data_4177 #Corrected using PDB structure: 1BO0_ # #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 # 19 K HA 2.43 4.38 # 55 P HA 3.93 4.69 # 56 T HA 3.98 4.84 # 58 K HA 3.72 4.58 # 60 V HA 2.73 3.47 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 36 C CB 37.28 44.46 # 52 C CB 45.68 40.63 # 56 T CB 69.18 76.29 # 71 T CB 69.48 76.01 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 3 V N 120.49 110.16 # 60 V N 122.69 112.36 # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 20 I H 6.06 8.26 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.06 -0.05 -0.32 N/A 0.09 -0.04 # #bmr4177.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4177.str file): #HA CA CB CO N HN #N/A -0.19 -0.19 N/A +0.09 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.04 +/-0.20 +/-0.18 N/A +/-0.51 +/-0.07 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.706 0.943 0.992 N/A 0.566 0.554 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.175 0.848 0.758 N/A 2.127 0.289 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Monocyte Chemoattractant Protein-3 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kwon D. . . 2 Lee D. . . 3 Sykes B. D. . 4 Kim K.-S. . . stop_ _BMRB_accession_number 4177 _BMRB_flat_file_name bmr4177.str _Entry_type new _Submission_date 1998-08-11 _Accession_date 1998-08-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 494 '13C chemical shifts' 247 '15N chemical shifts' 81 'coupling constants' 68 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Structural Characterization of a Monomeric Chemokine: Monocyte Chemoattractant Protein-3 ; _Citation_status published _Citation_type journal _MEDLINE_UI_code ? _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kim K.-S. . . 2 Rajarathnam K. . . 3 Clark-Lewis I. . . 4 Sykes B. D. . stop_ _Journal_abbreviation 'FEBS Lett.' _Journal_name_full ? _Journal_volume 395 _Page_first 277 _Page_last ? _Year 1996 save_ ################################## # Molecular system description # ################################## save_system_MCP-3 _Saveframe_category molecular_system _Mol_system_name 'Monocyte chemoattractant protein-3' _Abbreviation_common MCP-3 loop_ _Mol_system_component_name _Mol_label MCP-3 $MCP-3 'N-terminal artifact' $cloning_artifact stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1bo0 . . stop_ save_ ######################## # Monomeric polymers # ######################## save_MCP-3 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Monocyte_chemoattractant_protein-3 _Abbreviation_common MCP-3 _Mol_thiol_state 'all disulfide bound' _Details ; N-terminal extension of Gly-Ser-His-Met by cloning artifact. Chemical shifts of N-terminal extension are not shown. ; ############################## # Polymer residue sequence # ############################## _Residue_count 76 _Mol_residue_sequence ; QPVGINTSTTCCYRFINKKI PKQRLESYRRTTSSHCPREA VIFKTKLDKEICADPTQKWV QDFMKHLDKKTQTPKL ; loop_ _Residue_seq_code _Residue_label 1 GLN 2 PRO 3 VAL 4 GLY 5 ILE 6 ASN 7 THR 8 SER 9 THR 10 THR 11 CYS 12 CYS 13 TYR 14 ARG 15 PHE 16 ILE 17 ASN 18 LYS 19 LYS 20 ILE 21 PRO 22 LYS 23 GLN 24 ARG 25 LEU 26 GLU 27 SER 28 TYR 29 ARG 30 ARG 31 THR 32 THR 33 SER 34 SER 35 HIS 36 CYS 37 PRO 38 ARG 39 GLU 40 ALA 41 VAL 42 ILE 43 PHE 44 LYS 45 THR 46 LYS 47 LEU 48 ASP 49 LYS 50 GLU 51 ILE 52 CYS 53 ALA 54 ASP 55 PRO 56 THR 57 GLN 58 LYS 59 TRP 60 VAL 61 GLN 62 ASP 63 PHE 64 MET 65 LYS 66 HIS 67 LEU 68 ASP 69 LYS 70 LYS 71 THR 72 GLN 73 THR 74 PRO 75 LYS 76 LEU 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 1NCV "A Chain A, Determination Cc-Chemokine Mcp-3,Nmr, 7 Structures" 100.00 76 100 100 5e-40 PDB 1BO0 "Monocyte Chemoattractant Protein-3, Nmr,Minimized Average Structure" 95.00 80 100 100 5e-40 EMBL CAA50407.1 "monocyte chemoattractant protein(MCP-3) [Homo sapiens]" 76.77 99 100 100 5e-40 EMBL CAA50406.1 "monocyte chemoattractant