data_4455
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Glycan-free mutant adhesion domain of human CD58 (LFA-3)
;
_BMRB_accession_number 4455
_BMRB_flat_file_name bmr4455.str
_Entry_type original
_Submission_date 1999-11-11
_Accession_date 1999-11-11
_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 Sun 'Z. Y.' J. .
2 Dotsch V. . .
3 Kim M. . .
4 Li J. . .
5 Reinherz E. L. .
6 Wagner G. . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 517
"13C chemical shifts" 375
"15N chemical shifts" 97
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
1999-12-22 original BMRB .
stop_
_Original_release_date 1999-11-11
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title
;
Functional Glycan-free Adhesion Domain of Human Cell Surface Receptor CD58:
Design, Production, and NMR Studies
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 99286218
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Sun 'Z. Y.' J. .
2 Dotsch V. . .
3 Kim M. . .
4 Li J. . .
5 Reinherz E. L. .
6 Wagner G. . .
stop_
_Journal_abbreviation 'EMBO J.'
_Journal_name_full 'EMBO Journal'
_Journal_volume 18
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 2941
_Page_last 2949
_Year 1999
_Details .
loop_
_Keyword
'adhesion glycoprotein'
'cell surface receptor'
'immunoglobulin superfamily V-set domain'
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full
;
Sun ZY, Dotsch V, Kim M, Li J, Reinherz EL, Wagner G
Functional glycan-free adhesion domain of human cell surface receptor CD58:
design, production and NMR studies. EMBO J. 1999 Jun 1;18(11):2941-9.
;
_Citation_title
;
Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies.
;
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 10357807
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Sun 'Z. Y.' Y. .
2 Dotsch V. . .
3 Kim M. . .
4 Li J. . .
5 Reinherz 'E. L.' L. .
6 Wagner G. . .
stop_
_Journal_abbreviation 'EMBO J.'
_Journal_name_full 'The EMBO journal'
_Journal_volume 18
_Journal_issue 11
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first 2941
_Page_last 2949
_Year 1999
_Details
;
A general strategy is presented here for producing glycan-free forms of
glycoproteins without loss of function by employing apolar-to-polar mutations
of surface residues in functionally irrelevant epitopes. The success of this
structure-based approach was demonstrated through the expression in Escherichia
coli of a soluble 11 kDa adhesion domain extracted from the heavily
glycosylated 55 kDa human CD58 ectodomain. The solution structure was
subsequently determined and binding to its counter-receptor CD2 studied by NMR.
This mutant adhesion domain is functional as determined by several experimental
methods, and the size of its binding site has been probed by chemical shift
perturbations in NMR titration experiments. The new structural information
supports a 'hand-shake' model of CD2-CD58 interaction involving the GFCC'C"
faces of both CD2 and CD58 adhesion domains. The region responsible for binding
specificity is most likely localized on the C, C' and C" strands and the C-C'
and C'-C" loops on CD58.
;
save_
save_ref_2
_Saveframe_category citation
_Citation_full
;
Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J.,
Oldfield, E., Markley, J. L., and Sykes, B. D.
J. Biomol. NMR 6, 135-140 (1995).
;
_Citation_title .
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Wishart D. . .
stop_
_Journal_abbreviation .
_Journal_name_full .
_Journal_volume .
_Journal_issue .
_Journal_CSD .
_Book_title .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_publisher .
_Book_publisher_city .
_Book_ISBN .
_Conference_title .
_Conference_site .
_Conference_state_province .
_Conference_country .
_Conference_start_date .
_Conference_end_date .
_Conference_abstract_number .
_Thesis_institution .
_Thesis_institution_city .
_Thesis_institution_country .
_Page_first .
_Page_last .
_Year .
_Details .
save_
##################################
# Molecular system description #
##################################
save_system_1dCD58
_Saveframe_category molecular_system
_Mol_system_name 'CD58 adhesion domain, 1dCD58'
_Abbreviation_common 1dCD58
_Enzyme_commission_number .
loop_
_Mol_system_component_name
_Mol_label
1dCD58 $1dCD58
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'not present'
_Database_query_date .
_Details
;
Biological_function:
CD58 adhesion domain responsible for binding to counter receptor CD2 on T-cell surface.
;
save_
########################
# Monomeric polymers #
########################
save_1dCD58
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 1dCD58
_Name_variant F1S/V9K/V21Q/V58K/T85S/L93G
_Abbreviation_common 1dCD58
_Molecular_mass 11200
_Mol_thiol_state 'not present'
_Details 'CD58 in human is heavily glycosylated'
##############################
# Polymer residue sequence #
##############################
_Residue_count 95
_Mol_residue_sequence
;
SSQQIYGVKYGNVTFHVPSN
QPLKEVLWKKQKDKVAELEN
SEFRAFSSFKNRVYLDTKSG
SLTIYNLTSSDEDEYEMESP
NITDSMKFFLYVGES
;
loop_
_Residue_seq_code
_Residue_label
1 SER 2 SER 3 GLN 4 GLN 5 ILE
6 TYR 7 GLY 8 VAL 9 LYS 10 TYR
11 GLY 12 ASN 13 VAL 14 THR 15 PHE
16 HIS 17 VAL 18 PRO 19 SER 20 ASN
21 GLN 22 PRO 23 LEU 24 LYS 25 GLU
26 VAL 27 LEU 28 TRP 29 LYS 30 LYS
31 GLN 32 LYS 33 ASP 34 LYS 35 VAL
36 ALA 37 GLU 38 LEU 39 GLU 40 ASN
41 SER 42 GLU 43 PHE 44 ARG 45 ALA
46 PHE 47 SER 48 SER 49 PHE 50 LYS
51 ASN 52 ARG 53 VAL 54 TYR 55 LEU
56 ASP 57 THR 58 LYS 59 SER 60 GLY
61 SER 62 LEU 63 THR 64 ILE 65 TYR
66 ASN 67 LEU 68 THR 69 SER 70 SER
71 ASP 72 GLU 73 ASP 74 GLU 75 TYR
76 GLU 77 MET 78 GLU 79 SER 80 PRO
81 ASN 82 ILE 83 THR 84 ASP 85 SER
86 MET 87 LYS 88 PHE 89 PHE 90 LEU
91 TYR 92 VAL 93 GLY 94 GLU 95 SER
stop_
_Sequence_homology_query_date 2008-08-19
_Sequence_homology_query_revised_last_date 2008-08-19
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 1CI5 'Glycan-Free Mutant Adhesion Domain Of Human Cd58 (Lfa-3)' 100.00 95 100.00 100.00 1.63e-48
PDB 1QA9 'Structure Of A Heterophilic Adhesion Complex Between The Human Cd2 And Cd58(Lfa-3) Counter-Receptors' 100.00 95 100.00 100.00 1.63e-48
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Plasmid
_Gene_mnemonic
$1dCD58 Human 9606 Eukaryota Metazoa Homo sapiens pET11a-1dCD58x6 1dCD58x6
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Vector_type
_Vector_name
$1dCD58 'recombinant technology' 'E. coli' Escherichia coli BL21(DE3) plasmid pET11a
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
$1dCD58 . mM 0.2 0.6 '[U-13C; U-15N]'
NaPO4 10 mM . . .
D2O 10 % . . .
stop_
save_
############################
# Computer software used #
############################
save_XEASY
_Saveframe_category software
_Name XEASY
_Version .
_Details .
save_
save_DIANA
_Saveframe_category software
_Name DIANA
_Version .
_Details .
save_
save_DYANA
_Saveframe_category software
_Name DYANA
_Version .
_Details .
save_
save_XPLOR
_Saveframe_category software
_Name XPLOR
_Version .
_Details .
