data_6649 #Corrected using PDB structure: 1X60A # #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 # 31 E HA 4.73 4.02 # 62 L HA 4.31 3.42 # #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 G N 102.52 112.63 # 51 G N 107.99 122.28 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 51 G H 7.02 9.25 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.05 -0.27 0.20 N/A -0.12 -0.04 # #bmr6649.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6649.str file): #HA CA CB CO N HN #N/A -0.04 -0.04 N/A -0.12 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.05 +/-0.14 +/-0.18 N/A +/-0.47 +/-0.08 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.795 0.979 0.995 N/A 0.808 0.548 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.189 0.617 0.751 N/A 1.985 0.346 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the peptidoglycan binding domain of B. subtilis cell wall lytic enzyme CwlC: Characterization of the sporulation-related repeats by NMR ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mishima M. . . 2 Shida T. . . 3 Yabuki K. . . 4 Kato K. . . 5 Sekiguchi J. . . 6 Kojima C. . . stop_ _BMRB_accession_number 6649 _BMRB_flat_file_name bmr6649.str _Entry_type new _Submission_date 2005-05-26 _Accession_date 2005-06-09 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 348 '15N chemical shifts' 72 '13C chemical shifts' 212 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR. ; _Citation_status published _Citation_type journal _MEDLINE_UI_code . _PubMed_ID 16042392 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Mishima M. . . 2 Shida T. . . 3 Yabuki K. . . 4 Kato K. . . 5 Sekiguchi J. . . 6 Kojima C. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 44 _Journal_issue 30 _Page_first 10153 _Page_last 10163 _Year 2005 loop_ _Keyword "CwlC" "CwlCr" "peptidoglycan" "cell wall lytic amidase" "tandem repeats" stop_ save_ ################################## # Molecular system description # ################################## save_system_CwlCr _Saveframe_category molecular_system _Mol_system_name "Sporulation-specific N-acetylmuramoyl-L-alanine amidase (E.C.3.5.1.28)" _Abbreviation_common CwlCr _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "Sporulation-specific N-acetylmuramoyl-L-alanine amidase" $CwlCr stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'not present' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1X60 ? . stop_ save_ ######################## # Monomeric polymers # ######################## save_CwlCr _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Sporulation-specific N-acetylmuramoyl-L-alanine amidase (E.C.3.5.1.28)" _Name_variant . _Abbreviation_common CwlCr _Mol_thiol_state 'not present' ############################## # Polymer residue sequence # ############################## _Residue_count 79 _Mol_residue_sequence ; LKKTSSSGLYKVQIGAFKVK ANADSLASNAEAKGFDSIVL LKDGLYKVQIGAFSSKDNAD TLAARAKNAGFDAIVILES ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 LYS 3 LYS 4 THR 5 SER 6 SER 7 SER 8 GLY 9 LEU 10 TYR 11 LYS 12 VAL 13 GLN 14 ILE 15 GLY 16 ALA 17 PHE 