data_5312 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N chemical shift assignments of aIF2beta from Methanobacterium themoautotrophicum ; _BMRB_accession_number 5312 _BMRB_flat_file_name bmr5312.str _Entry_type original _Submission_date 2002-03-07 _Accession_date 2002-03-07 _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 Gutierrez Pablo A. Sanchez 2 Coillet-Matillon Stephane . . 3 Arrowsmith Cheryl . . 4 Gehring Kalle B. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 430 "13C chemical shifts" 296 "15N chemical shifts" 122 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-02-20 original author . stop_ _Original_release_date 2003-02-20 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Zinc is required for Structural Stability of the C-terminus of Archaeal Translation Initiation Factor aIF2beta ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22057822 _PubMed_ID 12062427 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gutierrez Pablo A. Sanchez 2 Coillet-Matillon Stephane . . 3 Arrowsmith Cheryl . . 4 Gehring Kalle B. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_volume 517 _Journal_issue 1-3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 155 _Page_last 158 _Year 2002 _Details . loop_ _Keyword aIF2beta 'Zinc Finger' 'Translation initiation' stop_ save_ ################################## # Molecular system description # ################################## save_system_aIF2beta _Saveframe_category molecular_system _Mol_system_name aIF2beta _Abbreviation_common aIF2beta _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label aIF2beta $aIF2beta 'Zinc ion' $ZN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'Recognition of initiation codon' 'Interactions with mRNA' 'GAP for aIF2' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_aIF2beta _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'translation initiation factor 2 beta' _Abbreviation_common aIF2Beta _Molecular_mass 16200 _Mol_thiol_state 'all other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 135 _Mol_residue_sequence ; MDDYEKLLERAIDQLPPEVF ETKRFEVPKAYSVIQGNRTF IQNFREVADALNRDPQHLLK FLLRELGTAGNLEGGRAILQ GKFTHFLINERIEDYVNKFV ICHECNRPDTRIIREGRISL LKCEACGAKAPLKNV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 ASP 4 TYR 5 GLU 6 LYS 7 LEU 8 LEU 9 GLU 10 ARG 11 ALA 12 ILE 13 ASP 14 GLN 15 LEU 16 PRO 17 PRO 18 GLU 19 VAL 20 PHE 21 GLU 22 THR 23 LYS 24 ARG 25 PHE 26 GLU 27 VAL 28 PRO 29 LYS 30 ALA 31 TYR 32 SER 33 VAL 34 ILE 35 GLN 36 GLY 37 ASN 38 ARG 39 THR 40 PHE 41 ILE 42 GLN 43 ASN 44 PHE 45 ARG 46 GLU 47 VAL 48 ALA 49 ASP 50 ALA 51 LEU 52 ASN 53 ARG 54 ASP 55 PRO 56 GLN 57 HIS 58 LEU 59 LEU 60 LYS 61 PHE 62 LEU 63 LEU 64 ARG 65 GLU 66 LEU 67 GLY 68 THR 69 ALA 70 GLY 71 ASN 72 LEU 73 GLU 74 GLY 75 GLY 76 ARG 77 ALA 78 ILE 79 LEU 80 GLN 81 GLY 82 LYS 83 PHE 84 THR 85 HIS 86 PHE 87 LEU 88 ILE 89 ASN 90 GLU 91 ARG 92 ILE 93 GLU 94 ASP 95 TYR 96 VAL 97 ASN 98 LYS 99 PHE 100 VAL 101 ILE 102 CYS 103 HIS 104 GLU 105 CYS 106 ASN 107 ARG 108 PRO 109 ASP 110 THR 111 ARG 112 ILE 113 ILE 114 ARG 115 GLU 116 GLY 117 ARG 118 ILE 119 SER 120 LEU 121 LEU 122 LYS 123 CYS 124 GLU 125 ALA 126 CYS 127 GLY 128 ALA 129 LYS 130 ALA 131 PRO 132 LEU 133 LYS 134 ASN 135 VAL stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 REF NP_276875 'translation initiation factor IF-2 subunit beta [Methanothermobacter thermautotrophicus str. Delta H]' 100.00 135 100.00 100.00 2.59e-73 SWISS-PROT O27797 'Translation initiation factor 2 subunit beta (eIF-2-beta) (aIF2-beta)' 100.00 135 100.00 100.00 2.59e-73 PDB 1NEE 'Structure Of Archaeal Translation Factor Aif2beta From Methanobacterium Thermoautrophicum' 100.00 138 100.00 100.00 2.26e-73 GenBank AAB86235 'translation initiation factor eIF-2, beta subunit [Methanothermobacter thermautotrophicus str. Delta H]' 100.00 135 100.00 100.00 2.59e-73 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 Fri Jun 10 14:23:33 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 $aIF2beta 'Methanothermobacter thermautotrophicus' 145262 Archaea . Methanobacterium thermoautotrophicum 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 $aIF2beta '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 $aIF2beta . mM 1.0 2.0 '[U-13C; U-15N]' $ZN 51 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 $aIF2beta . mM 1.0 2.0 [U-15N] $ZN 51 mM . . . