data_7315 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The backbone chemical shifts of ribosomal protein L11 in the complex with rRNA and thiostrepton ; _BMRB_accession_number 7315 _BMRB_flat_file_name bmr7315.str _Entry_type original _Submission_date 2006-10-13 _Accession_date 2006-10-13 _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 Lee Donghan . . 2 Wang Yun-Xing . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 135 "13C chemical shifts" 263 "15N chemical shifts" 135 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2007-05-04 original author . stop_ _Original_release_date 2007-05-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The structure of free L11 and functional dyanamics of L11 in free, L11-rRNA(58nt) binary and L11-rRNA(58nt)-thiostrepton ternary complexes ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17292917 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lee D. . . 2 Walsh JD. . . 3 Yu P. . . 4 Markus MA. . . 5 Choli-Papadopoulou T. . . 6 Schwieters CD. . . 7 Krueger S. . . 8 Draper DE. . . 9 Wang YX. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 367 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1007 _Page_last 1022 _Year 2007 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'L11 in complex with rRNA' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label L11 $unlabelled RNA $RNA Thiostrepton $Thiostrepton stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state 'all free' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_unlabelled _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common L11 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 147 _Mol_residue_sequence ; MKKVVAVVKLQLPAGKATPA PPVGPALGQHGANIMEFVKA FNAATANMGDAIVPVEITIY ADRSFTFVTKTPPASYLIRK AAGLEKGAHKPGREKVGRIT WEQVLEIAKQKMPDLNTTDL EAAARMIAGSARSMGVEVVG APEVKDA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 LYS 4 VAL 5 VAL 6 ALA 7 VAL 8 VAL 9 LYS 10 LEU 11 GLN 12 LEU 13 PRO 14 ALA 15 GLY 16 LYS 17 ALA 18 THR 19 PRO 20 ALA 21 PRO 22 PRO 23 VAL 24 GLY 25 PRO 26 ALA 27 LEU 28 GLY 29 GLN 30 HIS 31 GLY 32 ALA 33 ASN 34 ILE 35 MET 36 GLU 37 PHE 38 VAL 39 LYS 40 ALA 41 PHE 42 ASN 43 ALA 44 ALA 45 THR 46 ALA 47 ASN 48 MET 49 GLY 50 ASP 51 ALA 52 ILE 53 VAL 54 PRO 55 VAL 56 GLU 57 ILE 58 THR 59 ILE 60 TYR 61 ALA 62 ASP 63 ARG 64 SER 65 PHE 66 THR 67 PHE 68 VAL 69 THR 70 LYS 71 THR 72 PRO 73 PRO 74 ALA 75 SER 76 TYR 77 LEU 78 ILE 79 ARG 80 LYS 81 ALA 82 ALA 83 GLY 84 LEU 85 GLU 86 LYS 87 GLY 88 ALA 89 HIS 90 LYS 91 PRO 92 GLY 93 ARG 94 GLU 95 LYS 96 VAL 97 GLY 98 ARG 99 ILE 100 THR 101 TRP 102 GLU 103 GLN 104 VAL 105 LEU 106 GLU 107 ILE 108 ALA 109 LYS 110 GLN 111 LYS 112 MET 113 PRO 114 ASP 115 LEU 116 ASN 117 THR 118 THR 119 ASP 120 LEU 121 GLU 122 ALA 123 ALA 124 ALA 125 ARG 126 MET 127 ILE 128 ALA 129 GLY 130 SER 131 ALA 132 ARG 133 SER 134 MET 135 GLY 136 VAL 137 GLU 138 VAL 139 VAL 140 GLY 141 ALA 142 PRO 143 GLU 144 VAL 145 LYS 146 ASP 147 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 4965 L11 100.00 147 100.00 100.00 1.03e-99 BMRB 7314 L11 100.00 147 100.00 100.00 1.03e-99 PDB 2E34 "L11 Structure With Rdc And Rg Refinement" 100.00 147 100.00 100.00 1.03e-99 PDB 2E35 "The Minimized Average Structure Of L11 With Rg Refinement" 100.00 147 100.00 100.00 1.03e-99 PDB 2E36 "L11 With Sans Refinement" 100.00 147 100.00 100.00 1.03e-99 PDB 2H8W "Solution Structure Of Ribosomal Protein L11" 100.00 147 100.00 100.00 1.03e-99 PDB 2HGJ "Crystal Structure Of The 70s Thermus Thermophilus Ribosome Showing How The 16s 3'-End Mimicks Mrna E And P Codons. This Entry 2" 100.00 147 100.00 100.00 1.03e-99 PDB 2HGQ "Crystal Structure Of The 70s Thermus Thermophilus Ribosome With Translocated And Rotated Shine-Dalgarno Duplex. This Entry 2hgq" 100.00 147 100.00 100.00 1.03e-99 PDB 2HGU "70s T.Th. Ribosome Functional Complex With Mrna And E- And P-Site Trnas At 4.5a. This Entry 2hgu Contains 50s Ribosomal Subunit" 100.00 147 100.00 100.00 1.03e-99 PDB 2J01 "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Mrna, Trna