18 LYS 19 VAL 20 LYS 21 ALA 22 ASN 23 ALA 24 ASP 25 SER 26 LEU 27 ALA 28 SER 29 ASN 30 ALA 31 GLU 32 ALA 33 LYS 34 GLY 35 PHE 36 ASP 37 SER 38 ILE 39 VAL 40 LEU 41 LEU 42 LYS 43 ASP 44 GLY 45 LEU 46 TYR 47 LYS 48 VAL 49 GLN 50 ILE 51 GLY 52 ALA 53 PHE 54 SER 55 SER 56 LYS 57 ASP 58 ASN 59 ALA 60 ASP 61 THR 62 LEU 63 ALA 64 ALA 65 ARG 66 ALA 67 LYS 68 ASN 69 ALA 70 GLY 71 PHE 72 ASP 73 ALA 74 ILE 75 VAL 76 ILE 77 LEU 78 GLU 79 SER stop_ _Sequence_homology_query_date 2006-01-30 _Sequence_homology_query_revised_last_date 2005-12-09 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 1X60 "A Chain A, Solution Structure Of ThePeptidoglycan Binding Domain Of B. Subtilis Cell WallLytic Enzyme Cwlc" 100.00 79 100 100 10e-36 DBJ BAA03500.1 "cell wall hydrolase [Bacillus subtilis]" 30.98 255 100 100 10e-36 EMBL CAA92813.1 "CwlC [Bacillus subtilis]" 56.03 141 100 100 10e-36 EMBL CAB13625.1 "N-acetylmuramoyl-L-alanine amidase[Bacillus subtilis subsp. subtilis str. 168]" 30.98 255 100 100 10e-36 REF NP_389623.1 "N-acetylmuramoyl-L-alanine amidase[Bacillus subtilis subsp. subtilis str. 168]" 30.98 255 100 100 10e-36 SWISS-PROT Q06320 "CWLC_BACSU Sporulation-specificN-acetylmuramoyl-L-alanine amidase (Cell wall hydrolase)(Autolysin)" 30.98 255 100 100 10e-36 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $CwlCr "Bacillus subtilis" 1423 Bacteria . Bacillus subtilis 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 $CwlCr 'recombinant technology' . . . . . 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 $CwlCr 1.7 mM "[U-15N; U-13C]" "phosphate buffer K" 50 mM . D2O 100 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $CwlCr 1.7 mM "[U-15N]" "phosphate buffer K" 50 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version "ver 2.3" loop_ _Task processing stop_ _Details "Delaglio, F." save_ save_Sparky _Saveframe_category software _Name Sparky _Version "ver 3.110" loop_ _Task "data analysis" stop_ _Details "Goddard, T.D." save_ save_CYANA _Saveframe_category software _Name CYANA _Version "ver 1.05" loop_ _Task "structure solution" stop_ _Details "Herrmann, T." save_ save_CNS _Saveframe_category software _Name CNS _Version "ver 1.1" loop_ _Task refinement stop_ _Details "Brunger, A.T." save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AVANCE _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 3D 13C-separated NOESY 3D 15N-separated NOESY ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.9 . pH temperature 303 . K 'ionic strength' 70 . mM 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 0.00 external direct cylindrical . parallel 1.0 DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530 DSS N 15 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_chemical_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 "Sporulation-specific N-acetylmuramoyl-L-alanine amidase" 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 LEU CA C 54.44 0.000 . 2 1 LEU CB C 40.91 0.000 . 3 1 LEU H H 8.20 0.000 . 4 1 LEU N N 120.42 0.000 . 5 2 LYS CA C 57.57 0.000 . 6 2 LYS CB C 33.58 0.000 . 7 2 LYS H H 7.64 0.000 . 