protein (MCP-3)[Homo sapiens]" 72.38 105 100 100 5e-40 EMBL CAA50405.1 "monocyte chemoattractant protein (MCP-3)[Homo sapiens]" 69.72 109 100 100 5e-40 EMBL CAA51055.1 "monocyte chemotactic protein-3 [Homosapiens]" 69.72 109 100 100 5e-40 EMBL CAB59723.1 "monocyte chemotactic protein-3 [Homosapiens]" 69.72 109 100 100 5e-40 GenBank AAC03538.1 "monocyte chemoattractant protein 3[Homo sapiens]" 100.00 76 100 100 5e-40 PIR A54678 "monocyte chemotactic protein 3 precursor -human" 69.72 109 100 100 5e-40 REF NP_006264.2 "small inducible cytokine A7precursor; monocyte chemoattractant protein 3; smallinducible cytokine A7 (monocyte chemotactic protein 3)[Homo sapiens]" 76.77 99 100 100 5e-40 SWISS-PROT P80098 "SY07_HUMAN Small inducible cytokine A7precursor (CCL7) (Monocyte chemotactic protein 3)(MCP-3) (Monocyte chemoattractant protein 3) (NC28)" 76.77 99 100 100 5e-40 stop_ save_ save_cloning_artifact _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'N-terminal cloning artifact' _Abbreviation_common 'cloning artifact' _Mol_thiol_state 'not present' _Details ; N-terminal extension of Gly-Ser-His-Met by cloning artifact. Chemical shifts of N-terminal extension are not shown. ; _Residue_count 4 _Mol_residue_sequence ; GSHM ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET stop_ _Sequence_homology_query_date 2003-03-09 _Sequence_homology_query_revised_last_date 2002-05-25 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_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_atom_name single disulfide $MCP-3 11 SG $MCP-3 36 SG single disulfide $MCP-3 12 SG $MCP-3 52 SG single peptide $cloning_artifact 4 C $MCP-3 1 N stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $MCP-3 human 9606 Eukaryota Metazoa Homo sapiens 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 $MCP-3 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $MCP-3 . mM 1.9 2.1 '[U-95% 13C; U-95% 15N]' stop_ save_ ############################ # Computer software used # ############################ save_software_one _Saveframe_category software _Name nmrpipe _Version 97.231.15.18 loop_ _Task processing stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_one _Saveframe_category NMR_spectrometer _Manufacturer ? _Model ? _Field_strength 600 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment_one _Saveframe_category NMR_applied_experiment _Sample_label $sample_one _Details ; 1H-15N 1H-13C NOESY 1H-15N TOCSY HNHA CBCA(CO)NH 1H-15N NOE ; save_ ####################### # Sample conditions # ####################### save_sample_conditions_one _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.1 0.05 n/a temperature 303 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_one _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 _Indirect_shift_ratio _Indirect_shift_ratio_citation_label DSS H 1 protons ppm 0.00 internal direct 1.0 $citation_one DSS C 13 protons ppm 0.00 . indirect 0.251449530 $citation_one DSS N 15 protons ppm 0.00 . indirect 0.101329118 $citation_one stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chemical_shifts_one _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Chem_shift_reference_set_label $chemical_shift_reference_one _Mol_system_component_name MCP-3 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 GLN H H 8.40 . 1 2 1 GLN HA H 4.65 . 1 3 1 GLN CA C 57.61 . 1 4 1 GLN N N 123.09 . 1 5 2 PRO HA H 4.48 . 1 6 2 PRO HB2 H 2.25 . 2 7 2 PRO HB3 H 1.89 . 2 8 2 PRO HG2 H 2.01 . 1 9 2 PRO HG3 H 2.01 . 1 10 2 PRO HD2 H 3.65 . 2 11 2 PRO HD3 H 3.80 . 2 12 2 PRO CA C 62.91 . 1 13 2 PRO CB C 32.01 . 1 14 2 PRO CG C 27.01 . 1 15 2 PRO CD C 50.51 . 1 16 3 VAL H H 8.26 . 1 17 3 VAL HA H 4.12 . 1 18 3 VAL HB H 2.07 . 1 19 3 VAL HG1 H 0.97 . 2 20 3 VAL HG2 H 0.95 . 2 21 3 VAL CA C 62.31 . 1 22 3 VAL CB C 32.81 . 1 23 3 VAL CG1 C 21.01 . 2 24 3 VAL CG2 C 20.41 . 2 25 3 VAL N N 120.49 . 