data_5898
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Backbone 1H, 13C and 15N resonance assignments for the 24.4 kDa human gankyrin
protein
;
_BMRB_accession_number 5898
_BMRB_flat_file_name bmr5898.str
_Entry_type original
_Submission_date 2003-08-05
_Accession_date 2003-08-05
_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 Yuan Chunhua . .
2 Li Junan . .
3 Poi Mingjye . .
4 Byeon In-Ja L. .
5 Tsai Ming-Daw . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 428
"13C chemical shifts" 642
"15N chemical shifts" 217
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2004-10-25 original author .
stop_
_Original_release_date 2004-10-25
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Solution structure of the human oncogenic protein gankyrin containing seven
ankyrin repeats and analysis of its structure--function relationship.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 15379554
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Yuan Chunhua . .
2 Li Junan . .
3 Mahajan A. . .
4 Poi Mingjye . .
5 Byeon In-Ja L. .
6 Tsai Ming-Daw . .
stop_
_Journal_abbreviation Biochemistry
_Journal_volume 43
_Journal_issue 38
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 12152
_Page_last 12161
_Year 2004
_Details .
loop_
_Keyword
gankyrin
oncoprotein
'resonance assignment'
TROSY
stop_
save_
##################################
# Molecular system description #
##################################
save_system_gankyrin
_Saveframe_category molecular_system
_Mol_system_name '26S proteasome non-ATPase regulatory subunit 10'
_Abbreviation_common gankyrin
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
gankyrin $gankyrin
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all free'
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_gankyrin
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common gankyrin
_Abbreviation_common gankyrin
_Molecular_mass .
_Mol_thiol_state 'all free'
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 226
_Mol_residue_sequence
;
MEGCVSNLMVCNLAYSGKLE
ELKESILADKSLATRTDQDS
RTALHWACSAGHTEIVEFLL
QLGVPVNDKDDAGWSPLHIA
ASAGRDEIVKALLGKGAQVN
AVNQNGCTPLHYAASKNRHE
IAVMLLEGGANPDAKDHYEA
TAMHRAAAKGNLKMIHILLY
YKASTNIQDTEGNTPLHLAC
DEERVEEAKLLVSQGASIYI
ENKEEKTPLQVAKGGLGLIL
KRMVEG
;
loop_
_Residue_seq_code
_Residue_label
1 MET 2 GLU 3 GLY 4 CYS 5 VAL
6 SER 7 ASN 8 LEU 9 MET 10 VAL
11 CYS 12 ASN 13 LEU 14 ALA 15 TYR
16 SER 17 GLY 18 LYS 19 LEU 20 GLU
21 GLU 22 LEU 23 LYS 24 GLU 25 SER
26 ILE 27 LEU 28 ALA 29 ASP 30 LYS
31 SER 32 LEU 33 ALA 34 THR 35 ARG
36 THR 37 ASP 38 GLN 39 ASP 40 SER
41 ARG 42 THR 43 ALA 44 LEU 45 HIS
46 TRP 47 ALA 48 CYS 49 SER 50 ALA
51 GLY 52 HIS 53 THR 54 GLU 55 ILE
56 VAL 57 GLU 58 PHE 59 LEU 60 LEU
61 GLN 62 LEU 63 GLY 64 VAL 65 PRO
66 VAL 67 ASN 68 ASP 69 LYS 70 ASP
71 ASP 72 ALA 73 GLY 74 TRP 75 SER
76 PRO 77 LEU 78 HIS 79 ILE 80 ALA
81 ALA 82 SER 83 ALA 84 GLY 85 ARG
86 ASP 87 GLU 88 ILE 89 VAL 90 LYS
91 ALA 92 LEU 93 LEU 94 GLY 95 LYS
96 GLY 97 ALA 98 GLN 99 VAL 100 ASN
101 ALA 102 VAL 103 ASN 104 GLN 105 ASN
106 GLY 107 CYS 108 THR 109 PRO 110 LEU
111 HIS 112 TYR 113 ALA 114 ALA 115 SER
116 LYS 117 ASN 118 ARG 119 HIS 120 GLU
121 ILE 122 ALA 123 VAL 124 MET 125 LEU
126 LEU 127 GLU 128 GLY 129 GLY 130 ALA
131 ASN 132 PRO 133 ASP 134 ALA 135 LYS
136 ASP 137 HIS 138 TYR 139 GLU 140 ALA
141 THR 142 ALA 143 MET 144 HIS 145 ARG
146 ALA 147 ALA 148 ALA 149 LYS 150 GLY
151 ASN 152 LEU 153 LYS 154 MET 155 ILE
156 HIS 157 ILE 158 LEU 159 LEU 160 TYR
161 TYR 162 LYS 163 ALA 164 SER 165 THR
166 ASN 167 ILE 168 GLN 169 ASP 170 THR
171 GLU 172 GLY 173 ASN 174 THR 175 PRO
176 LEU 177 HIS 178 LEU 179 ALA 180 CYS
181 ASP 182 GLU 183 GLU 184 ARG 185 VAL
186 GLU 187 GLU 188 ALA 189 LYS 190 LEU
191 LEU 192 VAL 193 SER 194 GLN 195 GLY
196 ALA 197 SER 198 ILE 199 TYR 200 ILE
201 GLU 202 ASN 203 LYS 204 GLU 205 GLU
206 LYS 207 THR 208 PRO 209 LEU 210 GLN
211 VAL 212 ALA 213 LYS 214 GLY 215 GLY
216 LEU 217 GLY 218 LEU 219 ILE 220 LEU
221 LYS 222 ARG 223 MET 224 VAL 225 GLU
226 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
PDB 1QYM "X-Ray Structure Of Human Gankyrin" 99.56 227 100.00 100.00 8.27e-163
PDB 1TR4 "Solution Structure Of Human Oncogenic Protein Gankyrin" 100.00 226 100.00 100.00 9.77e-164
PDB 1UOH "Human Gankyrin" 100.00 226 100.00 100.00 9.77e-164
PDB 4NIK "Structure Of Human Gankyrin In Complex To The Single Chain Antibody F5" 100.00 230 100.00 100.00 1.77e-163
DBJ BAA33215 "26S proteasome subunit p28 [Homo sapiens]" 100.00 226 100.00 100.00 9.77e-164
DBJ BAA34594 "gankyrin [Homo sapiens]" 100.00 226 100.00 100.00 9.77e-164
DBJ BAE87161 "unnamed protein product [Macaca fascicularis]" 100.00 226 99.56 99.56 9.51e-163
DBJ BAE87972 "unnamed protein product [Macaca fascicularis]" 100.00 226 99.56 99.56 9.51e-163
DBJ BAE88401 "unnamed protein product [Macaca fascicularis]" 100.00 226 99.56 99.56 9.51e-163
GB AAH11960 "Proteasome (prosome, macropain) 26S subunit, non-ATPase, 10 [Homo sapiens]" 100.00 226 100.00 100.00 9.77e-164
GB AAV38495 "proteasome (prosome, macropain) 26S subunit, non-ATPase, 10 [Homo sapiens]" 100.00 226 99.56 99.56 4.05e-163
GB AAX41449 "proteasome 26S subunit 10 [synthetic construct]" 100.00 226 99.56 99.56 4.05e-163
GB AAY18907 "proteasome 26S subunit non-ATPase 10-like [synthetic construct]" 99.56 250 100.00 100.00 5.00e-162
GB ACT64478 "proteasome (prosome, macropain) 26S subunit, non-ATPase, 10 protein [synthetic construct]" 100.00 226 100.00 100.00 9.77e-164
REF NP_001248034 "26S proteasome non-ATPase regulatory subunit 10 [Macaca mulatta]" 100.00 226 99.56 99.56 9.51e-163
REF NP_002805 "26S proteasome non-ATPase regulatory subunit 10 isoform 1 [Homo sapiens]" 100.00 226 100.00 100.00 9.77e-164
REF XP_001926942 "PREDICTED: 26S proteasome non-ATPase regulatory subunit 10 isoform 1 [Sus scrofa]" 99.56 226 99.56 99.56 4.03e-162
REF XP_002763200 "PREDICTED: 26S proteasome non-ATPase regulatory subunit 10 isoform X1 [Callithrix jacchus]" 100.00 226 98.23 98.67 2.55e-160
REF XP_002832022 "PREDICTED: 26S proteasome non-ATPase regulatory subunit 10 isoform X1 [Pongo abelii]" 100.00 226 100.00 100.00 9.77e-164
SP O75832 "RecName: Full=26S proteasome non-ATPase regulatory subunit 10; AltName: Full=26S proteasome regulatory subunit p28; AltName: Fu" 100.00 226 100.00 100.00 9.77e-164
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
$gankyrin Human 9606 Eukaryota Metazoa Homo sapiens
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_name
$gankyrin 'recombinant technology' . . . . .
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_1
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Concentration_min_value
_Concentration_max_value
_Isotopic_labeling
$gankyrin . mM 0.4 0.5 '[U-13C; U-15N; U-70% 2H]'
HEPES 5 mM . . .
EDTA 1 uM . . .
DTT 1 mM . . .
stop_
save_
############################
# Computer software used #
############################
save_XWINNMR
_Saveframe_category software
_Name XWINNMR
_Version 3.1
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DMX
_Field_strength 600
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 800
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_TROSY-HNCA_1
_Saveframe_category NMR_applied_experiment
_Experiment_name TROSY-HNCA
_Sample_label .
save_
save_TROSY-HN(CO)CA_2
_Saveframe_category NMR_applied_experiment
_Experiment_name TROSY-HN(CO)CA
_Sample_label .
save_
save_TROSY-HNCACB_3
_Saveframe_category NMR_applied_experiment
_Experiment_name TROSY-HNCACB
_Sample_label .
save_
save_TROSY-HNCO_4
_Saveframe_category NMR_applied_experiment
_Experiment_name TROSY-HNCO
_Sample_label .
save_
save_15N-edited_NOESY-HSQC_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-edited NOESY-HSQC'
_Sample_label .
save_
save_NMR_spec_expt__0_1
_Saveframe_category NMR_applied_experiment
_Experiment_name TROSY-HNCA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_2
_Saveframe_category NMR_applied_experiment
_Experiment_name TROSY-HN(CO)CA
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_3
_Saveframe_category NMR_applied_experiment
_Experiment_name TROSY-HNCACB
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_4
_Saveframe_category NMR_applied_experiment
_Experiment_name TROSY-HNCO
_BMRB_pulse_sequence_accession_number .