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 800 _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_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label . save_ save_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label . save_ save_1H-13C_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY' _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 HNCACB _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY' _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 310 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 internal 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_shift_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N NOESY' '1H-15N TOCSY' HNCA HNCACB CBCA(CO)NH '1H-13C NOESY' stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name aIF2beta _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 MET CA C 55.7 0.20 1 2 . 1 MET CB C 33.2 0.20 1 3 . 2 ASP CA C 54.7 0.20 1 4 . 2 ASP CB C 41.4 0.20 1 5 . 3 ASP CA C 54.9 0.20 1 6 . 3 ASP CB C 41.1 0.20 1 7 . 4 TYR N N 121.0 0.25 1 8 . 4 TYR H H 8.06 0.01 1 9 . 4 TYR CA C 59.7 0.20 1 10 . 4 TYR HA H 4.33 0.01 1 11 . 4 TYR CB C 38.4 0.20 1 12 . 4 TYR HB2 H 3.06 0.01 2 13 . 5 GLU N N 120.9 0.25 1 14 . 5 GLU H H 8.24 0.01 1 15 . 5 GLU CA C 58.4 0.20 1 16 . 5 GLU HA H 4.05 0.01 1 17 . 5 GLU CB C 29.3 0.20 1 18 . 6 LYS CA C 57.1 0.20 1 19 . 6 LYS CB C 32.6 0.20 1 20 . 7 LEU N N 121.8 0.25 1 21 . 7 LEU H H 7.88 0.01 1 22 . 7 LEU CA C 56.0 0.20 1 23 . 7 LEU HA H 4.08 0.01 1 24 . 7 LEU CB C 42.0 0.20 1 25 . 8 LEU N N 121.8 0.25 1 26 . 8 LEU H H 7.88 0.01 1 27 . 8 LEU CA C 55.4 0.20 1 28 . 8 LEU HA H 4.22 0.01 1 29 . 8 LEU CB C 42.3 0.20 1 30 . 8 LEU HB2 H 1.65 0.01 2 31 . 8 LEU HD1 H 0.86 0.01 2 32 . 9 GLU N N 121.8 0.25 1 33 . 9 GLU H H 8.36 0.01 1 34 . 9 GLU CA C 56.6 0.20 1 35 . 9 GLU HA H 4.35 0.01 1 36 . 9 GLU CB C 30.2 0.20 1 37 . 10 ARG N N 121.1 0.25 1 38 . 10 ARG H H 8.20 0.01 1 39 . 10 ARG CA C 56.1 0.20 1 40 . 10 ARG HA H 4.34 0.01 1 41 . 10 ARG CB C 30.8 0.20 1 42 . 11 ALA N N 125.3 0.25 1 43 . 11 ALA H H 8.14 0.01 1 44 . 11 ALA CA C 52.5 0.20 1 45 . 11 ALA HA H 4.32 0.01 1 46 . 11 ALA CB C 13.5 0.20 1 47 . 11 ALA HB H 1.40 0.01 1 48 . 12 ILE N N 119.3 0.25 1 49 . 12 ILE H H 7.95 0.01 1 50 . 12 ILE CA C 61.7 0.20 1 51 . 12 ILE HA H 4.14 0.01 1 52 . 12 ILE CB C 38.8 0.20 1 53 . 12 ILE HB H 1.88 0.01 1 54 . 12 ILE HG2 H 1.21 0.01 1 55 . 12 ILE HG12 H 0.92 0.01 2 56 . 13 ASP N N 122.7 0.25 1 57 . 13 ASP H H 8.25 0.01 1 58 . 13 ASP CA C 54.4 0.20 1 59 . 13 ASP HA H 4.43 0.01 1 60 . 13 ASP CB C 40.9 0.20 1 61 . 14 GLN CA C 55.3 0.20 1 62 . 14 GLN CB C 29.5 0.20 1 63 . 15 LEU CA C 53.1 0.20 1 64 . 15 LEU HA H 4.59 0.01 1 65 . 15 LEU CB C 41.8 0.20 1 66 . 15 LEU HB2 H 1.47 0.01 2 67 . 15 LEU HB3 H 1.66 0.01 2 68 . 15 LEU CD1 C 17.8 0.20 2 69 . 15 LEU HD1 H 0.88 0.01 2 70 . 16 PRO CD C 50.5 0.20 1 71 . 16 PRO CA C 61.5 0.20 1 72 . 16 PRO HA H 4.71 0.01 1 73 . 16 PRO CB C 31.103 0.20 1 74 . 16 PRO HB2 H 2.37 0.01 2 75 . 16 PRO CG C 21.7 0.20 1 76 . 16 PRO HG2 H 1.97 0.01 2 77 . 16 PRO HG3 H 2.05 0.01 2 78 . 16 PRO HD2 H 3.58 0.01 2 79 . 16 PRO HD3 H 3.86 0.01 2 80 . 17 PRO CA C 63.4 0.20 1 81 . 17 PRO CB C 32.2 0.20 1 82 . 17 PRO HD2 H 3.71 0.01 2 83 . 17 PRO HD3 H 3.83 0.01 2 84 . 18 GLU N N 120.2 0.25 1 85 . 18 GLU H H 8.51 0.01 1 86 . 18 GLU CA C 57.1 0.20 1 87 . 18 GLU HA H 4.22 0.01 1 88 . 