data_6686 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H NMR assignments of the Ce2-TR1C complex at 298 K ; _BMRB_accession_number 6686 _BMRB_flat_file_name bmr6686.str _Entry_type new _Submission_date 2005-06-13 _Accession_date 2005-06-13 _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 Hutchinson John A Jr. stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 356 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-02-15 original author . stop_ _Original_release_date 2013-02-15 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure of the Paramagnetic Complex of the N-Terminal Domain of Calmodulin with Two Ce3+ Ions by 1H NMR. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 9305950 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Bentrop Detlef . . 2 Bertini Ivano . . 3 Cremonini Mauro A . 4 Forsen Sture . . 5 Luchinat Claudio . . 6 Malmendal Anders . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 36 _Journal_issue 39 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11605 _Page_last 11618 _Year 1997 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Calmodulin N-Terminal Domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'calmodulin n-terminal domain' $calmodulin 'Ce2-TR1C 1' $entity_Ce2-TR1C 'Ce2-TR1C 2' $entity_Ce2-TR1C stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic yes _System_thiol_state 'not reported' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_calmodulin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'calmodulin n-terminal domain' _Molecular_mass . _Mol_thiol_state 'not reported' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 76 _Mol_residue_sequence ; MADQLTEEQIAEFKEAFSLF DKDGDGTITTKELGTVMRSL GQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARK ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 ASP 4 GLN 5 LEU 6 THR 7 GLU 8 GLU 9 GLN 10 ILE 11 ALA 12 GLU 13 PHE 14 LYS 15 GLU 16 ALA 17 PHE 18 SER 19 LEU 20 PHE 21 ASP 22 LYS 23 ASP 24 GLY 25 ASP 26 GLY 27 THR 28 ILE 29 THR 30 THR 31 LYS 32 GLU 33 LEU 34 GLY 35 THR 36 VAL 37 MET 38 ARG 39 SER 40 LEU 41 GLY 42 GLN 43 ASN 44 PRO 45 THR 46 GLU 47 ALA 48 GLU 49 LEU 50 GLN 51 ASP 52 MET 53 ILE 54 ASN 55 GLU 56 VAL 57 ASP 58 ALA 59 ASP 60 GLY 61 ASN 62 GLY 63 THR 64 ILE 65 ASP 66 PHE 67 PRO 68 GLU 69 PHE 70 LEU 71 THR 72 MET 73 MET 74 ALA 75 ARG 76 LYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 18082 "Calmodulin N-Lobe" 98.68 80 100.00 100.00 5.11e-45 BMRB 18302 "CaM N-terminal domain" 98.68 77 100.00 100.00 3.87e-45 BMRB 4174 TR1C 100.00 81 100.00 100.00 7.49e-46 BMRB 6861 