data_6404 #Corrected using PDB structure: 1SZ9A # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 45 V CA 56.34 66.22 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 45 V CB 38.34 31.23 # 46 D CB 31.04 40.56 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #N/A -0.26 0.04 N/A 0.67 -0.03 # #bmr6404.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr6404.str file): #HA CA CB CO N HN #N/A -0.11 -0.11 N/A +0.67 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN # N/A +/-0.14 +/-0.14 N/A +/-0.31 +/-0.06 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #N/A 0.946 0.992 N/A 0.750 0.566 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #N/A 0.818 0.765 N/A 1.740 0.329 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; HN, N, CA, CB Chemical Shift Assignments for the CID domain of Pcf11 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hollingworth David . . 2 Frenkiel Thomas A. . 3 Kelly Geoff . . 4 Noble Christian G. . 5 Taylor Ian A. . 6 Ramos Andres . . stop_ _BMRB_accession_number 6404 _BMRB_flat_file_name bmr6404.str _Entry_type new _Submission_date 2004-10-25 _Accession_date 2004-11-29 _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' 130 '15N chemical shifts' 130 '13C chemical shifts' 258 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Backbone assignment of PCF11 CTD binding domain ; _Citation_status published _Citation_type journal _PubMed_ID . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Hollingworth David . . 2 Kelly Geoff . . 3 Frenkiel Thomas A. . 4 Noble Christian G. . 5 Taylor Ian A. . 6 Ramos Andres . . stop_ _Journal_abbreviation "J. Biomol. NMR" _Journal_volume 31 _Journal_issue 4 _Page_first 363 _Page_last 363 _Year 2005 save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name "Pcf11 CID" _Abbreviation_common "Pcf11 CID" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "Pcf11 CID" $Pcf11_CID stop_ _System_physical_state native _System_oligomer_state protein _System_paramagnetic no _System_thiol_state "all free" save_ ######################## # Monomeric polymers # ######################## save_Pcf11_CID _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "Pcf11 CID" _Name_variant "Pcf11 CID" _Abbreviation_common "Pcf11 CID" _Mol_thiol_state "all free" ############################## # Polymer residue sequence # ############################## _Residue_count 142 _Mol_residue_sequence ; MDHDTEVIVKDFNSILEELT FNSRPIITTLTKLAEENISC AQYFVDAIESRIEKCMPKQK LYAFYALDSICKNVGSPYTI YFSRNLFNLYKRTYLLVDNT TRTKLINMFKLWLNPNDTGL PLFEGSALEKIEQFLIKASA LH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 HIS 4 ASP 5 THR 6 