data_4143 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H and 15N Resonance Assignment of Neural Cell Adhesion Molecule module 2 ; _BMRB_accession_number 4143 _BMRB_flat_file_name bmr4143.str _Entry_type original _Submission_date 1998-05-19 _Accession_date 1998-05-19 _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 Jensen Peter H. . 2 Thomsen Niels K. . 3 Soroka Vladislav . . 4 Berezin Vladimir . . 5 Bock Elisabeth . . 6 Poulsen Flemming M. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 526 "15N chemical shifts" 97 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-03-02 original author . stop_ _Original_release_date 2000-03-02 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Jensen, P. H., Thomsen, N. K., Soroka, V., Berezin, V., Bock, E., and Poulsen, F. M., "1H and 15N Resonance Assignment of Neural Cell Adhesion Molecule Module-2," J. Biomol. NMR. 12, 569-570 (1998). ; _Citation_title '1H and 15N Resonance Assignment of Neural Cell Adhesion Molecule module 2' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 99079126 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Jensen Peter H. . 2 Thomsen Niels K. . 3 Soroka Vladislav . . 4 Berezin Vladimir . . 5 Bock Elisabeth . . 6 Poulsen Flemming M. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of Biomolecular NMR' _Journal_volume 12 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 569 _Page_last 570 _Year 1998 _Details . loop_ _Keyword Adhesion Cell M2 'Module 2' Molecule NCAM Neural NMR 'nuclear magnetic resonance' protein stop_ save_ ################################## # Molecular system description # ################################## save_system_NCAM_M2 _Saveframe_category molecular_system _Mol_system_name 'Neural cell adhesion molecule module 2' _Abbreviation_common 'NCAM M2' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'NCAM M2' $NCAM_M2 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function 'Cell adhesion' 'Heterophilic binding' 'Homophilic binding' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NCAM_M2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Neural cell adhesion molecule module 2' _Abbreviation_common 'NCAM M2' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function 'Cell adhesion' 'Heterophilic binding' 'Homophilic binding' stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 92 _Mol_residue_sequence ; YVMFKNAPTPQEFKEGEDAV IVCDVVSSLPPTIIWKHKGR DVILKKDVRFIVLSNNYLQI RGIKKTDEGTYRCEGRILAR GEINFKDIQVIV ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 100 TYR 2 101 VAL 3 102 MET 4 103 PHE 5 104 LYS 6 105 ASN 7 106 ALA 8 107 PRO 9 108 THR 10 109 PRO 11 110 GLN 12 111 GLU 13 112 PHE 14 113 LYS 15 114 GLU 16 115 GLY 17 116 GLU 18 117 ASP 19 118 ALA 20 119 VAL 21 120 ILE 22 121 VAL 23 122 CYS 24 123 ASP 25 124 VAL 26 125 VAL 27 126 SER 28 127 SER 29 128 LEU 30 129 PRO 31 130 PRO 32 131 THR 33 132 ILE 34 133 ILE 35 134 TRP 36 135 LYS 37 136 HIS 38 137 LYS 39 138 GLY 40 139 ARG 41 140 ASP 42 141 VAL 43 142 ILE 44 143 LEU 45 144 LYS 46 145 LYS 47 146 ASP 48 147 VAL 49 148 ARG 50 149 PHE 51 