1 26 4 GLY H H 8.44 . 1 27 4 GLY HA2 H 3.97 . 1 28 4 GLY HA3 H 3.97 . 1 29 4 GLY CA C 45.11 . 1 30 4 GLY N N 112.49 . 1 31 5 ILE H H 7.94 . 1 32 5 ILE HA H 4.21 . 1 33 5 ILE HB H 1.85 . 1 34 5 ILE HG12 H 1.41 . 2 35 5 ILE HG13 H 1.16 . 2 36 5 ILE HG2 H 0.89 . 1 37 5 ILE HD1 H 0.83 . 1 38 5 ILE CA C 60.91 . 1 39 5 ILE CB C 38.81 . 1 40 5 ILE CG1 C 27.01 . 1 41 5 ILE CG2 C 17.31 . 1 42 5 ILE CD1 C 12.81 . 1 43 5 ILE N N 119.69 . 1 44 6 ASN H H 8.53 . 1 45 6 ASN HA H 4.82 . 1 46 6 ASN HB2 H 2.89 . 2 47 6 ASN HB3 H 2.77 . 2 48 6 ASN HD21 H 7.56 . 2 49 6 ASN HD22 H 6.91 . 2 50 6 ASN CA C 53.01 . 1 51 6 ASN CB C 38.71 . 1 52 6 ASN N N 122.49 . 1 53 6 ASN ND2 N 112.40 . 1 54 7 THR H H 8.18 . 1 55 7 THR HA H 4.36 . 1 56 7 THR HB H 4.28 . 1 57 7 THR HG2 H 1.20 . 1 58 7 THR CA C 61.91 . 1 59 7 THR CB C 69.51 . 1 60 7 THR CG2 C 21.01 . 1 61 7 THR N N 114.59 . 1 62 8 SER H H 8.34 . 1 63 8 SER HA H 4.55 . 1 64 8 SER HB2 H 3.93 . 2 65 8 SER HB3 H 3.88 . 2 66 8 SER CA C 58.61 . 1 67 8 SER CB C 64.71 . 1 68 8 SER N N 117.79 . 1 69 9 THR H H 8.39 . 1 70 9 THR HA H 4.38 . 1 71 9 THR HB H 4.19 . 1 72 9 THR HG2 H 1.15 . 1 73 9 THR CA C 62.21 . 1 74 9 THR CB C 69.51 . 1 75 9 THR CG2 C 21.51 . 1 76 9 THR N N 116.89 . 1 77 10 THR H H 8.24 . 1 78 10 THR HA H 4.30 . 1 79 10 THR HB H 4.14 . 1 80 10 THR HG2 H 1.22 . 1 81 10 THR CA C 62.91 . 1 82 10 THR CB C 69.71 . 1 83 10 THR CG2 C 21.91 . 1 84 10 THR N N 118.29 . 1 85 11 CYS H H 8.10 . 1 86 11 CYS HA H 4.98 . 1 87 11 CYS HB2 H 2.80 . 2 88 11 CYS HB3 H 2.54 . 2 89 11 CYS CA C 52.41 . 1 90 11 CYS CB C 39.81 . 1 91 11 CYS N N 118.59 . 1 92 12 CYS H H 8.34 . 1 93 12 CYS HA H 4.61 . 1 94 12 CYS HB2 H 2.41 . 2 95 12 CYS HB3 H 2.72 . 2 96 12 CYS CA C 55.51 . 1 97 12 CYS CB C 43.11 . 1 98 12 CYS N N 118.69 . 1 99 13 TYR H H 8.80 . 1 100 13 TYR HA H 4.42 . 1 101 13 TYR HB2 H 3.13 . 2 102 13 TYR HB3 H 2.71 . 2 103 13 TYR HD1 H 7.11 . 1 104 13 TYR HD2 H 7.11 . 1 105 13 TYR HE1 H 6.78 . 1 106 13 TYR HE2 H 6.78 . 1 107 13 TYR CA C 58.21 . 1 108 13 TYR CB C 39.41 . 1 109 13 TYR N N 121.09 . 1 110 14 ARG H H 7.44 . 1 111 14 ARG HA H 4.32 . 1 112 14 ARG HB2 H 1.78 . 2 113 14 ARG HB3 H 1.66 . 2 114 14 ARG HG2 H 1.50 . 2 115 14 ARG HG3 H 1.04 . 2 116 14 ARG HD2 H 3.20 . 1 117 14 ARG HD3 H 3.20 . 1 118 14 ARG HE H 7.18 . 1 119 14 ARG CA C 54.71 . 1 120 14 ARG CB C 32.21 . 1 121 14 ARG CG C 26.31 . 1 122 14 ARG CD C 43.11 . 1 123 14 ARG N N 119.09 . 1 124 15 PHE H H 8.50 . 1 125 15 PHE HA H 4.81 . 1 126 15 PHE HB2 H 2.90 . 2 127 15 PHE HB3 H 3.22 . 2 128 15 PHE HD1 H 7.03 . 1 129 15 PHE HD2 H 7.03 . 1 130 15 PHE HE1 H 7.20 . 1 131 15 PHE HE2 H 7.20 . 1 132 15 PHE HZ H 7.12 . 1 133 15 PHE CA C 55.81 . 1 134 15 PHE CB C 41.11 . 1 135 15 PHE N N 121.19 . 1 136 16 ILE H H 8.71 . 1 137 16 ILE HA H 4.41 . 1 138 16 ILE HB H 2.18 . 1 139 16 ILE HG12 H 1.62 . 2 140 16 ILE HG13 H 1.73 . 2 141 16 ILE HG2 H 1.25 . 1 142 16 ILE HD1 H 1.05 . 1 143 16 ILE CA C 61.01 . 1 144 16 ILE CB C 38.41 . 1 145 16 ILE CG1 C 28.21 . 1 146 16 ILE CG2 C 17.61 . 1 147 16 ILE CD1 C 13.41 . 1 148 16 ILE N N 122.19 . 1 149 17 ASN H H 8.63 . 1 150 17 ASN HA H 5.06 . 1 151 17 ASN HB2 H 2.94 . 1 152 17 ASN HB3 H 2.94 . 1 153 17 ASN HD21 H 7.65 . 2 154 17 ASN HD22 H 6.95 . 2 155 17 ASN CA C 53.21 . 1 156 17 ASN CB C 39.11 . 1 157 17 ASN N N 123.59 . 1 158 17 ASN ND2 N 111.90 . 1 159 18 LYS H H 7.39 . 1 160 18 LYS HA H 4.28 . 1 161 18 LYS HB2 H 1.71 . 2 162 18 LYS HB3 H 1.59 . 2 163 18 LYS HG2 H 1.29 . 1 164 18 LYS HG3 H 1.29 . 1 165 18 LYS HD2 H 1.59 . 1 166 18 LYS HD3 H 1.59 . 1 167 18 LYS HE2 H 2.95 . 1 168 18 LYS HE3 H 2.95 . 1 169 18 LYS CA C 54.91 . 1 170 18 LYS CB C 34.31 . 1 171 18 LYS CG C 23.91 . 1 172 18 LYS CD C 28.91 . 1 173 18 LYS CE C 42.01 . 1 174 18 LYS N N 119.39 . 1 175 19 LYS H H 7.68 . 1 176 19 LYS HA H 2.49 . 1 177 19 LYS HB2 H 1.05 . 2 178 19 LYS HB3 H 0.99 . 2 179 19 LYS HG2 H 0.70 . 2 180 19 LYS HG3 H 0.53 . 