data_4312
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
1H, 15N and 13C Resonance Assignments for the Bromodomain of the
Histone Acetyltransferase hsP/CAF
;
_BMRB_accession_number 4312
_BMRB_flat_file_name bmr4312.str
_Entry_type original
_Submission_date 1999-02-28
_Accession_date 1999-03-01
_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 Dhalluin Christophe . .
2 Carlson Justin . .
3 Zeng Lei . .
4 He Cheng . .
5 Aggarwal Aneel K. .
6 Zhou Ming-Ming . .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 608
"13C chemical shifts" 382
"15N chemical shifts" 107
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
1999-03-03 original author .
stop_
_Original_release_date 1999-03-03
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full
;
Dhalluin, C., Carlson, J., Zeng, L., He, C., Aggarwal, A. K., and
Zhou, M-M., "1H, 15N and 13C Resonance Assignments for the
Bromodomain of the Histone Acetyltransferase hsP/CAF,"
J. Biomol. NMR, in preparation.
;
_Citation_title
;
1H, 15N and 13C Resonance Assignments for the Bromodomain of the
Histone Acetyltransferase hsP/CAF
;
_Citation_status 'in preparation'
_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 Dhalluin Christophe . .
2 Carlson Justin . .
3 Zeng Lei . .
4 He Cheng . .
5 Aggarwal Aneel K. .
6 Zhou Ming-Ming . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_volume .
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first .
_Page_last .
_Year .
_Details .
loop_
_Keyword
'histone acetyltransferase bromodomain'
stop_
save_
#######################################
# Cited references within the entry #
#######################################
save_ref_1
_Saveframe_category citation
_Citation_full
;
Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G.
Pfeifer, J. and Bax, A (1995) J. Biomol. NMR 6, 277-293.
;
_Citation_title 'NMRPipe: a multidimensional spectral processing system based on UNIX pipes.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8520220
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Delaglio F . .
2 Grzesiek S . .
3 Vuister 'G W' W. .
4 Zhu G . .
5 Pfeifer J . .
6 Bax A . .
stop_
_Journal_abbreviation 'J. Biomol. NMR'
_Journal_name_full 'Journal of biomolecular NMR'
_Journal_volume 6
_Journal_issue 3
_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 277
_Page_last 293
_Year 1995
_Details
;
The NMRPipe system is a UNIX software environment of processing, graphics, and
analysis tools designed to meet current routine and research-oriented
multidimensional processing requirements, and to anticipate and accommodate
future demands and developments. The system is based on UNIX pipes, which allow
programs running simultaneously to exchange streams of data under user control.
In an NMRPipe processing scheme, a stream of spectral data flows through a
pipeline of processing programs, each of which performs one component of the
overall scheme, such as Fourier transformation or linear prediction. Complete
multidimensional processing schemes are constructed as simple UNIX shell
scripts. The processing modules themselves maintain and exploit accurate
records of data sizes, detection modes, and calibration information in all
dimensions, so that schemes can be constructed without the need to explicitly
define or anticipate data sizes or storage details of real and imaginary
channels during processing. The asynchronous pipeline scheme provides other
substantial advantages, including high flexibility, favorable processing
speeds, choice of both all-in-memory and disk-bound processing, easy adaptation
to different data formats, simpler software development and maintenance, and
the ability to distribute processing tasks on multi-CPU computers and computer
networks.
;
save_
save_ref_2
_Saveframe_category citation
_Citation_full 'Johnson, B. A. and Blevins, R. A. (1994) J. Biomol. NMR 4, 603-614.'
_Citation_title .
_Citation_status .
_Citation_type .
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID ?
_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_
save_ref_3
_Saveframe_category citation
_Citation_full 'X.J.Yang,V.V.Ogryzko,J.I.Nishikawa,B.H.Howard,Y.Nakatani, Nature (1996) 382, 319.'
_Citation_title 'A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A.'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code .
_PubMed_ID 8684459
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Yang 'X J' J. .
2 Ogryzko 'V V' V. .
3 Nishikawa J . .
4 Howard 'B H' H. .
5 Nakatani Y . .
stop_
_Journal_abbreviation Nature
_Journal_name_full Nature
_Journal_volume 382
_Journal_issue 6589
_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 319
_Page_last 324
_Year 1996
_Details
;
The adenoviral oncoprotein E1A induces progression through the cell cycle by
binding to the products of the p300/CBP and retinoblastoma gene families. A new
cellular p300/CBP-associated factor (P/CAF) having intrinsic histone acetylase
activity has been identified that competes with E1A. Exogenous expression of
P/CAF in HeLa cells inhibits cell-cycle progression and counteracts the
mitogenic activity of E1A. E1A disturbs the normal cellular interaction between
p300/CBP and its associated histone acetylase.
;
save_
##################################
# Molecular system description #
##################################
save_brd
_Saveframe_category molecular_system
_Mol_system_name bromodomain
_Abbreviation_common brd
_Enzyme_commission_number 2.3.1.48
loop_
_Mol_system_component_name
_Mol_label
'brd subunit 1' $brd_monomer
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state .
loop_
_Biological_function
'histone acetylated lysine recognition'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_brd_monomer
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'histone acetyltransferase bromodomain'
_Abbreviation_common brd
_Molecular_mass .
_Mol_thiol_state .
_Details
;
The first 4 residues (GSHM) do not belong to the protein.
First residue (Ser 719), last residue (Lys 832)
No disulfides exist in the molecule
;
##############################
# Polymer residue sequence #
##############################
_Residue_count 118
_Mol_residue_sequence
;
GSHMSKEPRDPDQLYSTLKS
ILQQVKSHQSAWPFMEPVKR
TEAPGYYEVIRSPMDLKTMS
ERLKNRYYVSKKLFMADLQR
VFTNCKEYNAPESEYYKCAN
ILEKFFFSKIKEAGLIDK
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 -4 GLY 2 -3 SER 3 -2 HIS 4 -1 MET 5 719 SER
6 720 LYS 7 721 GLU 8 722 PRO 9 723 ARG 10 724 ASP
11 725 PRO 12 726 ASP 13 727 GLN 14 728 LEU 15 729 TYR
16 730 SER 17 731 THR 18 732 LEU 19 733 LYS 20 734 SER
21 735 ILE 22 736 LEU 23 737 GLN 24 738 GLN 25 739 VAL
26 740 LYS 27 741 SER 28 742 HIS 29 743 GLN 30 744 SER
31 745 ALA 32 746 TRP 33 747 PRO 34 748 PHE 35 749 MET
36 750 GLU 37 751 PRO 38 752 VAL 39 753 LYS 40 754 ARG
41 755 THR 42 756 GLU 43 757 ALA 44 758 PRO 45 759 GLY
46 760 TYR 47 761 TYR 48 762 GLU 49 763 VAL 50 764 ILE
51 765 ARG 52 766 SER 53 767 PRO 54 768 MET 55 769 ASP
56 770 LEU 57 771 LYS 58 772 THR 59 773 MET 60 774 SER
61 775 GLU 62 776 ARG 63 777 LEU 64 778 LYS 65 779 ASN
66 780 ARG 67 781 TYR 68 782 TYR 69 783 VAL 70 784 SER
71 785 LYS 72 786 LYS 73 787 LEU 74 788 PHE 75 789 MET
76 790 ALA 77 791 ASP 78 792 LEU 79 793 GLN 80 794 ARG
81 795 VAL 82 796 PHE 83 797 THR 84 798 ASN 85 799 CYS
86 800 LYS 87 801 GLU 88 802 TYR 89 803 ASN 90 804 ALA
91 805 PRO 92 806 GLU 93 807 SER 94 808 GLU 95 809 TYR
96 810 TYR 97 811 LYS 98 812 CYS 99 813 ALA 100 814 ASN
101 815 ILE 102 816 LEU 103 817 GLU 104 818 LYS 105 819 PHE
106 820 PHE 107 821 PHE 108 822 SER 109 823 LYS 110 824 ILE
111 825 LYS 112 826 GLU 113 827 ALA 114 828 GLY 115 829 LEU
116 830 ILE 117 831 ASP 118 832 LYS
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-02-04
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 1JM4 "Nmr Structure Of PCAF BROMODOMAIN IN COMPLEX WITH HIV-1 Tat Peptide" 100.00 118 98.31 98.31 1.64e-79
PDB 1N72 "Structure And Ligand Of A Histone Acetyltransferase Bromodomain" 100.00 118 98.31 98.31 1.64e-79
PDB 1WUG "Complex Structure Of Pcaf Bromodomain With Small Chemical Ligand Np1" 100.00 118 98.31 98.31 1.64e-79
PDB 1WUM "Complex Structure Of Pcaf Bromodomain With Small Chemical Ligand Np2" 100.00 118 98.31 98.31 1.64e-79
PDB 1ZS5 "Structure-Based Evaluation Of Selective And Non-Selective Small Molecules That Block Hiv-1 Tat And Pcaf Association" 100.00 118 98.31 98.31 1.64e-79
PDB 2RNW "The Structural Basis For Site-Specific Lysine-Acetylated Histone Recognition By The Bromodomains Of The Human Transcriptional C" 100.00 118 98.31 98.31 1.64e-79
PDB 2RNX "The Structural Basis For Site-Specific Lysine-Acetylated Histone Recognition By The Bromodomains Of The Human Transcriptional C" 100.00 118 98.31 98.31 1.64e-79
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Fraction
$brd_monomer human 9606 Eukaryota Metazoa Homo sapiens cytoplasm
stop_
save_
#########################
# Experimental source #
#########################
save_experimental_source
_Saveframe_category experimental_source
loop_
_Mol_label
_Production_method
_Host_organism_name_common
_Genus
_Species
_Strain
_Cell_line
_Vector_type
_Vector_name
$brd_monomer 'recombinant technology' 'E. Coli' Escherichia coli . BL21(DE3) plasmid pET14b
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
_Isotopic_labeling
$brd_monomer 1.0 mM '[U-13C; U-15N; U-75% 2H]'
'phosphate buffer' 100 mM .
