data_4422 #Corrected using PDB structure: 1CCVA # #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 # 27 I HA 4.20 3.20 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.14 N/A N/A N/A N/A 0.06 # #bmr4422.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4422.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A 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 N/A +/-0.12 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.646 N/A N/A N/A N/A 0.428 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.187 N/A N/A N/A N/A 0.417 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Solution Structure of Apis mellifera Chymotrypsin Inhibitor (AMCI). ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cierpicki T. . . 2 Otlewski J. . . stop_ _BMRB_accession_number 4422 _BMRB_flat_file_name bmr4422.str _Entry_type new _Submission_date 1999-09-27 _Accession_date 1999-09-30 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 308 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Cierpicki, T., Bania, J., and Otlewski, J., "NMR Solution Structure of Apis mellifera Chymotrypsin/Cathepsin G Inhibitor-1 (AMCI-1): Structural Similarity with Ascaris Protease Inhibitors," Protein Sci. 9, 976-984 (2000). ; _Citation_title ; NMR Solution Structure of Apis mellifera Chymotrypsin/Cathepsin G Inhibitor-1 (AMCI-1): Structural Similarity with Ascaris Protease Inhibitors. ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 20306980 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cierpicki Tomasz . . 2 Bania Jacek . . 3 Otlewski Jacek . . stop_ _Journal_abbreviation "Protein Sci." _Journal_name_full "Protein Science" _Journal_volume 9 _Page_first 976 _Page_last 984 _Year 2000 loop_ _Keyword "protein inhibitor" "hemolymph" "Apis mellifera" "canonical inhibitor" stop_ save_ ################################## # Molecular system description # ################################## save_system_AMCI _Saveframe_category molecular_system _Mol_system_name "Apis mellifera chymotrypsin inhibitor" _Abbreviation_common AMCI _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label AMCI $AMCI stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state "all disulfide bound" loop_ _Biological_function "Protease inhibitor" stop_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1CCV "A Chain A, Nmr Solution Structure Of Apis Mellifera Chymotrypsin Inhibitor (Amci)" . stop_ save_ ######################## # Monomeric polymers # ######################## save_AMCI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Apis mellifera chymotrypsin inhibitor" _Abbreviation_common AMCI _Mol_thiol_state "all disulfide bound" ############################## # Polymer residue sequence # ############################## _Residue_count 56 _Mol_residue_sequence ; EECGPNEVFNTCGSACAPTC