data_5294 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of the beta subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: A representative of the eIF2beta/eIF5 family of proteins ; _BMRB_accession_number 5294 _BMRB_flat_file_name bmr5294.str _Entry_type original _Submission_date 2002-02-18 _Accession_date 2002-02-18 _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 Cho Seongeun . . 2 Hoffman David W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 397 "13C chemical shifts" 181 "15N chemical shifts" 103 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-09-11 original author . stop_ _Original_release_date 2002-09-11 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structure of the Beta Subunit of Translation Initiation Factor 2 from the Archaeon Methanococcus jannaschii: A Representative of the eIF2beta/eIF5 Family of Proteins ; _Citation_status submitted _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21976992 _PubMed_ID 11980477 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cho Seongeun . . 2 Hoffman David W. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue 18 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 5730 _Page_last 5742 _Year 2002 _Details . loop_ _Keyword 'translation initiation factor' 'protein structure' aIf2b stop_ save_ ################################## # Molecular system description # ################################## save_system_aIF2b _Saveframe_category molecular_system _Mol_system_name 'beta subunit of translation initiation factor 2' _Abbreviation_common aIF2b _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label aIF2b $aIF2b 'ZINC (II) ION' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' _Database_query_date . _Details ; N-terminal domain (residue 39-90)and C-terminal domain (residues 108-143) have been deposited separately. ; save_ ######################## # Monomeric polymers # ######################## save_aIF2b _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'translation initiation factor IF2b' _Abbreviation_common aIF2b _Molecular_mass . _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 143 _Mol_residue_sequence ; MSDLENIDYYDYKALLKRAR SQIPDYVFQKDRFELPEIEI LIEGNRTIIRNFRELAKAVN RDEEFFAKYLLKETGSAGNL EGGRLILQRRISPELLKSRI NDFLREYVICRECGKPDTKI IKEGRVHLLKCMACGAIRPI RMI ; loop_ _Residue_seq_code _Residue_label 1 MET 2 SER 3 ASP 4 LEU 5 GLU 6 ASN 7 ILE 8 ASP 9 TYR 10 TYR 11 ASP 12 TYR 13 LYS 14 ALA 15 LEU 16 LEU 17 LYS 18 ARG 19 ALA 20 ARG 21 SER 22 GLN 23 ILE 24 PRO 25 ASP 26 TYR 27 VAL 28 PHE 29 GLN 30 LYS 31 ASP 32 ARG 33 PHE 34 GLU 35 LEU 36 PRO 37 GLU 38 ILE 39 GLU 40 ILE 41 LEU 42 ILE 43 GLU 44 GLY 45 ASN 46 ARG 47 THR 48 ILE 49 ILE 50 ARG 51 ASN 52 PHE 53 ARG 54 GLU 55 LEU 56 ALA 57 LYS 58 ALA 59 VAL 60 ASN 61 ARG 62 ASP 63 GLU 64 GLU 65 PHE 66 PHE 67 ALA 68 LYS 69 TYR 70 LEU 71 LEU 72 LYS 73 GLU 74 THR 75 GLY 76 SER 77 ALA 78 GLY 79 ASN 80 LEU 81 GLU 82 GLY 83 GLY 84 ARG 85 LEU 86 ILE 87 LEU 88 GLN 89 ARG 90 ARG 91 ILE 92 SER 93 PRO 94 GLU 95 LEU 96 LEU 97 LYS 98 SER 99 ARG 100 ILE 101 ASN 102 ASP 103 PHE 104 LEU 105 ARG 106 GLU 107 TYR 108 VAL 109 ILE 110 CYS 111 ARG 112 GLU 113 CYS 114 GLY 115 LYS 116 PRO 117 ASP 118 THR 119 LYS 120 ILE 121 ILE 122 LYS 123 GLU 124 GLY 125 ARG 126 VAL 