data_4023 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C and 15N Resonance Assignments for the Z Domain of Staphylococcal Protein A at pH* 6.5 and Temperature of 30 deg. C ; _BMRB_accession_number 4023 _BMRB_flat_file_name bmr4023.str _Entry_type update _Submission_date 1997-01-15 _Accession_date 1997-04-25 _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 Tashiro Mitsuru . . 2 Tejero Roberto . . 3 Zimmerman Diane E. . 4 Celda Bernardo . . 5 Nilsson Bjorn . . 6 Montelione Gaetano T. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 445 "13C chemical shifts" 329 "15N chemical shifts" 82 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-02-16 reformat BMRB 'Format updated to NMR-STAR version 2.1' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; High Resolution Solution NMR Structure of the Z Domain of Staphylococcal Protein A ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9325113 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Tashiro Mitsuru . . 2 Tejero Roberto . . 3 Zimmerman Diane E. . 4 Celda Bernardo . . 5 Nilsson Bjorn . . 6 Montelione Gaetano T. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 272 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 573 _Page_last 590 _Year 1997 _Details . save_ ################################## # Molecular system description # ################################## save_system_staphylococcal_protein_A_Z_domain _Saveframe_category molecular_system _Mol_system_name 'staphylococcal protein A Z domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'staphylococcal protein A Z domain' $staphylococcal_protein_A_Z_domain 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_staphylococcal_protein_A_Z_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'staphylococcal protein A Z domain' _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 71 _Mol_residue_sequence ; KAIFVLNAQHDEAVDNKFNK EQQNAFYEILHLPNLNEEQR NAFIQSLKDDPSQSANLLAE AKKLNDAQAPK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -13 LYS 2 -12 ALA 3 -11 ILE 4 -10 PHE 5 -9 VAL 6 -8 LEU 7 -7 ASN 8 -6 ALA 9 -5 GLN 10 -4 HIS 11 -3 ASP 12 -2 GLU 13 -1 ALA 14 1 VAL 15 2 ASP 16 3 ASN 17 4 LYS 18 5 PHE 19 6 ASN 20 7 LYS 21 8 GLU 22 9 GLN 23 10 GLN 24 11 ASN 25 12 ALA 26 13 PHE 27 14 TYR 28 15 GLU 29 16 ILE 30 17 LEU 31 18 HIS 32 19 LEU 33 20 PRO 34 21 ASN 35 22 LEU 36 23 ASN 37 24 GLU 38 25 GLU 39 26 GLN 40 27 ARG 41 28 ASN 42 29 ALA 43 30 PHE 44 31 ILE 45 32 GLN 46 33 SER 47 34 LEU 48 35 LYS 49 36 ASP 50 37 ASP 51 38 PRO 52 39 SER 53 40 GLN 54 41 SER 55 42 ALA 56 43 ASN 57 44 LEU 58 45 LEU 59 46 ALA 60 47 GLU 61 48 ALA 62 49 LYS 63 50 LYS 64 51 LEU 65 52 ASN 66 53 ASP 67 54 ALA 68 55 GLN 69 56 ALA 70 57 PRO 71 58 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-09-16 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 19043 Z_domain 81.69 58 100.00 100.00 6.80e-31 PDB 1H0T "An Affibody In Complex With A Target Protein: Structure And Coupled Folding" 81.69 58 100.00 100.00 6.80e-31 PDB 1LP1 "Protein Z In Complex With An In Vitro Selected Affibody" 81.69 58 100.00 100.00 6.80e-31 PDB 1Q2N "Refined Solution Nmr Structure Of The Z Domain Of Staphylococcal Protein A" 81.69 58 100.00 100.00 6.80e-31 PDB 2M5A "Protein A Binding By An Engineered Affibody Molecule" 81.69 58 100.00 100.00 6.80e-31 PDB 2SPZ "Staphylococcal Protein A, Z-Domain, Nmr, 10 Structures" 81.69 58 100.00 100.00 6.80e-31 PDB 4GWP "Structure Of The Mediator Head Module From S. Cerevisiae" 81.69 407 98.28 98.28 2.13e-28 PDB 4GWQ "Structure Of The Mediator Head Module From S. Cerevisiae In Complex With The Carboxy-Terminal Domain (Ctd) Of Rna Polymerase Ii" 