18 GLU CB C 29.8 0.20 1 89 . 18 GLU HB2 H 1.89 0.01 2 90 . 19 VAL N N 120.2 0.25 1 91 . 19 VAL H H 7.87 0.01 1 92 . 19 VAL CA C 62.7 0.20 1 93 . 19 VAL HA H 4.06 0.01 1 94 . 19 VAL CB C 27.1 0.20 1 95 . 19 VAL HB H 1.98 0.01 1 96 . 19 VAL CG1 C 15.0 0.20 1 97 . 19 VAL HG1 H 0.82 0.01 2 98 . 19 VAL CG2 C 15.5 0.20 1 99 . 19 VAL HG2 H 0.78 0.01 2 100 . 20 PHE N N 123.5 0.25 1 101 . 20 PHE H H 8.05 0.01 1 102 . 20 PHE CA C 57.8 0.20 1 103 . 20 PHE HA H 4.63 0.01 1 104 . 20 PHE CB C 39.7 0.20 1 105 . 20 PHE HB2 H 3.16 0.01 2 106 . 20 PHE HB3 H 2.96 0.01 2 107 . 21 GLU N N 122.7 0.25 1 108 . 21 GLU H H 8.17 0.01 1 109 . 21 GLU CA C 56.6 0.20 1 110 . 21 GLU HA H 4.33 0.01 1 111 . 21 GLU CB C 30.6 0.20 1 112 . 21 GLU HB2 H 1.97 0.01 2 113 . 21 GLU HB3 H 1.89 0.01 2 114 . 22 THR N N 115.9 0.25 1 115 . 22 THR H H 8.08 0.01 1 116 . 22 THR CA C 69.5 0.20 1 117 . 22 THR HA H 4.34 0.01 1 118 . 22 THR CB C 69.7 0.20 1 119 . 22 THR HB H 4.15 0.01 1 120 . 22 THR CG2 C 16.0 0.20 1 121 . 22 THR HG2 H 1.21 0.01 1 122 . 23 LYS N N 125.1 0.25 1 123 . 23 LYS H H 8.28 0.01 1 124 . 23 LYS CA C 56.1 0.20 1 125 . 23 LYS HA H 4.32 0.01 1 126 . 23 LYS CB C 33.0 0.20 1 127 . 23 LYS HB2 H 1.79 0.01 2 128 . 24 ARG N N 123.7 0.25 1 129 . 24 ARG H H 8.32 0.01 1 130 . 24 ARG CA C 56.0 0.20 1 131 . 24 ARG HA H 4.34 0.01 1 132 . 24 ARG CB C 31.1 0.20 1 133 . 25 PHE N N 124.3 0.25 1 134 . 25 PHE H H 8.37 0.01 1 135 . 25 PHE CA C 58.0 0.20 1 136 . 25 PHE HA H 4.55 0.01 1 137 . 25 PHE CB C 39.9 0.20 1 138 . 25 PHE HB2 H 3.07 0.01 2 139 . 25 PHE HB3 H 2.87 0.01 2 140 . 25 PHE HD1 H 7.18 0.01 3 141 . 26 GLU N N 127.8 0.25 1 142 . 26 GLU H H 7.73 0.01 1 143 . 26 GLU CA C 54.5 0.20 1 144 . 26 GLU HA H 4.22 0.01 1 145 . 26 GLU CB C 31.1 0.20 1 146 . 26 GLU HB2 H 2.06 0.01 2 147 . 26 GLU HB3 H 1.70 0.01 2 148 . 27 VAL N N 126.1 0.25 1 149 . 27 VAL H H 8.17 0.01 1 150 . 27 VAL CA C 60.4 0.20 1 151 . 27 VAL HA H 3.75 0.01 1 152 . 27 VAL CB C 26.3 0.20 1 153 . 27 VAL HB H 1.97 0.01 1 154 . 29 LYS N N 120.0 0.25 1 155 . 29 LYS H H 7.89 0.01 1 156 . 29 LYS HA H 4.31 0.01 1 157 . 30 ALA N N 126.1 0.25 1 158 . 30 ALA H H 9.29 0.01 1 159 . 30 ALA CA C 51.7 0.20 1 160 . 30 ALA HA H 4.92 0.01 1 161 . 30 ALA CB C 13.7 0.20 1 162 . 30 ALA HB H 1.53 0.01 1 163 . 31 TYR N N 126.1 0.25 1 164 . 31 TYR H H 9.27 0.01 1 165 . 31 TYR CA C 56.9 0.20 1 166 . 31 TYR HA H 4.82 0.01 1 167 . 31 TYR CB C 38.9 0.20 1 168 . 31 TYR HB2 H 4.15 0.01 2 169 . 31 TYR HB3 H 2.99 0.01 2 170 . 32 SER N N 120.1 0.25 1 171 . 32 SER H H 8.11 0.01 1 172 . 32 SER CA C 56.299 0.20 1 173 . 32 SER HA H 5.89 0.01 1 174 . 32 SER CB C 67.5 0.20 1 175 . 32 SER HB2 H 3.35 0.01 2 176 . 32 SER HB3 H 3.75 0.01 2 177 . 33 VAL N N 118.4 0.25 1 178 . 33 VAL H H 8.76 0.01 1 179 . 33 VAL CA C 60.2 0.20 1 180 . 33 VAL HA H 4.58 0.01 1 181 . 33 VAL CB C 36.3 0.20 1 182 . 33 VAL HB H 2.09 0.01 1 183 . 33 VAL CG1 C 14.7 0.20 1 184 . 33 VAL HG1 H 0.93 0.01 2 185 . 33 VAL CG2 C 15.4 0.20 1 186 . 33 VAL HG2 H 1.00 0.01 2 187 . 34 ILE N N 127.0 0.25 1 188 . 34 ILE H H 8.51 0.01 1 189 . 34 ILE CA C 61.1 0.20 1 190 . 34 ILE HA H 4.82 0.01 1 191 . 34 ILE CB C 39.4 0.20 1 192 . 34 ILE HB H 1.69 0.01 1 193 . 34 ILE CG2 C 11.8 0.20 2 194 . 34 ILE HG2 H 0.91 0.01 1 195 . 34 ILE CD1 C 8.7 0.20 1 196 . 34 ILE HD1 H 0.73 0.01 1 197 . 35 GLN N N 129.4 0.25 1 198 . 35 GLN H H 8.91 0.01 1 199 . 35 GLN CA C 55.0 0.20 1 200 . 35 GLN HA H 4.62 0.01 1 201 . 35 GLN CB C 30.9 0.20 1 202 . 35 GLN HB2 H 2.18 0.01 2 203 . 36 GLY N N 118.5 0.25 1 204 . 36 GLY H H 9.02 0.01 1 205 . 36 GLY CA C 47.4 0.20 1 206 . 36 GLY HA2 H 3.96 0.01 2 207 . 36 GLY HA3 H 3.65 0.01 2 208 . 37 ASN N N 125.3 0.25 1 209 . 37 ASN H H 8.66 0.01 1 210 . 37 ASN CA C 52.0 0.20 1 211 . 37 ASN HA H 4.83 0.01 1 212 . 37 ASN CB C 38.7 0.20 1 213 . 37 ASN HB2 H 2.67 0.01 2 214 . 37 ASN HB3 H 2.97 0.01 2 215 . 38 ARG N N 118.4 0.25 1 216 . 38 ARG H H 7.65 0.01 1 217 . 