data_5514 #Corrected using PDB structure: 1YJFA # #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 # 43 T HA 3.95 4.88 # 53 L HA 4.62 3.70 # 61 V HA 4.53 3.64 # 82 D HA 4.54 3.67 # 92 Y HA 4.68 5.39 #106 Y HA 4.69 5.68 #108 T HA 4.05 5.17 #110 A HA 4.43 5.36 #113 K HA 3.88 4.77 #118 T HA 4.03 4.79 #120 V HA 3.85 4.88 #140 K HA 3.75 4.72 #182 Y HA 4.56 5.32 #185 N HA 4.16 5.75 #190 D HA 3.87 4.73 # #After reference correction, the following residues still #have a CA chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 44 L CA 58.47 52.45 #170 N CA 61.97 53.48 #199 H CA 61.01 55.44 #214 K CA 52.53 57.68 #230 T CA 54.84 61.89 # #After reference correction, the following residues still #have a CB chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 96 R CB 27.10 35.40 #167 I CB 31.88 39.61 #170 N CB 32.19 39.59 #214 K CB 38.97 32.92 # #After reference correction, the following residues still #have a CO chemical shift difference (obs*-pred) greater than 5.0ppm: #NUM AA CS Observed* Predicted # 6 E C 169.82 179.02 # 7 L C 170.89 177.51 # 37 A C 171.01 180.08 # 59 T C 168.92 175.43 # 61 V C 172.73 177.74 # 79 K C 172.73 178.54 # 84 F C 171.21 177.53 # 85 K C 170.97 179.62 # 86 S C 169.47 175.64 #137 L C 172.18 178.49 #172 E C 171.47 177.34 #188 I C 171.68 177.04 #194 L C 170.25 176.23 #214 K C 171.82 177.79 #218 M C 178.89 173.41 # #After reference correction, the following residues still #have a N chemical shift difference (obs*-pred) greater than 10.0ppm: #NUM AA CS Observed* Predicted # 12 V N 116.89 127.95 # 53 L N 139.31 129.14 # 74 Y N 115.13 126.00 #110 A N 137.57 127.51 #128 I N 128.78 117.37 #145 Y N 139.72 116.91 #160 G N 95.04 105.13 #180 D N 138.28 122.31 #193 V N 138.05 113.35 #200 Y N 131.90 115.36 #201 L N 130.21 120.08 #214 K N 114.09 126.19 #231 H N 131.24 118.74 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.04 3.23 2.98 2.76 -5.24 0.06 # #bmr5514.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr5514.str file): #HA CA CB CO N HN #N/A +3.11 +3.11 +2.76 -5.24 N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.04 +/-0.15 +/-0.21 +/-0.25 +/-0.47 +/-0.05 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.641 0.943 0.989 -0.082 0.828 0.746 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.179 0.971 1.169 1.329 2.628 0.300 # ####################### # 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 ; 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_ _BMRB_accession_number 5514 _BMRB_flat_file_name bmr5514.str _Entry_type new _Submission_date 2002-09-09 _Accession_date 2002-09-09 _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' 319 '15N chemical shifts' 184 '13C chemical shifts' 536 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Letter to the editor: Backbone HN, N, Ca and Cb assignment of the GFPuv mutant ; _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 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 _Page_first 161 _Page_last 162 _Year 2003 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_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_ loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1B9C ? ; x-ray structure additional mutations: N-terminus A2G, missing S3, random PCR Q80R ; stop_ _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 _Mol_thiol_state 'all free' ############################## # 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 2004-07-29 _Sequence_homology_query_revised_last_date 2004-03-03 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1QY3 "A Chain A, Crystal Structure Of PrecyclizedIntermediate For The Green Fluorescent Protein R96aVariant (B)" 104.37 229 98 99 10e-131 PDB 1QXT "A Chain A, Crystal Structure Of PrecyclizedIntermediate For The Green Fluorescent Protein R96aVariant (A)" 103.91 230 98 99 10e-131 PDB 1B9C "A Chain A, Green Fluorescent Protein MutantF99s, M153t And V163a" 101.27 236 98 99 10e-135 PDB 1QYQ "A Chain A, Crystal Structure Of The CyclizedS65g Y66g Gfp Variant" 100.84 237 98 98 1e-133 PDB 1GFL "A Chain A, Structure Of Green FluorescentProtein" 100.42 238 99 