data_15094 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for CutA1 from E. coli ; _BMRB_accession_number 15094 _BMRB_flat_file_name bmr15094.str _Entry_type original _Submission_date 2007-01-04 _Accession_date 2007-01-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; We applied a combined strategy of 1H and 13C detection experiments to assigne the trimeric protein CutA1 from E. coli. The CutA1 family of proteins is thought to bind divalent metal ions and are present in archaea, bacteria, plants, and animals. Their function is still unknown. In this work we demonstrate that the unique information available from 13C direct detection experiments makes it possible to assign the NMR resonances of this 37 KDa protein without the need of deuteration. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bertini Ivano . . 2 Jimenez Beatriz . . 3 Pierattelli Roberta . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 218 "13C chemical shifts" 383 "15N chemical shifts" 119 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-07-01 update BMRB 'complete entry citation' 2007-10-17 original author 'original release' stop_ save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'Protonless (13)C direct detection NMR: characterization of the 37 kiloDalton trimeric protein CutA1' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 17847095 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bertini Ivano . . 2 Jimenez Beatriz . . 3 Pierattelli Roberta . . 4 Wedd Anthony G. . 5 Xiao Zhiguang . . stop_ _Journal_abbreviation Proteins _Journal_volume 70 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1196 _Page_last 1205 _Year 2008 _Details . loop_ _Keyword '13C direct Detection' CutA1 NMR stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name homo-trimer _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'CutA1, chain 1' $CutA1 'CutA1, chain 2' $CutA1 'CutA1, chain 3' $CutA1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_CutA1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common CutA1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 112 _Mol_residue_sequence ; MLDEKSSNTASVVVLCTAPD EATAQDLAAKVLAEKLAACA TLIPGATSLYYWEGKLEQEY EVQMILKTTVSHQQALLECL KSHHPYQTPELLVLPVTHGD TDYLSWLNASLR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LEU 3 ASP 4 GLU 5 LYS 6 SER 7 SER 8 ASN 9 THR 10 ALA 11 SER 12 VAL 13 VAL 14 VAL 15 LEU 16 CYS 17 THR 18 ALA 19 PRO 20 ASP 21 GLU 22 ALA 23 THR 24 ALA 25 GLN 26 ASP 27 LEU 28 ALA 29 ALA 30 LYS 31 VAL 32 LEU 33 ALA 34 GLU 35 LYS 36 LEU 37 ALA 38 ALA 39 CYS 40 ALA 41 THR 42 LEU 43 ILE 44 PRO 45 GLY 46 ALA 47 THR 48 SER 49 LEU 50 TYR 51 TYR 52 TRP 53 GLU 54 GLY 55 LYS 56 LEU 57 GLU 58 GLN 59 GLU 60 TYR 61 GLU 62 VAL 63 GLN 64 MET 65 ILE 66 LEU 67 LYS 68 THR 69 THR 70 VAL 71 SER 72 HIS 73 GLN 74 GLN 75 ALA 76 LEU 77 LEU 78 GLU 79 CYS 80 LEU 81 LYS 82 SER 83 HIS 84 HIS 85 PRO 86 TYR 87 GLN 88 THR 89 PRO 90 GLU 91 LEU 92 LEU 93 VAL 94 LEU 95 PRO 96 VAL 97 THR 98 HIS 99 GLY 100 ASP 101 THR 102 ASP 103 TYR 104 LEU 105 SER 106 TRP 107 LEU 108 ASN 109 ALA 110 SER 111 LEU 112 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-08 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1NAQ "Crystal Structure Of Cuta1 From E.Coli At 1.7 A Resolution" 100.00 112 100.00 100.00 6.88e-74 PDB 3AA8 "Crystal Structure Analysis Of The Mutant Cuta1 (S11vE61V) FROM E. Coli" 100.00 112 98.21 98.21 6.95e-72 PDB 3AA9 "Crystal Structure Analysis Of The Mutant Cuta1 (E61v) From E. Coli" 100.00 112 99.11 99.11 7.84e-73 PDB 3AH6 "Remarkable Improvement Of The Heat Stability Of Cuta1 From E.Coli By Rational Protein Designing" 100.00 112 99.11 99.11 4.96e-73 PDB 3X3U "Crystal Structure Of Wild-type Of E. Coli Cuta1" 100.00 112 100.00 100.00 6.88e-74 PDB 4Y65 "Crystal Structure Of E.coli Cuta1 C16a/c39a/c79a Mutation" 100.00 112 97.32 97.32 4.74e-71 DBJ BAB38541 "divalent cation tolerance protein CutA [Escherichia coli O157:H7 str. Sakai]" 100.00 112 