data_6361 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Resonance Assignments for the SAP domain of the human protein DEK ; _BMRB_accession_number 6361 _BMRB_flat_file_name bmr6361.str _Entry_type original _Submission_date 2004-10-19 _Accession_date 2004-10-19 _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 Devany Matthew H. . 2 Kotharu N. Prasad . 3 Matsuo Hiroshi . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 605 "13C chemical shifts" 447 "15N chemical shifts" 112 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2005-02-10 original author . stop_ _Original_release_date 2005-02-10 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Letter to the Editor: NMR resonance assignments for the DNA-supercoiling domain of the human protein DEK ; _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 Devany Matthew H. . 2 Matsuo Hiroshi . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 31 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 65 _Page_last 65 _Year 2005 _Details . loop_ _Keyword 'DNA binding' 'SAP domain' '4-way junction' stop_ save_ ################################## # Molecular system description # ################################## save_system_DEK78-186 _Saveframe_category molecular_system _Mol_system_name 'DEK residues 78-186' _Abbreviation_common DEK78-186 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label DEK78-186 $DEK78-186 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Biological_function 'DNA binding' '4-way DNA binding' 'chromatin supercoil inducing' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_DEK78-186 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common DEK _Name_variant DEK78-208 _Abbreviation_common DEK _Molecular_mass 12688 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 109 _Mol_residue_sequence ; FTIAQGKGQKLCEIERIHFF LSKKKTDELRNLHKLLYNRP GTVSSLKKNVGQFSGFPFEK GSVQYKKKEEMLKKFRNAML KSICEVLDLERSGVNSELVK RILNFLMHP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 78 PHE 2 79 THR 3 80 ILE 4 81 ALA 5 82 GLN 6 83 GLY 7 84 LYS 8 85 GLY 9 86 GLN 10 87 LYS 11 88 LEU 12 89 CYS 13 90 GLU 14 91 ILE 15 92 GLU 16 93 ARG 17 94 ILE 18 95 HIS 19 96 PHE 20 97 PHE 21 98 LEU 22 99 SER 23 100 LYS 24 101 LYS 25 102 LYS 26 103 THR 27 104 ASP 28 105 GLU 29 106 LEU 30 107 ARG 31 108 ASN 32 109 LEU 33 110 HIS 34 111 LYS 35 112 LEU 36 113 LEU 37 114 TYR 38 115 ASN 39 116 ARG 40 117 PRO 41 118 GLY 42 119 THR 43 120 VAL 44 121 SER 45 122 SER 46 123 LEU 47 124 LYS 48 125 LYS 49 126 ASN 50 127 VAL 51 128 GLY 52 129 GLN 53 130 PHE 54 131 SER 55 132 GLY 56 133 PHE 57 134 PRO 58 135 PHE 59 136 GLU 60 137 LYS 61 138 GLY 62 139 SER 63 140 VAL 64 141 GLN 65 142 TYR 66 143 LYS 67 144 LYS 68 145 LYS 69 146 GLU 70 147 GLU 71 148 MET 72 149 LEU 73 150 LYS 74 151 LYS 75 152 PHE 76 153 ARG 77 154 ASN 78 155 ALA 79 156 MET 80 157 LEU 81 158 LYS 82 159 SER 83 160 ILE 84 161 CYS 85 162 GLU 86 163 VAL 87 164 LEU 88 165 ASP 89 166 LEU 90 167 GLU 91 168 ARG 92 169 SER 93 170 GLY 94 171 VAL 95 172 ASN 96 173 SER 97 174 GLU 98 175 LEU 99 176 VAL 100 177 LYS 101 178 ARG 102 179 ILE 103 180 LEU 104 181 ASN 105 182 PHE 106 183 LEU 107 184 MET 108 185 HIS 109 186 PRO 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 2JX3 "Nmr Solution Structure Of The N-Terminal Domain Of Dek" 100.00 131 100.00 100.00 2.15e-71 DBJ BAB25100 "unnamed protein product [Mus musculus]" 84.40 282 97.83 97.83 1.33e-57 DBJ BAG35503 "unnamed protein product [Homo sapiens]" 100.00 375 100.00 100.00 2.61e-72 DBJ BAG60099 "unnamed protein product [Homo sapiens]" 96.33 341 99.05 100.00 1.66e-68 DBJ BAG60375 "unnamed protein product [Homo sapiens]" 100.00 351 98.17 98.17 1.03e-69 DBJ BAG72522 "DEK oncogene [synthetic construct]" 100.00 375 99.08 99.08 9.32e-72 EMBL CAA45536 "putative oncogene [Homo sapiens]" 100.00 375 100.00 100.00 2.61e-72 GB AAH35259 "DEK oncogene [Homo sapiens]" 100.00 375 100.00 100.00 2.61e-72 GB AAH79344 "DEK oncogene [Rattus norvegicus]" 100.00 378 98.17 99.08 1.10e-71 GB AAI42199 "DEK protein [Bos taurus]" 100.00 375 99.08 100.00 4.63e-72 GB ABZ92195 "DEK oncogene (DNA binding) [synthetic construct]" 100.00 375 100.00 100.00 2.85e-72 GB ADP20523 "DEK [Fukomys anselli]" 100.00 377 99.08 100.00 1.61e-72 REF NP_001004255 "protein DEK [Rattus norvegicus]" 100.00 378 98.17 99.08 1.10e-71 REF NP_001093187 "protein DEK [Bos taurus]" 100.00 375 99.08 100.00 4.63e-72 REF NP_001128181 "protein DEK isoform 2 [Homo sapiens]" 96.33 341 99.05 100.00 1.66e-68 REF NP_001244457 "protein DEK [Macaca mulatta]" 100.00 375 100.00 100.00 1.97e-72 REF NP_001266767 "DEK oncogene [Heterocephalus glaber]" 100.00 375 99.08 100.00 2.64e-72 SP P35659 "RecName: Full=Protein DEK [Homo sapiens]" 100.00 375 100.00 100.00 2.61e-72 SP Q6AXS3 "RecName: Full=Protein DEK [Rattus norvegicus]" 100.00 378 98.17 99.08 1.10e-71 TPG DAA16149 "TPA: DEK oncogene [Bos taurus]" 100.00 375 99.08 100.00 4.63e-72 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Fraction _Gene_mnemonic $DEK78-186 Humans 9606 Eukaryota Metazoa Homo sapiens nucleus dek 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 $DEK78-186 'recombinant technology' . . . . . 