_Details .
save_
save_NMR_spec_expt__0_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N-edited NOESY-HSQC'
_BMRB_pulse_sequence_accession_number .
_Details .
save_
#######################
# Sample conditions #
#######################
save_Ex-cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 7.4 0.2 n/a
temperature 300 1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details
;
Calibation followed the reference Journal of Biolmolecular NMR 6 (1995) 135-140.
1H, 13C and 15N chemical shift referencing in biomolecular NMR
by Wishart et al.
;
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 external direct . . . 1.0
DSS C 13 'methyl carbons' ppm 0.0 external direct . . . 1.0
DSS N 15 'methyl protons' ppm 0.0 external indirect . . . 0.101329118
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_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $Ex-cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name gankyrin
_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 H H 8.37 0.03 1
2 . 1 MET C C 176.1 0.1 1
3 . 1 MET CA C 56.0 0.1 1
4 . 1 MET CB C 33.1 0.1 1
5 . 1 MET N N 122.2 0.1 1
6 . 2 GLU H H 8.29 0.03 1
7 . 2 GLU HA H 4.22 0.03 1
8 . 2 GLU C C 176.9 0.1 1
9 . 2 GLU CA C 57.5 0.1 1
10 . 2 GLU CB C 30.3 0.1 1
11 . 2 GLU N N 121.7 0.1 1
12 . 3 GLY H H 8.39 0.03 1
13 . 3 GLY C C 173.5 0.1 1
14 . 3 GLY CA C 45.9 0.1 1
15 . 3 GLY N N 110.2 0.1 1
16 . 4 CYS H H 7.86 0.03 1
17 . 4 CYS C C 174.4 0.1 1
18 . 4 CYS CA C 58.9 0.1 1
19 . 4 CYS CB C 28.7 0.1 1
20 . 4 CYS N N 119.1 0.1 1
21 . 5 VAL H H 7.42 0.03 1
22 . 5 VAL HA H 3.96 0.03 1
23 . 5 VAL C C 174.8 0.1 1
24 . 5 VAL CA C 61.7 0.1 1
25 . 5 VAL CB C 32.6 0.1 1
26 . 5 VAL N N 117.5 0.1 1
27 . 6 SER H H 7.83 0.03 1
28 . 6 SER HA H 4.64 0.03 1
29 . 6 SER C C 174.6 0.1 1
30 . 6 SER CA C 57.5 0.1 1
31 . 6 SER CB C 63.8 0.1 1
32 . 6 SER N N 115.1 0.1 1
33 . 7 ASN H H 8.78 0.03 1
34 . 7 ASN HA H 4.55 0.03 1
35 . 7 ASN C C 175.0 0.1 1
36 . 7 ASN CA C 54.3 0.1 1
37 . 7 ASN CB C 37.4 0.1 1
38 . 7 ASN N N 123.3 0.1 1
39 . 8 LEU H H 8.18 0.03 1
40 . 8 LEU CA C 53.4 0.1 1
41 . 8 LEU CB C 43.9 0.1 1
42 . 8 LEU N N 121.1 0.1 1
43 . 9 MET C C 179.2 0.1 1
44 . 9 MET CA C 59.4 0.1 1
45 . 10 VAL H H 8.88 0.03 1
46 . 10 VAL HA H 3.89 0.03 1
47 . 10 VAL C C 177.0 0.1 1
48 . 10 VAL CA C 66.3 0.1 1
49 . 10 VAL CB C 31.6 0.1 1
50 . 10 VAL N N 115.0 0.1 1
51 . 11 CYS H H 6.80 0.03 1
52 . 11 CYS HA H 4.02 0.03 1
53 . 11 CYS C C 175.8 0.1 1
54 . 11 CYS CA C 63.1 0.1 1
55 . 11 CYS CB C 27.8 0.1 1
56 . 11 CYS N N 118.6 0.1 1
57 . 12 ASN H H 7.31 0.03 1
58 . 12 ASN HA H 4.37 0.03 1
59 . 12 ASN C C 178.9 0.1 1
60 . 12 ASN CA C 57.2 0.1 1
61 . 12 ASN CB C 38.4 0.1 1
62 . 12 ASN N N 118.6 0.1 1
63 . 13 LEU H H 8.68 0.03 1
64 . 13 LEU HA H 4.00 0.03 1
65 . 13 LEU C C 178.5 0.1 1
66 . 13 LEU CA C 58.5 0.1 1
67 . 13 LEU CB C 42.5 0.1 1
68 . 13 LEU N N 121.2 0.1 1
69 . 14 ALA H H 7.71 0.03 1
70 . 14 ALA HA H 4.05 0.03 1
71 . 14 ALA C C 178.5 0.1 1
72 . 14 ALA CA C 55.6 0.1 1
73 . 14 ALA CB C 20.1 0.1 1
74 . 14 ALA N N 120.2 0.1 1
75 . 15 TYR H H 8.26 0.03 1
76 . 15 TYR HA H 4.26 0.03 1
77 . 15 TYR C C 177.3 0.1 1
78 . 15 TYR CA C 61.2 0.1 1
79 . 15 TYR CB C 39.9 0.1 1
80 . 15 TYR N N 116.3 0.1 1
81 . 16 SER H H 8.10 0.03 1
82 . 16 SER HA H 4.34 0.03 1
83 . 16 SER C C 174.7 0.1 1
84 . 16 SER CA C 59.9 0.1 1
85 . 16 SER CB C 64.6 0.1 1
86 . 16 SER N N 110.4 0.1 1
87 . 17 GLY H H 7.27 0.03 1
88 . 17 GLY HA2 H 3.15 0.03 2
89 . 17 GLY HA3 H 2.65 0.03 2
90 . 17 GLY C C 174.9 0.1 1
91 . 17 GLY CA C 44.7 0.1 1
92 . 17 GLY N N 109.6 0.1 1
93 . 18 LYS H H 7.69 0.03 1
94 . 18 LYS HA H 4.36 0.03 1
95 . 18 LYS C C 174.6 0.1 1
96 . 18 LYS CA C 55.1 0.1 1
97 . 18 LYS CB C 30.6 0.1 1
98 . 18 LYS N N 123.2 0.1 1
99 . 19 LEU H H 7.43 0.03 1
100 . 19 LEU HA H 3.62 0.03 1
101 . 19 LEU C C 177.2 0.1 1
102 . 19 LEU CA C 59.1 0.1 1
103 . 19 LEU CB C 41.6 0.1 1
104 . 19 LEU N N 124.2 0.1 1
105 . 20 GLU H H 8.70 0.03 1
106 . 20 GLU HA H 3.76 0.03 1
107 . 20 GLU C C 179.3 0.1 1
108 . 20 GLU CA C 60.8 0.1 1
109 . 20 GLU CB C 28.4 0.1 1
110 . 20 GLU N N 117.8 0.1 1
111 . 21 GLU H H 8.82 0.03 1
112 . 21 GLU HA H 3.99 0.03 1
113 . 21 GLU C C 179.6 0.1 1
114 . 21 GLU CA C 60.3 0.1 1
115 . 21 GLU CB C 29.9 0.1 1
116 . 21 GLU N N 120.4 0.1 1
117 . 22 LEU H H 8.30 0.03 1
118 . 22 LEU HA H 3.88 0.03 1
119 . 22 LEU C C 178.1 0.1 1
120 . 22 LEU CA C 59.3 0.1 1
121 . 22 LEU CB C 41.6 0.1 1
122 . 22 LEU N N 123.1 0.1 1
123 . 23 LYS H H 8.67 0.03 1
124 . 23 LYS HA H 3.56 0.03 1
125 . 23 LYS C C 178.5 0.1 1
126 . 23 LYS CA C 60.8 0.1 1
127 . 23 LYS CB C 32.3 0.1 1
128 . 23 LYS N N 119.8 0.1 1
129 . 24 GLU H H 7.83 0.03 1
130 . 24 GLU HA H 3.93 0.03 1
131 . 24 GLU C C 179.7 0.1 1
132 . 24 GLU CA C 59.9 0.1 1
133 . 24 GLU CB C 29.8 0.1 1
134 . 24 GLU N N 117.4 0.1 1
135 . 25 SER H H 7.85 0.03 1
136 . 25 SER HA H 4.22 0.03 1
137 . 25 SER C C 176.7 0.1 1
138 . 25 SER CA C 62.7 0.1 1
139 . 25 SER CB C 63.8 0.1 1
140 . 25 SER N N 114.9 0.1 1
141 . 26 ILE H H 8.09 0.03 1
142 . 26 ILE HA H 3.97 0.03 1
143 . 26 ILE C C 177.1 0.1 1
144 . 26 ILE CA C 63.7 0.1 1
145 . 26 ILE CB C 38.4 0.1 1
146 . 26 ILE N N 122.0 0.1 1
147 . 27 LEU H H 8.52 0.03 1
148 . 27 LEU HA H 4.13 0.03 1
149 . 27 LEU C C 179.6 0.1 1
150 . 27 LEU CA C 58.2 0.1 1
151 . 27 LEU CB C 41.1 0.1 1
152 . 27 LEU N N 119.3 0.1 1
153 . 28 ALA H H 7.10 0.03 1
154 . 28 ALA HA H 4.28 0.03 1
155 . 28 ALA C C 178.0 0.1 1
156 . 28 ALA CA C 54.1 0.1 1
157 . 28 ALA CB C 19.4 0.1 1
158 . 28 ALA N N 118.8 0.1 1
159 . 29 ASP H H 7.45 0.03 1
160 . 29 ASP HA H 4.66 0.03 1
161 . 29 ASP C C 175.3 0.1 1
162 . 29 ASP CA C 54.0 0.1 1
163 . 29 ASP CB C 40.6 0.1 1
164 . 29 ASP N N 117.4 0.1 1