100.00 100.00 6.88e-74 DBJ BAE78139 "copper binding protein, copper sensitivity [Escherichia coli str. K12 substr. W3110]" 100.00 112 100.00 100.00 6.88e-74 DBJ BAG66863 "copper binding protein, copper sensitivity [Escherichia coli O111:H-]" 100.00 112 100.00 100.00 6.88e-74 DBJ BAG79960 "divalent cation tolerance protein [Escherichia coli SE11]" 100.00 112 100.00 100.00 6.88e-74 DBJ BAI28441 "copper binding protein CutA, copper sensitivity [Escherichia coli O26:H11 str. 11368]" 100.00 112 99.11 100.00 3.50e-73 EMBL CAA54780 "orf112 [Escherichia coli K-12]" 100.00 112 100.00 100.00 6.88e-74 EMBL CAA85374 "periplasmic divalent cation tolerance protein [Escherichia coli str. K-12 substr. W3110]" 100.00 112 100.00 100.00 6.88e-74 EMBL CAP78655 "Divalent-cation tolerance protein cutA [Escherichia coli LF82]" 100.00 112 99.11 99.11 2.90e-73 EMBL CAQ34486 "copper binding protein CutA [Escherichia coli BL21(DE3)]" 100.00 112 100.00 100.00 6.88e-74 EMBL CAR01113 "copper binding protein, copper sensitivity [Escherichia coli IAI1]" 100.00 112 100.00 100.00 6.88e-74 GB AAA97036 "cycY [Escherichia coli str. K-12 substr. MG1655]" 100.00 112 100.00 100.00 6.88e-74 GB AAC77097 "divalent-cation tolerance protein, copper sensitivity [Escherichia coli str. K-12 substr. MG1655]" 100.00 112 100.00 100.00 6.88e-74 GB AAG59336 "divalent cation tolerance protein; cytochrome c biogenesis [Escherichia coli O157:H7 str. EDL933]" 100.00 112 100.00 100.00 6.88e-74 GB AAN45709 "divalent cation tolerance protein [Shigella flexneri 2a str. 301]" 100.00 112 99.11 99.11 2.90e-73 GB AAN83641 "Periplasmic divalent cation tolerance protein cutA [Escherichia coli CFT073]" 100.00 114 99.11 99.11 2.00e-73 REF NP_313145 "divalent-cation tolerance protein CutA [Escherichia coli O157:H7 str. Sakai]" 100.00 112 100.00 100.00 6.88e-74 REF NP_418560 "divalent-cation tolerance protein, copper sensitivity [Escherichia coli str. K-12 substr. MG1655]" 100.00 112 100.00 100.00 6.88e-74 REF NP_710002 "divalent-cation tolerance protein CutA [Shigella flexneri 2a str. 301]" 100.00 112 99.11 99.11 2.90e-73 REF WP_000883338 "divalent ion tolerance protein CutA [Escherichia coli]" 100.00 112 99.11 100.00 3.50e-73 REF WP_000883339 "divalent ion tolerance protein CutA [Escherichia coli]" 100.00 112 98.21 99.11 6.16e-72 SP A7ZV06 "RecName: Full=Divalent-cation tolerance protein CutA" 100.00 112 100.00 100.00 6.88e-74 SP A8A7N3 "RecName: Full=Divalent-cation tolerance protein CutA" 100.00 112 100.00 100.00 6.88e-74 SP B1ITR1 "RecName: Full=Divalent-cation tolerance protein CutA" 100.00 112 100.00 100.00 6.88e-74 SP B1LQF8 "RecName: Full=Divalent-cation tolerance protein CutA" 100.00 112 100.00 100.00 6.88e-74 SP B1XD17 "RecName: Full=Divalent-cation tolerance protein CutA" 100.00 112 100.00 100.00 6.88e-74 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Strain $CutA1 'E. coli' 562 Bacteria . Escherichia coli DH5a 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 $CutA1 'recombinant technology' . Escherichia coli BL21(DE3) pET11a 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 $CutA1 3.5 mM '[U-83% 13C; U-98% 15N]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CutA1 3.5 mM '[U-98% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_CARA _Saveframe_category software _Name CARA _Version 1.5 loop_ _Vendor _Address _Electronic_address 'Keller and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details 'Cryo-probe TCI' save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details 'Probe TXI' save_ save_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details 'Probe TXI' save_ save_spectrometer_4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details 'Probe TXO' save_ save_spectrometer_5 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details 'Cryo-Probe TXI' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_CACO_8 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CACO' _Sample_label $sample_1 save_ save_2D_CON_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CON' _Sample_label $sample_1 save_ save_2D_CBCACO_10 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CBCACO' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.04 0.0001 M pH 6.5 0.01 pH pressure 1 . atm temperature 298 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _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 C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 $citation_1 $citation_1 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 $citation_1 $citation_1 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_1 $citation_1 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_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $CARA stop_ loop_ _Experiment_label '3D CBCA(CO)NH' '2D CACO' '2D CON' '2D CBCACO' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'CutA1, chain 1' _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 HA H 4.01 0.07 1 2 1 1 MET C C 173.17 0.16 1 3 1 1 MET CA C 55.08 0.11 1 4 1 1 MET CB C 33.37 0.17 1 5 1 1 MET CG C 31.03 0.17 1 6 2 2 LEU HA H 4.32 0.07 1 7 2 2 LEU C C 176.54 0.16 1 8 2 2 LEU CA C 55.29 0.11 1 9 2 2 LEU CB C 42.21 0.17 1 10 2 2 LEU CG C 26.93 0.17 1 11 2 2 LEU CD1 C 24.71 0.17 2 12 2 2 LEU CD2 C 23.65 0.17 2 13 2 2 LEU N N 125.46 0.39 1 14 3 3 ASP H H 8.44 0.07 1 15 3 3 ASP HA H 4.57 0.07 1 16 3 3 ASP HB2 H 2.69 0.07 2 17 3 3 ASP HB3 H 2.53 0.07 2 18 3 3 ASP C C 176.31 0.16 1 19 3 3 ASP CA C 53.97 0.11 1 20 3 3 ASP CB C 41.19 0.17 1 21 3 3 ASP CG C 180.35 0.16 1 22 3 3 ASP N N 122.85 0.39 1 23 4 4 GLU H H 8.5 0.07 1 24 4 4 GLU HA H 4.2 0.07 1 25 4 4 GLU HB2 H 2.24 0.07 2 26 4 4 GLU HB3 H 2.02 0.07 2 27 4 4 GLU C C 176.95 0.16 1 28 4 4 GLU CA C 57.01 0.11 1 29 4 4 GLU CB C 30.17 0.17 1 30 4 4 GLU CG C 36.35 0.17 1 31 4 4 GLU CD C 183.98 0.16 1 32 4 4 GLU N N 123.08 0.39 1 33 5 5 LYS H H 8.39 0.07 1 34 5 5 LYS HA H 4.28 0.07 1 35 5 5 LYS HB2 H 1.82 0.07 2 36 5 5 LYS HB3 H 1.78 0.07 2 37 5 5 LYS HG2 H 1.41 0.07 2 38 5 5 LYS C C 177.12 0.16 1 39 5 5 LYS CA C 56.48 0.11 1 40 5 5 LYS CB C 32.55 0.17 1 41 5 5 LYS CG C 24.76 0.17 1 42 5 5 LYS CD C 29.08 0.17 1 43 5 5 LYS CE C 41.98 0.17 1 44 5 5 LYS N N 122.21 0.39 1 45 6 6 SER H H 8.2 0.07 1 46 6 6 SER HA H 4.42 0.07 1 47 6 6 SER HB2 H 3.87 0.07 2 48 6 6 SER HB3 H 4.42 0.07 2 49 6 6 SER C C 174.8 0.16 1 50 6 6 SER CA C 58.49 0.11 1 51 6 6 SER CB C 63.83 0.17 1 52 6 6 SER N N 117.03 0.39 1 53 7 7 SER H H 8.29 0.07 1 54 7 7 SER HA H 4.44 0.07 1 55 7 7 SER HB2 H 3.84 0.07 2 56 7 7 SER HB3 H 4.12 0.07 2 57 7 7 SER C C 174.44 0.16 1 58 7 7 SER CA C 58.43 0.11 1 59 7 7 SER CB C 63.77 0.17 1 60 7 7 SER N N 118.34 0.39 1 61 8 8 ASN H H 8.36 0.07 1 62 8 8 ASN HA H 4.61 0.07 1 63 8 8 ASN HB2 H 2.64 0.07 2 64 8 8 ASN HD21 H 6.91 0.07 2 65 8 8 ASN HD22 H 7.59 0.07 2 66 8 8 ASN C C 175.51 0.16 1 67 8 8 ASN CA C 53.47 0.11 1 68 8 8 ASN CB C 39.12 0.17 1 69 8 8 ASN CG C 176.58 0.16 1 70 8 8 ASN N N 121.58 0.39 1 71 8 8 ASN ND2 N 112.98 0.39 1 72 9 9 THR H H 8.12 0.07 1 73 9 9 THR HA H 4.26 0.07 1 74 9 9 THR HB H 4.32 0.07 1 75 9 9 THR HG2 H 1.12 0.07 1 76 9 9 THR C C 174.05 0.16 1 77 9 9 THR CA C 61.54 0.11 1 78 9 9 THR CB C 69.91 0.17 1 79 9 9 THR CG2 C 21.65 0.17 1 80 9 9 THR N N 113.95 0.39 1 81 10 10 ALA H H 8.14 0.07 1 82 10 10 ALA HA H 4.31 0.07 1 83 10 10 ALA C C 176.79 0.16 1 84 10 10 ALA CA C 52.74 0.11 1 85 10 10 ALA CB C 19.05 0.17 1 86 10 10 ALA N N 126.49 0.39 1 87 11 11 SER H H 8.87 0.07 1 88 11 11 SER HB2 H 3.68 0.07 2 89 11 11 SER HB3 H 3.72 0.07 2 90 11 11 SER C C 173 0.16 1 91 11 11 SER CA C 58.76 0.11 1 92 11 11 SER CB C 65.43 0.17 1 93 11 11 SER N N 117.94 0.39 1 94 12 12 VAL H H 8.42 0.07 1 95 12 12 VAL C C 174.56 0.16 1 96 12 12 VAL CA C 59.77 0.11 1 97 12 12 VAL CB C 36.09 0.17 1 98 12 12 VAL N N 113.97 0.39 1 99 13 13 VAL H H 8.77 0.07 1 100 13 13 VAL C C 174.12 0.16 1 101 13 13 VAL CA C 59.98 0.11 1 102 13 13 VAL CB C 34.67 0.17 1 103 13 13 VAL N N 118.01 