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 $DEK78-186 0.7 mM '[U-13C; U-15N]' Na2HPO4 25 mM . NaH2PO4 25 mM . KCl 100 mM . DTT 20 mM . pefabloc 0.4 mM . NaN3 0.02 % . DTT 20 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_CBCANH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _Sample_label . save_ save_CBCACONH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_HCCHTOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCHTOCSY _Sample_label . save_ save_1H-13C_NOESYHSQC_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESYHSQC' _Sample_label . save_ save_1H-15N_NOESYHSQC_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESYHSQC' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCANH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name HCCHTOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESYHSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_9 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESYHSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_cond-1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 0.2 n/a temperature 298 1 K 'ionic strength' 0.15 0.02 M 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 H2O C 13 protons ppm 0.0 external indirect . . . . H2O N 15 protons ppm 0.0 external indirect . . . . 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_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $cond-1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name DEK78-186 _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 PHE H H 8.052 0.02 1 2 . 1 PHE N N 120.600 0.05 1 3 . 1 PHE CA C 56.836 0.2 1 4 . 1 PHE HA H 4.390 0.02 1 5 . 1 PHE CB C 39.865 0.2 1 6 . 1 PHE HB2 H 3.016 0.02 2 7 . 1 PHE CD1 C 127.694 0.2 3 8 . 1 PHE HD1 H 7.056 0.02 3 9 . 1 PHE CE1 C 126.523 0.2 3 10 . 1 PHE HE1 H 6.902 0.02 3 11 . 2 THR H H 8.254 0.02 1 12 . 2 THR N N 118.705 0.1 1 13 . 2 THR CA C 62.028 0.2 1 14 . 2 THR HA H 4.167 0.02 1 15 . 2 THR CB C 70.199 0.2 1 16 . 2 THR HB H 4.015 0.02 1 17 . 2 THR HG2 H 1.127 0.02 1 18 . 2 THR CG2 C 21.535 0.2 1 19 . 3 ILE H H 8.425 0.02 1 20 . 3 ILE N N 126.700 0.1 1 21 . 3 ILE CA C 61.316 0.2 1 22 . 3 ILE HA H 4.063 0.02 1 23 . 3 ILE CB C 38.587 0.2 1 24 . 3 ILE HB H 1.677 0.02 1 25 . 3 ILE CG2 C 17.159 0.2 1 26 . 3 ILE HG2 H 1.035 0.02 1 27 . 3 ILE CG1 C 28.100 0.2 1 28 . 3 ILE HG12 H 0.830 0.02 2 29 . 3 ILE HG13 H 1.201 0.02 2 30 . 3 ILE CD1 C 13.095 0.2 2 31 . 3 ILE HD1 H 0.646 0.02 1 32 . 4 ALA H H 8.772 0.02 1 33 . 4 ALA N N 131.000 0.1 1 34 . 4 ALA CA C 51.798 0.2 1 35 . 4 ALA HA H 4.349 0.02 1 36 . 4 ALA C C 176.570 0.2 1 37 . 4 ALA CB C 19.774 0.2 1 38 . 4 ALA HB H 1.418 0.02 1 39 . 5 GLN H H 8.467 0.02 1 40 . 5 GLN N N 120.900 0.1 1 41 . 5 GLN CA C 55.869 0.2 1 42 . 5 GLN HA H 4.010 0.02 1 43 . 5 GLN C C 176.223 0.2 1 44 . 5 GLN CB C 29.518 0.2 1 45 . 5 GLN HB2 H 2.021 0.02 2 46 . 5 GLN CG C 33.414 0.2 1 47 . 5 GLN HG2 H 2.442 0.02 2 48 . 5 GLN HG3 H 2.514 0.02 2 49 . 5 GLN NE2 N 113.352 0.1 1 50 . 5 GLN HE21 H 6.872 0.02 2 51 . 5 GLN HE22 H 7.590 0.02 2 52 . 6 GLY H H 8.362 0.02 1 53 . 6 GLY N N 114.217 0.1 1 54 . 6 GLY CA C 43.423 0.2 1 55 . 6 GLY HA2 H 3.047 0.02 2 56 . 6 GLY HA3 H 4.050 0.02 2 57 . 6 GLY C C 174.557 0.2 1 58 . 7 LYS H H 8.991 0.02 1 59 . 7 LYS N N 117.470 0.1 1 60 . 7 LYS CA C 56.506 0.2 1 61 . 7 LYS HA H 4.166 0.02 1 62 . 7 LYS C C 177.131 0.2 1 63 . 7 LYS CB C 33.264 0.2 1 64 . 7 LYS HB2 H 1.531 0.02 2 65 . 7 LYS HB3 H 1.769 0.02 2 66 . 7 LYS CG C 24.974 0.2 1 67 . 7 LYS HG2 H 1.435 0.02 2 68 . 7 LYS HG3 H 1.526 0.02 2 69 . 7 LYS CD C 28.412 0.2 1 70 . 7 LYS HD2 H 1.688 0.02 2 71 . 7 LYS HE2 H 3.037 0.02 2 72 . 8 GLY H H 8.032 0.02 1 73 . 8 GLY N N 105.900 0.1 1 74 . 8 GLY CA C 43.886 0.2 1 75 . 8 GLY HA2 H 3.171 0.02 2 76 . 8 GLY HA3 H 4.258 0.02 2 77 . 8 GLY C C 172.149 0.2 1 78 . 9 GLN H H 7.658 0.02 1 79 . 9 GLN N N 120.600 0.1 1 80 . 9 GLN CA C 54.232 0.2 1 81 . 9 GLN HA H 4.360 0.02 1 82 . 9 GLN C C 174.554 0.2 1 83 . 9 GLN CB C 30.995 0.2 1 84 . 9 GLN HB2 H 1.679 0.02 2 85 . 9 GLN HB3 H 1.970 0.02 2 86 . 9 GLN CG C 34.664 0.2 1 87 . 9 GLN HG2 H 2.439 0.02 2 88 . 9 GLN NE2 N 111.301 0.1 1 89 . 9 GLN HE21 H 6.791 0.02 2 90 . 9 GLN HE22 H 7.398 0.02 2 91 . 10 LYS H H 8.019 0.02 1 92 . 10 LYS N N 117.700 0.1 1 93 . 10 LYS CA C 56.353 0.2 1 94 . 10 LYS HA H 4.420 0.02 1 95 . 10 LYS C C 179.785 0.2 1 96 . 10 LYS CB C 33.903 0.2 1 97 . 10 LYS HB2 H 1.414 0.02 2 98 . 10 LYS HB3 H 2.205 0.02 2 99 . 10 LYS CG C 26.231 0.2 1 100 . 10 LYS HG2 H 1.386 0.02 2 101 . 10 LYS HG3 H 1.556 0.02 2 102 . 10 LYS CD C 30.600 0.2 1 103 . 10 LYS HD2 H 1.569 0.02 2 104 . 10 LYS CE C 42.480 0.2 1 105 . 10 LYS HE2 H 3.007 0.02 2 106 . 11 LEU H H 8.578 0.02 1 107 . 11 LEU N N 120.600 0.1 1 108 . 11 LEU CA C 58.648 0.2 1 109 . 11 LEU HA H 4.036 0.02 1 110 . 11 LEU C C 179.101 0.2 1 111 . 11 LEU CB C 39.771 0.2 1 112 . 11 LEU HB2 H 1.519 0.02 2 113 . 11 LEU HB3 H 2.260 0.02 2 114 . 11 LEU CG C 26.537 0.2 1 115 . 11 LEU CD1 C 24.600 0.2 2 116 . 11 LEU HD1 H 1.028 0.02 2 117 . 11 LEU CD2 C 22.473 0.2 2 118 . 11 LEU HD2 H 1.129 0.02 2 119 . 11 LEU HG H 2.646 0.02 1 120 . 12 CYS H H 9.286 0.02 1 121 . 12 CYS N N 110.000 0.1 1 122 . 12 CYS CA C 59.208 0.2 1 123 . 12 CYS HA H 4.399 0.02 1 124 . 12 CYS C C 174.179 0.2 1 125 . 12 CYS CB C 26.904 0.2 1 126 . 12 CYS HB2 H 2.775 0.02 2 127 . 12 CYS HB3 H 3.028 0.02 2 128 . 13 GLU H H 7.990 0.02 1 129 . 13 GLU N N 121.400 0.1 1 130 . 13 GLU CA C 55.833 0.2 1 131 . 13 GLU HA H 4.279 0.02 1 132 . 13 GLU C C 175.537 0.2 1 133 . 13 GLU CB C 29.615 0.2 1 134 . 13 GLU HB2 H 2.130 0.02 2 135 . 13 GLU HB3 H 2.300 0.02 2 136 . 14 ILE H H 7.632 0.02 1 137 . 14 ILE N N 123.250 0.1 1 138 . 14 ILE CA C 61.526 0.2 1 139 . 14 ILE HA H 4.214 0.02 1 140 . 