165 . 30 LYS H H 8.73 0.03 1
166 . 30 LYS HA H 4.40 0.03 1
167 . 30 LYS C C 180.0 0.1 1
168 . 30 LYS CA C 59.6 0.1 1
169 . 30 LYS CB C 32.4 0.1 1
170 . 30 LYS N N 125.6 0.1 1
171 . 31 SER H H 8.31 0.03 1
172 . 31 SER HA H 4.26 0.03 1
173 . 31 SER C C 176.3 0.1 1
174 . 31 SER CA C 61.7 0.1 1
175 . 31 SER CB C 63.4 0.1 1
176 . 31 SER N N 116.9 0.1 1
177 . 32 LEU H H 8.08 0.03 1
178 . 32 LEU HA H 4.07 0.03 1
179 . 32 LEU C C 178.2 0.1 1
180 . 32 LEU CA C 57.5 0.1 1
181 . 32 LEU CB C 42.7 0.1 1
182 . 32 LEU N N 122.3 0.1 1
183 . 33 ALA H H 7.63 0.03 1
184 . 33 ALA HA H 3.96 0.03 1
185 . 33 ALA C C 176.0 0.1 1
186 . 33 ALA CA C 55.3 0.1 1
187 . 33 ALA CB C 19.5 0.1 1
188 . 33 ALA N N 117.2 0.1 1
189 . 34 THR H H 7.14 0.03 1
190 . 34 THR HA H 4.49 0.03 1
191 . 34 THR C C 173.8 0.1 1
192 . 34 THR CA C 60.4 0.1 1
193 . 34 THR CB C 69.5 0.1 1
194 . 34 THR N N 99.6 0.1 1
195 . 35 ARG H H 7.00 0.03 1
196 . 35 ARG HA H 4.29 0.03 1
197 . 35 ARG C C 175.2 0.1 1
198 . 35 ARG CA C 57.0 0.1 1
199 . 35 ARG CB C 30.7 0.1 1
200 . 35 ARG N N 125.1 0.1 1
201 . 36 THR H H 7.88 0.03 1
202 . 36 THR HA H 4.73 0.03 1
203 . 36 THR C C 175.7 0.1 1
204 . 36 THR CA C 59.5 0.1 1
205 . 36 THR CB C 71.7 0.1 1
206 . 36 THR N N 112.4 0.1 1
207 . 37 ASP H H 9.10 0.03 1
208 . 37 ASP C C 179.1 0.1 1
209 . 37 ASP CA C 52.1 0.1 1
210 . 37 ASP CB C 42.2 0.1 1
211 . 37 ASP N N 123.6 0.1 1
212 . 38 GLN H H 8.78 0.03 1
213 . 38 GLN HA H 4.29 0.03 1
214 . 38 GLN C C 176.0 0.1 1
215 . 38 GLN CA C 58.6 0.1 1
216 . 38 GLN CB C 27.2 0.1 1
217 . 38 GLN N N 118.2 0.1 1
218 . 39 ASP H H 8.39 0.03 1
219 . 39 ASP HA H 5.11 0.03 1
220 . 39 ASP C C 175.4 0.1 1
221 . 39 ASP CA C 55.0 0.1 1
222 . 39 ASP CB C 42.2 0.1 1
223 . 39 ASP N N 122.6 0.1 1
224 . 40 SER H H 8.46 0.03 1
225 . 40 SER HA H 3.81 0.03 1
226 . 40 SER C C 172.5 0.1 1
227 . 40 SER CA C 60.5 0.1 1
228 . 40 SER CB C 62.2 0.1 1
229 . 40 SER N N 111.6 0.1 1
230 . 41 ARG H H 8.25 0.03 1
231 . 41 ARG HA H 3.92 0.03 1
232 . 41 ARG C C 176.2 0.1 1
233 . 41 ARG CA C 55.8 0.1 1
234 . 41 ARG CB C 33.4 0.1 1
235 . 41 ARG N N 116.9 0.1 1
236 . 42 THR H H 9.73 0.03 1
237 . 42 THR HA H 5.04 0.03 1
238 . 42 THR C C 177.0 0.1 1
239 . 42 THR CA C 59.8 0.1 1
240 . 42 THR CB C 72.7 0.1 1
241 . 42 THR N N 112.3 0.1 1
242 . 43 ALA H H 9.62 0.03 1
243 . 43 ALA HA H 4.13 0.03 1
244 . 43 ALA C C 178.5 0.1 1
245 . 43 ALA CA C 56.3 0.1 1
246 . 43 ALA CB C 18.5 0.1 1
247 . 43 ALA N N 121.7 0.1 1
248 . 44 LEU H H 8.25 0.03 1
249 . 44 LEU HA H 4.00 0.03 1
250 . 44 LEU C C 178.9 0.1 1
251 . 44 LEU CA C 58.8 0.1 1
252 . 44 LEU CB C 41.9 0.1 1
253 . 44 LEU N N 115.4 0.1 1
254 . 45 HIS H H 7.65 0.03 1
255 . 45 HIS HA H 3.64 0.03 1
256 . 45 HIS C C 178.1 0.1 1
257 . 45 HIS CA C 64.3 0.1 1
258 . 45 HIS CB C 31.5 0.1 1
259 . 45 HIS N N 117.6 0.1 1
260 . 46 TRP H H 7.39 0.03 1
261 . 46 TRP HA H 4.60 0.03 1
262 . 46 TRP C C 178.6 0.1 1
263 . 46 TRP CA C 60.7 0.1 1
264 . 46 TRP CB C 31.4 0.1 1
265 . 46 TRP N N 116.3 0.1 1
266 . 47 ALA H H 8.85 0.03 1
267 . 47 ALA HA H 4.35 0.03 1
268 . 47 ALA C C 180.2 0.1 1
269 . 47 ALA CA C 56.0 0.1 1
270 . 47 ALA CB C 19.6 0.1 1
271 . 47 ALA N N 122.1 0.1 1
272 . 48 CYS H H 8.04 0.03 1
273 . 48 CYS HA H 4.10 0.03 1
274 . 48 CYS C C 175.3 0.1 1
275 . 48 CYS CA C 65.1 0.1 1
276 . 48 CYS CB C 27.7 0.1 1
277 . 48 CYS N N 114.2 0.1 1
278 . 49 SER H H 7.54 0.03 1
279 . 49 SER HA H 3.77 0.03 1
280 . 49 SER C C 177.1 0.1 1
281 . 49 SER CA C 61.6 0.1 1
282 . 49 SER CB C 64.0 0.1 1
283 . 49 SER N N 113.0 0.1 1
284 . 50 ALA H H 7.69 0.03 1
285 . 50 ALA HA H 4.15 0.03 1
286 . 50 ALA C C 177.1 0.1 1
287 . 50 ALA CA C 53.4 0.1 1
288 . 50 ALA CB C 22.2 0.1 1
289 . 50 ALA N N 119.0 0.1 1
290 . 51 GLY H H 7.40 0.03 1
291 . 51 GLY HA2 H 3.83 0.03 2
292 . 51 GLY HA3 H 3.28 0.03 2
293 . 51 GLY C C 173.7 0.1 1
294 . 51 GLY CA C 46.6 0.1 1
295 . 51 GLY N N 103.7 0.1 1
296 . 52 HIS H H 7.20 0.03 1
297 . 52 HIS HA H 5.26 0.03 1
298 . 52 HIS C C 175.6 0.1 1
299 . 52 HIS CA C 55.0 0.1 1
300 . 52 HIS CB C 30.6 0.1 1
301 . 52 HIS N N 118.7 0.1 1
302 . 53 THR H H 8.51 0.03 1
303 . 53 THR HA H 3.44 0.03 1
304 . 53 THR C C 175.5 0.1 1
305 . 53 THR CA C 67.2 0.1 1
306 . 53 THR CB C 69.1 0.1 1
307 . 53 THR N N 125.8 0.1 1
308 . 54 GLU H H 9.60 0.03 1
309 . 54 GLU HA H 4.20 0.03 1
310 . 54 GLU C C 180.1 0.1 1
311 . 54 GLU CA C 60.4 0.1 1
312 . 54 GLU CB C 29.2 0.1 1
313 . 54 GLU N N 119.8 0.1 1
314 . 55 ILE H H 7.38 0.03 1
315 . 55 ILE HA H 3.81 0.03 1
316 . 55 ILE C C 177.0 0.1 1
317 . 55 ILE CA C 65.8 0.1 1
318 . 55 ILE CB C 37.4 0.1 1
319 . 55 ILE N N 119.5 0.1 1
320 . 56 VAL H H 7.78 0.03 1
321 . 56 VAL HA H 3.38 0.03 1
322 . 56 VAL C C 177.0 0.1 1
323 . 56 VAL CA C 68.8 0.1 1
324 . 56 VAL CB C 31.6 0.1 1
325 . 56 VAL N N 120.1 0.1 1
326 . 57 GLU H H 8.74 0.03 1
327 . 57 GLU HA H 3.87 0.03 1
328 . 57 GLU C C 178.7 0.1 1
329 . 57 GLU CA C 60.6 0.1 1
330 . 57 GLU CB C 29.8 0.1 1
331 . 57 GLU N N 117.7 0.1 1
332 . 58 PHE H H 7.60 0.03 1
333 . 58 PHE HA H 4.35 0.03 1
334 . 58 PHE C C 176.8 0.1 1
335 . 58 PHE CA C 61.2 0.1 1
336 . 58 PHE CB C 39.3 0.1 1
337 . 58 PHE N N 119.7 0.1 1
338 . 59 LEU H H 8.13 0.03 1
339 . 59 LEU HA H 3.67 0.03 1
340 . 59 LEU C C 179.3 0.1 1
341 . 59 LEU CA C 58.0 0.1 1
342 . 59 LEU CB C 41.4 0.1 1
343 . 59 LEU N N 118.9 0.1 1
344 . 60 LEU H H 8.88 0.03 1
345 . 60 LEU HA H 4.00 0.03 1
346 . 60 LEU C C 181.9 0.1 1
347 . 60 LEU CA C 58.4 0.1 1
348 . 60 LEU CB C 40.2 0.1 1
349 . 60 LEU N N 118.4 0.1 1
350 . 61 GLN H H 8.07 0.03 1
351 . 61 GLN HA H 4.09 0.03 1
352 . 61 GLN C C 177.7 0.1 1
353 . 61 GLN CA C 58.6 0.1 1
354 . 61 GLN CB C 28.0 0.1 1
355 . 61 GLN N N 120.4 0.1 1
356 . 62 LEU H H 7.36 0.03 1
357 . 62 LEU HA H 4.10 0.03 1
