data_6299 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of a Chordin-like Cysteine-rich Repeat (VWC module) from Collagen IIA ; _BMRB_accession_number 6299 _BMRB_flat_file_name bmr6299.str _Entry_type original _Submission_date 2004-08-26 _Accession_date 2004-08-26 _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 O'Leary J. M. . 2 Hamilton J. M. . 3 Deane C. M. . 4 Valeyev N. V. . 5 Sandell L. J. . 6 Downing A. K. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 354 "13C chemical shifts" 177 "15N chemical shifts" 65 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-12-06 original BMRB . stop_ _Original_release_date 2004-08-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Solution Structure and Dynamics of a Prototypical Chordin-like Cysteine-rich Repeat (von Willebrand Factor Type C Module) from Collagen IIA ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 15466413 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 O'Leary J. M. . 2 Hamilton J. M. . 3 Deane C. M. . 4 Valeyev N. V. . 5 Sandell L. J. . 6 Downing A. K. . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 279 _Journal_issue 51 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 53857 _Page_last 53866 _Year 2004 _Details . loop_ _Keyword '5 disulfide bonds' beta-sheet 'two sub-domain architecture' stop_ save_ ################################## # Molecular system description # ################################## save_sysytem_collagen _Saveframe_category molecular_system _Mol_system_name 'alpha 1 type II collagen isoform 1' _Abbreviation_common 'alpha 1 type II collagen isoform 1' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'alpha 1 type II collagen isoform 1' $collagen stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_collagen _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'alpha 1 type II collagen isoform 1' _Abbreviation_common 'alpha 1 type II collagen isoform 1' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 73 _Mol_residue_sequence ; YVEFQEAGSCVQDGQRYNDK DVWKPEPCRICVCDTGTVLC DDIICEDVKDCLSPEIPFGE CCPICPADLAAAA ; loop_ _Residue_seq_code _Residue_label 1 TYR 2 VAL 3 GLU 4 PHE 5 GLN 6 GLU 7 ALA 8 GLY 9 SER 10 CYS 11 VAL 12 GLN 13 ASP 14 GLY 15 GLN 16 ARG 17 TYR 18 ASN 19 ASP 20 LYS 21 ASP 22 VAL 23 TRP 24 LYS 25 PRO 26 GLU 27 PRO 28 CYS 29 ARG 30 ILE 31 CYS 32 VAL 33 CYS 34 ASP 35 THR 36 GLY 37 THR 38 VAL 39 LEU 40 CYS 41 ASP 42 ASP 43 ILE 44 ILE 45 CYS 46 GLU 47 ASP 48 VAL 49 LYS 50 ASP 51 CYS 52 LEU 53 SER 54 PRO 55 GLU 56 ILE 57 PRO 58 PHE 59 GLY 60 GLU 61 CYS 62 CYS 63 PRO 64 ILE 65 CYS 66 PRO 67 ALA 68 ASP 69 LEU 70 ALA 71 ALA 72 ALA 73 ALA 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 1U5M 'Structure Of A Chordin-Like Cysteine-Rich Repeat (Vwc Module) From Collagen Iia' 100.00 73 100.00 100.00 6.15e-34 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $collagen 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 $collagen 'recombinant technology' 'Pichia pastoris' Pichia pastoris GS115 PPICK9K-CRCOLIIA 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 $collagen 0.8 mM [U-15N] 'phosphate buffer' 50 mM . NaN3 0.02 % . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $collagen 0.8 mM [U-15N] 'phosphate buffer' 50 mM . NaN3 0.02 % . D2O 99.9 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $collagen 0.8 mM '[U-13C; U-15N]' 'phosphate buffer' 50 mM . NaN3 0.02 % . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_CYANA _Saveframe_category software _Name CYANA _Version 1.0.6 loop_ _Task refinement 'structure solution' stop_ _Details 'Guntert, P.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer GE _Model Omega _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_15N-separated_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 15N-separated NOESY' _Sample_label . save_ save_HMQC-J_2 _Saveframe_category NMR_applied_experiment _Experiment_name HMQC-J _Sample_label . save_ save_2D_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 6.0 . n/a pressure 1 . atm temperature 298 . 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 . C 13 . ppm 76.01 . . . . . 1.0 water H 1 . ppm 4.75 . . . . . 1.0 . N 15 . ppm 39.04 . . . . . 1.0 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D 15N-separated NOESY' HMQC-J '2D NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'alpha 1 type II collagen isoform 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 TYR HA H 4.231 0.03 1 2 . 1 TYR HD2 H 7.024 0.03 3 3 . 1 TYR HE2 H 6.710 0.03 3 4 . 2 VAL CA C 61.884 0.3 1 5 . 2 VAL N N 119.504 0.3 1 6 . 2 VAL H H 8.274 0.03 1 7 . 2 VAL HA H 4.048 0.03 1 8 . 2 VAL HB H 2.165 0.03 1 9 . 2 VAL HG1 H 0.826 0.03 4 10 . 3 GLU CA C 56.229 0.3 1 11 . 3 GLU CB C 29.957 0.3 1 12 . 3 GLU N N 124.588 0.3 1 13 . 3 GLU H H 8.416 0.03 1 14 . 3 GLU HA H 4.152 0.03 1 15 . 3 GLU HB2 H 1.917 0.03 2 16 . 3 GLU HG2 H 1.863 0.03 2 17 . 4 PHE CA C 57.805 0.3 1 18 . 4 PHE CB C 38.962 0.3 1 19 . 4 PHE N N 121.697 0.3 1 20 . 4 PHE H H 8.284 0.03 1 21 . 4 PHE HA H 4.506 0.03 1 22 . 4 PHE HB2 H 2.976 0.03 2 23 . 4 PHE HB3 H 3.009 0.03 2 24 . 4 PHE HD2 H 7.119 0.03 3 25 . 4 PHE HE2 H 7.214 0.03 3 26 . 5 GLN CA C 54.653 0.3 1 27 . 5 GLN CB C 29.276 0.3 1 28 . 5 GLN N N 123.450 0.3 1 29 . 5 GLN H H 8.261 0.03 1 30 . 5 GLN HA H 4.244 0.03 1 31 . 5 GLN HB2 H 1.851 0.03 2 32 . 5 GLN HB3 H 1.964 0.03 2 33 . 5 GLN HG2 H 2.220 0.03 2 34 . 5 GLN HG3 H 2.251 0.03 2 35 . 5 GLN HE21 H 6.876 0.03 2 36 . 5 GLN HE22 H 7.125 0.03 2 37 . 6 GLU CA C 57.017 0.3 1 38 . 6 GLU CB C 29.609 0.3 1 39 . 6 GLU C C 177.437 0.3 1 40 . 6 GLU N N 122.397 0.3 1 41 . 6 GLU H H 8.387 0.03 1 42 . 6 GLU HA H 4.038 0.03 1 43 . 6 GLU HB2 H 1.926 0.03 2 44 . 6 GLU HB3 H 1.991 0.03 2 45 . 6 GLU HG2 H 2.263 0.03 2 46 . 7 ALA CA C 53.578 0.3 1 47 . 