data_5565 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for porcine MSP ; _BMRB_accession_number 5565 _BMRB_flat_file_name bmr5565.str _Entry_type original _Submission_date 2002-10-30 _Accession_date 2002-10-30 _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 Wang Iren . . 2 Lou Yuan-Chao . . 3 Wu Kuen-Phon . . 4 Wu Shih-Hsiung . . 5 Chang Wen-Chang . . 6 Chen Chinpan . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 517 "13C chemical shifts" 394 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-09-28 original author 'original release' 2004-09-22 update author 'addition of chemical shifts' stop_ _Original_release_date 2002-10-30 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Disulfide pairings and structure of porcine beta-microseminoprotein ; _Citation_status published _Citation_type 'BMRB only' _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wang Iren . . 2 Lou Yuan-Chao . . 3 Wu Kuen-Phon . . 4 Wu Shih-Hsiung . . 5 Chang Wen-Chang . . 6 Chen Chinpan . . stop_ _Journal_abbreviation . _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword MSP NMR 'Na+,K+-ATPase inhibitor' PSP94 beta-microseminoprotein structure stop_ save_ ################################## # Molecular system description # ################################## save_system_MSP _Saveframe_category molecular_system _Mol_system_name 'porcine MSP' _Abbreviation_common MSP _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'porcine MSP' $MSP stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_MSP _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common beta-microseminoprotein _Name_variant 'sperm motility inhibitor' _Abbreviation_common MSP _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 91 _Mol_residue_sequence ; QCYFIPNQSLKPNECQDLKG VSHPLNSVWKTKDCEECTCG QDAISCCNTAAIPTGYDTNK CQKILNKKTCTYTVVEKKDP GKTCDVTGWVL ; loop_ _Residue_seq_code _Residue_label 1 GLN 2 CYS 3 TYR 4 PHE 5 ILE 6 PRO 7 ASN 8 GLN 9 SER 10 LEU 11 LYS 12 PRO 13 ASN 14 GLU 15 CYS 16 GLN 17 ASP 18 LEU 19 LYS 20 GLY 21 VAL 22 SER 23 HIS 24 PRO 25 LEU 26 ASN 27 SER 28 VAL 29 TRP 30 LYS 31 THR 32 LYS 33 ASP 34 CYS 35 GLU 36 GLU 37 CYS 38 THR 39 CYS 40 GLY 41 GLN 42 ASP 43 ALA 44 ILE 45 SER 46 CYS 47 CYS 48 ASN 49 THR 50 ALA 51 ALA 52 ILE 53 PRO 54 THR 55 GLY 56 TYR 57 ASP 58 THR 59 ASN 60 LYS 61 CYS 62 GLN 63 LYS 64 ILE 65 LEU 66 ASN 67 LYS 68 LYS 69 THR 70 CYS 71 THR 72 TYR 73 THR 74 VAL 75 VAL 76 GLU 77 LYS 78 LYS 79 ASP 80 PRO 81 GLY 82 LYS 83 THR 84 CYS 85 ASP 86 VAL 87 THR 88 GLY 89 TRP 90 VAL 91 LEU stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 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 7243 beta-microseminoprotein 100.00 94 100.00 100.00 1.14e-45 BMRB 7304 beta-microseminoprotein 100.00 91 100.00 100.00 1.14e-45 PDB 1XHH 'Solution Structure Of Porcine Beta-Microseminoprotein' 100.00 91 100.00 100.00 1.14e-45 PDB 2IZ4 'Solution Structure Of Human And Porcine Beta- Microseminoprotein' 100.00 94 100.00 100.00 1.14e-45 GenBank AAB50711 'PSP94-like protein [Sus scrofa]' 100.00 111 98.90 100.00 7.92e-46 REF NP_999017 'beta-microseminoprotein [Sus scrofa]' 100.00 111 98.90 100.00 7.92e-46 SWISS-PROT O02826 'Beta-microseminoprotein precursor (Prostate secreted seminal plasma protein) (Prostate secretory protein PSP94) (PSP-94) (TS507)' 100.00 111 98.90 100.00 7.92e-46 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MSP Pig 9823 Eukaryota Metazoa Sus scrofa 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 $MSP 'recombinant technology' . . . . . 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 _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MSP 1.5 mM 1.0 1.5 '[U-13C; U-15N]' stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.5 loop_ _Task 'data processing' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N HSQC' _Sample_label . save_ save_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY' _Sample_label . save_ save_1H-15N_TOCSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N TOCSY' _Sample_label . save_ save_1H-13C_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-13C NOESY' _Sample_label . save_ save_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HN(CO)CACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CACB _Sample_label . save_ save_HNCO_7 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.2 n/a temperature 310 1 K 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 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_Shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N HSQC' '1H-15N NOESY' '1H-15N TOCSY' '1H-13C NOESY' HN(CO)CA HN(CO)CACB HNCO stop_ loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'porcine MSP' _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 GLN HA H 4.37 0.2 1 2 . 