GLU 7 VAL 8 ILE 9 VAL 10 LYS 11 ASP 12 PHE 13 ASN 14 SER 15 ILE 16 LEU 17 GLU 18 GLU 19 LEU 20 THR 21 PHE 22 ASN 23 SER 24 ARG 25 PRO 26 ILE 27 ILE 28 THR 29 THR 30 LEU 31 THR 32 LYS 33 LEU 34 ALA 35 GLU 36 GLU 37 ASN 38 ILE 39 SER 40 CYS 41 ALA 42 GLN 43 TYR 44 PHE 45 VAL 46 ASP 47 ALA 48 ILE 49 GLU 50 SER 51 ARG 52 ILE 53 GLU 54 LYS 55 CYS 56 MET 57 PRO 58 LYS 59 GLN 60 LYS 61 LEU 62 TYR 63 ALA 64 PHE 65 TYR 66 ALA 67 LEU 68 ASP 69 SER 70 ILE 71 CYS 72 LYS 73 ASN 74 VAL 75 GLY 76 SER 77 PRO 78 TYR 79 THR 80 ILE 81 TYR 82 PHE 83 SER 84 ARG 85 ASN 86 LEU 87 PHE 88 ASN 89 LEU 90 TYR 91 LYS 92 ARG 93 THR 94 TYR 95 LEU 96 LEU 97 VAL 98 ASP 99 ASN 100 THR 101 THR 102 ARG 103 THR 104 LYS 105 LEU 106 ILE 107 ASN 108 MET 109 PHE 110 LYS 111 LEU 112 TRP 113 LEU 114 ASN 115 PRO 116 ASN 117 ASP 118 THR 119 GLY 120 LEU 121 PRO 122 LEU 123 PHE 124 GLU 125 GLY 126 SER 127 ALA 128 LEU 129 GLU 130 LYS 131 ILE 132 GLU 133 GLN 134 PHE 135 LEU 136 ILE 137 LYS 138 ALA 139 SER 140 ALA 141 LEU 142 HIS stop_ _Sequence_homology_query_date 2005-09-22 _Sequence_homology_query_revised_last_date 2005-08-25 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 2BF0 "X Chain X, Crystal Structure Of The Rpr OfPcf11" 99.30 143 99 99 7e-73 PDB 1SZ9 "A Chain A, The Rna Polymerase Ii Ctd In MrnaProcessing: Beta-Turn Recognition And Beta-Spiral Model" 98.61 144 100 100 9e-76 PDB 1SZA "A Chain A, The Rna Polymerase Ii Ctd In MrnaProcessing: Beta-Turn Recognition And Beta-Spiral Model" 98.61 144 100 100 9e-76 EMBL CAA88508.1 "unknown [Saccharomyces cerevisiae]" 22.68 626 100 100 4e-77 REF NP_010514.1 "mRNA 3' end processing factor,essential component of cleavage and polyadenylationfactor IA (CF IA), involved in pre-mRNA 3' endprocessing and in transcription termination; bindsC-terminal domain of largest subunit of RNA pol II(Rpo21p); Pcf11p [Saccharomyces cerevisiae]" 22.68 626 100 100 4e-77 SWISS-PROT P39081 "PCF11_YEAST PCF11 protein" 22.68 626 100 100 4e-77 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Pcf11_CID "brewer's yeast" 4932 Eukaryota Fungi Saccharomices cerevisiae 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 $Pcf11_CID "recombinant technology" "Escherichia coli" Escherichia coli . . . 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 $Pcf11_CID 0.8 mM "[U-13C; U-15N; U-2H]" stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Pcf11_CID 0.8 mM "[U-13C; U-15N]" stop_ save_ save_sample_3 _Saveframe_category sample _Sample_type solution loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $Pcf11_CID 0.8 mM "[U-15N]" stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model Inova _Field_strength 800 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; HNCACB HNCA TROSY-HNCACB TROSY-HNCA 15N-edited NOESY ; save_ ####################### # Sample conditions # ####################### save_conditions_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.4 0.2 pH temperature 300 1 K "ionic strength" 0.1 0.001 M stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_referencing _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 "methyl protons" ppm 0.0 internal direct . . . 1.0 DSS C 13 "methyl protons" ppm 0.0 . indirect . . . 0.251449530 DSS N 15 "methyl protons" ppm 0.0 . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $conditions_1 _Chem_shift_reference_set_label $chemical_shift_referencing _Mol_system_component_name "Pcf11 CID" 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 5 THR H H 8.00 . 1 2 5 THR N N 116.97 . 1 3 5 THR CA C 66.09 . 1 4 5 THR CB C 68.39 . 1 5 6 GLU H H 8.18 . 1 6 6 GLU N N 120.87 . 1 7 6 GLU CA C 59.99 . 1 8 6 GLU CB C 29.19 . 1 9 7 VAL H H 7.66 . 1 10 7 VAL N N 117.57 . 1 11 7 VAL CA C 66.39 . 1 12 7 VAL CB C 31.79 . 1 13 8 ILE H H 7.39 . 1 14 8 ILE N N 120.77 . 1 15 8 ILE CA C 64.19 . 1 16 8 ILE CB C 38.19 . 1 17 9 VAL H H 8.41 . 1 18 9 VAL N N 120.17 . 1 19 9 VAL CA C 67.39 . 1 20 9 VAL CB C 31.69 . 1 21 10 LYS H H 8.37 . 1 22 10 LYS N N 121.37 . 1 23 10 LYS CA C 60.09 . 1 24 10 LYS CB C 31.79 . 1 25 11 ASP H H 8.45 . 1 26 11 ASP N N 121.67 . 1 27 11 ASP CA C 57.79 . 1 28 11 ASP CB C 39.99 . 1 29 12 PHE H H 8.50 . 1 30 12 PHE N N 121.17 . 1 31 12 PHE CA C 62.09 . 1 32 12 PHE CB C 40.89 . 1 33 13 ASN H H 8.63 . 1 34 13 ASN N N 115.37 . 1 35 13 ASN CA C 56.99 . 1 36 13 ASN CB C 39.29 . 1 37 14 SER H H 8.45 . 1 38 14 SER N N 115.87 . 1 39 14 SER CA C 61.99 . 1 40 14 SER CB C 63.39 . 1 41 15 ILE H H 7.81 . 1 42 15 ILE N N 122.97 . 1 43 15 ILE CA C 64.19 . 1 44 15 ILE CB C 37.69 . 1 45 16 LEU H H 7.83 . 1 46 16 LEU N N 119.67 . 1 47 16 LEU CA C 57.69 . 1 48 16 LEU CB C 41.79 . 1 49 17 GLU H H 7.50 . 1 50 17 GLU N N 114.17 . 1 51 17 GLU CA C 57.89 . 1 52 17 GLU CB C 29.39 . 1 53 18 GLU H H 7.50 . 1 54 18 GLU N N 114.87 . 1 55 18 GLU CA C 55.79 . 1 56 18 GLU CB C 29.29 . 1 57 19 LEU H H 7.80 . 1 58 19 LEU N N 123.17 . 1 59 19 LEU CA C 53.49 . 1 60 19 LEU CB C 39.89 . 1 61 20 THR H H 8.67 . 1 62 20 THR N N 114.87 . 1 63 20 THR CA C 61.19 . 1 64 20 THR CB C 69.69 . 1 65 21 PHE H H 7.67 . 1 67 21 PHE CA C 53.89 . 1 69 22 ASN H H 8.40 . 1 70 22 ASN N N 116.37 . 1 71 22 ASN CA C 51.89 . 1 72 22 ASN CB C 35.89 . 1 73 23 SER H H 6.81 . 1 74 23 SER N N 118.67 . 1 75 23 SER CA C 55.49 . 1 76 23 SER CB C 61.39 . 1 77 24 ARG H H 8.97 . 