127 HIS 128 LEU 129 LEU 130 LYS 131 CYS 132 MET 133 ALA 134 CYS 135 GLY 136 ALA 137 ILE 138 ARG 139 PRO 140 ILE 141 ARG 142 MET 143 ILE 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 GB AAB98077 "translation initiation factor aIF-2, subunit beta, putative (aIF2B) [Methanocaldococcus jannaschii DSM 2661]" 100.00 143 100.00 100.00 4.95e-97 GB ACV24219 "translation initiation factor aIF-2, beta subunit [Methanocaldococcus fervens AG86]" 100.00 143 97.20 100.00 7.36e-95 GB ADC69390 "translation initiation factor aIF-2, beta subunit [Methanocaldococcus sp. FS406-22]" 100.00 143 98.60 100.00 1.08e-95 GB AIJ05339 "translation initiation factor eIF-2, beta subunit [Methanocaldococcus sp. JH146]" 100.00 143 99.30 100.00 2.41e-96 REF NP_247061 "translation initiation factor IF-2 [Methanocaldococcus jannaschii DSM 2661]" 100.00 143 100.00 100.00 4.95e-97 REF WP_010869589 "translation initiation factor IF-2 [Methanocaldococcus jannaschii]" 100.00 143 100.00 100.00 4.95e-97 REF WP_012980300 "translation initiation factor IF-2 [Methanocaldococcus sp. FS406-22]" 100.00 143 98.60 100.00 1.08e-95 REF WP_015790959 "translation initiation factor IF-2 [Methanocaldococcus fervens]" 100.00 143 97.20 100.00 7.36e-95 REF YP_003127719 "translation initiation factor IF-2 [Methanocaldococcus fervens AG86]" 100.00 143 97.20 100.00 7.36e-95 SP Q57562 "RecName: Full=Translation initiation factor 2 subunit beta; AltName: Full=aIF2-beta; AltName: Full=eIF-2-beta [Methanocaldococc" 100.00 143 100.00 100.00 4.95e-97 stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common "ZN (ZINC ION)" _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Thu Jun 9 09:47:52 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $aIF2b 'Methanococcus jannaschii' 2190 Archaea . Methanococcus jannaschii 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 $aIF2b '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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $aIF2b . mM 0.5 1.5 '[U-13C; U-15N]' $ZN . mM . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $aIF2b . mM 0.5 1.5 [U-15N] $ZN . mM . . . stop_ save_ ############################ # Computer software used # ############################ save_felix _Saveframe_category software _Name felix _Version . loop_ _Task processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_HN(CO)CACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_3D-HCCH-TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HCCH-TOCSY _Sample_label . save_ save_15N-HMQC_6 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HMQC _Sample_label . save_ save_3D_1H-1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _Sample_label . save_ save_3D_1H-13C-1H_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C-1H HCCH-TOCSY' _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name 3D-HCCH-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name 15N-HMQC _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-1H-15N NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-13C-1H HCCH-TOCSY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 0.2 na temperature 303 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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H 1 'methyl protons' ppm 0.0 . direct . . . 