150 ILE 52 151 VAL 53 152 LEU 54 153 SER 55 154 ASN 56 155 ASN 57 156 TYR 58 157 LEU 59 158 GLN 60 159 ILE 61 160 ARG 62 161 GLY 63 162 ILE 64 163 LYS 65 164 LYS 66 165 THR 67 166 ASP 68 167 GLU 69 168 GLY 70 169 THR 71 170 TYR 72 171 ARG 73 172 CYS 74 173 GLU 75 174 GLY 76 175 ARG 77 176 ILE 78 177 LEU 79 178 ALA 80 179 ARG 81 180 GLY 82 181 GLU 83 182 ILE 84 183 ASN 85 184 PHE 86 185 LYS 87 186 ASP 88 187 ILE 89 188 GLN 90 189 VAL 91 190 ILE 92 191 VAL stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-07-14 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 1EPF "Crystal Structure Of The Two N-Terminal Immunoglobulin Domains Of The Neural Cell Adhesion Molecule (Ncam)" 98.91 191 98.90 100.00 1.85e-57 PDB 1QZ1 "Crystal Structure Of The Ig 1-2-3 Fragment Of Ncam" 98.91 291 98.90 100.00 1.48e-56 PDB 3NCM "Neural Cell Adhesion Molecule, Module 2, Nmr, 20 Structures" 100.00 92 100.00 100.00 1.53e-59 DBJ BAC34554 "unnamed protein product [Mus musculus]" 98.91 839 98.90 100.00 8.44e-54 DBJ BAC38551 "unnamed protein product [Mus musculus]" 98.91 839 98.90 100.00 8.96e-54 DBJ BAD92680 "Neural cell adhesion molecule 1, 120 kDa isoform precursor variant [Homo sapiens]" 98.91 807 97.80 100.00 1.30e-53 DBJ BAF85142 "unnamed protein product [Homo sapiens]" 98.91 858 97.80 100.00 1.97e-53 EMBL CAA29809 "unnamed protein product [Rattus norvegicus]" 98.91 858 98.90 100.00 8.63e-54 EMBL CAA33148 "cell adhesion molecule (AA 1 - 681) (2262 is 1st base in codon) [Mus musculus]" 98.91 681 98.90 100.00 3.96e-54 EMBL CAA34739 "unnamed protein product [Homo sapiens]" 98.91 761 97.80 100.00 4.16e-55 EMBL CAA68263 "unnamed protein product [Mus musculus]" 98.91 725 98.90 100.00 2.13e-55 GB AAB04558 "neural cell adhesion molecule CD56 [Homo sapiens]" 98.91 848 97.80 100.00 2.10e-53 GB AAB31836 "N-CAM [Homo sapiens]" 98.91 848 97.80 100.00 2.05e-53 GB AAH11310 "Ncam1 protein [Mus musculus]" 98.91 605 97.80 98.90 7.41e-54 GB AAH29119 "NCAM1 protein [Homo sapiens]" 98.91 364 97.80 100.00 1.03e-55 GB AAH47244 "Neural cell adhesion molecule 1 [Homo sapiens]" 98.91 858 97.80 100.00 1.91e-53 REF NP_000606 "neural cell adhesion molecule 1 isoform 1 precursor [Homo sapiens]" 98.91 848 97.80 100.00 2.05e-53 REF NP_001070150 "neural cell adhesion molecule 1 isoform 3 precursor [Homo sapiens]" 98.91 761 97.80 100.00 4.16e-55 REF NP_001074914 "neural cell adhesion molecule 1 isoform 1 precursor [Mus musculus]" 98.91 848 98.90 100.00 8.75e-54 REF NP_001106675 "neural cell adhesion molecule 1 isoform 3 precursor [Mus musculus]" 98.91 1115 98.90 100.00 3.50e-55 REF NP_001122300 "neural cell adhesion molecule 1 isoform 1 precursor [Gallus gallus]" 98.91 1109 97.80 100.00 1.87e-54 SP P13591 "RecName: Full=Neural cell adhesion molecule 1; Short=N-CAM-1; Short=NCAM-1; AltName: CD_antigen=CD56; Flags: Precursor" 98.91 858 97.80 100.00 1.97e-53 SP P13595 "RecName: Full=Neural cell adhesion molecule 1; Short=N-CAM-1; Short=NCAM-1; AltName: CD_antigen=CD56; Flags: Precursor" 98.91 1115 98.90 100.00 3.68e-55 SP P13596 "RecName: Full=Neural cell adhesion molecule 1; Short=N-CAM-1; Short=NCAM-1; AltName: CD_antigen=CD56; Flags: Precursor" 98.91 858 98.90 100.00 8.63e-54 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $NCAM_M2 fungi 4922 Eukaryota Fungi Pichia pastoris 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 $NCAM_M2 'not reported' . . . . . 