data_17346 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution NMR structure of PAP248-286 in 50% TFE ; _BMRB_accession_number 17346 _BMRB_flat_file_name bmr17346.str _Entry_type new _Submission_date 2010-12-03 _Accession_date 2010-12-03 _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 NANGA 'RAVI PRAKASH REDDY' . . 2 BRENDER JEFFREY R. . 3 POPOVYCH NATALIYA . . 4 RAMAMOORTHY AYYALUSAMY . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 226 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2011-03-24 update BMRB 'update entry citation' 2011-01-27 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 17347 'PAP248-286 in 30% TFE' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 21262195 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Brender Jeffrey R. . 2 Nanga 'Ravi Prakash Reddy' . . 3 Popovych Nataliya . . 4 Soong Ronald . . 5 Macdonald Peter M. . 6 Ramamoorthy Ayyalusamy . . stop_ _Journal_abbreviation 'Biochim. Biophys. Acta' _Journal_name_full 'Biochimica et biophysica acta' _Journal_volume 1808 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1161 _Page_last 1169 _Year 2011 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name PAP248-286 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label PAP248-286 $entity stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 4561.504 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 39 _Mol_residue_sequence ; GIHKQKEKSRLQGGVLVNEI LNHMKRATQIPSYKKLIMY ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 248 GLY 2 249 ILE 3 250 HIS 4 251 LYS 5 252 GLN 6 253 LYS 7 254 GLU 8 255 LYS 9 256 SER 10 257 ARG 11 258 LEU 12 259 GLN 13 260 GLY 14 261 GLY 15 262 VAL 16 263 LEU 17 264 VAL 18 265 ASN 19 266 GLU 20 267 ILE 21 268 LEU 22 269 ASN 23 270 HIS 24 271 MET 25 272 LYS 26 273 ARG 27 274 ALA 28 275 THR 29 276 GLN 30 277 ILE 31 278 PRO 32 279 SER 33 280 TYR 34 281 LYS 35 282 LYS 36 283 LEU 37 284 ILE 38 285 MET 39 286 TYR stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-30 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 17193 PAP248-286 100.00 39 100.00 100.00 2.43e-18 BMRB 17347 entity 100.00 39 100.00 100.00 2.43e-18 BMRB 17924 SEVI 100.00 39 100.00 100.00 2.43e-18 BMRB 17925 SEVI 100.00 39 100.00 100.00 2.43e-18 BMRB 18287 PAP248-286 100.00 39 100.00 100.00 2.43e-18 PDB 1CVI "Crystal Structure Of Human Prostatic Acid Phosphatase" 100.00 342 100.00 100.00 2.03e-17 PDB 1ND5 "Crystal Structures Of Human Prostatic Acid Phosphatase In Complex With A Phosphate Ion And Alpha-Benzylaminobenzylphosphonic Ac" 100.00 354 100.00 100.00 1.95e-17 PDB 1ND6 "Crystal Structures Of Human Prostatic Acid Phosphatase In Complex With A Phosphate Ion And Alpha-Benzylaminobenzylphosphonic Ac" 100.00 354 100.00 100.00 