data_4174 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Assignments of the Mg2+-Loaded State of the N-Terminal Domain of Calmodulin ; _BMRB_accession_number 4174 _BMRB_flat_file_name bmr4174.str _Entry_type original _Submission_date 1998-08-11 _Accession_date 1998-08-11 _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 Malmendal Anders . . 2 Evenas Johan . . 3 Thulin Eva . . 4 Gippert Garry P. . 5 Drakenberg Torbjorn . . 6 Forsen Sture . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 455 "15N chemical shifts" 84 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2000-04-03 original author . stop_ _Original_release_date 2000-04-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; When Size is Important: Accommodation of Magnesium in a Calcium Binding Regulatory Domain ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 9748232 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Malmendal Anders . . 2 Evenas Johan . . 3 Thulin Eva . . 4 Gippert Garry P. . 5 Drakenberg Torbjorn . . 6 Forsen Sture . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_name_full 'Journal of Biological Chemistry' _Journal_volume 273 _Journal_issue 44 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 28994 _Page_last 29001 _Year 1998 _Details . save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; _Citation_title '1H, 13C and 15N chemical shift referencing in biomolecular NMR.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 8589602 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wishart 'D S' S. . 2 Bigam 'C G' G. . 3 Yao J . . 4 Abildgaard F . . 5 Dyson 'H J' J. . 6 Oldfield E . . 7 Markley 'J L' L. . 8 Sykes 'B D' D. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 6 _Journal_issue 2 _Journal_CSD . _Book_title . _Book_chapter_title . _Book_volume . _Book_series . _Book_publisher . _Book_publisher_city . _Book_ISBN . _Conference_title . _Conference_site . _Conference_state_province . _Conference_country . _Conference_start_date . _Conference_end_date . _Conference_abstract_number . _Thesis_institution . _Thesis_institution_city . _Thesis_institution_country . _Page_first 135 _Page_last 140 _Year 1995 _Details ; A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here. ; save_ ################################## # Molecular system description # ################################## save_system_TR1C _Saveframe_category molecular_system _Mol_system_name 'N-terminal domain of calmodulin' _Abbreviation_common TR1C _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TR1C $TR1C Mg $MG 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_TR1C _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal domain of calmodulin' _Abbreviation_common TR1C _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 81 _Mol_residue_sequence ; MADQLTEEQIAEFKEAFSLF DKDGDGTITTKELGTVMRSL GQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDT D ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 0 MET 2 1 ALA 3 2 ASP 4 3 GLN 5 4 LEU 6 5 THR 7 6 GLU 8 7 GLU 9 8 GLN 10 9 ILE 11 10 ALA 12 11 GLU 13 12 PHE 14 13 LYS 15 14 GLU 16 15 ALA 17 16 PHE 18 17 SER 19 18 LEU 