'perdeuterated DTT' 5 mM .
EDTA 0.5 mM .
H2O 90 % .
D2O 10 % .
stop_
save_
save_sample_2
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Isotopic_labeling
$brd_monomer 1.0 mM '[U-13C; U-15N]'
'phosphate buffer' 100 mM .
'perdeuterated DTT' 5 mM .
EDTA 0.5 mM .
H2O 90 % .
D2O 10 % .
stop_
save_
############################
# Computer software used #
############################
save_NMRPipe
_Saveframe_category software
_Name NMRPipe
_Version 3.1
loop_
_Task
'spectra Processing'
stop_
_Details .
_Citation_label $ref_1
save_
save_NMRVIEW
_Saveframe_category software
_Name NMRVIEW
_Version 3.1
loop_
_Task
'spectra analysis'
stop_
_Details .
_Citation_label $ref_2
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_spectrometer_1
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 500
_Details .
save_
save_spectrometer_2
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save_2D_1H-15N_HSQC_1
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-15N HSQC'
_Sample_label .
save_
save_2D_1H-13C_HSQC_2
_Saveframe_category NMR_applied_experiment
_Experiment_name '2D 1H-13C HSQC'
_Sample_label .
save_
save_3D_HNCACB_3
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNCACB'
_Sample_label .
save_
save_3D_HN(CO)CACB_4
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HN(CO)CACB'
_Sample_label .
save_
save_3D_(H)C(CO)NH-TOCSY_5
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D (H)C(CO)NH-TOCSY'
_Sample_label .
save_
save_3D_HNHA_6
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HNHA'
_Sample_label .
save_
save_3D_HCCH_TOCSY_7
_Saveframe_category NMR_applied_experiment
_Experiment_name '3D HCCH TOCSY'
_Sample_label .
save_
save_15N_edited_TOCSY_8
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N edited TOCSY'
_Sample_label .
save_
save_15N_edited_NOESY_9
_Saveframe_category NMR_applied_experiment
_Experiment_name '15N edited NOESY'
_Sample_label .
save_
save_13C_edited_NOESY_10
_Saveframe_category NMR_applied_experiment
_Experiment_name '13C edited NOESY'
_Sample_label .
save_
#######################
# Sample conditions #
#######################
save_Ex-cond_1
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 6.5 0.1 na
temperature 303 0.1 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 0.0 . indirect . . . 0.251449530
DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.000000000
DSS N 15 'methyl protons' ppm 0.0 . 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_2
stop_
_Sample_conditions_label $Ex-cond_1
_Chem_shift_reference_set_label $chemical_shift_reference
_Mol_system_component_name 'brd subunit 1'
_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 . 6 LYS HA H 4.36 . 1
2 . 6 LYS HB2 H 1.68 . 1
3 . 6 LYS HB3 H 1.88 . 1
4 . 6 LYS HG2 H 1.43 . 1
5 . 6 LYS HG3 H 1.58 . 1
6 . 6 LYS HD3 H 1.70 . 1
7 . 6 LYS HE3 H 3.00 . 1
8 . 6 LYS CA C 56.30 . 1
9 . 6 LYS CB C 33.14 . 1
10 . 6 LYS CG C 25.43 . 1
11 . 6 LYS CD C 29.83 . 1
12 . 6 LYS CE C 41.96 . 1
13 . 7 GLU H H 8.32 . 1
14 . 7 GLU HA H 4.54 . 1
15 . 7 GLU HB2 H 1.89 . 1
16 . 7 GLU HB3 H 2.02 . 1
17 . 7 GLU HG3 H 2.27 . 1
18 . 7 GLU CA C 54.62 . 1
19 . 7 GLU CB C 29.83 . 1
20 . 7 GLU CG C 35.89 . 1
21 . 7 GLU N N 122.99 . 1
22 . 8 PRO HA H 4.39 . 1
23 . 8 PRO HB2 H 1.88 . 1
24 . 8 PRO HB3 H 2.22 . 1
25 . 8 PRO HG3 H 2.03 . 1
26 . 8 PRO HD2 H 3.66 . 1
27 . 8 PRO HD3 H 3.80 . 1
28 . 8 PRO CA C 63.43 . 1
29 . 8 PRO CB C 32.03 . 1
30 . 8 PRO CG C 27.63 . 1
31 . 8 PRO CD C 50.76 . 1
32 . 9 ARG H H 8.42 . 1
33 . 9 ARG HA H 4.33 . 1
34 . 9 ARG HB2 H 1.76 . 1
35 . 9 ARG HB3 H 1.81 . 1
36 . 9 ARG HG3 H 1.68 . 1
37 . 9 ARG HD3 H 3.16 . 1
38 . 9 ARG CA C 63.43 . 1
39 . 9 ARG CB C 30.93 . 1
40 . 9 ARG CG C 27.63 . 1
41 . 9 ARG CD C 43.60 . 1
42 . 9 ARG N N 121.19 . 1
43 . 10 ASP H H 8.27 . 1
44 . 10 ASP HA H 4.87 . 1
45 . 10 ASP HB2 H 2.69 . 1
46 . 10 ASP HB3 H 2.75 . 1
47 . 10 ASP CA C 52.41 . 1
48 . 10 ASP CB C 41.40 . 1
49 . 10 ASP N N 122.01 . 1
50 . 11 PRO HA H 4.33 . 1
51 . 11 PRO HB2 H 1.97 . 1
52 . 11 PRO HB3 H 2.33 . 1
53 . 11 PRO HG3 H 2.03 . 1
54 . 11 PRO HD3 H 3.87 . 1
55 . 11 PRO CA C 65.08 . 1
56 . 11 PRO CB C 32.59 . 1
57 . 11 PRO CG C 27.63 . 1
58 . 11 PRO CD C 51.31 . 1
59 . 12 ASP H H 8.40 . 1
60 . 12 ASP HA H 4.69 . 1
61 . 12 ASP HB2 H 2.73 . 1
62 . 12 ASP HB3 H 2.79 . 1
63 . 12 ASP CA C 55.72 . 1
64 . 12 ASP CB C 40.55 . 1
65 . 12 ASP N N 119.72 . 1
66 . 13 GLN H H 8.20 . 1
67 . 13 GLN HA H 4.16 . 1
68 . 13 GLN HB3 H 2.15 . 1
69 . 13 GLN HG2 H 2.37 . 1
70 . 13 GLN HG3 H 2.52 . 1
71 . 13 GLN CA C 55.92 . 1
72 . 13 GLN CB C 28.73 . 1
73 . 13 GLN CG C 34.24 . 1
74 . 13 GLN N N 121.36 . 1
75 . 14 LEU H H 8.21 . 1
76 . 14 LEU HA H 4.04 . 1
77 . 14 LEU HB2 H 1.55 . 1
78 . 14 LEU HB3 H 1.85 . 1
79 . 14 LEU HG H 1.48 . 1
80 . 14 LEU HD1 H 0.79 . 1
81 . 14 LEU HD2 H 0.79 . 1