And Paromomycin (Part 2 Of 4). This File Contains " 100.00 147 100.00 100.00 1.03e-99 PDB 2J03 "Structure Of The Thermus Thermophilus 70s Ribosome Complexed With Mrna, Trna And Paromomycin (Part 4 Of 4). This File Contains " 100.00 147 100.00 100.00 1.03e-99 PDB 2KLM "Solution Structure Of L11 With Saxs And Rdc" 100.00 147 100.00 100.00 1.03e-99 PDB 2NXN "T. Thermophilus Ribosomal Protein L11 Methyltransferase (Prma) In Complex With Ribosomal Protein L11" 100.00 147 100.00 100.00 1.03e-99 PDB 2WH2 "Insights Into Translational Termination From The Structure Of Rf2 Bound To The Ribosome" 100.00 147 100.00 100.00 1.03e-99 PDB 2WH4 "Insights Into Translational Termination From The Structure Of Rf2 Bound To The Ribosome" 100.00 147 100.00 100.00 1.03e-99 PDB 2WRJ "The Structure Of The Ribosome With Elongation Factor G Trapped In The Post-Translocational State (Part 2 Of 4)." 100.00 147 100.00 100.00 1.03e-99 PDB 2WRL "The Structure Of The Ribosome With Elongation Factor G Trapped In The Post-Translocational State. (Part 4 Of 4)." 100.00 147 100.00 100.00 1.03e-99 PDB 2X9S "Structure Of The 70s Ribosome Bound To Release Factor 2 And A Substrate Analog Provides Insights Into Catalysis Of Peptide Rele" 100.00 147 100.00 100.00 1.03e-99 PDB 2X9U "Structure Of The 70s Ribosome Bound To Release Factor 2 And A Substrate Analog Provides Insights Into Catalysis Of Peptide Rele" 100.00 147 100.00 100.00 1.03e-99 PDB 2XTG "Trna Tranlocation On The 70s Ribosome: The Pre- Translocational Translocation Intermediate Ti(Pre)" 100.00 147 100.00 100.00 1.03e-99 PDB 2XUX "Trna Translocation On The 70s Ribosome: The Post- Translocational Translocation Intermediate Ti(Post)" 100.00 147 100.00 100.00 1.03e-99 PDB 3CJQ "Ribosomal Protein L11 Methyltransferase (Prma) In Complex With Dimethylated Ribosomal Protein L11 In Space Group P212121" 99.32 146 99.32 99.32 6.00e-98 PDB 3CJR "Ribosomal Protein L11 Methyltransferase (prma) In Complex With Ribosomal Protein L11 (k39a) And Inhibitor Sinefungin" 100.00 147 99.32 99.32 7.70e-99 PDB 3CJT "Ribosomal Protein L11 Methyltransferase (prma) In Complex With Dimethylated Ribosomal Protein L11" 100.00 147 100.00 100.00 1.03e-99 PDB 3EGV "Ribosomal Protein L11 Methyltransferase (Prma) In Complex With Trimethylated Ribosomal Protein L11" 99.32 146 99.32 99.32 6.00e-98 PDB 3F1F "Crystal Structure Of A Translation Termination Complex Formed With Release Factor Rf2. This File Contains The 50s Subunit Of On" 100.00 147 100.00 100.00 1.03e-99 PDB 3F1H "Crystal Structure Of A Translation Termination Complex Formed With Release Factor Rf2. This File Contains The 50s Subunit Of Th" 100.00 147 100.00 100.00 1.03e-99 PDB 3FIN "T. Thermophilus 70s Ribosome In Complex With Mrna, Trnas And Ef- Tu.Gdp.Kirromycin Ternary Complex, Fitted To A 6.4 A Cryo-Em M" 93.88 138 100.00 100.00 4.55e-93 PDB 3I8I "Elongation Complex Of The 70s Ribosome With Three Trnas And Entry 3i8i Contains 50s Ribosomal Subnit. The 30s Ribosomal Can Be " 100.00 147 100.00 100.00 1.03e-99 PDB 4JUX "Crystal Structure Of The Ribosome Bound To Elongation Factor G In The Guanosine Triphosphatase State (this File Contains The 50" 100.00 147 100.00 100.00 1.03e-99 PDB 4KBU "70s Ribosome Translocation Intermediate Gdpnp-ii Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e Stat" 95.24 140 100.00 100.00 2.52e-94 PDB 4KBW "70s Ribosome Translocation Intermediate Gdpnp-ii Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e Stat" 95.24 140 100.00 100.00 2.52e-94 PDB 4KCZ "70s Ribosome Translocation Intermediate Gdpnp-i Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e State" 95.24 140 100.00 100.00 2.52e-94 PDB 4KD2 "70s Ribosome Translocation Intermediate Gdpnp-i Containing Elongation Factor Efg/gdpnp, Mrna, And Trna Bound In The Pe*/e State" 95.24 140 100.00 100.00 2.52e-94 PDB 4KD9 "70s Ribosome Translocation Intermediate Fa-3.6a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " 95.24 140 100.00 100.00 2.52e-94 PDB 4KDB "70s Ribosome Translocation Intermediate Fa-3.6a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " 95.24 140 100.00 100.00 2.52e-94 PDB 4KDH "70s Ribosome Translocation Intermediate Fa-4.2a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " 95.24 140 100.00 100.00 2.52e-94 PDB 4KDK "70s Ribosome Translocation Intermediate Fa-4.2a Containing Elongation Factor Efg/fusidic Acid/gdp, Mrna, And Trna Bound In The " 95.24 140 100.00 100.00 2.52e-94 PDB 4KFI "Crystal Structure Of The 70s Ribosome Bound With The Q253p Mutant Of Release Factor Rf2. 