data_4664 #Corrected using PDB structure: 1JZUA # #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 # 15 V HA 3.93 4.86 # 17 A HA 5.17 4.38 # 20 S HA 3.75 4.83 # 30 D HA 4.28 5.06 # 39 I HA 4.90 4.12 # 62 W HA 4.76 5.65 # 70 S HA 4.33 5.19 # 79 E HA 3.85 4.67 # 90 T HA 3.73 4.97 # 95 Y HA 6.06 5.22 #108 T HA 4.38 5.18 #111 M HA 4.47 5.26 #116 S HA 5.71 5.01 #117 R HA 3.58 4.44 #125 A HA 3.35 4.70 #138 Y HA 5.20 4.46 #142 M HA 4.40 5.52 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 66 F CA 61.45 55.76 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 66 F CB 32.28 41.27 # 89 D CB 45.68 40.66 #137 N CB 36.31 45.38 #145 M CB 29.30 36.16 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 79 E C 178.76 172.79 # 90 T C 179.02 173.56 #127 A C 171.52 179.67 #133 A C 171.05 179.89 #138 Y C 175.96 170.93 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 44 E N 120.87 110.61 # 69 T N 119.00 106.21 # 79 E N 130.53 119.96 # 90 T N 120.18 110.17 #144 A N 131.47 118.35 #149 Q N 115.44 127.83 #151 E N 119.58 133.09 #152 C N 122.53 112.05 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 89 D H 6.98 9.80 # 94 S H 11.25 7.15 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.02 -0.98 -0.83 -0.84 -0.35 -0.04 # #bmr4664.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4664.str file): #HA CA CB CO N HN #N/A -0.90 -0.90 -0.84 -0.35 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.03 +/-0.18 +/-0.20 +/-0.18 +/-0.42 +/-0.08 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.661 0.930 0.987 0.489 0.632 0.294 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.181 1.088 1.140 1.045 2.386 0.482 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequence-Specific Resonance Assignments of Q83, a Lipocalin Highly Expressed in v-myc-Transformed Avian Fibroblasts ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kontaxis Georg . . 2 Matt Theresia . . 3 Schuler Wolfgang . . 4 Krautler Bernhard . . 5 Bister Klaus . . 6 Konrat Robert . . stop_ _BMRB_accession_number 4664 _BMRB_flat_file_name bmr4664.str _Entry_type new _Submission_date 2000-02-07 _Accession_date 2000-02-10 _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' 465 '13C chemical shifts' 419 '15N chemical shifts' 138 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-07-05 update author 'residue 115 reassigned as a tyrosine' 2000-07-08 original author 'original release date' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Sequence-specific Resonance Assignments of Q83, a Lipocalin Highly Expressed in v-myc-transformed Avian Fibroblasts ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 20377250 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kontaxis Georg . . 2 Matt Theresia . . 3 Schuler Wolfgang . . 4 Krautler Bernhard . . 5 Bister Klaus . . 6 Konrat Robert . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_name_full "Journal of Biomolecular NMR" _Journal_volume 17 _Journal_issue 2 _Page_first 177 _Page_last 178 _Year 2000 _Details "G. Kontaxis and T. Matt contributed equally" loop_ _Keyword "NMR assignments" "protein structure" "cell proliferation" oncogenes stop_ save_ ################################## # Molecular system description # ################################## save_system_Q83 _Saveframe_category molecular_system _Mol_system_name "lipocalin Q83" _Abbreviation_common Q83 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Q83 $Q83 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' save_ ######################## # Monomeric polymers # ######################## save_Q83 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Q83 _Name_variant . _Abbreviation_common Q83 _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 157 _Mol_residue_sequence ; MTVPDRSEIAGKWYVVALAS NTEFFLREKDKMKMAMARIS FLGEDELKVSYAVPKPNGCR KWETTFKKTSDDGEVYYSEE AKKKVEVLDTDYKSYAVIYA TRVKDGRTLHMMRLYSRSPE VSPAATAIFRKLAGERNYTD EMVAMLPRQEECTVDEV ; loop_ _Residue_seq_code _Residue_label 1 MET 2 THR 3 VAL 4 PRO 5 ASP 6 ARG 7 SER 8 GLU 9 ILE 10 ALA 11 GLY 12 LYS 13 TRP 14 TYR 15 VAL 16 VAL 17 ALA 18 LEU 19 ALA 20 SER 21 ASN 22 THR 23 GLU 24 PHE 25 PHE 26 LEU 27 ARG 28 GLU 29 LYS 30 ASP 31 LYS 32 MET 33 LYS 34 MET 35 ALA 36 MET 37 ALA 38 ARG 39 ILE 40 SER 41 PHE 42 LEU 43 GLY 44 GLU 45 ASP 46 GLU 47 LEU 48 LYS 49 VAL 50 SER 51 TYR 52 ALA 53 VAL 54 PRO 55 LYS 56 PRO 57 ASN 58 GLY 59 CYS 60 ARG 61 LYS 62 TRP 63 GLU 64 THR 65 THR 66 PHE 67 LYS 68 LYS 69 