82 . 14 LEU CA C 58.47 . 1
83 . 14 LEU CB C 41.40 . 1
84 . 14 LEU CG C 27.08 . 1
85 . 14 LEU CD1 C 25.97 . 1
86 . 14 LEU CD2 C 23.23 . 1
87 . 14 LEU N N 121.36 . 1
88 . 15 TYR H H 8.02 . 1
89 . 15 TYR HA H 4.04 . 1
90 . 15 TYR HB2 H 3.02 . 1
91 . 15 TYR HB3 H 3.21 . 1
92 . 15 TYR HD1 H 7.05 . 3
93 . 15 TYR HE1 H 6.88 . 3
94 . 15 TYR CA C 62.32 . 1
95 . 15 TYR CB C 38.64 . 1
96 . 15 TYR CD1 C 134.35 . 3
97 . 15 TYR CE1 C 119.48 . 3
98 . 15 TYR N N 119.06 . 1
99 . 16 SER H H 8.17 . 1
100 . 16 SER HA H 3.92 . 1
101 . 16 SER HB3 H 4.00 . 1
102 . 16 SER N N 112.17 . 1
103 . 17 THR H H 8.06 . 1
104 . 17 THR HA H 3.92 . 1
105 . 17 THR HB H 4.25 . 1
106 . 17 THR HG2 H 1.14 . 1
107 . 17 THR CA C 66.73 . 1
108 . 17 THR CB C 68.93 . 1
109 . 17 THR CG2 C 21.57 . 1
110 . 17 THR N N 120.37 . 1
111 . 18 LEU H H 8.46 . 1
112 . 18 LEU HA H 3.29 . 1
113 . 18 LEU HB2 H 0.29 . 1
114 . 18 LEU HB3 H 1.53 . 1
115 . 18 LEU HG H 1.68 . 1
116 . 18 LEU HD1 H 0.47 . 1
117 . 18 LEU HD2 H -0.19 . 1
118 . 18 LEU CA C 57.92 . 1
119 . 18 LEU CB C 39.75 . 1
120 . 18 LEU CG C 24.88 . 1
121 . 18 LEU CD1 C 25.43 . 1
122 . 18 LEU CD2 C 19.92 . 1
123 . 18 LEU N N 120.54 . 1
124 . 19 LYS H H 8.56 . 1
125 . 19 LYS HA H 3.68 . 1
126 . 19 LYS HB2 H 1.36 . 1
127 . 19 LYS HB3 H 1.73 . 1
128 . 19 LYS HG3 H 1.28 . 1
129 . 19 LYS HD3 H 1.58 . 1
130 . 19 LYS HE3 H 2.92 . 1
131 . 19 LYS CA C 60.12 . 1
132 . 19 LYS CB C 32.59 . 1
133 . 19 LYS CG C 24.88 . 1
134 . 19 LYS CD C 29.84 . 1
135 . 19 LYS CE C 41.96 . 1
136 . 19 LYS N N 118.57 . 1
137 . 20 SER H H 7.54 . 1
138 . 20 SER HA H 4.28 . 1
139 . 20 SER HB3 H 4.06 . 1
140 . 20 SER CA C 61.23 . 1
141 . 20 SER CB C 63.88 . 1
142 . 20 SER N N 113.16 . 1
143 . 21 ILE H H 7.95 . 1
144 . 21 ILE HA H 3.79 . 1
145 . 21 ILE HB H 1.88 . 1
146 . 21 ILE HG12 H 1.05 . 1
147 . 21 ILE HG13 H 1.75 . 1
148 . 21 ILE HG2 H 1.00 . 1
149 . 21 ILE HD1 H 0.62 . 1
150 . 21 ILE CA C 65.08 . 1
151 . 21 ILE CB C 38.09 . 1
152 . 21 ILE CG1 C 28.73 . 1
153 . 21 ILE CG2 C 17.17 . 1
154 . 21 ILE CD1 C 13.86 . 1
155 . 21 ILE N N 120.70 . 1
156 . 22 LEU H H 8.84 . 1
157 . 22 LEU HA H 4.09 . 1
158 . 22 LEU HB2 H 1.70 . 1
159 . 22 LEU HB3 H 2.09 . 1
160 . 22 LEU HG H 1.76 . 1
161 . 22 LEU HD1 H 1.06 . 1
162 . 22 LEU HD2 H 0.98 . 1
163 . 22 LEU CA C 58.47 . 1
164 . 22 LEU CB C 41.95 . 1
165 . 22 LEU CG C 27.33 . 1
166 . 22 LEU CD1 C 26.53 . 1
167 . 22 LEU CD2 C 23.78 . 1
168 . 22 LEU N N 119.88 . 1
169 . 23 GLN H H 8.51 . 1
170 . 23 GLN HA H 4.03 . 1
171 . 23 GLN HB2 H 2.26 . 1
172 . 23 GLN HB3 H 2.33 . 1
173 . 23 GLN HG2 H 2.46 . 1
174 . 23 GLN HG3 H 2.54 . 1
175 . 23 GLN CA C 59.02 . 1
176 . 23 GLN CB C 28.18 . 1
177 . 23 GLN CG C 34.24 . 1
178 . 23 GLN N N 117.26 . 1
179 . 24 GLN H H 8.03 . 1
180 . 24 GLN HA H 4.20 . 1
181 . 24 GLN HB2 H 2.47 . 1
182 . 24 GLN HB3 H 2.48 . 1
183 . 24 GLN HG2 H 2.47 . 1
184 . 24 GLN HG3 H 2.84 . 1
185 . 24 GLN HE21 H 6.92 . 1
186 . 24 GLN HE22 H 7.02 . 1
187 . 24 GLN CA C 59.57 . 1
188 . 24 GLN CB C 29.84 . 1
189 . 24 GLN CG C 35.34 . 1
190 . 24 GLN N N 118.90 . 1
191 . 24 GLN NE2 N 110.37 . 1
192 . 25 VAL H H 8.53 . 1
193 . 25 VAL HA H 3.84 . 1
194 . 25 VAL HB H 2.38 . 1
195 . 25 VAL HG1 H 1.18 . 1
196 . 25 VAL HG2 H 1.03 . 1
197 . 25 VAL CA C 67.83 . 1
198 . 25 VAL CB C 32.03 . 1
199 . 25 VAL CG1 C 23.33 . 1
200 . 25 VAL CG2 C 22.12 . 1
201 . 25 VAL N N 119.72 . 1
202 . 26 LYS H H 8.57 . 1
203 . 26 LYS HA H 3.89 . 1
204 . 26 LYS HB3 H 1.87 . 1
205 . 26 LYS HG3 H 1.02 . 1
206 . 26 LYS HD3 H 1.52 . 1
207 . 26 LYS CA C 59.57 . 1
208 . 26 LYS CB C 32.38 . 1
209 . 26 LYS N N 114.63 . 1
210 . 27 SER H H 7.56 . 1
211 . 27 SER HA H 4.45 . 1
212 . 27 SER HB3 H 4.00 . 1
213 . 27 SER CA C 59.02 . 1
214 . 27 SER CB C 63.98 . 1
215 . 27 SER N N 110.37 . 1
216 . 28 HIS H H 7.54 . 1
217 . 28 HIS HA H 3.97 . 1
218 . 28 HIS HB2 H 2.80 . 1
219 . 28 HIS HB3 H 2.99 . 1
220 . 28 HIS HD2 H 4.98 . 1
221 . 28 HIS HE1 H 7.52 . 1
222 . 28 HIS CA C 58.47 . 1
223 . 28 HIS CB C 32.59 . 1
224 . 28 HIS CD2 C 118.93 . 1
225 . 28 HIS CE1 C 138.75 . 1
226 . 28 HIS N N 125.62 . 1
227 . 29 GLN H H 8.54 . 1
228 . 29 GLN HA H 4.21 . 1
229 . 29 GLN HB3 H 2.11 . 1
230 . 29 GLN HG3 H 2.39 . 1
231 . 29 GLN HE21 H 6.87 . 1
232 . 29 GLN HE22 H 7.58 . 1
233 . 29 GLN CA C 59.12 . 1
234 . 29 GLN CB C 29.83 . 1
235 . 29 GLN CG C 33.69 . 1
236 . 29 GLN N N 128.57 . 1
237 . 29 GLN NE2 N 112.17 . 1
238 . 30 SER H H 11.67 . 1
239 . 30 SER HA H 4.84 . 1
240 . 30 SER HB2 H 3.93 . 1
241 . 30 SER HB3 H 4.33 . 1
242 . 30 SER CA C 60.12 . 1
243 . 30 SER CB C 63.98 . 1
244 . 30 SER N N 119.06 . 1
245 . 31 ALA H H 7.87 . 1
246 . 31 ALA HA H 4.40 . 1
247 . 31 ALA HB H 1.69 . 1
248 . 31 ALA CA C 53.51 . 1
249 . 31 ALA CB C 20.47 . 1
250 . 31 ALA N N 117.58 . 1
251 . 32 TRP H H 7.13 . 1
252 . 32 TRP HA H 4.37 . 1
253 . 32 TRP HB2 H 3.35 . 1