38 ARG CA C 55.3 0.20 1 218 . 38 ARG HA H 5.18 0.01 1 219 . 38 ARG CB C 35.3 0.20 1 220 . 38 ARG HB2 H 1.79 0.01 2 221 . 38 ARG HB3 H 2.96 0.01 2 222 . 38 ARG CG C 21.8 0.20 1 223 . 38 ARG HG2 H 1.66 0.01 2 224 . 38 ARG CD C 44.1 0.20 1 225 . 38 ARG HD2 H 3.20 0.01 2 226 . 38 ARG HD3 H 2.96 0.01 2 227 . 39 THR N N 115.9 0.25 1 228 . 39 THR H H 8.82 0.01 1 229 . 39 THR CA C 62.4 0.20 1 230 . 39 THR HA H 5.01 0.01 1 231 . 39 THR CB C 71.6 0.20 1 232 . 39 THR HB H 3.95 0.01 1 233 . 39 THR CG2 C 21.034 0.20 1 234 . 39 THR HG2 H 1.30 0.01 1 235 . 40 PHE N N 126.9 0.25 1 236 . 40 PHE H H 9.61 0.01 1 237 . 40 PHE CA C 55.5 0.20 1 238 . 40 PHE HA H 5.21 0.01 1 239 . 40 PHE CB C 40.7 0.20 1 240 . 40 PHE HB2 H 2.77 0.01 2 241 . 40 PHE HB3 H 3.16 0.01 2 242 . 40 PHE HD2 H 7.12 0.01 3 243 . 41 ILE N N 122.7 0.25 1 244 . 41 ILE H H 9.55 0.01 1 245 . 41 ILE CA C 61.5 0.20 1 246 . 41 ILE HA H 4.62 0.01 1 247 . 41 ILE CB C 37.1 0.20 1 248 . 41 ILE HB H 2.00 0.01 1 249 . 41 ILE CG2 C 13.2 0.20 2 250 . 41 ILE HG2 H 1.11 0.01 1 251 . 41 ILE HG12 H 0.91 0.01 2 252 . 41 ILE CD1 C 8.7 0.20 1 253 . 41 ILE HD1 H 0.72 0.01 1 254 . 42 GLN N N 126.1 0.25 1 255 . 42 GLN H H 8.91 0.01 1 256 . 42 GLN CA C 58.7 0.20 1 257 . 42 GLN HA H 4.42 0.01 1 258 . 42 GLN CB C 30.1 0.20 1 259 . 43 ASN N N 116.8 0.25 1 260 . 43 ASN H H 8.53 0.01 1 261 . 43 ASN CA C 51.6 0.20 1 262 . 43 ASN HA H 5.41 0.01 1 263 . 43 ASN CB C 37.5 0.20 1 264 . 43 ASN HB2 H 3.26 0.01 2 265 . 43 ASN HB3 H 2.69 0.01 2 266 . 44 PHE N N 120.1 0.25 1 267 . 44 PHE H H 7.05 0.01 1 268 . 44 PHE CA C 63.9 0.20 1 269 . 44 PHE HA H 3.67 0.01 1 270 . 44 PHE CB C 40.7 0.20 1 271 . 44 PHE HB2 H 2.95 0.01 2 272 . 44 PHE HB3 H 3.05 0.01 2 273 . 45 ARG N N 117.6 0.25 1 274 . 45 ARG H H 8.34 0.01 1 275 . 45 ARG CA C 59.6 0.20 1 276 . 45 ARG HA H 3.74 0.01 1 277 . 45 ARG CB C 24.0 0.20 1 278 . 45 ARG HB2 H 2.06 0.01 2 279 . 45 ARG CG C 27.47 0.20 1 280 . 45 ARG HG2 H 1.74 0.01 2 281 . 45 ARG CD C 43.1 0.20 1 282 . 45 ARG HD2 H 3.29 0.01 2 283 . 46 GLU N N 120.0 0.25 1 284 . 46 GLU H H 7.99 0.01 1 285 . 46 GLU CA C 60.0 0.20 1 286 . 46 GLU HA H 4.09 0.01 1 287 . 46 GLU CB C 23.6 0.20 1 288 . 46 GLU HB2 H 2.17 0.01 2 289 . 46 GLU CG C 37.0 0.20 1 290 . 46 GLU HG2 H 2.37 0.01 2 291 . 47 VAL N N 121.8 0.25 1 292 . 47 VAL H H 7.71 0.01 1 293 . 47 VAL CA C 66.7 0.20 1 294 . 47 VAL HA H 3.33 0.01 1 295 . 47 VAL CB C 25.3 0.20 1 296 . 47 VAL HB H 1.89 0.01 1 297 . 47 VAL CG1 C 15.1 0.20 1 298 . 47 VAL HG1 H 0.53 0.01 2 299 . 47 VAL CG2 C 16.4 0.20 1 300 . 47 VAL HG2 H 0.72 0.01 2 301 . 48 ALA N N 121.0 0.25 1 302 . 48 ALA H H 7.56 0.01 1 303 . 48 ALA CA C 55.9 0.20 1 304 . 48 ALA HA H 3.55 0.01 1 305 . 48 ALA CB C 11.3 0.20 1 306 . 48 ALA HB H 1.19 0.01 1 307 . 49 ASP N N 118.4 0.25 1 308 . 49 ASP H H 8.93 0.01 1 309 . 49 ASP CA C 57.2 0.20 1 310 . 49 ASP HA H 4.53 0.01 1 311 . 49 ASP CB C 40.1 0.20 1 312 . 49 ASP HB2 H 2.64 0.01 2 313 . 49 ASP HB3 H 2.78 0.01 2 314 . 50 ALA N N 124.4 0.25 1 315 . 50 ALA H H 7.95 0.01 1 316 . 50 ALA CA C 54.7 0.20 1 317 . 50 ALA HA H 4.23 0.01 1 318 . 50 ALA CB C 12.5 0.20 1 319 . 50 ALA HB H 1.60 0.01 1 320 . 51 LEU N N 115.1 0.25 1 321 . 51 LEU H H 7.41 0.01 1 322 . 51 LEU CA C 54.1 0.20 1 323 . 51 LEU HA H 4.33 0.01 1 324 . 51 LEU CB C 42.3 0.20 1 325 . 51 LEU HB2 H 1.88 0.01 2 326 . 51 LEU CG C 21.4 0.20 1 327 . 51 LEU HG H 1.60 0.01 1 328 . 51 LEU CD1 C 18.4 0.20 2 329 . 51 LEU HD1 H 1.01 0.01 2 330 . 51 LEU CD2 C 20.5 0.20 2 331 . 51 LEU HD2 H 1.20 0.01 2 332 . 52 ASN N N 117.6 0.25 1 333 . 52 ASN H H 8.18 0.01 1 334 . 52 ASN CA C 54.0 0.20 1 335 . 52 ASN HA H 4.43 0.01 1 336 . 52 ASN CB C 37.3 0.20 1 337 . 52 ASN HB2 H 3.25 0.01 2 338 . 52 ASN HB3 H 2.86 0.01 2 339 . 53 ARG N N 118.5 0.25 1 340 . 53 ARG H H 8.05 0.01 1 341 . 53 ARG CA C 51.9 0.20 1 342 . 53 ARG HA H 4.86 0.01 1 343 . 53 ARG CB C 33.9 0.20 1 344 . 