data_5514 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone HN, N, Ca and Cb assignment of the GFPuv mutant, an 54 kDa protein ; _BMRB_accession_number 5514 _BMRB_flat_file_name bmr5514.str _Entry_type original _Submission_date 2002-09-09 _Accession_date 2002-09-09 _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 Georgescu Julia . . 2 Rehm Till . . 3 Wiehler Jens . . 4 Steipe Boris . . 5 Holak Tad A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 319 "13C chemical shifts" 536 "15N chemical shifts" 184 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-02-18 original author . stop_ _Original_release_date 2003-02-18 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Letter to the editor: Backbone HN, N, Ca and Cb assignment of the GFPuv mutant' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Georgescu Julia . . 2 Rehm Till . . 3 Wiehler Jens . . 4 Steipe Boris . . 5 Holak Tad A. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 25 _Journal_issue 2 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 161 _Page_last 162 _Year 2003 _Details . loop_ _Keyword 'green fluorescent protein' deuteration chromophore stop_ save_ ################################## # Molecular system description # ################################## save_system_GFPuv _Saveframe_category molecular_system _Mol_system_name GFPuv _Abbreviation_common GFPuv _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'GFPuv mutant, chain A' $GFPuv 'GFPuv mutant, chain B' $GFPuv stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state dimer _System_paramagnetic no _System_thiol_state 'all free' loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component 1 'GFPuv mutant, chain A' 1 'GFPuv mutant, chain B' stop_ _Database_query_date . _Details ; x-ray structure additional mutations: N-terminus A2G, missing S3, random PCR Q80R ; save_ ######################## # Monomeric polymers # ######################## save_GFPuv _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'green fluorescent protein uv' _Name_variant 'A2G, Q80R, F99S, M153T, V163A, missing S3' _Abbreviation_common gfpuv _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 239 _Mol_residue_sequence ; MGKGEELFTGVVPILVELDG DVNGHKFSVSGEGEGDATYG KLTLKFICTTGKLPVPWPTL VTTFSYGVQCFSRYPDHMKR HDFFKSAMPEGYVQERTISF KDDGNYKTRAEVKFEGDTLV NRIELKGIDFKEDGNILGHK LEYNYNSHNVYITADKQKNG IKANFKIRHNIEDGSVQLAD HYQQNTPIGDGPVLLPDNHY LSTQSALSKDPNEKRDHMVL LEFVTAAGITHGMDELYKG ; loop_ _Residue_seq_code _Residue_label 1 MET 2 GLY 3 LYS 4 GLY 5 GLU 6 GLU 7 LEU 8 PHE 9 THR 10 GLY 11 VAL 12 VAL 13 PRO 14 ILE 15 LEU 16 VAL 17 GLU 18 LEU 19 ASP 20 GLY 21 ASP 22 VAL 23 ASN 24 GLY 25 HIS 26 LYS 27 PHE 28 SER 29 VAL 30 SER 31 GLY 32 GLU 33 GLY 34 GLU 35 GLY 36 ASP 37 ALA 38 THR 39 TYR 40 GLY 41 LYS 42 LEU 43 THR 44 LEU 45 LYS 46 PHE 47 ILE 48 CYS 49 THR 50 THR 51 GLY 52 LYS 53 LEU 54 PRO 55 VAL 56 PRO 57 TRP 58 PRO 59 THR 60 LEU 61 VAL 62 THR 63 THR 64 PHE 65 SER 66 TYR 67 GLY 68 VAL 69 GLN 70 CYS 71 PHE 72 SER 73 ARG 74 TYR 75 PRO 76 ASP 77 HIS 78 MET 79 LYS 80 ARG 81 HIS 82 ASP 83 PHE 84 PHE 85 LYS 86 SER 87 ALA 88 MET 89 PRO 90 GLU 91 GLY 92 TYR 93 VAL 94 GLN 95 GLU 96 ARG 97 THR 98 ILE 99 SER 100 PHE 101 LYS 102 ASP 103 ASP 104 GLY 105 ASN 106 TYR 107 LYS 108 THR 109 ARG 110 ALA 111 GLU 112 VAL 113 LYS 114 PHE 115 GLU 116 GLY 117 ASP 118 THR 119 LEU 120 VAL 121 ASN 122 ARG 123 ILE 124 GLU 125 LEU 126 LYS 127 GLY 128 ILE 129 ASP 130 PHE 131 LYS 132 GLU 133 ASP 134 GLY 135 ASN 136 ILE 137 LEU 138 GLY 139 HIS 140 LYS 141 LEU 142 GLU 143 TYR 144 ASN 145 TYR 146 ASN 147 SER 148 HIS 149 ASN 150 VAL 151 TYR 152 ILE 153 THR 154 ALA 155 ASP 156 LYS 157 GLN 158 LYS 159 ASN 160 GLY 161 ILE 162 LYS 163 ALA 164 ASN 165 PHE 166 LYS 167 ILE 168 ARG 169 HIS 170 ASN 171 ILE 172 GLU 173 ASP 174 GLY 175 SER 176 VAL 177 GLN 178 LEU 179 ALA 180 ASP 181 HIS 182 TYR 183 GLN 184 GLN 185 ASN 186 THR 187 PRO 188 ILE 189 GLY 190 ASP 191 GLY 192 PRO 193 VAL 194 LEU 195 LEU 196 PRO 197 ASP 198 ASN 199 HIS 200 TYR 201 LEU 202 SER 203 THR 204 GLN 205 SER 206 ALA 207 LEU 208 SER 209 LYS 210 ASP 211 PRO 212 ASN 213 GLU 214 LYS 215 ARG 216 ASP 217 HIS 218 MET 219 VAL 220 LEU 221 LEU 222 GLU 223 PHE 224 VAL 225 THR 226 ALA 227 ALA 228 GLY 229 ILE 230 THR 231 HIS 232 GLY 233 MET 234 ASP 235 GLU 236 LEU 237 TYR 238 LYS 239 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-28 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 BMRB 5666 GFP 94.98 229 100.00 100.00 2.95e-166 PDB 1B9C "Green Fluorescent Protein Mutant F99s, M153t And V163a" 98.74 236 98.31 98.73 1.76e-168 PDB 1C4F "Green Fluorescent Protein S65t At Ph 4.6" 99.58 236 97.06 97.06 1.94e-167 PDB 1EMB "Green Fluorescent Protein (Gfp) From Aequorea Victoria, Gln 80 Replaced With Arg" 99.58 236 97.06 97.06 1.94e-167 PDB 1EMF "Green Fluorescent Protein From Aequorea Victoria, Mutant" 98.74 237 97.46 97.46 8.60e-167 PDB 1EMG "Green Fluorescent Protein (65-67 Replaced By Cro, S65t Substitution, Q80r)" 99.58 236 97.06 97.06 1.94e-167 PDB 1EMM "Green Fluorescent Protein From Aequorea Victoria, Mutant" 98.74 237 97.03 97.03 4.79e-166 PDB 1GFL "Structure Of Green Fluorescent Protein" 98.74 238 98.73 98.73 4.67e-171 PDB 1KYP "Crystal Structure Of An Apo Green Fluorescent Protein Zn Biosensor" 98.74 237 97.03 97.88 7.10e-166 PDB 1KYR "Crystal Structure Of A Cu-Bound Green Fluorescent Protein Zn Biosensor" 98.74 237 97.03 97.88 7.10e-166 PDB 1KYS "Crystal Structure Of A Zn-Bound Green Fluorescent Protein Biosensor" 98.74 237 97.03 97.88 7.10e-166 PDB 1OXD 'Expansion Of The Genetic Code Enables Design Of A Novel "gold" Class Of Green Fluorescent Proteins' 95.82 227 96.94 96.94 1.24e-159 PDB 1OXE 'Expansion Of The Genetic Code Enables Design Of A Novel "gold" Class Of Green Fluorescent Proteins' 95.82 