data_4466 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift assignments for Cu(I) Pseudoazurin from Paracoccus pantotrophus ; _BMRB_accession_number 4466 _BMRB_flat_file_name bmr4466.str _Entry_type original _Submission_date 1999-11-30 _Accession_date 1999-12-01 _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 Thompson Gary S. . 2 Leung Yun-Chung . . 3 Ferguson Stuart J. . 4 Radford Sheena E. . 5 Redfield Christina . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 694 "15N chemical shifts" 121 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-09 update author 'Correction of system description.' 2002-06-11 original author 'Original release.' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Structure and Dynamics in Solution of Cu(I) Pseudoazurin from Paracoccus pantotrophus. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Thompson Gary S. . 2 Leung Yun-Chung . . 3 Ferguson Stuart J. . 4 Radford Sheena E. . 5 Redfield Christina . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein Science' _Journal_volume 9 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 846 _Page_last 858 _Year 2000 _Details . loop_ _Keyword 'nuclear magnetic resonance' dynamics structure cupredoxin 'electron transfer' stop_ save_ ####################################### # Cited references within the entry # ####################################### save_live_cs_ref _Saveframe_category citation _Citation_full ; Protein NMR Spectroscopy, (Principles and Paractice) Cavanagh J., Fairbrother W. J., Palmer III A. G., & Skelton N. J. 1st Edn. Academic Press, 1996. page 175-176. ; _Citation_title . _Citation_status . _Citation_type . _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? _Journal_abbreviation . _Journal_name_full . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_system_pazcui _Saveframe_category molecular_system _Mol_system_name 'Cu(I) Pseudoazurin' _Abbreviation_common paz _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Pseudoazurin $paz 'Copper I ion' $CU1 stop_ _System_molecular_weight 13404.83 _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Biological_function 'Electron transfer' stop_ _Database_query_date . _Details 'The system contains a reduced [Cu(I)] ion.' save_ ######################## # Monomeric polymers # ######################## save_paz _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common pseudoazurin _Abbreviation_common paz _Molecular_mass 13341.29 _Mol_thiol_state 'all other bound' loop_ _Biological_function 'Electron transfer' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 123 _Mol_residue_sequence ; ATHEVHMLNKGESGAMVFEP AFVRAEPGDVINFVPTDKSH NVEAIKEILPEGVESFKSKI NESYTLTVTEPGLYGVKCTP HFGMGMVGLVQVGDAPENLD AAKTAKMPKKARERMDAELA QVN ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 THR 3 HIS 4 GLU 5 VAL 6 HIS 7 MET 8 LEU 9 ASN 10 LYS 11 GLY 12 GLU 13 SER 14 GLY 15 ALA 16 MET 17 VAL 18 PHE 19 GLU 20 PRO 21 ALA 22 PHE 23 VAL 24 ARG 25 ALA 26 GLU 27 PRO 28 GLY 29 ASP 30 VAL 31 ILE 32 ASN 33 PHE 34 VAL 35 PRO 36 THR 37 ASP 38 LYS 39 SER 40 HIS 41 ASN 42 VAL 43 GLU 44 ALA 45 ILE 46 LYS 47 GLU 48 ILE 49 LEU 50 PRO 51 GLU 52 GLY 53 VAL 54 GLU 55 SER 56 PHE 57 LYS 58 SER 59 LYS 60 ILE 61 ASN 62 GLU 63 SER 64 TYR 65 THR 66 LEU 67 THR 68 VAL 69 THR 70 GLU 71 PRO 72 GLY 73 LEU 74 TYR 75 GLY 76 VAL 77 LYS 78 CYS 79 THR 80 PRO 81 HIS 82 PHE 83 GLY 84 MET 85 GLY 86 MET 87 VAL 88 GLY 89 LEU 90 VAL 91 GLN 92 VAL 93 GLY 94 ASP 95 ALA 96 PRO 97 GLU 98 ASN 99 LEU 100 ASP 101 ALA 102 ALA 103 LYS 104 THR 105 ALA 106 LYS 107 MET 108 PRO 109 LYS 110 LYS 111 ALA 112 ARG 113 GLU 114 ARG 115 MET 116 ASP 117 ALA 118 GLU 119 LEU 120 ALA 121 GLN 122 VAL 123 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-06 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 1ADW Pseudoazurin 100.00 123 100.00 100.00 9.52e-84 PDB 3ERX "High-Resolution Structure Of Paracoccus Pantotrophus Pseudoazurin" 100.00 123 100.00 100.00 9.52e-84 PDB 4BWT "Three-dimensional Structure Of Paracoccus Pantotrophus Pseudoazurin At Ph 6.5" 100.00 123 100.00 100.00 9.52e-84 PDB 4BWU "Three-dimensional Structure Of The K109a Mutant Of Paracoccus Pantotrophus Pseudoazurin At Ph 5.5" 100.00 123 99.19 99.19 6.51e-83 PDB 4BXV "Three-dimensional Structure Of The Mutant K109a Of Paracoccus Pantotrophus Pseudoazurin At Ph 7.0" 100.00 123 99.19 99.19 6.51e-83 EMBL CAA93848 "pseudoazurin [Paracoccus denitrificans]" 100.00 145 100.00 100.00 6.55e-84 EMBL CAA97485 "pseudoazurin [Paracoccus denitrificans]" 100.00 145 100.00 100.00 6.55e-84 GB KGJ09874 "pseudoazurin [Paracoccus versutus]" 100.00 145 97.56 100.00 2.08e-82 REF WP_024842647 "pseudoazurin [Paracoccus pantotrophus]" 100.00 145 100.00 100.00 6.55e-84 REF WP_036756592 "pseudoazurin [Paracoccus versutus]" 100.00 145 97.56 100.00 2.08e-82 SP P80401 "RecName: Full=Pseudoazurin; Flags: Precursor" 100.00 145 100.00 100.00 6.55e-84 stop_ save_ ############# # Ligands # ############# save_CU1 _Saveframe_category ligand _Mol_type non-polymer _Name_common "CU1 (COPPER (I) ION)" _BMRB_code . _PDB_code CU1 _Molecular_mass 63.546 _Mol_charge 1 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 18 11:12:40 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CU CU CU . 