data_4202
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Solution Structure of Reduced Monomeric Q133M2 Copper, Zinc Superoxide Dismutase(SOD). Why SOD is a Dimeric Enzyme?
;
_BMRB_accession_number 4202
_BMRB_flat_file_name bmr4202.str
_Entry_type original
_Submission_date 1997-02-28
_Accession_date 1997-02-02
_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 Banci Lucia . .
2 Benedetto Marco . .
3 Bertini Ivano . .
4 'Del Conte' Rebecca . .
5 Piccioli Mario . .
6 Viezzoli Maria Silvia .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 799
"13C chemical shifts" 577
"15N chemical shifts" 157
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2012-11-07 update BMRB 'change CE1 and CE2 to HE1 and HE2 for residue 20 PHE'
2000-04-04 original author 'original release'
stop_
save_
#############################
# Citation for this entry #
#############################
save_entry_citation
_Saveframe_category entry_citation
_Citation_full .
_Citation_title 'Solution Structure of Reduced Monomeric Q133M2 Copper, Zinc Superoxide Dismutase (SOD). Why SOD is a Dimeric Enzyme?'
_Citation_status published
_Citation_type journal
_CAS_abstract_code .
_MEDLINE_UI_code 98384143
_PubMed_ID ?
loop_
_Author_ordinal
_Author_family_name
_Author_given_name
_Author_middle_initials
_Author_family_title
1 Banci Lucia . .
2 Benedetto Marco . .
3 Bertini Ivano . .
4 'Del Conte' Rebecca . .
5 Piccioli Mario . .
6 Viezzoli Maria Silvia .
stop_
_Journal_abbreviation Biochemistry
_Journal_volume 37
_Journal_issue 34
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 11780
_Page_last 11791
_Year 1998
_Details .
loop_
_Keyword
'copper-zinc enzyme'
'Superoxide dismutase'
stop_
save_
##################################
# Molecular system description #
##################################
save_system_SOD
_Saveframe_category molecular_system
_Mol_system_name 'Superoxide Dismutase'
_Abbreviation_common SOD
_Enzyme_commission_number 1.15.1.1
loop_
_Mol_system_component_name
_Mol_label
'Q133M2 SOD' $Q133M2_SOD
CU $entity_CU
Zn $entity_ZN
stop_
_System_molecular_weight .
_System_physical_state native
_System_oligomer_state monomer
_System_paramagnetic no
_System_thiol_state 'all disufide bound'
loop_
_Biological_function
'Dismutation of superoxide radicals to molecular oxygen and hydrogen peroxide"'
stop_
_Database_query_date .
_Details .
save_
########################
# Monomeric polymers #
########################
save_Q133M2_SOD
_Saveframe_category monomeric_polymer
_Mol_type polymer
_Mol_polymer_class protein
_Name_common 'Superoxide Dismutase'
_Name_variant 'E133Q, F50E, G51E'
_Abbreviation_common Q133M2SOD
_Molecular_mass 16000
_Mol_thiol_state 'all disulfide bound'
_Details
;
The SOD studied is in the reduced form:
Cu(I), Zn(II) superoxide dismutase
The mutations are:
E 133 Q, F 50 E, G 51 E
;
##############################
# Polymer residue sequence #
##############################
_Residue_count 153
_Mol_residue_sequence
;
ATKAVAVLKGDGPVQGIINF
EQKESNGPVKVWGSIKGLTE
GLHGFHVHEEEDNTAGCTSA
GPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIE
DSVISLSGDHSIIGRTLVVH
EKADDLGKGGNEQSTKTGNA
GSRLACGVIGIAQ
;
loop_
_Residue_seq_code
_Residue_author_seq_code
_Residue_label
1 1 ALA 2 2 THR 3 3 LYS 4 4 ALA 5 5 VAL
6 6 ALA 7 7 VAL 8 8 LEU 9 9 LYS 10 10 GLY
11 11 ASP 12 12 GLY 13 13 PRO 14 14 VAL 15 15 GLN
16 16 GLY 17 17 ILE 18 18 ILE 19 19 ASN 20 20 PHE
21 21 GLU 22 22 GLN 23 23 LYS 24 24 GLU 25 25 SER
26 26 ASN 27 27 GLY 28 28 PRO 29 29 VAL 30 30 LYS
31 31 VAL 32 32 TRP 33 33 GLY 34 34 SER 35 35 ILE
36 36 LYS 37 37 GLY 38 38 LEU 39 39 THR 40 40 GLU
41 41 GLY 42 42 LEU 43 43 HIS 44 44 GLY 45 45 PHE
46 46 HIS 47 47 VAL 48 48 HIS 49 49 GLU 50 50 GLU
51 51 GLU 52 52 ASP 53 53 ASN 54 54 THR 55 55 ALA
56 56 GLY 57 57 CYS 58 58 THR 59 59 SER 60 60 ALA
61 61 GLY 62 62 PRO 63 63 HIS 64 64 PHE 65 65 ASN
66 66 PRO 67 67 LEU 68 68 SER 69 69 ARG 70 70 LYS
71 71 HIS 72 72 GLY 73 73 GLY 74 74 PRO 75 75 LYS
76 76 ASP 77 77 GLU 78 78 GLU 79 79 ARG 80 80 HIS
81 81 VAL 82 82 GLY 83 83 ASP 84 84 LEU 85 85 GLY
86 86 ASN 87 87 VAL 88 88 THR 89 89 ALA 90 90 ASP
91 91 LYS 92 92 ASP 93 93 GLY 94 94 VAL 95 95 ALA
96 96 ASP 97 97 VAL 98 98 SER 99 99 ILE 100 100 GLU
101 101 ASP 102 102 SER 103 103 VAL 104 104 ILE 105 105 SER
106 106 LEU 107 107 SER 108 108 GLY 109 109 ASP 110 110 HIS
111 111 SER 112 112 ILE 113 113 ILE 114 114 GLY 115 115 ARG
116 116 THR 117 117 LEU 118 118 VAL 119 119 VAL 120 120 HIS
121 121 GLU 122 122 LYS 123 123 ALA 124 124 ASP 125 125 ASP
126 126 LEU 127 127 GLY 128 128 LYS 129 129 GLY 130 130 GLY
131 131 ASN 132 132 GLU 133 133 GLN 134 134 SER 135 135 THR
136 136 LYS 137 137 THR 138 138 GLY 139 139 ASN 140 140 ALA
141 141 GLY 142 142 SER 143 143 ARG 144 144 LEU 145 145 ALA
146 146 CYS 147 147 GLY 148 148 VAL 149 149 ILE 150 150 GLY
151 151 ILE 152 152 ALA 153 153 GLN
stop_
_Sequence_homology_query_date .
_Sequence_homology_query_revised_last_date 2015-08-04
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
BMRB 15711 SOD1 100.00 153 98.69 100.00 2.26e-102
BMRB 15712 SOD1 100.00 153 98.04 99.35 1.10e-101
BMRB 15713 SOD1 100.00 153 98.04 99.35 2.12e-101
BMRB 15714 SOD1 100.00 153 98.04 99.35 2.32e-101
BMRB 18509 Superoxide_dismutase_C6A-C111S_thermostable_mutant 100.00 153 98.04 98.69 2.17e-100
BMRB 18708 SUPEROXIDE_DISMUTASE_CU-ZN 100.00 153 98.04 98.69 2.17e-100
BMRB 18968 SOD1 100.00 153 98.69 100.00 2.26e-102
BMRB 26570 SOD1 100.00 153 98.04 98.69 2.17e-100
PDB 1BA9 "The Solution Structure Of Reduced Monomeric Superoxide Dismutase, Nmr, 36 Structures" 99.35 153 100.00 100.00 1.01e-102
PDB 1DSW "The Solution Structure Of A Monomeric, Reduced Form Of Human Copper, Zinc Superoxide Dismutase Bearing The Same Charge As The N" 99.35 153 98.03 98.68 4.05e-100
PDB 1FUN "Superoxide Dismutase Mutant With Lys 136 Replaced By Glu, Cys 6 Replaced By Ala And Cys 111 Replaced By Ser (K136e, C6a, C111s)" 100.00 153 97.39 98.69 9.60e-100
PDB 1KMG "The Solution Structure Of Monomeric Copper-Free Superoxide Dismutase" 100.00 153 100.00 100.00 2.41e-103
PDB 1L3N "The Solution Structure Of Reduced Dimeric Copper Zinc Sod: The Structural Effects Of Dimerization" 100.00 153 98.04 98.69 2.17e-100
PDB 1MFM "Monomeric Human Sod Mutant F50eG51EE133Q AT ATOMIC Resolution" 100.00 153 100.00 100.00 2.41e-103
PDB 1N18 "Thermostable Mutant Of Human Superoxide Dismutase, C6a, C111s" 100.00 154 98.04 98.69 1.48e-100
PDB 1N19 "Structure Of The Hsod A4v Mutant" 100.00 154 97.39 98.04 9.30e-100
PDB 1PTZ "Crystal Structure Of The Human Cu, Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (Fals) Mutant H43r" 100.00 153 97.39 98.04 1.71e-99
PDB 1RK7 "Solution Structure Of Apo Cu,Zn Superoxide Dismutase: Role Of Metal Ions In Protein Folding" 100.00 153 100.00 100.00 2.41e-103
PDB 1SOS "Atomic Structures Of Wild-type And Thermostable Mutant Recombinant Human Cu, Zn Superoxide Dismutase" 100.00 154 98.04 98.69 2.25e-100
PDB 2AF2 "Solution Structure Of Disulfide Reduced And Copper Depleted Human Superoxide Dismutase" 100.00 153 98.04 98.69 2.17e-100
PDB 2GBT "C6aC111A CUZN SUPEROXIDE DISMUTASE" 100.00 153 97.39 98.69 5.27e-100
PDB 2LU5 "Structure And Chemical Shifts Of Cu(I),Zn(Ii) Superoxide Dismutase By Solid-State Nmr" 100.00 153 98.04 98.69 2.17e-100
PDB 2XJK "Monomeric Human Cu,Zn Superoxide Dismutase" 100.00 153 98.69 100.00 2.26e-102
PDB 4BCY "Monomeric Human Cu,zn Superoxide Dismutase, Mutation H43f" 100.00 153 98.04 99.35 2.22e-101
PDB 4OH2 "Crystal Structure Of Cu/zn Superoxide Dismutase I149t" 100.00 153 97.39 98.04 1.29e-99
GB AAA72747 "CuZn superoxide dismutase [synthetic construct]" 100.00 154 98.04 98.69 1.48e-100
GB AAA80237 "HSOD-GlyProGly-A+, partial [synthetic construct]" 100.00 171 98.04 98.69 7.52e-100
stop_
save_
#############
# Ligands #
#############
save_CU
_Saveframe_category ligand
_Mol_type "non-polymer (NON-POLYMER)"
_Name_common 'COPPER (II) ION'
_BMRB_code CU
_PDB_code CU
_Molecular_mass 63.546
_Mol_charge 2
_Mol_paramagnetic .
_Mol_aromatic no
_Details .
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
CU CU CU . 2 . ?
stop_
_Mol_thiol_state .
_Sequence_homology_query_date .
save_
save_ZN
_Saveframe_category ligand
_Mol_type "non-polymer (NON-POLYMER)"
_Name_common 'ZINC ION'
_BMRB_code ZN
_PDB_code ZN
_Molecular_mass 65.409
_Mol_charge 2
_Mol_paramagnetic .
_Mol_aromatic no
_Details .
loop_
_Atom_name
_PDB_atom_name
_Atom_type
_Atom_chirality
_Atom_charge
_Atom_oxidation_number
_Atom_unpaired_electrons
ZN ZN ZN . 2 . ?
stop_
_Mol_thiol_state .
_Sequence_homology_query_date .