358 . 62 LEU C C 178.0 0.1 1
359 . 62 LEU CA C 56.1 0.1 1
360 . 62 LEU CB C 42.5 0.1 1
361 . 62 LEU N N 119.5 0.1 1
362 . 63 GLY H H 7.70 0.03 1
363 . 63 GLY HA2 H 4.15 0.03 2
364 . 63 GLY HA3 H 3.75 0.03 2
365 . 63 GLY C C 175.0 0.1 1
366 . 63 GLY CA C 45.8 0.1 1
367 . 63 GLY N N 105.2 0.1 1
368 . 64 VAL H H 6.84 0.03 1
369 . 64 VAL HA H 4.26 0.03 1
370 . 64 VAL CA C 60.8 0.1 1
371 . 64 VAL CB C 30.1 0.1 1
372 . 64 VAL N N 113.9 0.1 1
373 . 65 PRO HA H 4.48 0.03 1
374 . 65 PRO C C 179.2 0.1 1
375 . 65 PRO CA C 63.4 0.1 1
376 . 65 PRO CB C 32.9 0.1 1
377 . 66 VAL H H 8.18 0.03 1
378 . 66 VAL HA H 4.16 0.03 1
379 . 66 VAL C C 174.8 0.1 1
380 . 66 VAL CA C 62.2 0.1 1
381 . 66 VAL CB C 33.4 0.1 1
382 . 66 VAL N N 114.7 0.1 1
383 . 67 ASN H H 7.89 0.03 1
384 . 67 ASN HA H 5.16 0.03 1
385 . 67 ASN C C 176.0 0.1 1
386 . 67 ASN CA C 53.8 0.1 1
387 . 67 ASN CB C 41.7 0.1 1
388 . 67 ASN N N 116.6 0.1 1
389 . 68 ASP H H 8.15 0.03 1
390 . 68 ASP HA H 4.56 0.03 1
391 . 68 ASP C C 176.2 0.1 1
392 . 68 ASP CA C 56.0 0.1 1
393 . 68 ASP CB C 40.6 0.1 1
394 . 68 ASP N N 123.0 0.1 1
395 . 69 LYS H H 8.78 0.03 1
396 . 69 LYS HA H 4.63 0.03 1
397 . 69 LYS C C 177.1 0.1 1
398 . 69 LYS CA C 55.8 0.1 1
399 . 69 LYS CB C 35.7 0.1 1
400 . 69 LYS N N 122.6 0.1 1
401 . 70 ASP H H 8.06 0.03 1
402 . 70 ASP HA H 4.50 0.03 1
403 . 70 ASP C C 178.1 0.1 1
404 . 70 ASP CA C 52.7 0.1 1
405 . 70 ASP CB C 42.2 0.1 1
406 . 70 ASP N N 122.2 0.1 1
407 . 71 ASP H H 7.91 0.03 1
408 . 71 ASP HA H 4.44 0.03 1
409 . 71 ASP C C 176.8 0.1 1
410 . 71 ASP CA C 57.6 0.1 1
411 . 71 ASP CB C 40.4 0.1 1
412 . 71 ASP N N 117.0 0.1 1
413 . 72 ALA H H 7.99 0.03 1
414 . 72 ALA HA H 4.68 0.03 1
415 . 72 ALA C C 177.7 0.1 1
416 . 72 ALA CA C 51.7 0.1 1
417 . 72 ALA CB C 19.6 0.1 1
418 . 72 ALA N N 122.0 0.1 1
419 . 73 GLY H H 8.68 0.03 1
420 . 73 GLY HA2 H 3.83 0.03 1
421 . 73 GLY HA3 H 4.07 0.03 1
422 . 73 GLY C C 172.8 0.1 1
423 . 73 GLY CA C 46.7 0.1 1
424 . 73 GLY N N 110.8 0.1 1
425 . 74 TRP H H 9.00 0.03 1
426 . 74 TRP HA H 3.84 0.03 1
427 . 74 TRP C C 176.1 0.1 1
428 . 74 TRP CA C 59.8 0.1 1
429 . 74 TRP CB C 27.7 0.1 1
430 . 74 TRP N N 121.1 0.1 1
431 . 75 SER H H 9.05 0.03 1
432 . 75 SER HA H 5.31 0.03 1
433 . 75 SER CA C 56.9 0.1 1
434 . 75 SER CB C 65.1 0.1 1
435 . 75 SER N N 123.2 0.1 1
436 . 76 PRO C C 176.9 0.1 1
437 . 76 PRO CA C 67.7 0.1 1
438 . 77 LEU H H 8.82 0.03 1
439 . 77 LEU C C 179.3 0.1 1
440 . 77 LEU CA C 58.5 0.1 1
441 . 77 LEU CB C 42.1 0.1 1
442 . 77 LEU N N 116.5 0.1 1
443 . 78 HIS H H 7.95 0.03 1
444 . 78 HIS C C 177.4 0.1 1
445 . 78 HIS CA C 64.6 0.1 1
446 . 78 HIS CB C 32.3 0.1 1
447 . 78 HIS N N 117.0 0.1 1
448 . 79 ILE H H 7.94 0.03 1
449 . 79 ILE C C 178.2 0.1 1
450 . 79 ILE CA C 65.4 0.1 1
451 . 79 ILE CB C 40.9 0.1 1
452 . 79 ILE N N 117.5 0.1 1
453 . 80 ALA H H 8.89 0.03 1
454 . 80 ALA HA H 3.94 0.03 1
455 . 80 ALA C C 178.4 0.1 1
456 . 80 ALA CA C 55.2 0.1 1
457 . 80 ALA CB C 20.6 0.1 1
458 . 80 ALA N N 120.0 0.1 1
459 . 81 ALA H H 8.35 0.03 1
460 . 81 ALA HA H 4.12 0.03 1
461 . 81 ALA C C 178.9 0.1 1
462 . 81 ALA CA C 55.7 0.1 1
463 . 81 ALA CB C 19.4 0.1 1
464 . 81 ALA N N 118.5 0.1 1
465 . 82 SER H H 8.03 0.03 1
466 . 82 SER HA H 3.97 0.03 1
467 . 82 SER C C 177.4 0.1 1
468 . 82 SER CA C 62.0 0.1 1
469 . 82 SER CB C 64.2 0.1 1
470 . 82 SER N N 109.5 0.1 1
471 . 83 ALA H H 8.06 0.03 1
472 . 83 ALA HA H 4.44 0.03 1
473 . 83 ALA C C 177.3 0.1 1
474 . 83 ALA CA C 52.9 0.1 1
475 . 83 ALA CB C 19.9 0.1 1
476 . 83 ALA N N 118.1 0.1 1
477 . 84 GLY H H 7.51 0.03 1
478 . 84 GLY HA2 H 3.84 0.03 2
479 . 84 GLY HA3 H 3.52 0.03 2
480 . 84 GLY C C 174.0 0.1 1
481 . 84 GLY CA C 47.7 0.1 1
482 . 84 GLY N N 107.1 0.1 1
483 . 85 ARG H H 8.17 0.03 1
484 . 85 ARG C C 175.3 0.03 1
485 . 85 ARG CA C 51.6 0.1 1
486 . 85 ARG CB C 27.7 0.1 1
487 . 85 ARG N N 117.0 0.1 1
488 . 86 ASP H H 8.55 0.03 1
489 . 86 ASP HA H 3.72 0.03 1
490 . 86 ASP C C 177.1 0.1 1
491 . 86 ASP CA C 59.5 0.1 1
492 . 86 ASP CB C 40.5 0.1 1
493 . 86 ASP N N 125.1 0.1 1
494 . 87 GLU H H 8.92 0.03 1
495 . 87 GLU HA H 3.95 0.03 1
496 . 87 GLU C C 179.9 0.1 1
497 . 87 GLU CA C 59.9 0.1 1
498 . 87 GLU CB C 29.6 0.1 1
499 . 87 GLU N N 116.3 0.1 1
500 . 88 ILE H H 7.44 0.03 1
501 . 88 ILE HA H 3.67 0.03 1
502 . 88 ILE C C 177.1 0.1 1
503 . 88 ILE CA C 65.4 0.1 1
504 . 88 ILE CB C 38.0 0.1 1
505 . 88 ILE N N 120.6 0.1 1
506 . 89 VAL H H 8.10 0.03 1
507 . 89 VAL HA H 3.26 0.03 1
508 . 89 VAL C C 176.7 0.1 1
509 . 89 VAL CA C 68.7 0.1 1
510 . 89 VAL CB C 30.9 0.1 1
511 . 89 VAL N N 121.0 0.1 1
512 . 90 LYS H H 7.69 0.03 1
513 . 90 LYS HA H 3.81 0.03 1
514 . 90 LYS C C 179.3 0.1 1
515 . 90 LYS CA C 60.4 0.1 1
516 . 90 LYS CB C 33.1 0.1 1
517 . 90 LYS N N 118.6 0.1 1
518 . 91 ALA H H 7.66 0.03 1
519 . 91 ALA HA H 4.12 0.03 1
520 . 91 ALA C C 180.9 0.1 1
521 . 91 ALA CA C 55.2 0.1 1
522 . 91 ALA CB C 18.2 0.1 1
523 . 91 ALA N N 122.1 0.1 1
524 . 92 LEU H H 8.60 0.03 1
525 . 92 LEU HA H 3.80 0.03 1
526 . 92 LEU C C 180.2 0.1 1
527 . 92 LEU CA C 58.1 0.1 1
528 . 92 LEU CB C 41.7 0.1 1
529 . 92 LEU N N 117.6 0.1 1
530 . 93 LEU H H 8.62 0.03 1
531 . 93 LEU HA H 3.98 0.03 1
532 . 93 LEU C C 181.3 0.1 1
533 . 93 LEU CA C 58.8 0.1 1
534 . 93 LEU CB C 40.7 0.1 1
535 . 93 LEU N N 120.1 0.1 1
536 . 94 GLY H H 7.84 0.03 1
537 . 94 GLY HA2 H 4.09 0.03 2
538 . 94 GLY HA3 H 3.90 0.03 2
539 . 94 GLY C C 174.3 0.1 1
540 . 94 GLY CA C 46.7 0.1 1
541 . 94 GLY N N 106.7 0.1 1
542 . 95 LYS H H 7.24 0.03 1
543 . 95 LYS HA H 4.62 0.03 1
544 . 95 LYS C C 176.2 0.1 1
545 . 95 LYS CA C 53.8 0.1 1
546 . 95 LYS CB C 32.7 0.1 1
547 . 95 LYS N N 119.1 0.1 1
548 . 96 GLY H H 7.66 0.03 1
549 . 96 GLY HA2 H 4.14 0.03 2
550 . 96 GLY HA3 H 3.80 0.03 2