1 . ? 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 _Strain _Fraction _Gene_mnemonic _Details $paz 'Paracoccus pantotrophus' 82367 Prokaryote Monera Paracoccus pantotrophus 'LMD 82.5' cytoplasm pazS ; see: Leung Y. C., Chan C., Reader J. S., Willis A. C., van Spanning R. J. M., Ferguson & Radford S. E. (1997) The pseudoazurin gene from Thiosphaera pantotropha: Analysis of an upstream putative regulatory sequences and overexpression in Escherichia coli. Biochem J. 321, 699-705. ; stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name _Vendor_name _Details $paz 'recombinant technology' 'E. coli' Escherichia coli ; XL1-Blue {endA1,hsdR17 (rk-, mk+), supE44, thi-, k-, recA1, gyrA96, relA1 (lac), [F', proAB, lacIq, lacZDM15, Tn10Tc]' ; plasmid pJR2 'Stratgene, Cambridge, UK.' ; Pseudoazurin pazS (see Leung, Y. C., Chan, C., Reader, J.S., Willis, A.C.,van Spamming, R.J.M., Ferguson, S.J., & Radford, S.E. Biochem. J. v321, 699-705 (1997).) ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_pazcu1_h2o_sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $paz 3 mM [U-15N] $CU1 3 mM . H2O 95 % . D2O 5 % . Na2S2O4 6.6 mM . PO42- 20 mM . stop_ save_ save_pazcu1_d2o_sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $paz 3 mM [U-15N] $CU1 3 mM . D2O 100 % . Na2S2O4 6.6 mM . PO42- 20 mM . stop_ save_ ############################ # Computer software used # ############################ save_felix _Saveframe_category software _Name FELIX _Version 2.3 loop_ _Vendor _Address _Electronic_address MSI '9685 Scranton Road, San Diego, CA 92121-3752, U.S.A.' www.biosym.com stop_ loop_ _Task 'raw spectral data (FID) transformations' 'strip extraction' 'initial chemical shift measurements' stop_ _Details . save_ save_nmrview _Saveframe_category software _Name NMRView _Version '2.00 - 4.03' loop_ _Vendor _Address _Electronic_address 'Bruce Johnson, Merck and Co.' 'Whitehouse Station, NJ USA.' www.nmrview.com stop_ loop_ _Task 'peak picking' 'computer aided assignment' 'restraint generation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_oxford_omega _Saveframe_category NMR_spectrometer _Manufacturer homebuilt _Model . _Field_strength 750 _Details ; Homebuilt spectrometers using Oxford Instruments magnet, GE/Omega software and homebuilt probes homebuilt additions from OCMS. ; save_ ############################# # NMR applied experiments # ############################# save_1H_-_1H_double_quantum_filtered_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H - 1H double quantum filtered COSY' _Sample_label $pazcu1_d2o_sample1 save_ save_1H_-_1H_60ms_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H - 1H 60ms TOCSY' _Sample_label $pazcu1_d2o_sample1 save_ save_1H_-_1H_200ms_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H - 1H 200ms NOESY' _Sample_label $pazcu1_d2o_sample1 save_ ####################### # Sample conditions # ####################### save_standard_conditions _Saveframe_category sample_conditions _Details ; Identical conditions were used for both D2O and H2O samples except that for the D2O sample a pH* rather than a pH measurement was made. ; loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.6 . pH temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_standard_referencing _Saveframe_category chemical_shift_reference _Details ; All chemical shifts were related to the 1H chemical shift of H2O at pH 6.6 and 298K the 15N chemical shift corresponding to 76.016153 is calculated as 119.591ppm. ; 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 _Reference_correction_type _Correction_value H2O H 1 proton ppm 4.746 internal direct . . . 1.0 . pH -0.008 H2O N 15 proton ppm 4.746 internal indirect . . . 