data_4989 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution Structure of B.subtilis Acyl Carrier Protein ; _BMRB_accession_number 4989 _BMRB_flat_file_name bmr4989.str _Entry_type original _Submission_date 2001-04-16 _Accession_date 2001-04-17 _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 Xu G.-Y. . . 2 Tam A. . . 3 Lin L. . . 4 Hixon J. . . 5 Fritz C. C. . 6 Powers R. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 449 "13C chemical shifts" 259 "15N chemical shifts" 84 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-04-03 original author . stop_ _Original_release_date 2002-04-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Solution Structure of B.subtilis Acyl Carrier Protein' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21416009 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Xu G.-Y. . . 2 Tam A. . . 3 Lin L. . . 4 Hixon J. . . 5 Fritz C. C. . 6 Powers R. . . stop_ _Journal_abbreviation Structure _Journal_volume 9 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 277 _Page_last 287 _Year 2001 _Details . loop_ _Keyword apo-ACP holo-ACP ACPS 'Fatty Acid Biosynthesis' "4' phosphopantetheine prosthetic group" stop_ save_ ################################## # Molecular system description # ################################## save_system_ACP _Saveframe_category molecular_system _Mol_system_name 'B. subtilis ACYL CARRIER PROTEIN' _Abbreviation_common ACP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ACYL CARRIER PROTEIN' $ACYL_CARRIER_PROTEIN stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ACYL_CARRIER_PROTEIN _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'B. subtilis ACYL CARRIER PROTEIN' _Abbreviation_common ACP _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 81 _Mol_residue_sequence ; GPLGSADTLERVTKIIVDRL GVDEADVKLEASFKEDLGAD SLDVVELVMELEDEFDMEIS DEDAEKIATVGDAVNYIQNQ Q ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 PRO 3 LEU 4 GLY 5 SER 6 ALA 7 ASP 8 THR 9 LEU 10 GLU 11 ARG 12 VAL 13 THR 14 LYS 15 ILE 16 ILE 17 VAL 18 ASP 19 ARG 20 LEU 21 GLY 22 VAL 23 ASP 24 GLU 25 ALA 26 ASP 27 VAL 28 LYS 29 LEU 30 GLU 31 ALA 32 SER 33 PHE 34 LYS 35 GLU 36 ASP 37 LEU 38 GLY 39 ALA 40 ASP 41 SER 42 LEU 43 ASP 44 VAL 45 VAL 46 GLU 47 LEU 48 VAL 49 MET 50 GLU 51 LEU 52 GLU 53 ASP 54 GLU 55 PHE 56 ASP 57 MET 58 GLU 59 ILE 60 SER 61 ASP 62 GLU 63 ASP 64 ALA 65 GLU 66 LYS 67 ILE 68 ALA 69 THR 70 VAL 71 GLY 72 ASP 73 ALA 74 VAL 75 ASN 76 TYR 77 ILE 78 GLN 79 ASN 80 GLN 81 GLN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1F80 "Holo-(Acyl Carrier Protein) Synthase In Complex With Holo- (Acyl Carrier Protein)" 100.00 81 98.77 98.77 2.71e-46 PDB 1HY8 "Solution Structure Of B. Subtilis Acyl Carrier Protein" 92.59 76 100.00 100.00 7.18e-42 PDB 2X2B "Crystal Structure Of Malonyl-Acp (Acyl Carrier Protein) From Bacillus Subtilis" 96.30 78 98.72 98.72 2.31e-43 DBJ BAA10975 "ORF2 [Bacillus subtilis]" 93.83 77 100.00 100.00 1.10e-42 DBJ BAI85218 "acyl carrier protein [Bacillus subtilis subsp. natto BEST195]" 93.83 77 100.00 100.00 1.10e-42 DBJ BAM52238 "acyl carrier protein [Synechocystis sp. PCC 6803]" 93.83 77 100.00 100.00 1.10e-42 DBJ BAM57814 "acyl carrier protein [Bacillus subtilis BEST7003]" 93.83 77 100.00 100.00 1.10e-42 DBJ GAK80569 "acyl carrier protein [Bacillus subtilis Miyagi-4]" 93.83 77 100.00 100.00 1.10e-42 EMBL CAB13465 "acyl carrier protein [Bacillus subtilis subsp. subtilis str. 168]" 93.83 77 100.00 100.00 1.10e-42 EMBL CBI42790 "acyl carrier protein [Bacillus amyloliquefaciens DSM 7]" 93.83 77 100.00 100.00 1.10e-42 EMBL CCF05080 "Acyl carrier protein ACP [Bacillus amyloliquefaciens subsp. plantarum CAU B946]" 93.83 77 100.00 100.00 1.10e-42 EMBL CCG49565 "Acyl carrier protein ACP [Bacillus amyloliquefaciens