1 78 24 ARG N N 128.37 . 1 79 24 ARG CA C 59.69 . 1 80 24 ARG CB C 25.79 . 1 81 25 PRO CA C 66.69 . 1 82 26 ILE H H 7.54 . 1 83 26 ILE N N 118.17 . 1 84 26 ILE CA C 65.39 . 1 85 26 ILE CB C 36.69 . 1 86 27 ILE H H 8.18 . 1 87 27 ILE N N 119.87 . 1 88 27 ILE CA C 66.59 . 1 89 27 ILE CB C 37.19 . 1 90 28 THR H H 9.04 . 1 91 28 THR N N 119.97 . 1 92 28 THR CA C 67.39 . 1 93 28 THR CB C 68.79 . 1 94 29 THR H H 8.18 . 1 95 29 THR N N 121.87 . 1 96 29 THR CA C 67.39 . 1 97 29 THR CB C 68.69 . 1 98 30 LEU H H 8.59 . 1 99 30 LEU N N 120.17 . 1 100 30 LEU CA C 58.09 . 1 101 30 LEU CB C 41.59 . 1 102 31 THR H H 7.88 . 1 103 31 THR N N 114.67 . 1 104 31 THR CA C 67.29 . 1 105 31 THR CB C 68.89 . 1 106 32 LYS H H 8.12 . 1 107 32 LYS N N 122.67 . 1 108 32 LYS CA C 58.99 . 1 109 32 LYS CB C 31.79 . 1 110 33 LEU H H 8.42 . 1 111 33 LEU N N 118.47 . 1 112 33 LEU CA C 58.39 . 1 113 33 LEU CB C 42.49 . 1 114 34 ALA H H 8.10 . 1 115 34 ALA N N 119.67 . 1 116 34 ALA CA C 54.29 . 1 117 34 ALA CB C 17.59 . 1 118 35 GLU H H 8.13 . 1 119 35 GLU N N 118.87 . 1 120 35 GLU CA C 58.79 . 1 121 35 GLU CB C 30.49 . 1 122 36 GLU H H 8.43 . 1 123 36 GLU N N 115.87 . 1 124 36 GLU CA C 57.99 . 1 125 36 GLU CB C 30.89 . 1 126 37 ASN H H 7.71 . 1 127 37 ASN N N 116.67 . 1 128 37 ASN CA C 51.79 . 1 129 37 ASN CB C 39.69 . 1 130 38 ILE H H 7.72 . 1 131 38 ILE N N 121.17 . 1 132 38 ILE CA C 64.49 . 1 133 38 ILE CB C 37.99 . 1 134 39 SER H H 8.81 . 1 135 39 SER N N 117.67 . 1 136 39 SER CA C 61.09 . 1 137 39 SER CB C 61.99 . 1 138 40 CYS H H 7.97 . 1 139 40 CYS N N 118.37 . 1 140 40 CYS CA C 58.89 . 1 141 40 CYS CB C 27.39 . 1 142 41 ALA H H 7.58 . 1 143 41 ALA N N 120.87 . 1 144 41 ALA CA C 56.19 . 1 145 41 ALA CB C 18.79 . 1 146 42 GLN H H 8.70 . 1 147 42 GLN N N 113.87 . 1 148 42 GLN CA C 58.59 . 1 149 42 GLN CB C 27.79 . 1 150 43 TYR H H 6.86 . 1 151 43 TYR N N 116.37 . 1 152 43 TYR CA C 59.59 . 1 153 43 TYR CB C 37.69 . 1 154 44 PHE H H 7.54 . 1 155 44 PHE N N 120.17 . 1 156 44 PHE CA C 56.49 . 1 157 44 PHE CB C 36.49 . 1 158 45 VAL H H 8.29 . 1 159 45 VAL N N 121.07 . 1 160 45 VAL CA C 56.49 . 1 161 45 VAL CB C 38.19 . 1 162 46 ASP H H 8.09 . 1 163 46 ASP N N 119.17 . 1 164 46 ASP CA C 57.49 . 1 165 46 ASP CB C 30.89 . 1 166 47 ALA H H 8.09 . 1 167 47 ALA N N 121.87 . 1 168 47 ALA CA C 55.29 . 1 169 47 ALA CB C 18.59 . 1 170 48 ILE H H 8.52 . 1 171 48 ILE N N 119.97 . 1 172 48 ILE CA C 65.59 . 1 173 48 ILE CB C 37.29 . 1 174 49 GLU H H 9.09 . 1 175 49 GLU N N 118.97 . 1 176 49 GLU CA C 61.09 . 1 177 49 GLU CB C 28.69 . 1 178 50 SER H H 8.44 . 1 179 50 SER N N 113.37 . 1 180 50 SER CA C 61.49 . 