20 19 PHE 21 20 ASP 22 21 LYS 23 22 ASP 24 23 GLY 25 24 ASP 26 25 GLY 27 26 THR 28 27 ILE 29 28 THR 30 29 THR 31 30 LYS 32 31 GLU 33 32 LEU 34 33 GLY 35 34 THR 36 35 VAL 37 36 MET 38 37 ARG 39 38 SER 40 39 LEU 41 40 GLY 42 41 GLN 43 42 ASN 44 43 PRO 45 44 THR 46 45 GLU 47 46 ALA 48 47 GLU 49 48 LEU 50 49 GLN 51 50 ASP 52 51 MET 53 52 ILE 54 53 ASN 55 54 GLU 56 55 VAL 57 56 ASP 58 57 ALA 59 58 ASP 60 59 GLY 61 60 ASN 62 61 GLY 63 62 THR 64 63 ILE 65 64 ASP 66 65 PHE 67 66 PRO 68 67 GLU 69 68 PHE 70 69 LEU 71 70 THR 72 71 MET 73 72 MET 74 73 ALA 75 74 ARG 76 75 LYS 77 76 MET 78 77 LYS 79 78 ASP 80 79 THR 81 80 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-17 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 18082 "Calmodulin N-Lobe" 98.77 80 100.00 100.00 2.14e-48 BMRB 18302 "CaM N-terminal domain" 95.06 77 100.00 100.00 2.13e-46 PDB 1AK8 "Nmr Solution Structure Of Cerium-Loaded Calmodulin Amino- Terminal Domain (Ce2-Tr1c), 23 Structures" 92.59 76 100.00 100.00 8.09e-45 PDB 1F70 "Refined Solution Structure Of Calmodulin N-Terminal Domain" 93.83 76 100.00 100.00 1.15e-45 PDB 1J7O "Solution Structure Of Calcium-calmodulin N-terminal Domain" 92.59 76 100.00 100.00 6.73e-45 PDB 1SW8 "Solution Structure Of The N-Terminal Domain Of Human N60d Calmodulin Refined With Paramagnetism Based Strategy" 97.53 79 98.73 100.00 8.43e-47 PDB 2KUG "Halothane Binds To Druggable Sites In Calcium-calmodulin: Solution Structure Of Halothane-cam N-terminal Domain" 93.83 76 100.00 100.00 1.15e-45 PDB 2LLO "Solution Nmr-derived Structure Of Calmodulin N-lobe Bound With Er Alpha Peptide" 98.77 80 100.00 100.00 2.14e-48 PDB 2LQC "Nmr Solution Structure Of A Ca2+-Calmodulin With A Binding Motif (Nscate) Peptide From The N-Terminal Cytoplasmic Domain Of The" 95.06 77 100.00 100.00 2.13e-46 PDB 2PQ3 "N-Terminal Calmodulin Zn-Trapped Intermediate" 93.83 76 100.00 100.00 1.15e-45 PDB 3B32 "Crystal Structure Of Calcium-Saturated Calmodulin N-Terminal Domain Fragment, Residues 1-75" 92.59 75 100.00 100.00 7.88e-45 PDB 3IFK "Crystal Structure Of Calcium-Saturated Calmodulin N-Terminal Domain Fragment, Residues 1-90" 98.77 90 100.00 100.00 1.88e-48 PDB 3UCT "Structure Of Mn2+-Bound N-Terminal Domain Of Calmodulin In The Presence Of Zn2+" 97.53 79 100.00 100.00 1.04e-47 PDB 3UCW "Structure Of Mg2+ Bound N-Terminal Domain Of Calmodulin" 97.53 79 100.00 100.00 1.04e-47 PDB 3UCY "Structure Of Mg2+ Bound N-Terminal Domain Of Calmodulin In The Presence Of Zn2+" 97.53 79 100.00 100.00 1.04e-47 PDB 4Q57 "Crystal Structure Of The Plectin 1a Actin-binding Domain/n-terminal Domain Of Calmodulin Complex" 80.25 65 100.00 100.00 2.25e-37 EMBL CAA29381 "unnamed protein product [Drosophila melanogaster]" 71.60 58 100.00 100.00 3.48e-31 EMBL CAB65357 "putative calmodulin [Phallusia mammillata]" 61.73 71 100.00 100.00 2.95e-26 EMBL CCD82979 "putative calmodulin [Schistosoma mansoni]" 100.00 154 100.00 100.00 1.11e-48 EMBL CUA69889 "Calmodulin [Rhizoctonia solani]" 100.00 137 97.53 100.00 4.34e-48 GB AAH53790 "Cam protein, partial [Xenopus laevis]" 100.00 143 100.00 100.00 4.86e-51 GB ABY16748 "calmodulin 1 [Crassostrea ariakensis]" 64.20 52 100.00 100.00 1.39e-27 GB ABY16749 "calmodulin 2 [Crassostrea gigas]" 64.20 52 98.08 100.00 2.24e-27 GB ABY16752 "calmodulin 1 [Crassostrea sikamea]" 64.20 52 100.00 100.00 1.39e-27 GB ACH46202 "putative calmodulin variant 1 [Taeniopygia guttata]" 100.00 84 100.00 100.00 2.57e-49 REF XP_001869424 "calmodulin [Culex quinquefasciatus]" 72.84 110 100.00 100.00 7.89e-32 REF XP_001995129 "GH22800 [Drosophila grimshawi]" 98.77 122 100.00 100.00 3.93e-48 REF XP_002772218 "calmodulin, putative [Perkinsus marinus ATCC 50983]" 76.54 85 100.00 100.00 5.62e-35 REF XP_006032607 "PREDICTED: probable calcium-binding protein CML28 [Alligator sinensis]" 59.26 144 97.92 100.00 1.06e-23 REF XP_006137175 "PREDICTED: neo-calmodulin-like, partial [Pelodiscus sinensis]" 85.19 80 100.00 100.00 1.02e-40 stop_ save_ ############# # Ligands # ############# save_MG _Saveframe_category ligand _Mol_type non-polymer _Name_common "MG (MAGNESIUM ION)" _BMRB_code . _PDB_code MG _Molecular_mass 24.305 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Tue Jun 14 12:24:59 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons MG MG MG . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $TR1C human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $TR1C . . . . . . 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 $TR1C 4.0 mM . D2O 10 % . H2O 90 % . KCL 10 mM . Azide 100 uM . stop_ save_ save_sample_two _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $TR1C 4.0 mM [U-15N] D2O 10 % . H2O 90 % . KCL 10 mM . Azide 100 uM . stop_ 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_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 0.005 n/a pH 7.2 0.05 n/a temperature 298 1 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 H2O H 1 protons ppm 4.7548 internal direct . . . . . DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 $citation_one 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 $sample_two stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name TR1C _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 . 3 ASP HA H 4.57 0.005 1 2 . 3 ASP HB2 H 2.67 0.005 2 3 . 3 ASP HB3 H 2.56 0.005 2 4 . 3 ASP N N 119.9 0.05 1 5 . 4 GLN HA H 4.38 0.005 1 6 . 4 GLN HB2 H 2.08 0.005 2 7 . 4 GLN HB3 H 1.93 0.005 2 8 . 4 GLN HE21 H 7.54 0.005 2 9 . 4 GLN HE22 H 6.84 0.005 2 10 . 4 GLN HG2 H 2.31 0.005 1 11 . 4 GLN HG3 H 2.31 0.005 1 12 . 4 GLN H H 8.18 0.005 1 13 . 4 GLN N N 118.2 0.05 1 14 . 4 GLN NE2 N 112.4 0.05 1 15 . 5 LEU HA H 4.59 0.005 1 16 . 5 LEU HB2 H 1.7 0.005 2 17 . 5 LEU HB3 H 1.39 0.005 2 18 . 5 LEU HD1 H 0.9 0.005 2 19 . 5 LEU HD2 H 0.86 0.005 2 20 . 5 LEU HG H 1.68 0.005 1 21 . 5 LEU H H 8.29 0.005 1 22 . 5 LEU N N 121.8 0.05 1 23 . 6 THR HA H 4.42 0.005 1 24 . 6 THR HB H 4.76 0.005 1 25 . 6 THR HG1 H 5.61 0.005 1 26 . 6 THR HG2 H 1.29 0.005 1 27 . 6 THR H H 8.76 0.005 1 28 . 6 THR N N 112.8 0.05 1 29 . 7 GLU HA H 3.91 0.005 1 30 . 7 GLU HB2 H 2.01 0.005 1 31 . 7 GLU HB3 H 2.01 0.005 1 32 . 7 GLU HG2 H 2.37 0.005 2 33 . 7 GLU HG3 H 2.3 0.005 2 34 . 7 GLU H H 9.01 0.005 1 35 . 7 GLU N N 120.2 0.05 1 36 . 8 GLU HA H 4.01 0.005 1 37 . 