50s Of The A Subunit" 100.00 147 100.00 100.00 1.03e-99 PDB 4KFL "Crystal Structure Of The 70s Ribosome Bound With The Q253p Mutant Of Release Factor Rf2. 50s Of The B Subunit" 100.00 147 100.00 100.00 1.03e-99 PDB 4QJS "Crystal Structure Of Elongation Factor 4 (ef4/lepa) Bound To The Thermus Thermophilus 70s Ribosome, 50s Subunit Of The 70s Ribo" 100.00 147 100.00 100.00 1.03e-99 DBJ BAD70070 "50S ribosomal protein L11 [Thermus thermophilus HB8]" 100.00 147 100.00 100.00 1.03e-99 EMBL CAA57138 "ribosomal protein L11 [Thermus thermophilus]" 100.00 147 100.00 100.00 1.03e-99 GB AAS82080 "LSU ribosomal protein L11P [Thermus thermophilus HB27]" 100.00 147 100.00 100.00 1.03e-99 GB ADW20820 "50S ribosomal protein L11 [Thermus scotoductus SA-01]" 100.00 147 97.96 100.00 8.98e-99 GB AEG32574 "ribosomal protein L11 [Thermus thermophilus SG0.5JP17-16]" 100.00 147 99.32 100.00 4.27e-99 GB AEV17153 "50S ribosomal protein L11 [Thermus sp. CCB_US3_UF1]" 100.00 147 97.28 100.00 7.98e-98 GB AFH38065 "50S ribosomal protein L11 [Thermus thermophilus JL-18]" 100.00 147 97.96 99.32 3.40e-98 PIR S66576 "ribosomal protein L11 - Thermus aquaticus" 100.00 147 100.00 100.00 1.03e-99 PRF 2004301A "ribosomal protein L11" 100.00 147 97.28 97.28 1.24e-96 REF WP_008630514 "MULTISPECIES: 50S ribosomal protein L11 [Thermus]" 100.00 147 99.32 100.00 4.27e-99 REF WP_011174097 "50S ribosomal protein L11 [Thermus thermophilus]" 100.00 147 100.00 100.00 1.03e-99 REF WP_014516502 "50S ribosomal protein L11 [Thermus sp. CCB_US3_UF1]" 100.00 147 97.28 100.00 7.98e-98 REF WP_014628913 "50S ribosomal protein L11 [Thermus thermophilus]" 100.00 147 97.96 99.32 3.40e-98 REF WP_015716108 "MULTISPECIES: 50S ribosomal protein L11 [Thermus]" 100.00 147 97.96 100.00 8.98e-99 SP P36238 "RecName: Full=50S ribosomal protein L11 [Thermus thermophilus]" 100.00 147 100.00 100.00 1.03e-99 SP P62442 "RecName: Full=50S ribosomal protein L11 [Thermus thermophilus HB27]" 100.00 147 100.00 100.00 1.03e-99 SP Q5SLP6 "RecName: Full=50S ribosomal protein L11 [Thermus thermophilus HB8]" 100.00 147 100.00 100.00 1.03e-99 stop_ save_ save_RNA _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class RNA _Name_common RNA _Molecular_mass . _Mol_thiol_state 'not present' _Details . _Residue_count 58 _Mol_residue_sequence ; GCCAGGAUGUUGGCUUAGAA GCAGCCAUCAUUUAAAGAAA GCGUAAUAGCUCACUGGU ; loop_ _Residue_seq_code _Residue_label 1 G 2 C 3 C 4 A 5 G 6 G 7 A 8 U 9 G 10 U 11 U 12 G 13 G 14 C 15 U 16 U 17 A 18 G 19 A 20 A 21 G 22 C 23 A 24 G 25 C 26 C 27 A 28 U 29 C 30 A 31 U 32 U 33 U 34 A 35 A 36 A 37 G 38 A 39 A 40 A 41 G 42 C 43 G 44 U 45 A 46 A 47 U 48 A 49 G 50 C 51 U 52 C 53 A 54 C 55 U 56 G 57 G 58 U stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ save_Thiostrepton _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Thiostrepton antibiotic' _Molecular_mass . _Mol_thiol_state . _Details . _Residue_count . _Mol_residue_sequence . _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $unlabelled 'Thermus thermophilus' 274 Bacteria . . . $RNA 'Thermus thermophilus' 274 Bacteria . . . $Thiostrepton . . . . . . 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 $unlabelled 'recombinant technology' . . . . . $RNA 'chemical synthesis' . . . . . $Thiostrepton . . . . . . 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 $unlabelled 0.7 mM '[U-13C; U-15N; U-2H]' $RNA . mM . $Thiostrepton . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_1D_[15N,1H]-TRACT_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1D [15N,1H]-TRACT' _Sample_label $sample_1 save_ save_3D_TROSY-HNCA_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _Sample_label $sample_1 save_ save_3D_TROSY-HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCACB' _Sample_label $sample_1 save_ save_3D_aromatic_TROSY-hCCH_COSY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D aromatic TROSY-hCCH COSY' _Sample_label $sample_1 save_ save_3D_15N-resolved_NOESY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-resolved NOESY' _Sample_label $sample_1 save_ save_3D_13C-resolved_NOESY_(aromatic_carbon)_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-resolved NOESY (aromatic carbon)' _Sample_label $sample_1 save_ save_1D_15N-1H-TRACT _Saveframe_category NMR_applied_experiment _Experiment_name '1D [15N,1H]-TRACT' _BMRB_pulse_sequence_accession_number . _Details . save_ save_3D_TROSY-HNCA _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCA' _BMRB_pulse_sequence_accession_number . _Details . save_ save_3D_TROSY-HNCACB _Saveframe_category NMR_applied_experiment _Experiment_name '3D TROSY-HNCACB' _BMRB_pulse_sequence_accession_number . _Details . save_ save_3D_aromatic_TROSY-hCCH_COSY _Saveframe_category NMR_applied_experiment _Experiment_name '3D aromatic TROSY-hCCH COSY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_3D_15N-resolved_NOESY _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-resolved NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ save_3D_13C-resolved_NOESY_(aromatic_carbon) _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-resolved NOESY (aromatic carbon)' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 pH temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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_citation_label _Correction_value_citation_label L11 1H 1 protons ppm 0.01 internal indirect . . . $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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name L11 _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 1 MET H H 8.500 0.020 1 2 1 1 MET CA C 54.589 0.400 1 3 1 1 MET CB C 32.567 0.400 1 4 1 1 MET N N 122.211 0.400 1 5 2 2 LYS H H 8.167 0.020 1 6 2 2 LYS CA C 55.768 0.400 1 7 2 2 LYS CB C 32.931 0.400 1 8 2 2 LYS N N 121.418 0.400 1 9 3 3 LYS H H 8.405 0.020 1 10 3 3 LYS CA C 56.096 0.400 1 11 3 3 LYS N N 121.882 0.400 1 12 4 4 VAL H H 8.646 0.020 1 13 4 4 VAL CA C 63.715 0.400 1 14 4 4 VAL CB C 32.840 0.400 1 15 4 4 VAL N N 126.383 0.400 1 16 5 5 VAL H H 9.171 0.020 1 17 5 5 VAL CA C 61.934 0.400 1 18 5 5 VAL CB C 32.795 0.400 1 19 5 5 VAL N N 122.275 0.400 1 20 6 6 ALA H H 7.634 0.020 1 21 6 6 ALA CA C 52.150 0.400 1 22 6 6 ALA CB C 21.193 0.400 1 23 6 6 ALA N N 121.182 0.400 1 24 7 7 VAL H H 8.106 0.020 1 25 7 7 VAL CA C 61.742 0.400 1 26 7 7 VAL CB C 33.341 0.400 1 27 7 7 VAL N N 119.782 0.400 1 28 8 8 VAL H H 9.461 0.020 1 29 8 8 VAL CA C 60.893 0.400 1 30 8 8 VAL CB C 34.797 0.400 1 31 8 8 VAL N N 128.223 0.400 1 32 9 9 LYS H H 8.842 0.020 1 33 9 9 LYS CA C 55.302 0.400 1 34 9 9 LYS CB C 33.841 0.400 1 35 9 9 LYS N N 127.851 0.400 1 36 10 10 LEU H H 8.751 0.020 1 37 10 10 LEU CA C 53.191 0.400 1 38 10 10 LEU CB C 45.716 0.400 1 39 10 10 LEU N N 121.875 0.400 1 40 11 11 GLN H H 8.795 0.020 1 41 11 11 GLN CA C 55.165 0.400 1 42 11 11 GLN CB C 28.564 0.400 1 43 11 11 GLN N N 120.282 0.400 1 44 12 12 LEU H H 7.952 0.020 1 45 12 12 LEU CA C 51.136 0.400 1 46 12 12 LEU CB C 44.351 0.400 1 47 12 12 LEU N N 122.789 0.400 1 48 14 14 ALA H H 8.602 0.020 1 49 14 14 ALA CA C 53.438 0.400 1 50 14 14 ALA CB C 18.645 0.400 1 51 14 14 ALA N N 126.193 0.400 1 52 15 15 GLY H H 8.605 0.020 1 53 15 15 GLY CA C 45.846 0.400 1 54 15 15 GLY N N 108.176 0.400 1 55 16 16 LYS H H 7.760 0.020 1 56 16 16 LYS CA C 55.247 0.400 1 57 16 16 LYS CB C 33.159 0.400 1 58 16 16 LYS N N 119.568 0.400 1 59 17 17 ALA H H 9.837 0.020 1 60 17 17 ALA CA C 53.136 0.400 1 61 17 17 ALA CB C 19.237 0.400 1 62 17 17 ALA N N 124.521 0.400 1 63 18 18 THR H H 7.864 0.020 1 64 18 18 THR CA C 59.111 