1.000000000 $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 $entry_citation $entry_citation DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details ; Several residues (such as V59,E63,E64,A67,L71,K72,L80) had double peaks in both proton and nitrogen dimension for amide and nitrogen signals, probably due to conformational heterogeneity. ; loop_ _Experiment_label HNCA HNCO HNCACB HN(CO)CACB 3D-HCCH-TOCSY 15N-HMQC '3D 1H-1H-15N NOESY' '3D 1H-13C-1H HCCH-TOCSY' stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name aIF2b _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 . 21 SER N N 116.38 . 1 2 . 21 SER H H 8.28 . 1 3 . 21 SER CA C 58.49 . 1 4 . 21 SER HA H 4.46 . 1 5 . 21 SER HB2 H 3.84 . 2 6 . 22 GLN C C 174.60 . 1 7 . 23 ILE N N 124.70 . 1 8 . 23 ILE H H 7.19 . 1 9 . 23 ILE CA C 63.07 . 1 10 . 23 ILE HA H 4.14 . 1 11 . 23 ILE HB H 1.85 . 2 12 . 23 ILE HG2 H 0.95 . 4 13 . 25 ASP N N 119.93 . 1 14 . 25 ASP H H 8.22 . 1 15 . 25 ASP C C 175.02 . 1 16 . 25 ASP CA C 54.83 . 1 17 . 25 ASP HA H 4.65 . 1 18 . 25 ASP HB2 H 2.76 . 2 19 . 25 ASP HB3 H 3.75 . 2 20 . 26 TYR N N 119.05 . 1 21 . 26 TYR H H 7.82 . 1 22 . 26 TYR C C 175.07 . 1 23 . 26 TYR CA C 58.47 . 1 24 . 26 TYR HA H 4.43 . 1 25 . 26 TYR HB2 H 2.90 . 2 26 . 26 TYR HB3 H 2.96 . 2 27 . 26 TYR HD1 H 6.98 . 3 28 . 26 TYR HE1 H 6.74 . 3 29 . 27 VAL N N 121.82 . 1 30 . 27 VAL H H 7.71 . 1 31 . 27 VAL C C 176.44 . 1 32 . 27 VAL CA C 62.96 . 1 33 . 27 VAL HA H 3.88 . 1 34 . 27 VAL HB H 1.85 . 1 35 . 27 VAL HG1 H 0.70 . 1 36 . 27 VAL HG2 H 0.74 . 1 37 . 28 PHE N N 122.87 . 1 38 . 28 PHE H H 8.01 . 1 39 . 28 PHE C C 173.79 . 1 40 . 28 PHE CA C 58.11 . 1 41 . 28 PHE HA H 4.55 . 1 42 . 28 PHE HB2 H 2.98 . 2 43 . 28 PHE HB3 H 3.08 . 2 44 . 29 GLN N N 124.69 . 1 45 . 29 GLN H H 8.04 . 1 46 . 29 GLN C C 177.75 . 1 47 . 29 GLN CA C 55.41 . 1 48 . 29 GLN HA H 4.28 . 1 49 . 29 GLN HB2 H 1.74 . 2 50 . 29 GLN HG2 H 2.07 . 2 51 . 30 LYS N N 117.56 . 1 52 . 30 LYS H H 8.16 . 1 53 . 30 LYS C C 177.14 . 1 54 . 30 LYS CA C 60.39 . 1 55 . 30 LYS HA H 3.73 . 1 56 . 30 LYS HB2 H 1.25 . 2 57 . 31 ASP N N 111.98 . 1 58 . 31 ASP H H 7.87 . 1 59 . 31 ASP CA C 59.29 . 1 60 . 31 ASP HA H 4.50 . 1 61 . 31 ASP HB2 H 1.46 . 2 62 . 31 ASP HB3 H 2.62 . 2 63 . 33 PHE N N 124.70 . 1 64 . 33 PHE H H 7.19 . 1 65 . 33 PHE C C 177.01 . 1 66 . 33 PHE CA C 61.68 . 1 67 . 33 PHE HA H 4.20 . 1 68 . 33 PHE HB2 H 3.43 . 2 69 . 33 PHE HB3 H 3.15 . 2 70 . 38 ILE N N 110.80 . 1 71 . 38 ILE H H 7.44 . 1 72 . 38 ILE C C 174.39 . 1 73 . 38 ILE CA C 62.00 . 1 74 . 38 ILE HA H 3.96 . 1 75 . 39 GLU N N 130.23 . 1 76 . 39 GLU H H 8.66 . 1 77 . 39 GLU C C 175.10 . 1 78 . 39 GLU CA C 55.70 . 1 79 . 39 GLU HA H 4.45 . 1 80 . 39 GLU HB2 H 1.85 . 2 81 . 39 GLU HG2 H 2.18 . 2 82 . 40 ILE N N 126.08 . 1 83 . 40 ILE H H 8.27 . 1 84 . 40 ILE C C 174.41 . 1 85 . 40 ILE CA C 59.91 . 1 86 . 40 ILE HA H 5.07 . 1 87 . 40 ILE HB H 1.67 . 2 88 . 40 ILE HG2 H 0.7 . 4 89 . 40 ILE HD1 H 0.77 . 4 90 . 41 LEU N N 129.75 . 1 91 . 41 LEU H H 9.39 . 1 92 . 41 LEU CA C 53.82 . 1 93 . 41 LEU HA H 4.78 . 1 94 . 41 LEU HB2 H 1.54 . 2 95 . 41 LEU HB3 H 1.62 . 2 96 . 41 LEU HD1 H 0.88 . 4 97 . 42 ILE N N 124.70 . 1 98 . 42 ILE H H 8.60 . 1 99 . 42 ILE C C 175.39 . 1 100 . 42 ILE CA C 60.4 . 