254 . 32 TRP HB3 H 3.59 . 1
255 . 32 TRP HD1 H 7.90 . 1
256 . 32 TRP HE1 H 10.47 . 1
257 . 32 TRP HE3 H 7.34 . 1
258 . 32 TRP HZ2 H 7.38 . 1
259 . 32 TRP HZ3 H 7.20 . 1
260 . 32 TRP HH2 H 7.15 . 1
261 . 32 TRP CA C 60.69 . 1
262 . 32 TRP CB C 27.63 . 1
263 . 32 TRP CD1 C 128.84 . 1
264 . 32 TRP CE3 C 122.23 . 1
265 . 32 TRP CZ2 C 116.18 . 1
266 . 32 TRP CZ3 C 123.34 . 1
267 . 32 TRP CH2 C 126.09 . 1
268 . 32 TRP N N 116.60 . 1
269 . 32 TRP NE1 N 131.86 . 1
270 . 33 PRO HA H 3.76 . 1
271 . 33 PRO HB2 H -0.78 . 1
272 . 33 PRO HB3 H 0.49 . 1
273 . 33 PRO HG2 H -0.93 . 1
274 . 33 PRO HG3 H 0.23 . 1
275 . 33 PRO HD2 H 1.57 . 1
276 . 33 PRO HD3 H 2.18 . 1
277 . 33 PRO CA C 64.53 . 1
278 . 33 PRO CB C 29.84 . 1
279 . 33 PRO CG C 26.53 . 1
280 . 33 PRO CD C 50.21 . 1
281 . 34 PHE H H 7.58 . 1
282 . 34 PHE HA H 4.93 . 1
283 . 34 PHE HB2 H 2.53 . 1
284 . 34 PHE HB3 H 3.49 . 1
285 . 34 PHE HD1 H 7.10 . 3
286 . 34 PHE HE1 H 7.17 . 3
287 . 34 PHE HZ H 7.30 . 1
288 . 34 PHE CA C 55.72 . 1
289 . 34 PHE CB C 39.20 . 1
290 . 34 PHE CD1 C 133.25 . 3
291 . 34 PHE N N 113.32 . 1
292 . 35 MET H H 7.12 . 1
293 . 35 MET HA H 4.29 . 1
294 . 35 MET HB2 H 2.17 . 1
295 . 35 MET HB3 H 2.23 . 1
296 . 35 MET HG3 H 2.85 . 1
297 . 35 MET HE H 2.17 . 1
298 . 35 MET CA C 56.82 . 1
299 . 35 MET CB C 32.59 . 1
300 . 35 MET CG C 33.14 . 1
301 . 35 MET CE C 17.17 . 1
302 . 35 MET N N 117.75 . 1
303 . 36 GLU H H 7.71 . 1
304 . 36 GLU HA H 4.85 . 1
305 . 36 GLU HB2 H 1.73 . 1
306 . 36 GLU HB3 H 2.09 . 1
307 . 36 GLU HG3 H 2.16 . 1
308 . 36 GLU CA C 53.52 . 1
309 . 36 GLU CB C 31.49 . 1
310 . 36 GLU CG C 35.89 . 1
311 . 36 GLU N N 113.81 . 1
312 . 37 PRO HA H 4.24 . 1
313 . 37 PRO HB2 H 1.68 . 1
314 . 37 PRO HB3 H 2.33 . 1
315 . 37 PRO HG2 H 1.98 . 1
316 . 37 PRO HG3 H 2.13 . 1
317 . 37 PRO HD3 H 3.67 . 1
318 . 37 PRO CA C 62.88 . 1
319 . 37 PRO CB C 32.04 . 1
320 . 37 PRO CG C 27.08 . 1
321 . 37 PRO CD C 50.76 . 1
322 . 38 VAL H H 8.12 . 1
323 . 38 VAL HA H 3.55 . 1
324 . 38 VAL HB H 1.15 . 1
325 . 38 VAL HG1 H 0.46 . 1
326 . 38 VAL HG2 H 0.17 . 1
327 . 38 VAL CA C 63.43 . 1
328 . 38 VAL CB C 32.58 . 1
329 . 38 VAL CG1 C 21.57 . 1
330 . 38 VAL CG2 C 21.57 . 1
331 . 38 VAL N N 124.45 . 1
332 . 39 LYS H H 9.04 . 1
333 . 39 LYS HA H 4.37 . 1
334 . 39 LYS HB3 H 1.87 . 1
335 . 39 LYS HG3 H 1.44 . 1
336 . 39 LYS HD3 H 1.67 . 1
337 . 39 LYS HE3 H 2.98 . 1
338 . 39 LYS CA C 56.31 . 1
339 . 39 LYS CB C 32.88 . 1
340 . 39 LYS N N 129.88 . 1
341 . 40 ARG H H 8.05 . 1
342 . 40 ARG N N 120.21 . 1
343 . 41 THR HA H 4.04 . 1
344 . 41 THR HB H 4.29 . 1
345 . 41 THR HG2 H 1.27 . 1
346 . 41 THR CA C 63.43 . 1
347 . 41 THR CB C 68.38 . 1
348 . 41 THR CG2 C 22.67 . 1
349 . 42 GLU H H 7.21 . 1
350 . 42 GLU HA H 4.45 . 1
351 . 42 GLU HB2 H 2.00 . 1
352 . 42 GLU HB3 H 2.17 . 1
353 . 42 GLU HG3 H 2.29 . 1
354 . 42 GLU CA C 56.27 . 1
355 . 42 GLU CB C 30.93 . 1
356 . 42 GLU CG C 36.44 . 1
357 . 42 GLU N N 118.73 . 1
358 . 43 ALA H H 7.38 . 1
359 . 43 ALA HA H 4.94 . 1
360 . 43 ALA HB H 1.08 . 1
361 . 43 ALA CA C 50.22 . 1
362 . 43 ALA CB C 19.37 . 1
363 . 43 ALA N N 122.50 . 1
364 . 44 PRO HA H 4.50 . 1
365 . 44 PRO HB2 H 2.03 . 1
366 . 44 PRO HB3 H 2.37 . 1
367 . 44 PRO HG2 H 2.04 . 1
368 . 44 PRO HG3 H 2.12 . 1
369 . 44 PRO HD2 H 3.52 . 1
370 . 44 PRO HD3 H 3.72 . 1
371 . 44 PRO CA C 65.08 . 1
372 . 44 PRO CB C 31.49 . 1
373 . 44 PRO CG C 27.63 . 1
374 . 44 PRO CD C 50.21 . 1
375 . 46 TYR H H 7.95 . 1
376 . 46 TYR HA H 3.54 . 1
377 . 46 TYR HB2 H 2.49 . 1
378 . 46 TYR HB3 H 2.69 . 1
379 . 46 TYR HD1 H 5.12 . 3
380 . 46 TYR HE1 H 6.07 . 3
381 . 46 TYR CA C 62.33 . 1
382 . 46 TYR CB C 39.75 . 1
383 . 46 TYR CD1 C 133.80 . 3
384 . 46 TYR CE1 C 118.38 . 3
385 . 46 TYR N N 122.50 . 1
386 . 47 TYR H H 8.22 . 1
387 . 47 TYR HA H 4.10 . 1
388 . 47 TYR HB2 H 2.80 . 1
389 . 47 TYR HB3 H 3.19 . 1
390 . 47 TYR HD1 H 7.34 . 3
391 . 47 TYR HE1 H 6.65 . 3
392 . 47 TYR CA C 60.68 . 1
393 . 47 TYR CB C 37.55 . 1
394 . 47 TYR CD1 C 134.90 . 3
395 . 47 TYR CE1 C 118.93 . 3
396 . 47 TYR N N 113.16 . 1
397 . 48 GLU H H 7.70 . 1
398 . 48 GLU HA H 4.21 . 1
399 . 48 GLU HB3 H 2.09 . 1
400 . 48 GLU HG2 H 2.27 . 1
401 . 48 GLU HG3 H 2.33 . 1
402 . 48 GLU CA C 57.92 . 1
403 . 48 GLU CB C 29.48 . 1
404 . 48 GLU CG C 37.55 . 1
405 . 48 GLU N N 117.91 . 1
406 . 49 VAL H H 7.13 . 1
407 . 49 VAL HA H 4.08 . 1
408 . 49 VAL HB H 2.02 . 1
409 . 49 VAL HG1 H 1.04 . 1
410 . 49 VAL HG2 H 0.99 . 1
411 . 49 VAL CA C 63.43 . 1
412 . 49 VAL CB C 33.69 . 1
413 . 49 VAL CG1 C 21.02 . 1
414 . 49 VAL CG2 C 21.57 . 1
415 . 49 VAL N N 115.45 . 1
416 . 50 ILE H H 7.95 . 1
417 . 50 ILE HA H 3.92 . 1
418 . 50 ILE HB H 1.21 . 1
419 . 50 ILE HG12 H 0.22 . 1
420 . 50 ILE HG13 H 0.80 . 1
421 . 50 ILE HG2 H 0.38 . 1
422 . 50 ILE HD1 H 0.54 . 1
423 . 50 ILE CA C 57.92 . 1
424 . 50 ILE CB C 34.24 . 1