N-CamY 98.68 78 98.67 100.00 7.39e-45 BMRB 6862 N-CamY 98.68 78 98.67 100.00 7.39e-45 PDB 1AK8 "Nmr Solution Structure Of Cerium-Loaded Calmodulin Amino- Terminal Domain (Ce2-Tr1c), 23 Structures" 98.68 76 100.00 100.00 4.43e-45 PDB 1F70 "Refined Solution Structure Of Calmodulin N-Terminal Domain" 98.68 76 100.00 100.00 4.68e-45 PDB 1J7O "Solution Structure Of Calcium-calmodulin N-terminal Domain" 97.37 76 100.00 100.00 2.37e-44 PDB 1SW8 "Solution Structure Of The N-Terminal Domain Of Human N60d Calmodulin Refined With Paramagnetism Based Strategy" 98.68 79 98.67 100.00 3.23e-44 PDB 2I08 "Solvation Effect In Conformational Changes Of Ef-Hand Proteins: X-Ray Structure Of Ca2+-Saturated Double Mutant Q41l-K75i Of N-" 96.05 78 97.26 98.63 2.09e-42 PDB 2KUG "Halothane Binds To Druggable Sites In Calcium-calmodulin: Solution Structure Of Halothane-cam N-terminal Domain" 98.68 76 100.00 100.00 4.68e-45 PDB 2LLO "Solution Nmr-derived Structure Of Calmodulin N-lobe Bound With Er Alpha Peptide" 98.68 80 100.00 100.00 5.11e-45 PDB 2LQC "Nmr Solution Structure Of A Ca2+-Calmodulin With A Binding Motif (Nscate) Peptide From The N-Terminal Cytoplasmic Domain Of The" 98.68 77 100.00 100.00 3.87e-45 PDB 2PQ3 "N-Terminal Calmodulin Zn-Trapped Intermediate" 98.68 76 100.00 100.00 4.68e-45 PDB 3B32 "Crystal Structure Of Calcium-Saturated Calmodulin N-Terminal Domain Fragment, Residues 1-75" 98.68 75 100.00 100.00 4.31e-45 PDB 3IFK "Crystal Structure Of Calcium-Saturated Calmodulin N-Terminal Domain Fragment, Residues 1-90" 98.68 90 100.00 100.00 4.78e-45 PDB 3UCT "Structure Of Mn2+-Bound N-Terminal Domain Of Calmodulin In The Presence Of Zn2+" 98.68 79 100.00 100.00 4.71e-45 PDB 3UCW "Structure Of Mg2+ Bound N-Terminal Domain Of Calmodulin" 98.68 79 100.00 100.00 4.71e-45 PDB 3UCY "Structure Of Mg2+ Bound N-Terminal Domain Of Calmodulin In The Presence Of Zn2+" 98.68 79 100.00 100.00 4.71e-45 PDB 4Q57 "Crystal Structure Of The Plectin 1a Actin-binding Domain/n-terminal Domain Of Calmodulin Complex" 85.53 65 100.00 100.00 1.26e-37 EMBL CAA29381 "unnamed protein product [Drosophila melanogaster]" 76.32 58 100.00 100.00 1.86e-31 EMBL CAB65357 "putative calmodulin [Phallusia mammillata]" 59.21 71 100.00 100.00 7.75e-23 EMBL CCD82979 "putative calmodulin [Schistosoma mansoni]" 100.00 154 100.00 100.00 3.90e-45 GB AAH53790 "Cam protein, partial [Xenopus laevis]" 100.00 143 100.00 100.00 1.07e-47 GB ABW89042 "calmodulin [Helianthus annuus]" 51.32 39 97.44 97.44 5.31e-17 GB ABW89043 "calmodulin [Helianthus annuus]" 51.32 39 97.44 97.44 5.31e-17 GB