54 ASP N N 123.5 0.25 1 345 . 54 ASP H H 8.48 0.01 1 346 . 54 ASP CA C 51.5 0.20 1 347 . 54 ASP HA H 4.74 0.01 1 348 . 54 ASP CB C 42.0 0.20 1 349 . 55 PRO CA C 65.4 0.20 1 350 . 55 PRO HA H 4.00 0.01 1 351 . 55 PRO CB C 26.8 0.20 1 352 . 55 PRO HB2 H 2.15 0.01 2 353 . 56 GLN N N 115.9 0.25 1 354 . 56 GLN H H 8.73 0.01 1 355 . 56 GLN CA C 59.0 0.20 1 356 . 56 GLN CB C 28.3 0.20 1 357 . 56 GLN HB2 H 2.18 0.01 2 358 . 56 GLN HB3 H 2.09 0.01 2 359 . 56 GLN HG2 H 2.56 0.01 2 360 . 56 GLN HG3 H 2.38 0.01 2 361 . 57 HIS N N 122.7 0.25 1 362 . 57 HIS H H 7.67 0.01 1 363 . 57 HIS CA C 61.7 0.20 1 364 . 57 HIS HA H 4.04 0.01 1 365 . 57 HIS CB C 25.7 0.20 1 366 . 57 HIS HB2 H 3.26 0.01 2 367 . 58 LEU N N 119.4 0.25 1 368 . 58 LEU H H 7.05 0.01 1 369 . 58 LEU CA C 57.8 0.20 1 370 . 58 LEU HA H 3.67 0.01 1 371 . 58 LEU CB C 41.0 0.20 1 372 . 58 LEU HB2 H 1.61 0.01 2 373 . 58 LEU CG C 21.6 0.20 1 374 . 58 LEU HG H 1.11 0.01 1 375 . 58 LEU CD1 C 25.322 0.20 2 376 . 58 LEU HD1 H -0.07 0.01 2 377 . 58 LEU CD2 C 19.5 0.20 2 378 . 58 LEU HD2 H 0.06 0.01 2 379 . 59 LEU N N 118.5 0.25 1 380 . 59 LEU H H 8.62 0.01 1 381 . 59 LEU CA C 58.5 0.20 1 382 . 59 LEU CB C 41.2 0.20 1 383 . 60 LYS N N 118.4 0.25 1 384 . 60 LYS H H 8.05 0.01 1 385 . 60 LYS CA C 60.5 0.20 1 386 . 60 LYS CB C 32.1 0.20 1 387 . 61 PHE N N 119.3 0.25 1 388 . 61 PHE H H 7.54 0.01 1 389 . 61 PHE CA C 61.7 0.20 1 390 . 61 PHE HA H 4.13 0.01 1 391 . 61 PHE CB C 38.9 0.20 1 392 . 61 PHE HB2 H 3.27 0.01 2 393 . 61 PHE HB3 H 2.97 0.01 2 394 . 61 PHE HD1 H 6.21 0.01 3 395 . 62 LEU N N 120.1 0.25 1 396 . 62 LEU H H 8.15 0.01 1 397 . 62 LEU CA C 58.5 0.20 1 398 . 62 LEU HA H 4.06 0.01 1 399 . 62 LEU CB C 42.0 0.20 1 400 . 63 LEU N N 116.9 0.25 1 401 . 63 LEU H H 8.82 0.01 1 402 . 63 LEU CA C 58.2 0.20 1 403 . 63 LEU CB C 39.5 0.20 1 404 . 64 ARG N N 118.5 0.25 1 405 . 64 ARG H H 7.57 0.01 1 406 . 64 ARG CA C 58.6 0.20 1 407 . 64 ARG HA H 4.10 0.01 1 408 . 64 ARG CB C 30.0 0.20 1 409 . 64 ARG HB2 H 1.90 0.01 2 410 . 65 GLU N N 118.5 0.25 1 411 . 65 GLU H H 8.09 0.01 1 412 . 65 GLU CA C 58.3 0.20 1 413 . 65 GLU HA H 3.80 0.01 1 414 . 65 GLU CB C 29.8 0.20 1 415 . 66 LEU N N 116.8 0.25 1 416 . 66 LEU H H 8.24 0.01 1 417 . 66 LEU CA C 55.1 0.20 1 418 . 66 LEU HA H 4.14 0.01 1 419 . 66 LEU CB C 41.3 0.20 1 420 . 66 LEU HB2 H 0.93 0.01 2 421 . 66 LEU HB3 H 1.26 0.01 2 422 . 66 LEU CG C 21.2 0.20 1 423 . 66 LEU HG H 1.38 0.01 1 424 . 66 LEU CD1 C 19.3 0.20 2 425 . 66 LEU HD1 H -0.07 0.01 2 426 . 66 LEU CD2 C 16.4 0.20 2 427 . 66 LEU HD2 H 0.42 0.01 2 428 . 67 GLY N N 110.0 0.25 1 429 . 67 GLY H H 7.47 0.01 1 430 . 67 GLY CA C 46.9 0.20 1 431 . 67 GLY HA2 H 3.86 0.01 2 432 . 68 THR N N 113.3 0.25 1 433 . 68 THR H H 7.84 0.01 1 434 . 68 THR CA C 57.9 0.20 1 435 . 68 THR HA H 4.92 0.01 1 436 . 68 THR CB C 71.0 0.20 1 437 . 68 THR HB H 3.93 0.01 1 438 . 68 THR CG2 C 18.982 0.20 1 439 . 68 THR HG2 H 1.01 0.01 1 440 . 69 ALA N N 124.4 0.25 1 441 . 69 ALA H H 8.33 0.01 1 442 . 69 ALA CA C 50.3 0.20 1 443 . 69 ALA HA H 4.82 0.01 1 444 . 69 ALA CB C 16.4 0.20 1 445 . 69 ALA HB H 1.40 0.01 1 446 . 70 GLY N N 106.6 0.25 1 447 . 70 GLY H H 7.86 0.01 1 448 . 70 GLY CA C 46.8 0.20 1 449 . 70 GLY HA2 H 4.43 0.01 2 450 . 70 GLY HA3 H 4.23 0.01 2 451 . 71 ASN N N 113.4 0.25 1 452 . 71 ASN H H 8.59 0.01 1 453 . 71 ASN CA C 52.9 0.20 1 454 . 71 ASN HA H 4.87 0.01 1 455 . 71 ASN CB C 42.4 0.20 1 456 . 71 ASN HB2 H 2.72 0.01 2 457 . 71 ASN HB3 H 2.65 0.01 2 458 . 72 LEU N N 121.0 0.25 1 459 . 72 LEU H H 8.54 0.01 1 460 . 72 LEU CA C 54.0 0.20 1 461 . 72 LEU HA H 4.82 0.01 1 462 . 72 LEU CB C 43.6 0.20 1 463 . 72 LEU HB2 H 1.59 0.01 2 464 . 72 LEU CD1 C 19.6 0.20 2 465 . 72 LEU HD1 H 0.62 0.01 2 466 . 73 GLU N N 125.3 0.25 1 467 . 73 GLU H H 8.46 0.01 1 468 . 73 GLU CA C 55.1 0.20 1 469 . 73 GLU HA H 4.43 0.01 1 470 . 73 GLU CB C 32.1 0.20 1 471 . 73 GLU HB2 H 1.88 0.01 2 472 . 