425 . 50 ILE CG1 C 24.88 . 1
426 . 50 ILE CG2 C 16.62 . 1
427 . 50 ILE CD1 C 9.46 . 1
428 . 50 ILE N N 122.83 . 1
429 . 51 ARG H H 7.75 . 1
430 . 51 ARG HA H 3.88 . 1
431 . 51 ARG HB2 H 1.21 . 1
432 . 51 ARG HB3 H 1.39 . 1
433 . 51 ARG HG2 H 1.17 . 1
434 . 51 ARG HG3 H 1.32 . 1
435 . 51 ARG HD3 H 2.97 . 1
436 . 51 ARG CA C 57.37 . 1
437 . 51 ARG CB C 30.94 . 1
438 . 51 ARG CG C 27.08 . 1
439 . 51 ARG CD C 43.05 . 1
440 . 51 ARG N N 125.29 . 1
441 . 52 SER H H 8.39 . 1
442 . 52 SER HA H 4.98 . 1
443 . 52 SER HB2 H 2.91 . 1
444 . 52 SER HB3 H 3.03 . 1
445 . 52 SER CA C 54.62 . 1
446 . 52 SER CB C 66.20 . 1
447 . 52 SER N N 116.60 . 1
448 . 53 PRO HA H 4.08 . 1
449 . 53 PRO HB3 H 2.21 . 1
450 . 53 PRO HG2 H 1.88 . 1
451 . 53 PRO HG3 H 2.18 . 1
452 . 53 PRO HD2 H 3.39 . 1
453 . 53 PRO HD3 H 3.62 . 1
454 . 53 PRO CA C 63.43 . 1
455 . 53 PRO CB C 32.59 . 1
456 . 53 PRO CG C 28.18 . 1
457 . 53 PRO CD C 50.76 . 1
458 . 54 MET H H 8.43 . 1
459 . 54 MET HA H 4.93 . 1
460 . 54 MET HB2 H 1.35 . 1
461 . 54 MET HB3 H 1.99 . 1
462 . 54 MET HG3 H 2.69 . 1
463 . 54 MET HE H 1.93 . 1
464 . 54 MET CA C 54.07 . 1
465 . 54 MET CB C 31.49 . 1
466 . 54 MET CG C 30.93 . 1
467 . 54 MET CE C 14.41 . 1
468 . 54 MET N N 119.06 . 1
469 . 55 ASP H H 7.37 . 1
470 . 55 ASP HA H 4.75 . 1
471 . 55 ASP HB3 H 2.37 . 1
472 . 55 ASP CA C 53.52 . 1
473 . 55 ASP CB C 44.15 . 1
474 . 55 ASP N N 119.06 . 1
475 . 56 LEU H H 9.05 . 1
476 . 56 LEU HA H 4.04 . 1
477 . 56 LEU HB2 H 1.40 . 1
478 . 56 LEU HB3 H 2.10 . 1
479 . 56 LEU HG H 1.71 . 1
480 . 56 LEU HD1 H 0.94 . 1
481 . 56 LEU HD2 H 0.63 . 1
482 . 56 LEU CA C 57.92 . 1
483 . 56 LEU CB C 41.40 . 1
484 . 56 LEU CG C 27.08 . 1
485 . 56 LEU CD1 C 27.08 . 1
486 . 56 LEU CD2 C 22.68 . 1
487 . 56 LEU N N 116.27 . 1
488 . 57 LYS H H 8.74 . 1
489 . 57 LYS HA H 4.20 . 1
490 . 57 LYS HB2 H 2.22 . 1
491 . 57 LYS HB3 H 2.33 . 1
492 . 57 LYS HG2 H 1.40 . 1
493 . 57 LYS HG3 H 1.48 . 1
494 . 57 LYS HD2 H 1.70 . 1
495 . 57 LYS HD3 H 1.79 . 1
496 . 57 LYS HE3 H 2.96 . 1
497 . 57 LYS CA C 60.68 . 1
498 . 57 LYS CB C 32.04 . 1
499 . 57 LYS CG C 25.28 . 1
500 . 57 LYS CD C 30.39 . 1
501 . 57 LYS CE C 41.95 . 1
502 . 57 LYS N N 128.08 . 1
503 . 58 THR H H 9.45 . 1
504 . 58 THR HA H 3.85 . 1
505 . 58 THR HB H 4.09 . 1
506 . 58 THR HG2 H 1.06 . 1
507 . 58 THR CA C 67.04 . 1
508 . 58 THR CB C 67.83 . 1
509 . 58 THR CG2 C 22.12 . 1
510 . 58 THR N N 122.18 . 1
511 . 59 MET H H 7.88 . 1
512 . 59 MET HA H 4.32 . 1
513 . 59 MET HB2 H 1.92 . 1
514 . 59 MET HB3 H 2.09 . 1
515 . 59 MET HG2 H 2.50 . 1
516 . 59 MET HG3 H 2.62 . 1
517 . 59 MET HE H 1.24 . 1
518 . 59 MET CA C 60.68 . 1
519 . 59 MET CB C 33.34 . 1
520 . 59 MET CG C 33.14 . 1
521 . 59 MET CE C 16.62 . 1
522 . 59 MET N N 117.91 . 1
523 . 60 SER H H 7.96 . 1
524 . 60 SER HA H 4.20 . 1
525 . 60 SER HB2 H 4.04 . 1
526 . 60 SER HB3 H 4.37 . 1
527 . 60 SER CA C 62.88 . 1
528 . 60 SER CB C 62.88 . 1
529 . 60 SER N N 116.11 . 1
530 . 61 GLU H H 8.15 . 1
531 . 61 GLU HA H 4.04 . 1
532 . 61 GLU HB2 H 2.06 . 1
533 . 61 GLU HB3 H 2.25 . 1
534 . 61 GLU HG2 H 2.18 . 1
535 . 61 GLU HG3 H 2.35 . 1
536 . 61 GLU CA C 59.57 . 1
537 . 61 GLU CB C 29.28 . 1
538 . 61 GLU CG C 36.44 . 1
539 . 61 GLU N N 124.47 . 1
540 . 62 ARG H H 8.39 . 1
541 . 62 ARG HA H 3.87 . 1
542 . 62 ARG HB2 H 1.08 . 1
543 . 62 ARG HB3 H 2.05 . 1
544 . 62 ARG HG2 H 0.88 . 1
545 . 62 ARG HG3 H 1.72 . 1
546 . 62 ARG HD2 H 2.05 . 1
547 . 62 ARG HD3 H 2.58 . 1
548 . 62 ARG CA C 60.68 . 1
549 . 62 ARG CB C 30.39 . 1
550 . 62 ARG CG C 29.28 . 1
551 . 62 ARG CD C 44.15 . 1
552 . 62 ARG N N 120.37 . 1
553 . 63 LEU H H 8.86 . 1
554 . 63 LEU HA H 4.69 . 1
555 . 63 LEU HB2 H 1.93 . 1
556 . 63 LEU HB3 H 2.29 . 1
557 . 63 LEU HG H 1.83 . 1
558 . 63 LEU HD1 H 1.07 . 1
559 . 63 LEU HD2 H 0.87 . 1
560 . 63 LEU CA C 58.47 . 1
561 . 63 LEU CB C 42.62 . 1
562 . 63 LEU CG C 27.08 . 1
563 . 63 LEU CD1 C 25.43 . 1
564 . 63 LEU CD2 C 27.08 . 1
565 . 63 LEU N N 120.21 . 1
566 . 64 LYS H H 7.96 . 1
567 . 64 LYS HA H 4.33 . 1
568 . 64 LYS HB3 H 2.06 . 1
569 . 64 LYS HG3 H 1.60 . 1
570 . 64 LYS HD3 H 1.80 . 1
571 . 64 LYS HE3 H 2.99 . 1
572 . 64 LYS CA C 59.57 . 1
573 . 64 LYS CB C 32.59 . 1
574 . 64 LYS CG C 24.88 . 1
575 . 64 LYS CD C 29.84 . 1
576 . 64 LYS CE C 41.95 . 1
577 . 64 LYS N N 120.37 . 1
578 . 65 ASN H H 7.95 . 1
579 . 65 ASN HA H 4.77 . 1
580 . 65 ASN HB2 H 2.77 . 1
581 . 65 ASN HB3 H 3.02 . 1
582 . 65 ASN HD21 H 6.97 . 1
583 . 65 ASN HD22 H 7.60 . 1
584 . 65 ASN CA C 53.51 . 1
585 . 65 ASN CB C 38.09 . 1
586 . 65 ASN N N 116.11 . 1
587 . 65 ASN ND2 N 112.67 . 1
588 . 66 ARG H H 8.16 . 1
589 . 66 ARG HA H 4.41 . 1
590 . 66 ARG HB2 H 2.02 . 1
591 . 66 ARG HB3 H 2.10 . 1
592 . 66 ARG HG2 H 1.53 . 1
593 . 66 ARG HG3 H 1.54 . 1
594 . 66 ARG HD2 H 3.02 . 1
595 . 66 ARG HD3 H 3.06 . 1
596 . 66 ARG CA C 56.82 . 1