0.39 1 104 14 14 VAL H H 9.24 0.07 1 105 14 14 VAL C C 175.24 0.16 1 106 14 14 VAL CA C 59.83 0.11 1 107 14 14 VAL CB C 34.52 0.17 1 108 14 14 VAL N N 125.38 0.39 1 109 15 15 LEU H H 9.16 0.07 1 110 15 15 LEU HA H 4.87 0.07 1 111 15 15 LEU C C 175.04 0.16 1 112 15 15 LEU CA C 53.3 0.11 1 113 15 15 LEU CB C 43.19 0.17 1 114 15 15 LEU N N 128 0.39 1 115 16 16 CYS H H 7.74 0.07 1 116 16 16 CYS C C 172.93 0.16 1 117 16 16 CYS CA C 56.34 0.11 1 118 16 16 CYS CB C 30.14 0.17 1 119 16 16 CYS N N 120.36 0.39 1 120 17 17 THR H H 7.55 0.07 1 121 17 17 THR HB H 3.95 0.07 1 122 17 17 THR C C 173.12 0.16 1 123 17 17 THR CA C 59.64 0.11 1 124 17 17 THR CB C 71.92 0.17 1 125 17 17 THR N N 117.26 0.39 1 126 18 18 ALA H H 8.61 0.07 1 127 18 18 ALA C C 175.14 0.16 1 128 18 18 ALA CA C 48.57 0.11 1 129 18 18 ALA CB C 21.75 0.17 1 130 18 18 ALA N N 122.93 0.39 1 131 19 19 PRO C C 174.96 0.16 1 132 19 19 PRO CA C 64.35 0.11 1 133 19 19 PRO CB C 32.26 0.17 1 134 19 19 PRO N N 129.89 0.39 1 135 20 20 ASP H H 6.91 0.07 1 136 20 20 ASP HA H 4.56 0.07 1 137 20 20 ASP C C 175.5 0.16 1 138 20 20 ASP CA C 52.37 0.11 1 139 20 20 ASP CB C 41.98 0.17 1 140 20 20 ASP CG C 179.62 0.16 1 141 20 20 ASP N N 109.66 0.39 1 142 21 21 GLU H H 9.28 0.07 1 143 21 21 GLU C C 177.58 0.16 1 144 21 21 GLU CA C 61.06 0.11 1 145 21 21 GLU CB C 29.92 0.17 1 146 21 21 GLU CG C 38.34 0.17 1 147 21 21 GLU CD C 182.97 0.16 1 148 21 21 GLU N N 121.72 0.39 1 149 22 22 ALA H H 8.48 0.07 1 150 22 22 ALA HB H 0.66 0.07 1 151 22 22 ALA C C 180.92 0.16 1 152 22 22 ALA CA C 55.33 0.11 1 153 22 22 ALA CB C 17.67 0.17 1 154 22 22 ALA N N 123.81 0.39 1 155 23 23 THR H H 8.74 0.07 1 156 23 23 THR HA H 3.82 0.07 1 157 23 23 THR HB H 3.73 0.07 1 158 23 23 THR C C 176.21 0.16 1 159 23 23 THR CA C 66.43 0.11 1 160 23 23 THR CB C 67.77 0.17 1 161 23 23 THR N N 116.68 0.39 1 162 24 24 ALA H H 8.02 0.07 1 163 24 24 ALA HA H 3.79 0.07 1 164 24 24 ALA C C 178.61 0.16 1 165 24 24 ALA CA C 55.49 0.11 1 166 24 24 ALA CB C 19.35 0.17 1 167 24 24 ALA N N 124.01 0.39 1 168 25 25 GLN H H 8.49 0.07 1 169 25 25 GLN HA H 3.58 0.07 1 170 25 25 GLN HE21 H 6.64 0.07 2 171 25 25 GLN HE22 H 7.35 0.07 2 172 25 25 GLN C C 177.76 0.16 1 173 25 25 GLN CA C 59.74 0.11 1 174 25 25 GLN CB C 27.43 0.17 1 175 25 25 GLN CG C 34.18 0.17 1 176 25 25 GLN CD C 179.19 0.16 1 177 25 25 GLN N N 116.97 0.39 1 178 25 25 GLN NE2 N 110.32 0.39 1 179 26 26 ASP H H 7.88 0.07 1 180 26 26 ASP C C 178.91 0.16 1 181 26 26 ASP CA C 57.5 0.11 1 182 26 26 ASP CB C 41.45 0.17 1 183 26 26 ASP CG C 179.22 0.16 1 184 26 26 ASP N N 121.41 0.39 1 185 27 27 LEU H H 8.43 0.07 1 186 27 27 LEU C C 178.67 0.16 1 187 27 27 LEU CA C 57.69 0.11 1 188 27 27 LEU CB C 42.56 0.17 1 189 27 27 LEU N N 119.87 0.39 1 190 28 28 ALA H H 8.09 0.07 1 191 28 28 ALA C C 177.98 0.16 1 192 28 28 ALA CA C 54.57 0.11 1 193 28 28 ALA CB C 18.83 0.17 1 194 28 28 ALA N N 119.02 0.39 1 195 29 29 ALA H H 8.65 0.07 1 196 29 29 ALA C C 180.76 0.16 1 197 29 29 ALA CA C 55.6 0.11 1 198 29 29 ALA CB C 17.79 0.17 1 199 29 29 ALA N N 119.22 0.39 1 200 30 30 LYS H H 7.76 0.07 1 201 30 30 LYS HA H 4.69 0.07 1 202 30 30 LYS C C 178.73 0.16 1 203 30 30 LYS CA C 59.06 0.11 1 204 30 30 LYS CB C 31.8 0.17 1 205 30 30 LYS N N 118.52 0.39 1 206 31 31 VAL H H 7.6 0.07 1 207 31 31 VAL HA H 3.92 0.07 1 208 31 31 VAL C C 178.34 0.16 1 209 31 31 VAL CA C 64.7 0.11 1 210 31 31 VAL CB C 30.89 0.17 1 211 31 31 VAL N N 111.22 0.39 1 212 32 32 LEU H H 8.28 0.07 1 213 32 32 LEU HA H 5.55 0.07 1 214 32 32 LEU C C 181.1 0.16 1 215 32 32 LEU CA C 57.36 0.11 1 216 32 32 LEU CB C 41 0.17 1 217 32 32 LEU N N 123.08 0.39 1 218 33 33 ALA H H 8.18 0.07 1 219 33 33 ALA HA H 4.44 0.07 1 220 33 33 ALA HB H 1.34 0.07 1 221 33 33 ALA C C 180.03 0.16 1 222 33 33 ALA CA C 55.09 0.11 1 223 33 33 ALA CB C 17.78 0.17 1 224 33 33 ALA N N 125.25 0.39 1 225 34 34 GLU H H 7.31 0.07 1 226 34 34 GLU C C 174.75 0.16 1 227 34 34 GLU CA C 56 0.11 1 228 34 34 GLU CB C 30.15 0.17 