551 . 96 GLY C C 175.8 0.1 1
552 . 96 GLY CA C 46.4 0.1 1
553 . 96 GLY N N 105.2 0.1 1
554 . 97 ALA H H 7.76 0.03 1
555 . 97 ALA HA H 4.40 0.03 1
556 . 97 ALA C C 177.4 0.1 1
557 . 97 ALA CA C 52.9 0.1 1
558 . 97 ALA CB C 20.6 0.1 1
559 . 97 ALA N N 122.8 0.1 1
560 . 98 GLN H H 8.84 0.03 1
561 . 98 GLN HA H 4.25 0.03 1
562 . 98 GLN C C 177.5 0.1 1
563 . 98 GLN CA C 56.1 0.1 1
564 . 98 GLN CB C 28.8 0.1 1
565 . 98 GLN N N 121.2 0.1 1
566 . 99 VAL H H 8.16 0.03 1
567 . 99 VAL HA H 3.62 0.03 1
568 . 99 VAL C C 174.7 0.1 1
569 . 99 VAL CA C 64.6 0.1 1
570 . 99 VAL CB C 32.7 0.1 1
571 . 99 VAL N N 124.5 0.1 1
572 . 100 ASN H H 8.59 0.03 1
573 . 100 ASN HA H 5.07 0.03 1
574 . 100 ASN C C 173.9 0.1 1
575 . 100 ASN CA C 52.8 0.1 1
576 . 100 ASN CB C 39.2 0.1 1
577 . 100 ASN N N 116.8 0.1 1
578 . 101 ALA H H 6.46 0.03 1
579 . 101 ALA HA H 4.25 0.03 1
580 . 101 ALA C C 170.5 0.1 1
581 . 101 ALA CA C 53.1 0.1 1
582 . 101 ALA CB C 21.0 0.1 1
583 . 101 ALA N N 121.5 0.1 1
584 . 102 VAL H H 8.21 0.03 1
585 . 102 VAL HA H 5.00 0.03 1
586 . 102 VAL C C 176.0 0.1 1
587 . 102 VAL CA C 59.3 0.1 1
588 . 102 VAL CB C 35.7 0.1 1
589 . 102 VAL N N 111.6 0.1 1
590 . 103 ASN H H 7.34 0.03 1
591 . 103 ASN HA H 5.23 0.03 1
592 . 103 ASN C C 178.3 0.1 1
593 . 103 ASN CA C 50.8 0.1 1
594 . 103 ASN CB C 40.1 0.1 1
595 . 103 ASN N N 119.9 0.1 1
596 . 104 GLN H H 7.88 0.03 1
597 . 104 GLN HA H 4.20 0.03 1
598 . 104 GLN C C 175.5 0.1 1
599 . 104 GLN CA C 59.0 0.1 1
600 . 104 GLN CB C 28.1 0.1 1
601 . 104 GLN N N 117.1 0.1 1
602 . 105 ASN H H 7.23 0.03 1
603 . 105 ASN HA H 4.89 0.03 1
604 . 105 ASN C C 174.7 0.1 1
605 . 105 ASN CA C 53.5 0.1 1
606 . 105 ASN CB C 40.3 0.1 1
607 . 105 ASN N N 114.8 0.1 1
608 . 106 GLY H H 7.90 0.03 1
609 . 106 GLY HA2 H 3.35 0.03 1
610 . 106 GLY HA3 H 3.54 0.03 1
611 . 106 GLY C C 172.9 0.1 1
612 . 106 GLY CA C 46.1 0.1 1
613 . 106 GLY N N 108.0 0.1 1
614 . 107 CYS H H 7.33 0.03 1
615 . 107 CYS HA H 4.35 0.03 1
616 . 107 CYS C C 176.5 0.1 1
617 . 107 CYS CA C 58.7 0.1 1
618 . 107 CYS CB C 30.2 0.1 1
619 . 107 CYS N N 116.0 0.1 1
620 . 108 THR H H 10.76 0.03 1
621 . 108 THR HA H 5.67 0.03 1
622 . 108 THR CA C 59.8 0.1 1
623 . 108 THR CB C 69.3 0.1 1
624 . 108 THR N N 121.4 0.1 1
625 . 109 PRO C C 177.0 0.1 1
626 . 109 PRO CA C 66.7 0.1 1
627 . 109 PRO CB C 29.7 0.1 9
628 . 110 LEU H H 8.36 0.03 1
629 . 110 LEU HA H 3.94 0.03 1
630 . 110 LEU C C 177.9 0.1 1
631 . 110 LEU CA C 57.9 0.1 1
632 . 110 LEU CB C 40.8 0.1 1
633 . 110 LEU N N 117.0 0.1 1
634 . 111 HIS H H 7.60 0.03 1
635 . 111 HIS HA H 3.71 0.03 1
636 . 111 HIS C C 178.3 0.1 1
637 . 111 HIS CA C 64.5 0.1 1
638 . 111 HIS CB C 31.0 0.1 1
639 . 111 HIS N N 117.9 0.1 1
640 . 112 TYR H H 6.74 0.03 1
641 . 112 TYR HA H 4.40 0.03 1
642 . 112 TYR C C 177.8 0.1 1
643 . 112 TYR CA C 61.6 0.1 1
644 . 112 TYR CB C 38.4 0.1 1
645 . 112 TYR N N 114.9 0.1 1
646 . 113 ALA H H 8.27 0.03 1
647 . 113 ALA HA H 3.90 0.03 1
648 . 113 ALA C C 179.0 0.1 1
649 . 113 ALA CA C 55.6 0.1 1
650 . 113 ALA CB C 18.7 0.1 1
651 . 113 ALA N N 121.5 0.1 1
652 . 114 ALA H H 8.64 0.03 1
653 . 114 ALA HA H 4.24 0.03 1
654 . 114 ALA C C 179.8 0.1 1
655 . 114 ALA CA C 55.1 0.1 1
656 . 114 ALA CB C 20.0 0.1 1
657 . 114 ALA N N 117.1 0.1 1
658 . 115 SER H H 7.90 0.03 1
659 . 115 SER C C 175.7 0.1 1
660 . 115 SER CA C 62.3 0.1 1
661 . 115 SER N N 112.4 0.1 1
662 . 116 LYS H H 7.61 0.03 1
663 . 116 LYS HA H 4.54 0.03 1
664 . 116 LYS C C 175.1 0.1 1
665 . 116 LYS CA C 55.4 0.1 1
666 . 116 LYS CB C 32.5 0.1 1
667 . 116 LYS N N 116.4 0.1 1
668 . 117 ASN H H 7.44 0.03 1
669 . 117 ASN HA H 4.04 0.03 1
670 . 117 ASN C C 174.3 0.1 1
671 . 117 ASN CA C 54.7 0.1 1
672 . 117 ASN CB C 37.8 0.1 1
673 . 117 ASN N N 115.5 0.1 1
674 . 118 ARG H H 8.53 0.03 1
675 . 118 ARG HA H 4.62 0.03 1
676 . 118 ARG C C 175.8 0.1 1
677 . 118 ARG CA C 52.2 0.1 1
678 . 118 ARG CB C 27.1 0.1 1
679 . 118 ARG N N 115.6 0.1 1
680 . 119 HIS H H 7.39 0.03 1
681 . 119 HIS HA H 3.85 0.03 1
682 . 119 HIS C C 176.3 0.1 1
683 . 119 HIS CA C 62.1 0.1 1
684 . 119 HIS CB C 31.2 0.1 1
685 . 119 HIS N N 121.9 0.1 1
686 . 120 GLU H H 8.87 0.03 1
687 . 120 GLU HA H 4.01 0.03 1
688 . 120 GLU C C 180.6 0.1 1
689 . 120 GLU CA C 60.7 0.1 1
690 . 120 GLU CB C 28.2 0.1 1
691 . 120 GLU N N 118.8 0.1 1
692 . 121 ILE H H 8.12 0.03 1
693 . 121 ILE HA H 3.70 0.03 1
694 . 121 ILE C C 176.7 0.1 1
695 . 121 ILE CA C 65.6 0.1 1
696 . 121 ILE CB C 38.5 0.1 1
697 . 121 ILE N N 121.0 0.1 1
698 . 122 ALA H H 8.44 0.03 1
699 . 122 ALA HA H 3.67 0.03 1
700 . 122 ALA C C 178.4 0.1 1
701 . 122 ALA CA C 56.7 0.1 1
702 . 122 ALA CB C 18.2 0.1 1
703 . 122 ALA N N 121.9 0.1 1
704 . 123 VAL H H 7.82 0.03 1
705 . 123 VAL HA H 3.31 0.03 1
706 . 123 VAL C C 177.3 0.1 1
707 . 123 VAL CA C 68.2 0.1 1
708 . 123 VAL CB C 32.2 0.1 1
709 . 123 VAL N N 116.4 0.1 1
710 . 124 MET H H 7.77 0.03 1
711 . 124 MET HA H 3.86 0.03 1
712 . 124 MET C C 180.0 0.1 1
713 . 124 MET CA C 60.4 0.1 1
714 . 124 MET CB C 34.0 0.1 1
715 . 124 MET N N 117.5 0.1 1
716 . 125 LEU H H 8.36 0.03 1
717 . 125 LEU HA H 3.75 0.03 1
718 . 125 LEU C C 178.5 0.1 1
719 . 125 LEU CA C 58.0 0.1 1
720 . 125 LEU CB C 40.8 0.1 1
721 . 125 LEU N N 117.4 0.1 1
722 . 126 LEU H H 8.39 0.03 1
723 . 126 LEU HA H 3.73 0.03 1
724 . 126 LEU C C 181.7 0.1 1
725 . 126 LEU CA C 59.0 0.1 1
726 . 126 LEU CB C 38.9 0.1 1
727 . 126 LEU N N 122.3 0.1 1
728 . 127 GLU H H 9.20 0.03 1
729 . 127 GLU HA H 4.04 0.03 1
730 . 127 GLU C C 177.9 0.1 1
731 . 127 GLU CA C 59.5 0.1 1
732 . 127 GLU CB C 29.8 0.1 1
733 . 127 GLU N N 122.8 0.1 1
734 . 128 GLY H H 7.47 0.03 1
735 . 128 GLY HA2 H 4.34 0.03 2
736 . 128 GLY HA3 H 3.44 0.03 2
737 . 128 GLY C C 173.6 0.1 1