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 $NCAM_M2 1.0 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_software_PRONTO _Saveframe_category software _Name PRONTO _Version 970801 loop_ _Vendor _Address _Electronic_address 'Carlsberg A/S' 'gamle carlsberg vej 10, DK-2500 Valby' fmp@crc.dk stop_ loop_ _Task assignment stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.0 . n/a temperature 298 . 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 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 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 'NCAM M2' _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 TYR H H 7.46 . 1 2 . 1 TYR HA H 4.20 . 1 3 . 1 TYR HB3 H 3.058 . 1 4 . 1 TYR HB2 H 3.058 . 1 5 . 1 TYR HD1 H 6.880 . 1 6 . 1 TYR HD2 H 6.880 . 1 7 . 1 TYR HE1 H 6.594 . 1 8 . 1 TYR HE2 H 6.594 . 1 9 . 2 VAL H H 8.56 . 1 10 . 2 VAL HA H 3.94 . 1 11 . 2 VAL HB H 1.746 . 1 12 . 2 VAL HG1 H 0.395 . 2 13 . 2 VAL HG2 H 0.601 . 2 14 . 2 VAL N N 119.925 . 1 15 . 3 MET H H 9.01 . 1 16 . 3 MET HA H 4.56 . 1 17 . 3 MET HB3 H 1.851 . 2 18 . 3 MET HB2 H 1.955 . 2 19 . 3 MET HG2 H 2.327 . 1 20 . 3 MET HG3 H 2.327 . 1 21 . 3 MET N N 123.501 . 1 22 . 4 PHE H H 8.82 . 1 23 . 4 PHE HB3 H 2.841 . 2 24 . 4 PHE HB2 H 2.502 . 2 25 . 4 PHE HD1 H 6.978 . 1 26 . 4 PHE HD2 H 6.978 . 1 27 . 4 PHE HE1 H 6.833 . 1 28 . 4 PHE HE2 H 6.833 . 1 29 . 4 PHE HZ H 6.891 . 1 30 . 4 PHE N N 118.987 . 1 31 . 5 LYS H H 8.25 . 1 32 . 5 LYS HA H 4.15 . 1 33 . 5 LYS HB3 H 1.636 . 2 34 . 5 LYS HB2 H 1.563 . 2 35 . 5 LYS HG2 H 1.367 . 2 36 . 5 LYS HG3 H 1.260 . 2 37 . 5 LYS HE2 H 2.926 . 2 38 . 5 LYS HE3 H 2.883 . 2 39 . 5 LYS N N 124.935 . 1 40 . 6 ASN H H 7.47 . 1 41 . 6 ASN HB3 H 3.009 . 2 42 . 6 ASN HB2 H 2.797 . 2 43 . 6 ASN HD21 H 7.696 . 2 44 . 6 ASN HD22 H 6.899 . 2 45 . 6 ASN N N 111.064 . 1 46 . 6 ASN ND2 N 111.628 . 1 47 . 8 PRO HA H 4.32 . 1 48 . 8 PRO HB3 H 2.261 . 1 49 . 8 PRO HB2 H 2.261 . 1 50 . 8 PRO HG2 H 1.802 . 2 51 . 8 PRO HG3 H 1.916 . 2 52 . 8 PRO HD2 H 3.324 . 1 53 . 8 PRO HD3 H 3.324 . 1 54 . 9 THR H H 8.07 . 1 55 . 9 THR HA H 6.18 . 1 56 . 9 THR HB H 4.253 . 1 57 . 9 THR HG2 H 1.372 . 1 58 . 9 THR N N 110.482 . 1 59 . 10 PRO HA H 5.67 . 1 60 . 10 PRO HB3 H 2.268 . 2 61 . 10 PRO HB2 H 1.741 . 2 62 . 10 PRO HG2 H 1.785 . 2 63 . 10 PRO HG3 H 1.863 . 2 64 . 10 PRO HD2 H 3.598 . 2 65 . 10 PRO HD3 H 3.559 . 2 66 . 11 GLN H H 9.00 . 1 67 . 11 GLN HA H 4.35 . 1 68 . 11 GLN HB3 H 1.531 . 1 69 . 11 GLN HB2 H 1.531 . 1 70 . 11 GLN HG2 H 2.090 . 1 71 . 11 GLN HG3 H 2.090 . 1 72 . 11 GLN HE21 H 7.396 . 2 73 . 11 GLN HE22 H 6.849 . 2 74 . 11 GLN N N 117.776 . 1 75 . 11 GLN NE2 N 111.449 . 1 76 . 12 GLU H H 7.83 . 1 77 . 12 GLU HA H 5.16 . 1 78 . 12 GLU HB3 H 1.584 . 2 79 . 12 GLU HB2 H 1.656 . 2 80 . 12 GLU HG2 H 1.888 . 1 81 . 