8 GLU HB2 H 2 0.005 2 38 . 8 GLU HB3 H 1.89 0.005 2 39 . 8 GLU HG2 H 2.33 0.005 2 40 . 8 GLU HG3 H 2.24 0.005 2 41 . 8 GLU H H 8.69 0.005 1 42 . 8 GLU N N 119.3 0.05 1 43 . 9 GLN HA H 3.74 0.005 1 44 . 9 GLN HB2 H 2 0.005 2 45 . 9 GLN HB3 H 1.36 0.005 2 46 . 9 GLN HE21 H 6.69 0.005 1 47 . 9 GLN HE22 H 7.58 0.005 1 48 . 9 GLN HG2 H 2.26 0.005 2 49 . 9 GLN HG3 H 2.22 0.005 2 50 . 9 GLN H H 7.7 0.005 1 51 . 9 GLN N N 120.4 0.05 1 52 . 9 GLN NE2 N 111.0 0.05 1 53 . 10 ILE HA H 3.43 0.005 1 54 . 10 ILE HB H 1.81 0.005 1 55 . 10 ILE HD1 H 0.78 0.005 1 56 . 10 ILE HG12 H 1.76 0.005 2 57 . 10 ILE HG13 H 0.91 0.005 2 58 . 10 ILE HG2 H 1.09 0.005 1 59 . 10 ILE H H 8.24 0.005 1 60 . 10 ILE N N 118.4 0.05 1 61 . 11 ALA HA H 4.12 0.005 1 62 . 11 ALA HB H 1.48 0.005 1 63 . 11 ALA H H 7.92 0.005 1 64 . 11 ALA N N 120.3 0.05 1 65 . 12 GLU HA H 4.11 0.005 1 66 . 12 GLU HB2 H 2.07 0.005 2 67 . 12 GLU HB3 H 1.99 0.005 2 68 . 12 GLU HG2 H 2.4 0.005 2 69 . 12 GLU HG3 H 2.17 0.005 2 70 . 12 GLU H H 7.77 0.005 1 71 . 12 GLU N N 120.1 0.05 1 72 . 13 PHE HA H 4.91 0.005 1 73 . 13 PHE HB2 H 3.6 0.005 2 74 . 13 PHE HB3 H 3.49 0.005 2 75 . 13 PHE HD1 H 7.07 0.005 1 76 . 13 PHE HD2 H 7.07 0.005 1 77 . 13 PHE HE1 H 7.25 0.005 1 78 . 13 PHE HE2 H 7.25 0.005 1 79 . 13 PHE H H 8.7 0.005 1 80 . 13 PHE HZ H 7.21 0.005 1 81 . 13 PHE N N 120.2 0.05 1 82 . 14 LYS HA H 3.79 0.005 1 83 . 14 LYS HB2 H 1.82 0.005 2 84 . 14 LYS HB3 H 1.93 0.005 2 85 . 14 LYS HD2 H 1.3 0.005 2 86 . 14 LYS HD3 H 1.22 0.005 2 87 . 14 LYS HE2 H 2.64 0.005 1 88 . 14 LYS HE3 H 2.64 0.005 1 89 . 14 LYS HG2 H 1.12 0.005 2 90 . 14 LYS HG3 H 0.77 0.005 2 91 . 14 LYS H H 9.3 0.005 1 92 . 14 LYS N N 121.8 0.05 1 93 . 15 GLU HA H 4.01 0.005 1 94 . 15 GLU HB2 H 2.16 0.005 1 95 . 15 GLU HB3 H 2.16 0.005 1 96 . 15 GLU HG2 H 2.34 0.005 2 97 . 15 GLU HG3 H 2.28 0.005 2 98 . 15 GLU H H 8.1 0.005 1 99 . 15 GLU N N 120.5 0.05 1 100 . 16 ALA HA H 4.31 0.005 1 101 . 16 ALA HB H 1.7 0.005 1 102 . 16 ALA H H 7.71 0.005 1 103 . 16 ALA N N 120.9 0.05 1 104 . 17 PHE HA H 3.68 0.005 1 105 . 17 PHE HB2 H 2.91 0.005 2 106 . 17 PHE HB3 H 3.21 0.005 2 107 . 17 PHE HD1 H 6.54 0.005 1 108 . 17 PHE HD2 H 6.54 0.005 1 109 . 17 PHE HE1 H 6.84 0.005 1 110 . 17 PHE HE2 H 6.84 0.005 1 111 . 17 PHE H H 8.57 0.005 1 112 . 17 PHE HZ H 7.38 0.005 1 113 . 17 PHE N N 117.5 0.05 1 114 . 18 SER HA H 4.2 0.005 1 115 . 18 SER HB2 H 4 0.005 1 116 . 18 SER HB3 H 4 0.005 1 117 . 18 SER H H 8.52 0.005 1 118 . 18 SER N N 111.5 0.05 1 119 . 19 LEU HA H 3.88 0.005 1 120 . 19 LEU HB2 H 1.68 0.005 2 121 . 19 LEU HB3 H 1.29 0.005 2 122 . 19 LEU HD1 H 0.8 0.005 2 123 . 19 LEU HD2 H 0.71 0.005 2 124 . 19 LEU HG H 1.34 0.005 1 125 . 19 LEU H H 7.51 0.005 1 126 . 19 LEU N N 121.1 0.05 1 127 . 20 PHE HA H 4.26 0.005 1 128 . 20 PHE HB2 H 3 0.005 2 129 . 20 PHE HB3 H 2.37 0.005 2 130 . 20 PHE HD1 H 7.4 0.005 1 131 . 20 PHE HD2 H 7.4 0.005 1 132 . 20 PHE HE1 H 7.32 0.005 1 133 . 20 PHE HE2 H 7.32 0.005 1 134 . 20 PHE H H 7.11 0.005 1 135 . 20 PHE HZ H 7.19 0.005 1 136 . 20 PHE N N 113.7 0.05 1 137 . 21 ASP HA H 5.15 0.005 1 138 . 21 ASP HB2 H 2.75 0.005 2 139 . 21 ASP HB3 H 1.98 0.005 2 140 . 