0.101329144 $live_cs_ref pH -0.008 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_pazcui_chemical_shifts _Saveframe_category assigned_chemical_shifts _Details ; Chemical shifts are derived from 3D and 2D data set. Where possible shifts are measured from the higher resolution data set. Uncertainties are derived either from the measured scatter in the chemical shifts, or the chemical shift resolution whichever is the bigger. ; loop_ _Software_label $nmrview stop_ loop_ _Sample_label $pazcu1_h2o_sample1 $pazcu1_d2o_sample1 stop_ _Sample_conditions_label $standard_conditions _Chem_shift_reference_set_label $standard_referencing _Mol_system_component_name Pseudoazurin _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 ALA HA H 4.012 0.005 1 2 . 1 ALA HB H 1.311 0.005 1 3 . 2 THR N N 116.810 0.002 1 4 . 2 THR H H 8.375 0.002 1 5 . 2 THR HA H 5.149 0.005 1 6 . 2 THR HB H 3.770 0.005 2 7 . 2 THR HG2 H 0.988 0.005 1 8 . 3 HIS N N 126.211 0.002 1 9 . 3 HIS H H 8.993 0.002 1 10 . 3 HIS HA H 4.749 0.005 1 11 . 3 HIS HB2 H 2.862 0.001 2 12 . 3 HIS HB3 H 2.651 0.005 1 13 . 3 HIS HD1 H 6.594 0.005 1 14 . 3 HIS HE1 H 7.804 0.005 1 15 . 4 GLU N N 123.865 0.002 1 16 . 4 GLU H H 8.655 0.002 1 17 . 4 GLU HA H 5.001 0.005 1 18 . 4 GLU HB2 H 1.885 0.021 2 19 . 4 GLU HB3 H 1.946 0.008 2 20 . 4 GLU HG2 H 2.186 0.004 1 21 . 4 GLU HG3 H 2.186 0.004 1 22 . 5 VAL N N 127.316 0.002 1 23 . 5 VAL H H 8.954 0.002 1 24 . 5 VAL HA H 4.342 0.005 1 25 . 5 VAL HB H 1.337 0.005 1 26 . 5 VAL HG1 H 0.346 0.005 2 27 . 5 VAL HG2 H 1.105 0.005 2 28 . 6 HIS N N 124.761 0.002 1 29 . 6 HIS H H 9.100 0.002 1 30 . 6 HIS HA H 5.502 0.005 1 31 . 6 HIS HB2 H 3.171 0.019 1 32 . 6 HIS HB3 H 3.171 0.019 1 33 . 6 HIS HD1 H 7.044 0.005 1 34 . 6 HIS HE1 H 8.367 0.005 1 35 . 7 MET N N 121.057 0.002 1 36 . 7 MET H H 7.948 0.002 1 37 . 7 MET HA H 4.259 0.005 1 38 . 7 MET HB2 H 1.982 0.001 2 39 . 7 MET HB3 H 2.124 0.003 2 40 . 7 MET HG2 H 1.369 0.003 1 41 . 7 MET HG3 H 1.369 0.003 1 42 . 7 MET HE H 1.882 0.027 1 43 . 8 LEU N N 121.227 0.002 1 44 . 8 LEU H H 8.171 0.002 1 45 . 8 LEU HA H 4.851 0.005 1 46 . 8 LEU HB2 H 1.265 0.002 2 47 . 8 LEU HB3 H 1.457 0.008 2 48 . 8 LEU HG H 1.351 0.005 1 49 . 8 LEU HD1 H 0.825 0.005 2 50 . 8 LEU HD2 H 0.917 0.005 2 51 . 9 ASN N N 120.161 0.002 1 52 . 9 ASN H H 10.410 0.002 1 53 . 9 ASN HA H 4.835 0.005 1 54 . 9 ASN HB2 H 2.748 0.022 1 55 . 9 ASN HB3 H 2.748 0.022 1 56 . 9 ASN HD21 H 7.467 0.005 2 57 . 9 ASN HD22 H 7.375 0.005 2 58 . 9 ASN ND2 N 110.777 0.002 1 59 . 10 LYS N N 121.615 0.002 1 60 . 10 LYS H H 8.258 0.002 1 61 . 10 LYS HA H 4.723 0.005 1 62 . 10 LYS HB2 H 1.660 0.016 2 63 . 10 LYS HB3 H 1.765 0.002 2 64 . 10 LYS HG2 H 1.262 0.003 1 65 . 10 LYS HG3 H 1.262 0.003 1 66 . 10 LYS HD2 H 1.598 0.005 1 67 . 10 LYS HD3 H 1.598 0.005 1 68 . 10 LYS HE2 H 2.952 0.005 1 69 . 10 LYS HE3 H 2.952 0.005 1 70 . 11 GLY N N 112.478 0.002 1 71 . 11 GLY H H 8.586 0.002 1 72 . 11 GLY HA2 H 4.567 0.005 2 73 . 11 GLY HA3 H 3.840 0.003 2 74 . 12 GLU N N 123.993 0.002 1 75 . 12 GLU H H 9.660 0.002 1 76 . 12 GLU HA H 4.044 0.005 1 77 . 12 GLU HB2 H 2.072 0.006 1 78 . 12 GLU HB3 H 2.072 0.006 1 79 . 12 GLU HG2 H 2.368 0.003 1 80 . 12 GLU HG3 H 2.368 0.003 1 81 . 13 SER N N 110.387 0.002 1 82 . 13 SER H H 8.765 0.002 1 83 . 13 SER HA H 4.485 0.005 1 84 . 13 SER HB2 H 3.939 0.018 2 85 . 13 SER HB3 H 4.004 0.005 2 86 . 14 GLY N N 109.345 0.002 1 87 . 14 GLY H H 7.517 0.002 1 88 . 14 GLY HA2 H 4.373 0.005 2 89 . 14 GLY HA3 H 3.708 0.011 2 90 . 15 ALA N N 121.608 0.002 1 91 . 15 ALA H H 8.321 0.002 1 92 . 15 ALA HA H 4.871 0.005 1 93 . 15 ALA HB H 1.400 0.005 1 94 . 16 MET N N 120.219 0.002 1 95 . 16 MET H H 8.580 0.002 1 96 . 16 MET HA H 4.080 0.005 1 97 . 16 MET HB2 H 2.335 0.021 2 98 . 16 MET HB3 H 2.508 0.013 2 99 . 16 MET HG2 H 1.807 0.021 1 100 . 16 MET HG3 H 1.807 0.021 1 101 . 16 MET HE H 1.693 0.003 1 102 . 17 VAL N N 108.948 0.002 1 103 . 17 VAL H H 7.866 0.002 1 104 . 17 VAL HA H 5.037 0.005 1 105 . 17 VAL HB H 1.919 0.005 1 106 . 17 VAL HG1 H 0.471 0.005 2 107 . 17 VAL HG2 H 0.571 0.005 2 108 . 18 PHE N N 119.266 0.002 1 109 . 18 PHE H H 8.321 0.002 1 110 . 18 PHE HA H 4.931 0.005 1 111 . 18 PHE HB2 H 2.791 0.006 2 112 . 18 PHE HB3 H 2.578 0.005 2 113 . 18 PHE HD1 H 6.905 0.005 1 114 . 18 PHE HD2 H 6.905 0.005 1 115 . 18 PHE HE1 H 7.079 0.005 1 116 . 18 PHE HE2 H 7.079 0.005 1 117 . 18 PHE HZ H 7.144 0.005 1 118 . 19 GLU N N 121.227 0.002 1 119 . 19 GLU H H 9.067 0.002 1 120 . 19 GLU HA H 4.830 0.005 1 121 . 19 GLU HB2 H 1.798 0.003 2 122 . 19 GLU HB3 H 2.027 0.003 2 123 . 19 GLU HG2 H 2.099 0.019 1 124 . 19 GLU HG3 H 2.099 0.019 1 125 . 20 PRO HA H 4.835 0.002 1 126 . 20 PRO HB2 H 2.244 0.005 2 127 . 20 PRO HB3 H 2.588 0.001 2 128 . 