THR 70 SER 71 ASP 72 ASP 73 GLY 74 GLU 75 VAL 76 TYR 77 TYR 78 SER 79 GLU 80 GLU 81 ALA 82 LYS 83 LYS 84 LYS 85 VAL 86 GLU 87 VAL 88 LEU 89 ASP 90 THR 91 ASP 92 TYR 93 LYS 94 SER 95 TYR 96 ALA 97 VAL 98 ILE 99 TYR 100 ALA 101 THR 102 ARG 103 VAL 104 LYS 105 ASP 106 GLY 107 ARG 108 THR 109 LEU 110 HIS 111 MET 112 MET 113 ARG 114 LEU 115 TYR 116 SER 117 ARG 118 SER 119 PRO 120 GLU 121 VAL 122 SER 123 PRO 124 ALA 125 ALA 126 THR 127 ALA 128 ILE 129 PHE 130 ARG 131 LYS 132 LEU 133 ALA 134 GLY 135 GLU 136 ARG 137 ASN 138 TYR 139 THR 140 ASP 141 GLU 142 MET 143 VAL 144 ALA 145 MET 146 LEU 147 PRO 148 ARG 149 GLN 150 GLU 151 GLU 152 CYS 153 THR 154 VAL 155 ASP 156 GLU 157 VAL 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 1JZU "A Chain A, Cell Transformation By The MycOncogene Activates Expression Of A Lipocalin: AnalysisOf The Gene (Q83) And Solution Structure Of Its ProteinProduct" 100.00 157 100 100 7e-86 GenBank AAF35894.1 "lipocalin Q83 [Coturnix coturnix]" 88.20 178 100 100 3e-85 GenBank AAK31634.1 "lipocalin Q83 [Coturnix coturnix]" 88.20 178 99 100 7e-85 SWISS-PROT Q9I9P7 "EFAB_COTJA Extracellular fatty acid bindingprotein precursor (Ex-FABP) (Lipocalin Q83)" 88.20 178 100 100 3e-85 stop_ save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bond_definitions _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide Q83 59 CYS SG Q83 152 CYS SG stop_ loop_ _Deleted_atom_mol_system_component_name _Deleted_atom_residue_seq_code _Deleted_atom_residue_label _Deleted_atom_name Q83 59 CYS HG Q83 152 CYS HG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Q83 quail 9091 Eukaryota Metazoa Coturnix coturnix 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 $Q83 'recombinant technology' "E. coli" Escherichia coli BL21(DE3)pLysS plasmid pET3d-Q83 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Q83 3.0 mM "[U-13C; U-15N]" 'potassium phosphate' 20 mM . 'potassium chloride' 50 mM . dithiothreitol 0.5 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe loop_ _Task "spectra processing" stop_ _Citation_label $ref-2 save_ save_ANSIG _Saveframe_category software _Name ANSIG loop_ _Task "spectra assignment and evaluation" stop_ _Citation_label $ref-3 save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Details ; 1H-15N HSQC HNCO HNCA CBCA(CO)NNH HNCACB HCCH-TOCSY 1H-15N TOCSY-HSQC 1H-15N NOESY-HSQC ; save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.4 0.2 n/a temperature 299 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 0.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name Q83 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 4 PRO HA H 4.12 0.03 1 2 4 PRO HB2 H 1.93 0.03 2 3 4 PRO HB3 H 1.54 0.03 2 4 4 PRO CA C 63.22 0.50 1 5 4 PRO C C 175.86 0.50 1 6 4 PRO CB C 32.18 0.50 1 7 5 ASP H H 8.02 0.03 1 8 5 ASP HA H 4.42 0.03 1 9 5 ASP HB2 H 2.67 0.03 2 10 5 ASP HB3 H 2.50 0.03 2 11 5 ASP CA C 53.95 0.50 1 12 5 ASP C C 177.44 0.50 1 13 5 ASP CB C 41.68 0.50 1 14 5 ASP N N 119.58 0.25 1 15 6 ARG H H 8.53 0.03 1 16 6 ARG HA H 4.04 0.03 1 17 6 ARG HB2 H 1.76 0.03 2 18 6 ARG HB3 H 1.72 0.03 2 19 6 ARG CA C 58.47 0.50 1 20 6 ARG C C 177.66 0.50 1 21 6 ARG CB C 31.54 0.50 1 22 6 ARG N N 124.80 0.25 1 23 7 SER H H 8.32 0.03 1 24 7 SER HA H 4.09 0.03 1 25 7 SER HB2 H 3.85 0.03 1 26 7 SER HB3 H 3.85 0.03 1 27 7 SER CA C 61.46 0.50 1 28 7 SER C C 176.36 0.50 1 29 7 SER CB C 62.93 0.50 1 30 7 SER N N 114.85 0.25 1 31 8 GLU H H 7.90 0.03 1 32 8 GLU HA H 4.26 0.03 1 33 8 GLU HB2 H 2.22 0.03 2 34 8 GLU HB3 H 2.05 0.03 2 35 8 GLU CA C 57.64 0.50 1 36 8 GLU C C 177.16 0.50 1 38 8 GLU N N 120.52 0.25 1 39 9 ILE H H 7.39 0.03 1 40 9 ILE HA H 4.25 0.03 1 41 9 ILE HB H 2.04 0.03 1 42 9 ILE CA C 62.57 0.50 1 43 9 ILE C C 175.26 0.50 1 44 9 ILE CB C 39.64 0.50 1 45 9 ILE N N 114.65 0.25 1 46 10 ALA H H 7.37 0.03 1 47 10 ALA HA H 4.08 0.03 1 48 10 ALA HB H 1.57 0.03 1 49 10 ALA CA C 52.95 0.50 1 50 10 ALA C C 177.56 0.50 1 51 10 ALA CB C 19.63 0.50 1 52 10 ALA N N 120.33 0.25 1 53 11 GLY H H 8.62 0.03 1 54 11 GLY HA2 H 4.60 0.03 2 55 11 GLY HA3 H 3.62 0.03 2 56 11 GLY CA C 44.41 0.50 1 57 11 GLY C C 173.86 0.50 1 58 11 GLY N N 108.40 0.25 1 59 12 LYS H H 8.64 0.03 1 60 12 LYS HA H 4.76 0.03 1 61 12 LYS HB2 H 1.48 0.03 1 62 12 LYS HB3 H 1.48 0.03 1 63 12 LYS CA C 57.33 0.50 1 64 12 LYS C C 176.06 0.50 1 65 12 LYS CB C 33.88 0.50 1 66 12 LYS N N 122.97 0.25 1 67 13 TRP H H 9.36 0.03 1 68 13 TRP HA H 4.55 0.03 1 69 13 