data_4619 #Corrected using PDB structure: 1E0EB # #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 # 16 H HA 1.98 3.54 # 28 I HA 4.70 3.71 # 37 V HA 2.75 3.54 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #0.02 1.93 1.98 N/A -0.99 -0.02 # #bmr4619.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4619.str file): #HA CA CB CO N HN #N/A +1.96 +1.96 N/A -0.99 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.05 +/-0.33 +/-0.26 N/A +/-0.49 +/-0.11 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.681 0.951 0.995 N/A 0.763 0.524 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.150 1.109 0.877 N/A 1.604 0.354 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; N-terminal zinc-binding HHCC domain of HIV-2 integrase ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Eijkelenboom A. P.A.M. . 2 "van den Ent" F. M.I. . 3 Plasterk R. H.A. . 4 Kaptein R. . . 5 Boelens R. . . stop_ _BMRB_accession_number 4619 _BMRB_flat_file_name bmr4619.str _Entry_type new _Submission_date 2000-03-26 _Accession_date 2000-09-07 _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' 346 '13C chemical shifts' 184 '15N chemical shifts' 62 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Solution structure of the N-terminal HHCC domain of HIV-2 integrase: a three-helix bundle stabilized by zinc ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 98035191 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Eijkelenboom A. P.A.M. . 2 "van den Ent" F. M.I. . 3 Vos A. . . 4 Doreleijers J. F. . 5 Hard K. . . 6 Tullius T. D. . 7 Plasterk R. H.A. . 8 Kaptein R. . . 9 Boelens R. . . stop_ _Journal_abbreviation "Curr. Biol." _Journal_volume 7 _Page_first 739 _Page_last 746 _Year 1997 loop_ _Keyword "integrase" "AIDS" "polyprotein" "dimer" "zinc-binding protein" "helix-turn-helix" stop_ save_ ################################## # Molecular system description # ################################## save_HHCC_domain_HIV-2 _Saveframe_category molecular_system _Mol_system_name "Human immunodeficiency virus type 2 integrase" _Abbreviation_common "HHCC domain HIV-2" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "HHCC domain of HIV-2 monomer 1" $HHCC_domain "HHCC domain of HIV-2 monomer 2" $HHCC_domain Zn-1 $ZN_2+ Zn-2 $ZN_2+ stop_ _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all other bound' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 "HHCC domain of HIV-2 monomer 1" 1 "HHCC domain of HIV-2 monomer 2" 2 Zn-1 2 Zn-2 stop_ save_ ######################## # Monomeric polymers # ######################## save_HHCC_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Human immunodeficiency virus type 2 integrase" _Name_variant none _Abbreviation_common . _Mol_thiol_state 'all other bound' ############################## # Polymer residue sequence # ############################## _Residue_count 55 _Mol_residue_sequence ; FLEKIEPAQEEHEKYHSNVK ELSHKFGIPNLVARQIVNSC AQCQQKGEAIHGQVN ; loop_ _Residue_seq_code _Residue_label 1 PHE 2 LEU 3 GLU 4 LYS 5 ILE 6 GLU 7 PRO 8 ALA 9 GLN 10 GLU 11 GLU 12 HIS 13 GLU 14 LYS 15 TYR 16 HIS 17 SER 18 ASN 19 VAL 20 LYS 21 GLU 22 LEU 23 SER 24 HIS 25 LYS 26 PHE 27 GLY 28 ILE 29 PRO 30 ASN 31 LEU 32 VAL 33 ALA 34 ARG 35 GLN 36 ILE 37 VAL 38 ASN 39 SER 40 CYS 41 ALA 42 GLN 43 CYS 44 GLN 45 GLN 46 LYS 47 GLY 48 GLU 49 ALA 50 ILE 51 HIS 52 GLY 53 GLN 54 VAL 55 ASN stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-06-03 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 1E0E "A Chain A, N-Terminal Zinc-Binding HhccDomain Of Hiv-2 Integrase" 100.00 55 100 100 4e-25 EMBL CAA08033.1 "DNA polymerase [Human immunodeficiencyvirus 2]" 42.64 129 100 100 4e-25 EMBL CAA08005.1 "DNA polymerase [Human immunodeficiencyvirus 2]" 41.98 131 98 100 2e-25 EMBL CAA08041.1 "DNA polymerase [Human immunodeficiencyvirus 2]" 41.98 131 98 100 10e-26 GenBank AAB00764.1 "pol polyprotein" 6.28 876 100 100 8e-26 PIR GNLJG2 "HIV-1 retropepsin (EC 3.4.23.16) - humanimmunodeficiency virus type 2 (isolate ROD)" 5.31 1036 100 100 8e-26 PRF 1306388B "gene pol" 5.31 1036 100 100 8e-26 SWISS-PROT P04584 "POL_HV2RO Pol polyprotein [Contains: Protease(Retropepsin) ; Reverse transcriptase ; Ribonuclease H ]" 5.31 1036 100 100 8e-26 stop_ save_ ############# # Ligands # ############# save_ZN_2+ _Saveframe_category ligand _Mol_type non-polymer _Name_common 'ZINC (II) ION' _Abbreviation_common Zn _Name_IUPAC . _BMRB_code ZN_2+ _PDB_code ZN _Mol_empirical_formula Zn1 _Mol_charge 2+ _Mol_paramagnetic no _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN ? 2+ ? ? 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 coordinative Zn-1 . ZN ZN "HHCC domain of HIV-2 monomer 1" 12 HIS NE2 single coordinative Zn-1 . ZN ZN "HHCC domain of HIV-2 monomer 1" 16 HIS ND1 single coordinative Zn-1 . ZN ZN "HHCC domain of HIV-2 monomer 1" 40 CYS SG single coordinative Zn-1 . ZN ZN "HHCC domain of HIV-2 monomer 1" 43 CYS SG single coordinative Zn-2 . ZN ZN "HHCC domain of HIV-2 monomer 2" 12 HIS NE2 single coordinative Zn-2 . ZN ZN "HHCC domain of HIV-2 monomer 2" 16 HIS ND1 single coordinative Zn-2 . ZN ZN "HHCC domain of HIV-2 monomer 2" 40 CYS SG single coordinative Zn-2 . ZN ZN "HHCC domain of HIV-2 monomer 2" 43 CYS 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 _Details $HHCC_domain . 11720 . . . "Human immunodeficiency virus type 2" "isolate ROD" stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Vector_name $HHCC_domain 'recombinant technology' "Escherichia coli" Escherichia coli BL21(DE3) 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 $HHCC_domain 3.5 mM '[U-15N]' $ZN_2+ 1.1 eq . Tris 50 mM '[U-2H]' NaCl 150 mM . 