8 2 LYS N N 125.89 0.000 . 9 7 SER CA C 58.03 0.000 . 10 7 SER CB C 64.10 0.000 . 11 7 SER HA H 4.39 0.000 . 12 7 SER HB2 H 3.80 0.000 . 13 7 SER HB3 H 3.75 0.000 . 14 8 GLY CA C 45.05 0.000 . 15 8 GLY H H 8.03 0.000 . 16 8 GLY HA2 H 3.64 0.000 . 17 8 GLY HA3 H 3.71 0.000 . 18 8 GLY N N 109.55 0.000 . 19 9 LEU CA C 53.83 0.000 . 20 9 LEU CB C 44.68 0.000 . 21 9 LEU CD1 C 25.32 0.000 . 22 9 LEU CD2 C 23.41 0.000 . 23 9 LEU CG C 26.36 0.000 . 24 9 LEU H H 7.92 0.000 . 25 9 LEU HA H 4.36 0.000 . 26 9 LEU HB2 H 1.38 0.000 . 27 9 LEU HB3 H 1.08 0.000 . 28 9 LEU HG H 1.41 0.000 . 29 9 LEU HD1 H 0.70 0.000 . 30 9 LEU HD2 H 0.68 0.000 . 31 9 LEU N N 120.66 0.000 . 32 10 TYR CA C 58.38 0.000 . 33 10 TYR CB C 38.68 0.000 . 34 10 TYR H H 8.88 0.000 . 35 10 TYR HA H 4.63 0.000 . 36 10 TYR HB2 H 2.80 0.000 . 37 10 TYR HB3 H 2.39 0.000 . 38 10 TYR N N 119.05 0.000 . 39 11 LYS CA C 53.14 0.000 . 40 11 LYS CB C 34.22 0.000 . 41 11 LYS CG C 24.61 0.000 . 42 11 LYS H H 9.38 0.000 . 43 11 LYS HA H 5.11 0.000 . 44 11 LYS HB2 H 1.78 0.000 . 45 11 LYS HB3 H 1.45 0.000 . 46 11 LYS HG2 H 1.36 0.000 . 47 11 LYS HG3 H 1.50 0.000 . 48 11 LYS N N 123.20 0.000 . 49 12 VAL CA C 61.42 0.000 . 50 12 VAL CB C 32.06 0.000 . 51 12 VAL CG1 C 22.07 0.000 . 52 12 VAL CG2 C 22.86 0.000 . 53 12 VAL H H 8.18 0.000 . 54 12 VAL HA H 4.85 0.000 . 55 12 VAL HB H 1.90 0.000 . 56 12 VAL HG1 H 0.59 0.000 . 57 12 VAL HG2 H 1.11 0.000 . 58 12 VAL N N 119.51 0.000 . 59 13 GLN CA C 54.47 0.000 . 60 13 GLN CB C 33.67 0.000 . 61 13 GLN CG C 35.25 0.000 . 62 13 GLN H H 9.18 0.000 . 63 13 GLN HA H 5.18 0.000 . 64 13 GLN HB2 H 1.92 0.000 . 65 13 GLN HB3 H 1.80 0.000 . 66 13 GLN HG2 H 2.27 0.000 . 67 13 GLN HG3 H 2.19 0.000 . 68 13 GLN N N 129.43 0.000 . 69 14 ILE CA C 60.28 0.000 . 70 14 ILE CB C 38.32 0.000 . 71 14 ILE CD1 C 14.63 0.000 . 72 14 ILE CG1 C 26.33 0.000 . 73 14 ILE CG2 C 17.47 0.000 . 74 14 ILE H H 8.53 0.000 . 75 14 ILE HA H 5.00 0.000 . 76 14 ILE HB H 2.12 0.000 . 77 14 ILE HG12 H 1.02 0.000 . 78 14 ILE HG13 H 0.49 0.000 . 79 14 ILE HD1 H 0.05 0.000 . 80 14 ILE HG2 H 0.38 0.000 . 81 14 ILE N N 112.82 0.000 . 82 15 GLY CA C 46.35 0.000 . 83 15 GLY H H 7.13 0.000 . 84 15 GLY HA2 H 3.76 0.000 . 85 15 GLY HA3 H 3.83 0.000 . 86 15 GLY N N 108.03 0.000 . 87 16 ALA CA C 51.82 0.000 . 88 16 ALA CB C 21.20 0.000 . 89 16 ALA H H 7.62 0.000 . 90 16 ALA HA H 5.07 0.000 . 91 16 ALA HB H 1.10 0.000 . 92 16 ALA N N 122.42 0.000 . 93 17 PHE CA C 56.76 0.000 . 94 17 PHE CB C 44.00 0.000 . 95 17 PHE H H 8.94 0.000 . 96 17 PHE N N 119.34 0.000 . 97 19 VAL CA C 61.34 0.000 . 98 19 VAL CB C 33.25 0.000 . 99 19 VAL CG1 C 21.74 0.000 . 100 19 VAL CG2 C 21.14 0.000 . 101 19 VAL H H 7.78 0.000 . 102 19 VAL HA H 4.21 0.000 . 103 19 VAL HB H 2.11 0.000 . 104 19 VAL HG1 H 0.93 0.000 . 105 19 VAL HG2 H 0.97 0.000 . 106 19 VAL N N 117.95 0.000 . 107 20 LYS CA C 60.57 0.000 . 108 20 LYS CB C 31.38 0.000 . 109 20 LYS CD C 28.60 0.000 . 110 20 LYS CE C 42.17 0.000 . 111 20 LYS CG C 25.00 0.000 . 112 20 LYS H H 8.53 0.000 . 113 20 LYS HA H 2.71 0.000 . 114 20 LYS HB2 H 0.49 0.000 . 