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AMX
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UnityInova
_Field_strength 500
_Details .
save_
save_NMR_spectrometer_3
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model UnityInova
_Field_strength 750
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_NOESY_1
_Saveframe_category NMR_applied_experiment
_Experiment_name NOESY
_Sample_label $sample_1
save_
save_NOESY-HSQC_2
_Saveframe_category NMR_applied_experiment
_Experiment_name NOESY-HSQC
_Sample_label $sample_1
save_
save_HNCA_3
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCA
_Sample_label $sample_1
save_
save_CBCA(CO)NH_4
_Saveframe_category NMR_applied_experiment
_Experiment_name CBCA(CO)NH
_Sample_label $sample_1
save_
save_HBHA(CBCACO)NH_5
_Saveframe_category NMR_applied_experiment
_Experiment_name HBHA(CBCACO)NH
_Sample_label $sample_1
save_
save_HCCH-TOCSY_6
_Saveframe_category NMR_applied_experiment
_Experiment_name HCCH-TOCSY
_Sample_label $sample_1
save_
save_HNHA_7
_Saveframe_category NMR_applied_experiment
_Experiment_name HNHA
_Sample_label $sample_1
save_
save_HNHB_8
_Saveframe_category NMR_applied_experiment
_Experiment_name HNHB
_Sample_label $sample_1
save_
save_HNCO_9
_Saveframe_category NMR_applied_experiment
_Experiment_name HNCO
_Sample_label $sample_1
save_
save_HN(CA)CO_10
_Saveframe_category NMR_applied_experiment
_Experiment_name HN(CA)CO
_Sample_label $sample_1
save_
#######################
# Sample conditions #
#######################
save_sample_cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
'ionic strength' 0.01 . M
pH 7.5 0.1 n/a
pressure 1 . atm
temperature 298 1 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference
_Saveframe_category chemical_shift_reference
_Details .
loop_
_Mol_common_name
_Atom_type
_Atom_isotope_number
_Atom_group
_Chem_shift_units
_Chem_shift_value
_Reference_method
_Reference_type
_External_reference_sample_geometry
_External_reference_location
_External_reference_axis
_Indirect_shift_ratio
DSS C 13 'methyl protons' ppm 0.00 . indirect . . . 0.251449530
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0
DSS N 15 'methyl protons' ppm 0.00 . 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_chem_shift_set_1
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_1
stop_
_Sample_conditions_label $sample_cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 1dCD58
_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 . 2 SER HA H 4.78 . 1
2 . 2 SER HB2 H 3.73 . 2
3 . 2 SER HB3 H 3.67 . 2
4 . 2 SER C C 173.92 . 1
5 . 2 SER CA C 57.39 . 1
6 . 2 SER CB C 64.36 . 1
7 . 3 GLN H H 8.13 . 1
8 . 3 GLN HA H 4.59 . 1
9 . 3 GLN HB2 H 2.12 . 2
10 . 3 GLN HB3 H 1.88 . 2
11 . 3 GLN HG2 H 2.30 . 2
12 . 3 GLN HE21 H 7.53 . 2
13 . 3 GLN HE22 H 7.00 . 2
14 . 3 GLN C C 174.95 . 1
15 . 3 GLN CA C 55.23 . 1
16 . 3 GLN CB C 31.26 . 1
17 . 3 GLN CG C 34.10 . 1
18 . 3 GLN N N 122.48 . 1
19 . 3 GLN NE2 N 112.12 . 1
20 . 4 GLN H H 8.84 . 1
21 . 4 GLN HA H 5.18 . 1
22 . 4 GLN HB2 H 2.37 . 2
23 . 4 GLN HB3 H 2.14 . 2
24 . 4 GLN HG2 H 2.59 . 2
25 . 4 GLN HG3 H 2.54 . 2
26 . 4 GLN HE21 H 7.42 . 2
27 . 4 GLN HE22 H 6.89 . 2
28 . 4 GLN C C 174.56 . 1
29 . 4 GLN CA C 55.80 . 1
30 . 4 GLN CB C 30.37 . 1
31 . 4 GLN CG C 34.62 . 1
32 . 4 GLN N N 123.37 . 1
33 . 4 GLN NE2 N 112.42 . 1
34 . 5 ILE H H 9.44 . 1
35 . 5 ILE HA H 4.61 . 1
36 . 5 ILE HB H 2.00 . 1
37 . 5 ILE HG12 H 1.65 . 2
38 . 5 ILE HG13 H 1.55 . 2
39 . 5 ILE HG2 H 0.96 . 1
40 . 5 ILE HD1 H 1.01 . 1
41 . 5 ILE C C 172.92 . 1
42 . 5 ILE CA C 58.92 . 1
43 . 5 ILE CB C 39.86 . 1
44 . 5 ILE CG1 C 27.46 . 1
45 . 5 ILE CG2 C 18.00 . 1
46 . 5 ILE CD1 C 11.84 . 1
47 . 5 ILE N N 125.53 . 1
48 . 6 TYR H H 8.67 . 1
49 . 6 TYR HA H 5.13 . 1
50 . 6 TYR HB2 H 3.11 . 2
51 . 6 TYR HB3 H 2.88 . 2
52 . 6 TYR HD1 H 7.21 . 3
53 . 6 TYR HE1 H 6.55 . 3
54 . 6 TYR C C 175.70 . 1
55 . 6 TYR CA C 57.72 . 1
56 . 6 TYR CB C 39.02 . 1
57 . 6 TYR N N 125.09 . 1
58 . 7 GLY H H 9.14 . 1
59 . 7 GLY HA2 H 4.66 . 1
60 . 7 GLY HA3 H 3.20 . 1
61 . 7 GLY C C 172.02 . 1
62 . 7 GLY CA C 43.16 . 1
63 . 7 GLY N N 111.96 . 1
64 . 8 VAL H H 8.28 . 1
65 . 8 VAL HA H 4.57 . 1
66 . 8 VAL HB H 1.86 . 1
67 . 8 VAL HG1 H 0.87 . 2
68 . 8 VAL HG2 H 0.82 . 2
69 . 8 VAL C C 174.52 . 1
70 . 8 VAL CA C 59.60 . 1