597 . 66 ARG CB C 25.43 . 1
598 . 66 ARG CG C 27.63 . 1
599 . 66 ARG CD C 43.05 . 1
600 . 66 ARG N N 114.14 . 1
601 . 67 TYR H H 8.22 . 1
602 . 67 TYR HA H 4.06 . 1
603 . 67 TYR HB2 H 2.06 . 1
604 . 67 TYR HB3 H 2.95 . 1
605 . 67 TYR HD1 H 6.29 . 3
606 . 67 TYR HE1 H 6.71 . 3
607 . 67 TYR CA C 60.12 . 1
608 . 67 TYR CB C 40.85 . 1
609 . 67 TYR CD1 C 134.35 . 3
610 . 67 TYR CE1 C 118.93 . 3
611 . 67 TYR N N 116.76 . 1
612 . 68 TYR H H 8.01 . 1
613 . 68 TYR HA H 4.53 . 1
614 . 68 TYR HB2 H 2.91 . 1
615 . 68 TYR HB3 H 3.06 . 1
616 . 68 TYR HD1 H 7.17 . 3
617 . 68 TYR HE1 H 7.29 . 3
618 . 68 TYR CA C 57.92 . 1
619 . 68 TYR CB C 36.44 . 1
620 . 68 TYR CD1 C 133.25 . 3
621 . 68 TYR CE1 C 120.58 . 3
622 . 68 TYR N N 114.63 . 1
623 . 69 VAL H H 7.70 . 1
624 . 69 VAL HA H 4.08 . 1
625 . 69 VAL HB H 2.32 . 1
626 . 69 VAL HG1 H 0.94 . 1
627 . 69 VAL HG2 H 0.82 . 1
628 . 69 VAL CA C 62.33 . 1
629 . 69 VAL CB C 31.50 . 1
630 . 69 VAL CG1 C 21.57 . 1
631 . 69 VAL CG2 C 18.82 . 1
632 . 69 VAL N N 115.78 . 1
633 . 70 SER H H 7.42 . 1
634 . 70 SER HA H 4.74 . 1
635 . 70 SER HB2 H 3.75 . 1
636 . 70 SER HB3 H 4.20 . 1
637 . 70 SER CA C 55.72 . 1
638 . 70 SER CB C 66.18 . 1
639 . 70 SER N N 111.35 . 1
640 . 71 LYS HA H 4.02 . 1
641 . 71 LYS CA C 59.03 . 1
642 . 71 LYS CB C 31.59 . 1
643 . 72 LYS H H 8.24 . 1
644 . 72 LYS HA H 4.06 . 1
645 . 72 LYS HB3 H 1.78 . 1
646 . 72 LYS HD3 H 1.68 . 1
647 . 72 LYS HE2 H 3.04 . 1
648 . 72 LYS HE3 H 3.14 . 1
649 . 72 LYS CA C 59.72 . 1
650 . 72 LYS CB C 30.39 . 1
651 . 72 LYS CG C 24.53 . 1
652 . 72 LYS CD C 28.18 . 1
653 . 72 LYS CE C 41.67 . 1
654 . 72 LYS N N 120.21 . 1
655 . 73 LEU H H 7.42 . 1
656 . 73 LEU HA H 4.21 . 1
657 . 73 LEU HB2 H 1.89 . 1
658 . 73 LEU HB3 H 2.00 . 1
659 . 73 LEU HG H 1.79 . 1
660 . 73 LEU HD1 H 0.92 . 1
661 . 73 LEU HD2 H 0.90 . 1
662 . 73 LEU CA C 57.92 . 1
663 . 73 LEU CB C 43.60 . 1
664 . 73 LEU CG C 27.63 . 1
665 . 73 LEU CD1 C 25.98 . 1
666 . 73 LEU CD2 C 23.78 . 1
667 . 73 LEU N N 118.73 . 1
668 . 74 PHE H H 6.93 . 1
669 . 74 PHE HA H 3.76 . 1
670 . 74 PHE HB2 H 2.38 . 1
671 . 74 PHE HB3 H 2.94 . 1
672 . 74 PHE HD1 H 6.40 . 3
673 . 74 PHE HE1 H 6.93 . 3
674 . 74 PHE CA C 60.68 . 1
675 . 74 PHE CB C 39.75 . 1
676 . 74 PHE CD1 C 133.80 . 3
677 . 74 PHE CE1 C 131.60 . 3
678 . 74 PHE N N 118.73 . 1
679 . 75 MET H H 8.49 . 1
680 . 75 MET HA H 3.91 . 1
681 . 75 MET HB2 H 2.21 . 1
682 . 75 MET HB3 H 2.32 . 1
683 . 75 MET HG2 H 2.61 . 1
684 . 75 MET HG3 H 2.94 . 1
685 . 75 MET HE H 2.03 . 1
686 . 75 MET CA C 59.02 . 1
687 . 75 MET CB C 32.59 . 1
688 . 75 MET CG C 33.14 . 1
689 . 75 MET CE C 17.17 . 1
690 . 75 MET N N 116.27 . 1
691 . 76 ALA H H 8.00 . 1
692 . 76 ALA HA H 4.08 . 1
693 . 76 ALA HB H 1.49 . 1
694 . 76 ALA CA C 55.17 . 1
695 . 76 ALA CB C 18.27 . 1
696 . 76 ALA N N 119.72 . 1
697 . 77 ASP H H 7.38 . 1
698 . 77 ASP HA H 4.37 . 1
699 . 77 ASP HB3 H 2.73 . 1
700 . 77 ASP CA C 57.37 . 1
701 . 77 ASP CB C 38.65 . 1
702 . 77 ASP N N 119.72 . 1
703 . 78 LEU H H 7.36 . 1
704 . 78 LEU HA H 3.40 . 1
705 . 78 LEU HB2 H 0.44 . 1
706 . 78 LEU HB3 H 0.76 . 1
707 . 78 LEU HG H 0.71 . 1
708 . 78 LEU HD1 H 0.18 . 1
709 . 78 LEU HD2 H 0.06 . 1
710 . 78 LEU CA C 57.92 . 1
711 . 78 LEU CB C 40.30 . 1
712 . 78 LEU CG C 27.63 . 1
713 . 78 LEU CD1 C 24.33 . 1
714 . 78 LEU CD2 C 25.98 . 1
715 . 78 LEU N N 119.55 . 1
716 . 79 GLN H H 8.07 . 1
717 . 79 GLN HA H 3.80 . 1
718 . 79 GLN HB2 H 2.10 . 1
719 . 79 GLN HB3 H 2.16 . 1
720 . 79 GLN HG3 H 2.46 . 1
721 . 79 GLN HE21 H 7.22 . 1
722 . 79 GLN HE22 H 7.32 . 1
723 . 79 GLN CA C 59.02 . 1
724 . 79 GLN CB C 28.73 . 1
725 . 79 GLN CG C 35.34 . 1
726 . 79 GLN N N 114.14 . 1
727 . 79 GLN NE2 N 111.35 . 1
728 . 80 ARG H H 7.38 . 1
729 . 80 ARG HA H 4.08 . 1
730 . 80 ARG HB2 H 1.89 . 1
731 . 80 ARG HB3 H 1.97 . 1
732 . 80 ARG HG3 H 1.74 . 1
733 . 80 ARG HD2 H 3.33 . 1
734 . 80 ARG HD3 H 3.39 . 1
735 . 80 ARG CA C 58.47 . 1
736 . 80 ARG CB C 29.84 . 1
737 . 80 ARG CG C 27.08 . 1
738 . 80 ARG CD C 43.60 . 1
739 . 80 ARG N N 118.57 . 1
740 . 81 VAL H H 7.01 . 1
741 . 81 VAL HA H 3.04 . 1
742 . 81 VAL HB H 1.44 . 1
743 . 81 VAL HG1 H 0.48 . 1
744 . 81 VAL HG2 H 0.14 . 1
745 . 81 VAL CA C 66.73 . 1
746 . 81 VAL CB C 30.93 . 1
747 . 81 VAL CG1 C 22.12 . 1
748 . 81 VAL CG2 C 21.57 . 1
749 . 81 VAL N N 117.91 . 1
750 . 82 PHE H H 6.36 . 1
751 . 82 PHE HA H 4.16 . 1
752 . 82 PHE HB2 H 2.94 . 1
753 . 82 PHE HB3 H 3.09 . 1
754 . 82 PHE HD1 H 6.64 . 3
755 . 82 PHE HE1 H 6.46 . 3
756 . 82 PHE HZ H 6.41 . 1
757 . 82 PHE CA C 58.47 . 1
758 . 82 PHE CB C 38.10 . 1
759 . 82 PHE CD1 C 132.15 . 3
760 . 82 PHE CE1 C 131.60 . 3
761 . 82 PHE CZ C 129.39 . 1
762 . 82 PHE N N 116.93 . 1
763 . 83 THR H H 9.05 . 1
764 . 83 THR HA H 3.84 . 1
765 . 83 THR HB H 4.21 . 1
766 . 83 THR HG2 H 1.30 . 1
767 . 83 THR CA C 66.73 . 1