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Details
$Q133M2_SOD Human 9606 Eukaryota Metazoa Homo sapiens
;
expressed in E. coli TOPP I strain (Stratagene)
The human SOD gene has been expressed in the pBR322 plasmid
;
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
$Q133M2_SOD 'recombinant technology' 'E. coli' Escherichia coli TOPP_1 plasmid pBR322
stop_
save_
#####################################
# Sample contents and methodology #
#####################################
########################
# Sample description #
########################
save_sample_one
_Saveframe_category sample
_Sample_type solution
_Details .
loop_
_Mol_label
_Concentration_value
_Concentration_value_units
_Concentration_min_value
_Concentration_max_value
_Isotopic_labeling
$Q133M2_SOD . mM 2 3 '[U-13C; U-15N]'
stop_
save_
#########################
# Experimental detail #
#########################
##################################
# NMR Spectrometer definitions #
##################################
save_NMR_spectrometer_one
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model AMX
_Field_strength 600
_Details .
save_
save_NMR_spectrometer_two
_Saveframe_category NMR_spectrometer
_Manufacturer Bruker
_Model DRX
_Field_strength 600
_Details .
save_
save_NMR_spectrometer_three
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Avance
_Field_strength 800
_Details .
save_
save_NMR_spectrometer_four
_Saveframe_category NMR_spectrometer
_Manufacturer Varian
_Model Avance
_Field_strength 600
_Details .
save_
#############################
# NMR applied experiments #
#############################
save__1
_Saveframe_category NMR_applied_experiment
_Sample_label $sample_one
save_
#######################
# Sample conditions #
#######################
save_sample_conditions_one
_Saveframe_category sample_conditions
_Details .
loop_
_Variable_type
_Variable_value
_Variable_value_error
_Variable_value_units
pH 5.0 0.01 na
temperature 298 0.2 K
stop_
save_
####################
# NMR parameters #
####################
##############################
# Assigned chemical shifts #
##############################
################################
# Chemical shift referencing #
################################
save_chemical_shift_reference_one
_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 external indirect . . . 0.25144952
DSS H 1 'methyl protons' ppm 0.00 external direct . . . .
DSS N 15 'methyl protons' ppm 0.00 external indirect . . . 0.10132905
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_chemical_shift_assignment_one
_Saveframe_category assigned_chemical_shifts
_Details .
loop_
_Sample_label
$sample_one
stop_
_Sample_conditions_label $sample_conditions_one
_Chem_shift_reference_set_label $chemical_shift_reference_one
_Mol_system_component_name 'Q133M2 SOD'
_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 ALA C C 174.0 . 1
2 . 1 ALA CA C 52.3 . 1
3 . 1 ALA HA H 4.25 . 1
4 . 1 ALA CB C 20.3 . 1
5 . 1 ALA HB H 1.61 . 1
6 . 2 THR N N 116.5 . 1
7 . 2 THR H H 8.55 . 1
8 . 2 THR C C 172.4 . 1
9 . 2 THR CA C 62.5 . 1
10 . 2 THR HA H 4.45 . 1
11 . 2 THR CB C 70.1 . 1
12 . 2 THR HB H 3.98 . 1
13 . 2 THR CG2 C 22.4 . 1
14 . 2 THR HG2 H 1.31 . 1
15 . 3 LYS N N 126.3 . 1
16 . 3 LYS H H 8.73 . 1
17 . 3 LYS C C 174.5 . 1
18 . 3 LYS CA C 55.0 . 1
19 . 3 LYS HA H 5.38 . 1
20 . 3 LYS CB C 36.3 . 1
21 . 3 LYS HB2 H 2.02 . 1
22 . 3 LYS HB3 H 2.02 . 1
23 . 3 LYS CG C 25.4 . 1
24 . 3 LYS HG2 H 1.52 . 1
25 . 3 LYS HG3 H 1.52 . 1
26 . 3 LYS CD C 29.3 . 1
27 . 3 LYS HD2 H 1.81 . 1
28 . 3 LYS HD3 H 1.81 . 1
29 . 3 LYS CE C 42.0 . 1
30 . 3 LYS HE2 H 3.00 . 1
31 . 3 LYS HE3 H 3.00 . 1
32 . 4 ALA N N 123.5 . 1
33 . 4 ALA H H 9.18 . 1
34 . 4 ALA C C 175.3 . 1
35 . 4 ALA CA C 50.8 . 1
36 . 4 ALA HA H 5.32 . 1
37 . 4 ALA CB C 23.7 . 1
38 . 4 ALA HB H 1.06 . 1
39 . 5 VAL N N 121.3 . 1
40 . 5 VAL H H 9.49 . 1
41 . 5 VAL C C 173.1 . 1
42 . 5 VAL CA C 60.4 . 1
43 . 5 VAL HA H 5.35 . 1
44 . 5 VAL CB C 36.2 . 1
45 . 5 VAL HB H 2.00 . 1
46 . 5 VAL CG1 C 19.6 . 1
47 . 5 VAL HG1 H 0.86 . 1
48 . 5 VAL CG2 C 21.8 . 1
49 . 5 VAL HG2 H 0.83 . 1
50 . 6 ALA N N 129.6 . 1
51 . 6 ALA H H 9.45 . 1
52 . 6 ALA C C 174.5 . 1
53 . 6 ALA CA C 51.0 . 1
54 . 6 ALA HA H 4.89 . 1
55 . 6 ALA CB C 23.2 . 1
56 . 6 ALA HB H 1.15 . 1
57 . 7 VAL N N 125.9 . 1
58 . 7 VAL H H 9.30 . 1
59 . 7 VAL C C 175.7 . 1
60 . 7 VAL CA C 62.0 . 1
61 . 7 VAL HA H 4.34 . 1
62 . 7 VAL CB C 31.7 . 1
63 . 7 VAL HB H 2.03 . 1
64 . 7 VAL CG1 C 20.9 . 1
65 . 7 VAL HG1 H 0.96 . 1
66 . 7 VAL CG2 C 20.9 . 1
67 . 7 VAL HG2 H 0.91 . 1
68 . 8 LEU N N 126.7 . 1
69 . 8 LEU H H 8.78 . 1
70 . 8 LEU C C 176.1 . 1
71 . 8 LEU CA C 54.3 . 1
72 . 8 LEU HA H 4.30 . 1
73 . 8 LEU CB C 42.7 . 1
74 . 8 LEU HB2 H 1.36 . 1
75 . 8 LEU HB3 H 1.46 . 1
76 . 8 LEU CG C 26.1 . 1
77 . 8 LEU HG H 0.92 . 1
78 . 8 LEU CD1 C 23.6 . 1
79 . 8 LEU HD1 H 0.64 . 1
80 . 8 LEU CD2 C 23.6 . 1
81 . 8 LEU HD2 H 0.52 . 1
82 . 9 LYS N N 121.9 . 1
83 . 9 LYS H H 8.52 . 1
84 . 9 LYS C C 175.2 . 1
85 . 9 LYS CA C 55.3 . 1
86 . 9 LYS HA H 4.90 . 1
87 . 9 LYS CB C 35.6 . 1
88 . 9 LYS HB2 H 2.06 . 1
89 . 9 LYS HB3 H 1.99 . 1
90 . 9 LYS CG C 23.8 . 1
91 . 9 LYS HG2 H 1.49 . 2
92 . 9 LYS HG3 H 1.57 . 2
93 . 9 LYS CD C 29.2 . 1
94 . 9 LYS HD2 H 1.78 . 1
95 . 9 LYS HD3 H 1.78 . 1
96 . 9 LYS CE C 42.2 . 1
97 . 9 LYS HE2 H 3.03 . 1
98 . 9 LYS HE3 H 3.03 . 1
99 . 10 GLY N N 112.0 . 1
100 . 10 GLY H H 8.86 . 1
101 . 10 GLY C C 173.3 . 1
102 . 10 GLY CA C 45.7 . 1
103 . 10 GLY HA2 H 4.26 . 1
104 . 10 GLY HA3 H 4.88 . 1
105 . 11 ASP N N 121.9 . 1
106 . 11 ASP H H 8.62 . 1
107 . 11 ASP C C 176.5 . 1
108 . 11 ASP CA C 54.1 . 1
109 . 11 ASP HA H 4.82 . 1
110 . 11 ASP CB C 40.5 . 1
111 . 11 ASP HB2 H 2.7 . 1
112 . 11 ASP HB3 H 2.56 . 1
113 . 12 GLY N N 110.7 . 1
114 . 12 GLY H H 8.01 . 1
115 . 12 GLY C C 173.6 . 1
116 . 12 GLY CA C 44.4 . 1
117 . 12 GLY HA2 H 4.30 . 1
118 . 12 GLY HA3 H 4.20 . 1
119 . 13 PRO C C 176.7 . 1
120 . 13 PRO CA C 63.6 . 1
121 . 13 PRO HA H 4.51 . 1
122 . 13 PRO CB C 32.6 . 1
123 . 13 PRO HB2 H 2.19 . 1
124 . 13 PRO HB3 H 2.13 . 1
125 . 13 PRO CG C 26.0 . 1
126 . 13 PRO HG2 H 2.00 . 2
127 . 13 PRO HG3 H 2.07 . 2
128 . 13 PRO CD C 49.5 . 1
129 . 13 PRO HD2 H 3.58 . 2
130 . 13 PRO HD3 H 3.86 . 2
131 . 14 VAL N N 121.3 . 1
132 . 14 VAL H H 7.47 . 1
133 . 14 VAL C C 176.0 . 1
134 . 14 VAL CA C 63.0 . 1
135 . 14 VAL HA H 4.51 . 1
136 . 14 VAL CB C 30.3 . 1
137 . 14 VAL HB H 1.64 . 1
138 . 14 VAL CG1 C 22.1 . 1
139 . 14 VAL HG1 H 0.75 . 1
140 . 14 VAL CG2 C 19.7 . 1
141 . 14 VAL HG2 H 0.45 . 1
142 . 15 GLN N N 123.7 . 1
