data_5262 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H and 15N Chemical Shift Assignements for the first fibronectin type II module of MMP-2 (col-1) ; _BMRB_accession_number 5262 _BMRB_flat_file_name bmr5262.str _Entry_type original _Submission_date 2002-01-20 _Accession_date 2002-01-21 _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 Gehrmann Marion . . 2 Briknarova Klara . . 3 Banyai Laszlo . . 4 Patthy Laszlo . . 5 Llinas Miguel . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 365 "15N chemical shifts" 62 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-06-13 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 4510 'The Second Type II Module From Human Matrix Metalloproteinase 2' stop_ _Original_release_date 2002-01-21 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The Col-1 Module of Human Matrix Metalloproteinase-2 (MMP-2): Structural/Functional Relatedness between Gelatin-binding Fibronectin Type II Modules and Lysine-binding Kringle Domains ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21925710 _PubMed_ID 11928808 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Gehrmann Marion . . 2 Briknarova Klara . . 3 Banyai Laszlo . . 4 Patthy Laszlo . . 5 Llinas Miguel . . stop_ _Journal_abbreviation 'Biol. Chem.' _Journal_volume 383 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 137 _Page_last 148 _Year 2002 _Details . loop_ _Keyword 'Fibronectin type II modules' 'MMP-2 col-gelatin interactionn' 'kringle-fibronectin type II structural homology' stop_ save_ ################################## # Molecular system description # ################################## save_system_col-1 _Saveframe_category molecular_system _Mol_system_name 'first fibronectin type II module of human matrix metalloproteinase 2' _Abbreviation_common col-1 _Enzyme_commission_number 3.4.24.24 loop_ _Mol_system_component_name _Mol_label col-1 $col-1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state complex _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details 'The structure in 1KS0 was calculated for R1 to A59.' save_ ######################## # Monomeric polymers # ######################## save_col-1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'the first fibronectin type II module of human matrix metalloproteinase' _Abbreviation_common col-1 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 60 _Mol_residue_sequence ; RIPVKYGNADGEYCKFPFLF NGKEYNSCTDTGRSDGFLWC STTYNFEKDGKYGFCPHEAL ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 ILE 3 PRO 4 VAL 5 LYS 6 TYR 7 GLY 8 ASN 9 ALA 10 ASP 11 GLY 12 GLU 13 TYR 14 CYS 15 LYS 16 PHE 17 PRO 