1 GLN HB2 H 2.25 0.2 2 3 . 1 GLN HB3 H 2.08 0.2 2 4 . 1 GLN HG2 H 2.36 0.2 2 5 . 1 GLN HG3 H 2.19 0.2 2 6 . 1 GLN HE21 H 7.57 0.2 2 7 . 1 GLN HE22 H 6.72 0.2 2 8 . 1 GLN C C 175.95 0.2 1 9 . 1 GLN CA C 55.87 0.2 1 10 . 1 GLN CB C 28.61 0.2 1 11 . 1 GLN CG C 33.05 0.2 1 12 . 1 GLN NE2 N 111.95 0.2 1 13 . 2 CYS H H 8 0.2 1 14 . 2 CYS HA H 5.61 0.2 1 15 . 2 CYS HB2 H 2.83 0.2 2 16 . 2 CYS HB3 H 2.47 0.2 2 17 . 2 CYS C C 172.83 0.2 1 18 . 2 CYS CA C 54.8 0.2 1 19 . 2 CYS CB C 47.47 0.2 1 20 . 2 CYS N N 118.15 0.2 1 21 . 3 TYR H H 8.69 0.2 1 22 . 3 TYR HA H 4.71 0.2 1 23 . 3 TYR HB2 H 2.96 0.2 1 24 . 3 TYR HB3 H 2.96 0.2 1 25 . 3 TYR HD1 H 6.84 0.2 1 26 . 3 TYR HE1 H 6.58 0.2 1 27 . 3 TYR HE2 H 6.58 0.2 1 28 . 3 TYR HD2 H 6.84 0.2 1 29 . 3 TYR C C 172.85 0.2 1 30 . 3 TYR CA C 54.82 0.2 1 31 . 3 TYR CB C 39.33 0.2 1 32 . 3 TYR CD1 C 133.79 0.2 1 33 . 3 TYR CE1 C 117.67 0.2 1 34 . 3 TYR CD2 C 133.79 0.2 1 35 . 3 TYR CE2 C 117.67 0.2 1 36 . 3 TYR N N 118.77 0.2 1 37 . 4 PHE H H 8.48 0.2 1 38 . 4 PHE HA H 5.61 0.2 1 39 . 4 PHE HB2 H 2.84 0.2 1 40 . 4 PHE HB3 H 2.84 0.2 1 41 . 4 PHE HD1 H 7.24 0.2 1 42 . 4 PHE HE1 H 7.12 0.2 1 43 . 4 PHE HZ H 7.19 0.2 1 44 . 4 PHE HE2 H 7.12 0.2 1 45 . 4 PHE HD2 H 7.24 0.2 1 46 . 4 PHE C C 176.02 0.2 1 47 . 4 PHE CA C 55.15 0.2 1 48 . 4 PHE CB C 41.2 0.2 1 49 . 4 PHE CD1 C 131.99 0.2 1 50 . 4 PHE CE1 C 131.4 0.2 1 51 . 4 PHE CZ C 129.75 0.2 1 52 . 4 PHE CE2 C 131.4 0.2 1 53 . 4 PHE CD2 C 131.99 0.2 1 54 . 4 PHE N N 117.52 0.2 1 55 . 5 ILE H H 9.2 0.2 1 56 . 5 ILE HA H 4.75 0.2 1 57 . 5 ILE HB H 1.9 0.2 1 58 . 5 ILE HG12 H 1.56 0.2 2 59 . 5 ILE HG13 H 1.2 0.2 2 60 . 5 ILE HG2 H 1.09 0.2 1 61 . 5 ILE HD1 H 1.02 0.2 1 62 . 5 ILE C C 173.72 0.2 1 63 . 5 ILE CA C 57.1 0.2 1 64 . 5 ILE CB C 40.8 0.2 1 65 . 5 ILE CG1 C 26.05 0.2 1 66 . 5 ILE CG2 C 19.65 0.2 1 67 . 5 ILE CD1 C 13.51 0.2 1 68 . 5 ILE N N 122.58 0.2 1 69 . 6 PRO HA H 4.42 0.2 1 70 . 6 PRO HB2 H 2.38 0.2 1 71 . 6 PRO HB3 H 2.38 0.2 1 72 . 6 PRO HG2 H 2.1 0.2 1 73 . 6 PRO HG3 H 2.1 0.2 1 74 . 6 PRO HD2 H 3.85 0.2 2 75 . 6 PRO HD3 H 3.77 0.2 2 76 . 6 PRO C C 176.2 0.2 1 77 . 6 PRO CA C 62.17 0.2 1 78 . 6 PRO CB C 31.23 0.2 1 79 . 6 PRO CG C 26.84 0.2 1 80 . 6 PRO CD C 50.21 0.2 1 81 . 7 ASN H H 8.11 0.2 1 82 . 7 ASN HA H 4.73 0.2 1 83 . 7 ASN HB2 H 3.03 0.2 2 84 . 7 ASN HB3 H 2.43 0.2 2 85 . 7 ASN HD21 H 7.48 0.2 2 86 . 7 ASN HD22 H 7.19 0.2 2 87 . 7 ASN C C 176.2 0.2 1 88 . 7 ASN CA C 52.04 0.2 1 89 . 7 ASN CB C 37.69 0.2 1 90 . 7 ASN N N 120.08 0.2 1 91 . 7 ASN ND2 N 113.44 0.2 1 92 . 8 GLN H H 8.58 0.2 1 93 . 8 GLN HA H 4.36 0.2 1 94 . 8 GLN HB2 H 2.24 0.2 2 95 . 8 GLN HB3 H 1.72 0.2 2 96 . 8 GLN HG2 H 2.36 0.2 1 97 . 8 GLN HG3 H 2.36 0.2 1 98 . 8 GLN HE21 H 7.4 0.2 2 99 . 8 GLN HE22 H 6.91 0.2 2 100 . 8 GLN C C 176.59 0.2 1 101 . 8 GLN CA C 54.26 0.2 1 102 . 8 GLN CB C 28.59 0.2 1 103 . 8 GLN CG C 33.08 0.2 1 104 . 8 GLN N N 123.77 0.2 1 105 . 8 GLN NE2 N 112.9 0.2 1 106 . 9 SER H H 7.77 0.2 1 107 . 9 SER HA H 4.25 0.2 1 108 . 9 SER HB2 H 3.85 0.2 1 109 . 9 SER HB3 H 3.85 0.2 1 110 . 9 SER C C 175.21 0.2 1 111 . 9 SER CA C 57.75 0.2 1 112 . 9 SER CB C 63.49 0.2 1 113 . 9 SER N N 113.77 0.2 1 114 . 10 LEU H H 8.58 0.2 1 115 . 10 LEU HA H 4.35 0.2 1 116 . 10 LEU HB2 H 1.62 0.2 1 117 . 10 LEU HB3 H 1.62 0.2 1 118 . 10 LEU HG H 1.65 0.2 1 119 . 10 LEU HD1 H 0.88 0.2 1 120 . 10 LEU HD2 H 0.88 0.2 1 121 . 10 LEU C C 177.2 0.2 1 122 . 10 LEU CA C 54.39 0.2 1 123 . 10 LEU CB C 40.99 0.2 1 124 . 10 LEU CG C 26.32 0.2 1 125 . 10 LEU CD1 C 24.17 0.2 2 126 . 10 LEU CD2 C 22.09 0.2 2 127 . 10 LEU N N 125.02 0.2 1 128 . 11 LYS H H 8.11 0.2 1 129 . 11 LYS HA H 4.59 0.2 1 130 . 11 LYS HB2 H 1.72 0.2 1 131 . 11 LYS HB3 H 1.72 0.2 1 132 . 11 LYS HG2 H 1.32 0.2 1 133 . 11 LYS HG3 H 1.32 0.2 1 134 . 11 LYS HD2 H 1.5 0.2 1 135 . 11 LYS HD3 H 1.5 0.2 1 136 . 11 LYS C C 174.7 0.2 1 137 . 11 LYS CA C 52.53 0.2 1 138 . 11 LYS CB C 32.42 0.2 1 139 . 