99 10e-137 PDB 1QYO "A Chain A, Anaerobic PrecylizationIntermediate Crystal Structure For S65g Y66g Gfp Variant" 100.00 239 98 99 10e-136 DBJ BAB20665.1 "GFPuv4 [Cloning vector pCA24N]" 99.17 241 99 99 10e-137 DBJ BAA93576.1 "GFPuv4 [Cloning vector pGFPTA]" 91.22 262 98 99 10e-138 EMBL CAA10279.1 "green flourescent protein [Cloningvector pOT1]" 100.42 238 100 100 1e-138 EMBL CAB70975.1 "green fluorescent protein [Synechocystispromoter probe vector pIGA]" 100.42 238 100 100 1e-138 EMBL CAC27829.1 "green fluorescent protein [Cloningvector pOT2]" 100.42 238 100 100 1e-138 EMBL CAA65278.1 "green fluorescent protein [unidentified]" 100.42 238 99 99 10e-138 EMBL CAB61435.1 "green flourescent protein [Integrationvector pSMUG+]" 87.23 274 98 98 10e-137 GenBank AAB06048.1 GFPuv 100.42 238 100 100 1e-138 GenBank AAB16957.1 "soluble-modified green fluorescentprotein [Cloning vector pSMGFP]" 100.42 238 100 100 1e-138 GenBank AAB16958.1 "soluble-modified red-shifted greenfluorescent protein [Cloning vector pSMRSGFP]" 100.42 238 99 100 1e-138 GenBank AAB65663.1 "green fluorescent protein [Cloning vectorpGFPCR]" 100.42 238 100 100 1e-138 GenBank AAF65229.1 "FLARE16-S [Plastid transformation vectorpMSK51]" 45.96 520 100 100 1e-138 SWISS-PROT P42212 "GFP_AEQVI Green fluorescent protein" 100.42 238 98 98 10e-137 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 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 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 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 save_ save_NMR_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 750 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; 1H-15N NOESY HSQC 2D-TOCSY 2D NOESY in D2O HNCA HNCO CBCACONH ; save_ ####################### # Sample conditions # ####################### save_Ex-cond _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.0 0.1 n/a temperature 310 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio 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 # # # # 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_shift_set_1 _Saveframe_category assigned_chemical_shifts loop_ _Sample_label $sample1 $sample2 stop_ _Sample_conditions_label $Ex-cond _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "GFPuv mutant, chain A" 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 MET CA C 55.90 0.1 1 2 1 MET CB C 33.66 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 171.50 0.1 1 6 2 GLY CA C 46.70 0.1 1 7 2 GLY N N 110.57 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 172.73 0.1 1 11 3 LYS CA C 59.02 0.1 1 12 3 LYS CB C 29.47 0.3 1 13 3 LYS N N 122.46 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 171.83 0.1 1 17 4 GLY CA C 46.45 0.1 1 18 4 GLY N N 116.75 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 172.78 0.1 1 22 5 GLU CA C 58.84 0.1 1 23 5 GLU CB C 29.00 0.3 1 24 5 GLU N N 123.50 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 169.82 0.2 1 28 6 GLU CA C 57.47 0.2 1 29 6 GLU CB C 29.29 0.2 1 30 6 GLU N N 121.15 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 170.89 0.1 1 34 7 LEU CA C 54.95 0.1 1 35 7 LEU CB C 40.88 0.2 1 36 7 LEU N N 119.02 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 171.53 0.1 1 40 8 PHE CA C 57.25 0.2 1 41 8 PHE CB C 38.97 0.4 1 42 8 PHE N N 114.30 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 172.27 0.1 1 46 9 THR CA C 62.95 0.2 1 47 9 THR CB C 67.85 0.3 1 48 9 THR N N 113.45 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 174.45 0.1 1 53 10 GLY CA C 43.38 0.2 1 54 10 GLY N N 111.10 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 176.21 0.1 1 58 11 VAL CA C 62.57 0.2 1 59 11 VAL CB C 31.89 0.5 1 60 11 VAL N N 123.93 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 171.68 0.1 1 64 12 VAL CA C 58.79 0.2 1 65 12 VAL N N 116.89 0.3 1 66 14 ILE CA C 58.55 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 172.47 0.1 1 70 15 LEU CA C 53.27 0.2 1 71 15 LEU CB C 46.02 0.4 1 72 15 LEU N N 134.25 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 173.83 0.1 1 76 16 VAL CA C 59.29 0.1 1 77 16 VAL