TRP HB2 H 3.25 0.03 2 70 13 TRP HB3 H 2.68 0.03 2 71 13 TRP CA C 56.79 0.50 1 72 13 TRP C C 173.46 0.50 1 73 13 TRP CB C 34.27 0.50 1 74 13 TRP N N 126.59 0.25 1 75 14 TYR H H 9.29 0.03 1 76 14 TYR HA H 4.94 0.03 1 77 14 TYR HB2 H 2.85 0.03 2 78 14 TYR HB3 H 2.72 0.03 2 79 14 TYR CA C 58.03 0.50 1 80 14 TYR C C 175.56 0.50 1 81 14 TYR CB C 40.59 0.50 1 82 14 TYR N N 118.86 0.25 1 83 15 VAL H H 8.89 0.03 1 84 15 VAL HA H 3.95 0.03 1 85 15 VAL HB H 1.88 0.03 1 86 15 VAL CA C 61.98 0.50 1 87 15 VAL C C 175.66 0.50 1 88 15 VAL CB C 31.58 0.50 1 89 15 VAL N N 124.66 0.25 1 90 16 VAL H H 8.37 0.03 1 91 16 VAL HA H 4.55 0.03 1 92 16 VAL HB H 2.37 0.03 1 93 16 VAL CA C 61.41 0.50 1 94 16 VAL C C 176.06 0.50 1 95 16 VAL CB C 32.58 0.50 1 96 16 VAL N N 114.96 0.25 1 97 17 ALA H H 7.52 0.03 1 98 17 ALA HA H 5.19 0.03 1 99 17 ALA HB H 0.90 0.03 1 100 17 ALA CA C 52.22 0.50 1 101 17 ALA C C 179.06 0.50 1 102 17 ALA CB C 23.27 0.50 1 103 17 ALA N N 123.30 0.25 1 104 18 LEU H H 8.50 0.03 1 105 18 LEU HA H 5.40 0.03 1 106 18 LEU CA C 53.17 0.50 1 107 18 LEU C C 176.36 0.50 1 108 18 LEU CB C 49.13 0.50 1 109 18 LEU N N 118.58 0.25 1 110 19 ALA H H 8.26 0.03 1 111 19 ALA HA H 5.35 0.03 1 112 19 ALA HB H 0.71 0.03 1 113 19 ALA CA C 51.87 0.50 1 114 19 ALA C C 174.66 0.50 1 115 19 ALA CB C 22.31 0.50 1 116 19 ALA N N 120.60 0.25 1 117 20 SER H H 7.34 0.03 1 118 20 SER HA H 3.77 0.03 1 119 20 SER HB2 H 3.53 0.03 1 120 20 SER HB3 H 3.53 0.03 1 121 20 SER CA C 56.39 0.50 1 123 20 SER CB C 63.37 0.50 1 124 20 SER N N 114.41 0.25 1 125 21 ASN H H 7.85 0.03 1 126 21 ASN HA H 5.14 0.03 1 127 21 ASN HB2 H 3.40 0.03 2 128 21 ASN HB3 H 3.13 0.03 2 133 22 THR H H 8.00 0.03 1 134 22 THR HA H 4.33 0.03 1 139 23 GLU H H 8.89 0.03 1 140 23 GLU HA H 4.68 0.03 1 141 23 GLU CA C 60.40 0.50 1 142 23 GLU CB C 29.41 0.50 1 144 26 LEU CA C 57.78 0.50 1 145 26 LEU C C 179.46 0.50 1 146 26 LEU CB C 41.01 0.50 1 147 27 ARG H H 7.63 0.03 1 148 27 ARG HA H 4.06 0.03 1 149 27 ARG HB2 H 1.74 0.03 1 150 27 ARG HB3 H 1.74 0.03 1 151 27 ARG CA C 58.20 0.50 1 152 27 ARG C C 178.56 0.50 1 153 27 ARG CB C 31.13 0.50 1 154 27 ARG N N 117.32 0.25 1 155 28 GLU H H 7.55 0.03 1 156 28 GLU HA H 4.29 0.03 1 157 28 GLU CA C 55.85 0.50 1 158 28 GLU C C 178.56 0.50 1 159 28 GLU CB C 30.03 0.50 1 160 28 GLU N N 116.38 0.25 1 161 29 LYS H H 7.80 0.03 1 162 29 LYS CA C 59.03 0.50 1 163 29 LYS C C 177.96 0.50 1 164 29 LYS CB C 30.55 0.50 1 165 29 LYS N N 121.14 0.25 1 166 30 ASP H H 8.29 0.03 1 167 30 ASP HA H 4.30 0.03 1 168 30 ASP HB2 H 2.59 0.03 2 169 30 ASP HB3 H 2.53 0.03 2 170 30 ASP CA C 56.21 0.50 1 171 30 ASP C C 177.26 0.50 1 172 30 ASP CB C 39.69 0.50 1 173 30 ASP N N 119.25 0.25 1 174 31 LYS H H 8.01 0.03 1 175 31 LYS HA H 4.29 0.03 1 176 31 LYS HB2 H 1.88 0.03 1 177 31 LYS HB3 H 1.88 0.03 1 178 31 LYS CA C 56.04 0.50 1 179 31 LYS C C 177.36 0.50 1 180 31 LYS CB C 33.25 0.50 1 181 31 LYS N N 118.42 0.25 1 182 32 MET H H 7.13 0.03 1 183 32 MET HA H 4.43 0.03 1 184 32 MET HB2 H 2.07 0.03 1 185 32 MET HB3 H 2.07 0.03 1 186 32 MET CA C 57.02 0.50 1 187 32 MET C C 176.46 0.50 1 188 32 MET CB C 32.65 0.50 1 189 32 MET N N 120.74 0.25 1 190 33 LYS H H 8.45 0.03 1 191 33 LYS HA H 4.56 0.03 1 192 33 LYS HB2 H 1.59 0.03 1 193 33 LYS HB3 H 1.59 0.03 1 194 33 LYS CA C 55.01 0.50 1 195 33 LYS C C 173.16 0.50 1 196 33 LYS CB C 38.39 0.50 1 197 33 LYS N N 120.63 0.25 1 198 34 MET H H 8.24 0.03 1 199 34 MET HA H 4.31 0.03 1 200 34 MET CA C 58.62 0.50 1 201 34 MET C C 173.96 0.50 1 202 34 MET CB C 34.84 0.50 1 203 34 MET N N 118.70 0.25 1 204 35 ALA H H 7.33 0.03 1 205 35 ALA HA H 5.19 0.03 1 206 35 ALA HB H 1.78 0.03 1 207 35 ALA CA C 49.71 0.50 1 208 35 ALA C C 176.36 0.50 1 209 35 ALA CB C 22.92 0.50 1 210 35 ALA N N 126.38 0.25 1 211 36 MET H H 8.80 0.03 1 212 36 MET HA H 5.13 0.03 1 213 36 MET HB2 H 1.83 0.03 1 214 36 MET HB3 H 1.83 0.03 1 215 36 MET CA C 55.24 0.50 1 216 36 MET C C 172.66 0.50 1 217 36 MET CB C 38.58 0.50 1 218 36 MET N N 117.59 0.25 1 219 37 ALA H H 8.89 0.03 1 220 37 ALA HA H 5.32 0.03 1 221 37 ALA HB H 1.01 0.03 1 222 37 ALA CA C 50.18 0.50 1 223 37 ALA C C 175.76 0.50 1 224 37 ALA CB C 23.37 0.50 1 225 37 ALA N N 122.35 0.25 1 226 38 ARG H H 9.14 0.03 1 227 38 ARG HA H 5.02 0.03 1 228 38 ARG CA C 54.39 0.50 1 229 38 ARG C C 175.36 0.50 1 230 38 ARG CB C 33.46 0.50 1 231 38 ARG N N 121.09 0.25 1 232 39 ILE H H 8.85 0.03 1 233 39 ILE HA H 4.92 0.03 1 234 39 ILE HB H 1.44 