18 PHE 19 LEU 20 PHE 21 ASN 22 GLY 23 LYS 24 GLU 25 TYR 26 ASN 27 SER 28 CYS 29 THR 30 ASP 31 THR 32 GLY 33 ARG 34 SER 35 ASP 36 GLY 37 PHE 38 LEU 39 TRP 40 CYS 41 SER 42 THR 43 THR 44 TYR 45 ASN 46 PHE 47 GLU 48 LYS 49 ASP 50 GLY 51 LYS 52 TYR 53 GLY 54 PHE 55 CYS 56 PRO 57 HIS 58 GLU 59 ALA 60 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 PDB 1KS0 'The First Fibronectin Type Ii Module From Human Matrix Metalloproteinase 2' 100.00 63 100.00 100.00 5.15e-28 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $col-1 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_type _Vector_name _Details $col-1 'recombinant technology' 'E. coli' Escherichia coli . plasmid . 'The first three residues (Arg Ile Pro) are cloning artifacts.' 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 _Isotopic_labeling $col-1 0.5 mM . H2O 90 % . acetone 10 % [U-2H] stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $col-1 0.5 mM . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details ; The sample included the tail Leu Phe Thr Met, which wasn't present in the unlabelled sample. ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $col-1 0.7 mM [U-15N] stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Saveframe_category software _Name XWINNMR _Version 2.0 loop_ _Task 'experiment acquisition' stop_ _Details 'Bruker, Germany' save_ save_FELIX _Saveframe_category software _Name FELIX _Version 98 loop_ _Task 'data processing and assignment' stop_ _Details 'Molecular Simulations, Inc, San Diego, CA' save_ save_XPLOR _Saveframe_category software _Name XPLOR _Version 3.851 loop_ _Task 'structure calculation' stop_ _Details Brunger save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AvanceDMX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_COSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D COSY' _Sample_label . save_ save_2D_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_2D_1H-15N_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label . save_ save_3D_HNHA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _Sample_label . save_ save_3D_HNHB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHB' _Sample_label . save_ save_3D_15N-edited_TOCSY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited TOCSY' _Sample_label . save_ save_3D_15N-edited_NOESY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-edited NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 7.3 0.2 n/a temperature 298 1 K stop_ save_ save_condition_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 6.0 0.2 n/a temperature 298 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 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 '2D COSY' '2D TOCSY' '2D NOESY' '2D 1H-15N HSQC' '3D HNHA' '3D HNHB' '3D 15N-edited TOCSY' '3D 15N-edited NOESY' stop_ _Sample_conditions_label $condition_2 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name col-1 _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 ARG HA H 4.52 0.01 1 2 . 