1 101 . 42 ILE HA H 4.77 . 1 102 . 42 ILE HB H 1.77 . 2 103 . 42 ILE HG2 H 0.85 . 4 104 . 43 GLU N N 128.95 . 1 105 . 43 GLU H H 8.38 . 1 106 . 43 GLU C C 175.39 . 1 107 . 43 GLU CA C 54.78 . 1 108 . 43 GLU HA H 4.59 . 1 109 . 43 GLU HB2 H 1.71 . 2 110 . 43 GLU HG2 H 2.04 . 2 111 . 44 GLY N N 114.75 . 1 112 . 44 GLY H H 8.84 . 1 113 . 44 GLY C C 173.76 . 1 114 . 44 GLY CA C 47.54 . 1 115 . 44 GLY HA2 H 3.87 . 2 116 . 44 GLY HA3 H 3.61 . 2 117 . 45 ASN N N 123.72 . 1 118 . 45 ASN H H 8.57 . 1 119 . 45 ASN C C 172.40 . 1 120 . 45 ASN CA C 52.75 . 1 121 . 45 ASN HA H 4.48 . 1 122 . 45 ASN HB2 H 2.90 . 2 123 . 45 ASN HB3 H 2.61 . 2 124 . 46 ARG N N 115.74 . 1 125 . 46 ARG H H 7.58 . 1 126 . 46 ARG C C 173.68 . 1 127 . 46 ARG CA C 55.25 . 1 128 . 46 ARG HA H 4.81 . 1 129 . 46 ARG HB2 H 1.53 . 2 130 . 46 ARG HB3 H 1.81 . 2 131 . 47 THR N N 118.12 . 1 132 . 47 THR H H 8.62 . 1 133 . 47 THR C C 172.03 . 1 134 . 47 THR CA C 62.88 . 1 135 . 47 THR HA H 4.83 . 1 136 . 47 THR HB H 3.92 . 1 137 . 47 THR HG2 H 1.09 . 1 138 . 48 ILE N N 126.58 . 1 139 . 48 ILE H H 9.49 . 1 140 . 48 ILE C C 175.86 . 1 141 . 48 ILE CA C 59.90 . 1 142 . 48 ILE HA H 5.03 . 1 143 . 48 ILE HB H 1.82 . 1 144 . 48 ILE HG2 H 0.69 . 4 145 . 48 ILE HD1 H 0.76 . 4 146 . 49 ILE N N 125.53 . 1 147 . 49 ILE H H 9.12 . 1 148 . 49 ILE C C 176.36 . 1 149 . 49 ILE CA C 60.60 . 1 150 . 49 ILE HA H 4.78 . 1 151 . 49 ILE HB H 1.88 . 1 152 . 49 ILE HG2 H 0.73 . 4 153 . 49 ILE HD1 H 0.90 . 4 154 . 50 ARG N N 128.90 . 1 155 . 50 ARG H H 8.92 . 1 156 . 50 ARG C C 180.26 . 1 157 . 50 ARG CA C 59.46 . 1 158 . 50 ARG HA H 3.79 . 1 159 . 50 ARG HB2 H 1.63 . 2 160 . 51 ASN N N 115.35 . 1 161 . 51 ASN H H 8.49 . 1 162 . 51 ASN C C 174.78 . 1 163 . 51 ASN CA C 51.32 . 1 164 . 51 ASN HA H 5.25 . 1 165 . 51 ASN HB2 H 2.55 . 2 166 . 51 ASN HB3 H 3.11 . 2 167 . 51 ASN HD21 H 7.4 . 2 168 . 51 ASN HD22 H 7.6 . 2 169 . 52 PHE N N 120.22 . 1 170 . 52 PHE H H 7.07 . 1 171 . 52 PHE C C 175.49 . 1 172 . 52 PHE CA C 63.75 . 1 173 . 52 PHE HA H 3.75 . 1 174 . 52 PHE HB2 H 2.86 . 2 175 . 53 ARG N N 118.54 . 1 176 . 53 ARG H H 8.41 . 1 177 . 53 ARG CA C 60.08 . 1 178 . 53 ARG HA H 3.72 . 1 179 . 54 GLU N N 119.26 . 1 180 . 54 GLU H H 8.1 . 1 181 . 54 GLU HA H 3.90 . 1 182 . 54 GLU HB2 H 2.32 . 2 183 . 54 GLU HB3 H 2.14 . 2 184 . 55 LEU N N 121.60 . 1 185 . 55 LEU H H 7.79 . 1 186 . 55 LEU CA C 58.24 . 1 187 . 55 LEU HA H 3.89 . 1 188 . 55 LEU HB2 H 1.54 . 2 189 . 55 LEU HD1 H 0.76 . 2 190 . 56 ALA N N 120.37 . 1 191 . 56 ALA H H 8.05 . 1 192 . 56 ALA C C 178.61 . 1 193 . 56 ALA CA C 55.49 . 1 194 . 56 ALA HA H 3.87 . 1 195 . 56 ALA HB H 1.25 . 1 196 . 57 LYS N N 116.46 . 1 197 . 57 LYS H H 8.15 . 1 198 . 57 LYS C C 179.61 . 1 199 . 57 LYS CA C 59.08 . 1 200 . 57 LYS HA H 4.12 . 1 201 . 58 ALA N N 121.82 . 1 202 . 58 ALA H H 7.86 . 1 203 . 58 ALA C C 178.66 . 1 204 . 58 ALA CA C 55.01 . 1 205 . 58 ALA HA H 4.19 . 1 206 . 58 ALA HB H 1.63 . 1 207 . 59 VAL N N 106.45 . 1 208 . 59 VAL H H 7.39 . 1 209 . 59 VAL C C 177.83 . 9 210 . 59 VAL CA C 60.40 . 1 211 . 59 VAL HA H 4.27 . 1 212 . 59 VAL HB H 2.36 . 1 213 . 59 VAL HG1 H 0.76 . 2 214 . 60 ASN N N 118.62 . 1 215 . 60 ASN H H 7.92 . 1 216 . 60 ASN CA C 53.68 . 1 217 . 60 ASN HA H 4.31 . 1 218 . 60 ASN HB2 H 3.19 . 