21 ASP H H 7.61 0.005 1 141 . 21 ASP N N 122.2 0.05 1 142 . 22 LYS HA H 3.95 0.005 1 143 . 22 LYS HB2 H 1.83 0.005 1 144 . 22 LYS HB3 H 1.83 0.005 1 145 . 22 LYS HD2 H 1.66 0.005 1 146 . 22 LYS HD3 H 1.66 0.005 1 147 . 22 LYS HE2 H 2.98 0.005 1 148 . 22 LYS HE3 H 2.98 0.005 1 149 . 22 LYS HG2 H 1.47 0.005 2 150 . 22 LYS HG3 H 1.4 0.005 2 151 . 22 LYS H H 7.76 0.005 1 152 . 22 LYS N N 122.8 0.05 1 153 . 23 ASP HA H 4.51 0.005 1 154 . 23 ASP HB2 H 2.96 0.005 2 155 . 23 ASP HB3 H 2.62 0.005 2 156 . 23 ASP H H 8.07 0.005 1 157 . 23 ASP N N 114.1 0.05 1 158 . 24 GLY HA2 H 3.84 0.005 1 159 . 24 GLY HA3 H 3.84 0.005 1 160 . 24 GLY H H 7.72 0.005 1 161 . 24 GLY N N 108.5 0.05 1 162 . 25 ASP HA H 4.59 0.005 1 163 . 25 ASP HB2 H 3.02 0.005 2 164 . 25 ASP HB3 H 2.48 0.005 2 165 . 25 ASP H H 8.29 0.005 1 166 . 25 ASP N N 118.3 0.05 1 167 . 26 GLY HA2 H 4.4 0.005 2 168 . 26 GLY HA3 H 3.72 0.005 2 169 . 26 GLY H H 10.63 0.005 1 170 . 26 GLY N N 114.1 0.05 1 171 . 27 THR HA H 5.51 0.005 1 172 . 27 THR HB H 3.91 0.005 1 173 . 27 THR HG2 H 1.15 0.005 1 174 . 27 THR H H 8.22 0.005 1 175 . 27 THR N N 113.8 0.05 1 176 . 28 ILE HA H 5.01 0.005 1 177 . 28 ILE HB H 1.99 0.005 1 178 . 28 ILE HD1 H 0.22 0.005 1 179 . 28 ILE HG12 H 1.15 0.005 2 180 . 28 ILE HG13 H 0.84 0.005 2 181 . 28 ILE HG2 H 0.04 0.005 1 182 . 28 ILE H H 9.06 0.005 1 183 . 28 ILE N N 121.4 0.05 1 184 . 29 THR HA H 5.17 0.005 1 185 . 29 THR HB H 4.69 0.005 1 186 . 29 THR HG2 H 1.27 0.005 1 187 . 29 THR H H 8.3 0.005 1 188 . 29 THR N N 110.2 0.05 1 189 . 30 THR HA H 3.74 0.005 1 190 . 30 THR HB H 4.2 0.005 1 191 . 30 THR HG2 H 1.08 0.005 1 192 . 30 THR H H 8.22 0.005 1 193 . 30 THR N N 111.6 0.05 1 194 . 31 LYS HA H 4.11 0.005 1 195 . 31 LYS HB2 H 1.81 0.005 1 196 . 31 LYS HB3 H 1.81 0.005 1 197 . 31 LYS HD2 H 1.67 0.005 1 198 . 31 LYS HD3 H 1.67 0.005 1 199 . 31 LYS HE2 H 2.98 0.005 1 200 . 31 LYS HE3 H 2.98 0.005 1 201 . 31 LYS HG2 H 1.49 0.005 1 202 . 31 LYS HG3 H 1.49 0.005 1 203 . 31 LYS H H 7.66 0.005 1 204 . 31 LYS N N 119.4 0.05 1 205 . 32 GLU HA H 4.21 0.005 1 206 . 32 GLU HB2 H 2.14 0.005 2 207 . 32 GLU HB3 H 1.81 0.005 2 208 . 32 GLU HG2 H 2.32 0.005 1 209 . 32 GLU HG3 H 2.32 0.005 1 210 . 32 GLU H H 7.49 0.005 1 211 . 32 GLU N N 118.0 0.05 1 212 . 33 LEU HA H 3.74 0.005 1 213 . 33 LEU HB2 H 1.95 0.005 2 214 . 33 LEU HB3 H 1.35 0.005 2 215 . 33 LEU HD1 H 1.01 0.005 2 216 . 33 LEU HD2 H 0.9 0.005 2 217 . 33 LEU HG H 1.51 0.005 1 218 . 33 LEU H H 7.56 0.005 1 219 . 33 LEU N N 120.5 0.05 1 220 . 34 GLY HA2 H 3.84 0.005 2 221 . 34 GLY HA3 H 3.46 0.005 2 222 . 34 GLY H H 8.64 0.005 1 223 . 34 GLY N N 105.6 0.05 1 224 . 35 THR HA H 3.73 0.005 1 225 . 35 THR HB H 3.85 0.005 1 226 . 35 THR HG2 H 1.05 0.005 1 227 . 35 THR H H 7.48 0.005 1 228 . 35 THR N N 117.1 0.05 1 229 . 36 VAL HA H 3.21 0.005 1 230 . 36 VAL HB H 1.84 0.005 1 231 . 36 VAL HG1 H 0.66 0.005 2 232 . 36 VAL HG2 H 0.47 0.005 2 233 . 36 VAL H H 7.89 0.005 1 234 . 36 VAL N N 122.8 0.05 1 235 . 37 MET HA H 3.98 0.005 1 236 . 37 MET HB2 H 2.06 0.005 2 237 . 37 MET HB3 H 1.84 0.005 2 238 . 37 MET HG2 H 2.69 0.005 2 239 . 37 MET HG3 H 2.51 0.005 2 240 . 