11 LYS N N 121.27 0.2 1 140 . 12 PRO HA H 4.39 0.2 1 141 . 12 PRO HB2 H 2.23 0.2 1 142 . 12 PRO HB3 H 2.23 0.2 1 143 . 12 PRO HG2 H 2.01 0.2 2 144 . 12 PRO HG3 H 1.86 0.2 2 145 . 12 PRO HD2 H 3.81 0.2 2 146 . 12 PRO HD3 H 3.62 0.2 2 147 . 12 PRO C C 176.67 0.2 1 148 . 12 PRO CA C 62.44 0.2 1 149 . 12 PRO CB C 31.47 0.2 1 150 . 12 PRO CG C 26.32 0.2 1 151 . 12 PRO CD C 50.21 0.2 1 152 . 13 ASN H H 8.6 0.2 1 153 . 13 ASN HA H 4.42 0.2 1 154 . 13 ASN HB2 H 2.96 0.2 1 155 . 13 ASN HB3 H 2.96 0.2 1 156 . 13 ASN HD21 H 7.48 0.2 2 157 . 13 ASN HD22 H 6.81 0.2 2 158 . 13 ASN C C 173.86 0.2 1 159 . 13 ASN CA C 53.22 0.2 1 160 . 13 ASN CB C 36.7 0.2 1 161 . 13 ASN N N 113.77 0.2 1 162 . 13 ASN ND2 N 112.81 0.2 1 163 . 14 GLU H H 7.58 0.2 1 164 . 14 GLU HA H 4.83 0.2 1 165 . 14 GLU HB2 H 1.67 0.2 1 166 . 14 GLU HB3 H 1.67 0.2 1 167 . 14 GLU HG2 H 1.93 0.2 1 168 . 14 GLU HG3 H 1.93 0.2 1 169 . 14 GLU C C 174.68 0.2 1 170 . 14 GLU CA C 54.33 0.2 1 171 . 14 GLU CB C 32.77 0.2 1 172 . 14 GLU CG C 34.49 0.2 1 173 . 14 GLU N N 116.27 0.2 1 174 . 15 CYS H H 9.19 0.2 1 175 . 15 CYS HA H 5.18 0.2 1 176 . 15 CYS HB2 H 2.96 0.2 2 177 . 15 CYS HB3 H 2.74 0.2 2 178 . 15 CYS C C 173.76 0.2 1 179 . 15 CYS CA C 55.5 0.2 1 180 . 15 CYS CB C 42.26 0.2 1 181 . 15 CYS N N 115.65 0.2 1 182 . 16 GLN H H 8.35 0.2 1 183 . 16 GLN HA H 5 0.2 1 184 . 16 GLN HB2 H 1.86 0.2 2 185 . 16 GLN HB3 H 1.77 0.2 2 186 . 16 GLN HG2 H 2.26 0.2 1 187 . 16 GLN HG3 H 2.26 0.2 1 188 . 16 GLN HE21 H 7.46 0.2 2 189 . 16 GLN HE22 H 6.69 0.2 2 190 . 16 GLN C C 174.91 0.2 1 191 . 16 GLN CA C 54.06 0.2 1 192 . 16 GLN CB C 31 0.2 1 193 . 16 GLN CG C 33.16 0.2 1 194 . 16 GLN N N 122.52 0.2 1 195 . 16 GLN NE2 N 111.18 0.2 1 196 . 17 ASP H H 8.32 0.2 1 197 . 17 ASP HA H 4.65 0.2 1 198 . 17 ASP HB2 H 3.64 0.2 2 199 . 17 ASP HB3 H 2.43 0.2 2 200 . 17 ASP C C 177.15 0.2 1 201 . 17 ASP CA C 51.7 0.2 1 202 . 17 ASP CB C 41.2 0.2 1 203 . 17 ASP N N 123.77 0.2 1 204 . 18 LEU H H 8.23 0.2 1 205 . 18 LEU HA H 4.16 0.2 1 206 . 18 LEU HB2 H 1.78 0.2 2 207 . 18 LEU HB3 H 1.67 0.2 2 208 . 18 LEU HG H 1.77 0.2 1 209 . 18 LEU HD1 H 0.98 0.2 2 210 . 18 LEU HD2 H 0.9 0.2 2 211 . 18 LEU C C 178.31 0.2 1 212 . 18 LEU CA C 56.15 0.2 1 213 . 18 LEU CB C 40.54 0.2 1 214 . 18 LEU CG C 26.43 0.2 1 215 . 18 LEU CD1 C 24.37 0.2 2 216 . 18 LEU CD2 C 21.99 0.2 2 217 . 18 LEU N N 116.27 0.2 1 218 . 19 LYS H H 8.22 0.2 1 219 . 19 LYS HA H 4.41 0.2 1 220 . 19 LYS HB2 H 2.02 0.2 2 221 . 19 LYS HB3 H 1.86 0.2 2 222 . 19 LYS HG2 H 1.46 0.2 2 223 . 19 LYS HG3 H 1.36 0.2 2 224 . 19 LYS HD2 H 1.66 0.2 1 225 . 19 LYS HD3 H 1.66 0.2 1 226 . 19 LYS C C 176.74 0.2 1 227 . 19 LYS CA C 54.29 0.2 1 228 . 19 LYS CB C 31.28 0.2 1 229 . 19 LYS CG C 24.08 0.2 1 230 . 19 LYS CD C 27.66 0.2 1 231 . 19 LYS CE C 41.25 0.2 1 232 . 19 LYS N N 118.15 0.2 1 233 . 20 GLY H H 7.92 0.2 1 234 . 20 GLY HA2 H 3.5 0.2 2 235 . 20 GLY HA3 H 4.11 0.2 2 236 . 20 GLY C C 173.73 0.2 1 237 . 20 GLY CA C 44.37 0.2 1 238 . 20 GLY N N 107.52 0.2 1 239 . 21 VAL H H 8.02 0.2 1 240 . 21 VAL HA H 3.7 0.2 1 241 . 21 VAL HB H 2.2 0.2 1 242 . 21 VAL HG1 H 0.73 0.2 2 243 . 21 VAL HG2 H 0.34 0.2 2 244 . 21 VAL C C 175.67 0.2 1 245 . 21 VAL CA C 61.61 0.2 1 246 . 21 VAL CB C 30.59 0.2 1 247 . 21 VAL CG1 C 19.8 0.2 2 248 . 21 VAL CG2 C 18.55 0.2 2 249 . 21 VAL N N 124.4 0.2 1 250 . 22 SER H H 8.19 0.2 1 251 . 22 SER HA H 4.92 0.2 1 252 . 22 SER HB2 H 3.51 0.2 1 253 . 22 SER HB3 H 3.51 0.2 1 254 . 22 SER C C 173.41 0.2 1 255 . 22 SER CA C 56.85 0.2 1 256 . 22 SER CB C 63.19 0.2 1 257 . 22 SER N N 122.52 0.2 1 258 . 23 HIS H H 8.56 0.2 1 259 . 23 HIS HA H 4.65 0.2 1 260 . 23 HIS HB2 H 2.73 0.2 2 261 . 23 HIS HB3 H 2.19 0.2 2 262 . 23 HIS HE1 H 8.6 0.2 2 263 . 23 HIS HD2 H 7.34 0.2 2 264 . 23 HIS C C 171.98 0.2 1 265 . 23 HIS CA C 51.33 0.2 1 266 . 23 HIS CB C 30.74 0.2 1 267 . 23 HIS CE1 C 136.74 0.2 1 268 . 23 HIS CD2 C 120.58 0.2 1 269 . 23 HIS N N 120.65 0.2 1 270 . 24 PRO HA H 4.58 0.2 1 271 . 24 PRO HB2 H 2.52 0.2 2 272 . 24 PRO HB3 H 1.89 0.2 2 273 . 24 PRO HG2 H 2.05 0.2 1 274 . 24 PRO HG3 H 2.05 0.2 1 275 . 24 PRO HD2 H 3.8 0.2 2 276 . 24 PRO HD3 H 3.66 0.2 2 277 . 24 PRO C C 177.59 0.2 1 278 . 24 PRO CA C 61.61 0.2 1 279 . 24 PRO CB C 32.14 0.2 1 280 . 24 PRO CG C 26.6 0.2 1 281 . 24 PRO CD C 50.09 0.2 1 282 . 25 LEU H H 7.9 0.2 1 283 . 25 LEU HA H 3.9 0.2 1 284 . 