2 181 19 LYS HD2 H 1.35 . 1 182 19 LYS HD3 H 1.35 . 1 183 19 LYS HE2 H 2.76 . 1 184 19 LYS HE3 H 2.76 . 1 185 19 LYS CA C 56.21 . 1 186 19 LYS CB C 32.11 . 1 187 19 LYS CG C 23.91 . 1 188 19 LYS CD C 29.11 . 1 189 19 LYS CE C 41.61 . 1 190 19 LYS N N 120.09 . 1 191 20 ILE H H 6.10 . 1 192 20 ILE HA H 4.32 . 1 193 20 ILE HB H 1.64 . 1 194 20 ILE HG12 H 1.47 . 2 195 20 ILE HG13 H 1.05 . 2 196 20 ILE HG2 H 0.84 . 1 197 20 ILE HD1 H 0.83 . 1 198 20 ILE CB C 39.71 . 1 199 20 ILE CG1 C 26.41 . 1 200 20 ILE CG2 C 16.81 . 1 201 20 ILE CD1 C 12.81 . 1 202 20 ILE N N 122.59 . 1 203 21 PRO HA H 4.37 . 1 204 21 PRO HB2 H 2.35 . 2 205 21 PRO HB3 H 1.75 . 2 206 21 PRO HG2 H 1.97 . 2 207 21 PRO HG3 H 1.91 . 2 208 21 PRO HD2 H 3.35 . 2 209 21 PRO HD3 H 3.78 . 2 210 21 PRO CA C 62.71 . 1 211 21 PRO CB C 31.91 . 1 212 21 PRO CG C 27.71 . 1 213 21 PRO CD C 50.71 . 1 214 22 LYS H H 8.27 . 1 215 22 LYS HA H 3.32 . 1 216 22 LYS HB2 H 1.31 . 2 217 22 LYS HB3 H 1.17 . 2 218 22 LYS HG2 H 0.69 . 2 219 22 LYS HG3 H 0.88 . 2 220 22 LYS HD2 H 1.09 . 2 221 22 LYS HD3 H 1.15 . 2 222 22 LYS HE2 H 2.50 . 1 223 22 LYS HE3 H 2.50 . 1 224 22 LYS CA C 58.91 . 1 225 22 LYS CB C 31.81 . 1 226 22 LYS CG C 23.91 . 1 227 22 LYS CD C 28.91 . 1 228 22 LYS CE C 41.21 . 1 229 22 LYS N N 124.79 . 1 230 23 GLN H H 8.71 . 1 231 23 GLN HA H 4.19 . 1 232 23 GLN HB2 H 2.06 . 1 233 23 GLN HB3 H 2.06 . 1 234 23 GLN HG2 H 2.43 . 2 235 23 GLN HG3 H 2.37 . 2 236 23 GLN HE21 H 7.56 . 2 237 23 GLN HE22 H 6.89 . 2 238 23 GLN CA C 57.61 . 1 239 23 GLN CB C 28.91 . 1 240 23 GLN CG C 33.61 . 1 241 23 GLN N N 116.39 . 1 242 23 GLN NE2 N 111.20 . 1 243 24 ARG H H 7.76 . 1 244 24 ARG HA H 4.33 . 1 245 24 ARG HB2 H 2.07 . 2 246 24 ARG HB3 H 1.78 . 2 247 24 ARG HG2 H 1.66 . 1 248 24 ARG HG3 H 1.66 . 1 249 24 ARG HD2 H 3.13 . 2 250 24 ARG HD3 H 3.22 . 2 251 24 ARG HE H 7.40 . 1 252 24 ARG CA C 55.61 . 1 253 24 ARG CB C 30.31 . 1 254 24 ARG CG C 27.31 . 1 255 24 ARG CD C 42.91 . 1 256 24 ARG N N 115.99 . 1 257 24 ARG NE N 112.10 . 1 258 25 LEU H H 7.52 . 1 259 25 LEU HA H 4.35 . 1 260 25 LEU HB2 H 1.92 . 2 261 25 LEU HB3 H 1.26 . 2 262 25 LEU HG H 1.56 . 1 263 25 LEU HD1 H 0.28 . 2 264 25 LEU HD2 H 0.52 . 2 265 25 LEU CA C 55.01 . 1 266 25 LEU CB C 43.61 . 1 267 25 LEU CG C 25.71 . 1 268 25 LEU CD1 C 25.11 . 2 269 25 LEU CD2 C 22.91 . 2 270 25 LEU N N 118.99 . 1 271 26 GLU H H 9.16 . 1 272 26 GLU HA H 4.64 . 1 273 26 GLU HB2 H 1.93 . 2 274 26 GLU HB3 H 1.73 . 2 275 26 GLU HG2 H 2.21 . 1 276 26 GLU HG3 H 2.21 . 1 277 26 GLU CA C 57.01 . 1 278 26 GLU CB C 32.81 . 1 279 26 GLU CG C 35.11 . 1 280 26 GLU N N 120.39 . 1 281 27 SER H H 8.08 . 1 282 27 SER HA H 4.80 . 1 283 27 SER HB2 H 4.02 . 2 284 27 SER HB3 H 4.08 . 2 285 27 SER CA C 58.01 . 1 286 27 SER CB C 64.41 . 1 287 27 SER N N 109.29 . 1 288 28 TYR H H 8.60 . 1 289 28 TYR HA H 5.73 . 1 290 28 TYR HB2 H 2.42 . 2 291 28 TYR HB3 H 2.90 . 2 292 28 TYR HD1 H 6.77 . 1 293 28 TYR HD2 H 6.77 . 1 294 28 TYR HE1 H 6.86 . 1 295 28 TYR HE2 H 6.86 . 1 296 28 TYR CA C 56.61 . 1 297 28 TYR CB C 42.41 . 1 298 28 TYR N N 115.79 . 1 299 29 ARG H H 8.57 . 1 300 29 ARG HA H 4.58 . 1 301 29 ARG HB2 H 1.84 . 2 302 29 ARG HB3 H 1.70 . 2 303 29 ARG HG2 H 1.35 . 1 304 29 ARG HG3 H 1.35 . 1 305 29 ARG HD2 H 3.05 . 2 306 29 ARG HD3 H 3.17 . 2 307 29 ARG HE H 7.54 . 1 308 29 ARG CB C 33.11 . 1 309 29 ARG CG C 26.61 . 1 310 29 ARG CD C 43.41 . 1 311 29 ARG N N 117.29 . 1 312 29 ARG NE N 112.90 . 1 313 30 ARG H H 8.84 . 1 314 30 ARG HA H 5.18 . 1 315 30 ARG HB2 H 1.73 . 2 316 30 ARG HB3 H 2.09 . 2 317 30 ARG HG2 H 1.80 . 2 318 30 ARG HG3 H 1.65 . 2 319 30 ARG HD2 H 3.27 . 1 320 30 ARG HD3 H 3.27 . 1 321 30 ARG CA C 55.01 . 1 322 30 ARG CB C 32.41 . 1 323 30 ARG CG C 28.41 . 1 324 30 ARG CD C 43.31 . 1 325 30 ARG N N 121.09 . 1 326 31 THR H H 8.40 . 1 327 31 THR HA H 4.60 . 1 328 31 THR HB H 4.59 . 1 329 31 THR HG2 H 1.24 . 