37 MET H H 8.38 0.005 1 241 . 37 MET N N 118.3 0.05 1 242 . 38 ARG HA H 4.65 0.005 1 243 . 38 ARG HB2 H 1.86 0.005 1 244 . 38 ARG HB3 H 1.86 0.005 1 245 . 38 ARG HD2 H 3.25 0.005 2 246 . 38 ARG HD3 H 3.07 0.005 2 247 . 38 ARG HG2 H 1.8 0.005 1 248 . 38 ARG HG3 H 1.8 0.005 1 249 . 38 ARG H H 8.39 0.005 1 250 . 38 ARG N N 119.3 0.05 1 251 . 39 SER HA H 4.41 0.005 1 252 . 39 SER HB2 H 4.22 0.005 2 253 . 39 SER HB3 H 4.17 0.005 2 254 . 39 SER HG H 5.86 0.005 1 255 . 39 SER H H 8.04 0.005 1 256 . 39 SER N N 119.1 0.05 1 257 . 40 LEU HA H 4.59 0.005 1 258 . 40 LEU HB2 H 1.91 0.005 1 259 . 40 LEU HB3 H 1.91 0.005 1 260 . 40 LEU HD1 H 1.14 0.005 2 261 . 40 LEU HD2 H 1.04 0.005 2 262 . 40 LEU HG H 1.87 0.005 1 263 . 40 LEU H H 7.32 0.005 1 264 . 40 LEU N N 121.0 0.05 1 265 . 41 GLY HA2 H 4.25 0.005 2 266 . 41 GLY HA3 H 3.81 0.005 2 267 . 41 GLY H H 7.93 0.005 1 268 . 41 GLY N N 107.3 0.05 1 269 . 42 GLN HA H 4.42 0.005 1 270 . 42 GLN HB2 H 2.06 0.005 2 271 . 42 GLN HB3 H 1.56 0.005 2 272 . 42 GLN HE21 H 6.63 0.005 1 273 . 42 GLN HE22 H 7.49 0.005 1 274 . 42 GLN HG2 H 2.19 0.005 1 275 . 42 GLN HG3 H 2.19 0.005 1 276 . 42 GLN H H 7.75 0.005 1 277 . 42 GLN N N 117.9 0.05 1 278 . 42 GLN NE2 N 111.0 0.05 1 279 . 43 ASN HA H 5.14 0.005 1 280 . 43 ASN HB2 H 2.73 0.005 2 281 . 43 ASN HB3 H 2.5 0.005 2 282 . 43 ASN HD21 H 6.71 0.005 1 283 . 43 ASN HD22 H 7.5 0.005 1 284 . 43 ASN H H 8.65 0.005 1 285 . 43 ASN N N 116.6 0.05 1 286 . 43 ASN ND2 N 112.1 0.05 1 287 . 44 PRO HA H 4.7 0.005 1 288 . 44 PRO HB2 H 2.07 0.005 1 289 . 44 PRO HB3 H 2.07 0.005 1 290 . 44 PRO HD2 H 3.64 0.005 2 291 . 44 PRO HD3 H 3.28 0.005 2 292 . 44 PRO HG2 H 1.92 0.005 1 293 . 44 PRO HG3 H 1.92 0.005 1 294 . 45 THR HA H 4.39 0.005 1 295 . 45 THR HB H 4.7 0.005 1 296 . 45 THR HG1 H 5.71 0.005 1 297 . 45 THR HG2 H 1.34 0.005 1 298 . 45 THR H H 8.73 0.005 1 299 . 45 THR N N 113.1 0.05 1 300 . 46 GLU HA H 3.97 0.005 1 301 . 46 GLU HB2 H 2.02 0.005 1 302 . 46 GLU HB3 H 2.02 0.005 1 303 . 46 GLU HG2 H 2.34 0.005 2 304 . 46 GLU HG3 H 2.29 0.005 2 305 . 46 GLU H H 8.84 0.005 1 306 . 46 GLU N N 120.6 0.05 1 307 . 47 ALA HA H 4.08 0.005 1 308 . 47 ALA HB H 1.36 0.005 1 309 . 47 ALA H H 8.31 0.005 1 310 . 47 ALA N N 120.9 0.05 1 311 . 48 GLU HA H 4 0.005 1 312 . 48 GLU HB2 H 2.25 0.005 2 313 . 48 GLU HB3 H 1.85 0.005 2 314 . 48 GLU HG2 H 2.33 0.005 1 315 . 48 GLU HG3 H 2.33 0.005 1 316 . 48 GLU H H 7.73 0.005 1 317 . 48 GLU N N 119.0 0.05 1 318 . 49 LEU HA H 4.03 0.005 1 319 . 49 LEU HB2 H 1.72 0.005 2 320 . 49 LEU HB3 H 1.57 0.005 2 321 . 49 LEU HD1 H 0.8 0.005 1 322 . 49 LEU HD2 H 0.8 0.005 1 323 . 49 LEU HG H 1.6 0.005 1 324 . 49 LEU H H 8.37 0.005 1 325 . 49 LEU N N 120.2 0.05 1 326 . 50 GLN HA H 3.87 0.005 1 327 . 50 GLN HB2 H 2.13 0.005 1 328 . 50 GLN HB3 H 2.13 0.005 1 329 . 50 GLN HE21 H 6.87 0.005 1 330 . 50 GLN HE22 H 7.47 0.005 1 331 . 50 GLN HG2 H 2.4 0.005 1 332 . 50 GLN HG3 H 2.4 0.005 1 333 . 50 GLN H H 8.07 0.005 1 334 . 50 GLN N N 117.5 0.05 1 335 . 50 GLN NE2 N 113.3 0.05 1 336 . 51 ASP HA H 4.41 0.005 1 337 . 51 ASP HB2 H 2.76 0.005 2 338 . 51 ASP HB3 H 2.66 0.005 2 339 . 51 ASP H H 7.83 0.005 1 340 . 