2-mercaptoethanol 2 mM . D2O 99.99 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HHCC_domain 3.5 mM '[U-15N]' $ZN_2+ 1.1 eq . Tris 50 mM '[U-2H]' NaCl 150 mM . 2-mercaptoethanol 2 mM . H2O 95 % . D2O 5 % . stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HHCC_domain 3.5 mM '[U-15N; U-13C]' $ZN_2+ 1.1 eq . Tris 50 mM '[U-2H]' NaCl 150 mM . 2-mercaptoethanol 2 mM . D2O 5 % . stop_ save_ save_sample_4 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HHCC_domain 3.5 mM '[U-15N; U-13C]' $ZN_2+ 1.1 eq . Tris 50 mM '[U-2H]' NaCl 150 mM . 2-mercaptoethanol 2 mM . H2O 95 % . D2O 5 % . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 500 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 600 save_ save_NMR_spectrometer_3 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model 'Unity Plus' _Field_strength 750 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 2D (1H,15N)-HSQC 2D (1H,15N)-HSMQC 2D (1H,1H) NOESY 2D (1H,1H) TOCSY 3D TOCSY (15N,1H) HSQC 3D TOCSY (13C,1H) HSQC 3D NOESY (15N,1H) HSQC 3D NOESY (13C,1H) HSQC 3D (13C) HMQC NOESY (13C,1H) HSQC 2D 13C-filtered NOESY 3D 13C-filtered NOESY (13C,1H) HSQC 3D HNCO 3D HNCA 3D HN(CO)CA 3D HNHA 3D HNHB 3D H(C)CH DIPSI 3D HCC(H) DIPSI ; save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 . n/a temperature 300 . 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 H2O H 1 protons ppm 4.75 internal direct internal . . . DDS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.101329118 DDS N 15 'methyl protons' ppm 0.00 . 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 "HHCC domain of HIV-2 monomer 1" 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 PHE H H 8.30 . . 2 1 PHE HA H 4.58 . . 3 1 PHE HB3 H 3.15 . . 4 1 PHE HB2 H 3.15 . . 5 1 PHE HD1 H 7.24 . . 6 1 PHE HD2 H 7.24 . . 7 1 PHE HE1 H 7.36 . . 8 1 PHE HE2 H 7.36 . . 9 1 PHE N N 119.18 . . 10 1 PHE HZ H 7.32 . . 11 1 PHE CA C 58.67 . . 12 1 PHE CB C 38.99 . . 13 1 PHE CD1 C 131.27 . . 14 1 PHE CD2 C 131.27 . . 15 1 PHE CE1 C 131.36 . . 16 1 PHE CE2 C 131.36 . . 17 2 LEU H H 7.91 . . 18 2 LEU HA H 4.11 . . 19 2 LEU HB3 H 1.70 . . 20 2 LEU HB2 H 1.58 . . 21 2 LEU HG H 1.58 . . 22 2 LEU HD1 H 0.93 . . 23 2 LEU HD2 H 0.87 . . 24 2 LEU N N 121.86 . . 25 2 LEU CA C 56.67 . . 26 2 LEU CB C 41.91 . . 27 2 LEU CD1 C 25.12 . . 28 2 LEU CD2 C 23.67 . . 29 2 LEU CG C 26.96 . . 30 3 GLU H H 8.48 . . 31 3 GLU HA H 4.21 . . 32 3 GLU HB3 H 2.05 . . 33 3 GLU HB2 H 2.05 . . 34 3 GLU HG3 H 2.35 . . 35 3 GLU HG2 H 2.29 . . 36 3 GLU N N 118.01 . . 37 3 GLU CA C 57.64 . . 38 3 GLU CB C 29.72 . . 39 3 GLU CG C 36.40 . . 40 4 LYS N N 117.90 . . 41 4 LYS H H 8.06 . . 42 4 LYS HA H 4.43 . . 43 4 LYS HE3 H 3.09 . . 44 4 LYS HE2 H 3.09 . . 45 4 LYS HB3 H 2.02 . . 46 4 LYS HB2 H 1.93 . . 47 4 LYS HD3 H 1.84 . . 