1 ARG HB2 H 1.50 0.01 2 3 . 1 ARG HB3 H 1.59 0.01 2 4 . 1 ARG HG2 H 1.61 0.01 1 5 . 1 ARG HG3 H 1.61 0.01 1 6 . 1 ARG HD2 H 2.87 0.01 1 7 . 1 ARG HD3 H 2.87 0.01 1 8 . 2 ILE H H 7.91 0.01 1 9 . 2 ILE HA H 4.23 0.01 1 10 . 2 ILE HB H 1.56 0.01 1 11 . 2 ILE HG12 H 1.45 0.01 2 12 . 2 ILE HG13 H 0.85 0.01 2 13 . 2 ILE HG2 H 0.78 0.01 1 14 . 2 ILE HD1 H 0.94 0.01 1 15 . 2 ILE N N 119.2 0.1 1 16 . 3 PRO HA H 4.35 0.01 1 17 . 3 PRO HB2 H 1.79 0.01 1 18 . 3 PRO HB3 H 2.14 0.01 1 19 . 3 PRO HG2 H 1.95 0.01 1 20 . 3 PRO HG3 H 1.95 0.01 1 21 . 3 PRO HD2 H 3.73 0.01 1 22 . 3 PRO HD3 H 3.73 0.01 1 23 . 4 VAL H H 8.05 0.01 1 24 . 4 VAL HA H 4.61 0.01 1 25 . 4 VAL HB H 1.70 0.01 1 26 . 4 VAL HG1 H 0.59 0.01 1 27 . 4 VAL HG2 H 0.42 0.01 1 28 . 4 VAL N N 113.0 0.1 1 29 . 5 LYS H H 8.61 0.01 1 30 . 5 LYS HA H 4.63 0.01 1 31 . 5 LYS HB2 H 1.24 0.01 1 32 . 5 LYS HB3 H 1.24 0.01 1 33 . 5 LYS HG2 H 0.99 0.01 2 34 . 5 LYS HG3 H 1.15 0.01 2 35 . 5 LYS HD2 H 1.44 0.01 1 36 . 5 LYS HD3 H 1.44 0.01 1 37 . 5 LYS HE2 H 2.79 0.01 1 38 . 5 LYS HE3 H 2.79 0.01 1 39 . 5 LYS N N 120.7 0.1 1 40 . 6 TYR H H 8.09 0.01 1 41 . 6 TYR HA H 4.87 0.01 1 42 . 6 TYR HB2 H 2.96 0.01 1 43 . 6 TYR HB3 H 3.10 0.01 1 44 . 6 TYR HD1 H 7.03 0.01 1 45 . 6 TYR HD2 H 7.03 0.01 1 46 . 6 TYR HE1 H 6.80 0.01 1 47 . 6 TYR HE2 H 6.80 0.01 1 48 . 6 TYR N N 118.5 0.1 1 49 . 7 GLY H H 8.14 0.01 1 50 . 7 GLY HA2 H 3.52 0.01 1 51 . 7 GLY HA3 H 3.52 0.01 1 52 . 7 GLY N N 104.2 0.1 1 53 . 8 ASN H H 7.52 0.01 1 54 . 8 ASN HA H 4.87 0.01 1 55 . 8 ASN HB2 H 3.27 0.01 1 56 . 8 ASN HB3 H 2.62 0.01 1 57 . 8 ASN HD21 H 7.36 0.01 1 58 . 8 ASN HD22 H 7.83 0.01 1 59 . 8 ASN N N 121.4 0.1 1 60 . 8 ASN ND2 N 106.7 0.1 1 61 . 9 ALA H H 7.29 0.01 1 62 . 9 ALA HA H 4.51 0.01 1 63 . 9 ALA HB H 0.92 0.01 1 64 . 9 ALA N N 122.1 0.1 1 65 . 10 ASP H H 8.34 0.01 1 66 . 10 ASP HA H 4.65 0.01 1 67 . 10 ASP HB2 H 2.59 0.01 2 68 . 10 ASP HB3 H 2.78 0.01 2 69 . 10 ASP N N 121.4 0.1 1 70 . 11 GLY H H 8.29 0.01 1 71 . 11 GLY HA2 H 3.59 0.01 2 72 . 11 GLY HA3 H 4.24 0.01 2 73 . 11 GLY N N 113.0 0.1 1 74 . 12 GLU H H 8.21 0.01 1 75 . 12 GLU HA H 4.48 0.01 1 76 . 12 GLU HB2 H 1.96 0.01 1 77 . 12 GLU HB3 H 2.06 0.01 1 78 . 12 GLU HG2 H 2.48 0.01 2 79 . 12 GLU HG3 H 2.52 0.01 2 80 . 12 GLU N N 121.4 0.1 1 81 . 13 TYR H H 8.17 0.01 1 82 . 