25 LEU HB2 H 1.55 0.2 2 285 . 25 LEU HB3 H 1.26 0.2 2 286 . 25 LEU HG H 1.48 0.2 1 287 . 25 LEU HD1 H 0.82 0.2 2 288 . 25 LEU HD2 H 0.76 0.2 2 289 . 25 LEU C C 176.94 0.2 1 290 . 25 LEU CA C 56.48 0.2 1 291 . 25 LEU CB C 41.32 0.2 1 292 . 25 LEU CG C 25.76 0.2 1 293 . 25 LEU CD1 C 24.27 0.2 2 294 . 25 LEU CD2 C 22.65 0.2 2 295 . 25 LEU N N 124.4 0.2 1 296 . 26 ASN H H 8.76 0.2 1 297 . 26 ASN HA H 4.4 0.2 1 298 . 26 ASN HB2 H 3.25 0.2 2 299 . 26 ASN HB3 H 2.98 0.2 2 300 . 26 ASN HD21 H 7.57 0.2 2 301 . 26 ASN HD22 H 6.87 0.2 2 302 . 26 ASN C C 174.09 0.2 1 303 . 26 ASN CA C 54.73 0.2 1 304 . 26 ASN CB C 36.27 0.2 1 305 . 26 ASN N N 118.15 0.2 1 306 . 26 ASN ND2 N 112.98 0.2 1 307 . 27 SER H H 8.05 0.2 1 308 . 27 SER HA H 4.56 0.2 1 309 . 27 SER HB2 H 4.21 0.2 2 310 . 27 SER HB3 H 3.99 0.2 2 311 . 27 SER C C 172.46 0.2 1 312 . 27 SER CA C 58.08 0.2 1 313 . 27 SER CB C 64.45 0.2 1 314 . 27 SER N N 115.02 0.2 1 315 . 28 VAL H H 8.2 0.2 1 316 . 28 VAL HA H 5.29 0.2 1 317 . 28 VAL HB H 1.79 0.2 1 318 . 28 VAL HG1 H 0.72 0.2 2 319 . 28 VAL HG2 H 0.85 0.2 2 320 . 28 VAL C C 176.1 0.2 1 321 . 28 VAL CA C 59.35 0.2 1 322 . 28 VAL CB C 34.22 0.2 1 323 . 28 VAL CG1 C 20 0.2 1 324 . 28 VAL CG2 C 20 0.2 1 325 . 28 VAL N N 119.4 0.2 1 326 . 29 TRP H H 8.93 0.2 1 327 . 29 TRP HA H 5.08 0.2 1 328 . 29 TRP HB2 H 3.34 0.2 2 329 . 29 TRP HB3 H 3.19 0.2 2 330 . 29 TRP HE1 H 10.05 0.2 1 331 . 29 TRP HD1 H 6.77 0.2 1 332 . 29 TRP HE3 H 6.95 0.2 1 333 . 29 TRP HZ3 H 6.69 0.2 1 334 . 29 TRP HH2 H 6.24 0.2 1 335 . 29 TRP HZ2 H 6.76 0.2 1 336 . 29 TRP C C 172.39 0.2 1 337 . 29 TRP CA C 55.63 0.2 1 338 . 29 TRP CB C 31.09 0.2 1 339 . 29 TRP CD1 C 126.89 0.2 1 340 . 29 TRP CE3 C 123.5 0.2 1 341 . 29 TRP CZ3 C 118.73 0.2 1 342 . 29 TRP CH2 C 119.81 0.2 1 343 . 29 TRP CZ2 C 112.9 0.2 1 344 . 29 TRP N N 126.9 0.2 1 345 . 29 TRP NE1 N 128.44 0.2 1 346 . 30 LYS H H 8.5 0.2 1 347 . 30 LYS HA H 5.19 0.2 1 348 . 30 LYS HB2 H 1.93 0.2 2 349 . 30 LYS HB3 H 1.75 0.2 2 350 . 30 LYS HG2 H 1.52 0.2 2 351 . 30 LYS HG3 H 1.41 0.2 2 352 . 30 LYS HD2 H 1.66 0.2 1 353 . 30 LYS HD3 H 1.66 0.2 1 354 . 30 LYS C C 177.74 0.2 1 355 . 30 LYS CA C 53.68 0.2 1 356 . 30 LYS CB C 34.05 0.2 1 357 . 30 LYS CG C 24.47 0.2 1 358 . 30 LYS CD C 28.27 0.2 1 359 . 30 LYS CE C 41.18 0.2 1 360 . 30 LYS N N 119.4 0.2 1 361 . 31 THR H H 8.46 0.2 1 362 . 31 THR HA H 4.85 0.2 1 363 . 31 THR HB H 4.64 0.2 1 364 . 31 THR HG2 H 1.27 0.2 1 365 . 31 THR C C 175.68 0.2 1 366 . 31 THR CA C 58.83 0.2 1 367 . 31 THR CB C 69.98 0.2 1 368 . 31 THR CG2 C 19.77 0.2 1 369 . 31 THR N N 113.15 0.2 1 370 . 32 LYS HA H 4.39 0.2 1 371 . 32 LYS HB2 H 2.01 0.2 2 372 . 32 LYS HB3 H 1.86 0.2 2 373 . 32 LYS HG2 H 1.46 0.2 1 374 . 32 LYS HG3 H 1.46 0.2 1 375 . 32 LYS HD2 H 1.64 0.2 1 376 . 32 LYS HD3 H 1.64 0.2 1 377 . 32 LYS C C 175.88 0.2 1 378 . 32 LYS CA C 54.79 0.2 1 379 . 32 LYS CB C 31.32 0.2 1 380 . 32 LYS CG C 23.67 0.2 1 381 . 32 LYS CD C 28.18 0.2 1 382 . 33 ASP H H 7.9 0.2 1 383 . 33 ASP HA H 4.7 0.2 1 384 . 33 ASP HB2 H 2.8 0.2 2 385 . 33 ASP HB3 H 2.3 0.2 2 386 . 33 ASP C C 174.86 0.2 1 387 . 33 ASP CA C 53.37 0.2 1 388 . 33 ASP CB C 40 0.2 1 389 . 33 ASP N N 118.15 0.2 1 390 . 34 CYS H H 8.15 0.2 1 391 . 34 CYS HA H 4.31 0.2 1 392 . 34 CYS HB2 H 3.21 0.2 2 393 . 34 CYS HB3 H 3.12 0.2 2 394 . 34 CYS C C 174.07 0.2 1 395 . 34 CYS CA C 54.84 0.2 1 396 . 34 CYS CB C 34.75 0.2 1 397 . 34 CYS N N 111.27 0.2 1 398 . 35 GLU H H 7.18 0.2 1 399 . 35 GLU HA H 5.09 0.2 1 400 . 35 GLU HB2 H 1.63 0.2 1 401 . 35 GLU HB3 H 1.63 0.2 1 402 . 35 GLU HG2 H 1.95 0.2 1 403 . 35 GLU HG3 H 1.95 0.2 1 404 . 35 GLU C C 175.17 0.2 1 405 . 35 GLU CA C 53.45 0.2 1 406 . 35 GLU CB C 32.06 0.2 1 407 . 35 GLU CG C 34.75 0.2 1 408 . 35 GLU N N 116.27 0.2 1 409 . 36 GLU H H 8.6 0.2 1 410 . 36 GLU HA H 4.81 0.2 1 411 . 36 GLU HB2 H 1.57 0.2 1 412 . 36 GLU HB3 H 1.57 0.2 1 413 . 36 GLU HG2 H 1.79 0.2 1 414 . 36 GLU HG3 H 1.79 0.2 1 415 . 36 GLU C C 175.69 0.2 1 416 . 36 GLU CA C 53.89 0.2 1 417 . 36 GLU CB C 31.09 0.2 1 418 . 36 GLU CG C 35.93 0.2 1 419 . 36 GLU N N 122.52 0.2 1 420 . 37 CYS H H 8.93 0.2 1 421 . 37 CYS HA H 5.44 0.2 1 422 . 37 CYS HB2 H 1.59 0.2 2 423 . 37 CYS HB3 H 0.56 0.2 2 424 . 37 CYS C C 170.73 0.2 1 425 . 37 CYS CA C 53.89 0.2 1 426 . 37 CYS CB C 46.1 0.2 1 427 . 37 CYS N N 126.27 0.2 1 428 . 38 THR H H 8.53 0.2 1 429 . 