0.400 1 65 18 18 THR CB C 70.239 0.400 1 66 18 18 THR N N 111.207 0.400 1 67 19 19 PRO CA C 63.167 0.400 1 68 20 20 ALA H H 7.327 0.020 1 69 20 20 ALA CA C 51.191 0.400 1 70 20 20 ALA CB C 16.598 0.400 1 71 20 20 ALA N N 120.718 0.400 1 72 22 22 PRO CA C 63.715 0.400 1 73 22 22 PRO CB C 35.434 0.400 1 74 23 23 VAL H H 8.018 0.020 1 75 23 23 VAL CA C 66.949 0.400 1 76 23 23 VAL CB C 31.657 0.400 1 77 23 23 VAL N N 125.332 0.400 1 78 24 24 GLY H H 6.744 0.020 1 79 24 24 GLY CA C 48.642 0.400 1 80 24 24 GLY N N 102.199 0.400 1 81 25 25 PRO CA C 64.784 0.400 1 82 26 26 ALA H H 6.928 0.020 1 83 26 26 ALA CA C 54.644 0.400 1 84 26 26 ALA CB C 18.372 0.400 1 85 26 26 ALA N N 115.897 0.400 1 86 27 27 LEU H H 7.414 0.020 1 87 27 27 LEU CA C 56.782 0.400 1 88 27 27 LEU CB C 41.621 0.400 1 89 27 27 LEU N N 113.220 0.400 1 90 28 28 GLY H H 9.115 0.020 1 91 28 28 GLY CA C 46.833 0.400 1 92 28 28 GLY N N 109.262 0.400 1 93 29 29 GLN H H 7.667 0.020 1 94 29 29 GLN CA C 57.713 0.400 1 95 29 29 GLN CB C 26.607 0.400 1 96 29 29 GLN N N 118.211 0.400 1 97 30 30 HIS H H 6.773 0.020 1 98 30 30 HIS CA C 55.356 0.400 1 99 30 30 HIS CB C 32.203 0.400 1 100 30 30 HIS N N 114.142 0.400 1 101 31 31 GLY H H 7.831 0.020 1 102 31 31 GLY CA C 45.545 0.400 1 103 31 31 GLY N N 105.985 0.400 1 104 32 32 ALA H H 7.370 0.020 1 105 32 32 ALA CA C 51.054 0.400 1 106 32 32 ALA CB C 19.555 0.400 1 107 32 32 ALA N N 120.261 0.400 1 108 33 33 ASN H H 9.292 0.020 1 109 33 33 ASN CA C 53.849 0.400 1 110 33 33 ASN CB C 37.663 0.400 1 111 33 33 ASN N N 119.175 0.400 1 112 34 34 ILE H H 7.911 0.020 1 113 34 34 ILE CA C 65.415 0.400 1 114 34 34 ILE CB C 39.301 0.400 1 115 34 34 ILE N N 126.593 0.400 1 116 35 35 MET H H 8.301 0.020 1 117 35 35 MET CA C 56.645 0.400 1 118 35 35 MET CB C 29.610 0.400 1 119 35 35 MET N N 115.428 0.400 1 120 36 36 GLU H H 8.072 0.020 1 121 36 36 GLU CA C 59.111 0.400 1 122 36 36 GLU CB C 29.064 0.400 1 123 36 36 GLU N N 119.511 0.400 1 124 37 37 PHE H H 7.796 0.020 1 125 37 37 PHE CA C 62.208 0.400 1 126 37 37 PHE CB C 37.663 0.400 1 127 37 37 PHE N N 119.211 0.400 1 128 38 38 VAL H H 8.405 0.020 1 129 38 38 VAL CA C 67.224 0.400 1 130 38 38 VAL CB C 31.566 0.400 1 131 38 38 VAL N N 119.332 0.400 1 132 39 39 LYS H H 8.025 0.020 1 133 39 39 LYS CA C 59.440 0.400 1 134 39 39 LYS CB C 31.930 0.400 1 135 39 39 LYS N N 116.002 0.400 1 136 40 40 ALA H H 7.903 0.020 1 137 40 40 ALA CA C 54.863 0.400 1 138 40 40 ALA CB C 18.827 0.400 1 139 40 40 ALA N N 121.768 0.400 1 140 41 41 PHE H H 9.125 0.020 1 141 41 41 PHE CA C 61.907 0.400 1 142 41 41 PHE CB C 37.890 0.400 1 143 41 41 PHE N N 120.968 0.400 1 144 42 42 ASN H H 8.613 0.020 1 145 42 42 ASN CA C 55.822 0.400 1 146 42 42 ASN CB C 35.707 0.400 1 147 42 42 ASN N N 121.596 0.400 1 148 43 43 ALA H H 7.813 0.020 1 149 43 43 ALA CA C 54.616 0.400 1 150 43 43 ALA CB C 18.008 0.400 1 151 43 43 ALA N N 120.696 0.400 1 152 44 44 ALA H H 7.893 0.020 1 153 44 44 ALA CA C 54.096 0.400 1 154 44 44 ALA CB C 18.372 0.400 1 155 44 44 ALA N N 118.418 0.400 1 156 45 45 THR H H 7.427 0.020 1 157 45 45 THR CA C 60.865 0.400 1 158 45 45 THR CB C 69.648 0.400 1 159 45 45 THR N N 103.037 0.400 1 160 46 46 ALA H H 7.097 0.020 1 161 46 46 ALA CA C 54.906 0.400 1 162 46 46 ALA CB C 18.554 0.400 1 163 46 46 ALA N N 124.008 0.400 1 164 47 47 ASN H H 8.502 0.020 1 165 47 47 ASN CA C 52.999 0.400 1 166 47 47 ASN CB C 37.799 0.400 1 167 47 47 ASN N N 112.679 0.400 1 168 48 48 MET H H 7.696 0.020 1 169 48 48 MET CA C 55.959 0.400 1 170 48 48 MET CB C 32.067 0.400 1 171 48 48 MET N N 116.925 0.400 1 172 49 49 GLY H H 8.160 0.020 1 173 49 49 GLY CA C 46.531 0.400 1 174 49 49 GLY N N 109.324 0.400 1 175 50 50 ASP H H 8.387 0.020 1 176 50 50 ASP CA C 53.191 0.400 1 177 50 50 ASP CB C 40.211 0.400 1 178 50 50 ASP N N 123.468 0.400 1 179 51 51 ALA H H 7.345 0.020 1 180 51 51 ALA CA C 52.534 0.400 1 181 51 51 ALA CB C 19.100 0.400 1 182 51 51 ALA N N 121.075 0.400 1 183 53 53 VAL H H 9.302 0.020 1 184 53 53 VAL CA C 59.084 0.400 1 185 53 53 VAL CB C 