227 96.94 96.94 1.24e-159 PDB 1Q4A "S65t Q80r Green Fluorescent Protein (Gfp) Ph 8.5" 99.58 236 97.06 97.06 1.94e-167 PDB 1Q4B "S65t Q80r Green Fluorescent Protein (Gfp) Ph 5.5" 99.58 236 97.06 97.06 1.94e-167 PDB 1QXT "Crystal Structure Of Precyclized Intermediate For The Green Fluorescent Protein R96a Variant (A)" 94.98 230 98.24 99.12 9.87e-164 PDB 1QY3 "Crystal Structure Of Precyclized Intermediate For The Green Fluorescent Protein R96a Variant (B)" 95.82 229 97.82 98.69 2.13e-164 PDB 1QYF "Crystal Structure Of Matured Green Fluorescent Protein R96a Variant" 94.98 228 97.36 97.80 1.26e-159 PDB 1QYO "Anaerobic Precylization Intermediate Crystal Structure For S65g Y66g Gfp Variant" 99.58 238 97.90 98.32 1.54e-170 PDB 1QYQ "Crystal Structure Of The Cyclized S65g Y66g Gfp Variant" 98.74 237 97.88 98.31 6.80e-168 PDB 1W7S "Wild-type Aequorea Victoria Green Fluorescent Protein" 99.58 236 97.06 97.06 1.94e-167 PDB 1YHG "Uncyclized Precursor Structure Of S65g Y66s V68g Gfp Variant" 98.74 239 97.88 98.31 4.16e-169 PDB 1YHH "Uncyclized Precursor Structure Of S65a Y66s G67a Gfp Variant" 98.74 239 97.88 98.73 2.14e-170 PDB 1YHI "Uncyclized Precursor Structure Of S65a Y66s R96a Gfp Variant" 98.74 239 98.31 99.15 1.28e-170 PDB 1YJ2 "Cyclized, Non-Dehydrated Post-Translational Product For S65a Y66s H148g Gfp Variant" 98.74 237 97.88 98.31 4.46e-167 PDB 1YJF "Cyclized Post-Translational Product For S65a Y66s (Gfphal) Green Fluorescent Protein Variant" 98.74 237 98.31 98.73 1.02e-168 PDB 2AWJ "Gfp R96m Pre-Cyclized Intermediate In Chromophore Formation" 94.98 230 98.24 99.12 1.20e-163 PDB 2AWK "Gfp R96m Mature Chromophore" 94.98 228 97.36 97.80 1.29e-159 PDB 2AWL "Mature R96k Gfp Mutant" 94.98 228 97.36 98.24 4.56e-160 PDB 2AWM "Gfp R96a Chromophore Maturation Recovery Mutant R96a Q183r" 94.98 228 96.92 97.80 6.09e-159 PDB 2B3Q "Crystal Structure Of A Well-Folded Variant Of Green Fluorescent Protein" 100.00 244 97.91 97.91 7.50e-170 PDB 2EMD "Green Fluorescent Protein From Aequorea Victoria, Mutant" 98.74 237 97.03 97.03 4.79e-166 PDB 2EMN "Green Fluorescent Protein From Aequorea Victoria, Mutant" 98.74 237 97.03 97.03 4.79e-166 PDB 2EMO "Green Fluorescent Protein From Aequorea Victoria, Mutant" 98.74 237 97.46 97.46 8.60e-167 PDB 2FWQ "Reduced Enolate Chromophore Intermediate For Y66h Gfp Variant" 98.74 237 97.46 97.88 2.41e-166 PDB 2FZU "Reduced Enolate Chromophore Intermediate For Gfp Variant" 98.74 237 97.88 98.31 6.80e-168 PDB 2G16 "Structure Of S65a Y66s Gfp Variant After Backbone Fragmentation" 71.55 172 99.42 100.00 1.78e-121 PDB 2G2S "Structure Of S65g Y66s Gfp Variant After Spontaneous Peptide Hydrolysis" 71.97 173 99.42 100.00 3.31e-122 PDB 2G3D "Structure Of S65g Y66a Gfp Variant After Spontaneous Peptide Hydrolysis" 71.97 173 99.42 100.00 2.02e-122 PDB 2G5Z "Structure Of S65g Y66s Gfp Variant After Spontaneous Peptide Hydrolysis And Decarboxylation" 71.97 173 99.42 100.00 3.31e-122 PDB 2G6E "Structure Of Cyclized F64l S65a Y66s Gfp Variant" 98.74 237 97.88 98.31 6.80e-168 PDB 2HCG "Structure Of S65t Y66f Gfp Variant After Cyclization, Carbon-Carbon Bond Cleavage, And Oxygen Incorporation Reactions" 98.74 237 97.88 98.31 6.80e-168 PDB 2HFC "Structure Of S65t Y66f R96a Gfp Variant In Precursor State" 98.74 239 97.88 99.15 2.29e-170 PDB 2HGD "Structure Of S65a Y66f Gfp Variant With An Oxidized Chromophore" 98.74 237 98.31 98.73 1.02e-168 PDB 2HGY "Structure Of S65a Y66f E222a Gfp Variant After Cyclization And Carbon-Carbon Bond Cleavage" 98.74 237 97.88 98.31 7.75e-168 PDB 2QRF "Green Fluorescent Protein: Cyclized-Only Intermediate Of Chromophore Maturation In The Q183e Variant" 96.23 228 96.96 97.83 1.28e-161 PDB 2QT2 "Cyclized-Dehydrated Intermediate Of Gfp Variant Q183e In Chromophore Maturation" 99.58 236 97.06 97.90 4.52e-168 PDB 2QZ0 "Mature Q183e Variant Of Green Fluorescent Protein Chromophore" 94.98 228 97.36 98.24 4.51e-160 PDB 3G9A "Green Fluorescent Protein Bound To Minimizer Nanobody" 99.58 236 98.74 98.74 8.85e-171 PDB 3GJ1 "Non Photoactivated State Of Pa-Gfp" 96.23 229 97.83 97.83 1.57e-162 PDB 3GJ2 "Photoactivated State Of Pa-Gfp" 96.23 229 97.83 97.83 1.57e-162 PDB 3K1K "Green Fluorescent Protein Bound To Minimizer Nanobody" 99.16 236 97.05 97.05 3.00e-165 PDB 4GES "Crystal Structure Of Gfp-Tyr151pyz With An Unnatural Amino Acid Incorporation" 99.58 246 98.32 98.74 1.42e-171 PDB 4P1Q "Green Fluorescent Protein E222h Variant" 96.23 228 98.26 98.26 2.60e-163 DBJ BAA93576 "GFPuv4 [Cloning vector pGFPTA]" 99.58 262 98.32 98.74 3.07e-172 DBJ BAB32740 "red-shift green fluorescent protein-fused neomycin phosphotransferase [Cloning vector pLCPVRGNR104]" 99.16 506 97.05 97.05 2.28e-166 DBJ BAB68313 "codon-optimized GFPmut1 [Expression vector pTub-tel3 GFP3]" 99.58 241 97.06 97.90 1.10e-169 DBJ BAB68314 "codon-optimized GFPmut1 [Expression vector pTub-tel3 GFP4]" 99.58 241 97.06 97.90 1.10e-169 DBJ BAB72232 "green fluorescent protein GFP [Cloning vector pRTHSP70-GFP]" 99.58 238 97.48 98.32 1.06e-170 EMBL CAA10279 "green flourescent protein [Cloning vector pOT1]" 99.58 238 99.58 99.58 1.71e-174 EMBL CAA65278 "green fluorescent protein [unidentified]" 99.58 238 98.74 98.74 1.64e-172 EMBL CAB61435 "green flourescent protein [Integration vector pSMUG+]" 99.58 274 97.90 97.90 6.60e-171 EMBL CAB70975 "green fluorescent protein [Synechocystis promoter probe vector pIGA]" 99.58 238 99.58 99.58 1.71e-174 EMBL CAC27829 "green fluorescent protein [Cloning vector pOT2]" 99.58 238 99.58 99.58 1.71e-174 GB AAA27721 "green-fluorescent protein [Aequorea victoria]" 99.58 238 97.90 98.32 3.44e-171 GB AAA69542 "green fluorescent protein [Cloning vector pGFP-1]" 99.58 242 98.32 98.32 8.21e-172 GB AAA69544 "green fluorescent protein [Cloning vector pGFP-N3]" 