data_4396 #Corrected using PDB structure: 2H9EC # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 9 N HA 3.73 5.08 # 30 E HA 4.31 3.51 # 65 V HA 5.14 4.44 # 71 E HA 4.23 3.36 # 78 I HA 4.04 4.87 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.01 N/A N/A N/A 0.46 0.05 # #bmr4396.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4396.str file): #HA CA CB CO N HN #N/A N/A N/A N/A +0.46 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.05 N/A N/A N/A +/-0.69 +/-0.13 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.616 N/A N/A N/A 0.623 0.292 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.170 N/A N/A N/A 2.455 0.447 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Anticoagulant protein from the nematode Ancylostoma caninum ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Duggan Brendan M. . 2 Dyson H. Jane . 3 Wright Peter E. . stop_ _BMRB_accession_number 4396 _BMRB_flat_file_name bmr4396.str _Entry_type new _Submission_date 1999-09-09 _Accession_date 1999-09-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 463 '13C chemical shifts' 22 '15N chemical shifts' 85 'coupling constants' 76 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2 ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 99435967 _PubMed_ID 10504384 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Duggan Brendan M. . 2 Dyson H. Jane . 3 Wright Peter E. . stop_ _Journal_abbreviation 'Eur. J. Biochem.' _Journal_name_full . _Journal_volume 265 _Journal_issue . _Page_first 539 _Page_last 548 _Year 1999 loop_ _Keyword anticoagulant "protease inhibitor" stop_ save_ ################################## # Molecular system description # ################################## save_system_NAPc2 _Saveframe_category molecular_system _Mol_system_name "Nematode Anticoagulant Protein c2" _Abbreviation_common NAPc2 loop_ _Mol_system_component_name _Mol_label NAPc2 $NAPc2 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function "protease inhibitor" anticoagulant stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1COUA " Chain A, Anticoagulant Protein From The Nematode Ancylostoma Caninum" . stop_ save_ ######################## # Monomeric polymers # ######################## save_NAPc2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Nematode Anticoagulant Protein c2" _Abbreviation_common NAPc2 _Molecular_mass 9643 _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Sequence_citation_label $ref_4 ############################## # Polymer residue sequence # ############################## _Residue_count 85 _Mol_residue_sequence ; KATMQCGENEKYDSCGSKEC DKKCKYDGVEEEDDEEPNVP CLVRVCHQDCVCEEGFYRNK DDKCVSAEDCELDNMDFIYP GTRNP ; loop_ _Residue_seq_code _Residue_label 1 LYS 2 ALA 3 THR 4 MET 5 GLN 6 CYS 7 GLY 8 GLU 9 ASN 10 GLU 11 LYS 12 TYR 13 ASP 14 SER 15 CYS 16 GLY 17 SER 18 LYS 19 GLU 20 CYS 21 ASP 22 LYS 23 LYS 24 CYS 25 LYS 26 TYR 27 ASP 28 GLY 29 VAL 30 GLU 31 GLU 32 GLU 33 ASP 34 ASP 35 GLU 36 GLU 37 PRO 38 ASN 39 VAL 40 PRO 41 CYS 42 LEU 43 VAL 44 ARG 