14 ILE C C 176.033 0.2 1 141 . 14 ILE CB C 37.369 0.2 1 142 . 14 ILE HB H 2.301 0.02 1 143 . 14 ILE CG2 C 18.722 0.2 1 144 . 14 ILE HG2 H 1.150 0.02 1 145 . 14 ILE CG1 C 26.849 0.2 1 146 . 14 ILE HG12 H 1.996 0.02 2 147 . 14 ILE CD1 C 14.033 0.2 1 148 . 14 ILE HD1 H 0.757 0.02 1 149 . 15 GLU H H 9.027 0.02 1 150 . 15 GLU N N 128.600 0.1 1 151 . 15 GLU CA C 61.297 0.2 1 152 . 15 GLU HA H 4.069 0.02 1 153 . 15 GLU C C 179.331 0.2 1 154 . 15 GLU CB C 30.000 0.2 1 155 . 15 GLU HB2 H 2.069 0.02 2 156 . 15 GLU HB3 H 2.111 0.02 2 157 . 15 GLU CG C 36.227 0.2 1 158 . 15 GLU HG2 H 2.274 0.02 2 159 . 15 GLU HG3 H 2.353 0.02 2 160 . 16 ARG H H 9.417 0.02 1 161 . 16 ARG N N 117.525 0.1 1 162 . 16 ARG CA C 60.122 0.2 1 163 . 16 ARG HA H 3.736 0.02 1 164 . 16 ARG C C 177.115 0.2 1 165 . 16 ARG CB C 29.847 0.2 1 166 . 16 ARG HB2 H 1.680 0.02 2 167 . 16 ARG HB3 H 1.811 0.02 2 168 . 16 ARG CG C 28.100 0.2 1 169 . 16 ARG HG2 H 1.519 0.02 2 170 . 16 ARG HG3 H 1.689 0.02 2 171 . 16 ARG CD C 42.792 0.2 1 172 . 16 ARG HD2 H 2.960 0.02 2 173 . 16 ARG HD3 H 3.150 0.02 2 174 . 17 ILE H H 6.739 0.02 1 175 . 17 ILE N N 117.150 0.1 1 176 . 17 ILE CA C 65.432 0.2 1 177 . 17 ILE HA H 4.156 0.02 1 178 . 17 ILE C C 177.564 0.2 1 179 . 17 ILE CB C 37.949 0.2 1 180 . 17 ILE HB H 2.220 0.02 1 181 . 17 ILE CG2 C 15.917 0.2 1 182 . 17 ILE HG2 H 1.244 0.02 1 183 . 17 ILE CG1 C 28.106 0.2 1 184 . 17 ILE HG12 H 1.400 0.02 2 185 . 17 ILE HG13 H 1.789 0.02 2 186 . 17 ILE CD1 C 16.542 0.2 1 187 . 17 ILE HD1 H 1.144 0.02 1 188 . 18 HIS H H 8.950 0.02 1 189 . 18 HIS N N 119.300 0.1 1 190 . 18 HIS CA C 60.562 0.2 1 191 . 18 HIS HA H 4.022 0.02 1 192 . 18 HIS C C 178.212 0.2 1 193 . 18 HIS CB C 29.996 0.2 1 194 . 18 HIS HB2 H 3.240 0.02 2 195 . 18 HIS HD2 H 7.022 0.02 1 196 . 18 HIS HE1 H 7.972 0.02 1 197 . 19 PHE H H 7.968 0.02 1 198 . 19 PHE N N 118.700 0.1 1 199 . 19 PHE CA C 61.292 0.2 1 200 . 19 PHE HA H 4.150 0.02 1 201 . 19 PHE C C 178.116 0.2 1 202 . 19 PHE CB C 38.646 0.2 1 203 . 19 PHE HB2 H 3.037 0.02 2 204 . 19 PHE HB3 H 3.174 0.02 2 205 . 19 PHE HD1 H 6.908 0.02 3 206 . 19 PHE HE1 H 7.318 0.02 3 207 . 20 PHE H H 8.413 0.02 1 208 . 20 PHE N N 120.680 0.1 1 209 . 20 PHE CA C 60.209 0.2 1 210 . 20 PHE HA H 4.337 0.02 1 211 . 20 PHE C C 179.983 0.2 1 212 . 20 PHE CB C 38.182 0.2 1 213 . 20 PHE HB2 H 3.253 0.02 2 214 . 20 PHE HB3 H 3.528 0.02 2 215 . 20 PHE CD1 C 127.500 0.2 3 216 . 20 PHE HD1 H 7.337 0.02 3 217 . 20 PHE CE1 C 126.347 0.2 3 218 . 20 PHE HE1 H 7.320 0.02 3 219 . 21 LEU H H 9.410 0.02 1 220 . 21 LEU N N 119.260 0.1 1 221 . 21 LEU CA C 58.008 0.2 1 222 . 21 LEU HA H 3.870 0.02 1 223 . 21 LEU C C 179.014 0.2 1 224 . 21 LEU CB C 42.059 0.2 1 225 . 21 LEU HB2 H 1.367 0.02 2 226 . 21 LEU HB3 H 1.948 0.02 2 227 . 21 LEU CG C 26.537 0.2 1 228 . 21 LEU CD1 C 24.349 0.2 2 229 . 21 LEU HD1 H 0.743 0.02 2 230 . 21 LEU CD2 C 25.912 0.2 2 231 . 21 LEU HD2 H 0.796 0.02 2 232 . 21 LEU HG H 1.940 0.02 1 233 . 22 SER H H 7.680 0.02 1 234 . 22 SER N N 112.769 0.1 1 235 . 22 SER CA C 61.216 0.2 1 236 . 22 SER HA H 4.038 0.02 1 237 . 22 SER C C 174.929 0.2 1 238 . 22 SER CB C 63.080 0.2 1 239 . 22 SER HB2 H 3.754 0.02 2 240 . 23 LYS H H 7.145 0.02 1 241 . 23 LYS N N 118.741 0.1 1 242 . 23 LYS CA C 55.852 0.2 1 243 . 23 LYS HA H 4.264 0.02 1 244 . 23 LYS C C 177.216 0.2 1 245 . 23 LYS CB C 32.884 0.2 1 246 . 23 LYS HB2 H 1.679 0.02 2 247 . 23 LYS HB3 H 1.876 0.02 2 248 . 23 LYS CG C 24.036 0.2 1 249 . 23 LYS HG2 H 1.192 0.02 2 250 . 23 LYS CD C 28.100 0.2 1 251 . 23 LYS HD2 H 1.416 0.02 2 252 . 23 LYS CE C 41.541 0.2 1 253 . 23 LYS HE2 H 2.607 0.02 2 254 . 23 LYS HE3 H 2.789 0.02 2 255 . 24 LYS H H 7.319 0.02 1 256 . 24 LYS N N 118.740 0.1 1 257 . 24 LYS CA C 54.536 0.2 1 258 . 24 LYS HA H 4.357 0.02 1 259 . 24 LYS C C 176.237 0.2 1 260 . 24 LYS CB C 33.090 0.2 1 261 . 24 LYS HB2 H 1.713 0.02 2 262 . 24 LYS HB3 H 1.920 0.02 2 263 . 24 LYS CG C 24.349 0.2 1 264 . 24 LYS HG2 H 1.373 0.02 2 265 . 24 LYS HG3 H 1.721 0.02 2 266 . 24 LYS CD C 28.100 0.2 1 267 . 24 LYS HD2 H 1.565 0.02 2 268 . 24 LYS HD3 H 1.641 0.02 2 269 . 24 LYS CE C 41.854 0.2 1 270 . 24 LYS HE2 H 2.768 0.02 2 271 . 24 LYS HE3 H 2.833 0.02 2 272 . 25 LYS H H 8.914 0.02 1 273 . 25 LYS N N 121.400 0.1 1 274 . 25 LYS CA C 55.621 0.2 1 275 . 25 LYS HA H 4.480 0.02 1 276 . 25 LYS C C 178.404 0.2 1 277 . 25 LYS CB C 33.188 0.2 1 278 . 25 LYS HB2 H 1.790 0.02 2 279 . 25 LYS HB3 H 2.123 0.02 2 280 . 25 LYS CG C 25.286 0.2 1 281 . 25 LYS HG2 H 1.560 0.02 2 282 . 25 LYS HG3 H 1.640 0.02 2 283 . 25 LYS CD C 28.725 0.2 1 284 . 25 LYS HD2 H 1.736 0.02 2 285 . 25 LYS HD3 H 1.773 0.02 2 286 . 25 LYS CE C 41.854 0.2 1 287 . 25 LYS HE2 H 3.044 0.02 2 288 . 26 THR H H 8.642 0.02 1 289 . 26 THR N N 117.700 0.1 1 290 . 26 THR CA C 67.975 0.2 1 291 . 26 THR HA H 3.635 0.02 1 292 . 26 THR C C 176.318 0.2 1 293 . 26 THR CB C 68.757 0.2 1 294 . 26 THR HB H 4.161 0.02 1 295 . 26 THR HG2 H 1.319 0.02 1 296 . 26 THR CG2 C 23.098 0.2 1 297 . 27 ASP H H 8.681 0.02 1 298 . 27 ASP N N 116.900 0.1 1 299 . 27 ASP CA C 57.480 0.2 1 300 . 27 ASP HA H 4.264 0.02 1 301 . 27 ASP C C 178.420 0.2 1 302 . 27 ASP CB C 40.181 0.2 1 303 . 27 ASP HB2 H 2.585 0.02 2 304 . 27 ASP HB3 H 2.665 0.02 2 305 . 28 GLU H H 7.538 0.02 1 306 . 28 GLU N N 116.999 0.1 1 307 . 28 GLU CA C 57.969 0.2 1 308 . 28 GLU HA H 4.267 0.02 1 309 . 28 GLU C C 178.403 0.2 1 310 . 28 GLU CB C 30.053 0.2 1 311 . 28 GLU HB2 H 2.138 0.02 2 312 . 