115 20 LYS HB3 H 1.25 0.000 . 116 20 LYS HD2 H 1.33 0.000 . 117 20 LYS HD3 H 1.42 0.000 . 118 20 LYS HE2 H 2.94 0.000 . 119 20 LYS HE3 H 3.03 0.000 . 120 20 LYS HG2 H 0.37 0.000 . 121 20 LYS HG3 H 1.21 0.000 . 122 20 LYS N N 131.02 0.000 . 123 21 ALA CA C 55.11 0.000 . 124 21 ALA CB C 18.07 0.000 . 125 21 ALA H H 8.38 0.000 . 126 21 ALA HA H 3.96 0.000 . 127 21 ALA HB H 1.23 0.000 . 128 21 ALA N N 118.38 0.000 . 129 22 ASN CA C 55.53 0.000 . 130 22 ASN CB C 38.16 0.000 . 131 22 ASN H H 6.92 0.000 . 132 22 ASN HA H 4.12 0.000 . 133 22 ASN HB2 H 1.92 0.000 . 134 22 ASN HB3 H 2.28 0.000 . 135 22 ASN N N 113.53 0.000 . 136 23 ALA CA C 54.45 0.000 . 137 23 ALA CB C 19.06 0.000 . 138 23 ALA H H 6.79 0.000 . 139 23 ALA HA H 3.62 0.000 . 140 23 ALA HB H 1.37 0.000 . 141 23 ALA N N 123.87 0.000 . 142 24 ASP CA C 56.97 0.000 . 143 24 ASP CB C 39.73 0.000 . 144 24 ASP H H 8.60 0.000 . 145 24 ASP HA H 4.11 0.000 . 146 24 ASP HB2 H 2.42 0.000 . 147 24 ASP HB3 H 2.51 0.000 . 148 24 ASP N N 118.78 0.000 . 149 25 SER CA C 61.25 0.000 . 150 25 SER CB C 62.72 0.000 . 151 25 SER H H 7.68 0.000 . 152 25 SER HA H 4.13 0.000 . 153 25 SER HB2 H 3.76 0.000 . 154 25 SER HB3 H 3.81 0.000 . 155 25 SER N N 114.82 0.000 . 156 26 LEU CA C 57.88 0.000 . 157 26 LEU CB C 40.91 0.000 . 158 26 LEU CD1 C 23.35 0.000 . 159 26 LEU CD2 C 26.69 0.000 . 160 26 LEU CG C 26.91 0.000 . 161 26 LEU H H 7.16 0.000 . 162 26 LEU HA H 4.30 0.000 . 163 26 LEU HB2 H 1.90 0.000 . 164 26 LEU HB3 H 1.62 0.000 . 165 26 LEU HG H 1.51 0.000 . 166 26 LEU HD1 H 1.24 0.000 . 167 26 LEU HD2 H 1.10 0.000 . 168 26 LEU N N 123.04 0.000 . 169 27 ALA CA C 55.99 0.000 . 170 27 ALA CB C 17.48 0.000 . 171 27 ALA H H 8.76 0.000 . 172 27 ALA HA H 3.63 0.000 . 173 27 ALA HB H 1.36 0.000 . 174 27 ALA N N 120.90 0.000 . 175 28 SER CA C 61.56 0.000 . 176 28 SER CB C 62.90 0.000 . 177 28 SER H H 8.13 0.000 . 178 28 SER HA H 4.27 0.000 . 179 28 SER HB2 H 3.92 0.000 . 180 28 SER HB3 H 3.98 0.000 . 181 28 SER N N 114.65 0.000 . 182 29 ASN CA C 56.27 0.000 . 183 29 ASN CB C 38.68 0.000 . 184 29 ASN H H 7.95 0.000 . 185 29 ASN HA H 4.54 0.000 . 186 29 ASN HB2 H 3.07 0.000 . 187 29 ASN HB3 H 3.13 0.000 . 188 29 ASN N N 122.97 0.000 . 189 30 ALA CA C 55.48 0.000 . 190 30 ALA CB C 16.42 0.000 . 191 30 ALA H H 8.48 0.000 . 192 30 ALA HA H 4.07 0.000 . 193 30 ALA HB H 0.80 0.000 . 194 30 ALA N N 121.27 0.000 . 195 31 GLU CA C 59.21 0.000 . 196 31 GLU CB C 29.51 0.000 . 197 31 GLU CG C 36.34 0.000 . 198 31 GLU H H 8.29 0.000 . 199 31 GLU HA H 4.68 0.000 . 200 31 GLU HB2 H 2.22 0.000 . 201 31 GLU HB3 H 2.15 0.000 . 202 31 GLU HG2 H 2.30 0.000 . 203 31 GLU HG3 H 2.46 0.000 . 204 31 GLU N N 121.40 0.000 . 205 32 ALA CA C 54.62 0.000 . 206 32 ALA CB C 17.81 0.000 . 207 32 ALA H H 7.97 0.000 . 208 32 ALA HA H 4.22 0.000 . 209 32 ALA HB H 1.61 0.000 . 210 32 ALA N N 122.78 0.000 . 211 33 LYS CA C 55.62 0.000 . 212 33 LYS CB C 33.08 0.000 . 213 33 LYS CD C 29.51 0.000 . 214 33 LYS CE C 42.58 0.000 . 215 33 LYS CG C 25.92 0.000 . 216 33 LYS H H 7.45 0.000 . 217 33 LYS HA H 4.43 0.000 . 218 33 LYS HB2 H 2.15 0.000 . 