45 VAL 46 CYS 47 HIS 48 GLN 49 ASP 50 CYS 51 VAL 52 CYS 53 GLU 54 GLU 55 GLY 56 PHE 57 TYR 58 ARG 59 ASN 60 LYS 61 ASP 62 ASP 63 LYS 64 CYS 65 VAL 66 SER 67 ALA 68 GLU 69 ASP 70 CYS 71 GLU 72 LEU 73 ASP 74 ASN 75 MET 76 ASP 77 PHE 78 ILE 79 TYR 80 PRO 81 GLY 82 THR 83 ARG 84 ASN 85 PRO stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-07-16 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 1COU "A Chain A, Anticoagulant Protein From TheNematode Ancylostoma Caninum" 100.00 85 100 100 4e-49 GenBank AAC47080.1 "anti-coagulant protein C2 precursor" 93.41 91 100 100 2e-48 PRF 2208501A "anticoagulant protein:ISOTYPE=C2" 93.41 91 100 100 2e-48 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_atom_name single disulfide NAPc2 6 SG NAPc2 50 SG single disulfide NAPc2 15 SG NAPc2 46 SG single disulfide NAPc2 20 SG NAPc2 41 SG single disulfide NAPc2 24 SG NAPc2 70 SG single disulfide NAPc2 52 SG NAPc2 64 SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $NAPc2 "dog hookworm" 29170 Eukaryota Metazoa Ancylostoma caninum 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 $NAPc2 'recombinant technology' "Pichia pastoris" Pichia pastoris GS115 pYAM7SP8 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; The 15N label is around 50-60% ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $NAPc2 2.0 mM "[U-55% 15N]" 'sodium chloride' 50 mM . DSS 20 uM . stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version "95 and 97" loop_ _Task "data processing and analysis" stop_ save_ save_Dyana _Saveframe_category software _Name Dyana _Version 1.5 loop_ _Task "molecular dynamics" stop_ _Citation_label $ref_22 save_ save_Amber _Saveframe_category software _Name Amber _Version 5.1 loop_ _Task "molecular dynamics" stop_ save_ save_Procheck-NMR _Saveframe_category software _Name Procheck-NMR _Version 3.4.4 loop_ _Task "structure analysis" stop_ _Citation_label $ref_24 save_ save_SANE _Saveframe_category software _Name SANE _Version 1 loop_ _Task "In-house software: automated NOESY assignment and restraint generation" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 save_ save_NMR_spectrometer2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 save_ save_NMR_spectrometer3 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 save_ save_NMR_spectrometer4 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 500 save_ save_NMR_spectrometer5 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; NOESY DQ-COSY 15N HSQC 15N NOESY-HSQC 15N TOCSY-HSQC 15N HSQC-NOESY-HSQ HNHA 13C HSQC 15N {1H} NOE ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.5 0.05 n/a temperature 298 1 K 'ionic strength' 0.05 0.01 M pressure 1 . atm stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chem_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name NAPc2 loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 LYS HA H 3.99 . . 2 1 LYS HB2 H 1.89 . . 3 1 LYS HB3 H 1.89 . . 4 1 LYS HG2 H 1.44 . . 5 1 LYS HG3 H 1.44 . . 6 2 ALA N N 128.20 . . 7 2 ALA CB C 19.30 . . 