1 229 34 34 GLU CG C 36.2 0.17 1 230 34 34 GLU CD C 183.09 0.16 1 231 34 34 GLU N N 114.77 0.39 1 232 35 35 LYS H H 7.74 0.07 1 233 35 35 LYS C C 174.73 0.16 1 234 35 35 LYS CA C 57.54 0.11 1 235 35 35 LYS CB C 28.94 0.17 1 236 35 35 LYS N N 114.65 0.39 1 237 36 36 LEU H H 7.86 0.07 1 238 36 36 LEU C C 176.32 0.16 1 239 36 36 LEU CA C 54.24 0.11 1 240 36 36 LEU CB C 44.92 0.17 1 241 36 36 LEU N N 113.05 0.39 1 242 37 37 ALA H H 7.35 0.07 1 243 37 37 ALA HA H 4.39 0.07 1 244 37 37 ALA C C 174.19 0.16 1 245 37 37 ALA CA C 49.91 0.11 1 246 37 37 ALA CB C 22 0.17 1 247 37 37 ALA N N 118.42 0.39 1 248 38 38 ALA H H 8.46 0.07 1 249 38 38 ALA HA H 4.15 0.07 1 250 38 38 ALA C C 175.96 0.16 1 251 38 38 ALA CA C 52.73 0.11 1 252 38 38 ALA CB C 21.77 0.17 1 253 38 38 ALA N N 122.29 0.39 1 254 39 39 CYS H H 7.26 0.07 1 255 39 39 CYS C C 172.61 0.16 1 256 39 39 CYS CA C 55.64 0.11 1 257 39 39 CYS CB C 29.69 0.17 1 258 39 39 CYS N N 109.57 0.39 1 259 40 40 ALA H H 9.14 0.07 1 260 40 40 ALA HA H 5.28 0.07 1 261 40 40 ALA C C 174.35 0.16 1 262 40 40 ALA CA C 50.52 0.11 1 263 40 40 ALA CB C 23.28 0.17 1 264 40 40 ALA N N 127.28 0.39 1 265 41 41 THR H H 9.24 0.07 1 266 41 41 THR HB H 3.86 0.07 1 267 41 41 THR C C 172.81 0.16 1 268 41 41 THR CA C 62.08 0.11 1 269 41 41 THR CB C 70.86 0.17 1 270 41 41 THR N N 121.5 0.39 1 271 42 42 LEU H H 9.78 0.07 1 272 42 42 LEU HA H 5.04 0.07 1 273 42 42 LEU C C 175.84 0.16 1 274 42 42 LEU CA C 53.19 0.11 1 275 42 42 LEU CB C 43.32 0.17 1 276 42 42 LEU N N 129.28 0.39 1 277 43 43 ILE H H 9.18 0.07 1 278 43 43 ILE C C 172.85 0.16 1 279 43 43 ILE CA C 58.47 0.11 1 280 43 43 ILE CB C 39.87 0.17 1 281 43 43 ILE N N 122.6 0.39 1 282 44 44 PRO C C 175.59 0.16 1 283 44 44 PRO CA C 62.17 0.11 1 284 44 44 PRO CB C 32.78 0.17 1 285 44 44 PRO N N 136.52 0.39 1 286 45 45 GLY H H 8.01 0.07 1 287 45 45 GLY HA2 H 3.73 0.07 2 288 45 45 GLY HA3 H 4.08 0.07 2 289 45 45 GLY C C 174.59 0.16 1 290 45 45 GLY CA C 46.02 0.11 1 291 45 45 GLY N N 103.76 0.39 1 292 46 46 ALA H H 7.75 0.07 1 293 46 46 ALA HA H 5.07 0.07 1 294 46 46 ALA C C 176.87 0.16 1 295 46 46 ALA CA C 50.73 0.11 1 296 46 46 ALA CB C 20.11 0.17 1 297 46 46 ALA N N 123.11 0.39 1 298 47 47 THR H H 8.79 0.07 1 299 47 47 THR HB H 3.81 0.07 1 300 47 47 THR C C 173.71 0.16 1 301 47 47 THR CA C 61.73 0.11 1 302 47 47 THR CB C 71.92 0.17 1 303 47 47 THR N N 116.6 0.39 1 304 48 48 SER H H 9.51 0.07 1 305 48 48 SER C C 172.91 0.16 1 306 48 48 SER CA C 56.68 0.11 1 307 48 48 SER CB C 65.13 0.17 1 308 48 48 SER N N 123.56 0.39 1 309 49 49 LEU H H 9.17 0.07 1 310 49 49 LEU C C 175.32 0.16 1 311 49 49 LEU CA C 54.41 0.11 1 312 49 49 LEU CB C 45.82 0.17 1 313 49 49 LEU N N 125.28 0.39 1 314 50 50 TYR H H 8.12 0.07 1 315 50 50 TYR C C 172.56 0.16 1 316 50 50 TYR CA C 56.58 0.11 1 317 50 50 TYR CB C 39.64 0.17 1 318 50 50 TYR N N 117.36 0.39 1 319 51 51 TYR H H 9.66 0.07 1 320 51 51 TYR C C 176.34 0.16 1 321 51 51 TYR CA C 57.8 0.11 1 322 51 51 TYR CB C 40.93 0.17 1 323 51 51 TYR N N 122.55 0.39 1 324 52 52 TRP H H 9.09 0.07 1 325 52 52 TRP HD1 H 7.28 0.07 1 326 52 52 TRP HE1 H 10.04 0.07 1 327 52 52 TRP HZ2 H 7.41 0.07 1 328 52 52 TRP HH2 H 7.12 0.07 1 329 52 52 TRP C C 175.72 0.16 1 330 52 52 TRP CA C 56.8 0.11 1 331 52 52 TRP CB C 32.26 0.17 1 332 52 52 TRP N N 124.53 0.39 1 333 52 52 TRP NE1 N 130.37 0.39 1 334 53 53 GLU H H 9 0.07 1 335 53 53 GLU C C 176.61 0.16 1 336 53 53 GLU CA C 56.74 0.11 1 337 53 53 GLU CB C 27.24 0.17 1 338 53 53 GLU CG C 35.62 0.17 1 339 53 53 GLU CD C 184.36 0.16 1 340 53 53 GLU N N 127.35 0.39 1 341 54 54 GLY H H 8.31 0.07 1 342 54 54 GLY HA2 H 3.57 0.07 2 343 54 54 GLY HA3 H 4.06 0.07 2 344 54 54 GLY C C 173.55 0.16 1 345 54 54 GLY CA C 45.39 0.11 1 346 54 54 GLY N N 103.5 0.39 1 347 55 55 LYS H H 7.69 0.07 1 348 55 55 LYS HA H 4.52 0.07 1 349 55 55 LYS HB2 H 1.76 0.07 2 350 55 55 LYS C C 173.93 0.16 1 351 55 55 LYS CA C 54.37 0.11 1 352 55 55 LYS CB C 35.23 0.17 1 353 55 55 LYS CG C 24.38 