73 GLU HB3 H 1.71 0.01 2 473 . 74 GLY N N 118.4 0.25 1 474 . 74 GLY H H 9.08 0.01 1 475 . 74 GLY CA C 47.2 0.20 1 476 . 74 GLY HA2 H 3.94 0.01 2 477 . 74 GLY HA3 H 3.64 0.01 2 478 . 75 GLY N N 115.0 0.25 1 479 . 75 GLY H H 9.01 0.01 1 480 . 75 GLY CA C 45.9 0.20 1 481 . 75 GLY HA2 H 4.24 0.01 2 482 . 75 GLY HA3 H 4.03 0.01 2 483 . 76 ARG N N 119.3 0.25 1 484 . 76 ARG H H 8.20 0.01 1 485 . 76 ARG CA C 54.6 0.20 1 486 . 76 ARG HA H 5.21 0.01 1 487 . 76 ARG CB C 33.74 0.20 1 488 . 76 ARG HB2 H 2.08 0.01 2 489 . 76 ARG HB3 H 1.78 0.01 2 490 . 76 ARG HG2 H 1.61 0.01 2 491 . 76 ARG CD C 40.8 0.20 1 492 . 76 ARG HD2 H 2.96 0.01 2 493 . 76 ARG HD3 H 3.22 0.01 2 494 . 77 ALA N N 121.0 0.25 1 495 . 77 ALA H H 7.80 0.01 1 496 . 77 ALA CA C 50.3 0.20 1 497 . 77 ALA HA H 4.84 0.01 1 498 . 77 ALA CB C 16.0 0.20 1 499 . 77 ALA HB H 0.32 0.01 1 500 . 78 ILE N N 122.7 0.25 1 501 . 78 ILE H H 8.71 0.01 1 502 . 78 ILE CA C 60.8 0.20 1 503 . 78 ILE HA H 4.34 0.01 1 504 . 78 ILE CB C 39.5 0.20 1 505 . 78 ILE HB H 1.59 0.01 1 506 . 78 ILE CG2 C 12.5 0.20 2 507 . 78 ILE HG2 H 0.33 0.01 1 508 . 78 ILE HG12 H 1.20 0.01 2 509 . 78 ILE CD1 C 8.8 0.20 1 510 . 78 ILE HD1 H 0.71 0.01 1 511 . 79 LEU N N 126.1 0.25 1 512 . 79 LEU H H 9.30 0.01 1 513 . 79 LEU CA C 53.1 0.20 1 514 . 79 LEU HA H 4.92 0.01 1 515 . 79 LEU CB C 44.0 0.20 1 516 . 79 LEU HB2 H 1.77 0.01 2 517 . 79 LEU HB3 H 1.40 0.01 2 518 . 79 LEU CD1 C 18.6 0.20 2 519 . 79 LEU HD1 H 0.35 0.01 2 520 . 79 LEU CD2 C 19.5 0.20 2 521 . 79 LEU HD2 H 0.42 0.01 2 522 . 80 GLN N N 121.1 0.25 1 523 . 80 GLN H H 8.54 0.01 1 524 . 80 GLN CA C 56.3 0.20 1 525 . 80 GLN HA H 4.33 0.01 1 526 . 80 GLN CB C 27.4 0.20 1 527 . 80 GLN HB2 H 1.99 0.01 2 528 . 80 GLN HB3 H 2.20 0.01 2 529 . 81 GLY N N 115.9 0.25 1 530 . 81 GLY H H 8.28 0.01 1 531 . 81 GLY CA C 43.9 0.20 1 532 . 81 GLY HA2 H 4.14 0.01 2 533 . 81 GLY HA3 H 3.55 0.01 2 534 . 82 LYS N N 117.7 0.25 1 535 . 82 LYS H H 7.45 0.01 1 536 . 82 LYS CA C 55.3 0.20 1 537 . 82 LYS HA H 3.84 0.01 1 538 . 82 LYS CB C 32.9 0.20 1 539 . 82 LYS HB2 H 1.572 0.01 2 540 . 83 PHE N N 122.7 0.25 1 541 . 83 PHE H H 8.20 0.01 1 542 . 83 PHE CA C 55.9 0.20 1 543 . 83 PHE HA H 4.92 0.01 1 544 . 83 PHE CB C 42.2 0.20 1 545 . 83 PHE HB2 H 2.57 0.01 2 546 . 83 PHE HB3 H 2.94 0.01 2 547 . 84 THR N N 111.7 0.25 1 548 . 84 THR H H 8.13 0.01 1 549 . 84 THR CA C 60.7 0.20 1 550 . 84 THR HA H 4.33 0.01 1 551 . 84 THR CB C 71.6 0.20 1 552 . 84 THR HB H 4.62 0.01 1 553 . 84 THR CG2 C 16.2 0.20 1 554 . 84 THR HG2 H 1.46 0.01 1 555 . 85 HIS CA C 59.1 0.20 1 556 . 85 HIS HA H 4.31 0.01 1 557 . 85 HIS CB C 24.2 0.20 1 558 . 85 HIS HB2 H 3.27 0.01 2 559 . 85 HIS HB3 H 3.20 0.01 2 560 . 86 PHE N N 119.3 0.25 1 561 . 86 PHE H H 6.95 0.01 1 562 . 86 PHE HA H 4.62 0.01 1 563 . 86 PHE CB C 38.7 0.20 1 564 . 86 PHE HB2 H 3.16 0.01 2 565 . 86 PHE HB3 H 2.96 0.01 2 566 . 87 LEU N N 122.7 0.25 1 567 . 87 LEU H H 7.37 0.01 1 568 . 87 LEU CA C 58.0 0.20 1 569 . 87 LEU HA H 4.20 0.01 1 570 . 87 LEU CB C 42.2 0.20 1 571 . 88 ILE N N 118.0 0.25 1 572 . 88 ILE H H 7.93 0.01 1 573 . 88 ILE CA C 64.8 0.20 1 574 . 88 ILE HA H 3.37 0.01 1 575 . 88 ILE CB C 37.4 0.20 1 576 . 88 ILE HB H 1.89 0.01 1 577 . 88 ILE CG2 C 17.37 0.20 2 578 . 88 ILE HG2 H 0.72 0.01 1 579 . 88 ILE CD1 C 12.47 0.20 1 580 . 88 ILE HD1 H 0.64 0.01 1 581 . 89 ASN N N 117.6 0.25 1 582 . 89 ASN H H 8.12 0.01 1 583 . 89 ASN CA C 58.3 0.20 1 584 . 89 ASN HA H 4.33 0.01 1 585 . 89 ASN CB C 38.8 0.20 1 586 . 89 ASN HB2 H 2.77 0.01 2 587 . 90 GLU N N 122.9 0.25 1 588 . 90 GLU H H 8.22 0.01 1 589 . 90 GLU CA C 60.2 0.20 1 590 . 90 GLU CB C 29.4 0.20 1 591 . 91 ARG N N 117.6 0.25 1 592 . 91 ARG H H 7.93 0.01 1 593 . 91 ARG CA C 57.8 0.20 1 594 . 91 ARG CB C 31.3 0.20 1 595 . 92 ILE N N 121.9 0.25 1 596 . 92 ILE H H 8.28 0.01 1 597 . 92 ILE CA C 65.6 0.20 1 598 . 92 ILE HA H 3.74 0.01 1 599 . 