143 . 15 GLN H H 8.02 . 1
144 . 15 GLN C C 174.3 . 1
145 . 15 GLN CA C 53.7 . 1
146 . 15 GLN HA H 4.87 . 1
147 . 15 GLN CB C 32.9 . 1
148 . 15 GLN HB2 H 2.04 . 1
149 . 15 GLN HB3 H 2.04 . 1
150 . 15 GLN CG C 32.9 . 1
151 . 15 GLN HG2 H 2.18 . 2
152 . 15 GLN HG3 H 2.36 . 2
153 . 16 GLY N N 107.9 . 1
154 . 16 GLY H H 8.27 . 1
155 . 16 GLY C C 171.0 . 1
156 . 16 GLY CA C 46.9 . 1
157 . 16 GLY HA2 H 4.45 . 1
158 . 16 GLY HA3 H 4.56 . 1
159 . 17 ILE N N 121.0 . 1
160 . 17 ILE H H 8.07 . 1
161 . 17 ILE C C 174.1 . 1
162 . 17 ILE CA C 61.3 . 1
163 . 17 ILE HA H 4.73 . 1
164 . 17 ILE CB C 40.7 . 1
165 . 17 ILE HB H 1.72 . 1
166 . 17 ILE CG1 C 8.0 . 1
167 . 17 ILE HG12 H 1.04 . 2
168 . 17 ILE HG13 H 1.58 . 2
169 . 17 ILE CG2 C 16.8 . 1
170 . 17 ILE HG2 H 0.75 . 1
171 . 17 ILE CD1 C 13.6 . 1
172 . 17 ILE HD1 H 0.88 . 1
173 . 18 ILE N N 127.1 . 1
174 . 18 ILE H H 8.87 . 1
175 . 18 ILE C C 172.5 . 1
176 . 18 ILE CA C 56.9 . 1
177 . 18 ILE HA H 4.22 . 1
178 . 18 ILE CB C 37.6 . 1
179 . 18 ILE HB H 1.68 . 1
180 . 18 ILE HG12 H 1.34 . 1
181 . 18 ILE HG13 H 1.34 . 1
182 . 18 ILE HG2 H 0.43 . 1
183 . 18 ILE HD1 H 0.17 . 1
184 . 18 ILE CG1 C 25.6 . 1
185 . 18 ILE CG2 C 20.9 . 1
186 . 18 ILE CD1 C 18.8 . 1
187 . 19 ASN N N 125.1 . 1
188 . 19 ASN H H 8.81 . 1
189 . 19 ASN C C 172.3 . 1
190 . 19 ASN CA C 52.5 . 1
191 . 19 ASN HA H 4.82 . 1
192 . 19 ASN CB C 40.2 . 1
193 . 19 ASN HB2 H 0.32 . 1
194 . 19 ASN HB3 H 1.49 . 1
195 . 20 PHE N N 115.5 . 1
196 . 20 PHE H H 8.52 . 1
197 . 20 PHE C C 176.3 . 1
198 . 20 PHE CA C 55.5 . 1
199 . 20 PHE HA H 5.80 . 1
200 . 20 PHE CB C 43.2 . 1
201 . 20 PHE HB2 H 2.69 . 1
202 . 20 PHE HB3 H 2.69 . 1
203 . 20 PHE HD1 H 6.83 . 2
204 . 20 PHE HD2 H 6.85 . 2
205 . 20 PHE HE1 H 7.9 . 1
206 . 20 PHE HE2 H 7.9 . 1
207 . 21 GLU N N 122.5 . 1
208 . 21 GLU H H 9.57 . 1
209 . 21 GLU C C 173.7 . 1
210 . 21 GLU CA C 56.0 . 1
211 . 21 GLU HA H 5.39 . 1
212 . 21 GLU CB C 34.2 . 1
213 . 21 GLU HB2 H 2.39 . 1
214 . 21 GLU HB3 H 2.29 . 1
215 . 21 GLU HG2 H 2.16 . 1
216 . 21 GLU HG3 H 2.16 . 1
217 . 21 GLU CG C 37.2 . 1
218 . 22 GLN N N 129.9 . 1
219 . 22 GLN H H 9.23 . 1
220 . 22 GLN C C 174.6 . 1
221 . 22 GLN CA C 54.5 . 1
222 . 22 GLN HA H 4.96 . 1
223 . 22 GLN CB C 33.1 . 1
224 . 22 GLN HB2 H 2.29 . 1
225 . 22 GLN HB3 H 2.29 . 1
226 . 22 GLN HG2 H 2.47 . 1
227 . 22 GLN HG3 H 2.47 . 1
228 . 22 GLN HE21 H 7.36 . 2
229 . 22 GLN HE22 H 8.39 . 2
230 . 22 GLN CG C 33.1 . 1
231 . 22 GLN NE2 N 115.9 . 1
232 . 23 LYS C C 176.2 . 1
233 . 23 LYS CA C 59.9 . 1
234 . 23 LYS HA H 4.07 . 1
235 . 23 LYS CB C 33.4 . 1
236 . 23 LYS HB2 H 1.95 . 1
237 . 23 LYS HB3 H 1.95 . 1
238 . 23 LYS HG2 H 1.50 . 2
239 . 23 LYS HG3 H 1.63 . 2
240 . 23 LYS HD2 H 1.75 . 1
241 . 23 LYS HD3 H 1.75 . 1
242 . 23 LYS HE2 H 3.02 . 1
243 . 23 LYS HE3 H 3.02 . 1
244 . 23 LYS CG C 25.7 . 1
245 . 23 LYS CD C 29.4 . 1
246 . 23 LYS CE C 41.9 . 1
247 . 24 GLU N N 116.3 . 1
248 . 24 GLU H H 8.20 . 1
249 . 24 GLU C C 177.2 . 1
250 . 24 GLU CA C 54.3 . 1
251 . 24 GLU HA H 4.66 . 1
252 . 24 GLU CB C 32.4 . 1
253 . 24 GLU HB2 H 2.16 . 1
254 . 24 GLU HB3 H 1.84 . 1
255 . 24 GLU HG2 H 2.22 . 1
256 . 24 GLU HG3 H 2.22 . 1
257 . 24 GLU CG C 35.4 . 1
258 . 25 SER H H 8.41 . 1
259 . 25 SER C C 174.7 . 1
260 . 25 SER CA C 60.6 . 1
261 . 25 SER HA H 3.98 . 1
262 . 25 SER CB C 62.5 . 1
263 . 25 SER HB2 H 3.8 . 1
264 . 25 SER HB3 H 3.8 . 1
265 . 26 ASN N N 117.8 . 1
266 . 26 ASN H H 8.40 . 1
267 . 26 ASN C C 175.0 . 1
268 . 26 ASN CA C 53.2 . 1
269 . 26 ASN HA H 4.68 . 1
270 . 26 ASN CB C 38.0 . 1
271 . 26 ASN HB2 H 2.93 . 1
272 . 26 ASN HB3 H 2.93 . 1
273 . 26 ASN HD21 H 6.89 . 2
274 . 26 ASN HD22 H 7.60 . 2
275 . 26 ASN ND2 N 113.5 . 1
276 . 27 GLY N N 108.3 . 1
277 . 27 GLY H H 8.00 . 1
278 . 27 GLY C C 172.1 . 1
279 . 27 GLY CA C 44.8 . 1
280 . 27 GLY HA2 H 4.02 . 1
281 . 27 GLY HA3 H 4.58 . 1
282 . 28 PRO C C 176.2 . 1
283 . 28 PRO CA C 63.1 . 1
284 . 28 PRO HA H 4.62 . 1
285 . 28 PRO CB C 32.4 . 1
286 . 28 PRO HB2 H 2.22 . 1
287 . 28 PRO HB3 H 1.78 . 1
288 . 28 PRO HG2 H 2.04 . 1
289 . 28 PRO HG3 H 2.04 . 1
290 . 28 PRO HD2 H 3.72 . 1
291 . 28 PRO HD3 H 3.72 . 1
292 . 28 PRO CG C 27.0 . 1
293 . 28 PRO CD C 49.4 . 1
294 . 29 VAL N N 122.0 . 1
295 . 29 VAL H H 9.09 . 1
296 . 29 VAL C C 175.4 . 1
297 . 29 VAL CA C 61.0 . 1
298 . 29 VAL HA H 4.60 . 1
299 . 29 VAL CB C 33.3 . 1
300 . 29 VAL HB H 2.16 . 1
301 . 29 VAL HG1 H 1.02 . 1
302 . 29 VAL HG2 H 0.91 . 1
303 . 29 VAL CG1 C 23.2 . 1
304 . 29 VAL CG2 C 23.7 . 1
305 . 30 LYS N N 128.5 . 1
306 . 30 LYS H H 9.19 . 1
307 . 30 LYS C C 175.3 . 1
308 . 30 LYS CA C 55.9 . 1
309 . 30 LYS HA H 4.99 . 1
310 . 30 LYS CB C 34.2 . 1
311 . 30 LYS HB2 H 2.07 . 1
312 . 30 LYS HB3 H 1.98 . 1
313 . 30 LYS HE2 H 2.63 . 2
314 . 30 LYS HE3 H 2.72 . 2
315 . 30 LYS CE C 41.7 . 1
316 . 31 VAL N N 127.3 . 1
317 . 31 VAL H H 9.30 . 1
318 . 31 VAL C C 175.5 . 1
319 . 31 VAL CA C 60.5 . 1
320 . 31 VAL HA H 4.94 . 1
321 . 31 VAL CB C 33.4 . 1
322 . 31 VAL HB H 2.10 . 1
323 . 31 VAL HG1 H 0.88 . 1
324 . 31 VAL HG2 H 0.29 . 1
325 . 31 VAL CG1 C 20.1 . 1
326 . 31 VAL CG2 C 20.8 . 1
327 . 32 TRP N N 126.4 . 1
328 . 32 TRP H H 9.04 . 1
329 . 32 TRP C C 173.4 . 1
330 . 32 TRP CA C 56.2 . 1
331 . 32 TRP HA H 5.60 . 1
332 . 32 TRP CB C 32.1 . 1
333 . 32 TRP HB2 H 3.34 . 1
334 . 32 TRP HB3 H 3.49 . 1
335 . 32 TRP HD1 H 7.11 . 1
336 . 32 TRP HE1 H 10.32 . 1
337 . 32 TRP HE3 H 7.33 . 1
338 . 32 TRP HZ2 H 7.43 . 1
339 . 32 TRP HZ3 H 6.97 . 1
340 . 32 TRP HH2 H 7.15 . 1
341 . 33 GLY N N 109.0 . 1
342 . 33 GLY H H 8.46 . 1
343 . 33 GLY C C 171.5 . 1
344 . 33 GLY CA C 44.8 . 1
345 . 33 GLY HA2 H 3.90 . 1
346 . 33 GLY HA3 H 4.99 . 1
347 . 34 SER N N 114.7 . 1
348 . 34 SER H H 7.91 . 1
349 . 34 SER C C 173.0 . 1
350 . 34 SER CA C 56.7 . 1
351 . 34 SER HA H 5.56 . 1
352 . 34 SER CB C 65.2 . 1
353 . 34 SER HB2 H 3.73 . 1
354 . 34 SER HB3 H 3.78 . 1
355 . 35 ILE N N 124.1 . 1
356 . 35 ILE H H 8.58 . 1
357 . 35 ILE C C 173.0 . 1
358 . 35 ILE CA C 60.3 . 1
359 . 35 ILE HA H 4.59 . 1
360 . 35 ILE CB C 41.1 . 1
361 . 35 ILE HB H 1.47 . 1
362 . 35 ILE HG12 H 1.30 . 1
363 . 35 ILE HG13 H 1.30 . 1
364 . 35 ILE HG2 H 0.65 . 1
365 . 35 ILE HD1 H 0.47 . 1
366 . 35 ILE CG1 C 18.9 . 1
367 . 35 ILE CG2 C 27.3 . 1
368 . 35 ILE CD1 C 14.5 . 1
369 . 36 LYS N N 125.1 . 1
370 . 36 LYS H H 9.11 . 1
371 . 36 LYS C C 175.5 . 1
372 . 36 LYS CA C 54.6 . 1
373 . 36 LYS HA H 5.33 . 1
374 . 36 LYS CB C 35.1 . 1
375 . 36 LYS HB2 H 1.85 . 1
376 . 36 LYS HB3 H 1.85 . 1
377 . 36 LYS HG2 H 1.38 . 1
378 . 36 LYS HG3 H 1.38 . 1
379 . 36 LYS HD2 H 1.63 . 1
380 . 36 LYS HD3 H 1.63 . 1