0.17 1 354 55 55 LYS CD C 29.09 0.17 1 355 55 55 LYS CE C 42.29 0.17 1 356 55 55 LYS N N 121.69 0.39 1 357 56 56 LEU H H 8.22 0.07 1 358 56 56 LEU HA H 4.41 0.07 1 359 56 56 LEU HB2 H 1.42 0.07 2 360 56 56 LEU C C 175.71 0.16 1 361 56 56 LEU CA C 55.03 0.11 1 362 56 56 LEU CB C 41.72 0.17 1 363 56 56 LEU N N 125.46 0.39 1 364 57 57 GLU H H 9.04 0.07 1 365 57 57 GLU C C 173.9 0.16 1 366 57 57 GLU CA C 54.51 0.11 1 367 57 57 GLU CB C 31.37 0.17 1 368 57 57 GLU CG C 34.96 0.17 1 369 57 57 GLU CD C 183.21 0.16 1 370 57 57 GLU N N 131.43 0.39 1 371 58 58 GLN H H 8.12 0.07 1 372 58 58 GLN HA H 5.35 0.07 1 373 58 58 GLN HE21 H 6.57 0.07 2 374 58 58 GLN HE22 H 7.14 0.07 2 375 58 58 GLN C C 175.12 0.16 1 376 58 58 GLN CA C 53.75 0.11 1 377 58 58 GLN CB C 31.69 0.17 1 378 58 58 GLN CG C 33.39 0.17 1 379 58 58 GLN CD C 180.12 0.16 1 380 58 58 GLN N N 118.99 0.39 1 381 58 58 GLN NE2 N 110.88 0.39 1 382 59 59 GLU H H 8.94 0.07 1 383 59 59 GLU C C 174.87 0.16 1 384 59 59 GLU CA C 54.18 0.11 1 385 59 59 GLU CB C 33.63 0.17 1 386 59 59 GLU CG C 35.36 0.17 1 387 59 59 GLU CD C 183.72 0.16 1 388 59 59 GLU N N 123.69 0.39 1 389 60 60 TYR H H 8.76 0.07 1 390 60 60 TYR C C 175.61 0.16 1 391 60 60 TYR CA C 58.34 0.11 1 392 60 60 TYR CB C 38.59 0.17 1 393 60 60 TYR N N 126.03 0.39 1 394 61 61 GLU H H 8.29 0.07 1 395 61 61 GLU HB2 H 2.65 0.07 2 396 61 61 GLU C C 173.63 0.16 1 397 61 61 GLU CA C 54.36 0.11 1 398 61 61 GLU CB C 34.49 0.17 1 399 61 61 GLU N N 121.85 0.39 1 400 62 62 VAL H H 8.76 0.07 1 401 62 62 VAL C C 176.66 0.16 1 402 62 62 VAL CA C 60.38 0.11 1 403 62 62 VAL CB C 34.47 0.17 1 404 62 62 VAL CG1 C 20.6 0.17 1 405 62 62 VAL N N 118.26 0.39 1 406 63 63 GLN H H 8.59 0.07 1 407 63 63 GLN C C 174.09 0.16 1 408 63 63 GLN CA C 55.04 0.11 1 409 63 63 GLN CB C 30.52 0.17 1 410 63 63 GLN N N 127.54 0.39 1 411 64 64 MET H H 9.35 0.07 1 412 64 64 MET C C 176.27 0.16 1 413 64 64 MET CA C 54.3 0.11 1 414 64 64 MET CB C 35.83 0.17 1 415 64 64 MET N N 126.52 0.39 1 416 65 65 ILE H H 9.22 0.07 1 417 65 65 ILE C C 176.41 0.16 1 418 65 65 ILE CA C 61.15 0.11 1 419 65 65 ILE CB C 40.17 0.17 1 420 65 65 ILE CG1 C 32.77 0.17 1 421 65 65 ILE N N 122.63 0.39 1 422 66 66 LEU H H 10.1 0.07 1 423 66 66 LEU C C 175.29 0.16 1 424 66 66 LEU CA C 54.5 0.11 1 425 66 66 LEU CB C 44.36 0.17 1 426 66 66 LEU CD1 C 26.53 0.17 2 427 66 66 LEU CD2 C 23.52 0.17 2 428 66 66 LEU N N 128.56 0.39 1 429 67 67 LYS H H 8.04 0.07 1 430 67 67 LYS C C 175.55 0.16 1 431 67 67 LYS CA C 56.36 0.11 1 432 67 67 LYS CB C 33.09 0.17 1 433 67 67 LYS N N 122.05 0.39 1 434 68 68 THR H H 8.34 0.07 1 435 68 68 THR HA H 4.5 0.07 1 436 68 68 THR C C 171.86 0.16 1 437 68 68 THR CA C 59.92 0.11 1 438 68 68 THR CB C 68.7 0.17 1 439 68 68 THR CG2 C 21.87 0.17 1 440 68 68 THR N N 119.34 0.39 1 441 69 69 THR H H 8.06 0.07 1 442 69 69 THR HB H 4.54 0.07 1 443 69 69 THR C C 177.07 0.16 1 444 69 69 THR CA C 58.87 0.11 1 445 69 69 THR CB C 72.22 0.17 1 446 69 69 THR CG2 C 21.07 0.17 1 447 69 69 THR N N 110.57 0.39 1 448 70 70 VAL H H 8.86 0.07 1 449 70 70 VAL HA H 3.62 0.07 1 450 70 70 VAL C C 178.51 0.16 1 451 70 70 VAL CA C 65.75 0.11 1 452 70 70 VAL CB C 31.8 0.17 1 453 70 70 VAL CG1 C 22.09 0.17 2 454 70 70 VAL N N 121.58 0.39 1 455 71 71 SER H H 7.98 0.07 1 456 71 71 SER HA H 4.74 0.07 1 457 71 71 SER C C 175.31 0.16 1 458 71 71 SER CA C 60.31 0.11 1 459 71 71 SER CB C 62.94 0.17 1 460 71 71 SER N N 114.16 0.39 1 461 72 72 HIS H H 7.66 0.07 1 462 72 72 HIS C C 175.63 0.16 1 463 72 72 HIS CA C 56.33 0.11 1 464 72 72 HIS CB C 31.14 0.17 1 465 72 72 HIS N N 118.31 0.39 1 466 73 73 GLN H H 7.52 0.07 1 467 73 73 GLN HE21 H 5.92 0.07 2 468 73 73 GLN HE22 H 6.89 0.07 2 469 73 73 GLN C C 175.64 0.16 1 470 73 73 GLN CA C 60.21 0.11 1 471 73 73 GLN CB C 27.28 0.17 1 472 73 73 GLN CG C 31.82 0.17 1 473 73 73 GLN CD C 177.12 0.16 1 474 73 73 GLN N N 120.19 0.39 1 475 73 73 GLN NE2 N 106.39 0.39 1 476 74 74 GLN H H 8.41 0.07 1 477 74 74 GLN HA H 4.74 