.050 1 514 . 127 ILE H H 7.830 0.010 1 515 . 127 ILE CA C 61.230 0.200 1 516 . 127 ILE C C 175.140 0.200 1 517 . 128 GLU N N 127.870 0.050 1 518 . 128 GLU H H 8.980 0.010 1 519 . 128 GLU HA H 4.130 0.010 1 520 . 128 GLU CA C 56.480 0.200 1 521 . 128 GLU C C 177.240 0.200 1 522 . 129 ASP N N 124.720 0.050 1 523 . 129 ASP H H 8.860 0.010 1 524 . 129 ASP HA H 4.640 0.010 1 525 . 129 ASP CA C 52.270 0.200 1 526 . 130 PRO CA C 62.200 0.200 1 527 . 130 PRO C C 176.150 0.200 1 528 . 131 TYR N N 122.420 0.050 1 529 . 131 TYR H H 7.440 0.010 1 530 . 131 TYR HA H 3.860 0.010 1 531 . 131 TYR CA C 62.380 0.200 1 532 . 131 TYR C C 177.580 0.200 1 533 . 132 TYR N N 116.520 0.050 1 534 . 132 TYR H H 8.690 0.010 1 535 . 132 TYR HA H 4.640 0.010 1 536 . 132 TYR CA C 58.140 0.200 1 537 . 132 TYR C C 175.470 0.200 1 538 . 133 GLY N N 110.640 0.050 1 539 . 133 GLY H H 8.040 0.010 1 540 . 133 GLY HA2 H 4.380 0.010 2 541 . 133 GLY CA C 44.240 0.200 1 542 . 133 GLY C C 173.360 0.200 1 543 . 134 ASN N N 120.260 0.050 1 544 . 134 ASN H H 9.460 0.010 1 545 . 134 ASN HA H 5.290 0.010 1 546 . 134 ASN CA C 51.190 0.200 1 547 . 134 ASN C C 171.310 0.200 1 548 . 135 ASP N N 117.950 0.050 1 549 . 135 ASP H H 8.520 0.010 1 550 . 135 ASP HA H 4.770 0.010 1 551 . 135 ASP CA C 58.110 0.200 1 552 . 136 SER CA C 59.250 0.200 1 553 . 136 SER C C 178.840 0.200 1 554 . 137 ASP N N 122.170 0.050 1 555 . 137 ASP H H 7.870 0.010 1 556 . 137 ASP HA H 5.160 0.010 1 557 . 137 ASP CA C 57.010 0.200 1 558 . 137 ASP C C 178.600 0.200 1 559 . 138 PHE N N 118.530 0.050 1 560 . 138 PHE H H 7.790 0.010 1 561 . 138 PHE HA H 3.740 0.010 1 562 . 138 PHE CA C 63.430 0.200 1 563 . 138 PHE C C 176.650 0.200 1 564 . 139 GLU N N 120.180 0.050 1 565 . 139 GLU H H 7.920 0.010 1 566 . 139 GLU HA H 3.990 0.010 1 567 . 139 GLU CA C 58.900 0.200 1 568 . 139 GLU C C 178.620 0.200 1 569 . 140 THR N N 118.010 0.050 1 570 . 140 THR H H 8.160 0.010 1 571 . 140 THR CA C 67.310 0.200 1 572 . 140 THR C C 175.610 0.200 1 573 . 141 VAL N N 120.820 0.050 1 574 . 141 VAL H H 7.730 0.010 1 575 . 141 VAL CA C 66.900 0.200 1 576 . 141 VAL C C 177.210 0.200 1 577 . 142 TYR N N 121.450 0.050 1 578 . 142 TYR H H 8.690 0.010 1 579 . 142 TYR CA C 62.450 0.200 1 580 . 142 TYR C C 175.650 0.200 1 581 . 143 GLN N N 117.850 0.050 1 582 . 143 GLN H H 8.470 0.010 1 583 . 143 GLN CA C 58.850 0.010 1 584 . 143 GLN C C 180.020 0.200 1 585 . 144 GLN N N 118.260 0.050 1 586 . 144 GLN H H 8.700 0.010 1 587 . 144 GLN CA C 60.790 0.200 1 588 . 144 GLN C C 178.820 0.200 1 589 . 145 CYS N N 117.510 0.050 1 590 . 145 CYS H H 8.720 0.010 1 591 . 145 CYS CA C 66.020 0.200 1 592 . 145 CYS C C 176.930 0.200 1 593 . 146 VAL N N 120.790 0.050 1 594 . 146 VAL H H 8.420 0.010 1 595 . 146 VAL CA C 67.770 0.200 1 596 . 146 VAL C C 177.440 0.200 1 597 . 147 ARG N N 115.510 0.050 1 598 . 147 ARG H H 7.430 0.010 1 599 . 147 ARG CA C 60.340 0.200 1 600 . 147 ARG C C 180.640 0.200 1 601 . 148 CYS N N 116.350 0.050 1 602 . 148 CYS H H 8.490 0.010 1 603 . 148 CYS CA C 64.070 0.200 1 604 . 148 CYS C C 175.440 0.200 1 605 . 149 CYS N N 116.270 0.050 1 606 . 149 CYS H H 8.870 0.010 1 607 . 149 CYS CA C 65.260 0.200 1 608 . 149 CYS C C 176.140 0.200 1 609 . 150 ARG N N 117.810 0.050 1 610 . 150 ARG H H 7.850 0.010 1 611 . 150 ARG HA H 3.780 0.010 1 612 . 150 ARG CA C 60.230 0.200 1 613 . 150 ARG C C 178.200 0.200 1 614 . 151 ALA N N 120.930 0.050 1 615 . 151 ALA H H 7.260 0.010 1 616 . 151 ALA HA H 4.290 0.010 1 617 . 151 ALA CA C 55.240 0.200 1 618 . 151 ALA C C 179.900 0.200 1 619 . 152 PHE N N 120.290 0.050 1 620 . 152 PHE H H 8.480 0.010 1 621 . 152 PHE HA H 4.250 0.010 1 622 . 152 PHE CA C 60.900 0.200 1 623 . 152 PHE C C 176.450 0.200 1 624 . 153 LEU N N 118.180 0.050 1 625 . 153 LEU H H 7.760 0.010 1 626 . 153 LEU HA H 3.730 0.010 1 627 . 153 LEU CA C 57.270 0.200 1 628 . 153 LEU C C 178.850 0.200 1 629 . 154 GLU N N 117.210 0.050 1 630 . 154 GLU H H 7.480 0.010 1 631 . 154 GLU HA H 4.000 0.010 1 632 . 154 GLU CA C 58.700 0.200 1 633 . 154 GLU C C 177.850 0.200 1 634 . 155 LYS N N 118.100 0.050 1 635 . 155 LYS H H 7.660 0.010 1 636 . 155 LYS HA H 4.250 0.010 1 637 . 155 LYS CA C 56.940 0.200 1 638 . 155 LYS C C 175.690 0.200 1 639 . 156 ALA N N 125.900 0.050 1 640 . 156 ALA H H 8.020 0.010 1 641 . 156 ALA HA H 4.250 0.010 1 642 . 156 ALA CA C 52.840 0.200 1 643 . 156 ALA C C 177.210 0.200 1 644 . 157 HIS N N 122.750 0.050 1 645 . 157 HIS H H 8.220 0.010 1 646 . 157 HIS HA H 4.620 0.010 1 647 . 157 HIS CA C 57.270 0.200 1 stop_ save_