CB C 37.55 0.2 1 78 16 VAL N N 126.07 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 173.73 0.1 1 82 17 GLU CA C 54.77 0.1 1 83 17 GLU CB C 33.77 0.3 1 84 17 GLU N N 130.56 0.3 1 85 18 LEU H H 9.24 0.02 1 86 18 LEU C C 174.58 0.1 1 87 18 LEU CA C 53.58 0.1 1 88 18 LEU CB C 43.27 0.2 1 89 18 LEU N N 128.85 0.3 1 90 19 ASP H H 8.26 0.02 1 91 19 ASP C C 174.59 0.1 1 92 19 ASP CA C 53.32 0.3 1 93 19 ASP CB C 42.92 0.3 1 94 19 ASP N N 133.30 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 173.93 0.1 1 99 20 GLY CA C 43.25 0.3 1 100 20 GLY N N 109.67 0.2 1 101 21 ASP H H 7.18 0.03 1 102 21 ASP C C 176.44 0.1 1 103 21 ASP CA C 52.87 0.2 1 104 21 ASP CB C 43.41 0.3 1 105 21 ASP N N 122.83 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 173.19 0.1 1 109 22 VAL CA C 60.13 0.2 1 110 22 VAL CB C 34.06 0.3 1 111 22 VAL N N 127.15 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 173.55 0.1 1 115 23 ASN CA C 53.83 0.1 1 116 23 ASN CB C 36.75 0.4 1 117 23 ASN N N 132.25 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 174.71 0.1 1 122 24 GLY CA C 45.08 0.1 1 123 24 GLY N N 101.66 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 174.06 0.1 1 127 25 HIS CA C 54.77 0.2 1 128 25 HIS CB C 29.13 0.3 1 129 25 HIS N N 123.96 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 173.63 0.1 1 133 26 LYS CA C 54.97 0.2 1 134 26 LYS CB C 33.31 0.3 1 135 26 LYS N N 130.63 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 171.47 0.1 1 139 27 PHE CA C 55.23 0.3 1 140 27 PHE CB C 40.90 0.3 1 141 27 PHE N N 120.32 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 176.04 0.1 1 145 28 SER CA C 56.80 0.2 1 146 28 SER CB C 65.17 0.4 1 147 28 SER N N 115.16 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 175.43 0.1 1 151 29 VAL CA C 59.74 0.1 1 152 29 VAL CB C 37.48 0.4 1 153 29 VAL N N 125.86 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 174.18 0.1 1 157 30 SER CA C 56.24 0.2 1 158 30 SER CB C 64.93 0.3 1 159 30 SER N N 125.66 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 174.84 0.1 1 164 31 GLY CA C 44.77 0.2 1 165 31 GLY N N 112.03 0.3 1 166 32 GLU H H 8.25 0.03 1 167 32 GLU C C 176.90 0.1 1 168 32 GLU CA C 53.56 0.1 1 169 32 GLU CB C 33.54 0.3 1 170 32 GLU N N 118.71 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 173.19 0.1 1 175 33 GLY CA C 45.37 0.1 1 176 33 GLY N N 108.65 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 176.28 0.1 1 180 34 GLU CA C 54.44 0.2 1 181 34 GLU CB C 33.30 0.3 1 182 34 GLU N N 124.61 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 174.53 0.1 1 186 35 GLY CA C 43.36 0.2 1 187 35 GLY N N 107.03 0.2 1 188 36 ASP H H 9.01 0.04 1 189 36 ASP C C 176.95 0.1 1 190 36 ASP CA C 51.73 0.1 1 191 36 ASP CB C 42.41 0.4 1 192 36 ASP N N 125.16 0.4 1 193 37 ALA H H 10.79 0.02 1 194 37 ALA C C 171.01 0.1 1 195 37 ALA CA C 53.34 0.2 1 196 37 ALA CB C 20.30 0.4 1 197 37 ALA N N 136.10 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 169.98 0.1 1 201 38 THR CA C 65.69 0.1 1 202 38 THR CB C 67.56 1 1 203 38 THR N N 116.86 0.2 1 204 39 TYR H H 7.17 0.03 1 205 39 TYR C C 173.35 0.1 1 206 39 TYR CA C 57.60 0.2 1 207 39 TYR N N 117.74 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 171.75 0.1 1 212 40 GLY CA C 46.09 0.2 1 213 40 GLY N N 111.72 0.2 1 214 41 LYS H H 8.45 0.02 1 215 41 LYS C C 175.78 0.1 1 216 41 LYS CA C 55.18 0.2 1 217 41 LYS N N 122.00 0.2 1 218 42 LEU CA C 53.57 0.1 1 219 42 LEU CB C 45.52 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 173.29 0.1 1 223 43 THR CA C 59.73 0.1 1 224 43 THR CB C 69.44 0.4 1 225 43 THR N N 115.81 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 174.73 0.1 1 229 44 LEU CA C 58.35 0.1 1 230 44 LEU N N 129.70 0.03 1 231 46 PHE CA C 55.43 0.2 1 232 46 PHE CB C 42.81 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 174.18 0.1 1 236 47 ILE CA C 58.61 0.1 1 237 47 ILE CB C 39.79 0.3 1 238 47 ILE N N 120.44 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 171.38 0.1 1 242 48 CYS CA C 55.02 0.3 1 243 48 CYS N N 128.45 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 171.03 