data_5383 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The CXCR3 binding chemokine IP-10/CXCL10: Structure and receptor interactions ; _BMRB_accession_number 5383 _BMRB_flat_file_name bmr5383.str _Entry_type original _Submission_date 2002-06-04 _Accession_date 2002-06-04 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Booth Valerie . . 2 Keizer David W. . 3 Kamphuis Monique B. . 4 Clark-Lewis Ian . . 5 Sykes Brian D. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 304 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2008-08-12 update BMRB 'Updating non-standard residue' 2008-07-17 update BMRB 'Updating non-standard residue' 2003-01-06 original author . stop_ _Original_release_date 2002-06-04 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The CXCR3 Binding Chemokine IP-10/CXCL10: Structure and Receptor Interactions ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22163955 _PubMed_ID 12173928 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Booth Valerie . . 2 Keizer David W. . 3 Kamphuis Monique B. . 4 Clark-Lewis Ian . . 5 Sykes Brian D. . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue 33 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10418 _Page_last 10425 _Year 2002 _Details . loop_ _Keyword 'chemical shift mapping' chemokine stop_ save_ ################################## # Molecular system description # ################################## save_CXCL10 _Saveframe_category molecular_system _Mol_system_name IP-10 _Abbreviation_common CXCL10 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label IP-10 $IP-10 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_IP-10 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common IP-10 _Name_variant CXCL10 _Abbreviation_common IP-10 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details 'Mutant: NMeLeu 27' ############################## # Polymer residue sequence # ############################## _Residue_count 77 _Mol_residue_sequence ; VPLSRTVRCTCISISNQPVN PRSLEKXEIIPASQFCPRVE IIATMKKKGEKRCLNPESKA IKNLLKAVSKEMSKRSP ; loop_ _Residue_seq_code _Residue_label 1 VAL 2 PRO 3 LEU 4 SER 5 ARG 6 THR 7 VAL 8 ARG 9 CYS 10 THR 11 CYS 12 ILE 13 SER 14 ILE 15 SER 16 ASN 17 GLN 18 PRO 19 VAL 20 ASN 21 PRO 22 ARG 23 SER 24 LEU 25 GLU 26 LYS 27 MLE 28 GLU 29 ILE 30 ILE 31 PRO 32 ALA 33 SER 34 GLN 35 PHE 36 CYS 37 PRO 38 ARG 39 VAL 40 GLU 41 ILE 42 ILE 43 ALA 44 THR 45 MET 46 LYS 47 LYS 48 LYS 49 GLY 50 GLU 51 LYS 52 