ABW89044 "calmodulin [Helianthus annuus]" 51.32 39 97.44 97.44 5.31e-17 GB ABW89045 "calmodulin [Helianthus annuus]" 51.32 39 97.44 97.44 5.31e-17 REF XP_001869424 "calmodulin [Culex quinquefasciatus]" 77.63 110 100.00 100.00 5.11e-32 REF XP_001995129 "GH22800 [Drosophila grimshawi]" 98.68 122 100.00 100.00 9.34e-45 REF XP_002772218 "calmodulin, putative [Perkinsus marinus ATCC 50983]" 81.58 85 100.00 100.00 3.09e-35 REF XP_005112967 "PREDICTED: calmodulin-like, partial [Aplysia californica]" 61.84 78 100.00 100.00 4.30e-24 REF XP_005391108 "PREDICTED: calmodulin, partial [Chinchilla lanigera]" 100.00 95 100.00 100.00 8.87e-46 stop_ save_ ############# # Ligands # ############# save_Ce2-TR1C _Saveframe_category ligand _Mol_type complex _Name_common 'Ce2-TR1C complex' _BMRB_code . _PDB_code 1CLL _Molecular_mass . _Mol_charge 0 _Mol_paramagnetic yes _Mol_aromatic no _Details . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $calmodulin bovine 9913 Eukaryota Metazoa Bos taurus 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 $calmodulin 'recombinant technology' 'E. Coli' . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type 'lyophilized powder' _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $calmodulin . mM . stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name UXNMR _Version . loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task 'NMR data processing' stop_ _Details . save_ save_software_2 _Saveframe_category software _Name XWINNMR _Version . loop_ _Vendor _Address _Electronic_address Bruker . . stop_ loop_ _Task 'NMR data processing' stop_ _Details . save_ save_software_3 _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Prof. Kurt Wuthrich' . . stop_ loop_ _Task '2D spectra analysis' stop_ _Details . save_ save_software_4 _Saveframe_category software _Name DYANA _Version . loop_ _Vendor _Address _Electronic_address 'Peter Guntert' . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ save_software_5 _Saveframe_category software _Name CALIBRA _Version . loop_ _Vendor _Address _Electronic_address 'Peter Guntert' . . stop_ _Details . save_ save_software_6 _Saveframe_category software _Name FANTASIA _Version . loop_ _Vendor _Address _Electronic_address 'L. Banci' . . stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_500MHz_spectometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'DRX 500' _Field_strength 500 _Details . save_ save_300MHz_spectometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model 'AC-P 300' _Field_strength 300 _Details . save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 298 0 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _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 protons ppm 4.81 direct internal . . . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name 'calmodulin n-terminal domain' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 2 2 ALA HA H 4.12 . . 2 2 2 ALA HB H 1.55 . . 3 3 3 ASP H H 8.70 . . 4 3 3 ASP HA H 4.67 . . 5 3 3 ASP HB2 H 2.59 . . 6 3 3 ASP HB3 H 2.74 . . 7 4 4 GLN H H 8.74 . . 8 4 4 GLN HA H 4.41 . . 9 4 4 GLN HB2 H 2.02 . . 10 4 4 GLN HB3 H 2.14 . . 11 4 4 GLN HG2 H 2.41 . . 12 5 5 LEU H H 8.40 . . 13 5 5 LEU HA H 4.71 . . 14 5 5 LEU HB2 H 1.57 . . 15 5 5 LEU HB3 H 1.81 . . 16 5 5 LEU HG H 1.76 . . 17 5 5 LEU HD1 H 0.98 . . 18 6 6 THR H H 8.82 . . 19 6 6 THR HA H 4.53 . . 20 6 6 THR HB H 4.85 . . 21 6 6 THR HG2 H 1.40 . . 22 7 7 GLU H H 9.11 . . 23 7 7 GLU HA H 4.08 . . 24 7 7 GLU HB2 H 2.15 . . 25 7 7 GLU HG2 H 2.45 . . 26 7 7 GLU HG3 H 2.52 . . 27 8 8 GLU H H 8.79 . . 28 8 8 GLU HA H 4.16 . . 29 8 8 GLU HB2 H 2.01 . . 30 8 8 GLU HB3 H 2.13 . . 31 8 8 GLU HG2 H 2.36 . . 32 8 8 GLU HG3 H 2.44 . . 33 9 9 GLN H H 7.85 . . 34 9 9 GLN HA H 3.96 . . 35 9 9 GLN HB2 H 1.84 . . 36 9 9 GLN HB3 H 2.46 . . 37 9 9 GLN HG2 H 2.44 . . 38 9 9 GLN HE21 H 6.86 . . 39 9 9 GLN HE22 H 7.56 . . 40 10 10 ILE H H 8.51 . . 41 10 10 ILE HA H 3.87 . . 42 10 10 ILE HB H 2.10 . . 43 10 10 ILE HG12 H 1.24 . . 44 10 10 ILE HG13 H 1.90 . . 45 10 10 ILE HG2 H 1.25 . . 46 10 10 ILE HD1 H 0.98 . . 47 11 11 ALA H H 8.14 . . 48 11 11 ALA HA H 4.22 . . 49 11 11 ALA HB H 1.62 . . 50 12 12 GLU H H 7.90 . . 51 12 12 GLU HA H 4.20 . . 52 12 12 GLU HB2 H 1.97 . . 53 12 12 GLU HB3 H 2.12 . . 54 12 12 GLU HG2 H 2.26 . . 55 12 12 GLU HG3 H 2.52 . . 56 13 13 PHE H H 8.63 . . 57 13 13 PHE HA H 4.93 . . 58 13 13 PHE HB2 H 3.44 . . 59 13 13 PHE HB3 H 3.51 . . 60 13 13 PHE HD1 H 7.18 . . 61 13 13 PHE HE1 H 7.25 . . 62 14 14 LYS H H 9.25 . . 63 14 14 LYS HA H 4.04 . . 64 14 14 LYS HB2 H 2.01 . . 65 14 14 LYS HG2 H 1.13 . . 66 14 14 LYS HG3 H 1.41 . . 67 14 14 LYS HD2 H 1.55 . . 68 14 14 LYS HE2 H 2.79 . . 69 15 15 GLU H H 7.86 . . 70 15 15 GLU HA H 4.19 . . 71 15 15 GLU HB2 H 2.19 . . 72 15 15 GLU HB3 H 2.29 . . 73 15 15 GLU HG2 H 2.41 . . 74 15 15 GLU HG3 H 2.51 . . 75 16 16 ALA H H 8.01 . . 76 16 16 ALA HA H 4.07 . . 77 16 16 ALA HB H 1.78 . . 78 17 17 PHE H H 8.70 . . 79 17 17 PHE HA H 2.59 . . 80 17 17 PHE HB2 H 2.73 . . 81 17 17 PHE HB3 H 3.05 . . 82 17 17 PHE HD1 H 6.30 . . 83 17 17 PHE HE1 H 7.01 . . 84 17 17 PHE HZ H 7.62 . . 85 18 18 SER H H 7.74 . . 