7 ALA CB C 18.758 0.3 1 48 . 7 ALA C C 178.646 0.3 1 49 . 7 ALA N N 124.763 0.3 1 50 . 7 ALA H H 8.494 0.03 1 51 . 7 ALA HA H 4.245 0.03 1 52 . 7 ALA HB H 1.368 0.03 1 53 . 8 GLY CA C 45.827 0.3 1 54 . 8 GLY C C 172.339 0.3 1 55 . 8 GLY N N 110.658 0.3 1 56 . 8 GLY H H 8.715 0.03 1 57 . 8 GLY HA2 H 3.577 0.03 2 58 . 8 GLY HA3 H 3.934 0.03 2 59 . 9 SER CA C 58.335 0.3 1 60 . 9 SER CB C 64.612 0.3 1 61 . 9 SER C C 173.751 0.3 1 62 . 9 SER N N 112.039 0.3 1 63 . 9 SER H H 7.559 0.03 1 64 . 9 SER HA H 4.627 0.03 1 65 . 9 SER HB2 H 4.089 0.03 2 66 . 10 CYS CA C 56.531 0.3 1 67 . 10 CYS CB C 44.898 0.3 1 68 . 10 CYS C C 174.315 0.3 1 69 . 10 CYS N N 115.377 0.3 1 70 . 10 CYS H H 9.130 0.03 1 71 . 10 CYS HA H 5.030 0.03 1 72 . 10 CYS HB2 H 2.611 0.03 2 73 . 10 CYS HB3 H 3.106 0.03 2 74 . 11 VAL CA C 59.998 0.3 1 75 . 11 VAL CB C 38.341 0.3 1 76 . 11 VAL C C 174.412 0.3 1 77 . 11 VAL N N 120.193 0.3 1 78 . 11 VAL H H 8.413 0.03 1 79 . 11 VAL HA H 5.019 0.03 1 80 . 11 VAL HB H 1.821 0.03 1 81 . 11 VAL HG1 H 0.747 0.03 4 82 . 11 VAL HG2 H 0.729 0.03 4 83 . 12 GLN CA C 55.571 0.3 1 84 . 12 GLN CB C 34.027 0.3 1 85 . 12 GLN C C 174.748 0.3 1 86 . 12 GLN N N 124.939 0.3 1 87 . 12 GLN H H 8.844 0.03 1 88 . 12 GLN HA H 4.596 0.03 1 89 . 12 GLN HB2 H 2.231 0.03 2 90 . 12 GLN HB3 H 2.476 0.03 2 91 . 12 GLN HG2 H 1.985 0.03 2 92 . 12 GLN NE2 N 111.830 0.3 1 93 . 12 GLN HE21 H 6.242 0.03 2 94 . 12 GLN HE22 H 8.159 0.03 2 95 . 13 ASP CA C 55.534 0.3 1 96 . 13 ASP CB C 39.622 0.3 1 97 . 13 ASP C C 175.500 0.3 1 98 . 13 ASP N N 129.583 0.3 1 99 . 13 ASP H H 9.615 0.03 1 100 . 13 ASP HA H 4.310 0.03 1 101 . 13 ASP HB2 H 2.673 0.03 2 102 . 13 ASP HB3 H 2.977 0.03 2 103 . 14 GLY CA C 45.267 0.3 1 104 . 14 GLY C C 173.205 0.3 1 105 . 14 GLY N N 103.423 0.3 1 106 . 14 GLY H H 8.352 0.03 1 107 . 14 GLY HA2 H 3.494 0.03 2 108 . 14 GLY HA3 H 4.073 0.03 2 109 . 15 GLN CA C 53.650 0.3 1 110 . 15 GLN CB C 29.914 0.3 1 111 . 15 GLN C C 172.765 0.3 1 112 . 15 GLN N N 120.743 0.3 1 113 . 15 GLN H H 7.789 0.03 1 114 . 15 GLN HA H 4.302 0.03 1 115 . 15 GLN HB2 H 1.664 0.03 2 116 . 15 GLN HB3 H 1.995 0.03 2 117 . 15 GLN HG2 H 1.869 0.03 2 118 . 15 GLN HE21 H 5.878 0.03 2 119 . 15 GLN HE22 H 5.923 0.03 2 120 . 16 ARG CA C 54.592 0.3 1 121 . 16 ARG C C 174.428 0.3 1 122 . 16 ARG N N 122.130 0.3 1 123 . 16 ARG H H 7.926 0.03 1 124 . 16 ARG HA H 4.872 0.03 1 125 . 16 ARG HB2 H 1.343 0.03 2 126 . 16 ARG HB3 H 1.391 0.03 2 127 . 16 ARG HG2 H 1.297 0.03 2 128 . 16 ARG HG3 H 1.263 0.03 2 129 . 16 ARG HD2 H 2.809 0.03 2 130 . 16 ARG HD3 H 2.884 0.03 2 131 . 17 TYR CA C 57.048 0.3 1 132 . 17 TYR CB C 42.236 0.3 1 133 . 17 TYR C C 174.572 0.3 1 134 . 17 TYR N N 122.781 0.3 1 135 . 17 TYR H H 8.735 0.03 1 136 . 17 TYR HA H 4.312 0.03 1 137 . 17 TYR HB2 H 1.816 0.03 2 138 . 17 TYR HB3 H 2.869 0.03 2 139 . 17 TYR HD2 H 6.166 0.03 3 140 . 