0.03 1 235 39 ILE CA C 59.21 0.50 1 236 39 ILE C C 175.26 0.50 1 237 39 ILE CB C 40.37 0.50 1 238 39 ILE N N 125.86 0.25 1 239 40 SER H H 8.66 0.03 1 240 40 SER HA H 4.55 0.03 1 241 40 SER HB2 H 3.69 0.03 2 242 40 SER HB3 H 3.57 0.03 2 243 40 SER CA C 57.05 0.50 1 244 40 SER C C 172.16 0.50 1 246 40 SER N N 121.45 0.25 1 247 41 PHE H H 8.96 0.03 1 248 41 PHE HA H 4.62 0.03 1 249 41 PHE HB2 H 3.17 0.03 2 250 41 PHE HB3 H 2.80 0.03 2 251 41 PHE CA C 59.02 0.50 1 252 41 PHE C C 175.96 0.50 1 253 41 PHE CB C 40.07 0.50 1 254 41 PHE N N 122.79 0.25 1 255 42 LEU H H 8.42 0.03 1 256 42 LEU HA H 4.53 0.03 1 257 42 LEU HB2 H 1.55 0.03 2 258 42 LEU HB3 H 1.38 0.03 2 259 42 LEU CA C 54.55 0.50 1 260 42 LEU C C 176.46 0.50 1 261 42 LEU CB C 42.96 0.50 1 262 42 LEU N N 125.70 0.25 1 263 43 GLY H H 8.25 0.03 1 264 43 GLY HA2 H 4.03 0.03 1 265 43 GLY HA3 H 4.03 0.03 1 266 43 GLY CA C 45.04 0.50 1 267 43 GLY C C 173.96 0.50 1 268 43 GLY N N 109.30 0.25 1 269 44 GLU H H 8.81 0.03 1 270 44 GLU HA H 4.06 0.03 1 271 44 GLU HB2 H 1.93 0.03 1 272 44 GLU HB3 H 1.93 0.03 1 273 44 GLU CA C 58.65 0.50 1 274 44 GLU C C 177.46 0.50 1 276 44 GLU N N 120.87 0.25 1 277 45 ASP H H 8.38 0.03 1 278 45 ASP HA H 4.82 0.03 1 279 45 ASP HB2 H 2.95 0.03 2 280 45 ASP HB3 H 2.74 0.03 2 281 45 ASP CA C 54.01 0.50 1 282 45 ASP C C 174.76 0.50 1 283 45 ASP CB C 41.91 0.50 1 284 45 ASP N N 115.47 0.25 1 285 46 GLU H H 7.38 0.03 1 286 46 GLU HA H 5.46 0.03 1 287 46 GLU HB2 H 1.94 0.03 1 288 46 GLU HB3 H 1.94 0.03 1 289 46 GLU CA C 55.55 0.50 1 290 46 GLU C C 175.20 0.50 1 291 46 GLU CB C 33.93 0.50 1 292 46 GLU N N 118.27 0.25 1 293 47 LEU H H 9.04 0.03 1 294 47 LEU HA H 4.80 0.03 1 295 47 LEU CA C 54.16 0.50 1 296 47 LEU C C 173.96 0.50 1 297 47 LEU N N 124.87 0.25 1 298 48 LYS H H 8.93 0.03 1 299 48 LYS HA H 4.88 0.03 1 300 48 LYS CA C 55.27 0.50 1 301 48 LYS C C 174.56 0.50 1 302 48 LYS CB C 34.73 0.50 1 303 48 LYS N N 124.80 0.25 1 304 49 VAL H H 8.80 0.03 1 305 49 VAL HA H 4.43 0.03 1 306 49 VAL HB H 1.57 0.03 1 307 49 VAL CA C 60.68 0.50 1 308 49 VAL C C 173.86 0.50 1 309 49 VAL CB C 34.49 0.50 1 310 49 VAL N N 127.11 0.25 1 311 50 SER H H 8.26 0.03 1 312 50 SER HA H 4.76 0.03 1 313 50 SER HB2 H 3.83 0.03 2 314 50 SER HB3 H 3.41 0.03 2 315 50 SER CA C 56.27 0.50 1 317 50 SER CB C 64.09 0.50 1 318 50 SER N N 121.32 0.25 1 319 51 TYR H H 8.90 0.03 1 320 51 TYR HA H 4.77 0.03 1 321 51 TYR HB2 H 3.18 0.03 2 322 51 TYR HB3 H 3.13 0.03 2 327 52 ALA H H 8.50 0.03 1 328 52 ALA HA H 4.81 0.03 1 329 52 ALA HB H 0.87 0.03 1 334 53 VAL H H 9.06 0.03 1 335 53 VAL HA H 4.64 0.03 1 336 53 VAL HB H 1.73 0.03 1 337 53 VAL CA C 58.39 0.50 1 338 53 VAL CB C 35.81 0.50 1 343 57 ASN H H 8.25 0.03 1 344 57 ASN HA H 4.65 0.03 1 345 57 ASN HB2 H 2.79 0.03 1 346 57 ASN HB3 H 2.79 0.03 1 351 58 GLY H H 7.70 0.03 1 352 58 GLY HA2 H 4.06 0.03 2 353 58 GLY HA3 H 3.94 0.03 2 354 58 GLY CA C 46.13 0.50 1 356 61 LYS HA H 5.40 0.03 1 357 61 LYS CA C 55.24 0.50 1 358 61 LYS C C 176.16 0.50 1 359 61 LYS CB C 35.35 0.50 1 360 62 TRP H H 7.95 0.03 1 361 62 TRP HA H 4.78 0.03 1 362 62 TRP HB2 H 3.15 0.03 1 363 62 TRP HB3 H 3.15 0.03 1 364 62 TRP CA C 56.98 0.50 1 365 62 TRP C C 171.96 0.50 1 366 62 TRP CB C 30.79 0.50 1 367 62 TRP N N 122.62 0.25 1 368 63 GLU H H 8.29 0.03 1 369 63 GLU HA H 5.53 0.03 1 370 63 GLU HB2 H 1.77 0.03 1 371 63 GLU HB3 H 1.77 0.03 1 372 63 GLU CA C 54.27 0.50 1 373 63 GLU C C 175.86 0.50 1 374 63 GLU CB C 34.11 0.50 1 375 63 GLU N N 117.77 0.25 1 376 64 THR H H 8.93 0.03 1 377 64 THR HA H 4.46 0.03 1 378 64 THR HB H 3.78 0.03 1 379 64 THR CA C 62.15 0.50 1 380 64 THR C C 171.96 0.50 1 381 64 THR CB C 72.22 0.50 1 382 64 THR N N 118.56 0.25 1 383 65 THR H H 8.36 0.03 1 384 65 THR HA H 5.13 0.03 1 385 65 THR HB H 3.91 0.03 1 386 65 THR CA C 61.79 0.50 1 387 65 THR C C 173.76 0.50 1 388 65 THR CB C 70.01 0.50 1 389 65 THR N N 120.39 0.25 1 390 66 PHE H H 8.24 0.03 1 391 66 PHE HA H 4.68 0.03 1 392 66 PHE CA C 61.53 0.50 1 393 66 PHE C C 174.46 0.50 1 394 66 PHE CB C 32.21 0.50 1 395 66 PHE N N 124.84 0.25 1 396 67 LYS H H 8.82 0.03 1 397 67 LYS HA H 5.41 0.03 1 398 67 LYS HB2 H 1.99 0.03 2 399 67 LYS HB3 H 1.83 0.03 2 400 67 LYS CA C 54.62 0.50 1 401 67 LYS C C 176.76 0.50 1 402 67 LYS CB C 36.32 0.50 1 403 67 LYS N N 120.33 0.25 1 404 68 LYS H H 8.83 0.03 1 405 68 LYS CA C 57.66 0.50 1 406 68 LYS C C 177.56 0.50 1 407 68 LYS CB C 34.33 0.50 1 408 68 LYS N N 129.53 0.25 1 409 69 