12 GLU HG3 H 1.888 . 1 82 . 12 GLU N N 120.227 . 1 83 . 13 PHE H H 8.64 . 1 84 . 13 PHE HB3 H 3.188 . 2 85 . 13 PHE HB2 H 2.227 . 2 86 . 13 PHE HD1 H 7.078 . 1 87 . 13 PHE HD2 H 7.078 . 1 88 . 13 PHE HE1 H 6.776 . 1 89 . 13 PHE HE2 H 6.776 . 1 90 . 13 PHE N N 118.558 . 1 91 . 14 LYS H H 9.07 . 1 92 . 14 LYS HA H 4.65 . 1 93 . 14 LYS HB3 H 1.727 . 1 94 . 14 LYS HB2 H 1.727 . 1 95 . 14 LYS HG2 H 1.451 . 2 96 . 14 LYS HG3 H 1.609 . 2 97 . 14 LYS HD2 H 1.658 . 1 98 . 14 LYS HD3 H 1.658 . 1 99 . 14 LYS HE2 H 2.972 . 1 100 . 14 LYS HE3 H 2.972 . 1 101 . 14 LYS N N 120.627 . 1 102 . 15 GLU H H 8.52 . 1 103 . 15 GLU HA H 3.54 . 1 104 . 15 GLU HB3 H 1.927 . 1 105 . 15 GLU HB2 H 1.927 . 1 106 . 15 GLU HG2 H 1.765 . 2 107 . 15 GLU HG3 H 2.262 . 2 108 . 15 GLU N N 121.372 . 1 109 . 16 GLY H H 9.62 . 1 110 . 16 GLY HA2 H 4.34 . 2 111 . 16 GLY HA3 H 3.38 . 2 112 . 16 GLY N N 113.408 . 1 113 . 17 GLU H H 8.03 . 1 114 . 17 GLU HA H 4.32 . 1 115 . 17 GLU HB3 H 2.256 . 2 116 . 17 GLU HB2 H 1.975 . 2 117 . 17 GLU HG2 H 2.408 . 2 118 . 17 GLU HG3 H 2.177 . 2 119 . 17 GLU N N 119.268 . 1 120 . 18 ASP H H 8.50 . 1 121 . 18 ASP HA H 5.12 . 1 122 . 18 ASP HB3 H 2.124 . 2 123 . 18 ASP HB2 H 2.616 . 2 124 . 18 ASP N N 119.414 . 1 125 . 19 ALA H H 8.00 . 1 126 . 19 ALA HA H 3.65 . 1 127 . 19 ALA HB H -0.097 . 1 128 . 19 ALA N N 123.723 . 1 129 . 20 VAL H H 7.18 . 1 130 . 20 VAL HA H 4.27 . 1 131 . 20 VAL HB H 1.888 . 1 132 . 20 VAL HG1 H 0.832 . 2 133 . 20 VAL HG2 H 0.800 . 2 134 . 20 VAL N N 119.625 . 1 135 . 21 ILE H H 9.36 . 1 136 . 21 ILE HA H 4.17 . 1 137 . 21 ILE HB H 1.272 . 1 138 . 21 ILE HG12 H 0.779 . 2 139 . 21 ILE HG13 H 0.519 . 2 140 . 21 ILE HG2 H 0.762 . 1 141 . 21 ILE HD1 H -0.104 . 1 142 . 21 ILE N N 127.553 . 1 143 . 22 VAL H H 8.73 . 1 144 . 22 VAL HA H 2.11 . 1 145 . 22 VAL HB H 1.462 . 1 146 . 22 VAL HG1 H 0.531 . 2 147 . 22 VAL HG2 H 0.686 . 2 148 . 22 VAL N N 125.874 . 1 149 . 23 CYS H H 6.22 . 1 150 . 23 CYS HA H 4.38 . 1 151 . 23 CYS HB3 H 3.722 . 2 152 . 23 CYS HB2 H 3.331 . 2 153 . 23 CYS N N 120.992 . 1 154 . 24 ASP H H 9.15 . 1 155 . 24 ASP HA H 5.36 . 1 156 . 24 ASP HB3 H 2.743 . 2 157 . 24 ASP HB2 H 2.815 . 2 158 . 24 ASP N N 124.850 . 1 159 . 25 VAL H H 8.80 . 1 160 . 25 VAL HA H 4.41 . 1 161 . 25 VAL HB H 1.698 . 1 162 . 25 VAL HG1 H 0.383 . 2 163 . 25 VAL HG2 H 0.519 . 2 164 . 25 VAL N N 123.616 . 1 165 . 26 VAL H H 8.83 . 1 166 . 26 VAL HA H 4.47 . 1 167 . 26 VAL HB H 1.932 . 1 168 . 26 VAL HG1 H 0.905 . 2 169 . 26 VAL HG2 H 0.847 . 2 170 . 26 VAL N N 122.605 . 1 171 . 27 SER H H 8.31 . 1 172 . 27 SER HA H 3.90 . 1 173 . 27 SER HB3 H 3.516 . 1 174 . 27 SER HB2 H 3.516 . 1 175 . 27 SER N N 115.281 . 1 176 . 28 SER H H 7.46 . 1 177 . 28 SER HA H 3.80 . 1 178 . 28 SER HB3 H 3.598 . 2 179 . 28 SER HB2 H 3.406 . 2 180 . 28 SER N N 112.138 . 1 181 . 29 LEU H H 6.93 . 1 182 . 29 LEU HB3 H 1.199 . 4 183 . 29 LEU HB2 H 1.199 . 4 184 . 29 LEU HG H 1.199 . 4 185 . 29 LEU HD1 H 1.446 . 4 186 . 29 LEU HD2 H 1.446 . 4 187 . 29 LEU N N 118.473 . 1 188 . 32 THR H H 9.12 . 1 189 . 32 THR HA H 4.47 . 1 190 . 32 THR HB H 3.923 . 