92 ILE CB C 37.1 0.20 1 600 . 92 ILE HB H 2.19 0.01 1 601 . 92 ILE CD1 C 13.17 0.20 1 602 . 92 ILE HD1 H 0.74 0.01 1 603 . 93 GLU N N 121.8 0.25 1 604 . 93 GLU H H 8.20 0.01 1 605 . 93 GLU CA C 60.8 0.20 1 606 . 93 GLU CB C 28.7 0.20 1 607 . 94 ASP N N 120.3 0.25 1 608 . 94 ASP H H 7.76 0.01 1 609 . 94 ASP CA C 57.7 0.20 1 610 . 95 TYR N N 121.1 0.25 1 611 . 95 TYR H H 8.36 0.01 1 612 . 95 TYR CA C 62.1 0.20 1 613 . 95 TYR CB C 37.1 0.20 1 614 . 96 VAL N N 121.0 0.25 1 615 . 96 VAL H H 8.69 0.01 1 616 . 96 VAL CA C 66.2 0.20 1 617 . 96 VAL HA H 3.84 0.01 1 618 . 96 VAL CB C 31.7 0.20 1 619 . 97 ASN N N 119.4 0.25 1 620 . 97 ASN H H 8.05 0.01 1 621 . 97 ASN CA C 56.1 0.20 1 622 . 97 ASN HA H 4.43 0.01 1 623 . 97 ASN CB C 38.8 0.20 1 624 . 98 LYS N N 118.5 0.25 1 625 . 98 LYS H H 7.78 0.01 1 626 . 98 LYS CA C 58.5 0.20 1 627 . 98 LYS HA H 4.04 0.01 1 628 . 98 LYS CB C 35.4 0.20 1 629 . 98 LYS HB2 H 1.23 0.01 2 630 . 99 PHE N N 112.5 0.25 1 631 . 99 PHE H H 8.63 0.01 1 632 . 99 PHE CA C 58.2 0.20 1 633 . 99 PHE HA H 4.53 0.01 1 634 . 99 PHE CB C 40.1 0.20 1 635 . 100 VAL N N 118.5 0.25 1 636 . 100 VAL H H 7.54 0.01 1 637 . 100 VAL CA C 64.3 0.20 1 638 . 100 VAL HA H 3.95 0.01 1 639 . 100 VAL CB C 33.9 0.20 1 640 . 101 ILE N N 120.2 0.25 1 641 . 101 ILE H H 7.75 0.01 1 642 . 101 ILE CA C 60.7 0.20 1 643 . 101 ILE HA H 4.43 0.01 1 644 . 101 ILE CB C 37.6 0.20 1 645 . 101 ILE HB H 2.38 0.01 1 646 . 102 CYS N N 128.7 0.25 1 647 . 102 CYS H H 8.24 0.01 1 648 . 102 CYS CA C 59.5 0.20 1 649 . 102 CYS HA H 4.63 0.01 1 650 . 102 CYS CB C 31.2 0.20 1 651 . 103 HIS N N 127.8 0.25 1 652 . 103 HIS H H 9.04 0.01 1 653 . 103 HIS CA C 57.2 0.20 1 654 . 103 HIS HA H 4.47 0.01 1 655 . 103 HIS CB C 28.0 0.20 1 656 . 103 HIS HB2 H 3.36 0.01 2 657 . 104 GLU N N 121.9 0.25 1 658 . 104 GLU H H 9.31 0.01 1 659 . 104 GLU CA C 57.9 0.20 1 660 . 104 GLU HA H 4.43 0.01 1 661 . 104 GLU CB C 30.1 0.20 1 662 . 104 GLU HB2 H 1.88 0.01 2 663 . 104 GLU HG2 H 2.09 0.01 2 664 . 105 CYS N N 119.3 0.25 1 665 . 105 CYS H H 8.58 0.01 1 666 . 105 CYS CA C 58.8 0.20 1 667 . 105 CYS HA H 4.92 0.01 1 668 . 105 CYS CB C 37.6 0.20 1 669 . 105 CYS HB2 H 3.15 0.01 2 670 . 105 CYS HB3 H 2.58 0.01 2 671 . 106 ASN N N 118.5 0.25 1 672 . 106 ASN H H 7.96 0.01 1 673 . 106 ASN CA C 55.2 0.20 1 674 . 106 ASN HA H 4.47 0.01 1 675 . 106 ASN CB C 37.6 0.20 1 676 . 106 ASN HB2 H 2.87 0.01 2 677 . 107 ARG N N 118.4 0.25 1 678 . 107 ARG H H 7.99 0.01 1 679 . 107 ARG CA C 54.0 0.20 1 680 . 107 ARG HA H 4.72 0.01 1 681 . 107 ARG CB C 30.6 0.20 1 682 . 108 PRO CA C 62.7 0.20 1 683 . 108 PRO CB C 30.7 0.20 1 684 . 109 ASP N N 123.6 0.25 1 685 . 109 ASP H H 6.93 0.01 1 686 . 109 ASP CA C 53.5 0.20 1 687 . 109 ASP HA H 4.81 0.01 1 688 . 109 ASP CB C 39.8 0.20 1 689 . 109 ASP HB2 H 2.76 0.01 2 690 . 109 ASP HB3 H 2.38 0.01 2 691 . 110 THR N N 110.0 0.25 1 692 . 110 THR H H 8.23 0.01 1 693 . 110 THR CA C 59.0 0.20 1 694 . 110 THR HA H 5.42 0.01 1 695 . 110 THR CB C 73.0 0.20 1 696 . 110 THR HB H 3.86 0.01 1 697 . 110 THR HG2 H 1.11 0.01 1 698 . 111 ARG N N 121.8 0.25 1 699 . 111 ARG H H 9.29 0.01 1 700 . 111 ARG CA C 54.3 0.20 1 701 . 111 ARG HA H 4.72 0.01 1 702 . 111 ARG CB C 33.9 0.20 1 703 . 112 ILE N N 122.7 0.25 1 704 . 112 ILE H H 8.58 0.01 1 705 . 112 ILE CA C 61.2 0.20 1 706 . 112 ILE HA H 4.80 0.01 1 707 . 112 ILE CB C 38.0 0.20 1 708 . 112 ILE HB H 1.60 0.01 1 709 . 112 ILE HG12 H 0.64 0.01 2 710 . 113 ILE N N 126.2 0.25 1 711 . 113 ILE H H 9.25 0.01 1 712 . 113 ILE CA C 59.2 0.20 1 713 . 113 ILE HA H 4.72 0.01 1 714 . 113 ILE CB C 41.2 0.20 1 715 . 114 ARG N N 122.7 0.25 1 716 . 114 ARG H H 8.43 0.01 1 717 . 114 ARG CA C 54.9 0.20 1 718 . 114 ARG HA H 5.11 0.01 1 719 . 114 ARG CB C 32.2 0.20 1 720 . 114 ARG HB2 H 1.72 0.01 2 721 . 114 ARG HB3 H 1.51 0.01 2 722 . 114 ARG HG2 H 1.88 0.01 2 723 . 115 GLU N N 126.9 0.25 1 724 . 115 GLU H H 8.55 0.01 1 725 . 