219 33 LYS HB3 H 2.45 0.000 . 220 33 LYS HD2 H 1.77 0.000 . 221 33 LYS HD3 H 1.87 0.000 . 222 33 LYS HE2 H 3.00 0.000 . 223 33 LYS HE3 H 3.06 0.000 . 224 33 LYS HG2 H 1.67 0.000 . 225 33 LYS HG3 H 1.81 0.000 . 226 33 LYS N N 115.67 0.000 . 227 34 GLY CA C 45.33 0.000 . 228 34 GLY H H 7.80 0.000 . 229 34 GLY HA2 H 3.93 0.000 . 230 34 GLY HA3 H 3.59 0.000 . 231 34 GLY N N 105.90 0.000 . 232 35 PHE CA C 56.99 0.000 . 233 35 PHE CB C 39.53 0.000 . 234 35 PHE H H 8.01 0.000 . 235 35 PHE HA H 4.57 0.000 . 236 35 PHE HB2 H 2.91 0.000 . 237 35 PHE HB3 H 2.37 0.000 . 238 35 PHE N N 119.57 0.000 . 239 36 ASP CA C 53.45 0.000 . 240 36 ASP CB C 40.61 0.000 . 241 36 ASP H H 9.23 0.000 . 242 36 ASP HA H 4.73 0.000 . 243 36 ASP HB2 H 2.53 0.000 . 244 36 ASP HB3 H 2.66 0.000 . 245 36 ASP N N 123.81 0.000 . 246 37 SER CA C 57.03 0.000 . 247 37 SER CB C 66.51 0.000 . 248 37 SER H H 8.08 0.000 . 249 37 SER HA H 5.00 0.000 . 250 37 SER HB2 H 3.42 0.000 . 251 37 SER HB3 H 3.50 0.000 . 252 37 SER N N 115.33 0.000 . 253 38 ILE CA C 59.88 0.000 . 254 38 ILE CB C 42.20 0.000 . 255 38 ILE CD1 C 14.03 0.000 . 256 38 ILE CG1 C 27.32 0.000 . 257 38 ILE CG2 C 17.53 0.000 . 258 38 ILE H H 8.71 0.000 . 259 38 ILE HA H 4.44 0.000 . 260 38 ILE HB H 1.70 0.000 . 261 38 ILE HG12 H 1.00 0.000 . 262 38 ILE HG13 H 1.38 0.000 . 263 38 ILE HD1 H 0.77 0.000 . 264 38 ILE HG2 H 0.79 0.000 . 265 38 ILE N N 120.09 0.000 . 266 39 VAL CA C 61.52 0.000 . 267 39 VAL CB C 32.80 0.000 . 268 39 VAL CG1 C 22.40 0.000 . 269 39 VAL CG2 C 21.85 0.000 . 270 39 VAL H H 8.17 0.000 . 271 39 VAL HA H 4.95 0.000 . 272 39 VAL HB H 1.92 0.000 . 273 39 VAL HG1 H 0.83 0.000 . 274 39 VAL HG2 H 0.84 0.000 . 275 39 VAL N N 124.29 0.000 . 276 40 LEU CA C 53.35 0.000 . 277 40 LEU CB C 45.50 0.000 . 278 40 LEU CD1 C 25.76 0.000 . 279 40 LEU CD2 C 23.41 0.000 . 280 40 LEU CG C 26.36 0.000 . 281 40 LEU H H 9.11 0.000 . 282 40 LEU HA H 4.69 0.000 . 283 40 LEU HB2 H 1.38 0.000 . 284 40 LEU HB3 H 1.45 0.000 . 285 40 LEU HG H 1.43 0.000 . 286 40 LEU HD1 H 0.73 0.000 . 287 40 LEU HD2 H 0.75 0.000 . 288 40 LEU N N 129.19 0.000 . 289 41 LEU CA C 53.68 0.000 . 290 41 LEU CB C 41.72 0.000 . 291 41 LEU CD1 C 19.91 0.000 . 292 41 LEU CD2 C 25.05 0.000 . 293 41 LEU CG C 26.58 0.000 . 294 41 LEU H H 8.40 0.000 . 295 41 LEU HA H 4.67 0.000 . 296 41 LEU HB2 H 1.03 0.000 . 297 41 LEU HB3 H 1.62 0.000 . 298 41 LEU HG H 1.03 0.000 . 299 41 LEU HD1 H -0.21 0.000 . 300 41 LEU HD2 H 0.68 0.000 . 301 41 LEU N N 125.75 0.000 . 302 42 LYS CA C 55.65 0.000 . 303 42 LYS CB C 35.79 0.000 . 304 42 LYS CD C 29.18 0.000 . 305 42 LYS CE C 38.26 0.000 . 306 42 LYS CG C 24.31 0.000 . 307 42 LYS H H 8.99 0.000 . 308 42 LYS HA H 4.30 0.000 . 309 42 LYS HB2 H 1.45 0.000 . 310 42 LYS HB3 H 1.50 0.000 . 311 42 LYS HD2 H 1.54 0.000 . 312 42 LYS HD3 H 1.60 0.000 . 313 42 LYS HE2 H 2.86 0.000 . 314 42 LYS HE3 H 2.37 0.000 . 315 42 LYS HG2 H 1.25 0.000 . 316 42 LYS HG3 H 1.32 0.000 . 317 42 LYS N N 129.20 0.000 . 318 43 ASP CA C 55.43 0.000 . 319 43 ASP CB C 39.79 0.000 . 320 43 ASP H H 9.21 0.000 . 321 43 ASP HA H 4.15 0.000 . 322 43 ASP HB2 H 2.80 0.000 . 