8 2 ALA H H 8.71 . . 9 2 ALA HA H 4.39 . . 10 2 ALA HB H 1.36 . . 11 3 THR N N 115.64 . . 12 3 THR CG2 C 21.50 . . 13 3 THR H H 8.12 . . 14 3 THR HA H 4.16 . . 15 3 THR HB H 3.99 . . 16 3 THR HG2 H 1.11 . . 17 4 MET N N 123.27 . . 18 4 MET CE C 17.10 . . 19 4 MET H H 7.74 . . 20 4 MET HA H 4.30 . . 21 4 MET HB2 H 1.91 . . 22 4 MET HB3 H 1.83 . . 23 4 MET HG2 H 2.37 . . 24 4 MET HG3 H 2.32 . . 25 4 MET HE H 2.08 . . 26 5 GLN N N 123.79 . . 27 5 GLN NE2 N 113.70 . . 28 5 GLN H H 8.36 . . 29 5 GLN HA H 4.37 . . 30 5 GLN HB2 H 2.06 . . 31 5 GLN HB3 H 1.94 . . 32 5 GLN HG2 H 2.33 . . 33 5 GLN HG3 H 2.33 . . 34 5 GLN HE21 H 7.49 . . 35 5 GLN HE22 H 6.78 . . 36 6 CYS N N 123.21 . . 37 6 CYS H H 8.52 . . 38 6 CYS HA H 5.05 . . 39 6 CYS HB2 H 3.37 . . 40 6 CYS HB3 H 2.64 . . 41 7 GLY N N 110.19 . . 42 7 GLY H H 8.44 . . 43 7 GLY HA2 H 4.36 . . 44 7 GLY HA3 H 3.58 . . 45 8 GLU N N 121.52 . . 46 8 GLU H H 8.30 . . 47 8 GLU HA H 3.93 . . 48 8 GLU HB2 H 1.93 . . 49 8 GLU HB3 H 1.93 . . 50 8 GLU HG2 H 2.33 . . 51 8 GLU HG3 H 2.33 . . 52 9 ASN N N 118.97 . . 53 9 ASN ND2 N 116.19 . . 54 9 ASN H H 8.94 . . 55 9 ASN HA H 3.73 . . 56 9 ASN HB2 H 2.65 . . 57 9 ASN HB3 H 1.25 . . 58 9 ASN HD21 H 7.35 . . 59 9 ASN HD22 H 6.84 . . 60 10 GLU N N 114.86 . . 61 10 GLU H H 7.19 . . 62 10 GLU HA H 5.15 . . 63 10 GLU HB2 H 1.94 . . 64 10 GLU HB3 H 1.61 . . 65 10 GLU HG2 H 2.13 . . 66 10 GLU HG3 H 2.07 . . 67 11 LYS N N 119.68 . . 68 11 LYS CG C 23.80 . . 69 11 LYS H H 9.52 . . 70 11 LYS HA H 4.69 . . 71 11 LYS HB2 H 1.71 . . 72 11 LYS HG2 H 1.18 . . 73 11 LYS HD2 H 1.64 . . 74 11 LYS HD3 H 1.64 . . 75 12 TYR N N 124.95 . . 76 12 TYR H H 8.59 . . 77 12 TYR HA H 4.62 . . 78 12 TYR HB2 H 3.07 . . 79 12 TYR HB3 H 2.78 . . 80 12 TYR HD1 H 6.92 . . 81 12 TYR HD2 H 6.92 . . 82 12 TYR HE1 H 6.69 . . 83 12 TYR HE2 H 6.69 . . 84 13 ASP N N 130.96 . . 85 13 ASP H H 8.45 . . 86 13 ASP HA H 4.59 . . 87 13 ASP HB2 H 2.51 . . 88 13 ASP HB3 H 2.23 . . 89 14 SER N N 120.66 . . 90 14 SER H H 8.36 . . 91 14 SER HA H 4.59 . . 92 14 SER HB2 H 4.04 . . 93 14 SER HB3 H 3.91 . . 94 15 CYS N N 125.31 . . 95 15 CYS H H 8.65 . . 96 15 CYS HA H 4.59 . . 97 15 CYS HB2 H 3.42 . . 98 15 CYS HB3 H 2.57 . . 99 16 GLY N N 111.85 . . 100 16 GLY H H 8.24 . . 101 16 GLY HA2 H 4.39 . . 102 16 GLY HA3 H 3.40 . . 103 17 SER N N 111.63 . . 104 17 SER H H 8.12 . . 105 17 SER HA H 4.88 . . 106 17 SER HB2 H 3.85 . . 107 17 SER HB3 H 3.55 . . 108 18 LYS N N 131.62 . . 109 18 LYS H H 9.25 . . 110 18 LYS HA H 4.16 . . 111 18 LYS HB2 H 1.89 . . 112 18 LYS HB3 H 1.75 . . 113 18 LYS HG2 H 1.44 . . 114 18 LYS HG3 H 1.44 . . 115 18 LYS HD2 H 1.59 . . 116 18 LYS HD3 H 1.59 . . 117 19 GLU N N 120.73 . . 118 19 GLU H H 8.55 . . 119 19 GLU HA H 4.17 . . 120 19 GLU HB2 H 2.10 . . 121 19 GLU HB3 H 1.98 . . 122 19 GLU HG2 H 2.39 . . 123 19 GLU HG3 H 2.39 . . 124 20 CYS N N 115.58 . . 125 20 CYS H H 7.64 . . 126 20 CYS HA H 4.78 . . 127 20 CYS HB2 H 3.48 . . 128 20 CYS HB3 H 3.11 . . 129 21 ASP N N 123.58 . . 130 21 ASP H H 7.48 . . 