1 330 31 THR CA C 61.31 . 1 331 31 THR CB C 69.91 . 1 332 31 THR CG2 C 21.91 . 1 333 31 THR N N 113.19 . 1 334 32 THR H H 8.31 . 1 335 32 THR HA H 4.51 . 1 336 32 THR HB H 4.32 . 1 337 32 THR HG2 H 1.21 . 1 338 32 THR CA C 61.61 . 1 339 32 THR CB C 70.11 . 1 340 32 THR CG2 C 21.81 . 1 341 32 THR N N 114.19 . 1 342 33 SER H H 8.42 . 1 343 33 SER HA H 4.50 . 1 344 33 SER HB2 H 4.02 . 2 345 33 SER HB3 H 3.91 . 2 346 33 SER CA C 58.71 . 1 347 33 SER CB C 63.31 . 1 348 33 SER N N 117.89 . 1 349 34 SER H H 8.50 . 1 350 34 SER HA H 4.34 . 1 351 34 SER HB2 H 3.86 . 1 352 34 SER HB3 H 3.86 . 1 353 34 SER CA C 59.71 . 1 354 34 SER CB C 63.01 . 1 355 34 SER N N 119.39 . 1 356 35 HIS H H 8.13 . 1 357 35 HIS HA H 4.69 . 1 358 35 HIS HB2 H 3.11 . 2 359 35 HIS HB3 H 3.35 . 2 360 35 HIS CA C 55.61 . 1 361 35 HIS CB C 28.91 . 1 362 35 HIS N N 116.89 . 1 363 36 CYS H H 7.68 . 1 364 36 CYS HA H 5.18 . 1 365 36 CYS HB2 H 2.68 . 2 366 36 CYS HB3 H 3.36 . 2 367 36 CYS CA C 51.31 . 1 368 36 CYS CB C 37.41 . 1 369 36 CYS N N 117.99 . 1 370 37 PRO HA H 4.38 . 1 371 37 PRO HB2 H 2.42 . 2 372 37 PRO HB3 H 2.00 . 2 373 37 PRO HG2 H 2.18 . 2 374 37 PRO HG3 H 2.08 . 2 375 37 PRO HD2 H 3.90 . 2 376 37 PRO HD3 H 3.65 . 2 377 37 PRO CA C 64.71 . 1 378 37 PRO CB C 31.91 . 1 379 37 PRO CG C 27.41 . 1 380 37 PRO CD C 50.21 . 1 381 38 ARG H H 7.19 . 1 382 38 ARG HA H 4.55 . 1 383 38 ARG HB2 H 1.71 . 2 384 38 ARG HB3 H 1.90 . 2 385 38 ARG HG2 H 1.53 . 1 386 38 ARG HG3 H 1.53 . 1 387 38 ARG HD2 H 3.06 . 1 388 38 ARG HD3 H 3.06 . 1 389 38 ARG HE H 7.15 . 1 390 38 ARG CA C 54.01 . 1 391 38 ARG CB C 32.61 . 1 392 38 ARG CG C 26.01 . 1 393 38 ARG CD C 43.21 . 1 394 38 ARG N N 113.29 . 1 395 38 ARG NE N 111.70 . 1 396 39 GLU H H 8.62 . 1 397 39 GLU HA H 4.09 . 1 398 39 GLU HB2 H 1.94 . 1 399 39 GLU HB3 H 1.94 . 1 400 39 GLU HG2 H 2.31 . 2 401 39 GLU HG3 H 2.18 . 2 402 39 GLU CA C 56.91 . 1 403 39 GLU CB C 29.71 . 1 404 39 GLU CG C 36.01 . 1 405 39 GLU N N 124.09 . 1 406 40 ALA H H 8.10 . 1 407 40 ALA HA H 4.97 . 1 408 40 ALA HB H 1.57 . 1 409 40 ALA CA C 50.81 . 1 410 40 ALA CB C 24.91 . 1 411 40 ALA N N 122.99 . 1 412 41 VAL H H 8.41 . 1 413 41 VAL HA H 4.46 . 1 414 41 VAL HB H 1.36 . 1 415 41 VAL HG1 H 0.60 . 2 416 41 VAL HG2 H 0.12 . 2 417 41 VAL CA C 61.21 . 1 418 41 VAL CB C 34.21 . 1 419 41 VAL CG1 C 21.71 . 2 420 41 VAL CG2 C 20.61 . 2 421 41 VAL N N 119.99 . 1 422 42 ILE H H 8.98 . 1 423 42 ILE HA H 4.93 . 1 424 42 ILE HB H 1.62 . 1 425 42 ILE HG12 H 1.41 . 2 426 42 ILE HG13 H 0.90 . 2 427 42 ILE HG2 H 0.74 . 1 428 42 ILE HD1 H 0.65 . 1 429 42 ILE CA C 59.41 . 1 430 42 ILE CB C 38.91 . 1 431 42 ILE CG1 C 28.01 . 2 432 42 ILE CG2 C 18.61 . 2 433 42 ILE CD1 C 13.91 . 1 434 42 ILE N N 125.09 . 1 435 43 PHE H H 9.30 . 1 436 43 PHE HA H 5.29 . 1 437 43 PHE HB2 H 2.93 . 2 438 43 PHE HB3 H 3.13 . 2 439 43 PHE HD1 H 7.24 . 1 440 43 PHE HD2 H 7.24 . 1 441 43 PHE HE1 H 6.91 . 1 442 43 PHE HE2 H 6.91 . 1 443 43 PHE HZ H 7.26 . 1 444 43 PHE CA C 57.81 . 1 445 43 PHE CB C 41.91 . 1 446 43 PHE N N 127.29 . 1 447 44 LYS H H 9.01 . 1 448 44 LYS HA H 5.43 . 1 449 44 LYS HB2 H 1.98 . 2 450 44 LYS HB3 H 1.85 . 2 451 44 LYS HG2 H 1.40 . 1 452 44 LYS HG3 H 1.40 . 1 453 44 LYS HD2 H 1.64 . 1 454 44 LYS HD3 H 1.64 . 1 455 44 LYS HE2 H 2.95 . 1 456 44 LYS HE3 H 2.95 . 1 457 44 LYS CA C 54.81 . 1 458 44 LYS CB C 34.21 . 1 459 44 LYS CG C 24.81 . 1 460 44 LYS CD C 29.01 . 1 461 44 LYS CE C 40.91 . 1 462 44 LYS N N 122.59 . 1 463 45 THR H H 9.14 . 1 464 45 THR HA H 5.23 . 1 465 45 THR HB H 4.78 . 1 466 45 THR HG2 H 1.22 . 1 467 45 THR CA C 60.11 . 1 468 45 THR CB C 71.81 . 1 469 45 THR CG2 C 21.01 . 1 470 45 THR N N 116.89 . 1 471 46 LYS H H 8.64 . 1 472 46 LYS HA H 4.21 . 1 473 46 LYS HB2 H 1.74 . 2 474 46 LYS HB3 H 2.03 . 2 475 46 LYS HG2 H 1.40 . 2 476 46 LYS HG3 H 1.50 . 2 477 46 LYS HD2 H 1.50 . 1 478 46 LYS HD3 H 1.50 . 1 479 46 LYS HE2 H 3.00 . 