2 219 . 60 ASN HB3 H 2.50 . 2 220 . 60 ASN HD21 H 6.78 . 2 221 . 60 ASN HD22 H 7.45 . 2 222 . 61 ARG N N 115.20 . 1 223 . 61 ARG H H 7.82 . 1 224 . 61 ARG CA C 52.37 . 1 225 . 61 ARG HB2 H 1.45 . 2 226 . 62 ASP N N 120.70 . 1 227 . 62 ASP H H 8.36 . 1 228 . 62 ASP CA C 55.05 . 1 229 . 62 ASP HA H 4.43 . 1 230 . 62 ASP HB2 H 2.74 . 2 231 . 63 GLU N N 124.87 . 1 232 . 63 GLU H H 8.97 . 1 233 . 63 GLU CA C 60.49 . 1 234 . 63 GLU HA H 3.83 . 1 235 . 63 GLU HB2 H 2.01 . 2 236 . 63 GLU HB3 H 2.17 . 2 237 . 63 GLU HG2 H 2.30 . 2 238 . 64 GLU N N 119.50 . 1 239 . 64 GLU H H 8.53 . 1 240 . 64 GLU CA C 60.30 . 1 241 . 64 GLU HA H 3.98 . 1 242 . 64 GLU HB2 H 2.14 . 2 243 . 66 PHE N N 119.95 . 1 244 . 66 PHE H H 8.24 . 1 245 . 66 PHE CA C 57.03 . 1 246 . 67 ALA N N 120.22 . 1 247 . 67 ALA H H 8.81 . 1 248 . 67 ALA CA C 55.85 . 1 249 . 67 ALA HA H 3.48 . 1 250 . 67 ALA HB H 1.22 . 1 251 . 68 LYS N N 116.36 . 1 252 . 68 LYS H H 8.32 . 1 253 . 68 LYS CA C 60.30 . 1 254 . 68 LYS HA H 3.73 . 1 255 . 69 TYR N N 120.27 . 1 256 . 69 TYR H H 7.57 . 1 257 . 69 TYR CA C 62.02 . 1 258 . 69 TYR HA H 4.11 . 1 259 . 69 TYR HB2 H 3.28 . 2 260 . 69 TYR HB3 H 2.81 . 2 261 . 70 LEU N N 118.12 . 1 262 . 70 LEU H H 7.77 . 1 263 . 70 LEU CA C 58.00 . 1 264 . 70 LEU HA H 3.77 . 1 265 . 70 LEU HB2 H 1.76 . 2 266 . 70 LEU HD1 H 0.97 . 2 267 . 70 LEU HD2 H 0.55 . 2 268 . 71 LEU N N 121.32 . 1 269 . 71 LEU H H 8.7 . 1 270 . 71 LEU CA C 58.83 . 1 271 . 71 LEU HA H 3.66 . 1 272 . 71 LEU HB2 H 1.62 . 2 273 . 71 LEU HD1 H 0.54 . 2 274 . 71 LEU HD2 H 0.44 . 2 275 . 72 LYS N N 119.14 . 1 276 . 72 LYS H H 7.88 . 1 277 . 72 LYS C C 180.26 . 1 278 . 72 LYS CA C 56.09 . 1 279 . 72 LYS HA H 4.04 . 1 280 . 73 GLU N N 115.78 . 1 281 . 73 GLU H H 8.48 . 1 282 . 73 GLU C C 177.50 . 1 283 . 73 GLU CA C 57.93 . 1 284 . 73 GLU HA H 4.07 . 1 285 . 73 GLU HB2 H 1.44 . 2 286 . 74 THR N N 105.51 . 1 287 . 74 THR H H 7.5 . 1 288 . 74 THR C C 174.78 . 1 289 . 74 THR CA C 61.92 . 1 290 . 74 THR HA H 4.39 . 1 291 . 74 THR HB H 4.17 . 1 292 . 74 THR HG2 H 1.06 . 1 293 . 75 GLY N N 112.48 . 1 294 . 75 GLY H H 7.57 . 1 295 . 75 GLY C C 175.96 . 1 296 . 75 GLY CA C 47.27 . 1 297 . 75 GLY HA2 H 3.83 . 2 298 . 76 SER N N 114.86 . 1 299 . 76 SER H H 8.1 . 1 300 . 76 SER CA C 57.7 . 1 301 . 76 SER HA H 4.64 . 1 302 . 76 SER HB2 H 3.30 . 2 303 . 76 SER HB3 H 3.56 . 2 304 . 77 ALA N N 125.58 . 1 305 . 77 ALA H H 8.27 . 1 306 . 77 ALA C C 176.50 . 1 307 . 77 ALA CA C 51.0 . 1 308 . 77 ALA HA H 4.58 . 1 309 . 77 ALA HB H 1.32 . 1 310 . 78 GLY N N 107.72 . 1 311 . 78 GLY H H 8.2 . 1 312 . 78 GLY C C 170.9 . 1 313 . 78 GLY CA C 46.54 . 1 314 . 78 GLY HA2 H 4.12 . 2 315 . 78 GLY HA3 H 4.49 . 2 316 . 79 ASN N N 113.31 . 1 317 . 79 ASN H H 8.58 . 1 318 . 79 ASN C C 173.81 . 1 319 . 79 ASN CA C 53.05 . 1 320 . 79 ASN HA H 4.77 . 1 321 . 79 ASN HB2 H 2.53 . 2 322 . 79 ASN HB3 H 2.72 . 2 323 . 79 ASN HD21 H 7.20 . 2 324 . 79 ASN HD22 H 6.86 . 2 325 . 80 LEU N N 123.39 . 1 326 . 80 LEU H H 8.48 . 1 327 . 80 LEU C C 176.23 . 1 328 . 80 LEU CA C 54.15 . 1 329 . 80 LEU HA H 4.91 . 1 330 . 80 LEU HB2 H 1.47 . 2 331 . 80 LEU HD1 H 0.73 . 2 332 . 80 LEU HD2 H 0.78 . 2 333 . 81 GLU N N 124.53 . 1 334 . 81 GLU H H 8.61 . 1 335 . 81 GLU C C 174.36 . 1 336 . 81 GLU CA C 55.98 . 