131 21 ASP HA H 4.55 . . 132 21 ASP HB2 H 2.80 . . 133 21 ASP HB3 H 2.73 . . 134 22 LYS N N 124.21 . . 135 22 LYS H H 8.94 . . 136 22 LYS HA H 4.35 . . 137 22 LYS HB2 H 1.95 . . 138 22 LYS HB3 H 1.95 . . 139 22 LYS HG2 H 1.56 . . 140 22 LYS HG3 H 1.56 . . 141 22 LYS HD2 H 1.70 . . 142 22 LYS HD3 H 1.70 . . 143 23 LYS N N 122.52 . . 144 23 LYS H H 8.59 . . 145 23 LYS HA H 4.98 . . 146 23 LYS HB2 H 2.10 . . 147 23 LYS HB3 H 2.10 . . 148 23 LYS HG2 H 1.56 . . 149 23 LYS HG3 H 1.56 . . 150 23 LYS HD2 H 1.70 . . 151 23 LYS HD3 H 1.70 . . 152 24 CYS N N 120.59 . . 153 24 CYS H H 8.40 . . 154 24 CYS HA H 4.08 . . 155 24 CYS HB2 H 2.72 . . 156 24 CYS HB3 H 2.64 . . 157 25 LYS HA H 4.20 . . 158 25 LYS HB2 H 2.10 . . 159 25 LYS HB3 H 1.98 . . 160 25 LYS HG2 H 1.24 . . 161 25 LYS HG3 H 1.24 . . 162 25 LYS HD2 H 1.61 . . 163 25 LYS HD3 H 1.61 . . 164 26 TYR N N 122.55 . . 165 26 TYR H H 8.22 . . 166 26 TYR HA H 4.62 . . 167 26 TYR HB2 H 3.17 . . 168 26 TYR HB3 H 2.78 . . 169 26 TYR HD1 H 7.05 . . 170 26 TYR HD2 H 7.05 . . 171 26 TYR HE1 H 6.84 . . 172 26 TYR HE2 H 6.84 . . 173 27 ASP N N 121.56 . . 174 27 ASP H H 8.24 . . 175 27 ASP HA H 4.59 . . 176 27 ASP HB2 H 2.72 . . 177 27 ASP HB3 H 2.72 . . 178 28 GLY N N 109.90 . . 179 28 GLY H H 8.10 . . 180 28 GLY HA2 H 4.01 . . 181 28 GLY HA3 H 3.85 . . 182 29 VAL N N 120.17 . . 183 29 VAL H H 7.85 . . 184 29 VAL HA H 4.10 . . 185 29 VAL HB H 2.10 . . 186 29 VAL HG1 H 0.90 . . 187 29 VAL HG2 H 0.90 . . 188 30 GLU N N 124.51 . . 189 30 GLU H H 8.47 . . 190 30 GLU HA H 4.32 . . 191 30 GLU HB2 H 2.10 . . 192 30 GLU HB3 H 1.98 . . 193 30 GLU HG2 H 2.34 . . 194 30 GLU HG3 H 2.34 . . 195 31 GLU N N 122.51 . . 196 31 GLU H H 8.32 . . 197 31 GLU HA H 4.32 . . 198 31 GLU HB2 H 2.10 . . 199 31 GLU HB3 H 1.98 . . 200 31 GLU HG2 H 2.37 . . 201 31 GLU HG3 H 2.37 . . 202 32 GLU N N 122.35 . . 203 32 GLU H H 8.36 . . 204 32 GLU HA H 4.32 . . 205 32 GLU HB2 H 2.10 . . 206 32 GLU HB3 H 1.98 . . 207 32 GLU HG2 H 2.39 . . 208 32 GLU HG3 H 2.39 . . 209 33 ASP N N 121.51 . . 210 33 ASP H H 8.41 . . 211 33 ASP HA H 4.65 . . 212 33 ASP HB2 H 2.84 . . 213 33 ASP HB3 H 2.76 . . 214 34 ASP N N 120.99 . . 215 34 ASP H H 8.28 . . 216 34 ASP HA H 4.65 . . 217 34 ASP HB2 H 2.84 . . 218 34 ASP HB3 H 2.76 . . 219 35 GLU N N 120.97 . . 220 35 GLU H H 8.19 . . 221 35 GLU HA H 4.34 . . 222 35 GLU HB2 H 2.14 . . 223 35 GLU HB3 H 1.99 . . 224 35 GLU HG2 H 2.41 . . 225 35 GLU HG3 H 2.41 . . 226 36 GLU N N 122.91 . . 227 36 GLU H H 8.16 . . 228 36 GLU HA H 4.65 . . 229 36 GLU HB2 H 2.13 . . 230 36 GLU HB3 H 1.95 . . 231 36 GLU HG2 H 2.43 . . 232 36 GLU HG3 H 2.43 . . 233 37 PRO CD C 50.80 . . 234 37 PRO HA H 4.40 . . 235 37 PRO HB2 H 2.29 . . 236 37 PRO HB3 H 2.02 . . 237 37 PRO HG2 H 1.90 . . 238 37 PRO HG3 H 1.90 . . 239 37 PRO HD2 H 3.76 . . 240 37 PRO HD3 H 3.69 . . 241 38 ASN N N 120.15 . . 242 38 ASN ND2 N 113.70 . . 243 38 ASN H H 8.54 . . 244 38 ASN HA H 4.68 . . 245 38 ASN HB2 H 2.84 . . 246 38 ASN HB3 H 2.77 . . 247 38 ASN HD21 H 7.60 . . 