81.69 407 98.28 98.28 2.13e-28 DBJ BAC76617 "protein A doublet [Cloning vector pscFvCA-E8VHd]" 90.14 68 100.00 100.00 2.35e-35 DBJ BAC76619 "protein A doublet [Cloning vector pFCAH9-E8d]" 81.69 126 100.00 100.00 4.87e-30 DBJ BAL27690 "FLAG-TEV cut site-protein A tag [Cloning vector pCtFLATAki-kanMX6]" 90.14 86 100.00 100.00 2.96e-35 DBJ BAL27694 "Spac323.08-FLATA [Targeting vector pCtFLATAki-Pspac323.08-SalI-spac323.08(+)-kanMX6T]" 90.14 298 100.00 100.00 2.32e-34 DBJ BAL27697 "HA-TEV cut site-protein A tag [Schizosaccharomyces pombe expression vector pFOX1-CHATA]" 90.14 87 100.00 100.00 3.90e-35 EMBL CAA49867 "staphylococcal protein A [synthetic construct]" 80.28 88 98.25 98.25 8.70e-30 EMBL CAA65431 "protein A [synthetic construct]" 81.69 318 100.00 100.00 1.10e-28 GB AAA72944 "bifunctional fusion protein, partial [synthetic construct]" 80.28 308 98.25 98.25 1.24e-30 GB AAB00807 "ZZ:beta-Gal' IgG-binding fusion protein [Cloning vector pKP497]" 81.69 215 100.00 100.00 1.06e-29 GB AAR10383 "C-terminal TAP tag [synthetic construct]" 81.69 194 100.00 100.00 2.74e-30 GB AAR10384 "N-terminal TAP tag [synthetic construct]" 81.69 199 100.00 100.00 2.39e-30 GB AAR10385 "N-terminal TAP tag [synthetic construct]" 81.69 200 100.00 100.00 1.74e-30 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $staphylococcal_protein_A_Z_domain 'S. aureus' 1280 Bacteria . Staphylococcus aureus 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 $staphylococcal_protein_A_Z_domain . . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $staphylococcal_protein_A_Z_domain . mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 303 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.25144953 $entry_citation $entry_citation DSS H 1 'methyl protons' ppm 0.00 . . . . . . $entry_citation $entry_citation DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $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_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name 'staphylococcal protein A Z domain' _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 LYS C C 174.5 . 1 2 . 1 LYS CA C 56.00 . 1 3 . 1 LYS HA H 4.35 . 1 4 . 1 LYS CB C 33.00 . 1 5 . 1 LYS HB2 H 1.75 . 2 6 . 1 LYS HB3 H 1.78 . 2 7 . 1 LYS CG C 24.4 . 1 8 . 1 LYS HG2 H 1.44 . 1 9 . 1 LYS HG3 H 1.44 . 1 10 . 1 LYS CD C 28.7 . 1 11 . 1 LYS HD2 H 1.68 . 1 12 . 1 LYS HD3 H 1.68 . 1 13 . 1 LYS CE C 41.5 . 1 14 . 1 LYS HE2 H 2.98 . 1 15 . 1 LYS HE3 H 2.98 . 1 16 . 2 ALA N N 126.2 . 1 17 . 2 ALA H H 8.4 . 1 18 . 2 ALA C C 175.9 . 1 19 . 2 ALA CA C 51.8 . 1 20 . 2 ALA HA H 4.3 . 1 21 . 2 ALA CB C 19.00 . 1 22 . 2 ALA HB H 1.3 . 1 23 . 3 ILE N N 119.7 . 1 24 . 3 ILE H H 8.02 . 1 25 . 3 ILE C C 174.4 . 1 26 . 3 ILE CA C 60.7 . 1 27 . 3 ILE HA H 4.12 . 1 28 . 3 ILE CB C 38.6 . 1 29 . 3 ILE HB H 1.75 . 1 30 . 3 ILE CG1 C 26.8 . 1 31 . 3 ILE CG2 C 17.2 . 1 32 . 3 ILE HG12 H 1.1 . 2 33 . 3 ILE HG13 H 1.36 . 2 34 . 3 ILE HG2 H 0.8 . 1 35 . 3 ILE CD1 C 12.6 . 1 36 . 3 ILE HD1 H 0.8 . 1 37 . 4 PHE N N 124.00 . 1 38 . 4 PHE H H 8.22 . 1 39 . 4 PHE C C 173.9 . 1 40 . 4 PHE CA C 57.1 . 1 41 . 4 PHE HA H 4.68 . 1 42 . 4 PHE CB C 39.5 . 1 43 . 4 PHE CD1 C 130.9 . 1 44 . 4 PHE CD2 C 130.9 . 1 45 . 4 PHE HD1 H 7.18 . 1 46 . 4 PHE HD2 H 7.18 . 1 47 . 5 VAL N N 122.8 . 1 48 . 5 VAL H H 7.99 . 1 49 . 5 VAL C C 174.2 . 1 50 . 5 VAL CA C 61.5 . 1 51 . 5 VAL HA H 4.04 . 1 52 . 5 VAL CB C 32.00 . 1 53 . 5 VAL HB H 1.97 . 1 54 . 5 VAL CG1 C 20.2 . 2 55 . 5 VAL CG2 C 20.7 . 2 56 . 5 VAL HG1 H 0.86 . 1 57 . 5 VAL HG2 H 0.86 . 1 58 . 6 LEU N N 125.8 . 1 59 . 6 LEU H H 8.23 . 1 60 . 6 LEU C C 174.5 . 1 61 . 6 LEU CA C 55.00 . 1 62 . 6 LEU HA H 4.25 . 