data_6178 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; N-terminal Domain of the Polypyrimidine Tract Binding Protein Contains a New RRM Variant That Contributes to High-Affinity RNA Binding ; _BMRB_accession_number 6178 _BMRB_flat_file_name bmr6178.str _Entry_type original _Submission_date 2004-04-15 _Accession_date 2004-04-15 _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 Simpson P. J. . 2 Monie T. P. . 3 Szendroi A. . . 4 Davydova N. . . 5 Tyzack J. K. . 6 Conte M. R. . 7 Read C. M. . 8 Cary P. D. . 9 Svergun D. I. . 10 Konarev P. V. . 11 Petoukhov M. V. . 12 Curry S. . . 13 Matthews S. J. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 529 "13C chemical shifts" 411 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-11-08 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 6177 'Polypyrimidine tract-binding protein 1 domain 2' stop_ _Original_release_date 2004-11-08 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure and RNA interactions of the N-terminal RRM domains of PTB' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15341728 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Simpson P. J. . 2 Monie T. P. . 3 Szendroi A. . . 4 Davydova N. . . 5 Tyzack J. K. . 6 Conte M. R. . 7 Read C. M. . 8 Cary P. D. . 9 Svergun D. I. . 10 Konarev P. V. . 11 Curry S. . . 12 Matthews S. J. . stop_ _Journal_abbreviation 'Structure (Camb)' _Journal_volume 12 _Journal_issue 9 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1631 _Page_last 1643 _Year 2004 _Details . loop_ _Keyword 'BABBAB motif' stop_ save_ ################################## # Molecular system description # ################################## save_system_PTB1-1 _Saveframe_category molecular_system _Mol_system_name 'Polypyrimidine tract-binding protein 1 domain 1' _Abbreviation_common PTB1-1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'PTB1-1 monomer' $PTB1-1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Biological_function 'RNA binding module' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_PTB1-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'polypyrimidine tract binding protein 1 domain 1' _Abbreviation_common 'PTB1 RRM1' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; MRGSHHHHHHGSGVPSRVIH IRKLPIDVTEGEVISLGLPF GKVTNLLMLKGKNQAFIEMN TEEAANTMVNYYTSVTPVLR GQPIYIQFSNHKELKTDSSP NQARA ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 ARG 3 3 GLY 4 4 SER 5 5 HIS 6 6 HIS 7 7 HIS 8 8 HIS 9 9 HIS 10 10 HIS 11 11 GLY 12 12 SER 13 13 GLY 14 14 VAL 15 15 PRO 16 16 SER 17 17 ARG 18 18 VAL 19 19 ILE 20 20 HIS 21 21 ILE 22 22 ARG 23 23 LYS 24 24 LEU 25 25 PRO 26 26 ILE 27 27 ASP 28 28 VAL 29 29 THR 30 30 GLU 31 31 GLY 32 32 GLU 33 33 VAL 34 34 ILE 35 35 SER 36 36 LEU 37 37 GLY 38 38 LEU 39 39 PRO 40 40 PHE 41 41 GLY 42 42 LYS 43 43 VAL 44 44 THR 45 45 ASN 46 46 LEU 47 47 LEU 48 48 MET 49 49 LEU 50 50 LYS 51 51 GLY 52 52 LYS 53 53 ASN 54 54 GLN 55 55 ALA 56 56 PHE 57 57 ILE 58 58 GLU 59 59 MET 60 60 ASN 61 61 THR 62 62 GLU 63 63 GLU 64 64 ALA 65 65 ALA 66 66 ASN 67 67 THR 68 68 MET 69 69 VAL 70 70 ASN 71 71 TYR 72 72 TYR 73 73 THR 74 74 SER 75 75 VAL 76 76 THR 77 77 PRO 78 78 VAL 79 79 LEU 80 80 ARG 81 81 GLY 82 82 GLN 83 83 PRO 84 84 ILE 85 85 TYR 86 86 ILE 87 87 GLN 88 88 PHE 89 89 SER 90 90 ASN 91 91 HIS 92 92 LYS 93 93 GLU 94 94 LEU 95 95 LYS 96 96 THR 97 97 ASP 98 98 SER 99 99 SER 100 100 PRO 101 101 ASN 102 102 GLN 103 103 ALA 104 104 ARG 105 105 ALA stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-06-11 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 1SJQ "Nmr Structure Of Rrm1 From Human Polypyrimidine Tract Binding Protein Isoform 1 (Ptb1)" 100.00 105 100.00 100.00 1.33e-70 DBJ BAC29560 "unnamed protein product [Mus musculus]" 67.62 489 97.18 97.18 7.45e-39 DBJ BAD92147 "polypyrimidine tract-binding protein 1 isoform c variant [Homo sapiens]" 89.52 329 98.94 100.00 6.41e-58 DBJ BAI46909 "polypyrimidine tract binding protein 1 [synthetic construct]" 89.52 531 98.94 100.00 7.44e-57 EMBL CAA43056 "polypyrimidine tract-binding protein (pPTB) [Homo sapiens]" 89.52 531 98.94 100.00 7.44e-57 EMBL CAA43973 "polypirimidine tract binding protein [Homo sapiens]" 89.52 531 98.94 100.00 7.44e-57 EMBL CAA46443 "polypirimidine tract binding protein [Homo sapiens]" 89.52 550 98.94 100.00 1.37e-56 EMBL CAA46444 "polypirimidine tract binding protein [Homo sapiens]" 89.52 557 98.94 100.00 1.29e-56 EMBL CAA47386 "nuclear ribonucleoprotein [Homo sapiens]" 89.52 557 98.94 100.00 1.29e-56 GB AAC99798 "PTB_HUMAN [Homo sapiens]" 89.52 531 98.94 100.00 7.44e-57 GB AAH02397 "Polypyrimidine tract binding protein 1 [Homo sapiens]" 89.52 557 98.94 100.00 1.29e-56 GB AAH04383 "Polypyrimidine tract binding protein 1 [Homo sapiens]" 89.52 531 98.94 100.00 7.44e-57 GB AAH13694 "Polypyrimidine tract binding protein 1 [Homo sapiens]" 89.52 557 98.94 100.00 1.29e-56 GB AAP35465 "polypyrimidine tract binding protein 1 [Homo sapiens]" 89.52 557 98.94 100.00 1.29e-56 REF NP_001269942 "polypyrimidine tract-binding protein 1 isoform 3 [Mus musculus]" 67.62 489 97.18 97.18 7.45e-39 REF NP_002810 "polypyrimidine tract-binding protein 1 isoform a [Homo sapiens]" 89.52 557 98.94 100.00 1.29e-56 REF NP_114367 "polypyrimidine tract-binding protein 1 isoform b [Homo sapiens]" 89.52 550 98.94 100.00 1.37e-56 REF NP_114368 "polypyrimidine tract-binding protein 1 isoform c [Homo sapiens]" 89.52 531 98.94 100.00 7.44e-57 REF XP_001092088 "PREDICTED: polypyrimidine tract-binding protein 1 isoform 1 [Macaca mulatta]" 89.52 556 98.94 100.00 1.60e-56 SP P26599 "RecName: Full=Polypyrimidine tract-binding protein 1; Short=PTB; AltName: Full=57 kDa RNA-binding protein PPTB-1; AltName: Full" 89.52 531 98.94 100.00 7.44e-57 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $PTB1-1 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 $PTB1-1 'recombinant technology' 'E. coli' Escherichia coli . . 