248 38 ASN HD22 H 6.92 . . 249 39 VAL N N 122.94 . . 250 39 VAL H H 8.01 . . 251 39 VAL HA H 4.39 . . 252 39 VAL HB H 2.12 . . 253 39 VAL HG1 H 0.95 . . 254 39 VAL HG2 H 0.95 . . 255 40 PRO HA H 4.37 . . 256 40 PRO HB2 H 2.29 . . 257 40 PRO HB3 H 2.09 . . 258 40 PRO HG2 H 1.98 . . 259 40 PRO HG3 H 1.82 . . 260 40 PRO HD2 H 3.81 . . 261 40 PRO HD3 H 3.69 . . 262 41 CYS N N 121.59 . . 263 41 CYS H H 8.44 . . 264 41 CYS HA H 4.51 . . 265 41 CYS HB2 H 3.19 . . 266 41 CYS HB3 H 3.11 . . 267 42 LEU N N 128.92 . . 268 42 LEU CB C 42.60 . . 269 42 LEU H H 8.44 . . 270 42 LEU HA H 4.43 . . 271 42 LEU HB2 H 1.63 . . 272 42 LEU HB3 H 1.56 . . 273 42 LEU HD1 H 0.89 . . 274 42 LEU HD2 H 0.85 . . 275 43 VAL N N 123.19 . . 276 43 VAL H H 8.11 . . 277 43 VAL HA H 4.08 . . 278 43 VAL HB H 2.02 . . 279 43 VAL HG1 H 0.88 . . 280 43 VAL HG2 H 0.88 . . 281 44 ARG N N 126.30 . . 282 44 ARG H H 8.44 . . 283 44 ARG HA H 4.24 . . 284 44 ARG HB2 H 1.91 . . 285 44 ARG HB3 H 1.79 . . 286 44 ARG HG2 H 1.62 . . 287 44 ARG HG3 H 1.62 . . 288 44 ARG HD2 H 3.17 . . 289 44 ARG HD3 H 3.17 . . 290 45 VAL N N 119.93 . . 291 45 VAL H H 7.60 . . 292 45 VAL HA H 4.11 . . 293 45 VAL HB H 1.92 . . 294 45 VAL HG1 H 0.86 . . 295 45 VAL HG2 H 0.86 . . 296 46 CYS N N 124.49 . . 297 46 CYS H H 8.63 . . 298 46 CYS HA H 4.55 . . 299 46 CYS HB2 H 3.11 . . 300 46 CYS HB3 H 2.84 . . 301 47 HIS HA H 4.85 . . 302 47 HIS HB2 H 3.26 . . 303 47 HIS HB3 H 3.26 . . 304 47 HIS HD2 H 7.35 . . 305 47 HIS HE1 H 8.70 . . 306 48 GLN N N 121.12 . . 307 48 GLN NE2 N 113.00 . . 308 48 GLN H H 8.41 . . 309 48 GLN HA H 4.85 . . 310 48 GLN HB2 H 2.29 . . 311 48 GLN HB3 H 2.10 . . 312 48 GLN HG2 H 2.47 . . 313 48 GLN HG3 H 2.47 . . 314 48 GLN HE21 H 7.54 . . 315 48 GLN HE22 H 6.88 . . 316 49 ASP N N 123.95 . . 317 49 ASP H H 8.55 . . 318 49 ASP HA H 4.86 . . 319 49 ASP HB2 H 2.49 . . 320 49 ASP HB3 H 2.26 . . 321 50 CYS N N 119.98 . . 322 50 CYS H H 8.64 . . 323 50 CYS HA H 5.21 . . 324 50 CYS HB2 H 2.96 . . 325 50 CYS HB3 H 2.84 . . 326 51 VAL N N 116.66 . . 327 51 VAL CG1 C 21.40 . . 328 51 VAL H H 8.71 . . 329 51 VAL HA H 4.67 . . 330 51 VAL HB H 2.84 . . 331 51 VAL HG1 H 0.76 . . 332 51 VAL HG2 H 0.64 . . 333 52 CYS N N 118.84 . . 334 52 CYS H H 9.45 . . 335 52 CYS HA H 4.91 . . 336 52 CYS HB2 H 3.15 . . 337 52 CYS HB3 H 2.65 . . 338 53 GLU N N 121.67 . . 339 53 GLU H H 8.33 . . 340 53 GLU HA H 3.96 . . 341 53 GLU HB2 H 1.66 . . 342 53 GLU HB3 H 1.66 . . 343 53 GLU HG2 H 2.10 . . 344 53 GLU HG3 H 2.10 . . 345 54 GLU N N 123.12 . . 346 54 GLU H H 8.67 . . 347 54 GLU HA H 4.05 . . 348 54 GLU HB2 H 2.06 . . 349 54 GLU HB3 H 1.99 . . 350 54 GLU HG2 H 2.40 . . 351 54 GLU HG3 H 2.40 . . 352 55 GLY N N 113.93 . . 353 55 GLY H H 8.51 . . 354 55 GLY HA2 H 4.06 . . 355 55 GLY HA3 H 3.45 . . 356 56 PHE N N 118.67 . . 357 56 PHE H H 7.74 . . 358 56 PHE HA H 4.86 . . 359 56 PHE HB2 H 3.04 . . 360 56 PHE HB3 H 2.65 . . 361 56 PHE HD1 H 6.73 . . 362 56 PHE HD2 H 6.73 . . 363 56 PHE HE1 H 7.19 . . 364 56 PHE HE2 H 7.19 . . 365 56 PHE HZ H 7.35 . . 