1.95e-17 PDB 2HPA "Structural Origins Of L(+)-Tartrate Inhibition Of Human Prostatic Acid Phosphatase" 100.00 342 100.00 100.00 2.03e-17 PDB 2L3H "Nmr Structure In A Membrane Environment Reveals Putative Amyloidogenic Regions Of The Sevi Precursor Peptide Pap248-286" 97.44 39 100.00 100.00 2.42e-17 PDB 2L77 "Solution Nmr Structure Of Pap248-286 In 50% Tfe" 97.44 39 100.00 100.00 2.42e-17 PDB 2L79 "Solution Nmr Structure Of Pap248-286 In 30% Tfe" 97.44 39 100.00 100.00 2.42e-17 DBJ BAD89417 "Acid phosphatase prostate nirs variant 1 [Homo sapiens]" 100.00 353 100.00 100.00 3.85e-18 DBJ BAG62248 "unnamed protein product [Homo sapiens]" 100.00 353 100.00 100.00 3.85e-18 EMBL CAA36422 "unnamed protein product [Homo sapiens]" 100.00 386 100.00 100.00 3.05e-18 EMBL CAA37673 "unnamed protein product [Homo sapiens]" 100.00 386 100.00 100.00 5.55e-18 GB AAA60021 "prostatic acid phosphatase [Homo sapiens]" 100.00 386 100.00 100.00 1.02e-17 GB AAA60022 "acid phosphatase [Homo sapiens]" 100.00 386 100.00 100.00 6.90e-18 GB AAA69694 "acid phosphatase [Homo sapiens]" 100.00 386 100.00 100.00 1.02e-17 GB AAB60640 "prostatic acid phosphatase [Homo sapiens]" 100.00 386 100.00 100.00 1.02e-17 GB AAH07460 "ACPP protein [Homo sapiens]" 100.00 418 100.00 100.00 1.43e-17 REF NP_001090 "prostatic acid phosphatase isoform PAP precursor [Homo sapiens]" 100.00 386 100.00 100.00 1.02e-17 REF NP_001127666 "prostatic acid phosphatase isoform TM-PAP precursor [Homo sapiens]" 100.00 418 100.00 100.00 1.48e-17 REF NP_001278966 "prostatic acid phosphatase isoform 3 [Homo sapiens]" 100.00 353 100.00 100.00 3.85e-18 REF XP_001115549 "PREDICTED: prostatic acid phosphatase [Macaca mulatta]" 100.00 418 97.44 100.00 1.49e-17 REF XP_001148736 "PREDICTED: prostatic acid phosphatase [Pan troglodytes]" 100.00 418 97.44 97.44 6.83e-17 SP P15309 "RecName: Full=Prostatic acid phosphatase; Short=PAP; AltName: Full=5'-nucleotidase; Short=5'-NT; AltName: Full=Ecto-5'-nucleoti" 100.00 386 100.00 100.00 1.02e-17 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity Human 9606 Eukaryota Metazoa Homo sapiens 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 $entity 'obtained from a vendor' . . . . . 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 $entity 1.2 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' D2O 10 % '[U-99% 2H]' TFE 50 % '[U-99% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_TALOS _Saveframe_category software _Name TALOS _Version . loop_ _Vendor _Address _Electronic_address 'Cornilescu, Delaglio and Bax' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' refinement stop_ _Details . save_ save_Molmol _Saveframe_category software _Name Molmol _Version . loop_ _Vendor _Address _Electronic_address 