17 TYR HE2 H 5.880 0.03 3 141 . 18 ASN CA C 52.273 0.3 1 142 . 18 ASN CB C 39.778 0.3 1 143 . 18 ASN C C 175.551 0.3 1 144 . 18 ASN N N 120.637 0.3 1 145 . 18 ASN H H 9.037 0.03 1 146 . 18 ASN HA H 4.625 0.03 1 147 . 18 ASN HB2 H 2.662 0.03 2 148 . 18 ASN HB3 H 2.712 0.03 2 149 . 18 ASN ND2 N 113.695 0.3 1 150 . 18 ASN HD21 H 7.894 0.03 2 151 . 18 ASN HD22 H 6.877 0.03 2 152 . 19 ASP CA C 57.174 0.3 1 153 . 19 ASP CB C 40.638 0.3 1 154 . 19 ASP C C 177.231 0.3 1 155 . 19 ASP N N 120.131 0.3 1 156 . 19 ASP H H 8.655 0.03 1 157 . 19 ASP HA H 4.315 0.03 1 158 . 19 ASP HB2 H 2.425 0.03 2 159 . 19 ASP HB3 H 2.747 0.03 2 160 . 20 LYS CA C 58.522 0.3 1 161 . 20 LYS CB C 29.597 0.3 1 162 . 20 LYS N N 120.100 0.3 1 163 . 20 LYS H H 9.102 0.03 1 164 . 20 LYS HA H 3.895 0.03 1 165 . 20 LYS HB2 H 2.010 0.03 2 166 . 20 LYS HB3 H 2.446 0.03 2 167 . 20 LYS HG2 H 1.369 0.03 2 168 . 20 LYS HD2 H 1.659 0.03 2 169 . 20 LYS HE2 H 2.967 0.03 2 170 . 21 ASP CA C 56.051 0.3 1 171 . 21 ASP CB C 41.446 0.3 1 172 . 21 ASP C C 174.419 0.3 1 173 . 21 ASP N N 121.903 0.3 1 174 . 21 ASP H H 8.501 0.03 1 175 . 21 ASP HA H 4.725 0.03 1 176 . 21 ASP HB2 H 2.892 0.03 2 177 . 21 ASP HB3 H 3.326 0.03 2 178 . 22 VAL CA C 60.171 0.3 1 179 . 22 VAL CB C 34.892 0.3 1 180 . 22 VAL CG1 C 21.085 0.3 2 181 . 22 VAL C C 176.154 0.3 1 182 . 22 VAL N N 116.760 0.3 1 183 . 22 VAL H H 7.945 0.03 1 184 . 22 VAL HA H 5.241 0.03 1 185 . 22 VAL HB H 1.885 0.03 1 186 . 22 VAL HG1 H 0.987 0.03 4 187 . 22 VAL HG2 H 0.860 0.03 4 188 . 23 TRP CA C 56.775 0.3 1 189 . 23 TRP CB C 32.014 0.3 1 190 . 23 TRP C C 172.351 0.3 1 191 . 23 TRP N N 127.762 0.3 1 192 . 23 TRP H H 8.988 0.03 1 193 . 23 TRP HA H 4.970 0.03 1 194 . 23 TRP HB2 H 3.019 0.03 2 195 . 23 TRP HB3 H 3.241 0.03 2 196 . 23 TRP NE1 N 126.347 0.3 1 197 . 23 TRP HD1 H 6.534 0.03 1 198 . 23 TRP HE3 H 6.601 0.03 1 199 . 23 TRP HE1 H 9.701 0.03 1 200 . 23 TRP HZ3 H 6.491 0.03 1 201 . 23 TRP HZ2 H 6.436 0.03 1 202 . 23 TRP HH2 H 6.186 0.03 1 203 . 24 LYS CA C 52.513 0.3 1 204 . 24 LYS N N 117.962 0.3 1 205 . 24 LYS H H 8.500 0.03 1 206 . 24 LYS HA H 5.430 0.03 1 207 . 24 LYS HB2 H 2.004 0.03 2 208 . 24 LYS HG2 H 1.446 0.03 2 209 . 24 LYS HG3 H 1.481 0.03 2 210 . 24 LYS HD2 H 1.604 0.03 2 211 . 24 LYS HE2 H 2.981 0.03 2 212 . 24 LYS HE3 H 3.061 0.03 2 213 . 25 PRO CA C 64.015 0.3 1 214 . 25 PRO CB C 32.131 0.3 1 215 . 25 PRO CD C 50.551 0.3 1 216 . 25 PRO HA H 4.623 0.03 1 217 . 25 PRO HB2 H 2.168 0.03 2 218 . 25 PRO HB3 H 2.501 0.03 2 219 . 25 PRO HG2 H 1.904 0.03 2 220 . 25 PRO HG3 H 1.945 0.03 2 221 . 25 PRO HD2 H 3.146 0.03 2 222 . 25 PRO HD3 H 3.899 0.03 2 223 . 26 GLU CA C 53.703 0.3 1 224 . 26 GLU N N 113.161 0.3 1 225 . 26 GLU H H 7.557 0.03 1 226 . 26 GLU HA H 4.627 0.03 1 227 . 26 GLU HB2 H 1.866 0.03 2 228 . 26 GLU HG2 H 2.135 0.03 2 229 . 26 GLU HG3 H 2.292 0.03 2 230 . 27 PRO CA C 66.403 0.3 1 231 . 