1 63 . 6 LEU CB C 41.9 . 1 64 . 6 LEU HB2 H 1.97 . 1 65 . 6 LEU HB3 H 1.97 . 1 66 . 6 LEU CG C 26.7 . 1 67 . 6 LEU HG H 1.57 . 1 68 . 6 LEU CD1 C 23.3 . 2 69 . 6 LEU CD2 C 24.8 . 2 70 . 6 LEU HD1 H 0.86 . 2 71 . 6 LEU HD2 H 0.91 . 2 72 . 7 ASN N N 119.1 . 1 73 . 7 ASN H H 8.42 . 1 74 . 7 ASN C C 173.7 . 1 75 . 7 ASN CA C 52.8 . 1 76 . 7 ASN HA H 4.66 . 1 77 . 7 ASN CB C 38.5 . 1 78 . 7 ASN HB2 H 2.76 . 2 79 . 7 ASN HB3 H 2.82 . 2 80 . 7 ASN CG C 176.00 . 1 81 . 7 ASN ND2 N 112.6 . 1 82 . 7 ASN HD21 H 6.91 . 2 83 . 7 ASN HD22 H 7.61 . 2 84 . 8 ALA N N 123.7 . 1 85 . 8 ALA H H 8.2 . 1 86 . 8 ALA C C 176.9 . 1 87 . 8 ALA CA C 52.1 . 1 88 . 8 ALA HA H 4.26 . 1 89 . 8 ALA CB C 18.6 . 1 90 . 8 ALA HB H 1.35 . 1 91 . 9 GLN N N 118.7 . 1 92 . 9 GLN H H 8.24 . 1 93 . 9 GLN C C 173.2 . 1 94 . 9 GLN CA C 55.5 . 1 95 . 9 GLN HA H 4.27 . 1 96 . 9 GLN CB C 28.7 . 1 97 . 9 GLN HB2 H 1.97 . 2 98 . 9 GLN HB3 H 2.06 . 2 99 . 9 GLN CG C 33.1 . 1 100 . 9 GLN HG2 H 2.32 . 2 101 . 9 GLN HG3 H 2.49 . 2 102 . 9 GLN CD C 179.3 . 1 103 . 9 GLN HE21 H 6.82 . 2 104 . 9 GLN HE22 H 7.55 . 2 105 . 10 HIS N N 119.1 . 1 106 . 10 HIS H H 8.37 . 1 107 . 10 HIS C C 176.4 . 1 108 . 10 HIS CA C 55.2 . 1 109 . 10 HIS HA H 4.67 . 1 110 . 10 HIS CB C 29.5 . 1 111 . 10 HIS HB2 H 3.13 . 2 112 . 10 HIS HB3 H 3.21 . 2 113 . 10 HIS HD2 H 8.3 . 1 114 . 10 HIS HE1 H 7.17 . 1 115 . 11 ASP N N 122.00 . 1 116 . 11 ASP H H 8.35 . 1 117 . 11 ASP C C 174.9 . 1 118 . 11 ASP CA C 54.00 . 1 119 . 11 ASP HA H 4.61 . 1 120 . 11 ASP CB C 41.1 . 1 121 . 11 ASP HB2 H 2.59 . 2 122 . 11 ASP HB3 H 2.67 . 2 123 . 12 GLU N N 122.00 . 1 124 . 12 GLU H H 8.52 . 1 125 . 12 GLU C C 175.2 . 1 126 . 12 GLU CA C 56.7 . 1 127 . 12 GLU HA H 4.22 . 1 128 . 12 GLU CB C 29.9 . 1 129 . 12 GLU HB2 H 1.96 . 2 130 . 12 GLU HB3 H 2.05 . 2 131 . 12 GLU CG C 36.1 . 1 132 . 12 GLU HG2 H 2.27 . 1 133 . 12 GLU HG3 H 2.27 . 1 134 . 13 ALA N N 123.9 . 1 135 . 13 ALA H H 8.28 . 1 136 . 13 ALA C C 176.9 . 1 137 . 13 ALA CA C 52.2 . 1 138 . 13 ALA HA H 4.26 . 1 139 . 13 ALA CB C 18.4 . 1 140 . 13 ALA HB H 1.35 . 1 141 . 14 VAL N N 118.2 . 1 142 . 14 VAL H H 7.84 . 1 143 . 14 VAL C C 174.8 . 1 144 . 14 VAL CA C 62.2 . 1 145 . 14 VAL HA H 3.78 . 1 146 . 14 VAL CB C 32.1 . 1 147 . 14 VAL HB H 1.95 . 1 148 . 14 VAL CG1 C 17.1 . 2 149 . 14 VAL CG2 C 20.1 . 2 150 . 14 VAL HG1 H 0.74 . 2 151 . 14 VAL HG2 H 0.76 . 2 152 . 15 ASP N N 121.9 . 1 153 . 15 ASP H H 8.03 . 1 154 . 15 ASP C C 175.2 . 1 155 . 15 ASP CA C 54.4 . 1 156 . 15 ASP HA H 4.42 . 1 157 . 15 ASP CB C 39.7 . 1 158 . 15 ASP HB2 H 2.46 . 2 159 . 15 ASP HB3 H 2.47 . 2 160 . 16 ASN N N 118.8 . 1 161 . 16 ASN H H 8.13 . 1 162 . 16 ASN C C 174.2 . 1 163 . 16 ASN CA C 53.2 . 1 164 . 16 ASN HA H 4.57 . 1 165 . 16 ASN CB C 38.4 . 1 166 . 16 ASN HB2 H 2.56 . 2 167 . 16 ASN HB3 H 2.59 . 2 168 . 16 ASN CG C 175.7 . 1 169 . 16 ASN HD21 H 7.46 . 2 170 . 16 ASN HD22 H 6.82 . 2 171 . 16 ASN ND2 N 112.5 . 1 172 . 17 LYS N N 119.5 . 1 173 . 17 LYS H H 8.21 . 1 174 . 17 LYS C C 175.5 . 1 175 . 17 LYS CA C 56.8 . 1 176 . 17 LYS HA H 4.21 . 1 177 . 17 LYS CB C 32.2 . 1 178 . 17 LYS HB2 H 1.61 . 2 179 . 17 LYS HB3 H 1.74 . 2 180 . 17 LYS CG C 24.00 . 1 181 . 17 LYS HG2 H 1.24 . 1 182 . 17 LYS HG3 H 1.24 . 1 183 . 17 LYS CD C 28.3 . 1 184 . 17 LYS HD2 H 1.69 . 1 185 . 17 LYS HD3 H 1.69 . 1 186 . 17 LYS CE C 41.3 . 1 187 . 17 LYS HE2 H 2.9 . 1 188 . 17 LYS HE3 H 2.9 . 1 189 . 18 PHE N N 118.7 . 1 190 . 18 PHE H H 7.89 . 1 191 . 18 PHE C C 175.6 . 1 192 . 18 PHE CA C 54.8 . 1 193 . 18 PHE HA H 5.07 . 1 194 . 18 PHE CB C 39.5 . 1 195 . 18 PHE HB2 H 3.13 . 2 196 . 18 PHE HB3 H 3.41 . 2 197 . 18 PHE CD1 C 122.3 . 1 198 . 