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 $PTB1-1 1 mM . 'Na phosphate' 50 mM . NaCl 100 mM . 'sodium azide' 2 mM . DTT 10 mM . stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 3.1 loop_ _Task collection processing stop_ _Details 'Bruker Biospin' save_ save_AURELIA _Saveframe_category software _Name AURELIA _Version 2.8.11 loop_ _Task 'data analysis' stop_ _Details 'Bruker Analytik GmbH' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1 loop_ _Task processing stop_ _Details 'Delaglio, F.' save_ save_NMRView _Saveframe_category software _Name NMRView _Version 4.1.3 loop_ _Task 'data analysis' stop_ _Details 'Johnson, B. and Blevins, R.' save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task 'structure solution' refinement stop_ _Details 'Brunger, A.T' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 800 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details 'DRX500 was equipped with cryoprobe' save_ ############################# # NMR applied experiments # ############################# save_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name HSQC _Sample_label $sample_1 save_ save_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name HNCACB _Sample_label $sample_1 save_ save_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name CBCA(CO)NH _Sample_label $sample_1 save_ save_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label $sample_1 save_ save_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CA)CO _Sample_label $sample_1 save_ save_HCCH-TOCSY_6 _Saveframe_category NMR_applied_experiment _Experiment_name HCCH-TOCSY _Sample_label $sample_1 save_ save_3D_13C-separated_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 13C-separated NOESY' _Sample_label $sample_1 save_ save_3D_15N-separated_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.2 pH temperature 303 2 K 'ionic strength' 0.3 0.05 M pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label TSP H 1 'methyl protons' ppm 0.00 internal direct cylindrical internal parallel 1.0 $entry_citation $entry_citation TSP N 15 'methyl protons' ppm 0.00 internal indirect cylindrical internal parallel 0.101329118 $entry_citation $entry_citation TSP C 13 'methyl protons' ppm 0.00 internal indirect cylindrical internal parallel 0.251449530 $entry_citation $entry_citation stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'PTB1-1 monomer' _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 CE C 16.720 0.75 1 2 1 1 MET HE H 2.030 0.03 1 3 12 12 SER CA C 58.000 0.75 1 4 12 12 SER CB C 63.440 0.75 1 5 12 12 SER C C 174.810 0.75 1 6 13 13 GLY N N 112.550 0.5 1 7 13 13 GLY H H 8.410 0.03 1 8 13 13 GLY CA C 44.360 0.75 1 9 13 13 GLY HA3 H 3.920 0.03 1 10 13 13 GLY HA2 H 3.920 0.03 1 11 13 13 GLY C C 173.430 0.75 1 12 14 14 VAL CA C 59.070 0.75 1 13 14 14 VAL CB C 32.250 0.75 1 14 14 14 VAL CG2 C 20.680 0.75 1 15 14 14 VAL HG2 H 0.780 0.03 2 16 14 14 VAL CG1 C 20.680 0.75 1 17 14 14 VAL HG1 H 0.710 0.03 2 18 14 14 VAL C C 174.600 0.75 1 19 15 15 PRO CA C 62.520 0.75 1 20 15 15 PRO HA H 3.380 0.03 1 21 15 15 PRO CB C 30.870 0.75 1 22 15 15 PRO HB3 H 1.830 0.03 2 23 15 15 PRO HB2 H 1.680 0.03 2 24 15 15 PRO CG C 30.800 0.75 1 25 15 15 PRO HG3 H 1.800 0.03 2 26 15 15 PRO HG2 H 1.690 0.03 2 27 15 15 PRO CD C 50.160 0.75 1 28 15 15 PRO HD3 H 3.660 0.03 2 29 15 15 PRO HD2 H 3.280 0.03 2 30 15 15 PRO C C 175.400 0.75 1 31 16 16 SER N N 116.790 0.5 1 32 16 16 SER H H 7.360 0.03 1 33 16 16 SER CA C 56.010 0.75 1 34 16 16 SER HA H 4.530 0.03 1 35 16 16 SER CB C 64.050 0.75 1 36 16 16 SER HB3 H 3.920 0.03 2 37 16 16 SER HB2 H 3.670 0.03 2 38 16 16 SER C C 173.180 0.75 1 39 17 17 ARG N N 120.900 0.5 1 40 17 17 ARG H H 8.540 0.03 1 41 17 17 ARG CA C 56.160 0.75 1 42 17 17 ARG HA H 4.370 0.03 1 43 17 17 ARG CB C 30.950 0.75 1 44 17 17 ARG HB3 H 2.170 0.03 2 45 17 17 ARG HB2 H 1.780 0.03 2 46 17 17 ARG C C 174.760 0.75 1 47 18 18 VAL N N 121.290 0.5 1 48 18 18 VAL H H 8.590 0.03 1 49 18 18 VAL CA C 61.520 0.75 1 50 18 18 VAL HA H 4.810 0.03 1 51 18 18 VAL CB C 31.640 0.75 1 52 18 18 VAL HB H 2.030 0.03 1 53 18 18 VAL CG2 C 22.280 0.75 1 54 18 18 VAL HG2 H 0.900 0.03 2 55 18 18 VAL CG1 C 21.630 0.75 1 56 18 18 VAL HG1 H 0.740 0.03 2 57 18 18 VAL C C 174.460 0.75 1 58 19 19 ILE N N 131.370 0.5 1 59 19 19 ILE H H 9.470 0.03 1 60 19 19 ILE CA C 58.920 0.75 1 61 19 19 ILE HA H 4.360 0.03 1 62 19 19 ILE CB C 39.760 0.75 1 63 19 19 ILE HB H 1.800 0.03 1 64 19 19 ILE CG1 C 28.200 0.75 2 65 19 19 ILE HG13 H 1.430 0.03 1 66 19 19 ILE HG12 H 1.020 0.03 1 67 19 19 ILE CD1 C 14.060 0.75 1 68 19 19 ILE HD1 H 0.730 0.03 1 69 19 19 ILE CG2 C 19.130 0.75 1 70 19 19 ILE HG2 H 0.670 0.03 1 71 19 19 ILE C C 173.830 0.75 1 72 20 20 