34.160 0.400 1 186 53 53 VAL N N 126.472 0.400 1 187 54 54 PRO CA C 61.304 0.400 1 188 54 54 PRO CB C 31.339 0.400 1 189 55 55 VAL H H 9.305 0.020 1 190 55 55 VAL CA C 58.453 0.400 1 191 55 55 VAL CB C 35.434 0.400 1 192 55 55 VAL N N 120.446 0.400 1 193 56 56 GLU H H 8.711 0.020 1 194 56 56 GLU CA C 54.781 0.400 1 195 56 56 GLU CB C 31.475 0.400 1 196 56 56 GLU N N 125.560 0.400 1 197 57 57 ILE H H 10.097 0.020 1 198 57 57 ILE CA C 60.838 0.400 1 199 57 57 ILE CB C 39.892 0.400 1 200 57 57 ILE N N 131.207 0.400 1 201 58 58 THR H H 9.462 0.020 1 202 58 58 THR CA C 63.304 0.400 1 203 58 58 THR CB C 69.466 0.400 1 204 58 58 THR N N 125.794 0.400 1 205 59 59 ILE H H 8.846 0.020 1 206 59 59 ILE CA C 60.070 0.400 1 207 59 59 ILE CB C 38.800 0.400 1 208 59 59 ILE N N 125.099 0.400 1 209 60 60 TYR H H 8.803 0.020 1 210 60 60 TYR CA C 57.686 0.400 1 211 60 60 TYR CB C 40.074 0.400 1 212 60 60 TYR N N 125.994 0.400 1 213 61 61 ALA H H 8.938 0.020 1 214 61 61 ALA CA C 54.808 0.400 1 215 61 61 ALA CB C 18.372 0.400 1 216 61 61 ALA N N 122.232 0.400 1 217 62 62 ASP H H 7.885 0.020 1 218 62 62 ASP CA C 53.383 0.400 1 219 62 62 ASP CB C 39.346 0.400 1 220 62 62 ASP N N 115.306 0.400 1 221 63 63 ARG H H 8.589 0.020 1 222 63 63 ARG CA C 58.864 0.400 1 223 63 63 ARG CB C 26.152 0.400 1 224 63 63 ARG N N 112.420 0.400 1 225 64 64 SER H H 8.180 0.020 1 226 64 64 SER CA C 58.919 0.400 1 227 64 64 SER CB C 65.143 0.400 1 228 64 64 SER N N 114.506 0.400 1 229 65 65 PHE H H 7.935 0.020 1 230 65 65 PHE CA C 56.261 0.400 1 231 65 65 PHE CB C 43.077 0.400 1 232 65 65 PHE N N 111.272 0.400 1 233 66 66 THR H H 9.364 0.020 1 234 66 66 THR CA C 60.564 0.400 1 235 66 66 THR CB C 72.605 0.400 1 236 66 66 THR N N 111.951 0.400 1 237 67 67 PHE H H 8.976 0.020 1 238 67 67 PHE CA C 56.316 0.400 1 239 67 67 PHE CB C 43.168 0.400 1 240 67 67 PHE N N 116.350 0.400 1 241 68 68 VAL H H 8.567 0.020 1 242 68 68 VAL CA C 60.043 0.400 1 243 68 68 VAL CB C 35.297 0.400 1 244 68 68 VAL N N 116.471 0.400 1 245 69 69 THR H H 8.567 0.020 1 246 69 69 THR CA C 59.851 0.400 1 247 69 69 THR CB C 69.966 0.400 1 248 69 69 THR N N 114.215 0.400 1 249 70 70 LYS H H 8.234 0.020 1 250 70 70 LYS CA C 53.904 0.400 1 251 70 70 LYS CB C 33.614 0.400 1 252 70 70 LYS N N 121.011 0.400 1 253 71 71 THR H H 8.852 0.020 1 254 71 71 THR CA C 61.550 0.400 1 255 71 71 THR CB C 69.147 0.400 1 256 71 71 THR N N 112.638 0.400 1 257 73 73 PRO CA C 61.852 0.400 1 258 73 73 PRO CB C 31.430 0.400 1 259 74 74 ALA H H 9.774 0.020 1 260 74 74 ALA CA C 56.370 0.400 1 261 74 74 ALA CB C 16.871 0.400 1 262 74 74 ALA N N 126.478 0.400 1 263 75 75 SER H H 8.908 0.020 1 264 75 75 SER CA C 60.317 0.400 1 265 75 75 SER CB C 62.505 0.400 1 266 75 75 SER N N 109.559 0.400 1 267 76 76 TYR H H 7.025 0.020 1 268 76 76 TYR CA C 61.413 0.400 1 269 76 76 TYR CB C 37.845 0.400 1 270 76 76 TYR N N 122.689 0.400 1 271 77 77 LEU H H 7.849 0.020 1 272 77 77 LEU CA C 57.494 0.400 1 273 77 77 LEU CB C 41.894 0.400 1 274 77 77 LEU N N 118.068 0.400 1 275 78 78 ILE H H 8.889 0.020 1 276 78 78 ILE CA C 65.607 0.400 1 277 78 78 ILE CB C 37.208 0.400 1 278 78 78 ILE N N 119.825 0.400 1 279 79 79 ARG H H 8.008 0.020 1 280 79 79 ARG CA C 61.139 0.400 1 281 79 79 ARG CB C 28.473 0.400 1 282 79 79 ARG N N 118.111 0.400 1 283 80 80 LYS H H 7.985 0.020 1 284 80 80 LYS CA C 57.686 0.400 1 285 80 80 LYS CB C 30.565 0.400 1 286 80 80 LYS N N 117.797 0.400 1 287 81 81 ALA H H 7.716 0.020 1 288 81 81 ALA CA C 54.616 0.400 1 289 81 81 ALA CB C 18.236 0.400 1 290 81 81 ALA N N 122.046 0.400 1 291 82 82 ALA H H 8.136 0.020 1 292 82 82 ALA CA C 51.766 0.400 1 293 82 82 ALA CB C 19.146 0.400 1 294 82 82 ALA N N 116.228 0.400 1 295 83 83 GLY H H 7.835 0.020 1 296 83 83 GLY CA C 46.531 0.400 1 297 83 83 GLY N N 108.484 0.400 1 298 84 84 LEU H H 8.269 0.020 1 299 84 84 LEU CA C 53.164 0.400 1 300 84 84 LEU CB C 44.761 0.400 1 301 84 84 LEU N N 117.947 0.400 1 302 85 85 GLU H H 8.861 0.020 1 303 85 85 GLU CA C 57.412 0.400 1 304 85 85 GLU N N 120.246 0.400 1 305 86 86 LYS