48 4 LYS HD2 H 1.80 . . 49 4 LYS HG3 H 1.63 . . 50 4 LYS HG2 H 1.50 . . 51 4 LYS CA C 56.27 . . 52 4 LYS CG C 25.18 . . 53 4 LYS CE C 42.34 . . 54 4 LYS CD C 28.92 . . 55 4 LYS CB C 33.31 . . 56 5 ILE H H 7.65 . . 57 5 ILE HA H 3.69 . . 58 5 ILE HB H 1.83 . . 59 5 ILE HG13 H 1.64 . . 60 5 ILE HG12 H 1.04 . . 61 5 ILE HG2 H 0.81 . . 62 5 ILE HD1 H 0.87 . . 63 5 ILE N N 119.01 . . 64 5 ILE CA C 64.16 . . 65 5 ILE CB C 37.93 . . 66 5 ILE CG1 C 28.67 . . 67 5 ILE CG2 C 17.52 . . 68 5 ILE CD1 C 13.54 . . 69 6 GLU H H 8.61 . . 70 6 GLU HA H 4.24 . . 71 6 GLU HB3 H 2.03 . . 72 6 GLU HB2 H 1.94 . . 73 6 GLU HG3 H 2.29 . . 74 6 GLU HG2 H 2.22 . . 75 6 GLU N N 121.13 . . 76 6 GLU CA C 60.41 . . 77 6 GLU CB C 26.80 . . 78 6 GLU CG C 36.26 . . 79 7 PRO HA H 4.24 . . 80 7 PRO HB3 H 2.32 . . 81 7 PRO HB2 H 1.70 . . 82 7 PRO HG3 H 2.08 . . 83 7 PRO HG2 H 2.02 . . 84 7 PRO HD3 H 3.61 . . 85 7 PRO HD2 H 3.49 . . 86 7 PRO CD C 49.82 . . 87 7 PRO CA C 65.56 . . 88 7 PRO CB C 30.78 . . 89 7 PRO CG C 27.86 . . 90 8 ALA H H 7.21 . . 91 8 ALA HA H 3.12 . . 92 8 ALA HB H 1.02 . . 93 8 ALA N N 121.51 . . 94 8 ALA CB C 18.80 . . 95 8 ALA CA C 54.17 . . 96 9 GLN H H 8.28 . . 97 9 GLN HA H 3.81 . . 98 9 GLN HB3 H 2.24 . . 99 9 GLN HB2 H 2.14 . . 100 9 GLN HG3 H 2.35 . . 101 9 GLN HG2 H 2.29 . . 102 9 GLN HE21 H 7.53 . . 103 9 GLN HE22 H 6.80 . . 104 9 GLN N N 119.37 . . 105 9 GLN CA C 59.22 . . 106 9 GLN CB C 28.17 . . 107 9 GLN CG C 33.98 . . 108 9 GLN NE2 N 112.22 . . 109 10 GLU H H 8.12 . . 110 10 GLU HA H 3.94 . . 111 10 GLU HB3 H 2.02 . . 112 10 GLU HB2 H 2.02 . . 113 10 GLU HG3 H 2.36 . . 114 10 GLU HG2 H 2.18 . . 115 10 GLU N N 119.97 . . 116 10 GLU CA C 59.08 . . 117 10 GLU CB C 29.20 . . 118 10 GLU CG C 36.18 . . 119 11 GLU H H 8.00 . . 120 11 GLU HA H 4.17 . . 121 11 GLU HB3 H 2.13 . . 122 11 GLU HB2 H 2.45 . . 123 11 GLU HG3 H 2.55 . . 124 11 GLU HG2 H 2.55 . . 125 11 GLU N N 120.07 . . 126 11 GLU CA C 59.21 . . 127 11 GLU CB C 28.83 . . 128 11 GLU CG C 34.58 . . 129 12 HIS H H 8.43 . . 130 12 HIS HA H 3.59 . . 131 12 HIS HB3 H 3.26 . . 132 12 HIS HB2 H 2.97 . . 133 12 HIS HD1 H 12.63 . . 134 12 HIS HE1 H 8.12 . . 135 12 HIS HD2 H 6.91 . . 136 12 HIS N N 117.82 . . 137 12 HIS CA C 60.92 . . 138 12 HIS CB C 28.47 . . 139 12 HIS CD2 C 140.81 . . 140 13 GLU H H 8.30 . . 141 13 GLU HA H 3.67 . . 142 13 GLU HB3 H 2.09 . . 143 13 GLU HB2 H 2.00 . . 144 13 GLU HG3 H 2.42 . . 145 13 GLU HG2 H 2.30 . . 146 13 GLU N N 118.31 . . 147 13 GLU CA C 58.92 . . 148 13 GLU CB C 29.06 . . 149 13 GLU CG C 36.24 . . 150 14 LYS H H 7.15 . . 151 14 LYS HA H 3.90 . . 152 14 LYS HB3 H 1.20 . . 153 14 LYS HG3 H 1.20 . . 154 14 LYS HB2 H 0.79 . . 155 14 LYS HG2 H 0.79 . . 156 14 LYS HD3 H 1.43 . . 157 14 LYS HD2 H 1.43 . . 158 14 LYS HE3 H 2.81 . . 159 14 LYS HE2 H 2.81 . . 160 14 LYS N N 114.02 . . 