HIS N N 130.600 0.5 1 73 20 20 HIS H H 9.370 0.03 1 74 20 20 HIS CA C 52.630 0.75 1 75 20 20 HIS HA H 4.960 0.03 1 76 20 20 HIS CB C 34.630 0.75 1 77 20 20 HIS HB3 H 3.140 0.03 2 78 20 20 HIS HB2 H 2.630 0.03 2 79 20 20 HIS CD2 C 116.300 0.75 1 80 20 20 HIS HD2 H 6.100 0.03 1 81 20 20 HIS C C 173.400 0.75 1 82 21 21 ILE N N 129.890 0.5 1 83 21 21 ILE H H 9.210 0.03 1 84 21 21 ILE CA C 59.450 0.75 1 85 21 21 ILE HA H 4.800 0.03 1 86 21 21 ILE CB C 38.920 0.75 1 87 21 21 ILE HB H 1.500 0.03 1 88 21 21 ILE HG13 H 1.390 0.03 1 89 21 21 ILE HG12 H 0.830 0.03 1 90 21 21 ILE CD1 C 14.340 0.75 1 91 21 21 ILE HD1 H 0.580 0.03 1 92 21 21 ILE CG2 C 19.100 0.75 1 93 21 21 ILE HG2 H 0.700 0.03 1 94 21 21 ILE C C 174.570 0.75 1 95 22 22 ARG N N 125.400 0.5 1 96 22 22 ARG H H 8.850 0.03 1 97 22 22 ARG CA C 53.860 0.75 1 98 22 22 ARG HA H 4.820 0.03 1 99 22 22 ARG CB C 34.090 0.75 1 100 22 22 ARG HB3 H 1.800 0.03 2 101 22 22 ARG HB2 H 1.520 0.03 2 102 22 22 ARG CG C 27.870 0.75 1 103 22 22 ARG HG3 H 1.090 0.03 2 104 22 22 ARG HG2 H 0.940 0.03 2 105 22 22 ARG CD C 43.040 0.75 1 106 22 22 ARG HD3 H 2.780 0.03 1 107 22 22 ARG HD2 H 2.780 0.03 1 108 22 22 ARG C C 174.110 0.75 1 109 23 23 LYS N N 116.280 0.5 1 110 23 23 LYS H H 8.580 0.03 1 111 23 23 LYS CA C 56.240 0.75 1 112 23 23 LYS HA H 3.800 0.03 1 113 23 23 LYS CB C 28.880 0.75 1 114 23 23 LYS HB3 H 2.110 0.03 1 115 23 23 LYS HB2 H 2.110 0.03 1 116 23 23 LYS CG C 25.670 0.75 1 117 23 23 LYS HG3 H 1.320 0.03 1 118 23 23 LYS HG2 H 1.320 0.03 1 119 23 23 LYS CD C 29.000 0.75 1 120 23 23 LYS HD3 H 1.590 0.03 1 121 23 23 LYS HD2 H 1.590 0.03 1 122 23 23 LYS CE C 41.800 0.75 1 123 23 23 LYS HE3 H 2.860 0.03 1 124 23 23 LYS HE2 H 2.860 0.03 1 125 23 23 LYS C C 175.200 0.75 1 126 24 24 LEU N N 117.690 0.5 1 127 24 24 LEU H H 7.820 0.03 1 128 24 24 LEU CA C 52.790 0.75 1 129 24 24 LEU HA H 4.070 0.03 1 130 24 24 LEU CB C 41.370 0.75 1 131 24 24 LEU HB3 H 1.150 0.03 2 132 24 24 LEU HB2 H 1.120 0.03 2 133 24 24 LEU CG C 26.680 0.75 1 134 24 24 LEU HG H 1.310 0.03 1 135 24 24 LEU CD1 C 24.320 0.75 1 136 24 24 LEU HD1 H 0.660 0.03 2 137 24 24 LEU CD2 C 26.280 0.75 1 138 24 24 LEU HD2 H 0.500 0.03 2 139 24 24 LEU C C 175.110 0.75 1 140 25 25 PRO CA C 61.750 0.75 1 141 25 25 PRO HA H 4.460 0.03 1 142 25 25 PRO CB C 31.410 0.75 1 143 25 25 PRO HB3 H 2.320 0.03 2 144 25 25 PRO HB2 H 1.780 0.03 2 145 25 25 PRO CG C 27.700 0.75 1 146 25 25 PRO HG3 H 1.910 0.03 2 147 25 25 PRO HG2 H 1.680 0.03 2 148 25 25 PRO CD C 49.460 0.75 1 149 25 25 PRO HD3 H 3.670 0.03 2 150 25 25 PRO HD2 H 3.180 0.03 2 151 25 25 PRO C C 177.650 0.75 1 152 26 26 ILE N N 123.020 0.5 1 153 26 26 ILE H H 8.430 0.03 1 154 26 26 ILE CA C 62.520 0.75 1 155 26 26 ILE HA H 3.850 0.03 1 156 26 26 ILE CB C 37.850 0.75 1 157 26 26 ILE HB H 1.820 0.03 1 158 26 26 ILE CG1 C 28.060 0.75 2 159 26 26 ILE HG13 H 1.450 0.03 1 160 26 26 ILE HG12 H 1.250 0.03 1 161 26 26 ILE CD1 C 13.530 0.75 1 162 26 26 ILE HD1 H 0.890 0.03 1 163 26 26 ILE CG2 C 17.410 0.75 1 164 26 26 ILE HG2 H 0.920 0.03 1 165 26 26 ILE C C 175.580 0.75 1 166 27 27 ASP N N 119.740 0.5 1 167 27 27 ASP H H 8.330 0.03 1 168 27 27 ASP CA C 52.940 0.75 1 169 27 27 ASP HA H 4.520 0.03 1 170 27 27 ASP CB C 38.990 0.75 1 171 27 27 ASP HB3 H 2.830 0.03 2 172 27 27 ASP HB2 H 2.610 0.03 2 173 27 27 ASP C C 175.580 0.75 1 174 28 28 VAL N N 119.740 0.5 1 175 28 28 VAL H H 6.970 0.03 1 176 28 28 VAL CA C 61.520 0.75 1 177 28 28 VAL HA H 4.000 0.03 1 178 28 28 VAL CB C 31.410 0.75 1 179 28 28 VAL HB H 2.010 0.03 1 180 28 28 VAL CG2 C 23.160 0.75 1 181 28 28 VAL HG2 H 1.050 0.03 2 182 28 28 VAL CG1 C 20.770 0.75 1 183 28 28 VAL HG1 H 0.740 0.03 2 184 28 28 VAL C C 173.630 0.75 1 185 29 29 THR N N 117.690 0.5 1 186 29 29 THR H H 8.140 0.03 1 187 29 29 THR CA C 59.530 0.75 1 188 29 29 THR HA H 4.690 0.03 1 189 29 29 THR CB C 71.640 0.75 1 190 29 29 THR HB H 4.590 0.03 1 191 29 29 THR CG2 C 21.830 0.75 1 192 29 29 THR HG2 H 1.240 0.03 1 193 29 29 THR C C 175.690 0.75 1 194 30 30 GLU N N 123.210 0.5 1 195 30 30 GLU H H 9.310 0.03 1 196 30 30 GLU CA C 60.300 0.75 1 197 30 30 GLU HA H 3.850 0.03 1 198 30 30 GLU CB C 28.800 0.75 1 199 30 30 GLU HB3 H 2.020 0.03 2 200 30 30 GLU HB2 H 1.900 0.03 2 201 30 30 GLU CG C 37.400 0.75 1 202 30 30 GLU HG3 H 2.380 0.03 2 203 30 30 GLU HG2 H 2.350 0.03 2 204 30 30 GLU C C 178.860 0.75 1 205 31 31 GLY N N 106.510 0.5 1 206 31 31 GLY H H 8.700 0.03 1 207 31 31 GLY CA C 46.580 0.75 1 208 31 31 GLY HA3 H 3.870 0.03 2 209 31 31 GLY HA2 H 3.710 0.03 2 210 31 31 GLY C C 177.110 0.75 1 211 32 32 GLU N N 123.080 0.5 1 212 32 32 GLU H H 7.660 0.03 1 213 32 32 GLU CA C 58.460 0.75 1 214 32 32 GLU HA H 3.960 0.03 1 215 32 32 GLU CB C 30.410 0.75 1 216 32 32 GLU HB3 H 2.350 0.03 2 217 32 32 GLU HB2 H 1.890 0.03 2 218 32 32 GLU CG C 38.240 0.75 1 219 32 32 GLU HG3 H 2.220 0.03 1 220 32 32 GLU HG2 H 2.220 0.03 1 221 32 32 GLU C C 178.650 0.75 1 222 33 33 VAL N N 120.960 0.5 1 223 33 33 VAL H H 7.440 0.03 1 224 33 33 VAL CA C 66.200 0.75 1 225 33 33 VAL HA H 3.440 0.03 1 226 33 33 VAL CB C 30.640 0.75 1 227 33 33 VAL HB H 2.110 0.03 1 228 33 33 VAL CG2 C 24.030 0.75 1 229 33 33 VAL HG2 H 0.830 0.03 2 230 33 33 VAL CG1 C 22.910 0.75 1 231 33 33 VAL HG1 H 0.690 0.03 2 232 33 33 VAL C C 177.870 0.75 1 233 34 34 ILE N N 120.390 0.5 1 234 34 34 ILE H H 8.500 