1 191 . 32 THR HG2 H 1.201 . 1 192 . 32 THR N N 113.864 . 1 193 . 33 ILE H H 8.62 . 1 194 . 33 ILE HA H 5.24 . 1 195 . 33 ILE HB H 1.725 . 1 196 . 33 ILE HG2 H 0.705 . 1 197 . 33 ILE N N 126.536 . 1 198 . 34 ILE H H 9.10 . 1 199 . 34 ILE HA H 4.44 . 1 200 . 34 ILE HB H 1.654 . 1 201 . 34 ILE HG12 H 1.097 . 1 202 . 34 ILE HG13 H 1.097 . 1 203 . 34 ILE HG2 H 0.829 . 1 204 . 34 ILE HD1 H 0.779 . 1 205 . 34 ILE N N 126.843 . 1 206 . 35 TRP H H 9.62 . 1 207 . 35 TRP HA H 5.63 . 1 208 . 35 TRP HB3 H 2.966 . 2 209 . 35 TRP HB2 H 3.171 . 2 210 . 35 TRP HD1 H 7.052 . 1 211 . 35 TRP HE1 H 10.638 . 1 212 . 35 TRP HE3 H 7.354 . 1 213 . 35 TRP HZ2 H 7.540 . 1 214 . 35 TRP HZ3 H 6.802 . 1 215 . 35 TRP HH2 H 6.789 . 1 216 . 35 TRP N N 124.468 . 1 217 . 35 TRP NE1 N 127.054 . 1 218 . 36 LYS H H 9.36 . 1 219 . 36 LYS HA H 5.24 . 1 220 . 36 LYS HB3 H 1.53 . 1 221 . 36 LYS HB2 H 1.53 . 1 222 . 36 LYS HG2 H 1.257 . 2 223 . 36 LYS HG3 H 2.497 . 2 224 . 36 LYS HD2 H 1.209 . 2 225 . 36 LYS HD3 H 1.318 . 2 226 . 36 LYS HE2 H 2.727 . 2 227 . 36 LYS HE3 H 2.668 . 2 228 . 36 LYS N N 117.603 . 1 229 . 37 HIS H H 8.77 . 1 230 . 37 HIS HA H 4.63 . 1 231 . 37 HIS N N 118.150 . 1 232 . 38 LYS H H 9.25 . 1 233 . 38 LYS HA H 3.55 . 1 234 . 38 LYS HB3 H 1.700 . 2 235 . 38 LYS HB2 H 1.466 . 2 236 . 38 LYS HG2 H 0.291 . 2 237 . 38 LYS HG3 H 0.786 . 2 238 . 38 LYS HD2 H 1.412 . 2 239 . 38 LYS HD3 H 1.376 . 2 240 . 38 LYS HE2 H 2.799 . 1 241 . 38 LYS HE3 H 2.799 . 1 242 . 38 LYS N N 125.754 . 1 243 . 39 GLY H H 8.70 . 1 244 . 39 GLY HA2 H 4.01 . 2 245 . 39 GLY HA3 H 3.48 . 2 246 . 39 GLY N N 100.916 . 1 247 . 40 ARG H H 7.41 . 1 248 . 40 ARG HA H 4.68 . 1 249 . 40 ARG HB3 H 1.616 . 1 250 . 40 ARG HB2 H 1.616 . 1 251 . 40 ARG HG2 H 1.748 . 1 252 . 40 ARG HG3 H 1.748 . 1 253 . 40 ARG HD2 H 1.547 . 1 254 . 40 ARG HD3 H 1.547 . 1 255 . 40 ARG HE H 7.110 . 1 256 . 40 ARG N N 117.328 . 1 257 . 40 ARG NE N 123.229 . 1 258 . 42 VAL H H 9.27 . 1 259 . 42 VAL HA H 3.87 . 1 260 . 42 VAL HB H 2.002 . 2 261 . 42 VAL HG1 H 1.065 . 2 262 . 42 VAL HG2 H 1.102 . 2 263 . 42 VAL N N 123.430 . 1 264 . 43 ILE H H 9.00 . 1 265 . 43 ILE HA H 4.05 . 1 266 . 43 ILE HB H 2.084 . 1 267 . 43 ILE HG2 H 0.985 . 1 268 . 43 ILE N N 120.376 . 1 269 . 44 LEU H H 7.76 . 1 270 . 44 LEU HA H 4.14 . 1 271 . 44 LEU HB3 H 1.853 . 1 272 . 44 LEU HB2 H 1.853 . 1 273 . 44 LEU HG H 1.586 . 2 274 . 44 LEU HD1 H 0.861 . 2 275 . 44 LEU HD2 H 1.008 . 2 276 . 44 LEU N N 117.590 . 1 277 . 45 LYS H H 7.47 . 1 278 . 45 LYS HA H 3.93 . 1 279 . 45 LYS HB3 H 1.729 . 1 280 . 45 LYS HB2 H 1.729 . 1 281 . 45 LYS HG2 H 1.403 . 1 282 . 45 LYS HG3 H 1.403 . 1 283 . 45 LYS HD2 H 1.181 . 2 284 . 45 LYS HD3 H 1.043 . 2 285 . 45 LYS HE2 H 2.664 . 2 286 . 45 LYS HE3 H 2.588 . 2 287 . 45 LYS N N 115.602 . 1 288 . 46 LYS H H 7.67 . 1 289 . 46 LYS HA H 3.88 . 1 290 . 46 LYS HB3 H 1.929 . 1 291 . 46 LYS HB2 H 1.929 . 1 292 . 46 LYS HG2 H 1.346 . 1 293 . 46 LYS HG3 H 1.346 . 1 294 . 46 LYS HD2 H 1.863 . 1 295 . 46 LYS HD3 H 1.863 . 1 296 . 46 LYS HE2 H 2.977 . 1 297 . 46 LYS HE3 H 2.977 . 1 298 . 46 LYS N N 111.479 . 1 299 . 