28 GLU HB3 H 2.331 0.02 2 313 . 28 GLU CG C 34.039 0.2 1 314 . 28 GLU HG2 H 2.302 0.02 2 315 . 29 LEU H H 7.871 0.02 1 316 . 29 LEU N N 118.500 0.1 1 317 . 29 LEU CA C 55.264 0.2 1 318 . 29 LEU HA H 4.421 0.02 1 319 . 29 LEU CB C 43.416 0.2 1 320 . 29 LEU HB2 H 1.572 0.02 2 321 . 29 LEU HB3 H 1.996 0.02 2 322 . 29 LEU CG C 26.500 0.2 1 323 . 29 LEU CD1 C 23.098 0.2 2 324 . 29 LEU HD1 H 0.858 0.02 2 325 . 29 LEU HG H 1.692 0.02 1 326 . 31 ASN H H 8.397 0.02 1 327 . 31 ASN N N 117.677 0.1 1 328 . 31 ASN CA C 56.129 0.2 1 329 . 31 ASN HA H 4.515 0.02 1 330 . 31 ASN C C 177.708 0.2 1 331 . 31 ASN CB C 37.382 0.2 1 332 . 31 ASN HB2 H 2.428 0.02 2 333 . 31 ASN HB3 H 2.852 0.02 2 334 . 31 ASN ND2 N 113.329 0.1 1 335 . 31 ASN HD21 H 6.956 0.02 2 336 . 31 ASN HD22 H 7.398 0.02 2 337 . 32 LEU H H 7.921 0.02 1 338 . 32 LEU N N 120.300 0.1 1 339 . 32 LEU CA C 57.751 0.2 1 340 . 32 LEU HA H 4.080 0.02 1 341 . 32 LEU C C 171.558 0.2 1 342 . 32 LEU CB C 41.354 0.2 1 343 . 32 LEU HB2 H 1.567 0.02 2 344 . 32 LEU HB3 H 1.903 0.02 2 345 . 32 LEU CG C 27.160 0.2 1 346 . 32 LEU CD1 C 23.098 0.2 2 347 . 32 LEU HD1 H 0.856 0.02 1 348 . 32 LEU CD2 C 26.224 0.2 2 349 . 32 LEU HD2 H 0.856 0.02 1 350 . 32 LEU HG H 1.530 0.02 1 351 . 33 HIS H H 8.608 0.02 1 352 . 33 HIS N N 119.000 0.1 1 353 . 33 HIS CA C 62.246 0.2 1 354 . 33 HIS HA H 3.794 0.02 1 355 . 33 HIS C C 177.382 0.2 1 356 . 33 HIS CB C 29.074 0.2 1 357 . 33 HIS HB2 H 3.081 0.02 2 358 . 33 HIS HB3 H 3.376 0.02 2 359 . 33 HIS HD2 H 6.750 0.02 1 360 . 33 HIS HE1 H 7.376 0.02 1 361 . 34 LYS H H 8.250 0.02 1 362 . 34 LYS N N 118.500 0.1 1 363 . 34 LYS CA C 60.142 0.2 1 364 . 34 LYS HA H 4.064 0.02 1 365 . 34 LYS C C 178.840 0.2 1 366 . 34 LYS CB C 32.315 0.2 1 367 . 34 LYS HB2 H 1.969 0.02 2 368 . 34 LYS HB3 H 2.030 0.02 2 369 . 34 LYS CG C 25.599 0.2 1 370 . 34 LYS HG2 H 1.366 0.02 2 371 . 34 LYS HG3 H 1.583 0.02 2 372 . 34 LYS CD C 29.663 0.2 1 373 . 34 LYS HD2 H 1.686 0.02 2 374 . 34 LYS CE C 41.541 0.2 1 375 . 34 LYS HE2 H 2.929 0.02 2 376 . 35 LEU H H 7.952 0.02 1 377 . 35 LEU N N 120.900 0.1 1 378 . 35 LEU CA C 57.979 0.2 1 379 . 35 LEU HA H 4.269 0.02 1 380 . 35 LEU C C 178.271 0.2 1 381 . 35 LEU CB C 42.085 0.2 1 382 . 35 LEU HB2 H 1.581 0.02 2 383 . 35 LEU HB3 H 2.217 0.02 2 384 . 35 LEU CG C 27.474 0.2 1 385 . 35 LEU CD1 C 26.849 0.2 2 386 . 35 LEU HD1 H 0.877 0.02 2 387 . 35 LEU CD2 C 23.723 0.2 2 388 . 35 LEU HD2 H 0.975 0.02 2 389 . 35 LEU HG H 1.531 0.02 1 390 . 36 LEU H H 8.134 0.02 1 391 . 36 LEU N N 116.361 0.1 1 392 . 36 LEU CA C 57.763 0.2 1 393 . 36 LEU HA H 3.742 0.02 1 394 . 36 LEU C C 179.121 0.2 1 395 . 36 LEU CB C 38.785 0.2 1 396 . 36 LEU HB2 H -0.075 0.02 2 397 . 36 LEU HB3 H 0.693 0.02 2 398 . 36 LEU CG C 25.000 0.2 1 399 . 36 LEU CD1 C 21.223 0.2 2 400 . 36 LEU HD1 H -0.537 0.02 2 401 . 36 LEU CD2 C 25.599 0.2 2 402 . 36 LEU HD2 H 0.272 0.02 2 403 . 36 LEU HG H 1.408 0.02 1 404 . 37 TYR H H 7.953 0.02 1 405 . 37 TYR N N 112.556 0.1 1 406 . 37 TYR CA C 57.287 0.2 1 407 . 37 TYR HA H 5.164 0.02 1 408 . 37 TYR C C 176.446 0.2 1 409 . 37 TYR CB C 40.503 0.2 1 410 . 37 TYR HB2 H 2.303 0.02 2 411 . 37 TYR HB3 H 3.137 0.02 2 412 . 37 TYR HD1 H 6.404 0.02 3 413 . 37 TYR CE1 C 113.467 0.2 3 414 . 37 TYR HE1 H 6.657 0.02 3 415 . 38 ASN H H 8.932 0.02 1 416 . 38 ASN N N 117.400 0.1 1 417 . 38 ASN CA C 54.399 0.2 1 418 . 38 ASN HA H 4.634 0.02 1 419 . 38 ASN C C 173.594 0.2 1 420 . 38 ASN CB C 37.614 0.2 1 421 . 38 ASN HB2 H 2.828 0.02 2 422 . 38 ASN HB3 H 3.355 0.02 2 423 . 38 ASN ND2 N 112.652 0.1 1 424 . 38 ASN HD21 H 7.641 0.02 2 425 . 38 ASN HD22 H 6.900 0.02 2 426 . 39 ARG H H 7.213 0.02 1 427 . 39 ARG N N 113.119 0.1 1 428 . 39 ARG CA C 53.115 0.2 1 429 . 39 ARG HA H 4.949 0.02 1 430 . 39 ARG CB C 32.319 0.2 1 431 . 39 ARG HB2 H 1.533 0.02 2 432 . 39 ARG HB3 H 2.078 0.02 2 433 . 39 ARG CG C 25.912 0.2 1 434 . 39 ARG HG2 H 1.469 0.02 2 435 . 39 ARG HG3 H 1.753 0.02 2 436 . 39 ARG CD C 43.104 0.2 1 437 . 39 ARG HD2 H 2.716 0.02 2 438 . 39 ARG HD3 H 2.775 0.02 2 439 . 40 PRO CA C 63.753 0.2 1 440 . 40 PRO HA H 4.549 0.02 1 441 . 40 PRO C C 176.505 0.2 1 442 . 40 PRO CB C 32.281 0.2 1 443 . 40 PRO HB2 H 2.041 0.02 2 444 . 40 PRO HB3 H 2.269 0.02 2 445 . 40 PRO CG C 27.162 0.2 1 446 . 40 PRO HG2 H 2.016 0.02 2 447 . 40 PRO HG3 H 2.142 0.02 2 448 . 40 PRO CD C 50.294 0.2 1 449 . 40 PRO HD2 H 3.821 0.02 2 450 . 41 GLY H H 7.916 0.02 1 451 . 41 GLY N N 105.720 0.1 1 452 . 41 GLY CA C 43.373 0.2 1 453 . 41 GLY HA2 H 2.936 0.02 2 454 . 41 GLY HA3 H 3.640 0.02 2 455 . 41 GLY C C 172.906 0.2 1 456 . 42 THR H H 7.665 0.02 1 457 . 42 THR N N 111.496 0.1 1 458 . 42 THR CA C 59.470 0.2 1 459 . 42 THR HA H 4.657 0.02 1 460 . 42 THR CB C 71.152 0.2 1 461 . 42 THR HB H 4.363 0.02 1 462 . 42 THR HG2 H 1.202 0.02 1 463 . 42 THR CG2 C 21.535 0.2 1 464 . 43 VAL H H 8.760 0.02 1 465 . 43 VAL N N 121.620 0.1 1 466 . 43 VAL CA C 66.811 0.2 1 467 . 43 VAL HA H 3.673 0.02 1 468 . 43 VAL C C 177.731 0.2 1 469 . 43 VAL CB C 31.484 0.2 1 470 . 43 VAL HB H 2.164 0.02 1 471 . 43 VAL CG1 C 20.910 0.2 2 472 . 43 VAL HG1 H 1.014 0.02 2 473 . 43 VAL CG2 C 21.848 0.2 2 474 . 43 VAL HG2 H 1.083 0.02 2 475 . 44 SER H H 7.647 0.02 1 476 . 44 SER N N 112.600 0.1 1 477 . 44 SER CA C 60.451 0.2 1 478 . 44 SER HA H 4.357 0.02 1 479 . 44 SER C C 175.747 0.2 1 480 . 44 SER CB C 63.130 0.2 1 481 . 44 SER HB2 H 3.919 0.02 2 482 . 45 SER N N 114.500 0.1 1 483 . 45 SER CA C 58.540 0.2 1 484 . 