'Koradi, Billeter and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ save_ProcheckNMR _Saveframe_category software _Name ProcheckNMR _Version . loop_ _Vendor _Address _Electronic_address 'Laskowski and MacArthur' . . stop_ loop_ _Task 'data analysis' 'structure solution' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _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 temperature 298 . K pH 7.5 . pH pressure 1 . atm 'ionic strength' 0 . M 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 water H 1 protons ppm 4.7 internal direct . . . 1.0 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_ _Experiment_label '2D 1H-1H TOCSY' '2D 1H-1H NOESY' 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 PAP248-286 _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 1 249 2 ILE H H 8.037 0.02 1 2 249 2 ILE HA H 4.111 0.02 1 3 249 2 ILE HB H 2.181 0.02 1 4 249 2 ILE HD1 H 0.972 0.02 1 5 250 3 HIS H H 8.543 0.02 1 6 250 3 HIS HA H 4.544 0.02 1 7 250 3 HIS HB2 H 3.262 0.02 1 8 250 3 HIS HB3 H 3.262 0.02 1 9 250 3 HIS HD2 H 7.155 0.02 1 10 250 3 HIS HE1 H 8.037 0.02 1 11 251 4 LYS H H 8.477 0.02 1 12 251 4 LYS HA H 4.224 0.02 1 13 252 5 GLN H H 8.399 0.02 1 14 252 5 GLN HA H 4.173 0.02 1 15 252 5 GLN HB2 H 2.179 0.02 1 16 252 5 GLN HB3 H 2.179 0.02 1 17 252 5 GLN HG2 H 2.463 0.02 1 18 252 5 GLN HG3 H 2.463 0.02 1 19 252 5 GLN HE21 H 7.419 0.02 1 20 252 5 GLN HE22 H 6.772 0.02 1 21 253 6 LYS H H 8.432 0.02 1 22 253 6 LYS HA H 4.166 0.02 1 23 253 6 LYS HB2 H 1.943 0.02 1 24 253 6 LYS HB3 H 1.943 0.02 1 25 253 6 LYS HG2 H 1.479 0.02 1 26 253 6 LYS HG3 H 1.479 0.02 1 27 253 6 LYS HD2 H 1.593 0.02 1 28 253 6 LYS HD3 H 1.736 0.02 1 29 254 7 GLU H H 8.422 0.02 1 30 254 7 GLU HA H 4.173 0.02 1 31 254 7 GLU HB2 H 2.141 0.02 1 32 254 7 GLU HB3 H 2.141 0.02 1 33 254 7 GLU HG2 H 2.365 0.02 1 34 254 7 GLU HG3 H 2.365 0.02 1 35 255 8 LYS H H 8.314 0.02 1 36 255 8 LYS HA H 4.109 0.02 1 37 255 8 LYS HB2 H 1.949 0.02 1 38 255 8 LYS HB3 H 1.949 0.02 1 39 255 8 LYS HG2 H 1.466 0.02 1 40 255 8 LYS HG3 H 1.466 0.02 1 41 255 8 LYS HD2 H 1.617 0.02 1 42 255 8 LYS HD3 H 1.726 0.02 1 43 256 9 SER H H 8.150 0.02 1 44 256 9 SER HA H 4.352 0.02 1 45 256 9 SER HB2 H 4.016 0.02 2 46 256 9 SER HB3 H 4.083 0.02 2 47 257 10 ARG H H 8.034 0.02 1 48 257 10 ARG HA H 4.229 0.02 1 49 257 10 ARG HB2 H 1.993 0.02 2 50 257 10 ARG HB3 H 2.030 0.02 2 51 257 10 ARG HG2 H 1.701 0.02 2 52 257 10 ARG HG3 H 1.829 0.02 2 53 258 11 LEU H H 8.064 0.02 1 54 258 11 LEU HA H 4.265 0.02 1 55 258 11 LEU HB2 H 1.771 0.02 2 56 258 11 LEU HB3 H 1.852 0.02 2 57 258 11 LEU HG H 1.709 0.02 1 58 258 11 LEU HD1 H 0.932 0.02 2 59 258 11 LEU HD2 H 1.114 0.02 2 60 259 12 GLN H H 8.276 0.02 1 61 259 12 GLN HA H 4.128 0.02 1 62 259 12 GLN HB2 H 2.191 0.02 