20 PRO HG2 H 2.042 0.018 2 129 . 20 PRO HG3 H 2.174 0.003 2 130 . 20 PRO HD2 H 3.667 0.003 2 131 . 20 PRO HD3 H 4.097 0.003 2 132 . 21 ALA N N 121.195 0.002 1 133 . 21 ALA H H 8.329 0.002 1 134 . 21 ALA HA H 4.199 0.005 1 135 . 21 ALA HB H 1.839 0.005 1 136 . 22 PHE N N 114.992 0.002 1 137 . 22 PHE H H 7.333 0.002 1 138 . 22 PHE HA H 5.708 0.005 1 139 . 22 PHE HB2 H 2.930 0.005 2 140 . 22 PHE HB3 H 2.774 0.015 2 141 . 22 PHE HD1 H 6.965 0.005 1 142 . 22 PHE HD2 H 6.965 0.005 1 143 . 22 PHE HE1 H 7.085 0.005 1 144 . 22 PHE HE2 H 7.085 0.005 1 145 . 22 PHE HZ H 7.589 0.005 1 146 . 23 VAL N N 126.871 0.002 1 147 . 23 VAL H H 7.659 0.002 1 148 . 23 VAL HA H 3.701 0.005 1 149 . 23 VAL HB H 1.368 0.005 1 150 . 23 VAL HG1 H 0.099 0.005 2 151 . 23 VAL HG2 H 0.490 0.005 2 152 . 24 ARG N N 126.682 0.002 1 153 . 24 ARG H H 8.177 0.002 1 154 . 24 ARG HA H 4.676 0.005 1 155 . 24 ARG HB2 H 1.933 0.028 1 156 . 24 ARG HB3 H 1.933 0.028 1 157 . 24 ARG HG2 H 1.711 0.018 1 158 . 24 ARG HG3 H 1.711 0.018 1 159 . 24 ARG HD2 H 3.059 0.003 2 160 . 24 ARG HD3 H 3.317 0.007 2 161 . 25 ALA N N 130.728 0.002 1 162 . 25 ALA H H 9.388 0.002 1 163 . 25 ALA HA H 4.740 0.005 1 164 . 25 ALA HB H 0.968 0.005 1 165 . 26 GLU N N 119.266 0.002 1 166 . 26 GLU H H 8.316 0.002 1 167 . 26 GLU HA H 4.805 0.005 1 168 . 26 GLU HB2 H 1.529 0.003 2 169 . 26 GLU HB3 H 2.071 0.003 2 170 . 26 GLU HG2 H 2.191 0.003 2 171 . 26 GLU HG3 H 2.379 0.003 2 172 . 27 PRO HA H 3.903 0.004 1 173 . 27 PRO HB2 H 1.870 0.003 2 174 . 27 PRO HB3 H 2.399 0.027 2 175 . 27 PRO HG2 H 2.266 0.003 1 176 . 27 PRO HG3 H 2.266 0.003 1 177 . 27 PRO HD2 H 3.445 0.012 2 178 . 27 PRO HD3 H 3.729 0.011 2 179 . 28 GLY N N 114.741 0.002 1 180 . 28 GLY H H 9.392 0.002 1 181 . 28 GLY HA2 H 4.384 0.005 2 182 . 28 GLY HA3 H 3.447 0.003 2 183 . 29 ASP N N 121.495 0.002 1 184 . 29 ASP H H 8.051 0.002 1 185 . 29 ASP HA H 4.835 0.005 1 186 . 29 ASP HB2 H 2.955 0.005 2 187 . 29 ASP HB3 H 2.653 0.001 2 188 . 30 VAL N N 115.739 0.002 1 189 . 30 VAL H H 7.997 0.002 1 190 . 30 VAL HA H 4.697 0.005 1 191 . 30 VAL HB H 1.769 0.005 1 192 . 30 VAL HG1 H 0.681 0.005 2 193 . 30 VAL HG2 H 0.836 0.005 2 194 . 31 ILE N N 126.266 0.002 1 195 . 31 ILE H H 9.397 0.002 1 196 . 31 ILE HA H 4.556 0.005 1 197 . 31 ILE HB H 1.741 0.005 1 198 . 31 ILE HG13 H 1.037 0.005 2 199 . 31 ILE HG12 H 0.948 0.003 2 200 . 31 ILE HG2 H -0.074 0.005 1 201 . 31 ILE HD1 H 0.396 0.005 1 202 . 32 ASN N N 125.100 0.002 1 203 . 32 ASN H H 8.764 0.002 1 204 . 32 ASN HA H 5.220 0.005 1 205 . 32 ASN HB2 H 2.510 0.003 2 206 . 32 ASN HB3 H 2.428 0.001 2 207 . 32 ASN HD21 H 7.397 0.008 2 208 . 32 ASN HD22 H 6.491 0.005 2 209 . 32 ASN ND2 N 111.285 0.002 1 210 . 33 PHE N N 124.024 0.002 1 211 . 33 PHE H H 9.432 0.002 1 212 . 33 PHE HA H 5.170 0.005 1 213 . 33 PHE HB2 H 3.013 0.008 2 214 . 33 PHE HB3 H 3.247 0.002 2 215 . 33 PHE HD1 H 7.211 0.005 1 216 . 33 PHE HD2 H 7.211 0.005 1 217 . 33 PHE HE1 H 6.869 0.005 1 218 . 33 PHE HE2 H 6.869 0.005 1 219 . 33 PHE HZ H 6.626 0.005 1 220 . 34 VAL N N 123.839 0.002 1 221 . 34 VAL H H 9.240 0.002 1 222 . 34 VAL HA H 4.627 0.005 1 223 . 34 VAL HB H 1.716 0.005 1 224 . 34 VAL HG1 H 0.770 0.005 2 225 . 34 VAL HG2 H 0.809 0.005 2 226 . 35 PRO HA H 4.966 0.004 1 227 . 35 PRO HB2 H 1.878 0.003 2 228 . 35 PRO HB3 H 1.899 0.003 2 229 . 35 PRO HG2 H 2.108 0.003 2 230 . 35 PRO HG3 H 2.292 0.019 2 231 . 35 PRO HD2 H 3.579 0.029 2 232 . 35 PRO HD3 H 3.880 0.001 2 233 . 36 THR N N 124.921 0.002 1 234 . 36 THR H H 8.728 0.002 1 235 . 36 THR HA H 3.887 0.005 1 236 . 36 THR HB H 3.997 0.001 2 237 . 36 THR HG2 H 1.163 0.001 1 238 . 37 ASP N N 116.880 0.002 1 239 . 37 ASP H H 7.577 0.002 1 240 . 37 ASP HA H 5.164 0.005 1 241 . 37 ASP HB2 H 2.458 0.004 2 242 . 37 ASP HB3 H 2.841 0.024 2 243 . 38 LYS N N 117.549 0.002 1 244 . 38 LYS H H 8.167 0.002 1 245 . 38 LYS HA H 4.459 0.005 1 246 . 38 LYS HB2 H 1.732 0.001 2 247 . 38 LYS HB3 H 1.913 0.002 2 248 . 38 LYS HG2 H 1.480 0.009 2 249 . 38 LYS HG3 H 1.618 0.004 2 250 . 38 LYS HD2 H 1.694 0.005 1 251 . 38 LYS HD3 H 1.694 0.005 1 252 . 38 LYS HE2 H 2.910 0.005 1 253 . 38 LYS HE3 H 2.910 0.005 1 254 . 39 SER N N 113.520 0.002 1 255 . 39 SER H H 9.185 0.002 1 256 . 39 SER HA H 3.816 0.005 1 257 . 39 SER HB2 H 3.728 0.003 2 258 . 39 SER HB3 H 3.982 0.003 2 259 . 40 HIS N N 120.605 0.002 1 260 . 40 HIS H H 8.017 0.002 1 261 . 40 HIS HA H 5.703 0.005 1 262 . 40 HIS HB2 H 2.736 0.007 2 263 . 40 HIS HB3 H 3.370 0.001 1 264 . 40 HIS HD1 H 6.696 0.005 1 265 . 40 HIS HE1 H 7.510 0.005 1 266 . 41 ASN N N 125.416 0.002 1 267 . 