38 THR HA H 5.02 0.2 1 430 . 38 THR HB H 3.75 0.2 1 431 . 38 THR HG2 H 0.95 0.2 1 432 . 38 THR C C 173.61 0.2 1 433 . 38 THR CA C 58.83 0.2 1 434 . 38 THR CB C 70.31 0.2 1 435 . 38 THR CG2 C 19.21 0.2 1 436 . 38 THR N N 112.52 0.2 1 437 . 39 CYS H H 8.24 0.2 1 438 . 39 CYS HA H 5.09 0.2 1 439 . 39 CYS HB2 H 3.13 0.2 1 440 . 39 CYS HB3 H 3.13 0.2 1 441 . 39 CYS C C 173.46 0.2 1 442 . 39 CYS CA C 53.89 0.2 1 443 . 39 CYS CB C 36.42 0.2 1 444 . 39 CYS N N 123.15 0.2 1 445 . 40 GLY H H 8.12 0.2 1 446 . 40 GLY HA2 H 3.85 0.2 2 447 . 40 GLY HA3 H 4.7 0.2 2 448 . 40 GLY C C 172.4 0.2 1 449 . 40 GLY CA C 42.78 0.2 1 450 . 40 GLY N N 118.77 0.2 1 451 . 41 GLN H H 8.45 0.2 1 452 . 41 GLN HA H 3.86 0.2 1 453 . 41 GLN HB2 H 1.99 0.2 1 454 . 41 GLN HB3 H 1.99 0.2 1 455 . 41 GLN HG2 H 2.37 0.2 1 456 . 41 GLN HG3 H 2.37 0.2 1 457 . 41 GLN HE21 H 7.48 0.2 2 458 . 41 GLN HE22 H 6.87 0.2 2 459 . 41 GLN C C 177.14 0.2 1 460 . 41 GLN CA C 57.91 0.2 1 461 . 41 GLN CB C 28.12 0.2 1 462 . 41 GLN CG C 33.04 0.2 1 463 . 41 GLN N N 116.9 0.2 1 464 . 41 GLN NE2 N 111.9 0.2 1 465 . 42 ASP H H 8.62 0.2 1 466 . 42 ASP HA H 4.89 0.2 1 467 . 42 ASP HB2 H 2.84 0.2 2 468 . 42 ASP HB3 H 2.67 0.2 2 469 . 42 ASP C C 175.26 0.2 1 470 . 42 ASP CA C 52.65 0.2 1 471 . 42 ASP CB C 38.93 0.2 1 472 . 42 ASP N N 112.52 0.2 1 473 . 43 ALA H H 7.45 0.2 1 474 . 43 ALA HA H 4.73 0.2 1 475 . 43 ALA HB H 1.27 0.2 1 476 . 43 ALA C C 176.14 0.2 1 477 . 43 ALA CA C 51.35 0.2 1 478 . 43 ALA CB C 21.29 0.2 1 479 . 43 ALA N N 120.02 0.2 1 480 . 44 ILE H H 8.85 0.2 1 481 . 44 ILE HA H 4.79 0.2 1 482 . 44 ILE HB H 1.95 0.2 1 483 . 44 ILE HG12 H 1.89 0.2 2 484 . 44 ILE HG13 H 1.09 0.2 2 485 . 44 ILE HG2 H 0.91 0.2 1 486 . 44 ILE HD1 H 0.98 0.2 1 487 . 44 ILE C C 175.3 0.2 1 488 . 44 ILE CA C 60.02 0.2 1 489 . 44 ILE CB C 39.66 0.2 1 490 . 44 ILE CG1 C 28.75 0.2 1 491 . 44 ILE CG2 C 18.82 0.2 1 492 . 44 ILE CD1 C 14.14 0.2 1 493 . 44 ILE N N 121.9 0.2 1 494 . 45 SER H H 8.35 0.2 1 495 . 45 SER HA H 4.99 0.2 1 496 . 45 SER HB2 H 3.49 0.2 1 497 . 45 SER HB3 H 3.49 0.2 1 498 . 45 SER C C 174.45 0.2 1 499 . 45 SER CA C 54.2 0.2 1 500 . 45 SER CB C 63.38 0.2 1 501 . 45 SER N N 120.65 0.2 1 502 . 46 CYS H H 8.47 0.2 1 503 . 46 CYS HA H 5.16 0.2 1 504 . 46 CYS HB2 H 2.18 0.2 2 505 . 46 CYS HB3 H 1.72 0.2 2 506 . 46 CYS C C 172.8 0.2 1 507 . 46 CYS CA C 53.85 0.2 1 508 . 46 CYS CB C 46.51 0.2 1 509 . 46 CYS N N 123.77 0.2 1 510 . 47 CYS H H 8.6 0.2 1 511 . 47 CYS HA H 5.25 0.2 1 512 . 47 CYS HB2 H 2.75 0.2 2 513 . 47 CYS HB3 H 2.68 0.2 2 514 . 47 CYS C C 173.63 0.2 1 515 . 47 CYS CA C 53.85 0.2 1 516 . 47 CYS CB C 47.22 0.2 1 517 . 47 CYS N N 117.52 0.2 1 518 . 48 ASN H H 8.54 0.2 1 519 . 48 ASN HA H 4.87 0.2 1 520 . 48 ASN HB2 H 2.98 0.2 1 521 . 48 ASN HB3 H 2.98 0.2 1 522 . 48 ASN HD21 H 7.53 0.2 2 523 . 48 ASN HD22 H 6.84 0.2 2 524 . 48 ASN C C 176.13 0.2 1 525 . 48 ASN CA C 53.25 0.2 1 526 . 48 ASN CB C 38.61 0.2 1 527 . 48 ASN N N 121.9 0.2 1 528 . 48 ASN ND2 N 112.6 0.2 1 529 . 49 THR H H 8.35 0.2 1 530 . 49 THR HA H 4.32 0.2 1 531 . 49 THR HB H 4.29 0.2 1 532 . 49 THR HG2 H 1.01 0.2 1 533 . 49 THR C C 174.57 0.2 1 534 . 49 THR CA C 60.73 0.2 1 535 . 49 THR CB C 68.15 0.2 1 536 . 49 THR CG2 C 21.37 0.2 1 537 . 49 THR N N 115.02 0.2 1 538 . 50 ALA H H 8 0.2 1 539 . 50 ALA HA H 4.48 0.2 1 540 . 50 ALA HB H 1.12 0.2 1 541 . 50 ALA C C 176.59 0.2 1 542 . 50 ALA CA C 50.76 0.2 1 543 . 50 ALA CB C 19.76 0.2 1 544 . 50 ALA N N 126.27 0.2 1 545 . 51 ALA H H 8.37 0.2 1 546 . 51 ALA HA H 4.42 0.2 1 547 . 51 ALA HB H 1.37 0.2 1 548 . 51 ALA C C 177.55 0.2 1 549 . 51 ALA CA C 51.61 0.2 1 550 . 51 ALA CB C 18.49 0.2 1 551 . 51 ALA N N 125.65 0.2 1 552 . 52 ILE H H 8.88 0.2 1 553 . 52 ILE HA H 4.3 0.2 1 554 . 52 ILE HB H 1.81 0.2 1 555 . 52 ILE HG12 H 1.14 0.2 1 556 . 52 ILE HG13 H 1.14 0.2 1 557 . 52 ILE HG2 H 0.7 0.2 1 558 . 52 ILE HD1 H 0.81 0.2 1 559 . 52 ILE C C 174.41 0.2 1 560 . 52 ILE CA C 57.13 0.2 1 561 . 52 ILE CB C 39.1 0.2 1 562 . 52 ILE CG1 C 26.05 0.2 1 563 . 52 ILE CG2 C 15.99 0.2 1 564 . 52 ILE CD1 C 12.3 0.2 1 565 . 52 ILE N N 124.4 0.2 1 566 . 53 PRO HA H 4.06 0.2 1 567 . 53 PRO HB2 H 1.22 0.2 2 568 . 53 PRO HB3 H 1.06 0.2 2 569 . 53 PRO HG2 H 1.67 0.2 2 570 . 53 PRO HG3 H 1.37 0.2 2 571 . 53 PRO HD2 H 3.77 0.2 2 572 . 53 PRO HD3 H 3.12 0.2 2 573 . 53 PRO C C 175.78 0.2 1 574 . 53 PRO CA C 60.7 0.2 1 575 . 