0.1 1 247 49 THR CA C 62.74 0.2 1 248 49 THR CB C 67.12 0.3 1 249 49 THR N N 115.99 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 172.57 0.1 1 253 50 THR CA C 60.66 0.2 1 254 50 THR CB C 68.03 0.3 1 255 50 THR N N 109.36 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 174.43 0.1 1 260 51 GLY CA C 44.87 0.1 1 261 51 GLY N N 109.88 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 176.30 0.1 1 265 52 LYS CA C 54.10 0.2 1 266 52 LYS CB C 33.03 0.3 1 267 52 LYS N N 129.90 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 171.19 0.1 1 271 53 LEU CA C 52.66 0.2 1 272 53 LEU N N 139.31 0.2 1 273 54 PRO CA C 63.15 0.1 1 274 54 PRO CB C 31.33 0.3 1 275 55 VAL H H 6.21 0.02 1 276 55 VAL C C 173.55 0.1 1 277 55 VAL CA C 55.70 0.2 1 278 55 VAL N N 105.10 0.2 1 279 58 PRO CA C 64.84 0.3 1 280 58 PRO CB C 32.44 0.3 1 281 59 THR H H 7.77 0.02 1 282 59 THR C C 168.92 0.1 1 283 59 THR CA C 63.75 0.2 1 284 59 THR CB C 67.80 0.3 1 285 59 THR N N 100.27 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 174.17 0.1 1 289 60 LEU CA C 53.79 0.2 1 290 60 LEU CB C 42.90 0.3 1 291 60 LEU N N 121.82 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 172.73 0.1 1 295 61 VAL CA C 68.22 0.2 1 296 61 VAL N N 121.93 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 172.83 0.2 1 300 62 THR CA C 62.51 0.1 1 301 62 THR CB C 67.48 0.3 1 302 62 THR N N 102.83 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 171.50 0.2 1 306 63 THR CA C 66.16 0.1 1 307 63 THR N N 123.60 0.03 1 308 64 PHE H H 7.71 0.04 1 309 64 PHE C C 173.72 0.1 1 310 64 PHE CA C 56.55 0.1 1 311 64 PHE CB C 40.82 0.4 1 312 64 PHE N N 118.49 0.4 1 313 65 SER H H 8.47 0.03 1 314 65 SER C C 172.99 0.2 1 315 65 SER CA C 48.24 0.3 1 316 65 SER N N 110.43 0.3 1 317 69 GLN CA C 57.32 0.2 1 318 69 GLN CB C 28.54 0.3 1 319 70 CYS H H 7.33 0.04 1 320 70 CYS C C 171.34 0.1 1 321 70 CYS CA C 56.51 0.1 1 322 70 CYS CB C 27.55 0.4 1 323 70 CYS N N 116.81 0.3 1 324 71 PHE H H 7.74 0.04 1 325 71 PHE C C 176.08 0.1 1 326 71 PHE CA C 60.18 0.2 1 327 71 PHE CB C 37.95 0.4 1 328 71 PHE N N 118.83 0.4 1 329 72 SER H H 6.76 0.02 1 330 72 SER C C 176.33 0.1 1 331 72 SER CA C 58.60 0.1 1 332 72 SER N N 109.27 0.2 1 333 73 ARG CA C 55.40 0.1 1 334 73 ARG CB C 28.95 0.2 1 335 74 TYR CA C 54.46 0.1 1 336 74 TYR C C 177.43 0.2 1 337 74 TYR H H 8.51 0.1 1 338 74 TYR N N 115.13 0.2 1 339 77 HIS H H 8.19 0.04 1 340 77 HIS C C 172.82 0.1 1 341 77 HIS CA C 57.43 0.2 1 342 77 HIS N N 118.89 0.4 1 343 78 MET H H 8.18 0.04 1 344 78 MET C C 173.94 0.1 1 345 78 MET CA C 54.21 0.2 1 346 78 MET CB C 33.66 0.3 1 347 78 MET N N 119.35 0.4 1 348 79 LYS H H 7.37 0.03 1 349 79 LYS C C 172.73 0.1 1 350 79 LYS CA C 59.90 0.1 1 351 79 LYS CB C 32.27 0.3 1 352 79 LYS N N 124.06 0.3 1 353 80 ARG H H 8.25 0.04 1 354 80 ARG C C 170.20 0.1 1 355 80 ARG CA C 56.32 0.1 1 356 80 ARG CB C 28.22 0.4 1 357 80 ARG N N 117.75 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 174.68 0.1 1 361 81 HIS CA C 54.39 0.2 1 362 81 HIS CB C 31.00 0.3 1 363 81 HIS N N 115.83 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 174.64 0.1 1 367 82 ASP CA C 51.40 0.2 1 368 82 ASP CB C 37.83 0.4 1 369 82 ASP N N 120.65 0.2 1 370 83 PHE H H 8.33 0.02 1 371 83 PHE C C 173.49 0.1 1 372 83 PHE CA C 59.59 0.2 1 373 83 PHE CB C 40.48 0.4 1 374 83 PHE N N 130.77 0.2 1 375 84 PHE H H 6.95 0.03 1 376 84 PHE C C 171.21 0.1 1 377 84 PHE CA C 59.12 0.1 1 378 84 PHE N N 113.06 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 170.97 0.1 1 382 85 LYS CA C 59.06 0.2 1 383 85 LYS N N 112.12 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 169.47 0.1 1 387 86 SER CA C 60.21 0.1 1 388 86 SER CB C 62.21 0.3 1 389 86 SER N N 115.43 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 174.53 0.1 1 393 87 ALA CA C 51.28 0.1 1 394 87 ALA CB C 19.17 0.3 1 395 87 ALA N N 123.31 0.2 1 396 88 MET H H 7.77 0.03 1 397 88 MET C C 171.75 0.1 1 398 88 MET CA C 52.23 0.2 1 399 88 MET N N 116.80 0.3 1 400 90 GLU CA C 61.10 0.2 1 401 90 GLU CB C 28.79 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 171.28 0.1 1 405 91 GLY