99.58 242 98.32 98.32 8.21e-172 GB AAA69546 "green fluorescent protein [Cloning vector pGFP-C3]" 99.58 264 98.74 98.74 2.83e-172 GB AAA69548 "green fluorescent protein [Cloning vector pGFP-N1]" 99.58 242 98.32 98.32 8.21e-172 REF WP_006462513 "green fluorescent protein [Herbaspirillum frisingense]" 99.58 238 97.06 97.90 1.47e-169 REF WP_012569506 "MULTISPECIES: green fluorescent protein [Proteobacteria]" 99.58 238 97.06 97.90 8.12e-170 REF YP_002302326 "green fluorescent protein [Neisseria gonorrhoeae]" 99.58 238 97.06 97.90 8.12e-170 SP P42212 "RecName: Full=Green fluorescent protein [Aequorea victoria]" 99.58 238 97.90 98.32 3.44e-171 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $GFPuv Jellyfish 6100 Eukaryota Metazoa Aequorea victoria 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 $GFPuv 'recombinant technology' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GFPuv . mM 0.8 1.5 [U-15N] stop_ save_ save_sample2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $GFPuv . mM 0.8 1.5 '[U-15N; U-13C; U-70% 2H]' stop_ save_ ############################ # Computer software used # ############################ save_ccnmr-glxcc _Saveframe_category software _Name ccnmr-glxcc _Version . loop_ _Task processing assignment stop_ _Details ; In house developed software: Cieslar, C., Ross, A., Zink, T. and Holak, T. A. (1993) J. Magn. Reson. B 101, 97-101 ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 600 _Details . save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-15N_NOESY_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY HSQC' _Sample_label . save_ save_2D-TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-TOCSY _Sample_label . save_ save_2D_NOESY_in_D2O_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY in D2O' _Sample_label . save_ save_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HNCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_CBCACONH_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-15N NOESY HSQC' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name 2D-TOCSY _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY in D2O' _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_4 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_5 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_6 _Saveframe_category NMR_applied_experiment _Experiment_name CBCACONH _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_Ex-cond _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 na temperature 310 0.5 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 TMS C 13 'methyl protons' ppm . external indirect . external . . ammonia N 15 nitrogen ppm . internal indirect . internal . . 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-15N NOESY HSQC' 2D-TOCSY '2D NOESY in D2O' HNCA HNCO CBCACONH stop_ _Sample_conditions_label $Ex-cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'GFPuv mutant, chain A' _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 . 1 MET CA C 52.79 0.1 1 2 . 1 MET CB C 30.55 0.4 1 3 . 2 GLY H H 8.54 0.02 1 4 . 2 GLY HA2 H 4.22 0.03 2 5 . 2 GLY C C 168.74 0.1 1 6 . 2 GLY CA C 43.59 0.1 1 7 . 2 GLY N N 115.81 0.2 1 8 . 3 LYS H H 8.75 0.04 1 9 . 3 LYS HA H 4.10 0.03 1 10 . 3 LYS C C 169.97 0.1 1 11 . 3 LYS CA C 55.91 0.1 1 12 . 3 LYS CB C 26.36 0.3 1 13 . 3 LYS N N 127.70 0.4 1 14 . 4 GLY H H 8.90 0.02 1 15 . 4 GLY HA2 H 3.68 0.03 2 16 . 4 GLY C C 169.07 0.1 1 17 . 4 GLY CA C 43.34 0.1 1 18 . 4 GLY N N 121.99 0.2 1 19 . 5 GLU H H 8.79 0.03 1 20 . 5 GLU HA H 4.03 0.04 1 21 . 5 GLU C C 170.02 0.1 1 22 . 5 GLU CA C 55.73 0.1 1 23 . 5 GLU CB C 25.89 0.3 1 24 . 5 GLU N N 128.74 0.2 1 25 . 6 GLU H H 8.16 0.02 1 26 . 6 GLU HA H 4.17 0.03 1 27 . 6 GLU C C 167.06 0.2 1 28 . 6 GLU CA C 54.36 0.2 1 29 . 6 GLU CB C 26.18 0.2 1 30 . 6 GLU N N 126.39 0.2 1 31 . 7 LEU H H 7.67 0.03 1 32 . 7 LEU HA H 4.02 0.02 1 33 . 7 LEU C C 168.13 0.1 1 34 . 7 LEU CA C 51.84 0.1 1 35 . 7 LEU CB C 37.77 0.2 1 36 . 7 LEU N N 124.26 0.3 1 37 . 8 PHE H H 7.73 0.03 1 38 . 8 PHE HA H 4.32 0.02 1 39 . 8 PHE C C 168.77 0.1 1 40 . 8 PHE CA C 54.14 0.2 1 41 . 8 PHE CB C 35.86 0.4 1 42 . 8 PHE N N 119.54 0.2 1 43 . 9 THR H H 7.55 0.02 1 44 . 9 THR HA H 4.20 0.03 1 45 . 9 THR C C 169.51 0.1 1 46 . 9 THR CA C 59.84 0.2 1 47 . 9 THR CB C 64.74 0.3 1 48 . 9 THR N N 118.69 0.1 1 49 . 10 GLY H H 8.22 0.02 1 50 . 10 GLY HA2 H 4.55 0.05 2 51 . 10 GLY HA3 H 4.43 0.05 2 52 . 10 GLY C C 171.69 0.1 1 53 . 10 GLY CA C 40.27 0.2 1 54 . 10 GLY N N 116.34 0.2 1 55 . 11 VAL H H 8.31 0.02 1 56 . 11 VAL HA H 4.52 0.05 1 57 . 11 VAL C C 173.45 0.1 1 58 . 11 VAL CA C 59.46 0.2 1 59 . 11 VAL CB C 28.78 0.5 1 60 . 11 VAL N N 129.17 0.1 1 61 . 12 VAL H H 8.08 0.03 1 62 . 12 VAL HA H 4.15 0.04 1 63 . 12 VAL C C 168.92 0.1 1 64 . 12 VAL CA C 55.68 0.2 1 65 . 12 VAL N N 122.13 0.3 1 66 . 14 ILE CA C 55.44 0.4 1 67 . 15 LEU H H 8.90 0.02 1 68 . 15 LEU HA H 5.13 0.02 1 69 . 15 LEU C C 169.71 0.1 1 70 . 15 LEU CA C 50.16 0.2 1 71 . 15 LEU CB C 42.91 0.4 1 72 . 15 LEU N N 139.49 0.2 1 73 . 16 VAL H H 8.78 0.02 1 74 . 16 VAL HA H 5.29 0.03 1 75 . 16 VAL C C 171.07 0.1 1 76 . 16 VAL CA C 56.18 0.1 1 77 . 16 VAL CB C 34.44 0.2 1 78 . 16 VAL N N 131.31 0.1 1 79 . 17 GLU H H 8.92 0.04 1 80 . 17 GLU HA H 5.17 0.02 1 81 . 17 GLU C C 170.97 0.1 1 82 . 17 GLU CA C 51.66 0.1 1 83 . 17 GLU CB C 30.66 0.3 1 84 . 17 GLU N N 135.80 0.3 1 85 . 18 LEU H H 9.24 0.02 1 86 . 18 LEU C C 171.82 0.1 1 87 . 18 LEU CA C 50.47 0.1 1 88 . 18 LEU CB C 40.16 0.2 1 89 . 18 LEU N N 134.09 0.3 1 90 . 19 ASP H H 8.26 0.02 1 91 . 19 ASP C C 171.83 0.1 1 92 . 19 ASP CA C 50.21 0.3 1 93 . 19 ASP CB C 39.81 0.3 1 94 . 19 ASP N N 138.54 0.3 1 95 . 20 GLY H H 8.56 0.02 1 96 . 20 GLY HA2 H 3.74 0.04 2 97 . 20 GLY HA3 H 4.07 0.03 2 98 . 20 GLY C C 171.17 0.1 1 99 . 