0.03 1 235 34 34 ILE CA C 65.280 0.75 1 236 34 34 ILE HA H 3.540 0.03 1 237 34 34 ILE CB C 37.850 0.75 1 238 34 34 ILE HB H 1.840 0.03 1 239 34 34 ILE CG1 C 30.530 0.75 2 240 34 34 ILE HG13 H 1.750 0.03 1 241 34 34 ILE HG12 H 1.020 0.03 1 242 34 34 ILE CD1 C 13.260 0.75 1 243 34 34 ILE HD1 H 0.820 0.03 1 244 34 34 ILE CG2 C 17.330 0.75 1 245 34 34 ILE HG2 H 0.950 0.03 1 246 34 34 ILE C C 179.070 0.75 1 247 35 35 SER N N 116.020 0.5 1 248 35 35 SER H H 7.890 0.03 1 249 35 35 SER CA C 62.290 0.75 1 250 35 35 SER HA H 4.020 0.03 1 251 35 35 SER CB C 62.440 0.75 1 252 35 35 SER HB3 H 4.020 0.03 1 253 35 35 SER HB2 H 4.020 0.03 1 254 35 35 SER C C 175.400 0.75 1 255 36 36 LEU N N 121.610 0.5 1 256 36 36 LEU H H 7.510 0.03 1 257 36 36 LEU CA C 56.160 0.75 1 258 36 36 LEU HA H 4.280 0.03 1 259 36 36 LEU CB C 42.210 0.75 1 260 36 36 LEU HB3 H 1.960 0.03 2 261 36 36 LEU HB2 H 1.180 0.03 2 262 36 36 LEU CG C 26.520 0.75 1 263 36 36 LEU CD1 C 22.180 0.75 1 264 36 36 LEU HD1 H 0.710 0.03 1 265 36 36 LEU CD2 C 22.180 0.75 1 266 36 36 LEU HD2 H 0.710 0.03 1 267 36 36 LEU C C 179.680 0.75 1 268 37 37 GLY N N 104.200 0.5 1 269 37 37 GLY H H 7.950 0.03 1 270 37 37 GLY CA C 45.510 0.75 1 271 37 37 GLY HA3 H 5.000 0.03 2 272 37 37 GLY HA2 H 3.380 0.03 2 273 37 37 GLY C C 173.650 0.75 1 274 38 38 LEU N N 121.990 0.5 1 275 38 38 LEU H H 7.190 0.03 1 276 38 38 LEU CA C 57.390 0.75 1 277 38 38 LEU HA H 4.630 0.03 1 278 38 38 LEU CB C 39.610 0.75 1 279 38 38 LEU HB3 H 1.800 0.03 2 280 38 38 LEU HB2 H 1.510 0.03 2 281 38 38 LEU CG C 26.340 0.75 1 282 38 38 LEU HG H 1.860 0.03 1 283 38 38 LEU CD1 C 25.060 0.75 1 284 38 38 LEU HD1 H 0.920 0.03 1 285 38 38 LEU CD2 C 21.880 0.75 1 286 38 38 LEU HD2 H 0.920 0.03 1 287 38 38 LEU C C 175.470 0.75 1 288 39 39 PRO CA C 64.130 0.75 1 289 39 39 PRO HA H 4.030 0.03 1 290 39 39 PRO CB C 30.030 0.75 1 291 39 39 PRO HB3 H 1.700 0.03 2 292 39 39 PRO HB2 H -0.090 0.03 2 293 39 39 PRO CG C 27.700 0.75 1 294 39 39 PRO HG3 H 1.650 0.03 2 295 39 39 PRO HG2 H 1.610 0.03 2 296 39 39 PRO CD C 50.700 0.75 1 297 39 39 PRO HD3 H 3.740 0.03 2 298 39 39 PRO HD2 H 3.080 0.03 2 299 39 39 PRO C C 176.550 0.75 1 300 40 40 PHE N N 114.090 0.5 1 301 40 40 PHE H H 7.770 0.03 1 302 40 40 PHE CA C 57.390 0.75 1 303 40 40 PHE HA H 4.410 0.03 1 304 40 40 PHE CB C 40.140 0.75 1 305 40 40 PHE HB3 H 3.440 0.03 2 306 40 40 PHE HB2 H 2.720 0.03 2 307 40 40 PHE CD1 C 131.700 0.75 1 308 40 40 PHE HD1 H 7.250 0.03 1 309 40 40 PHE CE1 C 131.300 0.75 1 310 40 40 PHE HE1 H 7.080 0.03 1 311 40 40 PHE CZ C 129.580 0.75 1 312 40 40 PHE HZ H 6.110 0.03 1 313 40 40 PHE CE2 C 131.300 0.75 1 314 40 40 PHE HE2 H 7.080 0.03 1 315 40 40 PHE CD2 C 131.700 0.75 1 316 40 40 PHE HD2 H 7.250 0.03 1 317 40 40 PHE C C 175.150 0.75 1 318 41 41 GLY N N 108.440 0.5 1 319 41 41 GLY H H 7.600 0.03 1 320 41 41 GLY CA C 45.120 0.75 1 321 41 41 GLY HA3 H 4.000 0.03 2 322 41 41 GLY HA2 H 3.960 0.03 2 323 41 41 GLY C C 170.220 0.75 1 324 42 42 LYS N N 120.510 0.5 1 325 42 42 LYS H H 7.540 0.03 1 326 42 42 LYS CA C 54.400 0.75 1 327 42 42 LYS HA H 4.410 0.03 1 328 42 42 LYS CB C 33.630 0.75 1 329 42 42 LYS HB3 H 1.610 0.03 2 330 42 42 LYS HB2 H 1.480 0.03 2 331 42 42 LYS CG C 24.880 0.75 1 332 42 42 LYS HG3 H 1.420 0.03 2 333 42 42 LYS HG2 H 1.240 0.03 2 334 42 42 LYS CD C 28.500 0.75 1 335 42 42 LYS HD3 H 1.600 0.03 1 336 42 42 LYS HD2 H 1.600 0.03 1 337 42 42 LYS CE C 41.300 0.75 1 338 42 42 LYS HE3 H 2.920 0.03 1 339 42 42 LYS HE2 H 2.920 0.03 1 340 42 42 LYS C C 175.070 0.75 1 341 43 43 VAL N N 126.750 0.5 1 342 43 43 VAL H H 8.060 0.03 1 343 43 43 VAL CA C 61.370 0.75 1 344 43 43 VAL HA H 4.590 0.03 1 345 43 43 VAL CB C 31.710 0.75 1 346 43 43 VAL HB H 2.010 0.03 1 347 43 43 VAL CG2 C 21.870 0.75 1 348 43 43 VAL HG2 H 0.960 0.03 2 349 43 43 VAL CG1 C 21.150 0.75 1 350 43 43 VAL HG1 H 1.080 0.03 2 351 43 43 VAL C C 177.220 0.75 1 352 44 44 THR N N 122.890 0.5 1 353 44 44 THR H H 9.200 0.03 1 354 44 44 THR CA C 62.060 0.75 1 355 44 44 THR HA H 4.240 0.03 1 356 44 44 THR CB C 67.810 0.75 1 357 44 44 THR HB H 4.170 0.03 1 358 44 44 THR CG2 C 22.650 0.75 1 359 44 44 THR HG2 H 1.030 0.03 1 360 44 44 THR C C 175.170 0.75 1 361 45 45 ASN N N 119.810 0.5 1 362 45 45 ASN H H 7.750 0.03 1 363 45 45 ASN CA C 52.790 0.75 1 364 45 45 ASN HA H 4.790 0.03 1 365 45 45 ASN CB C 41.830 0.75 1 366 45 45 ASN HB3 H 2.800 0.03 2 367 45 45 ASN HB2 H 2.390 0.03 2 368 45 45 ASN ND2 N 114.780 0.5 1 369 45 45 ASN HD21 H 6.760 0.03 2 370 45 45 ASN HD22 H 7.860 0.03 2 371 45 45 ASN C C 172.020 0.75 1 372 46 46 LEU N N 124.430 0.5 1 373 46 46 LEU H H 8.360 0.03 1 374 46 46 LEU CA C 53.940 0.75 1 375 46 46 LEU HA H 5.010 0.03 1 376 46 46 LEU CB C 44.890 0.75 1 377 46 46 LEU HB3 H 1.690 0.03 2 378 46 46 LEU HB2 H 1.330 0.03 2 379 46 46 LEU CG C 27.820 0.75 1 380 46 46 LEU HG H 1.390 0.03 1 381 46 46 LEU CD1 C 25.190 0.75 1 382 46 46 LEU HD1 H 0.820 0.03 2 383 46 46 LEU CD2 C 26.280 0.75 1 384 46 46 LEU HD2 H 0.890 0.03 2 385 46 46 LEU C C 173.960 0.75 1 386 47 47 LEU N N 129.760 0.5 1 387 47 47 LEU H H 9.130 0.03 1 388 47 47 LEU CA C 53.630 0.75 1 389 47 47 LEU HA H 4.760 0.03 1 390 47 47 LEU CB C 44.820 0.75 1 391 47 47 LEU HB3 H 1.830 0.03 2 392 47 47 LEU HB2 H 1.440 0.03 2 393 47 47 LEU CG C 27.500 0.75 1 394 47 47 LEU HG H 1.510 0.03 1 395 47 47 LEU CD1 C 23.140 