subsp. plantarum YAU B9601-Y2]" 93.83 77 100.00 100.00 1.10e-42 EMBL CCP21556 "acyl carrier protein [Bacillus amyloliquefaciens subsp. plantarum UCMB5036]" 93.83 77 100.00 100.00 1.10e-42 GB ABS73938 "AcpA [Bacillus amyloliquefaciens subsp. plantarum str. FZB42]" 93.83 77 100.00 100.00 1.10e-42 GB ADM37686 "acyl carrier protein [Bacillus subtilis subsp. spizizenii str. W23]" 93.83 77 100.00 100.00 1.10e-42 GB ADP32105 "acyl carrier protein [Bacillus atrophaeus 1942]" 93.83 77 98.68 98.68 7.07e-42 GB ADV96618 "acyl carrier protein [Bacillus subtilis BSn5]" 93.83 77 100.00 100.00 1.10e-42 GB AEB24004 "acyl carrier protein [Bacillus amyloliquefaciens TA208]" 93.83 77 100.00 100.00 1.10e-42 REF NP_389474 "acyl carrier protein [Bacillus subtilis subsp. subtilis str. 168]" 93.83 77 100.00 100.00 1.10e-42 REF WP_003154310 "MULTISPECIES: acyl carrier protein [Bacillales]" 93.83 77 100.00 100.00 1.10e-42 REF WP_003328976 "MULTISPECIES: acyl carrier protein [Bacillus subtilis group]" 93.83 77 98.68 98.68 7.07e-42 REF YP_001421169 "acyl carrier protein [Bacillus amyloliquefaciens subsp. plantarum str. FZB42]" 93.83 77 100.00 100.00 1.10e-42 REF YP_003865995 "acyl carrier protein [Bacillus subtilis subsp. spizizenii str. W23]" 93.83 77 100.00 100.00 1.10e-42 SP A7Z4L2 "RecName: Full=Acyl carrier protein; Short=ACP [Bacillus amyloliquefaciens subsp. plantarum str. FZB42]" 93.83 77 100.00 100.00 1.10e-42 SP P80643 "RecName: Full=Acyl carrier protein; Short=ACP [Bacillus subtilis subsp. subtilis str. 168]" 93.83 77 100.00 100.00 1.10e-42 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ACYL_CARRIER_PROTEIN 'Bacillus subtilis' 1423 Eubacteria . Bacillus subtilis 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 $ACYL_CARRIER_PROTEIN 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'The sample is the mixture of U-15N/13C labeled holo- (60%)and apo-ACP (40%)' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $ACYL_CARRIER_PROTEIN 1 mM '[U-15N; U-13C]' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 98.0 loop_ _Task 'structure solution' stop_ _Details 'Badger, J., Kumar, R.A., Yip, P.' save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version '1.8, 2000' loop_ _Task processing stop_ _Details 'Delaglio, F.' save_ save_pipp _Saveframe_category software _Name pipp _Version '4.2.2, 1998' loop_ _Task 'data analysis' stop_ _Details 'Garrett, D.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UNITYplus _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0 n/a temperature 298 0 K 'ionic strength' 3.4 . mM pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_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 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_ref_1 _Mol_system_component_name 'ACYL CARRIER PROTEIN' _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 GLY CA C 43.5300 . . 2 . 1 GLY HA2 H 4.0400 . . 3 . 1 GLY HA3 H 4.0400 . . 4 . 2 PRO CA C 63.2000 . . 5 . 2 PRO CB C 32.3700 . . 6 . 2 PRO CG C 27.0500 . . 7 . 2 PRO CD C 49.6300 . . 8 . 2 PRO HA H 4.5300 . . 9 . 2 PRO HB2 H 2.3178 . . 10 . 2 PRO HB3 H 2.3178 . . 11 . 2 PRO HG2 H 2.0400 . . 12 . 2 PRO HG3 H 2.0400 . . 13 . 2 PRO HD2 H 3.6200 . . 14 . 2 PRO HD3 H 3.6200 . . 15 . 3 LEU H H 8.6200 . . 16 . 3 LEU N N 122.6100 . . 17 . 3 LEU CA C 55.2500 . . 18 . 3 LEU CB C 42.3400 . . 19 . 3 LEU CG C 27.0700 . . 20 . 3 LEU CD1 C 25.0500 . . 21 . 3 LEU CD2 C 23.5000 . . 22 . 3 LEU HA H 4.4363 . . 23 . 3 LEU HD1 H 0.9565 . . 24 . 3 LEU HD2 H 0.9565 . . 25 . 3 LEU HB2 H 1.7309 . . 26 . 3 LEU HB3 H 1.7309 . . 27 . 3 LEU HG H 1.6317 . . 28 . 4 GLY H H 8.5200 . . 29 . 4 GLY N N 110.2000 . . 30 . 4 GLY CA C 45.2500 . . 31 . 4 GLY HA2 H 4.0770 . . 32 . 4 GLY HA3 H 4.0770 . . 33 . 5 SER H H 8.4000 . . 34 . 