20 GLY CA C 40.14 0.3 1 100 . 20 GLY N N 114.91 0.2 1 101 . 21 ASP H H 7.18 0.03 1 102 . 21 ASP C C 173.68 0.1 1 103 . 21 ASP CA C 49.76 0.2 1 104 . 21 ASP CB C 40.30 0.3 1 105 . 21 ASP N N 128.07 0.2 1 106 . 22 VAL H H 8.76 0.02 1 107 . 22 VAL HA H 5.11 0.03 1 108 . 22 VAL C C 170.43 0.1 1 109 . 22 VAL CA C 57.02 0.2 1 110 . 22 VAL CB C 30.95 0.3 1 111 . 22 VAL N N 132.39 0.3 1 112 . 23 ASN H H 9.16 0.02 1 113 . 23 ASN HA H 4.48 0.02 1 114 . 23 ASN C C 170.79 0.1 1 115 . 23 ASN CA C 50.72 0.1 1 116 . 23 ASN CB C 33.64 0.4 1 117 . 23 ASN N N 137.49 0.02 1 118 . 24 GLY H H 8.31 0.02 1 119 . 24 GLY HA2 H 4.18 0.02 2 120 . 24 GLY HA3 H 3.89 0.03 2 121 . 24 GLY C C 171.95 0.1 1 122 . 24 GLY CA C 41.97 0.1 1 123 . 24 GLY N N 106.90 0.2 1 124 . 25 HIS H H 8.19 0.02 1 125 . 25 HIS HA H 4.74 0.03 1 126 . 25 HIS C C 171.307 0.1 1 127 . 25 HIS CA C 51.66 0.2 1 128 . 25 HIS CB C 26.02 0.3 1 129 . 25 HIS N N 129.20 0.3 1 130 . 26 LYS H H 8.73 0.03 1 131 . 26 LYS HA H 5.18 0.01 1 132 . 26 LYS C C 170.87 0.1 1 133 . 26 LYS CA C 51.86 0.2 1 134 . 26 LYS CB C 30.2 0.3 1 135 . 26 LYS N N 135.87 0.3 1 136 . 27 PHE H H 8.53 0.02 1 137 . 27 PHE HA H 5.18 0.04 1 138 . 27 PHE C C 168.71 0.1 1 139 . 27 PHE CA C 52.12 0.3 1 140 . 27 PHE CB C 37.79 0.3 1 141 . 27 PHE N N 125.56 0.2 1 142 . 28 SER H H 8.00 0.03 1 143 . 28 SER HA H 5.14 0.02 1 144 . 28 SER C C 173.28 0.1 1 145 . 28 SER CA C 53.69 0.2 1 146 . 28 SER CB C 62.06 0.4 1 147 . 28 SER N N 120.40 0.03 1 148 . 29 VAL H H 9.17 0.02 1 149 . 29 VAL HA H 5.39 0.03 1 150 . 29 VAL C C 172.67 0.1 1 151 . 29 VAL CA C 56.63 0.1 1 152 . 29 VAL CB C 34.37 0.4 1 153 . 29 VAL N N 131.10 0.2 1 154 . 30 SER H H 8.89 0.03 1 155 . 30 SER HA H 5.14 0.02 1 156 . 30 SER C C 171.42 0.1 1 157 . 30 SER CA C 53.13 0.2 1 158 . 30 SER CB C 61.82 0.3 1 159 . 30 SER N N 130.9 0.4 1 160 . 31 GLY H H 9.89 0.03 1 161 . 31 GLY HA2 H 4.09 0.02 2 162 . 31 GLY HA3 H 3.91 0.03 2 163 . 31 GLY C C 172.08 0.1 1 164 . 31 GLY CA C 41.66 0.2 1 165 . 31 GLY N N 117.27 0.3 1 166 . 32 GLU H H 8.25 0.03 1 167 . 32 GLU C C 174.14 0.1 1 168 . 32 GLU CA C 50.45 0.1 1 169 . 32 GLU CB C 30.43 0.3 1 170 . 32 GLU N N 123.95 0.04 1 171 . 33 GLY H H 8.22 0.02 1 172 . 33 GLY HA2 H 3.63 0.02 2 173 . 33 GLY HA3 H 3.46 0.03 2 174 . 33 GLY C C 170.43 0.1 1 175 . 33 GLY CA C 42.26 0.1 1 176 . 33 GLY N N 113.89 0.2 1 177 . 34 GLU H H 8.88 0.04 1 178 . 34 GLU HA H 4.46 0.03 1 179 . 34 GLU C C 173.52 0.1 1 180 . 34 GLU CA C 51.33 0.2 1 181 . 34 GLU CB C 30.19 0.3 1 182 . 34 GLU N N 129.85 0.4 1 183 . 35 GLY H H 8.85 0.02 1 184 . 35 GLY HA2 H 4.01 0.03 2 185 . 35 GLY C C 171.77 0.1 1 186 . 35 GLY CA C 40.25 0.2 1 187 . 35 GLY N N 112.27 0.2 1 188 . 36 ASP H H 9.01 0.04 1 189 . 36 ASP C C 174.19 0.1 1 190 . 36 ASP CA C 48.62 0.1 1 191 . 36 ASP CB C 39.30 0.4 1 192 . 36 ASP N N 130.40 0.4 1 193 . 37 ALA H H 10.79 0.02 1 194 . 37 ALA C C 168.25 0.1 1 195 . 37 ALA CA C 50.23 0.2 1 196 . 37 ALA CB C 17.19 0.4 1 197 . 37 ALA N N 141.34 0.2 1 198 . 38 THR H H 9.13 0.02 1 199 . 38 THR HA H 4.26 0.03 1 200 . 38 THR C C 167.22 0.1 1 201 . 38 THR CA C 62.58 0.1 1 202 . 38 THR CB C 64.45 1 1 203 . 38 THR N N 122.10 0.2 1 204 . 39 TYR H H 7.17 0.03 1 205 . 39 TYR C C 170.59 0.1 1 206 . 39 TYR CA C 54.49 0.2 1 207 . 39 TYR N N 122.98 0.3 1 208 . 40 GLY H H 8.67 0.02 1 209 . 40 GLY HA2 H 3.91 0.02 2 210 . 40 GLY HA3 H 3.74 0.03 2 211 . 40 GLY C C 168.99 0.1 1 212 . 40 GLY CA C 42.98 0.2 1 213 . 40 GLY N N 116.96 0.2 1 214 . 41 LYS H H 8.45 0.02 1 215 . 41 LYS C C 173.02 0.1 1 216 . 41 LYS CA C 52.07 0.2 1 217 . 41 LYS N N 127.24 0.2 1 218 . 42 LEU CA C 50.46 0.1 1 219 . 42 LEU CB C 42.41 0.2 1 220 . 43 THR H H 8.10 0.03 1 221 . 43 THR HA H 3.99 0.03 1 222 . 43 THR C C 170.53 0.1 1 223 . 43 THR CA C 56.62 0.1 1 224 . 43 THR CB C 66.33 0.4 1 225 . 43 THR N N 121.05 0.3 1 226 . 44 LEU H H 8.97 0.03 1 227 . 44 LEU HA H 4.56 0.02 1 228 . 44 LEU C C 171.97 0.1 1 229 . 44 LEU CA C 55.24 0.1 1 230 . 44 LEU N N 134.94 0.03 1 231 . 46 PHE CA C 52.32 0.2 1 232 . 46 PHE CB C 39.7 0.4 1 233 . 47 ILE H H 9.36 0.02 1 234 . 47 ILE HA H 4.95 0.04 1 235 . 47 ILE C C 171.42 0.1 1 236 . 47 ILE CA C 55.50 0.1 1 237 . 47 ILE CB C 36.68 0.3 1 238 . 47 ILE N N 125.68 0.2 1 239 . 48 CYS H H 9.28 0.03 1 240 . 48 CYS HA H 5.03 0.04 1 241 . 48 CYS C C 168.62 0.1 1 242 . 48 CYS CA C 51.91 0.3 1 243 . 48 CYS N N 133.69 0.4 1 244 . 49 THR H H 8.28 0.02 1 245 . 49 THR HA H 4.06 0.03 1 246 . 49 THR C C 168.27 0.1 1 247 . 49 THR CA C 59.63 0.2 1 248 . 49 THR CB C 64.01 0.3 1 249 . 49 THR N N 121.23 0.2 1 250 . 50 THR H H 8.13 0.02 1 251 . 50 THR HA H 4.59 0.04 1 252 . 50 THR C C 169.81 0.1 1 253 . 50 THR CA C 57.55 0.2 1 254 . 50 THR CB C 64.92 0.3 1 255 . 50 THR N N 114.60 0.2 1 256 . 51 GLY H H 7.48 0.03 1 257 . 51 GLY HA2 H 3.52 0.03 2 258 . 51 GLY HA3 H 3.65 0.04 2 259 . 51 GLY C C 171.67 0.1 1 260 . 51 GLY CA C 41.76 0.1 1 261 . 51 GLY N N 115.12 0.3 1 262 . 52 LYS H H 8.51 0.03 1 263 . 52 LYS HA H 4.43 0.03 1 264 . 52 LYS C C 173.54 0.1 1 265 . 52 LYS CA C 50.99 0.2 1 266 . 52 LYS CB C 29.92 0.3 1 267 . 52 LYS N N 135.14 0.3 1 268 . 53 LEU H H 9.58 0.02 1 269 . 53 LEU HA H 4.66 0.03 1 270 . 53 LEU C C 168.43 0.1 1 271 . 53 LEU CA C 49.55 0.2 1 272 . 53 LEU N N 144.55 0.2 1 273 . 54 PRO CA C 60.04 0.1 1 274 . 54 PRO CB C 28.22 0.3 1 275 . 55 VAL H H 6.21 0.02 1 276 . 55 VAL C C 170.79 0.1 1 277 . 55 VAL CA C 52.59 0.2 1 278 . 55 VAL N N 110.34 0.2 1 279 . 58 PRO CA C 61.73 0.3 1 280 . 58 PRO CB C 29.33 0.3 1 281 . 59 THR H H 7.77 0.02 1 282 . 59 THR C C 166.16 0.1 1 283 . 59 THR CA C 60.64 0.2 1 284 . 59 THR CB C 64.69 0.3 1 285 . 59 THR N N 105.51 0.2 1 286 . 60 LEU H H 7.71 0.03 1 287 . 60 LEU HA H 4.29 0.02 1 288 . 60 LEU C C 171.41 0.1 1 289 . 60 LEU CA C 50.68 0.2 1 290 . 60 LEU CB C 39.79 0.3 1 291 . 