381 . 36 LYS HE2 H 2.93 . 1
382 . 36 LYS HE3 H 2.93 . 1
383 . 36 LYS CG C 24.4 . 1
384 . 36 LYS CD C 29.4 . 1
385 . 36 LYS CE C 42.0 . 1
386 . 37 GLY N N 106.7 . 1
387 . 37 GLY H H 8.25 . 1
388 . 37 GLY C C 174.9 . 1
389 . 37 GLY CA C 45.6 . 1
390 . 37 GLY HA2 H 3.84 . 1
391 . 37 GLY HA3 H 4.00 . 1
392 . 38 LEU N N 121.6 . 1
393 . 38 LEU H H 8.17 . 1
394 . 38 LEU C C 177.0 . 1
395 . 38 LEU CA C 53.5 . 1
396 . 38 LEU HA H 3.98 . 1
397 . 38 LEU CB C 44.3 . 1
398 . 38 LEU HB2 H 1.29 . 1
399 . 38 LEU HB3 H 0.55 . 1
400 . 38 LEU HG H 0.31 . 1
401 . 38 LEU HD1 H -0.02 . 1
402 . 38 LEU HD2 H -0.02 . 1
403 . 38 LEU CG C 26.4 . 1
404 . 38 LEU CD1 C 23.2 . 1
405 . 38 LEU CD2 C 23.2 . 1
406 . 39 THR N N 111.1 . 1
407 . 39 THR H H 8.50 . 1
408 . 39 THR C C 176.1 . 1
409 . 39 THR CA C 61.2 . 1
410 . 39 THR HA H 4.20 . 1
411 . 39 THR CB C 69.5 . 1
412 . 39 THR HB H 4.34 . 1
413 . 39 THR HG2 H 1.38 . 1
414 . 39 THR CG2 C 22.5 . 1
415 . 40 GLU N N 126.8 . 1
416 . 40 GLU H H 8.81 . 1
417 . 40 GLU C C 176.2 . 1
418 . 40 GLU CA C 57.7 . 1
419 . 40 GLU HA H 3.69 . 1
420 . 40 GLU CB C 30.2 . 1
421 . 40 GLU HB2 H 1.88 . 1
422 . 40 GLU HB3 H 2.11 . 1
423 . 40 GLU HG2 H 2.38 . 1
424 . 40 GLU HG3 H 2.38 . 1
425 . 40 GLU CG C 34.9 . 1
426 . 41 GLY N N 114.7 . 1
427 . 41 GLY H H 8.79 . 1
428 . 41 GLY C C 173.2 . 1
429 . 41 GLY CA C 43.3 . 1
430 . 41 GLY HA2 H 3.78 . 1
431 . 41 GLY HA3 H 4.68 . 1
432 . 42 LEU N N 121.1 . 1
433 . 42 LEU H H 8.30 . 1
434 . 42 LEU C C 177.4 . 1
435 . 42 LEU CA C 55.8 . 1
436 . 42 LEU HA H 4.81 . 1
437 . 42 LEU CB C 44.2 . 1
438 . 42 LEU HB2 H 1.63 . 1
439 . 42 LEU HB3 H 1.63 . 1
440 . 42 LEU HG H 1.04 . 1
441 . 42 LEU HD1 H 0.81 . 1
442 . 42 LEU HD2 H 0.85 . 1
443 . 42 LEU CG C 27.6 . 1
444 . 42 LEU CD1 C 25.1 . 1
445 . 42 LEU CD2 C 24.1 . 1
446 . 43 HIS N N 115.7 . 1
447 . 43 HIS H H 8.76 . 1
448 . 43 HIS C C 164.7 . 1
449 . 43 HIS CA C 54.3 . 1
450 . 43 HIS HA H 4.33 . 1
451 . 43 HIS CB C 31.6 . 1
452 . 43 HIS HB2 H 3.53 . 1
453 . 43 HIS HB3 H 2.57 . 1
454 . 43 HIS HD1 H 13.0 . 1
455 . 43 HIS HD2 H 7.08 . 1
456 . 43 HIS HE1 H 8.59 . 1
457 . 43 HIS HE2 H 14.1 . 1
458 . 44 GLY N N 110.5 . 1
459 . 44 GLY H H 8.96 . 1
460 . 44 GLY C C 171.8 . 1
461 . 44 GLY CA C 47.4 . 1
462 . 44 GLY HA2 H 3.21 . 1
463 . 44 GLY HA3 H 4.68 . 1
464 . 45 PHE N N 127.1 . 1
465 . 45 PHE H H 8.17 . 1
466 . 45 PHE C C 172.3 . 1
467 . 45 PHE CA C 56.0 . 1
468 . 45 PHE HA H 5.61 . 1
469 . 45 PHE CB C 42.6 . 1
470 . 45 PHE HB2 H 2.73 . 1
471 . 45 PHE HB3 H 2.93 . 1
472 . 45 PHE HE1 H 6.75 . 1
473 . 45 PHE HE2 H 6.75 . 1
474 . 45 PHE HZ H 7.09 . 1
475 . 46 HIS N N 116.8 . 1
476 . 46 HIS H H 8.25 . 1
477 . 46 HIS C C 175.2 . 1
478 . 46 HIS CA C 52.3 . 1
479 . 46 HIS HA H 5.65 . 1
480 . 46 HIS CB C 36.4 . 1
481 . 46 HIS HB2 H 2.73 . 1
482 . 46 HIS HB3 H 3.07 . 1
483 . 46 HIS HD2 H 7.08 . 1
484 . 46 HIS HE1 H 6.77 . 1
485 . 46 HIS HE2 H 13.4 . 1
486 . 46 HIS ND1 N 234.6 . 1
487 . 46 HIS NE2 N 178.0 . 1
488 . 47 VAL N N 121.1 . 1
489 . 47 VAL H H 9.41 . 1
490 . 47 VAL C C 176.8 . 1
491 . 47 VAL CA C 62.2 . 1
492 . 47 VAL HA H 4.62 . 1
493 . 47 VAL CB C 32.4 . 1
494 . 47 VAL HB H 2.05 . 1
495 . 47 VAL HG1 H 0.87 . 1
496 . 47 VAL HG2 H 0.85 . 1
497 . 47 VAL CG1 C 22.2 . 1
498 . 47 VAL CG2 C 20.8 . 1
499 . 48 HIS N N 130.3 . 1
500 . 48 HIS H H 10.34 . 1
501 . 48 HIS C C 174.8 . 1
502 . 48 HIS CA C 56.2 . 1
503 . 48 HIS HA H 5.00 . 1
504 . 48 HIS CB C 30.6 . 1
505 . 48 HIS HB2 H 2.86 . 1
506 . 48 HIS HB3 H 3.45 . 1
507 . 48 HIS HD1 H 12.4 . 1
508 . 48 HIS HD2 H 7.01 . 1
509 . 48 HIS HE1 H 8.57 . 1
510 . 48 HIS ND1 N 171.0 . 1
511 . 48 HIS NE2 N 215.0 . 1
512 . 49 GLU N N 118.4 . 1
513 . 49 GLU H H 8.59 . 1
514 . 49 GLU C C 174.8 . 1
515 . 49 GLU CA C 60.1 . 1
516 . 49 GLU HA H 3.83 . 1
517 . 49 GLU CB C 32.4 . 1
518 . 49 GLU HB2 H 2.12 . 1
519 . 49 GLU HB3 H 2.12 . 1
520 . 49 GLU HG2 H 2.32 . 1
521 . 49 GLU HG3 H 2.32 . 1
522 . 49 GLU CG C 35.9 . 1
523 . 50 GLU C C 175.5 . 1
524 . 50 GLU CA C 55.4 . 1
525 . 50 GLU HA H 4.49 . 1
526 . 50 GLU CB C 30.8 . 1
527 . 50 GLU HB2 H 2.12 . 1
528 . 50 GLU HB3 H 1.94 . 1
529 . 50 GLU HG2 H 2.32 . 2
530 . 50 GLU HG3 H 2.40 . 2
531 . 50 GLU CG C 35.8 . 1
532 . 51 GLU N N 123.8 . 1
533 . 51 GLU H H 8.71 . 1
534 . 51 GLU C C 174.5 . 1
535 . 51 GLU CA C 56.4 . 1
536 . 51 GLU HA H 3.82 . 1
537 . 51 GLU CB C 23.3 . 1
538 . 51 GLU HB2 H 1.99 . 1
539 . 51 GLU HB3 H 1.99 . 1
540 . 51 GLU HG2 H 2.24 . 1
541 . 51 GLU HG3 H 2.24 . 1
542 . 51 GLU CG C 33.3 . 1
543 . 52 ASP C C 174.5 . 1
544 . 52 ASP CA C 53.8 . 1
545 . 52 ASP HA H 4.59 . 1
546 . 52 ASP CB C 41.9 . 1
547 . 52 ASP HB2 H 2.74 . 1
548 . 52 ASP HB3 H 2.06 . 1
549 . 53 ASN N N 121.9 . 1
550 . 53 ASN H H 8.54 . 1
551 . 53 ASN C C 176.4 . 1
552 . 53 ASN CA C 53.0 . 1
553 . 53 ASN HA H 4.90 . 1
554 . 53 ASN CB C 39.4 . 1
555 . 53 ASN HB2 H 2.64 . 1
556 . 53 ASN HB3 H 2.88 . 1
557 . 53 ASN HD21 H 7.16 . 2
558 . 53 ASN HD22 H 7.51 . 2
559 . 53 ASN ND2 N 114.1 . 1
560 . 54 THR N N 115.5 . 1
561 . 54 THR H H 8.82 . 1
562 . 54 THR C C 175.7 . 1
563 . 54 THR CA C 62.2 . 1
564 . 54 THR HA H 4.32 . 1
565 . 54 THR CB C 71.0 . 1
566 . 54 THR HB H 4.38 . 1
567 . 54 THR HG2 H 1.29 . 1
568 . 54 THR CG2 C 22.0 . 1
569 . 55 ALA N N 124.3 . 1
570 . 55 ALA H H 8.58 . 1
571 . 55 ALA C C 178.1 . 1
572 . 55 ALA CA C 53.8 . 1
573 . 55 ALA HA H 4.15 . 1
574 . 55 ALA CB C 18.4 . 1
575 . 55 ALA HB H 1.34 . 1
576 . 56 GLY N N 103.4 . 1
577 . 56 GLY H H 8.13 . 1
578 . 56 GLY C C 175.0 . 1
579 . 56 GLY CA C 45.3 . 1
580 . 56 GLY HA2 H 4.06 . 1
581 . 56 GLY HA3 H 3.84 . 1
582 . 59 SER C C 174.4 . 1
583 . 59 SER CA C 58.5 . 1
584 . 59 SER HA H 4.66 . 1
585 . 59 SER CB C 63.8 . 1
586 . 59 SER HB2 H 3.94 . 1
587 . 59 SER HB3 H 3.66 . 1
588 . 60 ALA N N 122.0 . 1
589 . 60 ALA H H 7.40 . 1
590 . 60 ALA C C 176.6 . 1
591 . 60 ALA CA C 54.2 . 1
592 . 60 ALA HA H 4.00 . 1
593 . 60 ALA CB C 18.5 . 1
594 . 60 ALA HB H 1.25 . 1
595 . 61 GLY N N 105.3 . 1
596 . 61 GLY H H 8.23 . 1
597 . 61 GLY CA C 44.8 . 1
598 . 61 GLY HA2 H 4.01 . 1
599 . 61 GLY HA3 H 4.33 . 1
600 . 62 PRO C C 175.5 . 1
601 . 62 PRO CA C 62.3 . 1
602 . 62 PRO HA H 4.82 . 1
603 . 62 PRO CB C 32.2 . 1
604 . 62 PRO HB2 H 2.16 . 1
605 . 62 PRO HB3 H 1.87 . 1
606 . 62 PRO HG2 H 2.06 . 1
607 . 62 PRO HG3 H 2.06 . 1
608 . 62 PRO CG C 26.7 . 1
609 . 62 PRO CD C 34.0 . 1
610 . 63 HIS N N 116.3 . 1
611 . 63 HIS H H 7.71 . 1
612 . 63 HIS C C 175.0 . 1
613 . 63 HIS CA C 54.8 . 1
614 . 63 HIS HA H 3.95 . 1
615 . 63 HIS CB C 30.6 . 1
616 . 63 HIS HB2 H 2.61 . 1
617 . 63 HIS HB3 H 2.47 . 1
618 . 63 HIS HD2 H 5.79 . 1
619 . 63 HIS HE1 H 6.47 . 1