41 ASN H H 9.803 0.002 1 268 . 41 ASN HA H 4.845 0.005 1 269 . 41 ASN HB2 H 2.285 0.011 2 270 . 41 ASN HB3 H 2.761 0.018 2 271 . 41 ASN HD21 H 7.253 0.005 2 272 . 41 ASN HD22 H 6.823 0.005 2 273 . 41 ASN ND2 N 107.448 0.002 1 274 . 42 VAL N N 111.818 0.002 1 275 . 42 VAL H H 7.485 0.002 1 276 . 42 VAL HA H 4.787 0.005 1 277 . 42 VAL HB H 1.581 0.005 1 278 . 42 VAL HG1 H 0.199 0.005 2 279 . 42 VAL HG2 H 0.386 0.005 2 280 . 43 GLU N N 126.213 0.002 1 281 . 43 GLU H H 9.295 0.002 1 282 . 43 GLU HA H 4.487 0.005 1 283 . 43 GLU HB2 H 1.529 0.003 1 284 . 43 GLU HB3 H 1.529 0.003 1 285 . 43 GLU HG2 H 2.186 0.039 2 286 . 43 GLU HG3 H 2.397 0.005 2 287 . 44 ALA N N 124.867 0.002 1 288 . 44 ALA H H 7.162 0.002 1 289 . 44 ALA HA H 3.872 0.005 1 290 . 44 ALA HB H 0.609 0.005 1 291 . 45 ILE N N 122.597 0.002 1 292 . 45 ILE H H 8.022 0.002 1 293 . 45 ILE HA H 3.804 0.005 1 294 . 45 ILE HB H 1.527 0.005 1 295 . 45 ILE HG13 H 0.824 0.018 2 296 . 45 ILE HG12 H 1.227 0.003 2 297 . 45 ILE HG2 H 0.909 0.005 1 298 . 45 ILE HD1 H 0.441 0.059 1 299 . 46 LYS N N 127.697 0.002 1 300 . 46 LYS H H 8.307 0.002 1 301 . 46 LYS HA H 3.596 0.005 1 302 . 46 LYS HB2 H 1.685 0.013 2 303 . 46 LYS HB3 H 1.754 0.003 2 304 . 46 LYS HG2 H 1.339 0.011 1 305 . 46 LYS HG3 H 1.339 0.011 1 306 . 46 LYS HD2 H 1.643 0.005 1 307 . 46 LYS HD3 H 1.643 0.005 1 308 . 46 LYS HE2 H 2.951 0.005 1 309 . 46 LYS HE3 H 2.951 0.005 1 310 . 47 GLU N N 114.058 0.002 1 311 . 47 GLU H H 8.764 0.002 1 312 . 47 GLU HA H 4.049 0.005 1 313 . 47 GLU HB2 H 1.802 0.006 2 314 . 47 GLU HB3 H 2.087 0.007 2 315 . 47 GLU HG2 H 2.265 0.003 2 316 . 47 GLU HG3 H 2.542 0.009 2 317 . 48 ILE N N 120.735 0.002 1 318 . 48 ILE H H 8.274 0.002 1 319 . 48 ILE HA H 3.989 0.005 1 320 . 48 ILE HB H 1.653 0.006 1 321 . 48 ILE HG13 H 0.807 0.003 2 322 . 48 ILE HG12 H 1.327 0.009 2 323 . 48 ILE HG2 H 0.648 0.024 1 324 . 48 ILE HD1 H 0.557 0.003 1 325 . 49 LEU N N 121.073 0.002 1 326 . 49 LEU H H 7.154 0.002 1 327 . 49 LEU HA H 4.794 0.005 1 328 . 49 LEU HB2 H 1.452 0.003 2 329 . 49 LEU HB3 H 1.236 0.003 2 330 . 49 LEU HG H 1.675 0.005 1 331 . 49 LEU HD1 H 0.765 0.005 2 332 . 49 LEU HD2 H 0.920 0.005 2 333 . 50 PRO HA H 4.254 0.003 1 334 . 50 PRO HB2 H 1.476 0.005 2 335 . 50 PRO HB3 H 2.414 0.003 2 336 . 50 PRO HG2 H 1.202 0.003 2 337 . 50 PRO HG3 H 1.348 0.003 2 338 . 50 PRO HD2 H 2.228 0.003 2 339 . 50 PRO HD3 H 3.005 0.003 2 340 . 51 GLU N N 122.248 0.002 1 341 . 51 GLU H H 8.575 0.002 1 342 . 51 GLU HA H 3.994 0.005 1 343 . 51 GLU HB2 H 1.962 0.002 1 344 . 51 GLU HB3 H 1.962 0.002 1 345 . 51 GLU HG2 H 2.290 0.006 1 346 . 51 GLU HG3 H 2.290 0.006 1 347 . 52 GLY N N 111.661 0.002 1 348 . 52 GLY H H 8.713 0.002 1 349 . 52 GLY HA2 H 3.650 0.005 2 350 . 52 GLY HA3 H 4.225 0.005 2 351 . 53 VAL N N 121.210 0.002 1 352 . 53 VAL H H 7.423 0.002 1 353 . 53 VAL HA H 4.118 0.005 1 354 . 53 VAL HB H 1.986 0.005 1 355 . 53 VAL HG1 H 0.854 0.005 2 356 . 53 VAL HG2 H 1.247 0.005 2 357 . 54 GLU N N 127.311 0.002 1 358 . 54 GLU H H 8.644 0.002 1 359 . 54 GLU HA H 4.259 0.005 1 360 . 54 GLU HB2 H 2.163 0.003 2 361 . 54 GLU HB3 H 2.026 0.003 2 362 . 54 GLU HG2 H 2.436 0.001 1 363 . 54 GLU HG3 H 2.436 0.001 1 364 . 55 SER N N 114.975 0.002 1 365 . 55 SER H H 8.361 0.002 1 366 . 55 SER HA H 3.792 0.005 1 367 . 55 SER HB2 H 3.711 0.003 1 368 . 55 SER HB3 H 3.711 0.003 1 369 . 56 PHE N N 117.037 0.002 1 370 . 56 PHE H H 6.134 0.002 1 371 . 56 PHE HA H 4.938 0.005 1 372 . 56 PHE HB2 H 2.976 0.009 2 373 . 56 PHE HB3 H 3.122 0.005 2 374 . 56 PHE HD1 H 6.897 0.016 4 375 . 56 PHE HD2 H 6.897 0.016 4 376 . 56 PHE HE1 H 6.897 0.016 4 377 . 56 PHE HE2 H 6.897 0.016 4 378 . 56 PHE HZ H 6.897 0.016 4 379 . 57 LYS N N 119.557 0.002 1 380 . 57 LYS H H 8.348 0.002 1 381 . 57 LYS HA H 4.678 0.005 1 382 . 57 LYS HB2 H 1.683 0.019 2 383 . 57 LYS HB3 H 1.684 0.003 2 384 . 57 LYS HG2 H 1.231 0.017 1 385 . 57 LYS HG3 H 1.231 0.017 1 386 . 57 LYS HD2 H 1.495 0.018 1 387 . 57 LYS HD3 H 1.495 0.018 1 388 . 57 LYS HE2 H 2.895 0.005 1 389 . 57 LYS HE3 H 2.895 0.005 1 390 . 58 SER N N 123.731 0.002 1 391 . 58 SER H H 9.335 0.002 1 392 . 58 SER HA H 4.660 0.005 1 393 . 58 SER HB2 H 4.223 0.002 2 394 . 58 SER HB3 H 3.354 0.001 2 395 . 59 LYS N N 120.251 0.002 1 396 . 59 LYS H H 8.711 0.002 1 397 . 59 LYS HA H 4.416 0.005 1 398 . 59 LYS HB2 H 1.647 0.016 2 399 . 59 LYS HB3 H 1.877 0.002 2 400 . 59 LYS HG2 H 1.522 0.017 1 401 . 59 LYS HG3 H 1.522 0.017 1 402 . 59 LYS HD2 H 1.759 0.012 1 403 . 59 LYS HD3 H 1.759 0.012 1 404 . 59 LYS HE2 H 3.064 0.005 1 405 . 59 LYS HE3 H 3.064 0.005 1 406 . 