5 SER N N 116.8400 . . 35 . 5 SER CA C 59.4000 . . 36 . 5 SER CB C 63.3460 . . 37 . 5 SER HA H 4.3522 . . 38 . 5 SER HB2 H 3.9247 . . 39 . 5 SER HB3 H 3.9247 . . 40 . 6 ALA H H 8.4600 . . 41 . 6 ALA N N 126.0900 . . 42 . 6 ALA CA C 53.7885 . . 43 . 6 ALA CB C 18.8033 . . 44 . 6 ALA HA H 4.3491 . . 45 . 6 ALA HB H 1.4860 . . 46 . 7 ASP H H 8.2500 . . 47 . 7 ASP N N 119.9000 . . 48 . 7 ASP CA C 55.4285 . . 49 . 7 ASP CB C 41.4332 . . 50 . 7 ASP HA H 4.6202 . . 51 . 7 ASP HB2 H 2.8817 . . 52 . 7 ASP HB3 H 2.7724 . . 53 . 8 THR H H 8.1500 . . 54 . 8 THR N N 117.0800 . . 55 . 8 THR CA C 67.7352 . . 56 . 8 THR CB C 68.210 . . 57 . 8 THR CG2 C 23.3870 . . 58 . 8 THR HA H 3.9529 . . 59 . 8 THR HB H 4.1633 . . 60 . 8 THR HG2 H 1.1180 . . 61 . 9 LEU H H 8.5374 . . 62 . 9 LEU N N 121.3981 . . 63 . 9 LEU CA C 58.4930 . . 64 . 9 LEU CB C 40.7890 . . 65 . 9 LEU CG C 27.2552 . . 66 . 9 LEU CD1 C 22.6690 . . 67 . 9 LEU CD2 C 25.5125 . . 68 . 9 LEU HA H 3.9866 . . 69 . 9 LEU HB2 H 1.9854 . . 70 . 9 LEU HB3 H 1.5600 . . 71 . 9 LEU HG H 1.5509 . . 72 . 9 LEU HD1 H 0.7700 . . 73 . 9 LEU HD2 H 0.9600 . . 74 . 10 GLU H H 8.7000 . . 75 . 10 GLU N N 124.1800 . . 76 . 10 GLU CA C 60.2906 . . 77 . 10 GLU CB C 29.3541 . . 78 . 10 GLU CG C 36.2910 . . 79 . 10 GLU HA H 4.0247 . . 80 . 10 GLU HB2 H 2.1800 . . 81 . 10 GLU HB3 H 2.2300 . . 82 . 10 GLU HG2 H 2.3100 . . 83 . 10 GLU HG3 H 2.4200 . . 84 . 11 ARG H H 8.1200 . . 85 . 11 ARG N N 119.7400 . . 86 . 11 ARG CA C 59.7246 . . 87 . 11 ARG CB C 32.5726 . . 88 . 11 ARG CG C 27.2190 . . 89 . 11 ARG CD C 44.6792 . . 90 . 11 ARG HA H 4.0843 . . 91 . 11 ARG HB2 H 2.0789 . . 92 . 11 ARG HB3 H 1.9608 . . 93 . 11 ARG HG2 H 1.7141 . . 94 . 11 ARG HG3 H 1.9800 . . 95 . 11 ARG HD2 H 3.3015 . . 96 . 11 ARG HD3 H 3.0257 . . 97 . 12 VAL H H 8.7900 . . 98 . 12 VAL N N 119.2200 . . 99 . 12 VAL CA C 66.9383 . . 100 . 12 VAL CB C 31.9191 . . 101 . 12 VAL CG1 C 24.3348 . . 102 . 12 VAL CG2 C 21.4790 . . 103 . 12 VAL HA H 3.6607 . . 104 . 12 VAL HB H 2.1885 . . 105 . 12 VAL HG1 H 1.1000 . . 106 . 12 VAL HG2 H 0.9500 . . 107 . 13 THR H H 8.6500 . . 108 . 13 THR N N 116.8600 . . 109 . 13 THR CA C 68.4050 . . 110 . 13 THR CB C 68.5100 . . 111 . 13 THR CG2 C 20.4200 . . 112 . 13 THR HA H 3.7100 . . 113 . 13 THR HB H 4.4300 . . 114 . 13 THR HG2 H 1.2508 . . 115 . 14 LYS H H 7.6039 . . 116 . 14 LYS N N 120.3407 . . 117 . 14 LYS CA C 59.6130 . . 118 . 14 LYS CB C 32.1445 . . 119 . 14 LYS CG C 24.7739 . . 120 . 14 LYS CD C 28.9239 . . 121 . 14 LYS CE C 42.2060 . . 122 . 14 LYS HA H 3.9581 . . 123 . 14 LYS HB2 H 1.9560 . . 124 . 14 LYS HB3 H 1.9560 . . 125 . 14 LYS HG2 H 1.4525 . . 126 . 14 LYS HG3 H 1.5800 . . 127 . 14 LYS HD2 H 1.6565 . . 128 . 14 LYS HD3 H 1.6565 . . 129 . 14 LYS HE2 H 3.0046 . . 130 . 14 LYS HE3 H 3.0046 . . 131 . 15 ILE H H 7.1800 . . 132 . 15 ILE N N 118.4300 . . 133 . 15 ILE CA C 64.5400 . . 134 . 15 ILE CB C 38.4500 . . 135 . 15 ILE CG1 C 29.5214 . . 136 . 15 ILE CG2 C 17.1736 . . 137 . 15 ILE CD1 C 14.1182 . . 138 . 15 ILE HA H 3.8757 . . 139 . 15 ILE HB H 2.0135 . . 140 . 15 ILE HG12 H 1.8000 . . 141 . 15 ILE HG13 H 1.3100 . . 142 . 15 ILE HG2 H 0.8900 . . 143 . 15 ILE HD1 H 0.8800 . . 144 . 16 ILE H H 8.1627 . . 145 . 16 ILE N N 120.1274 . . 146 . 16 ILE CA C 66.1900 . . 147 . 16 ILE CB C 38.0900 . . 148 . 16 ILE CG1 C 30.0393 . . 149 . 16 ILE CG2 C 18.6231 . . 150 . 16 ILE CD1 C 16.6970 . . 151 . 16 ILE HA H 3.4970 . . 152 . 16 ILE HB H 2.0413 . . 153 . 16 ILE HG12 H 2.0900 . . 154 . 16 ILE HG13 H 1.0400 . . 155 . 16 ILE HG2 H 0.9100 . . 156 . 16 ILE HD1 H 0.9155 . . 157 . 17 VAL H H 8.7870 . . 158 . 17 VAL N N 120.9983 . . 159 . 17 VAL CA C 66.8968 . . 160 . 17 VAL CB C 32.0926 . . 161 . 17 VAL CG1 C 20.5609 . . 162 . 17 VAL CG2 C 22.5660 . . 163 . 17 VAL HA H 3.5299 . . 