620 . 63 HIS HE2 H 12.6 . 1
621 . 63 HIS ND1 N 210.0 . 1
622 . 63 HIS NE2 N 171.0 . 1
623 . 64 PHE N N 122.6 . 1
624 . 64 PHE H H 9.58 . 1
625 . 64 PHE C C 175.3 . 1
626 . 64 PHE CA C 57.8 . 1
627 . 64 PHE HA H 4.52 . 1
628 . 64 PHE CB C 38.7 . 1
629 . 64 PHE HB2 H 2.68 . 1
630 . 64 PHE HB3 H 2.45 . 1
631 . 65 ASN N N 127.9 . 1
632 . 65 ASN H H 9.42 . 1
633 . 65 ASN C C 172.9 . 1
634 . 65 ASN CA C 51.2 . 1
635 . 65 ASN HA H 5.17 . 1
636 . 65 ASN CB C 39.9 . 1
637 . 65 ASN HB2 H 2.84 . 1
638 . 65 ASN HB3 H 1.74 . 1
639 . 65 ASN HD21 H 7.78 . 2
640 . 65 ASN HD22 H 8.02 . 2
641 . 65 ASN ND2 N 114.1 . 1
642 . 66 PRO C C 177.1 . 1
643 . 66 PRO CA C 64.5 . 1
644 . 66 PRO HA H 4.34 . 1
645 . 66 PRO CB C 30.7 . 1
646 . 66 PRO HB2 H 1.73 . 1
647 . 66 PRO HB3 H 1.73 . 1
648 . 66 PRO HG2 H 1.18 . 1
649 . 66 PRO HG3 H 1.18 . 1
650 . 66 PRO HD2 H 2.09 . 1
651 . 66 PRO HD3 H 2.09 . 1
652 . 66 PRO CG C 27.5 . 1
653 . 66 PRO CD C 48.1 . 1
654 . 67 LEU N N 117.6 . 1
655 . 67 LEU H H 7.64 . 1
656 . 67 LEU C C 175.8 . 1
657 . 67 LEU CA C 54.2 . 1
658 . 67 LEU HA H 4.46 . 1
659 . 67 LEU CB C 40.5 . 1
660 . 67 LEU HB2 H 1.73 . 1
661 . 67 LEU HB3 H 1.68 . 1
662 . 67 LEU HG H 1.25 . 1
663 . 67 LEU HD1 H 0.82 . 1
664 . 67 LEU HD2 H 0.82 . 1
665 . 67 LEU CG C 27.3 . 1
666 . 67 LEU CD1 C 24.7 . 1
667 . 67 LEU CD2 C 22.4 . 1
668 . 68 SER N N 113.1 . 1
669 . 68 SER H H 7.50 . 1
670 . 68 SER C C 174.0 . 1
671 . 68 SER CA C 59.2 . 1
672 . 68 SER HA H 3.92 . 1
673 . 68 SER CB C 60.4 . 1
674 . 68 SER HB2 H 4.04 . 1
675 . 68 SER HB3 H 4.04 . 1
676 . 69 ARG N N 121.1 . 1
677 . 69 ARG H H 8.58 . 1
678 . 69 ARG C C 176.6 . 1
679 . 69 ARG CA C 53.9 . 1
680 . 69 ARG HA H 4.63 . 1
681 . 69 ARG CB C 32.7 . 1
682 . 69 ARG HB2 H 1.80 . 1
683 . 69 ARG HB3 H 1.98 . 1
684 . 69 ARG HG2 H 1.49 . 2
685 . 69 ARG HG3 H 1.55 . 2
686 . 69 ARG HD2 H 3.24 . 1
687 . 69 ARG HD3 H 3.24 . 1
688 . 69 ARG CG C 27.7 . 1
689 . 69 ARG CD C 42.6 . 1
690 . 70 LYS N N 119.3 . 1
691 . 70 LYS H H 8.82 . 1
692 . 70 LYS C C 173.1 . 1
693 . 70 LYS CA C 56.0 . 1
694 . 70 LYS HA H 4.45 . 1
695 . 70 LYS CB C 33.4 . 1
696 . 70 LYS HB2 H 1.90 . 1
697 . 70 LYS HB3 H 1.67 . 1
698 . 70 LYS HG2 H 1.51 . 2
699 . 70 LYS HG3 H 1.57 . 2
700 . 70 LYS HD2 H 1.66 . 1
701 . 70 LYS HD3 H 1.66 . 1
702 . 70 LYS HE2 H 3.00 . 1
703 . 70 LYS HE3 H 3.00 . 1
704 . 70 LYS CG C 25.5 . 1
705 . 70 LYS CD C 29.4 . 1
706 . 70 LYS CE C 41.9 . 1
707 . 71 HIS N N 113.1 . 1
708 . 71 HIS H H 7.14 . 1
709 . 71 HIS C C 174.5 . 1
710 . 71 HIS CA C 56.0 . 1
711 . 71 HIS HA H 2.88 . 1
712 . 71 HIS CB C 31.4 . 1
713 . 71 HIS HB2 H 2.32 . 1
714 . 71 HIS HB3 H 2.69 . 1
715 . 71 HIS HD2 H 6.80 . 1
716 . 71 HIS HE1 H 7.74 . 1
717 . 71 HIS HE2 H 15.3 . 1
718 . 71 HIS ND1 N 208.6 . 1
719 . 71 HIS NE2 N 17.0 . 1
720 . 72 GLY N N 114.0 . 1
721 . 72 GLY H H 7.29 . 1
722 . 72 GLY C C 171.8 . 1
723 . 72 GLY CA C 44.7 . 1
724 . 72 GLY HA2 H 4.01 . 1
725 . 72 GLY HA3 H 3.86 . 1
726 . 73 GLY N N 106.3 . 1
727 . 73 GLY H H 8.83 . 1
728 . 73 GLY C C 172.7 . 1
729 . 73 GLY CA C 40.3 . 1
730 . 73 GLY HA2 H 3.75 . 1
731 . 73 GLY HA3 H 4.40 . 1
732 . 74 PRO C C 178.8 . 1
733 . 74 PRO CA C 63.8 . 1
734 . 74 PRO HA H 4.46 . 1
735 . 74 PRO CB C 31.0 . 1
736 . 74 PRO HB2 H 2.55 . 1
737 . 74 PRO HB3 H 2.13 . 1
738 . 74 PRO HG2 H 2.04 . 1
739 . 74 PRO HG3 H 2.04 . 1
740 . 74 PRO HD2 H 3.19 . 2
741 . 74 PRO HD3 H 3.78 . 2
742 . 74 PRO CG C 27.4 . 1
743 . 74 PRO CD C 48.6 . 1
744 . 75 LYS N N 116.0 . 1
745 . 75 LYS H H 8.65 . 1
746 . 75 LYS C C 176.8 . 1
747 . 75 LYS CA C 55.0 . 1
748 . 75 LYS HA H 4.38 . 1
749 . 75 LYS CB C 31.3 . 1
750 . 75 LYS HB2 H 2.03 . 1
751 . 75 LYS HB3 H 1.78 . 1
752 . 75 LYS HG2 H 1.43 . 1
753 . 75 LYS HG3 H 1.55 . 1
754 . 75 LYS HD2 H 1.70 . 1
755 . 75 LYS HD3 H 1.70 . 1
756 . 75 LYS HE2 H 3.07 . 1
757 . 75 LYS HE3 H 3.07 . 1
758 . 75 LYS CG C 24.8 . 1
759 . 75 LYS CD C 28.3 . 1
760 . 75 LYS CE C 42.2 . 1
761 . 76 ASP N N 121.5 . 1
762 . 76 ASP H H 7.52 . 1
763 . 76 ASP C C 175.8 . 1
764 . 76 ASP CA C 54.6 . 1
765 . 76 ASP HA H 4.52 . 1
766 . 76 ASP CB C 41.9 . 1
767 . 76 ASP HB2 H 2.66 . 1
768 . 76 ASP HB3 H 2.61 . 1
769 . 77 GLU N N 121.4 . 1
770 . 77 GLU H H 8.30 . 1
771 . 77 GLU C C 177.2 . 1
772 . 77 GLU CA C 58.7 . 1
773 . 77 GLU HA H 3.95 . 1
774 . 77 GLU CB C 29.7 . 1
775 . 77 GLU HB2 H 2.02 . 1
776 . 77 GLU HB3 H 2.02 . 1
777 . 77 GLU HG2 H 2.31 . 1
778 . 77 GLU HG3 H 2.37 . 1
779 . 77 GLU CG C 36.2 . 1
780 . 78 GLU N N 120.3 . 1
781 . 78 GLU H H 8.10 . 1
782 . 78 GLU C C 171.5 . 1
783 . 78 GLU CA C 55.3 . 1
784 . 78 GLU HA H 4.15 . 1
785 . 78 GLU CB C 27.8 . 1
786 . 78 GLU HB2 H 1.97 . 1
787 . 78 GLU HB3 H 1.97 . 1
788 . 78 GLU HG2 H 1.90 . 1
789 . 78 GLU HG3 H 2.26 . 1
790 . 78 GLU CG C 35.9 . 1
791 . 79 ARG N N 119.8 . 1
792 . 79 ARG H H 7.04 . 1
793 . 79 ARG C C 175.4 . 1
794 . 79 ARG CA C 54.6 . 1
795 . 79 ARG HA H 4.67 . 1
796 . 79 ARG CB C 32.1 . 1
797 . 79 ARG HB2 H 1.70 . 1
798 . 79 ARG HB3 H 1.70 . 1
799 . 79 ARG HG2 H 1.89 . 1
800 . 79 ARG HG3 H 1.89 . 1
801 . 79 ARG HD2 H 3.38 . 1
802 . 79 ARG HD3 H 3.38 . 1
803 . 79 ARG CG C 23.8 . 1
804 . 79 ARG CD C 44.3 . 1
805 . 80 HIS N N 119.2 . 1
806 . 80 HIS H H 8.38 . 1
807 . 80 HIS C C 179.0 . 1
808 . 80 HIS CA C 53.8 . 1
809 . 80 HIS HA H 4.56 . 1
810 . 80 HIS CB C 29.0 . 1
811 . 80 HIS HB2 H 3.26 . 1
812 . 80 HIS HB3 H 2.89 . 1
813 . 80 HIS HD2 H 6.85 . 1
814 . 80 HIS HE1 H 8.49 . 1
815 . 80 HIS HE2 H 12.8 . 1
816 . 80 HIS ND1 N 201.0 . 1
817 . 80 HIS NE2 N 177.0 . 1
818 . 81 VAL N N 129.8 . 1
819 . 81 VAL H H 8.10 . 1
820 . 81 VAL C C 176.7 . 1
821 . 81 VAL CA C 61.4 . 1
822 . 81 VAL HA H 3.50 . 1
823 . 81 VAL HB H 2.87 . 1
824 . 81 VAL HG1 H 0.57 . 1
825 . 81 VAL HG2 H 1.21 . 1
826 . 82 GLY N N 98.6 . 1
827 . 82 GLY H H 8.53 . 1
828 . 82 GLY C C 173.5 . 1
829 . 82 GLY CA C 46.2 . 1
830 . 82 GLY HA2 H 4.12 . 1
831 . 82 GLY HA3 H 4.48 . 1
832 . 83 ASP N N 122.2 . 1
833 . 83 ASP H H 7.19 . 1
834 . 83 ASP C C 172.2 . 1
835 . 83 ASP CA C 55.9 . 1
836 . 83 ASP HA H 4.90 . 1
837 . 83 ASP CB C 39.4 . 1
838 . 83 ASP HB2 H 2.96 . 1
839 . 83 ASP HB3 H 2.84 . 1
840 . 84 LEU N N 121.1 . 1
841 . 84 LEU H H 7.21 . 1
842 . 84 LEU C C 176.5 . 1
843 . 84 LEU CA C 53.8 . 1
844 . 84 LEU HA H 4.65 . 1
845 . 84 LEU CB C 41.7 . 1
846 . 84 LEU HB2 H 1.81 . 1
847 . 84 LEU HB3 H 1.81 . 1
848 . 84 LEU HG H 1.61 . 1
849 . 84 LEU HD1 H 0.86 . 1
850 . 84 LEU HD2 H 0.59 . 1
851 . 84 LEU CG C 25.5 . 1
852 . 84 LEU CD1 C 22.0 . 1
853 . 84 LEU CD2 C 22.0 . 1
854 . 85 GLY N N 108.3 . 1
855 . 85 GLY H H 8.31 . 1
856 . 85 GLY C C 170.9 . 1
857 . 85 GLY CA C 46.6 . 1