45 SER HA H 4.397 0.02 1 485 . 45 SER C C 174.757 0.2 1 486 . 45 SER CB C 65.372 0.2 1 487 . 45 SER HB2 H 3.808 0.02 2 488 . 46 LEU H H 7.800 0.02 1 489 . 46 LEU N N 123.500 0.1 1 490 . 46 LEU CA C 60.952 0.2 1 491 . 46 LEU HA H 4.002 0.02 1 492 . 46 LEU C C 178.655 0.2 1 493 . 46 LEU CB C 43.071 0.2 1 494 . 46 LEU HB2 H 1.474 0.02 2 495 . 46 LEU HB3 H 1.876 0.02 2 496 . 46 LEU CG C 27.108 0.2 1 497 . 46 LEU CD1 C 25.300 0.2 2 498 . 46 LEU HD1 H 0.769 0.02 2 499 . 46 LEU HG H 1.732 0.02 1 500 . 47 LYS H H 8.628 0.02 1 501 . 47 LYS N N 117.400 0.1 1 502 . 47 LYS CA C 61.421 0.2 1 503 . 47 LYS HA H 3.780 0.02 1 504 . 47 LYS C C 176.208 0.2 1 505 . 47 LYS CB C 32.110 0.2 1 506 . 47 LYS HB2 H 1.727 0.02 2 507 . 47 LYS HB3 H 1.787 0.02 2 508 . 47 LYS CG C 29.663 0.2 1 509 . 47 LYS HG2 H 1.524 0.02 2 510 . 47 LYS HG3 H 1.635 0.02 2 511 . 47 LYS CD C 27.162 0.2 1 512 . 47 LYS HD2 H 1.241 0.02 2 513 . 47 LYS HD3 H 1.536 0.02 2 514 . 47 LYS HE2 H 2.946 0.02 2 515 . 48 LYS H H 8.332 0.02 1 516 . 48 LYS N N 121.400 0.1 1 517 . 48 LYS CA C 59.340 0.2 1 518 . 48 LYS HA H 4.080 0.02 1 519 . 48 LYS C C 179.216 0.2 1 520 . 48 LYS CB C 31.832 0.2 1 521 . 48 LYS HB2 H 1.883 0.02 2 522 . 48 LYS CG C 24.661 0.2 1 523 . 48 LYS HG2 H 1.523 0.02 2 524 . 48 LYS HE2 H 3.017 0.02 2 525 . 49 ASN H H 8.796 0.02 1 526 . 49 ASN N N 117.400 0.1 1 527 . 49 ASN CA C 55.626 0.2 1 528 . 49 ASN HA H 4.371 0.02 1 529 . 49 ASN C C 180.639 0.2 1 530 . 49 ASN CB C 37.401 0.2 1 531 . 49 ASN HB2 H 2.783 0.02 2 532 . 49 ASN HB3 H 3.482 0.02 2 533 . 49 ASN ND2 N 111.763 0.1 1 534 . 49 ASN HD21 H 6.575 0.02 2 535 . 49 ASN HD22 H 9.316 0.02 2 536 . 50 VAL H H 8.774 0.02 1 537 . 50 VAL N N 121.610 0.1 1 538 . 50 VAL CA C 67.589 0.2 1 539 . 50 VAL HA H 3.815 0.02 1 540 . 50 VAL C C 176.666 0.2 1 541 . 50 VAL CB C 31.429 0.2 1 542 . 50 VAL HB H 2.331 0.02 1 543 . 50 VAL CG1 C 22.786 0.2 2 544 . 50 VAL HG1 H 0.982 0.02 2 545 . 50 VAL CG2 C 23.098 0.2 2 546 . 50 VAL HG2 H 1.307 0.02 2 547 . 51 GLY H H 8.057 0.02 1 548 . 51 GLY N N 103.600 0.1 1 549 . 51 GLY CA C 46.825 0.2 1 550 . 51 GLY HA2 H 3.790 0.02 2 551 . 51 GLY HA3 H 4.150 0.02 2 552 . 51 GLY C C 173.947 0.2 1 553 . 52 GLN H H 7.342 0.02 1 554 . 52 GLN N N 114.640 0.1 1 555 . 52 GLN CA C 55.398 0.2 1 556 . 52 GLN HA H 4.161 0.02 1 557 . 52 GLN C C 174.560 0.2 1 558 . 52 GLN CB C 30.412 0.2 1 559 . 52 GLN HB2 H 2.166 0.02 2 560 . 52 GLN HB3 H 2.410 0.02 2 561 . 52 GLN CG C 34.039 0.2 1 562 . 52 GLN HG2 H 2.407 0.02 2 563 . 52 GLN HG3 H 2.666 0.02 2 564 . 52 GLN NE2 N 116.606 0.1 1 565 . 52 GLN HE21 H 7.263 0.02 2 566 . 52 GLN HE22 H 7.822 0.02 2 567 . 53 PHE H H 7.630 0.02 1 568 . 53 PHE N N 121.100 0.1 1 569 . 53 PHE CA C 60.488 0.2 1 570 . 53 PHE HA H 4.254 0.02 1 571 . 53 PHE C C 177.107 0.2 1 572 . 53 PHE CB C 39.504 0.2 1 573 . 53 PHE HB2 H 3.098 0.02 2 574 . 53 PHE HB3 H 3.671 0.02 2 575 . 53 PHE CD1 C 129.391 0.2 3 576 . 53 PHE HD1 H 7.361 0.02 3 577 . 53 PHE CE1 C 126.054 0.2 3 578 . 53 PHE HE1 H 6.749 0.02 3 579 . 54 SER H H 8.560 0.02 1 580 . 54 SER N N 119.000 0.1 1 581 . 54 SER CA C 56.594 0.2 1 582 . 54 SER HA H 4.290 0.02 1 583 . 54 SER CB C 63.643 0.2 1 584 . 54 SER HB2 H 4.170 0.02 2 585 . 55 GLY CA C 42.890 0.2 1 586 . 55 GLY HA2 H 3.579 0.02 2 587 . 55 GLY HA3 H 4.371 0.02 2 588 . 55 GLY C C 174.384 0.2 1 589 . 56 PHE H H 7.470 0.02 1 590 . 56 PHE N N 120.830 0.1 1 591 . 56 PHE CA C 55.816 0.2 1 592 . 56 PHE HA H 4.284 0.02 1 593 . 56 PHE C C 174.318 0.2 1 594 . 56 PHE CB C 37.152 0.2 1 595 . 56 PHE HB2 H 2.240 0.02 2 596 . 56 PHE HB3 H 2.458 0.02 2 597 . 56 PHE HD1 H 6.750 0.02 3 598 . 56 PHE HE1 H 6.928 0.02 3 599 . 57 PRO CA C 62.485 0.2 1 600 . 57 PRO HA H 4.709 0.02 1 601 . 57 PRO C C 174.653 0.2 1 602 . 57 PRO CB C 32.481 0.2 1 603 . 57 PRO HB2 H 2.096 0.02 2 604 . 57 PRO HB3 H 2.666 0.02 2 605 . 57 PRO CG C 27.800 0.2 1 606 . 57 PRO HG2 H 2.154 0.02 2 607 . 57 PRO HG3 H 2.267 0.02 2 608 . 57 PRO CD C 50.900 0.2 1 609 . 57 PRO HD2 H 3.780 0.02 2 610 . 58 PHE H H 6.724 0.02 1 611 . 58 PHE N N 115.779 0.1 1 612 . 58 PHE CA C 54.352 0.2 1 613 . 58 PHE HA H 4.961 0.02 1 614 . 58 PHE C C 174.318 0.2 1 615 . 58 PHE CB C 39.479 0.2 1 616 . 58 PHE HB2 H 3.227 0.02 2 617 . 58 PHE HB3 H 3.464 0.02 2 618 . 58 PHE CD1 C 128.396 0.2 3 619 . 58 PHE HD1 H 7.040 0.02 3 620 . 58 PHE CE1 C 126.054 0.2 3 621 . 58 PHE HE1 H 6.959 0.02 3 622 . 59 GLU H H 8.836 0.02 1 623 . 59 GLU N N 115.798 0.1 1 624 . 59 GLU CA C 55.258 0.2 1 625 . 59 GLU HA H 4.605 0.02 1 626 . 59 GLU C C 178.639 0.2 1 627 . 59 GLU CB C 31.483 0.2 1 628 . 59 GLU HB2 H 1.941 0.02 2 629 . 59 GLU HB3 H 2.207 0.02 2 630 . 59 GLU CG C 35.915 0.2 1 631 . 59 GLU HG2 H 2.369 0.02 2 632 . 59 GLU HG3 H 2.463 0.02 2 633 . 60 LYS H H 9.281 0.02 1 634 . 60 LYS N N 124.600 0.1 1 635 . 60 LYS CA C 58.458 0.2 1 636 . 60 LYS HA H 3.197 0.02 1 637 . 60 LYS C C 176.934 0.2 1 638 . 60 LYS CB C 30.893 0.2 1 639 . 60 LYS HB2 H 1.573 0.02 2 640 . 60 LYS HB3 H 1.615 0.02 2 641 . 60 LYS CG C 24.974 0.2 1 642 . 60 LYS HG2 H 0.939 0.02 2 643 . 60 LYS HG3 H 1.007 0.02 2 644 . 60 LYS CD C 29.350 0.2 1 645 . 60 LYS HD2 H 1.620 0.02 2 646 . 60 LYS HE2 H 2.942 0.02 2 647 . 60 LYS HE3 H 2.975 0.02 2 648 . 61 GLY H H 6.064 0.02 1 649 . 61 GLY N N 110.800 0.1 1 650 . 61 GLY CA C 45.156 0.2 1 651 . 61 GLY HA2 H 3.725 0.02 2 652 . 61 GLY HA3 H 4.126 0.02 2 653 . 61 GLY C C 173.047 0.2 1 654 . 62 SER H H 7.434 0.02 1 655 . 62 SER N N 114.264 0.2 1 656 . 62 SER CA C 57.991 0.2 1 657 . 