H H 7.451 0.020 1 306 86 86 LYS CA C 54.616 0.400 1 307 86 86 LYS CB C 36.571 0.400 1 308 86 86 LYS N N 115.096 0.400 1 309 87 87 GLY H H 9.029 0.020 1 310 87 87 GLY CA C 43.489 0.400 1 311 87 87 GLY N N 105.746 0.400 1 312 88 88 ALA H H 7.831 0.020 1 313 88 88 ALA CA C 52.205 0.400 1 314 88 88 ALA CB C 19.464 0.400 1 315 88 88 ALA N N 116.304 0.400 1 316 89 89 HIS H H 8.195 0.020 1 317 89 89 HIS CA C 58.042 0.400 1 318 89 89 HIS CB C 27.972 0.400 1 319 89 89 HIS N N 117.268 0.400 1 320 90 90 LYS H H 8.579 0.020 1 321 90 90 LYS CA C 53.602 0.400 1 322 90 90 LYS CB C 33.022 0.400 1 323 90 90 LYS N N 117.682 0.400 1 324 91 91 PRO CA C 64.346 0.400 1 325 91 91 PRO CB C 32.249 0.400 1 326 92 92 GLY H H 8.180 0.020 1 327 92 92 GLY CA C 46.444 0.400 1 328 92 92 GLY N N 113.220 0.400 1 329 93 93 ARG H H 7.714 0.020 1 330 93 93 ARG CA C 56.891 0.400 1 331 93 93 ARG CB C 29.519 0.400 1 332 93 93 ARG N N 118.775 0.400 1 333 94 94 GLU H H 8.123 0.020 1 334 94 94 GLU CA C 54.397 0.400 1 335 94 94 GLU CB C 31.885 0.400 1 336 94 94 GLU N N 117.490 0.400 1 337 96 96 VAL H H 8.843 0.020 1 338 96 96 VAL CA C 61.276 0.400 1 339 96 96 VAL CB C 32.795 0.400 1 340 96 96 VAL N N 115.080 0.400 1 341 97 97 GLY H H 7.564 0.020 1 342 97 97 GLY CA C 45.079 0.400 1 343 97 97 GLY N N 104.827 0.400 1 344 98 98 ARG H H 8.882 0.020 1 345 98 98 ARG CA C 54.836 0.400 1 346 98 98 ARG CB C 33.432 0.400 1 347 98 98 ARG N N 119.697 0.400 1 348 99 99 ILE H H 8.945 0.020 1 349 99 99 ILE CA C 59.002 0.400 1 350 99 99 ILE CB C 41.530 0.400 1 351 99 99 ILE N N 115.986 0.400 1 352 100 100 THR H H 9.109 0.020 1 353 100 100 THR CA C 60.207 0.400 1 354 100 100 THR CB C 71.513 0.400 1 355 100 100 THR N N 112.663 0.400 1 356 101 101 TRP H H 8.700 0.020 1 357 101 101 TRP HE1 H 10.660 0.020 1 358 101 101 TRP CA C 59.851 0.400 1 359 101 101 TRP CB C 29.428 0.400 1 360 101 101 TRP N N 121.982 0.400 1 361 101 101 TRP NE1 N 129.697 0.400 1 362 102 102 GLU H H 8.604 0.020 1 363 102 102 GLU CA C 60.701 0.400 1 364 102 102 GLU CB C 28.655 0.400 1 365 102 102 GLU N N 115.775 0.400 1 366 103 103 GLN H H 7.829 0.020 1 367 103 103 GLN CA C 59.358 0.400 1 368 103 103 GLN CB C 29.064 0.400 1 369 103 103 GLN N N 118.532 0.400 1 370 104 104 VAL H H 8.272 0.020 1 371 104 104 VAL CA C 67.278 0.400 1 372 104 104 VAL N N 121.418 0.400 1 373 105 105 LEU H H 8.280 0.020 1 374 105 105 LEU CA C 58.015 0.400 1 375 105 105 LEU CB C 41.439 0.400 1 376 105 105 LEU N N 119.225 0.400 1 377 106 106 GLU H H 7.534 0.020 1 378 106 106 GLU CA C 59.248 0.400 1 379 106 106 GLU CB C 28.791 0.400 1 380 106 106 GLU N N 117.840 0.400 1 381 107 107 ILE H H 8.085 0.020 1 382 107 107 ILE CA C 65.552 0.400 1 383 107 107 ILE CB C 37.663 0.400 1 384 107 107 ILE N N 121.646 0.400 1 385 108 108 ALA H H 8.815 0.020 1 386 108 108 ALA CA C 55.548 0.400 1 387 108 108 ALA N N 121.882 0.400 1 388 109 109 LYS H H 8.081 0.020 1 389 109 109 LYS CA C 59.933 0.400 1 390 109 109 LYS CB C 32.203 0.400 1 391 109 109 LYS N N 114.740 0.400 1 392 110 110 GLN H H 7.719 0.020 1 393 110 110 GLN CA C 58.481 0.400 1 394 110 110 GLN CB C 28.382 0.400 1 395 110 110 GLN N N 117.475 0.400 1 396 111 111 LYS H H 8.059 0.020 1 397 111 111 LYS CA C 54.890 0.400 1 398 111 111 LYS CB C 30.520 0.400 1 399 111 111 LYS N N 113.932 0.400 1 400 112 112 MET H H 7.542 0.020 1 401 112 112 MET CA C 59.988 0.400 1 402 112 112 MET CB C 30.065 0.400 1 403 112 112 MET N N 118.768 0.400 1 404 113 113 PRO CA C 66.292 0.400 1 405 113 113 PRO CB C 31.157 0.400 1 406 114 114 ASP H H 8.477 0.020 1 407 114 114 ASP CA C 54.370 0.400 1 408 114 114 ASP CB C 42.440 0.400 1 409 114 114 ASP N N 113.811 0.400 1 410 115 115 LEU H H 7.885 0.020 1 411 115 115 LEU CA C 53.082 0.400 1 412 115 115 LEU CB C 42.850 0.400 1 413 115 115 LEU N N 116.975 0.400 1 414 116 116 ASN H H 7.762 0.020 1 415 116 116 ASN CA C 51.985 0.400 1 416 116 116 ASN CB C 37.390 0.400 1 417 116 116 ASN N N 116.447 0.400 1 418 117 117 THR H H 6.898 0.020 1 419 117 117 THR CA C 58.810 0.400 1 420 117 117 THR CB C 69.147 0.400 1 421 