858 . 85 GLY HA2 H 3.65 . 1
859 . 85 GLY HA3 H 3.99 . 1
860 . 86 ASN N N 118.2 . 1
861 . 86 ASN H H 8.07 . 1
862 . 86 ASN C C 177.2 . 1
863 . 86 ASN CA C 52.3 . 1
864 . 86 ASN HA H 5.81 . 1
865 . 86 ASN CB C 44.2 . 1
866 . 86 ASN HB2 H 2.28 . 1
867 . 86 ASN HB3 H 2.54 . 1
868 . 87 VAL N N 114.8 . 1
869 . 87 VAL H H 9.03 . 1
870 . 87 VAL C C 174.7 . 1
871 . 87 VAL CA C 59.1 . 1
872 . 87 VAL HA H 4.57 . 1
873 . 87 VAL CB C 32.0 . 1
874 . 87 VAL HB H 1.79 . 1
875 . 87 VAL HG1 H 0.44 . 1
876 . 87 VAL HG2 H -0.02 . 1
877 . 87 VAL CG1 C 21.3 . 1
878 . 87 VAL CG2 C 17.8 . 1
879 . 88 THR N N 118.9 . 1
880 . 88 THR H H 8.70 . 1
881 . 88 THR C C 173.5 . 1
882 . 88 THR CA C 62.0 . 1
883 . 88 THR HA H 4.63 . 1
884 . 88 THR CB C 69.6 . 1
885 . 88 THR HB H 3.94 . 1
886 . 88 THR HG2 H 1.03 . 1
887 . 88 THR CG2 C 21.4 . 1
888 . 89 ALA N N 129.9 . 1
889 . 89 ALA H H 9.38 . 1
890 . 89 ALA C C 177.5 . 1
891 . 89 ALA CA C 49.7 . 1
892 . 89 ALA HA H 4.62 . 1
893 . 89 ALA CB C 20.9 . 1
894 . 89 ALA HB H 1.28 . 1
895 . 90 ASP N N 125.5 . 1
896 . 90 ASP H H 8.50 . 1
897 . 90 ASP C C 177.1 . 1
898 . 90 ASP CA C 52.8 . 1
899 . 90 ASP HA H 4.54 . 1
900 . 90 ASP CB C 41.6 . 1
901 . 90 ASP HB2 H 3.35 . 1
902 . 90 ASP HB3 H 2.85 . 1
903 . 91 LYS N N 115.5 . 1
904 . 91 LYS H H 8.20 . 1
905 . 91 LYS C C 177.4 . 1
906 . 91 LYS CA C 58.5 . 1
907 . 91 LYS HA H 3.94 . 1
908 . 91 LYS CB C 31.6 . 1
909 . 91 LYS HB2 H 1.87 . 1
910 . 91 LYS HB3 H 1.83 . 1
911 . 91 LYS HG2 H 1.38 . 2
912 . 91 LYS HG3 H 1.44 . 2
913 . 91 LYS HD2 H 1.68 . 1
914 . 91 LYS HD3 H 1.68 . 1
915 . 91 LYS HE2 H 3.04 . 1
916 . 91 LYS HE3 H 3.04 . 1
917 . 91 LYS CG C 23.7 . 1
918 . 91 LYS CD C 29.1 . 1
919 . 91 LYS CE C 42.1 . 1
920 . 92 ASP N N 120.5 . 1
921 . 92 ASP H H 8.20 . 1
922 . 92 ASP C C 176.3 . 1
923 . 92 ASP CA C 54.3 . 1
924 . 92 ASP HA H 4.76 . 1
925 . 92 ASP CB C 41.2 . 1
926 . 92 ASP HB2 H 2.89 . 1
927 . 92 ASP HB3 H 2.82 . 1
928 . 93 GLY N N 112.0 . 1
929 . 93 GLY H H 8.43 . 1
930 . 93 GLY C C 172.9 . 1
931 . 93 GLY CA C 46.9 . 1
932 . 93 GLY HA2 H 3.93 . 1
933 . 93 GLY HA3 H 4.17 . 1
934 . 94 VAL N N 119.5 . 1
935 . 94 VAL H H 7.94 . 1
936 . 94 VAL C C 176.6 . 1
937 . 94 VAL CA C 61.5 . 1
938 . 94 VAL HA H 4.69 . 1
939 . 94 VAL CB C 32.6 . 1
940 . 94 VAL HB H 2.20 . 1
941 . 94 VAL HG1 H 0.75 . 1
942 . 94 VAL HG2 H 0.86 . 1
943 . 94 VAL CG1 C 21.4 . 1
944 . 94 VAL CG2 C 21.4 . 1
945 . 95 ALA N N 132.2 . 1
946 . 95 ALA H H 9.75 . 1
947 . 95 ALA C C 174.9 . 1
948 . 95 ALA CA C 50.2 . 1
949 . 95 ALA HA H 5.15 . 1
950 . 95 ALA CB C 20.2 . 1
951 . 95 ALA HB H 0.78 . 1
952 . 96 ASP N N 126.3 . 1
953 . 96 ASP H H 8.56 . 1
954 . 96 ASP C C 175.8 . 1
955 . 96 ASP CA C 54.0 . 1
956 . 96 ASP HA H 5.00 . 1
957 . 96 ASP CB C 41.2 . 1
958 . 96 ASP HB2 H 2.68 . 1
959 . 96 ASP HB3 H 2.52 . 1
960 . 97 VAL N N 126.8 . 1
961 . 97 VAL H H 8.71 . 1
962 . 97 VAL C C 176.5 . 1
963 . 97 VAL CA C 62.2 . 1
964 . 97 VAL HA H 4.07 . 1
965 . 97 VAL CB C 32.9 . 1
966 . 97 VAL HB H 1.60 . 1
967 . 97 VAL HG1 H 0.71 . 1
968 . 97 VAL HG2 H 0.48 . 1
969 . 97 VAL CG1 C 20.70 . 1
970 . 97 VAL CG2 C 21.20 . 1
971 . 98 SER N N 124.2 . 1
972 . 98 SER H H 8.80 . 1
973 . 98 SER C C 173.1 . 1
974 . 98 SER CA C 58.0 . 1
975 . 98 SER HA H 5.17 . 1
976 . 98 SER CB C 62.3 . 1
977 . 98 SER HB2 H 3.92 . 1
978 . 98 SER HB3 H 3.86 . 1
979 . 99 ILE N N 126.9 . 1
980 . 99 ILE H H 9.44 . 1
981 . 99 ILE C C 174.3 . 1
982 . 99 ILE CA C 60.2 . 1
983 . 99 ILE HA H 4.69 . 1
984 . 99 ILE CB C 44.2 . 1
985 . 99 ILE HB H 1.80 . 1
986 . 99 ILE HG12 H 1.21 . 1
987 . 99 ILE HG13 H 1.51 . 1
988 . 99 ILE HG2 H 1.03 . 1
989 . 99 ILE HD1 H 1.03 . 1
990 . 99 ILE CG1 C 27.4 . 1
991 . 99 ILE CG2 C 17.4 . 1
992 . 99 ILE CD1 C 14.9 . 1
993 . 100 GLU N N 125.2 . 1
994 . 100 GLU H H 8.63 . 1
995 . 100 GLU C C 175.4 . 1
996 . 100 GLU CA C 55.5 . 1
997 . 100 GLU HA H 5.42 . 1
998 . 100 GLU CB C 32.4 . 1
999 . 100 GLU HB2 H 2.02 . 1
1000 . 100 GLU HB3 H 1.97 . 1
1001 . 100 GLU HG2 H 2.13 . 1
1002 . 100 GLU HG3 H 2.13 . 1
1003 . 100 GLU CG C 37.4 . 1
1004 . 101 ASP N N 127.2 . 1
1005 . 101 ASP H H 9.31 . 1
1006 . 101 ASP C C 174.5 . 1
1007 . 101 ASP CA C 54.7 . 1
1008 . 101 ASP HA H 5.13 . 1
1009 . 101 ASP CB C 47.1 . 1
1010 . 101 ASP HB2 H 2.58 . 1
1011 . 101 ASP HB3 H 2.37 . 1
1012 . 102 SER N N 119.3 . 1
1013 . 102 SER H H 8.98 . 1
1014 . 102 SER C C 172.8 . 1
1015 . 102 SER CA C 58.4 . 1
1016 . 102 SER HA H 4.82 . 1
1017 . 102 SER CB C 63.8 . 1
1018 . 102 SER HB2 H 4.09 . 1
1019 . 102 SER HB3 H 3.94 . 1
1020 . 103 VAL N N 124.2 . 1
1021 . 103 VAL H H 8.17 . 1
1022 . 103 VAL C C 178.4 . 1
1023 . 103 VAL CA C 64.1 . 1
1024 . 103 VAL HA H 4.06 . 1
1025 . 103 VAL CB C 32.0 . 1
1026 . 103 VAL HB H 2.44 . 1
1027 . 103 VAL HG1 H 0.96 . 1
1028 . 103 VAL HG2 H 0.96 . 1
1029 . 103 VAL CG1 C 22.9 . 1
1030 . 103 VAL CG2 C 22.9 . 1
1031 . 104 ILE N N 112.5 . 1
1032 . 104 ILE H H 8.08 . 1
1033 . 104 ILE C C 172.7 . 1
1034 . 104 ILE CA C 62.9 . 1
1035 . 104 ILE HA H 4.14 . 1
1036 . 104 ILE CB C 39.8 . 1
1037 . 104 ILE HB H 1.85 . 1
1038 . 104 ILE HG12 H 1.33 . 1
1039 . 104 ILE HG13 H 1.33 . 1
1040 . 104 ILE HG2 H 0.89 . 1
1041 . 104 ILE HD1 H 1.03 . 1
1042 . 104 ILE CG1 C 24.0 . 1
1043 . 104 ILE CG2 C 21.7 . 1
1044 . 104 ILE CD1 C 19.1 . 1
1045 . 105 SER N N 109.0 . 1
1046 . 105 SER H H 7.32 . 1
1047 . 105 SER C C 173.2 . 1
1048 . 105 SER CA C 55.8 . 1
1049 . 105 SER HA H 4.52 . 1
1050 . 105 SER CB C 65.3 . 1
1051 . 105 SER HB2 H 3.84 . 1
1052 . 105 SER HB3 H 3.55 . 1
1053 . 106 LEU N N 121.7 . 1
1054 . 106 LEU H H 8.32 . 1
1055 . 106 LEU C C 174.9 . 1
1056 . 106 LEU CA C 54.0 . 1
1057 . 106 LEU HA H 4.58 . 1
1058 . 106 LEU CB C 40.1 . 1
1059 . 106 LEU HB2 H 1.87 . 1
1060 . 106 LEU HB3 H 1.60 . 1
1061 . 106 LEU HG H 1.48 . 1
1062 . 106 LEU HD1 H 0.72 . 1
1063 . 106 LEU HD2 H 0.43 . 1
1064 . 106 LEU CG C 26.2 . 1
1065 . 106 LEU CD1 C 14.5 . 1
1066 . 107 SER N N 111.5 . 1
1067 . 107 SER H H 8.16 . 1
1068 . 107 SER C C 173.8 . 1
1069 . 107 SER CA C 57.8 . 1
1070 . 107 SER HA H 4.64 . 1
1071 . 107 SER CB C 65.4 . 1
1072 . 107 SER HB2 H 3.85 . 1
1073 . 107 SER HB3 H 3.85 . 1
1074 . 107 SER HG H 5.70 . 1
1075 . 108 GLY N N 108.3 . 1
1076 . 108 GLY H H 8.68 . 1
1077 . 108 GLY C C 175.8 . 1
1078 . 108 GLY CA C 44.8 . 1
1079 . 108 GLY HA2 H 4.26 . 1
1080 . 108 GLY HA3 H 3.89 . 1
1081 . 109 ASP N N 121.1 . 1
1082 . 109 ASP H H 8.70 . 1
1083 . 109 ASP C C 178.1 . 1
1084 . 109 ASP CA C 57.0 . 1
1085 . 109 ASP HA H 4.34 . 1
1086 . 109 ASP CB C 40.0 . 1
1087 . 109 ASP HB2 H 2.63 . 1
1088 . 109 ASP HB3 H 2.57 . 1
1089 . 110 HIS N N 118.4 . 1