71 . 8 VAL CB C 35.23 . 1
72 . 8 VAL CG1 C 21.43 . 1
73 . 8 VAL CG2 C 20.18 . 1
74 . 8 VAL N N 117.29 . 1
75 . 9 LYS H H 8.19 . 1
76 . 9 LYS HA H 3.25 . 1
77 . 9 LYS HB2 H 1.37 . 2
78 . 9 LYS HB3 H 1.30 . 2
79 . 9 LYS HG2 H 1.49 . 2
80 . 9 LYS HD2 H 0.98 . 2
81 . 9 LYS HD3 H 0.35 . 2
82 . 9 LYS HE2 H 2.77 . 2
83 . 9 LYS C C 176.60 . 1
84 . 9 LYS CA C 58.35 . 1
85 . 9 LYS CB C 32.32 . 1
86 . 9 LYS CG C 29.57 . 1
87 . 9 LYS CD C 24.96 . 1
88 . 9 LYS CE C 41.52 . 1
89 . 9 LYS N N 124.77 . 1
90 . 10 TYR H H 9.60 . 1
91 . 10 TYR HA H 4.41 . 1
92 . 10 TYR HB2 H 3.35 . 2
93 . 10 TYR HD1 H 7.15 . 3
94 . 10 TYR HE1 H 6.83 . 3
95 . 10 TYR C C 176.05 . 1
96 . 10 TYR CA C 59.57 . 1
97 . 10 TYR CB C 35.95 . 1
98 . 10 TYR N N 119.31 . 1
99 . 11 GLY H H 8.89 . 1
100 . 11 GLY HA2 H 4.47 . 1
101 . 11 GLY HA3 H 3.81 . 1
102 . 11 GLY C C 171.09 . 1
103 . 11 GLY CA C 44.01 . 1
104 . 11 GLY N N 111.17 . 1
105 . 12 ASN H H 8.19 . 1
106 . 12 ASN HA H 5.72 . 1
107 . 12 ASN HB2 H 2.41 . 2
108 . 12 ASN HB3 H 2.23 . 2
109 . 12 ASN HD21 H 7.46 . 2
110 . 12 ASN HD22 H 7.00 . 2
111 . 12 ASN C C 175.13 . 1
112 . 12 ASN CA C 50.75 . 1
113 . 12 ASN CB C 42.37 . 1
114 . 12 ASN N N 112.75 . 1
115 . 12 ASN ND2 N 113.52 . 1
116 . 13 VAL H H 8.35 . 1
117 . 13 VAL HA H 4.44 . 1
118 . 13 VAL HB H 1.74 . 1
119 . 13 VAL HG1 H 0.55 . 2
120 . 13 VAL HG2 H 0.54 . 2
121 . 13 VAL C C 171.71 . 1
122 . 13 VAL CA C 60.20 . 1
123 . 13 VAL CB C 35.65 . 1
124 . 13 VAL CG1 C 21.21 . 1
125 . 13 VAL CG2 C 20.55 . 1
126 . 13 VAL N N 116.49 . 1
127 . 14 THR H H 7.86 . 1
128 . 14 THR HA H 4.80 . 1
129 . 14 THR HB H 3.33 . 1
130 . 14 THR HG2 H 0.38 . 1
131 . 14 THR C C 172.17 . 1
132 . 14 THR CA C 60.80 . 1
133 . 14 THR CB C 71.63 . 1
134 . 14 THR CG2 C 19.96 . 1
135 . 14 THR N N 118.54 . 1
136 . 15 PHE H H 8.80 . 1
137 . 15 PHE HA H 4.35 . 1
138 . 15 PHE HB2 H 2.29 . 2
139 . 15 PHE HB3 H 1.33 . 2
140 . 15 PHE HD1 H 6.20 . 3
141 . 15 PHE HE1 H 6.26 . 3
142 . 15 PHE HZ H 5.99 . 1
143 . 15 PHE C C 173.53 . 1
144 . 15 PHE CA C 52.72 . 1
145 . 15 PHE CB C 37.50 . 1
146 . 15 PHE N N 126.78 . 1
147 . 16 HIS H H 8.50 . 1
148 . 16 HIS HA H 4.44 . 1
149 . 16 HIS HB2 H 3.04 . 2
150 . 16 HIS HB3 H 2.98 . 2
151 . 16 HIS HD2 H 7.03 . 1
152 . 16 HIS HE1 H 7.73 . 1
153 . 16 HIS C C 175.02 . 1
154 . 16 HIS CA C 57.06 . 1
155 . 16 HIS CB C 31.01 . 1
156 . 16 HIS N N 122.43 . 1
157 . 17 VAL H H 8.53 . 1
158 . 17 VAL HA H 4.57 . 1
159 . 17 VAL HB H 2.14 . 1
160 . 17 VAL HG1 H 1.11 . 2
161 . 17 VAL HG2 H 1.19 . 2
162 . 17 VAL C C 174.88 . 1
163 . 17 VAL CA C 59.02 . 1
164 . 17 VAL CB C 33.65 . 1
165 . 17 VAL CG1 C 21.52 . 1
166 . 17 VAL CG2 C 21.52 . 1
167 . 17 VAL N N 125.38 . 1
168 . 18 PRO HA H 4.57 . 1
169 . 18 PRO HB2 H 2.21 . 2
170 . 18 PRO HG2 H 2.10 . 2
171 . 18 PRO HD2 H 3.92 . 2
172 . 18 PRO HD3 H 3.75 . 2
173 . 18 PRO C C 176.44 . 1
174 . 18 PRO CA C 62.62 . 1
175 . 18 PRO CB C 31.05 . 1
176 . 18 PRO CG C 27.47 . 1
177 . 18 PRO CD C 51.19 . 1
178 . 19 SER H H 8.25 . 1
179 . 19 SER HA H 4.47 . 1
180 . 19 SER HB2 H 3.87 . 2
181 . 19 SER C C 174.97 . 1
182 . 19 SER CA C 58.34 . 1
183 . 19 SER CB C 63.95 . 1
184 . 19 SER N N 115.94 . 1
185 . 20 ASN H H 8.77 . 1
186 . 20 ASN HA H 4.75 . 1
187 . 20 ASN HB2 H 2.87 . 2
188 . 20 ASN HD21 H 7.64 . 2
189 . 20 ASN HD22 H 6.94 . 2
190 . 20 ASN C C 174.35 . 1
191 . 20 ASN CA C 53.74 . 1
192 . 20 ASN CB C 38.87 . 1
193 . 20 ASN N N 121.53 . 1
194 . 20 ASN ND2 N 112.17 . 1
195 . 21 GLN H H 7.96 . 1
196 . 21 GLN HA H 4.78 . 1
197 . 21 GLN HB2 H 2.12 . 2
198 . 21 GLN HB3 H 1.91 . 2
199 . 21 GLN HG2 H 2.31 . 2
200 . 21 GLN HE21 H 7.49 . 2
201 . 21 GLN HE22 H 6.89 . 2
202 . 21 GLN C C 172.85 . 1
203 . 21 GLN CA C 53.48 . 1
204 . 21 GLN CB C 29.81 . 1
205 . 21 GLN CG C 33.23 . 1
206 . 21 GLN N N 118.67 . 1
207 . 21 GLN NE2 N 111.78 . 1
208 . 22 PRO HA H 4.43 . 1
209 . 22 PRO HB2 H 2.29 . 2
210 . 22 PRO HB3 H 1.83 . 2
211 . 22 PRO HG2 H 2.11 . 2
212 . 22 PRO HG3 H 1.97 . 2
213 . 22 PRO HD2 H 3.80 . 2
214 . 22 PRO HD3 H 3.63 . 2
215 . 22 PRO C C 176.55 . 1
216 . 22 PRO CA C 63.20 . 1
217 . 22 PRO CB C 31.79 . 1
218 . 22 PRO CG C 27.75 . 1
219 . 22 PRO CD C 50.58 . 1
220 . 23 LEU H H 8.37 . 1
221 . 23 LEU HA H 4.36 . 1
222 . 23 LEU HB2 H 1.53 . 2
223 . 23 LEU HB3 H 1.29 . 2
224 . 23 LEU HG H 1.69 . 1