86 18 18 SER HA H 3.81 . . 87 18 18 SER HB2 H 4.05 . . 88 19 19 LEU H H 7.19 . . 89 19 19 LEU HA H 3.92 . . 90 19 19 LEU HB2 H 1.48 . . 91 19 19 LEU HG H 1.28 . . 92 19 19 LEU HD1 H 0.62 . . 93 19 19 LEU HD2 H 0.79 . . 94 20 20 PHE H H 6.46 . . 95 20 20 PHE HA H 3.64 . . 96 20 20 PHE HB2 H 0.68 . . 97 20 20 PHE HB3 H 1.05 . . 98 20 20 PHE HD1 H 6.63 . . 99 20 20 PHE HE1 H 6.95 . . 100 21 21 ASP H H 6.29 . . 101 21 21 ASP HA H -3.75 . . 102 21 21 ASP HB2 H -5.2 . . 103 21 21 ASP HB3 H 0.48 . . 104 22 22 LYS H H 8.76 . . 105 23 23 ASP H H 12.6 . . 106 24 24 GLY H H 9.2 . . 107 25 25 ASP H H 11.8 . . 108 25 25 ASP HA H 6.04 . . 109 25 25 ASP HB2 H 0.34 . . 110 25 25 ASP HB3 H 4.18 . . 111 26 26 GLY H H 15.7 . . 112 26 26 GLY HA2 H 6.11 . . 113 26 26 GLY HA3 H 7.36 . . 114 27 27 THR H H 21.7 . . 115 27 27 THR HA H 7.23 . . 116 28 28 ILE H H 8.53 . . 117 28 28 ILE HA H -9.0 . . 118 28 28 ILE HB H -1.13 . . 119 28 28 ILE HG12 H -5.4 . . 120 28 28 ILE HG13 H -3.1 . . 121 28 28 ILE HG2 H -1.88 . . 122 28 28 ILE HD1 H -1.77 . . 123 29 29 THR H H 6.4 . . 124 29 29 THR HA H 4.05 . . 125 29 29 THR HG1 H 5.25 . . 126 30 30 THR H H 8.82 . . 127 30 30 THR HA H 3.35 . . 128 30 30 THR HB H 4.09 . . 129 30 30 THR HG2 H 0.98 . . 130 31 31 LYS H H 7.93 . . 131 31 31 LYS HA H 4.49 . . 132 31 31 LYS HB2 H 2.65 . . 133 31 31 LYS HB3 H 2.81 . . 134 31 31 LYS HG2 H 2.12 . . 135 31 31 LYS HD2 H 2.32 . . 136 31 31 LYS HD3 H 2.26 . . 137 31 31 LYS HE2 H 3.47 . . 138 32 32 GLU H H 8.92 . . 139 32 32 GLU HA H 5.25 . . 140 32 32 GLU HB2 H 1.82 . . 141 32 32 GLU HB3 H 1.99 . . 142 33 33 LEU H H 8.16 . . 143 33 33 LEU HA H 3.60 . . 144 33 33 LEU HB2 H 0.81 . . 145 33 33 LEU HB3 H 1.36 . . 146 33 33 LEU HG H 0.93 . . 147 33 33 LEU HD1 H -.01 . . 148 33 33 LEU HD2 H 0.08 . . 149 34 34 GLY H H 8.63 . . 150 34 34 GLY HA2 H 3.51 . . 151 34 34 GLY HA3 H 4.03 . . 152 35 35 THR H H 8.29 . . 153 35 35 THR HA H 4.11 . . 154 35 35 THR HB H 4.66 . . 155 35 35 THR HG2 H 1.66 . . 156 36 36 VAL H H 7.24 . . 157 36 36 VAL HA H 3.49 . . 158 36 36 VAL HB H 1.65 . . 159 36 36 VAL HG1 H 0.14 . . 160 36 36 VAL HG2 H 0.40 . . 161 37 37 MET H H 8.23 . . 162 37 37 MET HA H 3.90 . . 163 37 37 MET HB2 H 1.77 . . 164 37 37 MET HB3 H 1.89 . . 165 37 37 MET HG2 H 2.39 . . 166 37 37 MET HG3 H 2.48 . . 167 38 38 ARG H H 8.54 . . 168 38 38 ARG HA H 4.78 . . 169 38 38 ARG HB2 H 1.89 . . 170 38 38 ARG HG2 H 1.96 . . 171 38 38 ARG HD2 H 3.21 . . 172 38 38 ARG HD3 H 3.37 . . 173 38 38 ARG HE H 7.60 . . 174 39 39 SER H H 7.84 . . 175 39 39 SER HA H 4.40 . . 176 39 39 SER HB2 H 4.08 . . 