117 117 THR N N 109.897 0.400 1 422 118 118 THR H H 8.251 0.020 1 423 118 118 THR CA C 61.139 0.400 1 424 118 118 THR CB C 69.193 0.400 1 425 118 118 THR N N 113.786 0.400 1 426 119 119 ASP H H 8.700 0.020 1 427 119 119 ASP CA C 53.328 0.400 1 428 119 119 ASP CB C 42.668 0.400 1 429 119 119 ASP N N 126.483 0.400 1 430 120 120 LEU H H 8.789 0.020 1 431 120 120 LEU CA C 58.179 0.400 1 432 120 120 LEU CB C 41.758 0.400 1 433 120 120 LEU N N 128.444 0.400 1 434 121 121 GLU H H 8.121 0.020 1 435 121 121 GLU CA C 60.070 0.400 1 436 121 121 GLU CB C 28.336 0.400 1 437 121 121 GLU N N 116.575 0.400 1 438 122 122 ALA H H 7.903 0.020 1 439 122 122 ALA CA C 55.055 0.400 1 440 122 122 ALA CB C 18.736 0.400 1 441 122 122 ALA N N 123.146 0.400 1 442 123 123 ALA H H 8.751 0.020 1 443 123 123 ALA CA C 54.973 0.400 1 444 123 123 ALA CB C 18.918 0.400 1 445 123 123 ALA N N 121.375 0.400 1 446 124 124 ALA H H 8.423 0.020 1 447 124 124 ALA CA C 54.836 0.400 1 448 124 124 ALA CB C 19.874 0.400 1 449 124 124 ALA N N 119.689 0.400 1 450 125 125 ARG H H 8.308 0.020 1 451 125 125 ARG CA C 61.359 0.400 1 452 125 125 ARG CB C 30.565 0.400 1 453 125 125 ARG N N 117.032 0.400 1 454 126 126 MET H H 7.878 0.020 1 455 126 126 MET CA C 61.331 0.400 1 456 126 126 MET CB C 33.705 0.400 1 457 126 126 MET N N 121.189 0.400 1 458 127 127 ILE H H 8.213 0.020 1 459 127 127 ILE CA C 61.907 0.400 1 460 127 127 ILE N N 120.596 0.400 1 461 128 128 ALA H H 9.279 0.020 1 462 128 128 ALA CA C 55.274 0.400 1 463 128 128 ALA CB C 17.553 0.400 1 464 128 128 ALA N N 122.753 0.400 1 465 129 129 GLY H H 8.286 0.020 1 466 129 129 GLY CA C 47.518 0.400 1 467 129 129 GLY N N 109.887 0.400 1 468 130 130 SER H H 8.646 0.020 1 469 130 130 SER CA C 63.030 0.400 1 470 130 130 SER N N 122.689 0.400 1 471 131 131 ALA H H 8.964 0.020 1 472 131 131 ALA CA C 56.398 0.400 1 473 131 131 ALA CB C 16.006 0.400 1 474 131 131 ALA N N 127.634 0.400 1 475 132 132 ARG H H 8.236 0.020 1 476 132 132 ARG CA C 59.796 0.400 1 477 132 132 ARG CB C 29.564 0.400 1 478 132 132 ARG N N 119.504 0.400 1 479 133 133 SER H H 7.622 0.020 1 480 133 133 SER CA C 61.249 0.400 1 481 133 133 SER CB C 64.461 0.400 1 482 133 133 SER N N 115.622 0.400 1 483 134 134 MET H H 7.383 0.020 1 484 134 134 MET CA C 54.370 0.400 1 485 134 134 MET CB C 36.116 0.400 1 486 134 134 MET N N 113.697 0.400 1 487 135 135 GLY H H 8.038 0.020 1 488 135 135 GLY CA C 46.367 0.400 1 489 135 135 GLY N N 106.323 0.400 1 490 136 136 VAL H H 7.901 0.020 1 491 136 136 VAL CA C 61.194 0.400 1 492 136 136 VAL CB C 32.385 0.400 1 493 136 136 VAL N N 120.325 0.400 1 494 137 137 GLU H H 8.477 0.020 1 495 137 137 GLU CA C 56.042 0.400 1 496 137 137 GLU CB C 31.521 0.400 1 497 137 137 GLU N N 128.323 0.400 1 498 138 138 VAL H H 8.431 0.020 1 499 138 138 VAL CA C 61.084 0.400 1 500 138 138 VAL CB C 32.158 0.400 1 501 138 138 VAL N N 124.743 0.400 1 502 139 139 VAL H H 9.128 0.020 1 503 139 139 VAL CA C 60.947 0.400 1 504 139 139 VAL CB C 33.477 0.400 1 505 139 139 VAL N N 126.033 0.400 1 506 140 140 GLY H H 8.818 0.020 1 507 140 140 GLY CA C 45.243 0.400 1 508 140 140 GLY N N 111.975 0.400 1 509 141 141 ALA H H 8.057 0.020 1 510 141 141 ALA CA C 50.341 0.400 1 511 141 141 ALA CB C 17.553 0.400 1 512 141 141 ALA N N 123.018 0.400 1 513 142 142 PRO CA C 62.811 0.400 1 514 143 143 GLU H H 8.323 0.020 1 515 143 143 GLU CA C 56.042 0.400 1 516 143 143 GLU CB C 30.201 0.400 1 517 143 143 GLU N N 121.175 0.400 1 518 144 144 VAL H H 8.218 0.020 1 519 144 144 VAL CA C 62.208 0.400 1 520 144 144 VAL CB C 32.385 0.400 1 521 144 144 VAL N N 121.882 0.400 1 522 145 145 LYS H H 8.379 0.020 1 523 145 145 LYS CA C 55.850 0.400 1 524 145 145 LYS CB C 32.658 0.400 1 525 145 145 LYS N N 125.210 0.400 1 526 146 146 ASP H H 8.364 0.020 1 527 146 146 ASP CA C 54.397 0.400 1 528 146 146 ASP CB C 40.802 0.400 1 529 146 146 ASP N N 121.882 0.400 1 530 147 147 ALA H H 7.810 0.020 1 531 147 147 ALA CA C 53.685 0.400 1 532 147 147 ALA CB C 20.237 0.400 1 533 147 147 ALA N N 128.779 0.400 1 stop_ save_