225 . 23 LEU HD1 H 0.81 . 2
226 . 23 LEU HD2 H 0.77 . 2
227 . 23 LEU C C 176.63 . 1
228 . 23 LEU CA C 54.55 . 1
229 . 23 LEU CB C 42.84 . 1
230 . 23 LEU CG C 26.83 . 1
231 . 23 LEU CD1 C 26.14 . 1
232 . 23 LEU CD2 C 23.93 . 1
233 . 23 LEU N N 123.54 . 1
234 . 24 LYS H H 8.37 . 1
235 . 24 LYS HA H 4.29 . 1
236 . 24 LYS HB2 H 1.92 . 2
237 . 24 LYS HG2 H 1.73 . 2
238 . 24 LYS HD2 H 1.42 . 2
239 . 24 LYS HE2 H 2.99 . 2
240 . 24 LYS C C 175.97 . 1
241 . 24 LYS CA C 57.27 . 1
242 . 24 LYS CB C 33.70 . 1
243 . 24 LYS CG C 29.17 . 1
244 . 24 LYS CD C 25.14 . 1
245 . 24 LYS CE C 42.23 . 1
246 . 24 LYS N N 120.01 . 1
247 . 25 GLU H H 7.80 . 1
248 . 25 GLU HA H 4.96 . 1
249 . 25 GLU HB2 H 2.08 . 2
250 . 25 GLU HB3 H 1.95 . 2
251 . 25 GLU HG2 H 2.30 . 2
252 . 25 GLU C C 174.64 . 1
253 . 25 GLU CA C 55.22 . 1
254 . 25 GLU CB C 32.51 . 1
255 . 25 GLU CG C 36.59 . 1
256 . 25 GLU N N 118.23 . 1
257 . 26 VAL H H 8.53 . 1
258 . 26 VAL HA H 4.68 . 1
259 . 26 VAL HB H 2.12 . 1
260 . 26 VAL HG1 H 1.01 . 2
261 . 26 VAL HG2 H 0.94 . 2
262 . 26 VAL C C 172.17 . 1
263 . 26 VAL CA C 61.02 . 1
264 . 26 VAL CB C 35.88 . 1
265 . 26 VAL CG1 C 22.11 . 1
266 . 26 VAL CG2 C 23.08 . 1
267 . 26 VAL N N 120.39 . 1
268 . 27 LEU H H 8.80 . 1
269 . 27 LEU HA H 5.15 . 1
270 . 27 LEU HB2 H 1.77 . 2
271 . 27 LEU HB3 H 1.68 . 2
272 . 27 LEU HG H 1.44 . 1
273 . 27 LEU HD1 H 1.02 . 2
274 . 27 LEU HD2 H 0.88 . 2
275 . 27 LEU C C 174.05 . 1
276 . 27 LEU CA C 54.58 . 1
277 . 27 LEU CB C 45.24 . 1
278 . 27 LEU CG C 28.05 . 1
279 . 27 LEU CD1 C 23.64 . 1
280 . 27 LEU CD2 C 26.12 . 1
281 . 27 LEU N N 127.12 . 1
282 . 28 TRP H H 9.16 . 1
283 . 28 TRP HA H 5.49 . 1
284 . 28 TRP HB2 H 3.04 . 2
285 . 28 TRP HB3 H 2.91 . 2
286 . 28 TRP HD1 H 6.73 . 1
287 . 28 TRP HE1 H 10.16 . 1
288 . 28 TRP HE3 H 7.28 . 1
289 . 28 TRP HZ2 H 7.47 . 1
290 . 28 TRP HZ3 H 6.48 . 1
291 . 28 TRP HH2 H 6.67 . 1
292 . 28 TRP C C 175.89 . 1
293 . 28 TRP CA C 56.33 . 1
294 . 28 TRP CB C 32.20 . 1
295 . 28 TRP N N 124.08 . 1
296 . 28 TRP NE1 N 127.59 . 1
297 . 29 LYS H H 9.64 . 1
298 . 29 LYS HA H 5.07 . 1
299 . 29 LYS HB2 H 1.65 . 2
300 . 29 LYS HB3 H 1.59 . 2
301 . 29 LYS HG2 H 1.49 . 2
302 . 29 LYS HD2 H 1.28 . 2
303 . 29 LYS HD3 H 1.09 . 2
304 . 29 LYS HE2 H 2.68 . 2
305 . 29 LYS C C 173.77 . 1
306 . 29 LYS CA C 54.73 . 1
307 . 29 LYS CB C 37.19 . 1
308 . 29 LYS CG C 29.33 . 1
309 . 29 LYS CD C 24.96 . 1
310 . 29 LYS CE C 41.49 . 1
311 . 29 LYS N N 122.31 . 1
312 . 30 LYS H H 8.69 . 1
313 . 30 LYS HA H 4.26 . 1
314 . 30 LYS HB2 H 1.44 . 2
315 . 30 LYS HB3 H 1.11 . 2
316 . 30 LYS HG2 H 0.93 . 2
317 . 30 LYS HG3 H 0.24 . 2
318 . 30 LYS HD2 H 1.89 . 2
319 . 30 LYS HD3 H 1.74 . 2
320 . 30 LYS HE2 H 3.38 . 2
321 . 30 LYS HE3 H 2.94 . 2
322 . 30 LYS C C 176.38 . 1
323 . 30 LYS CA C 54.70 . 1
324 . 30 LYS CB C 35.37 . 1
325 . 30 LYS CG C 24.33 . 1
326 . 30 LYS CD C 30.58 . 1
327 . 30 LYS CE C 42.77 . 1
328 . 30 LYS N N 122.73 . 1
329 . 31 GLN H H 8.76 . 1
330 . 31 GLN HA H 3.67 . 1
331 . 31 GLN HB2 H 2.35 . 2
332 . 31 GLN HB3 H 2.25 . 2
333 . 31 GLN HG2 H 2.63 . 2
334 . 31 GLN HG3 H 2.38 . 2
335 . 31 GLN HE21 H 8.78 . 2
336 . 31 GLN HE22 H 6.90 . 2
337 . 31 GLN C C 175.25 . 1
338 . 31 GLN CA C 58.93 . 1
339 . 31 GLN CB C 26.61 . 1
340 . 31 GLN CG C 34.06 . 1
341 . 31 GLN N N 125.09 . 1
342 . 31 GLN NE2 N 114.15 . 1
343 . 32 LYS H H 8.33 . 1
344 . 32 LYS HA H 4.20 . 1
345 . 32 LYS HB2 H 1.98 . 2
346 . 32 LYS HB3 H 1.86 . 2
347 . 32 LYS HG2 H 1.64 . 2
348 . 32 LYS HD2 H 1.46 . 2
349 . 32 LYS HD3 H 1.37 . 2
350 . 32 LYS HE2 H 2.96 . 2
351 . 32 LYS C C 176.19 . 1
352 . 32 LYS CA C 56.48 . 1
353 . 32 LYS CB C 32.17 . 1
354 . 32 LYS CG C 28.79 . 1
355 . 32 LYS CD C 25.14 . 1
356 . 32 LYS CE C 42.23 . 1
357 . 32 LYS N N 118.23 . 1
358 . 33 ASP H H 8.06 . 1
359 . 33 ASP HA H 4.79 . 1
360 . 33 ASP HB2 H 2.71 . 2
361 . 33 ASP C C 175.39 . 1
362 . 33 ASP CA C 53.38 . 1
363 . 33 ASP CB C 42.72 . 1
364 . 33 ASP N N 120.29 . 1
365 . 34 LYS H H 8.38 . 1
366 . 34 LYS HA H 4.04 . 1
367 . 34 LYS HB2 H 1.03 . 2
368 . 34 LYS HG2 H 1.15 . 2
369 . 34 LYS HG3 H 1.05 . 2
370 . 34 LYS HD2 H 1.44 . 2
371 . 34 LYS HD3 H 0.96 . 2
372 . 34 LYS HE2 H 2.51 . 2
373 . 34 LYS HE3 H 2.37 . 2
374 . 34 LYS C C 175.90 . 1
375 . 34 LYS CA C 58.61 . 1
376 . 34 LYS CB C 33.50 . 1
377 . 34 LYS CG C 29.64 . 1