323 43 ASP HB3 H 2.59 0.000 . 324 43 ASP N N 125.13 0.000 . 325 44 GLY CA C 45.37 0.000 . 326 44 GLY H H 8.30 0.000 . 327 44 GLY HA2 H 3.95 0.000 . 328 44 GLY HA3 H 3.37 0.000 . 329 44 GLY N N 102.52 0.000 . 330 45 LEU CA C 52.53 0.000 . 331 45 LEU CB C 45.79 0.000 . 332 45 LEU CD1 C 25.46 0.000 . 333 45 LEU CD2 C 23.44 0.000 . 334 45 LEU CG C 25.62 0.000 . 335 45 LEU H H 7.53 0.000 . 336 45 LEU HA H 4.50 0.000 . 337 45 LEU HB2 H 1.52 0.000 . 338 45 LEU HB3 H 1.00 0.000 . 339 45 LEU HG H 1.40 0.000 . 340 45 LEU HD1 H 0.69 0.000 . 341 45 LEU HD2 H 0.66 0.000 . 342 45 LEU N N 120.60 0.000 . 343 46 TYR CA C 58.16 0.000 . 344 46 TYR CB C 38.35 0.000 . 345 46 TYR H H 9.15 0.000 . 346 46 TYR HA H 4.64 0.000 . 347 46 TYR HB2 H 2.80 0.000 . 348 46 TYR HB3 H 2.33 0.000 . 349 46 TYR N N 119.88 0.000 . 350 47 LYS CA C 55.19 0.000 . 351 47 LYS CB C 34.15 0.000 . 352 47 LYS CD C 30.27 0.000 . 353 47 LYS CE C 41.88 0.000 . 354 47 LYS CG C 25.30 0.000 . 355 47 LYS H H 9.44 0.000 . 356 47 LYS HA H 4.90 0.000 . 357 47 LYS HB2 H 1.63 0.000 . 358 47 LYS HB3 H 1.74 0.000 . 359 47 LYS HD2 H 1.53 0.000 . 360 47 LYS HD3 H 1.64 0.000 . 361 47 LYS HE2 H 2.76 0.000 . 362 47 LYS HE3 H 2.84 0.000 . 363 47 LYS HG2 H 1.21 0.000 . 364 47 LYS HG3 H 1.50 0.000 . 365 47 LYS N N 125.32 0.000 . 366 48 VAL CA C 61.45 0.000 . 367 48 VAL CB C 32.00 0.000 . 368 48 VAL CG1 C 21.41 0.000 . 369 48 VAL CG2 C 22.40 0.000 . 370 48 VAL H H 8.51 0.000 . 371 48 VAL HA H 4.86 0.000 . 372 48 VAL HB H 1.92 0.000 . 373 48 VAL HG1 H 0.62 0.000 . 374 48 VAL HG2 H 1.15 0.000 . 375 48 VAL N N 120.76 0.000 . 376 49 GLN CA C 54.04 0.000 . 377 49 GLN CB C 32.51 0.000 . 378 49 GLN CG C 34.81 0.000 . 379 49 GLN H H 9.07 0.000 . 380 49 GLN HA H 5.29 0.000 . 381 49 GLN HB2 H 1.85 0.000 . 382 49 GLN HB3 H 1.92 0.000 . 383 49 GLN HG2 H 2.11 0.000 . 384 49 GLN HG3 H 2.23 0.000 . 385 49 GLN N N 127.77 0.000 . 386 50 ILE CA C 59.97 0.000 . 387 50 ILE CB C 38.24 0.000 . 388 50 ILE CD1 C 14.79 0.000 . 389 50 ILE CG1 C 26.50 0.000 . 390 50 ILE CG2 C 16.54 0.000 . 391 50 ILE H H 8.51 0.000 . 392 50 ILE HA H 5.22 0.000 . 393 50 ILE HB H 2.29 0.000 . 394 50 ILE HG12 H 1.07 0.000 . 395 50 ILE HG13 H 0.55 0.000 . 396 50 ILE HD1 H 0.24 0.000 . 397 50 ILE HG2 H 0.39 0.000 . 398 50 ILE N N 111.02 0.000 . 399 51 GLY CA C 46.53 0.000 . 400 51 GLY H H 7.07 0.000 . 401 51 GLY HA2 H 3.77 0.000 . 402 51 GLY HA3 H 3.85 0.000 . 403 51 GLY N N 107.99 0.000 . 404 52 ALA CA C 51.61 0.000 . 405 52 ALA CB C 21.65 0.000 . 406 52 ALA H H 7.51 0.000 . 407 52 ALA HA H 5.06 0.000 . 408 52 ALA HB H 1.07 0.000 . 409 52 ALA N N 123.09 0.000 . 410 53 PHE CA C 56.71 0.000 . 411 53 PHE CB C 44.41 0.000 . 412 53 PHE H H 9.17 0.000 . 413 53 PHE N N 119.14 0.000 . 414 55 SER CA C 55.78 0.000 . 415 55 SER CB C 63.98 0.000 . 416 55 SER H H 7.75 0.000 . 417 55 SER HA H 4.76 0.000 . 418 55 SER HB2 H 3.89 0.000 . 419 55 SER HB3 H 3.84 0.000 . 420 55 SER N N 114.45 0.000 . 421 56 LYS CA C 59.36 0.000 . 422 56 LYS CB C 32.19 0.000 . 423 56 LYS CD C 29.23 0.000 . 424 56 LYS CE C 41.76 0.000 . 425 56 LYS CG C 25.51 0.000 . 