164 . 17 VAL HB H 2.1953 . . 165 . 17 VAL HG1 H 1.0865 . . 166 . 17 VAL HG2 H 0.9876 . . 167 . 18 ASP H H 8.1600 . . 168 . 18 ASP N N 119.4400 . . 169 . 18 ASP CA C 57.1600 . . 170 . 18 ASP CB C 40.8400 . . 171 . 18 ASP HA H 4.4033 . . 172 . 18 ASP HB2 H 2.8353 . . 173 . 18 ASP HB3 H 2.6861 . . 174 . 19 ARG H H 8.3200 . . 175 . 19 ARG N N 116.4000 . . 176 . 19 ARG CA C 57.4000 . . 177 . 19 ARG CB C 30.4258 . . 178 . 19 ARG CG C 26.6580 . . 179 . 19 ARG CD C 42.0691 . . 180 . 19 ARG HA H 4.3434 . . 181 . 19 ARG HB2 H 2.0615 . . 182 . 19 ARG HB3 H 1.8969 . . 183 . 19 ARG HG2 H 1.5687 . . 184 . 19 ARG HG3 H 1.6605 . . 185 . 19 ARG HD2 H 3.2000 . . 186 . 19 ARG HD3 H 3.3000 . . 187 . 20 LEU H H 8.7400 . . 188 . 20 LEU N N 114.5500 . . 189 . 20 LEU CA C 54.6100 . . 190 . 20 LEU CB C 42.3000 . . 191 . 20 LEU CG C 26.7210 . . 192 . 20 LEU CD1 C 22.2021 . . 193 . 20 LEU CD2 C 22.2021 . . 194 . 20 LEU HA H 4.6180 . . 195 . 20 LEU HB2 H 1.9902 . . 196 . 20 LEU HB3 H 1.7580 . . 197 . 20 LEU HD1 H 0.8227 . . 198 . 20 LEU HD2 H 0.9935 . . 199 . 21 GLY H H 8.0400 . . 200 . 21 GLY N N 108.9600 . . 201 . 21 GLY CA C 47.0084 . . 202 . 21 GLY HA2 H 4.0624 . . 203 . 21 GLY HA3 H 3.9487 . . 204 . 22 VAL H H 6.4000 . . 205 . 22 VAL N N 109.4500 . . 206 . 22 VAL CA C 58.8975 . . 207 . 22 VAL CB C 32.6744 . . 208 . 22 VAL CG1 C 19.4285 . . 209 . 22 VAL CG2 C 22.4646 . . 210 . 22 VAL HA H 4.4320 . . 211 . 22 VAL HB H 2.4872 . . 212 . 22 VAL HG1 H 0.6950 . . 213 . 22 VAL HG2 H 0.9700 . . 214 . 23 ASP H H 8.5635 . . 215 . 23 ASP N N 121.1378 . . 216 . 23 ASP CA C 53.9500 . . 217 . 23 ASP CB C 42.5500 . . 218 . 23 ASP HA H 4.5844 . . 219 . 23 ASP HB2 H 2.5682 . . 220 . 23 ASP HB3 H 2.6697 . . 221 . 24 GLU H H 8.9600 . . 222 . 24 GLU N N 125.6200 . . 223 . 24 GLU CA C 60.2381 . . 224 . 24 GLU CB C 29.2443 . . 225 . 24 GLU CG C 36.2356 . . 226 . 24 GLU HA H 3.6353 . . 227 . 24 GLU HB2 H 2.0245 . . 228 . 24 GLU HB3 H 1.9800 . . 229 . 24 GLU HG2 H 2.2585 . . 230 . 24 GLU HG3 H 2.2585 . . 231 . 25 ALA H H 8.7104 . . 232 . 25 ALA N N 120.2743 . . 233 . 25 ALA CA C 53.9615 . . 234 . 25 ALA CB C 18.5750 . . 235 . 25 ALA HA H 4.0690 . . 236 . 25 ALA HB H 1.3773 . . 237 . 26 ASP H H 7.7552 . . 238 . 26 ASP N N 114.9379 . . 239 . 26 ASP CA C 54.8256 . . 240 . 26 ASP CB C 40.9824 . . 241 . 26 ASP HA H 4.5786 . . 242 . 26 ASP HB2 H 2.6869 . . 243 . 26 ASP HB3 H 2.6869 . . 244 . 27 VAL H H 7.6000 . . 245 . 27 VAL N N 121.5400 . . 246 . 27 VAL CA C 63.8477 . . 247 . 27 VAL CB C 29.2863 . . 248 . 27 VAL CG1 C 24.0204 . . 249 . 27 VAL CG2 C 22.3278 . . 250 . 27 VAL HA H 3.5340 . . 251 . 27 VAL HB H 2.3698 . . 252 . 27 VAL HG1 H 0.9300 . . 253 . 27 VAL HG2 H 0.8800 . . 254 . 28 LYS H H 6.7100 . . 255 . 28 LYS N N 125.2300 . . 256 . 28 LYS CA C 53.4424 . . 257 . 28 LYS CB C 35.2857 . . 258 . 28 LYS CG C 24.5975 . . 259 . 28 LYS CD C 29.0238 . . 260 . 28 LYS CE C 42.2352 . . 261 . 28 LYS HA H 4.6457 . . 262 . 28 LYS HB2 H 2.1148 . . 263 . 28 LYS HB3 H 1.4828 . . 264 . 28 LYS HG2 H 1.3000 . . 265 . 28 LYS HG3 H 1.3800 . . 266 . 28 LYS HD2 H 1.7100 . . 267 . 28 LYS HD3 H 1.7100 . . 268 . 28 LYS HE2 H 3.0251 . . 269 . 28 LYS HE3 H 3.0251 . . 270 . 29 LEU H H 8.8133 . . 271 . 29 LEU N N 121.3330 . . 272 . 29 LEU CA C 58.0785 . . 273 . 29 LEU CB C 41.2714 . . 274 . 29 LEU CG C 26.9730 . . 275 . 29 LEU CD1 C 23.0091 . . 276 . 29 LEU CD2 C 25.2563 . . 277 . 29 LEU HA H 3.6800 . . 278 . 29 LEU HB2 H 1.8000 . . 279 . 29 LEU HB3 H 1.4200 . . 280 . 29 LEU HG H 1.8300 . . 281 . 29 LEU HD1 H 0.8500 . . 282 . 29 LEU HD2 H 0.9600 . . 283 . 30 GLU H H 9.0400 . . 284 . 30 GLU N N 114.2600 . . 285 . 30 GLU CA C 56.7800 . . 286 . 30 GLU CB C 28.8120 . . 287 . 30 GLU CG C 36.0469 . . 288 . 30 GLU HA H 4.1964 . . 289 . 30 GLU HB2 H 2.0000 . . 