378 . 34 LYS CD C 25.85 . 1
379 . 34 LYS CE C 41.49 . 1
380 . 34 LYS N N 120.83 . 1
381 . 35 VAL H H 9.12 . 1
382 . 35 VAL HA H 4.13 . 1
383 . 35 VAL HB H 1.64 . 1
384 . 35 VAL HG1 H 0.27 . 2
385 . 35 VAL HG2 H 0.56 . 2
386 . 35 VAL C C 175.18 . 1
387 . 35 VAL CA C 63.29 . 1
388 . 35 VAL CB C 33.47 . 1
389 . 35 VAL CG1 C 20.24 . 1
390 . 35 VAL CG2 C 21.80 . 1
391 . 35 VAL N N 120.86 . 1
392 . 36 ALA H H 7.71 . 1
393 . 36 ALA HA H 5.36 . 1
394 . 36 ALA HB H 1.45 . 1
395 . 36 ALA C C 174.49 . 1
396 . 36 ALA CA C 51.48 . 1
397 . 36 ALA CB C 22.32 . 1
398 . 36 ALA N N 115.19 . 1
399 . 37 GLU H H 9.35 . 1
400 . 37 GLU HA H 5.44 . 1
401 . 37 GLU HB2 H 2.24 . 2
402 . 37 GLU HG2 H 2.33 . 2
403 . 37 GLU C C 173.06 . 1
404 . 37 GLU CA C 54.57 . 1
405 . 37 GLU CB C 35.34 . 1
406 . 37 GLU CG C 35.89 . 1
407 . 37 GLU N N 118.62 . 1
408 . 38 LEU H H 9.06 . 1
409 . 38 LEU HA H 5.30 . 1
410 . 38 LEU HB2 H 1.78 . 2
411 . 38 LEU HB3 H 1.40 . 2
412 . 38 LEU HG H 1.55 . 1
413 . 38 LEU HD1 H 0.80 . 1
414 . 38 LEU HD2 H 0.80 . 1
415 . 38 LEU C C 175.62 . 1
416 . 38 LEU CA C 53.63 . 1
417 . 38 LEU CB C 46.49 . 1
418 . 38 LEU CG C 27.46 . 1
419 . 38 LEU CD1 C 23.98 . 1
420 . 38 LEU CD2 C 25.85 . 1
421 . 38 LEU N N 122.83 . 1
422 . 39 GLU H H 8.82 . 1
423 . 39 GLU HA H 4.69 . 1
424 . 39 GLU HB2 H 2.08 . 2
425 . 39 GLU HB3 H 1.95 . 2
426 . 39 GLU HG2 H 2.30 . 2
427 . 39 GLU C C 175.87 . 1
428 . 39 GLU CA C 55.82 . 1
429 . 39 GLU CB C 32.10 . 1
430 . 39 GLU CG C 35.89 . 1
431 . 39 GLU N N 124.93 . 1
432 . 40 ASN H H 9.76 . 1
433 . 40 ASN HA H 4.38 . 1
434 . 40 ASN HB2 H 3.13 . 2
435 . 40 ASN HB3 H 2.82 . 2
436 . 40 ASN HD21 H 7.83 . 2
437 . 40 ASN HD22 H 6.91 . 2
438 . 40 ASN C C 174.72 . 1
439 . 40 ASN CA C 55.09 . 1
440 . 40 ASN CB C 37.21 . 1
441 . 40 ASN N N 126.80 . 1
442 . 40 ASN ND2 N 113.20 . 1
443 . 41 SER H H 8.89 . 1
444 . 41 SER HA H 3.99 . 1
445 . 41 SER HB2 H 4.24 . 2
446 . 41 SER HB3 H 4.10 . 2
447 . 41 SER C C 172.69 . 1
448 . 41 SER CA C 60.43 . 1
449 . 41 SER CB C 62.62 . 1
450 . 41 SER N N 107.11 . 1
451 . 42 GLU H H 8.15 . 1
452 . 42 GLU HA H 4.69 . 1
453 . 42 GLU HB2 H 2.08 . 2
454 . 42 GLU HG2 H 2.34 . 2
455 . 42 GLU HG3 H 2.21 . 2
456 . 42 GLU C C 174.53 . 1
457 . 42 GLU CA C 55.20 . 1
458 . 42 GLU CB C 31.69 . 1
459 . 42 GLU CG C 36.26 . 1
460 . 42 GLU N N 121.34 . 1
461 . 43 PHE H H 8.65 . 1
462 . 43 PHE HA H 5.76 . 1
463 . 43 PHE HB2 H 3.17 . 2
464 . 43 PHE HB3 H 2.83 . 2
465 . 43 PHE HD1 H 7.15 . 3
466 . 43 PHE HE1 H 7.21 . 3
467 . 43 PHE C C 174.44 . 1
468 . 43 PHE CA C 55.22 . 1
469 . 43 PHE CB C 41.91 . 1
470 . 43 PHE N N 123.27 . 1
471 . 44 ARG H H 8.54 . 1
472 . 44 ARG HA H 4.08 . 1
473 . 44 ARG HB2 H 1.47 . 2
474 . 44 ARG HB3 H 1.42 . 2
475 . 44 ARG HG2 H 1.38 . 2
476 . 44 ARG HG3 H 1.31 . 2
477 . 44 ARG HD2 H 3.13 . 2
478 . 44 ARG C C 172.30 . 1
479 . 44 ARG CA C 54.59 . 1
480 . 44 ARG CB C 34.16 . 1
481 . 44 ARG CG C 27.46 . 1
482 . 44 ARG CD C 43.35 . 1
483 . 44 ARG N N 125.09 . 1
484 . 45 ALA H H 7.91 . 1
485 . 45 ALA HA H 4.85 . 1
486 . 45 ALA HB H 1.33 . 1
487 . 45 ALA C C 175.79 . 1
488 . 45 ALA CA C 50.10 . 1
489 . 45 ALA CB C 22.95 . 1
490 . 45 ALA N N 122.03 . 1
491 . 46 PHE H H 7.61 . 1
492 . 46 PHE HA H 4.75 . 1
493 . 46 PHE HB2 H 2.82 . 2
494 . 46 PHE HB3 H 3.22 . 2
495 . 46 PHE HD1 H 6.98 . 3
496 . 46 PHE HE1 H 7.08 . 3
497 . 46 PHE HZ H 7.22 . 1
498 . 46 PHE C C 175.41 . 1
499 . 46 PHE CA C 57.55 . 1
500 . 46 PHE CB C 42.54 . 1
501 . 46 PHE N N 114.74 . 1
502 . 47 SER H H 9.34 . 1
503 . 47 SER HA H 4.06 . 1
504 . 47 SER HB2 H 4.34 . 2
505 . 47 SER HB3 H 4.18 . 2
506 . 47 SER CA C 58.52 . 1
507 . 47 SER CB C 62.14 . 1
508 . 47 SER N N 113.70 . 1
509 . 48 SER HA H 4.34 . 1
510 . 48 SER HB2 H 3.90 . 2
511 . 48 SER HB3 H 3.77 . 2
512 . 48 SER C C 175.03 . 1
513 . 48 SER CA C 60.04 . 1
514 . 48 SER CB C 62.70 . 1
515 . 49 PHE H H 8.62 . 1
516 . 49 PHE HA H 4.28 . 1
517 . 49 PHE HB2 H 3.51 . 2
518 . 49 PHE HB3 H 3.37 . 2
519 . 49 PHE HD1 H 7.22 . 3
520 . 49 PHE HE1 H 7.34 . 3
521 . 49 PHE HZ H 7.50 . 1
522 . 49 PHE C C 175.39 . 1
523 . 49 PHE CA C 59.67 . 1
524 . 49 PHE CB C 38.41 . 1
525 . 49 PHE N N 121.19 . 1
526 . 50 LYS H H 7.05 . 1
527 . 50 LYS HA H 3.76 . 1
528 . 50 LYS HB2 H 1.72 . 2
529 . 50 LYS HB3 H 1.63 . 2
530 . 50 LYS HG2 H 1.71 . 2
531 . 50 LYS HD2 H 1.42 . 2