53 PRO CB C 31.4 0.2 1 576 . 53 PRO CG C 26.06 0.2 1 577 . 53 PRO CD C 49.2 0.2 1 578 . 54 THR H H 8.22 0.2 1 579 . 54 THR HA H 4.46 0.2 1 580 . 54 THR HB H 3.91 0.2 1 581 . 54 THR HG2 H 0.85 0.2 1 582 . 54 THR C C 174.04 0.2 1 583 . 54 THR CA C 59 0.2 1 584 . 54 THR CB C 69.94 0.2 1 585 . 54 THR CG2 C 19.96 0.2 1 586 . 54 THR N N 112.52 0.2 1 587 . 55 GLY H H 8.11 0.2 1 588 . 55 GLY HA2 H 3.61 0.2 2 589 . 55 GLY HA3 H 4.14 0.2 2 590 . 55 GLY C C 173.52 0.2 1 591 . 55 GLY CA C 45.51 0.2 1 592 . 55 GLY N N 109.4 0.2 1 593 . 56 TYR H H 6.91 0.2 1 594 . 56 TYR HA H 4.9 0.2 1 595 . 56 TYR HB2 H 2.8 0.2 1 596 . 56 TYR HB3 H 2.8 0.2 1 597 . 56 TYR HD1 H 6.35 0.2 1 598 . 56 TYR HE1 H 6.42 0.2 1 599 . 56 TYR HE2 H 6.42 0.2 1 600 . 56 TYR HD2 H 6.35 0.2 1 601 . 56 TYR C C 173.8 0.2 1 602 . 56 TYR CA C 53.25 0.2 1 603 . 56 TYR CB C 40.25 0.2 1 604 . 56 TYR CD1 C 133.26 0.2 1 605 . 56 TYR CE1 C 117.67 0.2 1 606 . 56 TYR CD2 C 133.26 0.2 1 607 . 56 TYR CE2 C 117.67 0.2 1 608 . 56 TYR N N 115.02 0.2 1 609 . 57 ASP H H 8.18 0.2 1 610 . 57 ASP HA H 4.57 0.2 1 611 . 57 ASP HB2 H 2.64 0.2 1 612 . 57 ASP HB3 H 2.64 0.2 1 613 . 57 ASP C C 172.51 0.2 1 614 . 57 ASP CA C 53.6 0.2 1 615 . 57 ASP CB C 40.13 0.2 1 616 . 57 ASP N N 120.02 0.2 1 617 . 58 THR H H 8.05 0.2 1 618 . 58 THR HA H 4.16 0.2 1 619 . 58 THR HB H 4.35 0.2 1 620 . 58 THR HG2 H 0.88 0.2 1 621 . 58 THR C C 175.95 0.2 1 622 . 58 THR CA C 62.35 0.2 1 623 . 58 THR CB C 67.61 0.2 1 624 . 58 THR CG2 C 20.8 0.2 1 625 . 58 THR N N 118.77 0.2 1 626 . 59 ASN H H 8.48 0.2 1 627 . 59 ASN HA H 4.65 0.2 1 628 . 59 ASN HB2 H 2.93 0.2 2 629 . 59 ASN HB3 H 2.79 0.2 2 630 . 59 ASN HD21 H 7.85 0.2 2 631 . 59 ASN HD22 H 6.94 0.2 2 632 . 59 ASN C C 177.75 0.2 1 633 . 59 ASN CA C 54.37 0.2 1 634 . 59 ASN CB C 38.04 0.2 1 635 . 59 ASN N N 118.77 0.2 1 636 . 59 ASN ND2 N 115.01 0.2 1 637 . 60 LYS H H 7.6 0.2 1 638 . 60 LYS HA H 4.25 0.2 1 639 . 60 LYS HB2 H 1.75 0.2 1 640 . 60 LYS HB3 H 1.75 0.2 1 641 . 60 LYS HG2 H 1.46 0.2 1 642 . 60 LYS HG3 H 1.46 0.2 1 643 . 60 LYS HD2 H 1.65 0.2 1 644 . 60 LYS HD3 H 1.65 0.2 1 645 . 60 LYS C C 177.17 0.2 1 646 . 60 LYS CA C 56.49 0.2 1 647 . 60 LYS CB C 34.97 0.2 1 648 . 60 LYS CG C 24.66 0.2 1 649 . 60 LYS CD C 28.38 0.2 1 650 . 60 LYS CE C 40.95 0.2 1 651 . 60 LYS N N 118.15 0.2 1 652 . 61 CYS H H 8.27 0.2 1 653 . 61 CYS HA H 5.41 0.2 1 654 . 61 CYS HB2 H 3.57 0.2 2 655 . 61 CYS HB3 H 2.59 0.2 2 656 . 61 CYS C C 171.35 0.2 1 657 . 61 CYS CA C 55.62 0.2 1 658 . 61 CYS CB C 49.02 0.2 1 659 . 61 CYS N N 116.9 0.2 1 660 . 62 GLN H H 9.42 0.2 1 661 . 62 GLN HA H 4.79 0.2 1 662 . 62 GLN HB2 H 1.72 0.2 1 663 . 62 GLN HB3 H 1.72 0.2 1 664 . 62 GLN HG2 H 2.05 0.2 1 665 . 62 GLN HG3 H 2.05 0.2 1 666 . 62 GLN HE21 H 6.99 0.2 2 667 . 62 GLN HE22 H 6.86 0.2 2 668 . 62 GLN C C 172.7 0.2 1 669 . 62 GLN CA C 52.31 0.2 1 670 . 62 GLN CB C 31.19 0.2 1 671 . 62 GLN CG C 31.19 0.2 1 672 . 62 GLN N N 116.9 0.2 1 673 . 62 GLN NE2 N 110.89 0.2 1 674 . 63 LYS H H 8.35 0.2 1 675 . 63 LYS HA H 5.25 0.2 1 676 . 63 LYS HB2 H 1.46 0.2 2 677 . 63 LYS HB3 H 1.32 0.2 2 678 . 63 LYS HG2 H 1.44 0.2 2 679 . 63 LYS HG3 H 1.21 0.2 2 680 . 63 LYS HD2 H 1.33 0.2 2 681 . 63 LYS HD3 H 0.51 0.2 2 682 . 63 LYS C C 174.45 0.2 1 683 . 63 LYS CA C 53.1 0.2 1 684 . 63 LYS CB C 33.87 0.2 1 685 . 63 LYS CG C 23.07 0.2 1 686 . 63 LYS CD C 28.62 0.2 1 687 . 63 LYS CE C 40.96 0.2 1 688 . 63 LYS N N 120.65 0.2 1 689 . 64 ILE H H 9.11 0.2 1 690 . 64 ILE HA H 4.41 0.2 1 691 . 64 ILE HB H 1.77 0.2 1 692 . 64 ILE HG12 H 1.37 0.2 2 693 . 64 ILE HG13 H 1.03 0.2 2 694 . 64 ILE HG2 H 0.76 0.2 1 695 . 64 ILE HD1 H 0.7 0.2 1 696 . 64 ILE C C 175.28 0.2 1 697 . 64 ILE CA C 59.07 0.2 1 698 . 64 ILE CB C 39.9 0.2 1 699 . 64 ILE CG1 C 26.06 0.2 1 700 . 64 ILE CG2 C 16.4 0.2 1 701 . 64 ILE CD1 C 12.21 0.2 1 702 . 64 ILE N N 123.15 0.2 1 703 . 65 LEU H H 8.86 0.2 1 704 . 65 LEU HA H 3.8 0.2 1 705 . 65 LEU HB2 H 1.64 0.2 2 706 . 65 LEU HB3 H 0.99 0.2 2 707 . 65 LEU HG H 0.82 0.2 1 708 . 65 LEU HD1 H 0.59 0.2 2 709 . 65 LEU HD2 H -0.1 0.2 2 710 . 65 LEU C C 175.12 0.2 1 711 . 65 LEU CA C 53.62 0.2 1 712 . 65 LEU CB C 41.4 0.2 1 713 . 65 LEU CG C 25.53 0.2 1 714 . 65 LEU CD1 C 25.53 0.2 2 715 . 65 LEU CD2 C 20.26 0.2 2 716 . 65 LEU N N 130.65 0.2 1 717 . 66 ASN H H 8.74 0.2 1 718 . 66 ASN HA H 4.72 0.2 1 719 . 66 ASN HB2 H 3.22 0.2 2 720 . 