290 . 30 GLU HB3 H 2.0800 . . 291 . 30 GLU HG2 H 2.2500 . . 292 . 30 GLU HG3 H 2.2500 . . 293 . 31 ALA H H 7.6900 . . 294 . 31 ALA N N 123.1000 . . 295 . 31 ALA CA C 52.2181 . . 296 . 31 ALA CB C 18.7904 . . 297 . 31 ALA HA H 4.3491 . . 298 . 31 ALA HB H 1.4044 . . 299 . 32 SER H H 10.0100 . . 300 . 32 SER N N 118.5700 . . 301 . 32 SER CA C 55.9287 . . 302 . 32 SER CB C 63.5943 . . 303 . 32 SER HA H 4.7630 . . 304 . 32 SER HB2 H 3.9156 . . 305 . 32 SER HB3 H 4.0782 . . 306 . 33 PHE H H 8.2233 . . 307 . 33 PHE N N 125.9693 . . 308 . 33 PHE CA C 61.9737 . . 309 . 33 PHE CB C 38.2329 . . 310 . 33 PHE CD1 C 130.7500 . . 311 . 33 PHE CE1 C 127.7200 . . 312 . 33 PHE HA H 4.1367 . . 313 . 33 PHE HB2 H 2.8759 . . 314 . 33 PHE HB3 H 2.9881 . . 315 . 33 PHE HD1 H 6.9700 . . 316 . 33 PHE HD2 H 6.9700 . . 317 . 33 PHE HE1 H 6.7800 . . 318 . 33 PHE HE2 H 6.7800 . . 319 . 34 LYS H H 8.7200 . . 320 . 34 LYS N N 115.8600 . . 321 . 34 LYS CA C 58.4806 . . 322 . 34 LYS CB C 33.0113 . . 323 . 34 LYS CG C 25.1185 . . 324 . 34 LYS CD C 29.4451 . . 325 . 34 LYS CE C 41.9547 . . 326 . 34 LYS HA H 4.7572 . . 327 . 34 LYS HB2 H 1.8320 . . 328 . 34 LYS HB3 H 1.8320 . . 329 . 34 LYS HG2 H 1.5489 . . 330 . 34 LYS HG3 H 1.3000 . . 331 . 34 LYS HD2 H 1.7400 . . 332 . 34 LYS HD3 H 1.7400 . . 333 . 34 LYS HE2 H 2.9542 . . 334 . 34 LYS HE3 H 2.9542 . . 335 . 35 GLU H H 8.1800 . . 336 . 35 GLU N N 115.5900 . . 337 . 35 GLU CA C 59.3800 . . 338 . 35 GLU CB C 29.7610 . . 339 . 35 GLU CG C 36.8294 . . 340 . 35 GLU HA H 4.2049 . . 341 . 35 GLU HB2 H 2.0786 . . 342 . 35 GLU HB3 H 1.9079 . . 343 . 35 GLU HG2 H 2.3278 . . 344 . 35 GLU HG3 H 2.3278 . . 345 . 36 ASP H H 7.8700 . . 346 . 36 ASP N N 114.8400 . . 347 . 36 ASP CA C 56.2510 . . 348 . 36 ASP CB C 42.0997 . . 349 . 36 ASP HA H 4.9900 . . 350 . 36 ASP HB2 H 2.7740 . . 351 . 36 ASP HB3 H 3.1416 . . 352 . 37 LEU H H 7.3700 . . 353 . 37 LEU N N 115.5900 . . 354 . 37 LEU CA C 54.3359 . . 355 . 37 LEU CB C 41.4647 . . 356 . 37 LEU CG C 26.4600 . . 357 . 37 LEU CD1 C 22.4000 . . 358 . 37 LEU CD2 C 26.2900 . . 359 . 37 LEU HA H 4.5850 . . 360 . 37 LEU HB2 H 2.3229 . . 361 . 37 LEU HB3 H 1.7106 . . 362 . 37 LEU HG H 1.5200 . . 363 . 37 LEU HD1 H 0.7450 . . 364 . 37 LEU HD2 H 0.6900 . . 365 . 38 GLY H H 7.2600 . . 366 . 38 GLY N N 105.8600 . . 367 . 38 GLY CA C 46.4980 . . 368 . 38 GLY HA2 H 3.8674 . . 369 . 38 GLY HA3 H 3.9528 . . 370 . 39 ALA H H 8.4600 . . 371 . 39 ALA N N 123.3500 . . 372 . 39 ALA CA C 51.4851 . . 373 . 39 ALA CB C 20.5511 . . 374 . 39 ALA HA H 4.5962 . . 375 . 39 ALA HB H 1.2508 . . 376 . 40 ASP H H 9.2400 . . 377 . 40 ASP N N 122.5100 . . 378 . 40 ASP CA C 52.1307 . . 379 . 40 ASP CB C 41.8246 . . 380 . 40 ASP HA H 4.9020 . . 381 . 40 ASP HB2 H 3.1981 . . 382 . 40 ASP HB3 H 2.8247 . . 383 . 41 SER H H 8.7600 . . 384 . 41 SER N N 112.7300 . . 385 . 41 SER CA C 60.9389 . . 386 . 41 SER CB C 65.5145 . . 387 . 41 SER HA H 4.1796 . . 388 . 41 SER HB2 H 4.1280 . . 389 . 41 SER HB3 H 4.1280 . . 390 . 42 LEU H H 7.9900 . . 391 . 42 LEU N N 124.4100 . . 392 . 42 LEU CA C 57.6143 . . 393 . 42 LEU CB C 40.8533 . . 394 . 42 LEU CG C 27.1738 . . 395 . 42 LEU CD1 C 24.1673 . . 396 . 42 LEU CD2 C 24.3700 . . 397 . 42 LEU HA H 4.1987 . . 398 . 42 LEU HB2 H 1.7690 . . 399 . 42 LEU HB3 H 1.7690 . . 400 . 42 LEU HG H 1.6600 . . 401 . 42 LEU HD1 H 0.9407 . . 402 . 42 LEU HD2 H 0.9000 . . 403 . 43 ASP H H 8.3455 . . 404 . 43 ASP N N 119.9904 . . 405 . 43 ASP CA C 57.4600 . . 406 . 43 ASP CB C 41.6700 . . 407 . 43 ASP HA H 4.3200 . . 408 . 43 ASP HB2 H 2.3300 . . 409 . 43 ASP HB3 H 3.1500 . . 410 . 44 VAL H H 7.8100 . . 411 . 44 VAL N N 117.5100 . . 412 . 44 VAL CA C 67.3524 . . 413 . 44 VAL CB C 31.1756 . . 414 . 44 VAL CG1 C 23.1085 . . 415 . 44 VAL CG2 C 21.4147 . . 