532 . 50 LYS HD3 H 1.28 . 2
533 . 50 LYS HE2 H 3.03 . 2
534 . 50 LYS CA C 58.94 . 1
535 . 50 LYS CB C 32.40 . 1
536 . 50 LYS CG C 29.33 . 1
537 . 50 LYS CD C 25.14 . 1
538 . 50 LYS CE C 41.85 . 1
539 . 50 LYS N N 119.55 . 1
540 . 51 ASN H H 8.95 . 1
541 . 51 ASN HA H 4.62 . 1
542 . 51 ASN HB2 H 3.03 . 2
543 . 51 ASN HD21 H 7.72 . 2
544 . 51 ASN HD22 H 6.99 . 2
545 . 51 ASN C C 175.43 . 1
546 . 51 ASN CA C 54.67 . 1
547 . 51 ASN CB C 38.39 . 1
548 . 51 ASN N N 115.63 . 1
549 . 51 ASN ND2 N 113.46 . 1
550 . 52 ARG H H 8.20 . 1
551 . 52 ARG HA H 4.89 . 1
552 . 52 ARG HB2 H 1.98 . 2
553 . 52 ARG HG2 H 1.77 . 2
554 . 52 ARG HG3 H 1.60 . 2
555 . 52 ARG HD2 H 3.51 . 2
556 . 52 ARG HD3 H 3.14 . 2
557 . 52 ARG C C 173.43 . 1
558 . 52 ARG CA C 55.84 . 1
559 . 52 ARG CB C 31.61 . 1
560 . 52 ARG CG C 27.77 . 1
561 . 52 ARG CD C 43.70 . 1
562 . 52 ARG N N 115.88 . 1
563 . 53 VAL H H 7.40 . 1
564 . 53 VAL HA H 5.72 . 1
565 . 53 VAL HB H 1.97 . 1
566 . 53 VAL HG1 H 1.11 . 2
567 . 53 VAL HG2 H 0.95 . 2
568 . 53 VAL C C 175.16 . 1
569 . 53 VAL CA C 58.03 . 1
570 . 53 VAL CB C 36.67 . 1
571 . 53 VAL CG1 C 23.99 . 1
572 . 53 VAL CG2 C 19.02 . 1
573 . 53 VAL N N 108.31 . 1
574 . 54 TYR H H 8.77 . 1
575 . 54 TYR HA H 4.43 . 1
576 . 54 TYR HB2 H 3.15 . 2
577 . 54 TYR HB3 H 2.54 . 2
578 . 54 TYR HD1 H 6.50 . 3
579 . 54 TYR HE1 H 6.89 . 3
580 . 54 TYR CA C 57.58 . 1
581 . 54 TYR CB C 42.47 . 1
582 . 54 TYR N N 121.47 . 1
583 . 55 LEU HA H 4.55 . 1
584 . 55 LEU HB2 H 1.05 . 2
585 . 55 LEU HB3 H 0.63 . 2
586 . 55 LEU HG H 1.22 . 1
587 . 55 LEU HD1 H 0.81 . 2
588 . 55 LEU HD2 H 0.72 . 2
589 . 55 LEU C C 173.28 . 1
590 . 55 LEU CA C 52.12 . 1
591 . 55 LEU CB C 44.71 . 1
592 . 55 LEU CG C 27.64 . 1
593 . 55 LEU CD1 C 26.76 . 1
594 . 55 LEU CD2 C 26.83 . 1
595 . 56 ASP H H 8.11 . 1
596 . 56 ASP HA H 4.35 . 1
597 . 56 ASP HB2 H 2.59 . 2
598 . 56 ASP HB3 H 2.92 . 2
599 . 56 ASP C C 177.26 . 1
600 . 56 ASP CA C 53.37 . 1
601 . 56 ASP CB C 42.24 . 1
602 . 56 ASP N N 123.50 . 1
603 . 57 THR H H 8.48 . 1
604 . 57 THR HA H 3.79 . 1
605 . 57 THR HB H 4.37 . 1
606 . 57 THR HG2 H 1.28 . 1
607 . 57 THR C C 174.72 . 1
608 . 57 THR CA C 64.05 . 1
609 . 57 THR CB C 68.26 . 1
610 . 57 THR CG2 C 22.05 . 1
611 . 57 THR N N 119.62 . 1
612 . 58 LYS H H 8.17 . 1
613 . 58 LYS HA H 4.30 . 1
614 . 58 LYS HB2 H 2.01 . 2
615 . 58 LYS HB3 H 1.93 . 2
616 . 58 LYS HG2 H 1.73 . 2
617 . 58 LYS HD2 H 1.52 . 2
618 . 58 LYS HD3 H 1.42 . 2
619 . 58 LYS HE2 H 3.02 . 2
620 . 58 LYS C C 176.68 . 1
621 . 58 LYS CA C 57.72 . 1
622 . 58 LYS CB C 32.31 . 1
623 . 58 LYS CG C 28.80 . 1
624 . 58 LYS CD C 25.14 . 1
625 . 58 LYS CE C 41.85 . 1
626 . 58 LYS N N 118.68 . 1
627 . 59 SER H H 7.59 . 1
628 . 59 SER HA H 4.63 . 1
629 . 59 SER HB2 H 4.30 . 2
630 . 59 SER HB3 H 3.83 . 2
631 . 59 SER C C 173.98 . 1
632 . 59 SER CA C 58.40 . 1
633 . 59 SER CB C 67.07 . 1
634 . 59 SER N N 108.82 . 1
635 . 60 GLY H H 8.53 . 1
636 . 60 GLY HA2 H 3.44 . 1
637 . 60 GLY HA3 H 4.41 . 1
638 . 60 GLY C C 172.53 . 1
639 . 60 GLY CA C 45.30 . 1
640 . 60 GLY N N 109.13 . 1
641 . 61 SER H H 8.03 . 1
642 . 61 SER HA H 4.61 . 1
643 . 61 SER HB2 H 3.72 . 2
644 . 61 SER HB3 H 3.65 . 2
645 . 61 SER C C 172.63 . 1
646 . 61 SER CA C 60.83 . 1
647 . 61 SER CB C 63.36 . 1
648 . 61 SER N N 113.85 . 1
649 . 62 LEU H H 7.21 . 1
650 . 62 LEU HA H 4.56 . 1
651 . 62 LEU HB2 H -0.46 . 2
652 . 62 LEU HB3 H 0.24 . 2
653 . 62 LEU HG H 0.52 . 1
654 . 62 LEU HD1 H 0.17 . 2
655 . 62 LEU HD2 H -0.34 . 2
656 . 62 LEU C C 174.03 . 1
657 . 62 LEU CA C 52.83 . 1
658 . 62 LEU CB C 44.01 . 1
659 . 62 LEU CG C 26.14 . 1
660 . 62 LEU CD1 C 23.08 . 1
661 . 62 LEU CD2 C 24.29 . 1
662 . 62 LEU N N 126.55 . 1
663 . 63 THR H H 9.05 . 1
664 . 63 THR HA H 5.05 . 1
665 . 63 THR HB H 3.70 . 1
666 . 63 THR HG2 H 0.35 . 1
667 . 63 THR C C 172.73 . 1
668 . 63 THR CA C 60.84 . 1
669 . 63 THR CB C 71.06 . 1
670 . 63 THR CG2 C 19.91 . 1
671 . 63 THR N N 123.69 . 1
672 . 64 ILE H H 8.32 . 1
673 . 64 ILE HA H 4.36 . 1
674 . 64 ILE HB H 1.11 . 1
675 . 64 ILE HG12 H 0.85 . 2
676 . 64 ILE HG13 H 0.38 . 2
677 . 64 ILE HG2 H 0.85 . 1
678 . 64 ILE HD1 H 0.16 . 1
679 . 64 ILE C C 174.19 . 1
680 . 64 ILE CA C 60.26 . 1
681 . 64 ILE CB C 40.26 . 1
682 . 64 ILE CG1 C 26.76 . 1
683 . 64 ILE CG2 C 18.29 . 1
684 . 64 ILE CD1 C 13.95 . 1