1 337 . 81 GLU HA H 4.52 . 1 338 . 81 GLU HB2 H 1.77 . 2 339 . 82 GLY N N 117.11 . 1 340 . 82 GLY H H 9.11 . 1 341 . 82 GLY C C 174.49 . 1 342 . 82 GLY CA C 47.43 . 1 343 . 82 GLY HA2 H 4.71 . 2 344 . 82 GLY HA3 H 3.88 . 2 345 . 83 GLY N N 108.60 . 1 346 . 83 GLY H H 8.73 . 1 347 . 83 GLY C C 172.16 . 1 348 . 83 GLY CA C 45.84 . 1 349 . 83 GLY HA2 H 4.20 . 2 350 . 83 GLY HA3 H 3.84 . 2 351 . 84 ARG N N 117.68 . 1 352 . 84 ARG H H 7.88 . 1 353 . 84 ARG CA C 54.50 . 1 354 . 84 ARG HA H 4.93 . 1 355 . 84 ARG HB2 H 1.77 . 2 356 . 84 ARG HB3 H 2.02 . 2 357 . 84 ARG HG2 H 3.23 . 2 358 . 85 LEU N N 121.82 . 1 359 . 85 LEU H H 7.69 . 1 360 . 85 LEU C C 173.00 . 1 361 . 85 LEU CA C 53.80 . 1 362 . 85 LEU HA H 4.60 . 1 363 . 85 LEU HB2 H 1.10 . 2 364 . 85 LEU HG H 0.90 . 1 365 . 85 LEU HD1 H 0.26 . 2 366 . 85 LEU HD2 H -0.02 . 2 367 . 86 ILE N N 128.29 . 1 368 . 86 ILE H H 8.7 . 1 369 . 86 ILE C C 174.11 . 1 370 . 86 ILE CA C 61.12 . 1 371 . 86 ILE HA H 4.33 . 1 372 . 86 ILE HB H 1.91 . 1 373 . 86 ILE HG2 H 0.67 . 4 374 . 87 LEU N N 125.76 . 1 375 . 87 LEU H H 9.31 . 1 376 . 87 LEU C C 177.25 . 1 377 . 87 LEU CA C 55.01 . 1 378 . 87 LEU HA H 4.80 . 1 379 . 87 LEU HB2 H 1.87 . 2 380 . 88 GLN N N 123.81 . 1 381 . 88 GLN H H 8.7 . 1 382 . 88 GLN CA C 55.40 . 1 383 . 88 GLN HA H 4.34 . 1 384 . 88 GLN HB2 H 1.60 . 2 385 . 88 GLN HB3 H 2.12 . 2 386 . 88 GLN HG2 H 2.32 . 2 387 . 88 GLN HE21 H 6.67 . 2 388 . 88 GLN HE22 H 7.33 . 2 389 . 89 ARG N N 119.00 . 1 390 . 89 ARG H H 8.01 . 1 391 . 89 ARG C C 174.36 . 1 392 . 89 ARG CA C 55.83 . 1 393 . 89 ARG HA H 4.00 . 1 394 . 90 ARG N N 122.13 . 1 395 . 90 ARG H H 8.41 . 1 396 . 90 ARG C C 174.07 . 1 397 . 90 ARG CA C 56.80 . 1 398 . 90 ARG HA H 3.93 . 1 399 . 90 ARG HB2 H 1.70 . 2 400 . 90 ARG HB3 H 1.85 . 4 401 . 90 ARG HG2 H 1.55 . 4 402 . 90 ARG HG3 H 1.35 . 4 403 . 91 ILE N N 128.51 . 1 404 . 91 ILE H H 7.95 . 1 405 . 91 ILE C C 174.45 . 1 406 . 91 ILE CA C 59.54 . 1 407 . 91 ILE HA H 4.21 . 1 408 . 91 ILE HB H 1.50 . 1 409 . 91 ILE HG12 H 1.74 . 2 410 . 91 ILE HG2 H 0.75 . 1 411 . 91 ILE HD1 H 0.96 . 1 412 . 92 SER N N 120.20 . 1 413 . 92 SER H H 8.24 . 1 414 . 92 SER CA C 65.74 . 1 415 . 93 PRO CA C 65.83 . 1 416 . 93 PRO HA H 4.05 . 1 417 . 93 PRO HB2 H 1.88 . 2 418 . 93 PRO HB3 H 2.05 . 2 419 . 94 GLU N N 115.56 . 1 420 . 94 GLU H H 8.43 . 1 421 . 94 GLU C C 177.51 . 1 422 . 94 GLU CA C 59.97 . 1 423 . 94 GLU HA H 3.95 . 1 424 . 94 GLU HB2 H 1.97 . 2 425 . 94 GLU HG2 H 2.30 . 2 426 . 95 LEU N N 122.76 . 1 427 . 95 LEU H H 7.49 . 1 428 . 95 LEU C C 178.64 . 1 429 . 95 LEU CA C 57.90 . 1 430 . 95 LEU HA H 4.20 . 1 431 . 95 LEU HB2 H 1.82 . 2 432 . 95 LEU HG H 1.74 . 1 433 . 95 LEU HD1 H 0.91 . 2 434 . 95 LEU HD2 H 0.95 . 2 435 . 96 LEU H H 7.82 . 1 436 . 96 LEU C C 178.23 . 1 437 . 96 LEU CA C 58.35 . 1 438 . 97 LYS N N 117.40 . 1 439 . 97 LYS H H 8.55 . 1 440 . 97 LYS C C 178.04 . 1 441 . 97 LYS CA C 61.00 . 1 442 . 97 LYS HA H 3.80 . 1 443 . 97 LYS HB2 H 1.88 . 2 444 . 98 SER N N 115.80 . 1 445 . 98 SER H H 7.91 . 1 446 . 98 SER C C 179.00 . 1 447 . 98 SER CA C 62.88 . 1 448 . 98 SER HA H 4.13 . 1 449 . 98 SER HB2 H 4.32 . 2 450 . 99 ARG H H 8.08 . 1 451 . 99 ARG CA C 55.88 . 1 452 . 100 ILE N N 121.42 . 1 453 . 100 ILE H H 8.42 . 1 454 . 