60 ILE N N 123.464 0.002 1 407 . 60 ILE H H 8.357 0.002 1 408 . 60 ILE HA H 3.995 0.005 1 409 . 60 ILE HB H 1.642 0.005 1 410 . 60 ILE HG13 H 1.368 0.005 2 411 . 60 ILE HG12 H 1.024 0.005 2 412 . 60 ILE HG2 H 0.787 0.005 1 413 . 60 ILE HD1 H 0.694 0.005 1 414 . 61 ASN N N 116.163 0.002 1 415 . 61 ASN H H 8.590 0.002 1 416 . 61 ASN HA H 4.649 0.005 1 417 . 61 ASN HB2 H 3.495 0.016 2 418 . 61 ASN HB3 H 3.069 0.019 2 419 . 61 ASN HD21 H 7.623 0.005 2 420 . 61 ASN HD22 H 7.031 0.005 2 421 . 61 ASN ND2 N 112.245 0.002 1 422 . 62 GLU N N 118.413 0.002 1 423 . 62 GLU H H 7.664 0.002 1 424 . 62 GLU HA H 4.745 0.005 1 425 . 62 GLU HB2 H 2.043 0.017 2 426 . 62 GLU HB3 H 1.871 0.039 2 427 . 62 GLU HG2 H 2.375 0.001 1 428 . 62 GLU HG3 H 2.375 0.001 1 429 . 63 SER N N 117.434 0.002 1 430 . 63 SER H H 8.614 0.002 1 431 . 63 SER HA H 5.001 0.005 1 432 . 63 SER HB2 H 4.016 0.003 1 433 . 63 SER HB3 H 4.016 0.003 1 434 . 64 TYR N N 122.724 0.002 1 435 . 64 TYR H H 8.724 0.002 1 436 . 64 TYR HA H 4.777 0.005 1 437 . 64 TYR HB2 H 3.016 0.003 2 438 . 64 TYR HB3 H 2.732 0.007 2 439 . 64 TYR HD1 H 6.908 0.005 1 440 . 64 TYR HD2 H 6.908 0.005 1 441 . 64 TYR HE1 H 6.406 0.005 1 442 . 64 TYR HE2 H 6.406 0.005 1 443 . 65 THR N N 123.729 0.002 1 444 . 65 THR H H 7.487 0.002 1 445 . 65 THR HA H 4.954 0.005 1 446 . 65 THR HB H 3.573 0.005 2 447 . 65 THR HG2 H 0.948 0.005 1 448 . 66 LEU N N 129.992 0.002 1 449 . 66 LEU H H 9.164 0.002 1 450 . 66 LEU HA H 4.382 0.005 1 451 . 66 LEU HB2 H 1.950 0.003 2 452 . 66 LEU HB3 H 1.730 0.003 2 453 . 66 LEU HG H 1.040 0.005 1 454 . 66 LEU HD1 H 0.453 0.005 2 455 . 66 LEU HD2 H 0.439 0.004 2 456 . 67 THR N N 124.605 0.002 1 457 . 67 THR H H 8.574 0.002 1 458 . 67 THR HA H 4.788 0.005 1 459 . 67 THR HB H 3.918 0.005 2 460 . 67 THR HG2 H 0.959 0.021 1 461 . 68 VAL N N 119.690 0.002 1 462 . 68 VAL H H 8.274 0.002 1 463 . 68 VAL HA H 4.380 0.005 1 464 . 68 VAL HB H 1.637 0.005 1 465 . 68 VAL HG1 H -0.035 0.005 2 466 . 68 VAL HG2 H 0.659 0.005 2 467 . 69 THR N N 116.484 0.002 1 468 . 69 THR H H 8.503 0.002 1 469 . 69 THR HA H 4.137 0.005 1 470 . 69 THR HB H 4.152 0.005 2 471 . 69 THR HG2 H 1.126 0.001 1 472 . 70 GLU N N 120.106 0.002 1 473 . 70 GLU H H 7.777 0.002 1 474 . 70 GLU HA H 4.720 0.005 1 475 . 70 GLU HB2 H 2.067 0.003 2 476 . 70 GLU HB3 H 2.401 0.003 2 477 . 70 GLU HG2 H 2.280 0.003 2 478 . 70 GLU HG3 H 2.282 0.003 2 479 . 71 PRO HA H 4.365 0.003 1 480 . 71 PRO HB2 H 2.016 0.003 2 481 . 71 PRO HB3 H 2.309 0.003 2 482 . 71 PRO HG2 H 2.181 0.003 1 483 . 71 PRO HG3 H 2.181 0.003 1 484 . 71 PRO HD2 H 3.835 0.001 2 485 . 71 PRO HD3 H 3.881 0.001 2 486 . 72 GLY N N 106.922 0.002 1 487 . 72 GLY H H 9.074 0.002 1 488 . 72 GLY HA2 H 3.662 0.005 2 489 . 72 GLY HA3 H 4.607 0.005 2 490 . 73 LEU N N 119.333 0.002 1 491 . 73 LEU H H 9.513 0.002 1 492 . 73 LEU HA H 5.366 0.005 1 493 . 73 LEU HB2 H 1.135 0.003 2 494 . 73 LEU HB3 H 1.599 0.003 2 495 . 73 LEU HG H 1.615 0.005 1 496 . 73 LEU HD1 H 0.825 0.005 2 497 . 73 LEU HD2 H 0.963 0.005 2 498 . 74 TYR N N 120.321 0.002 1 499 . 74 TYR H H 9.480 0.002 1 500 . 74 TYR HA H 5.180 0.005 1 501 . 74 TYR HB2 H 3.239 0.003 1 502 . 74 TYR HB3 H 3.239 0.003 1 503 . 74 TYR HD1 H 7.112 0.005 1 504 . 74 TYR HD2 H 7.112 0.005 1 505 . 74 TYR HE1 H 6.809 0.005 1 506 . 74 TYR HE2 H 6.809 0.005 1 507 . 75 GLY N N 111.328 0.002 1 508 . 75 GLY H H 9.749 0.002 1 509 . 75 GLY HA2 H 3.246 0.013 2 510 . 75 GLY HA3 H 5.022 0.023 2 511 . 76 VAL N N 116.483 0.002 1 512 . 76 VAL H H 8.705 0.002 1 513 . 76 VAL HA H 4.995 0.005 1 514 . 76 VAL HB H 1.556 0.005 1 515 . 76 VAL HG1 H -0.030 0.005 2 516 . 76 VAL HG2 H 0.569 0.005 2 517 . 77 LYS N N 117.382 0.002 1 518 . 77 LYS H H 9.264 0.002 1 519 . 77 LYS HA H 5.615 0.005 1 520 . 77 LYS HB2 H 1.243 0.001 1 521 . 77 LYS HB3 H 1.243 0.001 1 522 . 77 LYS HG2 H 1.507 0.003 1 523 . 77 LYS HG3 H 1.507 0.003 1 524 . 78 CYS N N 124.921 0.002 1 525 . 78 CYS H H 7.530 0.002 1 526 . 78 CYS HA H 5.081 0.005 1 527 . 78 CYS HB2 H 2.782 0.015 2 528 . 78 CYS HB3 H 3.068 0.027 2 529 . 79 THR N N 124.729 0.002 1 530 . 79 THR H H 9.464 0.002 1 531 . 79 THR HA H 3.739 0.005 1 532 . 79 THR HB H 4.294 0.005 2 533 . 79 THR HG2 H 1.208 0.005 1 534 . 80 PRO HA H 3.847 0.005 1 535 . 80 PRO HB2 H 3.214 0.021 1 536 . 80 PRO HB3 H 3.214 0.021 1 537 . 80 PRO HG2 H 1.114 0.003 2 538 . 80 PRO HG3 H 1.656 0.003 2 539 . 80 PRO HD2 H 5.357 0.003 1 540 . 80 PRO HD3 H 5.357 0.003 1 541 . 81 HIS N N 116.820 0.002 1 542 . 81 HIS H H 8.258 0.002 1 543 . 81 HIS HA H 5.197 0.005 1 544 . 81 HIS HB2 H 3.435 0.002 2 545 . 