1 181 50 SER CB C 62.89 . 1 182 51 ARG H H 7.84 . 1 183 51 ARG N N 119.87 . 1 184 51 ARG CA C 58.59 . 1 185 51 ARG CB C 28.99 . 1 186 52 ILE H H 8.26 . 1 187 52 ILE N N 118.27 . 1 188 52 ILE CA C 66.59 . 1 189 52 ILE CB C 37.89 . 1 190 53 GLU H H 8.02 . 1 194 54 LYS H H 8.23 . 1 195 54 LYS N N 115.37 . 1 196 54 LYS CA C 58.09 . 1 197 54 LYS CB C 34.39 . 1 198 55 CYS H H 8.48 . 1 199 55 CYS N N 116.57 . 1 200 55 CYS CA C 58.39 . 1 201 55 CYS CB C 28.09 . 1 202 56 MET H H 8.61 . 1 203 56 MET N N 119.37 . 1 204 56 MET CA C 54.29 . 1 205 56 MET CB C 31.09 . 1 206 58 LYS H H 8.19 . 1 207 58 LYS N N 113.37 . 1 208 58 LYS CA C 58.89 . 1 209 58 LYS CB C 31.89 . 1 210 59 GLN H H 8.01 . 1 211 59 GLN N N 114.17 . 1 212 59 GLN CA C 55.79 . 1 213 59 GLN CB C 29.39 . 1 214 60 LYS H H 7.51 . 1 215 60 LYS N N 122.37 . 1 216 60 LYS CA C 60.99 . 1 217 60 LYS CB C 34.09 . 1 218 61 LEU H H 8.50 . 1 219 61 LEU N N 116.37 . 1 220 61 LEU CA C 57.39 . 1 221 61 LEU CB C 41.29 . 1 222 62 TYR H H 5.97 . 1 223 62 TYR N N 113.87 . 1 224 62 TYR CA C 58.49 . 1 225 62 TYR CB C 36.19 . 1 226 63 ALA H H 7.07 . 1 227 63 ALA N N 119.37 . 1 228 63 ALA CA C 55.09 . 1 229 63 ALA CB C 17.79 . 1 230 64 PHE H H 7.81 . 1 231 64 PHE N N 118.67 . 1 232 64 PHE CA C 63.39 . 1 233 64 PHE CB C 38.39 . 1 234 65 TYR H H 8.55 . 1 235 65 TYR N N 118.17 . 1 236 65 TYR CA C 58.29 . 1 237 65 TYR CB C 35.89 . 1 238 66 ALA H H 7.85 . 1 239 66 ALA N N 123.87 . 1 240 66 ALA CA C 55.89 . 1 241 66 ALA CB C 17.09 . 1 242 67 LEU H H 7.75 . 1 243 67 LEU N N 120.87 . 1 244 67 LEU CA C 60.39 . 1 245 67 LEU CB C 42.89 . 1 246 68 ASP H H 9.12 . 1 247 68 ASP N N 120.37 . 1 248 68 ASP CA C 58.89 . 1 249 68 ASP CB C 44.39 . 1 250 69 SER H H 8.09 . 1 251 69 SER N N 110.17 . 1 252 69 SER CA C 60.99 . 1 253 69 SER CB C 62.99 . 1 254 70 ILE H H 8.49 . 1 255 70 ILE N N 119.67 . 1 256 70 ILE CA C 66.29 . 1 257 70 ILE CB C 37.89 . 1 258 71 CYS H H 8.36 . 1 259 71 CYS N N 117.17 . 1 260 71 CYS CA C 66.09 . 1 262 72 LYS H H 8.53 . 1 263 72 LYS N N 118.37 . 1 264 72 LYS CA C 59.29 . 1 265 72 LYS CB C 33.29 . 1 266 73 ASN H H 8.22 . 1 270 74 VAL H H 8.11 . 1 271 74 VAL N N 119.17 . 1 272 74 VAL CA C 64.29 . 1 273 74 VAL CB C 32.09 . 1 274 75 GLY H H 7.45 . 1 275 75 GLY N N 105.17 . 1 276 75 GLY CA C 45.49 . 1 277 76 SER H H 8.79 . 1 278 76 SER N N 122.37 . 1 279 76 SER CA C 57.59 . 1 280 76 SER CB C 62.99 . 1 281 78 TYR H H 8.28 . 1 282 78 TYR N N 126.67 . 1 283 78 TYR CA C 64.19 . 1 284 78 TYR CB C 33.09 . 1 285 79 THR H H 7.52 . 1 286 79 THR N N 106.67 . 1 287 79 THR CA C 64.29 . 1 289 80 ILE H H 6.74 . 1 290 80 ILE N N 121.17 . 1 291 80 ILE CA C 63.99 . 