18 PHE CD2 C 122.3 . 1 199 . 18 PHE HD1 H 7.07 . 1 200 . 18 PHE HD2 H 7.07 . 1 201 . 18 PHE CE1 C 127.1 . 1 202 . 18 PHE CE2 C 127.1 . 1 203 . 18 PHE HE1 H 6.95 . 1 204 . 18 PHE HE2 H 6.95 . 1 205 . 18 PHE CZ C 128.8 . 1 206 . 18 PHE HZ H 7.25 . 1 207 . 19 ASN N N 120.6 . 1 208 . 19 ASN H H 8.47 . 1 209 . 19 ASN C C 174.6 . 1 210 . 19 ASN CA C 51.3 . 1 211 . 19 ASN HA H 4.78 . 1 212 . 19 ASN CB C 37.8 . 1 213 . 19 ASN HB2 H 2.95 . 2 214 . 19 ASN HB3 H 3.35 . 2 215 . 19 ASN CG C 174.3 . 1 216 . 19 ASN HD21 H 7.44 . 2 217 . 19 ASN HD22 H 6.87 . 2 218 . 19 ASN ND2 N 110.2 . 1 219 . 20 LYS N N 118.7 . 1 220 . 20 LYS H H 8.35 . 1 221 . 20 LYS C C 177.2 . 1 222 . 20 LYS CA C 59.5 . 1 223 . 20 LYS HA H 3.99 . 1 224 . 20 LYS CB C 31.6 . 1 225 . 20 LYS HB2 H 1.82 . 2 226 . 20 LYS HB3 H 1.88 . 2 227 . 20 LYS CG C 24.3 . 1 228 . 20 LYS HG2 H 1.45 . 1 229 . 20 LYS HG3 H 1.45 . 1 230 . 20 LYS CD C 28.3 . 1 231 . 20 LYS HD2 H 1.72 . 1 232 . 20 LYS HD3 H 1.72 . 1 233 . 20 LYS CE C 41.5 . 1 234 . 20 LYS HE2 H 3.02 . 1 235 . 20 LYS HE3 H 3.02 . 1 236 . 21 GLU N N 119.6 . 1 237 . 21 GLU H H 8.25 . 1 238 . 21 GLU C C 178.9 . 1 239 . 21 GLU CA C 59.4 . 1 240 . 21 GLU HA H 4.11 . 1 241 . 21 GLU CB C 28.7 . 1 242 . 21 GLU HB2 H 1.79 . 2 243 . 21 GLU HB3 H 2.1 . 2 244 . 21 GLU CG C 36.3 . 1 245 . 21 GLU HG2 H 2.32 . 1 246 . 21 GLU HG3 H 2.32 . 1 247 . 22 GLN N N 121.6 . 1 248 . 22 GLN H H 8.54 . 1 249 . 22 GLN C C 176.5 . 1 250 . 22 GLN CA C 57.3 . 1 251 . 22 GLN HA H 3.88 . 1 252 . 22 GLN CB C 28.6 . 1 253 . 22 GLN HB2 H 1.54 . 2 254 . 22 GLN HB3 H 2.25 . 2 255 . 22 GLN CG C 33.2 . 1 256 . 22 GLN HG2 H 2.49 . 1 257 . 22 GLN HG3 H 2.49 . 1 258 . 22 GLN CD C 178.6 . 1 259 . 22 GLN HE21 H 6.96 . 2 260 . 22 GLN HE22 H 7.26 . 2 261 . 22 GLN NE2 N 110.7 . 1 262 . 23 GLN N N 119.00 . 1 263 . 23 GLN H H 8.77 . 1 264 . 23 GLN C C 177.00 . 1 265 . 23 GLN CA C 58.3 . 1 266 . 23 GLN HA H 3.93 . 1 267 . 23 GLN CB C 28.00 . 1 268 . 23 GLN HB2 H 2.18 . 2 269 . 23 GLN HB3 H 2.57 . 2 270 . 23 GLN CG C 33.8 . 1 271 . 23 GLN HG2 H 2.42 . 1 272 . 23 GLN HG3 H 2.42 . 1 273 . 23 GLN CD C 178.5 . 1 274 . 23 GLN HE21 H 6.89 . 2 275 . 23 GLN HE22 H 7.27 . 2 276 . 23 GLN NE2 N 111.5 . 1 277 . 24 ASN N N 117.6 . 1 278 . 24 ASN H H 8.34 . 1 279 . 24 ASN C C 176.2 . 1 280 . 24 ASN CA C 56.00 . 1 281 . 24 ASN HA H 4.62 . 1 282 . 24 ASN CB C 37.7 . 1 283 . 24 ASN HB2 H 2.92 . 1 284 . 24 ASN HB3 H 2.92 . 1 285 . 24 ASN CG C 175.00 . 1 286 . 24 ASN HD21 H 7.73 . 2 287 . 24 ASN HD22 H 7.05 . 2 288 . 24 ASN ND2 N 112.3 . 1 289 . 25 ALA N N 122.3 . 1 290 . 25 ALA H H 7.91 . 1 291 . 25 ALA C C 176.9 . 1 292 . 25 ALA CA C 55.1 . 1 293 . 25 ALA HA H 4.1 . 1 294 . 25 ALA CB C 17.8 . 1 295 . 25 ALA HB H 1.47 . 1 296 . 26 PHE N N 118.1 . 1 297 . 26 PHE H H 8.15 . 1 298 . 26 PHE C C 174.9 . 1 299 . 26 PHE CA C 60.8 . 1 300 . 26 PHE HA H 3.81 . 1 301 . 26 PHE CB C 38.7 . 1 302 . 26 PHE HB2 H 2.95 . 2 303 . 26 PHE HB3 H 3.32 . 2 304 . 26 PHE CD1 C 129.6 . 1 305 . 26 PHE CD2 C 129.6 . 1 306 . 26 PHE HD1 H 6.92 . 1 307 . 26 PHE HD2 H 6.92 . 1 308 . 26 PHE CE1 C 129.00 . 1 309 . 26 PHE CE2 C 129.00 . 1 310 . 26 PHE HE1 H 7.06 . 1 311 . 26 PHE HE2 H 7.06 . 1 312 . 26 PHE CZ C 128.8 . 1 313 . 26 PHE HZ H 7.25 . 1 314 . 27 TYR N N 116.7 . 1 315 . 27 TYR H H 8.19 . 1 316 . 27 TYR C C 177.5 . 1 317 . 27 TYR CA C 61.9 . 1 318 . 27 TYR HA H 3.95 . 1 319 . 27 TYR CB C 37.8 . 1 320 . 27 TYR HB2 H 3.16 . 1 321 . 27 TYR HB3 H 3.16 . 1 322 . 27 TYR CD1 C 130.5 . 1 323 . 27 TYR CD2 C 130.5 . 1 324 . 27 TYR HD1 H 7.17 . 1 325 . 27 TYR HD2 H 7.17 . 1 326 . 27 TYR CE1 C 116.5 . 1 327 . 27 TYR CE2 C 116.5 . 1 328 . 27 TYR HE1 H 6.78 . 