0.75 1 396 47 47 LEU HD1 H 0.910 0.03 2 397 47 47 LEU CD2 C 25.050 0.75 1 398 47 47 LEU HD2 H 0.780 0.03 2 399 47 47 LEU C C 174.980 0.75 1 400 48 48 MET N N 127.900 0.5 1 401 48 48 MET H H 9.140 0.03 1 402 48 48 MET CA C 53.860 0.75 1 403 48 48 MET HA H 4.690 0.03 1 404 48 48 MET CB C 32.560 0.75 1 405 48 48 MET HB3 H 2.030 0.03 1 406 48 48 MET HB2 H 2.030 0.03 1 407 48 48 MET CG C 31.780 0.75 1 408 48 48 MET HG3 H 2.600 0.03 2 409 48 48 MET HG2 H 2.420 0.03 2 410 48 48 MET CE C 16.850 0.75 1 411 48 48 MET HE H 1.850 0.03 1 412 48 48 MET C C 175.290 0.75 1 413 49 49 LEU N N 129.190 0.5 1 414 49 49 LEU H H 8.430 0.03 1 415 49 49 LEU CA C 53.020 0.75 1 416 49 49 LEU HA H 4.740 0.03 1 417 49 49 LEU CB C 40.530 0.75 1 418 49 49 LEU HB3 H 1.580 0.03 2 419 49 49 LEU HB2 H 1.470 0.03 2 420 49 49 LEU CG C 27.700 0.75 1 421 49 49 LEU HG H 1.530 0.03 1 422 49 49 LEU CD1 C 24.150 0.75 1 423 49 49 LEU HD1 H 0.890 0.03 1 424 49 49 LEU CD2 C 25.580 0.75 1 425 49 49 LEU HD2 H 0.890 0.03 1 426 49 49 LEU C C 177.060 0.75 1 427 50 50 LYS N N 126.360 0.5 1 428 50 50 LYS H H 8.420 0.03 1 429 50 50 LYS CA C 58.920 0.75 1 430 50 50 LYS HA H 4.040 0.03 1 431 50 50 LYS CB C 31.790 0.75 1 432 50 50 LYS HB3 H 1.830 0.03 1 433 50 50 LYS HB2 H 1.830 0.03 1 434 50 50 LYS CG C 25.460 0.75 1 435 50 50 LYS HG3 H 1.520 0.03 2 436 50 50 LYS HG2 H 1.420 0.03 2 437 50 50 LYS CD C 29.250 0.75 1 438 50 50 LYS HD3 H 1.730 0.03 1 439 50 50 LYS HD2 H 1.730 0.03 1 440 50 50 LYS CE C 41.810 0.75 1 441 50 50 LYS HE3 H 3.000 0.03 1 442 50 50 LYS HE2 H 3.000 0.03 1 443 51 51 GLY N N 111.200 0.5 1 444 51 51 GLY H H 8.940 0.03 1 445 51 51 GLY CA C 45.430 0.75 1 446 51 51 GLY HA3 H 4.000 0.03 1 447 51 51 GLY HA2 H 4.000 0.03 1 448 51 51 GLY C C 174.470 0.75 1 449 52 52 LYS N N 118.200 0.5 1 450 52 52 LYS H H 7.470 0.03 1 451 52 52 LYS CA C 54.170 0.75 1 452 52 52 LYS CB C 33.250 0.75 1 453 52 52 LYS C C 175.940 0.75 1 454 53 53 ASN N N 118.270 0.5 1 455 53 53 ASN H H 8.250 0.03 1 456 53 53 ASN CA C 53.860 0.75 1 457 53 53 ASN HA H 4.490 0.03 1 458 53 53 ASN CB C 36.390 0.75 1 459 53 53 ASN HB3 H 3.280 0.03 2 460 53 53 ASN HB2 H 3.020 0.03 2 461 53 53 ASN ND2 N 113.450 0.5 1 462 53 53 ASN HD21 H 6.540 0.03 2 463 53 53 ASN HD22 H 7.650 0.03 2 464 53 53 ASN C C 174.010 0.75 1 465 54 54 GLN N N 114.730 0.5 1 466 54 54 GLN H H 7.410 0.03 1 467 54 54 GLN CA C 53.090 0.75 1 468 54 54 GLN HA H 5.280 0.03 1 469 54 54 GLN CB C 35.010 0.75 1 470 54 54 GLN HB3 H 2.070 0.03 2 471 54 54 GLN HB2 H 1.710 0.03 2 472 54 54 GLN CG C 34.070 0.75 1 473 54 54 GLN HG3 H 2.590 0.03 2 474 54 54 GLN HG2 H 2.380 0.03 2 475 54 54 GLN C C 174.240 0.75 1 476 55 55 ALA N N 121.670 0.5 1 477 55 55 ALA H H 8.890 0.03 1 478 55 55 ALA CA C 50.870 0.75 1 479 55 55 ALA HA H 5.060 0.03 1 480 55 55 ALA CB C 24.050 0.75 1 481 55 55 ALA HB H 1.270 0.03 1 482 55 55 ALA C C 174.460 0.75 1 483 56 56 PHE N N 119.490 0.5 1 484 56 56 PHE H H 9.210 0.03 1 485 56 56 PHE CA C 55.780 0.75 1 486 56 56 PHE HA H 5.730 0.03 1 487 56 56 PHE CB C 41.980 0.75 1 488 56 56 PHE HB3 H 2.740 0.03 1 489 56 56 PHE HB2 H 2.740 0.03 1 490 56 56 PHE CD1 C 130.900 0.75 1 491 56 56 PHE HD1 H 6.940 0.03 1 492 56 56 PHE CE1 C 130.900 0.75 1 493 56 56 PHE HE1 H 6.860 0.03 1 494 56 56 PHE CZ C 129.100 0.75 1 495 56 56 PHE HZ H 6.730 0.03 1 496 56 56 PHE CE2 C 130.900 0.75 1 497 56 56 PHE HE2 H 6.860 0.03 1 498 56 56 PHE CD2 C 130.900 0.75 1 499 56 56 PHE HD2 H 6.940 0.03 1 500 56 56 PHE C C 175.180 0.75 1 501 57 57 ILE N N 120.900 0.5 1 502 57 57 ILE H H 9.210 0.03 1 503 57 57 ILE CA C 58.760 0.75 1 504 57 57 ILE HA H 4.830 0.03 1 505 57 57 ILE CB C 41.750 0.75 1 506 57 57 ILE HB H 1.630 0.03 1 507 57 57 ILE CG1 C 27.180 0.75 2 508 57 57 ILE HG13 H 1.550 0.03 1 509 57 57 ILE HG12 H 0.920 0.03 1 510 57 57 ILE CD1 C 14.090 0.75 1 511 57 57 ILE HD1 H 0.770 0.03 1 512 57 57 ILE CG2 C 18.600 0.75 1 513 57 57 ILE HG2 H 0.870 0.03 1 514 57 57 ILE C C 172.700 0.75 1 515 58 58 GLU N N 128.800 0.5 1 516 58 58 GLU H H 8.610 0.03 1 517 58 58 GLU CA C 53.860 0.75 1 518 58 58 GLU HA H 5.030 0.03 1 519 58 58 GLU CB C 33.170 0.75 1 520 58 58 GLU HB3 H 2.090 0.03 2 521 58 58 GLU HB2 H 1.660 0.03 2 522 58 58 GLU CG C 37.330 0.75 1 523 58 58 GLU HG3 H 2.220 0.03 2 524 58 58 GLU HG2 H 1.930 0.03 2 525 58 58 GLU C C 175.050 0.75 1 526 59 59 MET N N 124.630 0.5 1 527 59 59 MET H H 8.780 0.03 1 528 59 59 MET CA C 51.410 0.75 1 529 59 59 MET HA H 5.680 0.03 1 530 59 59 MET CB C 32.020 0.75 1 531 59 59 MET HB3 H 2.230 0.03 2 532 59 59 MET HB2 H 2.150 0.03 2 533 59 59 MET CG C 32.980 0.75 1 534 59 59 MET HG3 H 2.550 0.03 2 535 59 59 MET HG2 H 2.310 0.03 2 536 59 59 MET CE C 15.990 0.75 1 537 59 59 MET HE H 1.850 0.03 1 538 59 59 MET C C 177.780 0.75 1 539 60 60 ASN N N 118.520 0.5 1 540 60 60 ASN H H 9.100 0.03 1 541 60 60 ASN CA C 56.010 0.75 1 542 60 60 ASN HA H 4.320 0.03 1 543 60 60 ASN CB C 37.160 0.75 1 544 60 60 ASN HB3 H 2.920 0.03 2 545 60 60 ASN HB2 H 2.800 0.03 2 546 60 60 ASN ND2 N 117.620 0.5 1 547 60 60 ASN HD21 H 7.260 0.03 2 548 60 60 ASN HD22 H 7.900 0.03 2 549 60 60 ASN C C 175.110 0.75 1 550 61 61 THR N N 106.510 0.5 1 551 61 61 THR H H 7.270 0.03 1 552 61 61 THR CA C 58.300 0.75 1 553 61 61 THR HA H 4.750 0.03 1 554 61 61 THR CB C 72.940 0.75 1 555 61 61 THR HB H 4.750 0.03 1 556 61 61 THR CG2 C 21.840 0.75 1 557 61 