2 63 259 12 GLN HB3 H 2.191 0.02 2 64 259 12 GLN HG2 H 2.394 0.02 2 65 259 12 GLN HG3 H 2.533 0.02 2 66 259 12 GLN HE21 H 7.077 0.02 1 67 259 12 GLN HE22 H 6.694 0.02 1 68 260 13 GLY H H 8.270 0.02 1 69 260 13 GLY HA2 H 3.931 0.02 1 70 260 13 GLY HA3 H 3.931 0.02 1 71 261 14 GLY H H 8.068 0.02 1 72 261 14 GLY HA2 H 3.927 0.02 1 73 261 14 GLY HA3 H 3.927 0.02 1 74 262 15 VAL H H 7.944 0.02 1 75 262 15 VAL HA H 3.793 0.02 1 76 262 15 VAL HB H 2.286 0.02 1 77 262 15 VAL HG1 H 1.045 0.02 2 78 262 15 VAL HG2 H 1.116 0.02 2 79 263 16 LEU H H 7.833 0.02 1 80 263 16 LEU HA H 4.188 0.02 1 81 263 16 LEU HB2 H 1.778 0.02 2 82 263 16 LEU HB3 H 1.885 0.02 2 83 263 16 LEU HG H 1.730 0.02 1 84 263 16 LEU HD1 H 0.935 0.02 2 85 263 16 LEU HD2 H 0.974 0.02 2 86 264 17 VAL H H 8.197 0.02 1 87 264 17 VAL HA H 3.659 0.02 1 88 264 17 VAL HB H 2.146 0.02 1 89 264 17 VAL HG1 H 0.993 0.02 2 90 264 17 VAL HG2 H 1.108 0.02 2 91 265 18 ASN H H 7.931 0.02 1 92 265 18 ASN HA H 4.413 0.02 1 93 265 18 ASN HB2 H 2.869 0.02 2 94 265 18 ASN HB3 H 2.924 0.02 2 95 265 18 ASN HD21 H 7.827 0.02 1 96 265 18 ASN HD22 H 6.700 0.02 1 97 266 19 GLU H H 8.267 0.02 1 98 266 19 GLU HA H 4.288 0.02 1 99 266 19 GLU HB2 H 2.262 0.02 2 100 266 19 GLU HB3 H 2.385 0.02 2 101 266 19 GLU HG2 H 2.516 0.02 1 102 266 19 GLU HG3 H 2.516 0.02 1 103 267 20 ILE H H 8.596 0.02 1 104 267 20 ILE HA H 3.760 0.02 1 105 267 20 ILE HB H 2.088 0.02 1 106 267 20 ILE HG2 H 0.988 0.02 1 107 267 20 ILE HD1 H 0.863 0.02 1 108 268 21 LEU H H 8.729 0.02 1 109 268 21 LEU HA H 4.177 0.02 1 110 268 21 LEU HB2 H 1.938 0.02 2 111 268 21 LEU HB3 H 1.994 0.02 2 112 268 21 LEU HG H 1.515 0.02 1 113 268 21 LEU HD1 H 0.920 0.02 2 114 268 21 LEU HD2 H 0.990 0.02 2 115 269 22 ASN H H 8.302 0.02 1 116 269 22 ASN HA H 4.490 0.02 1 117 269 22 ASN HB2 H 2.730 0.02 2 118 269 22 ASN HB3 H 3.072 0.02 2 119 269 22 ASN HD21 H 7.622 0.02 1 120 269 22 ASN HD22 H 6.718 0.02 1 121 270 23 HIS H H 8.312 0.02 1 122 270 23 HIS HA H 4.338 0.02 1 123 270 23 HIS HB2 H 3.382 0.02 2 124 270 23 HIS HB3 H 3.407 0.02 2 125 270 23 HIS HD2 H 7.041 0.02 1 126 270 23 HIS HE1 H 7.972 0.02 1 127 271 24 MET H H 8.678 0.02 1 128 271 24 MET HA H 4.161 0.02 1 129 271 24 MET HB2 H 2.175 0.02 2 130 271 24 MET HB3 H 2.348 0.02 2 131 271 24 MET HG2 H 2.628 0.02 2 132 271 24 MET HG3 H 2.829 0.02 2 133 272 25 LYS H H 8.513 0.02 1 134 272 25 LYS HA H 3.986 0.02 1 135 272 25 LYS HB2 H 1.946 0.02 2 136 272 25 LYS HB3 H 2.017 0.02 2 137 272 25 LYS HG2 H 1.445 0.02 1 138 272 25 LYS HG3 H 1.445 0.02 1 139 272 25 LYS HD2 H 1.672 0.02 1 140 272 25 LYS HD3 H 1.727 0.02 1 141 273 26 ARG H H 7.884 0.02 1 142 273 26 ARG HA H 4.078 0.02 1 143 273 26 ARG HB2 H 1.871 0.02 2 144 273 26 ARG HB3 H 1.959 0.02 2 145 273 26 ARG HG2 H 