THR H H 8.62 0.03 1 410 69 THR HA H 4.62 0.03 1 411 69 THR HB H 4.44 0.03 1 412 69 THR CA C 60.94 0.50 1 413 69 THR C C 174.86 0.50 1 414 69 THR CB C 69.72 0.50 1 415 69 THR N N 119.00 0.25 1 416 70 SER H H 8.24 0.03 1 417 70 SER HA H 4.35 0.03 1 418 70 SER HB2 H 3.98 0.03 2 419 70 SER HB3 H 3.79 0.03 2 420 70 SER CA C 58.31 0.50 1 421 70 SER C C 174.66 0.50 1 423 70 SER N N 112.36 0.25 1 424 71 ASP H H 7.86 0.03 1 425 71 ASP HA H 4.29 0.03 1 426 71 ASP HB2 H 2.61 0.03 2 427 71 ASP HB3 H 2.03 0.03 2 428 71 ASP CA C 55.19 0.50 1 429 71 ASP C C 175.76 0.50 1 430 71 ASP CB C 42.19 0.50 1 431 71 ASP N N 121.57 0.25 1 432 72 ASP H H 8.37 0.03 1 433 72 ASP HA H 4.37 0.03 1 434 72 ASP HB2 H 2.53 0.03 2 435 72 ASP HB3 H 2.45 0.03 2 436 72 ASP CA C 55.23 0.50 1 437 72 ASP C C 175.96 0.50 1 438 72 ASP CB C 41.21 0.50 1 439 72 ASP N N 121.19 0.25 1 440 73 GLY H H 8.08 0.03 1 441 73 GLY HA2 H 3.96 0.03 2 442 73 GLY HA3 H 3.69 0.03 2 443 73 GLY CA C 44.57 0.50 1 444 73 GLY C C 173.06 0.50 1 445 73 GLY N N 109.47 0.25 1 446 74 GLU H H 8.70 0.03 1 447 74 GLU HA H 4.60 0.03 1 448 74 GLU CA C 54.76 0.50 1 449 74 GLU C C 173.66 0.50 1 450 74 GLU CB C 30.08 0.50 1 451 74 GLU N N 123.83 0.25 1 452 75 VAL H H 7.80 0.03 1 453 75 VAL HA H 4.91 0.03 1 454 75 VAL HB H 1.96 0.03 1 455 75 VAL CA C 61.52 0.50 1 456 75 VAL C C 174.26 0.50 1 457 75 VAL CB C 33.34 0.50 1 458 75 VAL N N 124.15 0.25 1 459 76 TYR H H 9.19 0.03 1 460 76 TYR HA H 5.15 0.03 1 461 76 TYR HB2 H 2.64 0.03 1 462 76 TYR HB3 H 2.64 0.03 1 463 76 TYR CA C 56.82 0.50 1 464 76 TYR C C 174.66 0.50 1 465 76 TYR CB C 42.37 0.50 1 466 76 TYR N N 125.04 0.25 1 467 77 TYR H H 9.38 0.03 1 468 77 TYR HA H 5.79 0.03 1 469 77 TYR HB2 H 2.90 0.03 2 470 77 TYR HB3 H 2.88 0.03 2 471 77 TYR CA C 57.11 0.50 1 472 77 TYR C C 174.66 0.50 1 473 77 TYR CB C 43.81 0.50 1 474 77 TYR N N 120.97 0.25 1 475 78 SER H H 8.46 0.03 1 476 78 SER HA H 4.74 0.03 1 477 78 SER HB2 H 3.09 0.03 2 478 78 SER HB3 H 2.66 0.03 2 479 78 SER CA C 54.75 0.50 1 480 78 SER C C 174.26 0.50 1 481 78 SER CB C 63.51 0.50 1 482 78 SER N N 125.23 0.25 1 483 79 GLU H H 8.60 0.03 1 484 79 GLU HA H 3.87 0.03 1 485 79 GLU HB2 H 2.06 0.03 1 486 79 GLU HB3 H 2.06 0.03 1 487 79 GLU CA C 58.71 0.50 1 488 79 GLU C C 178.76 0.50 1 489 79 GLU CB C 29.68 0.50 1 490 79 GLU N N 130.53 0.25 1 491 80 GLU H H 8.42 0.03 1 492 80 GLU HA H 3.91 0.03 1 493 80 GLU HB2 H 1.96 0.03 2 494 80 GLU HB3 H 1.86 0.03 2 495 80 GLU CA C 59.26 0.50 1 497 80 GLU CB C 29.55 0.50 1 498 80 GLU N N 119.36 0.25 1 499 81 ALA H H 7.28 0.03 1 500 81 ALA HA H 4.28 0.03 1 501 81 ALA HB H 1.30 0.03 1 506 82 LYS H H 7.74 0.03 1 507 82 LYS HA H 3.82 0.03 1 512 83 LYS H H 7.07 0.03 1 513 83 LYS HA H 5.38 0.03 1 514 83 LYS CA C 54.60 0.50 1 515 83 LYS CB C 39.14 0.50 1 517 86 GLU CA C 53.85 0.50 1 518 86 GLU C C 175.96 0.50 1 519 86 GLU CB C 33.42 0.50 1 520 87 VAL H H 8.69 0.03 1 521 87 VAL HA H 4.14 0.03 1 522 87 VAL HB H 2.20 0.03 1 523 87 VAL CA C 62.47 0.50 1 524 87 VAL C C 176.16 0.50 1 525 87 VAL CB C 31.07 0.50 1 526 87 VAL N N 125.65 0.25 1 527 88 LEU H H 8.93 0.03 1 528 88 LEU CA C 56.04 0.50 1 529 88 LEU C C 177.36 0.50 1 530 88 LEU CB C 43.20 0.50 1 531 88 LEU N N 128.45 0.25 1 532 89 ASP H H 7.02 0.03 1 533 89 ASP HA H 4.70 0.03 1 534 89 ASP HB2 H 2.73 0.03 1 535 89 ASP HB3 H 2.73 0.03 1 536 89 ASP CA C 54.98 0.50 1 537 89 ASP C C 174.16 0.50 1 538 89 ASP CB C 45.61 0.50 1 539 89 ASP N N 114.23 0.25 1 540 90 THR H H 7.99 0.03 1 541 90 THR HA H 3.75 0.03 1 542 90 THR HB H 3.83 0.03 1 543 90 THR CA C 60.59 0.50 1 544 90 THR C C 179.02 0.50 1 545 90 THR CB C 68.25 0.50 1 546 90 THR N N 120.18 0.25 1 547 91 ASP H H 6.70 0.03 1 548 91 ASP HA H 4.76 0.03 1 549 91 ASP CA C 52.90 0.50 1 550 91 ASP C C 176.86 0.50 1 551 91 ASP CB C 41.00 0.50 1 552 91 ASP N N 122.65 0.25 1 553 92 TYR H H 9.30 0.03 1 554 92 TYR CA C 61.18 0.50 1 555 92 TYR C C 174.06 0.50 1 556 92 TYR CB C 35.87 0.50 1 557 92 TYR N N 115.55 0.25 1 558 93 LYS H H 7.99 0.03 1 559 93 LYS HA H 4.59 0.03 1 560 93 LYS HB2 H 1.62 0.03 1 561 93 LYS HB3 H 1.62 0.03 1 562 93 LYS CA C 58.40 0.50 1 563 93 LYS C C 175.76 0.50 1 564 93 LYS CB C 36.94 0.50 1 565 93 LYS N N 113.02 0.25 1 566 94 SER H H 11.29 0.03 1 567 94 SER HA H 4.78 0.03 1 568 94 SER HB2 H 4.17 0.03 2 569 94 SER HB3 H 3.81 0.03 2 570 94 SER CA C 60.15 0.50 1 571 94 SER C C 174.66 0.50 1 572 94 SER CB C 67.74 0.50 1 573 94 SER N N 120.60 0.25 1 574 95 TYR H H 