177 40 40 LEU H H 7.27 . . 178 40 40 LEU HA H 4.37 . . 179 40 40 LEU HB2 H 1.68 . . 180 40 40 LEU HB3 H 1.76 . . 181 40 40 LEU HG H 1.68 . . 182 40 40 LEU HD1 H 0.65 . . 183 41 41 GLY H H 7.77 . . 184 41 41 GLY HA2 H 3.73 . . 185 41 41 GLY HA3 H 4.20 . . 186 42 42 GLN H H 7.79 . . 187 42 42 GLN HA H 4.43 . . 188 42 42 GLN HB2 H 1.56 . . 189 42 42 GLN HB3 H 2.06 . . 190 42 42 GLN HG2 H 2.14 . . 191 42 42 GLN HE21 H 6.69 . . 192 42 42 GLN HE22 H 7.25 . . 193 43 43 ASN H H 8.70 . . 194 43 43 ASN HA H 5.17 . . 195 43 43 ASN HB2 H 2.50 . . 196 43 43 ASN HB3 H 2.78 . . 197 43 43 ASN HD21 H 6.75 . . 198 43 43 ASN HD22 H 7.56 . . 199 44 44 PRO HA H 4.69 . . 200 44 44 PRO HB2 H 1.83 . . 201 44 44 PRO HB3 H 2.15 . . 202 44 44 PRO HG2 H 1.86 . . 203 44 44 PRO HD2 H 3.22 . . 204 44 44 PRO HD3 H 3.55 . . 205 45 45 THR H H 8.67 . . 206 45 45 THR HA H 4.45 . . 207 45 45 THR HB H 4.71 . . 208 45 45 THR HG2 H 1.36 . . 209 46 46 GLU H H 8.84 . . 210 46 46 GLU HA H 3.97 . . 211 46 46 GLU HB2 H 2.07 . . 212 46 46 GLU HG2 H 2.39 . . 213 47 47 ALA H H 8.29 . . 214 47 47 ALA HA H 4.08 . . 215 47 47 ALA HB H 1.39 . . 216 48 48 GLU H H 7.67 . . 217 48 48 GLU HA H 3.93 . . 218 48 48 GLU HB2 H 2.26 . . 219 49 49 LEU H H 8.02 . . 220 49 49 LEU HA H 3.81 . . 221 49 49 LEU HB2 H 0.97 . . 222 49 49 LEU HB3 H 1.93 . . 223 49 49 LEU HG H 1.64 . . 224 49 49 LEU HD1 H 0.60 . . 225 49 49 LEU HD2 H 0.78 . . 226 50 50 GLN H H 8.12 . . 227 50 50 GLN HA H 3.55 . . 228 50 50 GLN HB2 H 2.11 . . 229 50 50 GLN HG2 H 2.40 . . 230 50 50 GLN HE21 H 6.90 . . 231 50 50 GLN HE22 H 7.50 . . 232 51 51 ASP H H 7.99 . . 233 51 51 ASP HA H 4.30 . . 234 51 51 ASP HB2 H 2.56 . . 235 51 51 ASP HB3 H 2.70 . . 236 52 52 MET H H 7.56 . . 237 52 52 MET HA H 3.65 . . 238 52 52 MET HB2 H 1.50 . . 239 52 52 MET HB3 H 1.84 . . 240 52 52 MET HG2 H 2.16 . . 241 52 52 MET HG3 H 2.45 . . 242 53 53 ILE H H 7.10 . . 243 53 53 ILE HA H 2.07 . . 244 53 53 ILE HB H 1.12 . . 245 53 53 ILE HG12 H -0.26 . . 246 53 53 ILE HG13 H 0.51 . . 247 53 53 ILE HG2 H -1.02 . . 248 53 53 ILE HD1 H -0.66 . . 249 54 54 ASN H H 8.23 . . 250 54 54 ASN HA H 4.40 . . 251 54 54 ASN HB2 H 2.96 . . 252 54 54 ASN HD21 H 7.15 . . 253 54 54 ASN HD22 H 7.95 . . 254 55 55 GLU H H 7.30 . . 255 55 55 GLU HA H 3.91 . . 256 55 55 GLU HB2 H 1.73 . . 257 55 55 GLU HB3 H 1.86 . . 258 55 55 GLU HG2 H 2.12 . . 259 55 55 GLU HG3 H 2.27 . . 260 56 56 VAL H H 6.23 . . 261 56 56 VAL HA H 3.98 . . 262 56 56 VAL HB H 1.37 . . 263 56 56 VAL HG1 H -0.59 . . 264 56 56 VAL HG2 H 0.15 . . 265 57 57 ASP H H 7.01 . . 266 57 57 ASP HA H 3.63 . . 