61 THR HG2 H 1.260 0.03 1 558 61 61 THR C C 174.360 0.75 1 559 62 62 GLU N N 124.430 0.5 1 560 62 62 GLU H H 9.330 0.03 1 561 62 62 GLU CA C 59.220 0.75 1 562 62 62 GLU HA H 3.950 0.03 1 563 62 62 GLU CB C 28.800 0.75 1 564 62 62 GLU HB3 H 2.030 0.03 2 565 62 62 GLU HB2 H 1.910 0.03 2 566 62 62 GLU HG3 H 2.210 0.03 1 567 62 62 GLU HG2 H 2.210 0.03 1 568 62 62 GLU C C 178.740 0.75 1 569 63 63 GLU N N 122.700 0.5 1 570 63 63 GLU H H 8.810 0.03 1 571 63 63 GLU CA C 59.830 0.75 1 572 63 63 GLU HA H 4.120 0.03 1 573 63 63 GLU CB C 28.650 0.75 1 574 63 63 GLU HB3 H 2.140 0.03 2 575 63 63 GLU HB2 H 2.000 0.03 2 576 63 63 GLU HG3 H 2.370 0.03 2 577 63 63 GLU HG2 H 2.320 0.03 2 578 63 63 GLU C C 179.000 0.75 1 579 64 64 ALA N N 126.230 0.5 1 580 64 64 ALA H H 8.410 0.03 1 581 64 64 ALA CA C 54.860 0.75 1 582 64 64 ALA HA H 4.190 0.03 1 583 64 64 ALA CB C 19.530 0.75 1 584 64 64 ALA HB H 1.550 0.03 1 585 64 64 ALA C C 179.390 0.75 1 586 65 65 ALA N N 120.260 0.5 1 587 65 65 ALA H H 7.480 0.03 1 588 65 65 ALA CA C 55.090 0.75 1 589 65 65 ALA HA H 3.960 0.03 1 590 65 65 ALA CB C 18.920 0.75 1 591 65 65 ALA HB H 1.710 0.03 1 592 65 65 ALA C C 178.380 0.75 1 593 66 66 ASN N N 118.140 0.5 1 594 66 66 ASN H H 8.870 0.03 1 595 66 66 ASN CA C 56.470 0.75 1 596 66 66 ASN HA H 4.560 0.03 1 597 66 66 ASN CB C 39.070 0.75 1 598 66 66 ASN HB3 H 2.960 0.03 2 599 66 66 ASN HB2 H 2.880 0.03 2 600 66 66 ASN ND2 N 115.440 0.5 1 601 66 66 ASN HD21 H 7.270 0.03 2 602 66 66 ASN HD22 H 7.750 0.03 2 603 66 66 ASN C C 177.670 0.75 1 604 67 67 THR N N 118.780 0.5 1 605 67 67 THR H H 8.630 0.03 1 606 67 67 THR CA C 66.350 0.75 1 607 67 67 THR HA H 3.870 0.03 1 608 67 67 THR CB C 67.810 0.75 1 609 67 67 THR HB H 4.37 0.03 1 610 67 67 THR CG2 C 22.410 0.75 1 611 67 67 THR HG2 H 1.420 0.03 1 612 67 67 THR C C 175.880 0.75 1 613 68 68 MET N N 124.950 0.5 1 614 68 68 MET H H 7.810 0.03 1 615 68 68 MET CA C 58.460 0.75 1 616 68 68 MET HA H 2.140 0.03 1 617 68 68 MET CB C 32.100 0.75 1 618 68 68 MET HB3 H 2.020 0.03 2 619 68 68 MET CG C 32.100 0.75 1 620 68 68 MET HG3 H 2.380 0.03 2 621 68 68 MET HG2 H 1.390 0.03 2 622 68 68 MET CE C 17.710 0.75 1 623 68 68 MET HE H 1.920 0.03 1 624 68 68 MET C C 176.550 0.75 1 625 69 69 VAL N N 120.000 0.5 1 626 69 69 VAL H H 8.150 0.03 1 627 69 69 VAL CA C 66.810 0.75 1 628 69 69 VAL HA H 3.210 0.03 1 629 69 69 VAL CB C 31.180 0.75 1 630 69 69 VAL HB H 1.570 0.03 1 631 69 69 VAL CG2 C 23.440 0.75 1 632 69 69 VAL HG2 H 0.040 0.03 2 633 69 69 VAL CG1 C 21.110 0.75 1 634 69 69 VAL HG1 H 0.540 0.03 2 635 69 69 VAL C C 179.100 0.75 1 636 70 70 ASN N N 120.450 0.5 1 637 70 70 ASN H H 8.370 0.03 1 638 70 70 ASN CA C 56.080 0.75 1 639 70 70 ASN HA H 4.330 0.03 1 640 70 70 ASN CB C 37.620 0.75 1 641 70 70 ASN HB3 H 2.880 0.03 2 642 70 70 ASN HB2 H 2.730 0.03 2 643 70 70 ASN ND2 N 114.280 0.5 1 644 70 70 ASN HD21 H 6.930 0.03 2 645 70 70 ASN HD22 H 7.610 0.03 2 646 70 70 ASN C C 178.350 0.75 1 647 71 71 TYR N N 125.400 0.5 1 648 71 71 TYR H H 8.320 0.03 1 649 71 71 TYR CA C 61.830 0.75 1 650 71 71 TYR HA H 4.030 0.03 1 651 71 71 TYR CB C 38.070 0.75 1 652 71 71 TYR HB3 H 2.940 0.03 2 653 71 71 TYR HB2 H 2.540 0.03 2 654 71 71 TYR CD1 C 133.300 0.75 1 655 71 71 TYR HD1 H 6.280 0.03 1 656 71 71 TYR CE1 C 118.100 0.75 1 657 71 71 TYR HE1 H 6.630 0.03 1 658 71 71 TYR CE2 C 118.100 0.75 1 659 71 71 TYR HE2 H 6.630 0.03 1 660 71 71 TYR CD2 C 133.300 0.75 1 661 71 71 TYR HD2 H 6.280 0.03 1 662 71 71 TYR C C 178.060 0.75 1 663 72 72 TYR N N 117.690 0.5 1 664 72 72 TYR H H 7.820 0.03 1 665 72 72 TYR CA C 58.760 0.75 1 666 72 72 TYR HA H 5.210 0.03 1 667 72 72 TYR CB C 36.770 0.75 1 668 72 72 TYR HB3 H 3.390 0.03 2 669 72 72 TYR HB2 H 2.590 0.03 2 670 72 72 TYR CD1 C 133.600 0.75 1 671 72 72 TYR HD1 H 7.190 0.03 1 672 72 72 TYR CE1 C 117.800 0.75 1 673 72 72 TYR HE1 H 6.990 0.03 1 674 72 72 TYR CE2 C 117.800 0.75 1 675 72 72 TYR HE2 H 6.990 0.03 1 676 72 72 TYR CD2 C 133.600 0.75 1 677 72 72 TYR HD2 H 7.190 0.03 1 678 72 72 TYR C C 175.690 0.75 1 679 73 73 THR N N 115.310 0.5 1 680 73 73 THR H H 7.620 0.03 1 681 73 73 THR CA C 64.360 0.75 1 682 73 73 THR HA H 4.300 0.03 1 683 73 73 THR CB C 68.570 0.75 1 684 73 73 THR HB H 4.360 0.03 1 685 73 73 THR CG2 C 21.100 0.75 1 686 73 73 THR HG2 H 1.290 0.03 1 687 73 73 THR C C 175.130 0.75 1 688 74 74 SER N N 118.010 0.5 1 689 74 74 SER H H 7.330 0.03 1 690 74 74 SER CA C 59.220 0.75 1 691 74 74 SER HA H 4.500 0.03 1 692 74 74 SER CB C 63.670 0.75 1 693 74 74 SER HB3 H 3.850 0.03 2 694 74 74 SER HB2 H 3.810 0.03 2 695 74 74 SER C C 173.590 0.75 1 696 75 75 VAL N N 125.140 0.5 1 697 75 75 VAL H H 7.710 0.03 1 698 75 75 VAL CA C 60.330 0.75 1 699 75 75 VAL HA H 4.080 0.03 1 700 75 75 VAL CB C 32.710 0.75 1 701 75 75 VAL HB H 1.500 0.03 1 702 75 75 VAL CG2 C 20.940 0.75 1 703 75 75 VAL HG2 H 0.790 0.03 2 704 75 75 VAL CG1 C 20.420 0.75 1 705 75 75 VAL HG1 H 0.490 0.03 2 706 75 75 VAL C C 174.180 0.75 1 707 76 76 THR N N 123.340 0.5 1 708 76 76 THR H H 8.130 0.03 1 709 76 76 THR CA C 60.370 0.75 1 710 76 76 THR HA H 4.310 0.03 1 711 76 76 THR CB C 69.260 0.75 1 712 76 76 THR HB H 3.950 0.03 1 713 76 76 THR CG2 C 20.800 0.75 1 714 76 76 THR HG2 H 1.220 0.03 1 715 76 76 THR C C 173.050 0.75 1 716 77 77 PRO CA C 61.910 0.75 1 717 77 77 PRO HA H 4.540 0.03 1 718 77 77 PRO CB C 30.110 