27 PRO CB C 31.997 0.3 1 232 . 27 PRO CD C 49.905 0.3 1 233 . 27 PRO C C 177.478 0.3 1 234 . 27 PRO HA H 4.058 0.03 1 235 . 27 PRO HB2 H 1.705 0.03 2 236 . 27 PRO HB3 H 1.914 0.03 2 237 . 27 PRO HG2 H 2.195 0.03 2 238 . 27 PRO HG3 H 1.991 0.03 2 239 . 27 PRO HD2 H 3.714 0.03 2 240 . 27 PRO HD3 H 3.702 0.03 2 241 . 28 CYS CA C 53.223 0.3 1 242 . 28 CYS CB C 41.241 0.3 1 243 . 28 CYS C C 173.726 0.3 1 244 . 28 CYS N N 108.859 0.3 1 245 . 28 CYS H H 8.428 0.03 1 246 . 28 CYS HA H 4.852 0.03 1 247 . 28 CYS HB2 H 2.944 0.03 2 248 . 28 CYS HB3 H 3.728 0.03 2 249 . 29 ARG CA C 55.227 0.3 1 250 . 29 ARG C C 175.582 0.3 1 251 . 29 ARG N N 123.457 0.3 1 252 . 29 ARG H H 7.844 0.03 1 253 . 29 ARG HA H 5.113 0.03 1 254 . 29 ARG HB2 H 1.554 0.03 2 255 . 29 ARG HG2 H 1.437 0.03 2 256 . 29 ARG HD2 H 2.981 0.03 2 257 . 29 ARG HD3 H 3.060 0.03 2 258 . 30 ILE CA C 59.129 0.3 1 259 . 30 ILE C C 174.140 0.3 1 260 . 30 ILE N N 120.357 0.3 1 261 . 30 ILE H H 8.505 0.03 1 262 . 30 ILE HA H 4.634 0.03 1 263 . 30 ILE HB H 1.415 0.03 1 264 . 30 ILE HG2 H 0.744 0.03 1 265 . 30 ILE HD1 H 0.744 0.03 1 266 . 31 CYS CA C 54.314 0.3 1 267 . 31 CYS CB C 47.318 0.3 1 268 . 31 CYS C C 169.736 0.3 1 269 . 31 CYS N N 125.160 0.3 1 270 . 31 CYS H H 8.836 0.03 1 271 . 31 CYS HA H 5.131 0.03 1 272 . 31 CYS HB2 H 0.481 0.03 2 273 . 31 CYS HB3 H 1.423 0.03 2 274 . 32 VAL CA C 58.397 0.3 1 275 . 32 VAL CB C 35.925 0.3 1 276 . 32 VAL C C 173.735 0.3 1 277 . 32 VAL N N 116.593 0.3 1 278 . 32 VAL H H 8.287 0.03 1 279 . 32 VAL HA H 5.039 0.03 1 280 . 32 VAL HB H 1.834 0.03 1 281 . 32 VAL HG1 H 0.837 0.03 4 282 . 32 VAL HG2 H 0.820 0.03 4 283 . 33 CYS CA C 53.044 0.3 1 284 . 33 CYS CB C 38.686 0.3 1 285 . 33 CYS C C 173.702 0.3 1 286 . 33 CYS N N 122.202 0.3 1 287 . 33 CYS H H 8.154 0.03 1 288 . 33 CYS HA H 5.286 0.03 1 289 . 33 CYS HB2 H 3.025 0.03 2 290 . 33 CYS HB3 H 3.480 0.03 2 291 . 34 ASP CA C 52.071 0.3 1 292 . 34 ASP CB C 38.532 0.3 1 293 . 34 ASP C C 176.203 0.3 1 294 . 34 ASP N N 130.486 0.3 1 295 . 34 ASP H H 9.486 0.03 1 296 . 34 ASP HA H 5.260 0.03 1 297 . 34 ASP HB2 H 2.346 0.03 2 298 . 34 ASP HB3 H 2.921 0.03 2 299 . 35 THR CA C 61.870 0.3 1 300 . 35 THR CB C 67.836 0.3 1 301 . 35 THR C C 175.098 0.3 1 302 . 35 THR N N 120.933 0.3 1 303 . 35 THR H H 9.498 0.03 1 304 . 35 THR HA H 4.328 0.03 1 305 . 35 THR HB H 3.681 0.03 1 306 . 35 THR HG2 H 1.303 0.03 1 307 . 36 GLY CA C 45.333 0.3 1 308 . 36 GLY C C 174.680 0.3 1 309 . 36 GLY N N 106.115 0.3 1 310 . 36 GLY H H 6.962 0.03 1 311 . 36 GLY HA2 H 3.830 0.03 2 312 . 36 GLY HA3 H 4.260 0.03 2 313 . 37 THR CA C 62.603 0.3 1 314 . 37 THR CB C 70.790 0.3 1 315 . 37 THR C C 172.267 0.3 1 316 . 37 THR N N 119.744 0.3 1 317 . 37 THR H H 7.977 0.03 1 318 . 37 THR HA H 4.475 0.03 1 319 . 37 THR HB H 4.137 0.03 1 320 . 37 THR HG2 H 1.175 0.03 1 321 . 38 VAL CA C 62.533 0.3 1 322 . 38 VAL CB C 32.126 0.3 1 323 . 