13 TYR HA H 5.22 0.01 1 83 . 13 TYR HB2 H 2.59 0.01 1 84 . 13 TYR HB3 H 2.89 0.01 1 85 . 13 TYR HD1 H 6.91 0.01 1 86 . 13 TYR HD2 H 6.91 0.01 1 87 . 13 TYR HE1 H 6.70 0.01 1 88 . 13 TYR HE2 H 6.70 0.01 1 89 . 13 TYR N N 115.7 0.1 1 90 . 14 CYS H H 8.49 0.01 1 91 . 14 CYS HA H 3.94 0.01 1 92 . 14 CYS HB2 H 1.63 0.01 2 93 . 14 CYS HB3 H 1.73 0.01 2 94 . 14 CYS N N 116.9 0.1 1 95 . 15 LYS H H 8.50 0.01 1 96 . 15 LYS HA H 4.29 0.01 1 97 . 15 LYS HB2 H 1.56 0.01 1 98 . 15 LYS HB3 H 1.56 0.01 1 99 . 15 LYS HG2 H 1.23 0.01 1 100 . 15 LYS HG3 H 1.23 0.01 1 101 . 15 LYS HD2 H 1.56 0.01 1 102 . 15 LYS HD3 H 1.56 0.01 1 103 . 15 LYS N N 125.9 0.1 1 104 . 16 PHE H H 7.95 0.01 1 105 . 16 PHE HA H 5.67 0.01 1 106 . 16 PHE HB2 H 2.82 0.01 1 107 . 16 PHE HB3 H 2.91 0.01 1 108 . 16 PHE HD1 H 7.43 0.01 1 109 . 16 PHE HD2 H 7.43 0.01 1 110 . 16 PHE HE1 H 7.11 0.01 1 111 . 16 PHE HE2 H 7.11 0.01 1 112 . 16 PHE HZ H 7.52 0.01 1 113 . 16 PHE N N 118.9 0.1 1 114 . 17 PRO HA H 5.58 0.01 1 115 . 17 PRO HB2 H 1.86 0.01 1 116 . 17 PRO HB3 H 2.56 0.01 1 117 . 17 PRO HG2 H 2.00 0.01 1 118 . 17 PRO HG3 H 2.00 0.01 1 119 . 17 PRO HD2 H 3.54 0.01 2 120 . 17 PRO HD3 H 3.80 0.01 2 121 . 18 PHE H H 8.60 0.01 1 122 . 18 PHE HA H 5.39 0.01 1 123 . 18 PHE HB2 H 3.39 0.01 1 124 . 18 PHE HB3 H 3.80 0.01 1 125 . 18 PHE HD1 H 7.12 0.01 2 126 . 18 PHE HD2 H 8.15 0.01 2 127 . 18 PHE HE1 H 6.47 0.01 1 128 . 18 PHE HE2 H 6.47 0.01 1 129 . 18 PHE HZ H 6.18 0.01 1 130 . 18 PHE N N 112.5 0.1 1 131 . 19 LEU H H 9.20 0.01 1 132 . 19 LEU HA H 5.03 0.01 1 133 . 19 LEU HB2 H 1.66 0.01 1 134 . 19 LEU HB3 H 1.66 0.01 1 135 . 19 LEU HG H 1.66 0.01 1 136 . 19 LEU HD1 H 0.96 0.01 1 137 . 19 LEU HD2 H 0.96 0.01 1 138 . 19 LEU N N 124.2 0.1 1 139 . 20 PHE H H 9.61 0.01 1 140 . 20 PHE HA H 5.32 0.01 1 141 . 20 PHE HB2 H 3.56 0.01 1 142 . 20 PHE HB3 H 3.26 0.01 1 143 . 20 PHE HD1 H 7.42 0.01 1 144 . 20 PHE HD2 H 7.42 0.01 1 145 . 20 PHE HE1 H 7.36 0.01 1 146 . 20 PHE HE2 H 7.36 0.01 1 147 . 20 PHE HZ H 7.36 0.01 1 148 . 20 PHE N N 126.1 0.1 1 149 . 21 ASN H H 9.72 0.01 1 150 . 21 ASN HA H 4.23 0.01 1 151 . 21 ASN HB2 H 1.77 0.01 2 152 . 21 ASN HB3 H 2.87 0.01 2 153 . 21 ASN HD21 H 7.06 0.01 1 154 . 21 ASN HD22 H 6.63 0.01 1 155 . 21 ASN N N 130.4 0.1 1 156 . 21 ASN ND2 N 110.3 0.1 1 157 . 22 GLY H H 8.75 0.01 1 158 . 22 GLY HA2 H 3.64 0.01 2 159 . 22 GLY HA3 H 4.11 0.01 2 160 . 22 GLY N N 102.2 0.1 1 161 . 23 LYS H H 7.83 0.01 1 162 . 23 LYS HA H 4.61 0.01 1 163 . 23 LYS HB2 H 1.72 0.01 1 164 . 23 LYS HB3 H 1.63 0.01 1 165 . 23 LYS HG2 H 1.12 0.01 2 166 . 23 LYS HG3 H 1.32 0.01 2 167 . 23 LYS HD2 H 1.58 0.01 1 168 . 