60 LEU N N 127.06 0.3 1 292 . 61 VAL H H 6.95 0.02 1 293 . 61 VAL HA H 4.57 0.03 1 294 . 61 VAL C C 169.97 0.1 1 295 . 61 VAL CA C 65.11 0.2 1 296 . 61 VAL N N 127.17 0.2 1 297 . 62 THR H H 7.89 0.03 1 298 . 62 THR HA H 4.58 0.03 1 299 . 62 THR C C 170.07 0.2 1 300 . 62 THR CA C 59.4 0.1 1 301 . 62 THR CB C 64.37 0.3 1 302 . 62 THR N N 108.07 0.3 1 303 . 63 THR H H 7.39 0.03 1 304 . 63 THR HA H 4.69 0.04 1 305 . 63 THR C C 168.74 0.2 1 306 . 63 THR CA C 63.05 0.1 1 307 . 63 THR N N 128.84 0.03 1 308 . 64 PHE H H 7.71 0.04 1 309 . 64 PHE C C 170.96 0.1 1 310 . 64 PHE CA C 53.44 0.1 1 311 . 64 PHE CB C 37.71 0.4 1 312 . 64 PHE N N 123.73 0.4 1 313 . 65 SER H H 8.47 0.03 1 314 . 65 SER C C 170.23 0.2 1 315 . 65 SER CA C 45.13 0.3 1 316 . 65 SER N N 115.67 0.3 1 317 . 69 GLN CA C 54.21 0.2 1 318 . 69 GLN CB C 25.43 0.3 1 319 . 70 CYS H H 7.33 0.04 1 320 . 70 CYS C C 168.58 0.1 1 321 . 70 CYS CA C 53.40 0.1 1 322 . 70 CYS CB C 24.44 0.4 1 323 . 70 CYS N N 122.05 0.3 1 324 . 71 PHE H H 7.74 0.04 1 325 . 71 PHE C C 173.32 0.1 1 326 . 71 PHE CA C 57.07 0.2 1 327 . 71 PHE CB C 34.84 0.4 1 328 . 71 PHE N N 124.07 0.4 1 329 . 72 SER H H 6.76 0.02 1 330 . 72 SER C C 173.57 0.1 1 331 . 72 SER CA C 55.49 0.1 1 332 . 72 SER N N 114.51 0.2 1 333 . 73 ARG CA C 52.29 0.1 1 334 . 73 ARG CB C 25.84 0.2 1 335 . 74 TYR CA C 51.35 0.1 1 336 . 74 TYR C C 174.67 0.2 1 337 . 74 TYR H H 8.51 0.1 1 338 . 74 TYR N N 120.37 0.2 1 339 . 77 HIS H H 8.19 0.04 1 340 . 77 HIS C C 170.06 0.1 1 341 . 77 HIS CA C 54.32 0.2 1 342 . 77 HIS N N 124.13 0.4 1 343 . 78 MET H H 8.18 0.04 1 344 . 78 MET C C 171.18 0.1 1 345 . 78 MET CA C 51.10 0.2 1 346 . 78 MET CB C 30.55 0.3 1 347 . 78 MET N N 124.59 0.4 1 348 . 79 LYS H H 7.37 0.03 1 349 . 79 LYS C C 169.97 0.1 1 350 . 79 LYS CA C 56.79 0.1 1 351 . 79 LYS CB C 29.16 0.3 1 352 . 79 LYS N N 129.30 0.3 1 353 . 80 ARG H H 8.25 0.04 1 354 . 80 ARG C C 167.44 0.1 1 355 . 80 ARG CA C 53.21 0.1 1 356 . 80 ARG CB C 25.11 0.4 1 357 . 80 ARG N N 122.99 0.4 1 358 . 81 HIS H H 7.73 0.02 1 359 . 81 HIS HA H 4.12 0.03 1 360 . 81 HIS C C 171.92 0.1 1 361 . 81 HIS CA C 51.28 0.2 1 362 . 81 HIS CB C 27.89 0.3 1 363 . 81 HIS N N 121.07 0.2 1 364 . 82 ASP H H 6.65 0.02 1 365 . 82 ASP HA H 4.58 0.03 1 366 . 82 ASP C C 171.88 0.1 1 367 . 82 ASP CA C 48.29 0.2 1 368 . 82 ASP CB C 34.72 0.4 1 369 . 82 ASP N N 125.89 0.2 1 370 . 83 PHE H H 8.33 0.02 1 371 . 83 PHE C C 170.73 0.1 1 372 . 83 PHE CA C 56.48 0.2 1 373 . 83 PHE CB C 37.37 0.4 1 374 . 83 PHE N N 136.01 0.2 1 375 . 84 PHE H H 6.95 0.03 1 376 . 84 PHE C C 168.45 0.1 1 377 . 84 PHE CA C 56.01 0.1 1 378 . 84 PHE N N 118.30 0.3 1 379 . 85 LYS H H 7.43 0.04 1 380 . 85 LYS HA H 4.02 0.03 1 381 . 85 LYS C C 168.21 0.1 1 382 . 85 LYS CA C 55.95 0.2 1 383 . 85 LYS N N 117.36 0.4 1 384 . 86 SER H H 7.05 0.02 1 385 . 86 SER HA H 4.29 0.03 1 386 . 86 SER C C 166.71 0.1 1 387 . 86 SER CA C 57.10 0.1 1 388 . 86 SER CB C 59.10 0.3 1 389 . 86 SER N N 120.67 0.2 1 390 . 87 ALA H H 6.81 0.02 1 391 . 87 ALA HA H 4.33 0.03 1 392 . 87 ALA C C 171.77 0.1 1 393 . 87 ALA CA C 48.17 0.1 1 394 . 87 ALA CB C 16.06 0.3 1 395 . 87 ALA N N 128.55 0.2 1 396 . 88 MET H H 7.77 0.03 1 397 . 88 MET C C 168.99 0.1 1 398 . 88 MET CA C 49.12 0.2 1 399 . 88 MET N N 122.04 0.3 1 400 . 90 GLU CA C 57.99 0.2 1 401 . 90 GLU CB C 25.68 0.4 1 402 . 91 GLY H H 8.71 0.02 1 403 . 91 GLY HA2 H 3.92 0.02 2 404 . 91 GLY C C 168.52 0.1 1 405 . 91 GLY CA C 41.45 0.1 1 406 . 91 GLY N N 101.75 0.2 1 407 . 92 TYR H H 8.86 0.03 1 408 . 92 TYR HA H 4.72 0.03 1 409 . 92 TYR C C 171.19 0.1 1 410 . 92 TYR CA C 51.27 0.2 1 411 . 92 TYR CB C 37.98 0.3 1 412 . 92 TYR N N 116.73 0.3 1 413 . 93 VAL H H 9.66 0.03 1 414 . 93 VAL HA H 4.94 0.03 1 415 . 93 VAL C C 172.60 0.1 1 416 . 93 VAL CA C 57.32 0.1 1 417 . 93 VAL CB C 29.30 0.3 1 418 . 93 VAL N N 129.02 0.3 1 419 . 94 GLN H H 9.78 0.02 1 420 . 94 GLN HA H 5.02 0.03 1 421 . 94 GLN C C 169.03 0.1 1 422 . 94 GLN CA C 51.37 0.1 1 423 . 94 GLN N N 139.55 0.2 1 424 . 95 GLU CA C 51.47 0.1 1 425 . 95 GLU CB C 28.59 0.3 1 426 . 96 ARG H H 7.88 0.03 1 427 . 96 ARG CA C 55.18 0.1 1 428 . 96 ARG CB C 24.12 0.3 1 429 . 96 ARG N N 133.63 0.3 1 430 . 97 THR H H 8.67 0.03 1 431 . 97 THR HA H 4.63 0.03 1 432 . 97 THR C C 170.51 0.1 1 433 . 97 THR CA C 59.66 0.1 1 434 . 97 THR CB C 66.61 0.3 1 435 . 97 THR N N 130.23 0.3 1 436 . 98 ILE H H 9.63 0.02 1 437 . 98 ILE HA H 4.99 0.04 1 438 . 98 ILE C C 172.29 0.1 1 439 . 98 ILE CA C 55.98 0.2 1 440 . 98 ILE N N 138.12 0.2 1 441 . 99 SER H H 8.90 0.03 1 442 . 99 SER HA H 4.62 0.03 1 443 . 99 SER C C 171.05 0.2 1 444 . 99 SER CA C 52.54 0.2 1 445 . 99 SER CB C 59.62 0.4 1 446 . 99 SER N N 130.23 0.3 1 447 . 100 PHE H H 8.70 0.02 1 448 . 100 PHE HA H 4.82 0.03 1 449 . 100 PHE C C 170.97 0.1 1 450 . 100 PHE CA C 54.39 0.1 1 451 . 100 PHE CB C 38.48 0.3 1 452 . 100 PHE N N 139.02 0.2 1 453 . 101 LYS H H 7.83 0.02 1 454 . 101 LYS HA H 4.73 0.04 1 455 . 101 LYS C C 170.96 0.2 1 456 . 101 LYS CA C 54.60 0.1 1 457 . 101 LYS CB C 29.09 0.3 1 458 . 101 LYS N N 137.49 0.2 1 459 . 102 ASP H H 9.26 0.03 1 460 . 102 ASP HA H 4.39 0.03 1 461 . 102 ASP C C 168.69 0.1 1 462 . 102 ASP CA C 52.51 0.1 1 463 . 102 ASP CB C 36.54 0.5 1 464 . 102 ASP N N 130.44 0.3 1 465 . 103 ASP H H 8.69 0.02 1 466 . 103 ASP HA H 4.87 0.02 1 467 . 103 ASP C C 171.68 0.1 1 468 . 103 ASP CA C 49.81 0.1 1 469 . 103 ASP CB C 40.57 0.3 1 470 . 103 ASP N N 131.73 0.3 1 471 . 104 GLY H H 7.85 0.02 1 472 . 104 GLY HA2 H 3.69 0.03 2 473 . 104 GLY C C 168.88 0.1 1 474 . 104 GLY CA C 40.38 0.1 1 475 . 104 GLY N N 111.83 0.2 1 476 . 105 ASN H H 7.89 0.02 1 477 . 105 ASN C C 174.68 0.1 1 478 . 105 ASN CA C 47.71 0.1 1 479 . 105 ASN CB C 39.84 0.3 1 480 . 105 ASN N N 116.34 0.2 1 481 . 106 TYR H H 9.62 0.02 1 482 . 106 TYR HA H 4.73 0.03 1 483 . 