267 57 57 ASP HB2 H -1.17 . . 268 59 59 ASP H H 11.6 . . 269 59 59 ASP HA H 5.49 . . 270 59 59 ASP HB2 H 0.48 . . 271 59 59 ASP HB3 H 1.47 . . 272 60 60 GLY H H 14.8 . . 273 60 60 GLY HA2 H 6.42 . . 274 60 60 GLY HA3 H 7.69 . . 275 61 61 ASN H H 20.4 . . 276 61 61 ASN HA H 6.61 . . 277 61 61 ASN HB2 H 3.38 . . 278 61 61 ASN HB3 H 3.00 . . 279 62 62 GLY H H 14.8 . . 280 62 62 GLY HA2 H 4.0 . . 281 63 63 THR HA H 2.14 . . 282 64 64 ILE H H 7.16 . . 283 64 64 ILE HA H 0.4 . . 284 64 64 ILE HB H 0.13 . . 285 64 64 ILE HG12 H -1.41 . . 286 64 64 ILE HG13 H -2.41 . . 287 64 64 ILE HG2 H -0.36 . . 288 64 64 ILE HD1 H -1.71 . . 289 65 65 ASP H H 17.5 . . 290 65 65 ASP HA H 8.36 . . 291 65 65 ASP HB2 H 6.77 . . 292 65 65 ASP HB3 H 10.08 . . 293 66 66 PHE H H 10.65 . . 294 66 66 PHE HA H 4.59 . . 295 66 66 PHE HB2 H 2.81 . . 296 66 66 PHE HB3 H 3.65 . . 297 66 66 PHE HD1 H 7.06 . . 298 66 66 PHE HE1 H 7.36 . . 299 66 66 PHE HZ H 7.50 . . 300 67 67 PRO HA H 4.32 . . 301 67 67 PRO HB2 H 2.48 . . 302 67 67 PRO HB3 H 2.62 . . 303 67 67 PRO HG2 H 2.47 . . 304 67 67 PRO HG3 H 3.02 . . 305 67 67 PRO HD2 H 4.71 . . 306 67 67 PRO HD3 H 5.36 . . 307 68 68 GLU H H 9.86 . . 308 68 68 GLU HA H 4.21 . . 309 68 68 GLU HB2 H 0.93 . . 310 68 68 GLU HB3 H 4.08 . . 311 69 69 PHE H H 9.44 . . 312 69 69 PHE HA H 3.58 . . 313 69 69 PHE HB2 H 2.96 . . 314 69 69 PHE HD1 H 6.49 . . 315 69 69 PHE HE1 H 6.69 . . 316 69 69 PHE HZ H 6.81 . . 317 70 70 LEU H H 8.38 . . 318 70 70 LEU HA H 3.25 . . 319 70 70 LEU HB2 H 1.13 . . 320 70 70 LEU HB3 H 1.77 . . 321 70 70 LEU HG H 1.07 . . 322 70 70 LEU HD1 H 0.53 . . 323 70 70 LEU HD2 H 0.70 . . 324 71 71 THR H H 7.44 . . 325 71 71 THR HA H 3.73 . . 326 71 71 THR HB H 4.14 . . 327 71 71 THR HG2 H 1.08 . . 328 72 72 MET H H 7.45 . . 329 72 72 MET HA H 3.47 . . 330 72 72 MET HB2 H 1.41 . . 331 72 72 MET HB3 H 1.70 . . 332 72 72 MET HG2 H 1.82 . . 333 72 72 MET HG3 H 1.95 . . 334 73 73 MET H H 7.57 . . 335 73 73 MET HA H 3.97 . . 336 73 73 MET HB2 H 1.04 . . 337 73 73 MET HG2 H 1.15 . . 338 73 73 MET HG3 H 1.26 . . 339 73 73 MET HE H 1.40 . . 340 74 74 ALA H H 7.48 . . 341 74 74 ALA HA H 4.22 . . 342 74 74 ALA HB H 1.30 . . 343 75 75 ARG H H 7.36 . . 344 75 75 ARG HA H 4.18 . . 345 75 75 ARG HB2 H 1.69 . . 346 75 75 ARG HB3 H 1.81 . . 347 75 75 ARG HG2 H 1.55 . . 348 75 75 ARG HD2 H 3.04 . . 349 75 75 ARG HE H 7.06 . . 350 76 76 LYS H H 7.66 . . 351 76 76 LYS HA H 4.09 . . 352 76 76 LYS HB2 H 1.68 . . 353 76 76 LYS HB3 H 1.80 . . 354 76 76 LYS HG2 H 1.38 . . 355 76 76 LYS HD2 H 1.62 . . 356 76 76 LYS HE2 H 2.94 . . stop_ save_