738 . 128 GLY CA C 45.4 0.1 1
739 . 128 GLY N N 105.2 0.1 1
740 . 129 GLY H H 7.33 0.03 1
741 . 129 GLY HA2 H 3.76 0.03 1
742 . 129 GLY HA3 H 4.35 0.03 1
743 . 129 GLY C C 175.2 0.1 1
744 . 129 GLY CA C 45.3 0.1 1
745 . 129 GLY N N 104.9 0.1 1
746 . 130 ALA H H 8.51 0.03 1
747 . 130 ALA HA H 3.98 0.03 1
748 . 130 ALA C C 176.1 0.1 1
749 . 130 ALA CA C 52.9 0.1 1
750 . 130 ALA CB C 19.3 0.1 1
751 . 130 ALA N N 123.9 0.1 1
752 . 131 ASN H H 9.04 0.03 1
753 . 131 ASN HA H 4.93 0.03 1
754 . 131 ASN CA C 50.1 0.1 1
755 . 131 ASN CB C 38.4 0.1 1
756 . 131 ASN N N 121.2 0.1 1
757 . 132 PRO C C 177.3 0.1 1
758 . 132 PRO CA C 64.5 0.1 1
759 . 133 ASP H H 7.63 0.03 1
760 . 133 ASP HA H 4.79 0.03 9
761 . 133 ASP C C 174.3 0.1 1
762 . 133 ASP CA C 53.6 0.1 1
763 . 133 ASP CB C 40.8 0.1 1
764 . 133 ASP N N 118.6 0.1 1
765 . 134 ALA H H 6.62 0.03 1
766 . 134 ALA HA H 4.03 0.03 1
767 . 134 ALA C C 177.9 0.1 1
768 . 134 ALA CA C 54.3 0.1 1
769 . 134 ALA CB C 19.1 0.1 1
770 . 134 ALA N N 122.6 0.1 1
771 . 135 LYS H H 8.85 0.03 1
772 . 135 LYS C C 176.9 0.1 1
773 . 135 LYS CA C 55.4 0.1 1
774 . 135 LYS CB C 36.8 0.1 1
775 . 135 LYS N N 123.7 0.1 1
776 . 136 ASP H H 8.55 0.03 1
777 . 136 ASP HA H 4.82 0.03 1
778 . 136 ASP C C 178.8 0.1 1
779 . 136 ASP CA C 52.9 0.1 1
780 . 136 ASP CB C 42.2 0.1 1
781 . 136 ASP N N 124.0 0.1 1
782 . 137 HIS H H 7.67 0.03 1
783 . 137 HIS HA H 4.57 0.03 1
784 . 137 HIS C C 176.1 0.1 1
785 . 137 HIS CA C 57.6 0.1 1
786 . 137 HIS CB C 30.2 0.1 1
787 . 137 HIS N N 115.6 0.1 1
788 . 138 TYR H H 8.52 0.03 1
789 . 138 TYR HA H 4.59 0.03 1
790 . 138 TYR C C 174.0 0.1 1
791 . 138 TYR CA C 57.9 0.1 1
792 . 138 TYR CB C 38.0 0.1 1
793 . 138 TYR N N 122.1 0.1 1
794 . 139 GLU H H 8.23 0.03 1
795 . 139 GLU HA H 3.62 0.03 1
796 . 139 GLU C C 171.3 0.1 1
797 . 139 GLU CA C 58.2 0.1 1
798 . 139 GLU CB C 27.0 0.1 1
799 . 139 GLU N N 113.2 0.1 1
800 . 140 ALA H H 8.11 0.03 1
801 . 140 ALA HA H 4.15 0.03 1
802 . 140 ALA C C 179.2 0.1 1
803 . 140 ALA CA C 51.1 0.1 1
804 . 140 ALA CB C 21.6 0.1 1
805 . 140 ALA N N 116.1 0.1 1
806 . 141 THR H H 9.14 0.03 1
807 . 141 THR HA H 5.23 0.03 1
808 . 141 THR C C 176.9 0.1 1
809 . 141 THR CA C 60.8 0.1 1
810 . 141 THR CB C 74.5 0.1 1
811 . 141 THR N N 114.6 0.1 1
812 . 142 ALA H H 10.24 0.03 1
813 . 142 ALA HA H 3.90 0.03 1
814 . 142 ALA C C 178.4 0.1 1
815 . 142 ALA CA C 56.1 0.1 1
816 . 142 ALA CB C 18.3 0.1 1
817 . 142 ALA N N 125.3 0.1 1
818 . 143 MET H H 9.15 0.03 1
819 . 143 MET HA H 3.90 0.03 1
820 . 143 MET C C 178.8 0.1 1
821 . 143 MET CA C 58.5 0.1 1
822 . 143 MET CB C 31.6 0.1 1
823 . 143 MET N N 119.0 0.1 1
824 . 144 HIS H H 8.04 0.03 1
825 . 144 HIS HA H 3.73 0.03 1
826 . 144 HIS C C 177.5 0.1 1
827 . 144 HIS CA C 64.6 0.1 1
828 . 144 HIS CB C 30.9 0.1 1
829 . 144 HIS N N 118.8 0.1 1
830 . 145 ARG H H 7.26 0.03 1
831 . 145 ARG HA H 4.10 0.03 1
832 . 145 ARG C C 178.5 0.1 1
833 . 145 ARG CA C 58.2 0.1 1
834 . 145 ARG CB C 30.2 0.1 1
835 . 145 ARG N N 115.2 0.1 1
836 . 146 ALA H H 8.37 0.03 1
837 . 146 ALA HA H 4.11 0.03 1
838 . 146 ALA C C 179.0 0.1 1
839 . 146 ALA CA C 55.2 0.1 1
840 . 146 ALA CB C 19.3 0.1 1
841 . 146 ALA N N 119.5 0.1 1
842 . 147 ALA H H 8.43 0.03 1
843 . 147 ALA HA H 3.85 0.03 1
844 . 147 ALA C C 178.0 0.1 1
845 . 147 ALA CA C 56.0 0.1 1
846 . 147 ALA CB C 20.2 0.1 1
847 . 147 ALA N N 119.5 0.1 1
848 . 148 ALA H H 7.59 0.03 1
849 . 148 ALA HA H 3.83 0.03 1
850 . 148 ALA C C 179.5 0.1 1
851 . 148 ALA CA C 55.3 0.1 1
852 . 148 ALA CB C 20.2 0.1 1
853 . 148 ALA N N 116.2 0.1 1
854 . 149 LYS H H 7.36 0.03 1
855 . 149 LYS HA H 4.28 0.03 1
856 . 149 LYS CA C 55.7 0.1 1
857 . 149 LYS CB C 33.4 0.1 1
858 . 149 LYS N N 111.4 0.1 1
859 . 150 GLY C C 173.3 0.1 1
860 . 150 GLY CA C 47.1 0.1 1
861 . 151 ASN H H 8.25 0.03 1
862 . 151 ASN HA H 5.11 0.03 1
863 . 151 ASN C C 175.2 0.1 1
864 . 151 ASN CA C 51.7 0.1 1
865 . 151 ASN CB C 38.5 0.1 1
866 . 151 ASN N N 119.4 0.1 1
867 . 152 LEU H H 7.60 0.03 1
868 . 152 LEU C C 178.0 0.1 1
869 . 152 LEU CA C 59.9 0.1 1
870 . 152 LEU N N 124.3 0.1 1
871 . 153 LYS H H 8.53 0.03 1
872 . 153 LYS C C 178.7 0.1 1
873 . 153 LYS CA C 60.1 0.1 1
874 . 153 LYS CB C 31.9 0.1 1
875 . 153 LYS N N 117.8 0.1 1
876 . 154 MET H H 7.90 0.03 1
877 . 154 MET C C 177.7 0.1 1
878 . 154 MET CA C 56.2 0.1 1
879 . 154 MET N N 116.7 0.1 1
880 . 155 ILE H H 7.88 0.03 1
881 . 155 ILE HA H 3.51 0.03 1
882 . 155 ILE C C 177.4 0.1 1
883 . 155 ILE CA C 67.1 0.1 1
884 . 155 ILE CB C 37.6 0.1 1
885 . 155 ILE N N 119.6 0.1 1
886 . 156 HIS H H 7.98 0.03 1
887 . 156 HIS HA H 4.09 0.03 1
888 . 156 HIS C C 179.3 0.1 1
889 . 156 HIS CA C 61.8 0.1 1
890 . 156 HIS N N 117.7 0.1 1
891 . 157 ILE H H 8.05 0.03 1
892 . 157 ILE HA H 3.82 0.03 1
893 . 157 ILE C C 177.5 0.1 1
894 . 157 ILE CA C 66.0 0.1 1
895 . 157 ILE CB C 39.1 0.1 1
896 . 157 ILE N N 120.9 0.1 1
897 . 158 LEU H H 8.30 0.03 1
898 . 158 LEU C C 179.4 0.1 1
899 . 158 LEU CA C 59.3 0.1 1
900 . 158 LEU CB C 41.2 0.1 1
901 . 158 LEU N N 119.0 0.1 1
902 . 159 LEU H H 8.64 0.03 1
903 . 159 LEU HA H 4.08 0.03 1
904 . 159 LEU C C 181.4 0.1 1
905 . 159 LEU CA C 58.2 0.1 1
906 . 159 LEU CB C 41.4 0.1 1
907 . 159 LEU N N 117.8 0.1 1
908 . 160 TYR H H 8.32 0.03 1
909 . 160 TYR HA H 4.03 0.03 1
910 . 160 TYR C C 177.3 0.1 1
911 . 160 TYR CA C 61.9 0.1 1
912 . 160 TYR CB C 37.9 0.1 1
913 . 160 TYR N N 124.5 0.1 1
914 . 161 TYR H H 7.49 0.03 1
915 . 161 TYR HA H 4.29 0.03 1
916 . 161 TYR C C 173.2 0.1 1
917 . 161 TYR CA C 59.8 0.1 1
918 . 161 TYR CB C 38.1 0.1 1
919 . 161 TYR N N 115.8 0.1 1
920 . 162 LYS H H 7.67 0.03 1
921 . 162 LYS HA H 3.85 0.03 1
922 . 162 LYS C C 176.3 0.1 1
923 . 162 LYS CA C 57.2 0.1 1
924 . 162 LYS CB C 27.9 0.1 1