106 TYR C C 170.24 0.1 1 484 . 106 TYR CA C 49.11 0.2 1 485 . 106 TYR CB C 37.15 0.3 1 486 . 106 TYR N N 123.53 0.2 1 487 . 107 LYS H H 9.46 0.02 1 488 . 107 LYS HA H 5.39 0.04 1 489 . 107 LYS C C 170.32 0.1 1 490 . 107 LYS CA C 51.85 0.1 1 491 . 107 LYS CB C 31.14 0.4 1 492 . 107 LYS N N 131.29 0.5 1 493 . 108 THR H H 9.33 0.02 1 494 . 108 THR HA H 4.09 0.03 1 495 . 108 THR C C 168.79 0.1 1 496 . 108 THR CA C 55.50 0.1 1 497 . 108 THR CB C 66.75 0.3 1 498 . 108 THR N N 120.68 0.2 1 499 . 109 ARG H H 8.79 0.04 1 500 . 109 ARG C C 172.05 0.1 1 501 . 109 ARG CA C 52.98 0.1 1 502 . 109 ARG CB C 29.29 0.3 1 503 . 109 ARG N N 132.79 0.4 1 504 . 110 ALA H H 9.18 0.02 1 505 . 110 ALA HA H 4.47 0.03 1 506 . 110 ALA C C 172.42 0.1 1 507 . 110 ALA CA C 46.04 0.2 1 508 . 110 ALA CB C 22.12 0.3 1 509 . 110 ALA N N 142.81 0.2 1 510 . 111 GLU H H 8.65 0.04 1 511 . 111 GLU C C 169.57 0.1 1 512 . 111 GLU CA C 52.02 0.2 1 513 . 111 GLU CB C 29.21 0.4 1 514 . 111 GLU N N 127.07 0.4 1 515 . 112 VAL H H 8.76 0.03 1 516 . 112 VAL HA H 5.21 0.04 1 517 . 112 VAL C C 171.40 0.1 1 518 . 112 VAL CA C 56.85 0.1 1 519 . 112 VAL CB C 28.48 0.4 1 520 . 112 VAL N N 135.49 0.3 1 521 . 113 LYS H H 8.68 0.03 1 522 . 113 LYS HA H 3.92 0.04 1 523 . 113 LYS C C 173.23 0.1 1 524 . 113 LYS CA C 51.14 0.2 1 525 . 113 LYS CB C 31.98 0.3 1 526 . 113 LYS N N 127.74 0.3 1 527 . 114 PHE H H 7.73 0.02 1 528 . 114 PHE C C 171.37 0.2 1 529 . 114 PHE CA C 55.46 0.1 1 530 . 114 PHE CB C 41.94 0.3 1 531 . 114 PHE N N 125.12 0.2 1 532 . 115 GLU H H 8.37 0.02 1 533 . 115 GLU C C 172.15 0.1 1 534 . 115 GLU CA C 52.05 0.1 1 535 . 115 GLU CB C 31.04 0.2 1 536 . 115 GLU N N 135.32 0.2 1 537 . 116 GLY H H 8.28 0.02 1 538 . 116 GLY HA2 H 3.99 0.04 2 539 . 116 GLY HA3 H 4.05 0.04 2 540 . 116 GLY C C 168.71 0.1 1 541 . 116 GLY CA C 43.36 0.1 1 542 . 116 GLY N N 115.64 0.2 1 543 . 117 ASP H H 8.59 0.04 1 544 . 117 ASP HA H 4.45 0.04 1 545 . 117 ASP C C 171.58 0.1 1 546 . 117 ASP CA C 50.45 0.1 1 547 . 117 ASP CB C 37.95 0.3 1 548 . 117 ASP N N 135.79 0.4 1 549 . 118 THR H H 7.73 0.02 1 550 . 118 THR HA H 4.07 0.04 1 551 . 118 THR C C 170.61 0.1 1 552 . 118 THR CA C 58.27 0.1 1 553 . 118 THR CB C 67.46 0.2 1 554 . 118 THR N N 121.06 0.2 1 555 . 119 LEU H H 8.64 0.02 1 556 . 119 LEU HA H 4.05 0.03 1 557 . 119 LEU C C 174.46 0.2 1 558 . 119 LEU CA C 49.01 0.2 1 559 . 119 LEU CB C 37.71 0.4 1 560 . 119 LEU N N 141.91 0.2 1 561 . 120 VAL H H 9.05 0.04 1 562 . 120 VAL HA H 3.89 0.03 1 563 . 120 VAL C C 171.33 0.1 1 564 . 120 VAL CA C 56.39 0.1 1 565 . 120 VAL CB C 30.92 0.4 1 566 . 120 VAL N N 134.76 0.4 1 567 . 121 ASN H H 8.64 0.03 1 568 . 121 ASN C C 171.79 0.2 1 569 . 121 ASN CA C 47.30 0.2 1 570 . 121 ASN CB C 37.14 0.3 1 571 . 121 ASN N N 131.10 0.3 1 572 . 122 ARG H H 8.71 0.03 1 573 . 122 ARG HA H 4.69 0.03 1 574 . 122 ARG C C 171.60 0.2 1 575 . 122 ARG CA C 52.28 0.1 1 576 . 122 ARG CB C 28.44 0.2 1 577 . 122 ARG N N 134.49 0.3 1 578 . 123 ILE H H 9.41 0.02 1 579 . 123 ILE HA H 4.96 0.04 1 580 . 123 ILE C C 169.23 0.1 1 581 . 123 ILE CA C 57.77 0.1 1 582 . 123 ILE CB C 40.15 0.4 1 583 . 123 ILE N N 133.06 0.2 1 584 . 124 GLU H H 9.10 0.03 1 585 . 124 GLU HA H 5.17 0.03 1 586 . 124 GLU C C 170.06 0.1 1 587 . 124 GLU CA C 51.59 0.2 1 588 . 124 GLU CB C 29.64 0.4 1 589 . 124 GLU N N 137.59 0.3 1 590 . 125 LEU H H 8.64 0.02 1 591 . 125 LEU HA H 5.02 0.03 1 592 . 125 LEU C C 171.24 0.1 1 593 . 125 LEU CA C 50.47 0.1 1 594 . 125 LEU CB C 42.93 0.3 1 595 . 125 LEU N N 136.66 0.2 1 596 . 126 LYS H H 9.18 0.02 1 597 . 126 LYS HA H 5.37 0.03 1 598 . 126 LYS C C 171.24 0.1 1 599 . 126 LYS CA C 50.91 0.1 1 600 . 126 LYS CB C 32.15 0.3 1 601 . 126 LYS N N 139.67 0.2 1 602 . 127 GLY H H 10.37 0.02 1 603 . 127 GLY HA2 H 4.76 0.03 2 604 . 127 GLY HA3 H 4.49 0.04 2 605 . 127 GLY C C 170.24 0.1 1 606 . 127 GLY CA C 41.72 0.1 1 607 . 127 GLY N N 121.33 0.2 1 608 . 128 ILE H H 9.20 0.03 1 609 . 128 ILE C C 173.36 0.1 1 610 . 128 ILE CA C 56.18 0.2 1 611 . 128 ILE N N 134.02 0.3 1 612 . 129 ASP CA C 50.18 0.2 1 613 . 129 ASP CB C 38.08 0.4 1 614 . 130 PHE H H 8.99 0.03 1 615 . 130 PHE HA H 4.72 0.02 1 616 . 130 PHE C C 170.05 0.1 1 617 . 130 PHE CA C 50.67 0.2 1 618 . 130 PHE N N 128.99 0.3 1 619 . 131 LYS CA C 56.85 0.2 1 620 . 131 LYS CB C 31.17 0.4 1 621 . 132 GLU H H 8.48 0.03 1 622 . 132 GLU HA H 4.57 0.03 1 623 . 132 GLU C C 170.76 0.1 1 624 . 132 GLU CA C 51.33 0.1 1 625 . 132 GLU CB C 26.11 0.4 1 626 . 132 GLU N N 128.98 0.3 1 627 . 133 ASP H H 8.34 0.04 1 628 . 133 ASP HA H 4.44 0.03 1 629 . 133 ASP C C 170.34 0.1 1 630 . 133 ASP CA C 48.65 0.2 1 631 . 133 ASP CB C 36.48 0.3 1 632 . 133 ASP N N 119.56 0.4 1 633 . 134 GLY H H 7.22 0.02 1 634 . 134 GLY HA2 H 3.77 0.02 2 635 . 134 GLY HA3 H 3.92 0.03 2 636 . 134 GLY C C 169.11 0.1 1 637 . 134 GLY CA C 40.39 0.2 1 638 . 134 GLY N N 107.02 0.2 1 639 . 135 ASN H H 9.24 0.02 1 640 . 135 ASN HA H 4.44 0.03 1 641 . 135 ASN C C 171.33 0.1 1 642 . 135 ASN CA C 51.83 0.1 1 643 . 135 ASN CB C 35.20 0.4 1 644 . 135 ASN N N 120.19 0.2 1 645 . 136 ILE H H 7.20 0.02 1 646 . 136 ILE HA H 4.35 0.03 1 647 . 136 ILE C C 170.59 0.1 1 648 . 136 ILE CA C 60.23 0.1 1 649 . 136 ILE N N 122.57 0.2 1 650 . 137 LEU H H 9.07 0.02 1 651 . 137 LEU HA H 3.92 0.03 1 652 . 137 LEU C C 169.42 0.1 1 653 . 137 LEU CA C 52.75 0.1 1 654 . 137 LEU CB C 35.96 0.5 1 655 . 137 LEU N N 124.87 0.2 1 656 . 138 GLY H H 7.22 0.02 1 657 . 138 GLY HA2 H 3.77 0.02 2 658 . 138 GLY HA3 H 3.93 0.03 2 659 . 138 GLY C C 167.38 0.1 1 660 . 138 GLY CA C 41.11 0.1 1 661 . 138 GLY N N 105.40 0.2 1 662 . 139 HIS H H 7.57 0.02 1 663 . 139 HIS HA H 4.35 0.02 1 664 . 139 HIS C C 171.78 0.1 1 665 . 139 HIS CA C 54.24 0.1 1 666 . 139 HIS CB C 25.18 0.4 1 667 . 139 HIS N N 122.55 0.2 1 668 . 140 LYS H H 7.95 0.03 1 669 . 