38 VAL CG1 C 23.501 0.3 2 324 . 38 VAL C C 175.221 0.3 1 325 . 38 VAL N N 127.742 0.3 1 326 . 38 VAL H H 8.807 0.03 1 327 . 38 VAL HA H 4.577 0.03 1 328 . 38 VAL HB H 2.088 0.03 1 329 . 38 VAL HG1 H 1.106 0.03 4 330 . 38 VAL HG2 H 0.955 0.03 4 331 . 39 LEU CA C 54.008 0.3 1 332 . 39 LEU CB C 43.189 0.3 1 333 . 39 LEU N N 130.882 0.3 1 334 . 39 LEU H H 8.832 0.03 1 335 . 39 LEU HA H 4.727 0.03 1 336 . 39 LEU HB2 H 1.656 0.03 2 337 . 39 LEU HB3 H 1.488 0.03 2 338 . 39 LEU HG H 1.457 0.03 1 339 . 39 LEU HD1 H 0.893 0.03 4 340 . 39 LEU HD2 H 0.844 0.03 4 341 . 40 CYS CA C 54.795 0.3 1 342 . 40 CYS CB C 47.834 0.3 1 343 . 40 CYS C C 172.417 0.3 1 344 . 40 CYS N N 121.163 0.3 1 345 . 40 CYS H H 8.624 0.03 1 346 . 40 CYS HA H 5.627 0.03 1 347 . 40 CYS HB2 H 2.423 0.03 2 348 . 40 CYS HB3 H 2.954 0.03 2 349 . 41 ASP CA C 44.807 0.3 1 350 . 41 ASP CB C 44.987 0.3 1 351 . 41 ASP N N 121.413 0.3 1 352 . 41 ASP H H 9.087 0.03 1 353 . 41 ASP HA H 4.872 0.03 1 354 . 41 ASP HB2 H 2.312 0.03 2 355 . 41 ASP HB3 H 2.492 0.03 2 356 . 42 ASP CA C 55.203 0.3 1 357 . 42 ASP CB C 41.845 0.3 1 358 . 42 ASP N N 120.200 0.3 1 359 . 42 ASP H H 8.407 0.03 1 360 . 42 ASP HA H 5.070 0.03 1 361 . 42 ASP HB2 H 2.356 0.03 2 362 . 42 ASP HB3 H 2.587 0.03 2 363 . 43 ILE CA C 61.961 0.3 1 364 . 43 ILE CB C 38.226 0.3 1 365 . 43 ILE C C 174.473 0.3 1 366 . 43 ILE N N 123.936 0.3 1 367 . 43 ILE H H 8.143 0.03 1 368 . 43 ILE HA H 3.823 0.03 1 369 . 43 ILE HB H 1.769 0.03 1 370 . 43 ILE HG2 H 0.822 0.03 1 371 . 43 ILE HG12 H 1.001 0.03 2 372 . 43 ILE HG13 H 1.388 0.03 2 373 . 43 ILE HD1 H 0.750 0.03 1 374 . 44 ILE CA C 59.812 0.3 1 375 . 44 ILE CB C 41.623 0.3 1 376 . 44 ILE C C 176.384 0.3 1 377 . 44 ILE N N 127.259 0.3 1 378 . 44 ILE H H 8.339 0.03 1 379 . 44 ILE HA H 4.221 0.03 1 380 . 44 ILE HB H 1.785 0.03 1 381 . 44 ILE HG2 H 0.787 0.03 1 382 . 44 ILE HG12 H 1.180 0.03 2 383 . 44 ILE HG13 H 1.422 0.03 2 384 . 44 ILE HD1 H 0.822 0.03 1 385 . 45 CYS CA C 52.528 0.3 1 386 . 45 CYS CB C 37.858 0.3 1 387 . 45 CYS C C 175.141 0.3 1 388 . 45 CYS N N 126.074 0.3 1 389 . 45 CYS H H 8.752 0.03 1 390 . 45 CYS HA H 4.897 0.03 1 391 . 45 CYS HB2 H 2.620 0.03 1 392 . 45 CYS HB3 H 3.335 0.03 1 393 . 46 GLU CA C 55.943 0.3 1 394 . 46 GLU CB C 29.827 0.3 1 395 . 46 GLU C C 176.230 0.3 1 396 . 46 GLU N N 123.635 0.3 1 397 . 46 GLU H H 8.808 0.03 1 398 . 46 GLU HA H 4.272 0.03 1 399 . 46 GLU HB2 H 2.001 0.03 2 400 . 46 GLU HB3 H 1.900 0.03 2 401 . 46 GLU HG2 H 2.288 0.03 2 402 . 47 ASP CA C 54.889 0.3 1 403 . 47 ASP CB C 40.607 0.3 1 404 . 47 ASP N N 122.925 0.3 1 405 . 47 ASP H H 8.609 0.03 1 406 . 47 ASP HA H 4.435 0.03 1 407 . 47 ASP HB2 H 2.603 0.03 2 408 . 47 ASP HB3 H 2.568 0.03 2 409 . 48 VAL CA C 61.818 0.3 1 410 . 48 VAL CB C 32.580 0.3 1 411 . 48 VAL C C 176.161 0.3 1 412 . 48 VAL N N 121.449 0.3 1 413 . 48 VAL H H 8.343 0.03 1 414 . 48 VAL HA H 4.221 0.03 1 415 . 