161 14 LYS CA C 58.35 . . 162 14 LYS CB C 33.32 . . 163 14 LYS CG C 25.22 . . 164 14 LYS CD C 29.13 . . 165 14 LYS CE C 41.73 . . 166 15 TYR H H 7.92 . . 167 15 TYR HA H 4.83 . . 168 15 TYR HB3 H 3.33 . . 169 15 TYR HB2 H 2.64 . . 170 15 TYR HD1 H 7.15 . . 171 15 TYR HD2 H 7.15 . . 172 15 TYR HE1 H 6.82 . . 173 15 TYR HE2 H 6.82 . . 174 15 TYR N N 114.38 . . 175 15 TYR CA C 57.12 . . 176 15 TYR CB C 40.26 . . 177 15 TYR CD1 C 132.99 . . 178 15 TYR CD2 C 132.99 . . 179 15 TYR CE1 C 117.45 . . 180 15 TYR CE2 C 117.45 . . 181 16 HIS H H 8.62 . . 182 16 HIS HB2 H 2.96 . . 183 16 HIS HB3 H 2.82 . . 184 16 HIS HA H 1.95 . . 185 16 HIS HD2 H 6.75 . . 186 16 HIS HE1 H 7.86 . . 187 16 HIS N N 116.97 . . 188 16 HIS CA C 56.55 . . 189 16 HIS CB C 26.92 . . 190 16 HIS CD2 C 138.82 . . 191 17 SER H H 6.66 . . 192 17 SER HA H 4.39 . . 193 17 SER HB3 H 4.06 . . 194 17 SER HB2 H 3.46 . . 195 17 SER N N 110.20 . . 196 17 SER CA C 58.54 . . 197 17 SER CB C 63.17 . . 198 18 ASN H H 8.92 . . 199 18 ASN HA H 4.67 . . 200 18 ASN HB3 H 3.61 . . 201 18 ASN HB2 H 3.12 . . 202 18 ASN HD21 H 7.59 . . 203 18 ASN HD22 H 6.86 . . 204 18 ASN N N 122.77 . . 205 18 ASN CA C 52.18 . . 206 18 ASN CB C 38.58 . . 207 18 ASN ND2 N 112.11 . . 208 19 VAL H H 8.24 . . 209 19 VAL HA H 3.37 . . 210 19 VAL HB H 2.07 . . 211 19 VAL HG1 H 0.94 . . 212 19 VAL HG2 H 1.02 . . 213 19 VAL N N 115.47 . . 214 19 VAL CB C 32.01 . . 215 19 VAL CG1 C 21.36 . . 216 19 VAL CG2 C 23.61 . . 217 19 VAL CA C 67.23 . . 218 20 LYS H H 8.04 . . 219 20 LYS HA H 3.97 . . 220 20 LYS HB3 H 1.89 . . 221 20 LYS HB2 H 1.83 . . 222 20 LYS HG3 H 1.49 . . 223 20 LYS HG2 H 1.36 . . 224 20 LYS HD3 H 1.69 . . 225 20 LYS HD2 H 1.69 . . 226 20 LYS HE3 H 2.97 . . 227 20 LYS HE2 H 2.97 . . 228 20 LYS N N 120.03 . . 229 20 LYS CA C 59.51 . . 230 20 LYS CB C 32.02 . . 231 20 LYS CG C 25.21 . . 232 20 LYS CD C 29.00 . . 233 20 LYS CE C 41.75 . . 234 21 GLU H H 8.47 . . 235 21 GLU HA H 4.13 . . 236 21 GLU HB3 H 2.22 . . 237 21 GLU HB2 H 2.02 . . 238 21 GLU HG3 H 2.48 . . 239 21 GLU HG2 H 2.31 . . 240 21 GLU N N 119.86 . . 241 21 GLU CA C 59.17 . . 242 21 GLU CB C 29.76 . . 243 21 GLU CG C 36.65 . . 244 22 LEU H H 8.81 . . 245 22 LEU HA H 4.34 . . 246 22 LEU HB3 H 1.31 . . 247 22 LEU HB2 H 2.10 . . 248 22 LEU HG H 2.00 . . 249 22 LEU HD1 H 1.10 . . 250 22 LEU HD2 H 0.86 . . 251 22 LEU N N 118.63 . . 252 22 LEU CA C 57.90 . . 253 22 LEU CB C 43.69 . . 254 22 LEU CG C 26.16 . . 255 22 LEU CD1 C 24.43 . . 256 22 LEU CD2 C 27.10 . . 257 23 SER H H 8.48 . . 258 23 SER HA H 4.29 . . 259 23 SER HB3 H 3.94 . . 260 23 SER HB2 H 3.94 . . 261 23 SER N N 114.10 . . 262 23 SER CA C 62.36 . . 263 23 SER CB C 63.06 . . 264 24 HIS H H 8.22 . . 265 24 HIS HA H 4.38 . . 266 24 HIS HB3 H 3.29 . . 267 24 HIS HB2 H 3.19 . . 268 24 HIS HD2 H 7.09 . . 