CA C 44.56 0.1 1 406 91 GLY N N 96.51 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 173.95 0.1 1 410 92 TYR CA C 54.38 0.2 1 411 92 TYR CB C 41.09 0.3 1 412 92 TYR N N 111.49 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 175.36 0.1 1 416 93 VAL CA C 60.43 0.1 1 417 93 VAL CB C 32.41 0.3 1 418 93 VAL N N 123.78 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 171.79 0.1 1 422 94 GLN CA C 54.48 0.1 1 423 94 GLN N N 134.31 0.2 1 424 95 GLU CA C 54.58 0.1 1 425 95 GLU CB C 31.70 0.3 1 426 96 ARG H H 7.88 0.03 1 427 96 ARG CA C 58.29 0.1 1 428 96 ARG CB C 27.23 0.3 1 429 96 ARG N N 128.39 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 173.27 0.1 1 433 97 THR CA C 62.77 0.1 1 434 97 THR CB C 69.72 0.3 1 435 97 THR N N 124.99 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 175.05 0.1 1 439 98 ILE CA C 59.09 0.2 1 440 98 ILE N N 132.88 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 173.81 0.2 1 444 99 SER CA C 55.65 0.2 1 445 99 SER CB C 62.73 0.4 1 446 99 SER N N 124.99 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 173.73 0.1 1 450 100 PHE CA C 57.50 0.1 1 451 100 PHE CB C 41.59 0.3 1 452 100 PHE N N 133.78 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 173.72 0.2 1 456 101 LYS CA C 57.71 0.1 1 457 101 LYS CB C 32.20 0.3 1 458 101 LYS N N 132.25 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 171.45 0.1 1 462 102 ASP CA C 55.62 0.1 1 463 102 ASP CB C 39.65 0.5 1 464 102 ASP N N 125.20 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 174.44 0.1 1 468 103 ASP CA C 52.92 0.1 1 469 103 ASP CB C 43.68 0.3 1 470 103 ASP N N 126.49 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 171.64 0.1 1 474 104 GLY CA C 43.49 0.1 1 475 104 GLY N N 106.59 0.2 1 476 105 ASN H H 7.89 0.02 1 477 105 ASN C C 177.44 0.1 1 478 105 ASN CA C 50.82 0.1 1 479 105 ASN CB C 42.95 0.3 1 480 105 ASN N N 111.10 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 173.00 0.1 1 484 106 TYR CA C 52.22 0.2 1 485 106 TYR CB C 40.26 0.3 1 486 106 TYR N N 118.29 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 173.08 0.1 1 490 107 LYS CA C 54.96 0.1 1 491 107 LYS CB C 34.25 0.4 1 492 107 LYS N N 126.05 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 171.55 0.1 1 496 108 THR CA C 58.61 0.1 1 497 108 THR CB C 69.86 0.3 1 498 108 THR N N 115.44 0.2 1 499 109 ARG H H 8.79 0.04 1 500 109 ARG C C 174.81 0.1 1 501 109 ARG CA C 56.09 0.1 1 502 109 ARG CB C 32.40 0.3 1 503 109 ARG N N 127.55 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 175.18 0.1 1 507 110 ALA CA C 49.15 0.2 1 508 110 ALA CB C 25.23 0.3 1 509 110 ALA N N 137.57 0.2 1 510 111 GLU H H 8.65 0.04 1 511 111 GLU C C 172.33 0.1 1 512 111 GLU CA C 55.13 0.2 1 513 111 GLU CB C 32.32 0.4 1 514 111 GLU N N 121.83 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 174.16 0.1 1 518 112 VAL CA C 59.96 0.1 1 519 112 VAL CB C 31.59 0.4 1 520 112 VAL N N 130.25 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 175.99 0.1 1 524 113 LYS CA C 54.25 0.2 1 525 113 LYS CB C 35.09 0.3 1 526 113 LYS N N 122.50 0.3 1 527 114 PHE H H 7.73 0.02 1 528 114 PHE C C 174.13 0.2 1 529 114 PHE CA C 58.57 0.1 1 530 114 PHE CB C 45.05 0.3 1 531 114 PHE N N 119.88 0.2 1 532 115 GLU H H 8.37 0.02 1 533 115 GLU C C 174.91 0.1 1 534 115 GLU CA C 55.16 0.1 1 535 115 GLU CB C 34.15 0.2 1 536 115 GLU N N 130.08 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 171.47 0.1 1 541 116 GLY CA C 46.47 0.1 1 542 116 GLY N N 110.40 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 174.34 0.1 1 546 117 ASP CA C 53.56 0.1 1 547 117 ASP CB C 41.06 0.3 1 548 117 ASP N N 130.55 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 173.37 0.1 1 552 118 THR CA C 61.38 0.1 1 553 118 THR CB C 70.57 0.2 1 554 118 THR N N 115.82 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 177.22 0.2 1 558 119 LEU CA C 52.12 0.2 1 559 119 LEU CB C 40.82 0.4 1 560 119 LEU N N 136.67 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 174.09 0.1 1 564 120 VAL CA C 59.50 0.1 1 565 120 VAL CB C 34.03 0.4 1 566 120 VAL N N 129.52 0.4 1 567 121 ASN H H 8.64 