47 ASP H H 8.23 . 1 300 . 47 ASP HA H 4.93 . 1 301 . 47 ASP HB3 H 2.935 . 2 302 . 47 ASP HB2 H 2.277 . 2 303 . 47 ASP N N 117.282 . 1 304 . 48 VAL H H 8.34 . 1 305 . 48 VAL HA H 4.10 . 1 306 . 48 VAL HB H 2.332 . 1 307 . 48 VAL HG1 H 0.915 . 2 308 . 48 VAL HG2 H 1.026 . 2 309 . 48 VAL N N 119.547 . 1 310 . 49 ARG H H 8.54 . 1 311 . 49 ARG HA H 3.88 . 1 312 . 49 ARG HB3 H 3.143 . 2 313 . 49 ARG HB2 H 2.994 . 2 314 . 49 ARG N N 117.588 . 1 315 . 50 PHE H H 7.64 . 1 316 . 50 PHE HA H 4.89 . 1 317 . 50 PHE HB3 H 3.193 . 2 318 . 50 PHE HB2 H 2.336 . 2 319 . 50 PHE HD1 H 6.987 . 1 320 . 50 PHE HD2 H 6.987 . 1 321 . 50 PHE HE1 H 7.179 . 1 322 . 50 PHE HE2 H 7.179 . 1 323 . 50 PHE HZ H 7.225 . 1 324 . 50 PHE N N 114.479 . 1 325 . 51 ILE H H 8.96 . 1 326 . 51 ILE HA H 4.20 . 1 327 . 51 ILE HB H 1.680 . 1 328 . 51 ILE HG12 H 0.943 . 1 329 . 51 ILE HG13 H 0.943 . 1 330 . 51 ILE HG2 H 0.711 . 1 331 . 51 ILE HD1 H 1.300 . 1 332 . 51 ILE N N 122.503 . 1 333 . 52 VAL H H 8.53 . 1 334 . 52 VAL HA H 4.36 . 1 335 . 52 VAL HB H 2.071 . 1 336 . 52 VAL HG1 H 1.201 . 2 337 . 52 VAL HG2 H 1.075 . 2 338 . 52 VAL N N 125.168 . 1 339 . 53 LEU H H 8.92 . 1 340 . 53 LEU HA H 4.32 . 1 341 . 53 LEU HB3 H 1.506 . 2 342 . 53 LEU HB2 H 2.185 . 2 343 . 53 LEU HG H 1.596 . 2 344 . 53 LEU HD1 H 0.690 . 2 345 . 53 LEU HD2 H 0.853 . 2 346 . 53 LEU N N 126.956 . 1 347 . 54 SER H H 8.79 . 1 348 . 54 SER HA H 4.16 . 1 349 . 54 SER HB3 H 3.914 . 2 350 . 54 SER HB2 H 3.934 . 2 351 . 54 SER N N 114.241 . 1 352 . 55 ASN H H 7.32 . 1 353 . 55 ASN HA H 4.47 . 1 354 . 55 ASN HB3 H 2.398 . 2 355 . 55 ASN HB2 H 2.772 . 2 356 . 55 ASN HD21 H 6.836 . 2 357 . 55 ASN HD22 H 5.115 . 2 358 . 55 ASN N N 115.409 . 1 359 . 55 ASN ND2 N 104.972 . 1 360 . 56 ASN H H 8.12 . 1 361 . 56 ASN HA H 4.33 . 1 362 . 56 ASN HB3 H 3.704 . 2 363 . 56 ASN HB2 H 3.048 . 2 364 . 56 ASN HD21 H 7.637 . 2 365 . 56 ASN HD22 H 7.128 . 2 366 . 56 ASN N N 106.342 . 1 367 . 56 ASN ND2 N 112.742 . 1 368 . 57 TYR H H 7.69 . 1 369 . 57 TYR HA H 5.09 . 1 370 . 57 TYR HB3 H 3.235 . 2 371 . 57 TYR HB2 H 3.083 . 2 372 . 57 TYR HD1 H 7.006 . 1 373 . 57 TYR HD2 H 7.006 . 1 374 . 57 TYR HE1 H 6.901 . 1 375 . 57 TYR HE2 H 6.901 . 1 376 . 57 TYR N N 117.369 . 1 377 . 58 LEU H H 7.13 . 1 378 . 58 LEU HA H 4.28 . 1 379 . 58 LEU HB3 H 0.071 . 2 380 . 58 LEU HB2 H -1.313 . 2 381 . 58 LEU HG H 0.628 . 1 382 . 58 LEU HD1 H 0.492 . 2 383 . 58 LEU HD2 H 0.191 . 2 384 . 58 LEU N N 119.224 . 1 385 . 59 GLN H H 9.30 . 1 386 . 59 GLN HA H 5.30 . 1 387 . 59 GLN HB3 H 1.831 . 2 388 . 59 GLN HB2 H 2.226 . 2 389 . 59 GLN HG2 H 1.590 . 2 390 . 59 GLN HG3 H 1.454 . 2 391 . 59 GLN HE21 H 6.360 . 2 392 . 59 GLN HE22 H 6.632 . 2 393 . 59 GLN N N 126.292 . 1 394 . 59 GLN NE2 N 107.197 . 1 395 . 60 ILE H H 8.30 . 1 396 . 60 ILE HA H 3.86 . 1 397 . 60 ILE HB H 0.921 . 1 398 . 60 ILE HG12 H -0.327 . 1 399 . 60 ILE HG13 H -0.327 . 1 400 . 60 ILE HG2 H -0.244 . 1 401 . 60 ILE HD1 H -0.010 . 1 402 . 60 ILE N N 122.944 . 1 403 . 61 ARG H H 8.73 . 1 404 . 61 ARG HA H 3.89 . 1 405 . 61 ARG HB3 H 1.439 . 2 406 . 61 ARG HB2 H 1.595 . 2 407 . 