1 480 46 LYS HE3 H 3.00 . 1 481 46 LYS CA C 58.21 . 1 482 46 LYS CB C 32.61 . 1 483 46 LYS CG C 25.91 . 1 484 46 LYS CD C 29.31 . 1 485 46 LYS CE C 42.01 . 1 486 46 LYS N N 119.39 . 1 487 47 LEU H H 7.62 . 1 488 47 LEU HA H 4.52 . 1 489 47 LEU HB2 H 1.81 . 2 490 47 LEU HB3 H 1.56 . 2 491 47 LEU HG H 1.59 . 1 492 47 LEU HD1 H 0.93 . 2 493 47 LEU HD2 H 0.87 . 2 494 47 LEU CA C 54.31 . 1 495 47 LEU CB C 40.61 . 1 496 47 LEU CG C 27.41 . 1 497 47 LEU CD1 C 24.91 . 2 498 47 LEU CD2 C 22.71 . 2 499 47 LEU N N 117.89 . 1 500 48 ASP H H 8.09 . 1 501 48 ASP HA H 4.27 . 1 502 48 ASP HB2 H 3.05 . 2 503 48 ASP HB3 H 2.71 . 2 504 48 ASP CA C 55.51 . 1 505 48 ASP CB C 38.81 . 1 506 48 ASP N N 116.09 . 1 507 49 LYS H H 7.29 . 1 508 49 LYS HA H 4.59 . 1 509 49 LYS HB2 H 1.74 . 2 510 49 LYS HB3 H 1.82 . 2 511 49 LYS HG2 H 1.31 . 1 512 49 LYS HG3 H 1.31 . 1 513 49 LYS HD2 H 1.44 . 1 514 49 LYS HD3 H 1.44 . 1 515 49 LYS HE2 H 3.01 . 1 516 49 LYS HE3 H 3.01 . 1 517 49 LYS CA C 54.71 . 1 518 49 LYS CB C 33.51 . 1 519 49 LYS CG C 24.61 . 1 520 49 LYS N N 117.19 . 1 521 50 GLU H H 8.48 . 1 522 50 GLU HA H 5.50 . 1 523 50 GLU HB2 H 1.96 . 2 524 50 GLU HB3 H 1.78 . 2 525 50 GLU HG2 H 2.00 . 2 526 50 GLU HG3 H 2.43 . 2 527 50 GLU CA C 55.11 . 1 528 50 GLU CB C 32.01 . 1 529 50 GLU CG C 37.61 . 1 530 50 GLU N N 121.19 . 1 531 51 ILE H H 9.17 . 1 532 51 ILE HA H 4.53 . 1 533 51 ILE HB H 1.95 . 1 534 51 ILE HG12 H 1.23 . 2 535 51 ILE HG13 H 1.57 . 2 536 51 ILE HG2 H 1.12 . 1 537 51 ILE HD1 H 0.88 . 1 538 51 ILE CA C 59.81 . 1 539 51 ILE CB C 42.21 . 1 540 51 ILE CG1 C 26.91 . 1 541 51 ILE CG2 C 18.01 . 1 542 51 ILE CD1 C 13.61 . 1 543 51 ILE N N 121.59 . 1 544 52 CYS H H 8.83 . 1 545 52 CYS HA H 5.06 . 1 546 52 CYS HB2 H 3.48 . 2 547 52 CYS HB3 H 2.78 . 2 548 52 CYS CA C 58.01 . 1 549 52 CYS CB C 45.81 . 1 550 52 CYS N N 125.89 . 1 551 53 ALA H H 9.85 . 1 552 53 ALA HA H 4.99 . 1 553 53 ALA HB H 1.32 . 1 554 53 ALA CA C 50.81 . 1 555 53 ALA CB C 23.91 . 1 556 53 ALA N N 126.99 . 1 557 54 ASP H H 8.42 . 1 558 54 ASP HA H 4.07 . 1 559 54 ASP HB2 H 2.60 . 2 560 54 ASP HB3 H 1.64 . 2 561 54 ASP CA C 49.81 . 1 562 54 ASP CB C 41.71 . 1 563 54 ASP N N 121.59 . 1 564 55 PRO HA H 3.99 . 1 565 55 PRO HB2 H 1.92 . 1 566 55 PRO HB3 H 1.92 . 1 567 55 PRO HG2 H 1.70 . 2 568 55 PRO HG3 H 1.82 . 2 569 55 PRO HD2 H 4.00 . 2 570 55 PRO HD3 H 3.90 . 2 571 55 PRO CA C 63.51 . 1 572 55 PRO CB C 31.61 . 1 573 55 PRO CG C 28.41 . 1 574 55 PRO CD C 50.81 . 1 575 56 THR H H 8.26 . 1 576 56 THR HA H 4.04 . 1 577 56 THR HB H 4.20 . 1 578 56 THR HG2 H 1.18 . 1 579 56 THR CA C 63.01 . 1 580 56 THR CB C 69.31 . 1 581 56 THR CG2 C 21.41 . 1 582 56 THR N N 109.99 . 1 583 57 GLN H H 7.43 . 1 584 57 GLN HA H 4.21 . 1 585 57 GLN HB2 H 1.65 . 2 586 57 GLN HB3 H 1.85 . 2 587 57 GLN HG2 H 2.37 . 2 588 57 GLN HG3 H 2.23 . 2 589 57 GLN HE21 H 7.38 . 2 590 57 GLN HE22 H 6.96 . 2 591 57 GLN CA C 54.51 . 1 592 57 GLN CB C 28.81 . 1 593 57 GLN CG C 33.81 . 1 594 57 GLN N N 120.79 . 1 595 57 GLN NE2 N 112.80 . 1 596 58 LYS H H 8.78 . 1 597 58 LYS HA H 3.78 . 1 598 58 LYS HB2 H 1.92 . 1 599 58 LYS HB3 H 1.92 . 1 600 58 LYS HG2 H 1.48 . 1 601 58 LYS HG3 H 1.48 . 1 602 58 LYS HD2 H 1.75 . 2 603 58 LYS HD3 H 1.65 . 2 604 58 LYS HE2 H 3.06 . 1 605 58 LYS HE3 H 3.06 . 1 606 58 LYS CA C 59.71 . 1 607 58 LYS CB C 31.51 . 1 608 58 LYS CG C 24.71 . 1 609 58 LYS CD C 28.71 . 1 610 58 LYS CE C 42.01 . 1 611 58 LYS N N 126.19 . 1 612 59 TRP H H 8.28 . 1 613 59 TRP HA H 4.30 . 1 614 59 TRP HB2 H 3.05 . 2 615 59 TRP HB3 H 3.01 . 2 616 59 TRP HD1 H 7.58 . 1 617 59 TRP HE1 H 10.06 . 1 618 59 TRP HE3 H 6.35 . 1 619 59 TRP HZ2 H 7.38 . 1 620 59 TRP HZ3 H 6.51 . 1 621 59 TRP HH2 H 6.94 . 1 622 59 TRP CA C 59.11 . 1 623 59 TRP CB C 26.51 . 1 624 59 TRP N N 115.79 . 1 625 59 TRP NE1 N 129.70 . 1 626 60 VAL H H 5.70 . 1 627 60 VAL HA H 2.79 . 1 628 60 VAL HB H 1.78 . 1 629 60 VAL HG1 H -0.67 . 