62 SER HA H 4.448 0.02 1 658 . 62 SER C C 174.706 0.2 1 659 . 62 SER CB C 66.234 0.2 1 660 . 62 SER HB2 H 4.099 0.02 2 661 . 63 VAL H H 8.851 0.02 1 662 . 63 VAL N N 120.900 0.1 1 663 . 63 VAL CA C 66.616 0.2 1 664 . 63 VAL HA H 3.673 0.02 1 665 . 63 VAL C C 178.518 0.2 1 666 . 63 VAL CB C 31.514 0.2 1 667 . 63 VAL HB H 2.053 0.02 1 668 . 63 VAL CG1 C 20.597 0.2 2 669 . 63 VAL HG1 H 0.940 0.02 2 670 . 63 VAL CG2 C 21.848 0.2 2 671 . 63 VAL HG2 H 1.088 0.02 2 672 . 64 GLN H H 8.219 0.02 1 673 . 64 GLN N N 117.150 0.1 1 674 . 64 GLN CA C 59.584 0.2 1 675 . 64 GLN HA H 3.534 0.02 1 676 . 64 GLN C C 177.790 0.2 1 677 . 64 GLN CB C 27.329 0.2 1 678 . 64 GLN HB2 H 0.704 0.02 2 679 . 64 GLN HB3 H 0.763 0.02 2 680 . 64 GLN CG C 34.664 0.2 1 681 . 64 GLN HG2 H 2.207 0.02 2 682 . 64 GLN NE2 N 112.870 0.1 1 683 . 64 GLN HE21 H 7.018 0.02 2 684 . 64 GLN HE22 H 7.570 0.02 2 685 . 65 TYR H H 7.087 0.02 1 686 . 65 TYR N N 120.300 0.1 1 687 . 65 TYR CA C 62.019 0.2 1 688 . 65 TYR HA H 3.536 0.02 1 689 . 65 TYR C C 176.634 0.2 1 690 . 65 TYR CB C 38.479 0.2 1 691 . 65 TYR HB2 H 3.050 0.02 2 692 . 65 TYR HB3 H 3.414 0.02 2 693 . 65 TYR CD1 C 129.099 0.2 3 694 . 65 TYR HD1 H 7.221 0.02 3 695 . 65 TYR CE1 C 114.814 0.2 3 696 . 65 TYR HE1 H 6.915 0.02 3 697 . 66 LYS H H 8.254 0.02 1 698 . 66 LYS N N 119.000 0.1 1 699 . 66 LYS CA C 59.198 0.2 1 700 . 66 LYS HA H 4.065 0.02 1 701 . 66 LYS C C 179.473 0.2 1 702 . 66 LYS CB C 31.822 0.2 1 703 . 66 LYS HB2 H 1.939 0.02 2 704 . 66 LYS CG C 29.037 0.2 1 705 . 66 LYS HG2 H 1.723 0.02 2 706 . 66 LYS CD C 24.661 0.2 1 707 . 66 LYS HD2 H 1.447 0.02 2 708 . 66 LYS HD3 H 1.524 0.02 2 709 . 66 LYS HE2 H 2.988 0.02 2 710 . 67 LYS H H 7.827 0.02 1 711 . 67 LYS N N 118.200 0.1 1 712 . 67 LYS CA C 58.854 0.2 1 713 . 67 LYS HA H 4.010 0.02 1 714 . 67 LYS C C 179.969 0.2 1 715 . 67 LYS CB C 31.748 0.2 1 716 . 67 LYS HB2 H 1.744 0.02 2 717 . 67 LYS HB3 H 1.816 0.02 2 718 . 67 LYS CG C 24.974 0.2 1 719 . 67 LYS HG2 H 1.419 0.02 2 720 . 67 LYS HG3 H 1.529 0.02 2 721 . 67 LYS CD C 28.412 0.2 1 722 . 67 LYS HD2 H 1.581 0.02 2 723 . 67 LYS HE2 H 2.837 0.02 2 724 . 67 LYS HE3 H 2.871 0.02 2 725 . 68 LYS H H 7.465 0.02 1 726 . 68 LYS N N 119.000 0.1 1 727 . 68 LYS CA C 57.117 0.2 1 728 . 68 LYS HA H 4.161 0.02 1 729 . 68 LYS C C 178.073 0.2 1 730 . 68 LYS CB C 30.472 0.2 1 731 . 68 LYS HB2 H 1.681 0.02 2 732 . 68 LYS HB3 H 1.848 0.02 2 733 . 68 LYS CG C 26.849 0.2 1 734 . 68 LYS HG2 H 1.607 0.02 2 735 . 68 LYS CE C 43.104 0.2 1 736 . 68 LYS HE2 H 3.203 0.02 2 737 . 69 GLU H H 8.020 0.02 1 738 . 69 GLU N N 119.500 0.1 1 739 . 69 GLU CA C 60.505 0.2 1 740 . 69 GLU HA H 3.503 0.02 1 741 . 69 GLU C C 175.902 0.2 1 742 . 69 GLU CB C 29.807 0.2 1 743 . 69 GLU HB2 H 1.764 0.02 2 744 . 69 GLU HB3 H 2.117 0.02 2 745 . 69 GLU CG C 36.852 0.2 1 746 . 69 GLU HG2 H 1.915 0.02 2 747 . 69 GLU HG3 H 1.949 0.02 2 748 . 70 GLU H H 8.106 0.02 1 749 . 70 GLU N N 116.654 0.1 1 750 . 70 GLU CA C 59.019 0.2 1 751 . 70 GLU HA H 3.997 0.02 1 752 . 70 GLU C C 178.627 0.2 1 753 . 70 GLU CB C 29.559 0.2 1 754 . 70 GLU HB2 H 1.650 0.02 2 755 . 71 MET H H 7.543 0.02 1 756 . 71 MET N N 118.000 0.1 1 757 . 71 MET CA C 58.994 0.2 1 758 . 71 MET HA H 3.851 0.02 1 759 . 71 MET C C 178.559 0.2 1 760 . 71 MET CB C 32.993 0.2 1 761 . 71 MET HB2 H 1.998 0.02 2 762 . 71 MET HB3 H 2.169 0.02 2 763 . 71 MET CG C 31.538 0.2 1 764 . 71 MET HG2 H 2.594 0.02 2 765 . 72 LEU H H 7.769 0.02 1 766 . 72 LEU N N 118.200 0.1 1 767 . 72 LEU CA C 57.230 0.2 1 768 . 72 LEU HA H 3.380 0.02 1 769 . 72 LEU C C 178.796 0.2 1 770 . 72 LEU CB C 43.292 0.2 1 771 . 72 LEU HB2 H 1.371 0.02 2 772 . 72 LEU HB3 H 1.831 0.02 2 773 . 72 LEU CG C 27.162 0.2 1 774 . 72 LEU CD1 C 24.349 0.2 2 775 . 72 LEU HD1 H 0.688 0.02 2 776 . 72 LEU CD2 C 26.224 0.2 2 777 . 72 LEU HD2 H 0.783 0.02 2 778 . 72 LEU HG H 1.562 0.02 1 779 . 73 LYS H H 7.960 0.02 1 780 . 73 LYS N N 116.192 0.1 1 781 . 73 LYS CA C 58.957 0.2 1 782 . 73 LYS HA H 3.983 0.02 1 783 . 73 LYS C C 177.373 0.2 1 784 . 73 LYS CB C 32.447 0.2 1 785 . 73 LYS HB2 H 1.828 0.02 2 786 . 73 LYS HB3 H 1.932 0.02 2 787 . 73 LYS CG C 26.537 0.2 1 788 . 73 LYS HG2 H 1.473 0.02 2 789 . 73 LYS HG3 H 1.728 0.02 2 790 . 73 LYS HE2 H 2.858 0.02 2 791 . 73 LYS HE3 H 2.922 0.02 2 792 . 74 LYS H H 7.124 0.02 1 793 . 74 LYS N N 116.136 0.1 1 794 . 74 LYS CA C 56.363 0.2 1 795 . 74 LYS HA H 4.350 0.02 1 796 . 74 LYS C C 177.670 0.2 1 797 . 74 LYS CB C 32.722 0.2 1 798 . 74 LYS HB2 H 1.790 0.02 2 799 . 74 LYS HB3 H 1.851 0.02 2 800 . 74 LYS CG C 24.349 0.2 1 801 . 74 LYS HG2 H 1.428 0.02 2 802 . 74 LYS HG3 H 1.474 0.02 2 803 . 74 LYS CD C 29.000 0.2 1 804 . 74 LYS HD2 H 1.687 0.02 2 805 . 74 LYS CE C 41.541 0.2 1 806 . 74 LYS HE2 H 3.002 0.02 2 807 . 75 PHE H H 7.577 0.02 1 808 . 75 PHE N N 120.300 0.1 1 809 . 75 PHE CA C 55.660 0.2 1 810 . 75 PHE HA H 4.824 0.02 1 811 . 75 PHE C C 175.955 0.2 1 812 . 75 PHE CB C 38.049 0.2 1 813 . 75 PHE HB2 H 3.052 0.02 2 814 . 75 PHE HB3 H 3.516 0.02 2 815 . 75 PHE HD1 H 7.142 0.02 3 816 . 75 PHE HE1 H 7.142 0.02 3 817 . 76 ARG H H 8.298 0.02 1 818 . 76 ARG N N 118.643 0.1 1 819 . 76 ARG CA C 55.381 0.2 1 820 . 76 ARG HA H 4.517 0.02 1 821 . 76 ARG CB C 31.114 0.2 1 822 . 76 ARG HB2 H 1.882 0.02 2 823 . 76 ARG HB3 H 2.275 0.02 2 824 . 76 ARG CG C 27.787 0.2 1 825 . 76 ARG HG2 H 1.911 0.02 2 826 . 76 ARG CD C 42.792 0.2 1 827 . 76 ARG HD2 H 3.336 0.02 2 828 . 77 ASN H H 9.312 0.02 1 829 . 