61 ARG HG2 H 1.130 . 1 408 . 61 ARG HG3 H 1.130 . 1 409 . 61 ARG HD2 H 3.001 . 2 410 . 61 ARG HD3 H 2.958 . 2 411 . 61 ARG HE H 6.769 . 2 412 . 61 ARG N N 123.176 . 1 413 . 61 ARG NE N 121.660 . 1 414 . 62 GLY H H 8.34 . 1 415 . 62 GLY HA2 H 3.40 . 2 416 . 62 GLY HA3 H 3.33 . 2 417 . 62 GLY N N 109.534 . 1 418 . 63 ILE H H 8.15 . 1 419 . 63 ILE HA H 3.44 . 1 420 . 63 ILE HB H 1.370 . 1 421 . 63 ILE HG12 H 1.558 . 2 422 . 63 ILE HG13 H 1.214 . 2 423 . 63 ILE HG2 H 0.794 . 1 424 . 63 ILE HD1 H 0.195 . 1 425 . 63 ILE N N 119.422 . 1 426 . 64 LYS H H 9.21 . 1 427 . 64 LYS HA H 4.87 . 1 428 . 64 LYS HB3 H 1.559 . 1 429 . 64 LYS HB2 H 1.559 . 1 430 . 64 LYS N N 124.386 . 1 431 . 65 LYS H H 9.25 . 1 432 . 65 LYS HA H 3.84 . 1 433 . 65 LYS HB3 H 1.924 . 2 434 . 65 LYS HB2 H 1.832 . 2 435 . 65 LYS HG2 H 1.443 . 1 436 . 65 LYS HG3 H 1.443 . 1 437 . 65 LYS HD2 H 1.589 . 1 438 . 65 LYS HD3 H 1.589 . 1 439 . 65 LYS N N 121.681 . 1 440 . 66 THR H H 7.22 . 1 441 . 66 THR HA H 4.19 . 1 442 . 66 THR HG2 H 1.255 . 1 443 . 66 THR N N 101.242 . 1 444 . 67 ASP H H 8.09 . 1 445 . 67 ASP HB3 H 2.909 . 2 446 . 67 ASP HB2 H 2.636 . 2 447 . 67 ASP N N 117.316 . 1 448 . 68 GLU H H 7.47 . 1 449 . 68 GLU HA H 4.07 . 1 450 . 68 GLU HB3 H 2.454 . 2 451 . 68 GLU HB2 H 2.170 . 2 452 . 68 GLU HG2 H 2.859 . 1 453 . 68 GLU HG3 H 2.859 . 1 454 . 68 GLU N N 116.959 . 1 455 . 69 GLY H H 8.47 . 1 456 . 69 GLY HA2 H 4.07 . 2 457 . 69 GLY HA3 H 5.42 . 2 458 . 69 GLY N N 107.845 . 1 459 . 70 THR H H 8.78 . 1 460 . 70 THR HA H 5.02 . 1 461 . 70 THR HB H 3.847 . 1 462 . 70 THR HG2 H 1.020 . 1 463 . 70 THR N N 115.779 . 1 464 . 71 TYR H H 10.10 . 1 465 . 71 TYR HA H 5.18 . 1 466 . 71 TYR HB3 H 3.026 . 1 467 . 71 TYR HB2 H 3.026 . 1 468 . 71 TYR HD1 H 6.952 . 1 469 . 71 TYR HD2 H 6.952 . 1 470 . 71 TYR HE1 H 6.427 . 1 471 . 71 TYR HE2 H 6.427 . 1 472 . 71 TYR N N 129.489 . 1 473 . 72 ARG H H 9.60 . 1 474 . 72 ARG HA H 5.09 . 1 475 . 72 ARG HB3 H 1.642 . 1 476 . 72 ARG HB2 H 1.642 . 1 477 . 72 ARG HG2 H 1.251 . 2 478 . 72 ARG HG3 H 1.203 . 2 479 . 72 ARG N N 122.749 . 1 480 . 73 CYS H H 8.62 . 1 481 . 73 CYS HA H 3.36 . 1 482 . 73 CYS HB3 H 2.298 . 2 483 . 73 CYS HB2 H 2.608 . 2 484 . 73 CYS N N 126.288 . 1 485 . 74 GLU H H 8.74 . 1 486 . 74 GLU HA H 4.98 . 1 487 . 74 GLU HB3 H 1.793 . 2 488 . 74 GLU HB2 H 2.213 . 2 489 . 74 GLU HG2 H 1.657 . 1 490 . 74 GLU HG3 H 1.657 . 1 491 . 74 GLU N N 126.343 . 1 492 . 75 GLY H H 9.07 . 1 493 . 75 GLY HA2 H 5.23 . 2 494 . 75 GLY HA3 H 2.91 . 2 495 . 75 GLY N N 109.069 . 1 496 . 76 ARG H H 8.91 . 1 497 . 76 ARG HA H 5.33 . 1 498 . 76 ARG HB3 H 1.548 . 2 499 . 76 ARG HB2 H 1.599 . 2 500 . 76 ARG HG2 H 1.735 . 1 501 . 76 ARG HG3 H 1.735 . 1 502 . 76 ARG HD2 H 3.028 . 1 503 . 76 ARG HD3 H 3.028 . 1 504 . 76 ARG HE H 7.513 . 1 505 . 76 ARG N N 118.184 . 1 506 . 76 ARG NE N 122.946 . 1 507 . 77 ILE H H 8.29 . 1 508 . 77 ILE HA H 4.37 . 1 509 . 77 ILE HB H 1.648 . 1 510 . 77 ILE HG12 H 0.703 . 1 511 . 77 ILE HG13 H 0.703 . 1 512 . 77 ILE HG2 H 0.739 . 1 513 . 77 ILE N N 117.638 . 1 514 . 78 LEU H H 8.76 . 1 515 . 78 LEU HA H 4.03 . 1 516 . 