416 . 44 VAL HA H 3.3027 . . 417 . 44 VAL HB H 2.1159 . . 418 . 44 VAL HG1 H 0.8653 . . 419 . 44 VAL HG2 H 0.8100 . . 420 . 45 VAL H H 7.4000 . . 421 . 45 VAL N N 119.8000 . . 422 . 45 VAL CA C 66.5814 . . 423 . 45 VAL CB C 31.7889 . . 424 . 45 VAL CG1 C 22.9102 . . 425 . 45 VAL CG2 C 21.1243 . . 426 . 45 VAL HA H 3.5869 . . 427 . 45 VAL HB H 2.2681 . . 428 . 45 VAL HG1 H 1.1219 . . 429 . 45 VAL HG2 H 1.0167 . . 430 . 46 GLU H H 7.9600 . . 431 . 46 GLU N N 118.7100 . . 432 . 46 GLU CA C 59.3822 . . 433 . 46 GLU CB C 28.8964 . . 434 . 46 GLU CG C 36.3286 . . 435 . 46 GLU HA H 4.0812 . . 436 . 46 GLU HB2 H 2.0800 . . 437 . 46 GLU HB3 H 2.0800 . . 438 . 46 GLU HG2 H 2.5189 . . 439 . 46 GLU HG3 H 2.2700 . . 440 . 47 LEU H H 8.5000 . . 441 . 47 LEU N N 121.9700 . . 442 . 47 LEU CA C 58.3224 . . 443 . 47 LEU CB C 41.9720 . . 444 . 47 LEU CG C 27.0072 . . 445 . 47 LEU CD1 C 25.3810 . . 446 . 47 LEU CD2 C 25.3810 . . 447 . 47 LEU HA H 3.8922 . . 448 . 47 LEU HB2 H 1.6805 . . 449 . 47 LEU HB3 H 1.5149 . . 450 . 47 LEU HG H 1.5600 . . 451 . 47 LEU HD1 H 0.5404 . . 452 . 47 LEU HD2 H 0.4900 . . 453 . 48 VAL H H 8.4621 . . 454 . 48 VAL N N 119.9763 . . 455 . 48 VAL CA C 67.7089 . . 456 . 48 VAL CB C 30.9822 . . 457 . 48 VAL CG1 C 23.1656 . . 458 . 48 VAL CG2 C 21.7771 . . 459 . 48 VAL HA H 3.3715 . . 460 . 48 VAL HB H 2.2236 . . 461 . 48 VAL HG1 H 0.9200 . . 462 . 48 VAL HG2 H 0.8200 . . 463 . 49 MET H H 7.7613 . . 464 . 49 MET N N 118.3709 . . 465 . 49 MET CA C 59.2503 . . 466 . 49 MET CB C 32.8491 . . 467 . 49 MET CG C 32.3337 . . 468 . 49 MET CE C 16.9800 . . 469 . 49 MET HA H 4.4569 . . 470 . 49 MET HB2 H 2.2610 . . 471 . 49 MET HB3 H 2.2610 . . 472 . 49 MET HG2 H 2.8200 . . 473 . 49 MET HG3 H 2.6100 . . 474 . 49 MET HE H 2.1200 . . 475 . 50 GLU H H 8.0700 . . 476 . 50 GLU N N 120.0500 . . 477 . 50 GLU CA C 59.6273 . . 478 . 50 GLU CB C 29.1870 . . 479 . 50 GLU CG C 35.9909 . . 480 . 50 GLU HA H 4.2785 . . 481 . 50 GLU HB2 H 2.2545 . . 482 . 50 GLU HB3 H 2.1605 . . 483 . 50 GLU HG2 H 2.4245 . . 484 . 50 GLU HG3 H 2.5200 . . 485 . 51 LEU H H 8.6500 . . 486 . 51 LEU N N 121.3800 . . 487 . 51 LEU CA C 58.4227 . . 488 . 51 LEU CB C 41.3227 . . 489 . 51 LEU CG C 26.2046 . . 490 . 51 LEU CD1 C 24.1527 . . 491 . 51 LEU CD2 C 24.9277 . . 492 . 51 LEU HA H 4.2027 . . 493 . 51 LEU HB2 H 2.3200 . . 494 . 51 LEU HB3 H 1.3600 . . 495 . 51 LEU HG H 0.9800 . . 496 . 51 LEU HD1 H 1.0264 . . 497 . 51 LEU HD2 H 0.7700 . . 498 . 52 GLU H H 8.5500 . . 499 . 52 GLU N N 119.0600 . . 500 . 52 GLU CA C 60.1410 . . 501 . 52 GLU CB C 30.1427 . . 502 . 52 GLU CG C 37.1136 . . 503 . 52 GLU HA H 3.9667 . . 504 . 52 GLU HB2 H 2.2300 . . 505 . 52 GLU HB3 H 2.5800 . . 506 . 52 GLU HG2 H 2.8000 . . 507 . 52 GLU HG3 H 2.2100 . . 508 . 53 ASP H H 7.6284 . . 509 . 53 ASP N N 117.4887 . . 510 . 53 ASP CA C 56.5762 . . 511 . 53 ASP CB C 41.2471 . . 512 . 53 ASP HA H 4.5681 . . 513 . 53 ASP HB2 H 2.8267 . . 514 . 53 ASP HB3 H 2.8267 . . 515 . 54 GLU H H 8.4700 . . 516 . 54 GLU N N 120.4500 . . 517 . 54 GLU CA C 58.1193 . . 518 . 54 GLU CB C 29.4366 . . 519 . 54 GLU CG C 34.6928 . . 520 . 54 GLU HA H 4.0107 . . 521 . 54 GLU HB2 H 2.1200 . . 522 . 54 GLU HB3 H 1.7049 . . 523 . 54 GLU HG2 H 1.8900 . . 524 . 54 GLU HG3 H 0.9928 . . 525 . 55 PHE H H 8.0600 . . 526 . 55 PHE N N 112.7100 . . 527 . 55 PHE CA C 58.4982 . . 528 . 55 PHE CB C 38.7773 . . 529 . 55 PHE CD1 C 132.4400 . . 530 . 55 PHE CE1 C 130.1300 . . 531 . 55 PHE HA H 4.4932 . . 532 . 55 PHE HB2 H 3.4188 . . 533 . 55 PHE HB3 H 2.7690 . . 534 . 55 PHE HD1 H 7.5800 . . 535 . 55 PHE HD2 H 7.5800 . . 536 . 55 PHE HE1 H 7.1800 . . 537 . 55 PHE HE2 H 7.1800 . . 538 . 56 ASP H H 7.7864 . . 539 . 56 ASP N N 121.7356 . . 540 . 56 ASP CA C 54.8934 . . 541 . 56 ASP CB C 38.9500 . . 