1 292 80 ILE CB C 37.59 . 1 293 81 TYR H H 8.43 . 1 294 81 TYR N N 119.37 . 1 295 81 TYR CA C 58.49 . 1 296 81 TYR CB C 37.69 . 1 297 82 PHE H H 9.49 . 1 298 82 PHE N N 116.37 . 1 299 82 PHE CA C 61.69 . 1 300 82 PHE CB C 38.79 . 1 301 83 SER H H 7.70 . 1 302 83 SER N N 111.87 . 1 303 83 SER CA C 63.39 . 1 304 84 ARG H H 7.03 . 1 305 84 ARG N N 119.87 . 1 306 84 ARG CA C 60.09 . 1 307 84 ARG CB C 29.19 . 1 308 85 ASN H H 8.85 . 1 309 85 ASN N N 114.17 . 1 310 85 ASN CA C 52.49 . 1 311 85 ASN CB C 38.69 . 1 312 86 LEU H H 6.80 . 1 313 86 LEU N N 120.87 . 1 314 86 LEU CA C 58.79 . 1 315 86 LEU CB C 42.79 . 1 316 87 PHE H H 8.83 . 1 317 87 PHE N N 115.17 . 1 318 87 PHE CA C 61.09 . 1 319 87 PHE CB C 37.49 . 1 320 88 ASN H H 8.15 . 1 321 88 ASN N N 117.07 . 1 322 88 ASN CA C 56.29 . 1 323 88 ASN CB C 37.89 . 1 324 89 LEU H H 8.35 . 1 325 89 LEU N N 118.17 . 1 326 89 LEU CA C 57.79 . 1 328 90 TYR H H 9.25 . 1 329 90 TYR N N 123.97 . 1 330 90 TYR CA C 62.79 . 1 331 90 TYR CB C 39.59 . 1 332 91 LYS H H 8.69 . 1 333 91 LYS N N 119.17 . 1 334 91 LYS CA C 59.69 . 1 335 91 LYS CB C 31.19 . 1 336 92 ARG H H 7.67 . 1 337 92 ARG N N 114.97 . 1 338 92 ARG CA C 59.29 . 1 339 92 ARG CB C 30.29 . 1 340 93 THR H H 7.42 . 1 341 93 THR N N 112.67 . 1 342 93 THR CA C 67.89 . 1 343 94 TYR H H 8.77 . 1 344 94 TYR N N 120.87 . 1 345 94 TYR CA C 62.29 . 1 346 94 TYR CB C 38.69 . 1 347 95 LEU H H 7.88 . 1 348 95 LEU N N 113.67 . 1 349 95 LEU CA C 57.29 . 1 350 95 LEU CB C 41.79 . 1 351 96 LEU H H 7.47 . 1 352 96 LEU N N 117.37 . 1 353 96 LEU CA C 55.59 . 1 354 96 LEU CB C 44.59 . 1 355 97 VAL H H 7.10 . 1 356 97 VAL N N 110.67 . 1 357 97 VAL CA C 60.29 . 1 358 97 VAL CB C 33.39 . 1 359 98 ASP H H 7.84 . 1 360 98 ASP N N 115.67 . 1 361 98 ASP CA C 52.49 . 1 362 98 ASP CB C 41.49 . 1 363 99 ASN H H 7.78 . 1 364 99 ASN N N 123.47 . 1 365 99 ASN CA C 53.29 . 1 366 99 ASN CB C 37.99 . 1 367 100 THR H H 8.80 . 1 368 100 THR N N 113.87 . 1 369 100 THR CA C 66.39 . 1 370 100 THR CB C 69.49 . 1 371 101 THR H H 8.25 . 1 372 101 THR N N 121.17 . 1 373 101 THR CA C 67.19 . 1 374 101 THR CB C 68.49 . 1 375 102 ARG H H 8.67 . 1 376 102 ARG N N 123.17 . 1 377 102 ARG CA C 61.19 . 1 378 102 ARG CB C 29.19 . 1 379 103 THR H H 7.78 . 1 380 103 THR N N 113.87 . 1 381 103 THR CA C 67.19 . 1 382 103 THR CB C 68.49 . 1 383 104 LYS H H 7.29 . 1 384 104 LYS N N 120.17 . 1 385 104 LYS CA C 59.59 . 1 386 104 LYS CB C 32.09 . 1 387 105 LEU H H 8.42 . 1 388 105 LEU N N 121.17 . 1 389 105 LEU CA C 57.89 . 1 390 105 LEU CB C 40.89 . 1 391 106 ILE H H 8.84 . 1 392 106 ILE N N 127.67 . 1 393 106 ILE CA C 66.49 . 1 394 106 ILE CB C 37.89 . 