ARG 53 CYS 54 LEU 55 ASN 56 PRO 57 GLU 58 SER 59 LYS 60 ALA 61 ILE 62 LYS 63 ASN 64 LEU 65 LEU 66 LYS 67 ALA 68 VAL 69 SER 70 LYS 71 GLU 72 MET 73 SER 74 LYS 75 ARG 76 SER 77 PRO stop_ _Sequence_homology_query_date 2008-03-24 _Sequence_homology_query_revised_last_date 2007-08-23 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 1LV9 'A Chain A, Cxcr3 Binding ChemokineIp-10CXCL10' 100.00 77 100 100 4e-36 PDB 1O7Y 'A Chain A, Crystal Structure Of Ip-10 M-Form' 100.00 77 99 99 4e-36 PDB 1O7Z 'A Chain A, Crystal Structure Of Ip-10 T-Form' 100.00 77 99 99 4e-36 PDB 1O80 'A Chain A, Crystal Structure Of Ip-10 H-Form' 100.00 77 99 99 4e-36 EMBL CAA26370.1 'gamma-interferon inducible earlyresponse polypeptide precursor [Homo sapiens]' 78.57 98 99 99 4e-36 PRF 1107274A 'interferon gamma' 78.57 98 99 99 4e-36 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_MLE _Saveframe_category polymer_residue _Mol_type 'L-peptide linking' _Name_common N-METHYLLEUCINE _BMRB_code . _PDB_code MLE _Standard_residue_derivative . _Molecular_mass 145.199 _Mol_paramagnetic . _Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Jul 25 15:09:59 2011 ; loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CN CN C . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? CD1 CD1 C . 0 . ? CD2 CD2 C . 0 . ? C C C . 0 . ? O O O . 0 . ? OXT OXT O . 0 . ? H H H . 0 . ? HN1 HN1 H . 0 . ? HN2 HN2 H . 0 . ? HN3 HN3 H . 0 . ? HA HA H . 0 . ? HB2 HB2 H . 0 . ? HB3 HB3 H . 0 . ? HG HG H . 0 . ? HD11 HD11 H . 0 . ? HD12 HD12 H . 0 . ? HD13 HD13 H . 0 . ? HD21 HD21 H . 0 . ? HD22 HD22 H . 0 . ? HD23 HD23 H . 0 . ? HXT HXT H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CN ? ? SING N CA ? ? SING N H ? ? SING CN HN1 ? ? SING CN HN2 ? ? SING CN HN3 ? ? SING CA CB ? ? SING CA C ? ? SING CA HA ? ? SING CB CG ? ? SING CB HB2 ? ? SING CB HB3 ? ? SING CG CD1 ? ? SING CG CD2 ? ? SING CG HG ? ? SING CD1 HD11 ? ? SING CD1 HD12 ? ? SING CD1 HD13 ? ? SING CD2 HD21 ? ? SING CD2 HD22 ? ? SING CD2 HD23 ? ? DOUB C O ? ? SING C OXT ? ? SING OXT HXT ? ? stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $IP-10 . . . . . . 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 $IP-10 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $IP-10 2 mM . stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.0 0.1 n/a temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . 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 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 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) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_IP-10_cs _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H NOESY' '2D 1H-1H TOCSY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name IP-10 _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 7 VAL H H 8.050 0.02 . 2 . 7 VAL HA H 4.260 0.02 . 3 . 7 VAL HB H 2.080 0.02 . 4 . 7 VAL HG2 H 0.920 0.02 . 5 . 7 VAL HG1 H 0.950 0.02 . 6 . 8 ARG H H 8.580 0.02 . 7 . 8 ARG HA H 4.680 0.02 . 8 . 8 ARG HB2 H 1.990 0.02 . 9 . 8 ARG HB3 H 1.990 0.02 . 10 . 8 ARG HG3 H 1.690 0.02 . 11 . 8 ARG HG2 H 1.560 0.02 . 12 . 9 CYS H H 8.050 0.02 . 13 . 9 CYS HA H 4.720 0.02 . 14 . 9 CYS HB3 H 3.810 0.02 . 15 . 9 CYS HB2 H 2.700 0.02 . 16 . 10 THR H H 10.470 0.02 . 17 . 10 THR HA H 4.250 0.02 . 18 . 10 THR HB H 4.140 0.02 . 19 . 10 THR HG2 H 1.180 0.02 . 20 . 11 CYS H H 9.360 0.02 . 21 . 11 CYS HA H 4.570 0.02 . 22 . 11 CYS HB3 H 2.760 0.02 . 23 . 11 CYS HB2 H 3.280 0.02 . 24 . 12 ILE H H 8.680 0.02 . 25 . 12 ILE HA H 4.110 0.02 . 26 . 12 ILE HB H 1.940 0.02 . 27 . 12 ILE HG12 H 1.250 0.02 . 28 . 12 ILE HG13 H 1.250 0.02 . 29 . 13 SER H H 7.800 0.02 . 30 . 13 SER HA H 4.620 0.02 . 31 . 13 SER HB2 H 3.800 0.02 . 32 . 13 SER HB3 H 3.800 0.02 . 33 . 14 ILE H H 8.500 0.02 . 34 . 14 ILE HA H 4.230 0.02 . 35 . 14 ILE HB H 1.720 0.02 . 36 . 14 ILE HG2 H 0.760 0.02 . 37 . 15 SER H H 8.710 0.02 . 38 . 15 SER HA H 4.640 0.02 . 39 . 15 SER HB3 H 4.000 0.02 . 40 . 15 SER HB2 H 3.840 0.02 . 41 . 16 ASN H H 8.960 0.02 . 42 . 16 ASN HA H 4.970 0.02 . 43 . 16 ASN HB3 H 3.010 0.02 . 44 . 16 ASN HB2 H 2.790 0.02 . 45 . 17 GLN H H 7.930 0.02 . 46 . 17 GLN HA H 4.590 0.02 . 47 . 17 GLN HB3 H 2.070 0.02 . 48 . 17 GLN HB2 H 1.870 0.02 . 49 . 17 GLN HG2 H 2.430 0.02 . 50 . 17 GLN HG3 H 2.430 0.02 . 51 . 18 PRO HA H 4.320 0.02 . 52 . 18 PRO HB3 H 2.050 0.02 . 53 . 18 PRO HB2 H 2.200 0.02 . 54 . 18 PRO HG3 H 1.900 0.02 . 55 . 18 PRO HG2 H 1.990 0.02 . 56 . 18 PRO HD3 H 3.680 0.02 . 57 . 18 PRO HD2 H 3.830 0.02 . 58 . 19 VAL H H 7.550 0.02 . 59 . 19 VAL HA H 4.250 0.02 . 60 . 19 VAL HB H 1.870 0.02 . 61 . 19 VAL HG1 H 0.760 0.02 . 62 . 19 VAL HG2 H 0.760 0.02 . 63 . 20 ASN H H 8.550 0.02 . 64 . 20 ASN HA H 4.920 0.02 . 65 . 20 ASN HB3 H 2.810 0.02 . 66 . 20 ASN HB2 H 2.920 0.02 . 67 . 20 ASN HD21 H 7.550 0.02 . 68 . 20 ASN HD22 H 6.950 0.02 . 69 . 21 PRO HB2 H 2.140 0.02 . 70 . 21 PRO HB3 H 2.140 0.02 . 