542 . 56 ASP HA H 4.4690 . . 543 . 56 ASP HB2 H 3.1510 . . 544 . 56 ASP HB3 H 2.5310 . . 545 . 57 MET H H 8.4500 . . 546 . 57 MET N N 115.6500 . . 547 . 57 MET CA C 54.0768 . . 548 . 57 MET CB C 36.3670 . . 549 . 57 MET CG C 31.2293 . . 550 . 57 MET CE C 17.4600 . . 551 . 57 MET HA H 4.8938 . . 552 . 57 MET HB2 H 2.0900 . . 553 . 57 MET HB3 H 1.9500 . . 554 . 57 MET HG2 H 2.4842 . . 555 . 57 MET HG3 H 2.3380 . . 556 . 57 MET HE H 2.0000 . . 557 . 58 GLU H H 8.3645 . . 558 . 58 GLU N N 120.2770 . . 559 . 58 GLU CA C 55.1955 . . 560 . 58 GLU CB C 31.5860 . . 561 . 58 GLU CG C 36.1564 . . 562 . 58 GLU HA H 4.6500 . . 563 . 58 GLU HB2 H 2.1193 . . 564 . 58 GLU HB3 H 2.2074 . . 565 . 58 GLU HG2 H 1.9013 . . 566 . 58 GLU HG3 H 1.9013 . . 567 . 59 ILE H H 9.5600 . . 568 . 59 ILE N N 127.8600 . . 569 . 59 ILE CA C 60.7349 . . 570 . 59 ILE CB C 38.5086 . . 571 . 59 ILE CG1 C 27.4838 . . 572 . 59 ILE CG2 C 16.0969 . . 573 . 59 ILE CD1 C 12.5051 . . 574 . 59 ILE HA H 4.2891 . . 575 . 59 ILE HB H 1.5583 . . 576 . 59 ILE HG12 H 1.5000 . . 577 . 59 ILE HG13 H 0.9600 . . 578 . 59 ILE HG2 H 0.5700 . . 579 . 59 ILE HD1 H 0.5830 . . 580 . 60 SER H H 9.0500 . . 581 . 60 SER N N 125.4900 . . 582 . 60 SER CA C 57.9456 . . 583 . 60 SER CB C 64.4839 . . 584 . 60 SER HA H 4.4000 . . 585 . 60 SER HB2 H 4.3000 . . 586 . 60 SER HB3 H 4.0900 . . 587 . 61 ASP H H 8.8600 . . 588 . 61 ASP N N 122.7500 . . 589 . 61 ASP CA C 57.7270 . . 590 . 61 ASP CB C 39.7000 . . 591 . 61 ASP HA H 4.3084 . . 592 . 61 ASP HB2 H 2.7206 . . 593 . 61 ASP HB3 H 2.6110 . . 594 . 62 GLU H H 8.5800 . . 595 . 62 GLU N N 118.5700 . . 596 . 62 GLU CA C 59.3360 . . 597 . 62 GLU CB C 29.2075 . . 598 . 62 GLU CG C 36.5248 . . 599 . 62 GLU HA H 4.0198 . . 600 . 62 GLU HB2 H 1.9606 . . 601 . 62 GLU HB3 H 1.9606 . . 602 . 62 GLU HG2 H 2.3009 . . 603 . 62 GLU HG3 H 2.3009 . . 604 . 63 ASP H H 7.6649 . . 605 . 63 ASP N N 120.2465 . . 606 . 63 ASP CA C 56.6600 . . 607 . 63 ASP CB C 40.0926 . . 608 . 63 ASP HA H 4.4435 . . 609 . 63 ASP HB2 H 2.7022 . . 610 . 63 ASP HB3 H 2.2713 . . 611 . 64 ALA H H 8.6172 . . 612 . 64 ALA N N 123.3045 . . 613 . 64 ALA CA C 54.9506 . . 614 . 64 ALA CB C 18.2274 . . 615 . 64 ALA HA H 3.6719 . . 616 . 64 ALA HB H 1.3933 . . 617 . 65 GLU H H 7.4900 . . 618 . 65 GLU N N 115.3200 . . 619 . 65 GLU CA C 57.9956 . . 620 . 65 GLU CB C 29.6806 . . 621 . 65 GLU CG C 36.0403 . . 622 . 65 GLU HA H 4.0250 . . 623 . 65 GLU HB2 H 2.0862 . . 624 . 65 GLU HB3 H 2.0862 . . 625 . 65 GLU HG2 H 2.3482 . . 626 . 65 GLU HG3 H 2.4254 . . 627 . 66 LYS H H 7.1900 . . 628 . 66 LYS N N 115.6200 . . 629 . 66 LYS CA C 55.8446 . . 630 . 66 LYS CB C 32.7785 . . 631 . 66 LYS CG C 25.1594 . . 632 . 66 LYS CD C 29.3103 . . 633 . 66 LYS CE C 42.2884 . . 634 . 66 LYS HA H 4.3166 . . 635 . 66 LYS HB2 H 2.1055 . . 636 . 66 LYS HB3 H 1.8855 . . 637 . 66 LYS HG2 H 1.6802 . . 638 . 66 LYS HG3 H 1.7000 . . 639 . 66 LYS HD2 H 1.4872 . . 640 . 66 LYS HD3 H 1.4872 . . 641 . 66 LYS HE2 H 3.0407 . . 642 . 66 LYS HE3 H 3.0407 . . 643 . 67 ILE H H 7.3100 . . 644 . 67 ILE N N 121.6100 . . 645 . 67 ILE CA C 61.8550 . . 646 . 67 ILE CB C 36.7340 . . 647 . 67 ILE CG1 C 27.5037 . . 648 . 67 ILE CG2 C 17.3997 . . 649 . 67 ILE CD1 C 12.2600 . . 650 . 67 ILE HA H 3.9587 . . 651 . 67 ILE HB H 1.9630 . . 652 . 67 ILE HG12 H 1.6966 . . 653 . 67 ILE HG13 H 0.7500 . . 654 . 67 ILE HG2 H 0.8826 . . 655 . 67 ILE HD1 H 0.4184 . . 656 . 68 ALA H H 9.0700 . . 657 . 68 ALA N N 130.8100 . . 658 . 68 ALA CA C 52.8011 . . 659 . 68 ALA CB C 21.5856 . . 660 . 68 ALA HA H 4.8220 . . 661 . 68 ALA HB H 1.6000 . . 662 . 69 THR H H 8.4300 . . 663 . 69 THR N N 110.2500 . . 664 . 69 THR CA C 58.1844 . . 665 . 69 THR CB C 73.5000 . . 666 . 69 THR CG2 C 21.2065 . . 667 . 69 THR HA H 5.0110 . . 668 . 