0.07 1 478 74 74 GLN HE21 H 6.89 0.07 2 479 74 74 GLN HE22 H 7.91 0.07 2 480 74 74 GLN C C 177.93 0.16 1 481 74 74 GLN CA C 59.06 0.11 1 482 74 74 GLN CB C 27.61 0.17 1 483 74 74 GLN CG C 33.28 0.17 1 484 74 74 GLN CD C 180.08 0.16 1 485 74 74 GLN N N 121.83 0.39 1 486 74 74 GLN NE2 N 113.69 0.39 1 487 75 75 ALA H H 8.49 0.07 1 488 75 75 ALA HA H 4.74 0.07 1 489 75 75 ALA C C 181.46 0.16 1 490 75 75 ALA CA C 54.57 0.11 1 491 75 75 ALA CB C 18.61 0.17 1 492 75 75 ALA N N 123.28 0.39 1 493 76 76 LEU H H 8.67 0.07 1 494 76 76 LEU C C 177.85 0.16 1 495 76 76 LEU CA C 58.57 0.11 1 496 76 76 LEU CB C 39.87 0.17 1 497 76 76 LEU N N 120.19 0.39 1 498 77 77 LEU H H 8.1 0.07 1 499 77 77 LEU C C 179.17 0.16 1 500 77 77 LEU CA C 59.38 0.11 1 501 77 77 LEU CB C 40.25 0.17 1 502 77 77 LEU CD1 C 27.99 0.17 2 503 77 77 LEU CD2 C 21.83 0.17 2 504 77 77 LEU N N 120.38 0.39 1 505 78 78 GLU H H 8.2 0.07 1 506 78 78 GLU HA H 4.33 0.07 1 507 78 78 GLU C C 178.96 0.16 1 508 78 78 GLU CA C 59.27 0.11 1 509 78 78 GLU CB C 29.39 0.17 1 510 78 78 GLU CG C 36.55 0.17 1 511 78 78 GLU CD C 183.48 0.16 1 512 78 78 GLU N N 117.99 0.39 1 513 79 79 CYS H H 8.11 0.07 1 514 79 79 CYS C C 178.07 0.16 1 515 79 79 CYS CA C 62.63 0.11 1 516 79 79 CYS CB C 27.44 0.17 1 517 79 79 CYS N N 122.13 0.39 1 518 80 80 LEU H H 8.46 0.07 1 519 80 80 LEU C C 178.32 0.16 1 520 80 80 LEU CA C 58.41 0.11 1 521 80 80 LEU N N 119.43 0.39 1 522 81 81 LYS H H 8.42 0.07 1 523 81 81 LYS C C 179.04 0.16 1 524 81 81 LYS CA C 59.79 0.11 1 525 81 81 LYS CB C 33.61 0.17 1 526 81 81 LYS N N 118.2 0.39 1 527 82 82 SER H H 7.97 0.07 1 528 82 82 SER HA H 4.13 0.07 1 529 82 82 SER C C 175.39 0.16 1 530 82 82 SER CA C 60.96 0.11 1 531 82 82 SER CB C 63.17 0.17 1 532 82 82 SER N N 112 0.39 1 533 83 83 HIS H H 7.28 0.07 1 534 83 83 HIS HA H 3.49 0.07 1 535 83 83 HIS C C 173.63 0.16 1 536 83 83 HIS CA C 56.67 0.11 1 537 83 83 HIS CB C 30.72 0.17 1 538 83 83 HIS N N 116.72 0.39 1 539 84 84 HIS H H 7.84 0.07 1 540 84 84 HIS C C 174.68 0.16 1 541 84 84 HIS CA C 56.58 0.11 1 542 84 84 HIS CB C 31.54 0.17 1 543 84 84 HIS N N 126.27 0.39 1 544 85 85 PRO C C 178.44 0.16 1 545 85 85 PRO CA C 63.76 0.11 1 546 85 85 PRO CB C 32.01 0.17 1 547 85 85 PRO N N 136.19 0.39 1 548 86 86 TYR H H 10.82 0.07 1 549 86 86 TYR C C 176.17 0.16 1 550 86 86 TYR CA C 54.04 0.11 1 551 86 86 TYR CB C 37.05 0.17 1 552 86 86 TYR N N 124.39 0.39 1 553 87 87 GLN H H 8.3 0.07 1 554 87 87 GLN HA H 4.25 0.07 1 555 87 87 GLN HB2 H 2.34 0.07 2 556 87 87 GLN HB3 H 1.94 0.07 2 557 87 87 GLN HE21 H 6.79 0.07 2 558 87 87 GLN HE22 H 7.5 0.07 2 559 87 87 GLN C C 177.19 0.16 1 560 87 87 GLN CA C 58.22 0.11 1 561 87 87 GLN CB C 29.23 0.17 1 562 87 87 GLN CG C 33.96 0.17 1 563 87 87 GLN CD C 180.67 0.16 1 564 87 87 GLN N N 120.39 0.39 1 565 87 87 GLN NE2 N 113.53 0.39 1 566 88 88 THR H H 7.75 0.07 1 567 88 88 THR HA H 4.28 0.07 1 568 88 88 THR HB H 3.62 0.07 1 569 88 88 THR HG2 H -0.84 0.07 1 570 88 88 THR C C 171.31 0.16 1 571 88 88 THR CA C 58.02 0.11 1 572 88 88 THR CB C 68.88 0.17 1 573 88 88 THR CG2 C 21.83 0.17 1 574 88 88 THR N N 112.93 0.39 1 575 89 89 PRO HA H 3.89 0.07 1 576 89 89 PRO C C 175.33 0.16 1 577 89 89 PRO CA C 61.63 0.11 1 578 89 89 PRO CB C 30.9 0.17 1 579 89 89 PRO CG C 27.75 0.17 1 580 89 89 PRO N N 137.43 0.39 1 581 90 90 GLU H H 8.15 0.07 1 582 90 90 GLU HA H 4.58 0.07 1 583 90 90 GLU HB2 H 3.03 0.07 1 584 90 90 GLU HB3 H 2.88 0.07 1 585 90 90 GLU C C 174.86 0.16 1 586 90 90 GLU CA C 56.46 0.11 1 587 90 90 GLU N N 121.23 0.39 1 588 91 91 LEU C C 175.11 0.16 1 589 91 91 LEU CA C 53.52 0.11 1 590 91 91 LEU CB C 46.02 0.17 1 591 92 92 LEU H H 7.99 0.07 1 592 92 92 LEU HA H 4.22 0.07 1 593 92 92 LEU C C 174.17 0.16 1 594 92 92 LEU CA C 53.28 0.11 1 595 92 92 LEU CB C 47.48 0.17 1 596 92 92 LEU N N 122.17 0.39 1 597 93 93 VAL H H 8.58 0.07 1 598 93 93 VAL HA H 4.71 0.07 1 599 93 93 VAL C C 173.68 0.16 1 600 93 93 VAL CA C 61.75 0.11 1 601 93 93 VAL CB C 32.71 0.17 1 