685 . 64 ILE N N 124.47 . 1
686 . 65 TYR H H 8.41 . 1
687 . 65 TYR HA H 4.74 . 1
688 . 65 TYR HB2 H 2.90 . 2
689 . 65 TYR HB3 H 2.63 . 2
690 . 65 TYR HD1 H 6.88 . 3
691 . 65 TYR HE1 H 6.95 . 3
692 . 65 TYR CA C 56.58 . 1
693 . 65 TYR CB C 40.27 . 1
694 . 65 TYR N N 122.74 . 1
695 . 66 ASN C C 174.10 . 1
696 . 66 ASN CA C 52.84 . 1
697 . 66 ASN CB C 36.61 . 1
698 . 67 LEU H H 8.44 . 1
699 . 67 LEU HA H 4.23 . 1
700 . 67 LEU HB2 H 1.78 . 2
701 . 67 LEU HB3 H 1.01 . 2
702 . 67 LEU HG H 1.65 . 1
703 . 67 LEU HD1 H 0.62 . 2
704 . 67 LEU HD2 H 0.67 . 2
705 . 67 LEU C C 178.40 . 1
706 . 67 LEU CA C 55.28 . 1
707 . 67 LEU CB C 43.37 . 1
708 . 67 LEU CG C 26.81 . 1
709 . 67 LEU CD1 C 26.10 . 1
710 . 67 LEU CD2 C 23.71 . 1
711 . 67 LEU N N 116.02 . 1
712 . 68 THR H H 9.16 . 1
713 . 68 THR HA H 4.57 . 1
714 . 68 THR HB H 4.38 . 1
715 . 68 THR HG2 H 1.23 . 1
716 . 68 THR C C 175.66 . 1
717 . 68 THR CA C 59.54 . 1
718 . 68 THR CB C 72.57 . 1
719 . 68 THR CG2 C 20.90 . 1
720 . 68 THR N N 112.13 . 1
721 . 69 SER H H 8.99 . 1
722 . 69 SER HA H 4.09 . 1
723 . 69 SER HB2 H 3.94 . 2
724 . 69 SER CA C 62.21 . 1
725 . 69 SER CB C 62.22 . 1
726 . 69 SER N N 117.12 . 1
727 . 70 SER H H 7.91 . 1
728 . 70 SER HA H 4.38 . 1
729 . 70 SER HB2 H 3.85 . 2
730 . 70 SER C C 174.04 . 1
731 . 70 SER CA C 60.20 . 1
732 . 70 SER CB C 62.68 . 1
733 . 70 SER N N 115.09 . 1
734 . 71 ASP H H 7.98 . 1
735 . 71 ASP HA H 4.65 . 1
736 . 71 ASP HB2 H 2.87 . 2
737 . 71 ASP HB3 H 2.73 . 2
738 . 71 ASP C C 176.52 . 1
739 . 71 ASP CA C 55.32 . 1
740 . 71 ASP CB C 41.37 . 1
741 . 71 ASP N N 118.67 . 1
742 . 72 GLU H H 7.19 . 1
743 . 72 GLU HA H 4.49 . 1
744 . 72 GLU HB2 H 2.27 . 2
745 . 72 GLU HB3 H 2.14 . 2
746 . 72 GLU HG2 H 3.26 . 2
747 . 72 GLU HG3 H 2.14 . 2
748 . 72 GLU C C 174.46 . 1
749 . 72 GLU CA C 57.01 . 1
750 . 72 GLU CB C 30.21 . 1
751 . 72 GLU CG C 36.23 . 1
752 . 72 GLU N N 120.87 . 1
753 . 73 ASP H H 8.02 . 1
754 . 73 ASP HA H 4.37 . 1
755 . 73 ASP HB2 H 2.48 . 2
756 . 73 ASP HB3 H 2.05 . 2
757 . 73 ASP C C 172.88 . 1
758 . 73 ASP CA C 52.68 . 1
759 . 73 ASP CB C 44.03 . 1
760 . 73 ASP N N 127.54 . 1
761 . 74 GLU H H 9.05 . 1
762 . 74 GLU HA H 4.80 . 1
763 . 74 GLU HB2 H 1.94 . 2
764 . 74 GLU HB3 H 1.88 . 2
765 . 74 GLU HG2 H 2.06 . 2
766 . 74 GLU C C 174.77 . 1
767 . 74 GLU CA C 55.21 . 1
768 . 74 GLU CB C 32.27 . 1
769 . 74 GLU CG C 37.40 . 1
770 . 74 GLU N N 118.34 . 1
771 . 75 TYR H H 9.37 . 1
772 . 75 TYR HA H 5.51 . 1
773 . 75 TYR HB2 H 2.86 . 2
774 . 75 TYR HB3 H 2.68 . 2
775 . 75 TYR HD1 H 6.88 . 3
776 . 75 TYR HE1 H 6.59 . 3
777 . 75 TYR C C 175.54 . 1
778 . 75 TYR CA C 56.35 . 1
779 . 75 TYR CB C 42.34 . 1
780 . 75 TYR N N 124.14 . 1
781 . 76 GLU H H 9.15 . 1
782 . 76 GLU HA H 5.45 . 1
783 . 76 GLU HB2 H 1.84 . 2
784 . 76 GLU HG2 H 2.06 . 2
785 . 76 GLU HG3 H 1.96 . 2
786 . 76 GLU C C 173.11 . 1
787 . 76 GLU CA C 54.54 . 1
788 . 76 GLU CB C 34.77 . 1
789 . 76 GLU CG C 36.59 . 1
790 . 76 GLU N N 120.32 . 1
791 . 77 MET H H 8.58 . 1
792 . 77 MET HA H 4.44 . 1
793 . 77 MET HB2 H 1.33 . 2
794 . 77 MET HB3 H 1.24 . 2
795 . 77 MET HG2 H -0.36 . 2
796 . 77 MET HE H 1.87 . 1
797 . 77 MET C C 174.74 . 1
798 . 77 MET CA C 53.87 . 1
799 . 77 MET CB C 32.87 . 1
800 . 77 MET CG C 33.08 . 1
801 . 77 MET CE C 18.71 . 1
802 . 77 MET N N 126.05 . 1
803 . 78 GLU H H 8.91 . 1
804 . 78 GLU HA H 4.63 . 1
805 . 78 GLU HB2 H 1.87 . 2
806 . 78 GLU HB3 H 1.79 . 2
807 . 78 GLU HG2 H 2.03 . 2
808 . 78 GLU C C 175.22 . 1
809 . 78 GLU CA C 54.24 . 1
810 . 78 GLU CB C 33.69 . 1
811 . 78 GLU CG C 36.60 . 1
812 . 78 GLU N N 123.61 . 1
813 . 79 SER H H 8.56 . 1
814 . 79 SER HA H 5.07 . 1
815 . 79 SER HB2 H 4.25 . 2
816 . 79 SER HB3 H 3.39 . 2
817 . 79 SER C C 173.79 . 1
818 . 79 SER CA C 55.32 . 1
819 . 79 SER CB C 66.51 . 1
820 . 79 SER N N 116.96 . 1
821 . 80 PRO HA H 4.56 . 1
822 . 80 PRO HB2 H 2.37 . 2
823 . 80 PRO HB3 H 1.96 . 2
824 . 80 PRO HG2 H 2.03 . 2
825 . 80 PRO HG3 H 1.96 . 2
826 . 80 PRO HD2 H 3.92 . 2
827 . 80 PRO HD3 H 3.80 . 2
828 . 80 PRO C C 177.03 . 1
829 . 80 PRO CA C 63.93 . 1
830 . 80 PRO CB C 32.26 . 1
831 . 80 PRO CG C 27.16 . 1
832 . 80 PRO CD C 51.53 . 1
833 . 81 ASN H H 8.32 . 1
834 . 81 ASN HA H 4.73 . 1
835 . 81 ASN HB2 H 3.12 . 2
836 . 81 ASN HB3 H 2.60 . 2
837 . 81 ASN HD21 H 7.64 . 2
838 . 81 ASN HD22 H 7.13 . 2