77 ASN N N 121.661 0.1 1 830 . 77 ASN CA C 59.213 0.2 1 831 . 77 ASN HA H 4.266 0.02 1 832 . 77 ASN C C 177.097 0.2 1 833 . 77 ASN CB C 40.089 0.2 1 834 . 77 ASN HB2 H 2.625 0.02 2 835 . 77 ASN HB3 H 3.421 0.02 2 836 . 77 ASN ND2 N 110.200 0.1 1 837 . 77 ASN HD21 H 7.062 0.02 2 838 . 77 ASN HD22 H 7.970 0.02 2 839 . 78 ALA H H 9.059 0.02 1 840 . 78 ALA N N 118.200 0.1 1 841 . 78 ALA CA C 55.490 0.2 1 842 . 78 ALA HA H 3.990 0.02 1 843 . 78 ALA C C 180.512 0.2 1 844 . 78 ALA CB C 18.423 0.2 1 845 . 78 ALA HB H 1.470 0.02 1 846 . 79 MET H H 7.162 0.02 1 847 . 79 MET N N 116.896 0.1 1 848 . 79 MET CA C 57.446 0.2 1 849 . 79 MET HA H 4.341 0.02 1 850 . 79 MET C C 178.909 0.2 1 851 . 79 MET CB C 32.536 0.2 1 852 . 79 MET HB2 H 2.061 0.02 2 853 . 79 MET HB3 H 2.219 0.02 2 854 . 79 MET CG C 31.538 0.2 1 855 . 79 MET HG2 H 2.273 0.02 2 856 . 80 LEU H H 7.949 0.02 1 857 . 80 LEU N N 119.500 0.1 1 858 . 80 LEU CA C 58.194 0.2 1 859 . 80 LEU HA H 3.980 0.02 1 860 . 80 LEU C C 179.522 0.2 1 861 . 80 LEU CB C 42.776 0.2 1 862 . 80 LEU HB2 H 1.283 0.02 2 863 . 80 LEU HB3 H 2.152 0.02 2 864 . 80 LEU CG C 26.849 0.2 1 865 . 80 LEU CD1 C 24.036 0.2 2 866 . 80 LEU HD1 H 0.899 0.02 2 867 . 80 LEU CD2 C 25.912 0.2 2 868 . 80 LEU HD2 H 0.961 0.02 2 869 . 80 LEU HG H 1.767 0.02 1 870 . 81 LYS H H 8.738 0.02 1 871 . 81 LYS N N 118.700 0.1 1 872 . 81 LYS CA C 61.549 0.2 1 873 . 81 LYS HA H 3.779 0.02 1 874 . 81 LYS CB C 32.653 0.2 1 875 . 81 LYS HB2 H 1.801 0.02 2 876 . 81 LYS CG C 29.350 0.2 1 877 . 81 LYS HG2 H 1.737 0.02 2 878 . 81 LYS CD C 26.537 0.2 1 879 . 81 LYS HD2 H 1.527 0.02 2 880 . 81 LYS HD3 H 1.726 0.02 2 881 . 81 LYS HE2 H 3.029 0.02 2 882 . 82 SER H H 7.648 0.02 1 883 . 82 SER N N 114.555 0.1 1 884 . 82 SER CA C 61.682 0.2 1 885 . 82 SER HA H 4.043 0.02 1 886 . 82 SER C C 177.063 0.2 1 887 . 82 SER CB C 62.774 0.2 1 888 . 82 SER HB2 H 3.962 0.02 2 889 . 83 ILE H H 7.701 0.02 1 890 . 83 ILE N N 121.900 0.1 1 891 . 83 ILE CA C 65.004 0.2 1 892 . 83 ILE HA H 3.679 0.02 1 893 . 83 ILE C C 177.769 0.2 1 894 . 83 ILE CB C 37.286 0.2 1 895 . 83 ILE HB H 2.065 0.02 1 896 . 83 ILE CG2 C 18.722 0.2 1 897 . 83 ILE HG2 H 0.801 0.02 1 898 . 83 ILE CG1 C 29.350 0.2 1 899 . 83 ILE HG12 H 1.866 0.02 2 900 . 83 ILE HG13 H 0.994 0.02 2 901 . 83 ILE CD1 C 12.782 0.2 1 902 . 83 ILE HD1 H 0.722 0.02 1 903 . 84 CYS H H 8.108 0.02 1 904 . 84 CYS N N 116.920 0.1 1 905 . 84 CYS CA C 65.502 0.2 1 906 . 84 CYS HA H 3.730 0.02 1 907 . 84 CYS CB C 29.430 0.2 1 908 . 84 CYS HB2 H 2.584 0.02 2 909 . 84 CYS HB3 H 3.131 0.02 2 910 . 85 GLU CA C 59.277 0.2 1 911 . 85 GLU C C 179.108 0.2 1 912 . 86 VAL H H 7.185 0.02 1 913 . 86 VAL N N 116.350 0.1 1 914 . 86 VAL CA C 64.380 0.2 1 915 . 86 VAL HA H 3.760 0.02 1 916 . 86 VAL C C 173.025 0.2 1 917 . 86 VAL CB C 31.618 0.2 1 918 . 86 VAL HB H 2.069 0.02 1 919 . 86 VAL CG1 C 21.535 0.2 2 920 . 86 VAL HG1 H 0.987 0.02 2 921 . 86 VAL CG2 C 22.786 0.2 2 922 . 86 VAL HG2 H 1.025 0.02 2 923 . 87 LEU H H 7.004 0.02 1 924 . 87 LEU N N 113.100 0.1 1 925 . 87 LEU CA C 53.510 0.2 1 926 . 87 LEU HA H 4.214 0.02 1 927 . 87 LEU C C 173.846 0.2 1 928 . 87 LEU CB C 40.342 0.2 1 929 . 87 LEU HB2 H 1.193 0.02 2 930 . 87 LEU HB3 H 1.281 0.02 2 931 . 87 LEU CG C 25.912 0.2 1 932 . 87 LEU CD1 C 26.849 0.2 2 933 . 87 LEU HD1 H 0.793 0.02 2 934 . 87 LEU CD2 C 21.535 0.2 2 935 . 87 LEU HD2 H 0.860 0.02 2 936 . 87 LEU HG H 1.959 0.02 1 937 . 88 ASP H H 7.702 0.02 1 938 . 88 ASP N N 116.400 0.1 1 939 . 88 ASP CA C 54.250 0.2 1 940 . 88 ASP HA H 4.298 0.02 1 941 . 88 ASP C C 175.065 0.2 1 942 . 88 ASP CB C 40.567 0.2 1 943 . 88 ASP HB2 H 2.070 0.02 2 944 . 88 ASP HB3 H 3.473 0.02 2 945 . 89 LEU H H 8.427 0.02 1 946 . 89 LEU N N 117.200 0.1 1 947 . 89 LEU CA C 52.152 0.2 1 948 . 89 LEU HA H 4.562 0.02 1 949 . 89 LEU C C 177.341 0.2 1 950 . 89 LEU CB C 44.450 0.2 1 951 . 89 LEU HB2 H 1.195 0.02 2 952 . 89 LEU HB3 H 1.404 0.02 2 953 . 89 LEU CG C 25.286 0.2 1 954 . 89 LEU CD1 C 22.160 0.2 2 955 . 89 LEU HD1 H 0.573 0.02 2 956 . 89 LEU CD2 C 26.537 0.2 2 957 . 89 LEU HD2 H 0.663 0.02 2 958 . 89 LEU HG H 1.212 0.02 1 959 . 90 GLU CA C 63.015 0.2 1 960 . 90 GLU HA H 3.367 0.02 1 961 . 90 GLU C C 177.341 0.2 1 962 . 91 ARG H H 8.376 0.02 1 963 . 91 ARG N N 121.138 0.1 1 964 . 91 ARG CA C 56.401 0.2 1 965 . 91 ARG HA H 4.325 0.02 1 966 . 91 ARG C C 175.341 0.2 1 967 . 91 ARG CB C 31.712 0.2 1 968 . 91 ARG HB2 H 1.819 0.02 2 969 . 91 ARG CG C 27.474 0.2 1 970 . 91 ARG HG2 H 1.676 0.02 2 971 . 91 ARG HD2 H 3.103 0.02 2 972 . 91 ARG HD3 H 3.225 0.02 2 973 . 92 SER H H 7.719 0.02 1 974 . 92 SER N N 113.922 0.1 1 975 . 92 SER CA C 58.274 0.2 1 976 . 92 SER HA H 4.433 0.02 1 977 . 92 SER C C 173.962 0.2 1 978 . 92 SER CB C 64.348 0.2 1 979 . 92 SER HB2 H 3.889 0.02 2 980 . 93 GLY H H 8.417 0.02 1 981 . 93 GLY N N 110.000 0.1 1 982 . 93 GLY CA C 43.776 0.2 1 983 . 93 GLY HA2 H 3.869 0.02 2 984 . 93 GLY HA3 H 4.565 0.02 2 985 . 93 GLY C C 174.535 0.2 1 986 . 94 VAL H H 8.056 0.02 1 987 . 94 VAL N N 111.800 0.1 1 988 . 94 VAL CA C 60.743 0.2 1 989 . 94 VAL HA H 4.475 0.02 1 990 . 94 VAL C C 177.791 0.2 1 991 . 94 VAL CB C 32.616 0.2 1 992 . 94 VAL HB H 2.539 0.02 1 993 . 94 VAL CG1 C 21.848 0.2 2 994 . 94 VAL HG1 H 1.077 0.02 2 995 . 95 ASN H H 8.877 0.02 1 996 . 95 ASN N N 120.600 0.1 1 997 . 95 ASN CA C 57.715 0.2 1 998 . 95 ASN HA H 4.212 0.02 1 999 . 95 ASN C C 177.310 0.2 1 1000 . 95 ASN CB C 37.325 0.2 1 1001 . 95 ASN HB2 H 2.805 0.02 2 1002 . 