0.03 1 568 121 ASN C C 174.55 0.2 1 569 121 ASN CA C 50.41 0.2 1 570 121 ASN CB C 40.25 0.3 1 571 121 ASN N N 125.86 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 174.36 0.2 1 575 122 ARG CA C 55.39 0.1 1 576 122 ARG CB C 31.55 0.2 1 577 122 ARG N N 129.25 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 171.99 0.1 1 581 123 ILE CA C 60.88 0.1 1 582 123 ILE CB C 43.26 0.4 1 583 123 ILE N N 127.82 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 172.82 0.1 1 587 124 GLU CA C 54.70 0.2 1 588 124 GLU CB C 32.75 0.4 1 589 124 GLU N N 132.35 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 174.00 0.1 1 593 125 LEU CA C 53.58 0.1 1 594 125 LEU CB C 46.04 0.3 1 595 125 LEU N N 131.42 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 174.00 0.1 1 599 126 LYS CA C 54.02 0.1 1 600 126 LYS CB C 35.26 0.3 1 601 126 LYS N N 134.43 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 173.00 0.1 1 606 127 GLY CA C 44.83 0.1 1 607 127 GLY N N 116.09 0.2 1 608 128 ILE H H 9.20 0.03 1 609 128 ILE C C 176.12 0.1 1 610 128 ILE CA C 59.29 0.2 1 611 128 ILE N N 128.78 0.3 1 612 129 ASP CA C 53.29 0.2 1 613 129 ASP CB C 41.19 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 172.81 0.1 1 617 130 PHE CA C 53.78 0.2 1 618 130 PHE N N 123.75 0.3 1 619 131 LYS CA C 59.96 0.2 1 620 131 LYS CB C 34.28 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 173.52 0.1 1 624 132 GLU CA C 54.44 0.1 1 625 132 GLU CB C 29.22 0.4 1 626 132 GLU N N 123.74 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 173.10 0.1 1 630 133 ASP CA C 51.76 0.2 1 631 133 ASP CB C 39.59 0.3 1 632 133 ASP N N 114.32 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 171.87 0.1 1 637 134 GLY CA C 43.50 0.2 1 638 134 GLY N N 101.78 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 174.09 0.1 1 642 135 ASN CA C 54.94 0.1 1 643 135 ASN CB C 38.31 0.4 1 644 135 ASN N N 114.95 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 173.35 0.1 1 648 136 ILE CA C 63.34 0.1 1 649 136 ILE N N 117.33 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 172.18 0.1 1 653 137 LEU CA C 55.86 0.1 1 654 137 LEU CB C 39.07 0.5 1 655 137 LEU N N 119.63 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 170.14 0.1 1 660 138 GLY CA C 44.22 0.1 1 661 138 GLY N N 100.16 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 174.54 0.1 1 665 139 HIS CA C 57.35 0.1 1 666 139 HIS CB C 28.29 0.4 1 667 139 HIS N N 117.31 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 173.27 0.1 1 671 140 LYS CA C 54.27 0.1 1 672 140 LYS CB C 32.45 0.4 1 673 140 LYS N N 115.42 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 172.83 0.1 1 677 141 LEU CA C 54.97 0.1 1 678 141 LEU CB C 41.30 0.3 1 679 141 LEU N N 120.67 0.3 1 680 142 GLU H H 8.39 0.02 1 681 142 GLU C C 172.01 0.1 1 682 142 GLU CA C 55.86 0.2 1 683 142 GLU N N 128.48 0.2 1 684 143 TYR H H 9.30 0.02 1 685 143 TYR C C 172.73 0.1 1 686 143 TYR CA C 55.00 0.2 1 687 143 TYR N N 129.29 0.2 1 688 144 ASN CA C 55.27 0.2 1 689 145 TYR H H 9.23 0.02 1 690 145 TYR C C 172.48 0.1 1 691 145 TYR CA C 54.81 0.3 1 692 145 TYR CB C 42.23 0.4 1 693 145 TYR N N 139.72 0.2 1 694 146 ASN H H 8.69 0.03 1 695 146 ASN C C 175.51 0.2 1 696 146 ASN CA C 51.95 0.2 1 697 146 ASN N N 116.85 0.3 1 698 147 SER H H 9.34 0.02 1 699 147 SER C C 170.93 0.2 1 700 147 SER CA C 56.56 0.2 1 701 147 SER N N 125.02 0.2 1 702 151 TYR CA C 59.20 0.2 1 703 151 TYR CB C 37.76 0.4 1 704 152 ILE H H 8.92 0.03 1 705 152 ILE C C 173.27 0.1 1 706 152 ILE CA C 59.80 0.1 1 707 152 ILE N N 131.22 0.3 1 708 153 THR H H 8.85 0.02 1 709 153 THR CA C 59.03 0.2 1 710 153 THR CB C 70.86 0.3 1 711 153 THR N N 121.23 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 176.09 0.1 1 715 154 ALA CA C 52.19 0.1 1 716 154 ALA CB C 20.15 0.3 1 717 154 ALA N N 129.62 0.3 1 718 155 ASP H H 8.93 0.04 1 719 155 ASP C C 171.75 0.1 1 720 155 ASP CA C 51.73 0.2 1 721 155 ASP N N 125.79 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 174.52 0.2 1 725 156 LYS CA C 57.72 0.1 1 726 156 LYS N N 114.73 0.4 1 727 157 GLN CA C 57.68 0.2 1 728 158 LYS H H 