1.628 0.02 1 146 273 26 ARG HG3 H 1.628 0.02 1 147 274 27 ALA H H 8.283 0.02 1 148 274 27 ALA HA H 4.150 0.02 1 149 274 27 ALA HB H 1.456 0.02 1 150 275 28 THR H H 7.689 0.02 1 151 275 28 THR HA H 4.381 0.02 1 152 275 28 THR HB H 4.249 0.02 1 153 275 28 THR HG2 H 1.365 0.02 1 154 276 29 GLN H H 7.753 0.02 1 155 276 29 GLN HA H 4.384 0.02 1 156 276 29 GLN HB2 H 2.139 0.02 2 157 276 29 GLN HB3 H 2.241 0.02 2 158 276 29 GLN HG2 H 2.432 0.02 2 159 276 29 GLN HG3 H 2.497 0.02 2 160 276 29 GLN HE21 H 7.370 0.02 1 161 276 29 GLN HE22 H 6.641 0.02 1 162 277 30 ILE H H 7.759 0.02 1 163 277 30 ILE HA H 4.331 0.02 1 164 277 30 ILE HB H 2.011 0.02 1 165 277 30 ILE HG12 H 1.240 0.02 1 166 277 30 ILE HG13 H 1.240 0.02 1 167 277 30 ILE HG2 H 0.996 0.02 1 168 277 30 ILE HD1 H 0.929 0.02 1 169 278 31 PRO HA H 4.397 0.02 1 170 278 31 PRO HB2 H 2.018 0.02 2 171 278 31 PRO HB3 H 2.301 0.02 2 172 278 31 PRO HD2 H 3.658 0.02 2 173 278 31 PRO HD3 H 3.940 0.02 2 174 279 32 SER H H 7.893 0.02 1 175 279 32 SER HA H 4.333 0.02 1 176 279 32 SER HB2 H 3.870 0.02 2 177 279 32 SER HB3 H 3.976 0.02 2 178 280 33 TYR H H 7.895 0.02 1 179 280 33 TYR HA H 4.447 0.02 1 180 280 33 TYR HB2 H 3.120 0.02 1 181 280 33 TYR HB3 H 3.120 0.02 1 182 280 33 TYR HD1 H 7.106 0.02 1 183 280 33 TYR HD2 H 7.106 0.02 1 184 280 33 TYR HE1 H 6.834 0.02 1 185 280 33 TYR HE2 H 6.834 0.02 1 186 281 34 LYS H H 7.834 0.02 1 187 281 34 LYS HA H 4.108 0.02 1 188 281 34 LYS HB2 H 1.768 0.02 2 189 281 34 LYS HB3 H 1.859 0.02 2 190 281 34 LYS HG2 H 1.401 0.02 1 191 281 34 LYS HG3 H 1.401 0.02 1 192 281 34 LYS HD2 H 1.701 0.02 1 193 281 34 LYS HD3 H 1.701 0.02 1 194 282 35 LYS H H 7.716 0.02 1 195 282 35 LYS HA H 4.239 0.02 1 196 282 35 LYS HB2 H 1.855 0.02 2 197 282 35 LYS HB3 H 1.915 0.02 2 198 282 35 LYS HG2 H 1.469 0.02 2 199 282 35 LYS HG3 H 1.520 0.02 2 200 283 36 LEU H H 7.779 0.02 1 201 283 36 LEU HA H 4.324 0.02 1 202 283 36 LEU HB2 H 1.697 0.02 2 203 283 36 LEU HB3 H 1.769 0.02 2 204 283 36 LEU HG H 1.636 0.02 1 205 283 36 LEU HD1 H 0.891 0.02 2 206 283 36 LEU HD2 H 0.950 0.02 2 207 284 37 ILE H H 7.562 0.02 1 208 284 37 ILE HA H 4.198 0.02 1 209 284 37 ILE HB H 1.909 0.02 1 210 284 37 ILE HG12 H 1.204 0.02 2 211 284 37 ILE HG13 H 1.472 0.02 2 212 284 37 ILE HD1 H 0.871 0.02 1 213 285 38 MET H H 7.872 0.02 1 214 285 38 MET HA H 4.466 0.02 1 215 285 38 MET HB2 H 1.966 0.02 2 216 285 38 MET HB3 H 2.070 0.02 2 217 285 38 MET HG2 H 2.466 0.02 2 218 285 38 MET HG3 H 2.541 0.02 2 219 286 39 TYR H H 7.390 0.02 1 220 286 39 TYR HA H 4.416 0.02 1 221 286 39 TYR HB2 H 2.965 0.02 2 222 286 39 TYR HB3 H 3.112 0.02 2 223 286 39 TYR HD1 H 7.126 0.02 1 224 286 39 TYR HD2 H 7.126 0.02 1 225 286 39 TYR HE1 H 6.832 0.02 1 226 286 39 TYR HE2 H 6.832 0.02 1 stop_ save_