95 ASN HB3 H 2.946 0.02 2 1003 . 95 ASN ND2 N 109.723 0.1 1 1004 . 95 ASN HD21 H 6.712 0.02 2 1005 . 95 ASN HD22 H 7.579 0.02 2 1006 . 96 SER H H 8.806 0.02 1 1007 . 96 SER N N 112.600 0.1 1 1008 . 96 SER CA C 61.534 0.2 1 1009 . 96 SER HA H 4.002 0.02 1 1010 . 96 SER C C 177.350 0.2 1 1011 . 96 SER CB C 61.780 0.2 1 1012 . 96 SER HB2 H 3.912 0.02 2 1013 . 97 GLU H H 7.290 0.02 1 1014 . 97 GLU N N 121.400 0.1 1 1015 . 97 GLU CA C 58.534 0.2 1 1016 . 97 GLU HA H 4.152 0.02 1 1017 . 97 GLU C C 179.037 0.2 1 1018 . 97 GLU CB C 29.693 0.2 1 1019 . 97 GLU HB2 H 2.100 0.02 2 1020 . 97 GLU HB3 H 2.318 0.02 2 1021 . 97 GLU CG C 36.227 0.2 1 1022 . 97 GLU HG2 H 2.288 0.02 2 1023 . 98 LEU H H 7.660 0.02 1 1024 . 98 LEU N N 121.100 0.1 1 1025 . 98 LEU CA C 58.995 0.2 1 1026 . 98 LEU HA H 3.872 0.02 1 1027 . 98 LEU C C 178.503 0.2 1 1028 . 98 LEU CB C 42.016 0.2 1 1029 . 98 LEU HB2 H 1.213 0.02 2 1030 . 98 LEU HB3 H 2.036 0.02 2 1031 . 98 LEU CG C 28.100 0.2 1 1032 . 98 LEU CD1 C 23.723 0.2 2 1033 . 98 LEU HD1 H 0.693 0.02 2 1034 . 98 LEU CD2 C 26.224 0.2 2 1035 . 98 LEU HD2 H 0.746 0.02 2 1036 . 98 LEU HG H 1.604 0.02 1 1037 . 99 VAL H H 8.443 0.02 1 1038 . 99 VAL N N 117.700 0.1 1 1039 . 99 VAL CA C 67.782 0.2 1 1040 . 99 VAL HA H 3.304 0.02 1 1041 . 99 VAL C C 176.864 0.2 1 1042 . 99 VAL CB C 32.318 0.2 1 1043 . 99 VAL HB H 2.110 0.02 1 1044 . 99 VAL CG1 C 21.223 0.2 2 1045 . 99 VAL HG1 H 0.960 0.02 2 1046 . 100 LYS H H 7.110 0.02 1 1047 . 100 LYS N N 116.361 0.1 1 1048 . 100 LYS CA C 59.532 0.2 1 1049 . 100 LYS HA H 3.972 0.02 1 1050 . 100 LYS C C 178.174 0.2 1 1051 . 100 LYS CB C 32.707 0.2 1 1052 . 100 LYS HB2 H 1.926 0.02 2 1053 . 100 LYS CG C 24.974 0.2 1 1054 . 100 LYS HG2 H 1.530 0.02 2 1055 . 100 LYS HG3 H 1.669 0.02 2 1056 . 100 LYS CD C 29.350 0.2 1 1057 . 100 LYS HD2 H 1.761 0.02 2 1058 . 100 LYS HE2 H 3.014 0.02 2 1059 . 101 ARG H H 7.977 0.02 1 1060 . 101 ARG N N 119.000 0.1 1 1061 . 101 ARG CA C 59.609 0.2 1 1062 . 101 ARG HA H 4.109 0.02 1 1063 . 101 ARG C C 179.881 0.2 1 1064 . 101 ARG CB C 31.475 0.2 1 1065 . 101 ARG HB2 H 1.826 0.02 2 1066 . 101 ARG HB3 H 2.008 0.02 2 1067 . 101 ARG CG C 27.474 0.2 1 1068 . 101 ARG HG2 H 1.784 0.02 2 1069 . 101 ARG HG3 H 1.914 0.02 2 1070 . 101 ARG HD2 H 3.575 0.02 2 1071 . 102 ILE H H 8.492 0.02 1 1072 . 102 ILE N N 119.800 0.1 1 1073 . 102 ILE CA C 65.885 0.2 1 1074 . 102 ILE HA H 3.484 0.02 1 1075 . 102 ILE C C 177.555 0.2 1 1076 . 102 ILE CB C 38.736 0.2 1 1077 . 102 ILE HB H 1.823 0.02 1 1078 . 102 ILE CG2 C 18.409 0.2 1 1079 . 102 ILE HG2 H 0.778 0.02 1 1080 . 102 ILE CG1 C 30.606 0.2 1 1081 . 102 ILE HG12 H 1.896 0.02 2 1082 . 102 ILE CD1 C 15.283 0.2 1 1083 . 102 ILE HD1 H 0.862 0.02 1 1084 . 103 LEU H H 8.413 0.02 1 1085 . 103 LEU N N 119.000 0.1 1 1086 . 103 LEU CA C 58.927 0.2 1 1087 . 103 LEU HA H 4.007 0.02 1 1088 . 103 LEU C C 178.270 0.2 1 1089 . 103 LEU CB C 41.385 0.2 1 1090 . 103 LEU HB2 H 1.744 0.02 2 1091 . 103 LEU CG C 26.537 0.2 1 1092 . 103 LEU CD1 C 23.411 0.2 2 1093 . 103 LEU HD1 H 0.495 0.02 2 1094 . 103 LEU CD2 C 24.349 0.2 2 1095 . 103 LEU HD2 H 0.649 0.02 2 1096 . 103 LEU HG H 1.673 0.02 1 1097 . 104 ASN H H 8.534 0.02 1 1098 . 104 ASN N N 114.635 0.1 1 1099 . 104 ASN CA C 56.378 0.2 1 1100 . 104 ASN HA H 4.511 0.02 1 1101 . 104 ASN C C 178.732 0.2 1 1102 . 104 ASN CB C 38.207 0.2 1 1103 . 104 ASN HB2 H 2.882 0.02 2 1104 . 104 ASN HB3 H 3.036 0.02 2 1105 . 104 ASN ND2 N 112.612 0.1 1 1106 . 104 ASN HD21 H 6.992 0.02 2 1107 . 104 ASN HD22 H 7.783 0.02 2 1108 . 105 PHE H H 7.797 0.02 1 1109 . 105 PHE N N 119.800 0.1 1 1110 . 105 PHE CA C 62.228 0.2 1 1111 . 105 PHE HA H 4.280 0.02 1 1112 . 105 PHE C C 177.222 0.2 1 1113 . 105 PHE CB C 40.236 0.2 1 1114 . 105 PHE HB2 H 3.239 0.02 2 1115 . 105 PHE HB3 H 3.396 0.02 2 1116 . 105 PHE CD1 C 128.396 0.2 3 1117 . 105 PHE HD1 H 7.323 0.02 3 1118 . 105 PHE CE1 C 126.523 0.2 3 1119 . 105 PHE HE1 H 7.617 0.02 3 1120 . 106 LEU H H 8.626 0.02 1 1121 . 106 LEU N N 116.600 0.1 1 1122 . 106 LEU CA C 56.821 0.2 1 1123 . 106 LEU HA H 3.870 0.02 1 1124 . 106 LEU C C 178.023 0.2 1 1125 . 106 LEU CB C 41.658 0.2 1 1126 . 106 LEU HB2 H 1.056 0.02 2 1127 . 106 LEU HB3 H 1.894 0.02 2 1128 . 106 LEU CG C 26.537 0.2 1 1129 . 106 LEU CD1 C 27.162 0.2 2 1130 . 106 LEU HD1 H 0.677 0.02 2 1131 . 106 LEU CD2 C 21.848 0.2 2 1132 . 106 LEU HD2 H 0.780 0.02 2 1133 . 106 LEU HG H 2.227 0.02 1 1134 . 107 MET H H 7.788 0.02 1 1135 . 107 MET N N 115.101 0.1 1 1136 . 107 MET CA C 55.889 0.2 1 1137 . 107 MET C C 178.804 0.2 1 1138 . 107 MET CB C 30.576 0.2 1 1139 . 107 MET HB2 H 2.320 0.02 2 1140 . 107 MET HB3 H 2.537 0.02 2 1141 . 107 MET CG C 32.163 0.2 1 1142 . 107 MET HG2 H 2.988 0.02 2 1143 . 107 MET HG3 H 3.410 0.02 2 1144 . 108 HIS H H 7.661 0.02 1 1145 . 108 HIS N N 115.800 0.1 1 1146 . 108 HIS CA C 54.848 0.2 1 1147 . 108 HIS HA H 4.128 0.02 1 1148 . 108 HIS CB C 29.880 0.2 1 1149 . 108 HIS HB2 H 2.923 0.02 2 1150 . 108 HIS HB3 H 3.150 0.02 2 1151 . 108 HIS HD2 H 6.558 0.02 1 1152 . 108 HIS HE1 H 7.882 0.02 1 1153 . 109 PRO CA C 64.430 0.2 1 1154 . 109 PRO HA H 2.890 0.02 1 1155 . 109 PRO C C 175.546 0.2 1 1156 . 109 PRO CB C 31.483 0.2 1 1157 . 109 PRO HB2 H 1.588 0.02 2 1158 . 109 PRO HB3 H 2.203 0.02 2 1159 . 109 PRO CG C 27.474 0.2 1 1160 . 109 PRO HG2 H 1.438 0.02 2 1161 . 109 PRO HG3 H 1.723 0.02 2 1162 . 109 PRO CD C 49.356 0.2 1 1163 . 109 PRO HD2 H 2.931 0.02 2 1164 . 109 PRO HD3 H 3.310 0.02 2 stop_ save_