426 56 LYS H H 8.53 0.000 . 427 56 LYS HA H 2.76 0.000 . 428 56 LYS HB2 H 0.61 0.000 . 429 56 LYS HB3 H 1.25 0.000 . 430 56 LYS HD2 H 1.41 0.000 . 431 56 LYS HD3 H 1.48 0.000 . 432 56 LYS HE2 H 2.85 0.000 . 433 56 LYS HE3 H 2.92 0.000 . 434 56 LYS HG2 H 0.61 0.000 . 435 56 LYS HG3 H 1.29 0.000 . 436 56 LYS N N 129.50 0.000 . 437 57 ASP CA C 57.18 0.000 . 438 57 ASP CB C 39.71 0.000 . 439 57 ASP H H 8.02 0.000 . 440 57 ASP HA H 4.12 0.000 . 441 57 ASP HB2 H 2.51 0.000 . 442 57 ASP HB3 H 2.35 0.000 . 443 57 ASP N N 116.45 0.000 . 444 58 ASN CA C 55.83 0.000 . 445 58 ASN CB C 38.13 0.000 . 446 58 ASN H H 7.29 0.000 . 447 58 ASN HA H 4.11 0.000 . 448 58 ASN HB2 H 1.99 0.000 . 449 58 ASN HB3 H 2.27 0.000 . 450 58 ASN N N 116.84 0.000 . 451 59 ALA CA C 54.75 0.000 . 452 59 ALA CB C 18.80 0.000 . 453 59 ALA H H 6.90 0.000 . 454 59 ALA HA H 3.49 0.000 . 455 59 ALA HB H 1.29 0.000 . 456 59 ALA N N 123.43 0.000 . 457 60 ASP CA C 57.10 0.000 . 458 60 ASP CB C 39.84 0.000 . 459 60 ASP H H 8.80 0.000 . 460 60 ASP HA H 4.12 0.000 . 461 60 ASP HB2 H 2.64 0.000 . 462 60 ASP HB3 H 2.44 0.000 . 463 60 ASP N N 119.25 0.000 . 464 61 THR CA C 66.56 0.000 . 465 61 THR CB C 68.57 0.000 . 466 61 THR CG2 C 22.01 0.000 . 467 61 THR H H 7.86 0.000 . 468 61 THR HA H 3.84 0.000 . 469 61 THR HB H 4.01 0.000 . 470 61 THR HG2 H 1.17 0.000 . 471 61 THR N N 117.75 0.000 . 472 62 LEU CA C 57.83 0.000 . 473 62 LEU CB C 40.51 0.000 . 474 62 LEU CD1 C 23.74 0.000 . 475 62 LEU CD2 C 26.31 0.000 . 476 62 LEU CG C 26.91 0.000 . 477 62 LEU H H 7.21 0.000 . 478 62 LEU HA H 4.26 0.000 . 479 62 LEU HB2 H 1.61 0.000 . 480 62 LEU HB3 H 1.91 0.000 . 481 62 LEU HG H 1.56 0.000 . 482 62 LEU HD1 H 1.28 0.000 . 483 62 LEU HD2 H 1.16 0.000 . 484 62 LEU N N 123.53 0.000 . 485 63 ALA CA C 54.77 0.000 . 486 63 ALA CB C 17.37 0.000 . 487 63 ALA H H 8.81 0.000 . 488 63 ALA HA H 3.52 0.000 . 489 63 ALA HB H 1.26 0.000 . 490 63 ALA N N 121.05 0.000 . 491 64 ALA CA C 55.40 0.000 . 492 64 ALA CB C 17.61 0.000 . 493 64 ALA H H 7.88 0.000 . 494 64 ALA HA H 4.03 0.000 . 495 64 ALA HB H 1.48 0.000 . 496 64 ALA N N 119.20 0.000 . 497 65 ARG CA C 59.69 0.000 . 498 65 ARG CB C 30.44 0.000 . 499 65 ARG CD C 44.37 0.000 . 500 65 ARG CG C 27.76 0.000 . 501 65 ARG H H 7.64 0.000 . 502 65 ARG HA H 4.16 0.000 . 503 65 ARG HB2 H 2.13 0.000 . 504 65 ARG HB3 H 2.21 0.000 . 505 65 ARG HD2 H 3.21 0.000 . 506 65 ARG HD3 H 3.25 0.000 . 507 65 ARG HG2 H 1.73 0.000 . 508 65 ARG HG3 H 2.00 0.000 . 509 65 ARG N N 119.71 0.000 . 510 66 ALA CA C 54.90 0.000 . 511 66 ALA CB C 17.40 0.000 . 512 66 ALA H H 8.67 0.000 . 513 66 ALA HA H 4.02 0.000 . 514 66 ALA HB H 0.87 0.000 . 515 66 ALA N N 123.01 0.000 . 516 67 LYS CA C 59.12 0.000 . 517 67 LYS CB C 32.04 0.000 . 518 67 LYS CD C 29.51 0.000 . 519 67 LYS CE C 41.94 0.000 . 520 67 LYS CG C 25.68 0.000 . 521 67 LYS H H 8.75 0.000 . 522 67 LYS HA H 4.98 0.000 . 523 67 LYS HB2 H 1.95 0.000 . 524 67 LYS HB3 H 2.02 0.000 . 525 67 LYS HD2 H 1.72 0.000 . 526 67 LYS HD3 H 1.80 0.000 . 527 67 LYS HE2 H 2.96 0.000 . 528 67 LYS HE3 H 3.00 0.000 . 529 67 LYS HG2 H 1.62 0.000 . 