925 . 162 LYS N N 109.5 0.1 1
926 . 163 ALA H H 8.14 0.03 1
927 . 163 ALA HA H 4.10 0.03 1
928 . 163 ALA C C 177.2 0.1 1
929 . 163 ALA CA C 53.2 0.1 1
930 . 163 ALA CB C 21.5 0.1 1
931 . 163 ALA N N 121.7 0.1 1
932 . 164 SER H H 10.09 0.03 1
933 . 164 SER HA H 4.51 0.03 1
934 . 164 SER C C 176.3 0.1 1
935 . 164 SER CA C 59.7 0.1 1
936 . 164 SER CB C 63.6 0.1 1
937 . 164 SER N N 118.9 0.1 1
938 . 165 THR H H 8.43 0.03 1
939 . 165 THR HA H 4.18 0.03 1
940 . 165 THR C C 175.2 0.1 1
941 . 165 THR CA C 63.1 0.1 1
942 . 165 THR CB C 70.3 0.1 1
943 . 165 THR N N 112.0 0.1 1
944 . 166 ASN H H 8.08 0.03 1
945 . 166 ASN HA H 5.11 0.03 1
946 . 166 ASN C C 174.0 0.1 1
947 . 166 ASN CA C 53.7 0.1 1
948 . 166 ASN CB C 39.7 0.1 1
949 . 166 ASN N N 119.0 0.1 1
950 . 167 ILE H H 6.96 0.03 1
951 . 167 ILE HA H 4.10 0.03 1
952 . 167 ILE C C 174.9 0.1 1
953 . 167 ILE CA C 62.4 0.1 1
954 . 167 ILE CB C 38.6 0.1 1
955 . 167 ILE N N 120.1 0.1 1
956 . 168 GLN H H 8.52 0.03 1
957 . 168 GLN HA H 4.57 0.03 1
958 . 168 GLN C C 174.9 0.1 1
959 . 168 GLN CA C 55.3 0.1 1
960 . 168 GLN CB C 33.9 0.1 1
961 . 168 GLN N N 124.7 0.1 1
962 . 169 ASP H H 8.20 0.03 1
963 . 169 ASP HA H 4.95 0.03 1
964 . 169 ASP C C 179.8 0.1 1
965 . 169 ASP CA C 53.4 0.1 1
966 . 169 ASP CB C 41.7 0.1 1
967 . 169 ASP N N 122.0 0.1 1
968 . 170 THR H H 7.92 0.03 1
969 . 170 THR HA H 4.01 0.03 1
970 . 170 THR C C 176.1 0.1 1
971 . 170 THR CA C 65.5 0.1 1
972 . 170 THR CB C 69.4 0.1 1
973 . 170 THR N N 111.3 0.1 1
974 . 171 GLU H H 8.18 0.03 1
975 . 171 GLU HA H 4.49 0.03 1
976 . 171 GLU C C 177.0 0.1 1
977 . 171 GLU CA C 56.7 0.1 1
978 . 171 GLU CB C 30.0 0.1 1
979 . 171 GLU N N 120.2 0.1 1
980 . 172 GLY H H 8.73 0.03 1
981 . 172 GLY C C 172.9 0.1 1
982 . 172 GLY CA C 46.2 0.1 1
983 . 172 GLY N N 110.6 0.1 1
984 . 173 ASN H H 8.69 0.03 1
985 . 173 ASN HA H 4.53 0.03 1
986 . 173 ASN C C 178.0 0.1 1
987 . 173 ASN CA C 54.3 0.1 1
988 . 173 ASN CB C 39.4 0.1 1
989 . 173 ASN N N 119.8 0.1 1
990 . 174 THR H H 10.78 0.03 1
991 . 174 THR HA H 5.63 0.03 1
992 . 174 THR CA C 60.1 0.1 1
993 . 174 THR CB C 69.1 0.1 1
994 . 174 THR N N 122.1 0.1 1
995 . 175 PRO C C 176.8 0.1 1
996 . 175 PRO CA C 66.2 0.1 1
997 . 175 PRO CB C 31.5 0.1 1
998 . 176 LEU H H 8.60 0.03 1
999 . 176 LEU HA H 4.01 0.03 1
1000 . 176 LEU C C 179.3 0.1 1
1001 . 176 LEU CA C 58.0 0.1 1
1002 . 176 LEU CB C 41.5 0.1 1
1003 . 176 LEU N N 115.3 0.1 1
1004 . 177 HIS H H 7.82 0.03 1
1005 . 177 HIS HA H 3.65 0.03 1
1006 . 177 HIS C C 177.5 0.1 1
1007 . 177 HIS CA C 64.7 0.1 1
1008 . 177 HIS CB C 31.9 0.1 1
1009 . 177 HIS N N 118.3 0.1 1
1010 . 178 LEU H H 7.18 0.03 1
1011 . 178 LEU HA H 4.16 0.03 1
1012 . 178 LEU C C 179.2 0.1 1
1013 . 178 LEU CA C 58.1 0.1 1
1014 . 178 LEU CB C 40.4 0.1 1
1015 . 178 LEU N N 114.7 0.1 1
1016 . 179 ALA H H 8.22 0.03 1
1017 . 179 ALA C C 179.7 0.1 1
1018 . 179 ALA CA C 55.1 0.1 1
1019 . 179 ALA CB C 18.2 0.1 1
1020 . 179 ALA N N 119.7 0.1 1
1021 . 180 CYS H H 8.22 0.03 1
1022 . 180 CYS HA H 4.00 0.03 1
1023 . 180 CYS C C 177.8 0.1 1
1024 . 180 CYS CA C 65.0 0.1 1
1025 . 180 CYS CB C 27.6 0.1 1
1026 . 180 CYS N N 114.8 0.1 1
1027 . 181 ASP H H 8.56 0.03 1
1028 . 181 ASP HA H 4.55 0.03 1
1029 . 181 ASP C C 177.2 0.1 1
1030 . 181 ASP CA C 57.8 0.1 1
1031 . 181 ASP CB C 42.6 0.1 1
1032 . 181 ASP N N 122.5 0.1 1
1033 . 182 GLU H H 7.40 0.03 1
1034 . 182 GLU HA H 4.49 0.03 1
1035 . 182 GLU C C 174.8 0.1 1
1036 . 182 GLU CA C 56.6 0.1 1
1037 . 182 GLU CB C 30.3 0.1 1
1038 . 182 GLU N N 113.0 0.1 1
1039 . 183 GLU H H 7.78 0.03 1
1040 . 183 GLU HA H 3.46 0.03 1
1041 . 183 GLU C C 174.9 0.1 1
1042 . 183 GLU CA C 58.0 0.1 1
1043 . 183 GLU CB C 28.9 0.1 1
1044 . 183 GLU N N 118.2 0.1 1
1045 . 184 ARG H H 8.83 0.03 1
1046 . 184 ARG HA H 4.52 0.03 1
1047 . 184 ARG C C 175.5 0.1 1
1048 . 184 ARG CA C 53.1 0.1 1
1049 . 184 ARG CB C 28.8 0.1 1
1050 . 184 ARG N N 119.5 0.1 1
1051 . 185 VAL H H 7.47 0.03 1
1052 . 185 VAL HA H 3.46 0.03 1
1053 . 185 VAL C C 177.6 0.1 1
1054 . 185 VAL CA C 67.8 0.1 1
1055 . 185 VAL CB C 32.8 0.1 1
1056 . 185 VAL N N 122.1 0.1 1
1057 . 186 GLU H H 8.79 0.03 1
1058 . 186 GLU HA H 3.90 0.03 1
1059 . 186 GLU C C 179.7 0.1 1
1060 . 186 GLU CA C 59.5 0.1 1
1061 . 186 GLU CB C 28.8 0.1 1
1062 . 186 GLU N N 117.8 0.1 1
1063 . 187 GLU H H 10.24 0.03 1
1064 . 187 GLU HA H 3.58 0.03 1
1065 . 187 GLU C C 177.4 0.1 1
1066 . 187 GLU CA C 62.1 0.1 1
1067 . 187 GLU CB C 28.2 0.1 1
1068 . 187 GLU N N 123.7 0.1 1
1069 . 188 ALA H H 8.45 0.03 1
1070 . 188 ALA HA H 3.76 0.03 1
1071 . 188 ALA C C 178.8 0.1 1
1072 . 188 ALA CA C 55.7 0.1 1
1073 . 188 ALA CB C 19.7 0.1 1
1074 . 188 ALA N N 120.7 0.1 1
1075 . 189 LYS H H 8.06 0.03 1
1076 . 189 LYS HA H 3.57 0.03 1
1077 . 189 LYS C C 178.6 0.1 1
1078 . 189 LYS CA C 60.5 0.1 1
1079 . 189 LYS CB C 32.9 0.1 1
1080 . 189 LYS N N 115.6 0.1 1
1081 . 190 LEU H H 7.92 0.03 1
1082 . 190 LEU HA H 4.07 0.03 1
1083 . 190 LEU C C 179.7 0.1 1
1084 . 190 LEU CA C 58.0 0.1 1
1085 . 190 LEU CB C 41.2 0.1 1
1086 . 190 LEU N N 120.5 0.1 1
1087 . 191 LEU H H 8.13 0.03 1
1088 . 191 LEU HA H 3.70 0.03 1
1089 . 191 LEU C C 179.2 0.1 1
1090 . 191 LEU CA C 59.2 0.1 1
1091 . 191 LEU CB C 41.1 0.1 1
1092 . 191 LEU N N 118.6 0.1 1
1093 . 192 VAL H H 8.20 0.03 1
1094 . 192 VAL HA H 3.88 0.03 1
1095 . 192 VAL C C 179.9 0.1 1
1096 . 192 VAL CA C 67.4 0.1 1
1097 . 192 VAL CB C 31.8 0.1 1
1098 . 192 VAL N N 119.5 0.1 1
1099 . 193 SER H H 8.56 0.03 1
1100 . 193 SER HA H 4.30 0.03 1
1101 . 193 SER C C 174.9 0.1 1
1102 . 193 SER CA C 61.9 0.1 1
1103 . 193 SER CB C 63.6 0.1 1
1104 . 193 SER N N 118.2 0.1 1
1105 . 194 GLN H H 7.35 0.03 1
1106 . 194 GLN HA H 4.53 0.03 1
1107 . 194 GLN C C 175.7 0.1 1