66 ASN HB3 H 2.65 0.2 2 721 . 66 ASN HD21 H 7.94 0.2 2 722 . 66 ASN HD22 H 6.77 0.2 2 723 . 66 ASN C C 176.28 0.2 1 724 . 66 ASN CA C 51.2 0.2 1 725 . 66 ASN CB C 37.49 0.2 1 726 . 66 ASN N N 126.9 0.2 1 727 . 66 ASN ND2 N 113.67 0.2 1 728 . 67 LYS H H 8.82 0.2 1 729 . 67 LYS HA H 3.9 0.2 1 730 . 67 LYS HB2 H 1.99 0.2 1 731 . 67 LYS HB3 H 1.99 0.2 1 732 . 67 LYS HG2 H 1.46 0.2 2 733 . 67 LYS HG3 H 1.22 0.2 2 734 . 67 LYS HD2 H 1.67 0.2 1 735 . 67 LYS HD3 H 1.67 0.2 1 736 . 67 LYS C C 176.32 0.2 1 737 . 67 LYS CA C 57.73 0.2 1 738 . 67 LYS CB C 31.3 0.2 1 739 . 67 LYS CG C 25.72 0.2 1 740 . 67 LYS CD C 28.47 0.2 1 741 . 67 LYS CE C 41.27 0.2 1 742 . 67 LYS N N 125.02 0.2 1 743 . 68 LYS H H 8.33 0.2 1 744 . 68 LYS HA H 4.17 0.2 1 745 . 68 LYS HB2 H 1.91 0.2 1 746 . 68 LYS HB3 H 1.91 0.2 1 747 . 68 LYS HG2 H 1.47 0.2 2 748 . 68 LYS HG3 H 1.36 0.2 2 749 . 68 LYS HD2 H 1.65 0.2 1 750 . 68 LYS HD3 H 1.65 0.2 1 751 . 68 LYS C C 178.38 0.2 1 752 . 68 LYS CA C 57.91 0.2 1 753 . 68 LYS CB C 31.39 0.2 1 754 . 68 LYS CG C 24.31 0.2 1 755 . 68 LYS CD C 28.06 0.2 1 756 . 68 LYS CE C 41.11 0.2 1 757 . 68 LYS N N 118.15 0.2 1 758 . 69 THR H H 7.06 0.2 1 759 . 69 THR HA H 4.25 0.2 1 760 . 69 THR HB H 4.25 0.2 1 761 . 69 THR HG2 H 1.01 0.2 1 762 . 69 THR C C 175.04 0.2 1 763 . 69 THR CA C 59.83 0.2 1 764 . 69 THR CB C 68.27 0.2 1 765 . 69 THR CG2 C 21.02 0.2 1 766 . 69 THR N N 104.4 0.2 1 767 . 70 CYS H H 8.2 0.2 1 768 . 70 CYS HA H 4.22 0.2 1 769 . 70 CYS HB2 H 2.95 0.2 2 770 . 70 CYS HB3 H 2.87 0.2 2 771 . 70 CYS C C 173.55 0.2 1 772 . 70 CYS CA C 54.32 0.2 1 773 . 70 CYS CB C 34.64 0.2 1 774 . 70 CYS N N 119.4 0.2 1 775 . 71 THR H H 7.36 0.2 1 776 . 71 THR HA H 4.7 0.2 1 777 . 71 THR HB H 4 0.2 1 778 . 71 THR HG2 H 1.1 0.2 1 779 . 71 THR C C 173.68 0.2 1 780 . 71 THR CA C 58.49 0.2 1 781 . 71 THR CB C 71.23 0.2 1 782 . 71 THR CG2 C 20.93 0.2 1 783 . 71 THR N N 107.52 0.2 1 784 . 72 TYR H H 9.48 0.2 1 785 . 72 TYR HA H 5.33 0.2 1 786 . 72 TYR HB2 H 3.04 0.2 2 787 . 72 TYR HB3 H 2.73 0.2 2 788 . 72 TYR HD1 H 7.12 0.2 1 789 . 72 TYR HE1 H 6.69 0.2 1 790 . 72 TYR HE2 H 6.69 0.2 1 791 . 72 TYR HD2 H 7.12 0.2 1 792 . 72 TYR C C 176.54 0.2 1 793 . 72 TYR CA C 58.52 0.2 1 794 . 72 TYR CB C 40.69 0.2 1 795 . 72 TYR CD1 C 133.46 0.2 1 796 . 72 TYR CE1 C 118.73 0.2 1 797 . 72 TYR CD2 C 133.46 0.2 1 798 . 72 TYR CE2 C 118.73 0.2 1 799 . 72 TYR N N 122.52 0.2 1 800 . 73 THR H H 8.72 0.2 1 801 . 73 THR HA H 4.64 0.2 1 802 . 73 THR HB H 4.02 0.2 1 803 . 73 THR HG2 H 1.19 0.2 1 804 . 73 THR C C 172.95 0.2 1 805 . 73 THR CA C 59.46 0.2 1 806 . 73 THR CB C 70.07 0.2 1 807 . 73 THR CG2 C 21.14 0.2 1 808 . 73 THR N N 113.77 0.2 1 809 . 74 VAL H H 8.42 0.2 1 810 . 74 VAL HA H 4.68 0.2 1 811 . 74 VAL HB H 1.59 0.2 1 812 . 74 VAL HG1 H -0.02 0.2 2 813 . 74 VAL HG2 H 0.19 0.2 2 814 . 74 VAL C C 175.42 0.2 1 815 . 74 VAL CA C 60.73 0.2 1 816 . 74 VAL CB C 31.05 0.2 1 817 . 74 VAL CG1 C 21.1 0.2 1 818 . 74 VAL CG2 C 21.1 0.2 1 819 . 74 VAL N N 123.77 0.2 1 820 . 75 VAL H H 8.43 0.2 1 821 . 75 VAL HA H 5.22 0.2 1 822 . 75 VAL HB H 2.26 0.2 1 823 . 75 VAL HG1 H 0.75 0.2 2 824 . 75 VAL HG2 H 0.7 0.2 2 825 . 75 VAL C C 175.83 0.2 1 826 . 75 VAL CA C 57.46 0.2 1 827 . 75 VAL CB C 35.42 0.2 1 828 . 75 VAL CG1 C 20.74 0.2 2 829 . 75 VAL CG2 C 17.52 0.2 2 830 . 75 VAL N N 119.4 0.2 1 831 . 76 GLU H H 8.34 0.2 1 832 . 76 GLU HA H 4.3 0.2 1 833 . 76 GLU HB2 H 2.08 0.2 1 834 . 76 GLU HB3 H 2.08 0.2 1 835 . 76 GLU HG2 H 2.37 0.2 1 836 . 76 GLU HG3 H 2.37 0.2 1 837 . 76 GLU C C 178.09 0.2 1 838 . 76 GLU CA C 56.87 0.2 1 839 . 76 GLU CB C 28.55 0.2 1 840 . 76 GLU CG C 36.55 0.2 1 841 . 76 GLU N N 121.27 0.2 1 842 . 77 LYS H H 8.62 0.2 1 843 . 77 LYS HA H 3.83 0.2 1 844 . 77 LYS HB2 H 1.79 0.2 1 845 . 77 LYS HB3 H 1.79 0.2 1 846 . 77 LYS HG2 H 1.17 0.2 2 847 . 77 LYS HG3 H 0.98 0.2 2 848 . 77 LYS HD2 H 1.54 0.2 1 849 . 77 LYS HD3 H 1.54 0.2 1 850 . 77 LYS C C 178.82 0.2 1 851 . 77 LYS CA C 58.73 0.2 1 852 . 77 LYS CB C 31.88 0.2 1 853 . 77 LYS CG C 26.07 0.2 1 854 . 77 LYS CD C 28.74 0.2 1 855 . 77 LYS CE C 41.32 0.2 1 856 . 77 LYS N N 121.9 0.2 1 857 . 78 LYS H H 8.17 0.2 1 858 . 78 LYS HA H 4.19 0.2 1 859 . 78 LYS HB2 H 1.86 0.2 2 860 . 78 LYS HB3 H 1.76 0.2 2 861 . 78 LYS HG2 H 1.42 0.2 1 862 . 78 LYS HG3 H 1.42 0.2 1 863 . 78 LYS HD2 H 1.66 0.2 1 864 . 78 LYS HD3 H 1.66 0.2 1 865 . 