71 . 21 PRO HG2 H 1.930 0.02 . 72 . 21 PRO HG3 H 1.930 0.02 . 73 . 21 PRO HD3 H 4.000 0.02 . 74 . 21 PRO HD2 H 3.880 0.02 . 75 . 23 SER H H 8.090 0.02 . 76 . 23 SER HA H 4.530 0.02 . 77 . 23 SER HB2 H 3.990 0.02 . 78 . 23 SER HB3 H 3.990 0.02 . 79 . 24 LEU H H 7.270 0.02 . 80 . 24 LEU HA H 4.420 0.02 . 81 . 24 LEU HB2 H 1.680 0.02 . 82 . 24 LEU HB3 H 1.680 0.02 . 83 . 24 LEU HD1 H 1.400 0.02 . 84 . 24 LEU HD2 H 1.400 0.02 . 85 . 25 GLU H H 9.400 0.02 . 86 . 25 GLU HA H 4.470 0.02 . 87 . 25 GLU HB2 H 1.700 0.02 . 88 . 25 GLU HB3 H 1.700 0.02 . 89 . 25 GLU HG2 H 2.190 0.02 . 90 . 25 GLU HG3 H 2.190 0.02 . 91 . 26 LYS H H 7.770 0.02 . 92 . 26 LYS HA H 5.130 0.02 . 93 . 26 LYS HB3 H 1.890 0.02 . 94 . 26 LYS HB2 H 1.780 0.02 . 95 . 26 LYS HG2 H 1.390 0.02 . 96 . 26 LYS HG3 H 1.390 0.02 . 97 . 27 MLE HA H 5.400 0.02 . 98 . 27 MLE HB3 H 1.890 0.02 . 99 . 27 MLE HB2 H 1.230 0.02 . 100 . 27 MLE HG H 1.310 0.02 . 101 . 27 MLE HD11 H 0.760 0.02 . 102 . 27 MLE HD12 H 0.760 0.02 . 103 . 27 MLE HD13 H 0.760 0.02 . 104 . 27 MLE HD21 H 0.760 0.02 . 105 . 27 MLE HD22 H 0.760 0.02 . 106 . 27 MLE HD23 H 0.760 0.02 . 107 . 27 MLE HN1 H 3.130 0.02 . 108 . 27 MLE HN2 H 3.130 0.02 . 109 . 27 MLE HN3 H 3.130 0.02 . 110 . 28 GLU H H 8.490 0.02 . 111 . 28 GLU HA H 4.460 0.02 . 112 . 28 GLU HB3 H 2.020 0.02 . 113 . 28 GLU HB2 H 1.970 0.02 . 114 . 28 GLU HG3 H 2.150 0.02 . 115 . 28 GLU HG2 H 2.250 0.02 . 116 . 29 ILE H H 8.450 0.02 . 117 . 29 ILE HA H 4.680 0.02 . 118 . 29 ILE HB H 1.750 0.02 . 119 . 29 ILE HG13 H 0.950 0.02 . 120 . 29 ILE HG12 H 0.950 0.02 . 121 . 29 ILE HD1 H 0.730 0.02 . 122 . 29 ILE HG2 H 0.860 0.02 . 123 . 30 ILE H H 9.640 0.02 . 124 . 30 ILE HA H 4.690 0.02 . 125 . 30 ILE HB H 2.130 0.02 . 126 . 30 ILE HG2 H 1.080 0.02 . 127 . 30 ILE HD1 H 0.830 0.02 . 128 . 30 ILE HG12 H 1.130 0.02 . 129 . 30 ILE HG13 H 1.450 0.02 . 130 . 31 PRO HD3 H 3.820 0.02 . 131 . 31 PRO HD2 H 4.040 0.02 . 132 . 32 ALA H H 8.180 0.02 . 133 . 32 ALA HA H 4.270 0.02 . 134 . 32 ALA HB H 1.170 0.02 . 135 . 33 SER H H 8.850 0.02 . 136 . 33 SER HA H 4.780 0.02 . 137 . 33 SER HB3 H 3.920 0.02 . 138 . 33 SER HB2 H 4.170 0.02 . 139 . 34 GLN H H 8.820 0.02 . 140 . 34 GLN HA H 3.980 0.02 . 141 . 34 GLN HB3 H 1.620 0.02 . 142 . 34 GLN HB2 H 1.790 0.02 . 143 . 34 GLN HG2 H 1.700 0.02 . 144 . 34 GLN HG3 H 1.700 0.02 . 145 . 35 PHE H H 7.720 0.02 . 146 . 35 PHE HA H 4.670 0.02 . 147 . 35 PHE HB3 H 3.280 0.02 . 148 . 35 PHE HB2 H 2.720 0.02 . 149 . 