7.31 0.03 1 729 158 LYS C C 172.91 0.1 1 730 158 LYS CA C 54.28 0.2 1 731 158 LYS CB C 32.49 0.3 1 732 158 LYS N N 117.28 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 173.01 0.1 1 736 159 ASN CA C 53.51 0.2 1 737 159 ASN CB C 37.95 0.4 1 738 159 ASN N N 120.05 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 176.39 0.1 1 743 160 GLY CA C 44.19 0.1 1 744 160 GLY N N 95.04 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 175.45 0.1 1 748 161 ILE CA C 57.70 0.2 1 749 161 ILE CB C 42.43 0.3 1 750 161 ILE N N 109.39 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 174.01 0.1 1 754 162 LYS CA C 53.97 0.3 1 755 162 LYS CB C 36.49 0.3 1 756 162 LYS N N 123.08 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 173.99 0.1 1 760 163 ALA CA C 49.85 0.1 1 761 163 ALA CB C 23.07 0.3 1 762 163 ALA N N 122.06 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 172.56 0.1 1 766 164 ASN CA C 52.55 0.2 1 767 164 ASN CB C 42.60 0.3 1 768 164 ASN N N 118.54 0.2 1 769 165 PHE H H 8.20 0.04 1 770 165 PHE C C 175.90 0.1 1 771 165 PHE CA C 56.31 0.2 1 772 165 PHE N N 116.93 0.4 1 773 166 LYS H H 8.67 0.04 1 774 166 LYS C C 173.88 0.1 1 775 166 LYS CA C 54.48 0.2 1 776 166 LYS N N 122.85 0.4 1 777 167 ILE H H 8.68 0.04 1 778 167 ILE C C 172.81 0.1 1 779 167 ILE CA C 58.69 0.1 1 780 167 ILE CB C 32.01 0.3 1 781 167 ILE N N 129.74 0.4 1 782 168 ARG CA C 57.64 0.2 1 783 170 ASN CA C 61.85 0.1 1 784 170 ASN CB C 32.32 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 173.55 0.1 1 788 171 ILE CA C 58.64 0.1 1 789 171 ILE CB C 36.94 0.3 1 790 171 ILE N N 121.58 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 171.47 0.1 1 794 172 GLU CA C 58.39 0.2 1 795 172 GLU CB C 29.71 0.4 1 796 172 GLU N N 128.41 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 172.90 0.1 1 800 173 ASP CA C 53.12 0.1 1 801 173 ASP CB C 39.92 0.3 1 802 173 ASP N N 119.54 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 171.44 0.1 1 807 174 GLY CA C 44.46 0.2 1 808 174 GLY N N 107.64 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 173.27 0.1 1 812 175 SER CA C 57.43 0.1 1 813 175 SER CB C 63.16 0.4 1 814 175 SER N N 119.04 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 174.72 0.1 1 818 176 VAL CA C 60.18 0.2 1 819 176 VAL CB C 35.67 0.3 1 820 176 VAL N N 117.18 0.4 1 821 177 GLN H H 9.49 0.02 1 822 177 GLN C C 173.55 0.1 1 823 177 GLN CA C 52.39 0.2 1 824 177 GLN CB C 31.71 0.4 1 825 177 GLN N N 131.85 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 174.09 0.1 1 829 178 LEU CA C 53.94 0.2 1 830 178 LEU CB C 43.58 0.3 1 831 178 LEU N N 136.47 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 170.02 0.1 1 835 179 ALA CA C 49.90 0.1 1 836 179 ALA CB C 21.47 0.4 1 837 179 ALA N N 130.59 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 171.13 0.1 1 841 180 ASP CA C 55.27 0.2 1 842 180 ASP CB C 41.73 0.3 1 843 180 ASP N N 138.28 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 173.64 0.1 1 847 181 HIS CA C 55.30 0.2 1 848 181 HIS CB C 29.80 0.4 1 849 181 HIS N N 126.52 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 175.26 0.1 1 853 182 TYR CA C 56.77 0.2 1 854 182 TYR CB C 39.34 0.4 1 855 182 TYR N N 126.72 0.3 1 856 183 GLN H H 8.72 0.02 1 857 183 GLN C C 174.09 0.1 1 858 183 GLN CA C 53.02 0.2 1 859 183 GLN CB C 33.53 0.4 1 860 183 GLN N N 132.07 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 173.06 0.1 1 864 184 GLN CA C 54.41 0.2 1 865 184 GLN CB C 32.96 0.3 1 866 184 GLN N N 127.99 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 174.01 0.1 1 870 185 ASN CA C 51.73 0.1 1 871 185 ASN N N 124.62 0.4 1 872 187 PRO CA C 62.87 0.2 1 873 187 PRO CB C 32.20 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 171.68 0.1 1 877 188 ILE CA C 63.38 0.2 1 878 188 ILE CB C 38.45 0.3 1 879 188 ILE N N 128.03 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 170.93 0.1 1 884 189 GLY CA C 43.44 0.2 1 885 189 GLY N N 108.84 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 175.03 0.1 1 889 190 ASP CA C 53.12 0.1 1 890 190 ASP CB C 41.30 0.3 1 891 190 ASP N N 118.70 