115 GLU CA C 55.4 0.20 1 726 . 115 GLU HA H 4.51 0.01 1 727 . 115 GLU CB C 31.1 0.20 1 728 . 115 GLU HB2 H 2.09 0.01 2 729 . 115 GLU HB3 H 1.75 0.01 2 730 . 116 GLY N N 116.3 0.25 1 731 . 116 GLY H H 8.83 0.01 1 732 . 116 GLY CA C 47.1 0.20 1 733 . 117 ARG N N 125.3 0.25 1 734 . 117 ARG H H 8.91 0.01 1 735 . 117 ARG CA C 56.5 0.20 1 736 . 117 ARG HA H 4.33 0.01 1 737 . 117 ARG CB C 30.5 0.20 1 738 . 118 ILE N N 119.3 0.25 1 739 . 118 ILE H H 7.81 0.01 1 740 . 118 ILE CA C 60.1 0.20 1 741 . 118 ILE HA H 4.53 0.01 1 742 . 118 ILE CB C 40.5 0.20 1 743 . 118 ILE HB H 2.16 0.01 1 744 . 118 ILE HG2 H 0.91 0.01 1 745 . 118 ILE HG12 H 1.30 0.01 2 746 . 118 ILE HD1 H 0.81 0.01 1 747 . 119 SER N N 121.0 0.25 1 748 . 119 SER H H 8.57 0.01 1 749 . 119 SER CA C 57.9 0.20 1 750 . 119 SER HA H 5.32 0.01 1 751 . 119 SER CB C 64.8 0.20 1 752 . 119 SER HB2 H 3.82 0.01 2 753 . 119 SER HB3 H 3.67 0.01 2 754 . 120 LEU N N 123.5 0.25 1 755 . 120 LEU H H 9.20 0.01 1 756 . 120 LEU CA C 53.9 0.20 1 757 . 120 LEU HA H 5.01 0.01 1 758 . 120 LEU CB C 45.8 0.20 1 759 . 121 LEU N N 123.7 0.25 1 760 . 121 LEU H H 9.13 0.01 1 761 . 121 LEU CA C 53.8 0.20 1 762 . 121 LEU HA H 4.72 0.01 1 763 . 121 LEU CB C 43.7 0.20 1 764 . 122 LYS N N 129.5 0.25 1 765 . 122 LYS H H 9.24 0.01 1 766 . 122 LYS CA C 54.0 0.20 1 767 . 122 LYS HA H 5.01 0.01 1 768 . 122 LYS CB C 35.4 0.20 1 769 . 123 CYS N N 131.1 0.25 1 770 . 123 CYS H H 9.19 0.01 1 771 . 123 CYS CA C 59.1 0.20 1 772 . 123 CYS HA H 4.53 0.01 1 773 . 123 CYS CB C 32.7 0.20 1 774 . 123 CYS HB2 H 3.26 0.01 2 775 . 123 CYS HB3 H 2.67 0.01 2 776 . 124 GLU N N 129.5 0.25 1 777 . 124 GLU H H 9.22 0.01 1 778 . 124 GLU CA C 57.1 0.20 1 779 . 124 GLU HA H 4.24 0.01 1 780 . 124 GLU CB C 29.6 0.20 1 781 . 124 GLU HB2 H 1.88 0.01 2 782 . 124 GLU HG2 H 2.26 0.01 2 783 . 124 GLU HG3 H 2.11 0.01 2 784 . 125 ALA N N 126.1 0.25 1 785 . 125 ALA H H 9.21 0.01 1 786 . 125 ALA CA C 54.5 0.20 1 787 . 125 ALA HA H 4.44 0.01 1 788 . 125 ALA CB C 20.3 0.20 1 789 . 125 ALA HB H 1.48 0.01 1 790 . 126 CYS N N 121.0 0.25 1 791 . 126 CYS H H 9.62 0.01 1 792 . 126 CYS CA C 58.7 0.20 1 793 . 126 CYS HA H 5.01 0.01 1 794 . 126 CYS CB C 32.7 0.20 1 795 . 126 CYS HB2 H 3.26 0.01 2 796 . 126 CYS HB3 H 2.58 0.01 2 797 . 127 GLY N N 113.3 0.25 1 798 . 127 GLY H H 7.31 0.01 1 799 . 127 GLY CA C 46.0 0.20 1 800 . 127 GLY HA2 H 3.84 0.01 2 801 . 127 GLY HA3 H 3.75 0.01 2 802 . 128 ALA N N 127.0 0.25 1 803 . 128 ALA H H 8.88 0.01 1 804 . 128 ALA CA C 53.9 0.20 1 805 . 128 ALA HA H 4.13 0.01 1 806 . 128 ALA CB C 20.8 0.20 1 807 . 128 ALA HB H 1.40 0.01 1 808 . 129 LYS N N 120.1 0.25 1 809 . 129 LYS H H 8.21 0.01 1 810 . 129 LYS CA C 54.8 0.20 1 811 . 129 LYS HA H 5.40 0.01 1 812 . 129 LYS CB C 35.5 0.20 1 813 . 129 LYS HB2 H 1.60 0.01 2 814 . 130 ALA N N 126.9 0.25 1 815 . 130 ALA H H 8.52 0.01 1 816 . 130 ALA CA C 49.2 0.20 1 817 . 130 ALA HA H 5.01 0.01 1 818 . 130 ALA CB C 21.3 0.20 1 819 . 130 ALA HB H 1.40 0.01 1 820 . 131 PRO CA C 63.1 0.20 1 821 . 131 PRO CB C 32.3 0.20 1 822 . 132 LEU N N 124.3 0.25 1 823 . 132 LEU H H 8.38 0.01 1 824 . 132 LEU CA C 53.5 0.20 1 825 . 132 LEU HA H 4.55 0.01 1 826 . 132 LEU CB C 44.2 0.20 1 827 . 132 LEU HB2 H 1.51 0.01 2 828 . 133 LYS N N 123.4 0.25 1 829 . 133 LYS H H 8.25 0.01 1 830 . 133 LYS CA C 56.5 0.20 1 831 . 133 LYS HA H 4.43 0.01 1 832 . 133 LYS CB C 32.3 0.20 1 833 . 133 LYS HB2 H 1.79 0.01 2 834 . 133 LYS HG2 H 1.50 0.01 2 835 . 134 ASN N N 121.0 0.25 1 836 . 134 ASN H H 8.52 0.01 1 837 . 134 ASN CA C 53.5 0.20 1 838 . 134 ASN HA H 4.80 0.01 1 839 . 134 ASN CB C 39.0 0.20 1 840 . 134 ASN HB2 H 2.97 0.01 2 841 . 134 ASN HB3 H 2.77 0.01 2 842 . 135 VAL N N 123.6 0.25 1 843 . 135 VAL H H 7.64 0.01 1 844 . 135 VAL CA C 63.7 0.20 1 845 . 135 VAL HA H 4.05 0.01 1 846 . 135 VAL CB C 33.2 0.20 1 847 . 135 VAL HB H 1.99 0.01 1 848 . 135 VAL HG1 H 0.81 0.01 2 stop_ save_