100 ILE CA C 58.87 . 1 455 . 100 ILE HA H 3.84 . 1 456 . 101 ASN N N 119.00 . 1 457 . 101 ASN H H 8.19 . 1 458 . 101 ASN HA H 4.56 . 1 459 . 103 PHE N N 122.47 . 1 460 . 103 PHE H H 8.2 . 1 461 . 103 PHE C C 176.80 . 1 462 . 103 PHE CA C 62.18 . 1 463 . 103 PHE HA H 3.61 . 1 464 . 103 PHE HB2 H 3.02 . 2 465 . 103 PHE HB3 H 3.35 . 2 466 . 104 LEU N N 117.62 . 1 467 . 104 LEU H H 8.39 . 1 468 . 104 LEU C C 178.98 . 1 469 . 104 LEU CA C 57.90 . 1 470 . 104 LEU HA H 4.45 . 1 471 . 105 ARG H H 8.08 . 1 472 . 105 ARG CA C 56.80 . 1 473 . 105 ARG HA H 4.06 . 1 474 . 106 GLU C C 177.22 . 1 475 . 106 GLU CA C 57.87 . 1 476 . 107 TYR N N 110.21 . 1 477 . 107 TYR H H 7.93 . 1 478 . 107 TYR C C 175.04 . 1 479 . 107 TYR CA C 58.59 . 1 480 . 107 TYR HA H 4.44 . 1 481 . 107 TYR HB2 H 2.70 . 2 482 . 107 TYR HB3 H 3.18 . 2 483 . 107 TYR HD1 H 6.54 . 3 484 . 107 TYR HE1 H 6.81 . 3 485 . 108 VAL N N 117.68 . 1 486 . 108 VAL H H 7.44 . 1 487 . 108 VAL CA C 64.70 . 1 488 . 108 VAL HA H 3.89 . 1 489 . 108 VAL HB H 2.06 . 1 490 . 108 VAL HG1 H 0.54 . 2 491 . 108 VAL HG2 H 0.78 . 2 492 . 109 ILE N N 119.90 . 1 493 . 109 ILE H H 8.01 . 1 494 . 109 ILE C C 175.36 . 1 495 . 109 ILE CA C 61.00 . 1 496 . 109 ILE HA H 3.51 . 1 497 . 109 ILE HB H 1.04 . 1 498 . 109 ILE HG2 H 0.55 . 4 499 . 110 CYS N N 131.24 . 1 500 . 110 CYS H H 8.45 . 1 501 . 110 CYS C C 173.50 . 1 502 . 110 CYS CA C 60.65 . 1 503 . 110 CYS HA H 3.88 . 1 504 . 110 CYS HB2 H 3.13 . 2 505 . 111 ARG N N 130.72 . 1 506 . 111 ARG H H 9.07 . 1 507 . 111 ARG C C 175.86 . 1 508 . 111 ARG CA C 58.08 . 1 509 . 111 ARG HA H 3.98 . 1 510 . 111 ARG HB2 H 1.69 . 2 511 . 111 ARG HB3 H 1.87 . 2 512 . 112 GLU N N 120.72 . 1 513 . 112 GLU H H 9.14 . 1 514 . 112 GLU C C 177.17 . 1 515 . 112 GLU CA C 57.87 . 1 516 . 112 GLU HA H 4.34 . 1 517 . 112 GLU HB2 H 1.84 . 2 518 . 112 GLU HB3 H 2.12 . 2 519 . 113 CYS N N 118.89 . 1 520 . 113 CYS H H 8.8 . 1 521 . 113 CYS C C 176.17 . 1 522 . 113 CYS CA C 58.6 . 1 523 . 113 CYS HA H 5.00 . 1 524 . 113 CYS HB2 H 3.15 . 2 525 . 113 CYS HB3 H 2.69 . 2 526 . 114 GLY N N 109.64 . 1 527 . 114 GLY H H 8.37 . 1 528 . 114 GLY CA C 45.34 . 1 529 . 114 GLY HA2 H 3.92 . 2 530 . 115 LYS N N 125.25 . 1 531 . 115 LYS H H 7.99 . 1 532 . 115 LYS CA C 52.37 . 1 533 . 115 LYS HA H 4.35 . 2 534 . 115 LYS HB2 H 1.33 . 2 535 . 117 ASP N N 123.11 . 1 536 . 117 ASP H H 6.74 . 1 537 . 117 ASP C C 176.67 . 1 538 . 117 ASP CA C 53.35 . 1 539 . 117 ASP HA H 4.74 . 1 540 . 117 ASP HB2 H 2.36 . 2 541 . 117 ASP HB3 H 2.73 . 2 542 . 118 THR N N 110.48 . 1 543 . 118 THR H H 8.25 . 1 544 . 118 THR C C 174.63 . 1 545 . 118 THR CA C 58.95 . 1 546 . 118 THR HA H 5.35 . 1 547 . 118 THR HB H 3.80 . 1 548 . 118 THR HG2 H 1.01 . 1 549 . 119 LYS N N 121.80 . 1 550 . 119 LYS H H 9.28 . 1 551 . 119 LYS CA C 54.89 . 1 552 . 119 LYS HA H 4.75 . 1 553 . 119 LYS HB2 H 1.61 . 2 554 . 119 LYS HG2 H 1.36 . 2 555 . 120 ILE H H 8.58 . 1 556 . 120 ILE CA C 55.73 . 1 557 . 120 ILE HA H 4.87 . 1 558 . 121 ILE N N 126.96 . 1 559 . 121 ILE H H 9.38 . 1 560 . 121 ILE C C 173.42 . 1 561 . 121 ILE CA C 59.39 . 1 562 . 121 ILE HA H 4.56 . 1 563 . 121 ILE HB H 1.84 . 1 564 . 121 ILE HG2 H 0.81 . 4 565 . 122 LYS N N 124.05 . 1 566 . 122 LYS H H 8.38 . 1 567 . 122 LYS C C 175.04 . 1 568 . 