35 PHE HD1 H 7.270 0.02 . 150 . 35 PHE HD2 H 7.270 0.02 . 151 . 35 PHE HE1 H 7.380 0.02 . 152 . 35 PHE HE2 H 7.380 0.02 . 153 . 35 PHE HZ H 7.300 0.02 . 154 . 36 CYS H H 7.240 0.02 . 155 . 36 CYS HA H 5.140 0.02 . 156 . 36 CYS HB3 H 3.310 0.02 . 157 . 36 CYS HB2 H 2.880 0.02 . 158 . 37 PRO HA H 4.860 0.02 . 159 . 37 PRO HB2 H 2.120 0.02 . 160 . 37 PRO HB3 H 2.120 0.02 . 161 . 37 PRO HG2 H 1.820 0.02 . 162 . 37 PRO HG3 H 1.820 0.02 . 163 . 37 PRO HD3 H 3.650 0.02 . 164 . 37 PRO HD2 H 3.700 0.02 . 165 . 38 ARG H H 7.920 0.02 . 166 . 38 ARG HA H 4.740 0.02 . 167 . 38 ARG HB3 H 1.760 0.02 . 168 . 38 ARG HB2 H 1.840 0.02 . 169 . 39 VAL H H 8.260 0.02 . 170 . 39 VAL HA H 4.220 0.02 . 171 . 39 VAL HB H 1.880 0.02 . 172 . 39 VAL HG1 H 1.050 0.02 . 173 . 39 VAL HG2 H 0.830 0.02 . 174 . 40 GLU H H 8.410 0.02 . 175 . 40 GLU HA H 4.780 0.02 . 176 . 40 GLU HB3 H 1.900 0.02 . 177 . 40 GLU HB2 H 2.060 0.02 . 178 . 40 GLU HG2 H 2.560 0.02 . 179 . 40 GLU HG3 H 2.560 0.02 . 180 . 41 ILE H H 9.310 0.02 . 181 . 41 ILE HA H 4.850 0.02 . 182 . 41 ILE HB H 1.890 0.02 . 183 . 41 ILE HG12 H 1.040 0.02 . 184 . 41 ILE HG13 H 1.040 0.02 . 185 . 41 ILE HG2 H 0.720 0.02 . 186 . 42 ILE H H 9.210 0.02 . 187 . 42 ILE HA H 4.580 0.02 . 188 . 42 ILE HB H 1.820 0.02 . 189 . 42 ILE HG12 H 1.100 0.02 . 190 . 42 ILE HG13 H 1.100 0.02 . 191 . 42 ILE HG2 H 0.750 0.02 . 192 . 43 ALA H H 9.500 0.02 . 193 . 43 ALA HA H 5.030 0.02 . 194 . 43 ALA HB H 1.290 0.02 . 195 . 44 THR H H 8.560 0.02 . 196 . 44 THR HA H 4.810 0.02 . 197 . 44 THR HB H 3.950 0.02 . 198 . 44 THR HG2 H 1.160 0.02 . 199 . 45 MET H H 9.280 0.02 . 200 . 45 MET HA H 4.920 0.02 . 201 . 45 MET HB3 H 2.160 0.02 . 202 . 45 MET HB2 H 2.400 0.02 . 203 . 45 MET HG2 H 2.500 0.02 . 204 . 45 MET HG3 H 2.500 0.02 . 205 . 46 LYS H H 8.230 0.02 . 206 . 46 LYS HA H 4.020 0.02 . 207 . 47 LYS H H 8.160 0.02 . 208 . 47 LYS HA H 4.230 0.02 . 209 . 47 LYS HB3 H 1.760 0.02 . 210 . 47 LYS HB2 H 1.930 0.02 . 211 . 47 LYS HG3 H 1.680 0.02 . 212 . 47 LYS HG2 H 1.450 0.02 . 213 . 48 LYS H H 8.660 0.02 . 214 . 48 LYS HA H 4.060 0.02 . 215 . 48 LYS HB3 H 1.640 0.02 . 216 . 48 LYS HB2 H 1.690 0.02 . 217 . 48 LYS HG2 H 1.460 0.02 . 218 . 48 LYS HG3 H 2.500 0.02 . 219 . 49 GLY H H 7.830 0.02 . 220 . 49 GLY HA3 H 3.930 0.02 . 221 . 49 GLY HA2 H 3.930 0.02 . 222 . 50 GLU H H 7.470 0.02 . 223 . 50 GLU HA H 4.180 0.02 . 224 . 50 GLU HB2 H 1.910 0.02 . 225 . 50 GLU HB3 H 1.910 0.02 . 226 . 51 LYS H H 8.480 0.02 . 227 . 