51 ASP N N 119.0 0.05 1 341 . 52 MET HA H 4.02 0.005 1 342 . 52 MET HB2 H 2.27 0.005 2 343 . 52 MET HB3 H 2.04 0.005 2 344 . 52 MET HG2 H 2.8 0.005 2 345 . 52 MET HG3 H 2.55 0.005 2 346 . 52 MET H H 7.94 0.005 1 347 . 52 MET N N 119.1 0.05 1 348 . 53 ILE HA H 3.46 0.005 1 349 . 53 ILE HB H 1.85 0.005 1 350 . 53 ILE HD1 H 1.75 0.005 1 351 . 53 ILE HG12 H 0.9 0.005 2 352 . 53 ILE HG13 H 0.78 0.005 2 353 . 53 ILE HG2 H 0.89 0.005 1 354 . 53 ILE H H 8.35 0.005 1 355 . 53 ILE N N 119.3 0.05 1 356 . 54 ASN HA H 4.36 0.005 1 357 . 54 ASN HB2 H 2.93 0.005 2 358 . 54 ASN HB3 H 2.8 0.005 2 359 . 54 ASN HD21 H 6.91 0.005 1 360 . 54 ASN HD22 H 7.77 0.005 1 361 . 54 ASN H H 8.34 0.005 1 362 . 54 ASN N N 117.4 0.05 1 363 . 54 ASN ND2 N 111.7 0.05 1 364 . 55 GLU HA H 4.11 0.005 1 365 . 55 GLU HB2 H 2.09 0.005 1 366 . 55 GLU HB3 H 2.09 0.005 1 367 . 55 GLU HG2 H 2.38 0.005 2 368 . 55 GLU HG3 H 2.17 0.005 2 369 . 55 GLU H H 7.49 0.005 1 370 . 55 GLU N N 117.0 0.05 1 371 . 56 VAL HA H 4.38 0.005 1 372 . 56 VAL HB H 2.24 0.005 1 373 . 56 VAL HG1 H 0.95 0.005 2 374 . 56 VAL HG2 H 0.99 0.005 2 375 . 56 VAL H H 7.64 0.005 1 376 . 56 VAL N N 112.5 0.05 1 377 . 57 ASP HA H 5.19 0.005 1 378 . 57 ASP HB2 H 2.82 0.005 2 379 . 57 ASP HB3 H 2.27 0.005 2 380 . 57 ASP H H 8.42 0.005 1 381 . 57 ASP N N 122.6 0.05 1 382 . 58 ALA HA H 4.12 0.005 1 383 . 58 ALA HB H 1.44 0.005 1 384 . 58 ALA H H 7.86 0.005 1 385 . 58 ALA N N 125.3 0.05 1 386 . 59 ASP HA H 4.49 0.005 1 387 . 59 ASP HB2 H 2.83 0.005 2 388 . 59 ASP HB3 H 2.68 0.005 2 389 . 59 ASP H H 8.29 0.005 1 390 . 59 ASP N N 113.7 0.05 1 391 . 60 GLY HA2 H 3.91 0.005 2 392 . 60 GLY HA3 H 3.81 0.005 2 393 . 60 GLY H H 7.84 0.005 1 394 . 60 GLY N N 108.6 0.05 1 395 . 61 ASN HA H 4.66 0.005 1 396 . 61 ASN HB2 H 2.93 0.005 2 397 . 61 ASN HB3 H 2.79 0.005 2 398 . 61 ASN H H 8.78 0.005 1 399 . 61 ASN N N 118.7 0.05 1 400 . 61 ASN ND2 N 114.5 0.05 1 401 . 62 GLY HA2 H 4.1 0.005 2 402 . 62 GLY HA3 H 3.78 0.005 2 403 . 62 GLY H H 10.42 0.005 1 404 . 62 GLY N N 111.8 0.05 1 405 . 63 THR HA H 5.04 0.005 1 406 . 63 THR HB H 4.12 0.005 1 407 . 63 THR HG2 H 1.05 0.005 1 408 . 63 THR H H 7.44 0.005 1 409 . 63 THR N N 108.7 0.05 1 410 . 64 ILE HA H 4.71 0.005 1 411 . 64 ILE HB H 1.78 0.005 1 412 . 64 ILE HD1 H 0.84 0.005 1 413 . 64 ILE HG12 H 1.5 0.005 2 414 . 64 ILE HG13 H 1.08 0.005 2 415 . 64 ILE HG2 H 1.02 0.005 1 416 . 64 ILE H H 9.16 0.005 1 417 . 64 ILE N N 121.8 0.05 1 418 . 65 ASP HA H 5.75 0.005 1 419 . 65 ASP HB2 H 3.05 0.005 2 420 . 65 ASP HB3 H 2.76 0.005 2 421 . 65 ASP N N 125.6 0.05 1 422 . 66 PHE HA H 3.72 0.005 1 423 . 66 PHE HB2 H 2.26 0.005 2 424 . 66 PHE HB3 H 2.9 0.005 2 425 . 66 PHE HD1 H 6.54 0.005 1 426 . 66 PHE HD2 H 6.54 0.005 1 427 . 66 PHE HE1 H 7.16 0.005 1 428 . 66 PHE HE2 H 7.16 0.005 1 429 . 66 PHE H H 8.65 0.005 1 430 . 66 PHE HZ H 7.33 0.005 1 431 . 66 PHE N N 118.8 0.05 1 432 . 67 PRO HA H 3.84 0.005 1 433 . 67 PRO HB2 H 2.23 0.005 2 434 . 67 PRO HB3 H 1.89 0.005 2 435 . 67 PRO HD2 H 3.78 0.005 1 436 . 67 PRO HD3 H 3.78 0.005 1 437 . 67 PRO HG2 H 2.17 0.005 1 438 . 67 PRO HG3 H 2.17 0.005 1 439 . 68 GLU HA H 3.97 0.005 1 440 . 