1 329 . 27 TYR HE2 H 6.78 . 1 330 . 28 GLU N N 119.1 . 1 331 . 28 GLU H H 8.53 . 1 332 . 28 GLU C C 179.2 . 1 333 . 28 GLU CA C 59.6 . 1 334 . 28 GLU HA H 4.03 . 1 335 . 28 GLU CB C 29.2 . 1 336 . 28 GLU HB2 H 1.96 . 2 337 . 28 GLU HB3 H 2.15 . 2 338 . 28 GLU CG C 36.5 . 1 339 . 28 GLU HG2 H 2.42 . 1 340 . 28 GLU HG3 H 2.42 . 1 341 . 29 ILE N N 119.5 . 1 342 . 29 ILE H H 8.42 . 1 343 . 29 ILE C C 176.7 . 1 344 . 29 ILE CA C 65.4 . 1 345 . 29 ILE HA H 3.39 . 1 346 . 29 ILE CB C 37.1 . 1 347 . 29 ILE HB H 1.78 . 1 348 . 29 ILE CG1 C 29.9 . 1 349 . 29 ILE CG2 C 17.6 . 1 350 . 29 ILE HG12 H 1.78 . 2 351 . 29 ILE HG13 H 1.88 . 2 352 . 29 ILE HG2 H 0.75 . 1 353 . 29 ILE CD1 C 12.5 . 1 354 . 29 ILE HD1 H 0.53 . 1 355 . 30 LEU N N 117.7 . 1 356 . 30 LEU H H 7.9 . 1 357 . 30 LEU C C 175.8 . 1 358 . 30 LEU CA C 56.8 . 1 359 . 30 LEU HA H 3.68 . 1 360 . 30 LEU CB C 41.5 . 1 361 . 30 LEU HB2 H 1.13 . 2 362 . 30 LEU HB3 H 1.45 . 2 363 . 30 LEU CG C 26.2 . 1 364 . 30 LEU HG H 1.32 . 1 365 . 30 LEU CD1 C 23.2 . 2 366 . 30 LEU CD2 C 24.5 . 2 367 . 30 LEU HD1 H 0.53 . 2 368 . 30 LEU HD2 H 0.63 . 2 369 . 31 HIS N N 111.8 . 1 370 . 31 HIS H H 7.23 . 1 371 . 31 HIS C C 173.6 . 1 372 . 31 HIS CA C 55.3 . 1 373 . 31 HIS HA H 4.52 . 1 374 . 31 HIS CB C 29.1 . 1 375 . 31 HIS HB2 H 2.84 . 2 376 . 31 HIS HB3 H 3.45 . 2 377 . 31 HIS HD2 H 7.09 . 1 378 . 31 HIS HE1 H 8.21 . 1 379 . 32 LEU N N 124.5 . 1 380 . 32 LEU H H 7.26 . 1 381 . 32 LEU C C 176.5 . 1 382 . 32 LEU CA C 52.9 . 1 383 . 32 LEU HA H 4.49 . 1 384 . 32 LEU CB C 40.2 . 1 385 . 32 LEU HB2 H 1.38 . 2 386 . 32 LEU HB3 H 1.75 . 2 387 . 32 LEU CG C 24.9 . 1 388 . 32 LEU HG H 2.23 . 1 389 . 32 LEU CD1 C 23.1 . 2 390 . 32 LEU CD2 C 27.00 . 2 391 . 32 LEU HD1 H 0.86 . 2 392 . 32 LEU HD2 H 0.68 . 2 393 . 33 PRO C C 176.9 . 1 394 . 33 PRO CA C 64.8 . 1 395 . 33 PRO HA H 4.42 . 1 396 . 33 PRO CB C 32.5 . 1 397 . 33 PRO HB2 H 2.33 . 1 398 . 33 PRO HB3 H 2.33 . 1 399 . 33 PRO CG C 26.8 . 1 400 . 33 PRO HG2 H 2.17 . 1 401 . 33 PRO HG3 H 2.17 . 1 402 . 33 PRO CD C 51.00 . 1 403 . 33 PRO HD2 H 3.82 . 2 404 . 33 PRO HD3 H 4.08 . 2 405 . 34 ASN N N 113.8 . 1 406 . 34 ASN H H 8.91 . 1 407 . 34 ASN C C 175.1 . 1 408 . 34 ASN CA C 52.1 . 1 409 . 34 ASN HA H 5.03 . 1 410 . 34 ASN CB C 38.3 . 1 411 . 34 ASN HB2 H 2.9 . 1 412 . 34 ASN HB3 H 2.9 . 1 413 . 34 ASN CG C 176.1 . 1 414 . 34 ASN HD21 H 6.99 . 2 415 . 34 ASN HD22 H 7.42 . 2 416 . 34 ASN ND2 N 114.5 . 1 417 . 35 LEU N N 117.4 . 1 418 . 35 LEU H H 6.53 . 1 419 . 35 LEU C C 175.3 . 1 420 . 35 LEU CA C 54.2 . 1 421 . 35 LEU HA H 4.43 . 1 422 . 35 LEU CB C 42.8 . 1 423 . 35 LEU HB2 H 1.62 . 2 424 . 35 LEU HB3 H 1.69 . 2 425 . 35 LEU CG C 24.4 . 1 426 . 35 LEU HG H 1.69 . 1 427 . 35 LEU CD1 C 22.1 . 2 428 . 35 LEU CD2 C 26.3 . 2 429 . 35 LEU HD1 H 0.88 . 2 430 . 35 LEU HD2 H 0.96 . 2 431 . 36 ASN N N 119.1 . 1 432 . 36 ASN H H 8.56 . 1 433 . 36 ASN C C 174.6 . 1 434 . 36 ASN CA C 51.00 . 1 435 . 36 ASN HA H 4.94 . 1 436 . 36 ASN CB C 38.4 . 1 437 . 36 ASN HB2 H 2.83 . 2 438 . 36 ASN HB3 H 3.28 . 2 439 . 36 ASN CG C 174.4 . 1 440 . 36 ASN HD21 H 7.05 . 2 441 . 36 ASN HD22 H 7.51 . 2 442 . 36 ASN ND2 N 111.9 . 1 443 . 37 GLU N N 118.4 . 1 444 . 37 GLU H H 8.65 . 1 445 . 37 GLU C C 177.1 . 1 446 . 37 GLU CA C 59.5 . 1 447 . 37 GLU HA H 3.98 . 1 448 . 37 GLU CB C 29.1 . 1 449 . 37 GLU HB2 H 2.00 . 2 450 . 37 GLU HB3 H 2.05 . 2 451 . 37 GLU CG C 35.7 . 1 452 . 37 GLU HG2 H 2.37 . 1 453 . 37 GLU HG3 H 2.37 . 1 454 . 38 GLU N N 119.8 . 1 455 . 38 GLU H H 8.28 . 1 456 . 38 GLU C C 179.00 . 1 457 . 38 GLU CA C 59.5 . 1 458 . 38 GLU HA H 4.03 . 1 459 . 38 GLU CB C 28.6 . 1 460 . 38 GLU HB2 H 2.04 . 