23 LYS HD3 H 1.58 0.01 1 169 . 23 LYS HE2 H 2.88 0.01 1 170 . 23 LYS HE3 H 2.88 0.01 1 171 . 23 LYS N N 121.0 0.1 1 172 . 24 GLU H H 8.27 0.01 1 173 . 24 GLU HA H 5.23 0.01 1 174 . 24 GLU HB2 H 1.90 0.01 1 175 . 24 GLU HB3 H 1.96 0.01 1 176 . 24 GLU HG2 H 2.48 0.01 1 177 . 24 GLU HG3 H 2.48 0.01 1 178 . 24 GLU N N 119.8 0.1 1 179 . 25 TYR H H 9.25 0.01 1 180 . 25 TYR HA H 4.21 0.01 1 181 . 25 TYR HB2 H 1.09 0.01 1 182 . 25 TYR HB3 H 2.59 0.01 1 183 . 25 TYR HD1 H 6.95 0.01 1 184 . 25 TYR HD2 H 6.95 0.01 1 185 . 25 TYR HE1 H 7.09 0.01 1 186 . 25 TYR HE2 H 7.09 0.01 1 187 . 25 TYR N N 122.2 0.1 1 188 . 26 ASN H H 8.67 0.01 1 189 . 26 ASN HA H 4.78 0.01 1 190 . 26 ASN HB2 H 2.36 0.01 1 191 . 26 ASN HB3 H 2.66 0.01 1 192 . 26 ASN HD21 H 7.41 0.01 1 193 . 26 ASN HD22 H 6.94 0.01 1 194 . 26 ASN N N 118.7 0.1 1 195 . 26 ASN ND2 N 111.9 0.1 1 196 . 27 SER H H 7.54 0.01 1 197 . 27 SER HA H 3.59 0.01 1 198 . 27 SER HB2 H 3.83 0.01 1 199 . 27 SER HB3 H 3.63 0.01 1 200 . 27 SER N N 111.0 0.1 1 201 . 28 CYS H H 8.54 0.01 1 202 . 28 CYS HA H 4.76 0.01 1 203 . 28 CYS HB2 H 3.61 0.01 1 204 . 28 CYS HB3 H 2.82 0.01 1 205 . 28 CYS N N 114.9 0.1 1 206 . 29 THR H H 8.83 0.01 1 207 . 29 THR HA H 4.88 0.01 1 208 . 29 THR HB H 3.79 0.01 1 209 . 29 THR HG2 H 0.10 0.01 1 210 . 29 THR N N 116.0 0.1 1 211 . 30 ASP H H 8.13 0.01 1 212 . 30 ASP HA H 5.30 0.01 1 213 . 30 ASP HB2 H 2.35 0.01 1 214 . 30 ASP HB3 H 3.10 0.01 1 215 . 30 ASP N N 122.8 0.1 1 216 . 31 THR H H 8.40 0.01 1 217 . 31 THR HA H 4.17 0.01 1 218 . 31 THR HB H 4.13 0.01 1 219 . 31 THR HG2 H 1.50 0.01 1 220 . 31 THR N N 118.2 0.1 1 221 . 32 GLY H H 8.93 0.01 1 222 . 32 GLY HA2 H 3.86 0.01 2 223 . 32 GLY HA3 H 4.32 0.01 2 224 . 32 GLY N N 112.4 0.1 1 225 . 33 ARG H H 8.13 0.01 1 226 . 33 ARG HA H 4.79 0.01 1 227 . 33 ARG HB2 H 2.33 0.01 1 228 . 33 ARG HB3 H 2.16 0.01 1 229 . 33 ARG HG2 H 1.29 0.01 2 230 . 33 ARG HG3 H 1.55 0.01 2 231 . 33 ARG HD2 H 2.87 0.01 1 232 . 33 ARG HD3 H 2.87 0.01 1 233 . 33 ARG HE H 9.41 0.01 1 234 . 33 ARG N N 116.8 0.1 1 235 . 33 ARG NE N 84.0 0.1 1 236 . 34 SER H H 9.29 0.01 1 237 . 34 SER HA H 4.25 0.01 1 238 . 34 SER HB2 H 3.46 0.01 1 239 . 34 SER HB3 H 3.46 0.01 1 240 . 34 SER N N 117.3 0.1 1 241 . 35 ASP H H 7.74 0.01 1 242 . 35 ASP HA H 4.56 0.01 1 243 . 35 ASP HB2 H 2.52 0.01 1 244 . 35 ASP HB3 H 2.82 0.01 1 245 . 35 ASP N N 118.2 0.1 1 246 . 36 GLY H H 8.40 0.01 1 247 . 36 GLY HA2 H 3.88 0.01 2 248 . 36 GLY HA3 H 4.04 0.01 2 249 . 36 GLY N N 107.3 0.1 1 250 . 37 PHE H H 7.98 0.01 1 251 . 37 PHE HA H 4.61 0.01 1 252 . 37 PHE HB2 H 3.26 0.01 1 253 . 37 PHE HB3 H 3.13 0.01 1 254 . 37 PHE HD1 H 7.12 0.01 1 255 . 