81 HIS HB3 H 3.837 0.012 1 546 . 81 HIS HD1 H 6.426 0.005 1 547 . 81 HIS HE1 H 6.981 0.005 1 548 . 82 PHE N N 128.739 0.002 1 549 . 82 PHE H H 8.178 0.005 1 550 . 82 PHE HA H 4.659 0.006 1 551 . 82 PHE HB2 H 3.215 0.005 2 552 . 82 PHE HB3 H 3.843 0.003 2 553 . 82 PHE HD1 H 7.324 0.005 1 554 . 82 PHE HD2 H 7.324 0.005 1 555 . 82 PHE HE1 H 7.371 0.005 1 556 . 82 PHE HE2 H 7.371 0.005 1 557 . 82 PHE HZ H 7.349 0.081 1 558 . 83 GLY N N 103.404 0.002 1 559 . 83 GLY H H 9.051 0.002 1 560 . 83 GLY HA2 H 3.912 0.001 2 561 . 83 GLY HA3 H 3.614 0.005 2 562 . 84 MET N N 117.173 0.002 1 563 . 84 MET H H 7.610 0.002 1 564 . 84 MET HA H 4.550 0.005 1 565 . 84 MET HB2 H 2.114 0.003 2 566 . 84 MET HB3 H 2.501 0.013 2 567 . 84 MET HG2 H 2.777 0.006 2 568 . 84 MET HG3 H 2.710 0.003 2 569 . 84 MET HE H 2.706 0.003 1 570 . 85 GLY N N 105.083 0.002 1 571 . 85 GLY H H 8.204 0.002 1 572 . 85 GLY HA2 H 3.172 0.016 2 573 . 85 GLY HA3 H 4.189 0.005 2 574 . 86 MET N N 123.669 0.002 1 575 . 86 MET H H 7.612 0.002 1 576 . 86 MET HA H 4.643 0.005 1 577 . 86 MET HB2 H 2.166 0.003 2 578 . 86 MET HB3 H 2.286 0.018 2 579 . 86 MET HG2 H 1.320 0.021 2 580 . 86 MET HG3 H 1.809 0.003 2 581 . 86 MET HE H 0.677 0.015 1 582 . 87 VAL N N 118.580 0.002 1 583 . 87 VAL H H 7.953 0.002 1 584 . 87 VAL HA H 5.762 0.005 1 585 . 87 VAL HB H 2.417 0.005 1 586 . 87 VAL HG1 H 1.122 0.005 2 587 . 87 VAL HG2 H 1.335 0.005 2 588 . 88 GLY N N 115.182 0.002 1 589 . 88 GLY H H 9.322 0.002 1 590 . 88 GLY HA2 H 4.885 0.005 2 591 . 88 GLY HA3 H 3.121 0.009 2 592 . 89 LEU N N 119.979 0.002 1 593 . 89 LEU H H 8.534 0.002 1 594 . 89 LEU HA H 5.218 0.005 1 595 . 89 LEU HB2 H 1.990 0.003 2 596 . 89 LEU HB3 H 1.720 0.013 2 597 . 89 LEU HG H 1.470 0.005 1 598 . 89 LEU HD1 H 1.029 0.005 1 599 . 89 LEU HD2 H 1.029 0.005 1 600 . 90 VAL N N 124.191 0.002 1 601 . 90 VAL H H 9.036 0.002 1 602 . 90 VAL HA H 4.570 0.005 1 603 . 90 VAL HB H 1.999 0.005 1 604 . 90 VAL HG1 H 0.361 0.005 2 605 . 90 VAL HG2 H 0.601 0.005 2 606 . 91 GLN N N 127.039 0.002 1 607 . 91 GLN H H 8.979 0.002 1 608 . 91 GLN HA H 4.719 0.005 1 609 . 91 GLN HB2 H 2.015 0.045 1 610 . 91 GLN HB3 H 2.015 0.045 1 611 . 91 GLN HG2 H 2.460 0.021 1 612 . 91 GLN HG3 H 2.460 0.021 1 613 . 91 GLN HE21 H 7.893 0.005 2 614 . 91 GLN HE22 H 7.463 0.005 2 615 . 91 GLN NE2 N 108.181 0.002 1 616 . 92 VAL N N 128.424 0.002 1 617 . 92 VAL H H 9.076 0.002 1 618 . 92 VAL HA H 4.379 0.005 1 619 . 92 VAL HB H 2.635 0.005 1 620 . 92 VAL HG1 H 0.470 0.005 2 621 . 92 VAL HG2 H 0.621 0.005 2 622 . 93 GLY N N 114.561 0.002 1 623 . 93 GLY H H 8.264 0.002 1 624 . 93 GLY HA2 H 4.341 0.005 2 625 . 93 GLY HA3 H 4.085 0.002 2 626 . 94 ASP N N 116.006 0.002 1 627 . 94 ASP H H 8.168 0.002 1 628 . 94 ASP HA H 4.443 0.005 1 629 . 94 ASP HB2 H 2.655 0.018 2 630 . 94 ASP HB3 H 2.580 0.003 2 631 . 95 ALA N N 121.934 0.002 1 632 . 95 ALA H H 9.017 0.002 1 633 . 95 ALA HA H 4.158 0.005 1 634 . 95 ALA HB H 1.279 0.005 1 635 . 96 PRO HA H 4.606 0.009 1 636 . 96 PRO HB2 H 1.892 0.027 2 637 . 96 PRO HB3 H 2.027 0.003 2 638 . 96 PRO HG2 H 3.600 0.003 1 639 . 96 PRO HG3 H 3.600 0.003 1 640 . 96 PRO HD2 H 3.604 0.009 1 641 . 96 PRO HD3 H 3.604 0.009 1 642 . 97 GLU N N 123.282 0.002 1 643 . 97 GLU H H 9.306 0.002 1 644 . 97 GLU HA H 4.188 0.005 1 645 . 97 GLU HB2 H 2.196 0.007 2 646 . 97 GLU HB3 H 2.063 0.003 2 647 . 97 GLU HG2 H 2.488 0.009 2 648 . 97 GLU HG3 H 2.396 0.021 2 649 . 98 ASN N N 114.460 0.002 1 650 . 98 ASN H H 8.383 0.002 1 651 . 98 ASN HA H 5.215 0.005 1 652 . 98 ASN HB2 H 2.736 0.013 2 653 . 98 ASN HB3 H 3.367 0.011 2 654 . 98 ASN HD21 H 7.359 0.005 2 655 . 98 ASN HD22 H 7.790 0.005 2 656 . 98 ASN ND2 N 109.735 0.002 1 657 . 99 LEU N N 119.799 0.002 1 658 . 99 LEU H H 6.986 0.002 1 659 . 99 LEU HA H 3.989 0.005 1 660 . 99 LEU HB2 H 1.490 0.003 2 661 . 99 LEU HB3 H 1.872 0.003 2 662 . 99 LEU HG H 1.522 0.005 1 663 . 99 LEU HD1 H 0.936 0.005 2 664 . 99 LEU HD2 H 0.979 0.005 2 665 . 100 ASP N N 117.413 0.002 1 666 . 100 ASP H H 8.819 0.002 1 667 . 100 ASP HA H 4.288 0.005 1 668 . 100 ASP HB2 H 2.608 0.013 1 669 . 100 ASP HB3 H 2.608 0.013 1 670 . 101 ALA N N 122.560 0.002 1 671 . 101 ALA H H 7.793 0.002 1 672 . 101 ALA HA H 4.020 0.005 1 673 . 101 ALA HB H 1.597 0.005 1 674 . 102 ALA N N 118.269 0.002 1 675 . 102 ALA H H 7.658 0.002 1 676 . 102 ALA HA H 3.997 0.005 1 677 . 102 ALA HB H 1.551 0.005 1 678 . 103 LYS N N 118.055 0.002 1 679 . 103 LYS H H 8.270 0.002 1 680 . 103 LYS HA H 3.906 0.005 1 681 . 103 LYS HB2 H 1.917 0.001 2 682 . 103 LYS HB3 H 2.076 0.009 2 683 . 103 LYS HG2 H 1.453 0.022 2 684 . 