269 24 HIS HE1 H 8.07 . . 270 24 HIS N N 119.33 . . 271 24 HIS CA C 58.72 . . 272 24 HIS CB C 29.67 . . 273 24 HIS CD2 C 136.49 . . 274 25 LYS H H 8.39 . . 275 25 LYS HA H 3.73 . . 276 25 LYS HB3 H 1.69 . . 277 25 LYS HB2 H 1.32 . . 278 25 LYS HG3 H 0.98 . . 279 25 LYS HG2 H 0.08 . . 280 25 LYS HD3 H 1.40 . . 281 25 LYS HD2 H 1.40 . . 282 25 LYS HE3 H 2.71 . . 283 25 LYS HE2 H 2.71 . . 284 25 LYS N N 118.03 . . 285 25 LYS CA C 59.26 . . 286 25 LYS CB C 33.02 . . 287 25 LYS CG C 25.24 . . 288 25 LYS CD C 29.44 . . 289 25 LYS CE C 41.55 . . 290 26 PHE H H 7.81 . . 291 26 PHE HA H 4.62 . . 292 26 PHE HB3 H 3.49 . . 293 26 PHE HB2 H 2.82 . . 294 26 PHE HD1 H 7.55 . . 295 26 PHE HD2 H 7.55 . . 296 26 PHE HE1 H 7.29 . . 297 26 PHE HE2 H 7.29 . . 298 26 PHE HZ H 7.22 . . 299 26 PHE N N 111.13 . . 300 26 PHE CA C 58.45 . . 301 26 PHE CB C 40.10 . . 302 26 PHE CD1 C 131.25 . . 303 26 PHE CD2 C 131.25 . . 304 27 GLY H H 7.71 . . 305 27 GLY HA3 H 4.00 . . 306 27 GLY HA2 H 3.92 . . 307 27 GLY N N 109.42 . . 308 27 GLY CA C 46.99 . . 309 28 ILE H H 6.80 . . 310 28 ILE HA H 4.68 . . 311 28 ILE HB H 1.64 . . 312 28 ILE HG13 H 1.43 . . 313 28 ILE HG12 H 0.96 . . 314 28 ILE HG2 H 0.88 . . 315 28 ILE HD1 H 0.62 . . 316 28 ILE N N 109.21 . . 317 28 ILE CB C 37.97 . . 318 28 ILE CG1 C 25.13 . . 319 28 ILE CG2 C 18.58 . . 320 28 ILE CD1 C 14.12 . . 321 28 ILE CA C 57.43 . . 322 29 PRO HA H 4.48 . . 323 29 PRO HB3 H 2.57 . . 324 29 PRO HB2 H 1.76 . . 325 29 PRO HG3 H 2.02 . . 326 29 PRO HG2 H 1.94 . . 327 29 PRO HD3 H 3.70 . . 328 29 PRO HD2 H 3.10 . . 329 29 PRO CA C 62.24 . . 330 29 PRO CB C 32.69 . . 331 29 PRO CG C 27.75 . . 332 29 PRO CD C 50.50 . . 333 30 ASN HA H 4.17 . . 334 30 ASN HB3 H 2.87 . . 335 30 ASN HB2 H 2.65 . . 336 30 ASN HD21 H 7.73 . . 337 30 ASN HD22 H 7.10 . . 338 30 ASN CA C 57.33 . . 339 30 ASN CB C 38.65 . . 340 30 ASN ND2 N 112.94 . . 341 31 LEU H H 8.76 . . 342 31 LEU HA H 3.98 . . 343 31 LEU HB3 H 1.74 . . 344 31 LEU HB2 H 1.51 . . 345 31 LEU HG H 1.65 . . 346 31 LEU HD1 H 0.92 . . 347 31 LEU HD2 H 0.88 . . 348 31 LEU N N 116.98 . . 349 31 LEU CB C 42.19 . . 350 31 LEU CA C 58.42 . . 351 31 LEU CD2 C 24.63 . . 352 31 LEU CD1 C 24.68 . . 353 31 LEU CG C 27.06 . . 354 32 VAL H H 6.79 . . 355 32 VAL HA H 3.71 . . 356 32 VAL HB H 1.94 . . 357 32 VAL HG1 H 0.91 . . 358 32 VAL HG2 H 0.97 . . 359 32 VAL N N 118.05 . . 360 32 VAL CA C 64.92 . . 361 32 VAL CB C 31.92 . . 362 32 VAL CG1 C 21.74 . . 363 32 VAL CG2 C 22.64 . . 364 33 ALA H H 7.82 . . 365 33 ALA HA H 3.81 . . 366 33 ALA HB H 1.52 . . 367 33 ALA N N 121.94 . . 368 33 ALA CB C 19.87 . . 369 33 ALA CA C 55.33 . . 370 34 ARG H H 8.80 . . 371 34 ARG HA H 3.77 . . 372 34 ARG HB3 H 1.89 . . 373 34 ARG HB2 H 1.85 . . 374 34 ARG HG3 H 1.72 . . 375 34 ARG HG2 H 1.68 . . 376 34 ARG HD3 H 3.20 . . 