366 57 TYR N N 120.79 . . 367 57 TYR H H 9.75 . . 368 57 TYR HA H 4.56 . . 369 57 TYR HB2 H 2.64 . . 370 57 TYR HB3 H 2.53 . . 371 57 TYR HD1 H 6.88 . . 372 57 TYR HD2 H 6.88 . . 373 57 TYR HE1 H 6.67 . . 374 57 TYR HE2 H 6.67 . . 375 58 ARG N N 120.56 . . 376 58 ARG H H 9.25 . . 377 58 ARG HA H 4.90 . . 378 58 ARG HB2 H 2.10 . . 379 58 ARG HB3 H 1.95 . . 380 58 ARG HG2 H 1.87 . . 381 58 ARG HG3 H 1.72 . . 382 59 ASN N N 128.38 . . 383 59 ASN ND2 N 113.60 . . 384 59 ASN H H 9.29 . . 385 59 ASN HA H 4.79 . . 386 59 ASN HB2 H 4.34 . . 387 59 ASN HB3 H 3.03 . . 388 59 ASN HD21 H 7.74 . . 389 59 ASN HD22 H 7.23 . . 390 60 LYS N N 119.97 . . 391 60 LYS H H 8.86 . . 392 60 LYS HA H 4.17 . . 393 60 LYS HB2 H 1.87 . . 394 60 LYS HB3 H 1.78 . . 395 60 LYS HG2 H 1.36 . . 396 60 LYS HG3 H 1.36 . . 397 60 LYS HD2 H 1.58 . . 398 60 LYS HD3 H 1.58 . . 399 61 ASP N N 119.97 . . 400 61 ASP H H 7.46 . . 401 61 ASP HA H 4.90 . . 402 61 ASP HB2 H 3.00 . . 403 61 ASP HB3 H 2.53 . . 404 62 ASP N N 117.67 . . 405 62 ASP CB C 39.10 . . 406 62 ASP H H 8.51 . . 407 62 ASP HA H 4.35 . . 408 62 ASP HB2 H 3.30 . . 409 62 ASP HB3 H 2.67 . . 410 63 LYS N N 121.07 . . 411 63 LYS H H 8.13 . . 412 63 LYS HA H 4.58 . . 413 63 LYS HB2 H 1.83 . . 414 63 LYS HB3 H 1.83 . . 415 63 LYS HG2 H 1.46 . . 416 63 LYS HG3 H 1.35 . . 417 63 LYS HD2 H 1.65 . . 418 63 LYS HD3 H 1.65 . . 419 64 CYS N N 122.92 . . 420 64 CYS H H 9.22 . . 421 64 CYS HA H 4.94 . . 422 64 CYS HB2 H 2.99 . . 423 64 CYS HB3 H 2.48 . . 424 65 VAL N N 121.39 . . 425 65 VAL CG2 C 18.60 . . 426 65 VAL H H 10.07 . . 427 65 VAL HA H 5.15 . . 428 65 VAL HB H 2.61 . . 429 65 VAL HG1 H 1.05 . . 430 65 VAL HG2 H 0.94 . . 431 66 SER N N 119.19 . . 432 66 SER H H 9.25 . . 433 66 SER HA H 4.24 . . 434 66 SER HB2 H 3.96 . . 435 66 SER HB3 H 3.96 . . 436 67 ALA N N 122.82 . . 437 67 ALA CA C 56.00 . . 438 67 ALA CB C 18.10 . . 439 67 ALA H H 8.94 . . 440 67 ALA HA H 3.64 . . 441 67 ALA HB H 1.32 . . 442 68 GLU N N 117.24 . . 443 68 GLU H H 8.51 . . 444 68 GLU HA H 4.05 . . 445 68 GLU HB2 H 2.06 . . 446 68 GLU HB3 H 1.98 . . 447 68 GLU HG2 H 2.46 . . 448 68 GLU HG3 H 2.37 . . 449 69 ASP N N 122.32 . . 450 69 ASP H H 7.85 . . 451 69 ASP HA H 4.67 . . 452 69 ASP HB2 H 3.03 . . 453 69 ASP HB3 H 2.76 . . 454 70 CYS N N 122.93 . . 455 70 CYS H H 8.28 . . 456 70 CYS HA H 4.37 . . 457 70 CYS HB2 H 3.21 . . 458 70 CYS HB3 H 2.90 . . 459 71 GLU N N 117.75 . . 460 71 GLU H H 7.67 . . 461 71 GLU HA H 4.24 . . 462 71 GLU HB2 H 2.21 . . 463 71 GLU HB3 H 2.10 . . 464 71 GLU HG2 H 2.49 . . 465 71 GLU HG3 H 2.49 . . 466 72 LEU N N 120.25 . . 467 72 LEU CB C 41.60 . . 468 72 LEU H H 7.62 . . 469 72 LEU HA H 4.22 . . 470 72 LEU HB2 H 1.90 . . 471 72 LEU HB3 H 1.65 . . 472 72 LEU HG H 1.77 . . 473 72 LEU HD1 H 0.96 . . 474 72 LEU HD2 H 0.89 . . 475 73 ASP N N 119.69 . . 476 73 ASP H H 7.87 . . 477 73 ASP HA H 4.57 . . 478 73 ASP HB3 H 2.90 . . 479 73 ASP HB2 H 2.78 . . 480 74 ASN N N 118.68 . . 481 74 ASN ND2 N 112.90 . . 482 74 ASN H H 7.83 . . 