48 VAL HB H 2.101 0.03 1 416 . 48 VAL HG1 H 0.857 0.03 4 417 . 49 LYS CA C 56.444 0.3 1 418 . 49 LYS C C 176.501 0.3 1 419 . 49 LYS N N 123.842 0.3 1 420 . 49 LYS H H 8.449 0.03 1 421 . 49 LYS HA H 4.307 0.03 1 422 . 49 LYS HB2 H 1.757 0.03 2 423 . 49 LYS HB3 H 1.809 0.03 2 424 . 49 LYS HG2 H 1.357 0.03 2 425 . 49 LYS HG3 H 1.366 0.03 2 426 . 49 LYS HD2 H 2.448 0.03 2 427 . 49 LYS HE2 H 2.985 0.03 2 428 . 49 LYS HE3 H 3.066 0.03 2 429 . 50 ASP CA C 54.510 0.3 1 430 . 50 ASP CB C 39.907 0.3 1 431 . 50 ASP C C 174.446 0.3 1 432 . 50 ASP N N 117.722 0.3 1 433 . 50 ASP H H 8.368 0.03 1 434 . 50 ASP HA H 4.475 0.03 1 435 . 50 ASP HB2 H 2.620 0.03 2 436 . 50 ASP HB3 H 2.750 0.03 2 437 . 51 CYS CA C 55.553 0.3 1 438 . 51 CYS CB C 43.586 0.3 1 439 . 51 CYS N N 116.087 0.3 1 440 . 51 CYS H H 7.764 0.03 1 441 . 51 CYS HA H 4.734 0.03 1 442 . 51 CYS HB2 H 3.136 0.03 2 443 . 52 LEU CA C 56.946 0.3 1 444 . 52 LEU CB C 42.258 0.3 1 445 . 52 LEU C C 177.679 0.3 1 446 . 52 LEU N N 125.885 0.3 1 447 . 52 LEU H H 8.750 0.03 1 448 . 52 LEU HA H 4.209 0.03 1 449 . 52 LEU HB2 H 1.666 0.03 2 450 . 52 LEU HG H 1.571 0.03 1 451 . 52 LEU HD1 H 0.908 0.03 4 452 . 52 LEU HD2 H 0.860 0.03 4 453 . 53 SER CA C 54.662 0.3 1 454 . 53 SER CB C 63.453 0.3 1 455 . 53 SER N N 110.993 0.3 1 456 . 53 SER H H 7.770 0.03 1 457 . 53 SER HA H 4.799 0.03 1 458 . 53 SER HB2 H 3.590 0.03 2 459 . 53 SER HB3 H 3.893 0.03 2 460 . 54 PRO CA C 63.487 0.3 1 461 . 54 PRO CB C 32.804 0.3 1 462 . 54 PRO CD C 49.992 0.3 1 463 . 54 PRO C C 176.009 0.3 1 464 . 54 PRO HA H 4.768 0.03 1 465 . 54 PRO HB2 H 1.769 0.03 2 466 . 54 PRO HB3 H 1.947 0.03 2 467 . 54 PRO HG2 H 1.877 0.03 2 468 . 54 PRO HD2 H 3.298 0.03 2 469 . 54 PRO HD3 H 3.594 0.03 2 470 . 55 GLU CA C 54.438 0.3 1 471 . 55 GLU CB C 33.627 0.3 1 472 . 55 GLU N N 118.200 0.3 1 473 . 55 GLU H H 8.635 0.03 1 474 . 55 GLU HA H 4.695 0.03 1 475 . 55 GLU HB2 H 1.779 0.03 2 476 . 55 GLU HB3 H 2.074 0.03 2 477 . 55 GLU HG2 H 1.916 0.03 2 478 . 56 ILE CA C 59.020 0.3 1 479 . 56 ILE CB C 38.686 0.3 1 480 . 56 ILE CG1 C 28.073 0.3 2 481 . 56 ILE CG2 C 13.146 0.3 2 482 . 56 ILE N N 124.324 0.3 1 483 . 56 ILE H H 8.800 0.03 1 484 . 56 ILE HA H 4.446 0.03 1 485 . 56 ILE HB H 1.658 0.03 1 486 . 56 ILE HG2 H 0.590 0.03 1 487 . 56 ILE HG12 H 0.862 0.03 2 488 . 56 ILE HG13 H 1.545 0.03 2 489 . 56 ILE HD1 H 0.469 0.03 1 490 . 57 PRO CA C 61.889 0.3 1 491 . 57 PRO CB C 31.838 0.3 1 492 . 57 PRO CD C 52.150 0.3 1 493 . 57 PRO C C 176.311 0.3 1 494 . 57 PRO HA H 4.375 0.03 1 495 . 57 PRO HB2 H 1.629 0.03 2 496 . 57 PRO HB3 H 2.392 0.03 2 497 . 57 PRO HG2 H 1.853 0.03 2 498 . 57 PRO HG3 H 2.010 0.03 2 499 . 57 PRO HD2 H 3.427 0.03 2 500 . 57 PRO HD3 H 4.294 0.03 2 501 . 58 PHE CA C 60.204 0.3 1 502 . 58 PHE CB C 38.432 0.3 1 503 . 58 PHE C C 177.396 0.3 1 504 . 58 PHE N N 121.639 0.3 1 505 . 58 PHE H H 8.506 0.03 1 506 . 