2 461 . 38 GLU HB3 H 2.26 . 2 462 . 38 GLU CG C 36.1 . 1 463 . 38 GLU HG2 H 1.94 . 1 464 . 38 GLU HG3 H 1.94 . 1 465 . 39 GLN N N 119.7 . 1 466 . 39 GLN H H 8.46 . 1 467 . 39 GLN C C 177.3 . 1 468 . 39 GLN CA C 57.5 . 1 469 . 39 GLN HA H 3.97 . 1 470 . 39 GLN CB C 28.7 . 1 471 . 39 GLN HB2 H 2.06 . 2 472 . 39 GLN HB3 H 2.48 . 2 473 . 39 GLN CG C 33.3 . 1 474 . 39 GLN HG2 H 2.35 . 1 475 . 39 GLN HG3 H 2.35 . 1 476 . 39 GLN CD C 179.2 . 1 477 . 39 GLN HE21 H 7.65 . 2 478 . 39 GLN HE22 H 8.26 . 2 479 . 39 GLN NE2 N 112.8 . 1 480 . 40 ARG N N 118.9 . 1 481 . 40 ARG H H 8.58 . 1 482 . 40 ARG C C 176.7 . 1 483 . 40 ARG CA C 60.3 . 1 484 . 40 ARG HA H 3.78 . 1 485 . 40 ARG CB C 30.1 . 1 486 . 40 ARG HB2 H 1.75 . 2 487 . 40 ARG HB3 H 1.85 . 2 488 . 40 ARG CG C 26.4 . 1 489 . 40 ARG HG2 H 1.46 . 2 490 . 40 ARG HG3 H 1.73 . 2 491 . 40 ARG CD C 42.4 . 1 492 . 40 ARG HD2 H 3.23 . 2 493 . 40 ARG HD3 H 3.43 . 2 494 . 40 ARG HE H 7.68 . 1 495 . 41 ASN N N 115.1 . 1 496 . 41 ASN H H 8.48 . 1 497 . 41 ASN C C 176.4 . 1 498 . 41 ASN CA C 55.5 . 1 499 . 41 ASN HA H 4.4 . 1 500 . 41 ASN CB C 37.6 . 1 501 . 41 ASN HB2 H 2.79 . 2 502 . 41 ASN HB3 H 2.9 . 2 503 . 41 ASN CG C 175.00 . 1 504 . 41 ASN HD21 H 7.63 . 2 505 . 41 ASN HD22 H 7.02 . 2 506 . 41 ASN ND2 N 112.2 . 1 507 . 42 ALA N N 122.8 . 1 508 . 42 ALA H H 7.88 . 1 509 . 42 ALA C C 179.8 . 1 510 . 42 ALA CA C 54.9 . 1 511 . 42 ALA HA H 4.17 . 1 512 . 42 ALA CB C 17.5 . 1 513 . 42 ALA HB H 1.33 . 1 514 . 43 PHE N N 117.00 . 1 515 . 43 PHE H H 7.96 . 1 516 . 43 PHE C C 176.9 . 1 517 . 43 PHE CA C 61.9 . 1 518 . 43 PHE HA H 4.37 . 1 519 . 43 PHE CB C 39.5 . 1 520 . 43 PHE HB2 H 2.99 . 2 521 . 43 PHE HB3 H 3.1 . 2 522 . 43 PHE CD1 C 130.2 . 1 523 . 43 PHE CD2 C 130.2 . 1 524 . 43 PHE HD1 H 7.31 . 1 525 . 43 PHE HD2 H 7.31 . 1 526 . 43 PHE CE1 C 129.9 . 1 527 . 43 PHE CE2 C 129.9 . 1 528 . 43 PHE HE1 H 7.2 . 1 529 . 43 PHE HE2 H 7.2 . 1 530 . 43 PHE CZ C 130.3 . 1 531 . 43 PHE HZ H 7.14 . 1 532 . 44 ILE N N 118.4 . 1 533 . 44 ILE H H 8.3 . 1 534 . 44 ILE C C 176.5 . 1 535 . 44 ILE CA C 64.1 . 1 536 . 44 ILE HA H 3.75 . 1 537 . 44 ILE CB C 36.4 . 1 538 . 44 ILE HB H 2.11 . 1 539 . 44 ILE CG1 C 28.2 . 1 540 . 44 ILE CG2 C 17.5 . 1 541 . 44 ILE HG12 H 1.35 . 2 542 . 44 ILE HG13 H 1.59 . 2 543 . 44 ILE HG2 H 0.97 . 1 544 . 44 ILE CD1 C 11.7 . 1 545 . 44 ILE HD1 H 0.62 . 1 546 . 45 GLN N N 119.5 . 1 547 . 45 GLN H H 8.46 . 1 548 . 45 GLN C C 177.1 . 1 549 . 45 GLN CA C 58.5 . 1 550 . 45 GLN HA H 3.94 . 1 551 . 45 GLN CB C 27.9 . 1 552 . 45 GLN HB2 H 2.12 . 2 553 . 45 GLN HB3 H 2.26 . 2 554 . 45 GLN CG C 33.2 . 1 555 . 45 GLN HG2 H 2.42 . 1 556 . 45 GLN HG3 H 2.42 . 1 557 . 45 GLN CD C 179.5 . 1 558 . 45 GLN HE21 H 7.87 . 2 559 . 45 GLN HE22 H 6.94 . 2 560 . 45 GLN NE2 N 116.1 . 1 561 . 46 SER N N 115.1 . 1 562 . 46 SER H H 8.06 . 1 563 . 46 SER C C 177.1 . 1 564 . 46 SER CA C 62.2 . 1 565 . 46 SER HA H 4.28 . 1 566 . 46 SER CB C 63.00 . 1 567 . 46 SER HB2 H 3.98 . 2 568 . 46 SER HB3 H 4.1 . 2 569 . 47 LEU N N 124.2 . 1 570 . 47 LEU H H 8.13 . 1 571 . 47 LEU C C 176.2 . 1 572 . 47 LEU CA C 57.00 . 1 573 . 47 LEU HA H 3.78 . 1 574 . 47 LEU CB C 42.2 . 1 575 . 47 LEU HB2 H 1.64 . 2 576 . 47 LEU HB3 H 1.95 . 2 577 . 47 LEU CG C 26.00 . 1 578 . 47 LEU HG H 1.64 . 1 579 . 47 LEU CD1 C 25.1 . 2 580 . 47 LEU CD2 C 26.1 . 2 581 . 47 LEU HD1 H 0.78 . 2 582 . 47 LEU HD2 H 0.76 . 2 583 . 48 LYS N N 115.6 . 1 584 . 48 LYS H H 8.02 . 1 585 . 48 LYS C C 177.8 . 1 586 . 48 LYS CA C 58.9 . 1 587 . 48 LYS HA H 4.00 . 1 588 . 48 LYS CB C 31.8 . 1 589 . 48 LYS HB2 H 1.92 . 2 590 . 48 LYS HB3 H 1.98 . 2 591 . 48 LYS CG C 25.7 . 1 592 . 48 LYS HG2 H 1.4 . 