AQPKTRICTMQCRIGCQCQE GFLRNGEGACVLPENC ; loop_ _Residue_seq_code _Residue_label 1 GLU 2 GLU 3 CYS 4 GLY 5 PRO 6 ASN 7 GLU 8 VAL 9 PHE 10 ASN 11 THR 12 CYS 13 GLY 14 SER 15 ALA 16 CYS 17 ALA 18 PRO 19 THR 20 CYS 21 ALA 22 GLN 23 PRO 24 LYS 25 THR 26 ARG 27 ILE 28 CYS 29 THR 30 MET 31 GLN 32 CYS 33 ARG 34 ILE 35 GLY 36 CYS 37 GLN 38 CYS 39 GLN 40 GLU 41 GLY 42 PHE 43 LEU 44 ARG 45 ASN 46 GLY 47 GLU 48 GLY 49 ALA 50 CYS 51 VAL 52 LEU 53 PRO 54 GLU 55 ASN 56 CYS stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-04-29 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 1CCV "A Chain A, Nmr Solution Structure Of ApisMellifera Chymotrypsin Inhibitor (Amci)" 100.00 56 100 100 4e-30 SWISS-PROT P56682 "AMCI_APIME Chymotrypsin inhibitor (AMCI)" 100.00 56 100 100 4e-30 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 AMCI 3 SG AMCI 36 SG single disulfide AMCI 12 SG AMCI 32 SG single disulfide AMCI 16 SG AMCI 28 SG single disulfide AMCI 20 SG AMCI 56 SG single disulfide AMCI 38 SG AMCI 50 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 _Tissue $AMCI Honeybee 7460 Eukaryota Metazoa Apis mellifera hemolymph stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method $AMCI 'purified from natural source' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $AMCI 6.6 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe loop_ _Task "spectra processing" stop_ _Citation_label $ref_1 save_ save_SPARKY _Saveframe_category software _Name SPARKY loop_ _Task "analysis and intergation of NMR spectra" stop_ save_ save_DYANA _Saveframe_category software _Name DYANA loop_ _Task "structure calculation" stop_ _Citation_label $ref_2 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model UnityPlus _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; NOESY TOCSY DQFCOSY ; save_ ####################### # Sample conditions # ####################### save_sample_conditions _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH* 2.5 0.1 na temperature 288 1 K 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 0.00 External_in_the_sample direct cylindrical External_in_the_sample parallel_to_Bo . 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_assigned_chemical_shifts _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name AMCI 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 GLU HA H 3.79 0.01 1 2 1 GLU HB2 H 1.69 0.01 2 3 1 GLU HB3 H 1.72 0.01 2 4 1 GLU HG2 H 2.13 0.01 1 5 1 GLU HG3 H 2.13 0.01 1 6 2 GLU H H 8.69 0.01 1 7 2 GLU HA H 4.28 0.01 1 8 2 GLU HB2 H 1.84 0.01 2 9 2 GLU HB3 H 1.94 0.01 2 10 2 GLU HG2 H 2.30 0.01 1 11 2 GLU HG3 H 2.30 0.01 1 12 3 CYS H H 8.53 0.01 1 13 3 CYS HA H 4.89 0.01 1 14 3 CYS HB2 H 2.53 0.01 2 15 3 CYS HB3 H 3.18 0.01 2 16 4 GLY H H 7.51 0.01 1 17 4 GLY HA2 H 3.66 0.01 2 18 4 GLY HA3 H 4.12 0.01 2 19 5 PRO HA H 4.05 0.01 1 20 5 PRO HB2 H 