0.75 1 719 77 77 PRO HB3 H 1.420 0.03 2 720 77 77 PRO HB2 H 1.270 0.03 2 721 77 77 PRO CG C 26.180 0.75 1 722 77 77 PRO HG3 H 2.060 0.03 2 723 77 77 PRO HG2 H 1.480 0.03 2 724 77 77 PRO CD C 50.090 0.75 1 725 77 77 PRO HD3 H 4.360 0.03 2 726 77 77 PRO HD2 H 4.030 0.03 2 727 77 77 PRO C C 173.700 0.75 1 728 78 78 VAL N N 119.810 0.5 1 729 78 78 VAL H H 7.750 0.03 1 730 78 78 VAL CA C 59.220 0.75 1 731 78 78 VAL HA H 4.740 0.03 1 732 78 78 VAL CB C 35.470 0.75 1 733 78 78 VAL HB H 1.580 0.03 1 734 78 78 VAL CG2 C 21.080 0.75 1 735 78 78 VAL HG2 H 0.570 0.03 2 736 78 78 VAL CG1 C 20.120 0.75 1 737 78 78 VAL HG1 H 0.710 0.03 2 738 78 78 VAL C C 175.330 0.75 1 739 79 79 LEU N N 125.650 0.5 1 740 79 79 LEU H H 8.450 0.03 1 741 79 79 LEU CA C 53.480 0.75 1 742 79 79 LEU HA H 4.560 0.03 1 743 79 79 LEU CB C 46.270 0.75 1 744 79 79 LEU HB3 H 1.310 0.03 2 745 79 79 LEU HB2 H 1.260 0.03 2 746 79 79 LEU CG C 27.180 0.75 1 747 79 79 LEU HG H 1.470 0.03 1 748 79 79 LEU CD1 C 24.580 0.75 1 749 79 79 LEU HD1 H 0.750 0.03 1 750 79 79 LEU CD2 C 25.680 0.75 1 751 79 79 LEU HD2 H 0.750 0.03 1 752 79 79 LEU C C 175.750 0.75 1 753 80 80 ARG N N 124.300 0.5 1 754 80 80 ARG H H 9.480 0.03 1 755 80 80 ARG CA C 56.080 0.75 1 756 80 80 ARG HA H 3.870 0.03 1 757 80 80 ARG CB C 27.500 0.75 1 758 80 80 ARG CG C 27.300 0.75 1 759 80 80 ARG HG3 H 1.810 0.03 2 760 80 80 ARG CD C 43.380 0.75 1 761 80 80 ARG HD3 H 3.170 0.03 2 762 80 80 ARG HD2 H 2.950 0.03 2 763 80 80 ARG NE N 85.790 0.5 1 764 80 80 ARG HE H 8.920 0.03 1 765 80 80 ARG C C 176.780 0.75 1 766 81 81 GLY N N 104.910 0.5 1 767 81 81 GLY H H 8.370 0.03 1 768 81 81 GLY CA C 44.970 0.75 1 769 81 81 GLY HA3 H 4.080 0.03 2 770 81 81 GLY HA2 H 3.470 0.03 2 771 81 81 GLY C C 173.370 0.75 1 772 82 82 GLN N N 123.660 0.5 1 773 82 82 GLN H H 7.990 0.03 1 774 82 82 GLN CA C 51.480 0.75 1 775 82 82 GLN HA H 4.920 0.03 1 776 82 82 GLN CB C 30.030 0.75 1 777 82 82 GLN HB3 H 2.160 0.03 2 778 82 82 GLN HB2 H 1.970 0.03 2 779 82 82 GLN CG C 33.280 0.75 1 780 82 82 GLN HG3 H 2.320 0.03 1 781 82 82 GLN HG2 H 2.320 0.03 1 782 82 82 GLN NE2 N 115.050 0.5 1 783 82 82 GLN HE21 H 6.870 0.03 2 784 82 82 GLN HE22 H 7.550 0.03 2 785 82 82 GLN C C 172.370 0.75 1 786 83 83 PRO CA C 62.140 0.75 1 787 83 83 PRO HA H 4.840 0.03 1 788 83 83 PRO CB C 31.640 0.75 1 789 83 83 PRO HB3 H 2.060 0.03 2 790 83 83 PRO HB2 H 1.770 0.03 2 791 83 83 PRO CG C 27.580 0.75 1 792 83 83 PRO HG3 H 2.120 0.03 2 793 83 83 PRO HG2 H 1.890 0.03 2 794 83 83 PRO CD C 50.530 0.75 1 795 83 83 PRO HD3 H 3.840 0.03 2 796 83 83 PRO HD2 H 3.710 0.03 2 797 83 83 PRO C C 176.370 0.75 1 798 84 84 ILE N N 119.170 0.5 1 799 84 84 ILE H H 7.750 0.03 1 800 84 84 ILE CA C 58.530 0.75 1 801 84 84 ILE HA H 4.560 0.03 1 802 84 84 ILE CB C 39.220 0.75 1 803 84 84 ILE HB H 1.830 0.03 1 804 84 84 ILE CD1 C 14.480 0.75 1 805 84 84 ILE HD1 H 0.530 0.03 1 806 84 84 ILE CG2 C 18.200 0.75 1 807 84 84 ILE HG2 H 0.820 0.03 1 808 84 84 ILE C C 173.720 0.75 1 809 85 85 TYR N N 120.580 0.5 1 810 85 85 TYR H H 7.710 0.03 1 811 85 85 TYR CA C 56.160 0.75 1 812 85 85 TYR HA H 4.820 0.03 1 813 85 85 TYR CB C 40.600 0.75 1 814 85 85 TYR HB3 H 2.710 0.03 2 815 85 85 TYR HB2 H 2.540 0.03 2 816 85 85 TYR CD1 C 132.700 0.75 1 817 85 85 TYR HD1 H 6.900 0.03 1 818 85 85 TYR CE1 C 118.400 0.75 1 819 85 85 TYR HE1 H 6.720 0.03 1 820 85 85 TYR CE2 C 118.400 0.75 1 821 85 85 TYR HE2 H 6.720 0.03 1 822 85 85 TYR CD2 C 132.700 0.75 1 823 85 85 TYR HD2 H 6.900 0.03 1 824 85 85 TYR C C 174.240 0.75 1 825 86 86 ILE N N 126.420 0.5 1 826 86 86 ILE H H 8.310 0.03 1 827 86 86 ILE CA C 59.760 0.75 1 828 86 86 ILE HA H 4.600 0.03 1 829 86 86 ILE CB C 40.300 0.75 1 830 86 86 ILE HB H 1.470 0.03 1 831 86 86 ILE CG1 C 28.100 0.75 2 832 86 86 ILE HG13 H 1.200 0.03 1 833 86 86 ILE HG12 H 0.780 0.03 1 834 86 86 ILE CD1 C 14.270 0.75 1 835 86 86 ILE HD1 H 0.330 0.03 1 836 86 86 ILE CG2 C 17.450 0.75 1 837 86 86 ILE HG2 H 0.580 0.03 1 838 86 86 ILE C C 173.540 0.75 1 839 87 87 GLN N N 124.240 0.5 1 840 87 87 GLN H H 8.420 0.03 1 841 87 87 GLN CA C 53.550 0.75 1 842 87 87 GLN HA H 4.510 0.03 1 843 87 87 GLN CB C 32.860 0.75 1 844 87 87 GLN HB3 H 2.290 0.03 2 845 87 87 GLN HB2 H 2.050 0.03 2 846 87 87 GLN CG C 33.280 0.75 1 847 87 87 GLN HG3 H 2.350 0.03 2 848 87 87 GLN HG2 H 2.270 0.03 2 849 87 87 GLN C C 174.750 0.75 1 850 88 88 PHE N N 121.860 0.5 1 851 88 88 PHE H H 8.880 0.03 1 852 88 88 PHE CA C 60.140 0.75 1 853 88 88 PHE HA H 4.710 0.03 1 854 88 88 PHE CB C 39.450 0.75 1 855 88 88 PHE HB3 H 3.320 0.03 2 856 88 88 PHE HB2 H 2.840 0.03 2 857 88 88 PHE CD1 C 131.700 0.75 1 858 88 88 PHE HD1 H 7.400 0.03 1 859 88 88 PHE CE1 C 131.700 0.75 1 860 88 88 PHE HE1 H 7.300 0.03 1 861 88 88 PHE CZ C 130.150 0.75 1 862 88 88 PHE HZ H 7.320 0.03 1 863 88 88 PHE CE2 C 131.700 0.75 1 864 88 88 PHE HE2 H 7.300 0.03 1 865 88 88 PHE CD2 C 131.700 0.75 1 866 88 88 PHE HD2 H 7.400 0.03 1 867 88 88 PHE C C 177.200 0.75 1 868 89 89 SER N N 117.170 0.5 1 869 89 89 SER H H 8.820 0.03 1 870 89 89 SER CA C 56.700 0.75 1 871 89 89 SER HA H 4.730 0.03 1 872 89 89 SER CB C 64.050 0.75 1 873 89 89 SER HB3 H 3.930 0.03 2 874 89 89 SER HB2 H 3.830 0.03 2 875 89 89 SER C C 175.050 0.75 1 876 90 90 ASN N N 123.730 0.5 1 877 90 90 ASN H H 8.780 0.03 1 878 90 90 ASN CA C 53.250 0.75 1 879 90 90 ASN HA H 4.710 