483 74 ASN HA H 4.67 . . 484 74 ASN HB2 H 2.89 . . 485 74 ASN HB3 H 2.67 . . 486 74 ASN HD21 H 7.50 . . 487 74 ASN HD22 H 6.72 . . 488 75 MET N N 121.26 . . 489 75 MET CE C 17.10 . . 490 75 MET H H 8.08 . . 491 75 MET HA H 4.41 . . 492 75 MET HB2 H 2.06 . . 493 75 MET HB3 H 1.97 . . 494 75 MET HG2 H 2.51 . . 495 75 MET HG3 H 2.51 . . 496 75 MET HE H 2.08 . . 497 76 ASP N N 120.56 . . 498 76 ASP H H 8.21 . . 499 76 ASP HA H 4.59 . . 500 76 ASP HB2 H 2.72 . . 501 76 ASP HB3 H 2.63 . . 502 77 PHE N N 121.05 . . 503 77 PHE H H 7.89 . . 504 77 PHE HA H 4.52 . . 505 77 PHE HB2 H 3.00 . . 506 77 PHE HB3 H 3.00 . . 507 77 PHE HD1 H 7.10 . . 508 77 PHE HD2 H 7.10 . .3 509 77 PHE HE1 H 7.21 . . 510 77 PHE HE2 H 7.21 . . 511 77 PHE HZ H 7.32 . . 512 78 ILE N N 123.66 . . 513 78 ILE CB C 38.70 . . 514 78 ILE CG1 C 27.10 . . 515 78 ILE CG2 C 17.40 . . 516 78 ILE CD1 C 12.70 . . 517 78 ILE H H 7.74 . . 518 78 ILE HA H 4.04 . . 519 78 ILE HB H 1.67 . . 520 78 ILE HG12 H 1.34 . . 521 78 ILE HG13 H 1.06 . . 522 78 ILE HG2 H 0.72 . . 523 78 ILE HD1 H 0.78 . . 524 79 TYR N N 126.74 . . 525 79 TYR CA C 55.90 . . 526 79 TYR H H 8.22 . . 527 79 TYR HA H 4.74 . . 528 79 TYR HB3 H 3.05 . . 529 79 TYR HB2 H 2.89 . . 530 79 TYR HD1 H 7.19 . . 531 79 TYR HD2 H 7.19 . . 532 79 TYR HE1 H 6.84 . . 533 79 TYR HE2 H 6.84 . . 534 80 PRO CD C 50.80 . . 535 80 PRO HA H 4.40 . . 536 80 PRO HB2 H 2.25 . . 537 80 PRO HB3 H 1.98 . . 538 80 PRO HD2 H 3.82 . . 539 80 PRO HD3 H 3.54 . . 540 81 GLY N N 109.90 . . 541 81 GLY H H 8.05 . . 542 81 GLY HA2 H 4.01 . . 543 81 GLY HA3 H 3.97 . . 544 82 THR N N 115.04 . . 545 82 THR CG2 C 21.60 . . 546 82 THR H H 7.99 . . 547 82 THR HA H 4.34 . . 548 82 THR HB H 4.20 . . 549 82 THR HG2 H 1.23 . . 550 83 ARG N N 124.73 . . 551 83 ARG H H 8.36 . . 552 83 ARG HA H 4.35 . . 553 83 ARG HB2 H 1.83 . . 554 83 ARG HB3 H 1.75 . . 555 83 ARG HG2 H 1.59 . . 556 83 ARG HG3 H 1.59 . . 557 83 ARG HD2 H 3.14 . . 558 83 ARG HD3 H 3.14 . . 559 84 ASN N N 122.83 . . 560 84 ASN CA C 51.50 . . 561 84 ASN ND2 N 114.20 . . 562 84 ASN H H 8.45 . . 563 84 ASN HA H 4.96 . . 564 84 ASN HB2 H 2.83 . . 565 84 ASN HB3 H 2.64 . . 566 84 ASN HD21 H 7.60 . . 567 84 ASN HD22 H 6.90 . . 568 85 PRO CD C 50.50 . . 569 85 PRO HD2 H 3.73 . . 570 85 PRO HD3 H 3.68 . . stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constants_set_1 _Saveframe_category coupling_constants loop_ _Sample_label $sample_1 stop_ _Spectrometer_frequency_1H 750 _Mol_system_component_name NAPc2 loop_ _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_value_error 3JHNHA 2 ALA H 2 ALA HA 5.24 0.1 3JHNHA 3 THR H 3 THR HA 7.13 0.1 3JHNHA 4 MET H 4 MET HA 6.23 0.1 3JHNHA 5 GLN H 5 GLN HA 7.44 0.1 3JHNHA 6 CYS H 6 CYS HA 7.53 0.1 3JHNHA 7 GLY H 7 GLY HA 6.62 0.1 3JHNHA 8 GLU H 8 GLU HA 2.69 0.1 3JHNHA 9 ASN H 9 ASN HA 6.37 0.1 3JHNHA 10 GLU H 10 GLU HA 8.14 0.1 3JHNHA 11 LYS H 11 LYS HA 8.11 0.1 3JHNHA 12 TYR H 12 TYR HA 3.99 0.1 3JHNHA 13 ASP H 13 ASP HA 8.67 0.1 3JHNHA 14 SER H 14 SER HA 3.90 0.1 3JHNHA 15 CYS