8.40 0.03 1 575 95 TYR HA H 6.08 0.03 1 576 95 TYR HB2 H 3.22 0.03 2 577 95 TYR HB3 H 3.08 0.03 2 578 95 TYR CA C 57.62 0.50 1 579 95 TYR C C 173.76 0.50 1 580 95 TYR CB C 41.85 0.50 1 581 95 TYR N N 123.15 0.25 1 582 96 ALA H H 9.01 0.03 1 583 96 ALA HA H 4.53 0.03 1 584 96 ALA HB H 0.90 0.03 1 585 96 ALA CA C 52.47 0.50 1 586 96 ALA C C 174.86 0.50 1 587 96 ALA CB C 23.33 0.50 1 588 96 ALA N N 121.32 0.25 1 589 97 VAL H H 9.26 0.03 1 590 97 VAL HA H 4.95 0.03 1 591 97 VAL HB H 2.09 0.03 1 592 97 VAL CA C 62.55 0.50 1 593 97 VAL C C 174.16 0.50 1 594 97 VAL CB C 32.58 0.50 1 595 97 VAL N N 122.20 0.25 1 596 98 ILE H H 9.50 0.03 1 597 98 ILE HA H 5.07 0.03 1 598 98 ILE HB H 1.91 0.03 1 599 98 ILE CA C 58.01 0.50 1 600 98 ILE C C 174.36 0.50 1 601 98 ILE CB C 41.64 0.50 1 602 98 ILE N N 130.76 0.25 1 603 99 TYR H H 9.47 0.03 1 604 99 TYR HA H 5.19 0.03 1 605 99 TYR HB2 H 2.59 0.03 1 606 99 TYR HB3 H 2.59 0.03 1 607 99 TYR CA C 56.89 0.50 1 608 99 TYR C C 173.96 0.50 1 609 99 TYR CB C 41.27 0.50 1 610 99 TYR N N 128.52 0.25 1 611 100 ALA H H 9.53 0.03 1 612 100 ALA HA H 5.63 0.03 1 613 100 ALA HB H 1.42 0.03 1 614 100 ALA CA C 50.51 0.50 1 615 100 ALA C C 175.76 0.50 1 616 100 ALA CB C 23.95 0.50 1 617 100 ALA N N 134.91 0.25 1 618 101 THR H H 9.35 0.03 1 619 101 THR HA H 5.33 0.03 1 620 101 THR HB H 3.94 0.03 1 621 101 THR CA C 61.15 0.50 1 623 101 THR CB C 72.22 0.50 1 624 101 THR N N 117.00 0.25 1 625 102 ARG H H 8.91 0.03 1 626 102 ARG HA H 5.17 0.03 1 627 102 ARG CA C 54.48 0.50 1 628 102 ARG C C 174.16 0.50 1 629 102 ARG CB C 35.32 0.50 1 630 102 ARG N N 126.40 0.25 1 631 103 VAL H H 7.74 0.03 1 632 103 VAL HA H 4.68 0.03 1 633 103 VAL CA C 61.53 0.50 1 634 103 VAL C C 175.86 0.50 1 636 103 VAL N N 122.81 0.25 1 637 104 LYS H H 8.88 0.03 1 638 104 LYS HA H 4.33 0.03 1 639 104 LYS HB2 H 1.41 0.03 1 640 104 LYS HB3 H 1.41 0.03 1 641 104 LYS CA C 55.07 0.50 1 642 104 LYS CB C 35.65 0.50 1 643 104 LYS N N 130.58 0.25 1 644 105 ASP H H 9.39 0.03 1 645 105 ASP HA H 4.66 0.03 1 646 105 ASP CA C 55.55 0.50 1 647 105 ASP C C 175.96 0.50 1 648 105 ASP CB C 39.63 0.50 1 649 105 ASP N N 129.69 0.25 1 650 106 GLY H H 8.24 0.03 1 651 106 GLY HA2 H 4.02 0.03 2 652 106 GLY HA3 H 3.45 0.03 2 653 106 GLY CA C 45.44 0.50 1 654 106 GLY C C 173.76 0.50 1 655 106 GLY N N 103.28 0.25 1 656 107 ARG H H 7.78 0.03 1 657 107 ARG HA H 4.58 0.03 1 658 107 ARG HB2 H 1.73 0.03 1 659 107 ARG HB3 H 1.73 0.03 1 660 107 ARG CA C 54.50 0.50 1 661 107 ARG C C 174.76 0.50 1 662 107 ARG CB C 32.45 0.50 1 663 107 ARG N N 121.65 0.25 1 664 108 THR H H 8.56 0.03 1 665 108 THR HA H 4.40 0.03 1 666 108 THR HB H 3.86 0.03 1 667 108 THR CA C 63.28 0.50 1 668 108 THR C C 173.56 0.50 1 669 108 THR CB C 68.83 0.50 1 670 108 THR N N 119.27 0.25 1 671 109 LEU H H 9.13 0.03 1 672 109 LEU HA H 4.63 0.03 1 673 109 LEU CA C 53.37 0.50 1 674 109 LEU C C 175.86 0.50 1 675 109 LEU N N 129.38 0.25 1 676 110 HIS H H 8.39 0.03 1 677 110 HIS HA H 5.94 0.03 1 678 110 HIS HB2 H 2.96 0.03 2 679 110 HIS HB3 H 2.89 0.03 2 680 110 HIS CA C 54.38 0.50 1 681 110 HIS C C 175.26 0.50 1 682 110 HIS CB C 33.49 0.50 1 683 110 HIS N N 116.56 0.25 1 684 111 MET H H 9.01 0.03 1 685 111 MET HA H 4.49 0.03 1 686 111 MET HB2 H 1.83 0.03 1 687 111 MET HB3 H 1.83 0.03 1 688 111 MET CA C 55.35 0.50 1 689 111 MET C C 174.06 0.50 1 690 111 MET CB C 36.68 0.50 1 691 111 MET N N 123.83 0.25 1 692 112 MET H H 9.06 0.03 1 693 112 MET HA H 5.58 0.03 1 694 112 MET HB2 H 2.05 0.03 1 695 112 MET HB3 H 2.05 0.03 1 696 112 MET CA C 54.42 0.50 1 697 112 MET C C 175.66 0.50 1 699 112 MET N N 123.51 0.25 1 700 113 ARG H H 9.37 0.03 1 701 113 ARG HA H 5.00 0.03 1 702 113 ARG CA C 54.77 0.50 1 703 113 ARG C C 174.16 0.50 1 704 113 ARG CB C 37.37 0.50 1 705 113 ARG N N 119.69 0.25 1 706 114 LEU H H 7.96 0.03 1 707 114 LEU HA H 4.99 0.03 1 708 114 LEU HB2 H 2.24 0.03 1 709 114 LEU HB3 H 2.24 0.03 1 710 114 LEU CA C 53.35 0.50 1 711 114 LEU C C 174.49 0.50 1 712 114 LEU CB C 42.99 0.50 1 713 114 LEU N N 124.96 0.25 1 714 115 TYR H H 9.54 0.03 1 715 115 TYR CA C 57.21 0.50 1 717 115 TYR N N 126.41 0.25 1 718 116 SER H H 9.85 0.03 1 719 116 SER HA H 5.73 0.03 1 720 116 SER HB2 H 3.89 0.03 2 721 116 SER HB3 H 3.59 0.03 2 722 116 SER CA C 55.65 0.50 1 723 116 SER C C 175.56 0.50 1 724 116 SER CB C 66.76 0.50 1 726 117 ARG H H 8.25 0.03 1 727 117 ARG HA H 3.60 0.03 1 728 117 ARG HB2 H 1.79 0.03 2 729 117 ARG HB3 H 1.28 0.03 2 