58 PHE HA H 4.232 0.03 1 507 . 58 PHE HB2 H 2.884 0.03 2 508 . 58 PHE HB3 H 3.217 0.03 2 509 . 58 PHE HD2 H 7.267 0.03 3 510 . 58 PHE HE2 H 7.383 0.03 3 511 . 58 PHE HZ H 7.336 0.03 1 512 . 59 GLY CA C 44.739 0.3 1 513 . 59 GLY C C 173.453 0.3 1 514 . 59 GLY N N 114.836 0.3 1 515 . 59 GLY H H 8.323 0.03 1 516 . 59 GLY HA2 H 3.256 0.03 2 517 . 59 GLY HA3 H 3.897 0.03 2 518 . 60 GLU CA C 54.080 0.3 1 519 . 60 GLU C C 174.541 0.3 1 520 . 60 GLU N N 117.893 0.3 1 521 . 60 GLU H H 7.919 0.03 1 522 . 60 GLU HA H 4.554 0.03 1 523 . 60 GLU HB2 H 1.842 0.03 2 524 . 60 GLU HG2 H 2.016 0.03 2 525 . 60 GLU HG3 H 2.181 0.03 2 526 . 61 CYS CA C 57.659 0.3 1 527 . 61 CYS C C 175.100 0.3 1 528 . 61 CYS N N 115.263 0.3 1 529 . 61 CYS H H 8.229 0.03 1 530 . 61 CYS HA H 4.259 0.03 1 531 . 61 CYS HB2 H 2.992 0.03 2 532 . 61 CYS HB3 H 3.068 0.03 2 533 . 62 CYS CA C 50.998 0.3 1 534 . 62 CYS CB C 38.272 0.3 1 535 . 62 CYS N N 114.334 0.3 1 536 . 62 CYS H H 7.883 0.03 1 537 . 62 CYS HA H 5.191 0.03 1 538 . 62 CYS HB2 H 2.556 0.03 2 539 . 62 CYS HB3 H 3.438 0.03 2 540 . 63 PRO CA C 62.311 0.3 1 541 . 63 PRO CB C 32.476 0.3 1 542 . 63 PRO CD C 50.560 0.3 1 543 . 63 PRO C C 175.718 0.3 1 544 . 63 PRO HA H 4.516 0.03 1 545 . 63 PRO HB2 H 1.680 0.03 2 546 . 63 PRO HG2 H 2.006 0.03 2 547 . 63 PRO HG3 H 2.058 0.03 2 548 . 63 PRO HD2 H 3.767 0.03 2 549 . 63 PRO HD3 H 3.847 0.03 2 550 . 64 ILE CA C 59.310 0.3 1 551 . 64 ILE CB C 42.059 0.3 1 552 . 64 ILE C C 174.808 0.3 1 553 . 64 ILE N N 115.753 0.3 1 554 . 64 ILE H H 8.833 0.03 1 555 . 64 ILE HA H 4.550 0.03 1 556 . 64 ILE HB H 1.855 0.03 1 557 . 64 ILE HG2 H 0.874 0.03 1 558 . 64 ILE HG12 H 1.099 0.03 2 559 . 64 ILE HG13 H 1.301 0.03 2 560 . 64 ILE HD1 H 0.757 0.03 1 561 . 65 CYS CA C 52.762 0.3 1 562 . 65 CYS CB C 41.217 0.3 1 563 . 65 CYS N N 121.678 0.3 1 564 . 65 CYS H H 8.886 0.03 1 565 . 65 CYS HA H 5.267 0.03 1 566 . 65 CYS HB2 H 2.697 0.03 2 567 . 65 CYS HB3 H 3.282 0.03 2 568 . 66 PRO CA C 63.581 0.3 1 569 . 66 PRO CB C 32.131 0.3 1 570 . 66 PRO CD C 51.747 0.3 1 571 . 66 PRO HA H 4.294 0.03 1 572 . 66 PRO HB2 H 1.949 0.03 2 573 . 66 PRO HG2 H 2.082 0.03 2 574 . 66 PRO HD2 H 3.784 0.03 2 575 . 66 PRO HD3 H 3.952 0.03 2 576 . 67 ALA CA C 52.784 0.3 1 577 . 67 ALA N N 122.924 0.3 1 578 . 67 ALA H H 8.331 0.03 1 579 . 67 ALA HA H 4.325 0.03 1 580 . 67 ALA HB H 1.375 0.03 1 581 . 68 ASP CA C 54.200 0.3 1 582 . 68 ASP CB C 41.105 0.3 1 583 . 68 ASP N N 118.170 0.3 1 584 . 68 ASP H H 8.183 0.03 1 585 . 68 ASP HA H 4.563 0.03 1 586 . 68 ASP HB2 H 2.576 0.03 2 587 . 68 ASP HB3 H 2.629 0.03 2 588 . 69 LEU CA C 55.210 0.3 1 589 . 69 LEU N N 121.984 0.3 1 590 . 69 LEU H H 7.968 0.03 1 591 . 69 LEU HA H 4.276 0.03 1 592 . 69 LEU HB2 H 1.410 0.03 2 593 . 69 LEU HB3 H 1.503 0.03 2 594 . 69 LEU HG H 1.651 0.03 1 595 . 69 LEU HD1 H 0.898 0.03 4 596 . 69 LEU HD2 H 0.850 0.03 4 stop_ save_