1 593 . 48 LYS HG3 H 1.4 . 1 594 . 48 LYS CD C 29.5 . 1 595 . 48 LYS HD2 H 1.68 . 1 596 . 48 LYS HD3 H 1.68 . 1 597 . 48 LYS CE C 41.00 . 1 598 . 48 LYS HE2 H 2.88 . 1 599 . 48 LYS HE3 H 2.88 . 1 600 . 49 ASP N N 118.1 . 1 601 . 49 ASP H H 8.15 . 1 602 . 49 ASP C C 176.2 . 1 603 . 49 ASP CA C 55.9 . 1 604 . 49 ASP HA H 4.43 . 1 605 . 49 ASP CB C 40.7 . 1 606 . 49 ASP HB2 H 2.68 . 2 607 . 49 ASP HB3 H 2.78 . 2 608 . 50 ASP N N 113.8 . 1 609 . 50 ASP H H 7.6 . 1 610 . 50 ASP C C 171.7 . 1 611 . 50 ASP CA C 51.00 . 1 612 . 50 ASP HA H 4.93 . 1 613 . 50 ASP CB C 40.1 . 1 614 . 50 ASP HB2 H 2.57 . 2 615 . 50 ASP HB3 H 2.99 . 2 616 . 51 PRO C C 177.3 . 1 617 . 51 PRO CA C 64.1 . 1 618 . 51 PRO HA H 4.51 . 1 619 . 51 PRO CB C 31.6 . 1 620 . 51 PRO HB2 H 1.91 . 2 621 . 51 PRO HB3 H 2.16 . 2 622 . 51 PRO CG C 26.8 . 1 623 . 51 PRO HG2 H 2.24 . 1 624 . 51 PRO HG3 H 2.24 . 1 625 . 51 PRO CD C 49.7 . 1 626 . 51 PRO HD2 H 3.7 . 2 627 . 51 PRO HD3 H 3.87 . 2 628 . 52 SER N N 112.7 . 1 629 . 52 SER H H 8.05 . 1 630 . 52 SER C C 175.1 . 1 631 . 52 SER CA C 62.1 . 1 632 . 52 SER HA H 4.36 . 1 633 . 52 SER CB C 62.3 . 1 634 . 52 SER HB2 H 3.98 . 2 635 . 52 SER HB3 H 4.04 . 2 636 . 53 GLN N N 120.4 . 1 637 . 53 GLN H H 7.88 . 1 638 . 53 GLN C C 175.2 . 1 639 . 53 GLN CA C 54.00 . 1 640 . 53 GLN HA H 4.62 . 1 641 . 53 GLN CB C 27.7 . 1 642 . 53 GLN HB2 H 2.00 . 2 643 . 53 GLN HB3 H 2.66 . 2 644 . 53 GLN CG C 33.4 . 1 645 . 53 GLN HG2 H 2.32 . 2 646 . 53 GLN HG3 H 2.46 . 2 647 . 53 GLN CD C 179.4 . 1 648 . 53 GLN HE21 H 7.63 . 2 649 . 53 GLN HE22 H 6.86 . 2 650 . 53 GLN NE2 N 114.00 . 1 651 . 54 SER N N 115.6 . 1 652 . 54 SER H H 7.8 . 1 653 . 54 SER C C 173.00 . 1 654 . 54 SER CA C 63.00 . 1 655 . 54 SER HA H 3.74 . 1 656 . 54 SER CB C 61.1 . 1 657 . 54 SER HB2 H 4.00 . 1 658 . 54 SER HB3 H 4.00 . 1 659 . 55 ALA N N 123.00 . 1 660 . 55 ALA H H 8.44 . 1 661 . 55 ALA C C 179.9 . 1 662 . 55 ALA CA C 55.3 . 1 663 . 55 ALA HA H 4.15 . 1 664 . 55 ALA CB C 17.5 . 1 665 . 55 ALA HB H 1.42 . 1 666 . 56 ASN N N 118.5 . 1 667 . 56 ASN H H 7.92 . 1 668 . 56 ASN C C 176.7 . 1 669 . 56 ASN CA C 55.5 . 1 670 . 56 ASN HA H 4.54 . 1 671 . 56 ASN CB C 37.7 . 1 672 . 56 ASN HB2 H 2.89 . 2 673 . 56 ASN HB3 H 2.91 . 2 674 . 56 ASN CG C 175.00 . 1 675 . 56 ASN HD21 H 7.78 . 2 676 . 56 ASN HD22 H 7.03 . 2 677 . 56 ASN ND2 N 112.9 . 1 678 . 57 LEU N N 121.5 . 1 679 . 57 LEU H H 8.61 . 1 680 . 57 LEU C C 177.2 . 1 681 . 57 LEU CA C 57.4 . 1 682 . 57 LEU HA H 4.18 . 1 683 . 57 LEU CB C 42.2 . 1 684 . 57 LEU HB2 H 1.31 . 2 685 . 57 LEU HB3 H 1.74 . 2 686 . 57 LEU CG C 25.9 . 1 687 . 57 LEU HG H 1.87 . 1 688 . 57 LEU CD1 C 22.9 . 2 689 . 57 LEU CD2 C 26.00 . 2 690 . 57 LEU HD1 H 1.11 . 2 691 . 57 LEU HD2 H 0.79 . 2 692 . 58 LEU N N 118.8 . 1 693 . 58 LEU H H 8.43 . 1 694 . 58 LEU C C 176.8 . 1 695 . 58 LEU CA C 57.6 . 1 696 . 58 LEU HA H 3.83 . 1 697 . 58 LEU CB C 41.5 . 1 698 . 58 LEU HB2 H 1.46 . 2 699 . 58 LEU HB3 H 1.92 . 2 700 . 58 LEU CG C 24.5 . 1 701 . 58 LEU HG H 1.53 . 1 702 . 58 LEU CD1 C 23.2 . 2 703 . 58 LEU CD2 C 24.4 . 2 704 . 58 LEU HD1 H 0.91 . 1 705 . 58 LEU HD2 H 0.91 . 1 706 . 59 ALA N N 119.5 . 1 707 . 59 ALA H H 7.61 . 1 708 . 59 ALA C C 180.2 . 1 709 . 59 ALA CA C 54.9 . 1 710 . 59 ALA HA H 4.05 . 1 711 . 59 ALA CB C 17.5 . 1 712 . 59 ALA HB H 1.54 . 1 713 . 60 GLU N N 119.1 . 1 714 . 60 GLU H H 8.07 . 1 715 . 60 GLU C C 177.8 . 1 716 . 60 GLU CA C 58.7 . 1 717 . 60 GLU HA H 4.04 . 1 718 . 60 GLU CB C 28.8 . 1 719 . 60 GLU HB2 H 2.23 . 2 720 . 60 GLU HB3 H 2.28 . 2 721 . 60 GLU CG C 35.6 . 1 722 . 60 GLU HG2 H 2.46 . 1 723 . 60 GLU HG3 H 2.46 . 1 724 . 61 ALA N N 124.00 . 