140 LYS HA H 3.79 0.03 1 670 . 140 LYS C C 170.51 0.1 1 671 . 140 LYS CA C 51.16 0.1 1 672 . 140 LYS CB C 29.34 0.4 1 673 . 140 LYS N N 120.66 0.3 1 674 . 141 LEU H H 7.21 0.03 1 675 . 141 LEU HA H 4.68 0.04 1 676 . 141 LEU C C 170.07 0.1 1 677 . 141 LEU CA C 51.86 0.1 1 678 . 141 LEU CB C 38.19 0.3 1 679 . 141 LEU N N 125.91 0.3 1 680 . 142 GLU H H 8.39 0.02 1 681 . 142 GLU C C 169.25 0.1 1 682 . 142 GLU CA C 52.75 0.2 1 683 . 142 GLU N N 133.72 0.2 1 684 . 143 TYR H H 9.30 0.02 1 685 . 143 TYR C C 169.97 0.1 1 686 . 143 TYR CA C 51.89 0.2 1 687 . 143 TYR N N 134.53 0.2 1 688 . 144 ASN CA C 52.16 0.2 1 689 . 145 TYR H H 9.23 0.02 1 690 . 145 TYR C C 169.72 0.1 1 691 . 145 TYR CA C 51.70 0.3 1 692 . 145 TYR CB C 39.12 0.4 1 693 . 145 TYR N N 144.96 0.2 1 694 . 146 ASN H H 8.69 0.03 1 695 . 146 ASN C C 172.75 0.2 1 696 . 146 ASN CA C 48.84 0.2 1 697 . 146 ASN N N 122.09 0.3 1 698 . 147 SER H H 9.34 0.02 1 699 . 147 SER C C 168.17 0.2 1 700 . 147 SER CA C 53.45 0.2 1 701 . 147 SER N N 130.26 0.2 1 702 . 151 TYR CA C 56.09 0.2 1 703 . 151 TYR CB C 34.65 0.4 1 704 . 152 ILE H H 8.92 0.03 1 705 . 152 ILE C C 170.51 0.1 1 706 . 152 ILE CA C 56.69 0.1 1 707 . 152 ILE N N 136.46 0.3 1 708 . 153 THR H H 8.85 0.02 1 709 . 153 THR CA C 55.92 0.2 1 710 . 153 THR CB C 67.75 0.3 1 711 . 153 THR N N 126.47 0.2 1 712 . 154 ALA H H 9.13 0.03 1 713 . 154 ALA HA H 4.09 0.02 1 714 . 154 ALA C C 173.33 0.1 1 715 . 154 ALA CA C 49.08 0.1 1 716 . 154 ALA CB C 17.04 0.3 1 717 . 154 ALA N N 134.86 0.3 1 718 . 155 ASP H H 8.93 0.04 1 719 . 155 ASP C C 168.99 0.1 1 720 . 155 ASP CA C 48.62 0.2 1 721 . 155 ASP N N 131.03 0.4 1 722 . 156 LYS H H 8.81 0.04 1 723 . 156 LYS HA H 4.31 0.03 1 724 . 156 LYS C C 171.76 0.2 1 725 . 156 LYS CA C 54.61 0.1 1 726 . 156 LYS N N 119.97 0.4 1 727 . 157 GLN CA C 54.57 0.2 1 728 . 158 LYS H H 7.31 0.03 1 729 . 158 LYS C C 170.15 0.1 1 730 . 158 LYS CA C 51.17 0.2 1 731 . 158 LYS CB C 29.38 0.3 1 732 . 158 LYS N N 122.52 0.3 1 733 . 159 ASN H H 7.97 0.03 1 734 . 159 ASN HA H 4.35 0.03 1 735 . 159 ASN C C 170.25 0.1 1 736 . 159 ASN CA C 50.40 0.2 1 737 . 159 ASN CB C 34.84 0.4 1 738 . 159 ASN N N 125.29 0.3 1 739 . 160 GLY H H 7.37 0.02 1 740 . 160 GLY HA2 H 4.19 0.03 2 741 . 160 GLY HA3 H 4.04 0.04 2 742 . 160 GLY C C 173.63 0.1 1 743 . 160 GLY CA C 41.08 0.1 1 744 . 160 GLY N N 100.28 0.2 1 745 . 161 ILE H H 7.69 0.03 1 746 . 161 ILE HA H 4.97 0.03 1 747 . 161 ILE C C 172.69 0.1 1 748 . 161 ILE CA C 54.59 0.2 1 749 . 161 ILE CB C 39.32 0.3 1 750 . 161 ILE N N 114.63 0.3 1 751 . 162 LYS H H 9.21 0.02 1 752 . 162 LYS HA H 5.26 0.04 1 753 . 162 LYS C C 171.25 0.1 1 754 . 162 LYS CA C 50.86 0.3 1 755 . 162 LYS CB C 33.38 0.3 1 756 . 162 LYS N N 128.32 0.2 1 757 . 163 ALA H H 8.83 0.02 1 758 . 163 ALA HA H 5.86 0.04 1 759 . 163 ALA C C 171.23 0.1 1 760 . 163 ALA CA C 46.74 0.1 1 761 . 163 ALA CB C 19.96 0.3 1 762 . 163 ALA N N 127.30 0.2 1 763 . 164 ASN H H 8.67 0.02 1 764 . 164 ASN HA H 5.64 0.04 1 765 . 164 ASN C C 169.80 0.1 1 766 . 164 ASN CA C 49.44 0.2 1 767 . 164 ASN CB C 39.49 0.3 1 768 . 164 ASN N N 123.78 0.2 1 769 . 165 PHE H H 8.20 0.04 1 770 . 165 PHE C C 173.14 0.1 1 771 . 165 PHE CA C 53.20 0.2 1 772 . 165 PHE N N 122.17 0.4 1 773 . 166 LYS H H 8.67 0.04 1 774 . 166 LYS C C 171.12 0.1 1 775 . 166 LYS CA C 51.37 0.2 1 776 . 166 LYS N N 128.09 0.4 1 777 . 167 ILE H H 8.68 0.04 1 778 . 167 ILE C C 170.05 0.1 1 779 . 167 ILE CA C 55.58 0.1 1 780 . 167 ILE CB C 28.90 0.3 1 781 . 167 ILE N N 134.98 0.4 1 782 . 168 ARG CA C 54.53 0.2 1 783 . 170 ASN CA C 58.74 0.1 1 784 . 170 ASN CB C 29.21 0.3 1 785 . 171 ILE H H 8.23 0.03 1 786 . 171 ILE HA H 4.93 0.04 1 787 . 171 ILE C C 170.79 0.1 1 788 . 171 ILE CA C 55.53 0.1 1 789 . 171 ILE CB C 33.83 0.3 1 790 . 171 ILE N N 126.82 0.3 1 791 . 172 GLU H H 8.57 0.02 1 792 . 172 GLU HA H 4.24 0.03 1 793 . 172 GLU C C 168.71 0.1 1 794 . 172 GLU CA C 55.28 0.2 1 795 . 172 GLU CB C 26.60 0.4 1 796 . 172 GLU N N 133.65 0.2 1 797 . 173 ASP H H 7.45 0.02 1 798 . 173 ASP HA H 4.60 0.03 1 799 . 173 ASP C C 170.14 0.1 1 800 . 173 ASP CA C 50.01 0.1 1 801 . 173 ASP CB C 36.81 0.3 1 802 . 173 ASP N N 124.78 0.2 1 803 . 174 GLY H H 8.37 0.02 1 804 . 174 GLY HA2 H 3.89 0.03 2 805 . 174 GLY HA3 H 3.64 0.04 2 806 . 174 GLY C C 168.68 0.1 1 807 . 174 GLY CA C 41.35 0.2 1 808 . 174 GLY N N 112.88 0.2 1 809 . 175 SER H H 8.13 0.04 1 810 . 175 SER HA H 4.44 0.03 1 811 . 175 SER C C 170.51 0.1 1 812 . 175 SER CA C 54.32 0.1 1 813 . 175 SER CB C 60.05 0.4 1 814 . 175 SER N N 124.28 0.4 1 815 . 176 VAL H H 8.22 0.04 1 816 . 176 VAL HA H 4.69 0.04 1 817 . 176 VAL C C 171.96 0.1 1 818 . 176 VAL CA C 57.07 0.2 1 819 . 176 VAL CB C 32.56 0.3 1 820 . 176 VAL N N 122.42 0.4 1 821 . 177 GLN H H 9.49 0.02 1 822 . 177 GLN C C 170.79 0.1 1 823 . 177 GLN CA C 49.28 0.2 1 824 . 177 GLN CB C 28.60 0.4 1 825 . 177 GLN N N 137.09 0.2 1 826 . 178 LEU H H 9.06 0.02 1 827 . 178 LEU HA H 4.96 0.04 1 828 . 178 LEU C C 171.33 0.1 1 829 . 178 LEU CA C 50.83 0.2 1 830 . 178 LEU CB C 40.47 0.3 1 831 . 178 LEU N N 141.71 0.2 1 832 . 179 ALA H H 9.30 1 1 833 . 179 ALA HA H 4.84 0.04 1 834 . 179 ALA C C 167.26 0.1 1 835 . 179 ALA CA C 46.79 0.1 1 836 . 179 ALA CB C 18.36 0.4 1 837 . 179 ALA N N 135.83 0.2 1 838 . 180 ASP H H 8.93 0.02 1 839 . 180 ASP HA H 4.62 0.04 1 840 . 180 ASP C C 168.37 0.1 1 841 . 180 ASP CA C 52.16 0.2 1 842 . 180 ASP CB C 38.62 0.3 1 843 . 180 ASP N N 143.52 0.2 1 844 . 181 HIS H H 9.26 0.02 1 845 . 181 HIS HA H 4.95 0.05 1 846 . 181 HIS C C 170.88 0.1 1 847 . 181 HIS CA C 52.19 0.2 1 848 . 181 HIS CB C 26.69 0.4 1 849 . 181 HIS N N 131.76 0.2 1 850 . 182 TYR H H 8.53 0.03 1 851 . 182 TYR HA H 4.60 0.03 1 852 . 182 TYR C C 172.50 0.1 1 853 . 182 TYR CA C 53.66 0.2 1 854 . 182 TYR CB C 36.23 0.4 1 855 . 