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 171.39 0.1 1 896 191 GLY CA C 43.92 0.2 1 897 191 GLY N N 108.64 0.2 1 898 192 PRO CA C 62.46 0.1 1 899 192 PRO CB C 31.70 0.3 1 900 193 VAL CA C 58.38 0.1 1 901 193 VAL C C 171.95 0.3 1 902 193 VAL H H 9.14 0.1 1 903 193 VAL N N 138.05 0.3 1 904 193 VAL CB C 33.17 0.4 1 905 194 LEU C C 170.25 0.2 1 906 194 LEU CA C 53.40 0.2 1 907 194 LEU CB C 40.86 0.5 1 908 195 LEU H H 8.04 0.03 1 909 195 LEU C C 173.81 0.2 1 910 195 LEU CA C 49.47 0.2 1 911 195 LEU N N 124.15 0.3 1 912 199 HIS H H 8.69 0.04 1 913 199 HIS C C 174.37 0.1 1 914 199 HIS CA C 60.89 0.1 1 915 199 HIS N N 125.00 0.4 1 916 200 TYR H H 7.65 0.03 1 917 200 TYR C C 173.73 0.1 1 918 200 TYR CA C 59.77 0.1 1 919 200 TYR CB C 41.54 0.4 1 920 200 TYR N N 131.90 0.3 1 921 201 LEU H H 8.99 0.04 1 922 201 LEU C C 172.64 0.1 1 923 201 LEU CA C 53.33 0.1 1 924 201 LEU N N 130.21 0.4 1 925 206 ALA CA C 50.40 0.1 1 926 206 ALA CB C 22.63 0.2 1 927 207 LEU H H 9.08 0.03 1 928 207 LEU C C 174.89 0.2 1 929 207 LEU CA C 52.21 0.1 1 930 207 LEU N N 126.27 0.3 1 931 214 LYS H H 8.29 0.03 1 932 214 LYS C C 171.82 0.1 1 933 214 LYS CA C 52.41 0.2 1 934 214 LYS CB C 39.10 0.4 1 935 214 LYS N N 114.09 0.3 1 936 215 ARG H H 8.81 0.02 1 937 215 ARG C C 174.19 0.1 1 938 215 ARG CA C 54.26 0.2 1 939 215 ARG CB C 33.67 0.4 1 940 215 ARG N N 120.03 0.2 1 941 216 ASP C C 172.65 0.1 1 942 216 ASP CA C 55.18 0.1 1 943 216 ASP CB C 41.25 0.4 1 944 217 HIS H H 8.39 0.02 1 945 217 HIS C C 172.01 0.1 1 946 217 HIS CA C 55.87 0.2 1 947 217 HIS CB C 32.80 0.3 1 948 217 HIS N N 128.48 0.2 1 949 218 MET H H 7.78 0.03 1 950 218 MET C C 178.89 0.1 1 951 218 MET CA C 54.19 0.3 1 952 218 MET CB C 37.82 0.4 1 953 218 MET N N 116.80 0.3 1 954 219 VAL H H 7.62 0.03 1 955 219 VAL C C 174.72 0.1 1 956 219 VAL CA C 61.58 0.2 1 957 219 VAL CB C 32.29 0.3 1 958 219 VAL N N 131.39 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 175.45 0.1 1 962 220 LEU CA C 52.88 0.1 1 963 220 LEU CB C 46.72 0.5 1 964 220 LEU N N 135.98 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 175.63 0.1 1 968 221 LEU CA C 52.95 0.2 1 969 221 LEU N N 135.44 0.2 1 970 222 GLU CA C 54.25 0.3 1 971 222 GLU CB C 34.77 0.4 1 972 223 PHE H H 9.05 0.02 1 973 223 PHE C C 174.28 0.1 1 974 223 PHE CA C 55.39 0.1 1 975 223 PHE N N 128.51 0.2 1 976 224 VAL H H 9.61 0.02 1 977 224 VAL C C 172.27 0.1 1 978 224 VAL CA C 59.98 0.1 1 979 224 VAL CB C 34.25 0.4 1 980 224 VAL N N 127.58 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 173.52 0.1 1 984 225 THR CA C 59.20 0.1 1 985 225 THR CB C 70.82 0.2 1 986 225 THR N N 123.72 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 176.35 0.1 1 990 226 ALA CA C 50.73 0.1 1 991 226 ALA CB C 19.29 0.3 1 992 226 ALA N N 133.55 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 173.00 0.1 1 996 227 ALA CA C 50.83 0.1 1 997 227 ALA CB C 22.07 0.2 1 998 227 ALA N N 124.99 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 172.91 0.1 1 1003 228 GLY CA C 44.80 0.1 1 1004 228 GLY N N 100.60 0.2 1 1005 229 ILE H H 7.24 0.02 1 1006 229 ILE C C 174.63 0.1 1 1007 229 ILE CA C 59.83 0.1 1 1008 229 ILE N N 121.11 0.2 1 1009 230 THR CA C 54.72 0.2 1 1010 230 THR CB C 68.84 0.4 1 1011 231 HIS H H 8.02 0.02 1 1012 231 HIS C C 173.59 0.2 1 1013 231 HIS CA C 55.24 0.3 1 1014 231 HIS CB C 32.88 0.2 1 1015 231 HIS N N 131.24 0.2 1 1016 232 GLY H H 7.43 0.02 1 1017 232 GLY C C 173.00 0.2 1 1018 232 GLY CA C 45.49 0.2 1 1019 232 GLY N N 116.28 0.2 1 1020 233 MET CA C 55.33 0.1 1 1021 233 MET CB C 32.61 0.4 1 1022 234 ASP H H 8.43 0.04 1 1023 234 ASP C C 172.55 0.1 1 1024 234 ASP CA C 54.15 0.1 1 1025 234 ASP N N 123.32 0.4 1 1026 235 GLU H H 8.26 0.02 1 1027 235 GLU C C 174.61 0.1 1 1028 235 GLU CA C 55.76 0.1 1 1029 235 GLU CB C 30.17 0.3 1 1030 235 GLU N N 122.65 0.2 1 1031 236 LEU H H 8.09 0.04 1 1032 236 LEU C C 172.73 0.1 1 1033 236 LEU CA C 54.46 0.1 1 1034 236 LEU CB C 42.10 0.3 1 1035 236 LEU N N 125.83 0.4 1 1036 237 TYR H H 7.59 0.02 1 1037 237 TYR C C 172.73 0.1 1 1038 237 TYR CA C 58.35 0.1 1 1039 237 TYR N N 128.95 0.2 1 stop_ save_