37 PHE HD2 H 7.12 0.01 1 256 . 37 PHE HE1 H 7.81 0.01 1 257 . 37 PHE HE2 H 7.81 0.01 1 258 . 37 PHE HZ H 7.03 0.01 1 259 . 37 PHE N N 120.4 0.1 1 260 . 38 LEU H H 9.02 0.01 1 261 . 38 LEU HA H 4.69 0.01 1 262 . 38 LEU HB2 H 1.80 0.01 1 263 . 38 LEU HB3 H 1.80 0.01 1 264 . 38 LEU HG H 1.80 0.01 1 265 . 38 LEU HD1 H 0.94 0.01 1 266 . 38 LEU HD2 H 0.94 0.01 1 267 . 38 LEU N N 125.3 0.1 1 268 . 39 TRP H H 9.83 0.01 1 269 . 39 TRP HA H 5.60 0.01 1 270 . 39 TRP HB2 H 3.55 0.01 1 271 . 39 TRP HB3 H 2.66 0.01 1 272 . 39 TRP HD1 H 7.29 0.01 1 273 . 39 TRP HE1 H 9.86 0.01 1 274 . 39 TRP HE3 H 6.61 0.01 1 275 . 39 TRP HZ2 H 5.96 0.01 1 276 . 39 TRP HZ3 H 5.22 0.01 1 277 . 39 TRP HH2 H 5.28 0.01 1 278 . 39 TRP N N 122.8 0.1 1 279 . 39 TRP NE1 N 127.8 0.1 1 280 . 40 CYS H H 8.60 0.01 1 281 . 40 CYS HA H 4.06 0.01 1 282 . 40 CYS HB2 H 3.09 0.01 1 283 . 40 CYS HB3 H 2.87 0.01 1 284 . 40 CYS N N 110.1 0.1 1 285 . 41 SER H H 3.76 0.01 1 286 . 41 SER HA H 5.25 0.01 1 287 . 41 SER HB2 H 3.28 0.01 1 288 . 41 SER HB3 H 3.28 0.01 1 289 . 41 SER N N 110.4 0.1 1 290 . 42 THR H H 7.93 0.01 1 291 . 42 THR HA H 4.71 0.01 1 292 . 42 THR HB H 4.52 0.01 1 293 . 42 THR HG2 H 1.16 0.01 1 294 . 42 THR N N 111.4 0.1 1 295 . 43 THR H H 8.14 0.01 1 296 . 43 THR HA H 4.35 0.01 1 297 . 43 THR HB H 4.24 0.01 1 298 . 43 THR HG2 H 1.18 0.01 1 299 . 43 THR N N 114.0 0.1 1 300 . 44 TYR H H 7.99 0.01 1 301 . 44 TYR HA H 4.75 0.01 1 302 . 44 TYR HB2 H 3.06 0.01 1 303 . 44 TYR HB3 H 3.24 0.01 1 304 . 44 TYR HD1 H 7.40 0.01 1 305 . 44 TYR HD2 H 7.40 0.01 1 306 . 44 TYR HE1 H 6.70 0.01 1 307 . 44 TYR HE2 H 6.70 0.01 1 308 . 44 TYR N N 118.6 0.1 1 309 . 45 ASN H H 8.83 0.01 1 310 . 45 ASN HA H 4.91 0.01 1 311 . 45 ASN HB2 H 2.80 0.01 1 312 . 45 ASN HB3 H 3.36 0.01 1 313 . 45 ASN HD21 H 8.04 0.01 1 314 . 45 ASN HD22 H 7.22 0.01 1 315 . 45 ASN N N 115.5 0.1 1 316 . 45 ASN ND2 N 111.7 0.1 1 317 . 46 PHE H H 8.10 0.01 1 318 . 46 PHE HA H 5.00 0.01 1 319 . 46 PHE HB2 H 3.14 0.01 1 320 . 46 PHE HB3 H 2.97 0.01 1 321 . 46 PHE HD1 H 7.52 0.01 1 322 . 46 PHE HD2 H 7.52 0.01 1 323 . 46 PHE HE1 H 6.96 0.01 1 324 . 46 PHE HE2 H 6.96 0.01 1 325 . 46 PHE HZ H 6.58 0.01 1 326 . 46 PHE N N 124.9 0.1 1 327 . 47 GLU H H 9.23 0.01 1 328 . 47 GLU HA H 3.83 0.01 1 329 . 47 GLU HB2 H 2.25 0.01 1 330 . 47 GLU HB3 H 2.17 0.01 1 331 . 47 GLU HG2 H 2.44 0.01 2 332 . 47 GLU HG3 H 2.55 0.01 2 333 . 47 GLU N N 117.3 0.1 1 334 . 48 LYS H H 7.14 0.01 1 335 . 48 LYS HA H 4.23 0.01 1 336 . 48 LYS HB2 H 1.74 0.01 1 337 . 48 LYS HB3 H 1.77 0.01 1 338 . 48 LYS HG2 H 1.40 0.01 1 339 . 48 LYS HG3 H 1.40 0.01 1 340 . 48 LYS HD2 H 1.70 0.01 1 341 . 48 LYS HD3 H 1.70 0.01 1 342 . 