H 15 CYS HA 6.40 0.1 3JHNHA 16 GLY H 16 GLY HA 6.69 0.1 3JHNHA 16 GLY H 16 GLY HA 1.82 0.1 3JHNHA 17 SER H 17 SER HA 6.38 0.1 3JHNHA 19 GLU H 19 GLU HA 5.50 0.1 3JHNHA 20 CYS H 20 CYS HA 3.18 0.1 3JHNHA 21 ASP H 21 ASP HA 4.13 0.1 3JHNHA 22 LYS H 22 LYS HA 5.26 0.1 3JHNHA 23 LYS H 23 LYS HA 7.53 0.1 3JHNHA 26 TYR H 26 TYR HA 7.30 0.1 3JHNHA 27 ASP H 27 ASP HA 5.65 0.1 3JHNHA 28 GLY H 28 GLY HA 6.16 0.1 3JHNHA 28 GLY H 28 GLY HA 4.58 0.1 3JHNHA 29 VAL H 29 VAL HA 7.24 0.1 3JHNHA 30 GLU H 30 GLU HA 6.05 0.1 3JHNHA 31 GLU H 31 GLU HA 6.19 0.1 3JHNHA 32 GLU H 32 GLU HA 6.49 0.1 3JHNHA 33 ASP H 33 ASP HA 6.24 0.1 3JHNHA 34 ASP H 34 ASP HA 7.08 0.1 3JHNHA 35 GLU H 35 GLU HA 5.95 0.1 3JHNHA 36 GLU H 36 GLU HA 6.56 0.1 3JHNHA 38 ASN H 38 ASN HA 7.07 0.1 3JHNHA 39 VAL H 39 VAL HA 7.09 0.1 3JHNHA 41 CYS H 41 CYS HA 4.06 0.1 3JHNHA 42 LEU H 42 LEU HA 6.79 0.1 3JHNHA 43 VAL H 43 VAL HA 6.35 0.1 3JHNHA 44 ARG H 44 ARG HA 6.62 0.1 3JHNHA 45 VAL H 45 VAL HA 6.25 0.1 3JHNHA 46 CYS H 46 CYS HA 4.20 0.1 3JHNHA 48 GLN H 48 GLN HA 4.74 0.1 3JHNHA 49 ASP H 49 ASP HA 6.43 0.1 3JHNHA 50 CYS H 50 CYS HA 8.22 0.1 3JHNHA 51 VAL H 51 VAL HA 8.18 0.1 3JHNHA 53 GLU H 53 GLU HA 2.65 0.1 3JHNHA 54 GLU H 54 GLU HA 2.31 0.1 3JHNHA 55 GLY H 55 GLY HA 7.21 0.1 3JHNHA 55 GLY H 55 GLY HA 4.14 0.1 3JHNHA 56 PHE H 56 PHE HA 8.55 0.1 3JHNHA 57 TYR H 57 TYR HA 8.56 0.1 3JHNHA 58 ARG H 58 ARG HA 4.64 0.1 3JHNHA 59 ASN H 59 ASN HA 6.73 0.1 3JHNHA 61 ASP H 61 ASP HA 8.58 0.1 3JHNHA 62 ASP H 62 ASP HA 5.21 0.1 3JHNHA 63 LYS H 63 LYS HA 5.66 0.1 3JHNHA 64 CYS H 64 CYS HA 6.27 0.1 3JHNHA 65 VAL H 65 VAL HA 8.48 0.1 3JHNHA 66 SER H 66 SER HA 3.68 0.1 3JHNHA 67 ALA H 67 ALA HA 1.88 0.1 3JHNHA 68 GLU H 68 GLU HA 4.00 0.1 3JHNHA 69 ASP H 69 ASP HA 6.10 0.1 3JHNHA 70 CYS H 70 CYS HA 4.05 0.1 3JHNHA 71 GLU H 71 GLU HA 4.60 0.1 3JHNHA 72 LEU H 72 LEU HA 4.63 0.1 3JHNHA 73 ASP H 73 ASP HA 5.70 0.1 3JHNHA 74 ASN H 74 ASN HA 7.18 0.1 3JHNHA 75 MET H 75 MET HA 6.14 0.1 3JHNHA 76 ASP H 76 ASP HA 6.15 0.1 3JHNHA 77 PHE H 77 PHE HA 6.81 0.1 3JHNHA 78 ILE H 78 ILE HA 7.60 0.1 3JHNHA 79 TYR H 79 TYR HA 6.41 0.1 3JHNHA 82 THR H 82 THR HA 7.11 0.1 3JHNHA 83 ARG H 83 ARG HA 6.82 0.1 3JHNHA 84 ASN H 84 ASN HA 14.09 0.1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_4 _Saveframe_category citation _MEDLINE_UI_code 96312555 _Citation_full ; Stassens P, Bergum PW, Gansemans Y, Jespers L, Laroche Y, Huang S, Maki S, Messens J, Lauwereys M, Cappello M, Hotez PJ, Lasters I, Vlasuk GP. Anticoagulant repertoire of the hookworm Ancylostoma caninum. Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2149-54. ; save_ save_ref_22 _Saveframe_category citation _MEDLINE_UI_code 98035057 _Citation_full ; Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol. 1997 Oct 17;273(1):283-98. ; save_ save_ref_24 _Saveframe_category citation _MEDLINE_UI_code 92253561 _Citation_full ; Morris AL, MacArthur MW, Hutchinson EG, Thornton JM. Stereochemical quality of protein structure coordinates. Proteins. 1992 Apr;12(4):345-64. ; save_