51 LYS HA H 5.340 0.02 . 228 . 52 ARG H H 9.070 0.02 . 229 . 52 ARG HA H 4.650 0.02 . 230 . 52 ARG HB3 H 1.730 0.02 . 231 . 52 ARG HB2 H 1.620 0.02 . 232 . 53 CYS H H 9.080 0.02 . 233 . 53 CYS HA H 5.800 0.02 . 234 . 53 CYS HB3 H 4.190 0.02 . 235 . 53 CYS HB2 H 3.270 0.02 . 236 . 54 LEU H H 8.890 0.02 . 237 . 54 LEU HA H 5.010 0.02 . 238 . 54 LEU HB3 H 1.440 0.02 . 239 . 54 LEU HB2 H 1.440 0.02 . 240 . 54 LEU HG H 1.650 0.02 . 241 . 55 ASN H H 8.470 0.02 . 242 . 55 ASN HA H 4.670 0.02 . 243 . 56 PRO HA H 4.180 0.02 . 244 . 56 PRO HB2 H 2.120 0.02 . 245 . 56 PRO HB3 H 2.120 0.02 . 246 . 56 PRO HG3 H 2.010 0.02 . 247 . 56 PRO HG2 H 2.080 0.02 . 248 . 56 PRO HD3 H 3.960 0.02 . 249 . 56 PRO HD2 H 3.960 0.02 . 250 . 57 GLU H H 7.660 0.02 . 251 . 57 GLU HA H 4.280 0.02 . 252 . 57 GLU HB3 H 1.820 0.02 . 253 . 57 GLU HB2 H 2.230 0.02 . 254 . 57 GLU HG3 H 2.680 0.02 . 255 . 57 GLU HG2 H 2.360 0.02 . 256 . 58 SER H H 7.290 0.02 . 257 . 58 SER HA H 4.500 0.02 . 258 . 58 SER HB3 H 4.040 0.02 . 259 . 58 SER HB2 H 4.140 0.02 . 260 . 59 LYS H H 9.120 0.02 . 261 . 59 LYS HA H 3.910 0.02 . 262 . 59 LYS HB3 H 1.920 0.02 . 263 . 59 LYS HB2 H 1.890 0.02 . 264 . 60 ALA H H 8.210 0.02 . 265 . 60 ALA HA H 4.210 0.02 . 266 . 60 ALA HB H 1.440 0.02 . 267 . 61 ILE H H 7.300 0.02 . 268 . 61 ILE HA H 3.890 0.02 . 269 . 61 ILE HB H 2.400 0.02 . 270 . 61 ILE HG13 H 1.510 0.02 . 271 . 61 ILE HG12 H 1.630 0.02 . 272 . 61 ILE HD1 H 0.700 0.02 . 273 . 61 ILE HG2 H 0.760 0.02 . 274 . 62 LYS H H 8.310 0.02 . 275 . 62 LYS HA H 3.900 0.02 . 276 . 63 ASN H H 8.060 0.02 . 277 . 63 ASN HA H 4.500 0.02 . 278 . 64 LEU H H 7.750 0.02 . 279 . 64 LEU HA H 4.220 0.02 . 280 . 64 LEU HB2 H 2.050 0.02 . 281 . 64 LEU HB3 H 2.050 0.02 . 282 . 64 LEU HG H 1.590 0.02 . 283 . 64 LEU HD1 H 0.830 0.02 . 284 . 64 LEU HD2 H 0.830 0.02 . 285 . 65 LEU H H 8.300 0.02 . 286 . 65 LEU HA H 3.900 0.02 . 287 . 65 LEU HD1 H 0.760 0.02 . 288 . 65 LEU HD2 H 0.760 0.02 . 289 . 66 LYS H H 7.520 0.02 . 290 . 66 LYS HA H 4.110 0.02 . 291 . 66 LYS HB3 H 1.950 0.02 . 292 . 66 LYS HB2 H 1.620 0.02 . 293 . 67 ALA H H 7.800 0.02 . 294 . 67 ALA HA H 4.260 0.02 . 295 . 67 ALA HB H 1.560 0.02 . 296 . 68 VAL H H 8.080 0.02 . 297 . 68 VAL HA H 4.120 0.02 . 298 . 68 VAL HB H 2.240 0.02 . 299 . 68 VAL HG1 H 0.970 0.02 . 300 . 68 VAL HG2 H 1.000 0.02 . 301 . 69 SER H H 7.950 0.02 . 302 . 69 SER HA H 4.340 0.02 . 303 . 69 SER HB2 H 4.000 0.02 . 304 . 69 SER HB3 H 4.000 0.02 . stop_ save_