48 LYS HE2 H 3.04 0.01 1 343 . 48 LYS HE3 H 3.04 0.01 1 344 . 48 LYS N N 115.6 0.1 1 345 . 49 ASP H H 7.98 0.01 1 346 . 49 ASP HA H 4.53 0.01 1 347 . 49 ASP HB2 H 2.73 0.01 1 348 . 49 ASP HB3 H 2.51 0.01 1 349 . 49 ASP N N 116.8 0.1 1 350 . 50 GLY H H 8.61 0.01 1 351 . 50 GLY HA2 H 2.86 0.01 2 352 . 50 GLY HA3 H 3.53 0.01 2 353 . 50 GLY N N 108.6 0.1 1 354 . 51 LYS H H 9.16 0.01 1 355 . 51 LYS HA H 5.13 0.01 1 356 . 51 LYS HB2 H 2.02 0.01 1 357 . 51 LYS HB3 H 1.60 0.01 1 358 . 51 LYS HG2 H 1.23 0.01 1 359 . 51 LYS HG3 H 1.23 0.01 1 360 . 51 LYS HD2 H 1.58 0.01 1 361 . 51 LYS HD3 H 1.58 0.01 1 362 . 51 LYS HE2 H 2.90 0.01 1 363 . 51 LYS HE3 H 2.90 0.01 1 364 . 51 LYS N N 122.8 0.1 1 365 . 52 TYR H H 9.30 0.01 1 366 . 52 TYR HA H 5.45 0.01 1 367 . 52 TYR HB2 H 2.87 0.01 1 368 . 52 TYR HB3 H 3.04 0.01 1 369 . 52 TYR HD1 H 6.61 0.01 1 370 . 52 TYR HD2 H 6.61 0.01 1 371 . 52 TYR HE1 H 6.49 0.01 1 372 . 52 TYR HE2 H 6.49 0.01 1 373 . 52 TYR N N 120.1 0.1 1 374 . 53 GLY H H 7.80 0.01 1 375 . 53 GLY HA2 H 3.31 0.01 2 376 . 53 GLY HA3 H 3.50 0.01 2 377 . 53 GLY N N 101.8 0.1 1 378 . 54 PHE H H 9.08 0.01 1 379 . 54 PHE HA H 5.23 0.01 1 380 . 54 PHE HB2 H 3.03 0.01 1 381 . 54 PHE HB3 H 3.43 0.01 1 382 . 54 PHE HD1 H 7.59 0.01 1 383 . 54 PHE HD2 H 7.59 0.01 1 384 . 54 PHE HE1 H 7.32 0.01 1 385 . 54 PHE HE2 H 7.32 0.01 1 386 . 54 PHE HZ H 7.37 0.01 1 387 . 54 PHE N N 115.7 0.1 1 388 . 55 CYS H H 8.70 0.01 1 389 . 55 CYS HA H 4.79 0.01 1 390 . 55 CYS HB2 H 3.35 0.01 1 391 . 55 CYS HB3 H 3.10 0.01 1 392 . 55 CYS N N 120.3 0.1 1 393 . 56 PRO HA H 4.44 0.01 1 394 . 56 PRO HB2 H 1.99 0.01 1 395 . 56 PRO HB3 H 2.32 0.01 1 396 . 56 PRO HG2 H 1.99 0.01 1 397 . 56 PRO HG3 H 1.99 0.01 1 398 . 56 PRO HD2 H 3.52 0.01 2 399 . 56 PRO HD3 H 3.82 0.01 2 400 . 57 HIS H H 7.99 0.01 1 401 . 57 HIS HA H 4.60 0.01 1 402 . 57 HIS HB2 H 3.10 0.01 2 403 . 57 HIS HB3 H 3.29 0.01 2 404 . 57 HIS HD1 H 7.79 0.01 1 405 . 57 HIS HD2 H 7.79 0.01 1 406 . 57 HIS HE1 H 7.12 0.01 1 407 . 57 HIS HE2 H 7.12 0.01 1 408 . 57 HIS N N 118.4 0.1 1 409 . 58 GLU H H 8.76 0.01 1 410 . 58 GLU HA H 4.16 0.01 1 411 . 58 GLU HB2 H 1.97 0.01 2 412 . 58 GLU HB3 H 2.24 0.01 2 413 . 58 GLU HG2 H 2.24 0.01 1 414 . 58 GLU HG3 H 2.24 0.01 1 415 . 58 GLU N N 120.8 0.1 1 416 . 59 ALA H H 8.30 0.01 1 417 . 59 ALA HA H 4.35 0.01 1 418 . 59 ALA HB H 1.43 0.01 1 419 . 59 ALA N N 124.1 0.1 1 420 . 60 LEU H H 7.77 0.01 1 421 . 60 LEU HA H 4.20 0.01 1 422 . 60 LEU HB2 H 1.60 0.01 1 423 . 60 LEU HB3 H 1.58 0.01 1 424 . 60 LEU HG H 1.60 0.01 1 425 . 60 LEU HD1 H 0.90 0.01 1 426 . 60 LEU HD2 H 0.90 0.01 1 427 . 60 LEU N N 127.3 0.1 1 stop_ save_