68 GLU HB2 H 2.6 0.005 2 441 . 68 GLU HB3 H 1.81 0.005 2 442 . 68 GLU HG2 H 2.3 0.005 2 443 . 68 GLU HG3 H 2.01 0.005 2 444 . 68 GLU H H 7.98 0.005 1 445 . 68 GLU N N 117.4 0.05 1 446 . 69 PHE HA H 4.06 0.005 1 447 . 69 PHE HB2 H 3.24 0.005 2 448 . 69 PHE HB3 H 3.05 0.005 2 449 . 69 PHE HD1 H 6.93 0.005 1 450 . 69 PHE HD2 H 6.93 0.005 1 451 . 69 PHE HE1 H 7.11 0.005 1 452 . 69 PHE HE2 H 7.11 0.005 1 453 . 69 PHE H H 8.43 0.005 1 454 . 69 PHE HZ H 6.97 0.005 1 455 . 69 PHE N N 122.2 0.05 1 456 . 70 LEU HA H 3.29 0.005 1 457 . 70 LEU HB2 H 1.37 0.005 2 458 . 70 LEU HB3 H 1.2 0.005 2 459 . 70 LEU HD1 H 0.73 0.005 2 460 . 70 LEU HD2 H 0.69 0.005 2 461 . 70 LEU HG H 0.95 0.005 1 462 . 70 LEU H H 8.43 0.005 1 463 . 70 LEU N N 118.8 0.05 1 464 . 71 THR HA H 3.75 0.005 1 465 . 71 THR HB H 4.24 0.005 1 466 . 71 THR HG2 H 1.16 0.005 1 467 . 71 THR H H 7.73 0.005 1 468 . 71 THR N N 115.5 0.05 1 469 . 72 MET HA H 3.93 0.005 1 470 . 72 MET HB2 H 2.03 0.005 2 471 . 72 MET HB3 H 1.93 0.005 2 472 . 72 MET HG2 H 2.56 0.005 2 473 . 72 MET HG3 H 2.36 0.005 2 474 . 72 MET H H 7.71 0.005 1 475 . 72 MET N N 121.0 0.05 1 476 . 73 MET HA H 4.02 0.005 1 477 . 73 MET HB2 H 1.41 0.005 2 478 . 73 MET HB3 H 1.23 0.005 2 479 . 73 MET HG2 H 1.14 0.005 2 480 . 73 MET HG3 H 0.86 0.005 2 481 . 73 MET H H 8 0.005 1 482 . 73 MET N N 117.6 0.05 1 483 . 74 ALA HA H 3.96 0.005 1 484 . 74 ALA HB H 1.4 0.005 1 485 . 74 ALA H H 8.3 0.005 1 486 . 74 ALA N N 121.3 0.05 1 487 . 75 ARG HA H 4.03 0.005 1 488 . 75 ARG HB2 H 1.89 0.005 1 489 . 75 ARG HB3 H 1.89 0.005 1 490 . 75 ARG HD2 H 3.13 0.005 1 491 . 75 ARG HD3 H 3.13 0.005 1 492 . 75 ARG HG2 H 1.76 0.005 2 493 . 75 ARG HG3 H 1.62 0.005 2 494 . 75 ARG H H 7.45 0.005 1 495 . 75 ARG N N 116.4 0.05 1 496 . 76 LYS HA H 4.2 0.005 1 497 . 76 LYS HB2 H 1.89 0.005 2 498 . 76 LYS HB3 H 1.76 0.005 2 499 . 76 LYS HD2 H 1.66 0.005 2 500 . 76 LYS HD3 H 1.57 0.005 2 501 . 76 LYS HE2 H 2.92 0.005 2 502 . 76 LYS HE3 H 2.82 0.005 2 503 . 76 LYS HG2 H 1.41 0.005 1 504 . 76 LYS HG3 H 1.41 0.005 1 505 . 76 LYS H H 7.72 0.005 1 506 . 76 LYS N N 118.3 0.05 1 507 . 77 MET HA H 4.34 0.005 1 508 . 77 MET HB2 H 2.18 0.005 2 509 . 77 MET HB3 H 2.02 0.005 2 510 . 77 MET HG2 H 2.63 0.005 1 511 . 77 MET HG3 H 2.63 0.005 1 512 . 77 MET H H 7.89 0.005 1 513 . 77 MET N N 117.3 0.05 1 514 . 78 LYS HA H 4.29 0.005 1 515 . 78 LYS HB2 H 1.84 0.005 1 516 . 78 LYS HB3 H 1.84 0.005 1 517 . 78 LYS HD2 H 1.66 0.005 1 518 . 78 LYS HD3 H 1.66 0.005 1 519 . 78 LYS HE2 H 2.98 0.005 1 520 . 78 LYS HE3 H 2.98 0.005 1 521 . 78 LYS HG2 H 1.47 0.005 1 522 . 78 LYS HG3 H 1.47 0.005 1 523 . 78 LYS H H 7.67 0.005 1 524 . 78 LYS N N 120.1 0.05 1 525 . 79 ASP HA H 4.69 0.005 1 526 . 79 ASP HB2 H 2.78 0.005 2 527 . 79 ASP HB3 H 2.64 0.005 2 528 . 79 ASP H H 8.2 0.005 1 529 . 79 ASP N N 121.2 0.05 1 530 . 80 THR HA H 4.36 0.005 1 531 . 80 THR HB H 4.3 0.005 1 532 . 80 THR HG2 H 1.19 0.005 1 533 . 80 THR H H 7.95 0.005 1 534 . 80 THR N N 113.3 0.05 1 535 . 81 ASP HA H 4.39 0.005 1 536 . 81 ASP HB2 H 2.67 0.005 2 537 . 81 ASP HB3 H 2.57 0.005 2 538 . 81 ASP H H 8.03 0.005 1 539 . 81 ASP N N 128.0 0.05 1 stop_ save_