2.10 0.01 2 21 5 PRO HB3 H 1.65 0.01 2 22 5 PRO HG2 H 1.82 0.01 2 23 5 PRO HG3 H 1.95 0.01 2 24 5 PRO HD2 H 3.49 0.01 2 25 5 PRO HD3 H 3.35 0.01 2 26 6 ASN H H 8.91 0.01 1 27 6 ASN HA H 3.61 0.01 1 28 6 ASN HB2 H 2.39 0.01 2 29 6 ASN HB3 H 0.98 0.01 2 30 6 ASN HD21 H 6.80 0.01 2 31 6 ASN HD22 H 6.92 0.01 2 32 7 GLU H H 7.14 0.01 1 33 7 GLU HA H 5.14 0.01 1 34 7 GLU HB2 H 1.97 0.01 2 35 7 GLU HB3 H 1.61 0.01 2 36 7 GLU HG2 H 2.16 0.01 2 37 7 GLU HG3 H 2.22 0.01 2 38 8 VAL H H 9.09 0.01 1 39 8 VAL HA H 4.38 0.01 1 40 8 VAL HB H 1.90 0.01 1 41 8 VAL HG1 H 0.80 0.01 2 42 8 VAL HG2 H 0.72 0.01 2 43 9 PHE H H 8.88 0.01 1 44 9 PHE HA H 4.20 0.01 1 45 9 PHE HB2 H 2.94 0.01 2 46 9 PHE HB3 H 2.82 0.01 2 47 9 PHE HD1 H 6.89 0.01 1 48 9 PHE HD2 H 6.89 0.01 1 49 9 PHE HE1 H 7.11 0.01 1 50 9 PHE HE2 H 7.11 0.01 1 51 9 PHE HZ H 7.05 0.01 1 52 10 ASN H H 7.56 0.01 1 53 10 ASN HA H 4.76 0.01 1 54 10 ASN HB2 H 2.61 0.01 2 55 10 ASN HB3 H 2.21 0.01 2 56 10 ASN HD21 H 6.70 0.01 2 57 10 ASN HD22 H 7.54 0.01 2 58 11 THR H H 8.28 0.01 1 59 11 THR HA H 3.86 0.01 1 60 11 THR HB H 4.20 0.01 1 61 11 THR HG2 H 1.22 0.01 1 62 12 CYS H H 8.58 0.01 1 63 12 CYS HA H 4.23 0.01 1 64 12 CYS HB2 H 2.59 0.01 2 65 12 CYS HB3 H 3.13 0.01 2 66 13 GLY H H 8.44 0.01 1 67 13 GLY HA2 H 3.62 0.01 2 68 13 GLY HA3 H 4.12 0.01 2 69 14 SER H H 8.29 0.01 1 70 14 SER HA H 4.33 0.01 1 71 14 SER HB2 H 3.88 0.01 2 72 14 SER HB3 H 3.45 0.01 2 73 15 ALA H H 9.23 0.01 1 74 15 ALA HA H 4.12 0.01 1 75 15 ALA HB H 1.35 0.01 1 76 16 CYS H H 8.55 0.01 1 77 16 CYS HA H 4.74 0.01 1 78 16 CYS HB2 H 2.91 0.01 1 79 16 CYS HB3 H 2.91 0.01 1 80 17 ALA H H 7.43 0.01 1 81 17 ALA HA H 4.32 0.01 1 82 17 ALA HB H 1.31 0.01 1 83 18 PRO HA H 4.51 0.01 1 84 18 PRO HB2 H 1.75 0.01 2 85 18 PRO HB3 H 2.16 0.01 2 86 18 PRO HG2 H 1.85 0.01 2 87 18 PRO HG3 H 1.93 0.01 2 88 18 PRO HD2 H 3.58 0.01 2 89 18 PRO HD3 H 3.79 0.01 2 90 19 THR H H 7.87 0.01 1 91 19 THR HA H 4.76 0.01 1 92 19 THR HB H 4.57 0.01 1 93 19 THR HG2 H 1.14 0.01 1 94 20 CYS H H 8.52 0.01 1 95 20 CYS HA H 4.08 0.01 1 96 20 CYS HB2 H 2.91 0.01 2 97 20 CYS HB3 H 2.82 0.01 2 98 21 ALA H H 7.93 0.01 1 99 21 ALA HA H 4.05 0.01 1 100 21 ALA HB H 1.25 0.01 1 101 22 GLN H H 7.58 0.01 1 102 22 GLN HA H 4.60 0.01 1 103 22 GLN HB2 H 1.78 0.01 2 104 22 GLN HB3 H 1.92 0.01 2 105 22 GLN HG2 H 2.04 0.01 2 106 22 GLN HG3 H 2.08 0.01 2 107 22 GLN HE21 H 6.73 0.01 2 108 22 GLN HE22 H 7.42 0.01 2 109 23 PRO HA H 4.56 0.01 1 110 23 PRO HB2 H 2.10 0.01 2 111 23 PRO HB3 H 1.84 0.01 2 112 23 PRO HG2 H 1.73 0.01 2 113 23 PRO HG3 H 1.92 0.01 2 114 23 PRO HD2 H 3.52 0.01 2 115 23 PRO HD3 H 3.25 0.01 2 116 24 LYS H H 7.82 0.01 1 117 24 LYS HA H 4.31 0.01 1 118 24 LYS HB2 H 1.62 0.01 2 119 24 LYS HB3 H 1.65 0.01 2 120 24 LYS HG2 H 1.26 0.01 2 121 24 LYS HG3 H 1.30 0.01 2 122 24 LYS HD2 H 1.54 0.01 1 123 24 LYS