1090 . 110 HIS H H 9.16 . 1
1091 . 110 HIS C C 173.1 . 1
1092 . 110 HIS CA C 53.2 . 1
1093 . 110 HIS HA H 5.00 . 1
1094 . 110 HIS CB C 28.4 . 1
1095 . 110 HIS HB2 H 3.53 . 1
1096 . 110 HIS HB3 H 3.28 . 1
1097 . 111 SER N N 111.0 . 1
1098 . 111 SER H H 7.11 . 1
1099 . 111 SER C C 177.0 . 1
1100 . 111 SER CA C 57.4 . 1
1101 . 111 SER HA H 3.94 . 1
1102 . 111 SER CB C 64.1 . 1
1103 . 111 SER HB2 H 3.71 . 1
1104 . 111 SER HB3 H 3.61 . 1
1105 . 112 ILE N N 116.7 . 1
1106 . 112 ILE H H 7.85 . 1
1107 . 112 ILE C C 174.9 . 1
1108 . 112 ILE CA C 60.8 . 1
1109 . 112 ILE HA H 3.79 . 1
1110 . 112 ILE CB C 36.6 . 1
1111 . 112 ILE HB H 1.98 . 1
1112 . 112 ILE HG12 H 0.68 . 2
1113 . 112 ILE HG13 H 1.25 . 2
1114 . 112 ILE HD1 H 0.29 . 1
1115 . 112 ILE CG1 C 24.1 . 1
1116 . 112 ILE CG2 C 17.4 . 1
1117 . 112 ILE CD1 C 14.9 . 1
1118 . 113 ILE N N 122.2 . 1
1119 . 113 ILE H H 7.77 . 1
1120 . 113 ILE C C 177.5 . 1
1121 . 113 ILE CA C 61.8 . 1
1122 . 113 ILE HA H 3.25 . 1
1123 . 113 ILE CB C 34.5 . 1
1124 . 113 ILE HB H 1.75 . 1
1125 . 113 ILE HG12 H 1.15 . 2
1126 . 113 ILE HG13 H 1.38 . 2
1127 . 113 ILE HG2 H 0.90 . 1
1128 . 113 ILE HD1 H 0.59 . 1
1129 . 113 ILE CG1 C 27.4 . 1
1130 . 113 ILE CG2 C 17.5 . 1
1131 . 113 ILE CD1 C 11.2 . 1
1132 . 114 GLY N N 117.3 . 1
1133 . 114 GLY H H 9.21 . 1
1134 . 114 GLY C C 173.2 . 1
1135 . 114 GLY CA C 45.0 . 1
1136 . 114 GLY HA2 H 3.47 . 1
1137 . 114 GLY HA3 H 4.20 . 1
1138 . 115 ARG N N 118.4 . 1
1139 . 115 ARG H H 7.43 . 1
1140 . 115 ARG C C 174.5 . 1
1141 . 115 ARG CA C 54.1 . 1
1142 . 115 ARG HA H 4.31 . 1
1143 . 115 ARG CB C 28.4 . 1
1144 . 115 ARG HB2 H 1.35 . 1
1145 . 115 ARG HB3 H 1.35 . 1
1146 . 115 ARG HG2 H 0.73 . 1
1147 . 115 ARG HG3 H 0.99 . 1
1148 . 115 ARG HD2 H 2.08 . 1
1149 . 115 ARG HD3 H 2.44 . 1
1150 . 115 ARG CG C 28.7 . 1
1151 . 115 ARG CD C 42.4 . 1
1152 . 116 THR N N 113.7 . 1
1153 . 116 THR H H 6.98 . 1
1154 . 116 THR C C 173.1 . 1
1155 . 116 THR CA C 63.0 . 1
1156 . 116 THR HA H 4.82 . 1
1157 . 116 THR CB C 70.5 . 1
1158 . 116 THR HB H 3.70 . 1
1159 . 116 THR HG2 H 1.03 . 1
1160 . 116 THR CG2 C 22.4 . 1
1161 . 117 LEU N N 132.3 . 1
1162 . 117 LEU H H 9.23 . 1
1163 . 117 LEU C C 174.7 . 1
1164 . 117 LEU CA C 53.8 . 1
1165 . 117 LEU HA H 4.80 . 1
1166 . 117 LEU CB C 44.1 . 1
1167 . 117 LEU HB2 H 1.81 . 1
1168 . 117 LEU HB3 H 1.22 . 1
1169 . 117 LEU HG H 1.02 . 1
1170 . 117 LEU HD1 H 0.83 . 1
1171 . 117 LEU HD2 H 0.18 . 1
1172 . 117 LEU CG C 27.1 . 1
1173 . 117 LEU CD1 C 20.5 . 1
1174 . 117 LEU CD2 C 20.5 . 1
1175 . 118 VAL N N 125.7 . 1
1176 . 118 VAL H H 8.95 . 1
1177 . 118 VAL C C 173.8 . 1
1178 . 118 VAL CA C 61.4 . 1
1179 . 118 VAL HA H 4.68 . 1
1180 . 118 VAL CB C 35.8 . 1
1181 . 118 VAL HB H 2.10 . 1
1182 . 118 VAL HG1 H 0.28 . 1
1183 . 118 VAL HG2 H 0.30 . 1
1184 . 118 VAL CG1 C 21.6 . 1
1185 . 118 VAL CG2 C 21.6 . 1
1186 . 119 VAL N N 121.9 . 1
1187 . 119 VAL H H 8.04 . 1
1188 . 119 VAL C C 174.6 . 1
1189 . 119 VAL CA C 58.4 . 1
1190 . 119 VAL HA H 5.71 . 1
1191 . 119 VAL CB C 35.4 . 1
1192 . 119 VAL HB H 1.82 . 1
1193 . 119 VAL HG1 H 1.02 . 1
1194 . 119 VAL HG2 H 0.84 . 1
1195 . 119 VAL CG1 C 22.3 . 1
1196 . 119 VAL CG2 C 22.3 . 1
1197 . 120 HIS N N 126.3 . 1
1198 . 120 HIS H H 8.93 . 1
1199 . 120 HIS C C 176.0 . 1
1200 . 120 HIS CA C 56.7 . 1
1201 . 120 HIS HA H 5.33 . 1
1202 . 120 HIS CB C 33.4 . 1
1203 . 120 HIS HB2 H 4.14 . 1
1204 . 120 HIS HB3 H 3.00 . 1
1205 . 120 HIS HD1 H 10.4 . 1
1206 . 120 HIS HD2 H 6.56 . 1
1207 . 120 HIS HE1 H 8.21 . 1
1208 . 120 HIS ND1 N 165.0 . 1
1209 . 120 HIS NE2 N 225.0 . 1
1210 . 121 GLU N N 122.4 . 1
1211 . 121 GLU H H 9.19 . 1
1212 . 121 GLU C C 175.5 . 1
1213 . 121 GLU CA C 59.0 . 1
1214 . 121 GLU HA H 4.12 . 1
1215 . 121 GLU CB C 32.5 . 1
1216 . 121 GLU HB2 H 2.38 . 1
1217 . 121 GLU HB3 H 2.27 . 1
1218 . 121 GLU HG2 H 2.48 . 1
1219 . 121 GLU HG3 H 2.48 . 1
1220 . 121 GLU CG C 35.0 . 1
1221 . 122 LYS N N 116.1 . 1
1222 . 122 LYS H H 8.43 . 1
1223 . 122 LYS C C 174.7 . 1
1224 . 122 LYS CA C 53.9 . 1
1225 . 122 LYS HA H 4.72 . 1
1226 . 122 LYS CB C 34.8 . 1
1227 . 122 LYS HB2 H 1.99 . 1
1228 . 122 LYS HB3 H 1.75 . 1
1229 . 122 LYS HG2 H 1.36 . 1
1230 . 122 LYS HG3 H 1.36 . 1
1231 . 122 LYS HD2 H 1.65 . 1
1232 . 122 LYS HD3 H 1.65 . 1
1233 . 122 LYS HE2 H 3.01 . 1
1234 . 122 LYS HE3 H 3.01 . 1
1235 . 122 LYS CG C 24.4 . 1
1236 . 122 LYS CD C 29.3 . 1
1237 . 122 LYS CE C 41.8 . 1
1238 . 123 ALA N N 121.9 . 1
1239 . 123 ALA H H 7.82 . 1
1240 . 123 ALA C C 176.5 . 1
1241 . 123 ALA CA C 52.2 . 1
1242 . 123 ALA HA H 3.64 . 1
1243 . 123 ALA CB C 19.9 . 1
1244 . 123 ALA HB H 1.11 . 1
1245 . 124 ASP N N 122.9 . 1
1246 . 124 ASP H H 10.19 . 1
1247 . 124 ASP C C 177.6 . 1
1248 . 124 ASP CA C 52.7 . 1
1249 . 124 ASP HA H 4.64 . 1
1250 . 124 ASP CB C 42.9 . 1
1251 . 124 ASP HB2 H 3.08 . 1
1252 . 124 ASP HB3 H 2.44 . 1
1253 . 125 ASP N N 130.4 . 1
1254 . 125 ASP H H 10.02 . 1
1255 . 125 ASP C C 178.4 . 1
1256 . 125 ASP CA C 54.3 . 1
1257 . 125 ASP HA H 4.30 . 1
1258 . 125 ASP CB C 39.3 . 1
1259 . 125 ASP HB2 H 2.96 . 1
1260 . 125 ASP HB3 H 2.65 . 1
1261 . 126 LEU N N 117.9 . 1
1262 . 126 LEU H H 10.53 . 1
1263 . 126 LEU C C 177.0 . 1
1264 . 126 LEU CA C 54.6 . 1
1265 . 126 LEU HA H 3.44 . 1
1266 . 126 LEU CB C 38.0 . 1
1267 . 126 LEU HB2 H 2.13 . 1
1268 . 126 LEU HB3 H 1.61 . 1
1269 . 126 LEU HG H 1.48 . 1
1270 . 126 LEU HD1 H 0.97 . 1
1271 . 126 LEU HD2 H 0.82 . 1
1272 . 126 LEU CG C 25.6 . 1
1273 . 126 LEU CD1 C 25.7 . 1
1274 . 126 LEU CD2 C 21.9 . 1
1275 . 127 GLY N N 104.8 . 1
1276 . 127 GLY H H 8.73 . 1
1277 . 127 GLY C C 177.1 . 1
1278 . 127 GLY CA C 45.6 . 1
1279 . 127 GLY HA2 H 4.15 . 1
1280 . 127 GLY HA3 H 3.96 . 1
1281 . 128 LYS N N 119.2 . 1
1282 . 128 LYS H H 7.28 . 1
1283 . 128 LYS C C 177.5 . 1
1284 . 128 LYS CA C 54.5 . 1
1285 . 128 LYS HA H 4.56 . 1
1286 . 128 LYS CB C 31.7 . 1
1287 . 128 LYS HB2 H 2.18 . 1
1288 . 128 LYS HB3 H 1.64 . 1
1289 . 128 LYS HG2 H 1.29 . 2
1290 . 128 LYS HG3 H 1.36 . 2
1291 . 128 LYS HD2 H 1.61 . 1
1292 . 128 LYS HD3 H 1.61 . 1
1293 . 128 LYS HE2 H 3.09 . 1
1294 . 128 LYS HE3 H 3.09 . 1
1295 . 128 LYS CG C 24.2 . 1
1296 . 128 LYS CD C 28.1 . 1
1297 . 128 LYS CE C 42.3 . 1
1298 . 129 GLY N N 108.8 . 1
1299 . 129 GLY H H 8.54 . 1
1300 . 129 GLY C C 175.3 . 1
1301 . 129 GLY CA C 45.8 . 1
1302 . 129 GLY HA2 H 3.75 . 1
1303 . 129 GLY HA3 H 4.06 . 1
1304 . 130 GLY N N 108.1 . 1
1305 . 130 GLY H H 8.88 . 1
1306 . 130 GLY C C 173.5 . 1
1307 . 130 GLY CA C 45.8 . 1
1308 . 130 GLY HA2 H 3.76 . 1
1309 . 130 GLY HA3 H 4.00 . 1
1310 . 131 ASN N N 113.1 . 1
1311 . 131 ASN H H 7.14 . 1