0.03 1 880 90 90 ASN CB C 38.070 0.75 1 881 90 90 ASN HB3 H 2.720 0.03 1 882 90 90 ASN HB2 H 2.720 0.03 1 883 90 90 ASN ND2 N 114.280 0.5 1 884 90 90 ASN HD21 H 6.860 0.03 2 885 90 90 ASN HD22 H 7.610 0.03 2 886 90 90 ASN C C 175.260 0.75 1 887 91 91 HIS N N 121.220 0.5 1 888 91 91 HIS H H 8.310 0.03 1 889 91 91 HIS CA C 56.010 0.75 1 890 91 91 HIS HA H 4.500 0.03 1 891 91 91 HIS CB C 30.340 0.75 1 892 91 91 HIS HB3 H 3.030 0.03 2 893 91 91 HIS HB2 H 2.810 0.03 2 894 91 91 HIS CD2 C 119.700 0.75 1 895 91 91 HIS HD2 H 6.760 0.03 1 896 93 93 GLU N N 119.420 0.5 1 897 93 93 GLU H H 7.920 0.03 1 898 93 93 GLU CA C 55.090 0.75 1 899 93 93 GLU HA H 4.210 0.03 1 900 93 93 GLU CB C 30.570 0.75 1 901 93 93 GLU HB3 H 1.910 0.03 2 902 93 93 GLU HB2 H 1.800 0.03 2 903 93 93 GLU CG C 35.750 0.75 1 904 93 93 GLU HG3 H 2.090 0.03 1 905 93 93 GLU HG2 H 2.090 0.03 1 906 93 93 GLU C C 175.310 0.75 1 907 94 94 LEU N N 124.500 0.5 1 908 94 94 LEU H H 8.430 0.03 1 909 94 94 LEU CA C 54.010 0.75 1 910 94 94 LEU HA H 4.170 0.03 1 911 94 94 LEU CB C 41.750 0.75 1 912 94 94 LEU HB3 H 1.390 0.03 1 913 94 94 LEU HB2 H 1.390 0.03 1 914 94 94 LEU CG C 26.930 0.75 1 915 94 94 LEU HG H 1.380 0.03 1 916 94 94 LEU CD1 C 23.840 0.75 1 917 94 94 LEU HD1 H 0.540 0.03 2 918 94 94 LEU CD2 C 25.100 0.75 1 919 94 94 LEU HD2 H 0.620 0.03 2 920 94 94 LEU C C 176.160 0.75 1 921 95 95 LYS N N 124.500 0.5 1 922 95 95 LYS H H 8.100 0.03 1 923 95 95 LYS CA C 55.240 0.75 1 924 95 95 LYS HA H 4.350 0.03 1 925 95 95 LYS CB C 32.560 0.75 1 926 95 95 LYS HB3 H 1.700 0.03 1 927 95 95 LYS HB2 H 1.700 0.03 1 928 95 95 LYS CG C 24.880 0.75 1 929 95 95 LYS HG3 H 1.310 0.03 1 930 95 95 LYS HG2 H 1.310 0.03 1 931 95 95 LYS CD C 28.700 0.75 1 932 95 95 LYS HD3 H 1.600 0.03 1 933 95 95 LYS HD2 H 1.600 0.03 1 934 95 95 LYS CE C 41.730 0.75 1 935 95 95 LYS HE3 H 2.910 0.03 1 936 95 95 LYS HE2 H 2.910 0.03 1 937 95 95 LYS C C 176.330 0.75 1 938 96 96 THR N N 117.240 0.5 1 939 96 96 THR H H 8.200 0.03 1 940 96 96 THR CA C 60.910 0.75 1 941 96 96 THR HA H 4.300 0.03 1 942 96 96 THR CB C 69.030 0.75 1 943 96 96 THR HB H 4.210 0.03 1 944 96 96 THR CG2 C 21.640 0.75 1 945 96 96 THR HG2 H 1.100 0.03 1 946 96 96 THR C C 174.250 0.75 1 947 97 97 ASP N N 124.430 0.5 1 948 97 97 ASP H H 8.360 0.03 1 949 97 97 ASP CA C 53.710 0.75 1 950 97 97 ASP HA H 4.630 0.03 1 951 97 97 ASP CB C 40.680 0.75 1 952 97 97 ASP HB3 H 2.680 0.03 2 953 97 97 ASP HB2 H 2.620 0.03 2 954 97 97 ASP C C 176.040 0.75 1 955 98 98 SER N N 117.950 0.5 1 956 98 98 SER H H 8.210 0.03 1 957 98 98 SER CA C 57.690 0.75 1 958 98 98 SER HA H 4.450 0.03 1 959 98 98 SER CB C 63.210 0.75 1 960 98 98 SER HB3 H 3.830 0.03 1 961 98 98 SER HB2 H 3.830 0.03 1 962 98 98 SER C C 174.240 0.75 1 963 99 99 SER N N 121.220 0.5 1 964 99 99 SER H H 8.310 0.03 1 965 99 99 SER CA C 56.240 0.75 1 966 99 99 SER HA H 4.710 0.03 1 967 99 99 SER CB C 62.830 0.75 1 968 99 99 SER HB3 H 3.850 0.03 1 969 99 99 SER HB2 H 3.850 0.03 1 970 99 99 SER C C 175.300 0.75 1 971 100 100 PRO CA C 62.830 0.75 1 972 100 100 PRO HA H 4.410 0.03 1 973 100 100 PRO CB C 31.480 0.75 1 974 100 100 PRO HB3 H 2.250 0.03 2 975 100 100 PRO HB2 H 1.890 0.03 2 976 100 100 PRO CG C 27.220 0.75 1 977 100 100 PRO HG3 H 1.960 0.03 1 978 100 100 PRO HG2 H 1.960 0.03 1 979 100 100 PRO CD C 50.280 0.75 1 980 100 100 PRO HD3 H 3.920 0.03 2 981 100 100 PRO HD2 H 3.680 0.03 2 982 100 100 PRO C C 176.790 0.75 1 983 101 101 ASN N N 120.000 0.5 1 984 101 101 ASN H H 8.390 0.03 1 985 101 101 ASN CA C 52.940 0.75 1 986 101 101 ASN HA H 4.630 0.03 1 987 101 101 ASN CB C 38.000 0.75 1 988 101 101 ASN HB3 H 2.800 0.03 2 989 101 101 ASN HB2 H 2.730 0.03 2 990 101 101 ASN ND2 N 114.860 0.5 1 991 101 101 ASN HD21 H 6.930 0.03 2 992 101 101 ASN HD22 H 7.600 0.03 2 993 101 101 ASN C C 175.140 0.75 1 994 102 102 GLN N N 122.510 0.5 1 995 102 102 GLN H H 8.190 0.03 1 996 102 102 GLN CA C 55.470 0.75 1 997 102 102 GLN HA H 4.270 0.03 1 998 102 102 GLN CB C 29.030 0.75 1 999 102 102 GLN HB3 H 2.080 0.03 2 1000 102 102 GLN HB2 H 1.950 0.03 2 1001 102 102 GLN CG C 33.740 0.75 1 1002 102 102 GLN HG3 H 2.320 0.03 1 1003 102 102 GLN HG2 H 2.320 0.03 1 1004 102 102 GLN NE2 N 114.280 0.5 1 1005 102 102 GLN HE21 H 6.860 0.03 2 1006 102 102 GLN HE22 H 7.530 0.03 2 1007 102 102 GLN C C 175.450 0.75 1 1008 103 103 ALA N N 127.130 0.5 1 1009 103 103 ALA H H 8.270 0.03 1 1010 103 103 ALA CA C 52.020 0.75 1 1011 103 103 ALA HA H 4.280 0.03 1 1012 103 103 ALA CB C 18.990 0.75 1 1013 103 103 ALA HB H 1.360 0.03 1 1014 103 103 ALA C C 177.420 0.75 1 1015 104 104 ARG N N 122.760 0.5 1 1016 104 104 ARG H H 8.220 0.03 1 1017 104 104 ARG CA C 55.390 0.75 1 1018 104 104 ARG HA H 4.310 0.03 1 1019 104 104 ARG CB C 30.490 0.75 1 1020 104 104 ARG HB3 H 1.850 0.03 2 1021 104 104 ARG HB2 H 1.740 0.03 2 1022 104 104 ARG CG C 27.050 0.75 1 1023 104 104 ARG HG3 H 1.620 0.03 1 1024 104 104 ARG HG2 H 1.620 0.03 1 1025 104 104 ARG CD C 42.940 0.75 1 1026 104 104 ARG HD3 H 3.170 0.03 1 1027 104 104 ARG HD2 H 3.170 0.03 1 1028 104 104 ARG C C 174.920 0.75 1 1029 105 105 ALA N N 132.980 0.5 1 1030 105 105 ALA H H 7.940 0.03 1 1031 105 105 ALA CA C 53.250 0.75 1 1032 105 105 ALA HA H 4.090 0.03 1 1033 105 105 ALA CB C 19.990 0.75 1 1034 105 105 ALA HB H 1.290 0.03 1 1035 105 105 ALA C C 182.300 0.75 1 stop_ save_