377 34 ARG HD2 H 3.16 . . 378 34 ARG N N 116.73 . . 379 34 ARG CA C 59.12 . . 380 34 ARG CB C 29.76 . . 381 34 ARG CG C 27.59 . . 382 34 ARG CD C 43.35 . . 383 35 GLN H H 7.45 . . 384 35 GLN HA H 4.00 . . 385 35 GLN HB3 H 2.27 . . 386 35 GLN HB2 H 2.15 . . 387 35 GLN HG3 H 2.48 . . 388 35 GLN HG2 H 2.40 . . 389 35 GLN HE21 H 7.33 . . 390 35 GLN HE22 H 6.78 . . 391 35 GLN N N 118.72 . . 392 35 GLN CA C 58.58 . . 393 35 GLN CB C 27.78 . . 394 35 GLN CG C 33.57 . . 395 35 GLN NE2 N 111.93 . . 396 36 ILE H H 7.55 . . 397 36 ILE HA H 3.53 . . 398 36 ILE HB H 1.85 . . 399 36 ILE HG13 H 1.83 . . 400 36 ILE HG12 H 0.92 . . 401 36 ILE HG2 H 0.59 . . 402 36 ILE HD1 H 0.63 . . 403 36 ILE N N 120.18 . . 404 36 ILE CA C 65.07 . . 405 36 ILE CB C 37.89 . . 406 36 ILE CG1 C 28.36 . . 407 36 ILE CG2 C 16.74 . . 408 36 ILE CD1 C 14.68 . . 409 37 VAL H H 7.60 . . 410 37 VAL HA H 2.73 . . 411 37 VAL HB H 1.83 . . 412 37 VAL HG1 H 0.97 . . 413 37 VAL HG2 H 0.93 . . 414 37 VAL N N 119.85 . . 415 37 VAL CA C 66.81 . . 416 37 VAL CB C 31.40 . . 417 37 VAL CG1 C 21.57 . . 418 37 VAL CG2 C 23.27 . . 419 38 ASN H H 8.63 . . 420 38 ASN HA H 4.44 . . 421 38 ASN HB3 H 2.82 . . 422 38 ASN HB2 H 2.76 . . 423 38 ASN HD21 H 7.47 . . 424 38 ASN HD22 H 6.79 . . 425 38 ASN N N 115.65 . . 426 38 ASN CA C 54.50 . . 427 38 ASN CB C 37.81 . . 428 38 ASN ND2 N 111.15 . . 429 39 SER H H 7.34 . . 430 39 SER HA H 4.37 . . 431 39 SER HB3 H 3.98 . . 432 39 SER HB2 H 3.98 . . 433 39 SER N N 112.96 . . 434 39 SER CA C 58.77 . . 435 39 SER CB C 63.56 . . 436 40 CYS H H 7.39 . . 437 40 CYS HA H 4.47 . . 438 40 CYS HB3 H 3.54 . . 439 40 CYS HB2 H 2.87 . . 440 40 CYS N N 124.94 . . 441 40 CYS CA C 58.17 . . 442 40 CYS CB C 28.85 . . 443 41 ALA H H 9.14 . . 444 41 ALA HA H 4.10 . . 445 41 ALA HB H 1.52 . . 446 41 ALA N N 133.19 . . 447 41 ALA CB C 18.51 . . 448 41 ALA CA C 55.10 . . 449 42 GLN H H 8.42 . . 450 42 GLN HA H 4.17 . . 451 42 GLN HB3 H 2.06 . . 452 42 GLN HB2 H 1.88 . . 453 42 GLN HG3 H 2.27 . . 454 42 GLN HG2 H 2.19 . . 455 42 GLN HE21 H 7.37 . . 456 42 GLN HE22 H 6.62 . . 457 42 GLN N N 118.40 . . 458 42 GLN CA C 58.88 . . 459 42 GLN CB C 29.77 . . 460 42 GLN CG C 34.19 . . 461 42 GLN NE2 N 112.82 . . 462 43 CYS H H 8.56 . . 463 43 CYS HA H 4.22 . . 464 43 CYS HB3 H 3.11 . . 465 43 CYS HB2 H 3.09 . . 466 43 CYS N N 121.16 . . 467 43 CYS CA C 64.02 . . 468 43 CYS CB C 29.25 . . 469 44 GLN H H 8.13 . . 470 44 GLN HA H 4.18 . . 471 44 GLN HB3 H 2.15 . . 472 44 GLN HB2 H 2.14 . . 473 44 GLN HG3 H 2.48 . . 474 44 GLN HG2 H 2.44 . . 475 44 GLN HE21 H 7.32 . . 476 44 GLN HE22 H 6.82 . . 477 44 GLN N N 118.86 . . 478 44 GLN CA C 57.00 . . 479 44 GLN CB C 28.57 . . 480 44 GLN CG C 33.60 . . 481 44 GLN NE2 N 113.23 . . 482 45 GLN H H 7.89 . . 483 45 GLN HA H 4.25 . . 484 45 GLN HB3 H 2.17 . . 