768 . 83 THR CB C 68.38 . 1
769 . 83 THR CG2 C 22.12 . 1
770 . 83 THR N N 115.29 . 1
771 . 84 ASN H H 8.85 . 1
772 . 84 ASN HA H 4.32 . 1
773 . 84 ASN HB2 H 2.66 . 1
774 . 84 ASN HB3 H 2.98 . 1
775 . 84 ASN CA C 55.17 . 1
776 . 84 ASN CB C 38.09 . 1
777 . 84 ASN N N 120.70 . 1
778 . 85 CYS H H 6.89 . 1
779 . 85 CYS HA H 4.41 . 1
780 . 85 CYS HB2 H 3.03 . 1
781 . 85 CYS HB3 H 3.30 . 1
782 . 85 CYS CA C 62.16 . 1
783 . 85 CYS CB C 26.53 . 1
784 . 85 CYS N N 116.93 . 1
785 . 86 LYS H H 7.80 . 1
786 . 86 LYS HA H 4.20 . 1
787 . 86 LYS HB3 H 1.74 . 1
788 . 86 LYS HG2 H 0.14 . 1
789 . 86 LYS HG3 H 1.31 . 1
790 . 86 LYS HD3 H 1.29 . 1
791 . 86 LYS HE2 H 2.42 . 1
792 . 86 LYS HE3 H 2.49 . 1
793 . 86 LYS CA C 58.47 . 1
794 . 86 LYS CB C 32.59 . 1
795 . 86 LYS CG C 25.43 . 1
796 . 86 LYS CD C 29.84 . 1
797 . 86 LYS CE C 41.40 . 1
798 . 86 LYS N N 116.76 . 1
799 . 87 GLU H H 7.95 . 1
800 . 87 GLU HA H 4.25 . 1
801 . 87 GLU HB2 H 2.00 . 1
802 . 87 GLU HB3 H 2.17 . 1
803 . 87 GLU HG2 H 2.20 . 1
804 . 87 GLU HG3 H 2.41 . 1
805 . 87 GLU CA C 57.99 . 1
806 . 87 GLU CB C 30.39 . 1
807 . 87 GLU CG C 36.99 . 1
808 . 87 GLU N N 117.91 . 1
809 . 88 TYR H H 7.74 . 1
810 . 88 TYR HA H 4.37 . 1
811 . 88 TYR HB3 H 2.93 . 1
812 . 88 TYR HD1 H 6.99 . 3
813 . 88 TYR HE1 H 6.82 . 3
814 . 88 TYR CA C 60.68 . 1
815 . 88 TYR CB C 41.40 . 1
816 . 88 TYR CD1 C 134.90 . 3
817 . 88 TYR CE1 C 119.48 . 3
818 . 88 TYR N N 116.60 . 1
819 . 89 ASN H H 8.24 . 1
820 . 89 ASN HA H 5.02 . 1
821 . 89 ASN HB2 H 2.91 . 1
822 . 89 ASN HB3 H 3.07 . 1
823 . 89 ASN HD21 H 7.81 . 1
824 . 89 ASN HD22 H 8.32 . 1
825 . 89 ASN CA C 51.86 . 1
826 . 89 ASN CB C 40.85 . 1
827 . 89 ASN N N 115.94 . 1
828 . 89 ASN ND2 N 118.73 . 1
829 . 91 PRO HA H 2.42 . 1
830 . 91 PRO HB3 H 1.95 . 1
831 . 91 PRO HG2 H 1.56 . 1
832 . 91 PRO HG3 H 1.65 . 1
833 . 91 PRO HD2 H 3.60 . 1
834 . 91 PRO HD3 H 3.71 . 1
835 . 91 PRO CA C 63.98 . 1
836 . 91 PRO CD C 50.76 . 1
837 . 92 GLU H H 8.25 . 1
838 . 92 GLU HA H 4.18 . 1
839 . 92 GLU HB2 H 1.97 . 1
840 . 92 GLU HB3 H 2.10 . 1
841 . 92 GLU HG3 H 2.20 . 1
842 . 92 GLU CA C 56.82 . 1
843 . 92 GLU CB C 28.73 . 1
844 . 92 GLU CG C 36.27 . 1
845 . 92 GLU N N 112.99 . 1
846 . 93 SER H H 8.11 . 1
847 . 93 SER HA H 4.41 . 1
848 . 93 SER HB2 H 4.16 . 1
849 . 93 SER HB3 H 4.39 . 1
850 . 93 SER CA C 58.47 . 1
851 . 93 SER CB C 66.18 . 1
852 . 93 SER N N 115.78 . 1
853 . 94 GLU H H 9.06 . 1
854 . 94 GLU HA H 4.23 . 1
855 . 94 GLU HB3 H 2.17 . 1
856 . 94 GLU HG3 H 2.53 . 1
857 . 94 GLU CA C 59.57 . 1
858 . 94 GLU CB C 29.84 . 1
859 . 94 GLU CG C 36.44 . 1
860 . 94 GLU N N 123.49 . 1
861 . 95 TYR H H 8.07 . 1
862 . 95 TYR HA H 3.83 . 1
863 . 95 TYR HB2 H 2.74 . 1
864 . 95 TYR HB3 H 3.02 . 1
865 . 95 TYR HD1 H 6.89 . 3
866 . 95 TYR HE1 H 7.01 . 3
867 . 95 TYR CA C 60.12 . 1
868 . 95 TYR CB C 37.55 . 1
869 . 95 TYR CD1 C 132.70 . 3
870 . 95 TYR CE1 C 120.03 . 3
871 . 95 TYR N N 116.44 . 1
872 . 96 TYR H H 7.36 . 1
873 . 96 TYR HA H 3.82 . 1
874 . 96 TYR HB2 H 2.50 . 1
875 . 96 TYR HB3 H 3.39 . 1
876 . 96 TYR HD1 H 7.09 . 3
877 . 96 TYR HE1 H 7.00 . 3
878 . 96 TYR CA C 61.78 . 1
879 . 96 TYR CB C 40.30 . 1
880 . 96 TYR CD1 C 136.55 . 3
881 . 96 TYR CE1 C 119.48 . 3
882 . 96 TYR N N 119.88 . 1
883 . 97 LYS H H 8.07 . 1
884 . 97 LYS HA H 4.20 . 1
885 . 97 LYS HB3 H 2.09 . 1
886 . 97 LYS HG2 H 1.58 . 1
887 . 97 LYS HG3 H 1.82 . 1
888 . 97 LYS HD3 H 1.81 . 1
889 . 97 LYS HE3 H 2.96 . 1
890 . 97 LYS CA C 60.68 . 1
891 . 97 LYS CB C 32.59 . 1
892 . 97 LYS CG C 25.98 . 1
893 . 97 LYS CD C 29.83 . 1
894 . 97 LYS CE C 41.96 . 1
895 . 97 LYS N N 118.08 . 1
896 . 98 CYS H H 8.52 . 1
897 . 98 CYS HA H 4.20 . 1
898 . 98 CYS HB2 H 3.06 . 1
899 . 98 CYS HB3 H 3.40 . 1
900 . 98 CYS CA C 65.09 . 1
901 . 98 CYS CB C 27.08 . 1
902 . 98 CYS N N 116.76 . 1
903 . 99 ALA H H 8.31 . 1
904 . 99 ALA HA H 3.83 . 1
905 . 99 ALA HB H 1.60 . 1
906 . 99 ALA CA C 55.56 . 1
907 . 99 ALA CB C 18.27 . 1
908 . 99 ALA N N 120.70 . 1
909 . 100 ASN H H 8.07 . 1
910 . 100 ASN HA H 4.33 . 1
911 . 100 ASN HB2 H 2.83 . 1
912 . 100 ASN HB3 H 2.88 . 1
913 . 100 ASN CA C 56.27 . 1
914 . 100 ASN CB C 38.65 . 1
915 . 100 ASN N N 115.45 . 1
916 . 101 ILE H H 7.91 . 1
917 . 101 ILE HA H 3.65 . 1
918 . 101 ILE HB H 1.92 . 1
919 . 101 ILE HG12 H 1.20 . 1
920 . 101 ILE HG13 H 1.88 . 1
921 . 101 ILE HG2 H 1.02 . 1
922 . 101 ILE HD1 H 0.94 . 1
923 . 101 ILE CA C 65.08 . 1
924 . 101 ILE CB C 39.20 . 1
925 . 101 ILE CG1 C 29.28 . 1
926 . 101 ILE CG2 C 17.72 . 1
927 . 101 ILE CD1 C 13.86 . 1
928 . 101 ILE N N 119.88 . 1
929 . 102 LEU H H 8.56 . 1
930 . 102 LEU HA H 3.67 . 1
931 . 102 LEU HB2 H 1.20 . 1
932 . 102 LEU HB3 H 1.41 . 1
933 . 102 LEU HG H 1.58 . 1
934 . 102 LEU HD1 H 0.70 . 1
935 . 102 LEU HD2 H 0.70 . 1
936 . 102 LEU CA C 56.82 . 1
937 . 102 LEU CB C 41.95 . 1