730 117 ARG CA C 57.18 0.50 1 731 117 ARG C C 175.56 0.50 1 732 117 ARG CB C 31.55 0.50 1 733 117 ARG N N 131.03 0.25 1 734 118 SER H H 7.87 0.03 1 735 118 SER HA H 4.90 0.03 1 736 118 SER HB2 H 3.88 0.03 2 737 118 SER HB3 H 3.59 0.03 2 738 118 SER CA C 53.89 0.50 1 739 118 SER CB C 64.87 0.50 1 740 118 SER N N 111.59 0.25 1 741 119 PRO HA H 4.01 0.03 1 742 119 PRO HB2 H 2.23 0.03 2 743 119 PRO HB3 H 1.94 0.03 2 744 119 PRO CA C 64.07 0.50 1 746 119 PRO CB C 31.53 0.50 1 747 120 GLU H H 7.30 0.03 1 748 120 GLU HA H 4.17 0.03 1 749 120 GLU HB2 H 1.74 0.03 2 750 120 GLU HB3 H 1.69 0.03 2 751 120 GLU CA C 54.98 0.50 1 752 120 GLU C C 174.66 0.50 1 753 120 GLU CB C 28.81 0.50 1 755 121 VAL H H 7.81 0.03 1 756 121 VAL HA H 4.07 0.03 1 757 121 VAL HB H 1.76 0.03 1 758 121 VAL CA C 60.81 0.50 1 759 121 VAL C C 174.66 0.50 1 760 121 VAL CB C 33.32 0.50 1 761 121 VAL N N 125.36 0.25 1 762 122 SER H H 8.57 0.03 1 763 122 SER HA H 4.68 0.03 1 764 122 SER HB2 H 4.20 0.03 2 765 122 SER HB3 H 3.88 0.03 2 766 122 SER CA C 56.33 0.50 1 767 122 SER CB C 63.50 0.50 1 768 122 SER N N 124.83 0.25 1 769 123 PRO HA H 4.26 0.03 1 770 123 PRO HB2 H 2.29 0.03 2 771 123 PRO HB3 H 1.87 0.03 2 772 123 PRO CA C 65.01 0.50 1 773 123 PRO C C 179.56 0.50 1 774 123 PRO CB C 31.67 0.50 1 775 124 ALA H H 7.93 0.03 1 776 124 ALA HA H 4.01 0.03 1 777 124 ALA HB H 1.23 0.03 1 778 124 ALA CA C 55.02 0.50 1 779 124 ALA C C 180.06 0.50 1 780 124 ALA CB C 18.25 0.50 1 781 124 ALA N N 120.53 0.25 1 782 125 ALA H H 7.41 0.03 1 783 125 ALA HA H 3.37 0.03 1 784 125 ALA HB H 1.08 0.03 1 785 125 ALA CA C 54.69 0.50 1 786 125 ALA C C 179.36 0.50 1 787 125 ALA CB C 18.46 0.50 1 788 125 ALA N N 121.41 0.25 1 789 126 THR H H 7.73 0.03 1 790 126 THR HA H 4.08 0.03 1 791 126 THR HB H 3.52 0.03 1 792 126 THR CA C 66.76 0.50 1 793 126 THR C C 176.36 0.50 1 794 126 THR CB C 67.98 0.50 1 795 126 THR N N 113.63 0.25 1 796 127 ALA H H 7.80 0.03 1 797 127 ALA HA H 4.01 0.03 1 798 127 ALA HB H 1.36 0.03 1 799 127 ALA CA C 55.43 0.50 1 800 127 ALA C C 171.52 0.50 1 801 127 ALA CB C 17.86 0.50 1 802 127 ALA N N 123.57 0.25 1 803 128 ILE H H 7.55 0.03 1 804 128 ILE HA H 3.67 0.03 1 805 128 ILE HB H 1.62 0.03 1 806 128 ILE CA C 64.77 0.50 1 807 128 ILE C C 177.56 0.50 1 808 128 ILE CB C 38.61 0.50 1 809 128 ILE N N 121.34 0.25 1 810 129 PHE H H 8.16 0.03 1 811 129 PHE HA H 3.94 0.03 1 812 129 PHE HB2 H 3.20 0.03 2 813 129 PHE HB3 H 3.13 0.03 2 814 129 PHE CA C 62.45 0.50 1 815 129 PHE C C 176.26 0.50 1 816 129 PHE CB C 40.22 0.50 1 817 129 PHE N N 120.61 0.25 1 818 130 ARG H H 8.55 0.03 1 819 130 ARG HA H 3.48 0.03 1 820 130 ARG HB2 H 1.88 0.03 2 821 130 ARG HB3 H 1.75 0.03 2 822 130 ARG CA C 60.14 0.50 1 823 130 ARG C C 179.56 0.50 1 824 130 ARG CB C 29.85 0.50 1 825 130 ARG N N 116.71 0.25 1 826 131 LYS H H 7.92 0.03 1 827 131 LYS HA H 3.95 0.03 1 828 131 LYS HB2 H 1.83 0.03 1 829 131 LYS HB3 H 1.83 0.03 1 830 131 LYS CA C 59.51 0.50 1 831 131 LYS C C 179.46 0.50 1 833 131 LYS N N 122.56 0.25 1 834 132 LEU H H 8.35 0.03 1 835 132 LEU HA H 3.86 0.03 1 836 132 LEU HB2 H 1.63 0.03 1 837 132 LEU HB3 H 1.63 0.03 1 838 132 LEU CA C 57.68 0.50 1 839 132 LEU C C 179.76 0.50 1 840 132 LEU CB C 41.55 0.50 1 841 132 LEU N N 120.60 0.25 1 842 133 ALA H H 8.66 0.03 1 843 133 ALA HA H 3.89 0.03 1 844 133 ALA HB H 0.79 0.03 1 845 133 ALA CA C 55.14 0.50 1 846 133 ALA C C 171.05 0.50 1 847 133 ALA CB C 16.03 0.50 1 848 133 ALA N N 122.83 0.25 1 849 134 GLY H H 8.03 0.03 1 850 134 GLY HA2 H 3.81 0.03 1 851 134 GLY HA3 H 3.81 0.03 1 852 134 GLY CA C 47.18 0.50 1 853 134 GLY C C 178.36 0.50 1 854 134 GLY N N 107.83 0.25 1 855 135 GLU H H 7.63 0.03 1 856 135 GLU HA H 3.98 0.03 1 857 135 GLU HB2 H 1.95 0.03 1 858 135 GLU HB3 H 1.95 0.03 1 859 135 GLU CA C 58.48 0.50 1 860 135 GLU C C 177.56 0.50 1 861 135 GLU CB C 29.61 0.50 1 862 135 GLU N N 122.28 0.25 1 863 136 ARG H H 7.03 0.03 1 864 136 ARG HA H 4.05 0.03 1 865 136 ARG HB2 H 1.30 0.03 1 866 136 ARG HB3 H 1.30 0.03 1 867 136 ARG CA C 54.88 0.50 1 868 136 ARG C C 173.66 0.50 1 869 136 ARG CB C 28.58 0.50 1 870 136 ARG N N 118.40 0.25 1 871 137 ASN H H 7.47 0.03 1 872 137 ASN HA H 4.06 0.03 1 873 137 ASN HB2 H 2.79 0.03 2 874 137 ASN HB3 H 2.72 0.03 2 875 137 ASN CA C 54.89 0.50 1 876 137 ASN C C 174.36 0.50 1 877 137 ASN CB C 36.24 0.50 1 878 137 ASN N N 109.98 0.25 1 879 138 TYR H H 7.92 0.03 1 880 138 TYR HA H 5.22 0.03 1 881 138 TYR HB2 H 2.50 0.03 2 