530 67 LYS HG3 H 1.69 0.000 . 531 67 LYS N N 121.58 0.000 . 532 68 ASN CA C 55.58 0.000 . 533 68 ASN CB C 38.18 0.000 . 534 68 ASN H H 8.05 0.000 . 535 68 ASN HA H 4.49 0.000 . 536 68 ASN HB2 H 2.88 0.000 . 537 68 ASN HB3 H 2.95 0.000 . 538 68 ASN N N 119.68 0.000 . 539 69 ALA CA C 52.25 0.000 . 540 69 ALA CB C 19.37 0.000 . 541 69 ALA H H 7.51 0.000 . 542 69 ALA HA H 4.49 0.000 . 543 69 ALA HB H 1.83 0.000 . 544 69 ALA N N 120.09 0.000 . 545 70 GLY CA C 44.85 0.000 . 546 70 GLY H H 7.65 0.000 . 547 70 GLY HA2 H 3.95 0.000 . 548 70 GLY HA3 H 3.56 0.000 . 549 70 GLY N N 104.82 0.000 . 550 71 PHE CA C 57.25 0.000 . 551 71 PHE CB C 40.35 0.000 . 552 71 PHE H H 8.00 0.000 . 553 71 PHE HA H 4.70 0.000 . 554 71 PHE HB2 H 2.94 0.000 . 555 71 PHE HB3 H 2.24 0.000 . 556 71 PHE N N 118.80 0.000 . 557 72 ASP CA C 52.59 0.000 . 558 72 ASP CB C 39.72 0.000 . 559 72 ASP H H 9.67 0.000 . 560 72 ASP HA H 4.70 0.000 . 561 72 ASP HB2 H 2.74 0.000 . 562 72 ASP HB3 H 2.49 0.000 . 563 72 ASP N N 125.12 0.000 . 564 73 ALA CA C 51.46 0.000 . 565 73 ALA CB C 21.53 0.000 . 566 73 ALA H H 7.00 0.000 . 567 73 ALA HA H 4.71 0.000 . 568 73 ALA HB H 1.06 0.000 . 569 73 ALA N N 121.77 0.000 . 570 74 ILE CA C 59.54 0.000 . 571 74 ILE CB C 42.02 0.000 . 572 74 ILE CD1 C 13.70 0.000 . 573 74 ILE CG1 C 26.23 0.000 . 574 74 ILE CG2 C 17.09 0.000 . 575 74 ILE H H 8.84 0.000 . 576 74 ILE HA H 4.49 0.000 . 577 74 ILE HB H 1.72 0.000 . 578 74 ILE HG12 H 1.28 0.000 . 579 74 ILE HG13 H 1.05 0.000 . 580 74 ILE HD1 H 0.71 0.000 . 581 74 ILE HG2 H 0.80 0.000 . 582 74 ILE N N 119.96 0.000 . 583 75 VAL CA C 61.54 0.000 . 584 75 VAL CB C 32.57 0.000 . 585 75 VAL CG1 C 22.89 0.000 . 586 75 VAL CG2 C 21.96 0.000 . 587 75 VAL H H 8.31 0.000 . 588 75 VAL HA H 4.98 0.000 . 589 75 VAL HB H 1.90 0.000 . 590 75 VAL HG1 H 0.88 0.000 . 591 75 VAL HG2 H 0.88 0.000 . 592 75 VAL N N 123.68 0.000 . 593 76 ILE CA C 59.06 0.000 . 594 76 ILE CB C 42.04 0.000 . 595 76 ILE CD1 C 13.65 0.000 . 596 76 ILE CG1 C 26.88 0.000 . 597 76 ILE CG2 C 17.69 0.000 . 598 76 ILE H H 9.05 0.000 . 599 76 ILE HA H 4.49 0.000 . 600 76 ILE HB H 1.61 0.000 . 601 76 ILE HG12 H 1.30 0.000 . 602 76 ILE HG13 H 0.92 0.000 . 603 76 ILE HD1 H 0.66 0.000 . 604 76 ILE HG2 H 0.75 0.000 . 605 76 ILE N N 126.45 0.000 . 606 77 LEU CA C 54.10 0.000 . 607 77 LEU CB C 41.94 0.000 . 608 77 LEU CD1 C 21.30 0.000 . 609 77 LEU CD2 C 25.13 0.000 . 610 77 LEU CG C 26.61 0.000 . 611 77 LEU H H 8.39 0.000 . 612 77 LEU HA H 4.52 0.000 . 613 77 LEU HB2 H 1.59 0.000 . 614 77 LEU HB3 H 1.09 0.000 . 615 77 LEU HG H 1.04 0.000 . 616 77 LEU HD1 H -0.05 0.000 . 617 77 LEU HD2 H 0.57 0.000 . 618 77 LEU N N 127.54 0.000 . 619 78 GLU CA C 55.58 0.000 . 620 78 GLU CB C 32.31 0.000 . 621 78 GLU CG C 36.97 0.000 . 622 78 GLU H H 8.76 0.000 . 623 78 GLU HA H 4.48 0.000 . 624 78 GLU HB2 H 1.76 0.000 . 625 78 GLU HB3 H 1.97 0.000 . 626 78 GLU HG2 H 2.07 0.000 . 627 78 GLU HG3 H 2.14 0.000 . 628 78 GLU N N 127.68 0.000 . 629 79 SER CA C 60.17 0.000 . 630 79 SER CB C 64.83 0.000 . 631 79 SER H H 8.07 0.000 . 632 79 SER N N 123.99 0.000 . stop_ save_