122 LYS CA C 55.37 . 1 569 . 122 LYS HA H 4.60 . 1 570 . 122 LYS HB2 H 1.29 . 2 571 . 122 LYS HB3 H 1.56 . 2 572 . 123 GLU N N 127.96 . 1 573 . 123 GLU H H 8.5 . 1 574 . 123 GLU C C 175.46 . 1 575 . 123 GLU CA C 55.37 . 1 576 . 123 GLU HA H 4.45 . 1 577 . 123 GLU HB2 H 2.01 . 2 578 . 123 GLU HB3 H 2.06 . 2 579 . 123 GLU HG2 H 1.65 . 2 580 . 123 GLU HG3 H 1.83 . 2 581 . 124 GLY N N 116.08 . 1 582 . 124 GLY H H 8.76 . 1 583 . 124 GLY CA C 46.8 . 1 584 . 124 GLY HA2 H 3.99 . 2 585 . 124 GLY HA3 H 3.54 . 2 586 . 125 ARG N N 124.55 . 1 587 . 125 ARG H H 8.83 . 1 588 . 125 ARG C C 175.41 . 1 589 . 125 ARG CA C 56.51 . 1 590 . 125 ARG HA H 4.30 . 1 591 . 125 ARG HB2 H 1.76 . 2 592 . 126 VAL N N 119.50 . 1 593 . 126 VAL H H 7.75 . 1 594 . 126 VAL C C 173.44 . 1 595 . 126 VAL CA C 61.92 . 1 596 . 126 VAL HA H 4.29 . 1 597 . 126 VAL HB H 2.21 . 1 598 . 126 VAL HG1 H 1.83 . 2 599 . 126 VAL HG2 H 1.65 . 2 600 . 127 HIS N N 123.15 . 1 601 . 127 HIS H H 8.51 . 1 602 . 127 HIS C C 173.86 . 1 603 . 127 HIS CA C 56.1 . 1 604 . 127 HIS HA H 5.18 . 1 605 . 127 HIS HB2 H 2.72 . 2 606 . 127 HIS HB3 H 2.98 . 2 607 . 127 HIS HD1 H 6.68 . 4 608 . 127 HIS HE1 H 7.65 . 4 609 . 128 LEU N N 121.33 . 1 610 . 128 LEU H H 9.13 . 1 611 . 128 LEU C C 173.79 . 1 612 . 128 LEU CA C 53.30 . 1 613 . 128 LEU HA H 4.96 . 1 614 . 128 LEU HB2 H 1.44 . 2 615 . 128 LEU HD1 H 0.72 . 2 616 . 128 LEU HD2 H 0.76 . 2 617 . 129 LEU N N 123.11 . 1 618 . 129 LEU H H 9.14 . 1 619 . 129 LEU C C 174.70 . 1 620 . 129 LEU CA C 53.82 . 1 621 . 129 LEU HA H 4.85 . 1 622 . 129 LEU HB2 H 1.77 . 2 623 . 130 LYS N N 129.34 . 1 624 . 130 LYS H H 9.25 . 1 625 . 130 LYS C C 173.50 . 1 626 . 130 LYS CA C 54.20 . 1 627 . 130 LYS HA H 4.94 . 1 628 . 130 LYS HB2 H 1.70 . 2 629 . 131 CYS N N 128.79 . 1 630 . 131 CYS H H 9.02 . 1 631 . 131 CYS C C 177.17 . 1 632 . 131 CYS CA C 59.60 . 1 633 . 131 CYS HA H 4.44 . 1 634 . 131 CYS HB2 H 2.73 . 2 635 . 131 CYS HB3 H 3.27 . 2 636 . 132 MET N N 128.95 . 1 637 . 132 MET H H 9.37 . 1 638 . 132 MET C C 174.21 . 1 639 . 132 MET CA C 55.93 . 1 640 . 132 MET HA H 4.40 . 1 641 . 132 MET HB2 H 2.02 . 2 642 . 132 MET HB3 H 2.33 . 2 643 . 133 ALA N N 126.58 . 1 644 . 133 ALA H H 9.33 . 1 645 . 133 ALA C C 178.09 . 1 646 . 133 ALA CA C 54.66 . 1 647 . 133 ALA HA H 4.44 . 1 648 . 133 ALA HB H 1.47 . 1 649 . 134 CYS N N 120.83 . 1 650 . 134 CYS H H 9.7 . 1 651 . 134 CYS C C 176.42 . 1 652 . 134 CYS CA C 58.83 . 1 653 . 134 CYS HA H 5.01 . 1 654 . 134 CYS HB2 H 2.57 . 2 655 . 134 CYS HB3 H 3.27 . 2 656 . 135 GLY N N 112.42 . 1 657 . 135 GLY H H 7.3 . 1 658 . 135 GLY C C 173.44 . 1 659 . 135 GLY CA C 46.08 . 1 660 . 135 GLY HA2 H 4.30 . 2 661 . 135 GLY HA3 H 3.82 . 2 662 . 136 ALA N N 126.91 . 1 663 . 136 ALA H H 8.86 . 1 664 . 136 ALA CA C 54.18 . 1 665 . 136 ALA HA H 4.20 . 1 666 . 136 ALA HB H 1.39 . 1 667 . 137 ILE N N 119.35 . 1 668 . 137 ILE H H 8.3 . 1 669 . 137 ILE C C 175.07 . 1 670 . 137 ILE CA C 59.70 . 1 671 . 137 ILE HA H 5.41 . 1 672 . 137 ILE HB H 1.58 . 1 673 . 137 ILE HG2 H 0.82 . 4 674 . 138 ARG N N 123.15 . 1 675 . 138 ARG H H 8.42 . 1 676 . 138 ARG CA C 55.73 . 1 677 . 138 ARG HA H 5.03 . 1 678 . 140 ILE N N 115.80 . 1 679 . 140 ILE H H 8.11 . 1 680 . 140 ILE CA C 59.30 . 1 681 . 140 ILE HA H 4.17 . 1 stop_ save_