1 725 . 61 ALA H H 8.48 . 1 726 . 61 ALA C C 178.5 . 1 727 . 61 ALA CA C 54.8 . 1 728 . 61 ALA HA H 3.49 . 1 729 . 61 ALA CB C 17.00 . 1 730 . 61 ALA HB H 0.5 . 1 731 . 62 LYS N N 118.1 . 1 732 . 62 LYS H H 8.5 . 1 733 . 62 LYS C C 177.6 . 1 734 . 62 LYS CA C 60.3 . 1 735 . 62 LYS HA H 3.78 . 1 736 . 62 LYS CB C 31.8 . 1 737 . 62 LYS HB2 H 1.65 . 2 738 . 62 LYS HB3 H 1.95 . 2 739 . 62 LYS CG C 26.00 . 1 740 . 62 LYS HG2 H 1.34 . 1 741 . 62 LYS HG3 H 1.34 . 1 742 . 62 LYS CD C 28.8 . 1 743 . 62 LYS HD2 H 1.61 . 1 744 . 62 LYS HD3 H 1.61 . 1 745 . 62 LYS CE C 41.1 . 1 746 . 62 LYS HE2 H 2.84 . 2 747 . 62 LYS HE3 H 2.94 . 2 748 . 63 LYS N N 120.2 . 1 749 . 63 LYS H H 7.71 . 1 750 . 63 LYS C C 178.6 . 1 751 . 63 LYS CA C 59.7 . 1 752 . 63 LYS HA H 4.13 . 1 753 . 63 LYS CB C 32.1 . 1 754 . 63 LYS HB2 H 1.96 . 1 755 . 63 LYS HB3 H 1.96 . 1 756 . 63 LYS CG C 24.6 . 1 757 . 63 LYS HG2 H 1.41 . 1 758 . 63 LYS HG3 H 1.41 . 1 759 . 63 LYS CD C 28.8 . 1 760 . 63 LYS HD2 H 1.62 . 2 761 . 63 LYS HD3 H 1.72 . 2 762 . 63 LYS CE C 41.5 . 1 763 . 63 LYS HE2 H 2.96 . 1 764 . 63 LYS HE3 H 2.96 . 1 765 . 64 LEU N N 122.1 . 1 766 . 64 LEU H H 7.95 . 1 767 . 64 LEU C C 176.9 . 1 768 . 64 LEU CA C 57.1 . 1 769 . 64 LEU HA H 4.19 . 1 770 . 64 LEU CB C 41.6 . 1 771 . 64 LEU HB2 H 1.7 . 2 772 . 64 LEU HB3 H 1.76 . 2 773 . 64 LEU CG C 26.7 . 1 774 . 64 LEU HG H 1.57 . 1 775 . 64 LEU CD1 C 23.4 . 2 776 . 64 LEU CD2 C 24.4 . 2 777 . 64 LEU HD1 H 1.00 . 1 778 . 64 LEU HD2 H 1.00 . 1 779 . 65 ASN N N 117.00 . 1 780 . 65 ASN H H 8.58 . 1 781 . 65 ASN C C 176.4 . 1 782 . 65 ASN CA C 57.3 . 1 783 . 65 ASN HA H 3.97 . 1 784 . 65 ASN CB C 41.5 . 1 785 . 65 ASN HB2 H 2.39 . 2 786 . 65 ASN HB3 H 3.11 . 2 787 . 65 ASN CG C 179.5 . 1 788 . 65 ASN HD21 H 7.96 . 2 789 . 65 ASN HD22 H 6.85 . 2 790 . 65 ASN ND2 N 116.1 . 1 791 . 66 ASP N N 118.7 . 1 792 . 66 ASP H H 8.25 . 1 793 . 66 ASP C C 177.7 . 1 794 . 66 ASP CA C 56.5 . 1 795 . 66 ASP HA H 4.48 . 1 796 . 66 ASP CB C 39.6 . 1 797 . 66 ASP HB2 H 2.72 . 2 798 . 66 ASP HB3 H 2.77 . 2 799 . 67 ALA N N 122.9 . 1 800 . 67 ALA H H 8.06 . 1 801 . 67 ALA C C 178.2 . 1 802 . 67 ALA CA C 54.1 . 1 803 . 67 ALA HA H 4.24 . 1 804 . 67 ALA CB C 18.1 . 1 805 . 67 ALA HB H 1.58 . 1 806 . 68 GLN N N 115.00 . 1 807 . 68 GLN H H 7.57 . 1 808 . 68 GLN C C 172.9 . 1 809 . 68 GLN CA C 54.5 . 1 810 . 68 GLN HA H 4.4 . 1 811 . 68 GLN CB C 27.8 . 1 812 . 68 GLN HB2 H 1.82 . 2 813 . 68 GLN HB3 H 2.32 . 2 814 . 68 GLN CG C 35.4 . 1 815 . 68 GLN HG2 H 2.46 . 2 816 . 68 GLN HG3 H 2.67 . 2 817 . 68 GLN CD C 180.6 . 1 818 . 68 GLN HE21 H 8.75 . 2 819 . 68 GLN HE22 H 7.3 . 2 820 . 68 GLN NE2 N 111.00 . 1 821 . 69 ALA N N 124.4 . 1 822 . 69 ALA H H 7.14 . 1 823 . 69 ALA C C 174.3 . 1 824 . 69 ALA CA C 50.5 . 1 825 . 69 ALA HA H 4.36 . 1 826 . 69 ALA CB C 17.5 . 1 827 . 69 ALA HB H 1.45 . 1 828 . 70 PRO C C 174.9 . 1 829 . 70 PRO CA C 63.00 . 1 830 . 70 PRO HA H 4.43 . 1 831 . 70 PRO CB C 31.5 . 1 832 . 70 PRO HB2 H 1.97 . 2 833 . 70 PRO HB3 H 2.32 . 2 834 . 70 PRO CG C 26.8 . 1 835 . 70 PRO HG2 H 2.08 . 1 836 . 70 PRO HG3 H 2.08 . 1 837 . 70 PRO CD C 50.1 . 1 838 . 70 PRO HD2 H 3.64 . 2 839 . 70 PRO HD3 H 3.8 . 2 840 . 71 LYS N N 127.3 . 1 841 . 71 LYS H H 8.05 . 1 842 . 71 LYS C C 174.4 . 1 843 . 71 LYS CA C 56.7 . 1 844 . 71 LYS HA H 4.2 . 1 845 . 71 LYS CB C 33.3 . 1 846 . 71 LYS HB2 H 1.72 . 2 847 . 71 LYS HB3 H 1.86 . 2 848 . 71 LYS CG C 28.3 . 1 849 . 71 LYS HG2 H 1.44 . 1 850 . 71 LYS HG3 H 1.44 . 1 851 . 71 LYS CD C 28.6 . 1 852 . 71 LYS HD2 H 1.7 . 1 853 . 71 LYS HD3 H 1.7 . 1 854 . 71 LYS CE C 41.8 . 1 855 . 71 LYS HE2 H 3.04 . 1 856 . 71 LYS HE3 H 3.04 . 1 stop_ save_