103 LYS HG3 H 1.713 0.009 2 685 . 103 LYS HD2 H 1.638 0.005 1 686 . 103 LYS HD3 H 1.638 0.005 1 687 . 103 LYS HE2 H 2.806 0.005 1 688 . 103 LYS HE3 H 2.806 0.005 1 689 . 104 THR N N 104.913 0.002 1 690 . 104 THR H H 7.566 0.002 1 691 . 104 THR HA H 4.314 0.005 1 692 . 104 THR HB H 4.325 0.005 2 693 . 104 THR HG2 H 1.213 0.005 1 694 . 105 ALA N N 125.003 0.002 1 695 . 105 ALA H H 7.251 0.002 1 696 . 105 ALA HA H 4.111 0.005 1 697 . 105 ALA HB H 1.242 0.005 1 698 . 106 LYS N N 124.834 0.002 1 699 . 106 LYS H H 8.778 0.002 1 700 . 106 LYS HA H 4.308 0.005 1 701 . 106 LYS HB2 H 1.802 0.003 1 702 . 106 LYS HB3 H 1.802 0.003 1 703 . 106 LYS HG2 H 1.404 0.003 2 704 . 106 LYS HG3 H 1.558 0.028 2 705 . 106 LYS HD2 H 1.710 0.005 1 706 . 106 LYS HD3 H 1.710 0.005 1 707 . 106 LYS HE2 H 3.023 0.005 1 708 . 106 LYS HE3 H 3.023 0.005 1 709 . 107 MET N N 121.082 0.002 1 710 . 107 MET H H 8.190 0.002 1 711 . 107 MET HA H 4.767 0.005 1 712 . 107 MET HB2 H 2.293 0.003 2 713 . 107 MET HB3 H 2.583 0.003 2 714 . 107 MET HG2 H 2.087 0.003 1 715 . 107 MET HG3 H 2.087 0.003 1 716 . 108 PRO HB2 H 2.096 0.011 2 717 . 108 PRO HB3 H 2.267 0.003 2 718 . 109 LYS HA H 3.976 0.014 1 719 . 109 LYS HB2 H 1.794 0.005 2 720 . 109 LYS HB3 H 1.954 0.003 2 721 . 109 LYS HG2 H 1.771 0.001 2 722 . 109 LYS HG3 H 1.857 0.001 2 723 . 110 LYS N N 116.323 0.002 1 724 . 110 LYS H H 9.294 0.002 1 725 . 110 LYS HA H 4.145 0.005 1 726 . 110 LYS HB2 H 1.793 0.003 4 727 . 110 LYS HB3 H 1.793 0.003 4 728 . 110 LYS HG2 H 1.793 0.003 4 729 . 110 LYS HG3 H 1.793 0.003 4 730 . 110 LYS HD2 H 1.682 0.003 1 731 . 110 LYS HD3 H 1.682 0.003 1 732 . 111 ALA N N 118.760 0.002 1 733 . 111 ALA H H 6.937 0.002 1 734 . 111 ALA HA H 4.109 0.005 1 735 . 111 ALA HB H 1.414 0.005 1 736 . 112 ARG N N 120.182 0.002 1 737 . 112 ARG H H 8.449 0.002 1 738 . 112 ARG HA H 4.124 0.005 1 739 . 112 ARG HB2 H 2.190 0.003 1 740 . 112 ARG HB3 H 2.190 0.003 1 741 . 112 ARG HG2 H 1.711 0.003 2 742 . 113 GLU N N 118.556 0.002 1 743 . 113 GLU H H 8.183 0.002 1 744 . 113 GLU HA H 4.193 0.005 1 745 . 113 GLU HB2 H 2.108 0.024 2 746 . 113 GLU HB3 H 2.204 0.005 2 747 . 113 GLU HG2 H 2.280 0.003 2 748 . 113 GLU HG3 H 2.539 0.006 2 749 . 114 ARG N N 119.936 0.002 1 750 . 114 ARG H H 7.618 0.002 1 751 . 114 ARG HA H 4.237 0.005 1 752 . 114 ARG HB2 H 2.163 0.003 1 753 . 114 ARG HB3 H 2.163 0.003 1 754 . 114 ARG HG2 H 1.107 0.009 2 755 . 114 ARG HG3 H 1.869 0.006 2 756 . 115 MET N N 120.463 0.002 1 757 . 115 MET H H 9.240 0.002 1 758 . 115 MET HA H 4.552 0.005 1 759 . 115 MET HB2 H 2.108 0.003 1 760 . 115 MET HB3 H 2.108 0.003 1 761 . 115 MET HG2 H 2.383 0.014 2 762 . 115 MET HG3 H 2.582 0.007 2 763 . 115 MET HE H 1.967 0.026 1 764 . 116 ASP N N 120.300 0.002 1 765 . 116 ASP H H 8.735 0.002 1 766 . 116 ASP HA H 4.417 0.005 1 767 . 116 ASP HB2 H 2.923 0.001 2 768 . 116 ASP HB3 H 2.595 0.003 2 769 . 117 ALA N N 122.340 0.002 1 770 . 117 ALA H H 7.435 0.002 1 771 . 117 ALA HA H 4.228 0.005 1 772 . 117 ALA HB H 1.629 0.005 1 773 . 118 GLU N N 119.868 0.002 1 774 . 118 GLU H H 8.006 0.002 1 775 . 118 GLU HA H 4.152 0.005 1 776 . 118 GLU HB2 H 2.219 0.005 2 777 . 118 GLU HB3 H 2.506 0.012 2 778 . 118 GLU HG2 H 2.798 0.001 1 779 . 118 GLU HG3 H 2.798 0.001 1 780 . 119 LEU N N 118.857 0.002 1 781 . 119 LEU H H 8.973 0.002 1 782 . 119 LEU HA H 3.857 0.005 1 783 . 119 LEU HB2 H 1.937 0.012 2 784 . 119 LEU HB3 H 1.316 0.028 2 785 . 119 LEU HG H 1.796 0.005 1 786 . 119 LEU HD1 H 0.778 0.005 2 787 . 119 LEU HD2 H 0.836 0.005 2 788 . 120 ALA N N 119.944 0.002 1 789 . 120 ALA H H 7.282 0.002 1 790 . 120 ALA HA H 4.157 0.005 1 791 . 120 ALA HB H 1.467 0.005 1 792 . 121 GLN N N 114.581 0.002 1 793 . 121 GLN H H 7.431 0.002 1 794 . 121 GLN HA H 3.956 0.005 1 795 . 121 GLN HB2 H 1.458 0.003 1 796 . 121 GLN HB3 H 1.458 0.003 1 797 . 121 GLN HG2 H 2.065 0.004 1 798 . 121 GLN HG3 H 2.065 0.004 1 799 . 121 GLN HE21 H 7.194 0.005 2 800 . 121 GLN HE22 H 6.847 0.005 2 801 . 121 GLN NE2 N 111.873 0.002 1 802 . 122 VAL N N 120.257 0.002 1 803 . 122 VAL H H 7.025 0.002 1 804 . 122 VAL HA H 4.086 0.005 1 805 . 122 VAL HB H 2.143 0.005 1 806 . 122 VAL HG1 H 0.940 0.005 2 807 . 122 VAL HG2 H 1.137 0.005 2 808 . 123 ASN N N 131.138 0.002 1 809 . 123 ASN H H 8.421 0.002 1 810 . 123 ASN HA H 4.558 0.005 1 811 . 123 ASN HB2 H 2.813 0.004 2 812 . 123 ASN HB3 H 2.716 0.026 2 813 . 123 ASN HD21 H 7.394 0.001 2 814 . 123 ASN HD22 H 6.651 0.005 2 815 . 123 ASN ND2 N 111.352 0.002 1 stop_ loop_ _Atom_shift_assign_ID_ambiguity 378 377,376,375,374 729,728,727,726 stop_ save_