78 LYS C C 176.19 0.2 1 866 . 78 LYS CA C 55.67 0.2 1 867 . 78 LYS CB C 31.73 0.2 1 868 . 78 LYS CG C 24.03 0.2 1 869 . 78 LYS CD C 28.16 0.2 1 870 . 78 LYS CE C 41.06 0.2 1 871 . 78 LYS N N 113.77 0.2 1 872 . 79 ASP H H 6.65 0.2 1 873 . 79 ASP HA H 4.84 0.2 1 874 . 79 ASP HB2 H 2.87 0.2 2 875 . 79 ASP HB3 H 2.43 0.2 2 876 . 79 ASP C C 172.28 0.2 1 877 . 79 ASP CA C 50.64 0.2 1 878 . 79 ASP CB C 40.29 0.2 1 879 . 79 ASP N N 113.77 0.2 1 880 . 80 PRO HA H 4.52 0.2 1 881 . 80 PRO HB2 H 2.22 0.2 2 882 . 80 PRO HB3 H 1.94 0.2 2 883 . 80 PRO HG2 H 1.9 0.2 1 884 . 80 PRO HG3 H 1.9 0.2 1 885 . 80 PRO HD2 H 3.77 0.2 2 886 . 80 PRO HD3 H 3.43 0.2 2 887 . 80 PRO C C 176.36 0.2 1 888 . 80 PRO CA C 62.56 0.2 1 889 . 80 PRO CB C 30.92 0.2 1 890 . 80 PRO CG C 25.92 0.2 1 891 . 80 PRO CD C 49.42 0.2 1 892 . 81 GLY H H 8.09 0.2 1 893 . 81 GLY HA2 H 3.61 0.2 2 894 . 81 GLY HA3 H 4.11 0.2 2 895 . 81 GLY C C 173.92 0.2 1 896 . 81 GLY CA C 44.34 0.2 1 897 . 81 GLY N N 105.02 0.2 1 898 . 82 LYS H H 8.17 0.2 1 899 . 82 LYS HA H 4.6 0.2 1 900 . 82 LYS HB2 H 1.81 0.2 2 901 . 82 LYS HB3 H 1.71 0.2 2 902 . 82 LYS HG2 H 1.31 0.2 1 903 . 82 LYS HG3 H 1.31 0.2 1 904 . 82 LYS HD2 H 1.6 0.2 1 905 . 82 LYS HD3 H 1.6 0.2 1 906 . 82 LYS C C 175.27 0.2 1 907 . 82 LYS CA C 53.86 0.2 1 908 . 82 LYS CB C 32.96 0.2 1 909 . 82 LYS CG C 23.87 0.2 1 910 . 82 LYS CD C 27.93 0.2 1 911 . 82 LYS CE C 41.36 0.2 1 912 . 82 LYS N N 123.15 0.2 1 913 . 83 THR H H 8.1 0.2 1 914 . 83 THR HA H 4.71 0.2 1 915 . 83 THR HB H 4.28 0.2 1 916 . 83 THR HG2 H 1.27 0.2 1 917 . 83 THR C C 175.21 0.2 1 918 . 83 THR CA C 60.6 0.2 1 919 . 83 THR CB C 69.22 0.2 1 920 . 83 THR CG2 C 21.37 0.2 1 921 . 83 THR N N 115.02 0.2 1 922 . 84 CYS H H 8.02 0.2 1 923 . 84 CYS HA H 4.84 0.2 1 924 . 84 CYS HB2 H 3.18 0.2 2 925 . 84 CYS HB3 H 2.97 0.2 2 926 . 84 CYS C C 172.79 0.2 1 927 . 84 CYS CA C 53.7 0.2 1 928 . 84 CYS CB C 46.72 0.2 1 929 . 84 CYS N N 119.4 0.2 1 930 . 85 ASP H H 8.36 0.2 1 931 . 85 ASP HA H 4.48 0.2 1 932 . 85 ASP HB2 H 2.57 0.2 2 933 . 85 ASP HB3 H 2.46 0.2 2 934 . 85 ASP C C 178.11 0.2 1 935 . 85 ASP CA C 54.01 0.2 1 936 . 85 ASP CB C 40.5 0.2 1 937 . 85 ASP N N 121.27 0.2 1 938 . 86 VAL H H 8.05 0.2 1 939 . 86 VAL HA H 4.16 0.2 1 940 . 86 VAL HB H 1.98 0.2 1 941 . 86 VAL HG1 H 0.41 0.2 2 942 . 86 VAL HG2 H 0.59 0.2 2 943 . 86 VAL C C 176.45 0.2 1 944 . 86 VAL CA C 60.07 0.2 1 945 . 86 VAL CB C 33.82 0.2 1 946 . 86 VAL CG1 C 20.8 0.2 1 947 . 86 VAL CG2 C 20.8 0.2 1 948 . 86 VAL N N 118.77 0.2 1 949 . 87 THR H H 8.14 0.2 1 950 . 87 THR HA H 4.32 0.2 1 951 . 87 THR HB H 4.32 0.2 1 952 . 87 THR HG2 H 1.12 0.2 1 953 . 87 THR C C 174.67 0.2 1 954 . 87 THR CA C 61.97 0.2 1 955 . 87 THR CB C 68.25 0.2 1 956 . 87 THR CG2 C 20.87 0.2 1 957 . 87 THR N N 115.65 0.2 1 958 . 88 GLY H H 7.49 0.2 1 959 . 88 GLY HA2 H 3.72 0.2 2 960 . 88 GLY HA3 H 4.11 0.2 2 961 . 88 GLY C C 170.33 0.2 1 962 . 88 GLY CA C 44.51 0.2 1 963 . 88 GLY N N 110.02 0.2 1 964 . 89 TRP H H 7.99 0.2 1 965 . 89 TRP HA H 5.12 0.2 1 966 . 89 TRP HB2 H 2.9 0.2 2 967 . 89 TRP HB3 H 2.81 0.2 2 968 . 89 TRP HE1 H 10.09 0.2 1 969 . 89 TRP HD1 H 7.05 0.2 1 970 . 89 TRP HE3 H 7.21 0.2 1 971 . 89 TRP HZ3 H 7.22 0.2 1 972 . 89 TRP HH2 H 7.19 0.2 1 973 . 89 TRP HZ2 H 7.45 0.2 1 974 . 89 TRP C C 176.03 0.2 1 975 . 89 TRP CA C 55.15 0.2 1 976 . 89 TRP CB C 31.4 0.2 1 977 . 89 TRP CD1 C 127.06 0.2 1 978 . 89 TRP CE3 C 119.62 0.2 1 979 . 89 TRP CZ3 C 120.19 0.2 1 980 . 89 TRP CH2 C 120.19 0.2 1 981 . 89 TRP CZ2 C 114.73 0.2 1 982 . 89 TRP N N 118.15 0.2 1 983 . 89 TRP NE1 N 129.86 0.2 1 984 . 90 VAL H H 9.24 0.2 1 985 . 90 VAL HA H 4.27 0.2 1 986 . 90 VAL HB H 2.01 0.2 1 987 . 90 VAL HG1 H 0.83 0.2 1 988 . 90 VAL HG2 H 0.83 0.2 1 989 . 90 VAL C C 174.5 0.2 1 990 . 90 VAL CA C 61.07 0.2 1 991 . 90 VAL CB C 33.01 0.2 1 992 . 90 VAL CG1 C 20.13 0.2 1 993 . 90 VAL CG2 C 20.13 0.2 1 994 . 90 VAL N N 123.77 0.2 1 995 . 91 LEU H H 7.94 0.2 1 996 . 91 LEU HA H 4.29 0.2 1 997 . 91 LEU HB2 H 1.53 0.2 1 998 . 91 LEU HB3 H 1.53 0.2 1 999 . 91 LEU HG H 1.56 0.2 1 1000 . 91 LEU HD1 H 0.81 0.2 1 1001 . 91 LEU HD2 H 0.81 0.2 1 1002 . 91 LEU C C 181.65 0.2 1 1003 . 91 LEU CA C 55.68 0.2 1 1004 . 91 LEU CB C 43.15 0.2 1 1005 . 91 LEU CG C 26.05 0.2 1 1006 . 91 LEU CD1 C 23.55 0.2 1 1007 . 91 LEU CD2 C 23.55 0.2 1 1008 . 91 LEU N N 131.9 0.2 1 stop_ save_