485 45 GLN HB2 H 2.09 . . 486 45 GLN HG3 H 2.49 . . 487 45 GLN HG2 H 2.43 . . 488 45 GLN HE21 H 7.52 . . 489 45 GLN HE22 H 6.83 . . 490 45 GLN N N 118.66 . . 491 45 GLN CA C 56.45 . . 492 45 GLN CB C 28.76 . . 493 45 GLN CG C 33.81 . . 494 45 GLN NE2 N 113.05 . . 495 46 LYS H H 8.04 . . 496 46 LYS HA H 4.30 . . 497 46 LYS HB3 H 1.92 . . 498 46 LYS HB2 H 1.85 . . 499 46 LYS HG3 H 1.54 . . 500 46 LYS HG2 H 1.46 . . 501 46 LYS HD3 H 1.71 . . 502 46 LYS HD2 H 1.71 . . 503 46 LYS HE3 H 3.02 . . 504 46 LYS HE2 H 3.02 . . 505 46 LYS N N 120.60 . . 506 46 LYS CA C 56.66 . . 507 46 LYS CB C 32.87 . . 508 46 LYS CG C 24.98 . . 509 46 LYS CD C 28.96 . . 510 46 LYS CE C 41.86 . . 511 47 GLY H H 8.20 . . 512 47 GLY HA3 H 3.98 . . 513 47 GLY HA2 H 3.98 . . 514 47 GLY N N 108.80 . . 515 47 GLY CA C 45.26 . . 516 48 GLU H H 8.22 . . 517 48 GLU HA H 4.28 . . 518 48 GLU HB3 H 2.06 . . 519 48 GLU HB2 H 1.95 . . 520 48 GLU HG3 H 2.31 . . 521 48 GLU HG2 H 2.28 . . 522 48 GLU N N 120.45 . . 523 48 GLU CA C 56.35 . . 524 48 GLU CG C 36.09 . . 525 48 GLU CB C 30.27 . . 526 49 ALA H H 8.26 . . 527 49 ALA HA H 4.31 . . 528 49 ALA HB H 1.37 . . 529 49 ALA N N 124.66 . . 530 49 ALA CB C 19.11 . . 531 49 ALA CA C 52.37 . . 532 50 ILE H H 7.96 . . 533 50 ILE HA H 4.09 . . 534 50 ILE HB H 1.80 . . 535 50 ILE HG13 H 1.37 . . 536 50 ILE HG12 H 1.13 . . 537 50 ILE HG2 H 0.81 . . 538 50 ILE HD1 H 0.81 . . 539 50 ILE N N 119.18 . . 540 50 ILE CB C 38.48 . . 541 50 ILE CA C 61.03 . . 542 50 ILE CG1 C 27.15 . . 543 50 ILE CG2 C 17.50 . . 544 50 ILE CD1 C 12.95 . . 545 51 HIS H H 8.35 . . 546 51 HIS HA H 4.71 . . 547 51 HIS HB3 H 3.23 . . 548 51 HIS HB2 H 3.14 . . 549 51 HIS HD2 H 7.17 . . 550 51 HIS HE1 H 8.19 . . 551 51 HIS N N 122.40 . . 552 51 HIS CA C 55.43 . . 553 51 HIS CB C 29.58 . . 554 51 HIS CD2 C 136.83 . . 555 52 GLY HA3 H 3.96 . . 556 52 GLY HA2 H 3.96 . . 557 52 GLY CA C 45.05 . . 558 52 GLY H H 8.34 . . 559 52 GLY N N 109.97 . . 560 53 GLN H H 8.25 . . 561 53 GLN HA H 4.39 . . 562 53 GLN HB3 H 2.11 . . 563 53 GLN HB2 H 2.00 . . 564 53 GLN HG3 H 2.36 . . 565 53 GLN HG2 H 2.33 . . 566 53 GLN HE21 H 7.58 . . 567 53 GLN HE22 H 6.85 . . 568 53 GLN N N 120.19 . . 569 53 GLN CA C 55.62 . . 570 53 GLN CB C 29.53 . . 571 53 GLN CG C 33.66 . . 572 53 GLN NE2 N 113.59 . . 573 54 VAL H H 8.25 . . 574 54 VAL HA H 4.17 . . 575 54 VAL HB H 2.10 . . 576 54 VAL HG1 H 0.93 . . 577 54 VAL HG2 H 0.91 . . 578 54 VAL N N 121.52 . . 579 54 VAL CA C 62.07 . . 580 54 VAL CB C 32.77 . . 581 54 VAL CG1 C 21.34 . . 582 54 VAL CG2 C 20.32 . . 583 55 ASN H H 8.07 . . 584 55 ASN HA H 4.49 . . 585 55 ASN HB3 H 2.77 . . 586 55 ASN HB2 H 2.67 . . 587 55 ASN HD21 H 7.50 . . 588 55 ASN HD22 H 6.80 . . 589 55 ASN N N 127.52 . . 590 55 ASN CA C 54.62 . . 591 55 ASN CB C 40.39 . . 592 55 ASN ND2 N 113.75 . . stop_ save_