1108 . 194 GLN CA C 55.2 0.1 1
1109 . 194 GLN CB C 28.4 0.1 1
1110 . 194 GLN N N 118.3 0.1 1
1111 . 195 GLY H H 7.53 0.03 1
1112 . 195 GLY HA2 H 4.37 0.03 2
1113 . 195 GLY HA3 H 3.72 0.03 2
1114 . 195 GLY C C 174.9 0.1 1
1115 . 195 GLY CA C 46.1 0.1 1
1116 . 195 GLY N N 105.9 0.1 1
1117 . 196 ALA H H 8.39 0.03 1
1118 . 196 ALA HA H 4.38 0.03 1
1119 . 196 ALA C C 177.2 0.1 1
1120 . 196 ALA CA C 53.1 0.1 1
1121 . 196 ALA CB C 20.8 0.1 1
1122 . 196 ALA N N 125.8 0.1 1
1123 . 197 SER H H 9.04 0.03 1
1124 . 197 SER HA H 4.07 0.03 1
1125 . 197 SER C C 177.7 0.1 1
1126 . 197 SER CA C 57.4 0.1 1
1127 . 197 SER CB C 64.5 0.1 1
1128 . 197 SER N N 116.6 0.1 1
1129 . 198 ILE H H 7.97 0.03 1
1130 . 198 ILE HA H 3.87 0.03 1
1131 . 198 ILE C C 175.0 0.1 1
1132 . 198 ILE CA C 62.7 0.1 1
1133 . 198 ILE CB C 37.7 0.1 1
1134 . 198 ILE N N 118.4 0.1 1
1135 . 199 TYR H H 8.12 0.03 1
1136 . 199 TYR HA H 4.67 0.03 1
1137 . 199 TYR C C 175.5 0.1 1
1138 . 199 TYR CA C 58.4 0.1 1
1139 . 199 TYR CB C 40.5 0.1 1
1140 . 199 TYR N N 117.8 0.1 1
1141 . 200 ILE H H 6.36 0.03 1
1142 . 200 ILE HA H 3.98 0.03 1
1143 . 200 ILE C C 174.6 0.1 1
1144 . 200 ILE CA C 62.1 0.1 1
1145 . 200 ILE CB C 39.8 0.1 1
1146 . 200 ILE N N 120.1 0.1 1
1147 . 201 GLU H H 8.57 0.03 1
1148 . 201 GLU HA H 4.37 0.03 1
1149 . 201 GLU C C 176.9 0.1 1
1150 . 201 GLU CA C 55.8 0.1 1
1151 . 201 GLU CB C 32.4 0.1 1
1152 . 201 GLU N N 126.4 0.1 1
1153 . 202 ASN H H 8.13 0.03 1
1154 . 202 ASN C C 178.0 0.1 1
1155 . 202 ASN CA C 51.4 0.1 1
1156 . 202 ASN CB C 38.7 0.1 1
1157 . 202 ASN N N 119.6 0.1 1
1158 . 203 LYS H H 7.86 0.03 1
1159 . 203 LYS HA H 4.08 0.03 1
1160 . 203 LYS C C 177.6 0.1 1
1161 . 203 LYS CA C 59.8 0.1 1
1162 . 203 LYS CB C 32.3 0.1 1
1163 . 203 LYS N N 117.4 0.1 1
1164 . 204 GLU H H 7.44 0.03 1
1165 . 204 GLU HA H 4.38 0.03 1
1166 . 204 GLU C C 174.6 0.1 1
1167 . 204 GLU CA C 56.5 0.1 1
1168 . 204 GLU CB C 29.6 0.1 1
1169 . 204 GLU N N 119.0 0.1 1
1170 . 205 GLU H H 8.17 0.03 1
1171 . 205 GLU HA H 3.76 0.03 1
1172 . 205 GLU C C 174.8 0.1 1
1173 . 205 GLU CA C 58.2 0.1 1
1174 . 205 GLU CB C 26.7 0.1 1
1175 . 205 GLU N N 112.7 0.1 1
1176 . 206 LYS H H 7.67 0.03 1
1177 . 206 LYS HA H 5.27 0.03 1
1178 . 206 LYS C C 178.9 0.1 1
1179 . 206 LYS CA C 54.3 0.1 1
1180 . 206 LYS CB C 35.3 0.1 1
1181 . 206 LYS N N 114.7 0.1 1
1182 . 207 THR H H 9.29 0.03 1
1183 . 207 THR HA H 5.33 0.03 1
1184 . 207 THR CA C 60.8 0.1 1
1185 . 207 THR CB C 69.0 0.1 1
1186 . 207 THR N N 118.0 0.1 1
1187 . 208 PRO HA H 3.90 0.03 1
1188 . 208 PRO C C 176.8 0.1 1
1189 . 208 PRO CA C 65.5 0.1 1
1190 . 209 LEU H H 6.59 0.03 1
1191 . 209 LEU HA H 3.80 0.03 1
1192 . 209 LEU C C 179.2 0.1 1
1193 . 209 LEU CA C 57.5 0.1 1
1194 . 209 LEU CB C 40.6 0.1 1
1195 . 209 LEU N N 107.2 0.1 1
1196 . 210 GLN H H 7.35 0.03 1
1197 . 210 GLN HA H 4.21 0.03 1
1198 . 210 GLN C C 177.6 0.1 1
1199 . 210 GLN CA C 58.1 0.1 1
1200 . 210 GLN CB C 30.7 0.1 1
1201 . 210 GLN N N 116.1 0.1 1
1202 . 211 VAL H H 7.17 0.03 1
1203 . 211 VAL HA H 4.40 0.03 1
1204 . 211 VAL C C 175.2 0.1 1
1205 . 211 VAL CA C 61.9 0.1 1
1206 . 211 VAL CB C 32.3 0.1 1
1207 . 211 VAL N N 112.2 0.1 1
1208 . 212 ALA H H 6.94 0.03 1
1209 . 212 ALA HA H 4.10 0.03 1
1210 . 212 ALA C C 176.9 0.1 1
1211 . 212 ALA CA C 52.9 0.1 1
1212 . 212 ALA CB C 19.2 0.1 1
1213 . 212 ALA N N 121.5 0.1 1
1214 . 213 LYS H H 8.26 0.03 1
1215 . 213 LYS HA H 4.57 0.03 1
1216 . 213 LYS C C 177.9 0.1 1
1217 . 213 LYS CA C 55.5 0.1 1
1218 . 213 LYS CB C 35.3 0.1 1
1219 . 213 LYS N N 123.2 0.1 1
1220 . 214 GLY H H 8.76 0.03 1
1221 . 214 GLY CA C 47.4 0.1 1
1222 . 214 GLY N N 108.1 0.1 1
1223 . 215 GLY C C 175.9 0.1 1
1224 . 215 GLY CA C 45.7 0.1 1
1225 . 216 LEU H H 7.73 0.03 1
1226 . 216 LEU HA H 4.14 0.03 1
1227 . 216 LEU C C 177.5 0.1 1
1228 . 216 LEU CA C 58.0 0.1 1
1229 . 216 LEU CB C 42.2 0.1 1
1230 . 216 LEU N N 121.8 0.1 1
1231 . 217 GLY H H 8.60 0.03 1
1232 . 217 GLY HA2 H 3.95 0.03 2
1233 . 217 GLY HA3 H 3.47 0.03 2
1234 . 217 GLY C C 175.0 0.1 1
1235 . 217 GLY CA C 47.8 0.1 1
1236 . 217 GLY N N 106.2 0.1 1
1237 . 218 LEU H H 7.38 0.03 1
1238 . 218 LEU HA H 4.09 0.03 1
1239 . 218 LEU C C 179.3 0.1 1
1240 . 218 LEU CA C 58.0 0.1 1
1241 . 218 LEU CB C 41.9 0.1 1
1242 . 218 LEU N N 120.2 0.1 1
1243 . 219 ILE H H 7.12 0.03 1
1244 . 219 ILE HA H 3.60 0.03 1
1245 . 219 ILE C C 179.0 0.1 1
1246 . 219 ILE CA C 65.0 0.1 1
1247 . 219 ILE CB C 38.6 0.1 1
1248 . 219 ILE N N 119.1 0.1 1
1249 . 220 LEU H H 7.96 0.03 1
1250 . 220 LEU C C 178.4 0.1 1
1251 . 220 LEU CA C 57.8 0.1 1
1252 . 220 LEU CB C 39.0 0.1 1
1253 . 220 LEU N N 117.4 0.1 1
1254 . 221 LYS H H 8.07 0.03 1
1255 . 221 LYS C C 178.8 0.1 1
1256 . 221 LYS CA C 60.6 0.1 1
1257 . 221 LYS CB C 33.4 0.1 1
1258 . 221 LYS N N 118.3 0.1 1
1259 . 222 ARG H H 7.82 0.03 1
1260 . 222 ARG HA H 4.14 0.03 1
1261 . 222 ARG C C 179.3 0.1 1
1262 . 222 ARG CA C 58.9 0.1 1
1263 . 222 ARG CB C 29.8 0.1 1
1264 . 222 ARG N N 116.9 0.1 1
1265 . 223 MET H H 7.68 0.03 1
1266 . 223 MET HA H 4.00 0.03 1
1267 . 223 MET C C 177.3 0.1 1
1268 . 223 MET CA C 59.7 0.1 1
1269 . 223 MET CB C 33.7 0.1 1
1270 . 223 MET N N 118.1 0.1 1
1271 . 224 VAL H H 7.26 0.03 1
1272 . 224 VAL HA H 3.97 0.03 1
1273 . 224 VAL C C 177.3 0.1 1
1274 . 224 VAL CA C 65.2 0.1 1
1275 . 224 VAL CB C 34.1 0.1 1
1276 . 224 VAL N N 116.8 0.1 1
1277 . 225 GLU H H 8.62 0.03 1
1278 . 225 GLU HA H 4.33 0.03 1
1279 . 225 GLU C C 176.9 0.1 1
1280 . 225 GLU CA C 57.7 0.1 1
1281 . 225 GLU CB C 30.8 0.1 1
1282 . 225 GLU N N 117.9 0.1 1
1283 . 226 GLY H H 7.74 0.03 1
1284 . 226 GLY HA2 H 3.98 0.03 2
1285 . 226 GLY HA3 H 3.68 0.03 2
1286 . 226 GLY CA C 46.6 0.1 1
1287 . 226 GLY N N 115.1 0.1 1
stop_
save_