602 93 93 VAL N N 121.74 0.39 1 603 94 94 LEU H H 9.67 0.07 1 604 94 94 LEU HA H 5.4 0.07 1 605 94 94 LEU C C 174.11 0.16 1 606 94 94 LEU CA C 51.77 0.11 1 607 94 94 LEU N N 128.84 0.39 1 608 95 95 PRO C C 173.86 0.16 1 609 95 95 PRO CA C 62.44 0.11 1 610 95 95 PRO CB C 32.41 0.17 1 611 95 95 PRO N N 132.94 0.39 1 612 96 96 VAL H H 7.1 0.07 1 613 96 96 VAL C C 179.05 0.16 1 614 96 96 VAL CA C 60.6 0.11 1 615 96 96 VAL CB C 32.89 0.17 1 616 96 96 VAL CG1 C 21.46 0.17 1 617 96 96 VAL CG2 C 21.46 0.17 1 618 96 96 VAL N N 117.03 0.39 1 619 97 97 THR H H 8.98 0.07 1 620 97 97 THR C C 175.26 0.16 1 621 97 97 THR CA C 62.63 0.11 1 622 97 97 THR CB C 68.45 0.17 1 623 97 97 THR N N 120.08 0.39 1 624 98 98 HIS H H 7.84 0.07 1 625 98 98 HIS HA H 4.12 0.07 1 626 98 98 HIS C C 171.8 0.16 1 627 98 98 HIS CA C 55.69 0.11 1 628 98 98 HIS CB C 32.95 0.17 1 629 98 98 HIS N N 120.26 0.39 1 630 99 99 GLY H H 7.15 0.07 1 631 99 99 GLY HA2 H 3.75 0.07 2 632 99 99 GLY HA3 H 4.2 0.07 2 633 99 99 GLY C C 170.7 0.16 1 634 99 99 GLY CA C 44.7 0.11 1 635 99 99 GLY N N 108.27 0.39 1 636 100 100 ASP H H 7.49 0.07 1 637 100 100 ASP C C 176.53 0.16 1 638 100 100 ASP CA C 54.56 0.11 1 639 100 100 ASP CB C 45.98 0.17 1 640 100 100 ASP N N 119.72 0.39 1 641 101 101 THR H H 8.79 0.07 1 642 101 101 THR HB H 4.17 0.07 1 643 101 101 THR C C 176.44 0.16 1 644 101 101 THR CA C 66.54 0.11 1 645 101 101 THR CB C 68.67 0.17 1 646 101 101 THR CG2 C 21.94 0.17 1 647 101 101 THR N N 123.67 0.39 1 648 102 102 ASP H H 8.14 0.07 1 649 102 102 ASP C C 179.12 0.16 1 650 102 102 ASP CA C 57.62 0.11 1 651 102 102 ASP CB C 40.25 0.17 1 652 102 102 ASP CG C 179.59 0.16 1 653 102 102 ASP N N 123.52 0.39 1 654 103 103 TYR H H 8.67 0.07 1 655 103 103 TYR HA H 3.82 0.07 1 656 103 103 TYR C C 177.35 0.16 1 657 103 103 TYR CA C 63.03 0.11 1 658 103 103 TYR CB C 38.24 0.17 1 659 103 103 TYR N N 125.42 0.39 1 660 104 104 LEU H H 8.71 0.07 1 661 104 104 LEU C C 180.34 0.16 1 662 104 104 LEU CA C 58.06 0.11 1 663 104 104 LEU CB C 40.7 0.17 1 664 104 104 LEU N N 118.6 0.39 1 665 105 105 SER H H 8.35 0.07 1 666 105 105 SER C C 176.74 0.16 1 667 105 105 SER CA C 61.85 0.11 1 668 105 105 SER CB C 66.95 0.17 1 669 105 105 SER N N 117.03 0.39 1 670 106 106 TRP H H 7.95 0.07 1 671 106 106 TRP HA H 4.13 0.07 1 672 106 106 TRP HB2 H 3.396 0.07 2 673 106 106 TRP HB3 H 3.155 0.07 2 674 106 106 TRP HD1 H 7.22 0.07 1 675 106 106 TRP HE1 H 9.9 0.07 1 676 106 106 TRP HZ2 H 7.57 0.07 1 677 106 106 TRP HH2 H 6.99 0.07 1 678 106 106 TRP C C 178.28 0.16 1 679 106 106 TRP CA C 61.71 0.11 1 680 106 106 TRP CB C 27.5 0.17 1 681 106 106 TRP N N 126.3 0.39 1 682 106 106 TRP NE1 N 131.01 0.39 1 683 107 107 LEU H H 8.56 0.07 1 684 107 107 LEU HA H 4.15 0.07 1 685 107 107 LEU HB2 H 2.12 0.07 2 686 107 107 LEU HB3 H 1.83 0.07 2 687 107 107 LEU C C 178.21 0.16 1 688 107 107 LEU CA C 58.5 0.11 1 689 107 107 LEU CB C 42.21 0.17 1 690 107 107 LEU N N 123.73 0.39 1 691 108 108 ASN H H 7.55 0.07 1 692 108 108 ASN HD21 H 6.97 0.07 2 693 108 108 ASN HD22 H 7.39 0.07 2 694 108 108 ASN C C 178.11 0.16 1 695 108 108 ASN CA C 56.66 0.11 1 696 108 108 ASN CB C 39.57 0.17 1 697 108 108 ASN CG C 176.34 0.16 1 698 108 108 ASN N N 114.75 0.39 1 699 108 108 ASN ND2 N 112.72 0.39 1 700 109 109 ALA H H 8.17 0.07 1 701 109 109 ALA HA H 4.07 0.07 1 702 109 109 ALA HB H 0.85 0.07 1 703 109 109 ALA C C 179.78 0.16 1 704 109 109 ALA CA C 54.5 0.11 1 705 109 109 ALA CB C 17.94 0.17 1 706 109 109 ALA N N 122.25 0.39 1 707 110 110 SER H H 7.56 0.07 1 708 110 110 SER C C 173.7 0.16 1 709 110 110 SER CA C 60.6 0.11 1 710 110 110 SER CB C 63.09 0.17 1 711 110 110 SER N N 114.05 0.39 1 712 111 111 LEU H H 6.69 0.07 1 713 111 111 LEU HA H 4.69 0.07 1 714 111 111 LEU C C 176.31 0.16 1 715 111 111 LEU CA C 53.56 0.11 1 716 111 111 LEU CB C 42.06 0.17 1 717 111 111 LEU N N 119.08 0.39 1 718 112 112 ARG H H 7.44 0.07 1 719 112 112 ARG CA C 58.45 0.11 1 720 112 112 ARG N N 125.8 0.39 1 stop_ save_