69 THR HB H 4.2780 . . 669 . 69 THR HG2 H 1.0070 . . 670 . 70 VAL H H 7.9468 . . 671 . 70 VAL N N 120.6196 . . 672 . 70 VAL CA C 66.6823 . . 673 . 70 VAL CB C 31.4222 . . 674 . 70 VAL CG1 C 23.1125 . . 675 . 70 VAL CG2 C 20.3657 . . 676 . 70 VAL HA H 3.2987 . . 677 . 70 VAL HB H 2.4422 . . 678 . 70 VAL HG1 H 0.7921 . . 679 . 70 VAL HG2 H 0.5854 . . 680 . 71 GLY H H 9.3800 . . 681 . 71 GLY N N 107.7600 . . 682 . 71 GLY CA C 47.4230 . . 683 . 71 GLY HA2 H 3.6930 . . 684 . 71 GLY HA3 H 3.8946 . . 685 . 72 ASP H H 8.2200 . . 686 . 72 ASP N N 122.1100 . . 687 . 72 ASP CA C 57.2803 . . 688 . 72 ASP CB C 41.8680 . . 689 . 72 ASP HA H 4.5089 . . 690 . 72 ASP HB2 H 2.8687 . . 691 . 72 ASP HB3 H 3.2668 . . 692 . 73 ALA H H 7.7817 . . 693 . 73 ALA N N 122.8589 . . 694 . 73 ALA CA C 55.4620 . . 695 . 73 ALA CB C 16.7754 . . 696 . 73 ALA HA H 4.0200 . . 697 . 73 ALA HB H 1.5700 . . 698 . 74 VAL H H 8.3000 . . 699 . 74 VAL N N 117.1200 . . 700 . 74 VAL CA C 66.8134 . . 701 . 74 VAL CB C 31.8068 . . 702 . 74 VAL CG1 C 23.1962 . . 703 . 74 VAL CG2 C 20.8322 . . 704 . 74 VAL HA H 3.2930 . . 705 . 74 VAL HB H 2.0770 . . 706 . 74 VAL HG1 H 0.9200 . . 707 . 74 VAL HG2 H 0.8955 . . 708 . 75 ASN H H 8.7100 . . 709 . 75 ASN N N 117.2600 . . 710 . 75 ASN CA C 55.9496 . . 711 . 75 ASN CB C 38.0840 . . 712 . 75 ASN HA H 4.3744 . . 713 . 75 ASN HB2 H 2.7562 . . 714 . 75 ASN HB3 H 2.8747 . . 715 . 75 ASN ND2 N 111.9500 . . 716 . 75 ASN HD21 H 7.5600 . . 717 . 75 ASN HD22 H 6.8100 . . 718 . 76 TYR H H 7.9519 . . 719 . 76 TYR N N 120.2556 . . 720 . 76 TYR CA C 62.1013 . . 721 . 76 TYR CB C 38.1900 . . 722 . 76 TYR CD1 C 132.3000 . . 723 . 76 TYR CE1 C 118.2000 . . 724 . 76 TYR HA H 4.0052 . . 725 . 76 TYR HB2 H 3.0828 . . 726 . 76 TYR HB3 H 3.0828 . . 727 . 76 TYR HD1 H 6.9200 . . 728 . 76 TYR HD2 H 6.9200 . . 729 . 76 TYR HE1 H 6.7300 . . 730 . 76 TYR HE2 H 6.7300 . . 731 . 77 ILE H H 7.8600 . . 732 . 77 ILE N N 119.0300 . . 733 . 77 ILE CA C 64.5374 . . 734 . 77 ILE CB C 38.1800 . . 735 . 77 ILE CG1 C 28.8876 . . 736 . 77 ILE CG2 C 17.4149 . . 737 . 77 ILE CD1 C 14.0131 . . 738 . 77 ILE HA H 3.3770 . . 739 . 77 ILE HB H 1.5290 . . 740 . 77 ILE HG12 H 1.5300 . . 741 . 77 ILE HG13 H 0.8300 . . 742 . 77 ILE HG2 H 0.1800 . . 743 . 77 ILE HD1 H 0.2000 . . 744 . 78 GLN H H 8.3600 . . 745 . 78 GLN N N 117.0800 . . 746 . 78 GLN CA C 58.0560 . . 747 . 78 GLN CB C 29.0270 . . 748 . 78 GLN CG C 34.8047 . . 749 . 78 GLN HA H 4.0290 . . 750 . 78 GLN HB2 H 2.1300 . . 751 . 78 GLN HB3 H 2.0800 . . 752 . 78 GLN HG2 H 2.5300 . . 753 . 78 GLN HG3 H 2.3500 . . 754 . 78 GLN NE2 N 110.4100 . . 755 . 78 GLN HE21 H 7.3200 . . 756 . 78 GLN HE22 H 6.8200 . . 757 . 79 ASN H H 7.7704 . . 758 . 79 ASN N N 116.2448 . . 759 . 79 ASN CA C 53.9296 . . 760 . 79 ASN CB C 38.7038 . . 761 . 79 ASN HA H 4.6838 . . 762 . 79 ASN HB2 H 2.7695 . . 763 . 79 ASN HB3 H 2.7695 . . 764 . 79 ASN ND2 N 112.3800 . . 765 . 79 ASN HD21 H 7.5000 . . 766 . 79 ASN HD22 H 6.8100 . . 767 . 80 GLN H H 7.5300 . . 768 . 80 GLN N N 118.6100 . . 769 . 80 GLN CA C 55.3476 . . 770 . 80 GLN CB C 28.9238 . . 771 . 80 GLN CG C 33.4702 . . 772 . 80 GLN HA H 4.2820 . . 773 . 80 GLN HB2 H 2.2197 . . 774 . 80 GLN HB3 H 1.8918 . . 775 . 80 GLN HG2 H 2.3252 . . 776 . 80 GLN HG3 H 2.2300 . . 777 . 80 GLN NE2 N 113.3500 . . 778 . 80 GLN HE21 H 7.0800 . . 779 . 80 GLN HE22 H 6.6900 . . 780 . 81 GLN H H 7.6300 . . 781 . 81 GLN N N 125.3500 . . 782 . 81 GLN CA C 57.3795 . . 783 . 81 GLN CB C 30.2137 . . 784 . 81 GLN CG C 34.2900 . . 785 . 81 GLN HA H 4.1300 . . 786 . 81 GLN HB2 H 2.1700 . . 787 . 81 GLN HB3 H 1.9900 . . 788 . 81 GLN HG2 H 2.3900 . . 789 . 81 GLN HG3 H 2.3900 . . 790 . 81 GLN NE2 N 111.8800 . . 791 . 81 GLN HE21 H 7.4200 . . 792 . 81 GLN HE22 H 6.8400 . . stop_ save_