HD3 H 1.54 0.01 1 124 24 LYS HE2 H 2.86 0.01 1 125 24 LYS HE3 H 2.86 0.01 1 126 24 LYS HZ H 7.43 0.01 3 127 25 THR H H 8.26 0.01 1 128 25 THR HA H 4.03 0.01 1 129 25 THR HB H 3.91 0.01 1 130 25 THR HG2 H 1.06 0.01 1 131 26 ARG H H 8.58 0.01 1 132 26 ARG HA H 4.42 0.01 1 133 26 ARG HB2 H 1.65 0.01 1 134 26 ARG HB3 H 1.65 0.01 1 135 26 ARG HG2 H 1.48 0.01 1 136 26 ARG HG3 H 1.48 0.01 1 137 26 ARG HD2 H 3.02 0.01 1 138 26 ARG HD3 H 3.02 0.01 1 139 26 ARG HE H 7.29 0.01 1 140 27 ILE H H 8.16 0.01 1 141 27 ILE HA H 4.06 0.01 1 142 27 ILE HB H 1.64 0.01 1 143 27 ILE HG2 H 0.72 0.01 1 144 27 ILE HG12 H 1.05 0.01 2 145 27 ILE HG13 H 1.35 0.01 2 146 27 ILE HD1 H 0.69 0.01 1 147 28 CYS H H 8.52 0.01 1 148 28 CYS HA H 4.82 0.01 1 149 28 CYS HB2 H 3.11 0.01 2 150 28 CYS HB3 H 3.03 0.01 2 151 29 THR H H 8.22 0.01 1 152 29 THR HA H 4.13 0.01 1 153 29 THR HB H 4.12 0.01 1 154 29 THR HG2 H 1.06 0.01 1 155 30 MET H H 8.08 0.01 1 156 30 MET HA H 4.31 0.01 1 157 30 MET HB2 H 1.80 0.01 2 158 30 MET HB3 H 2.00 0.01 2 159 30 MET HG2 H 2.41 0.01 2 160 30 MET HG3 H 2.47 0.01 2 161 31 GLN H H 7.92 0.01 1 162 31 GLN HA H 4.10 0.01 1 163 31 GLN HB2 H 1.84 0.01 1 164 31 GLN HB3 H 1.84 0.01 1 165 31 GLN HG2 H 2.21 0.01 1 166 31 GLN HG3 H 2.21 0.01 1 167 31 GLN HE21 H 6.79 0.01 2 168 31 GLN HE22 H 7.46 0.01 2 169 32 CYS H H 8.56 0.01 1 170 32 CYS HA H 4.53 0.01 1 171 32 CYS HB2 H 2.79 0.01 2 172 32 CYS HB3 H 3.11 0.01 2 173 33 ARG H H 8.45 0.01 1 174 33 ARG HA H 4.52 0.01 1 175 33 ARG HB2 H 1.27 0.01 2 176 33 ARG HB3 H 1.35 0.01 2 177 33 ARG HG2 H 1.27 0.01 2 178 33 ARG HG3 H 1.35 0.01 2 179 33 ARG HD2 H 2.97 0.01 1 180 33 ARG HD3 H 2.97 0.01 1 181 33 ARG HE H 7.10 0.01 1 182 34 ILE H H 8.71 0.01 1 183 34 ILE HA H 4.18 0.01 1 184 34 ILE HB H 1.60 0.01 1 185 34 ILE HG2 H 0.84 0.01 1 186 34 ILE HG12 H 1.03 0.01 2 187 34 ILE HG13 H 1.44 0.01 2 188 34 ILE HD1 H 0.86 0.01 1 189 35 GLY H H 7.75 0.01 1 190 35 GLY HA2 H 3.61 0.01 2 191 35 GLY HA3 H 4.38 0.01 2 192 36 CYS H H 8.90 0.01 1 193 36 CYS HA H 4.76 0.01 1 194 36 CYS HB2 H 2.81 0.01 2 195 36 CYS HB3 H 2.71 0.01 2 196 37 GLN H H 9.03 0.01 1 197 37 GLN HA H 4.57 0.01 1 198 37 GLN HB2 H 2.02 0.01 2 199 37 GLN HB3 H 1.80 0.01 2 200 37 GLN HG2 H 2.14 0.01 2 201 37 GLN HG3 H 2.23 0.01 2 202 37 GLN HE21 H 6.90 0.01 2 203 37 GLN HE22 H 7.29 0.01 2 204 38 CYS H H 8.71 0.01 1 205 38 CYS HA H 4.82 0.01 1 206 38 CYS HB2 H 2.61 0.01 2 207 38 CYS HB3 H 3.04 0.01 2 208 39 GLN H H 8.41 0.01 1 209 39 GLN HA H 3.99 0.01 1 210 39 GLN HB2 H 1.52 0.01 2 211 39 GLN HB3 H 1.82 0.01 2 212 39 GLN HG2 H 1.90 0.01 2 213 39 GLN HG3 H 2.12 0.01 2 214 39 GLN HE21 H 6.76 0.01 2 215 39 GLN HE22 H 7.05 0.01 2 216 40 GLU H H 8.53 0.01 1 217 40 GLU HA H 4.01 0.01 1 218 40 GLU HB2 H 1.93 0.01 2 219 40 GLU HB3 H 1.99 0.01 2 220 40 GLU HG2 H 2.41 0.01 1 221 40 GLU HG3 H 2.41 0.01 1 