2 630 60 VAL HG2 H 0.42 . 2 631 60 VAL CA C 65.81 . 1 632 60 VAL CB C 30.91 . 1 633 60 VAL CG1 C 21.21 . 2 634 60 VAL CG2 C 21.01 . 2 635 60 VAL N N 122.69 . 1 636 61 GLN H H 7.20 . 1 637 61 GLN HA H 3.96 . 1 638 61 GLN HB2 H 2.14 . 2 639 61 GLN HB3 H 2.08 . 2 640 61 GLN HG2 H 2.40 . 2 641 61 GLN HG3 H 2.28 . 2 642 61 GLN HE21 H 6.62 . 2 643 61 GLN HE22 H 7.40 . 2 644 61 GLN CA C 58.61 . 1 645 61 GLN CB C 27.41 . 1 646 61 GLN CG C 32.90 . 1 647 61 GLN N N 118.59 . 1 648 61 GLN NE2 N 109.90 . 1 649 62 ASP H H 8.63 . 1 650 62 ASP HA H 4.44 . 1 651 62 ASP HB2 H 2.88 . 2 652 62 ASP HB3 H 2.78 . 2 653 62 ASP CA C 57.31 . 1 654 62 ASP CB C 40.01 . 1 655 62 ASP N N 120.19 . 1 656 63 PHE H H 8.60 . 1 657 63 PHE HA H 4.55 . 1 658 63 PHE HB2 H 3.53 . 2 659 63 PHE HB3 H 2.90 . 2 660 63 PHE HD1 H 7.01 . 1 661 63 PHE HD2 H 7.01 . 1 662 63 PHE HE1 H 7.44 . 1 663 63 PHE HE2 H 7.44 . 1 664 63 PHE HZ H 7.38 . 1 665 63 PHE CA C 59.11 . 1 666 63 PHE CB C 37.71 . 1 667 63 PHE N N 122.59 . 1 668 64 MET H H 8.41 . 1 669 64 MET HA H 3.68 . 1 670 64 MET HB2 H 2.39 . 2 671 64 MET HB3 H 2.09 . 2 672 64 MET HG2 H 2.28 . 2 673 64 MET HG3 H 0.61 . 2 674 64 MET HE H 1.79 . 1 675 64 MET CA C 60.51 . 1 676 64 MET CB C 34.11 . 1 677 64 MET CG C 30.41 . 1 678 64 MET CE C 15.91 . 1 679 64 MET N N 119.69 . 1 680 65 LYS H H 7.64 . 1 681 65 LYS HA H 4.14 . 1 682 65 LYS HB2 H 1.98 . 2 683 65 LYS HB3 H 1.77 . 2 684 65 LYS HG2 H 1.52 . 2 685 65 LYS HG3 H 1.66 . 2 686 65 LYS HD2 H 1.70 . 1 687 65 LYS HD3 H 1.70 . 1 688 65 LYS HE2 H 3.02 . 1 689 65 LYS HE3 H 3.02 . 1 690 65 LYS CA C 59.31 . 1 691 65 LYS CB C 32.11 . 1 692 65 LYS CG C 25.21 . 1 693 65 LYS CD C 28.91 . 1 694 65 LYS CE C 42.01 . 1 695 65 LYS N N 116.89 . 1 696 66 HIS H H 7.89 . 1 697 66 HIS HA H 4.42 . 1 698 66 HIS HB2 H 3.43 . 2 699 66 HIS HB3 H 3.24 . 2 700 66 HIS HD2 H 6.70 . 1 701 66 HIS HE1 H 7.22 . 1 702 66 HIS CA C 59.01 . 1 703 66 HIS CB C 29.71 . 1 704 66 HIS N N 117.59 . 1 705 67 LEU H H 8.17 . 1 706 67 LEU HA H 4.12 . 1 707 67 LEU HB2 H 2.22 . 2 708 67 LEU HB3 H 1.76 . 2 709 67 LEU HG H 2.01 . 1 710 67 LEU HD1 H 1.11 . 2 711 67 LEU HD2 H 0.85 . 2 712 67 LEU CA C 56.91 . 1 713 67 LEU CB C 41.91 . 1 714 67 LEU CG C 27.01 . 1 715 67 LEU CD1 C 26.61 . 2 716 67 LEU CD2 C 22.41 . 2 717 67 LEU N N 120.09 . 1 718 68 ASP H H 8.60 . 1 719 68 ASP HA H 4.60 . 1 720 68 ASP HB2 H 2.88 . 2 721 68 ASP HB3 H 2.76 . 2 722 68 ASP CA C 56.21 . 1 723 68 ASP CB C 40.41 . 1 724 68 ASP N N 121.19 . 1 725 69 LYS H H 7.62 . 1 726 69 LYS HA H 4.21 . 1 727 69 LYS HB2 H 1.86 . 2 728 69 LYS HB3 H 1.91 . 2 729 69 LYS HG2 H 1.48 . 1 730 69 LYS HG3 H 1.48 . 1 731 69 LYS HD2 H 1.58 . 1 732 69 LYS HD3 H 1.58 . 1 733 69 LYS HE2 H 3.02 . 1 734 69 LYS HE3 H 3.02 . 1 735 69 LYS CA C 57.21 . 1 736 69 LYS CB C 32.21 . 1 737 69 LYS CG C 24.81 . 1 738 69 LYS N N 119.29 . 1 739 70 LYS H H 7.91 . 1 740 70 LYS HA H 4.29 . 1 741 70 LYS HB2 H 1.89 . 2 742 70 LYS HB3 H 1.82 . 2 743 70 LYS HG2 H 1.48 . 1 744 70 LYS HG3 H 1.48 . 1 745 70 LYS HD2 H 1.70 . 1 746 70 LYS HD3 H 1.70 . 1 747 70 LYS HE2 H 3.04 . 1 748 70 LYS HE3 H 3.04 . 1 749 70 LYS CA C 57.01 . 1 750 70 LYS CB C 32.61 . 1 751 70 LYS CG C 24.41 . 1 752 70 LYS CD C 28.91 . 1 753 70 LYS CE C 42.01 . 1 754 70 LYS N N 120.49 . 1 755 71 THR H H 7.97 . 1 756 71 THR HA H 4.35 . 1 757 71 THR HB H 4.28 . 1 758 71 THR HG2 H 1.26 . 1 759 71 THR CA C 62.11 . 1 760 71 THR CB C 69.61 . 1 761 71 THR CG2 C 21.41 . 1 762 71 THR N N 113.59 . 1 763 72 GLN H H 8.20 . 1 764 72 GLN HA H 4.44 . 1 765 72 GLN HB2 H 2.03 . 2 766 72 GLN HB3 H 2.14 . 2 767 72 GLN HG2 H 2.41 . 1 768 72 GLN HG3 H 2.41 . 1 769 72 GLN HE21 H 7.52 . 2 770 72 GLN HE22 H 6.83 . 2 771 72 GLN CA C 55.61 . 1 772 72 GLN CB C 29.41 . 1 773 72 GLN CG C 33.21 . 1 774 72 GLN N N 122.59 . 1 775 72 GLN NE2 N 111.70 . 1 776 73 THR H H 8.20 . 1 777 73 THR HA H 4.59 . 1 778 73 THR HB H 4.17 . 