78 LEU HB3 H 1.690 . 2 517 . 78 LEU HB2 H 1.531 . 2 518 . 78 LEU HG H 1.600 . 1 519 . 78 LEU HD1 H 0.822 . 2 520 . 78 LEU HD2 H 0.886 . 2 521 . 78 LEU N N 127.372 . 1 522 . 79 ALA H H 8.92 . 1 523 . 79 ALA HA H 4.10 . 1 524 . 79 ALA HB H 1.329 . 1 525 . 79 ALA N N 117.085 . 1 526 . 80 ARG H H 6.93 . 1 527 . 80 ARG HA H 4.52 . 1 528 . 80 ARG HB3 H 1.306 . 2 529 . 80 ARG HB2 H 2.164 . 2 530 . 80 ARG HG2 H 1.439 . 2 531 . 80 ARG HG3 H 1.474 . 2 532 . 80 ARG HD2 H 3.111 . 2 533 . 80 ARG HD3 H 3.052 . 2 534 . 80 ARG HE H 7.327 . 1 535 . 80 ARG N N 118.552 . 1 536 . 80 ARG NE N 122.165 . 1 537 . 81 GLY H H 7.82 . 1 538 . 81 GLY HA2 H 3.94 . 2 539 . 81 GLY HA3 H 3.87 . 2 540 . 81 GLY N N 106.869 . 1 541 . 82 GLU H H 7.01 . 1 542 . 82 GLU HA H 4.49 . 1 543 . 82 GLU HB3 H 1.610 . 2 544 . 82 GLU HB2 H 1.870 . 2 545 . 82 GLU HG2 H 2.083 . 1 546 . 82 GLU HG3 H 2.083 . 1 547 . 82 GLU N N 115.247 . 1 548 . 83 ILE H H 8.57 . 1 549 . 83 ILE HA H 5.05 . 1 550 . 83 ILE HB H 1.725 . 1 551 . 83 ILE HG2 H 0.849 . 1 552 . 83 ILE HD1 H 0.754 . 1 553 . 83 ILE N N 120.899 . 1 554 . 84 ASN H H 9.11 . 1 555 . 84 ASN HA H 4.98 . 1 556 . 84 ASN HB3 H 2.570 . 2 557 . 84 ASN HB2 H 2.884 . 2 558 . 84 ASN HD21 H 7.821 . 2 559 . 84 ASN HD22 H 7.142 . 2 560 . 84 ASN N N 121.434 . 1 561 . 84 ASN ND2 N 107.894 . 1 562 . 85 PHE H H 8.13 . 1 563 . 85 PHE HA H 5.81 . 1 564 . 85 PHE HB3 H 2.880 . 2 565 . 85 PHE HB2 H 2.601 . 2 566 . 85 PHE HD1 H 6.643 . 1 567 . 85 PHE HD2 H 6.643 . 1 568 . 85 PHE HE1 H 7.211 . 1 569 . 85 PHE HE2 H 7.211 . 1 570 . 85 PHE N N 115.564 . 1 571 . 86 LYS H H 8.24 . 1 572 . 86 LYS HA H 4.13 . 1 573 . 86 LYS HB3 H 1.119 . 2 574 . 86 LYS HB2 H 0.461 . 2 575 . 86 LYS HG2 H 0.726 . 2 576 . 86 LYS HG3 H 0.813 . 2 577 . 86 LYS HD2 H 1.495 . 1 578 . 86 LYS HD3 H 1.495 . 1 579 . 86 LYS HE2 H 2.792 . 2 580 . 86 LYS HE3 H 2.915 . 2 581 . 86 LYS N N 117.972 . 1 582 . 87 ASP H H 8.62 . 1 583 . 87 ASP HA H 5.24 . 1 584 . 87 ASP HB3 H 2.511 . 2 585 . 87 ASP HB2 H 2.253 . 2 586 . 87 ASP N N 123.804 . 1 587 . 88 ILE H H 9.51 . 1 588 . 88 ILE HA H 4.14 . 1 589 . 88 ILE HB H 2.148 . 1 590 . 88 ILE HG12 H 0.978 . 1 591 . 88 ILE HG13 H 0.978 . 1 592 . 88 ILE HG2 H 1.105 . 1 593 . 88 ILE HD1 H 1.016 . 1 594 . 88 ILE N N 125.114 . 1 595 . 89 GLN H H 9.03 . 1 596 . 89 GLN HA H 4.55 . 1 597 . 89 GLN HB3 H 1.898 . 2 598 . 89 GLN HB2 H 1.940 . 2 599 . 89 GLN HG2 H 2.251 . 2 600 . 89 GLN HG3 H 2.304 . 2 601 . 89 GLN HE21 H 7.460 . 2 602 . 89 GLN HE22 H 6.889 . 2 603 . 89 GLN N N 126.945 . 1 604 . 89 GLN NE2 N 109.204 . 1 605 . 90 VAL H H 9.24 . 1 606 . 90 VAL HA H 5.05 . 1 607 . 90 VAL HB H 2.390 . 1 608 . 90 VAL HG1 H 0.779 . 2 609 . 90 VAL HG2 H 0.932 . 2 610 . 90 VAL N N 127.337 . 1 611 . 91 ILE H H 8.70 . 1 612 . 91 ILE HA H 4.40 . 1 613 . 91 ILE HB H 1.488 . 1 614 . 91 ILE HG12 H 1.056 . 1 615 . 91 ILE HG13 H 1.056 . 1 616 . 91 ILE HG2 H 0.839 . 1 617 . 91 ILE HD1 H 0.736 . 1 618 . 91 ILE N N 129.083 . 1 619 . 92 VAL H H 9.19 . 1 620 . 92 VAL HB H 1.879 . 1 621 . 92 VAL HG1 H 0.777 . 2 622 . 92 VAL HG2 H 0.619 . 2 623 . 92 VAL N N 125.659 . 1 stop_ save_