222 41 GLY H H 8.64 0.01 1 223 41 GLY HA2 H 3.31 0.01 2 224 41 GLY HA3 H 4.06 0.01 2 225 42 PHE H H 8.11 0.01 1 226 42 PHE HA H 4.67 0.01 1 227 42 PHE HB2 H 3.14 0.01 2 228 42 PHE HB3 H 2.44 0.01 2 229 42 PHE HD1 H 6.63 0.01 1 230 42 PHE HD2 H 6.63 0.01 1 231 42 PHE HE1 H 7.05 0.01 1 232 42 PHE HE2 H 7.05 0.01 1 233 43 LEU H H 9.59 0.01 1 234 43 LEU HA H 4.47 0.01 1 235 43 LEU HB2 H 1.33 0.01 2 236 43 LEU HB3 H 0.95 0.01 2 237 43 LEU HG H 1.23 0.01 1 238 43 LEU HD1 H 0.68 0.01 2 239 43 LEU HD2 H 0.57 0.01 2 240 44 ARG H H 7.52 0.01 1 241 44 ARG HA H 4.75 0.01 1 242 44 ARG HB2 H 1.63 0.01 2 243 44 ARG HB3 H 1.78 0.01 2 244 44 ARG HG2 H 1.52 0.01 2 245 44 ARG HG3 H 1.77 0.01 2 246 44 ARG HD2 H 2.92 0.01 1 247 44 ARG HD3 H 2.92 0.01 1 248 44 ARG HE H 7.06 0.01 1 249 45 ASN H H 9.41 0.01 1 250 45 ASN HA H 4.60 0.01 1 251 45 ASN HB2 H 3.59 0.01 2 252 45 ASN HB3 H 2.83 0.01 2 253 45 ASN HD21 H 7.30 0.01 2 254 45 ASN HD22 H 7.75 0.01 2 255 46 GLY H H 8.66 0.01 1 256 46 GLY HA2 H 3.78 0.01 1 257 46 GLY HA3 H 3.78 0.01 1 258 47 GLU H H 7.46 0.01 1 259 47 GLU HA H 4.41 0.01 1 260 47 GLU HB2 H 1.91 0.01 2 261 47 GLU HB3 H 2.22 0.01 2 262 47 GLU HG2 H 2.30 0.01 2 263 47 GLU HG3 H 2.42 0.01 2 264 48 GLY H H 7.86 0.01 1 265 48 GLY HA2 H 3.44 0.01 2 266 48 GLY HA3 H 4.19 0.01 2 267 49 ALA H H 7.96 0.01 1 268 49 ALA HA H 4.35 0.01 1 269 49 ALA HB H 1.20 0.01 1 270 50 CYS H H 8.68 0.01 1 271 50 CYS HA H 4.93 0.01 1 272 50 CYS HB2 H 2.66 0.01 2 273 50 CYS HB3 H 2.35 0.01 2 274 51 VAL H H 9.47 0.01 1 275 51 VAL HA H 4.90 0.01 1 276 51 VAL HB H 2.17 0.01 1 277 51 VAL HG1 H 0.74 0.01 2 278 51 VAL HG2 H 0.66 0.01 2 279 52 LEU H H 8.75 0.01 1 280 52 LEU HA H 4.15 0.01 1 281 52 LEU HB2 H 1.31 0.01 2 282 52 LEU HB3 H 1.39 0.01 2 283 52 LEU HG H 1.41 0.01 1 284 52 LEU HD1 H 0.71 0.01 2 285 52 LEU HD2 H 0.13 0.01 2 286 53 PRO HA H 4.12 0.01 1 287 53 PRO HB2 H 1.75 0.01 2 288 53 PRO HB3 H 2.17 0.01 2 289 53 PRO HG2 H 1.70 0.01 2 290 53 PRO HG3 H 1.99 0.01 2 291 53 PRO HD2 H 3.42 0.01 2 292 53 PRO HD3 H 3.87 0.01 2 293 54 GLU H H 8.31 0.01 1 294 54 GLU HA H 4.08 0.01 1 295 54 GLU HB2 H 1.91 0.01 2 296 54 GLU HB3 H 1.94 0.01 2 297 54 GLU HG2 H 2.20 0.01 2 298 54 GLU HG3 H 2.26 0.01 2 299 55 ASN H H 8.38 0.01 1 300 55 ASN HA H 4.93 0.01 1 301 55 ASN HB2 H 2.55 0.01 2 302 55 ASN HB3 H 3.10 0.01 2 303 55 ASN HD21 H 6.99 0.01 2 304 55 ASN HD22 H 7.74 0.01 2 305 56 CYS H H 7.39 0.01 1 306 56 CYS HA H 4.23 0.01 1 307 56 CYS HB2 H 2.89 0.01 2 308 56 CYS HB3 H 3.06 0.01 2 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _MEDLINE_UI_code 96088118 _Citation_full ; Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A, "NMRPipe: a multidimensional spectral processing system based on UNIX pipes," J Biomol NMR 1995 Nov;6(3):277-93 ; save_ save_ref_2 _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_