839 . 81 ASN C C 174.05 . 1
840 . 81 ASN CA C 53.92 . 1
841 . 81 ASN CB C 40.30 . 1
842 . 81 ASN N N 113.68 . 1
843 . 81 ASN ND2 N 110.41 . 1
844 . 82 ILE H H 7.49 . 1
845 . 82 ILE HA H 4.61 . 1
846 . 82 ILE HB H 1.97 . 1
847 . 82 ILE HG12 H 1.39 . 2
848 . 82 ILE HG13 H 1.19 . 2
849 . 82 ILE HG2 H 0.92 . 1
850 . 82 ILE HD1 H 0.86 . 1
851 . 82 ILE C C 175.66 . 1
852 . 82 ILE CA C 59.82 . 1
853 . 82 ILE CB C 40.27 . 1
854 . 82 ILE CG1 C 26.09 . 1
855 . 82 ILE CG2 C 18.00 . 1
856 . 82 ILE CD1 C 13.40 . 1
857 . 82 ILE N N 115.86 . 1
858 . 83 THR H H 8.41 . 1
859 . 83 THR HA H 4.16 . 1
860 . 83 THR HB H 4.20 . 1
861 . 83 THR HG2 H 1.21 . 1
862 . 83 THR C C 174.25 . 1
863 . 83 THR CA C 63.92 . 1
864 . 83 THR CB C 68.92 . 1
865 . 83 THR CG2 C 21.70 . 1
866 . 83 THR N N 116.12 . 1
867 . 84 ASP H H 7.68 . 1
868 . 84 ASP HA H 4.81 . 1
869 . 84 ASP HB2 H 2.54 . 2
870 . 84 ASP HB3 H 2.66 . 2
871 . 84 ASP C C 174.94 . 1
872 . 84 ASP CA C 53.38 . 1
873 . 84 ASP CB C 42.86 . 1
874 . 84 ASP N N 119.79 . 1
875 . 85 SER H H 8.36 . 1
876 . 85 SER HA H 4.55 . 1
877 . 85 SER HB2 H 3.88 . 2
878 . 85 SER HB3 H 3.82 . 2
879 . 85 SER C C 174.03 . 1
880 . 85 SER CA C 57.97 . 1
881 . 85 SER CB C 63.83 . 1
882 . 85 SER N N 116.57 . 1
883 . 86 MET H H 8.47 . 1
884 . 86 MET HA H 4.70 . 1
885 . 86 MET HB2 H 2.04 . 2
886 . 86 MET HB3 H 1.95 . 2
887 . 86 MET HG2 H 2.53 . 2
888 . 86 MET HG3 H 2.48 . 2
889 . 86 MET HE H 2.18 . 1
890 . 86 MET C C 174.02 . 1
891 . 86 MET CA C 54.62 . 1
892 . 86 MET CB C 35.21 . 1
893 . 86 MET CG C 32.50 . 1
894 . 86 MET CE C 17.46 . 1
895 . 86 MET N N 121.27 . 1
896 . 87 LYS H H 8.09 . 1
897 . 87 LYS HA H 5.33 . 1
898 . 87 LYS HB2 H 1.73 . 2
899 . 87 LYS HB3 H 1.70 . 2
900 . 87 LYS HG2 H 1.53 . 2
901 . 87 LYS HD2 H 1.34 . 2
902 . 87 LYS HD3 H 1.23 . 2
903 . 87 LYS HE2 H 2.79 . 2
904 . 87 LYS C C 175.72 . 1
905 . 87 LYS CA C 55.21 . 1
906 . 87 LYS CB C 35.60 . 1
907 . 87 LYS CG C 29.33 . 1
908 . 87 LYS CD C 25.80 . 1
909 . 87 LYS CE C 41.85 . 1
910 . 87 LYS N N 121.37 . 1
911 . 88 PHE H H 9.36 . 1
912 . 88 PHE HA H 5.16 . 1
913 . 88 PHE HB2 H 2.35 . 2
914 . 88 PHE HB3 H 2.27 . 2
915 . 88 PHE HD1 H 7.07 . 3
916 . 88 PHE HE1 H 7.39 . 3
917 . 88 PHE C C 173.98 . 1
918 . 88 PHE CA C 55.87 . 1
919 . 88 PHE CB C 42.85 . 1
920 . 88 PHE N N 121.36 . 1
921 . 89 PHE H H 9.23 . 1
922 . 89 PHE HA H 4.85 . 1
923 . 89 PHE HB2 H 3.01 . 2
924 . 89 PHE HB3 H 2.84 . 2
925 . 89 PHE HD1 H 6.65 . 3
926 . 89 PHE HE1 H 6.95 . 3
927 . 89 PHE HZ H 7.12 . 1
928 . 89 PHE C C 172.86 . 1
929 . 89 PHE CA C 57.73 . 1
930 . 89 PHE CB C 41.00 . 1
931 . 89 PHE N N 124.39 . 1
932 . 90 LEU H H 8.13 . 1
933 . 90 LEU HA H 5.03 . 1
934 . 90 LEU HB2 H 2.23 . 2
935 . 90 LEU HB3 H 1.25 . 2
936 . 90 LEU HG H 1.27 . 1
937 . 90 LEU HD1 H 0.75 . 2
938 . 90 LEU HD2 H 0.71 . 2
939 . 90 LEU C C 173.76 . 1
940 . 90 LEU CA C 52.90 . 1
941 . 90 LEU CB C 44.62 . 1
942 . 90 LEU CG C 28.08 . 1
943 . 90 LEU CD1 C 24.65 . 1
944 . 90 LEU CD2 C 25.55 . 1
945 . 90 LEU N N 128.23 . 1
946 . 91 TYR H H 8.78 . 1
947 . 91 TYR HA H 4.74 . 1
948 . 91 TYR HB2 H 2.69 . 2
949 . 91 TYR HB3 H 3.08 . 2
950 . 91 TYR HD1 H 6.86 . 3
951 . 91 TYR HE1 H 6.63 . 3
952 . 91 TYR C C 175.45 . 1
953 . 91 TYR CA C 57.10 . 1
954 . 91 TYR CB C 40.35 . 1
955 . 91 TYR N N 124.29 . 1
956 . 92 VAL H H 9.46 . 1
957 . 92 VAL HA H 4.17 . 1
958 . 92 VAL HB H 1.93 . 1
959 . 92 VAL HG1 H 0.45 . 2
960 . 92 VAL HG2 H 0.73 . 2
961 . 92 VAL C C 175.50 . 1
962 . 92 VAL CA C 61.48 . 1
963 . 92 VAL CB C 32.92 . 1
964 . 92 VAL CG1 C 20.90 . 1
965 . 92 VAL CG2 C 20.90 . 1
966 . 92 VAL N N 122.10 . 1
967 . 93 GLY H H 8.59 . 1
968 . 93 GLY HA2 H 4.61 . 1
969 . 93 GLY HA3 H 3.94 . 1
970 . 93 GLY C C 173.16 . 1
971 . 93 GLY CA C 44.03 . 1
972 . 93 GLY N N 114.61 . 1
973 . 94 GLU H H 8.62 . 1
974 . 94 GLU HA H 4.31 . 1
975 . 94 GLU HB2 H 1.97 . 2
976 . 94 GLU HB3 H 2.17 . 2
977 . 94 GLU HG2 H 2.38 . 2
978 . 94 GLU HG3 H 2.29 . 2
979 . 94 GLU C C 176.03 . 1
980 . 94 GLU CA C 57.01 . 1
981 . 94 GLU CB C 30.98 . 1
982 . 94 GLU CG C 36.63 . 1
983 . 94 GLU N N 118.53 . 1
984 . 95 SER H H 7.90 . 1
985 . 95 SER HA H 4.20 . 1
986 . 95 SER HB2 H 3.89 . 2
987 . 95 SER CA C 59.98 . 1
988 . 95 SER CB C 65.02 . 1
989 . 95 SER N N 118.84 . 1
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