1 395 107 ASN H H 8.12 . 1 396 107 ASN N N 118.87 . 1 397 107 ASN CA C 56.19 . 1 398 107 ASN CB C 37.49 . 1 399 108 MET H H 7.71 . 1 400 108 MET N N 118.67 . 1 401 108 MET CA C 58.59 . 1 402 108 MET CB C 33.39 . 1 403 109 PHE H H 7.20 . 1 404 109 PHE N N 118.97 . 1 405 109 PHE CA C 59.59 . 1 406 109 PHE CB C 38.09 . 1 407 110 LYS H H 8.15 . 1 408 110 LYS N N 117.37 . 1 409 110 LYS CA C 59.79 . 1 410 110 LYS CB C 31.69 . 1 411 111 LEU H H 7.03 . 1 415 112 TRP H H 7.73 . 1 419 113 LEU H H 7.23 . 1 423 114 ASN H H 7.24 . 1 424 114 ASN N N 112.07 . 1 425 114 ASN CA C 51.19 . 1 426 114 ASN CB C 38.39 . 1 427 118 THR H H 8.04 . 1 428 118 THR N N 108.17 . 1 429 118 THR CA C 62.59 . 1 430 118 THR CB C 70.59 . 1 431 119 GLY H H 8.31 . 1 432 119 GLY N N 109.37 . 1 433 119 GLY CA C 44.49 . 1 434 120 LEU H H 7.64 . 1 435 120 LEU N N 121.67 . 1 436 120 LEU CA C 51.19 . 1 437 120 LEU CB C 42.09 . 1 438 121 PRO CA C 62.39 . 1 440 122 LEU H H 8.55 . 1 444 123 PHE H H 6.13 . 1 445 123 PHE N N 107.47 . 1 446 123 PHE CA C 55.09 . 1 447 123 PHE CB C 42.39 . 1 448 124 GLU H H 8.23 . 1 449 124 GLU N N 119.37 . 1 450 124 GLU CA C 55.49 . 1 451 124 GLU CB C 30.69 . 1 452 125 GLY H H 8.75 . 1 453 125 GLY N N 110.67 . 1 454 125 GLY CA C 46.99 . 1 455 127 ALA H H 7.78 . 1 456 127 ALA N N 124.37 . 1 457 127 ALA CA C 55.89 . 1 458 127 ALA CB C 19.09 . 1 459 128 LEU H H 7.95 . 1 460 128 LEU N N 113.87 . 1 461 128 LEU CA C 57.79 . 1 462 128 LEU CB C 40.29 . 1 463 129 GLU H H 8.50 . 1 464 129 GLU N N 120.67 . 1 465 129 GLU CA C 57.79 . 1 466 129 GLU CB C 29.19 . 1 467 130 LYS H H 7.63 . 1 468 130 LYS N N 118.27 . 1 469 130 LYS CA C 59.49 . 1 470 130 LYS CB C 30.79 . 1 471 131 ILE H H 7.96 . 1 472 131 ILE N N 120.17 . 1 473 131 ILE CA C 66.79 . 1 474 131 ILE CB C 37.49 . 1 475 132 GLU H H 8.46 . 1 476 132 GLU N N 120.77 . 1 477 132 GLU CA C 60.39 . 1 478 132 GLU CB C 29.99 . 1 479 133 GLN H H 8.09 . 1 480 133 GLN N N 114.67 . 1 481 133 GLN CA C 58.79 . 1 482 133 GLN CB C 28.19 . 1 483 134 PHE H H 7.85 . 1 484 134 PHE N N 121.27 . 1 485 134 PHE CA C 60.69 . 1 486 134 PHE CB C 38.99 . 1 487 135 LEU H H 8.44 . 1 488 135 LEU N N 119.97 . 1 489 135 LEU CA C 57.19 . 1 490 135 LEU CB C 41.89 . 1 491 136 ILE H H 8.28 . 1 492 136 ILE N N 120.67 . 1 493 136 ILE CA C 64.99 . 1 494 136 ILE CB C 37.99 . 1 495 137 LYS H H 7.75 . 1 496 137 LYS N N 121.37 . 1 497 137 LYS CA C 58.59 . 1 498 137 LYS CB C 31.79 . 1 499 138 ALA H H 7.78 . 1 500 138 ALA N N 120.37 . 1 501 138 ALA CA C 52.39 . 1 502 138 ALA CB C 17.39 . 1 503 139 SER H H 7.88 . 1 507 140 ALA H H 7.85 . 1 511 141 LEU H H 7.44 . 1 515 142 HIS H H 7.70 . 1 stop_ save_