1 779 73 THR HG2 H 1.27 . 1 780 73 THR CA C 59.81 . 1 781 73 THR CB C 69.51 . 1 782 73 THR CG2 C 21.31 . 1 783 73 THR N N 118.29 . 1 784 74 PRO HA H 4.43 . 1 785 74 PRO HB2 H 2.31 . 2 786 74 PRO HB3 H 1.91 . 2 787 74 PRO HG2 H 2.04 . 1 788 74 PRO HG3 H 2.04 . 1 789 74 PRO HD2 H 3.86 . 2 790 74 PRO HD3 H 3.73 . 2 791 74 PRO CA C 63.11 . 1 792 74 PRO CB C 32.11 . 1 793 74 PRO CG C 27.11 . 1 794 74 PRO CD C 50.91 . 1 795 75 LYS H H 8.34 . 1 796 75 LYS HA H 4.32 . 1 797 75 LYS HB2 H 1.85 . 2 798 75 LYS HB3 H 1.75 . 2 799 75 LYS HG2 H 1.46 . 1 800 75 LYS HG3 H 1.46 . 1 801 75 LYS HD2 H 1.70 . 1 802 75 LYS HD3 H 1.70 . 1 803 75 LYS HE2 H 3.02 . 1 804 75 LYS HE3 H 3.02 . 1 805 75 LYS CA C 56.11 . 1 806 75 LYS CB C 32.81 . 1 807 75 LYS CG C 24.41 . 1 808 75 LYS CD C 28.91 . 1 809 75 LYS CE C 42.01 . 1 810 75 LYS N N 122.59 . 1 811 76 LEU H H 7.87 . 1 812 76 LEU HA H 4.21 . 1 813 76 LEU HB2 H 1.59 . 1 814 76 LEU HB3 H 1.59 . 1 815 76 LEU HG H 1.59 . 1 816 76 LEU HD1 H 0.86 . 2 817 76 LEU HD2 H 0.90 . 2 818 76 LEU CA C 56.11 . 1 819 76 LEU CB C 43.31 . 1 820 76 LEU CD1 C 23.41 . 2 821 76 LEU CD2 C 24.91 . 2 822 76 LEU N N 130.09 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_assigned_coupling_constants_one _Saveframe_category coupling_constants loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_conditions_one _Mol_system_component_name MCP-3 loop_ _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_value_error 3JHNHA 3 VAL H 3 VAL HA 7.6 . 3JHNHA 4 GLY H 4 GLY HA 7.9 . 3JHNHA 5 ILE H 5 ILE HA 8.2 . 3JHNHA 6 ASN H 6 ASN HA 7.9 . 3JHNHA 7 THR H 7 THR HA 8.1 . 3JHNHA 8 SER H 8 SER HA 6.6 . 3JHNHA 9 THR H 9 THR HA 7.3 . 3JHNHA 10 THR H 10 THR HA 6.9 . 3JHNHA 11 CYS H 11 CYS HA 9.4 . 3JHNHA 12 CYS H 12 CYS HA 6.8 . 3JHNHA 14 ARG H 14 ARG HA 8.4 . 3JHNHA 15 PHE H 15 PHE HA 9.5 . 3JHNHA 16 ILE H 16 ILE HA 7.9 . 3JHNHA 17 ASN H 17 ASN HA 8.6 . 3JHNHA 18 LYS H 18 LYS HA 9.1 . 3JHNHA 19 LYS H 19 LYS HA 4.3 . 3JHNHA 22 LYS H 22 LYS HA 2.4 . 3JHNHA 23 GLN H 23 GLN HA 4.4 . 3JHNHA 24 ARG H 24 ARG HA 9.1 . 3JHNHA 25 LEU H 25 LEU HA 7.4 . 3JHNHA 26 GLU H 26 GLU HA 12.2 . 3JHNHA 27 SER H 27 SER HA 6.1 . 3JHNHA 28 TYR H 28 TYR HA 6.6 . 3JHNHA 29 ARG H 29 ARG HA 8.9 . 3JHNHA 30 ARG H 30 ARG HA 9.1 . 3JHNHA 31 THR H 31 THR HA 7.5 . 3JHNHA 32 THR H 32 THR HA 8.8 . 3JHNHA 33 SER H 33 SER HA 4.9 . 3JHNHA 34 SER H 34 SER HA 6.2 . 3JHNHA 35 HIS H 35 HIS HA 9.0 . 3JHNHA 36 CYS H 36 CYS HA 8.0 . 3JHNHA 38 ARG H 38 ARG HA 8.7 . 3JHNHA 39 GLU H 39 GLU HA 5.1 . 3JHNHA 40 ALA H 40 ALA HA 8.9 . 3JHNHA 41 VAL H 41 VAL HA 10.2 . 3JHNHA 42 IEU H 42 IEU HA 11.8 . 3JHNHA 43 PHE H 43 PHE HA 10.1 . 3JHNHA 44 LYS H 44 LYS HA 10.2 . 3JHNHA 45 THR H 45 THR HA 9.6 . 3JHNHA 46 LYS H 46 LYS HA 3.9 . 3JHNHA 47 LEU H 47 LEU HA 10.2 . 3JHNHA 48 ASP H 48 ASP HA 7.6 . 3JHNHA 49 LYS H 49 LYS HA 10.1 . 3JHNHA 50 GLU H 50 GLU HA 8.9 . 3JHNHA 51 ILE H 51 ILE HA 11.6 . 3JHNHA 52 CYS H 52 CYS HA 6.9 . 3JHNHA 53 ALA H 53 ALA HA 11.3 . 3JHNHA 54 ASP H 54 ASP HA 3.1 . 3JHNHA 56 THR H 56 THR HA 8.0 . 3JHNHA 57 GLN H 57 GLN HA 7.6 . 3JHNHA 58 LYS H 58 LYS HA 2.5 . 3JHNHA 59 TRP H 59 TRP HA 2.6 . 3JHNHA 60 VAL H 60 VAL HA 6.9 . 3JHNHA 61 GLN H 61 GLN HA 4.5 . 3JHNHA 62 ASP H 62 ASP HA 3.5 . 3JHNHA 63 PHE H 63 PHE HA 4.7 . 3JHNHA 64 MET H 64 MET HA 3.9 . 3JHNHA 65 LYS H 65 LYS HA 4.1 . 3JHNHA 66 HIS H 66 HIS HA 4.6 . 3JHNHA 67 LEU H 67 LEU HA 5.1 . 3JHNHA 68 ASP H 68 ASP HA 4.5 . 3JHNHA 69 LYS H 69 LYS HA 6.0 . 3JHNHA 70 LYS H 70 LYS HA 6.3 . 3JHNHA 71 THR H 71 THR HA 7.9 . 3JHNHA 72 GLN H 72 GLN HA 7.5 . 3JHNHA 73 THR H 73 THR HA 7.7 . 3JHNHA 75 LYS H 75 LYS HA 7.5 . 3JHNHA 76 LEU H 76 LEU HA 9.4 . stop_ save_ ####################################### # Cited references within the entry # ####################################### save_citation_one _Saveframe_category citation _Citation_full ; Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995). ; save_