1312 . 131 ASN C C 175.5 . 1
1313 . 131 ASN CA C 50.7 . 1
1314 . 131 ASN HA H 4.83 . 1
1315 . 131 ASN CB C 40.4 . 1
1316 . 131 ASN HB2 H 3.19 . 1
1317 . 131 ASN HB3 H 2.94 . 1
1318 . 131 ASN HD21 H 6.69 . 1
1319 . 131 ASN HD22 H 7.54 . 1
1320 . 131 ASN ND2 N 114.1 . 1
1321 . 132 GLU C C 174.8 . 1
1322 . 132 GLU CA C 59.3 . 1
1323 . 132 GLU HA H 4.06 . 1
1324 . 132 GLU CB C 29.1 . 1
1325 . 132 GLU HB2 H 2.08 . 1
1326 . 132 GLU HB3 H 2.00 . 1
1327 . 132 GLU HG2 H 2.19 . 2
1328 . 132 GLU HG3 H 2.32 . 2
1329 . 132 GLU CG C 36.0 . 1
1330 . 133 GLN N N 118.4 . 1
1331 . 133 GLN H H 8.70 . 1
1332 . 133 GLN C C 179.3 . 1
1333 . 133 GLN CA C 58.1 . 1
1334 . 133 GLN HA H 4.01 . 1
1335 . 133 GLN CB C 28.1 . 1
1336 . 133 GLN HB2 H 2.09 . 1
1337 . 133 GLN HB3 H 2.09 . 1
1338 . 133 GLN HG2 H 2.33 . 2
1339 . 133 GLN HG3 H 2.46 . 2
1340 . 133 GLN HE21 H 7.45 . 2
1341 . 133 GLN HE22 H 8.48 . 2
1342 . 133 GLN CG C 34.0 . 1
1343 . 133 GLN NE2 N 117.9 . 1
1344 . 134 SER N N 117.0 . 1
1345 . 134 SER H H 8.19 . 1
1346 . 134 SER C C 176.4 . 1
1347 . 134 SER CA C 62.1 . 1
1348 . 134 SER HA H 3.85 . 1
1349 . 134 SER CB C 63.6 . 1
1350 . 134 SER HB2 H 3.75 . 1
1351 . 134 SER HB3 H 3.93 . 1
1352 . 135 THR N N 103.2 . 1
1353 . 135 THR H H 7.23 . 1
1354 . 135 THR C C 174.2 . 1
1355 . 135 THR CA C 62.8 . 1
1356 . 135 THR HA H 4.63 . 1
1357 . 135 THR CB C 69.2 . 1
1358 . 135 THR HB H 4.63 . 1
1359 . 135 THR HG2 H 1.44 . 1
1360 . 135 THR CG2 C 21.7 . 1
1361 . 136 LYS N N 122.8 . 1
1362 . 136 LYS H H 7.70 . 1
1363 . 136 LYS C C 176.7 . 1
1364 . 136 LYS CA C 58.6 . 1
1365 . 136 LYS HA H 4.69 . 1
1366 . 136 LYS CB C 35.4 . 1
1367 . 136 LYS HB2 H 1.91 . 1
1368 . 136 LYS HB3 H 1.77 . 1
1369 . 136 LYS HG2 H 1.38 . 2
1370 . 136 LYS HG3 H 1.55 . 2
1371 . 136 LYS HD2 H 1.69 . 1
1372 . 136 LYS HD3 H 1.69 . 1
1373 . 136 LYS HE2 H 2.90 . 1
1374 . 136 LYS HE3 H 2.90 . 1
1375 . 136 LYS CG C 25.0 . 1
1376 . 136 LYS CD C 29.2 . 1
1377 . 136 LYS CE C 42.0 . 1
1378 . 137 THR N N 106.8 . 1
1379 . 137 THR H H 8.48 . 1
1380 . 137 THR C C 176.0 . 1
1381 . 137 THR CA C 60.1 . 1
1382 . 137 THR HA H 3.62 . 1
1383 . 137 THR CB C 71.6 . 1
1384 . 137 THR HB H 4.39 . 1
1385 . 137 THR HG2 H 0.99 . 1
1386 . 137 THR CG2 C 21.1 . 1
1387 . 138 GLY N N 111.5 . 1
1388 . 138 GLY H H 7.36 . 1
1389 . 138 GLY C C 173.3 . 1
1390 . 138 GLY CA C 45.8 . 1
1391 . 138 GLY HA2 H 4.18 . 1
1392 . 138 GLY HA3 H 4.39 . 1
1393 . 139 ASN N N 109.0 . 1
1394 . 139 ASN H H 7.86 . 1
1395 . 139 ASN C C 174.0 . 1
1396 . 139 ASN CA C 55.4 . 1
1397 . 139 ASN HA H 4.02 . 1
1398 . 139 ASN CB C 36.8 . 1
1399 . 139 ASN HB2 H 2.90 . 1
1400 . 139 ASN HB3 H 2.90 . 1
1401 . 140 ALA N N 115.6 . 1
1402 . 140 ALA H H 6.45 . 1
1403 . 140 ALA C C 176.5 . 1
1404 . 140 ALA CA C 52.9 . 1
1405 . 140 ALA HA H 4.16 . 1
1406 . 140 ALA CB C 17.6 . 1
1407 . 140 ALA HB H 1.04 . 1
1408 . 141 GLY N N 105.8 . 1
1409 . 141 GLY H H 8.25 . 1
1410 . 141 GLY C C 176.7 . 1
1411 . 141 GLY CA C 45.3 . 1
1412 . 141 GLY HA2 H 3.90 . 1
1413 . 141 GLY HA3 H 4.20 . 1
1414 . 142 SER N N 120.5 . 1
1415 . 142 SER H H 9.30 . 1
1416 . 142 SER C C 173.5 . 1
1417 . 142 SER CA C 59.6 . 1
1418 . 142 SER HA H 4.38 . 1
1419 . 142 SER CB C 63.6 . 1
1420 . 142 SER HB2 H 3.94 . 1
1421 . 142 SER HB3 H 3.94 . 1
1422 . 143 ARG N N 122.3 . 1
1423 . 143 ARG H H 8.93 . 1
1424 . 143 ARG C C 174.9 . 1
1425 . 143 ARG CA C 55.7 . 1
1426 . 143 ARG HA H 3.73 . 1
1427 . 143 ARG CB C 29.3 . 1
1428 . 143 ARG HB2 H 1.96 . 1
1429 . 143 ARG HB3 H 1.93 . 1
1430 . 143 ARG HG2 H 1.16 . 1
1431 . 143 ARG HG3 H 1.16 . 1
1432 . 143 ARG HD2 H 2.94 . 2
1433 . 143 ARG HD3 H 3.10 . 2
1434 . 143 ARG CG C 27.4 . 1
1435 . 143 ARG CD C 43.8 . 1
1436 . 144 LEU N N 122.8 . 1
1437 . 144 LEU H H 8.56 . 1
1438 . 144 LEU C C 177.1 . 1
1439 . 144 LEU CA C 55.8 . 1
1440 . 144 LEU HA H 4.27 . 1
1441 . 144 LEU CB C 43.3 . 1
1442 . 144 LEU HB2 H 1.46 . 1
1443 . 144 LEU HB3 H 1.35 . 1
1444 . 144 LEU HG H 1.37 . 1
1445 . 144 LEU HD1 H 0.90 . 1
1446 . 144 LEU HD2 H 0.86 . 1
1447 . 144 LEU CG C 28.0 . 1
1448 . 144 LEU CD1 C 27.0 . 1
1449 . 144 LEU CD2 C 21.5 . 1
1450 . 145 ALA N N 115.3 . 1
1451 . 145 ALA H H 7.40 . 1
1452 . 145 ALA C C 174.8 . 1
1453 . 145 ALA CA C 51.6 . 1
1454 . 145 ALA HA H 4.42 . 1
1455 . 145 ALA CB C 21.2 . 1
1456 . 145 ALA HB H 0.91 . 1
1457 . 146 CYS N N 113.7 . 1
1458 . 146 CYS H H 8.89 . 1
1459 . 146 CYS C C 173.8 . 1
1460 . 146 CYS CA C 53.8 . 1
1461 . 146 CYS HA H 6.05 . 1
1462 . 146 CYS CB C 46.2 . 1
1463 . 146 CYS HB2 H 3.05 . 1
1464 . 146 CYS HB3 H 3.06 . 1
1465 . 147 GLY N N 107.3 . 1
1466 . 147 GLY H H 8.38 . 1
1467 . 147 GLY C C 171.7 . 1
1468 . 147 GLY CA C 42.4 . 1
1469 . 147 GLY HA2 H 3.81 . 1
1470 . 147 GLY HA3 H 4.55 . 1
1471 . 148 VAL N N 126.9 . 1
1472 . 148 VAL H H 8.85 . 1
1473 . 148 VAL C C 176.4 . 1
1474 . 148 VAL CA C 63.0 . 1
1475 . 148 VAL HA H 4.27 . 1
1476 . 148 VAL CB C 32.0 . 1
1477 . 148 VAL HB H 2.05 . 1
1478 . 148 VAL HG1 H 0.92 . 1
1479 . 148 VAL HG2 H 0.78 . 1
1480 . 148 VAL CG1 C 22.9 . 1
1481 . 148 VAL CG2 C 20.9 . 1
1482 . 149 ILE N N 130.3 . 1
1483 . 149 ILE H H 8.72 . 1
1484 . 149 ILE C C 175.5 . 1
1485 . 149 ILE CA C 61.8 . 1
1486 . 149 ILE HA H 3.96 . 1
1487 . 149 ILE CB C 37.3 . 1
1488 . 149 ILE HB H 1.83 . 1
1489 . 149 ILE HG12 H 0.59 . 2
1490 . 149 ILE HG13 H 1.76 . 2
1491 . 149 ILE HG2 H 0.09 . 1
1492 . 149 ILE HD1 H 0.47 . 1
1493 . 149 ILE CG1 C 27.9 . 1
1494 . 149 ILE CG2 C 18.2 . 1
1495 . 149 ILE CD1 C 15.3 . 1
1496 . 150 GLY N N 117.9 . 1
1497 . 150 GLY H H 8.85 . 1
1498 . 150 GLY C C 172.7 . 1
1499 . 150 GLY CA C 43.4 . 1
1500 . 150 GLY HA2 H 3.84 . 1
1501 . 150 GLY HA3 H 4.82 . 1
1502 . 151 ILE N N 121.9 . 1
1503 . 151 ILE H H 8.59 . 1
1504 . 151 ILE C C 175.5 . 1
1505 . 151 ILE CA C 61.5 . 1
1506 . 151 ILE HA H 4.18 . 1
1507 . 151 ILE CB C 38.1 . 1
1508 . 151 ILE HB H 1.86 . 1
1509 . 151 ILE HG12 H 1.35 . 2
1510 . 151 ILE HG13 H 1.70 . 2
1511 . 151 ILE HG2 H 1.01 . 1
1512 . 151 ILE HD1 H 1.03 . 1
1513 . 151 ILE CG1 C 28.0 . 1
1514 . 151 ILE CG2 C 17.5 . 1
1515 . 151 ILE CD1 C 12.1 . 1
1516 . 152 ALA N N 131.8 . 1
1517 . 152 ALA H H 8.37 . 1
1518 . 152 ALA C C 175.4 . 1
1519 . 152 ALA CA C 51.3 . 1
1520 . 152 ALA HA H 4.61 . 1
1521 . 152 ALA CB C 20.5 . 1
1522 . 152 ALA HB H 1.25 . 1
1523 . 153 GLN N N 125.4 . 1
1524 . 153 GLN H H 8.06 . 1
1525 . 153 GLN C C 180.8 . 1
1526 . 153 GLN CA C 57.3 . 1
1527 . 153 GLN HA H 4.23 . 1
1528 . 153 GLN CB C 30.7 . 1
1529 . 153 GLN HB2 H 2.14 . 1
1530 . 153 GLN HB3 H 1.96 . 1
1531 . 153 GLN HG2 H 2.36 . 1
1532 . 153 GLN HG3 H 2.36 . 1
1533 . 153 GLN CG C 34.4 . 1
stop_
save_