882 138 TYR HB3 H 2.45 0.03 2 883 138 TYR CA C 56.77 0.50 1 884 138 TYR C C 175.96 0.50 1 885 138 TYR CB C 36.67 0.50 1 886 138 TYR N N 119.05 0.25 1 887 139 THR H H 7.64 0.03 1 888 139 THR HA H 4.34 0.03 1 889 139 THR HB H 4.63 0.03 1 890 139 THR CA C 60.50 0.50 1 891 139 THR C C 175.66 0.50 1 892 139 THR CB C 70.29 0.50 1 893 139 THR N N 115.34 0.25 1 894 140 ASP H H 8.52 0.03 1 895 140 ASP HA H 4.18 0.03 1 896 140 ASP HB2 H 2.61 0.03 1 897 140 ASP HB3 H 2.61 0.03 1 898 140 ASP CA C 58.14 0.50 1 899 140 ASP C C 178.56 0.50 1 900 140 ASP CB C 40.99 0.50 1 901 140 ASP N N 118.31 0.25 1 902 141 GLU H H 8.41 0.03 1 903 141 GLU HA H 4.19 0.03 1 904 141 GLU HB2 H 2.03 0.03 2 905 141 GLU HB3 H 1.97 0.03 2 906 141 GLU CA C 58.18 0.50 1 907 141 GLU C C 176.36 0.50 1 908 141 GLU CB C 29.22 0.50 1 909 141 GLU N N 117.20 0.25 1 910 142 MET H H 7.87 0.03 1 911 142 MET HA H 4.42 0.03 1 912 142 MET CA C 56.05 0.50 1 913 142 MET C C 173.06 0.50 1 914 142 MET CB C 32.73 0.50 1 915 142 MET N N 117.89 0.25 1 916 143 VAL H H 7.03 0.03 1 917 143 VAL HA H 4.71 0.03 1 918 143 VAL HB H 2.04 0.03 1 921 143 VAL CB C 33.59 0.50 1 922 143 VAL N N 117.23 0.25 1 923 144 ALA H H 9.52 0.03 1 924 144 ALA HA H 4.74 0.03 1 925 144 ALA HB H 1.21 0.03 1 926 144 ALA CA C 50.59 0.50 1 927 144 ALA C C 175.96 0.50 1 928 144 ALA CB C 21.82 0.50 1 930 145 MET H H 8.53 0.03 1 931 145 MET HA H 4.85 0.03 1 932 145 MET HB2 H 1.99 0.03 2 933 145 MET HB3 H 1.93 0.03 2 934 145 MET CA C 53.16 0.50 1 935 145 MET C C 177.06 0.50 1 936 145 MET CB C 29.23 0.50 1 937 145 MET N N 122.75 0.25 1 938 146 LEU H H 7.81 0.03 1 939 146 LEU CB C 42.06 0.50 1 940 146 LEU N N 125.82 0.25 1 941 147 PRO HA H 4.49 0.03 1 942 147 PRO HB2 H 2.31 0.03 2 943 147 PRO HB3 H 1.84 0.03 2 944 147 PRO CA C 62.33 0.50 1 945 147 PRO C C 176.46 0.50 1 946 147 PRO CB C 32.83 0.50 1 947 148 ARG H H 8.43 0.03 1 948 148 ARG HA H 4.18 0.03 1 949 148 ARG HB2 H 1.74 0.03 2 950 148 ARG HB3 H 1.68 0.03 2 951 148 ARG CA C 57.45 0.50 1 952 148 ARG C C 175.66 0.50 1 953 148 ARG CB C 31.64 0.50 1 954 148 ARG N N 121.04 0.25 1 955 149 GLN H H 7.66 0.03 1 956 149 GLN HA H 4.61 0.03 1 957 149 GLN HB2 H 2.06 0.03 1 958 149 GLN HB3 H 2.06 0.03 1 959 149 GLN CA C 54.82 0.50 1 960 149 GLN C C 174.46 0.50 1 961 149 GLN CB C 28.77 0.50 1 962 149 GLN N N 115.44 0.25 1 963 150 GLU H H 8.47 0.03 1 964 150 GLU HA H 4.38 0.03 1 965 150 GLU HB2 H 2.12 0.03 2 966 150 GLU HB3 H 1.63 0.03 2 967 150 GLU CA C 55.32 0.50 1 968 150 GLU C C 175.86 0.50 1 969 150 GLU CB C 31.52 0.50 1 970 150 GLU N N 118.19 0.25 1 971 151 GLU H H 7.92 0.03 1 972 151 GLU HA H 4.17 0.03 1 973 151 GLU HB2 H 1.99 0.03 1 974 151 GLU HB3 H 1.99 0.03 1 975 151 GLU CA C 58.57 0.50 1 976 151 GLU C C 176.16 0.50 1 977 151 GLU CB C 31.39 0.50 1 978 151 GLU N N 119.58 0.25 1 979 152 CYS H H 9.52 0.03 1 980 152 CYS HA H 5.07 0.03 1 981 152 CYS HB2 H 3.01 0.03 1 982 152 CYS HB3 H 3.01 0.03 1 983 152 CYS CA C 53.09 0.50 1 984 152 CYS C C 172.96 0.50 1 985 152 CYS CB C 34.14 0.50 1 986 152 CYS N N 122.53 0.25 1 987 153 THR H H 8.40 0.03 1 988 153 THR HA H 4.80 0.03 1 989 153 THR HB H 4.03 0.03 1 990 153 THR CA C 58.96 0.50 1 991 153 THR C C 173.06 0.50 1 992 153 THR CB C 71.58 0.50 1 993 153 THR N N 118.49 0.25 1 994 154 VAL H H 6.85 0.03 1 995 154 VAL HA H 4.04 0.03 1 996 154 VAL HB H 1.91 0.03 1 997 154 VAL CA C 61.13 0.50 1 999 154 VAL CB C 32.42 0.50 1 1000 154 VAL N N 115.47 0.25 1 1001 155 ASP H H 8.29 0.03 1 1002 155 ASP HA H 4.42 0.03 1 1003 155 ASP HB2 H 2.59 0.03 2 1004 155 ASP HB3 H 2.34 0.03 2 1009 156 GLU H H 8.35 0.03 1 1010 156 GLU HA H 4.11 0.03 1 1011 156 GLU HB2 H 1.93 0.03 2 1012 156 GLU HB3 H 1.73 0.03 2 1017 157 VAL H H 7.52 0.03 1 1018 157 VAL HA H 3.88 0.03 1 1019 157 VAL HB H 1.94 0.03 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref-1 _Saveframe_category citation _MEDLINE_UI_code 8361751 _Citation_full ; Oncogene 1993 Sep;8(9):2317-24 Suppression in transformed avian fibroblasts of a gene (crp) encoding a cysteine-rich protein containing LIM domains. Weiskirchen R, Bister K ; save_ save_ref-2 _Saveframe_category citation _MEDLINE_UI_code 8520220 _Citation_full ; J Biomol NMR 1995 Nov;6(3):277-93 NMRPipe: a multidimensional spectral processing system based on UNIX pipes. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A ; save_ save_ref-3 _Saveframe_category citation _Citation_full "Kraulis, P.J., J. Magn. Reson. (1989) 24, 627-633" save_