182 TYR N N 131.96 0.3 1 856 . 183 GLN H H 8.72 0.02 1 857 . 183 GLN C C 171.33 0.1 1 858 . 183 GLN CA C 49.91 0.2 1 859 . 183 GLN CB C 30.42 0.4 1 860 . 183 GLN N N 137.31 0.2 1 861 . 184 GLN H H 9.24 0.03 1 862 . 184 GLN HA H 5.26 0.04 1 863 . 184 GLN C C 170.30 0.1 1 864 . 184 GLN CA C 51.30 0.2 1 865 . 184 GLN CB C 29.85 0.3 1 866 . 184 GLN N N 133.23 0.3 1 867 . 185 ASN H H 8.94 0.04 1 868 . 185 ASN HA H 4.20 0.03 1 869 . 185 ASN C C 171.25 0.1 1 870 . 185 ASN CA C 48.62 0.1 1 871 . 185 ASN N N 129.86 0.4 1 872 . 187 PRO CA C 59.76 0.2 1 873 . 187 PRO CB C 29.09 0.4 1 874 . 188 ILE H H 8.86 0.04 1 875 . 188 ILE HA H 4.32 0.03 1 876 . 188 ILE C C 168.92 0.1 1 877 . 188 ILE CA C 60.27 0.2 1 878 . 188 ILE CB C 35.34 0.3 1 879 . 188 ILE N N 133.27 0.4 1 880 . 189 GLY H H 9.33 0.02 1 881 . 189 GLY HA2 H 3.88 0.03 2 882 . 189 GLY HA3 H 3.96 0.04 2 883 . 189 GLY C C 168.17 0.1 1 884 . 189 GLY CA C 40.33 0.2 1 885 . 189 GLY N N 114.08 0.2 1 886 . 190 ASP H H 8.38 0.03 1 887 . 190 ASP HA H 3.91 0.03 1 888 . 190 ASP C C 172.27 0.1 1 889 . 190 ASP CA C 50.01 0.1 1 890 . 190 ASP CB C 38.19 0.3 1 891 . 190 ASP N N 123.94 0.3 1 892 . 191 GLY H H 8.41 0.02 1 893 . 191 GLY HA2 H 3.27 0.02 2 894 . 191 GLY HA3 H 3.96 0.03 2 895 . 191 GLY C C 168.63 0.1 1 896 . 191 GLY CA C 40.81 0.2 1 897 . 191 GLY N N 113.88 0.2 1 898 . 192 PRO CA C 59.35 0.1 1 899 . 192 PRO CB C 28.59 0.3 1 900 . 193 VAL CA C 55.27 0.1 1 901 . 193 VAL C C 169.19 0.3 1 902 . 193 VAL H H 9.14 0.1 1 903 . 193 VAL N N 143.29 0.3 1 904 . 193 VAL CB C 30.06 0.4 1 905 . 194 LEU C C 167.49 0.2 1 906 . 194 LEU CA C 50.29 0.2 1 907 . 194 LEU CB C 37.75 0.5 1 908 . 195 LEU H H 8.04 0.03 1 909 . 195 LEU C C 171.05 0.2 1 910 . 195 LEU CA C 46.36 0.2 1 911 . 195 LEU N N 129.39 0.3 1 912 . 199 HIS H H 8.69 0.04 1 913 . 199 HIS C C 171.61 0.1 1 914 . 199 HIS CA C 57.78 0.1 1 915 . 199 HIS N N 130.24 0.4 1 916 . 200 TYR H H 7.65 0.03 1 917 . 200 TYR C C 170.97 0.1 1 918 . 200 TYR CA C 56.66 0.1 1 919 . 200 TYR CB C 38.43 0.4 1 920 . 200 TYR N N 137.14 0.3 1 921 . 201 LEU H H 8.99 0.04 1 922 . 201 LEU C C 169.88 0.1 1 923 . 201 LEU CA C 50.22 0.1 1 924 . 201 LEU N N 135.45 0.4 1 925 . 206 ALA CA C 47.29 0.1 1 926 . 206 ALA CB C 19.52 0.2 1 927 . 207 LEU H H 9.08 0.03 1 928 . 207 LEU C C 172.13 0.2 1 929 . 207 LEU CA C 49.10 0.1 1 930 . 207 LEU N N 131.51 0.3 1 931 . 214 LYS H H 8.29 0.03 1 932 . 214 LYS C C 169.06 0.1 1 933 . 214 LYS CA C 49.30 0.2 1 934 . 214 LYS CB C 35.99 0.4 1 935 . 214 LYS N N 119.33 0.3 1 936 . 215 ARG H H 8.81 0.02 1 937 . 215 ARG C C 171.43 0.1 1 938 . 215 ARG CA C 51.15 0.2 1 939 . 215 ARG CB C 30.56 0.4 1 940 . 215 ARG N N 125.27 0.2 1 941 . 216 ASP C C 169.89 0.1 1 942 . 216 ASP CA C 52.07 0.1 1 943 . 216 ASP CB C 38.14 0.4 1 944 . 217 HIS H H 8.39 0.02 1 945 . 217 HIS C C 169.25 0.1 1 946 . 217 HIS CA C 52.76 0.2 1 947 . 217 HIS CB C 29.69 0.3 1 948 . 217 HIS N N 133.72 0.2 1 949 . 218 MET H H 7.78 0.03 1 950 . 218 MET C C 176.13 0.1 1 951 . 218 MET CA C 51.08 0.3 1 952 . 218 MET CB C 34.71 0.4 1 953 . 218 MET N N 122.04 0.3 1 954 . 219 VAL H H 7.62 0.03 1 955 . 219 VAL C C 171.96 0.1 1 956 . 219 VAL CA C 58.47 0.2 1 957 . 219 VAL CB C 29.18 0.3 1 958 . 219 VAL N N 136.63 0.3 1 959 . 220 LEU H H 9.40 0.02 1 960 . 220 LEU HA H 4.99 0.03 1 961 . 220 LEU C C 172.69 0.1 1 962 . 220 LEU CA C 49.77 0.1 1 963 . 220 LEU CB C 43.61 0.5 1 964 . 220 LEU N N 141.22 0.2 1 965 . 221 LEU H H 8.54 0.02 1 966 . 221 LEU HA H 5.17 0.03 1 967 . 221 LEU C C 172.87 0.1 1 968 . 221 LEU CA C 49.84 0.2 1 969 . 221 LEU N N 140.68 0.2 1 970 . 222 GLU CA C 51.14 0.3 1 971 . 222 GLU CB C 31.66 0.4 1 972 . 223 PHE H H 9.05 0.02 1 973 . 223 PHE C C 171.52 0.1 1 974 . 223 PHE CA C 52.28 0.1 1 975 . 223 PHE N N 133.75 0.2 1 976 . 224 VAL H H 9.61 0.02 1 977 . 224 VAL C C 169.51 0.1 1 978 . 224 VAL CA C 56.87 0.1 1 979 . 224 VAL CB C 31.14 0.4 1 980 . 224 VAL N N 132.82 0.2 1 981 . 225 THR H H 8.47 0.02 1 982 . 225 THR HA H 5.13 0.04 1 983 . 225 THR C C 170.76 0.1 1 984 . 225 THR CA C 56.09 0.1 1 985 . 225 THR CB C 67.71 0.2 1 986 . 225 THR N N 128.96 0.2 1 987 . 226 ALA H H 8.29 0.02 1 988 . 226 ALA HA H 4.71 0.03 1 989 . 226 ALA C C 173.59 0.1 1 990 . 226 ALA CA C 47.62 0.1 1 991 . 226 ALA CB C 16.18 0.3 1 992 . 226 ALA N N 138.79 0.2 1 993 . 227 ALA H H 8.82 0.04 1 994 . 227 ALA HA H 4.39 0.02 1 995 . 227 ALA C C 170.24 0.1 1 996 . 227 ALA CA C 47.72 0.1 1 997 . 227 ALA CB C 18.96 0.2 1 998 . 227 ALA N N 130.23 0.4 1 999 . 228 GLY H H 8.22 0.02 1 1000 . 228 GLY HA2 H 3.87 0.03 2 1001 . 228 GLY HA3 H 3.91 0.04 2 1002 . 228 GLY C C 170.15 0.1 1 1003 . 228 GLY CA C 41.69 0.1 1 1004 . 228 GLY N N 105.84 0.2 1 1005 . 229 ILE H H 7.24 0.02 1 1006 . 229 ILE C C 171.87 0.1 1 1007 . 229 ILE CA C 56.72 0.1 1 1008 . 229 ILE N N 126.35 0.2 1 1009 . 230 THR CA C 51.61 0.2 1 1010 . 230 THR CB C 65.73 0.4 1 1011 . 231 HIS H H 8.02 0.02 1 1012 . 231 HIS C C 170.83 0.2 1 1013 . 231 HIS CA C 52.13 0.3 1 1014 . 231 HIS CB C 29.77 0.2 1 1015 . 231 HIS N N 136.48 0.2 1 1016 . 232 GLY H H 7.43 0.02 1 1017 . 232 GLY C C 170.24 0.2 1 1018 . 232 GLY CA C 42.38 0.2 1 1019 . 232 GLY N N 121.52 0.2 1 1020 . 233 MET CA C 52.22 0.1 1 1021 . 233 MET CB C 29.5 0.4 1 1022 . 234 ASP H H 8.43 0.04 1 1023 . 234 ASP C C 169.79 0.1 1 1024 . 234 ASP CA C 51.04 0.1 1 1025 . 234 ASP N N 128.56 0.4 1 1026 . 235 GLU H H 8.26 0.02 1 1027 . 235 GLU C C 171.85 0.1 1 1028 . 235 GLU CA C 52.65 0.1 1 1029 . 235 GLU CB C 27.06 0.3 1 1030 . 235 GLU N N 127.89 0.2 1 1031 . 236 LEU H H 8.09 0.04 1 1032 . 236 LEU C C 169.97 0.1 1 1033 . 236 LEU CA C 51.35 0.1 1 1034 . 236 LEU CB C 38.99 0.3 1 1035 . 236 LEU N N 131.07 0.4 1 1036 . 237 TYR H H 7.59 0.02 1 1037 . 237 TYR C C 169.97 0.1 1 1038 . 237 TYR CA C 55.24 0.1 1 1039 . 237 TYR N N 134.19 0.2 1 stop_ save_