938 . 102 LEU CG C 26.53 . 1
939 . 102 LEU CD1 C 24.33 . 1
940 . 102 LEU CD2 C 25.43 . 1
941 . 102 LEU N N 122.50 . 1
942 . 103 GLU H H 8.07 . 1
943 . 103 GLU HA H 3.19 . 1
944 . 103 GLU HB2 H 1.31 . 1
945 . 103 GLU HB3 H 1.72 . 1
946 . 103 GLU HG2 H 1.92 . 1
947 . 103 GLU HG3 H 2.00 . 1
948 . 103 GLU CA C 60.12 . 1
949 . 103 GLU CB C 29.84 . 1
950 . 103 GLU CG C 37.55 . 1
951 . 103 GLU N N 120.70 . 1
952 . 104 LYS H H 7.14 . 1
953 . 104 LYS HA H 4.08 . 1
954 . 104 LYS HB3 H 1.93 . 1
955 . 104 LYS HG3 H 1.49 . 1
956 . 104 LYS HD3 H 1.68 . 1
957 . 104 LYS HE3 H 2.96 . 1
958 . 104 LYS CA C 59.69 . 1
959 . 104 LYS CB C 32.59 . 1
960 . 104 LYS CG C 25.64 . 1
961 . 104 LYS CD C 29.28 . 1
962 . 104 LYS CE C 41.96 . 1
963 . 104 LYS N N 117.58 . 1
964 . 105 PHE H H 7.87 . 1
965 . 105 PHE HA H 4.33 . 1
966 . 105 PHE HB2 H 3.05 . 1
967 . 105 PHE HB3 H 3.13 . 1
968 . 105 PHE HD1 H 7.18 . 3
969 . 105 PHE CA C 61.23 . 1
970 . 105 PHE CB C 39.20 . 1
971 . 105 PHE CD1 C 133.80 . 3
972 . 105 PHE N N 121.03 . 1
973 . 106 PHE H H 9.13 . 1
974 . 106 PHE HA H 3.96 . 1
975 . 106 PHE HB2 H 3.07 . 1
976 . 106 PHE HB3 H 3.29 . 1
977 . 106 PHE HD1 H 6.90 . 3
978 . 106 PHE HE1 H 7.01 . 3
979 . 106 PHE CA C 60.69 . 1
980 . 106 PHE CB C 38.64 . 1
981 . 106 PHE CD1 C 133.25 . 3
982 . 106 PHE CE1 C 132.70 . 3
983 . 106 PHE N N 120.70 . 1
984 . 107 PHE H H 8.36 . 1
985 . 107 PHE HA H 3.84 . 1
986 . 107 PHE HB3 H 3.06 . 1
987 . 107 PHE HD1 H 7.17 . 3
988 . 107 PHE HE1 H 7.29 . 3
989 . 107 PHE HZ H 7.43 . 1
990 . 107 PHE CA C 61.77 . 1
991 . 107 PHE CB C 38.09 . 1
992 . 107 PHE CD1 C 133.25 . 3
993 . 107 PHE CE1 C 132.70 . 3
994 . 107 PHE CZ C 131.60 . 1
995 . 107 PHE N N 118.08 . 1
996 . 108 SER H H 7.91 . 1
997 . 108 SER HA H 4.20 . 1
998 . 108 SER HB3 H 4.01 . 1
999 . 108 SER CA C 61.77 . 1
1000 . 108 SER CB C 62.88 . 1
1001 . 108 SER N N 114.96 . 1
1002 . 109 LYS H H 7.94 . 1
1003 . 109 LYS HA H 4.01 . 1
1004 . 109 LYS HB2 H 1.57 . 1
1005 . 109 LYS HB3 H 1.73 . 1
1006 . 109 LYS HG3 H 0.83 . 1
1007 . 109 LYS HD3 H 1.40 . 1
1008 . 109 LYS HE2 H 2.42 . 1
1009 . 109 LYS HE3 H 2.57 . 1
1010 . 109 LYS CA C 56.82 . 1
1011 . 109 LYS CB C 31.49 . 1
1012 . 109 LYS CG C 23.23 . 1
1013 . 109 LYS CD C 27.08 . 1
1014 . 109 LYS CE C 42.50 . 1
1015 . 109 LYS N N 120.86 . 1
1016 . 110 ILE H H 8.10 . 1
1017 . 110 ILE HA H 3.82 . 1
1018 . 110 ILE HB H 1.75 . 1
1019 . 110 ILE HG12 H 1.07 . 1
1020 . 110 ILE HG13 H 1.14 . 1
1021 . 110 ILE HG2 H 0.65 . 1
1022 . 110 ILE HD1 H 0.54 . 1
1023 . 110 ILE CA C 64.53 . 1
1024 . 110 ILE CB C 36.99 . 1
1025 . 110 ILE CG1 C 26.53 . 1
1026 . 110 ILE CG2 C 18.82 . 1
1027 . 110 ILE CD1 C 13.31 . 1
1028 . 110 ILE N N 116.93 . 1
1029 . 111 LYS H H 7.55 . 1
1030 . 111 LYS HA H 4.04 . 1
1031 . 111 LYS HB2 H 1.76 . 1
1032 . 111 LYS HB3 H 1.88 . 1
1033 . 111 LYS HG2 H 1.30 . 1
1034 . 111 LYS HG3 H 1.39 . 1
1035 . 111 LYS HD3 H 1.63 . 1
1036 . 111 LYS HE3 H 2.91 . 1
1037 . 111 LYS CA C 59.02 . 1
1038 . 111 LYS CB C 32.36 . 1
1039 . 111 LYS CG C 24.88 . 1
1040 . 111 LYS CD C 29.28 . 1
1041 . 111 LYS CE C 41.40 . 1
1042 . 111 LYS N N 122.18 . 1
1043 . 112 GLU H H 8.06 . 1
1044 . 112 GLU HA H 4.00 . 1
1045 . 112 GLU HB3 H 2.06 . 1
1046 . 112 GLU HG2 H 2.21 . 1
1047 . 112 GLU HG3 H 2.34 . 1
1048 . 112 GLU CA C 59.02 . 1
1049 . 112 GLU CB C 29.83 . 1
1050 . 112 GLU CG C 36.05 . 1
1051 . 112 GLU N N 121.19 . 1
1052 . 113 ALA H H 7.62 . 1
1053 . 113 ALA HA H 4.29 . 1
1054 . 113 ALA HB H 1.36 . 1
1055 . 113 ALA CA C 52.41 . 1
1056 . 113 ALA CB C 19.92 . 1
1057 . 113 ALA N N 117.75 . 1
1058 . 114 GLY H H 7.74 . 1
1059 . 114 GLY HA2 H 3.94 . 1
1060 . 114 GLY HA3 H 4.02 . 1
1061 . 114 GLY CA C 45.90 . 1
1062 . 114 GLY N N 105.85 . 1
1063 . 115 LEU H H 7.74 . 1
1064 . 115 LEU HA H 4.21 . 1
1065 . 115 LEU HB3 H 1.56 . 1
1066 . 115 LEU HG H 1.54 . 1
1067 . 115 LEU HD1 H 0.71 . 1
1068 . 115 LEU CA C 55.72 . 1
1069 . 115 LEU CB C 43.05 . 1
1070 . 115 LEU CG C 27.63 . 1
1071 . 115 LEU CD1 C 23.78 . 1
1072 . 115 LEU N N 117.91 . 1
1073 . 116 ILE H H 7.46 . 1
1074 . 116 ILE HA H 4.23 . 1
1075 . 116 ILE HB H 1.81 . 1
1076 . 116 ILE HG12 H 0.92 . 1
1077 . 116 ILE HG13 H 1.31 . 1
1078 . 116 ILE HG2 H 0.81 . 1
1079 . 116 ILE HD1 H 0.79 . 1
1080 . 116 ILE CA C 60.68 . 1
1081 . 116 ILE CB C 39.75 . 1
1082 . 116 ILE CG1 C 27.08 . 1
1083 . 116 ILE CG2 C 17.72 . 1
1084 . 116 ILE CD1 C 13.31 . 1
1085 . 116 ILE N N 115.45 . 1
1086 . 117 ASP H H 8.27 . 1
1087 . 117 ASP HA H 4.57 . 1
1088 . 117 ASP HB2 H 2.54 . 1
1089 . 117 ASP HB3 H 2.69 . 1
1090 . 117 ASP CA C 54.62 . 1
1091 . 117 ASP CB C 41.40 . 1
1092 . 117 ASP N N 123.49 . 1
1093 . 118 LYS H H 7.77 . 1
1094 . 118 LYS HA H 4.08 . 1
1095 . 118 LYS CA C 57.72 . 1
1096 . 118 LYS CB C 33.41 . 1
1097 . 118 LYS N N 125.45 . 1
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